data_9G8K
# 
_entry.id   9G8K 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9G8K         pdb_00009g8k 10.2210/pdb9g8k/pdb 
WWPDB D_1292139986 ?            ?                   
# 
_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       2025-06-04 
_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                        9G8K 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 keni.vidilaseris@helsinki.fi Keni   Vidilaseris ? 'principal investigator/group leader' 0000-0002-6453-6600 
3 adrian.goldman@helsinki.fi   Adrian Goldman     ? 'principal investigator/group leader' 0000-0001-8032-9700 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vidilaseris, K.' 1 0000-0002-6453-6600 
'Liu, J.'         2 0000-0003-0079-4712 
'Goldman, A.'     3 0000-0001-8032-9700 
# 
loop_
_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 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary Elife                            ?      ? 2050-084X ? ? ?  ? ?   ?   
'Conformational dynamics and asymmetry in multimodal inhibition of membrane-bound pyrophosphatases'           2024 ? 
10.7554/elife.102288.1    ?        ? ? 
? ? ? ? ? ? ? US ? ? 1       'Acta Crystallogr.,Sect.D'       ABCRE6 ? 1399-0047 ? ? 68 ? 352 367 
'Towards automated crystallographic structure refinement with phenix.refine.'                                 2012 ? 
10.1107/S0907444912001308 22505256 ? ? 
? ? ? ? ? ? ? ?  ? ? 2       'Acta Crystallogr D Struct Biol' ?      ? 2059-7983 ? ? 75 ? 861 877 
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.' 2019 ? 
10.1107/S2059798319011471 31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, J.'                1  ?                   
primary 'Shah, A.'               2  ?                   
primary 'Ma, Y.'                 3  ?                   
primary 'Hardman, K.'            4  ?                   
primary 'Johansson, N.G.'        5  ?                   
primary 'Ribeiro, O.'            6  ?                   
primary 'Brookfield, A.'         7  ?                   
primary 'Bowen, A.'              8  ?                   
primary 'Yli-Kauhaluoma, J.'     9  ?                   
primary 'Xhaard, H.'             10 ?                   
primary 'Jeuken, L.J.'           11 ?                   
primary 'Goldman, A.'            12 ?                   
primary 'Pliotas, C.'            13 ?                   
primary 'Vidilaseris, K.'        14 ?                   
1       'Afonine, P.V.'          15 ?                   
1       'Grosse-Kunstleve, R.W.' 16 ?                   
1       'Echols, N.'             17 ?                   
1       'Headd, J.J.'            18 ?                   
1       'Moriarty, N.W.'         19 ?                   
1       'Mustyakimov, M.'        20 ?                   
1       'Terwilliger, T.C.'      21 ?                   
1       'Urzhumtsev, A.'         22 ?                   
1       'Zwart, P.H.'            23 ?                   
1       'Adams, P.D.'            24 ?                   
2       'Liebschner, D.'         25 0000-0003-3921-3209 
2       'Afonine, P.V.'          26 0000-0002-5052-991X 
2       'Baker, M.L.'            27 ?                   
2       'Bunkoczi, G.'           28 ?                   
2       'Chen, V.B.'             29 ?                   
2       'Croll, T.I.'            30 ?                   
2       'Hintze, B.'             31 0000-0002-4871-2096 
2       'Hung, L.W.'             32 0000-0001-6690-8458 
2       'Jain, S.'               33 ?                   
2       'McCoy, A.J.'            34 ?                   
2       'Moriarty, N.W.'         35 0000-0001-8857-9464 
2       'Oeffner, R.D.'          36 0000-0003-3107-2202 
2       'Poon, B.K.'             37 0000-0001-9633-6067 
2       'Prisant, M.G.'          38 ?                   
2       'Read, R.J.'             39 0000-0001-8273-0047 
2       'Richardson, J.S.'       40 ?                   
2       'Richardson, D.C.'       41 ?                   
2       'Sammito, M.D.'          42 ?                   
2       'Sobolev, O.V.'          43 0000-0002-0623-3214 
2       'Stockwell, D.H.'        44 ?                   
2       'Terwilliger, T.C.'      45 0000-0001-6384-0320 
2       'Urzhumtsev, A.G.'       46 ?                   
2       'Videau, L.L.'           47 ?                   
2       'Williams, C.J.'         48 ?                   
2       'Adams, P.D.'            49 0000-0001-9333-8219 
# 
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 'K(+)-stimulated pyrophosphate-energized sodium pump' 78217.141 2 7.2.3.- ? ? ? 
2 non-polymer syn '(1-hydroxyethane-1,1-diyl)bis(phosphonic acid)'      206.028   2 ?       ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                       24.305    9 ?       ? ? ? 
4 non-polymer syn 'CALCIUM ION'                                         40.078    2 ?       ? ? ? 
5 non-polymer syn DODECYL-BETA-D-MALTOSIDE                              510.615   2 ?       ? ? ? 
6 water       nat water                                                 18.015    6 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Membrane-bound sodium-translocating pyrophosphatase,Pyrophosphate-energized inorganic pyrophosphatase,Na(+)-PPase,Tm-PPase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MRGSHHHHHHYVAALFFLIPLVALGFAAANFAAVVRKPEGTERMKEISSYIRSGADSFLAHETKAIFKVAIVIAILLMIF
TTWQTGVAFLLGAVMSASAGIVGMKMATRANVRVAEAARTTKKIGPALKVAYQGGSVMGLSVGGFALLGLVLVYLIFGKW
MGQVDNLNIYTNWLGINFVPFAMTVSGYALGCSIIAMFDRVGGGVYTKAADMAADLVGKTELNLPEDDPRNPATIADNVG
DNVGDVAGLGADLLESFVGAIVSSIILASYMFPIYVQKIGENLVHQVPKETIQALISYPIFFALVGLGCSMLGILYVIVK
KPSDNPQRELNISLWTSALLTVVLTAFLTYFYLKDLQGLDVLGFRFGAISPWFSAIIGIFSGILIGFWAEYYTSYRYKPT
QFLGKSSIEGTGMVISNGLSLGMKSVFPPTLTLVLGILFADYFAGLYGVAIAALGMLSFVATSVSVDSYGPIADNAGGIS
EMCELDPEVRKITDHLDAVGNTTAAIGKGFAIGSAIFAALSLFASYMFSQISPSDIGKPPSLVLLLNMLDARVIAGALLG
AAITYYFSGYLISAVTKAAMKMVDEIRRQAREIPGLLEGKAKPDYNRCIEITSDNALKQMGYPAFIAILTPLVTGFLLGA
EFVGGVLIGTVLSGAMLAILTANSGGAWDNAKKYLEAGNLEGYGKGSEPHKALVIGDTVGDPLKDTVGPSLDILIKIMSV
VSVIAVSIFKHVHLF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRGSHHHHHHYVAALFFLIPLVALGFAAANFAAVVRKPEGTERMKEISSYIRSGADSFLAHETKAIFKVAIVIAILLMIF
TTWQTGVAFLLGAVMSASAGIVGMKMATRANVRVAEAARTTKKIGPALKVAYQGGSVMGLSVGGFALLGLVLVYLIFGKW
MGQVDNLNIYTNWLGINFVPFAMTVSGYALGCSIIAMFDRVGGGVYTKAADMAADLVGKTELNLPEDDPRNPATIADNVG
DNVGDVAGLGADLLESFVGAIVSSIILASYMFPIYVQKIGENLVHQVPKETIQALISYPIFFALVGLGCSMLGILYVIVK
KPSDNPQRELNISLWTSALLTVVLTAFLTYFYLKDLQGLDVLGFRFGAISPWFSAIIGIFSGILIGFWAEYYTSYRYKPT
QFLGKSSIEGTGMVISNGLSLGMKSVFPPTLTLVLGILFADYFAGLYGVAIAALGMLSFVATSVSVDSYGPIADNAGGIS
EMCELDPEVRKITDHLDAVGNTTAAIGKGFAIGSAIFAALSLFASYMFSQISPSDIGKPPSLVLLLNMLDARVIAGALLG
AAITYYFSGYLISAVTKAAMKMVDEIRRQAREIPGLLEGKAKPDYNRCIEITSDNALKQMGYPAFIAILTPLVTGFLLGA
EFVGGVLIGTVLSGAMLAILTANSGGAWDNAKKYLEAGNLEGYGKGSEPHKALVIGDTVGDPLKDTVGPSLDILIKIMSV
VSVIAVSIFKHVHLF
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(1-hydroxyethane-1,1-diyl)bis(phosphonic acid)' 911 
3 'MAGNESIUM ION'                                  MG  
4 'CALCIUM ION'                                    CA  
5 DODECYL-BETA-D-MALTOSIDE                         LMT 
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   ARG n 
1 3   GLY n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  TYR n 
1 12  VAL n 
1 13  ALA n 
1 14  ALA n 
1 15  LEU n 
1 16  PHE n 
1 17  PHE n 
1 18  LEU n 
1 19  ILE n 
1 20  PRO n 
1 21  LEU n 
1 22  VAL n 
1 23  ALA n 
1 24  LEU n 
1 25  GLY n 
1 26  PHE n 
1 27  ALA n 
1 28  ALA n 
1 29  ALA n 
1 30  ASN n 
1 31  PHE n 
1 32  ALA n 
1 33  ALA n 
1 34  VAL n 
1 35  VAL n 
1 36  ARG n 
1 37  LYS n 
1 38  PRO n 
1 39  GLU n 
1 40  GLY n 
1 41  THR n 
1 42  GLU n 
1 43  ARG n 
1 44  MET n 
1 45  LYS n 
1 46  GLU n 
1 47  ILE n 
1 48  SER n 
1 49  SER n 
1 50  TYR n 
1 51  ILE n 
1 52  ARG n 
1 53  SER n 
1 54  GLY n 
1 55  ALA n 
1 56  ASP n 
1 57  SER n 
1 58  PHE n 
1 59  LEU n 
1 60  ALA n 
1 61  HIS n 
1 62  GLU n 
1 63  THR n 
1 64  LYS n 
1 65  ALA n 
1 66  ILE n 
1 67  PHE n 
1 68  LYS n 
1 69  VAL n 
1 70  ALA n 
1 71  ILE n 
1 72  VAL n 
1 73  ILE n 
1 74  ALA n 
1 75  ILE n 
1 76  LEU n 
1 77  LEU n 
1 78  MET n 
1 79  ILE n 
1 80  PHE n 
1 81  THR n 
1 82  THR n 
1 83  TRP n 
1 84  GLN n 
1 85  THR n 
1 86  GLY n 
1 87  VAL n 
1 88  ALA n 
1 89  PHE n 
1 90  LEU n 
1 91  LEU n 
1 92  GLY n 
1 93  ALA n 
1 94  VAL n 
1 95  MET n 
1 96  SER n 
1 97  ALA n 
1 98  SER n 
1 99  ALA n 
1 100 GLY n 
1 101 ILE n 
1 102 VAL n 
1 103 GLY n 
1 104 MET n 
1 105 LYS n 
1 106 MET n 
1 107 ALA n 
1 108 THR n 
1 109 ARG n 
1 110 ALA n 
1 111 ASN n 
1 112 VAL n 
1 113 ARG n 
1 114 VAL n 
1 115 ALA n 
1 116 GLU n 
1 117 ALA n 
1 118 ALA n 
1 119 ARG n 
1 120 THR n 
1 121 THR n 
1 122 LYS n 
1 123 LYS n 
1 124 ILE n 
1 125 GLY n 
1 126 PRO n 
1 127 ALA n 
1 128 LEU n 
1 129 LYS n 
1 130 VAL n 
1 131 ALA n 
1 132 TYR n 
1 133 GLN n 
1 134 GLY n 
1 135 GLY n 
1 136 SER n 
1 137 VAL n 
1 138 MET n 
1 139 GLY n 
1 140 LEU n 
1 141 SER n 
1 142 VAL n 
1 143 GLY n 
1 144 GLY n 
1 145 PHE n 
1 146 ALA n 
1 147 LEU n 
1 148 LEU n 
1 149 GLY n 
1 150 LEU n 
1 151 VAL n 
1 152 LEU n 
1 153 VAL n 
1 154 TYR n 
1 155 LEU n 
1 156 ILE n 
1 157 PHE n 
1 158 GLY n 
1 159 LYS n 
1 160 TRP n 
1 161 MET n 
1 162 GLY n 
1 163 GLN n 
1 164 VAL n 
1 165 ASP n 
1 166 ASN n 
1 167 LEU n 
1 168 ASN n 
1 169 ILE n 
1 170 TYR n 
1 171 THR n 
1 172 ASN n 
1 173 TRP n 
1 174 LEU n 
1 175 GLY n 
1 176 ILE n 
1 177 ASN n 
1 178 PHE n 
1 179 VAL n 
1 180 PRO n 
1 181 PHE n 
1 182 ALA n 
1 183 MET n 
1 184 THR n 
1 185 VAL n 
1 186 SER n 
1 187 GLY n 
1 188 TYR n 
1 189 ALA n 
1 190 LEU n 
1 191 GLY n 
1 192 CYS n 
1 193 SER n 
1 194 ILE n 
1 195 ILE n 
1 196 ALA n 
1 197 MET n 
1 198 PHE n 
1 199 ASP n 
1 200 ARG n 
1 201 VAL n 
1 202 GLY n 
1 203 GLY n 
1 204 GLY n 
1 205 VAL n 
1 206 TYR n 
1 207 THR n 
1 208 LYS n 
1 209 ALA n 
1 210 ALA n 
1 211 ASP n 
1 212 MET n 
1 213 ALA n 
1 214 ALA n 
1 215 ASP n 
1 216 LEU n 
1 217 VAL n 
1 218 GLY n 
1 219 LYS n 
1 220 THR n 
1 221 GLU n 
1 222 LEU n 
1 223 ASN n 
1 224 LEU n 
1 225 PRO n 
1 226 GLU n 
1 227 ASP n 
1 228 ASP n 
1 229 PRO n 
1 230 ARG n 
1 231 ASN n 
1 232 PRO n 
1 233 ALA n 
1 234 THR n 
1 235 ILE n 
1 236 ALA n 
1 237 ASP n 
1 238 ASN n 
1 239 VAL n 
1 240 GLY n 
1 241 ASP n 
1 242 ASN n 
1 243 VAL n 
1 244 GLY n 
1 245 ASP n 
1 246 VAL n 
1 247 ALA n 
1 248 GLY n 
1 249 LEU n 
1 250 GLY n 
1 251 ALA n 
1 252 ASP n 
1 253 LEU n 
1 254 LEU n 
1 255 GLU n 
1 256 SER n 
1 257 PHE n 
1 258 VAL n 
1 259 GLY n 
1 260 ALA n 
1 261 ILE n 
1 262 VAL n 
1 263 SER n 
1 264 SER n 
1 265 ILE n 
1 266 ILE n 
1 267 LEU n 
1 268 ALA n 
1 269 SER n 
1 270 TYR n 
1 271 MET n 
1 272 PHE n 
1 273 PRO n 
1 274 ILE n 
1 275 TYR n 
1 276 VAL n 
1 277 GLN n 
1 278 LYS n 
1 279 ILE n 
1 280 GLY n 
1 281 GLU n 
1 282 ASN n 
1 283 LEU n 
1 284 VAL n 
1 285 HIS n 
1 286 GLN n 
1 287 VAL n 
1 288 PRO n 
1 289 LYS n 
1 290 GLU n 
1 291 THR n 
1 292 ILE n 
1 293 GLN n 
1 294 ALA n 
1 295 LEU n 
1 296 ILE n 
1 297 SER n 
1 298 TYR n 
1 299 PRO n 
1 300 ILE n 
1 301 PHE n 
1 302 PHE n 
1 303 ALA n 
1 304 LEU n 
1 305 VAL n 
1 306 GLY n 
1 307 LEU n 
1 308 GLY n 
1 309 CYS n 
1 310 SER n 
1 311 MET n 
1 312 LEU n 
1 313 GLY n 
1 314 ILE n 
1 315 LEU n 
1 316 TYR n 
1 317 VAL n 
1 318 ILE n 
1 319 VAL n 
1 320 LYS n 
1 321 LYS n 
1 322 PRO n 
1 323 SER n 
1 324 ASP n 
1 325 ASN n 
1 326 PRO n 
1 327 GLN n 
1 328 ARG n 
1 329 GLU n 
1 330 LEU n 
1 331 ASN n 
1 332 ILE n 
1 333 SER n 
1 334 LEU n 
1 335 TRP n 
1 336 THR n 
1 337 SER n 
1 338 ALA n 
1 339 LEU n 
1 340 LEU n 
1 341 THR n 
1 342 VAL n 
1 343 VAL n 
1 344 LEU n 
1 345 THR n 
1 346 ALA n 
1 347 PHE n 
1 348 LEU n 
1 349 THR n 
1 350 TYR n 
1 351 PHE n 
1 352 TYR n 
1 353 LEU n 
1 354 LYS n 
1 355 ASP n 
1 356 LEU n 
1 357 GLN n 
1 358 GLY n 
1 359 LEU n 
1 360 ASP n 
1 361 VAL n 
1 362 LEU n 
1 363 GLY n 
1 364 PHE n 
1 365 ARG n 
1 366 PHE n 
1 367 GLY n 
1 368 ALA n 
1 369 ILE n 
1 370 SER n 
1 371 PRO n 
1 372 TRP n 
1 373 PHE n 
1 374 SER n 
1 375 ALA n 
1 376 ILE n 
1 377 ILE n 
1 378 GLY n 
1 379 ILE n 
1 380 PHE n 
1 381 SER n 
1 382 GLY n 
1 383 ILE n 
1 384 LEU n 
1 385 ILE n 
1 386 GLY n 
1 387 PHE n 
1 388 TRP n 
1 389 ALA n 
1 390 GLU n 
1 391 TYR n 
1 392 TYR n 
1 393 THR n 
1 394 SER n 
1 395 TYR n 
1 396 ARG n 
1 397 TYR n 
1 398 LYS n 
1 399 PRO n 
1 400 THR n 
1 401 GLN n 
1 402 PHE n 
1 403 LEU n 
1 404 GLY n 
1 405 LYS n 
1 406 SER n 
1 407 SER n 
1 408 ILE n 
1 409 GLU n 
1 410 GLY n 
1 411 THR n 
1 412 GLY n 
1 413 MET n 
1 414 VAL n 
1 415 ILE n 
1 416 SER n 
1 417 ASN n 
1 418 GLY n 
1 419 LEU n 
1 420 SER n 
1 421 LEU n 
1 422 GLY n 
1 423 MET n 
1 424 LYS n 
1 425 SER n 
1 426 VAL n 
1 427 PHE n 
1 428 PRO n 
1 429 PRO n 
1 430 THR n 
1 431 LEU n 
1 432 THR n 
1 433 LEU n 
1 434 VAL n 
1 435 LEU n 
1 436 GLY n 
1 437 ILE n 
1 438 LEU n 
1 439 PHE n 
1 440 ALA n 
1 441 ASP n 
1 442 TYR n 
1 443 PHE n 
1 444 ALA n 
1 445 GLY n 
1 446 LEU n 
1 447 TYR n 
1 448 GLY n 
1 449 VAL n 
1 450 ALA n 
1 451 ILE n 
1 452 ALA n 
1 453 ALA n 
1 454 LEU n 
1 455 GLY n 
1 456 MET n 
1 457 LEU n 
1 458 SER n 
1 459 PHE n 
1 460 VAL n 
1 461 ALA n 
1 462 THR n 
1 463 SER n 
1 464 VAL n 
1 465 SER n 
1 466 VAL n 
1 467 ASP n 
1 468 SER n 
1 469 TYR n 
1 470 GLY n 
1 471 PRO n 
1 472 ILE n 
1 473 ALA n 
1 474 ASP n 
1 475 ASN n 
1 476 ALA n 
1 477 GLY n 
1 478 GLY n 
1 479 ILE n 
1 480 SER n 
1 481 GLU n 
1 482 MET n 
1 483 CYS n 
1 484 GLU n 
1 485 LEU n 
1 486 ASP n 
1 487 PRO n 
1 488 GLU n 
1 489 VAL n 
1 490 ARG n 
1 491 LYS n 
1 492 ILE n 
1 493 THR n 
1 494 ASP n 
1 495 HIS n 
1 496 LEU n 
1 497 ASP n 
1 498 ALA n 
1 499 VAL n 
1 500 GLY n 
1 501 ASN n 
1 502 THR n 
1 503 THR n 
1 504 ALA n 
1 505 ALA n 
1 506 ILE n 
1 507 GLY n 
1 508 LYS n 
1 509 GLY n 
1 510 PHE n 
1 511 ALA n 
1 512 ILE n 
1 513 GLY n 
1 514 SER n 
1 515 ALA n 
1 516 ILE n 
1 517 PHE n 
1 518 ALA n 
1 519 ALA n 
1 520 LEU n 
1 521 SER n 
1 522 LEU n 
1 523 PHE n 
1 524 ALA n 
1 525 SER n 
1 526 TYR n 
1 527 MET n 
1 528 PHE n 
1 529 SER n 
1 530 GLN n 
1 531 ILE n 
1 532 SER n 
1 533 PRO n 
1 534 SER n 
1 535 ASP n 
1 536 ILE n 
1 537 GLY n 
1 538 LYS n 
1 539 PRO n 
1 540 PRO n 
1 541 SER n 
1 542 LEU n 
1 543 VAL n 
1 544 LEU n 
1 545 LEU n 
1 546 LEU n 
1 547 ASN n 
1 548 MET n 
1 549 LEU n 
1 550 ASP n 
1 551 ALA n 
1 552 ARG n 
1 553 VAL n 
1 554 ILE n 
1 555 ALA n 
1 556 GLY n 
1 557 ALA n 
1 558 LEU n 
1 559 LEU n 
1 560 GLY n 
1 561 ALA n 
1 562 ALA n 
1 563 ILE n 
1 564 THR n 
1 565 TYR n 
1 566 TYR n 
1 567 PHE n 
1 568 SER n 
1 569 GLY n 
1 570 TYR n 
1 571 LEU n 
1 572 ILE n 
1 573 SER n 
1 574 ALA n 
1 575 VAL n 
1 576 THR n 
1 577 LYS n 
1 578 ALA n 
1 579 ALA n 
1 580 MET n 
1 581 LYS n 
1 582 MET n 
1 583 VAL n 
1 584 ASP n 
1 585 GLU n 
1 586 ILE n 
1 587 ARG n 
1 588 ARG n 
1 589 GLN n 
1 590 ALA n 
1 591 ARG n 
1 592 GLU n 
1 593 ILE n 
1 594 PRO n 
1 595 GLY n 
1 596 LEU n 
1 597 LEU n 
1 598 GLU n 
1 599 GLY n 
1 600 LYS n 
1 601 ALA n 
1 602 LYS n 
1 603 PRO n 
1 604 ASP n 
1 605 TYR n 
1 606 ASN n 
1 607 ARG n 
1 608 CYS n 
1 609 ILE n 
1 610 GLU n 
1 611 ILE n 
1 612 THR n 
1 613 SER n 
1 614 ASP n 
1 615 ASN n 
1 616 ALA n 
1 617 LEU n 
1 618 LYS n 
1 619 GLN n 
1 620 MET n 
1 621 GLY n 
1 622 TYR n 
1 623 PRO n 
1 624 ALA n 
1 625 PHE n 
1 626 ILE n 
1 627 ALA n 
1 628 ILE n 
1 629 LEU n 
1 630 THR n 
1 631 PRO n 
1 632 LEU n 
1 633 VAL n 
1 634 THR n 
1 635 GLY n 
1 636 PHE n 
1 637 LEU n 
1 638 LEU n 
1 639 GLY n 
1 640 ALA n 
1 641 GLU n 
1 642 PHE n 
1 643 VAL n 
1 644 GLY n 
1 645 GLY n 
1 646 VAL n 
1 647 LEU n 
1 648 ILE n 
1 649 GLY n 
1 650 THR n 
1 651 VAL n 
1 652 LEU n 
1 653 SER n 
1 654 GLY n 
1 655 ALA n 
1 656 MET n 
1 657 LEU n 
1 658 ALA n 
1 659 ILE n 
1 660 LEU n 
1 661 THR n 
1 662 ALA n 
1 663 ASN n 
1 664 SER n 
1 665 GLY n 
1 666 GLY n 
1 667 ALA n 
1 668 TRP n 
1 669 ASP n 
1 670 ASN n 
1 671 ALA n 
1 672 LYS n 
1 673 LYS n 
1 674 TYR n 
1 675 LEU n 
1 676 GLU n 
1 677 ALA n 
1 678 GLY n 
1 679 ASN n 
1 680 LEU n 
1 681 GLU n 
1 682 GLY n 
1 683 TYR n 
1 684 GLY n 
1 685 LYS n 
1 686 GLY n 
1 687 SER n 
1 688 GLU n 
1 689 PRO n 
1 690 HIS n 
1 691 LYS n 
1 692 ALA n 
1 693 LEU n 
1 694 VAL n 
1 695 ILE n 
1 696 GLY n 
1 697 ASP n 
1 698 THR n 
1 699 VAL n 
1 700 GLY n 
1 701 ASP n 
1 702 PRO n 
1 703 LEU n 
1 704 LYS n 
1 705 ASP n 
1 706 THR n 
1 707 VAL n 
1 708 GLY n 
1 709 PRO n 
1 710 SER n 
1 711 LEU n 
1 712 ASP n 
1 713 ILE n 
1 714 LEU n 
1 715 ILE n 
1 716 LYS n 
1 717 ILE n 
1 718 MET n 
1 719 SER n 
1 720 VAL n 
1 721 VAL n 
1 722 SER n 
1 723 VAL n 
1 724 ILE n 
1 725 ALA n 
1 726 VAL n 
1 727 SER n 
1 728 ILE n 
1 729 PHE n 
1 730 LYS n 
1 731 HIS n 
1 732 VAL n 
1 733 HIS n 
1 734 LEU n 
1 735 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   735 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'hppA, TM_0174' 
_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      'Thermotoga maritima' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2336 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_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 
911 non-polymer         . '(1-hydroxyethane-1,1-diyl)bis(phosphonic acid)' 'Etidronic acid' 'C2 H8 O7 P2'    206.028 
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 
CA  non-polymer         . 'CALCIUM ION'                                    ?                'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE                                         ?                'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                        ?                'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                  ?                'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                          ?                'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                        ?                'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                            ?                'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                       ?                'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                          ?                'C6 H13 N O2'    131.173 
LMT D-saccharide        . DODECYL-BETA-D-MALTOSIDE                         ?                'C24 H46 O11'    510.615 
LYS 'L-peptide linking' y LYSINE                                           ?                'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                       ?                'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                  ?                'Mg 2'           24.305  
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   -8  ?   ?   ?   A . n 
A 1 2   ARG 2   -7  ?   ?   ?   A . n 
A 1 3   GLY 3   -6  ?   ?   ?   A . n 
A 1 4   SER 4   -5  ?   ?   ?   A . n 
A 1 5   HIS 5   -4  ?   ?   ?   A . n 
A 1 6   HIS 6   -3  ?   ?   ?   A . n 
A 1 7   HIS 7   -2  ?   ?   ?   A . n 
A 1 8   HIS 8   -1  ?   ?   ?   A . n 
A 1 9   HIS 9   0   ?   ?   ?   A . n 
A 1 10  HIS 10  1   ?   ?   ?   A . n 
A 1 11  TYR 11  2   2   TYR TYR A . n 
A 1 12  VAL 12  3   3   VAL VAL A . n 
A 1 13  ALA 13  4   4   ALA ALA A . n 
A 1 14  ALA 14  5   5   ALA ALA A . n 
A 1 15  LEU 15  6   6   LEU LEU A . n 
A 1 16  PHE 16  7   7   PHE PHE A . n 
A 1 17  PHE 17  8   8   PHE PHE A . n 
A 1 18  LEU 18  9   9   LEU LEU A . n 
A 1 19  ILE 19  10  10  ILE ILE A . n 
A 1 20  PRO 20  11  11  PRO PRO A . n 
A 1 21  LEU 21  12  12  LEU LEU A . n 
A 1 22  VAL 22  13  13  VAL VAL A . n 
A 1 23  ALA 23  14  14  ALA ALA A . n 
A 1 24  LEU 24  15  15  LEU LEU A . n 
A 1 25  GLY 25  16  16  GLY GLY A . n 
A 1 26  PHE 26  17  17  PHE PHE A . n 
A 1 27  ALA 27  18  18  ALA ALA A . n 
A 1 28  ALA 28  19  19  ALA ALA A . n 
A 1 29  ALA 29  20  20  ALA ALA A . n 
A 1 30  ASN 30  21  21  ASN ASN A . n 
A 1 31  PHE 31  22  22  PHE PHE A . n 
A 1 32  ALA 32  23  23  ALA ALA A . n 
A 1 33  ALA 33  24  24  ALA ALA A . n 
A 1 34  VAL 34  25  25  VAL VAL A . n 
A 1 35  VAL 35  26  26  VAL VAL A . n 
A 1 36  ARG 36  27  27  ARG ARG A . n 
A 1 37  LYS 37  28  28  LYS LYS A . n 
A 1 38  PRO 38  29  29  PRO PRO A . n 
A 1 39  GLU 39  30  30  GLU GLU A . n 
A 1 40  GLY 40  31  31  GLY GLY A . n 
A 1 41  THR 41  32  32  THR THR A . n 
A 1 42  GLU 42  33  33  GLU GLU A . n 
A 1 43  ARG 43  34  34  ARG ARG A . n 
A 1 44  MET 44  35  35  MET MET A . n 
A 1 45  LYS 45  36  36  LYS LYS A . n 
A 1 46  GLU 46  37  37  GLU GLU A . n 
A 1 47  ILE 47  38  38  ILE ILE A . n 
A 1 48  SER 48  39  39  SER SER A . n 
A 1 49  SER 49  40  40  SER SER A . n 
A 1 50  TYR 50  41  41  TYR TYR A . n 
A 1 51  ILE 51  42  42  ILE ILE A . n 
A 1 52  ARG 52  43  43  ARG ARG A . n 
A 1 53  SER 53  44  44  SER SER A . n 
A 1 54  GLY 54  45  45  GLY GLY A . n 
A 1 55  ALA 55  46  46  ALA ALA A . n 
A 1 56  ASP 56  47  47  ASP ASP A . n 
A 1 57  SER 57  48  48  SER SER A . n 
A 1 58  PHE 58  49  49  PHE PHE A . n 
A 1 59  LEU 59  50  50  LEU LEU A . n 
A 1 60  ALA 60  51  51  ALA ALA A . n 
A 1 61  HIS 61  52  52  HIS HIS A . n 
A 1 62  GLU 62  53  53  GLU GLU A . n 
A 1 63  THR 63  54  54  THR THR A . n 
A 1 64  LYS 64  55  55  LYS LYS A . n 
A 1 65  ALA 65  56  56  ALA ALA A . n 
A 1 66  ILE 66  57  57  ILE ILE A . n 
A 1 67  PHE 67  58  58  PHE PHE A . n 
A 1 68  LYS 68  59  59  LYS LYS A . n 
A 1 69  VAL 69  60  60  VAL VAL A . n 
A 1 70  ALA 70  61  61  ALA ALA A . n 
A 1 71  ILE 71  62  62  ILE ILE A . n 
A 1 72  VAL 72  63  63  VAL VAL A . n 
A 1 73  ILE 73  64  64  ILE ILE A . n 
A 1 74  ALA 74  65  65  ALA ALA A . n 
A 1 75  ILE 75  66  66  ILE ILE A . n 
A 1 76  LEU 76  67  67  LEU LEU A . n 
A 1 77  LEU 77  68  68  LEU LEU A . n 
A 1 78  MET 78  69  69  MET MET A . n 
A 1 79  ILE 79  70  70  ILE ILE A . n 
A 1 80  PHE 80  71  71  PHE PHE A . n 
A 1 81  THR 81  72  72  THR THR A . n 
A 1 82  THR 82  73  73  THR THR A . n 
A 1 83  TRP 83  74  74  TRP TRP A . n 
A 1 84  GLN 84  75  75  GLN GLN A . n 
A 1 85  THR 85  76  76  THR THR A . n 
A 1 86  GLY 86  77  77  GLY GLY A . n 
A 1 87  VAL 87  78  78  VAL VAL A . n 
A 1 88  ALA 88  79  79  ALA ALA A . n 
A 1 89  PHE 89  80  80  PHE PHE A . n 
A 1 90  LEU 90  81  81  LEU LEU A . n 
A 1 91  LEU 91  82  82  LEU LEU A . n 
A 1 92  GLY 92  83  83  GLY GLY A . n 
A 1 93  ALA 93  84  84  ALA ALA A . n 
A 1 94  VAL 94  85  85  VAL VAL A . n 
A 1 95  MET 95  86  86  MET MET A . n 
A 1 96  SER 96  87  87  SER SER A . n 
A 1 97  ALA 97  88  88  ALA ALA A . n 
A 1 98  SER 98  89  89  SER SER A . n 
A 1 99  ALA 99  90  90  ALA ALA A . n 
A 1 100 GLY 100 91  91  GLY GLY A . n 
A 1 101 ILE 101 92  92  ILE ILE A . n 
A 1 102 VAL 102 93  93  VAL VAL A . n 
A 1 103 GLY 103 94  94  GLY GLY A . n 
A 1 104 MET 104 95  95  MET MET A . n 
A 1 105 LYS 105 96  96  LYS LYS A . n 
A 1 106 MET 106 97  97  MET MET A . n 
A 1 107 ALA 107 98  98  ALA ALA A . n 
A 1 108 THR 108 99  99  THR THR A . n 
A 1 109 ARG 109 100 100 ARG ARG A . n 
A 1 110 ALA 110 101 101 ALA ALA A . n 
A 1 111 ASN 111 102 102 ASN ASN A . n 
A 1 112 VAL 112 103 103 VAL VAL A . n 
A 1 113 ARG 113 104 104 ARG ARG A . n 
A 1 114 VAL 114 105 105 VAL VAL A . n 
A 1 115 ALA 115 106 106 ALA ALA A . n 
A 1 116 GLU 116 107 107 GLU GLU A . n 
A 1 117 ALA 117 108 108 ALA ALA A . n 
A 1 118 ALA 118 109 109 ALA ALA A . n 
A 1 119 ARG 119 110 110 ARG ARG A . n 
A 1 120 THR 120 111 111 THR THR A . n 
A 1 121 THR 121 112 112 THR THR A . n 
A 1 122 LYS 122 113 113 LYS LYS A . n 
A 1 123 LYS 123 114 114 LYS LYS A . n 
A 1 124 ILE 124 115 115 ILE ILE A . n 
A 1 125 GLY 125 116 116 GLY GLY A . n 
A 1 126 PRO 126 117 117 PRO PRO A . n 
A 1 127 ALA 127 118 118 ALA ALA A . n 
A 1 128 LEU 128 119 119 LEU LEU A . n 
A 1 129 LYS 129 120 120 LYS LYS A . n 
A 1 130 VAL 130 121 121 VAL VAL A . n 
A 1 131 ALA 131 122 122 ALA ALA A . n 
A 1 132 TYR 132 123 123 TYR TYR A . n 
A 1 133 GLN 133 124 124 GLN GLN A . n 
A 1 134 GLY 134 125 125 GLY GLY A . n 
A 1 135 GLY 135 126 126 GLY GLY A . n 
A 1 136 SER 136 127 127 SER SER A . n 
A 1 137 VAL 137 128 128 VAL VAL A . n 
A 1 138 MET 138 129 129 MET MET A . n 
A 1 139 GLY 139 130 130 GLY GLY A . n 
A 1 140 LEU 140 131 131 LEU LEU A . n 
A 1 141 SER 141 132 132 SER SER A . n 
A 1 142 VAL 142 133 133 VAL VAL A . n 
A 1 143 GLY 143 134 134 GLY GLY A . n 
A 1 144 GLY 144 135 135 GLY GLY A . n 
A 1 145 PHE 145 136 136 PHE PHE A . n 
A 1 146 ALA 146 137 137 ALA ALA A . n 
A 1 147 LEU 147 138 138 LEU LEU A . n 
A 1 148 LEU 148 139 139 LEU LEU A . n 
A 1 149 GLY 149 140 140 GLY GLY A . n 
A 1 150 LEU 150 141 141 LEU LEU A . n 
A 1 151 VAL 151 142 142 VAL VAL A . n 
A 1 152 LEU 152 143 143 LEU LEU A . n 
A 1 153 VAL 153 144 144 VAL VAL A . n 
A 1 154 TYR 154 145 145 TYR TYR A . n 
A 1 155 LEU 155 146 146 LEU LEU A . n 
A 1 156 ILE 156 147 147 ILE ILE A . n 
A 1 157 PHE 157 148 148 PHE PHE A . n 
A 1 158 GLY 158 149 149 GLY GLY A . n 
A 1 159 LYS 159 150 150 LYS LYS A . n 
A 1 160 TRP 160 151 151 TRP TRP A . n 
A 1 161 MET 161 152 152 MET MET A . n 
A 1 162 GLY 162 153 153 GLY GLY A . n 
A 1 163 GLN 163 154 154 GLN GLN A . n 
A 1 164 VAL 164 155 155 VAL VAL A . n 
A 1 165 ASP 165 156 156 ASP ASP A . n 
A 1 166 ASN 166 157 157 ASN ASN A . n 
A 1 167 LEU 167 158 158 LEU LEU A . n 
A 1 168 ASN 168 159 159 ASN ASN A . n 
A 1 169 ILE 169 160 160 ILE ILE A . n 
A 1 170 TYR 170 161 161 TYR TYR A . n 
A 1 171 THR 171 162 162 THR THR A . n 
A 1 172 ASN 172 163 163 ASN ASN A . n 
A 1 173 TRP 173 164 164 TRP TRP A . n 
A 1 174 LEU 174 165 165 LEU LEU A . n 
A 1 175 GLY 175 166 166 GLY GLY A . n 
A 1 176 ILE 176 167 167 ILE ILE A . n 
A 1 177 ASN 177 168 168 ASN ASN A . n 
A 1 178 PHE 178 169 169 PHE PHE A . n 
A 1 179 VAL 179 170 170 VAL VAL A . n 
A 1 180 PRO 180 171 171 PRO PRO A . n 
A 1 181 PHE 181 172 172 PHE PHE A . n 
A 1 182 ALA 182 173 173 ALA ALA A . n 
A 1 183 MET 183 174 174 MET MET A . n 
A 1 184 THR 184 175 175 THR THR A . n 
A 1 185 VAL 185 176 176 VAL VAL A . n 
A 1 186 SER 186 177 177 SER SER A . n 
A 1 187 GLY 187 178 178 GLY GLY A . n 
A 1 188 TYR 188 179 179 TYR TYR A . n 
A 1 189 ALA 189 180 180 ALA ALA A . n 
A 1 190 LEU 190 181 181 LEU LEU A . n 
A 1 191 GLY 191 182 182 GLY GLY A . n 
A 1 192 CYS 192 183 183 CYS CYS A . n 
A 1 193 SER 193 184 184 SER SER A . n 
A 1 194 ILE 194 185 185 ILE ILE A . n 
A 1 195 ILE 195 186 186 ILE ILE A . n 
A 1 196 ALA 196 187 187 ALA ALA A . n 
A 1 197 MET 197 188 188 MET MET A . n 
A 1 198 PHE 198 189 189 PHE PHE A . n 
A 1 199 ASP 199 190 190 ASP ASP A . n 
A 1 200 ARG 200 191 191 ARG ARG A . n 
A 1 201 VAL 201 192 192 VAL VAL A . n 
A 1 202 GLY 202 193 193 GLY GLY A . n 
A 1 203 GLY 203 194 194 GLY GLY A . n 
A 1 204 GLY 204 195 195 GLY GLY A . n 
A 1 205 VAL 205 196 196 VAL VAL A . n 
A 1 206 TYR 206 197 197 TYR TYR A . n 
A 1 207 THR 207 198 198 THR THR A . n 
A 1 208 LYS 208 199 199 LYS LYS A . n 
A 1 209 ALA 209 200 200 ALA ALA A . n 
A 1 210 ALA 210 201 201 ALA ALA A . n 
A 1 211 ASP 211 202 202 ASP ASP A . n 
A 1 212 MET 212 203 203 MET MET A . n 
A 1 213 ALA 213 204 204 ALA ALA A . n 
A 1 214 ALA 214 205 205 ALA ALA A . n 
A 1 215 ASP 215 206 206 ASP ASP A . n 
A 1 216 LEU 216 207 207 LEU LEU A . n 
A 1 217 VAL 217 208 ?   ?   ?   A . n 
A 1 218 GLY 218 209 ?   ?   ?   A . n 
A 1 219 LYS 219 210 ?   ?   ?   A . n 
A 1 220 THR 220 211 ?   ?   ?   A . n 
A 1 221 GLU 221 212 ?   ?   ?   A . n 
A 1 222 LEU 222 213 ?   ?   ?   A . n 
A 1 223 ASN 223 214 ?   ?   ?   A . n 
A 1 224 LEU 224 215 ?   ?   ?   A . n 
A 1 225 PRO 225 216 216 PRO PRO A . n 
A 1 226 GLU 226 217 217 GLU GLU A . n 
A 1 227 ASP 227 218 218 ASP ASP A . n 
A 1 228 ASP 228 219 219 ASP ASP A . n 
A 1 229 PRO 229 220 220 PRO PRO A . n 
A 1 230 ARG 230 221 221 ARG ARG A . n 
A 1 231 ASN 231 222 222 ASN ASN A . n 
A 1 232 PRO 232 223 223 PRO PRO A . n 
A 1 233 ALA 233 224 224 ALA ALA A . n 
A 1 234 THR 234 225 225 THR THR A . n 
A 1 235 ILE 235 226 226 ILE ILE A . n 
A 1 236 ALA 236 227 227 ALA ALA A . n 
A 1 237 ASP 237 228 228 ASP ASP A . n 
A 1 238 ASN 238 229 229 ASN ASN A . n 
A 1 239 VAL 239 230 230 VAL VAL A . n 
A 1 240 GLY 240 231 231 GLY GLY A . n 
A 1 241 ASP 241 232 232 ASP ASP A . n 
A 1 242 ASN 242 233 233 ASN ASN A . n 
A 1 243 VAL 243 234 234 VAL VAL A . n 
A 1 244 GLY 244 235 235 GLY GLY A . n 
A 1 245 ASP 245 236 236 ASP ASP A . n 
A 1 246 VAL 246 237 237 VAL VAL A . n 
A 1 247 ALA 247 238 238 ALA ALA A . n 
A 1 248 GLY 248 239 239 GLY GLY A . n 
A 1 249 LEU 249 240 240 LEU LEU A . n 
A 1 250 GLY 250 241 241 GLY GLY A . n 
A 1 251 ALA 251 242 242 ALA ALA A . n 
A 1 252 ASP 252 243 243 ASP ASP A . n 
A 1 253 LEU 253 244 244 LEU LEU A . n 
A 1 254 LEU 254 245 245 LEU LEU A . n 
A 1 255 GLU 255 246 246 GLU GLU A . n 
A 1 256 SER 256 247 247 SER SER A . n 
A 1 257 PHE 257 248 248 PHE PHE A . n 
A 1 258 VAL 258 249 249 VAL VAL A . n 
A 1 259 GLY 259 250 250 GLY GLY A . n 
A 1 260 ALA 260 251 251 ALA ALA A . n 
A 1 261 ILE 261 252 252 ILE ILE A . n 
A 1 262 VAL 262 253 253 VAL VAL A . n 
A 1 263 SER 263 254 254 SER SER A . n 
A 1 264 SER 264 255 255 SER SER A . n 
A 1 265 ILE 265 256 256 ILE ILE A . n 
A 1 266 ILE 266 257 257 ILE ILE A . n 
A 1 267 LEU 267 258 258 LEU LEU A . n 
A 1 268 ALA 268 259 259 ALA ALA A . n 
A 1 269 SER 269 260 260 SER SER A . n 
A 1 270 TYR 270 261 261 TYR TYR A . n 
A 1 271 MET 271 262 262 MET MET A . n 
A 1 272 PHE 272 263 263 PHE PHE A . n 
A 1 273 PRO 273 264 264 PRO PRO A . n 
A 1 274 ILE 274 265 265 ILE ILE A . n 
A 1 275 TYR 275 266 266 TYR TYR A . n 
A 1 276 VAL 276 267 267 VAL VAL A . n 
A 1 277 GLN 277 268 268 GLN GLN A . n 
A 1 278 LYS 278 269 269 LYS LYS A . n 
A 1 279 ILE 279 270 270 ILE ILE A . n 
A 1 280 GLY 280 271 271 GLY GLY A . n 
A 1 281 GLU 281 272 272 GLU GLU A . n 
A 1 282 ASN 282 273 273 ASN ASN A . n 
A 1 283 LEU 283 274 274 LEU LEU A . n 
A 1 284 VAL 284 275 275 VAL VAL A . n 
A 1 285 HIS 285 276 276 HIS HIS A . n 
A 1 286 GLN 286 277 277 GLN GLN A . n 
A 1 287 VAL 287 278 278 VAL VAL A . n 
A 1 288 PRO 288 279 279 PRO PRO A . n 
A 1 289 LYS 289 280 280 LYS LYS A . n 
A 1 290 GLU 290 281 281 GLU GLU A . n 
A 1 291 THR 291 282 282 THR THR A . n 
A 1 292 ILE 292 283 283 ILE ILE A . n 
A 1 293 GLN 293 284 284 GLN GLN A . n 
A 1 294 ALA 294 285 285 ALA ALA A . n 
A 1 295 LEU 295 286 286 LEU LEU A . n 
A 1 296 ILE 296 287 287 ILE ILE A . n 
A 1 297 SER 297 288 288 SER SER A . n 
A 1 298 TYR 298 289 289 TYR TYR A . n 
A 1 299 PRO 299 290 290 PRO PRO A . n 
A 1 300 ILE 300 291 291 ILE ILE A . n 
A 1 301 PHE 301 292 292 PHE PHE A . n 
A 1 302 PHE 302 293 293 PHE PHE A . n 
A 1 303 ALA 303 294 294 ALA ALA A . n 
A 1 304 LEU 304 295 295 LEU LEU A . n 
A 1 305 VAL 305 296 296 VAL VAL A . n 
A 1 306 GLY 306 297 297 GLY GLY A . n 
A 1 307 LEU 307 298 298 LEU LEU A . n 
A 1 308 GLY 308 299 299 GLY GLY A . n 
A 1 309 CYS 309 300 300 CYS CYS A . n 
A 1 310 SER 310 301 301 SER SER A . n 
A 1 311 MET 311 302 302 MET MET A . n 
A 1 312 LEU 312 303 303 LEU LEU A . n 
A 1 313 GLY 313 304 304 GLY GLY A . n 
A 1 314 ILE 314 305 305 ILE ILE A . n 
A 1 315 LEU 315 306 306 LEU LEU A . n 
A 1 316 TYR 316 307 307 TYR TYR A . n 
A 1 317 VAL 317 308 308 VAL VAL A . n 
A 1 318 ILE 318 309 309 ILE ILE A . n 
A 1 319 VAL 319 310 310 VAL VAL A . n 
A 1 320 LYS 320 311 311 LYS LYS A . n 
A 1 321 LYS 321 312 312 LYS LYS A . n 
A 1 322 PRO 322 313 ?   ?   ?   A . n 
A 1 323 SER 323 314 ?   ?   ?   A . n 
A 1 324 ASP 324 315 ?   ?   ?   A . n 
A 1 325 ASN 325 316 316 ASN ASN A . n 
A 1 326 PRO 326 317 317 PRO PRO A . n 
A 1 327 GLN 327 318 318 GLN GLN A . n 
A 1 328 ARG 328 319 319 ARG ARG A . n 
A 1 329 GLU 329 320 320 GLU GLU A . n 
A 1 330 LEU 330 321 321 LEU LEU A . n 
A 1 331 ASN 331 322 322 ASN ASN A . n 
A 1 332 ILE 332 323 323 ILE ILE A . n 
A 1 333 SER 333 324 324 SER SER A . n 
A 1 334 LEU 334 325 325 LEU LEU A . n 
A 1 335 TRP 335 326 326 TRP TRP A . n 
A 1 336 THR 336 327 327 THR THR A . n 
A 1 337 SER 337 328 328 SER SER A . n 
A 1 338 ALA 338 329 329 ALA ALA A . n 
A 1 339 LEU 339 330 330 LEU LEU A . n 
A 1 340 LEU 340 331 331 LEU LEU A . n 
A 1 341 THR 341 332 332 THR THR A . n 
A 1 342 VAL 342 333 333 VAL VAL A . n 
A 1 343 VAL 343 334 334 VAL VAL A . n 
A 1 344 LEU 344 335 335 LEU LEU A . n 
A 1 345 THR 345 336 336 THR THR A . n 
A 1 346 ALA 346 337 337 ALA ALA A . n 
A 1 347 PHE 347 338 338 PHE PHE A . n 
A 1 348 LEU 348 339 339 LEU LEU A . n 
A 1 349 THR 349 340 340 THR THR A . n 
A 1 350 TYR 350 341 341 TYR TYR A . n 
A 1 351 PHE 351 342 342 PHE PHE A . n 
A 1 352 TYR 352 343 343 TYR TYR A . n 
A 1 353 LEU 353 344 344 LEU LEU A . n 
A 1 354 LYS 354 345 345 LYS LYS A . n 
A 1 355 ASP 355 346 346 ASP ASP A . n 
A 1 356 LEU 356 347 347 LEU LEU A . n 
A 1 357 GLN 357 348 348 GLN GLN A . n 
A 1 358 GLY 358 349 349 GLY GLY A . n 
A 1 359 LEU 359 350 350 LEU LEU A . n 
A 1 360 ASP 360 351 351 ASP ASP A . n 
A 1 361 VAL 361 352 352 VAL VAL A . n 
A 1 362 LEU 362 353 353 LEU LEU A . n 
A 1 363 GLY 363 354 354 GLY GLY A . n 
A 1 364 PHE 364 355 355 PHE PHE A . n 
A 1 365 ARG 365 356 356 ARG ARG A . n 
A 1 366 PHE 366 357 357 PHE PHE A . n 
A 1 367 GLY 367 358 358 GLY GLY A . n 
A 1 368 ALA 368 359 359 ALA ALA A . n 
A 1 369 ILE 369 360 360 ILE ILE A . n 
A 1 370 SER 370 361 361 SER SER A . n 
A 1 371 PRO 371 362 362 PRO PRO A . n 
A 1 372 TRP 372 363 363 TRP TRP A . n 
A 1 373 PHE 373 364 364 PHE PHE A . n 
A 1 374 SER 374 365 365 SER SER A . n 
A 1 375 ALA 375 366 366 ALA ALA A . n 
A 1 376 ILE 376 367 367 ILE ILE A . n 
A 1 377 ILE 377 368 368 ILE ILE A . n 
A 1 378 GLY 378 369 369 GLY GLY A . n 
A 1 379 ILE 379 370 370 ILE ILE A . n 
A 1 380 PHE 380 371 371 PHE PHE A . n 
A 1 381 SER 381 372 372 SER SER A . n 
A 1 382 GLY 382 373 373 GLY GLY A . n 
A 1 383 ILE 383 374 374 ILE ILE A . n 
A 1 384 LEU 384 375 375 LEU LEU A . n 
A 1 385 ILE 385 376 376 ILE ILE A . n 
A 1 386 GLY 386 377 377 GLY GLY A . n 
A 1 387 PHE 387 378 378 PHE PHE A . n 
A 1 388 TRP 388 379 379 TRP TRP A . n 
A 1 389 ALA 389 380 380 ALA ALA A . n 
A 1 390 GLU 390 381 381 GLU GLU A . n 
A 1 391 TYR 391 382 382 TYR TYR A . n 
A 1 392 TYR 392 383 383 TYR TYR A . n 
A 1 393 THR 393 384 384 THR THR A . n 
A 1 394 SER 394 385 385 SER SER A . n 
A 1 395 TYR 395 386 386 TYR TYR A . n 
A 1 396 ARG 396 387 387 ARG ARG A . n 
A 1 397 TYR 397 388 388 TYR TYR A . n 
A 1 398 LYS 398 389 389 LYS LYS A . n 
A 1 399 PRO 399 390 390 PRO PRO A . n 
A 1 400 THR 400 391 391 THR THR A . n 
A 1 401 GLN 401 392 392 GLN GLN A . n 
A 1 402 PHE 402 393 393 PHE PHE A . n 
A 1 403 LEU 403 394 394 LEU LEU A . n 
A 1 404 GLY 404 395 395 GLY GLY A . n 
A 1 405 LYS 405 396 396 LYS LYS A . n 
A 1 406 SER 406 397 397 SER SER A . n 
A 1 407 SER 407 398 398 SER SER A . n 
A 1 408 ILE 408 399 399 ILE ILE A . n 
A 1 409 GLU 409 400 400 GLU GLU A . n 
A 1 410 GLY 410 401 401 GLY GLY A . n 
A 1 411 THR 411 402 402 THR THR A . n 
A 1 412 GLY 412 403 403 GLY GLY A . n 
A 1 413 MET 413 404 404 MET MET A . n 
A 1 414 VAL 414 405 405 VAL VAL A . n 
A 1 415 ILE 415 406 406 ILE ILE A . n 
A 1 416 SER 416 407 407 SER SER A . n 
A 1 417 ASN 417 408 408 ASN ASN A . n 
A 1 418 GLY 418 409 409 GLY GLY A . n 
A 1 419 LEU 419 410 410 LEU LEU A . n 
A 1 420 SER 420 411 411 SER SER A . n 
A 1 421 LEU 421 412 412 LEU LEU A . n 
A 1 422 GLY 422 413 413 GLY GLY A . n 
A 1 423 MET 423 414 414 MET MET A . n 
A 1 424 LYS 424 415 415 LYS LYS A . n 
A 1 425 SER 425 416 416 SER SER A . n 
A 1 426 VAL 426 417 417 VAL VAL A . n 
A 1 427 PHE 427 418 418 PHE PHE A . n 
A 1 428 PRO 428 419 419 PRO PRO A . n 
A 1 429 PRO 429 420 420 PRO PRO A . n 
A 1 430 THR 430 421 421 THR THR A . n 
A 1 431 LEU 431 422 422 LEU LEU A . n 
A 1 432 THR 432 423 423 THR THR A . n 
A 1 433 LEU 433 424 424 LEU LEU A . n 
A 1 434 VAL 434 425 425 VAL VAL A . n 
A 1 435 LEU 435 426 426 LEU LEU A . n 
A 1 436 GLY 436 427 427 GLY GLY A . n 
A 1 437 ILE 437 428 428 ILE ILE A . n 
A 1 438 LEU 438 429 429 LEU LEU A . n 
A 1 439 PHE 439 430 430 PHE PHE A . n 
A 1 440 ALA 440 431 431 ALA ALA A . n 
A 1 441 ASP 441 432 432 ASP ASP A . n 
A 1 442 TYR 442 433 433 TYR TYR A . n 
A 1 443 PHE 443 434 434 PHE PHE A . n 
A 1 444 ALA 444 435 435 ALA ALA A . n 
A 1 445 GLY 445 436 436 GLY GLY A . n 
A 1 446 LEU 446 437 437 LEU LEU A . n 
A 1 447 TYR 447 438 438 TYR TYR A . n 
A 1 448 GLY 448 439 439 GLY GLY A . n 
A 1 449 VAL 449 440 440 VAL VAL A . n 
A 1 450 ALA 450 441 441 ALA ALA A . n 
A 1 451 ILE 451 442 442 ILE ILE A . n 
A 1 452 ALA 452 443 443 ALA ALA A . n 
A 1 453 ALA 453 444 444 ALA ALA A . n 
A 1 454 LEU 454 445 445 LEU LEU A . n 
A 1 455 GLY 455 446 446 GLY GLY A . n 
A 1 456 MET 456 447 447 MET MET A . n 
A 1 457 LEU 457 448 448 LEU LEU A . n 
A 1 458 SER 458 449 449 SER SER A . n 
A 1 459 PHE 459 450 450 PHE PHE A . n 
A 1 460 VAL 460 451 451 VAL VAL A . n 
A 1 461 ALA 461 452 452 ALA ALA A . n 
A 1 462 THR 462 453 453 THR THR A . n 
A 1 463 SER 463 454 454 SER SER A . n 
A 1 464 VAL 464 455 455 VAL VAL A . n 
A 1 465 SER 465 456 456 SER SER A . n 
A 1 466 VAL 466 457 457 VAL VAL A . n 
A 1 467 ASP 467 458 458 ASP ASP A . n 
A 1 468 SER 468 459 459 SER SER A . n 
A 1 469 TYR 469 460 460 TYR TYR A . n 
A 1 470 GLY 470 461 461 GLY GLY A . n 
A 1 471 PRO 471 462 462 PRO PRO A . n 
A 1 472 ILE 472 463 463 ILE ILE A . n 
A 1 473 ALA 473 464 464 ALA ALA A . n 
A 1 474 ASP 474 465 465 ASP ASP A . n 
A 1 475 ASN 475 466 466 ASN ASN A . n 
A 1 476 ALA 476 467 467 ALA ALA A . n 
A 1 477 GLY 477 468 468 GLY GLY A . n 
A 1 478 GLY 478 469 469 GLY GLY A . n 
A 1 479 ILE 479 470 470 ILE ILE A . n 
A 1 480 SER 480 471 471 SER SER A . n 
A 1 481 GLU 481 472 472 GLU GLU A . n 
A 1 482 MET 482 473 473 MET MET A . n 
A 1 483 CYS 483 474 474 CYS CYS A . n 
A 1 484 GLU 484 475 475 GLU GLU A . n 
A 1 485 LEU 485 476 476 LEU LEU A . n 
A 1 486 ASP 486 477 477 ASP ASP A . n 
A 1 487 PRO 487 478 478 PRO PRO A . n 
A 1 488 GLU 488 479 479 GLU GLU A . n 
A 1 489 VAL 489 480 480 VAL VAL A . n 
A 1 490 ARG 490 481 481 ARG ARG A . n 
A 1 491 LYS 491 482 482 LYS LYS A . n 
A 1 492 ILE 492 483 483 ILE ILE A . n 
A 1 493 THR 493 484 484 THR THR A . n 
A 1 494 ASP 494 485 485 ASP ASP A . n 
A 1 495 HIS 495 486 486 HIS HIS A . n 
A 1 496 LEU 496 487 487 LEU LEU A . n 
A 1 497 ASP 497 488 488 ASP ASP A . n 
A 1 498 ALA 498 489 489 ALA ALA A . n 
A 1 499 VAL 499 490 490 VAL VAL A . n 
A 1 500 GLY 500 491 491 GLY GLY A . n 
A 1 501 ASN 501 492 492 ASN ASN A . n 
A 1 502 THR 502 493 493 THR THR A . n 
A 1 503 THR 503 494 494 THR THR A . n 
A 1 504 ALA 504 495 495 ALA ALA A . n 
A 1 505 ALA 505 496 496 ALA ALA A . n 
A 1 506 ILE 506 497 497 ILE ILE A . n 
A 1 507 GLY 507 498 498 GLY GLY A . n 
A 1 508 LYS 508 499 499 LYS LYS A . n 
A 1 509 GLY 509 500 500 GLY GLY A . n 
A 1 510 PHE 510 501 501 PHE PHE A . n 
A 1 511 ALA 511 502 502 ALA ALA A . n 
A 1 512 ILE 512 503 503 ILE ILE A . n 
A 1 513 GLY 513 504 504 GLY GLY A . n 
A 1 514 SER 514 505 505 SER SER A . n 
A 1 515 ALA 515 506 506 ALA ALA A . n 
A 1 516 ILE 516 507 507 ILE ILE A . n 
A 1 517 PHE 517 508 508 PHE PHE A . n 
A 1 518 ALA 518 509 509 ALA ALA A . n 
A 1 519 ALA 519 510 510 ALA ALA A . n 
A 1 520 LEU 520 511 511 LEU LEU A . n 
A 1 521 SER 521 512 512 SER SER A . n 
A 1 522 LEU 522 513 513 LEU LEU A . n 
A 1 523 PHE 523 514 514 PHE PHE A . n 
A 1 524 ALA 524 515 515 ALA ALA A . n 
A 1 525 SER 525 516 516 SER SER A . n 
A 1 526 TYR 526 517 517 TYR TYR A . n 
A 1 527 MET 527 518 518 MET MET A . n 
A 1 528 PHE 528 519 519 PHE PHE A . n 
A 1 529 SER 529 520 520 SER SER A . n 
A 1 530 GLN 530 521 521 GLN GLN A . n 
A 1 531 ILE 531 522 522 ILE ILE A . n 
A 1 532 SER 532 523 523 SER SER A . n 
A 1 533 PRO 533 524 524 PRO PRO A . n 
A 1 534 SER 534 525 525 SER SER A . n 
A 1 535 ASP 535 526 526 ASP ASP A . n 
A 1 536 ILE 536 527 527 ILE ILE A . n 
A 1 537 GLY 537 528 528 GLY GLY A . n 
A 1 538 LYS 538 529 529 LYS LYS A . n 
A 1 539 PRO 539 530 530 PRO PRO A . n 
A 1 540 PRO 540 531 531 PRO PRO A . n 
A 1 541 SER 541 532 532 SER SER A . n 
A 1 542 LEU 542 533 533 LEU LEU A . n 
A 1 543 VAL 543 534 534 VAL VAL A . n 
A 1 544 LEU 544 535 535 LEU LEU A . n 
A 1 545 LEU 545 536 536 LEU LEU A . n 
A 1 546 LEU 546 537 537 LEU LEU A . n 
A 1 547 ASN 547 538 538 ASN ASN A . n 
A 1 548 MET 548 539 539 MET MET A . n 
A 1 549 LEU 549 540 540 LEU LEU A . n 
A 1 550 ASP 550 541 541 ASP ASP A . n 
A 1 551 ALA 551 542 542 ALA ALA A . n 
A 1 552 ARG 552 543 543 ARG ARG A . n 
A 1 553 VAL 553 544 544 VAL VAL A . n 
A 1 554 ILE 554 545 545 ILE ILE A . n 
A 1 555 ALA 555 546 546 ALA ALA A . n 
A 1 556 GLY 556 547 547 GLY GLY A . n 
A 1 557 ALA 557 548 548 ALA ALA A . n 
A 1 558 LEU 558 549 549 LEU LEU A . n 
A 1 559 LEU 559 550 550 LEU LEU A . n 
A 1 560 GLY 560 551 551 GLY GLY A . n 
A 1 561 ALA 561 552 552 ALA ALA A . n 
A 1 562 ALA 562 553 553 ALA ALA A . n 
A 1 563 ILE 563 554 554 ILE ILE A . n 
A 1 564 THR 564 555 555 THR THR A . n 
A 1 565 TYR 565 556 556 TYR TYR A . n 
A 1 566 TYR 566 557 557 TYR TYR A . n 
A 1 567 PHE 567 558 558 PHE PHE A . n 
A 1 568 SER 568 559 559 SER SER A . n 
A 1 569 GLY 569 560 560 GLY GLY A . n 
A 1 570 TYR 570 561 561 TYR TYR A . n 
A 1 571 LEU 571 562 562 LEU LEU A . n 
A 1 572 ILE 572 563 563 ILE ILE A . n 
A 1 573 SER 573 564 564 SER SER A . n 
A 1 574 ALA 574 565 565 ALA ALA A . n 
A 1 575 VAL 575 566 566 VAL VAL A . n 
A 1 576 THR 576 567 567 THR THR A . n 
A 1 577 LYS 577 568 568 LYS LYS A . n 
A 1 578 ALA 578 569 569 ALA ALA A . n 
A 1 579 ALA 579 570 570 ALA ALA A . n 
A 1 580 MET 580 571 571 MET MET A . n 
A 1 581 LYS 581 572 572 LYS LYS A . n 
A 1 582 MET 582 573 573 MET MET A . n 
A 1 583 VAL 583 574 574 VAL VAL A . n 
A 1 584 ASP 584 575 575 ASP ASP A . n 
A 1 585 GLU 585 576 576 GLU GLU A . n 
A 1 586 ILE 586 577 577 ILE ILE A . n 
A 1 587 ARG 587 578 578 ARG ARG A . n 
A 1 588 ARG 588 579 579 ARG ARG A . n 
A 1 589 GLN 589 580 580 GLN GLN A . n 
A 1 590 ALA 590 581 581 ALA ALA A . n 
A 1 591 ARG 591 582 ?   ?   ?   A . n 
A 1 592 GLU 592 583 ?   ?   ?   A . n 
A 1 593 ILE 593 584 ?   ?   ?   A . n 
A 1 594 PRO 594 585 ?   ?   ?   A . n 
A 1 595 GLY 595 586 ?   ?   ?   A . n 
A 1 596 LEU 596 587 ?   ?   ?   A . n 
A 1 597 LEU 597 588 ?   ?   ?   A . n 
A 1 598 GLU 598 589 ?   ?   ?   A . n 
A 1 599 GLY 599 590 ?   ?   ?   A . n 
A 1 600 LYS 600 591 ?   ?   ?   A . n 
A 1 601 ALA 601 592 ?   ?   ?   A . n 
A 1 602 LYS 602 593 ?   ?   ?   A . n 
A 1 603 PRO 603 594 ?   ?   ?   A . n 
A 1 604 ASP 604 595 ?   ?   ?   A . n 
A 1 605 TYR 605 596 596 TYR TYR A . n 
A 1 606 ASN 606 597 597 ASN ASN A . n 
A 1 607 ARG 607 598 598 ARG ARG A . n 
A 1 608 CYS 608 599 599 CYS CYS A . n 
A 1 609 ILE 609 600 600 ILE ILE A . n 
A 1 610 GLU 610 601 601 GLU GLU A . n 
A 1 611 ILE 611 602 602 ILE ILE A . n 
A 1 612 THR 612 603 603 THR THR A . n 
A 1 613 SER 613 604 604 SER SER A . n 
A 1 614 ASP 614 605 605 ASP ASP A . n 
A 1 615 ASN 615 606 606 ASN ASN A . n 
A 1 616 ALA 616 607 607 ALA ALA A . n 
A 1 617 LEU 617 608 608 LEU LEU A . n 
A 1 618 LYS 618 609 609 LYS LYS A . n 
A 1 619 GLN 619 610 610 GLN GLN A . n 
A 1 620 MET 620 611 611 MET MET A . n 
A 1 621 GLY 621 612 612 GLY GLY A . n 
A 1 622 TYR 622 613 613 TYR TYR A . n 
A 1 623 PRO 623 614 614 PRO PRO A . n 
A 1 624 ALA 624 615 615 ALA ALA A . n 
A 1 625 PHE 625 616 616 PHE PHE A . n 
A 1 626 ILE 626 617 617 ILE ILE A . n 
A 1 627 ALA 627 618 618 ALA ALA A . n 
A 1 628 ILE 628 619 619 ILE ILE A . n 
A 1 629 LEU 629 620 620 LEU LEU A . n 
A 1 630 THR 630 621 621 THR THR A . n 
A 1 631 PRO 631 622 622 PRO PRO A . n 
A 1 632 LEU 632 623 623 LEU LEU A . n 
A 1 633 VAL 633 624 624 VAL VAL A . n 
A 1 634 THR 634 625 625 THR THR A . n 
A 1 635 GLY 635 626 626 GLY GLY A . n 
A 1 636 PHE 636 627 627 PHE PHE A . n 
A 1 637 LEU 637 628 628 LEU LEU A . n 
A 1 638 LEU 638 629 629 LEU LEU A . n 
A 1 639 GLY 639 630 630 GLY GLY A . n 
A 1 640 ALA 640 631 631 ALA ALA A . n 
A 1 641 GLU 641 632 632 GLU GLU A . n 
A 1 642 PHE 642 633 633 PHE PHE A . n 
A 1 643 VAL 643 634 634 VAL VAL A . n 
A 1 644 GLY 644 635 635 GLY GLY A . n 
A 1 645 GLY 645 636 636 GLY GLY A . n 
A 1 646 VAL 646 637 637 VAL VAL A . n 
A 1 647 LEU 647 638 638 LEU LEU A . n 
A 1 648 ILE 648 639 639 ILE ILE A . n 
A 1 649 GLY 649 640 640 GLY GLY A . n 
A 1 650 THR 650 641 641 THR THR A . n 
A 1 651 VAL 651 642 642 VAL VAL A . n 
A 1 652 LEU 652 643 643 LEU LEU A . n 
A 1 653 SER 653 644 644 SER SER A . n 
A 1 654 GLY 654 645 645 GLY GLY A . n 
A 1 655 ALA 655 646 646 ALA ALA A . n 
A 1 656 MET 656 647 647 MET MET A . n 
A 1 657 LEU 657 648 648 LEU LEU A . n 
A 1 658 ALA 658 649 649 ALA ALA A . n 
A 1 659 ILE 659 650 650 ILE ILE A . n 
A 1 660 LEU 660 651 651 LEU LEU A . n 
A 1 661 THR 661 652 652 THR THR A . n 
A 1 662 ALA 662 653 653 ALA ALA A . n 
A 1 663 ASN 663 654 654 ASN ASN A . n 
A 1 664 SER 664 655 655 SER SER A . n 
A 1 665 GLY 665 656 656 GLY GLY A . n 
A 1 666 GLY 666 657 657 GLY GLY A . n 
A 1 667 ALA 667 658 658 ALA ALA A . n 
A 1 668 TRP 668 659 659 TRP TRP A . n 
A 1 669 ASP 669 660 660 ASP ASP A . n 
A 1 670 ASN 670 661 661 ASN ASN A . n 
A 1 671 ALA 671 662 662 ALA ALA A . n 
A 1 672 LYS 672 663 663 LYS LYS A . n 
A 1 673 LYS 673 664 664 LYS LYS A . n 
A 1 674 TYR 674 665 665 TYR TYR A . n 
A 1 675 LEU 675 666 666 LEU LEU A . n 
A 1 676 GLU 676 667 667 GLU GLU A . n 
A 1 677 ALA 677 668 668 ALA ALA A . n 
A 1 678 GLY 678 669 669 GLY GLY A . n 
A 1 679 ASN 679 670 670 ASN ASN A . n 
A 1 680 LEU 680 671 671 LEU LEU A . n 
A 1 681 GLU 681 672 672 GLU GLU A . n 
A 1 682 GLY 682 673 673 GLY GLY A . n 
A 1 683 TYR 683 674 674 TYR TYR A . n 
A 1 684 GLY 684 675 675 GLY GLY A . n 
A 1 685 LYS 685 676 676 LYS LYS A . n 
A 1 686 GLY 686 677 677 GLY GLY A . n 
A 1 687 SER 687 678 678 SER SER A . n 
A 1 688 GLU 688 679 679 GLU GLU A . n 
A 1 689 PRO 689 680 680 PRO PRO A . n 
A 1 690 HIS 690 681 681 HIS HIS A . n 
A 1 691 LYS 691 682 682 LYS LYS A . n 
A 1 692 ALA 692 683 683 ALA ALA A . n 
A 1 693 LEU 693 684 684 LEU LEU A . n 
A 1 694 VAL 694 685 685 VAL VAL A . n 
A 1 695 ILE 695 686 686 ILE ILE A . n 
A 1 696 GLY 696 687 687 GLY GLY A . n 
A 1 697 ASP 697 688 688 ASP ASP A . n 
A 1 698 THR 698 689 689 THR THR A . n 
A 1 699 VAL 699 690 690 VAL VAL A . n 
A 1 700 GLY 700 691 691 GLY GLY A . n 
A 1 701 ASP 701 692 692 ASP ASP A . n 
A 1 702 PRO 702 693 693 PRO PRO A . n 
A 1 703 LEU 703 694 694 LEU LEU A . n 
A 1 704 LYS 704 695 695 LYS LYS A . n 
A 1 705 ASP 705 696 696 ASP ASP A . n 
A 1 706 THR 706 697 697 THR THR A . n 
A 1 707 VAL 707 698 698 VAL VAL A . n 
A 1 708 GLY 708 699 699 GLY GLY A . n 
A 1 709 PRO 709 700 700 PRO PRO A . n 
A 1 710 SER 710 701 701 SER SER A . n 
A 1 711 LEU 711 702 702 LEU LEU A . n 
A 1 712 ASP 712 703 703 ASP ASP A . n 
A 1 713 ILE 713 704 704 ILE ILE A . n 
A 1 714 LEU 714 705 705 LEU LEU A . n 
A 1 715 ILE 715 706 706 ILE ILE A . n 
A 1 716 LYS 716 707 707 LYS LYS A . n 
A 1 717 ILE 717 708 708 ILE ILE A . n 
A 1 718 MET 718 709 709 MET MET A . n 
A 1 719 SER 719 710 710 SER SER A . n 
A 1 720 VAL 720 711 711 VAL VAL A . n 
A 1 721 VAL 721 712 712 VAL VAL A . n 
A 1 722 SER 722 713 713 SER SER A . n 
A 1 723 VAL 723 714 714 VAL VAL A . n 
A 1 724 ILE 724 715 715 ILE ILE A . n 
A 1 725 ALA 725 716 716 ALA ALA A . n 
A 1 726 VAL 726 717 717 VAL VAL A . n 
A 1 727 SER 727 718 718 SER SER A . n 
A 1 728 ILE 728 719 719 ILE ILE A . n 
A 1 729 PHE 729 720 720 PHE PHE A . n 
A 1 730 LYS 730 721 721 LYS LYS A . n 
A 1 731 HIS 731 722 722 HIS HIS A . n 
A 1 732 VAL 732 723 723 VAL VAL A . n 
A 1 733 HIS 733 724 724 HIS HIS A . n 
A 1 734 LEU 734 725 725 LEU LEU A . n 
A 1 735 PHE 735 726 726 PHE PHE A . n 
B 1 1   MET 1   -8  ?   ?   ?   B . n 
B 1 2   ARG 2   -7  ?   ?   ?   B . n 
B 1 3   GLY 3   -6  ?   ?   ?   B . n 
B 1 4   SER 4   -5  ?   ?   ?   B . n 
B 1 5   HIS 5   -4  ?   ?   ?   B . n 
B 1 6   HIS 6   -3  ?   ?   ?   B . n 
B 1 7   HIS 7   -2  ?   ?   ?   B . n 
B 1 8   HIS 8   -1  ?   ?   ?   B . n 
B 1 9   HIS 9   0   ?   ?   ?   B . n 
B 1 10  HIS 10  1   ?   ?   ?   B . n 
B 1 11  TYR 11  2   ?   ?   ?   B . n 
B 1 12  VAL 12  3   3   VAL VAL B . n 
B 1 13  ALA 13  4   4   ALA ALA B . n 
B 1 14  ALA 14  5   5   ALA ALA B . n 
B 1 15  LEU 15  6   6   LEU LEU B . n 
B 1 16  PHE 16  7   7   PHE PHE B . n 
B 1 17  PHE 17  8   8   PHE PHE B . n 
B 1 18  LEU 18  9   9   LEU LEU B . n 
B 1 19  ILE 19  10  10  ILE ILE B . n 
B 1 20  PRO 20  11  11  PRO PRO B . n 
B 1 21  LEU 21  12  12  LEU LEU B . n 
B 1 22  VAL 22  13  13  VAL VAL B . n 
B 1 23  ALA 23  14  14  ALA ALA B . n 
B 1 24  LEU 24  15  15  LEU LEU B . n 
B 1 25  GLY 25  16  16  GLY GLY B . n 
B 1 26  PHE 26  17  17  PHE PHE B . n 
B 1 27  ALA 27  18  18  ALA ALA B . n 
B 1 28  ALA 28  19  19  ALA ALA B . n 
B 1 29  ALA 29  20  20  ALA ALA B . n 
B 1 30  ASN 30  21  21  ASN ASN B . n 
B 1 31  PHE 31  22  22  PHE PHE B . n 
B 1 32  ALA 32  23  23  ALA ALA B . n 
B 1 33  ALA 33  24  24  ALA ALA B . n 
B 1 34  VAL 34  25  25  VAL VAL B . n 
B 1 35  VAL 35  26  26  VAL VAL B . n 
B 1 36  ARG 36  27  27  ARG ARG B . n 
B 1 37  LYS 37  28  28  LYS LYS B . n 
B 1 38  PRO 38  29  29  PRO PRO B . n 
B 1 39  GLU 39  30  30  GLU GLU B . n 
B 1 40  GLY 40  31  ?   ?   ?   B . n 
B 1 41  THR 41  32  ?   ?   ?   B . n 
B 1 42  GLU 42  33  33  GLU GLU B . n 
B 1 43  ARG 43  34  34  ARG ARG B . n 
B 1 44  MET 44  35  35  MET MET B . n 
B 1 45  LYS 45  36  36  LYS LYS B . n 
B 1 46  GLU 46  37  37  GLU GLU B . n 
B 1 47  ILE 47  38  38  ILE ILE B . n 
B 1 48  SER 48  39  39  SER SER B . n 
B 1 49  SER 49  40  40  SER SER B . n 
B 1 50  TYR 50  41  41  TYR TYR B . n 
B 1 51  ILE 51  42  42  ILE ILE B . n 
B 1 52  ARG 52  43  43  ARG ARG B . n 
B 1 53  SER 53  44  44  SER SER B . n 
B 1 54  GLY 54  45  45  GLY GLY B . n 
B 1 55  ALA 55  46  46  ALA ALA B . n 
B 1 56  ASP 56  47  47  ASP ASP B . n 
B 1 57  SER 57  48  48  SER SER B . n 
B 1 58  PHE 58  49  49  PHE PHE B . n 
B 1 59  LEU 59  50  50  LEU LEU B . n 
B 1 60  ALA 60  51  51  ALA ALA B . n 
B 1 61  HIS 61  52  52  HIS HIS B . n 
B 1 62  GLU 62  53  53  GLU GLU B . n 
B 1 63  THR 63  54  54  THR THR B . n 
B 1 64  LYS 64  55  55  LYS LYS B . n 
B 1 65  ALA 65  56  56  ALA ALA B . n 
B 1 66  ILE 66  57  57  ILE ILE B . n 
B 1 67  PHE 67  58  58  PHE PHE B . n 
B 1 68  LYS 68  59  59  LYS LYS B . n 
B 1 69  VAL 69  60  60  VAL VAL B . n 
B 1 70  ALA 70  61  61  ALA ALA B . n 
B 1 71  ILE 71  62  62  ILE ILE B . n 
B 1 72  VAL 72  63  63  VAL VAL B . n 
B 1 73  ILE 73  64  64  ILE ILE B . n 
B 1 74  ALA 74  65  65  ALA ALA B . n 
B 1 75  ILE 75  66  66  ILE ILE B . n 
B 1 76  LEU 76  67  67  LEU LEU B . n 
B 1 77  LEU 77  68  68  LEU LEU B . n 
B 1 78  MET 78  69  69  MET MET B . n 
B 1 79  ILE 79  70  70  ILE ILE B . n 
B 1 80  PHE 80  71  71  PHE PHE B . n 
B 1 81  THR 81  72  72  THR THR B . n 
B 1 82  THR 82  73  73  THR THR B . n 
B 1 83  TRP 83  74  74  TRP TRP B . n 
B 1 84  GLN 84  75  75  GLN GLN B . n 
B 1 85  THR 85  76  76  THR THR B . n 
B 1 86  GLY 86  77  77  GLY GLY B . n 
B 1 87  VAL 87  78  78  VAL VAL B . n 
B 1 88  ALA 88  79  79  ALA ALA B . n 
B 1 89  PHE 89  80  80  PHE PHE B . n 
B 1 90  LEU 90  81  81  LEU LEU B . n 
B 1 91  LEU 91  82  82  LEU LEU B . n 
B 1 92  GLY 92  83  83  GLY GLY B . n 
B 1 93  ALA 93  84  84  ALA ALA B . n 
B 1 94  VAL 94  85  85  VAL VAL B . n 
B 1 95  MET 95  86  86  MET MET B . n 
B 1 96  SER 96  87  87  SER SER B . n 
B 1 97  ALA 97  88  88  ALA ALA B . n 
B 1 98  SER 98  89  89  SER SER B . n 
B 1 99  ALA 99  90  90  ALA ALA B . n 
B 1 100 GLY 100 91  91  GLY GLY B . n 
B 1 101 ILE 101 92  92  ILE ILE B . n 
B 1 102 VAL 102 93  93  VAL VAL B . n 
B 1 103 GLY 103 94  94  GLY GLY B . n 
B 1 104 MET 104 95  95  MET MET B . n 
B 1 105 LYS 105 96  96  LYS LYS B . n 
B 1 106 MET 106 97  97  MET MET B . n 
B 1 107 ALA 107 98  98  ALA ALA B . n 
B 1 108 THR 108 99  99  THR THR B . n 
B 1 109 ARG 109 100 100 ARG ARG B . n 
B 1 110 ALA 110 101 101 ALA ALA B . n 
B 1 111 ASN 111 102 102 ASN ASN B . n 
B 1 112 VAL 112 103 103 VAL VAL B . n 
B 1 113 ARG 113 104 104 ARG ARG B . n 
B 1 114 VAL 114 105 105 VAL VAL B . n 
B 1 115 ALA 115 106 106 ALA ALA B . n 
B 1 116 GLU 116 107 107 GLU GLU B . n 
B 1 117 ALA 117 108 108 ALA ALA B . n 
B 1 118 ALA 118 109 109 ALA ALA B . n 
B 1 119 ARG 119 110 110 ARG ARG B . n 
B 1 120 THR 120 111 111 THR THR B . n 
B 1 121 THR 121 112 112 THR THR B . n 
B 1 122 LYS 122 113 113 LYS LYS B . n 
B 1 123 LYS 123 114 ?   ?   ?   B . n 
B 1 124 ILE 124 115 115 ILE ILE B . n 
B 1 125 GLY 125 116 116 GLY GLY B . n 
B 1 126 PRO 126 117 117 PRO PRO B . n 
B 1 127 ALA 127 118 118 ALA ALA B . n 
B 1 128 LEU 128 119 119 LEU LEU B . n 
B 1 129 LYS 129 120 120 LYS LYS B . n 
B 1 130 VAL 130 121 121 VAL VAL B . n 
B 1 131 ALA 131 122 122 ALA ALA B . n 
B 1 132 TYR 132 123 123 TYR TYR B . n 
B 1 133 GLN 133 124 124 GLN GLN B . n 
B 1 134 GLY 134 125 125 GLY GLY B . n 
B 1 135 GLY 135 126 126 GLY GLY B . n 
B 1 136 SER 136 127 127 SER SER B . n 
B 1 137 VAL 137 128 128 VAL VAL B . n 
B 1 138 MET 138 129 129 MET MET B . n 
B 1 139 GLY 139 130 130 GLY GLY B . n 
B 1 140 LEU 140 131 131 LEU LEU B . n 
B 1 141 SER 141 132 132 SER SER B . n 
B 1 142 VAL 142 133 133 VAL VAL B . n 
B 1 143 GLY 143 134 134 GLY GLY B . n 
B 1 144 GLY 144 135 135 GLY GLY B . n 
B 1 145 PHE 145 136 136 PHE PHE B . n 
B 1 146 ALA 146 137 137 ALA ALA B . n 
B 1 147 LEU 147 138 138 LEU LEU B . n 
B 1 148 LEU 148 139 139 LEU LEU B . n 
B 1 149 GLY 149 140 140 GLY GLY B . n 
B 1 150 LEU 150 141 141 LEU LEU B . n 
B 1 151 VAL 151 142 142 VAL VAL B . n 
B 1 152 LEU 152 143 143 LEU LEU B . n 
B 1 153 VAL 153 144 144 VAL VAL B . n 
B 1 154 TYR 154 145 145 TYR TYR B . n 
B 1 155 LEU 155 146 146 LEU LEU B . n 
B 1 156 ILE 156 147 147 ILE ILE B . n 
B 1 157 PHE 157 148 148 PHE PHE B . n 
B 1 158 GLY 158 149 149 GLY GLY B . n 
B 1 159 LYS 159 150 150 LYS LYS B . n 
B 1 160 TRP 160 151 151 TRP TRP B . n 
B 1 161 MET 161 152 152 MET MET B . n 
B 1 162 GLY 162 153 153 GLY GLY B . n 
B 1 163 GLN 163 154 154 GLN GLN B . n 
B 1 164 VAL 164 155 155 VAL VAL B . n 
B 1 165 ASP 165 156 156 ASP ASP B . n 
B 1 166 ASN 166 157 157 ASN ASN B . n 
B 1 167 LEU 167 158 158 LEU LEU B . n 
B 1 168 ASN 168 159 159 ASN ASN B . n 
B 1 169 ILE 169 160 160 ILE ILE B . n 
B 1 170 TYR 170 161 161 TYR TYR B . n 
B 1 171 THR 171 162 162 THR THR B . n 
B 1 172 ASN 172 163 163 ASN ASN B . n 
B 1 173 TRP 173 164 164 TRP TRP B . n 
B 1 174 LEU 174 165 165 LEU LEU B . n 
B 1 175 GLY 175 166 166 GLY GLY B . n 
B 1 176 ILE 176 167 167 ILE ILE B . n 
B 1 177 ASN 177 168 168 ASN ASN B . n 
B 1 178 PHE 178 169 169 PHE PHE B . n 
B 1 179 VAL 179 170 170 VAL VAL B . n 
B 1 180 PRO 180 171 171 PRO PRO B . n 
B 1 181 PHE 181 172 172 PHE PHE B . n 
B 1 182 ALA 182 173 173 ALA ALA B . n 
B 1 183 MET 183 174 174 MET MET B . n 
B 1 184 THR 184 175 175 THR THR B . n 
B 1 185 VAL 185 176 176 VAL VAL B . n 
B 1 186 SER 186 177 177 SER SER B . n 
B 1 187 GLY 187 178 178 GLY GLY B . n 
B 1 188 TYR 188 179 179 TYR TYR B . n 
B 1 189 ALA 189 180 180 ALA ALA B . n 
B 1 190 LEU 190 181 181 LEU LEU B . n 
B 1 191 GLY 191 182 182 GLY GLY B . n 
B 1 192 CYS 192 183 183 CYS CYS B . n 
B 1 193 SER 193 184 184 SER SER B . n 
B 1 194 ILE 194 185 185 ILE ILE B . n 
B 1 195 ILE 195 186 186 ILE ILE B . n 
B 1 196 ALA 196 187 187 ALA ALA B . n 
B 1 197 MET 197 188 188 MET MET B . n 
B 1 198 PHE 198 189 189 PHE PHE B . n 
B 1 199 ASP 199 190 190 ASP ASP B . n 
B 1 200 ARG 200 191 191 ARG ARG B . n 
B 1 201 VAL 201 192 192 VAL VAL B . n 
B 1 202 GLY 202 193 193 GLY GLY B . n 
B 1 203 GLY 203 194 194 GLY GLY B . n 
B 1 204 GLY 204 195 195 GLY GLY B . n 
B 1 205 VAL 205 196 196 VAL VAL B . n 
B 1 206 TYR 206 197 197 TYR TYR B . n 
B 1 207 THR 207 198 198 THR THR B . n 
B 1 208 LYS 208 199 199 LYS LYS B . n 
B 1 209 ALA 209 200 200 ALA ALA B . n 
B 1 210 ALA 210 201 201 ALA ALA B . n 
B 1 211 ASP 211 202 202 ASP ASP B . n 
B 1 212 MET 212 203 203 MET MET B . n 
B 1 213 ALA 213 204 204 ALA ALA B . n 
B 1 214 ALA 214 205 205 ALA ALA B . n 
B 1 215 ASP 215 206 206 ASP ASP B . n 
B 1 216 LEU 216 207 207 LEU LEU B . n 
B 1 217 VAL 217 208 208 VAL VAL B . n 
B 1 218 GLY 218 209 209 GLY GLY B . n 
B 1 219 LYS 219 210 210 LYS LYS B . n 
B 1 220 THR 220 211 211 THR THR B . n 
B 1 221 GLU 221 212 212 GLU GLU B . n 
B 1 222 LEU 222 213 ?   ?   ?   B . n 
B 1 223 ASN 223 214 ?   ?   ?   B . n 
B 1 224 LEU 224 215 ?   ?   ?   B . n 
B 1 225 PRO 225 216 216 PRO PRO B . n 
B 1 226 GLU 226 217 217 GLU GLU B . n 
B 1 227 ASP 227 218 218 ASP ASP B . n 
B 1 228 ASP 228 219 219 ASP ASP B . n 
B 1 229 PRO 229 220 220 PRO PRO B . n 
B 1 230 ARG 230 221 221 ARG ARG B . n 
B 1 231 ASN 231 222 222 ASN ASN B . n 
B 1 232 PRO 232 223 223 PRO PRO B . n 
B 1 233 ALA 233 224 224 ALA ALA B . n 
B 1 234 THR 234 225 225 THR THR B . n 
B 1 235 ILE 235 226 226 ILE ILE B . n 
B 1 236 ALA 236 227 227 ALA ALA B . n 
B 1 237 ASP 237 228 228 ASP ASP B . n 
B 1 238 ASN 238 229 229 ASN ASN B . n 
B 1 239 VAL 239 230 230 VAL VAL B . n 
B 1 240 GLY 240 231 231 GLY GLY B . n 
B 1 241 ASP 241 232 232 ASP ASP B . n 
B 1 242 ASN 242 233 233 ASN ASN B . n 
B 1 243 VAL 243 234 234 VAL VAL B . n 
B 1 244 GLY 244 235 235 GLY GLY B . n 
B 1 245 ASP 245 236 236 ASP ASP B . n 
B 1 246 VAL 246 237 237 VAL VAL B . n 
B 1 247 ALA 247 238 238 ALA ALA B . n 
B 1 248 GLY 248 239 239 GLY GLY B . n 
B 1 249 LEU 249 240 240 LEU LEU B . n 
B 1 250 GLY 250 241 241 GLY GLY B . n 
B 1 251 ALA 251 242 242 ALA ALA B . n 
B 1 252 ASP 252 243 243 ASP ASP B . n 
B 1 253 LEU 253 244 244 LEU LEU B . n 
B 1 254 LEU 254 245 245 LEU LEU B . n 
B 1 255 GLU 255 246 246 GLU GLU B . n 
B 1 256 SER 256 247 247 SER SER B . n 
B 1 257 PHE 257 248 248 PHE PHE B . n 
B 1 258 VAL 258 249 249 VAL VAL B . n 
B 1 259 GLY 259 250 250 GLY GLY B . n 
B 1 260 ALA 260 251 251 ALA ALA B . n 
B 1 261 ILE 261 252 252 ILE ILE B . n 
B 1 262 VAL 262 253 253 VAL VAL B . n 
B 1 263 SER 263 254 254 SER SER B . n 
B 1 264 SER 264 255 255 SER SER B . n 
B 1 265 ILE 265 256 256 ILE ILE B . n 
B 1 266 ILE 266 257 257 ILE ILE B . n 
B 1 267 LEU 267 258 258 LEU LEU B . n 
B 1 268 ALA 268 259 259 ALA ALA B . n 
B 1 269 SER 269 260 260 SER SER B . n 
B 1 270 TYR 270 261 261 TYR TYR B . n 
B 1 271 MET 271 262 262 MET MET B . n 
B 1 272 PHE 272 263 263 PHE PHE B . n 
B 1 273 PRO 273 264 264 PRO PRO B . n 
B 1 274 ILE 274 265 265 ILE ILE B . n 
B 1 275 TYR 275 266 266 TYR TYR B . n 
B 1 276 VAL 276 267 267 VAL VAL B . n 
B 1 277 GLN 277 268 268 GLN GLN B . n 
B 1 278 LYS 278 269 269 LYS LYS B . n 
B 1 279 ILE 279 270 270 ILE ILE B . n 
B 1 280 GLY 280 271 271 GLY GLY B . n 
B 1 281 GLU 281 272 272 GLU GLU B . n 
B 1 282 ASN 282 273 273 ASN ASN B . n 
B 1 283 LEU 283 274 274 LEU LEU B . n 
B 1 284 VAL 284 275 275 VAL VAL B . n 
B 1 285 HIS 285 276 276 HIS HIS B . n 
B 1 286 GLN 286 277 277 GLN GLN B . n 
B 1 287 VAL 287 278 278 VAL VAL B . n 
B 1 288 PRO 288 279 279 PRO PRO B . n 
B 1 289 LYS 289 280 280 LYS LYS B . n 
B 1 290 GLU 290 281 281 GLU GLU B . n 
B 1 291 THR 291 282 282 THR THR B . n 
B 1 292 ILE 292 283 283 ILE ILE B . n 
B 1 293 GLN 293 284 284 GLN GLN B . n 
B 1 294 ALA 294 285 285 ALA ALA B . n 
B 1 295 LEU 295 286 286 LEU LEU B . n 
B 1 296 ILE 296 287 287 ILE ILE B . n 
B 1 297 SER 297 288 288 SER SER B . n 
B 1 298 TYR 298 289 289 TYR TYR B . n 
B 1 299 PRO 299 290 290 PRO PRO B . n 
B 1 300 ILE 300 291 291 ILE ILE B . n 
B 1 301 PHE 301 292 292 PHE PHE B . n 
B 1 302 PHE 302 293 293 PHE PHE B . n 
B 1 303 ALA 303 294 294 ALA ALA B . n 
B 1 304 LEU 304 295 295 LEU LEU B . n 
B 1 305 VAL 305 296 296 VAL VAL B . n 
B 1 306 GLY 306 297 297 GLY GLY B . n 
B 1 307 LEU 307 298 298 LEU LEU B . n 
B 1 308 GLY 308 299 299 GLY GLY B . n 
B 1 309 CYS 309 300 300 CYS CYS B . n 
B 1 310 SER 310 301 301 SER SER B . n 
B 1 311 MET 311 302 302 MET MET B . n 
B 1 312 LEU 312 303 303 LEU LEU B . n 
B 1 313 GLY 313 304 304 GLY GLY B . n 
B 1 314 ILE 314 305 305 ILE ILE B . n 
B 1 315 LEU 315 306 306 LEU LEU B . n 
B 1 316 TYR 316 307 307 TYR TYR B . n 
B 1 317 VAL 317 308 308 VAL VAL B . n 
B 1 318 ILE 318 309 309 ILE ILE B . n 
B 1 319 VAL 319 310 310 VAL VAL B . n 
B 1 320 LYS 320 311 311 LYS LYS B . n 
B 1 321 LYS 321 312 312 LYS LYS B . n 
B 1 322 PRO 322 313 313 PRO PRO B . n 
B 1 323 SER 323 314 314 SER SER B . n 
B 1 324 ASP 324 315 315 ASP ASP B . n 
B 1 325 ASN 325 316 316 ASN ASN B . n 
B 1 326 PRO 326 317 317 PRO PRO B . n 
B 1 327 GLN 327 318 318 GLN GLN B . n 
B 1 328 ARG 328 319 319 ARG ARG B . n 
B 1 329 GLU 329 320 320 GLU GLU B . n 
B 1 330 LEU 330 321 321 LEU LEU B . n 
B 1 331 ASN 331 322 322 ASN ASN B . n 
B 1 332 ILE 332 323 323 ILE ILE B . n 
B 1 333 SER 333 324 324 SER SER B . n 
B 1 334 LEU 334 325 325 LEU LEU B . n 
B 1 335 TRP 335 326 326 TRP TRP B . n 
B 1 336 THR 336 327 327 THR THR B . n 
B 1 337 SER 337 328 328 SER SER B . n 
B 1 338 ALA 338 329 329 ALA ALA B . n 
B 1 339 LEU 339 330 330 LEU LEU B . n 
B 1 340 LEU 340 331 331 LEU LEU B . n 
B 1 341 THR 341 332 332 THR THR B . n 
B 1 342 VAL 342 333 333 VAL VAL B . n 
B 1 343 VAL 343 334 334 VAL VAL B . n 
B 1 344 LEU 344 335 335 LEU LEU B . n 
B 1 345 THR 345 336 336 THR THR B . n 
B 1 346 ALA 346 337 337 ALA ALA B . n 
B 1 347 PHE 347 338 338 PHE PHE B . n 
B 1 348 LEU 348 339 339 LEU LEU B . n 
B 1 349 THR 349 340 340 THR THR B . n 
B 1 350 TYR 350 341 341 TYR TYR B . n 
B 1 351 PHE 351 342 342 PHE PHE B . n 
B 1 352 TYR 352 343 343 TYR TYR B . n 
B 1 353 LEU 353 344 344 LEU LEU B . n 
B 1 354 LYS 354 345 345 LYS LYS B . n 
B 1 355 ASP 355 346 346 ASP ASP B . n 
B 1 356 LEU 356 347 347 LEU LEU B . n 
B 1 357 GLN 357 348 348 GLN GLN B . n 
B 1 358 GLY 358 349 349 GLY GLY B . n 
B 1 359 LEU 359 350 350 LEU LEU B . n 
B 1 360 ASP 360 351 351 ASP ASP B . n 
B 1 361 VAL 361 352 352 VAL VAL B . n 
B 1 362 LEU 362 353 353 LEU LEU B . n 
B 1 363 GLY 363 354 354 GLY GLY B . n 
B 1 364 PHE 364 355 355 PHE PHE B . n 
B 1 365 ARG 365 356 356 ARG ARG B . n 
B 1 366 PHE 366 357 357 PHE PHE B . n 
B 1 367 GLY 367 358 358 GLY GLY B . n 
B 1 368 ALA 368 359 359 ALA ALA B . n 
B 1 369 ILE 369 360 360 ILE ILE B . n 
B 1 370 SER 370 361 361 SER SER B . n 
B 1 371 PRO 371 362 362 PRO PRO B . n 
B 1 372 TRP 372 363 363 TRP TRP B . n 
B 1 373 PHE 373 364 364 PHE PHE B . n 
B 1 374 SER 374 365 365 SER SER B . n 
B 1 375 ALA 375 366 366 ALA ALA B . n 
B 1 376 ILE 376 367 367 ILE ILE B . n 
B 1 377 ILE 377 368 368 ILE ILE B . n 
B 1 378 GLY 378 369 369 GLY GLY B . n 
B 1 379 ILE 379 370 370 ILE ILE B . n 
B 1 380 PHE 380 371 371 PHE PHE B . n 
B 1 381 SER 381 372 372 SER SER B . n 
B 1 382 GLY 382 373 373 GLY GLY B . n 
B 1 383 ILE 383 374 374 ILE ILE B . n 
B 1 384 LEU 384 375 375 LEU LEU B . n 
B 1 385 ILE 385 376 376 ILE ILE B . n 
B 1 386 GLY 386 377 377 GLY GLY B . n 
B 1 387 PHE 387 378 378 PHE PHE B . n 
B 1 388 TRP 388 379 379 TRP TRP B . n 
B 1 389 ALA 389 380 380 ALA ALA B . n 
B 1 390 GLU 390 381 381 GLU GLU B . n 
B 1 391 TYR 391 382 382 TYR TYR B . n 
B 1 392 TYR 392 383 383 TYR TYR B . n 
B 1 393 THR 393 384 384 THR THR B . n 
B 1 394 SER 394 385 385 SER SER B . n 
B 1 395 TYR 395 386 386 TYR TYR B . n 
B 1 396 ARG 396 387 387 ARG ARG B . n 
B 1 397 TYR 397 388 388 TYR TYR B . n 
B 1 398 LYS 398 389 389 LYS LYS B . n 
B 1 399 PRO 399 390 390 PRO PRO B . n 
B 1 400 THR 400 391 391 THR THR B . n 
B 1 401 GLN 401 392 392 GLN GLN B . n 
B 1 402 PHE 402 393 393 PHE PHE B . n 
B 1 403 LEU 403 394 394 LEU LEU B . n 
B 1 404 GLY 404 395 395 GLY GLY B . n 
B 1 405 LYS 405 396 396 LYS LYS B . n 
B 1 406 SER 406 397 397 SER SER B . n 
B 1 407 SER 407 398 398 SER SER B . n 
B 1 408 ILE 408 399 399 ILE ILE B . n 
B 1 409 GLU 409 400 400 GLU GLU B . n 
B 1 410 GLY 410 401 401 GLY GLY B . n 
B 1 411 THR 411 402 402 THR THR B . n 
B 1 412 GLY 412 403 403 GLY GLY B . n 
B 1 413 MET 413 404 404 MET MET B . n 
B 1 414 VAL 414 405 405 VAL VAL B . n 
B 1 415 ILE 415 406 406 ILE ILE B . n 
B 1 416 SER 416 407 407 SER SER B . n 
B 1 417 ASN 417 408 408 ASN ASN B . n 
B 1 418 GLY 418 409 409 GLY GLY B . n 
B 1 419 LEU 419 410 410 LEU LEU B . n 
B 1 420 SER 420 411 411 SER SER B . n 
B 1 421 LEU 421 412 412 LEU LEU B . n 
B 1 422 GLY 422 413 413 GLY GLY B . n 
B 1 423 MET 423 414 414 MET MET B . n 
B 1 424 LYS 424 415 415 LYS LYS B . n 
B 1 425 SER 425 416 416 SER SER B . n 
B 1 426 VAL 426 417 417 VAL VAL B . n 
B 1 427 PHE 427 418 418 PHE PHE B . n 
B 1 428 PRO 428 419 419 PRO PRO B . n 
B 1 429 PRO 429 420 420 PRO PRO B . n 
B 1 430 THR 430 421 421 THR THR B . n 
B 1 431 LEU 431 422 422 LEU LEU B . n 
B 1 432 THR 432 423 423 THR THR B . n 
B 1 433 LEU 433 424 424 LEU LEU B . n 
B 1 434 VAL 434 425 425 VAL VAL B . n 
B 1 435 LEU 435 426 426 LEU LEU B . n 
B 1 436 GLY 436 427 427 GLY GLY B . n 
B 1 437 ILE 437 428 428 ILE ILE B . n 
B 1 438 LEU 438 429 429 LEU LEU B . n 
B 1 439 PHE 439 430 430 PHE PHE B . n 
B 1 440 ALA 440 431 431 ALA ALA B . n 
B 1 441 ASP 441 432 432 ASP ASP B . n 
B 1 442 TYR 442 433 433 TYR TYR B . n 
B 1 443 PHE 443 434 434 PHE PHE B . n 
B 1 444 ALA 444 435 435 ALA ALA B . n 
B 1 445 GLY 445 436 436 GLY GLY B . n 
B 1 446 LEU 446 437 437 LEU LEU B . n 
B 1 447 TYR 447 438 438 TYR TYR B . n 
B 1 448 GLY 448 439 439 GLY GLY B . n 
B 1 449 VAL 449 440 440 VAL VAL B . n 
B 1 450 ALA 450 441 441 ALA ALA B . n 
B 1 451 ILE 451 442 442 ILE ILE B . n 
B 1 452 ALA 452 443 443 ALA ALA B . n 
B 1 453 ALA 453 444 444 ALA ALA B . n 
B 1 454 LEU 454 445 445 LEU LEU B . n 
B 1 455 GLY 455 446 446 GLY GLY B . n 
B 1 456 MET 456 447 447 MET MET B . n 
B 1 457 LEU 457 448 448 LEU LEU B . n 
B 1 458 SER 458 449 449 SER SER B . n 
B 1 459 PHE 459 450 450 PHE PHE B . n 
B 1 460 VAL 460 451 451 VAL VAL B . n 
B 1 461 ALA 461 452 452 ALA ALA B . n 
B 1 462 THR 462 453 453 THR THR B . n 
B 1 463 SER 463 454 454 SER SER B . n 
B 1 464 VAL 464 455 455 VAL VAL B . n 
B 1 465 SER 465 456 456 SER SER B . n 
B 1 466 VAL 466 457 457 VAL VAL B . n 
B 1 467 ASP 467 458 458 ASP ASP B . n 
B 1 468 SER 468 459 459 SER SER B . n 
B 1 469 TYR 469 460 460 TYR TYR B . n 
B 1 470 GLY 470 461 461 GLY GLY B . n 
B 1 471 PRO 471 462 462 PRO PRO B . n 
B 1 472 ILE 472 463 463 ILE ILE B . n 
B 1 473 ALA 473 464 464 ALA ALA B . n 
B 1 474 ASP 474 465 465 ASP ASP B . n 
B 1 475 ASN 475 466 466 ASN ASN B . n 
B 1 476 ALA 476 467 467 ALA ALA B . n 
B 1 477 GLY 477 468 468 GLY GLY B . n 
B 1 478 GLY 478 469 469 GLY GLY B . n 
B 1 479 ILE 479 470 470 ILE ILE B . n 
B 1 480 SER 480 471 471 SER SER B . n 
B 1 481 GLU 481 472 472 GLU GLU B . n 
B 1 482 MET 482 473 473 MET MET B . n 
B 1 483 CYS 483 474 ?   ?   ?   B . n 
B 1 484 GLU 484 475 ?   ?   ?   B . n 
B 1 485 LEU 485 476 ?   ?   ?   B . n 
B 1 486 ASP 486 477 477 ASP ASP B . n 
B 1 487 PRO 487 478 478 PRO PRO B . n 
B 1 488 GLU 488 479 479 GLU GLU B . n 
B 1 489 VAL 489 480 480 VAL VAL B . n 
B 1 490 ARG 490 481 481 ARG ARG B . n 
B 1 491 LYS 491 482 482 LYS LYS B . n 
B 1 492 ILE 492 483 483 ILE ILE B . n 
B 1 493 THR 493 484 484 THR THR B . n 
B 1 494 ASP 494 485 485 ASP ASP B . n 
B 1 495 HIS 495 486 486 HIS HIS B . n 
B 1 496 LEU 496 487 487 LEU LEU B . n 
B 1 497 ASP 497 488 488 ASP ASP B . n 
B 1 498 ALA 498 489 489 ALA ALA B . n 
B 1 499 VAL 499 490 490 VAL VAL B . n 
B 1 500 GLY 500 491 491 GLY GLY B . n 
B 1 501 ASN 501 492 492 ASN ASN B . n 
B 1 502 THR 502 493 493 THR THR B . n 
B 1 503 THR 503 494 494 THR THR B . n 
B 1 504 ALA 504 495 495 ALA ALA B . n 
B 1 505 ALA 505 496 496 ALA ALA B . n 
B 1 506 ILE 506 497 497 ILE ILE B . n 
B 1 507 GLY 507 498 498 GLY GLY B . n 
B 1 508 LYS 508 499 499 LYS LYS B . n 
B 1 509 GLY 509 500 500 GLY GLY B . n 
B 1 510 PHE 510 501 501 PHE PHE B . n 
B 1 511 ALA 511 502 502 ALA ALA B . n 
B 1 512 ILE 512 503 503 ILE ILE B . n 
B 1 513 GLY 513 504 504 GLY GLY B . n 
B 1 514 SER 514 505 505 SER SER B . n 
B 1 515 ALA 515 506 506 ALA ALA B . n 
B 1 516 ILE 516 507 507 ILE ILE B . n 
B 1 517 PHE 517 508 508 PHE PHE B . n 
B 1 518 ALA 518 509 509 ALA ALA B . n 
B 1 519 ALA 519 510 510 ALA ALA B . n 
B 1 520 LEU 520 511 511 LEU LEU B . n 
B 1 521 SER 521 512 512 SER SER B . n 
B 1 522 LEU 522 513 513 LEU LEU B . n 
B 1 523 PHE 523 514 514 PHE PHE B . n 
B 1 524 ALA 524 515 515 ALA ALA B . n 
B 1 525 SER 525 516 516 SER SER B . n 
B 1 526 TYR 526 517 517 TYR TYR B . n 
B 1 527 MET 527 518 518 MET MET B . n 
B 1 528 PHE 528 519 519 PHE PHE B . n 
B 1 529 SER 529 520 520 SER SER B . n 
B 1 530 GLN 530 521 521 GLN GLN B . n 
B 1 531 ILE 531 522 522 ILE ILE B . n 
B 1 532 SER 532 523 523 SER SER B . n 
B 1 533 PRO 533 524 524 PRO PRO B . n 
B 1 534 SER 534 525 525 SER SER B . n 
B 1 535 ASP 535 526 526 ASP ASP B . n 
B 1 536 ILE 536 527 527 ILE ILE B . n 
B 1 537 GLY 537 528 528 GLY GLY B . n 
B 1 538 LYS 538 529 529 LYS LYS B . n 
B 1 539 PRO 539 530 530 PRO PRO B . n 
B 1 540 PRO 540 531 531 PRO PRO B . n 
B 1 541 SER 541 532 532 SER SER B . n 
B 1 542 LEU 542 533 533 LEU LEU B . n 
B 1 543 VAL 543 534 534 VAL VAL B . n 
B 1 544 LEU 544 535 535 LEU LEU B . n 
B 1 545 LEU 545 536 536 LEU LEU B . n 
B 1 546 LEU 546 537 537 LEU LEU B . n 
B 1 547 ASN 547 538 538 ASN ASN B . n 
B 1 548 MET 548 539 539 MET MET B . n 
B 1 549 LEU 549 540 540 LEU LEU B . n 
B 1 550 ASP 550 541 541 ASP ASP B . n 
B 1 551 ALA 551 542 542 ALA ALA B . n 
B 1 552 ARG 552 543 543 ARG ARG B . n 
B 1 553 VAL 553 544 544 VAL VAL B . n 
B 1 554 ILE 554 545 545 ILE ILE B . n 
B 1 555 ALA 555 546 546 ALA ALA B . n 
B 1 556 GLY 556 547 547 GLY GLY B . n 
B 1 557 ALA 557 548 548 ALA ALA B . n 
B 1 558 LEU 558 549 549 LEU LEU B . n 
B 1 559 LEU 559 550 550 LEU LEU B . n 
B 1 560 GLY 560 551 551 GLY GLY B . n 
B 1 561 ALA 561 552 552 ALA ALA B . n 
B 1 562 ALA 562 553 553 ALA ALA B . n 
B 1 563 ILE 563 554 554 ILE ILE B . n 
B 1 564 THR 564 555 555 THR THR B . n 
B 1 565 TYR 565 556 556 TYR TYR B . n 
B 1 566 TYR 566 557 557 TYR TYR B . n 
B 1 567 PHE 567 558 558 PHE PHE B . n 
B 1 568 SER 568 559 559 SER SER B . n 
B 1 569 GLY 569 560 560 GLY GLY B . n 
B 1 570 TYR 570 561 561 TYR TYR B . n 
B 1 571 LEU 571 562 562 LEU LEU B . n 
B 1 572 ILE 572 563 563 ILE ILE B . n 
B 1 573 SER 573 564 564 SER SER B . n 
B 1 574 ALA 574 565 565 ALA ALA B . n 
B 1 575 VAL 575 566 566 VAL VAL B . n 
B 1 576 THR 576 567 567 THR THR B . n 
B 1 577 LYS 577 568 568 LYS LYS B . n 
B 1 578 ALA 578 569 569 ALA ALA B . n 
B 1 579 ALA 579 570 570 ALA ALA B . n 
B 1 580 MET 580 571 571 MET MET B . n 
B 1 581 LYS 581 572 572 LYS LYS B . n 
B 1 582 MET 582 573 573 MET MET B . n 
B 1 583 VAL 583 574 574 VAL VAL B . n 
B 1 584 ASP 584 575 575 ASP ASP B . n 
B 1 585 GLU 585 576 576 GLU GLU B . n 
B 1 586 ILE 586 577 577 ILE ILE B . n 
B 1 587 ARG 587 578 ?   ?   ?   B . n 
B 1 588 ARG 588 579 ?   ?   ?   B . n 
B 1 589 GLN 589 580 ?   ?   ?   B . n 
B 1 590 ALA 590 581 ?   ?   ?   B . n 
B 1 591 ARG 591 582 ?   ?   ?   B . n 
B 1 592 GLU 592 583 ?   ?   ?   B . n 
B 1 593 ILE 593 584 ?   ?   ?   B . n 
B 1 594 PRO 594 585 ?   ?   ?   B . n 
B 1 595 GLY 595 586 ?   ?   ?   B . n 
B 1 596 LEU 596 587 ?   ?   ?   B . n 
B 1 597 LEU 597 588 ?   ?   ?   B . n 
B 1 598 GLU 598 589 ?   ?   ?   B . n 
B 1 599 GLY 599 590 ?   ?   ?   B . n 
B 1 600 LYS 600 591 ?   ?   ?   B . n 
B 1 601 ALA 601 592 592 ALA ALA B . n 
B 1 602 LYS 602 593 593 LYS LYS B . n 
B 1 603 PRO 603 594 594 PRO PRO B . n 
B 1 604 ASP 604 595 595 ASP ASP B . n 
B 1 605 TYR 605 596 596 TYR TYR B . n 
B 1 606 ASN 606 597 597 ASN ASN B . n 
B 1 607 ARG 607 598 598 ARG ARG B . n 
B 1 608 CYS 608 599 599 CYS CYS B . n 
B 1 609 ILE 609 600 600 ILE ILE B . n 
B 1 610 GLU 610 601 601 GLU GLU B . n 
B 1 611 ILE 611 602 602 ILE ILE B . n 
B 1 612 THR 612 603 603 THR THR B . n 
B 1 613 SER 613 604 604 SER SER B . n 
B 1 614 ASP 614 605 605 ASP ASP B . n 
B 1 615 ASN 615 606 606 ASN ASN B . n 
B 1 616 ALA 616 607 607 ALA ALA B . n 
B 1 617 LEU 617 608 608 LEU LEU B . n 
B 1 618 LYS 618 609 609 LYS LYS B . n 
B 1 619 GLN 619 610 610 GLN GLN B . n 
B 1 620 MET 620 611 611 MET MET B . n 
B 1 621 GLY 621 612 612 GLY GLY B . n 
B 1 622 TYR 622 613 613 TYR TYR B . n 
B 1 623 PRO 623 614 614 PRO PRO B . n 
B 1 624 ALA 624 615 615 ALA ALA B . n 
B 1 625 PHE 625 616 616 PHE PHE B . n 
B 1 626 ILE 626 617 617 ILE ILE B . n 
B 1 627 ALA 627 618 618 ALA ALA B . n 
B 1 628 ILE 628 619 619 ILE ILE B . n 
B 1 629 LEU 629 620 620 LEU LEU B . n 
B 1 630 THR 630 621 621 THR THR B . n 
B 1 631 PRO 631 622 622 PRO PRO B . n 
B 1 632 LEU 632 623 623 LEU LEU B . n 
B 1 633 VAL 633 624 624 VAL VAL B . n 
B 1 634 THR 634 625 625 THR THR B . n 
B 1 635 GLY 635 626 626 GLY GLY B . n 
B 1 636 PHE 636 627 627 PHE PHE B . n 
B 1 637 LEU 637 628 628 LEU LEU B . n 
B 1 638 LEU 638 629 629 LEU LEU B . n 
B 1 639 GLY 639 630 630 GLY GLY B . n 
B 1 640 ALA 640 631 631 ALA ALA B . n 
B 1 641 GLU 641 632 632 GLU GLU B . n 
B 1 642 PHE 642 633 633 PHE PHE B . n 
B 1 643 VAL 643 634 634 VAL VAL B . n 
B 1 644 GLY 644 635 635 GLY GLY B . n 
B 1 645 GLY 645 636 636 GLY GLY B . n 
B 1 646 VAL 646 637 637 VAL VAL B . n 
B 1 647 LEU 647 638 638 LEU LEU B . n 
B 1 648 ILE 648 639 639 ILE ILE B . n 
B 1 649 GLY 649 640 640 GLY GLY B . n 
B 1 650 THR 650 641 641 THR THR B . n 
B 1 651 VAL 651 642 642 VAL VAL B . n 
B 1 652 LEU 652 643 643 LEU LEU B . n 
B 1 653 SER 653 644 644 SER SER B . n 
B 1 654 GLY 654 645 645 GLY GLY B . n 
B 1 655 ALA 655 646 646 ALA ALA B . n 
B 1 656 MET 656 647 647 MET MET B . n 
B 1 657 LEU 657 648 648 LEU LEU B . n 
B 1 658 ALA 658 649 649 ALA ALA B . n 
B 1 659 ILE 659 650 650 ILE ILE B . n 
B 1 660 LEU 660 651 651 LEU LEU B . n 
B 1 661 THR 661 652 652 THR THR B . n 
B 1 662 ALA 662 653 653 ALA ALA B . n 
B 1 663 ASN 663 654 654 ASN ASN B . n 
B 1 664 SER 664 655 655 SER SER B . n 
B 1 665 GLY 665 656 656 GLY GLY B . n 
B 1 666 GLY 666 657 657 GLY GLY B . n 
B 1 667 ALA 667 658 658 ALA ALA B . n 
B 1 668 TRP 668 659 659 TRP TRP B . n 
B 1 669 ASP 669 660 660 ASP ASP B . n 
B 1 670 ASN 670 661 661 ASN ASN B . n 
B 1 671 ALA 671 662 662 ALA ALA B . n 
B 1 672 LYS 672 663 663 LYS LYS B . n 
B 1 673 LYS 673 664 664 LYS LYS B . n 
B 1 674 TYR 674 665 665 TYR TYR B . n 
B 1 675 LEU 675 666 666 LEU LEU B . n 
B 1 676 GLU 676 667 667 GLU GLU B . n 
B 1 677 ALA 677 668 668 ALA ALA B . n 
B 1 678 GLY 678 669 669 GLY GLY B . n 
B 1 679 ASN 679 670 670 ASN ASN B . n 
B 1 680 LEU 680 671 671 LEU LEU B . n 
B 1 681 GLU 681 672 672 GLU GLU B . n 
B 1 682 GLY 682 673 ?   ?   ?   B . n 
B 1 683 TYR 683 674 ?   ?   ?   B . n 
B 1 684 GLY 684 675 ?   ?   ?   B . n 
B 1 685 LYS 685 676 676 LYS LYS B . n 
B 1 686 GLY 686 677 677 GLY GLY B . n 
B 1 687 SER 687 678 678 SER SER B . n 
B 1 688 GLU 688 679 679 GLU GLU B . n 
B 1 689 PRO 689 680 680 PRO PRO B . n 
B 1 690 HIS 690 681 681 HIS HIS B . n 
B 1 691 LYS 691 682 682 LYS LYS B . n 
B 1 692 ALA 692 683 683 ALA ALA B . n 
B 1 693 LEU 693 684 684 LEU LEU B . n 
B 1 694 VAL 694 685 685 VAL VAL B . n 
B 1 695 ILE 695 686 686 ILE ILE B . n 
B 1 696 GLY 696 687 687 GLY GLY B . n 
B 1 697 ASP 697 688 688 ASP ASP B . n 
B 1 698 THR 698 689 689 THR THR B . n 
B 1 699 VAL 699 690 690 VAL VAL B . n 
B 1 700 GLY 700 691 691 GLY GLY B . n 
B 1 701 ASP 701 692 692 ASP ASP B . n 
B 1 702 PRO 702 693 693 PRO PRO B . n 
B 1 703 LEU 703 694 694 LEU LEU B . n 
B 1 704 LYS 704 695 695 LYS LYS B . n 
B 1 705 ASP 705 696 696 ASP ASP B . n 
B 1 706 THR 706 697 697 THR THR B . n 
B 1 707 VAL 707 698 698 VAL VAL B . n 
B 1 708 GLY 708 699 699 GLY GLY B . n 
B 1 709 PRO 709 700 700 PRO PRO B . n 
B 1 710 SER 710 701 701 SER SER B . n 
B 1 711 LEU 711 702 702 LEU LEU B . n 
B 1 712 ASP 712 703 703 ASP ASP B . n 
B 1 713 ILE 713 704 704 ILE ILE B . n 
B 1 714 LEU 714 705 705 LEU LEU B . n 
B 1 715 ILE 715 706 706 ILE ILE B . n 
B 1 716 LYS 716 707 707 LYS LYS B . n 
B 1 717 ILE 717 708 708 ILE ILE B . n 
B 1 718 MET 718 709 709 MET MET B . n 
B 1 719 SER 719 710 710 SER SER B . n 
B 1 720 VAL 720 711 711 VAL VAL B . n 
B 1 721 VAL 721 712 712 VAL VAL B . n 
B 1 722 SER 722 713 713 SER SER B . n 
B 1 723 VAL 723 714 714 VAL VAL B . n 
B 1 724 ILE 724 715 715 ILE ILE B . n 
B 1 725 ALA 725 716 716 ALA ALA B . n 
B 1 726 VAL 726 717 717 VAL VAL B . n 
B 1 727 SER 727 718 718 SER SER B . n 
B 1 728 ILE 728 719 719 ILE ILE B . n 
B 1 729 PHE 729 720 720 PHE PHE B . n 
B 1 730 LYS 730 721 721 LYS LYS B . n 
B 1 731 HIS 731 722 722 HIS HIS B . n 
B 1 732 VAL 732 723 723 VAL VAL B . n 
B 1 733 HIS 733 724 724 HIS HIS B . n 
B 1 734 LEU 734 725 725 LEU LEU B . n 
B 1 735 PHE 735 726 726 PHE PHE B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 911 1 801 801 911 ETD A . 
D 3 MG  1 802 5   MG  MG  A . 
E 3 MG  1 803 7   MG  MG  A . 
F 3 MG  1 804 8   MG  MG  A . 
G 3 MG  1 805 11  MG  MG  A . 
H 4 CA  1 806 3   CA  CA  A . 
I 2 911 1 801 801 911 ETD B . 
J 5 LMT 1 802 802 LMT LMT B . 
K 5 LMT 1 803 803 LMT LMT B . 
L 3 MG  1 804 1   MG  MG  B . 
M 3 MG  1 805 6   MG  MG  B . 
N 3 MG  1 806 9   MG  MG  B . 
O 3 MG  1 807 10  MG  MG  B . 
P 3 MG  1 808 12  MG  MG  B . 
Q 4 CA  1 809 2   CA  CA  B . 
R 6 HOH 1 901 16  HOH HOH A . 
R 6 HOH 2 902 11  HOH HOH A . 
S 6 HOH 1 901 13  HOH HOH B . 
S 6 HOH 2 902 9   HOH HOH B . 
S 6 HOH 3 903 2   HOH HOH B . 
S 6 HOH 4 904 10  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 28  ? CG  ? A LYS 37  CG  
2   1 Y 1 A LYS 28  ? CD  ? A LYS 37  CD  
3   1 Y 1 A LYS 28  ? CE  ? A LYS 37  CE  
4   1 Y 1 A LYS 28  ? NZ  ? A LYS 37  NZ  
5   1 Y 1 A GLU 33  ? CG  ? A GLU 42  CG  
6   1 Y 1 A GLU 33  ? CD  ? A GLU 42  CD  
7   1 Y 1 A GLU 33  ? OE1 ? A GLU 42  OE1 
8   1 Y 1 A GLU 33  ? OE2 ? A GLU 42  OE2 
9   1 Y 1 A LYS 36  ? CG  ? A LYS 45  CG  
10  1 Y 1 A LYS 36  ? CD  ? A LYS 45  CD  
11  1 Y 1 A LYS 36  ? CE  ? A LYS 45  CE  
12  1 Y 1 A LYS 36  ? NZ  ? A LYS 45  NZ  
13  1 Y 1 A GLU 37  ? CG  ? A GLU 46  CG  
14  1 Y 1 A GLU 37  ? CD  ? A GLU 46  CD  
15  1 Y 1 A GLU 37  ? OE1 ? A GLU 46  OE1 
16  1 Y 1 A GLU 37  ? OE2 ? A GLU 46  OE2 
17  1 Y 1 A TYR 41  ? CG  ? A TYR 50  CG  
18  1 Y 1 A TYR 41  ? CD1 ? A TYR 50  CD1 
19  1 Y 1 A TYR 41  ? CD2 ? A TYR 50  CD2 
20  1 Y 1 A TYR 41  ? CE1 ? A TYR 50  CE1 
21  1 Y 1 A TYR 41  ? CE2 ? A TYR 50  CE2 
22  1 Y 1 A TYR 41  ? CZ  ? A TYR 50  CZ  
23  1 Y 1 A TYR 41  ? OH  ? A TYR 50  OH  
24  1 Y 1 A ARG 43  ? CZ  ? A ARG 52  CZ  
25  1 Y 1 A ARG 43  ? NH1 ? A ARG 52  NH1 
26  1 Y 1 A ARG 43  ? NH2 ? A ARG 52  NH2 
27  1 Y 1 A LYS 55  ? CG  ? A LYS 64  CG  
28  1 Y 1 A LYS 55  ? CD  ? A LYS 64  CD  
29  1 Y 1 A LYS 55  ? CE  ? A LYS 64  CE  
30  1 Y 1 A LYS 55  ? NZ  ? A LYS 64  NZ  
31  1 Y 1 A LYS 59  ? CG  ? A LYS 68  CG  
32  1 Y 1 A LYS 59  ? CD  ? A LYS 68  CD  
33  1 Y 1 A LYS 59  ? CE  ? A LYS 68  CE  
34  1 Y 1 A LYS 59  ? NZ  ? A LYS 68  NZ  
35  1 Y 1 A LYS 96  ? CG  ? A LYS 105 CG  
36  1 Y 1 A LYS 96  ? CD  ? A LYS 105 CD  
37  1 Y 1 A LYS 96  ? CE  ? A LYS 105 CE  
38  1 Y 1 A LYS 96  ? NZ  ? A LYS 105 NZ  
39  1 Y 1 A LYS 114 ? CG  ? A LYS 123 CG  
40  1 Y 1 A LYS 114 ? CD  ? A LYS 123 CD  
41  1 Y 1 A LYS 114 ? CE  ? A LYS 123 CE  
42  1 Y 1 A LYS 114 ? NZ  ? A LYS 123 NZ  
43  1 Y 1 A LEU 138 ? CG  ? A LEU 147 CG  
44  1 Y 1 A LEU 138 ? CD1 ? A LEU 147 CD1 
45  1 Y 1 A LEU 138 ? CD2 ? A LEU 147 CD2 
46  1 Y 1 A LYS 150 ? CG  ? A LYS 159 CG  
47  1 Y 1 A LYS 150 ? CD  ? A LYS 159 CD  
48  1 Y 1 A LYS 150 ? CE  ? A LYS 159 CE  
49  1 Y 1 A LYS 150 ? NZ  ? A LYS 159 NZ  
50  1 Y 1 A ASN 159 ? CG  ? A ASN 168 CG  
51  1 Y 1 A ASN 159 ? OD1 ? A ASN 168 OD1 
52  1 Y 1 A ASN 159 ? ND2 ? A ASN 168 ND2 
53  1 Y 1 A PHE 189 ? CG  ? A PHE 198 CG  
54  1 Y 1 A PHE 189 ? CD1 ? A PHE 198 CD1 
55  1 Y 1 A PHE 189 ? CD2 ? A PHE 198 CD2 
56  1 Y 1 A PHE 189 ? CE1 ? A PHE 198 CE1 
57  1 Y 1 A PHE 189 ? CE2 ? A PHE 198 CE2 
58  1 Y 1 A PHE 189 ? CZ  ? A PHE 198 CZ  
59  1 Y 1 A ARG 191 ? CG  ? A ARG 200 CG  
60  1 Y 1 A ARG 191 ? CD  ? A ARG 200 CD  
61  1 Y 1 A ARG 191 ? NE  ? A ARG 200 NE  
62  1 Y 1 A ARG 191 ? CZ  ? A ARG 200 CZ  
63  1 Y 1 A ARG 191 ? NH1 ? A ARG 200 NH1 
64  1 Y 1 A ARG 191 ? NH2 ? A ARG 200 NH2 
65  1 Y 1 A GLN 268 ? CG  ? A GLN 277 CG  
66  1 Y 1 A GLN 268 ? CD  ? A GLN 277 CD  
67  1 Y 1 A GLN 268 ? OE1 ? A GLN 277 OE1 
68  1 Y 1 A GLN 268 ? NE2 ? A GLN 277 NE2 
69  1 Y 1 A GLU 281 ? CG  ? A GLU 290 CG  
70  1 Y 1 A GLU 281 ? CD  ? A GLU 290 CD  
71  1 Y 1 A GLU 281 ? OE1 ? A GLU 290 OE1 
72  1 Y 1 A GLU 281 ? OE2 ? A GLU 290 OE2 
73  1 Y 1 A LEU 303 ? CG  ? A LEU 312 CG  
74  1 Y 1 A LEU 303 ? CD1 ? A LEU 312 CD1 
75  1 Y 1 A LEU 303 ? CD2 ? A LEU 312 CD2 
76  1 Y 1 A LEU 306 ? CG  ? A LEU 315 CG  
77  1 Y 1 A LEU 306 ? CD1 ? A LEU 315 CD1 
78  1 Y 1 A LEU 306 ? CD2 ? A LEU 315 CD2 
79  1 Y 1 A LYS 311 ? CE  ? A LYS 320 CE  
80  1 Y 1 A LYS 311 ? NZ  ? A LYS 320 NZ  
81  1 Y 1 A ARG 319 ? CG  ? A ARG 328 CG  
82  1 Y 1 A ARG 319 ? CD  ? A ARG 328 CD  
83  1 Y 1 A ARG 319 ? NE  ? A ARG 328 NE  
84  1 Y 1 A ARG 319 ? CZ  ? A ARG 328 CZ  
85  1 Y 1 A ARG 319 ? NH1 ? A ARG 328 NH1 
86  1 Y 1 A ARG 319 ? NH2 ? A ARG 328 NH2 
87  1 Y 1 A LYS 345 ? CG  ? A LYS 354 CG  
88  1 Y 1 A LYS 345 ? CD  ? A LYS 354 CD  
89  1 Y 1 A LYS 345 ? CE  ? A LYS 354 CE  
90  1 Y 1 A LYS 345 ? NZ  ? A LYS 354 NZ  
91  1 Y 1 A LEU 347 ? CG  ? A LEU 356 CG  
92  1 Y 1 A LEU 347 ? CD1 ? A LEU 356 CD1 
93  1 Y 1 A LEU 347 ? CD2 ? A LEU 356 CD2 
94  1 Y 1 A GLN 348 ? CG  ? A GLN 357 CG  
95  1 Y 1 A GLN 348 ? CD  ? A GLN 357 CD  
96  1 Y 1 A GLN 348 ? OE1 ? A GLN 357 OE1 
97  1 Y 1 A GLN 348 ? NE2 ? A GLN 357 NE2 
98  1 Y 1 A ASP 351 ? CG  ? A ASP 360 CG  
99  1 Y 1 A ASP 351 ? OD1 ? A ASP 360 OD1 
100 1 Y 1 A ASP 351 ? OD2 ? A ASP 360 OD2 
101 1 Y 1 A PHE 378 ? CG  ? A PHE 387 CG  
102 1 Y 1 A PHE 378 ? CD1 ? A PHE 387 CD1 
103 1 Y 1 A PHE 378 ? CD2 ? A PHE 387 CD2 
104 1 Y 1 A PHE 378 ? CE1 ? A PHE 387 CE1 
105 1 Y 1 A PHE 378 ? CE2 ? A PHE 387 CE2 
106 1 Y 1 A PHE 378 ? CZ  ? A PHE 387 CZ  
107 1 Y 1 A ARG 387 ? CG  ? A ARG 396 CG  
108 1 Y 1 A ARG 387 ? CD  ? A ARG 396 CD  
109 1 Y 1 A ARG 387 ? NE  ? A ARG 396 NE  
110 1 Y 1 A ARG 387 ? CZ  ? A ARG 396 CZ  
111 1 Y 1 A ARG 387 ? NH1 ? A ARG 396 NH1 
112 1 Y 1 A ARG 387 ? NH2 ? A ARG 396 NH2 
113 1 Y 1 A LYS 389 ? CG  ? A LYS 398 CG  
114 1 Y 1 A LYS 389 ? CD  ? A LYS 398 CD  
115 1 Y 1 A LYS 389 ? CE  ? A LYS 398 CE  
116 1 Y 1 A LYS 389 ? NZ  ? A LYS 398 NZ  
117 1 Y 1 A LYS 396 ? CG  ? A LYS 405 CG  
118 1 Y 1 A LYS 396 ? CD  ? A LYS 405 CD  
119 1 Y 1 A LYS 396 ? CE  ? A LYS 405 CE  
120 1 Y 1 A LYS 396 ? NZ  ? A LYS 405 NZ  
121 1 Y 1 A LYS 499 ? CE  ? A LYS 508 CE  
122 1 Y 1 A LYS 499 ? NZ  ? A LYS 508 NZ  
123 1 Y 1 A LYS 529 ? CG  ? A LYS 538 CG  
124 1 Y 1 A LYS 529 ? CD  ? A LYS 538 CD  
125 1 Y 1 A LYS 529 ? CE  ? A LYS 538 CE  
126 1 Y 1 A LYS 529 ? NZ  ? A LYS 538 NZ  
127 1 Y 1 A LYS 568 ? CD  ? A LYS 577 CD  
128 1 Y 1 A LYS 568 ? CE  ? A LYS 577 CE  
129 1 Y 1 A LYS 568 ? NZ  ? A LYS 577 NZ  
130 1 Y 1 A LYS 572 ? CG  ? A LYS 581 CG  
131 1 Y 1 A LYS 572 ? CD  ? A LYS 581 CD  
132 1 Y 1 A LYS 572 ? CE  ? A LYS 581 CE  
133 1 Y 1 A LYS 572 ? NZ  ? A LYS 581 NZ  
134 1 Y 1 A GLU 601 ? CG  ? A GLU 610 CG  
135 1 Y 1 A GLU 601 ? CD  ? A GLU 610 CD  
136 1 Y 1 A GLU 601 ? OE1 ? A GLU 610 OE1 
137 1 Y 1 A GLU 601 ? OE2 ? A GLU 610 OE2 
138 1 Y 1 A LYS 609 ? CG  ? A LYS 618 CG  
139 1 Y 1 A LYS 609 ? CD  ? A LYS 618 CD  
140 1 Y 1 A LYS 609 ? CE  ? A LYS 618 CE  
141 1 Y 1 A LYS 609 ? NZ  ? A LYS 618 NZ  
142 1 Y 1 A GLU 679 ? CG  ? A GLU 688 CG  
143 1 Y 1 A GLU 679 ? CD  ? A GLU 688 CD  
144 1 Y 1 A GLU 679 ? OE1 ? A GLU 688 OE1 
145 1 Y 1 A GLU 679 ? OE2 ? A GLU 688 OE2 
146 1 Y 1 B PHE 8   ? CG  ? B PHE 17  CG  
147 1 Y 1 B PHE 8   ? CD1 ? B PHE 17  CD1 
148 1 Y 1 B PHE 8   ? CD2 ? B PHE 17  CD2 
149 1 Y 1 B PHE 8   ? CE1 ? B PHE 17  CE1 
150 1 Y 1 B PHE 8   ? CE2 ? B PHE 17  CE2 
151 1 Y 1 B PHE 8   ? CZ  ? B PHE 17  CZ  
152 1 Y 1 B ARG 27  ? CG  ? B ARG 36  CG  
153 1 Y 1 B ARG 27  ? CD  ? B ARG 36  CD  
154 1 Y 1 B ARG 27  ? NE  ? B ARG 36  NE  
155 1 Y 1 B ARG 27  ? CZ  ? B ARG 36  CZ  
156 1 Y 1 B ARG 27  ? NH1 ? B ARG 36  NH1 
157 1 Y 1 B ARG 27  ? NH2 ? B ARG 36  NH2 
158 1 Y 1 B GLU 33  ? CG  ? B GLU 42  CG  
159 1 Y 1 B GLU 33  ? CD  ? B GLU 42  CD  
160 1 Y 1 B GLU 33  ? OE1 ? B GLU 42  OE1 
161 1 Y 1 B GLU 33  ? OE2 ? B GLU 42  OE2 
162 1 Y 1 B ARG 34  ? CG  ? B ARG 43  CG  
163 1 Y 1 B ARG 34  ? CD  ? B ARG 43  CD  
164 1 Y 1 B ARG 34  ? NE  ? B ARG 43  NE  
165 1 Y 1 B ARG 34  ? CZ  ? B ARG 43  CZ  
166 1 Y 1 B ARG 34  ? NH1 ? B ARG 43  NH1 
167 1 Y 1 B ARG 34  ? NH2 ? B ARG 43  NH2 
168 1 Y 1 B MET 35  ? CG  ? B MET 44  CG  
169 1 Y 1 B MET 35  ? SD  ? B MET 44  SD  
170 1 Y 1 B MET 35  ? CE  ? B MET 44  CE  
171 1 Y 1 B LYS 36  ? CG  ? B LYS 45  CG  
172 1 Y 1 B LYS 36  ? CD  ? B LYS 45  CD  
173 1 Y 1 B LYS 36  ? CE  ? B LYS 45  CE  
174 1 Y 1 B LYS 36  ? NZ  ? B LYS 45  NZ  
175 1 Y 1 B GLU 37  ? CG  ? B GLU 46  CG  
176 1 Y 1 B GLU 37  ? CD  ? B GLU 46  CD  
177 1 Y 1 B GLU 37  ? OE1 ? B GLU 46  OE1 
178 1 Y 1 B GLU 37  ? OE2 ? B GLU 46  OE2 
179 1 Y 1 B ILE 38  ? CG1 ? B ILE 47  CG1 
180 1 Y 1 B ILE 38  ? CG2 ? B ILE 47  CG2 
181 1 Y 1 B ILE 38  ? CD1 ? B ILE 47  CD1 
182 1 Y 1 B ILE 42  ? CG1 ? B ILE 51  CG1 
183 1 Y 1 B ILE 42  ? CG2 ? B ILE 51  CG2 
184 1 Y 1 B ILE 42  ? CD1 ? B ILE 51  CD1 
185 1 Y 1 B ARG 43  ? CG  ? B ARG 52  CG  
186 1 Y 1 B ARG 43  ? CD  ? B ARG 52  CD  
187 1 Y 1 B ARG 43  ? NE  ? B ARG 52  NE  
188 1 Y 1 B ARG 43  ? CZ  ? B ARG 52  CZ  
189 1 Y 1 B ARG 43  ? NH1 ? B ARG 52  NH1 
190 1 Y 1 B ARG 43  ? NH2 ? B ARG 52  NH2 
191 1 Y 1 B LYS 55  ? CG  ? B LYS 64  CG  
192 1 Y 1 B LYS 55  ? CD  ? B LYS 64  CD  
193 1 Y 1 B LYS 55  ? CE  ? B LYS 64  CE  
194 1 Y 1 B LYS 55  ? NZ  ? B LYS 64  NZ  
195 1 Y 1 B LYS 59  ? CG  ? B LYS 68  CG  
196 1 Y 1 B LYS 59  ? CD  ? B LYS 68  CD  
197 1 Y 1 B LYS 59  ? CE  ? B LYS 68  CE  
198 1 Y 1 B LYS 59  ? NZ  ? B LYS 68  NZ  
199 1 Y 1 B LYS 96  ? CG  ? B LYS 105 CG  
200 1 Y 1 B LYS 96  ? CD  ? B LYS 105 CD  
201 1 Y 1 B LYS 96  ? CE  ? B LYS 105 CE  
202 1 Y 1 B LYS 96  ? NZ  ? B LYS 105 NZ  
203 1 Y 1 B ARG 100 ? CG  ? B ARG 109 CG  
204 1 Y 1 B ARG 100 ? CD  ? B ARG 109 CD  
205 1 Y 1 B ARG 100 ? NE  ? B ARG 109 NE  
206 1 Y 1 B ARG 100 ? CZ  ? B ARG 109 CZ  
207 1 Y 1 B ARG 100 ? NH1 ? B ARG 109 NH1 
208 1 Y 1 B ARG 100 ? NH2 ? B ARG 109 NH2 
209 1 Y 1 B ARG 104 ? CG  ? B ARG 113 CG  
210 1 Y 1 B ARG 104 ? CD  ? B ARG 113 CD  
211 1 Y 1 B ARG 104 ? NE  ? B ARG 113 NE  
212 1 Y 1 B ARG 104 ? CZ  ? B ARG 113 CZ  
213 1 Y 1 B ARG 104 ? NH1 ? B ARG 113 NH1 
214 1 Y 1 B ARG 104 ? NH2 ? B ARG 113 NH2 
215 1 Y 1 B LYS 113 ? CG  ? B LYS 122 CG  
216 1 Y 1 B LYS 113 ? CD  ? B LYS 122 CD  
217 1 Y 1 B LYS 113 ? CE  ? B LYS 122 CE  
218 1 Y 1 B LYS 113 ? NZ  ? B LYS 122 NZ  
219 1 Y 1 B LEU 119 ? CG  ? B LEU 128 CG  
220 1 Y 1 B LEU 119 ? CD1 ? B LEU 128 CD1 
221 1 Y 1 B LEU 119 ? CD2 ? B LEU 128 CD2 
222 1 Y 1 B GLN 124 ? CG  ? B GLN 133 CG  
223 1 Y 1 B GLN 124 ? CD  ? B GLN 133 CD  
224 1 Y 1 B GLN 124 ? OE1 ? B GLN 133 OE1 
225 1 Y 1 B GLN 124 ? NE2 ? B GLN 133 NE2 
226 1 Y 1 B ASP 156 ? CG  ? B ASP 165 CG  
227 1 Y 1 B ASP 156 ? OD1 ? B ASP 165 OD1 
228 1 Y 1 B ASP 156 ? OD2 ? B ASP 165 OD2 
229 1 Y 1 B LEU 165 ? CG  ? B LEU 174 CG  
230 1 Y 1 B LEU 165 ? CD1 ? B LEU 174 CD1 
231 1 Y 1 B LEU 165 ? CD2 ? B LEU 174 CD2 
232 1 Y 1 B MET 262 ? CG  ? B MET 271 CG  
233 1 Y 1 B MET 262 ? SD  ? B MET 271 SD  
234 1 Y 1 B MET 262 ? CE  ? B MET 271 CE  
235 1 Y 1 B PHE 263 ? CG  ? B PHE 272 CG  
236 1 Y 1 B PHE 263 ? CD1 ? B PHE 272 CD1 
237 1 Y 1 B PHE 263 ? CD2 ? B PHE 272 CD2 
238 1 Y 1 B PHE 263 ? CE1 ? B PHE 272 CE1 
239 1 Y 1 B PHE 263 ? CE2 ? B PHE 272 CE2 
240 1 Y 1 B PHE 263 ? CZ  ? B PHE 272 CZ  
241 1 Y 1 B LYS 269 ? CE  ? B LYS 278 CE  
242 1 Y 1 B LYS 269 ? NZ  ? B LYS 278 NZ  
243 1 Y 1 B LYS 280 ? CG  ? B LYS 289 CG  
244 1 Y 1 B LYS 280 ? CD  ? B LYS 289 CD  
245 1 Y 1 B LYS 280 ? CE  ? B LYS 289 CE  
246 1 Y 1 B LYS 280 ? NZ  ? B LYS 289 NZ  
247 1 Y 1 B LEU 303 ? CG  ? B LEU 312 CG  
248 1 Y 1 B LEU 303 ? CD1 ? B LEU 312 CD1 
249 1 Y 1 B LEU 303 ? CD2 ? B LEU 312 CD2 
250 1 Y 1 B LEU 306 ? CG  ? B LEU 315 CG  
251 1 Y 1 B LEU 306 ? CD1 ? B LEU 315 CD1 
252 1 Y 1 B LEU 306 ? CD2 ? B LEU 315 CD2 
253 1 Y 1 B VAL 310 ? CG1 ? B VAL 319 CG1 
254 1 Y 1 B VAL 310 ? CG2 ? B VAL 319 CG2 
255 1 Y 1 B ASN 316 ? CG  ? B ASN 325 CG  
256 1 Y 1 B ASN 316 ? OD1 ? B ASN 325 OD1 
257 1 Y 1 B ASN 316 ? ND2 ? B ASN 325 ND2 
258 1 Y 1 B GLN 318 ? CG  ? B GLN 327 CG  
259 1 Y 1 B GLN 318 ? CD  ? B GLN 327 CD  
260 1 Y 1 B GLN 318 ? OE1 ? B GLN 327 OE1 
261 1 Y 1 B GLN 318 ? NE2 ? B GLN 327 NE2 
262 1 Y 1 B ASN 322 ? CG  ? B ASN 331 CG  
263 1 Y 1 B ASN 322 ? OD1 ? B ASN 331 OD1 
264 1 Y 1 B ASN 322 ? ND2 ? B ASN 331 ND2 
265 1 Y 1 B LYS 345 ? CG  ? B LYS 354 CG  
266 1 Y 1 B LYS 345 ? CD  ? B LYS 354 CD  
267 1 Y 1 B LYS 345 ? CE  ? B LYS 354 CE  
268 1 Y 1 B LYS 345 ? NZ  ? B LYS 354 NZ  
269 1 Y 1 B GLN 348 ? CG  ? B GLN 357 CG  
270 1 Y 1 B GLN 348 ? CD  ? B GLN 357 CD  
271 1 Y 1 B GLN 348 ? OE1 ? B GLN 357 OE1 
272 1 Y 1 B GLN 348 ? NE2 ? B GLN 357 NE2 
273 1 Y 1 B PHE 378 ? CG  ? B PHE 387 CG  
274 1 Y 1 B PHE 378 ? CD1 ? B PHE 387 CD1 
275 1 Y 1 B PHE 378 ? CD2 ? B PHE 387 CD2 
276 1 Y 1 B PHE 378 ? CE1 ? B PHE 387 CE1 
277 1 Y 1 B PHE 378 ? CE2 ? B PHE 387 CE2 
278 1 Y 1 B PHE 378 ? CZ  ? B PHE 387 CZ  
279 1 Y 1 B GLU 381 ? CG  ? B GLU 390 CG  
280 1 Y 1 B GLU 381 ? CD  ? B GLU 390 CD  
281 1 Y 1 B GLU 381 ? OE1 ? B GLU 390 OE1 
282 1 Y 1 B GLU 381 ? OE2 ? B GLU 390 OE2 
283 1 Y 1 B ARG 387 ? CG  ? B ARG 396 CG  
284 1 Y 1 B ARG 387 ? CD  ? B ARG 396 CD  
285 1 Y 1 B ARG 387 ? NE  ? B ARG 396 NE  
286 1 Y 1 B ARG 387 ? CZ  ? B ARG 396 CZ  
287 1 Y 1 B ARG 387 ? NH1 ? B ARG 396 NH1 
288 1 Y 1 B ARG 387 ? NH2 ? B ARG 396 NH2 
289 1 Y 1 B LYS 389 ? CG  ? B LYS 398 CG  
290 1 Y 1 B LYS 389 ? CD  ? B LYS 398 CD  
291 1 Y 1 B LYS 389 ? CE  ? B LYS 398 CE  
292 1 Y 1 B LYS 389 ? NZ  ? B LYS 398 NZ  
293 1 Y 1 B THR 453 ? OG1 ? B THR 462 OG1 
294 1 Y 1 B THR 453 ? CG2 ? B THR 462 CG2 
295 1 Y 1 B GLU 479 ? CG  ? B GLU 488 CG  
296 1 Y 1 B GLU 479 ? CD  ? B GLU 488 CD  
297 1 Y 1 B GLU 479 ? OE1 ? B GLU 488 OE1 
298 1 Y 1 B GLU 479 ? OE2 ? B GLU 488 OE2 
299 1 Y 1 B LYS 499 ? CG  ? B LYS 508 CG  
300 1 Y 1 B LYS 499 ? CD  ? B LYS 508 CD  
301 1 Y 1 B LYS 499 ? CE  ? B LYS 508 CE  
302 1 Y 1 B LYS 499 ? NZ  ? B LYS 508 NZ  
303 1 Y 1 B ASP 526 ? CG  ? B ASP 535 CG  
304 1 Y 1 B ASP 526 ? OD1 ? B ASP 535 OD1 
305 1 Y 1 B ASP 526 ? OD2 ? B ASP 535 OD2 
306 1 Y 1 B LYS 529 ? CG  ? B LYS 538 CG  
307 1 Y 1 B LYS 529 ? CD  ? B LYS 538 CD  
308 1 Y 1 B LYS 529 ? CE  ? B LYS 538 CE  
309 1 Y 1 B LYS 529 ? NZ  ? B LYS 538 NZ  
310 1 Y 1 B LYS 568 ? CG  ? B LYS 577 CG  
311 1 Y 1 B LYS 568 ? CD  ? B LYS 577 CD  
312 1 Y 1 B LYS 568 ? CE  ? B LYS 577 CE  
313 1 Y 1 B LYS 568 ? NZ  ? B LYS 577 NZ  
314 1 Y 1 B GLU 601 ? CG  ? B GLU 610 CG  
315 1 Y 1 B GLU 601 ? CD  ? B GLU 610 CD  
316 1 Y 1 B GLU 601 ? OE1 ? B GLU 610 OE1 
317 1 Y 1 B GLU 601 ? OE2 ? B GLU 610 OE2 
318 1 Y 1 B ASP 605 ? CG  ? B ASP 614 CG  
319 1 Y 1 B ASP 605 ? OD1 ? B ASP 614 OD1 
320 1 Y 1 B ASP 605 ? OD2 ? B ASP 614 OD2 
321 1 Y 1 B LYS 609 ? CG  ? B LYS 618 CG  
322 1 Y 1 B LYS 609 ? CD  ? B LYS 618 CD  
323 1 Y 1 B LYS 609 ? CE  ? B LYS 618 CE  
324 1 Y 1 B LYS 609 ? NZ  ? B LYS 618 NZ  
325 1 Y 1 B LYS 682 ? CG  ? B LYS 691 CG  
326 1 Y 1 B LYS 682 ? CD  ? B LYS 691 CD  
327 1 Y 1 B LYS 682 ? CE  ? B LYS 691 CE  
328 1 Y 1 B LYS 682 ? NZ  ? B LYS 691 NZ  
329 1 Y 1 B LYS 721 ? CG  ? B LYS 730 CG  
330 1 Y 1 B LYS 721 ? CD  ? B LYS 730 CD  
331 1 Y 1 B LYS 721 ? CE  ? B LYS 730 CE  
332 1 Y 1 B LYS 721 ? NZ  ? B LYS 730 NZ  
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.670 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G8K 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     83.742 
_cell.length_a_esd                 ? 
_cell.length_b                     111.663 
_cell.length_b_esd                 ? 
_cell.length_c                     105.199 
_cell.length_c_esd                 ? 
_cell.volume                       942361.255 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9G8K 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   9G8K 
_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             3.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.16 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M CaCl2, 0.1 M HEPES pH 7.0, and 33 % PEG400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-06-24 
_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   0.91587 
_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                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91587 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          109.19 
_reflns.entry_id                                       9G8K 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.15 
_reflns.d_resolution_low                               80.22 
_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                                     19273 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           91.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.099 
_reflns.pdbx_Rpim_I_all                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.098 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.15 
_reflns_shell.d_res_low                                     3.56 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             964 
_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                               7.0 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.494 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          59.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.193 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               96.54 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9G8K 
_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                            3.15 
_refine.ls_d_res_low                             80.22 
_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                     19223 
_refine.ls_number_reflns_R_free                  960 
_refine.ls_number_reflns_R_work                  18263 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    59.50 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2706 
_refine.ls_R_factor_R_free                       0.2942 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2693 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 40.7838 
_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                             ? 
_refine.overall_SU_ML                            0.5046 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.15 
_refine_hist.d_res_low                        80.22 
_refine_hist.number_atoms_solvent             6 
_refine_hist.number_atoms_total               10216 
_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        10107 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         103 
_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' ? 0.0032  ? 10406 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6919  ? 14198 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0423  ? 1734  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0048  ? 1754  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.1119 ? 3465  ? f_dihedral_angle_d ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    1.30190924348 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.15 3.31  . . 10  175  4.05  . . . . 0.3665 . . . . . . . . . . . 0.5403 
'X-RAY DIFFRACTION' 3.31 3.52  . . 37  579  13.44 . . . . 0.3546 . . . . . . . . . . . 0.5130 
'X-RAY DIFFRACTION' 3.52 3.79  . . 87  1571 35.97 . . . . 0.3158 . . . . . . . . . . . 0.3440 
'X-RAY DIFFRACTION' 3.79 4.18  . . 165 3175 73.04 . . . . 0.2811 . . . . . . . . . . . 0.3408 
'X-RAY DIFFRACTION' 4.18 4.78  . . 216 3964 90.59 . . . . 0.2541 . . . . . . . . . . . 0.3055 
'X-RAY DIFFRACTION' 4.78 6.02  . . 229 4344 99.05 . . . . 0.2918 . . . . . . . . . . . 0.3140 
'X-RAY DIFFRACTION' 6.02 80.22 . . 216 4455 99.34 . . . . 0.2553 . . . . . . . . . . . 0.2505 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   0.582622134635 
_struct_ncs_oper.matrix[1][2]   0.0240946401217 
_struct_ncs_oper.matrix[1][3]   -0.812385928331 
_struct_ncs_oper.matrix[2][1]   0.024947374407 
_struct_ncs_oper.matrix[2][2]   -0.999619637632 
_struct_ncs_oper.matrix[2][3]   -0.0117562140895 
_struct_ncs_oper.matrix[3][1]   -0.812360189044 
_struct_ncs_oper.matrix[3][2]   -0.013417465369 
_struct_ncs_oper.matrix[3][3]   -0.583001625109 
_struct_ncs_oper.vector[1]      25.4176655853 
_struct_ncs_oper.vector[2]      -26.6567174403 
_struct_ncs_oper.vector[3]      48.6725007053 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 3 through 7 or (resid 8 and (name N or name CA or name C or name O or name CB )) or resid 9 through 26 or (resid 27 through 28 and (name N or name CA or name C or name O or name CB )) or resid 29 through 30 or (resid 33 through 38 and (name N or name CA or name C or name O or name CB )) or resid 39 through 41 or (resid 42 through 43 and (name N or name CA or name C or name O or name CB )) or resid 44 through 99 or (resid 100 through 101 and (name N or name CA or name C or name O or name CB )) or resid 102 through 103 or (resid 104 and (name N or name CA or name C or name O or name CB )) or resid 105 through 112 or (resid 113 and (name N or name CA or name C or name O or name CB )) or resid 115 through 118 or (resid 119 and (name N or name CA or name C or name O or name CB )) or resid 120 through 123 or (resid 124 and (name N or name CA or name C or name O or name CB )) or resid 125 through 155 or (resid 156 and (name N or name CA or name C or name O or name CB )) or resid 157 through 164 or (resid 165 and (name N or name CA or name C or name O or name CB )) or resid 166 through 261 or (resid 262 through 263 and (name N or name CA or name C or name O or name CB )) or resid 264 through 268 or (resid 269 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 270 through 279 or (resid 280 through 281 and (name N or name CA or name C or name O or name CB )) or resid 282 through 309 or (resid 310 and (name N or name CA or name C or name O or name CB )) or resid 311 through 312 or (resid 316 and (name N or name CA or name C or name O or name CB )) or resid 317 or (resid 318 through 319 and (name N or name CA or name C or name O or name CB )) or resid 320 through 321 or (resid 322 and (name N or name CA or name C or name O or name CB )) or resid 323 through 380 or (resid 381 and (name N or name CA or name C or name O or name CB )) or resid 382 through 452 or (resid 453 and (name N or name CA or name C or name O or name CB )) or resid 454 through 473 or resid 477 through 478 or (resid 479 and (name N or name CA or name C or name O or name CB )) or resid 480 through 498 or (resid 499 and (name N or name CA or name C or name O or name CB )) or resid 500 through 525 or (resid 526 and (name N or name CA or name C or name O or name CB )) or resid 527 through 567 or (resid 568 through 570 and (name N or name CA or name C or name O or name CB )) or resid 571 through 577 or resid 596 through 604 or (resid 605 and (name N or name CA or name C or name O or name CB )) or resid 606 through 672 or resid 676 through 681 or (resid 682 through 683 and (name N or name CA or name C or name O or name CB )) or resid 684 through 720 or (resid 721 and (name N or name CA or name C or name O or name CB )) or resid 722 through 726 or resid 801))
;
ens_1 d_2 
;(chain "B" and (resid 3 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB )) or resid 29 through 40 or (resid 41 through 43 and (name N or name CA or name C or name O or name CB )) or resid 44 through 137 or (resid 138 and (name N or name CA or name C or name O or name CB )) or resid 139 through 149 or (resid 150 and (name N or name CA or name C or name O or name CB )) or resid 151 through 158 or (resid 159 and (name N or name CA or name C or name O or name CB )) or resid 160 through 188 or (resid 189 and (name N or name CA or name C or name O or name CB )) or resid 190 or (resid 191 and (name N or name CA or name C or name O or name CB )) or resid 192 through 207 or resid 216 through 267 or (resid 268 and (name N or name CA or name C or name O or name CB )) or resid 269 through 280 or (resid 281 and (name N or name CA or name C or name O or name CB )) or resid 282 through 310 or (resid 311 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 312 or resid 316 through 318 or (resid 319 and (name N or name CA or name C or name O or name CB )) or resid 320 through 346 or (resid 347 through 348 and (name N or name CA or name C or name O or name CB )) or resid 349 through 350 or (resid 351 and (name N or name CA or name C or name O or name CB )) or resid 352 through 395 or (resid 396 and (name N or name CA or name C or name O or name CB )) or resid 397 through 571 or (resid 572 and (name N or name CA or name C or name O or name CB )) or resid 573 through 577 or resid 596 through 678 or (resid 679 and (name N or name CA or name C or name O or name CB )) or resid 680 through 726 or resid 801))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 A VAL 12  . A GLU 39  . A VAL 3   A GLU 30  ? ? 
ens_1 d_1 2 A GLU 42  . A LYS 122 . A GLU 33  A LYS 113 ? ? 
ens_1 d_1 3 A ILE 124 . A MET 482 . A ILE 115 A MET 473 ? ? 
ens_1 d_1 4 A ASP 486 . A ILE 586 . A ASP 477 A ILE 577 ? ? 
ens_1 d_1 5 A TYR 605 . A GLU 681 . A TYR 596 A GLU 672 ? ? 
ens_1 d_1 6 A LYS 685 . A PHE 735 . A LYS 676 A PHE 726 ? ? 
ens_1 d_1 7 C ETD .   . C ETD .   . A ETD 801 A ETD 801 ? ? 
ens_1 d_2 1 B VAL 12  . B LEU 216 . B VAL 3   B LEU 207 ? ? 
ens_1 d_2 2 B PRO 225 . B LYS 321 . B PRO 216 B LYS 312 ? ? 
ens_1 d_2 3 B ASN 325 . B ILE 586 . B ASN 316 B ILE 577 ? ? 
ens_1 d_2 4 B TYR 605 . B PHE 735 . B TYR 596 B PHE 726 ? ? 
ens_1 d_2 5 D ETD .   . D ETD .   . B ETD 801 B ETD 801 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     9G8K 
_struct.title                        
'Structure of K+-dependent Na+-PPase from Thermotoga maritima in complex with Ca2+ and Etidronate' 
_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        9G8K 
_struct_keywords.text            'Complex, Inhibitor, enzyme, transport, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 2 ? 
J N N 5 ? 
K N N 5 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 4 ? 
R N N 6 ? 
S N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HPPA_THEMA 
_struct_ref.pdbx_db_accession          Q9S5X0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;YVAALFFLIPLVALGFAAANFAAVVRKPEGTERMKEISSYIRSGADSFLAHETKAIFKVAIVIAILLMIFTTWQTGVAFL
LGAVMSASAGIVGMKMATRANVRVAEAARTTKKIGPALKVAYQGGSVMGLSVGGFALLGLVLVYLIFGKWMGQVDNLNIY
TNWLGINFVPFAMTVSGYALGCSIIAMFDRVGGGVYTKAADMAADLVGKTELNLPEDDPRNPATIADNVGDNVGDVAGLG
ADLLESFVGAIVSSIILASYMFPIYVQKIGENLVHQVPKETIQALISYPIFFALVGLGCSMLGILYVIVKKPSDNPQREL
NISLWTSALLTVVLTAFLTYFYLKDLQGLDVVGFRFGAISPWFSAIIGIFSGILIGFWAEYYTSYRYKPTQFLSKSSIEG
TGMVISNGLSLGMKSVFPPTLTLVLGILFADYFAGLYGVAIAALGMLSFVATSVSVDSYGPIADNAGGISEMCELDPEVR
KITDHLDAVGNTTAAIGKGFAIGSAIFAALSLFASYMFSQISPSDIGKPPSLVLLLNMLDARVIAGALLGAAITYYFSGY
LISAVTKAAMKMVDEIRRQAREIPGLLEGKAKPDYNRCIEITSDNALKQMGYPAFIAILTPLVTGFLLGAEFVGGVLIGT
VLSGAMLAILTANSGGAWDNAKKYLEAGNLEGYGKGSEPHKALVIGDTVGDPLKDTVGPSLDILIKIMSVVSVIAVSIFK
HVHLF
;
_struct_ref.pdbx_align_begin           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 9G8K A 11 ? 735 ? Q9S5X0 2 ? 726 ? 2 726 
2 1 9G8K B 11 ? 735 ? Q9S5X0 2 ? 726 ? 2 726 
# 
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 9G8K MET A 1   ? UNP Q9S5X0 ?   ?   'initiating methionine' -8  1  
1 9G8K ARG A 2   ? UNP Q9S5X0 ?   ?   'expression tag'        -7  2  
1 9G8K GLY A 3   ? UNP Q9S5X0 ?   ?   'expression tag'        -6  3  
1 9G8K SER A 4   ? UNP Q9S5X0 ?   ?   'expression tag'        -5  4  
1 9G8K HIS A 5   ? UNP Q9S5X0 ?   ?   'expression tag'        -4  5  
1 9G8K HIS A 6   ? UNP Q9S5X0 ?   ?   'expression tag'        -3  6  
1 9G8K HIS A 7   ? UNP Q9S5X0 ?   ?   'expression tag'        -2  7  
1 9G8K HIS A 8   ? UNP Q9S5X0 ?   ?   'expression tag'        -1  8  
1 9G8K HIS A 9   ? UNP Q9S5X0 ?   ?   'expression tag'        0   9  
1 9G8K HIS A 10  ? UNP Q9S5X0 ?   ?   'expression tag'        1   10 
1 9G8K LEU A 362 ? UNP Q9S5X0 VAL 353 'engineered mutation'   353 11 
1 9G8K GLY A 404 ? UNP Q9S5X0 SER 395 'engineered mutation'   395 12 
2 9G8K MET B 1   ? UNP Q9S5X0 ?   ?   'initiating methionine' -8  13 
2 9G8K ARG B 2   ? UNP Q9S5X0 ?   ?   'expression tag'        -7  14 
2 9G8K GLY B 3   ? UNP Q9S5X0 ?   ?   'expression tag'        -6  15 
2 9G8K SER B 4   ? UNP Q9S5X0 ?   ?   'expression tag'        -5  16 
2 9G8K HIS B 5   ? UNP Q9S5X0 ?   ?   'expression tag'        -4  17 
2 9G8K HIS B 6   ? UNP Q9S5X0 ?   ?   'expression tag'        -3  18 
2 9G8K HIS B 7   ? UNP Q9S5X0 ?   ?   'expression tag'        -2  19 
2 9G8K HIS B 8   ? UNP Q9S5X0 ?   ?   'expression tag'        -1  20 
2 9G8K HIS B 9   ? UNP Q9S5X0 ?   ?   'expression tag'        0   21 
2 9G8K HIS B 10  ? UNP Q9S5X0 ?   ?   'expression tag'        1   22 
2 9G8K LEU B 362 ? UNP Q9S5X0 VAL 353 'engineered mutation'   353 23 
2 9G8K GLY B 404 ? UNP Q9S5X0 SER 395 'engineered mutation'   395 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 7730  ? 
1 MORE         -190  ? 
1 'SSA (A^2)'  44850 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 ALA A 13  ? LEU A 18  ? ALA A 4   LEU A 9   1 ? 6  
HELX_P HELX_P2  AA2 LEU A 18  ? LYS A 37  ? LEU A 9   LYS A 28  1 ? 20 
HELX_P HELX_P3  AA3 THR A 41  ? THR A 81  ? THR A 32  THR A 72  1 ? 41 
HELX_P HELX_P4  AA4 THR A 82  ? ARG A 109 ? THR A 73  ARG A 100 1 ? 28 
HELX_P HELX_P5  AA5 ALA A 110 ? LYS A 122 ? ALA A 101 LYS A 113 1 ? 13 
HELX_P HELX_P6  AA6 LYS A 123 ? PHE A 157 ? LYS A 114 PHE A 148 1 ? 35 
HELX_P HELX_P7  AA7 GLY A 162 ? LEU A 167 ? GLY A 153 LEU A 158 1 ? 6  
HELX_P HELX_P8  AA8 VAL A 179 ? LEU A 216 ? VAL A 170 LEU A 207 1 ? 38 
HELX_P HELX_P9  AA9 ASN A 231 ? VAL A 246 ? ASN A 222 VAL A 237 1 ? 16 
HELX_P HELX_P10 AB1 ALA A 247 ? TYR A 275 ? ALA A 238 TYR A 266 1 ? 29 
HELX_P HELX_P11 AB2 LYS A 278 ? ASN A 282 ? LYS A 269 ASN A 273 5 ? 5  
HELX_P HELX_P12 AB3 PRO A 288 ? LYS A 320 ? PRO A 279 LYS A 311 1 ? 33 
HELX_P HELX_P13 AB4 PRO A 326 ? LEU A 353 ? PRO A 317 LEU A 344 1 ? 28 
HELX_P HELX_P14 AB5 GLY A 358 ? GLY A 363 ? GLY A 349 GLY A 354 1 ? 6  
HELX_P HELX_P15 AB6 ILE A 369 ? SER A 394 ? ILE A 360 SER A 385 1 ? 26 
HELX_P HELX_P16 AB7 TYR A 397 ? SER A 407 ? TYR A 388 SER A 398 1 ? 11 
HELX_P HELX_P17 AB8 GLY A 410 ? VAL A 426 ? GLY A 401 VAL A 417 1 ? 17 
HELX_P HELX_P18 AB9 VAL A 426 ? LEU A 457 ? VAL A 417 LEU A 448 1 ? 32 
HELX_P HELX_P19 AC1 PHE A 459 ? MET A 482 ? PHE A 450 MET A 473 1 ? 24 
HELX_P HELX_P20 AC2 ASP A 486 ? GLN A 530 ? ASP A 477 GLN A 521 1 ? 45 
HELX_P HELX_P21 AC3 PRO A 533 ? GLY A 537 ? PRO A 524 GLY A 528 5 ? 5  
HELX_P HELX_P22 AC4 PRO A 539 ? LEU A 544 ? PRO A 530 LEU A 535 1 ? 6  
HELX_P HELX_P23 AC5 ASP A 550 ? GLN A 589 ? ASP A 541 GLN A 580 1 ? 40 
HELX_P HELX_P24 AC6 ASN A 606 ? LEU A 638 ? ASN A 597 LEU A 629 1 ? 33 
HELX_P HELX_P25 AC7 GLY A 639 ? ALA A 677 ? GLY A 630 ALA A 668 1 ? 39 
HELX_P HELX_P26 AC8 SER A 687 ? THR A 706 ? SER A 678 THR A 697 1 ? 20 
HELX_P HELX_P27 AC9 THR A 706 ? LYS A 730 ? THR A 697 LYS A 721 1 ? 25 
HELX_P HELX_P28 AD1 ALA B 13  ? PHE B 17  ? ALA B 4   PHE B 8   1 ? 5  
HELX_P HELX_P29 AD2 PHE B 17  ? LYS B 37  ? PHE B 8   LYS B 28  1 ? 21 
HELX_P HELX_P30 AD3 ARG B 43  ? THR B 81  ? ARG B 34  THR B 72  1 ? 39 
HELX_P HELX_P31 AD4 THR B 82  ? ARG B 109 ? THR B 73  ARG B 100 1 ? 28 
HELX_P HELX_P32 AD5 ALA B 110 ? LYS B 122 ? ALA B 101 LYS B 113 1 ? 13 
HELX_P HELX_P33 AD6 GLY B 125 ? PHE B 157 ? GLY B 116 PHE B 148 1 ? 33 
HELX_P HELX_P34 AD7 GLY B 162 ? LEU B 167 ? GLY B 153 LEU B 158 1 ? 6  
HELX_P HELX_P35 AD8 VAL B 179 ? GLU B 221 ? VAL B 170 GLU B 212 1 ? 43 
HELX_P HELX_P36 AD9 ASN B 231 ? VAL B 246 ? ASN B 222 VAL B 237 1 ? 16 
HELX_P HELX_P37 AE1 VAL B 246 ? TYR B 275 ? VAL B 237 TYR B 266 1 ? 30 
HELX_P HELX_P38 AE2 PRO B 288 ? LYS B 320 ? PRO B 279 LYS B 311 1 ? 33 
HELX_P HELX_P39 AE3 ASN B 325 ? LEU B 353 ? ASN B 316 LEU B 344 1 ? 29 
HELX_P HELX_P40 AE4 GLY B 358 ? GLY B 363 ? GLY B 349 GLY B 354 1 ? 6  
HELX_P HELX_P41 AE5 ILE B 369 ? SER B 394 ? ILE B 360 SER B 385 1 ? 26 
HELX_P HELX_P42 AE6 TYR B 397 ? SER B 407 ? TYR B 388 SER B 398 1 ? 11 
HELX_P HELX_P43 AE7 GLY B 410 ? VAL B 426 ? GLY B 401 VAL B 417 1 ? 17 
HELX_P HELX_P44 AE8 VAL B 426 ? LEU B 457 ? VAL B 417 LEU B 448 1 ? 32 
HELX_P HELX_P45 AE9 PHE B 459 ? MET B 482 ? PHE B 450 MET B 473 1 ? 24 
HELX_P HELX_P46 AF1 PRO B 487 ? GLN B 530 ? PRO B 478 GLN B 521 1 ? 44 
HELX_P HELX_P47 AF2 SER B 532 ? GLY B 537 ? SER B 523 GLY B 528 5 ? 6  
HELX_P HELX_P48 AF3 PRO B 539 ? LEU B 544 ? PRO B 530 LEU B 535 1 ? 6  
HELX_P HELX_P49 AF4 ASP B 550 ? GLU B 585 ? ASP B 541 GLU B 576 1 ? 36 
HELX_P HELX_P50 AF5 CYS B 608 ? MET B 620 ? CYS B 599 MET B 611 1 ? 13 
HELX_P HELX_P51 AF6 MET B 620 ? LEU B 638 ? MET B 611 LEU B 629 1 ? 19 
HELX_P HELX_P52 AF7 GLY B 639 ? GLY B 678 ? GLY B 630 GLY B 669 1 ? 40 
HELX_P HELX_P53 AF8 SER B 687 ? THR B 706 ? SER B 678 THR B 697 1 ? 20 
HELX_P HELX_P54 AF9 THR B 706 ? LYS B 730 ? THR B 697 LYS B 721 1 ? 25 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 211 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASP 202 A MG  802 1_555 ? ? ? ? ? ? ? 2.434 ? ? 
metalc2  metalc ? ? A ASP 211 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 202 A MG  802 1_555 ? ? ? ? ? ? ? 1.973 ? ? 
metalc3  metalc ? ? A GLU 226 O   ? ? ? 1_555 G MG  . MG ? ? A GLU 217 A MG  805 1_555 ? ? ? ? ? ? ? 2.780 ? ? 
metalc4  metalc ? ? A GLU 226 OE2 ? ? ? 1_555 G MG  . MG ? ? A GLU 217 A MG  805 1_555 ? ? ? ? ? ? ? 2.745 ? ? 
metalc5  metalc ? ? A ASP 237 OD2 ? ? ? 1_555 F MG  . MG ? ? A ASP 228 A MG  804 1_555 ? ? ? ? ? ? ? 2.364 ? ? 
metalc6  metalc ? ? A ASP 241 OD1 ? ? ? 1_555 E MG  . MG ? ? A ASP 232 A MG  803 1_555 ? ? ? ? ? ? ? 2.709 ? ? 
metalc7  metalc ? ? A ASP 241 OD2 ? ? ? 1_555 F MG  . MG ? ? A ASP 232 A MG  804 1_555 ? ? ? ? ? ? ? 2.652 ? ? 
metalc8  metalc ? ? A ASP 701 OD1 ? ? ? 1_555 H CA  . CA ? ? A ASP 692 A CA  806 1_555 ? ? ? ? ? ? ? 3.159 ? ? 
metalc9  metalc ? ? C 911 .   O2  ? ? ? 1_555 E MG  . MG ? ? A 911 801 A MG  803 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc10 metalc ? ? C 911 .   O3  ? ? ? 1_555 E MG  . MG ? ? A 911 801 A MG  803 1_555 ? ? ? ? ? ? ? 2.538 ? ? 
metalc11 metalc ? ? C 911 .   O5  ? ? ? 1_555 E MG  . MG ? ? A 911 801 A MG  803 1_555 ? ? ? ? ? ? ? 2.997 ? ? 
metalc12 metalc ? ? C 911 .   O3  ? ? ? 1_555 F MG  . MG ? ? A 911 801 A MG  804 1_555 ? ? ? ? ? ? ? 2.391 ? ? 
metalc13 metalc ? ? C 911 .   O10 ? ? ? 1_555 G MG  . MG ? ? A 911 801 A MG  805 1_555 ? ? ? ? ? ? ? 2.618 ? ? 
metalc14 metalc ? ? C 911 .   O14 ? ? ? 1_555 H CA  . CA ? ? A 911 801 A CA  806 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc15 metalc ? ? H CA  .   CA  ? ? ? 1_555 R HOH . O  ? ? A CA  806 A HOH 901 1_555 ? ? ? ? ? ? ? 2.250 ? ? 
metalc16 metalc ? ? B ASP 227 OD2 ? ? ? 1_555 O MG  . MG ? ? B ASP 218 B MG  807 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
metalc17 metalc ? ? B ASP 241 OD1 ? ? ? 1_555 N MG  . MG ? ? B ASP 232 B MG  806 1_555 ? ? ? ? ? ? ? 2.780 ? ? 
metalc18 metalc ? ? B ASP 474 OD1 ? ? ? 1_555 L MG  . MG ? ? B ASP 465 B MG  804 1_555 ? ? ? ? ? ? ? 2.514 ? ? 
metalc19 metalc ? ? B ASP 474 OD2 ? ? ? 1_555 L MG  . MG ? ? B ASP 465 B MG  804 1_555 ? ? ? ? ? ? ? 2.396 ? ? 
metalc20 metalc ? ? B ASP 669 OD1 ? ? ? 1_555 Q CA  . CA ? ? B ASP 660 B CA  809 1_555 ? ? ? ? ? ? ? 2.620 ? ? 
metalc21 metalc ? ? B ASP 701 OD2 ? ? ? 1_555 M MG  . MG ? ? B ASP 692 B MG  805 1_555 ? ? ? ? ? ? ? 2.774 ? ? 
metalc22 metalc ? ? B ASP 701 OD1 ? ? ? 1_555 Q CA  . CA ? ? B ASP 692 B CA  809 1_555 ? ? ? ? ? ? ? 2.952 ? ? 
metalc23 metalc ? ? I 911 .   O3  ? ? ? 1_555 L MG  . MG ? ? B 911 801 B MG  804 1_555 ? ? ? ? ? ? ? 2.865 ? ? 
metalc24 metalc ? ? I 911 .   O2  ? ? ? 1_555 M MG  . MG ? ? B 911 801 B MG  805 1_555 ? ? ? ? ? ? ? 2.547 ? ? 
metalc25 metalc ? ? I 911 .   O9  ? ? ? 1_555 M MG  . MG ? ? B 911 801 B MG  805 1_555 ? ? ? ? ? ? ? 2.463 ? ? 
metalc26 metalc ? ? I 911 .   O3  ? ? ? 1_555 N MG  . MG ? ? B 911 801 B MG  806 1_555 ? ? ? ? ? ? ? 2.535 ? ? 
metalc27 metalc ? ? I 911 .   O5  ? ? ? 1_555 N MG  . MG ? ? B 911 801 B MG  806 1_555 ? ? ? ? ? ? ? 2.658 ? ? 
metalc28 metalc ? ? I 911 .   O9  ? ? ? 1_555 O MG  . MG ? ? B 911 801 B MG  807 1_555 ? ? ? ? ? ? ? 2.841 ? ? 
metalc29 metalc ? ? I 911 .   O12 ? ? ? 1_555 O MG  . MG ? ? B 911 801 B MG  807 1_555 ? ? ? ? ? ? ? 2.616 ? ? 
metalc30 metalc ? ? I 911 .   O10 ? ? ? 1_555 P MG  . MG ? ? B 911 801 B MG  808 1_555 ? ? ? ? ? ? ? 2.945 ? ? 
metalc31 metalc ? ? I 911 .   O14 ? ? ? 1_555 Q CA  . CA ? ? B 911 801 B CA  809 1_555 ? ? ? ? ? ? ? 2.730 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 211 ? A ASP 202 ? 1_555 MG ? D MG . ? A MG 802 ? 1_555 OD2 ? A ASP 211 ? A ASP 202 ? 1_555 58.6  ? 
2  O   ? A GLU 226 ? A GLU 217 ? 1_555 MG ? G MG . ? A MG 805 ? 1_555 OE2 ? A GLU 226 ? A GLU 217 ? 1_555 94.9  ? 
3  O   ? A GLU 226 ? A GLU 217 ? 1_555 MG ? G MG . ? A MG 805 ? 1_555 O10 ? C 911 .   ? A 911 801 ? 1_555 146.2 ? 
4  OE2 ? A GLU 226 ? A GLU 217 ? 1_555 MG ? G MG . ? A MG 805 ? 1_555 O10 ? C 911 .   ? A 911 801 ? 1_555 62.0  ? 
5  OD2 ? A ASP 237 ? A ASP 228 ? 1_555 MG ? F MG . ? A MG 804 ? 1_555 OD2 ? A ASP 241 ? A ASP 232 ? 1_555 122.8 ? 
6  OD2 ? A ASP 237 ? A ASP 228 ? 1_555 MG ? F MG . ? A MG 804 ? 1_555 O3  ? C 911 .   ? A 911 801 ? 1_555 124.6 ? 
7  OD2 ? A ASP 241 ? A ASP 232 ? 1_555 MG ? F MG . ? A MG 804 ? 1_555 O3  ? C 911 .   ? A 911 801 ? 1_555 104.9 ? 
8  OD1 ? A ASP 241 ? A ASP 232 ? 1_555 MG ? E MG . ? A MG 803 ? 1_555 O2  ? C 911 .   ? A 911 801 ? 1_555 145.2 ? 
9  OD1 ? A ASP 241 ? A ASP 232 ? 1_555 MG ? E MG . ? A MG 803 ? 1_555 O3  ? C 911 .   ? A 911 801 ? 1_555 108.7 ? 
10 O2  ? C 911 .   ? A 911 801 ? 1_555 MG ? E MG . ? A MG 803 ? 1_555 O3  ? C 911 .   ? A 911 801 ? 1_555 62.8  ? 
11 OD1 ? A ASP 241 ? A ASP 232 ? 1_555 MG ? E MG . ? A MG 803 ? 1_555 O5  ? C 911 .   ? A 911 801 ? 1_555 92.1  ? 
12 O2  ? C 911 .   ? A 911 801 ? 1_555 MG ? E MG . ? A MG 803 ? 1_555 O5  ? C 911 .   ? A 911 801 ? 1_555 55.0  ? 
13 O3  ? C 911 .   ? A 911 801 ? 1_555 MG ? E MG . ? A MG 803 ? 1_555 O5  ? C 911 .   ? A 911 801 ? 1_555 53.2  ? 
14 OD1 ? A ASP 701 ? A ASP 692 ? 1_555 CA ? H CA . ? A CA 806 ? 1_555 O14 ? C 911 .   ? A 911 801 ? 1_555 131.2 ? 
15 OD1 ? A ASP 701 ? A ASP 692 ? 1_555 CA ? H CA . ? A CA 806 ? 1_555 O   ? R HOH .   ? A HOH 901 ? 1_555 55.3  ? 
16 O14 ? C 911 .   ? A 911 801 ? 1_555 CA ? H CA . ? A CA 806 ? 1_555 O   ? R HOH .   ? A HOH 901 ? 1_555 99.7  ? 
17 OD2 ? B ASP 227 ? B ASP 218 ? 1_555 MG ? O MG . ? B MG 807 ? 1_555 O9  ? I 911 .   ? B 911 801 ? 1_555 100.9 ? 
18 OD2 ? B ASP 227 ? B ASP 218 ? 1_555 MG ? O MG . ? B MG 807 ? 1_555 O12 ? I 911 .   ? B 911 801 ? 1_555 111.6 ? 
19 O9  ? I 911 .   ? B 911 801 ? 1_555 MG ? O MG . ? B MG 807 ? 1_555 O12 ? I 911 .   ? B 911 801 ? 1_555 54.9  ? 
20 OD1 ? B ASP 241 ? B ASP 232 ? 1_555 MG ? N MG . ? B MG 806 ? 1_555 O3  ? I 911 .   ? B 911 801 ? 1_555 85.1  ? 
21 OD1 ? B ASP 241 ? B ASP 232 ? 1_555 MG ? N MG . ? B MG 806 ? 1_555 O5  ? I 911 .   ? B 911 801 ? 1_555 142.7 ? 
22 O3  ? I 911 .   ? B 911 801 ? 1_555 MG ? N MG . ? B MG 806 ? 1_555 O5  ? I 911 .   ? B 911 801 ? 1_555 57.6  ? 
23 OD1 ? B ASP 474 ? B ASP 465 ? 1_555 MG ? L MG . ? B MG 804 ? 1_555 OD2 ? B ASP 474 ? B ASP 465 ? 1_555 53.0  ? 
24 OD1 ? B ASP 474 ? B ASP 465 ? 1_555 MG ? L MG . ? B MG 804 ? 1_555 O3  ? I 911 .   ? B 911 801 ? 1_555 111.2 ? 
25 OD2 ? B ASP 474 ? B ASP 465 ? 1_555 MG ? L MG . ? B MG 804 ? 1_555 O3  ? I 911 .   ? B 911 801 ? 1_555 76.9  ? 
26 OD1 ? B ASP 669 ? B ASP 660 ? 1_555 CA ? Q CA . ? B CA 809 ? 1_555 OD1 ? B ASP 701 ? B ASP 692 ? 1_555 134.1 ? 
27 OD1 ? B ASP 669 ? B ASP 660 ? 1_555 CA ? Q CA . ? B CA 809 ? 1_555 O14 ? I 911 .   ? B 911 801 ? 1_555 73.0  ? 
28 OD1 ? B ASP 701 ? B ASP 692 ? 1_555 CA ? Q CA . ? B CA 809 ? 1_555 O14 ? I 911 .   ? B 911 801 ? 1_555 147.1 ? 
29 OD2 ? B ASP 701 ? B ASP 692 ? 1_555 MG ? M MG . ? B MG 805 ? 1_555 O2  ? I 911 .   ? B 911 801 ? 1_555 109.9 ? 
30 OD2 ? B ASP 701 ? B ASP 692 ? 1_555 MG ? M MG . ? B MG 805 ? 1_555 O9  ? I 911 .   ? B 911 801 ? 1_555 162.8 ? 
31 O2  ? I 911 .   ? B 911 801 ? 1_555 MG ? M MG . ? B MG 805 ? 1_555 O9  ? I 911 .   ? B 911 801 ? 1_555 87.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? 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 TYR A 170 ? THR A 171 ? TYR A 161 THR A 162 
AA1 2 ASN A 177 ? PHE A 178 ? ASN A 168 PHE A 169 
AA2 1 VAL A 276 ? GLN A 277 ? VAL A 267 GLN A 268 
AA2 2 VAL A 284 ? HIS A 285 ? VAL A 275 HIS A 276 
AA3 1 TYR B 170 ? THR B 171 ? TYR B 161 THR B 162 
AA3 2 ASN B 177 ? PHE B 178 ? ASN B 168 PHE B 169 
AA4 1 VAL B 276 ? GLN B 277 ? VAL B 267 GLN B 268 
AA4 2 VAL B 284 ? HIS B 285 ? VAL B 275 HIS B 276 
# 
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 TYR A 170 ? N TYR A 161 O PHE A 178 ? O PHE A 169 
AA2 1 2 N GLN A 277 ? N GLN A 268 O VAL A 284 ? O VAL A 275 
AA3 1 2 N TYR B 170 ? N TYR B 161 O PHE B 178 ? O PHE B 169 
AA4 1 2 N GLN B 277 ? N GLN B 268 O VAL B 284 ? O VAL B 275 
# 
_pdbx_entry_details.entry_id                   9G8K 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OH 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   TYR 
_pdbx_validate_close_contact.auth_seq_id_1    289 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG1 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   THR 
_pdbx_validate_close_contact.auth_seq_id_2    340 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              474 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              474 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             SG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              474 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                122.57 
_pdbx_validate_rmsd_angle.angle_target_value         114.20 
_pdbx_validate_rmsd_angle.angle_deviation            8.37 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 146 ? ? -91.71  -66.97  
2  1 ALA A 435 ? ? -147.40 40.12   
3  1 PHE A 450 ? ? -90.72  42.34   
4  1 CYS A 474 ? ? 42.18   -124.76 
5  1 THR A 697 ? ? -126.28 -55.75  
6  1 LEU B 146 ? ? -90.47  -65.75  
7  1 LEU B 158 ? ? 57.95   18.34   
8  1 GLU B 217 ? ? 42.68   -126.52 
9  1 VAL B 237 ? ? -101.15 -60.44  
10 1 ALA B 435 ? ? -146.73 38.76   
11 1 PHE B 450 ? ? -91.88  42.76   
12 1 ASP B 595 ? ? 55.80   -130.14 
13 1 THR B 697 ? ? -125.14 -58.73  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 -8  ? A MET 1   
2  1 Y 1 A ARG -7  ? A ARG 2   
3  1 Y 1 A GLY -6  ? A GLY 3   
4  1 Y 1 A SER -5  ? A SER 4   
5  1 Y 1 A HIS -4  ? A HIS 5   
6  1 Y 1 A HIS -3  ? A HIS 6   
7  1 Y 1 A HIS -2  ? A HIS 7   
8  1 Y 1 A HIS -1  ? A HIS 8   
9  1 Y 1 A HIS 0   ? A HIS 9   
10 1 Y 1 A HIS 1   ? A HIS 10  
11 1 Y 1 A VAL 208 ? A VAL 217 
12 1 Y 1 A GLY 209 ? A GLY 218 
13 1 Y 1 A LYS 210 ? A LYS 219 
14 1 Y 1 A THR 211 ? A THR 220 
15 1 Y 1 A GLU 212 ? A GLU 221 
16 1 Y 1 A LEU 213 ? A LEU 222 
17 1 Y 1 A ASN 214 ? A ASN 223 
18 1 Y 1 A LEU 215 ? A LEU 224 
19 1 Y 1 A PRO 313 ? A PRO 322 
20 1 Y 1 A SER 314 ? A SER 323 
21 1 Y 1 A ASP 315 ? A ASP 324 
22 1 Y 1 A ARG 582 ? A ARG 591 
23 1 Y 1 A GLU 583 ? A GLU 592 
24 1 Y 1 A ILE 584 ? A ILE 593 
25 1 Y 1 A PRO 585 ? A PRO 594 
26 1 Y 1 A GLY 586 ? A GLY 595 
27 1 Y 1 A LEU 587 ? A LEU 596 
28 1 Y 1 A LEU 588 ? A LEU 597 
29 1 Y 1 A GLU 589 ? A GLU 598 
30 1 Y 1 A GLY 590 ? A GLY 599 
31 1 Y 1 A LYS 591 ? A LYS 600 
32 1 Y 1 A ALA 592 ? A ALA 601 
33 1 Y 1 A LYS 593 ? A LYS 602 
34 1 Y 1 A PRO 594 ? A PRO 603 
35 1 Y 1 A ASP 595 ? A ASP 604 
36 1 Y 1 B MET -8  ? B MET 1   
37 1 Y 1 B ARG -7  ? B ARG 2   
38 1 Y 1 B GLY -6  ? B GLY 3   
39 1 Y 1 B SER -5  ? B SER 4   
40 1 Y 1 B HIS -4  ? B HIS 5   
41 1 Y 1 B HIS -3  ? B HIS 6   
42 1 Y 1 B HIS -2  ? B HIS 7   
43 1 Y 1 B HIS -1  ? B HIS 8   
44 1 Y 1 B HIS 0   ? B HIS 9   
45 1 Y 1 B HIS 1   ? B HIS 10  
46 1 Y 1 B TYR 2   ? B TYR 11  
47 1 Y 1 B GLY 31  ? B GLY 40  
48 1 Y 1 B THR 32  ? B THR 41  
49 1 Y 1 B LYS 114 ? B LYS 123 
50 1 Y 1 B LEU 213 ? B LEU 222 
51 1 Y 1 B ASN 214 ? B ASN 223 
52 1 Y 1 B LEU 215 ? B LEU 224 
53 1 Y 1 B CYS 474 ? B CYS 483 
54 1 Y 1 B GLU 475 ? B GLU 484 
55 1 Y 1 B LEU 476 ? B LEU 485 
56 1 Y 1 B ARG 578 ? B ARG 587 
57 1 Y 1 B ARG 579 ? B ARG 588 
58 1 Y 1 B GLN 580 ? B GLN 589 
59 1 Y 1 B ALA 581 ? B ALA 590 
60 1 Y 1 B ARG 582 ? B ARG 591 
61 1 Y 1 B GLU 583 ? B GLU 592 
62 1 Y 1 B ILE 584 ? B ILE 593 
63 1 Y 1 B PRO 585 ? B PRO 594 
64 1 Y 1 B GLY 586 ? B GLY 595 
65 1 Y 1 B LEU 587 ? B LEU 596 
66 1 Y 1 B LEU 588 ? B LEU 597 
67 1 Y 1 B GLU 589 ? B GLU 598 
68 1 Y 1 B GLY 590 ? B GLY 599 
69 1 Y 1 B LYS 591 ? B LYS 600 
70 1 Y 1 B GLY 673 ? B GLY 682 
71 1 Y 1 B TYR 674 ? B TYR 683 
72 1 Y 1 B GLY 675 ? B GLY 684 
# 
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 
911 P1     P  N N 1   
911 O2     O  N N 2   
911 O3     O  N N 3   
911 O5     O  N N 4   
911 C7     C  N N 5   
911 P8     P  N N 6   
911 O9     O  N N 7   
911 O10    O  N N 8   
911 O12    O  N N 9   
911 O14    O  N N 10  
911 C16    C  N N 11  
911 HO3    H  N N 12  
911 HO5    H  N N 13  
911 HO10   H  N N 14  
911 HO12   H  N N 15  
911 HO14   H  N N 16  
911 H16    H  N N 17  
911 H16A   H  N N 18  
911 H16B   H  N N 19  
ALA N      N  N N 20  
ALA CA     C  N S 21  
ALA C      C  N N 22  
ALA O      O  N N 23  
ALA CB     C  N N 24  
ALA OXT    O  N N 25  
ALA H      H  N N 26  
ALA H2     H  N N 27  
ALA HA     H  N N 28  
ALA HB1    H  N N 29  
ALA HB2    H  N N 30  
ALA HB3    H  N N 31  
ALA HXT    H  N N 32  
ARG N      N  N N 33  
ARG CA     C  N S 34  
ARG C      C  N N 35  
ARG O      O  N N 36  
ARG CB     C  N N 37  
ARG CG     C  N N 38  
ARG CD     C  N N 39  
ARG NE     N  N N 40  
ARG CZ     C  N N 41  
ARG NH1    N  N N 42  
ARG NH2    N  N N 43  
ARG OXT    O  N N 44  
ARG H      H  N N 45  
ARG H2     H  N N 46  
ARG HA     H  N N 47  
ARG HB2    H  N N 48  
ARG HB3    H  N N 49  
ARG HG2    H  N N 50  
ARG HG3    H  N N 51  
ARG HD2    H  N N 52  
ARG HD3    H  N N 53  
ARG HE     H  N N 54  
ARG HH11   H  N N 55  
ARG HH12   H  N N 56  
ARG HH21   H  N N 57  
ARG HH22   H  N N 58  
ARG HXT    H  N N 59  
ASN N      N  N N 60  
ASN CA     C  N S 61  
ASN C      C  N N 62  
ASN O      O  N N 63  
ASN CB     C  N N 64  
ASN CG     C  N N 65  
ASN OD1    O  N N 66  
ASN ND2    N  N N 67  
ASN OXT    O  N N 68  
ASN H      H  N N 69  
ASN H2     H  N N 70  
ASN HA     H  N N 71  
ASN HB2    H  N N 72  
ASN HB3    H  N N 73  
ASN HD21   H  N N 74  
ASN HD22   H  N N 75  
ASN HXT    H  N N 76  
ASP N      N  N N 77  
ASP CA     C  N S 78  
ASP C      C  N N 79  
ASP O      O  N N 80  
ASP CB     C  N N 81  
ASP CG     C  N N 82  
ASP OD1    O  N N 83  
ASP OD2    O  N N 84  
ASP OXT    O  N N 85  
ASP H      H  N N 86  
ASP H2     H  N N 87  
ASP HA     H  N N 88  
ASP HB2    H  N N 89  
ASP HB3    H  N N 90  
ASP HD2    H  N N 91  
ASP HXT    H  N N 92  
CA  CA     CA N N 93  
CYS N      N  N N 94  
CYS CA     C  N R 95  
CYS C      C  N N 96  
CYS O      O  N N 97  
CYS CB     C  N N 98  
CYS SG     S  N N 99  
CYS OXT    O  N N 100 
CYS H      H  N N 101 
CYS H2     H  N N 102 
CYS HA     H  N N 103 
CYS HB2    H  N N 104 
CYS HB3    H  N N 105 
CYS HG     H  N N 106 
CYS HXT    H  N N 107 
GLN N      N  N N 108 
GLN CA     C  N S 109 
GLN C      C  N N 110 
GLN O      O  N N 111 
GLN CB     C  N N 112 
GLN CG     C  N N 113 
GLN CD     C  N N 114 
GLN OE1    O  N N 115 
GLN NE2    N  N N 116 
GLN OXT    O  N N 117 
GLN H      H  N N 118 
GLN H2     H  N N 119 
GLN HA     H  N N 120 
GLN HB2    H  N N 121 
GLN HB3    H  N N 122 
GLN HG2    H  N N 123 
GLN HG3    H  N N 124 
GLN HE21   H  N N 125 
GLN HE22   H  N N 126 
GLN HXT    H  N N 127 
GLU N      N  N N 128 
GLU CA     C  N S 129 
GLU C      C  N N 130 
GLU O      O  N N 131 
GLU CB     C  N N 132 
GLU CG     C  N N 133 
GLU CD     C  N N 134 
GLU OE1    O  N N 135 
GLU OE2    O  N N 136 
GLU OXT    O  N N 137 
GLU H      H  N N 138 
GLU H2     H  N N 139 
GLU HA     H  N N 140 
GLU HB2    H  N N 141 
GLU HB3    H  N N 142 
GLU HG2    H  N N 143 
GLU HG3    H  N N 144 
GLU HE2    H  N N 145 
GLU HXT    H  N N 146 
GLY N      N  N N 147 
GLY CA     C  N N 148 
GLY C      C  N N 149 
GLY O      O  N N 150 
GLY OXT    O  N N 151 
GLY H      H  N N 152 
GLY H2     H  N N 153 
GLY HA2    H  N N 154 
GLY HA3    H  N N 155 
GLY HXT    H  N N 156 
HIS N      N  N N 157 
HIS CA     C  N S 158 
HIS C      C  N N 159 
HIS O      O  N N 160 
HIS CB     C  N N 161 
HIS CG     C  Y N 162 
HIS ND1    N  Y N 163 
HIS CD2    C  Y N 164 
HIS CE1    C  Y N 165 
HIS NE2    N  Y N 166 
HIS OXT    O  N N 167 
HIS H      H  N N 168 
HIS H2     H  N N 169 
HIS HA     H  N N 170 
HIS HB2    H  N N 171 
HIS HB3    H  N N 172 
HIS HD1    H  N N 173 
HIS HD2    H  N N 174 
HIS HE1    H  N N 175 
HIS HE2    H  N N 176 
HIS HXT    H  N N 177 
HOH O      O  N N 178 
HOH H1     H  N N 179 
HOH H2     H  N N 180 
ILE N      N  N N 181 
ILE CA     C  N S 182 
ILE C      C  N N 183 
ILE O      O  N N 184 
ILE CB     C  N S 185 
ILE CG1    C  N N 186 
ILE CG2    C  N N 187 
ILE CD1    C  N N 188 
ILE OXT    O  N N 189 
ILE H      H  N N 190 
ILE H2     H  N N 191 
ILE HA     H  N N 192 
ILE HB     H  N N 193 
ILE HG12   H  N N 194 
ILE HG13   H  N N 195 
ILE HG21   H  N N 196 
ILE HG22   H  N N 197 
ILE HG23   H  N N 198 
ILE HD11   H  N N 199 
ILE HD12   H  N N 200 
ILE HD13   H  N N 201 
ILE HXT    H  N N 202 
LEU N      N  N N 203 
LEU CA     C  N S 204 
LEU C      C  N N 205 
LEU O      O  N N 206 
LEU CB     C  N N 207 
LEU CG     C  N N 208 
LEU CD1    C  N N 209 
LEU CD2    C  N N 210 
LEU OXT    O  N N 211 
LEU H      H  N N 212 
LEU H2     H  N N 213 
LEU HA     H  N N 214 
LEU HB2    H  N N 215 
LEU HB3    H  N N 216 
LEU HG     H  N N 217 
LEU HD11   H  N N 218 
LEU HD12   H  N N 219 
LEU HD13   H  N N 220 
LEU HD21   H  N N 221 
LEU HD22   H  N N 222 
LEU HD23   H  N N 223 
LEU HXT    H  N N 224 
LMT C1B    C  N R 225 
LMT C2B    C  N R 226 
LMT C3B    C  N S 227 
LMT C4B    C  N S 228 
LMT C5B    C  N R 229 
LMT C6B    C  N N 230 
LMT O1B    O  N N 231 
LMT O2B    O  N N 232 
LMT O3B    O  N N 233 
LMT "O4'"  O  N N 234 
LMT O5B    O  N N 235 
LMT O6B    O  N N 236 
LMT "C1'"  C  N R 237 
LMT "C2'"  C  N R 238 
LMT "C3'"  C  N R 239 
LMT "C4'"  C  N S 240 
LMT "C5'"  C  N R 241 
LMT "C6'"  C  N N 242 
LMT "O1'"  O  N N 243 
LMT "O2'"  O  N N 244 
LMT "O3'"  O  N N 245 
LMT "O5'"  O  N N 246 
LMT "O6'"  O  N N 247 
LMT C1     C  N N 248 
LMT C2     C  N N 249 
LMT C3     C  N N 250 
LMT C4     C  N N 251 
LMT C5     C  N N 252 
LMT C6     C  N N 253 
LMT C7     C  N N 254 
LMT C8     C  N N 255 
LMT C9     C  N N 256 
LMT C10    C  N N 257 
LMT C11    C  N N 258 
LMT C12    C  N N 259 
LMT H1B    H  N N 260 
LMT H2B    H  N N 261 
LMT H3B    H  N N 262 
LMT H4B    H  N N 263 
LMT H5B    H  N N 264 
LMT "H6'2" H  N N 265 
LMT "H6'1" H  N N 266 
LMT H2O1   H  N N 267 
LMT H3O1   H  N N 268 
LMT H4O1   H  N N 269 
LMT H6B    H  N N 270 
LMT "H1'"  H  N N 271 
LMT "H2'"  H  N N 272 
LMT "H3'"  H  N N 273 
LMT "H4'"  H  N N 274 
LMT "H5'"  H  N N 275 
LMT H6D    H  N N 276 
LMT H6E    H  N N 277 
LMT H2O2   H  N N 278 
LMT H3O2   H  N N 279 
LMT "H6'"  H  N N 280 
LMT H12    H  N N 281 
LMT H11    H  N N 282 
LMT H22    H  N N 283 
LMT H21    H  N N 284 
LMT H32    H  N N 285 
LMT H31    H  N N 286 
LMT H42    H  N N 287 
LMT H41    H  N N 288 
LMT H52    H  N N 289 
LMT H51    H  N N 290 
LMT H62    H  N N 291 
LMT H61    H  N N 292 
LMT H72    H  N N 293 
LMT H71    H  N N 294 
LMT H82    H  N N 295 
LMT H81    H  N N 296 
LMT H92    H  N N 297 
LMT H91    H  N N 298 
LMT H102   H  N N 299 
LMT H101   H  N N 300 
LMT H112   H  N N 301 
LMT H111   H  N N 302 
LMT H123   H  N N 303 
LMT H122   H  N N 304 
LMT H121   H  N N 305 
LYS N      N  N N 306 
LYS CA     C  N S 307 
LYS C      C  N N 308 
LYS O      O  N N 309 
LYS CB     C  N N 310 
LYS CG     C  N N 311 
LYS CD     C  N N 312 
LYS CE     C  N N 313 
LYS NZ     N  N N 314 
LYS OXT    O  N N 315 
LYS H      H  N N 316 
LYS H2     H  N N 317 
LYS HA     H  N N 318 
LYS HB2    H  N N 319 
LYS HB3    H  N N 320 
LYS HG2    H  N N 321 
LYS HG3    H  N N 322 
LYS HD2    H  N N 323 
LYS HD3    H  N N 324 
LYS HE2    H  N N 325 
LYS HE3    H  N N 326 
LYS HZ1    H  N N 327 
LYS HZ2    H  N N 328 
LYS HZ3    H  N N 329 
LYS HXT    H  N N 330 
MET N      N  N N 331 
MET CA     C  N S 332 
MET C      C  N N 333 
MET O      O  N N 334 
MET CB     C  N N 335 
MET CG     C  N N 336 
MET SD     S  N N 337 
MET CE     C  N N 338 
MET OXT    O  N N 339 
MET H      H  N N 340 
MET H2     H  N N 341 
MET HA     H  N N 342 
MET HB2    H  N N 343 
MET HB3    H  N N 344 
MET HG2    H  N N 345 
MET HG3    H  N N 346 
MET HE1    H  N N 347 
MET HE2    H  N N 348 
MET HE3    H  N N 349 
MET HXT    H  N N 350 
MG  MG     MG N N 351 
PHE N      N  N N 352 
PHE CA     C  N S 353 
PHE C      C  N N 354 
PHE O      O  N N 355 
PHE CB     C  N N 356 
PHE CG     C  Y N 357 
PHE CD1    C  Y N 358 
PHE CD2    C  Y N 359 
PHE CE1    C  Y N 360 
PHE CE2    C  Y N 361 
PHE CZ     C  Y N 362 
PHE OXT    O  N N 363 
PHE H      H  N N 364 
PHE H2     H  N N 365 
PHE HA     H  N N 366 
PHE HB2    H  N N 367 
PHE HB3    H  N N 368 
PHE HD1    H  N N 369 
PHE HD2    H  N N 370 
PHE HE1    H  N N 371 
PHE HE2    H  N N 372 
PHE HZ     H  N N 373 
PHE HXT    H  N N 374 
PRO N      N  N N 375 
PRO CA     C  N S 376 
PRO C      C  N N 377 
PRO O      O  N N 378 
PRO CB     C  N N 379 
PRO CG     C  N N 380 
PRO CD     C  N N 381 
PRO OXT    O  N N 382 
PRO H      H  N N 383 
PRO HA     H  N N 384 
PRO HB2    H  N N 385 
PRO HB3    H  N N 386 
PRO HG2    H  N N 387 
PRO HG3    H  N N 388 
PRO HD2    H  N N 389 
PRO HD3    H  N N 390 
PRO HXT    H  N N 391 
SER N      N  N N 392 
SER CA     C  N S 393 
SER C      C  N N 394 
SER O      O  N N 395 
SER CB     C  N N 396 
SER OG     O  N N 397 
SER OXT    O  N N 398 
SER H      H  N N 399 
SER H2     H  N N 400 
SER HA     H  N N 401 
SER HB2    H  N N 402 
SER HB3    H  N N 403 
SER HG     H  N N 404 
SER HXT    H  N N 405 
THR N      N  N N 406 
THR CA     C  N S 407 
THR C      C  N N 408 
THR O      O  N N 409 
THR CB     C  N R 410 
THR OG1    O  N N 411 
THR CG2    C  N N 412 
THR OXT    O  N N 413 
THR H      H  N N 414 
THR H2     H  N N 415 
THR HA     H  N N 416 
THR HB     H  N N 417 
THR HG1    H  N N 418 
THR HG21   H  N N 419 
THR HG22   H  N N 420 
THR HG23   H  N N 421 
THR HXT    H  N N 422 
TRP N      N  N N 423 
TRP CA     C  N S 424 
TRP C      C  N N 425 
TRP O      O  N N 426 
TRP CB     C  N N 427 
TRP CG     C  Y N 428 
TRP CD1    C  Y N 429 
TRP CD2    C  Y N 430 
TRP NE1    N  Y N 431 
TRP CE2    C  Y N 432 
TRP CE3    C  Y N 433 
TRP CZ2    C  Y N 434 
TRP CZ3    C  Y N 435 
TRP CH2    C  Y N 436 
TRP OXT    O  N N 437 
TRP H      H  N N 438 
TRP H2     H  N N 439 
TRP HA     H  N N 440 
TRP HB2    H  N N 441 
TRP HB3    H  N N 442 
TRP HD1    H  N N 443 
TRP HE1    H  N N 444 
TRP HE3    H  N N 445 
TRP HZ2    H  N N 446 
TRP HZ3    H  N N 447 
TRP HH2    H  N N 448 
TRP HXT    H  N N 449 
TYR N      N  N N 450 
TYR CA     C  N S 451 
TYR C      C  N N 452 
TYR O      O  N N 453 
TYR CB     C  N N 454 
TYR CG     C  Y N 455 
TYR CD1    C  Y N 456 
TYR CD2    C  Y N 457 
TYR CE1    C  Y N 458 
TYR CE2    C  Y N 459 
TYR CZ     C  Y N 460 
TYR OH     O  N N 461 
TYR OXT    O  N N 462 
TYR H      H  N N 463 
TYR H2     H  N N 464 
TYR HA     H  N N 465 
TYR HB2    H  N N 466 
TYR HB3    H  N N 467 
TYR HD1    H  N N 468 
TYR HD2    H  N N 469 
TYR HE1    H  N N 470 
TYR HE2    H  N N 471 
TYR HH     H  N N 472 
TYR HXT    H  N N 473 
VAL N      N  N N 474 
VAL CA     C  N S 475 
VAL C      C  N N 476 
VAL O      O  N N 477 
VAL CB     C  N N 478 
VAL CG1    C  N N 479 
VAL CG2    C  N N 480 
VAL OXT    O  N N 481 
VAL H      H  N N 482 
VAL H2     H  N N 483 
VAL HA     H  N N 484 
VAL HB     H  N N 485 
VAL HG11   H  N N 486 
VAL HG12   H  N N 487 
VAL HG13   H  N N 488 
VAL HG21   H  N N 489 
VAL HG22   H  N N 490 
VAL HG23   H  N N 491 
VAL HXT    H  N N 492 
# 
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 
911 O2    P1     doub N N 1   
911 P1    O5     sing N N 2   
911 P1    C7     sing N N 3   
911 P1    O3     sing N N 4   
911 O3    HO3    sing N N 5   
911 O5    HO5    sing N N 6   
911 C16   C7     sing N N 7   
911 C7    O14    sing N N 8   
911 C7    P8     sing N N 9   
911 P8    O9     doub N N 10  
911 P8    O10    sing N N 11  
911 P8    O12    sing N N 12  
911 O10   HO10   sing N N 13  
911 O12   HO12   sing N N 14  
911 O14   HO14   sing N N 15  
911 C16   H16    sing N N 16  
911 C16   H16A   sing N N 17  
911 C16   H16B   sing N N 18  
ALA N     CA     sing N N 19  
ALA N     H      sing N N 20  
ALA N     H2     sing N N 21  
ALA CA    C      sing N N 22  
ALA CA    CB     sing N N 23  
ALA CA    HA     sing N N 24  
ALA C     O      doub N N 25  
ALA C     OXT    sing N N 26  
ALA CB    HB1    sing N N 27  
ALA CB    HB2    sing N N 28  
ALA CB    HB3    sing N N 29  
ALA OXT   HXT    sing N N 30  
ARG N     CA     sing N N 31  
ARG N     H      sing N N 32  
ARG N     H2     sing N N 33  
ARG CA    C      sing N N 34  
ARG CA    CB     sing N N 35  
ARG CA    HA     sing N N 36  
ARG C     O      doub N N 37  
ARG C     OXT    sing N N 38  
ARG CB    CG     sing N N 39  
ARG CB    HB2    sing N N 40  
ARG CB    HB3    sing N N 41  
ARG CG    CD     sing N N 42  
ARG CG    HG2    sing N N 43  
ARG CG    HG3    sing N N 44  
ARG CD    NE     sing N N 45  
ARG CD    HD2    sing N N 46  
ARG CD    HD3    sing N N 47  
ARG NE    CZ     sing N N 48  
ARG NE    HE     sing N N 49  
ARG CZ    NH1    sing N N 50  
ARG CZ    NH2    doub N N 51  
ARG NH1   HH11   sing N N 52  
ARG NH1   HH12   sing N N 53  
ARG NH2   HH21   sing N N 54  
ARG NH2   HH22   sing N N 55  
ARG OXT   HXT    sing N N 56  
ASN N     CA     sing N N 57  
ASN N     H      sing N N 58  
ASN N     H2     sing N N 59  
ASN CA    C      sing N N 60  
ASN CA    CB     sing N N 61  
ASN CA    HA     sing N N 62  
ASN C     O      doub N N 63  
ASN C     OXT    sing N N 64  
ASN CB    CG     sing N N 65  
ASN CB    HB2    sing N N 66  
ASN CB    HB3    sing N N 67  
ASN CG    OD1    doub N N 68  
ASN CG    ND2    sing N N 69  
ASN ND2   HD21   sing N N 70  
ASN ND2   HD22   sing N N 71  
ASN OXT   HXT    sing N N 72  
ASP N     CA     sing N N 73  
ASP N     H      sing N N 74  
ASP N     H2     sing N N 75  
ASP CA    C      sing N N 76  
ASP CA    CB     sing N N 77  
ASP CA    HA     sing N N 78  
ASP C     O      doub N N 79  
ASP C     OXT    sing N N 80  
ASP CB    CG     sing N N 81  
ASP CB    HB2    sing N N 82  
ASP CB    HB3    sing N N 83  
ASP CG    OD1    doub N N 84  
ASP CG    OD2    sing N N 85  
ASP OD2   HD2    sing N N 86  
ASP OXT   HXT    sing N N 87  
CYS N     CA     sing N N 88  
CYS N     H      sing N N 89  
CYS N     H2     sing N N 90  
CYS CA    C      sing N N 91  
CYS CA    CB     sing N N 92  
CYS CA    HA     sing N N 93  
CYS C     O      doub N N 94  
CYS C     OXT    sing N N 95  
CYS CB    SG     sing N N 96  
CYS CB    HB2    sing N N 97  
CYS CB    HB3    sing N N 98  
CYS SG    HG     sing N N 99  
CYS OXT   HXT    sing N N 100 
GLN N     CA     sing N N 101 
GLN N     H      sing N N 102 
GLN N     H2     sing N N 103 
GLN CA    C      sing N N 104 
GLN CA    CB     sing N N 105 
GLN CA    HA     sing N N 106 
GLN C     O      doub N N 107 
GLN C     OXT    sing N N 108 
GLN CB    CG     sing N N 109 
GLN CB    HB2    sing N N 110 
GLN CB    HB3    sing N N 111 
GLN CG    CD     sing N N 112 
GLN CG    HG2    sing N N 113 
GLN CG    HG3    sing N N 114 
GLN CD    OE1    doub N N 115 
GLN CD    NE2    sing N N 116 
GLN NE2   HE21   sing N N 117 
GLN NE2   HE22   sing N N 118 
GLN OXT   HXT    sing N N 119 
GLU N     CA     sing N N 120 
GLU N     H      sing N N 121 
GLU N     H2     sing N N 122 
GLU CA    C      sing N N 123 
GLU CA    CB     sing N N 124 
GLU CA    HA     sing N N 125 
GLU C     O      doub N N 126 
GLU C     OXT    sing N N 127 
GLU CB    CG     sing N N 128 
GLU CB    HB2    sing N N 129 
GLU CB    HB3    sing N N 130 
GLU CG    CD     sing N N 131 
GLU CG    HG2    sing N N 132 
GLU CG    HG3    sing N N 133 
GLU CD    OE1    doub N N 134 
GLU CD    OE2    sing N N 135 
GLU OE2   HE2    sing N N 136 
GLU OXT   HXT    sing N N 137 
GLY N     CA     sing N N 138 
GLY N     H      sing N N 139 
GLY N     H2     sing N N 140 
GLY CA    C      sing N N 141 
GLY CA    HA2    sing N N 142 
GLY CA    HA3    sing N N 143 
GLY C     O      doub N N 144 
GLY C     OXT    sing N N 145 
GLY OXT   HXT    sing N N 146 
HIS N     CA     sing N N 147 
HIS N     H      sing N N 148 
HIS N     H2     sing N N 149 
HIS CA    C      sing N N 150 
HIS CA    CB     sing N N 151 
HIS CA    HA     sing N N 152 
HIS C     O      doub N N 153 
HIS C     OXT    sing N N 154 
HIS CB    CG     sing N N 155 
HIS CB    HB2    sing N N 156 
HIS CB    HB3    sing N N 157 
HIS CG    ND1    sing Y N 158 
HIS CG    CD2    doub Y N 159 
HIS ND1   CE1    doub Y N 160 
HIS ND1   HD1    sing N N 161 
HIS CD2   NE2    sing Y N 162 
HIS CD2   HD2    sing N N 163 
HIS CE1   NE2    sing Y N 164 
HIS CE1   HE1    sing N N 165 
HIS NE2   HE2    sing N N 166 
HIS OXT   HXT    sing N N 167 
HOH O     H1     sing N N 168 
HOH O     H2     sing N N 169 
ILE N     CA     sing N N 170 
ILE N     H      sing N N 171 
ILE N     H2     sing N N 172 
ILE CA    C      sing N N 173 
ILE CA    CB     sing N N 174 
ILE CA    HA     sing N N 175 
ILE C     O      doub N N 176 
ILE C     OXT    sing N N 177 
ILE CB    CG1    sing N N 178 
ILE CB    CG2    sing N N 179 
ILE CB    HB     sing N N 180 
ILE CG1   CD1    sing N N 181 
ILE CG1   HG12   sing N N 182 
ILE CG1   HG13   sing N N 183 
ILE CG2   HG21   sing N N 184 
ILE CG2   HG22   sing N N 185 
ILE CG2   HG23   sing N N 186 
ILE CD1   HD11   sing N N 187 
ILE CD1   HD12   sing N N 188 
ILE CD1   HD13   sing N N 189 
ILE OXT   HXT    sing N N 190 
LEU N     CA     sing N N 191 
LEU N     H      sing N N 192 
LEU N     H2     sing N N 193 
LEU CA    C      sing N N 194 
LEU CA    CB     sing N N 195 
LEU CA    HA     sing N N 196 
LEU C     O      doub N N 197 
LEU C     OXT    sing N N 198 
LEU CB    CG     sing N N 199 
LEU CB    HB2    sing N N 200 
LEU CB    HB3    sing N N 201 
LEU CG    CD1    sing N N 202 
LEU CG    CD2    sing N N 203 
LEU CG    HG     sing N N 204 
LEU CD1   HD11   sing N N 205 
LEU CD1   HD12   sing N N 206 
LEU CD1   HD13   sing N N 207 
LEU CD2   HD21   sing N N 208 
LEU CD2   HD22   sing N N 209 
LEU CD2   HD23   sing N N 210 
LEU OXT   HXT    sing N N 211 
LMT C1B   C2B    sing N N 212 
LMT C1B   O1B    sing N N 213 
LMT C1B   O5B    sing N N 214 
LMT C1B   H1B    sing N N 215 
LMT C2B   C3B    sing N N 216 
LMT C2B   O2B    sing N N 217 
LMT C2B   H2B    sing N N 218 
LMT C3B   C4B    sing N N 219 
LMT C3B   O3B    sing N N 220 
LMT C3B   H3B    sing N N 221 
LMT C4B   C5B    sing N N 222 
LMT C4B   "O4'"  sing N N 223 
LMT C4B   H4B    sing N N 224 
LMT C5B   C6B    sing N N 225 
LMT C5B   O5B    sing N N 226 
LMT C5B   H5B    sing N N 227 
LMT C6B   O6B    sing N N 228 
LMT C6B   "H6'2" sing N N 229 
LMT C6B   "H6'1" sing N N 230 
LMT O1B   "C4'"  sing N N 231 
LMT O2B   H2O1   sing N N 232 
LMT O3B   H3O1   sing N N 233 
LMT "O4'" H4O1   sing N N 234 
LMT O6B   H6B    sing N N 235 
LMT "C1'" "C2'"  sing N N 236 
LMT "C1'" "O1'"  sing N N 237 
LMT "C1'" "O5'"  sing N N 238 
LMT "C1'" "H1'"  sing N N 239 
LMT "C2'" "C3'"  sing N N 240 
LMT "C2'" "O2'"  sing N N 241 
LMT "C2'" "H2'"  sing N N 242 
LMT "C3'" "C4'"  sing N N 243 
LMT "C3'" "O3'"  sing N N 244 
LMT "C3'" "H3'"  sing N N 245 
LMT "C4'" "C5'"  sing N N 246 
LMT "C4'" "H4'"  sing N N 247 
LMT "C5'" "C6'"  sing N N 248 
LMT "C5'" "O5'"  sing N N 249 
LMT "C5'" "H5'"  sing N N 250 
LMT "C6'" "O6'"  sing N N 251 
LMT "C6'" H6D    sing N N 252 
LMT "C6'" H6E    sing N N 253 
LMT "O1'" C1     sing N N 254 
LMT "O2'" H2O2   sing N N 255 
LMT "O3'" H3O2   sing N N 256 
LMT "O6'" "H6'"  sing N N 257 
LMT C1    C2     sing N N 258 
LMT C1    H12    sing N N 259 
LMT C1    H11    sing N N 260 
LMT C2    C3     sing N N 261 
LMT C2    H22    sing N N 262 
LMT C2    H21    sing N N 263 
LMT C3    C4     sing N N 264 
LMT C3    H32    sing N N 265 
LMT C3    H31    sing N N 266 
LMT C4    C5     sing N N 267 
LMT C4    H42    sing N N 268 
LMT C4    H41    sing N N 269 
LMT C5    C6     sing N N 270 
LMT C5    H52    sing N N 271 
LMT C5    H51    sing N N 272 
LMT C6    C7     sing N N 273 
LMT C6    H62    sing N N 274 
LMT C6    H61    sing N N 275 
LMT C7    C8     sing N N 276 
LMT C7    H72    sing N N 277 
LMT C7    H71    sing N N 278 
LMT C8    C9     sing N N 279 
LMT C8    H82    sing N N 280 
LMT C8    H81    sing N N 281 
LMT C9    C10    sing N N 282 
LMT C9    H92    sing N N 283 
LMT C9    H91    sing N N 284 
LMT C10   C11    sing N N 285 
LMT C10   H102   sing N N 286 
LMT C10   H101   sing N N 287 
LMT C11   C12    sing N N 288 
LMT C11   H112   sing N N 289 
LMT C11   H111   sing N N 290 
LMT C12   H123   sing N N 291 
LMT C12   H122   sing N N 292 
LMT C12   H121   sing N N 293 
LYS N     CA     sing N N 294 
LYS N     H      sing N N 295 
LYS N     H2     sing N N 296 
LYS CA    C      sing N N 297 
LYS CA    CB     sing N N 298 
LYS CA    HA     sing N N 299 
LYS C     O      doub N N 300 
LYS C     OXT    sing N N 301 
LYS CB    CG     sing N N 302 
LYS CB    HB2    sing N N 303 
LYS CB    HB3    sing N N 304 
LYS CG    CD     sing N N 305 
LYS CG    HG2    sing N N 306 
LYS CG    HG3    sing N N 307 
LYS CD    CE     sing N N 308 
LYS CD    HD2    sing N N 309 
LYS CD    HD3    sing N N 310 
LYS CE    NZ     sing N N 311 
LYS CE    HE2    sing N N 312 
LYS CE    HE3    sing N N 313 
LYS NZ    HZ1    sing N N 314 
LYS NZ    HZ2    sing N N 315 
LYS NZ    HZ3    sing N N 316 
LYS OXT   HXT    sing N N 317 
MET N     CA     sing N N 318 
MET N     H      sing N N 319 
MET N     H2     sing N N 320 
MET CA    C      sing N N 321 
MET CA    CB     sing N N 322 
MET CA    HA     sing N N 323 
MET C     O      doub N N 324 
MET C     OXT    sing N N 325 
MET CB    CG     sing N N 326 
MET CB    HB2    sing N N 327 
MET CB    HB3    sing N N 328 
MET CG    SD     sing N N 329 
MET CG    HG2    sing N N 330 
MET CG    HG3    sing N N 331 
MET SD    CE     sing N N 332 
MET CE    HE1    sing N N 333 
MET CE    HE2    sing N N 334 
MET CE    HE3    sing N N 335 
MET OXT   HXT    sing N N 336 
PHE N     CA     sing N N 337 
PHE N     H      sing N N 338 
PHE N     H2     sing N N 339 
PHE CA    C      sing N N 340 
PHE CA    CB     sing N N 341 
PHE CA    HA     sing N N 342 
PHE C     O      doub N N 343 
PHE C     OXT    sing N N 344 
PHE CB    CG     sing N N 345 
PHE CB    HB2    sing N N 346 
PHE CB    HB3    sing N N 347 
PHE CG    CD1    doub Y N 348 
PHE CG    CD2    sing Y N 349 
PHE CD1   CE1    sing Y N 350 
PHE CD1   HD1    sing N N 351 
PHE CD2   CE2    doub Y N 352 
PHE CD2   HD2    sing N N 353 
PHE CE1   CZ     doub Y N 354 
PHE CE1   HE1    sing N N 355 
PHE CE2   CZ     sing Y N 356 
PHE CE2   HE2    sing N N 357 
PHE CZ    HZ     sing N N 358 
PHE OXT   HXT    sing N N 359 
PRO N     CA     sing N N 360 
PRO N     CD     sing N N 361 
PRO N     H      sing N N 362 
PRO CA    C      sing N N 363 
PRO CA    CB     sing N N 364 
PRO CA    HA     sing N N 365 
PRO C     O      doub N N 366 
PRO C     OXT    sing N N 367 
PRO CB    CG     sing N N 368 
PRO CB    HB2    sing N N 369 
PRO CB    HB3    sing N N 370 
PRO CG    CD     sing N N 371 
PRO CG    HG2    sing N N 372 
PRO CG    HG3    sing N N 373 
PRO CD    HD2    sing N N 374 
PRO CD    HD3    sing N N 375 
PRO OXT   HXT    sing N N 376 
SER N     CA     sing N N 377 
SER N     H      sing N N 378 
SER N     H2     sing N N 379 
SER CA    C      sing N N 380 
SER CA    CB     sing N N 381 
SER CA    HA     sing N N 382 
SER C     O      doub N N 383 
SER C     OXT    sing N N 384 
SER CB    OG     sing N N 385 
SER CB    HB2    sing N N 386 
SER CB    HB3    sing N N 387 
SER OG    HG     sing N N 388 
SER OXT   HXT    sing N N 389 
THR N     CA     sing N N 390 
THR N     H      sing N N 391 
THR N     H2     sing N N 392 
THR CA    C      sing N N 393 
THR CA    CB     sing N N 394 
THR CA    HA     sing N N 395 
THR C     O      doub N N 396 
THR C     OXT    sing N N 397 
THR CB    OG1    sing N N 398 
THR CB    CG2    sing N N 399 
THR CB    HB     sing N N 400 
THR OG1   HG1    sing N N 401 
THR CG2   HG21   sing N N 402 
THR CG2   HG22   sing N N 403 
THR CG2   HG23   sing N N 404 
THR OXT   HXT    sing N N 405 
TRP N     CA     sing N N 406 
TRP N     H      sing N N 407 
TRP N     H2     sing N N 408 
TRP CA    C      sing N N 409 
TRP CA    CB     sing N N 410 
TRP CA    HA     sing N N 411 
TRP C     O      doub N N 412 
TRP C     OXT    sing N N 413 
TRP CB    CG     sing N N 414 
TRP CB    HB2    sing N N 415 
TRP CB    HB3    sing N N 416 
TRP CG    CD1    doub Y N 417 
TRP CG    CD2    sing Y N 418 
TRP CD1   NE1    sing Y N 419 
TRP CD1   HD1    sing N N 420 
TRP CD2   CE2    doub Y N 421 
TRP CD2   CE3    sing Y N 422 
TRP NE1   CE2    sing Y N 423 
TRP NE1   HE1    sing N N 424 
TRP CE2   CZ2    sing Y N 425 
TRP CE3   CZ3    doub Y N 426 
TRP CE3   HE3    sing N N 427 
TRP CZ2   CH2    doub Y N 428 
TRP CZ2   HZ2    sing N N 429 
TRP CZ3   CH2    sing Y N 430 
TRP CZ3   HZ3    sing N N 431 
TRP CH2   HH2    sing N N 432 
TRP OXT   HXT    sing N N 433 
TYR N     CA     sing N N 434 
TYR N     H      sing N N 435 
TYR N     H2     sing N N 436 
TYR CA    C      sing N N 437 
TYR CA    CB     sing N N 438 
TYR CA    HA     sing N N 439 
TYR C     O      doub N N 440 
TYR C     OXT    sing N N 441 
TYR CB    CG     sing N N 442 
TYR CB    HB2    sing N N 443 
TYR CB    HB3    sing N N 444 
TYR CG    CD1    doub Y N 445 
TYR CG    CD2    sing Y N 446 
TYR CD1   CE1    sing Y N 447 
TYR CD1   HD1    sing N N 448 
TYR CD2   CE2    doub Y N 449 
TYR CD2   HD2    sing N N 450 
TYR CE1   CZ     doub Y N 451 
TYR CE1   HE1    sing N N 452 
TYR CE2   CZ     sing Y N 453 
TYR CE2   HE2    sing N N 454 
TYR CZ    OH     sing N N 455 
TYR OH    HH     sing N N 456 
TYR OXT   HXT    sing N N 457 
VAL N     CA     sing N N 458 
VAL N     H      sing N N 459 
VAL N     H2     sing N N 460 
VAL CA    C      sing N N 461 
VAL CA    CB     sing N N 462 
VAL CA    HA     sing N N 463 
VAL C     O      doub N N 464 
VAL C     OXT    sing N N 465 
VAL CB    CG1    sing N N 466 
VAL CB    CG2    sing N N 467 
VAL CB    HB     sing N N 468 
VAL CG1   HG11   sing N N 469 
VAL CG1   HG12   sing N N 470 
VAL CG1   HG13   sing N N 471 
VAL CG2   HG21   sing N N 472 
VAL CG2   HG22   sing N N 473 
VAL CG2   HG23   sing N N 474 
VAL OXT   HXT    sing N N 475 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Academy of Finland'                                             Finland          308105       1 
'Academy of Finland'                                             Finland          1355187      2 
'Academy of Finland'                                             Finland          1322609      3 
'Academy of Finland'                                             Finland          13364501     4 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/T006048/1 5 
# 
_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   4av3 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9G8K 
_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]   0.011941 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003576 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008956 
_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]   0.009923 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CA ? ? 16.26893 3.65395 ? ? 3.58509  77.28589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.99627  ?       ? ? 14.84254 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153  2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 6.96715  ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 7.96527  ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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      . TYR A 1 11  ? 7.00800   0.44700   74.83000  1.000 157.46000 ? 2   TYR A N      1 
ATOM   2     C  CA     . TYR A 1 11  ? 6.69800   -0.86200  75.38900  1.000 151.84000 ? 2   TYR A CA     1 
ATOM   3     C  C      . TYR A 1 11  ? 7.77200   -1.86900  74.97800  1.000 148.93000 ? 2   TYR A C      1 
ATOM   4     O  O      . TYR A 1 11  ? 8.92100   -1.77400  75.41200  1.000 137.88000 ? 2   TYR A O      1 
ATOM   5     C  CB     . TYR A 1 11  ? 5.31200   -1.32500  74.93100  1.000 134.59000 ? 2   TYR A CB     1 
ATOM   6     C  CG     . TYR A 1 11  ? 4.71000   -2.43100  75.77100  1.000 149.21000 ? 2   TYR A CG     1 
ATOM   7     C  CD1    . TYR A 1 11  ? 4.15400   -2.16200  77.01600  1.000 154.43000 ? 2   TYR A CD1    1 
ATOM   8     C  CD2    . TYR A 1 11  ? 4.68700   -3.74300  75.31500  1.000 143.15000 ? 2   TYR A CD2    1 
ATOM   9     C  CE1    . TYR A 1 11  ? 3.59900   -3.17000  77.78400  1.000 152.79000 ? 2   TYR A CE1    1 
ATOM   10    C  CE2    . TYR A 1 11  ? 4.13500   -4.75700  76.07500  1.000 133.04000 ? 2   TYR A CE2    1 
ATOM   11    C  CZ     . TYR A 1 11  ? 3.59300   -4.46500  77.30800  1.000 142.77000 ? 2   TYR A CZ     1 
ATOM   12    O  OH     . TYR A 1 11  ? 3.04200   -5.47200  78.06600  1.000 140.84000 ? 2   TYR A OH     1 
ATOM   13    N  N      . VAL A 1 12  ? 7.39300   -2.82900  74.13700  1.000 155.38000 ? 3   VAL A N      1 
ATOM   14    C  CA     . VAL A 1 12  ? 8.31600   -3.82300  73.61100  1.000 151.44000 ? 3   VAL A CA     1 
ATOM   15    C  C      . VAL A 1 12  ? 8.65100   -3.55700  72.14900  1.000 143.77000 ? 3   VAL A C      1 
ATOM   16    O  O      . VAL A 1 12  ? 9.77800   -3.80200  71.71100  1.000 124.26000 ? 3   VAL A O      1 
ATOM   17    C  CB     . VAL A 1 12  ? 7.74900   -5.24800  73.79400  1.000 143.04000 ? 3   VAL A CB     1 
ATOM   18    C  CG1    . VAL A 1 12  ? 8.67300   -6.27500  73.15300  1.000 125.41000 ? 3   VAL A CG1    1 
ATOM   19    C  CG2    . VAL A 1 12  ? 7.53700   -5.55100  75.27000  1.000 144.54000 ? 3   VAL A CG2    1 
ATOM   20    N  N      . ALA A 1 13  ? 7.68200   -3.05500  71.38000  1.000 155.05000 ? 4   ALA A N      1 
ATOM   21    C  CA     . ALA A 1 13  ? 7.92400   -2.69400  69.99000  1.000 133.07000 ? 4   ALA A CA     1 
ATOM   22    C  C      . ALA A 1 13  ? 9.00000   -1.62800  69.85700  1.000 125.00000 ? 4   ALA A C      1 
ATOM   23    O  O      . ALA A 1 13  ? 9.62500   -1.52100  68.79600  1.000 140.88000 ? 4   ALA A O      1 
ATOM   24    C  CB     . ALA A 1 13  ? 6.62700   -2.21600  69.33500  1.000 124.76000 ? 4   ALA A CB     1 
ATOM   25    N  N      . ALA A 1 14  ? 9.23300   -0.84100  70.91000  1.000 95.54000  ? 5   ALA A N      1 
ATOM   26    C  CA     . ALA A 1 14  ? 10.27300  0.17900   70.86300  1.000 108.10000 ? 5   ALA A CA     1 
ATOM   27    C  C      . ALA A 1 14  ? 11.65900  -0.41700  70.65700  1.000 126.71000 ? 5   ALA A C      1 
ATOM   28    O  O      . ALA A 1 14  ? 12.56900  0.29900   70.22600  1.000 127.42000 ? 5   ALA A O      1 
ATOM   29    C  CB     . ALA A 1 14  ? 10.24700  1.01400   72.14400  1.000 107.04000 ? 5   ALA A CB     1 
ATOM   30    N  N      . LEU A 1 15  ? 11.84500  -1.70800  70.94400  1.000 131.12000 ? 6   LEU A N      1 
ATOM   31    C  CA     . LEU A 1 15  ? 13.12900  -2.34300  70.67500  1.000 135.54000 ? 6   LEU A CA     1 
ATOM   32    C  C      . LEU A 1 15  ? 13.25700  -2.81300  69.23200  1.000 129.45000 ? 6   LEU A C      1 
ATOM   33    O  O      . LEU A 1 15  ? 14.37400  -3.07900  68.77700  1.000 135.31000 ? 6   LEU A O      1 
ATOM   34    C  CB     . LEU A 1 15  ? 13.35000  -3.52300  71.62600  1.000 129.54000 ? 6   LEU A CB     1 
ATOM   35    C  CG     . LEU A 1 15  ? 13.55200  -3.16600  73.10100  1.000 117.83000 ? 6   LEU A CG     1 
ATOM   36    C  CD1    . LEU A 1 15  ? 12.21300  -3.04400  73.81300  1.000 128.89000 ? 6   LEU A CD1    1 
ATOM   37    C  CD2    . LEU A 1 15  ? 14.44200  -4.18900  73.78800  1.000 93.50000  ? 6   LEU A CD2    1 
ATOM   38    N  N      . PHE A 1 16  ? 12.14400  -2.92800  68.50800  1.000 115.35000 ? 7   PHE A N      1 
ATOM   39    C  CA     . PHE A 1 16  ? 12.18200  -3.11200  67.06200  1.000 110.29000 ? 7   PHE A CA     1 
ATOM   40    C  C      . PHE A 1 16  ? 12.29700  -1.78100  66.33000  1.000 119.07000 ? 7   PHE A C      1 
ATOM   41    O  O      . PHE A 1 16  ? 13.03000  -1.67400  65.34100  1.000 120.16000 ? 7   PHE A O      1 
ATOM   42    C  CB     . PHE A 1 16  ? 10.93700  -3.86700  66.58800  1.000 106.09000 ? 7   PHE A CB     1 
ATOM   43    C  CG     . PHE A 1 16  ? 10.77200  -5.21600  67.21900  1.000 98.02000  ? 7   PHE A CG     1 
ATOM   44    C  CD1    . PHE A 1 16  ? 11.60400  -6.26500  66.86500  1.000 96.66000  ? 7   PHE A CD1    1 
ATOM   45    C  CD2    . PHE A 1 16  ? 9.78600   -5.43800  68.16300  1.000 119.06000 ? 7   PHE A CD2    1 
ATOM   46    C  CE1    . PHE A 1 16  ? 11.45600  -7.51000  67.44300  1.000 113.60000 ? 7   PHE A CE1    1 
ATOM   47    C  CE2    . PHE A 1 16  ? 9.63200   -6.68300  68.74500  1.000 127.47000 ? 7   PHE A CE2    1 
ATOM   48    C  CZ     . PHE A 1 16  ? 10.46800  -7.72000  68.38400  1.000 113.25000 ? 7   PHE A CZ     1 
ATOM   49    N  N      . PHE A 1 17  ? 11.57300  -0.76500  66.80600  1.000 127.99000 ? 8   PHE A N      1 
ATOM   50    C  CA     . PHE A 1 17  ? 11.67000  0.58400   66.25900  1.000 144.45000 ? 8   PHE A CA     1 
ATOM   51    C  C      . PHE A 1 17  ? 13.10500  1.09400   66.18900  1.000 151.96000 ? 8   PHE A C      1 
ATOM   52    O  O      . PHE A 1 17  ? 13.40300  1.96800   65.36600  1.000 158.77000 ? 8   PHE A O      1 
ATOM   53    C  CB     . PHE A 1 17  ? 10.80200  1.51900   67.11200  1.000 146.07000 ? 8   PHE A CB     1 
ATOM   54    C  CG     . PHE A 1 17  ? 11.11300  2.97800   66.94100  1.000 154.19000 ? 8   PHE A CG     1 
ATOM   55    C  CD1    . PHE A 1 17  ? 10.72400  3.65900   65.80300  1.000 158.95000 ? 8   PHE A CD1    1 
ATOM   56    C  CD2    . PHE A 1 17  ? 11.77800  3.67500   67.93600  1.000 157.79000 ? 8   PHE A CD2    1 
ATOM   57    C  CE1    . PHE A 1 17  ? 11.00500  5.00100   65.65000  1.000 160.12000 ? 8   PHE A CE1    1 
ATOM   58    C  CE2    . PHE A 1 17  ? 12.06000  5.01700   67.79100  1.000 176.45000 ? 8   PHE A CE2    1 
ATOM   59    C  CZ     . PHE A 1 17  ? 11.67300  5.68200   66.64500  1.000 165.11000 ? 8   PHE A CZ     1 
ATOM   60    N  N      . LEU A 1 18  ? 13.99900  0.56800   67.02500  1.000 139.20000 ? 9   LEU A N      1 
ATOM   61    C  CA     . LEU A 1 18  ? 15.39000  1.00600   67.04200  1.000 131.99000 ? 9   LEU A CA     1 
ATOM   62    C  C      . LEU A 1 18  ? 16.25000  0.35500   65.96400  1.000 122.37000 ? 9   LEU A C      1 
ATOM   63    O  O      . LEU A 1 18  ? 17.34100  0.86300   65.67400  1.000 114.32000 ? 9   LEU A O      1 
ATOM   64    C  CB     . LEU A 1 18  ? 15.99600  0.74000   68.42300  1.000 144.08000 ? 9   LEU A CB     1 
ATOM   65    C  CG     . LEU A 1 18  ? 15.96900  -0.70100  68.94100  1.000 136.60000 ? 9   LEU A CG     1 
ATOM   66    C  CD1    . LEU A 1 18  ? 17.10300  -1.53000  68.35100  1.000 127.31000 ? 9   LEU A CD1    1 
ATOM   67    C  CD2    . LEU A 1 18  ? 16.01300  -0.73600  70.46400  1.000 143.04000 ? 9   LEU A CD2    1 
ATOM   68    N  N      . ILE A 1 19  ? 15.79200  -0.74300  65.35700  1.000 118.04000 ? 10  ILE A N      1 
ATOM   69    C  CA     . ILE A 1 19  ? 16.63800  -1.49500  64.42600  1.000 110.87000 ? 10  ILE A CA     1 
ATOM   70    C  C      . ILE A 1 19  ? 17.08700  -0.65200  63.23400  1.000 110.53000 ? 10  ILE A C      1 
ATOM   71    O  O      . ILE A 1 19  ? 18.26100  -0.74000  62.85000  1.000 111.93000 ? 10  ILE A O      1 
ATOM   72    C  CB     . ILE A 1 19  ? 15.95600  -2.79600  64.01500  1.000 107.39000 ? 10  ILE A CB     1 
ATOM   73    C  CG1    . ILE A 1 19  ? 15.77700  -3.71300  65.22900  1.000 105.57000 ? 10  ILE A CG1    1 
ATOM   74    C  CG2    . ILE A 1 19  ? 16.75900  -3.50900  62.93400  1.000 117.91000 ? 10  ILE A CG2    1 
ATOM   75    C  CD1    . ILE A 1 19  ? 15.19600  -5.06800  64.89300  1.000 110.13000 ? 10  ILE A CD1    1 
ATOM   76    N  N      . PRO A 1 20  ? 16.22900  0.14900   62.59400  1.000 109.64000 ? 11  PRO A N      1 
ATOM   77    C  CA     . PRO A 1 20  ? 16.71500  0.94500   61.45000  1.000 112.93000 ? 11  PRO A CA     1 
ATOM   78    C  C      . PRO A 1 20  ? 17.82200  1.91500   61.82700  1.000 112.04000 ? 11  PRO A C      1 
ATOM   79    O  O      . PRO A 1 20  ? 18.82800  2.02600   61.11000  1.000 96.55000  ? 11  PRO A O      1 
ATOM   80    C  CB     . PRO A 1 20  ? 15.45100  1.67800   60.97600  1.000 117.44000 ? 11  PRO A CB     1 
ATOM   81    C  CG     . PRO A 1 20  ? 14.31200  0.85600   61.49400  1.000 114.85000 ? 11  PRO A CG     1 
ATOM   82    C  CD     . PRO A 1 20  ? 14.78200  0.30800   62.80500  1.000 107.74000 ? 11  PRO A CD     1 
ATOM   83    N  N      . LEU A 1 21  ? 17.65900  2.62800   62.94200  1.000 123.07000 ? 12  LEU A N      1 
ATOM   84    C  CA     . LEU A 1 21  ? 18.70700  3.53300   63.39700  1.000 115.77000 ? 12  LEU A CA     1 
ATOM   85    C  C      . LEU A 1 21  ? 19.97400  2.76200   63.74200  1.000 106.64000 ? 12  LEU A C      1 
ATOM   86    O  O      . LEU A 1 21  ? 21.08800  3.24200   63.50500  1.000 90.21000  ? 12  LEU A O      1 
ATOM   87    C  CB     . LEU A 1 21  ? 18.21100  4.34200   64.59500  1.000 102.45000 ? 12  LEU A CB     1 
ATOM   88    C  CG     . LEU A 1 21  ? 17.04300  5.28400   64.29600  1.000 90.63000  ? 12  LEU A CG     1 
ATOM   89    C  CD1    . LEU A 1 21  ? 16.49000  5.88800   65.57400  1.000 74.21000  ? 12  LEU A CD1    1 
ATOM   90    C  CD2    . LEU A 1 21  ? 17.47800  6.37700   63.33100  1.000 98.80000  ? 12  LEU A CD2    1 
ATOM   91    N  N      . VAL A 1 22  ? 19.82100  1.56300   64.30800  1.000 107.91000 ? 13  VAL A N      1 
ATOM   92    C  CA     . VAL A 1 22  ? 20.97900  0.72100   64.59600  1.000 99.82000  ? 13  VAL A CA     1 
ATOM   93    C  C      . VAL A 1 22  ? 21.73500  0.41000   63.31300  1.000 103.71000 ? 13  VAL A C      1 
ATOM   94    O  O      . VAL A 1 22  ? 22.96400  0.51500   63.25300  1.000 105.22000 ? 13  VAL A O      1 
ATOM   95    C  CB     . VAL A 1 22  ? 20.54000  -0.56800  65.31400  1.000 93.05000  ? 13  VAL A CB     1 
ATOM   96    C  CG1    . VAL A 1 22  ? 21.68100  -1.57200  65.35200  1.000 56.23000  ? 13  VAL A CG1    1 
ATOM   97    C  CG2    . VAL A 1 22  ? 20.05600  -0.25400  66.71600  1.000 98.13000  ? 13  VAL A CG2    1 
ATOM   98    N  N      . ALA A 1 23  ? 21.00700  0.02200   62.26400  1.000 115.84000 ? 14  ALA A N      1 
ATOM   99    C  CA     . ALA A 1 23  ? 21.65700  -0.29600  60.99800  1.000 115.30000 ? 14  ALA A CA     1 
ATOM   100   C  C      . ALA A 1 23  ? 22.35100  0.92800   60.41700  1.000 112.76000 ? 14  ALA A C      1 
ATOM   101   O  O      . ALA A 1 23  ? 23.46200  0.82600   59.88500  1.000 104.98000 ? 14  ALA A O      1 
ATOM   102   C  CB     . ALA A 1 23  ? 20.63700  -0.85900  60.00900  1.000 121.15000 ? 14  ALA A CB     1 
ATOM   103   N  N      . LEU A 1 24  ? 21.71000  2.09600   60.50500  1.000 110.42000 ? 15  LEU A N      1 
ATOM   104   C  CA     . LEU A 1 24  ? 22.31700  3.31500   59.97300  1.000 111.17000 ? 15  LEU A CA     1 
ATOM   105   C  C      . LEU A 1 24  ? 23.59900  3.66600   60.72400  1.000 101.08000 ? 15  LEU A C      1 
ATOM   106   O  O      . LEU A 1 24  ? 24.63700  3.96500   60.11300  1.000 81.62000  ? 15  LEU A O      1 
ATOM   107   C  CB     . LEU A 1 24  ? 21.31600  4.46800   60.04700  1.000 99.78000  ? 15  LEU A CB     1 
ATOM   108   C  CG     . LEU A 1 24  ? 19.91200  4.17900   59.51600  1.000 87.08000  ? 15  LEU A CG     1 
ATOM   109   C  CD1    . LEU A 1 24  ? 18.95800  5.29400   59.90700  1.000 114.81000 ? 15  LEU A CD1    1 
ATOM   110   C  CD2    . LEU A 1 24  ? 19.93700  3.99500   58.00700  1.000 89.58000  ? 15  LEU A CD2    1 
ATOM   111   N  N      . GLY A 1 25  ? 23.54500  3.62600   62.05600  1.000 92.67000  ? 16  GLY A N      1 
ATOM   112   C  CA     . GLY A 1 25  ? 24.73000  3.91600   62.84200  1.000 103.32000 ? 16  GLY A CA     1 
ATOM   113   C  C      . GLY A 1 25  ? 25.84100  2.91500   62.59900  1.000 106.08000 ? 16  GLY A C      1 
ATOM   114   O  O      . GLY A 1 25  ? 27.01600  3.28000   62.53900  1.000 110.58000 ? 16  GLY A O      1 
ATOM   115   N  N      . PHE A 1 26  ? 25.48400  1.64000   62.44100  1.000 111.48000 ? 17  PHE A N      1 
ATOM   116   C  CA     . PHE A 1 26  ? 26.49700  0.62100   62.20400  1.000 111.76000 ? 17  PHE A CA     1 
ATOM   117   C  C      . PHE A 1 26  ? 27.11600  0.76600   60.81900  1.000 115.61000 ? 17  PHE A C      1 
ATOM   118   O  O      . PHE A 1 26  ? 28.31400  0.52200   60.64800  1.000 120.40000 ? 17  PHE A O      1 
ATOM   119   C  CB     . PHE A 1 26  ? 25.88800  -0.76700  62.40100  1.000 108.65000 ? 17  PHE A CB     1 
ATOM   120   C  CG     . PHE A 1 26  ? 26.82600  -1.88800  62.08800  1.000 108.19000 ? 17  PHE A CG     1 
ATOM   121   C  CD1    . PHE A 1 26  ? 28.06300  -1.95700  62.70100  1.000 133.27000 ? 17  PHE A CD1    1 
ATOM   122   C  CD2    . PHE A 1 26  ? 26.45800  -2.89300  61.21700  1.000 124.71000 ? 17  PHE A CD2    1 
ATOM   123   C  CE1    . PHE A 1 26  ? 28.92900  -2.99100  62.42500  1.000 141.96000 ? 17  PHE A CE1    1 
ATOM   124   C  CE2    . PHE A 1 26  ? 27.32000  -3.93500  60.93700  1.000 135.18000 ? 17  PHE A CE2    1 
ATOM   125   C  CZ     . PHE A 1 26  ? 28.55800  -3.98400  61.54300  1.000 123.38000 ? 17  PHE A CZ     1 
ATOM   126   N  N      . ALA A 1 27  ? 26.32600  1.17900   59.82500  1.000 117.79000 ? 18  ALA A N      1 
ATOM   127   C  CA     . ALA A 1 27  ? 26.89100  1.46400   58.51000  1.000 117.03000 ? 18  ALA A CA     1 
ATOM   128   C  C      . ALA A 1 27  ? 27.85100  2.64500   58.57400  1.000 110.25000 ? 18  ALA A C      1 
ATOM   129   O  O      . ALA A 1 27  ? 28.92800  2.61400   57.96600  1.000 116.42000 ? 18  ALA A O      1 
ATOM   130   C  CB     . ALA A 1 27  ? 25.77300  1.72900   57.50400  1.000 114.84000 ? 18  ALA A CB     1 
ATOM   131   N  N      . ALA A 1 28  ? 27.47500  3.70100   59.30200  1.000 103.59000 ? 19  ALA A N      1 
ATOM   132   C  CA     . ALA A 1 28  ? 28.38700  4.82900   59.47900  1.000 124.88000 ? 19  ALA A CA     1 
ATOM   133   C  C      . ALA A 1 28  ? 29.66800  4.40000   60.19000  1.000 126.31000 ? 19  ALA A C      1 
ATOM   134   O  O      . ALA A 1 28  ? 30.76600  4.86400   59.85200  1.000 115.60000 ? 19  ALA A O      1 
ATOM   135   C  CB     . ALA A 1 28  ? 27.69300  5.95200   60.25100  1.000 133.08000 ? 19  ALA A CB     1 
ATOM   136   N  N      . ALA A 1 29  ? 29.54600  3.51700   61.18300  1.000 126.50000 ? 20  ALA A N      1 
ATOM   137   C  CA     . ALA A 1 29  ? 30.72300  3.01900   61.88700  1.000 111.42000 ? 20  ALA A CA     1 
ATOM   138   C  C      . ALA A 1 29  ? 31.61200  2.19500   60.96800  1.000 116.05000 ? 20  ALA A C      1 
ATOM   139   O  O      . ALA A 1 29  ? 32.84100  2.28800   61.04300  1.000 112.86000 ? 20  ALA A O      1 
ATOM   140   C  CB     . ALA A 1 29  ? 30.30000  2.19500   63.10200  1.000 111.07000 ? 20  ALA A CB     1 
ATOM   141   N  N      . ASN A 1 30  ? 31.01200  1.36700   60.10700  1.000 126.70000 ? 21  ASN A N      1 
ATOM   142   C  CA     . ASN A 1 30  ? 31.79800  0.62500   59.12500  1.000 114.90000 ? 21  ASN A CA     1 
ATOM   143   C  C      . ASN A 1 30  ? 32.52000  1.57300   58.18100  1.000 122.04000 ? 21  ASN A C      1 
ATOM   144   O  O      . ASN A 1 30  ? 33.69200  1.36000   57.84600  1.000 130.82000 ? 21  ASN A O      1 
ATOM   145   C  CB     . ASN A 1 30  ? 30.89800  -0.32500  58.33400  1.000 107.18000 ? 21  ASN A CB     1 
ATOM   146   C  CG     . ASN A 1 30  ? 30.45800  -1.52800  59.14700  1.000 121.76000 ? 21  ASN A CG     1 
ATOM   147   O  OD1    . ASN A 1 30  ? 30.77500  -1.64200  60.33000  1.000 132.84000 ? 21  ASN A OD1    1 
ATOM   148   N  ND2    . ASN A 1 30  ? 29.72000  -2.43300  58.51500  1.000 123.34000 ? 21  ASN A ND2    1 
ATOM   149   N  N      . PHE A 1 31  ? 31.83800  2.63600   57.75200  1.000 120.60000 ? 22  PHE A N      1 
ATOM   150   C  CA     . PHE A 1 31  ? 32.47600  3.63400   56.90100  1.000 121.80000 ? 22  PHE A CA     1 
ATOM   151   C  C      . PHE A 1 31  ? 33.68100  4.25100   57.59800  1.000 134.26000 ? 22  PHE A C      1 
ATOM   152   O  O      . PHE A 1 31  ? 34.76400  4.36300   57.01200  1.000 138.38000 ? 22  PHE A O      1 
ATOM   153   C  CB     . PHE A 1 31  ? 31.46700  4.71700   56.51600  1.000 122.10000 ? 22  PHE A CB     1 
ATOM   154   C  CG     . PHE A 1 31  ? 32.07600  5.88700   55.79500  1.000 129.14000 ? 22  PHE A CG     1 
ATOM   155   C  CD1    . PHE A 1 31  ? 32.42400  5.79400   54.45800  1.000 131.73000 ? 22  PHE A CD1    1 
ATOM   156   C  CD2    . PHE A 1 31  ? 32.29900  7.08300   56.45800  1.000 127.30000 ? 22  PHE A CD2    1 
ATOM   157   C  CE1    . PHE A 1 31  ? 32.98100  6.87500   53.79400  1.000 140.43000 ? 22  PHE A CE1    1 
ATOM   158   C  CE2    . PHE A 1 31  ? 32.85600  8.16500   55.80200  1.000 140.88000 ? 22  PHE A CE2    1 
ATOM   159   C  CZ     . PHE A 1 31  ? 33.19700  8.06200   54.46900  1.000 153.96000 ? 22  PHE A CZ     1 
ATOM   160   N  N      . ALA A 1 32  ? 33.51300  4.65000   58.86000  1.000 133.45000 ? 23  ALA A N      1 
ATOM   161   C  CA     . ALA A 1 32  ? 34.61800  5.26700   59.58600  1.000 131.02000 ? 23  ALA A CA     1 
ATOM   162   C  C      . ALA A 1 32  ? 35.77100  4.28700   59.78800  1.000 138.56000 ? 23  ALA A C      1 
ATOM   163   O  O      . ALA A 1 32  ? 36.94100  4.64200   59.59500  1.000 146.06000 ? 23  ALA A O      1 
ATOM   164   C  CB     . ALA A 1 32  ? 34.12600  5.80700   60.93000  1.000 113.86000 ? 23  ALA A CB     1 
ATOM   165   N  N      . ALA A 1 33  ? 35.45900  3.04100   60.16000  1.000 129.07000 ? 24  ALA A N      1 
ATOM   166   C  CA     . ALA A 1 33  ? 36.50200  2.04900   60.40300  1.000 121.97000 ? 24  ALA A CA     1 
ATOM   167   C  C      . ALA A 1 33  ? 37.27200  1.71300   59.13100  1.000 132.75000 ? 24  ALA A C      1 
ATOM   168   O  O      . ALA A 1 33  ? 38.48400  1.47000   59.18000  1.000 145.52000 ? 24  ALA A O      1 
ATOM   169   C  CB     . ALA A 1 33  ? 35.89200  0.78500   61.00900  1.000 97.90000  ? 24  ALA A CB     1 
ATOM   170   N  N      . VAL A 1 34  ? 36.58900  1.67500   57.98500  1.000 128.66000 ? 25  VAL A N      1 
ATOM   171   C  CA     . VAL A 1 34  ? 37.29000  1.44500   56.72500  1.000 125.23000 ? 25  VAL A CA     1 
ATOM   172   C  C      . VAL A 1 34  ? 38.11500  2.66700   56.33600  1.000 131.37000 ? 25  VAL A C      1 
ATOM   173   O  O      . VAL A 1 34  ? 39.22200  2.53800   55.79900  1.000 132.56000 ? 25  VAL A O      1 
ATOM   174   C  CB     . VAL A 1 34  ? 36.29600  1.05600   55.61600  1.000 125.69000 ? 25  VAL A CB     1 
ATOM   175   C  CG1    . VAL A 1 34  ? 35.40500  -0.09000  56.07600  1.000 121.30000 ? 25  VAL A CG1    1 
ATOM   176   C  CG2    . VAL A 1 34  ? 35.46200  2.25700   55.22800  1.000 138.97000 ? 25  VAL A CG2    1 
ATOM   177   N  N      . VAL A 1 35  ? 37.59000  3.87000   56.59300  1.000 130.80000 ? 26  VAL A N      1 
ATOM   178   C  CA     . VAL A 1 35  ? 38.34400  5.09000   56.31700  1.000 136.95000 ? 26  VAL A CA     1 
ATOM   179   C  C      . VAL A 1 35  ? 39.62200  5.12400   57.13900  1.000 153.03000 ? 26  VAL A C      1 
ATOM   180   O  O      . VAL A 1 35  ? 40.63900  5.67600   56.70000  1.000 153.57000 ? 26  VAL A O      1 
ATOM   181   C  CB     . VAL A 1 35  ? 37.47100  6.33500   56.57700  1.000 124.68000 ? 26  VAL A CB     1 
ATOM   182   C  CG1    . VAL A 1 35  ? 38.30500  7.60200   56.46100  1.000 143.68000 ? 26  VAL A CG1    1 
ATOM   183   C  CG2    . VAL A 1 35  ? 36.30200  6.37700   55.60700  1.000 129.96000 ? 26  VAL A CG2    1 
ATOM   184   N  N      . ARG A 1 36  ? 39.59500  4.54900   58.34500  1.000 153.73000 ? 27  ARG A N      1 
ATOM   185   C  CA     . ARG A 1 36  ? 40.81400  4.46700   59.14300  1.000 151.26000 ? 27  ARG A CA     1 
ATOM   186   C  C      . ARG A 1 36  ? 41.87900  3.62600   58.44900  1.000 154.39000 ? 27  ARG A C      1 
ATOM   187   O  O      . ARG A 1 36  ? 43.07700  3.89100   58.60400  1.000 169.01000 ? 27  ARG A O      1 
ATOM   188   C  CB     . ARG A 1 36  ? 40.50200  3.89600   60.52800  1.000 140.06000 ? 27  ARG A CB     1 
ATOM   189   C  CG     . ARG A 1 36  ? 39.71600  4.83900   61.43200  1.000 140.95000 ? 27  ARG A CG     1 
ATOM   190   C  CD     . ARG A 1 36  ? 39.62600  4.31800   62.86300  1.000 127.50000 ? 27  ARG A CD     1 
ATOM   191   N  NE     . ARG A 1 36  ? 38.79800  3.12400   62.97700  1.000 119.99000 ? 27  ARG A NE     1 
ATOM   192   C  CZ     . ARG A 1 36  ? 39.27000  1.88600   63.04200  1.000 118.92000 ? 27  ARG A CZ     1 
ATOM   193   N  NH1    . ARG A 1 36  ? 40.56900  1.63900   63.00700  1.000 108.23000 ? 27  ARG A NH1    1 
ATOM   194   N  NH2    . ARG A 1 36  ? 38.41600  0.87100   63.14400  1.000 114.70000 ? 27  ARG A NH2    1 
ATOM   195   N  N      . LYS A 1 37  ? 41.46800  2.61400   57.69400  1.000 143.11000 ? 28  LYS A N      1 
ATOM   196   C  CA     . LYS A 1 37  ? 42.42000  1.74800   57.01400  1.000 152.94000 ? 28  LYS A CA     1 
ATOM   197   C  C      . LYS A 1 37  ? 43.25100  2.53700   56.00100  1.000 160.94000 ? 28  LYS A C      1 
ATOM   198   O  O      . LYS A 1 37  ? 42.73300  3.44400   55.33500  1.000 151.75000 ? 28  LYS A O      1 
ATOM   199   C  CB     . LYS A 1 37  ? 41.69200  0.59700   56.31500  1.000 146.37000 ? 28  LYS A CB     1 
ATOM   200   N  N      . PRO A 1 38  ? 44.53800  2.22800   55.87000  1.000 163.46000 ? 29  PRO A N      1 
ATOM   201   C  CA     . PRO A 1 38  ? 45.40500  2.95600   54.93800  1.000 147.73000 ? 29  PRO A CA     1 
ATOM   202   C  C      . PRO A 1 38  ? 45.17300  2.52400   53.49500  1.000 146.93000 ? 29  PRO A C      1 
ATOM   203   O  O      . PRO A 1 38  ? 44.65400  1.44300   53.21200  1.000 151.63000 ? 29  PRO A O      1 
ATOM   204   C  CB     . PRO A 1 38  ? 46.81300  2.57600   55.40700  1.000 149.44000 ? 29  PRO A CB     1 
ATOM   205   C  CG     . PRO A 1 38  ? 46.64500  1.20400   55.95500  1.000 156.29000 ? 29  PRO A CG     1 
ATOM   206   C  CD     . PRO A 1 38  ? 45.26500  1.16000   56.57700  1.000 169.34000 ? 29  PRO A CD     1 
ATOM   207   N  N      . GLU A 1 39  ? 45.58100  3.39900   52.57200  1.000 147.44000 ? 30  GLU A N      1 
ATOM   208   C  CA     . GLU A 1 39  ? 45.42300  3.13600   51.14500  1.000 132.93000 ? 30  GLU A CA     1 
ATOM   209   C  C      . GLU A 1 39  ? 46.68900  2.60700   50.48700  1.000 136.09000 ? 30  GLU A C      1 
ATOM   210   O  O      . GLU A 1 39  ? 46.60900  2.04400   49.38900  1.000 118.64000 ? 30  GLU A O      1 
ATOM   211   C  CB     . GLU A 1 39  ? 44.98200  4.40800   50.40800  1.000 127.55000 ? 30  GLU A CB     1 
ATOM   212   C  CG     . GLU A 1 39  ? 43.74900  5.09100   50.98700  1.000 143.14000 ? 30  GLU A CG     1 
ATOM   213   C  CD     . GLU A 1 39  ? 44.06800  5.97500   52.17700  1.000 157.19000 ? 30  GLU A CD     1 
ATOM   214   O  OE1    . GLU A 1 39  ? 45.21700  6.45900   52.27500  1.000 167.39000 ? 30  GLU A OE1    1 
ATOM   215   O  OE2    . GLU A 1 39  ? 43.16700  6.18300   53.01700  1.000 171.27000 ? 30  GLU A OE2    1 
ATOM   216   N  N      . GLY A 1 40  ? 47.83900  2.77100   51.12500  1.000 152.68000 ? 31  GLY A N      1 
ATOM   217   C  CA     . GLY A 1 40  ? 49.05900  2.16200   50.61800  1.000 139.59000 ? 31  GLY A CA     1 
ATOM   218   C  C      . GLY A 1 40  ? 49.71400  3.01000   49.54800  1.000 138.22000 ? 31  GLY A C      1 
ATOM   219   O  O      . GLY A 1 40  ? 49.88600  4.22300   49.71100  1.000 130.68000 ? 31  GLY A O      1 
ATOM   220   N  N      . THR A 1 41  ? 50.09000  2.36100   48.44700  1.000 142.93000 ? 32  THR A N      1 
ATOM   221   C  CA     . THR A 1 41  ? 50.82200  3.02800   47.37800  1.000 151.24000 ? 32  THR A CA     1 
ATOM   222   C  C      . THR A 1 41  ? 50.03900  4.22000   46.84000  1.000 153.17000 ? 32  THR A C      1 
ATOM   223   O  O      . THR A 1 41  ? 48.80800  4.19800   46.76900  1.000 164.24000 ? 32  THR A O      1 
ATOM   224   C  CB     . THR A 1 41  ? 51.11000  2.04200   46.24500  1.000 145.48000 ? 32  THR A CB     1 
ATOM   225   O  OG1    . THR A 1 41  ? 51.71600  0.85700   46.77900  1.000 116.93000 ? 32  THR A OG1    1 
ATOM   226   C  CG2    . THR A 1 41  ? 52.04900  2.66600   45.22700  1.000 146.76000 ? 32  THR A CG2    1 
ATOM   227   N  N      . GLU A 1 42  ? 50.77100  5.26300   46.44300  1.000 145.23000 ? 33  GLU A N      1 
ATOM   228   C  CA     . GLU A 1 42  ? 50.14400  6.50400   45.99800  1.000 156.62000 ? 33  GLU A CA     1 
ATOM   229   C  C      . GLU A 1 42  ? 49.66400  6.41700   44.55200  1.000 166.70000 ? 33  GLU A C      1 
ATOM   230   O  O      . GLU A 1 42  ? 48.63100  7.00300   44.20200  1.000 170.19000 ? 33  GLU A O      1 
ATOM   231   C  CB     . GLU A 1 42  ? 51.11700  7.67100   46.16900  1.000 176.01000 ? 33  GLU A CB     1 
ATOM   232   N  N      . ARG A 1 43  ? 50.40100  5.70500   43.69600  1.000 166.68000 ? 34  ARG A N      1 
ATOM   233   C  CA     . ARG A 1 43  ? 50.02100  5.62500   42.28900  1.000 160.27000 ? 34  ARG A CA     1 
ATOM   234   C  C      . ARG A 1 43  ? 48.64400  4.99200   42.12000  1.000 161.33000 ? 34  ARG A C      1 
ATOM   235   O  O      . ARG A 1 43  ? 47.83000  5.47000   41.32200  1.000 161.07000 ? 34  ARG A O      1 
ATOM   236   C  CB     . ARG A 1 43  ? 51.08400  4.84700   41.51300  1.000 157.13000 ? 34  ARG A CB     1 
ATOM   237   C  CG     . ARG A 1 43  ? 52.50300  5.36900   41.73500  1.000 143.04000 ? 34  ARG A CG     1 
ATOM   238   C  CD     . ARG A 1 43  ? 53.47600  4.84600   40.68700  1.000 151.32000 ? 34  ARG A CD     1 
ATOM   239   N  NE     . ARG A 1 43  ? 53.41200  3.39500   40.55200  1.000 169.72000 ? 34  ARG A NE     1 
ATOM   240   C  CZ     . ARG A 1 43  ? 54.10900  2.69300   39.66900  1.000 180.25000 ? 34  ARG A CZ     1 
ATOM   241   N  NH1    . ARG A 1 43  ? 54.93400  3.27900   38.81600  1.000 177.91000 ? 34  ARG A NH1    1 
ATOM   242   N  NH2    . ARG A 1 43  ? 53.98100  1.36900   39.64500  1.000 189.33000 ? 34  ARG A NH2    1 
ATOM   243   N  N      . MET A 1 44  ? 48.36500  3.91100   42.85500  1.000 164.89000 ? 35  MET A N      1 
ATOM   244   C  CA     . MET A 1 44  ? 47.03700  3.30200   42.80300  1.000 166.98000 ? 35  MET A CA     1 
ATOM   245   C  C      . MET A 1 44  ? 45.98500  4.23100   43.40600  1.000 167.19000 ? 35  MET A C      1 
ATOM   246   O  O      . MET A 1 44  ? 44.85400  4.32700   42.90100  1.000 168.34000 ? 35  MET A O      1 
ATOM   247   C  CB     . MET A 1 44  ? 47.06400  1.94400   43.51500  1.000 164.80000 ? 35  MET A CB     1 
ATOM   248   C  CG     . MET A 1 44  ? 47.52500  1.99200   44.97500  1.000 149.44000 ? 35  MET A CG     1 
ATOM   249   S  SD     . MET A 1 44  ? 47.56800  0.37400   45.78800  1.000 142.65000 ? 35  MET A SD     1 
ATOM   250   C  CE     . MET A 1 44  ? 48.56200  -0.57000  44.63400  1.000 131.23000 ? 35  MET A CE     1 
ATOM   251   N  N      . LYS A 1 45  ? 46.34700  4.92500   44.48800  1.000 159.71000 ? 36  LYS A N      1 
ATOM   252   C  CA     . LYS A 1 45  ? 45.40600  5.81800   45.14900  1.000 151.68000 ? 36  LYS A CA     1 
ATOM   253   C  C      . LYS A 1 45  ? 44.95200  6.92400   44.20700  1.000 156.21000 ? 36  LYS A C      1 
ATOM   254   O  O      . LYS A 1 45  ? 43.80900  7.38700   44.28800  1.000 174.86000 ? 36  LYS A O      1 
ATOM   255   C  CB     . LYS A 1 45  ? 46.04000  6.40500   46.40900  1.000 153.42000 ? 36  LYS A CB     1 
ATOM   256   N  N      . GLU A 1 46  ? 45.84600  7.38900   43.33000  1.000 155.28000 ? 37  GLU A N      1 
ATOM   257   C  CA     . GLU A 1 46  ? 45.47700  8.45000   42.39500  1.000 148.97000 ? 37  GLU A CA     1 
ATOM   258   C  C      . GLU A 1 46  ? 44.35200  7.99500   41.46800  1.000 155.02000 ? 37  GLU A C      1 
ATOM   259   O  O      . GLU A 1 46  ? 43.38100  8.72800   41.22600  1.000 156.79000 ? 37  GLU A O      1 
ATOM   260   C  CB     . GLU A 1 46  ? 46.70400  8.88300   41.59100  1.000 132.16000 ? 37  GLU A CB     1 
ATOM   261   N  N      . ILE A 1 47  ? 44.47300  6.78200   40.92800  1.000 156.25000 ? 38  ILE A N      1 
ATOM   262   C  CA     . ILE A 1 47  ? 43.42800  6.25600   40.05800  1.000 148.31000 ? 38  ILE A CA     1 
ATOM   263   C  C      . ILE A 1 47  ? 42.13700  6.07500   40.84700  1.000 147.67000 ? 38  ILE A C      1 
ATOM   264   O  O      . ILE A 1 47  ? 41.03200  6.32100   40.33800  1.000 150.18000 ? 38  ILE A O      1 
ATOM   265   C  CB     . ILE A 1 47  ? 43.89300  4.94400   39.39700  1.000 133.75000 ? 38  ILE A CB     1 
ATOM   266   C  CG1    . ILE A 1 47  ? 45.30700  5.10400   38.82600  1.000 136.17000 ? 38  ILE A CG1    1 
ATOM   267   C  CG2    . ILE A 1 47  ? 42.93300  4.53200   38.29400  1.000 133.59000 ? 38  ILE A CG2    1 
ATOM   268   C  CD1    . ILE A 1 47  ? 45.41100  6.09400   37.67500  1.000 119.81000 ? 38  ILE A CD1    1 
ATOM   269   N  N      . SER A 1 48  ? 42.25200  5.63000   42.10200  1.000 143.54000 ? 39  SER A N      1 
ATOM   270   C  CA     . SER A 1 48  ? 41.05300  5.49500   42.92600  1.000 137.01000 ? 39  SER A CA     1 
ATOM   271   C  C      . SER A 1 48  ? 40.36400  6.84400   43.11800  1.000 141.68000 ? 39  SER A C      1 
ATOM   272   O  O      . SER A 1 48  ? 39.13000  6.93400   43.10100  1.000 149.33000 ? 39  SER A O      1 
ATOM   273   C  CB     . SER A 1 48  ? 41.40400  4.86600   44.27400  1.000 134.10000 ? 39  SER A CB     1 
ATOM   274   O  OG     . SER A 1 48  ? 40.30300  4.91800   45.16400  1.000 129.47000 ? 39  SER A OG     1 
ATOM   275   N  N      . SER A 1 49  ? 41.15200  7.90500   43.31400  1.000 146.90000 ? 40  SER A N      1 
ATOM   276   C  CA     . SER A 1 49  ? 40.59100  9.24800   43.43300  1.000 154.19000 ? 40  SER A CA     1 
ATOM   277   C  C      . SER A 1 49  ? 39.88500  9.65400   42.14600  1.000 152.23000 ? 40  SER A C      1 
ATOM   278   O  O      . SER A 1 49  ? 38.82300  10.29200  42.17900  1.000 154.65000 ? 40  SER A O      1 
ATOM   279   C  CB     . SER A 1 49  ? 41.69900  10.24400  43.78900  1.000 164.62000 ? 40  SER A CB     1 
ATOM   280   O  OG     . SER A 1 49  ? 41.21000  11.57000  43.93000  1.000 186.00000 ? 40  SER A OG     1 
ATOM   281   N  N      . TYR A 1 50  ? 40.47600  9.31100   40.99900  1.000 137.05000 ? 41  TYR A N      1 
ATOM   282   C  CA     . TYR A 1 50  ? 39.82600  9.62400   39.73000  1.000 125.93000 ? 41  TYR A CA     1 
ATOM   283   C  C      . TYR A 1 50  ? 38.45700  8.95800   39.65100  1.000 134.73000 ? 41  TYR A C      1 
ATOM   284   O  O      . TYR A 1 50  ? 37.46300  9.58800   39.24900  1.000 139.23000 ? 41  TYR A O      1 
ATOM   285   C  CB     . TYR A 1 50  ? 40.70800  9.19200   38.55800  1.000 99.41000  ? 41  TYR A CB     1 
ATOM   286   N  N      . ILE A 1 51  ? 38.38600  7.68000   40.03100  1.000 146.11000 ? 42  ILE A N      1 
ATOM   287   C  CA     . ILE A 1 51  ? 37.10200  6.98400   39.99000  1.000 141.91000 ? 42  ILE A CA     1 
ATOM   288   C  C      . ILE A 1 51  ? 36.12200  7.63400   40.96100  1.000 143.92000 ? 42  ILE A C      1 
ATOM   289   O  O      . ILE A 1 51  ? 34.92400  7.75100   40.67200  1.000 149.72000 ? 42  ILE A O      1 
ATOM   290   C  CB     . ILE A 1 51  ? 37.26900  5.47800   40.27700  1.000 135.59000 ? 42  ILE A CB     1 
ATOM   291   C  CG1    . ILE A 1 51  ? 37.44100  5.22600   41.77500  1.000 115.67000 ? 42  ILE A CG1    1 
ATOM   292   C  CG2    . ILE A 1 51  ? 38.43500  4.90600   39.47600  1.000 155.84000 ? 42  ILE A CG2    1 
ATOM   293   C  CD1    . ILE A 1 51  ? 37.46800  3.76500   42.15600  1.000 100.18000 ? 42  ILE A CD1    1 
ATOM   294   N  N      . ARG A 1 52  ? 36.60600  8.04400   42.13900  1.000 138.16000 ? 43  ARG A N      1 
ATOM   295   C  CA     . ARG A 1 52  ? 35.71800  8.69300   43.10100  1.000 122.81000 ? 43  ARG A CA     1 
ATOM   296   C  C      . ARG A 1 52  ? 35.11300  9.95900   42.51400  1.000 124.28000 ? 43  ARG A C      1 
ATOM   297   O  O      . ARG A 1 52  ? 33.90900  10.20900  42.65700  1.000 122.85000 ? 43  ARG A O      1 
ATOM   298   C  CB     . ARG A 1 52  ? 36.46500  9.01500   44.39600  1.000 109.72000 ? 43  ARG A CB     1 
ATOM   299   C  CG     . ARG A 1 52  ? 35.59900  9.70400   45.44200  1.000 105.04000 ? 43  ARG A CG     1 
ATOM   300   C  CD     . ARG A 1 52  ? 36.29400  10.92900  46.01400  1.000 134.54000 ? 43  ARG A CD     1 
ATOM   301   N  NE     . ARG A 1 52  ? 36.47200  11.98200  45.02200  1.000 144.92000 ? 43  ARG A NE     1 
ATOM   302   N  N      . SER A 1 53  ? 35.93200  10.76200  41.83600  1.000 127.42000 ? 44  SER A N      1 
ATOM   303   C  CA     . SER A 1 53  ? 35.42700  12.01100  41.27800  1.000 117.35000 ? 44  SER A CA     1 
ATOM   304   C  C      . SER A 1 53  ? 34.40700  11.74900  40.18000  1.000 113.19000 ? 44  SER A C      1 
ATOM   305   O  O      . SER A 1 53  ? 33.36000  12.41100  40.12100  1.000 116.82000 ? 44  SER A O      1 
ATOM   306   C  CB     . SER A 1 53  ? 36.58100  12.85600  40.74300  1.000 126.53000 ? 44  SER A CB     1 
ATOM   307   O  OG     . SER A 1 53  ? 37.10700  12.31300  39.54400  1.000 139.74000 ? 44  SER A OG     1 
ATOM   308   N  N      . GLY A 1 54  ? 34.69100  10.78800  39.29900  1.000 119.72000 ? 45  GLY A N      1 
ATOM   309   C  CA     . GLY A 1 54  ? 33.72800  10.47000  38.25500  1.000 115.49000 ? 45  GLY A CA     1 
ATOM   310   C  C      . GLY A 1 54  ? 32.40400  9.98800   38.81800  1.000 102.92000 ? 45  GLY A C      1 
ATOM   311   O  O      . GLY A 1 54  ? 31.32500  10.42100  38.38800  1.000 82.08000  ? 45  GLY A O      1 
ATOM   312   N  N      . ALA A 1 55  ? 32.47000  9.08600   39.80300  1.000 110.88000 ? 46  ALA A N      1 
ATOM   313   C  CA     . ALA A 1 55  ? 31.25600  8.57100   40.42100  1.000 107.26000 ? 46  ALA A CA     1 
ATOM   314   C  C      . ALA A 1 55  ? 30.46900  9.68000   41.10400  1.000 107.85000 ? 46  ALA A C      1 
ATOM   315   O  O      . ALA A 1 55  ? 29.23700  9.71000   41.02900  1.000 106.41000 ? 46  ALA A O      1 
ATOM   316   C  CB     . ALA A 1 55  ? 31.60400  7.46700   41.41800  1.000 93.86000  ? 46  ALA A CB     1 
ATOM   317   N  N      . ASP A 1 56  ? 31.16100  10.60400  41.77400  1.000 112.43000 ? 47  ASP A N      1 
ATOM   318   C  CA     . ASP A 1 56  ? 30.45900  11.69600  42.44100  1.000 115.07000 ? 47  ASP A CA     1 
ATOM   319   C  C      . ASP A 1 56  ? 29.78900  12.62500  41.43500  1.000 108.20000 ? 47  ASP A C      1 
ATOM   320   O  O      . ASP A 1 56  ? 28.67000  13.09700  41.67100  1.000 110.08000 ? 47  ASP A O      1 
ATOM   321   C  CB     . ASP A 1 56  ? 31.42200  12.46700  43.34300  1.000 124.83000 ? 47  ASP A CB     1 
ATOM   322   C  CG     . ASP A 1 56  ? 31.77800  11.69900  44.60600  1.000 115.50000 ? 47  ASP A CG     1 
ATOM   323   O  OD1    . ASP A 1 56  ? 31.38900  10.51500  44.71700  1.000 110.77000 ? 47  ASP A OD1    1 
ATOM   324   O  OD2    . ASP A 1 56  ? 32.45200  12.27600  45.48500  1.000 113.13000 ? 47  ASP A OD2    1 
ATOM   325   N  N      . SER A 1 57  ? 30.44500  12.89500  40.30400  1.000 105.92000 ? 48  SER A N      1 
ATOM   326   C  CA     . SER A 1 57  ? 29.81400  13.73000  39.28300  1.000 109.29000 ? 48  SER A CA     1 
ATOM   327   C  C      . SER A 1 57  ? 28.54800  13.07000  38.74800  1.000 111.75000 ? 48  SER A C      1 
ATOM   328   O  O      . SER A 1 57  ? 27.49300  13.71600  38.61100  1.000 119.45000 ? 48  SER A O      1 
ATOM   329   C  CB     . SER A 1 57  ? 30.79900  14.00600  38.14500  1.000 102.96000 ? 48  SER A CB     1 
ATOM   330   O  OG     . SER A 1 57  ? 30.15600  14.65600  37.05900  1.000 86.43000  ? 48  SER A OG     1 
ATOM   331   N  N      . PHE A 1 58  ? 28.63600  11.77400  38.43200  1.000 109.02000 ? 49  PHE A N      1 
ATOM   332   C  CA     . PHE A 1 58  ? 27.45000  11.06100  37.96800  1.000 106.70000 ? 49  PHE A CA     1 
ATOM   333   C  C      . PHE A 1 58  ? 26.35000  11.09900  39.02000  1.000 98.76000  ? 49  PHE A C      1 
ATOM   334   O  O      . PHE A 1 58  ? 25.17400  11.31900  38.69800  1.000 102.80000 ? 49  PHE A O      1 
ATOM   335   C  CB     . PHE A 1 58  ? 27.80000  9.61700   37.61200  1.000 106.09000 ? 49  PHE A CB     1 
ATOM   336   C  CG     . PHE A 1 58  ? 26.60900  8.70400   37.56200  1.000 95.68000  ? 49  PHE A CG     1 
ATOM   337   C  CD1    . PHE A 1 58  ? 25.69700  8.79300   36.52300  1.000 99.17000  ? 49  PHE A CD1    1 
ATOM   338   C  CD2    . PHE A 1 58  ? 26.39600  7.76400   38.55600  1.000 90.36000  ? 49  PHE A CD2    1 
ATOM   339   C  CE1    . PHE A 1 58  ? 24.59700  7.95600   36.47300  1.000 103.91000 ? 49  PHE A CE1    1 
ATOM   340   C  CE2    . PHE A 1 58  ? 25.29700  6.92500   38.51200  1.000 105.04000 ? 49  PHE A CE2    1 
ATOM   341   C  CZ     . PHE A 1 58  ? 24.39700  7.02100   37.47000  1.000 105.14000 ? 49  PHE A CZ     1 
ATOM   342   N  N      . LEU A 1 59  ? 26.71600  10.89200  40.28800  1.000 89.43000  ? 50  LEU A N      1 
ATOM   343   C  CA     . LEU A 1 59  ? 25.72800  10.90000  41.35700  1.000 84.76000  ? 50  LEU A CA     1 
ATOM   344   C  C      . LEU A 1 59  ? 25.04800  12.25500  41.45900  1.000 102.52000 ? 50  LEU A C      1 
ATOM   345   O  O      . LEU A 1 59  ? 23.83500  12.33200  41.66800  1.000 118.50000 ? 50  LEU A O      1 
ATOM   346   C  CB     . LEU A 1 59  ? 26.38700  10.53900  42.68800  1.000 78.39000  ? 50  LEU A CB     1 
ATOM   347   C  CG     . LEU A 1 59  ? 27.00400  9.14700   42.80200  1.000 95.28000  ? 50  LEU A CG     1 
ATOM   348   C  CD1    . LEU A 1 59  ? 27.74900  8.99900   44.11900  1.000 106.37000 ? 50  LEU A CD1    1 
ATOM   349   C  CD2    . LEU A 1 59  ? 25.93400  8.07800   42.66400  1.000 92.34000  ? 50  LEU A CD2    1 
ATOM   350   N  N      . ALA A 1 60  ? 25.81100  13.33600  41.29600  1.000 100.97000 ? 51  ALA A N      1 
ATOM   351   C  CA     . ALA A 1 60  ? 25.22800  14.66900  41.40300  1.000 99.90000  ? 51  ALA A CA     1 
ATOM   352   C  C      . ALA A 1 60  ? 24.22700  14.91800  40.28200  1.000 96.27000  ? 51  ALA A C      1 
ATOM   353   O  O      . ALA A 1 60  ? 23.10700  15.39700  40.52500  1.000 103.03000 ? 51  ALA A O      1 
ATOM   354   C  CB     . ALA A 1 60  ? 26.33400  15.72500  41.38800  1.000 114.49000 ? 51  ALA A CB     1 
ATOM   355   N  N      . HIS A 1 61  ? 24.60900  14.59200  39.04400  1.000 95.68000  ? 52  HIS A N      1 
ATOM   356   C  CA     . HIS A 1 61  ? 23.67500  14.76100  37.93100  1.000 105.77000 ? 52  HIS A CA     1 
ATOM   357   C  C      . HIS A 1 61  ? 22.40000  13.95600  38.16800  1.000 103.20000 ? 52  HIS A C      1 
ATOM   358   O  O      . HIS A 1 61  ? 21.27400  14.47200  38.03100  1.000 103.55000 ? 52  HIS A O      1 
ATOM   359   C  CB     . HIS A 1 61  ? 24.34000  14.34300  36.61700  1.000 106.38000 ? 52  HIS A CB     1 
ATOM   360   C  CG     . HIS A 1 61  ? 25.34300  15.33000  36.10000  1.000 107.25000 ? 52  HIS A CG     1 
ATOM   361   N  ND1    . HIS A 1 61  ? 26.70200  15.14900  36.23700  1.000 111.06000 ? 52  HIS A ND1    1 
ATOM   362   C  CD2    . HIS A 1 61  ? 25.18500  16.50400  35.44400  1.000 101.24000 ? 52  HIS A CD2    1 
ATOM   363   C  CE1    . HIS A 1 61  ? 27.33900  16.16800  35.68900  1.000 117.27000 ? 52  HIS A CE1    1 
ATOM   364   N  NE2    . HIS A 1 61  ? 26.44200  17.00600  35.20100  1.000 124.93000 ? 52  HIS A NE2    1 
ATOM   365   N  N      . GLU A 1 62  ? 22.56500  12.68100  38.52900  1.000 96.63000  ? 53  GLU A N      1 
ATOM   366   C  CA     . GLU A 1 62  ? 21.41900  11.81100  38.75400  1.000 103.03000 ? 53  GLU A CA     1 
ATOM   367   C  C      . GLU A 1 62  ? 20.51600  12.36300  39.84800  1.000 111.65000 ? 53  GLU A C      1 
ATOM   368   O  O      . GLU A 1 62  ? 19.29100  12.39400  39.69800  1.000 119.40000 ? 53  GLU A O      1 
ATOM   369   C  CB     . GLU A 1 62  ? 21.90200  10.40800  39.11700  1.000 108.24000 ? 53  GLU A CB     1 
ATOM   370   C  CG     . GLU A 1 62  ? 20.78500  9.43500   39.45300  1.000 118.46000 ? 53  GLU A CG     1 
ATOM   371   C  CD     . GLU A 1 62  ? 21.27700  8.25500   40.26700  1.000 102.50000 ? 53  GLU A CD     1 
ATOM   372   O  OE1    . GLU A 1 62  ? 22.39600  8.33700   40.81900  1.000 87.37000  ? 53  GLU A OE1    1 
ATOM   373   O  OE2    . GLU A 1 62  ? 20.55000  7.24400   40.34900  1.000 109.45000 ? 53  GLU A OE2    1 
ATOM   374   N  N      . THR A 1 63  ? 21.10400  12.78100  40.96900  1.000 101.30000 ? 54  THR A N      1 
ATOM   375   C  CA     . THR A 1 63  ? 20.29700  13.25800  42.08400  1.000 91.13000  ? 54  THR A CA     1 
ATOM   376   C  C      . THR A 1 63  ? 19.52100  14.50700  41.70100  1.000 98.07000  ? 54  THR A C      1 
ATOM   377   O  O      . THR A 1 63  ? 18.33600  14.63100  42.02900  1.000 104.31000 ? 54  THR A O      1 
ATOM   378   C  CB     . THR A 1 63  ? 21.18000  13.52600  43.30200  1.000 87.19000  ? 54  THR A CB     1 
ATOM   379   O  OG1    . THR A 1 63  ? 21.76600  12.29600  43.74500  1.000 94.40000  ? 54  THR A OG1    1 
ATOM   380   C  CG2    . THR A 1 63  ? 20.36200  14.12500  44.43800  1.000 80.79000  ? 54  THR A CG2    1 
ATOM   381   N  N      . LYS A 1 64  ? 20.16000  15.44000  40.99100  1.000 100.45000 ? 55  LYS A N      1 
ATOM   382   C  CA     . LYS A 1 64  ? 19.43600  16.63700  40.57200  1.000 102.82000 ? 55  LYS A CA     1 
ATOM   383   C  C      . LYS A 1 64  ? 18.22100  16.27000  39.72600  1.000 105.89000 ? 55  LYS A C      1 
ATOM   384   O  O      . LYS A 1 64  ? 17.09200  16.71200  40.00100  1.000 116.10000 ? 55  LYS A O      1 
ATOM   385   C  CB     . LYS A 1 64  ? 20.37000  17.57700  39.80800  1.000 96.11000  ? 55  LYS A CB     1 
ATOM   386   N  N      . ALA A 1 65  ? 18.42900  15.43800  38.70000  1.000 91.54000  ? 56  ALA A N      1 
ATOM   387   C  CA     . ALA A 1 65  ? 17.31200  15.08500  37.82600  1.000 101.99000 ? 56  ALA A CA     1 
ATOM   388   C  C      . ALA A 1 65  ? 16.21100  14.35500  38.59400  1.000 97.92000  ? 56  ALA A C      1 
ATOM   389   O  O      . ALA A 1 65  ? 15.01700  14.67600  38.45700  1.000 95.63000  ? 56  ALA A O      1 
ATOM   390   C  CB     . ALA A 1 65  ? 17.81100  14.23300  36.66000  1.000 110.43000 ? 56  ALA A CB     1 
ATOM   391   N  N      . ILE A 1 66  ? 16.59800  13.38000  39.42000  1.000 93.16000  ? 57  ILE A N      1 
ATOM   392   C  CA     . ILE A 1 66  ? 15.62200  12.54900  40.11300  1.000 99.80000  ? 57  ILE A CA     1 
ATOM   393   C  C      . ILE A 1 66  ? 14.82700  13.37400  41.11100  1.000 92.22000  ? 57  ILE A C      1 
ATOM   394   O  O      . ILE A 1 66  ? 13.62400  13.16500  41.28300  1.000 79.26000  ? 57  ILE A O      1 
ATOM   395   C  CB     . ILE A 1 66  ? 16.31300  11.35200  40.79100  1.000 92.84000  ? 57  ILE A CB     1 
ATOM   396   C  CG1    . ILE A 1 66  ? 17.14800  11.81900  41.98400  1.000 96.44000  ? 57  ILE A CG1    1 
ATOM   397   C  CG2    . ILE A 1 66  ? 17.16400  10.59400  39.78800  1.000 96.22000  ? 57  ILE A CG2    1 
ATOM   398   C  CD1    . ILE A 1 66  ? 17.77700  10.68300  42.76200  1.000 107.11000 ? 57  ILE A CD1    1 
ATOM   399   N  N      . PHE A 1 67  ? 15.47700  14.31900  41.79000  1.000 91.95000  ? 58  PHE A N      1 
ATOM   400   C  CA     . PHE A 1 67  ? 14.75000  15.12800  42.75700  1.000 96.40000  ? 58  PHE A CA     1 
ATOM   401   C  C      . PHE A 1 67  ? 13.82700  16.12700  42.07400  1.000 85.22000  ? 58  PHE A C      1 
ATOM   402   O  O      . PHE A 1 67  ? 12.74800  16.41600  42.59900  1.000 87.49000  ? 58  PHE A O      1 
ATOM   403   C  CB     . PHE A 1 67  ? 15.72500  15.82500  43.70300  1.000 108.12000 ? 58  PHE A CB     1 
ATOM   404   C  CG     . PHE A 1 67  ? 16.17000  14.95700  44.84700  1.000 121.25000 ? 58  PHE A CG     1 
ATOM   405   C  CD1    . PHE A 1 67  ? 15.48100  13.79200  45.14700  1.000 108.36000 ? 58  PHE A CD1    1 
ATOM   406   C  CD2    . PHE A 1 67  ? 17.26600  15.29800  45.62300  1.000 137.33000 ? 58  PHE A CD2    1 
ATOM   407   C  CE1    . PHE A 1 67  ? 15.87300  12.98400  46.19700  1.000 107.51000 ? 58  PHE A CE1    1 
ATOM   408   C  CE2    . PHE A 1 67  ? 17.66500  14.49000  46.67700  1.000 120.37000 ? 58  PHE A CE2    1 
ATOM   409   C  CZ     . PHE A 1 67  ? 16.96400  13.33100  46.96300  1.000 107.51000 ? 58  PHE A CZ     1 
ATOM   410   N  N      . LYS A 1 68  ? 14.20000  16.64500  40.90000  1.000 74.95000  ? 59  LYS A N      1 
ATOM   411   C  CA     . LYS A 1 68  ? 13.23800  17.45400  40.15200  1.000 87.73000  ? 59  LYS A CA     1 
ATOM   412   C  C      . LYS A 1 68  ? 11.99500  16.63500  39.80000  1.000 91.73000  ? 59  LYS A C      1 
ATOM   413   O  O      . LYS A 1 68  ? 10.84800  17.07300  40.01300  1.000 76.49000  ? 59  LYS A O      1 
ATOM   414   C  CB     . LYS A 1 68  ? 13.89400  18.01800  38.88900  1.000 85.37000  ? 59  LYS A CB     1 
ATOM   415   N  N      . VAL A 1 69  ? 12.20800  15.42900  39.26600  1.000 99.33000  ? 60  VAL A N      1 
ATOM   416   C  CA     . VAL A 1 69  ? 11.07700  14.58100  38.89600  1.000 88.15000  ? 60  VAL A CA     1 
ATOM   417   C  C      . VAL A 1 69  ? 10.25300  14.22100  40.12700  1.000 88.32000  ? 60  VAL A C      1 
ATOM   418   O  O      . VAL A 1 69  ? 9.01700   14.18700  40.08000  1.000 77.36000  ? 60  VAL A O      1 
ATOM   419   C  CB     . VAL A 1 69  ? 11.56900  13.32600  38.15300  1.000 73.61000  ? 60  VAL A CB     1 
ATOM   420   C  CG1    . VAL A 1 69  ? 10.43000  12.33300  37.98600  1.000 67.29000  ? 60  VAL A CG1    1 
ATOM   421   C  CG2    . VAL A 1 69  ? 12.14500  13.71100  36.80600  1.000 82.46000  ? 60  VAL A CG2    1 
ATOM   422   N  N      . ALA A 1 70  ? 10.92200  13.95200  41.24900  1.000 83.43000  ? 61  ALA A N      1 
ATOM   423   C  CA     . ALA A 1 70  ? 10.21800  13.60800  42.47700  1.000 77.23000  ? 61  ALA A CA     1 
ATOM   424   C  C      . ALA A 1 70  ? 9.42100   14.78900  43.01000  1.000 82.21000  ? 61  ALA A C      1 
ATOM   425   O  O      . ALA A 1 70  ? 8.34200   14.60600  43.57800  1.000 90.51000  ? 61  ALA A O      1 
ATOM   426   C  CB     . ALA A 1 70  ? 11.21000  13.11700  43.52800  1.000 54.54000  ? 61  ALA A CB     1 
ATOM   427   N  N      . ILE A 1 71  ? 9.93700   16.00700  42.85100  1.000 69.83000  ? 62  ILE A N      1 
ATOM   428   C  CA     . ILE A 1 71  ? 9.17700   17.18600  43.25100  1.000 78.90000  ? 62  ILE A CA     1 
ATOM   429   C  C      . ILE A 1 71  ? 7.88400   17.26800  42.45300  1.000 82.05000  ? 62  ILE A C      1 
ATOM   430   O  O      . ILE A 1 71  ? 6.79500   17.47200  43.01000  1.000 78.78000  ? 62  ILE A O      1 
ATOM   431   C  CB     . ILE A 1 71  ? 10.02500  18.45700  43.07900  1.000 82.50000  ? 62  ILE A CB     1 
ATOM   432   C  CG1    . ILE A 1 71  ? 11.17200  18.47700  44.09200  1.000 75.71000  ? 62  ILE A CG1    1 
ATOM   433   C  CG2    . ILE A 1 71  ? 9.15200   19.69900  43.22200  1.000 85.87000  ? 62  ILE A CG2    1 
ATOM   434   C  CD1    . ILE A 1 71  ? 12.17700  19.58600  43.85500  1.000 76.97000  ? 62  ILE A CD1    1 
ATOM   435   N  N      . VAL A 1 72  ? 7.98500   17.10400  41.13200  1.000 77.69000  ? 63  VAL A N      1 
ATOM   436   C  CA     . VAL A 1 72  ? 6.77700   17.15600  40.30600  1.000 81.53000  ? 63  VAL A CA     1 
ATOM   437   C  C      . VAL A 1 72  ? 5.80500   16.05200  40.71700  1.000 75.41000  ? 63  VAL A C      1 
ATOM   438   O  O      . VAL A 1 72  ? 4.58900   16.27600  40.84400  1.000 58.15000  ? 63  VAL A O      1 
ATOM   439   C  CB     . VAL A 1 72  ? 7.14500   17.06500  38.81300  1.000 78.62000  ? 63  VAL A CB     1 
ATOM   440   C  CG1    . VAL A 1 72  ? 5.92800   17.37400  37.94200  1.000 65.82000  ? 63  VAL A CG1    1 
ATOM   441   C  CG2    . VAL A 1 72  ? 8.28800   18.00700  38.49100  1.000 76.03000  ? 63  VAL A CG2    1 
ATOM   442   N  N      . ILE A 1 73  ? 6.33100   14.84700  40.94700  1.000 75.23000  ? 64  ILE A N      1 
ATOM   443   C  CA     . ILE A 1 73  ? 5.48400   13.71500  41.31000  1.000 79.40000  ? 64  ILE A CA     1 
ATOM   444   C  C      . ILE A 1 73  ? 4.77900   13.97400  42.63200  1.000 81.64000  ? 64  ILE A C      1 
ATOM   445   O  O      . ILE A 1 73  ? 3.57500   13.72800  42.76900  1.000 76.11000  ? 64  ILE A O      1 
ATOM   446   C  CB     . ILE A 1 73  ? 6.32000   12.42300  41.36000  1.000 80.68000  ? 64  ILE A CB     1 
ATOM   447   C  CG1    . ILE A 1 73  ? 6.86800   12.09300  39.97000  1.000 78.12000  ? 64  ILE A CG1    1 
ATOM   448   C  CG2    . ILE A 1 73  ? 5.49600   11.27500  41.93000  1.000 66.62000  ? 64  ILE A CG2    1 
ATOM   449   C  CD1    . ILE A 1 73  ? 5.79500   11.80900  38.94100  1.000 81.27000  ? 64  ILE A CD1    1 
ATOM   450   N  N      . ALA A 1 74  ? 5.51500   14.47200  43.62500  1.000 83.36000  ? 65  ALA A N      1 
ATOM   451   C  CA     . ALA A 1 74  ? 4.92500   14.72800  44.93100  1.000 72.85000  ? 65  ALA A CA     1 
ATOM   452   C  C      . ALA A 1 74  ? 3.87200   15.82000  44.84700  1.000 82.12000  ? 65  ALA A C      1 
ATOM   453   O  O      . ALA A 1 74  ? 2.83700   15.74000  45.51700  1.000 89.14000  ? 65  ALA A O      1 
ATOM   454   C  CB     . ALA A 1 74  ? 6.01200   15.10500  45.93400  1.000 58.06000  ? 65  ALA A CB     1 
ATOM   455   N  N      . ILE A 1 75  ? 4.11500   16.84900  44.03100  1.000 81.63000  ? 66  ILE A N      1 
ATOM   456   C  CA     . ILE A 1 75  ? 3.11700   17.90400  43.86800  1.000 84.59000  ? 66  ILE A CA     1 
ATOM   457   C  C      . ILE A 1 75  ? 1.82400   17.32400  43.31200  1.000 83.46000  ? 66  ILE A C      1 
ATOM   458   O  O      . ILE A 1 75  ? 0.73100   17.56600  43.84300  1.000 67.90000  ? 66  ILE A O      1 
ATOM   459   C  CB     . ILE A 1 75  ? 3.66000   19.02800  42.96700  1.000 84.56000  ? 66  ILE A CB     1 
ATOM   460   C  CG1    . ILE A 1 75  ? 4.81700   19.75900  43.65500  1.000 84.24000  ? 66  ILE A CG1    1 
ATOM   461   C  CG2    . ILE A 1 75  ? 2.53800   19.98600  42.57800  1.000 80.41000  ? 66  ILE A CG2    1 
ATOM   462   C  CD1    . ILE A 1 75  ? 4.46600   20.33200  45.00700  1.000 83.60000  ? 66  ILE A CD1    1 
ATOM   463   N  N      . LEU A 1 76  ? 1.92800   16.54000  42.23600  1.000 86.16000  ? 67  LEU A N      1 
ATOM   464   C  CA     . LEU A 1 76  ? 0.72100   15.95100  41.66100  1.000 72.92000  ? 67  LEU A CA     1 
ATOM   465   C  C      . LEU A 1 76  ? 0.03800   15.01400  42.65000  1.000 65.64000  ? 67  LEU A C      1 
ATOM   466   O  O      . LEU A 1 76  ? -1.19600  14.99700  42.75300  1.000 75.02000  ? 67  LEU A O      1 
ATOM   467   C  CB     . LEU A 1 76  ? 1.05600   15.22000  40.36300  1.000 68.40000  ? 67  LEU A CB     1 
ATOM   468   C  CG     . LEU A 1 76  ? 1.50900   16.11300  39.20900  1.000 74.43000  ? 67  LEU A CG     1 
ATOM   469   C  CD1    . LEU A 1 76  ? 1.80400   15.27500  37.98400  1.000 84.04000  ? 67  LEU A CD1    1 
ATOM   470   C  CD2    . LEU A 1 76  ? 0.44700   17.15700  38.90100  1.000 79.99000  ? 67  LEU A CD2    1 
ATOM   471   N  N      . LEU A 1 77  ? 0.82600   14.23800  43.39700  1.000 59.67000  ? 68  LEU A N      1 
ATOM   472   C  CA     . LEU A 1 77  ? 0.25900   13.28700  44.34500  1.000 68.02000  ? 68  LEU A CA     1 
ATOM   473   C  C      . LEU A 1 77  ? -0.52000  14.00200  45.44000  1.000 79.97000  ? 68  LEU A C      1 
ATOM   474   O  O      . LEU A 1 77  ? -1.67300  13.65600  45.72600  1.000 86.76000  ? 68  LEU A O      1 
ATOM   475   C  CB     . LEU A 1 77  ? 1.37600   12.43000  44.94300  1.000 77.80000  ? 68  LEU A CB     1 
ATOM   476   C  CG     . LEU A 1 77  ? 0.95500   11.26800  45.84100  1.000 89.87000  ? 68  LEU A CG     1 
ATOM   477   C  CD1    . LEU A 1 77  ? 0.16300   10.24900  45.04100  1.000 101.99000 ? 68  LEU A CD1    1 
ATOM   478   C  CD2    . LEU A 1 77  ? 2.17500   10.61900  46.47400  1.000 86.89000  ? 68  LEU A CD2    1 
ATOM   479   N  N      . MET A 1 78  ? 0.08900   15.01700  46.05500  1.000 81.74000  ? 69  MET A N      1 
ATOM   480   C  CA     . MET A 1 78  ? -0.60300  15.75000  47.10700  1.000 81.82000  ? 69  MET A CA     1 
ATOM   481   C  C      . MET A 1 78  ? -1.81700  16.48400  46.55600  1.000 83.73000  ? 69  MET A C      1 
ATOM   482   O  O      . MET A 1 78  ? -2.83000  16.60400  47.25300  1.000 90.06000  ? 69  MET A O      1 
ATOM   483   C  CB     . MET A 1 78  ? 0.35700   16.71000  47.81000  1.000 83.40000  ? 69  MET A CB     1 
ATOM   484   C  CG     . MET A 1 78  ? 1.15100   17.60500  46.88700  1.000 92.64000  ? 69  MET A CG     1 
ATOM   485   S  SD     . MET A 1 78  ? 2.46600   18.45300  47.78200  1.000 134.57000 ? 69  MET A SD     1 
ATOM   486   C  CE     . MET A 1 78  ? 3.24100   17.07600  48.63000  1.000 78.57000  ? 69  MET A CE     1 
ATOM   487   N  N      . ILE A 1 79  ? -1.75100  16.95900  45.30900  1.000 90.99000  ? 70  ILE A N      1 
ATOM   488   C  CA     . ILE A 1 79  ? -2.90700  17.63100  44.72300  1.000 85.68000  ? 70  ILE A CA     1 
ATOM   489   C  C      . ILE A 1 79  ? -4.06900  16.65400  44.58500  1.000 84.91000  ? 70  ILE A C      1 
ATOM   490   O  O      . ILE A 1 79  ? -5.20400  16.94900  44.98000  1.000 84.88000  ? 70  ILE A O      1 
ATOM   491   C  CB     . ILE A 1 79  ? -2.53700  18.26000  43.36600  1.000 83.56000  ? 70  ILE A CB     1 
ATOM   492   C  CG1    . ILE A 1 79  ? -1.61200  19.46200  43.55900  1.000 84.76000  ? 70  ILE A CG1    1 
ATOM   493   C  CG2    . ILE A 1 79  ? -3.79100  18.67700  42.60900  1.000 55.53000  ? 70  ILE A CG2    1 
ATOM   494   C  CD1    . ILE A 1 79  ? -1.22300  20.14000  42.25900  1.000 79.31000  ? 70  ILE A CD1    1 
ATOM   495   N  N      . PHE A 1 80  ? -3.80100  15.46600  44.04300  1.000 91.31000  ? 71  PHE A N      1 
ATOM   496   C  CA     . PHE A 1 80  ? -4.86200  14.50800  43.75400  1.000 96.44000  ? 71  PHE A CA     1 
ATOM   497   C  C      . PHE A 1 80  ? -5.14600  13.53800  44.89500  1.000 102.01000 ? 71  PHE A C      1 
ATOM   498   O  O      . PHE A 1 80  ? -6.13400  12.80100  44.82200  1.000 102.47000 ? 71  PHE A O      1 
ATOM   499   C  CB     . PHE A 1 80  ? -4.52400  13.72300  42.48500  1.000 91.58000  ? 71  PHE A CB     1 
ATOM   500   C  CG     . PHE A 1 80  ? -4.63000  14.53800  41.23000  1.000 69.99000  ? 71  PHE A CG     1 
ATOM   501   C  CD1    . PHE A 1 80  ? -5.86800  14.81100  40.67500  1.000 59.92000  ? 71  PHE A CD1    1 
ATOM   502   C  CD2    . PHE A 1 80  ? -3.49900  15.06600  40.62700  1.000 57.86000  ? 71  PHE A CD2    1 
ATOM   503   C  CE1    . PHE A 1 80  ? -5.97900  15.56700  39.52300  1.000 65.16000  ? 71  PHE A CE1    1 
ATOM   504   C  CE2    . PHE A 1 80  ? -3.60300  15.82800  39.47700  1.000 60.19000  ? 71  PHE A CE2    1 
ATOM   505   C  CZ     . PHE A 1 80  ? -4.84500  16.07900  38.92500  1.000 73.80000  ? 71  PHE A CZ     1 
ATOM   506   N  N      . THR A 1 81  ? -4.32400  13.51500  45.94000  1.000 97.78000  ? 72  THR A N      1 
ATOM   507   C  CA     . THR A 1 81  ? -4.55100  12.61800  47.06900  1.000 97.39000  ? 72  THR A CA     1 
ATOM   508   C  C      . THR A 1 81  ? -4.25900  13.37400  48.36200  1.000 105.66000 ? 72  THR A C      1 
ATOM   509   O  O      . THR A 1 81  ? -4.02000  14.58500  48.36000  1.000 110.06000 ? 72  THR A O      1 
ATOM   510   C  CB     . THR A 1 81  ? -3.69400  11.35000  46.95400  1.000 99.06000  ? 72  THR A CB     1 
ATOM   511   O  OG1    . THR A 1 81  ? -2.33100  11.66100  47.27200  1.000 114.61000 ? 72  THR A OG1    1 
ATOM   512   C  CG2    . THR A 1 81  ? -3.78000  10.76400  45.55600  1.000 97.37000  ? 72  THR A CG2    1 
ATOM   513   N  N      . THR A 1 82  ? -4.27200  12.64500  49.47500  1.000 109.49000 ? 73  THR A N      1 
ATOM   514   C  CA     . THR A 1 82  ? -3.97700  13.23300  50.77500  1.000 132.14000 ? 73  THR A CA     1 
ATOM   515   C  C      . THR A 1 82  ? -2.50100  13.60700  50.88800  1.000 120.08000 ? 73  THR A C      1 
ATOM   516   O  O      . THR A 1 82  ? -1.62200  12.94000  50.33700  1.000 116.09000 ? 73  THR A O      1 
ATOM   517   C  CB     . THR A 1 82  ? -4.37100  12.27200  51.90200  1.000 135.57000 ? 73  THR A CB     1 
ATOM   518   O  OG1    . THR A 1 82  ? -4.02100  12.84100  53.17000  1.000 153.47000 ? 73  THR A OG1    1 
ATOM   519   C  CG2    . THR A 1 82  ? -3.67900  10.92900  51.74200  1.000 117.19000 ? 73  THR A CG2    1 
ATOM   520   N  N      . TRP A 1 83  ? -2.24000  14.70500  51.60700  1.000 115.39000 ? 74  TRP A N      1 
ATOM   521   C  CA     . TRP A 1 83  ? -0.87500  15.20800  51.74800  1.000 113.37000 ? 74  TRP A CA     1 
ATOM   522   C  C      . TRP A 1 83  ? 0.03100   14.19000  52.42700  1.000 127.04000 ? 74  TRP A C      1 
ATOM   523   O  O      . TRP A 1 83  ? 1.23900   14.15000  52.15200  1.000 126.01000 ? 74  TRP A O      1 
ATOM   524   C  CB     . TRP A 1 83  ? -0.87800  16.51300  52.54700  1.000 98.78000  ? 74  TRP A CB     1 
ATOM   525   C  CG     . TRP A 1 83  ? -1.40200  16.35100  53.95200  1.000 109.40000 ? 74  TRP A CG     1 
ATOM   526   C  CD1    . TRP A 1 83  ? -2.70900  16.37100  54.34500  1.000 126.44000 ? 74  TRP A CD1    1 
ATOM   527   C  CD2    . TRP A 1 83  ? -0.63100  16.12500  55.14100  1.000 119.08000 ? 74  TRP A CD2    1 
ATOM   528   N  NE1    . TRP A 1 83  ? -2.80100  16.18000  55.70200  1.000 128.96000 ? 74  TRP A NE1    1 
ATOM   529   C  CE2    . TRP A 1 83  ? -1.53900  16.02500  56.21500  1.000 113.40000 ? 74  TRP A CE2    1 
ATOM   530   C  CE3    . TRP A 1 83  ? 0.73700   16.00000  55.40200  1.000 122.92000 ? 74  TRP A CE3    1 
ATOM   531   C  CZ2    . TRP A 1 83  ? -1.12300  15.80700  57.52700  1.000 93.02000  ? 74  TRP A CZ2    1 
ATOM   532   C  CZ3    . TRP A 1 83  ? 1.14800   15.78300  56.70600  1.000 106.25000 ? 74  TRP A CZ3    1 
ATOM   533   C  CH2    . TRP A 1 83  ? 0.22100   15.68900  57.75200  1.000 80.15000  ? 74  TRP A CH2    1 
ATOM   534   N  N      . GLN A 1 84  ? -0.52500  13.38400  53.33700  1.000 124.72000 ? 75  GLN A N      1 
ATOM   535   C  CA     . GLN A 1 84  ? 0.27400   12.38200  54.03400  1.000 109.98000 ? 75  GLN A CA     1 
ATOM   536   C  C      . GLN A 1 84  ? 0.98000   11.46800  53.04300  1.000 120.21000 ? 75  GLN A C      1 
ATOM   537   O  O      . GLN A 1 84  ? 2.12600   11.05500  53.26500  1.000 128.91000 ? 75  GLN A O      1 
ATOM   538   C  CB     . GLN A 1 84  ? -0.61700  11.56700  54.97400  1.000 93.23000  ? 75  GLN A CB     1 
ATOM   539   C  CG     . GLN A 1 84  ? -1.43500  12.40700  55.95400  1.000 102.55000 ? 75  GLN A CG     1 
ATOM   540   C  CD     . GLN A 1 84  ? -2.80900  11.81500  56.23300  1.000 102.72000 ? 75  GLN A CD     1 
ATOM   541   O  OE1    . GLN A 1 84  ? -3.30100  10.97600  55.47700  1.000 106.09000 ? 75  GLN A OE1    1 
ATOM   542   N  NE2    . GLN A 1 84  ? -3.43500  12.25000  57.32200  1.000 100.02000 ? 75  GLN A NE2    1 
ATOM   543   N  N      . THR A 1 85  ? 0.31000   11.15400  51.93200  1.000 127.48000 ? 76  THR A N      1 
ATOM   544   C  CA     . THR A 1 85  ? 0.91300   10.31000  50.90800  1.000 124.95000 ? 76  THR A CA     1 
ATOM   545   C  C      . THR A 1 85  ? 2.10200   10.99700  50.24700  1.000 118.68000 ? 76  THR A C      1 
ATOM   546   O  O      . THR A 1 85  ? 3.13100   10.35900  50.00300  1.000 123.42000 ? 76  THR A O      1 
ATOM   547   C  CB     . THR A 1 85  ? -0.13800  9.92100   49.86900  1.000 130.79000 ? 76  THR A CB     1 
ATOM   548   O  OG1    . THR A 1 85  ? -0.58800  11.09400  49.17700  1.000 133.49000 ? 76  THR A OG1    1 
ATOM   549   C  CG2    . THR A 1 85  ? -1.32200  9.23000   50.53900  1.000 121.22000 ? 76  THR A CG2    1 
ATOM   550   N  N      . GLY A 1 86  ? 1.98600   12.29300  49.95000  1.000 102.75000 ? 77  GLY A N      1 
ATOM   551   C  CA     . GLY A 1 86  ? 3.12300   13.01100  49.39200  1.000 92.42000  ? 77  GLY A CA     1 
ATOM   552   C  C      . GLY A 1 86  ? 4.29400   13.07100  50.35400  1.000 97.89000  ? 77  GLY A C      1 
ATOM   553   O  O      . GLY A 1 86  ? 5.45500   12.91000  49.95600  1.000 92.41000  ? 77  GLY A O      1 
ATOM   554   N  N      . VAL A 1 87  ? 4.00400   13.30500  51.63500  1.000 104.97000 ? 78  VAL A N      1 
ATOM   555   C  CA     . VAL A 1 87  ? 5.06300   13.35000  52.63900  1.000 104.96000 ? 78  VAL A CA     1 
ATOM   556   C  C      . VAL A 1 87  ? 5.76500   12.00100  52.73200  1.000 109.07000 ? 78  VAL A C      1 
ATOM   557   O  O      . VAL A 1 87  ? 7.00000   11.92900  52.77400  1.000 128.23000 ? 78  VAL A O      1 
ATOM   558   C  CB     . VAL A 1 87  ? 4.48700   13.79000  53.99900  1.000 102.81000 ? 78  VAL A CB     1 
ATOM   559   C  CG1    . VAL A 1 87  ? 5.55800   13.73400  55.07900  1.000 121.11000 ? 78  VAL A CG1    1 
ATOM   560   C  CG2    . VAL A 1 87  ? 3.89600   15.18700  53.89800  1.000 96.05000  ? 78  VAL A CG2    1 
ATOM   561   N  N      . ALA A 1 88  ? 4.99600   10.90900  52.74600  1.000 101.60000 ? 79  ALA A N      1 
ATOM   562   C  CA     . ALA A 1 88  ? 5.60700   9.58400   52.81000  1.000 103.47000 ? 79  ALA A CA     1 
ATOM   563   C  C      . ALA A 1 88  ? 6.38800   9.26700   51.53900  1.000 111.41000 ? 79  ALA A C      1 
ATOM   564   O  O      . ALA A 1 88  ? 7.43000   8.60300   51.59500  1.000 119.35000 ? 79  ALA A O      1 
ATOM   565   C  CB     . ALA A 1 88  ? 4.54000   8.52200   53.06400  1.000 102.62000 ? 79  ALA A CB     1 
ATOM   566   N  N      . PHE A 1 89  ? 5.89700   9.72200   50.38400  1.000 104.92000 ? 80  PHE A N      1 
ATOM   567   C  CA     . PHE A 1 89  ? 6.62000   9.52700   49.13000  1.000 103.53000 ? 80  PHE A CA     1 
ATOM   568   C  C      . PHE A 1 89  ? 7.99000   10.18800  49.18700  1.000 108.24000 ? 80  PHE A C      1 
ATOM   569   O  O      . PHE A 1 89  ? 9.01200   9.57400   48.84700  1.000 109.00000 ? 80  PHE A O      1 
ATOM   570   C  CB     . PHE A 1 89  ? 5.78400   10.08400  47.97300  1.000 101.79000 ? 80  PHE A CB     1 
ATOM   571   C  CG     . PHE A 1 89  ? 6.57100   10.37900  46.72300  1.000 100.78000 ? 80  PHE A CG     1 
ATOM   572   C  CD1    . PHE A 1 89  ? 6.77400   9.39800   45.76700  1.000 97.17000  ? 80  PHE A CD1    1 
ATOM   573   C  CD2    . PHE A 1 89  ? 7.08200   11.64600  46.49200  1.000 111.45000 ? 80  PHE A CD2    1 
ATOM   574   C  CE1    . PHE A 1 89  ? 7.48700   9.67100   44.61500  1.000 99.75000  ? 80  PHE A CE1    1 
ATOM   575   C  CE2    . PHE A 1 89  ? 7.79500   11.92400  45.34500  1.000 110.84000 ? 80  PHE A CE2    1 
ATOM   576   C  CZ     . PHE A 1 89  ? 7.99800   10.93700  44.40400  1.000 102.65000 ? 80  PHE A CZ     1 
ATOM   577   N  N      . LEU A 1 90  ? 8.03000   11.44500  49.63200  1.000 108.02000 ? 81  LEU A N      1 
ATOM   578   C  CA     . LEU A 1 90  ? 9.31400   12.12800  49.75600  1.000 103.09000 ? 81  LEU A CA     1 
ATOM   579   C  C      . LEU A 1 90  ? 10.20400  11.43900  50.78600  1.000 102.86000 ? 81  LEU A C      1 
ATOM   580   O  O      . LEU A 1 90  ? 11.41700  11.30200  50.57900  1.000 103.36000 ? 81  LEU A O      1 
ATOM   581   C  CB     . LEU A 1 90  ? 9.09600   13.60100  50.10300  1.000 105.63000 ? 81  LEU A CB     1 
ATOM   582   C  CG     . LEU A 1 90  ? 8.49900   14.44700  48.97300  1.000 101.32000 ? 81  LEU A CG     1 
ATOM   583   C  CD1    . LEU A 1 90  ? 8.23900   15.87200  49.43500  1.000 104.01000 ? 81  LEU A CD1    1 
ATOM   584   C  CD2    . LEU A 1 90  ? 9.41000   14.43500  47.75400  1.000 80.22000  ? 81  LEU A CD2    1 
ATOM   585   N  N      . LEU A 1 91  ? 9.61700   10.99200  51.90100  1.000 97.65000  ? 82  LEU A N      1 
ATOM   586   C  CA     . LEU A 1 91  ? 10.38700  10.27600  52.91500  1.000 93.49000  ? 82  LEU A CA     1 
ATOM   587   C  C      . LEU A 1 91  ? 11.06100  9.04300   52.32400  1.000 110.37000 ? 82  LEU A C      1 
ATOM   588   O  O      . LEU A 1 91  ? 12.26200  8.82000   52.52100  1.000 114.21000 ? 82  LEU A O      1 
ATOM   589   C  CB     . LEU A 1 91  ? 9.47700   9.88900   54.08600  1.000 87.66000  ? 82  LEU A CB     1 
ATOM   590   C  CG     . LEU A 1 91  ? 10.04000  8.92800   55.14200  1.000 94.21000  ? 82  LEU A CG     1 
ATOM   591   C  CD1    . LEU A 1 91  ? 11.30100  9.49000   55.78700  1.000 107.22000 ? 82  LEU A CD1    1 
ATOM   592   C  CD2    . LEU A 1 91  ? 8.99800   8.59800   56.20100  1.000 86.29000  ? 82  LEU A CD2    1 
ATOM   593   N  N      . GLY A 1 92  ? 10.29700  8.22400   51.60100  1.000 103.12000 ? 83  GLY A N      1 
ATOM   594   C  CA     . GLY A 1 92  ? 10.86700  7.01400   51.03000  1.000 87.89000  ? 83  GLY A CA     1 
ATOM   595   C  C      . GLY A 1 92  ? 11.92500  7.31000   49.98400  1.000 89.76000  ? 83  GLY A C      1 
ATOM   596   O  O      . GLY A 1 92  ? 12.96500  6.64100   49.92800  1.000 102.99000 ? 83  GLY A O      1 
ATOM   597   N  N      . ALA A 1 93  ? 11.67300  8.31200   49.13600  1.000 82.01000  ? 84  ALA A N      1 
ATOM   598   C  CA     . ALA A 1 93  ? 12.66100  8.67500   48.12800  1.000 74.82000  ? 84  ALA A CA     1 
ATOM   599   C  C      . ALA A 1 93  ? 13.96600  9.10500   48.78100  1.000 93.16000  ? 84  ALA A C      1 
ATOM   600   O  O      . ALA A 1 93  ? 15.05300  8.71200   48.34000  1.000 94.10000  ? 84  ALA A O      1 
ATOM   601   C  CB     . ALA A 1 93  ? 12.11400  9.78500   47.23200  1.000 77.96000  ? 84  ALA A CB     1 
ATOM   602   N  N      . VAL A 1 94  ? 13.87600  9.90800   49.84200  1.000 103.95000 ? 85  VAL A N      1 
ATOM   603   C  CA     . VAL A 1 94  ? 15.07900  10.33900  50.54600  1.000 89.73000  ? 85  VAL A CA     1 
ATOM   604   C  C      . VAL A 1 94  ? 15.78100  9.15000   51.18800  1.000 84.94000  ? 85  VAL A C      1 
ATOM   605   O  O      . VAL A 1 94  ? 17.01300  9.05600   51.16100  1.000 95.76000  ? 85  VAL A O      1 
ATOM   606   C  CB     . VAL A 1 94  ? 14.73200  11.42600  51.57900  1.000 82.18000  ? 85  VAL A CB     1 
ATOM   607   C  CG1    . VAL A 1 94  ? 15.90900  11.67600  52.50200  1.000 92.27000  ? 85  VAL A CG1    1 
ATOM   608   C  CG2    . VAL A 1 94  ? 14.33400  12.71200  50.86900  1.000 87.76000  ? 85  VAL A CG2    1 
ATOM   609   N  N      . MET A 1 95  ? 15.01700  8.21700   51.76400  1.000 87.97000  ? 86  MET A N      1 
ATOM   610   C  CA     . MET A 1 95  ? 15.63000  7.04100   52.37900  1.000 93.67000  ? 86  MET A CA     1 
ATOM   611   C  C      . MET A 1 95  ? 16.46000  6.27200   51.35900  1.000 99.47000  ? 86  MET A C      1 
ATOM   612   O  O      . MET A 1 95  ? 17.63300  5.94500   51.59800  1.000 106.58000 ? 86  MET A O      1 
ATOM   613   C  CB     . MET A 1 95  ? 14.54900  6.12900   52.97000  1.000 100.47000 ? 86  MET A CB     1 
ATOM   614   C  CG     . MET A 1 95  ? 13.87100  6.64500   54.23100  1.000 96.72000  ? 86  MET A CG     1 
ATOM   615   S  SD     . MET A 1 95  ? 15.02000  6.75600   55.60800  1.000 92.03000  ? 86  MET A SD     1 
ATOM   616   C  CE     . MET A 1 95  ? 15.34400  8.51900   55.61400  1.000 80.85000  ? 86  MET A CE     1 
ATOM   617   N  N      . SER A 1 96  ? 15.86100  5.97800   50.20400  1.000 104.97000 ? 87  SER A N      1 
ATOM   618   C  CA     . SER A 1 96  ? 16.57200  5.20500   49.19100  1.000 111.78000 ? 87  SER A CA     1 
ATOM   619   C  C      . SER A 1 96  ? 17.76500  5.97700   48.64100  1.000 112.23000 ? 87  SER A C      1 
ATOM   620   O  O      . SER A 1 96  ? 18.83800  5.40000   48.42500  1.000 119.08000 ? 87  SER A O      1 
ATOM   621   C  CB     . SER A 1 96  ? 15.62200  4.80400   48.06300  1.000 121.40000 ? 87  SER A CB     1 
ATOM   622   O  OG     . SER A 1 96  ? 14.94800  5.93000   47.52800  1.000 139.34000 ? 87  SER A OG     1 
ATOM   623   N  N      . ALA A 1 97  ? 17.59800  7.28100   48.39700  1.000 98.28000  ? 88  ALA A N      1 
ATOM   624   C  CA     . ALA A 1 97  ? 18.70600  8.07300   47.87600  1.000 85.36000  ? 88  ALA A CA     1 
ATOM   625   C  C      . ALA A 1 97  ? 19.86800  8.10400   48.85700  1.000 87.88000  ? 88  ALA A C      1 
ATOM   626   O  O      . ALA A 1 97  ? 21.03400  8.01900   48.45300  1.000 92.74000  ? 88  ALA A O      1 
ATOM   627   C  CB     . ALA A 1 97  ? 18.23100  9.49000   47.55900  1.000 83.25000  ? 88  ALA A CB     1 
ATOM   628   N  N      . SER A 1 98  ? 19.57100  8.23900   50.15100  1.000 94.10000  ? 89  SER A N      1 
ATOM   629   C  CA     . SER A 1 98  ? 20.62000  8.23300   51.16300  1.000 94.88000  ? 89  SER A CA     1 
ATOM   630   C  C      . SER A 1 98  ? 21.34200  6.89500   51.18200  1.000 88.39000  ? 89  SER A C      1 
ATOM   631   O  O      . SER A 1 98  ? 22.57900  6.84100   51.23200  1.000 93.24000  ? 89  SER A O      1 
ATOM   632   C  CB     . SER A 1 98  ? 20.02600  8.54300   52.53700  1.000 84.88000  ? 89  SER A CB     1 
ATOM   633   O  OG     . SER A 1 98  ? 19.38600  9.80800   52.54400  1.000 103.44000 ? 89  SER A OG     1 
ATOM   634   N  N      . ALA A 1 99  ? 20.58200  5.79800   51.15300  1.000 82.11000  ? 90  ALA A N      1 
ATOM   635   C  CA     . ALA A 1 99  ? 21.21600  4.48600   51.13300  1.000 88.21000  ? 90  ALA A CA     1 
ATOM   636   C  C      . ALA A 1 99  ? 22.14600  4.36400   49.93300  1.000 91.34000  ? 90  ALA A C      1 
ATOM   637   O  O      . ALA A 1 99  ? 23.29500  3.92200   50.06100  1.000 103.32000 ? 90  ALA A O      1 
ATOM   638   C  CB     . ALA A 1 99  ? 20.15500  3.38500   51.11800  1.000 88.63000  ? 90  ALA A CB     1 
ATOM   639   N  N      . GLY A 1 100 ? 21.66700  4.77800   48.75900  1.000 88.89000  ? 91  GLY A N      1 
ATOM   640   C  CA     . GLY A 1 100 ? 22.47600  4.66800   47.55600  1.000 93.43000  ? 91  GLY A CA     1 
ATOM   641   C  C      . GLY A 1 100 ? 23.74100  5.50400   47.61500  1.000 99.66000  ? 91  GLY A C      1 
ATOM   642   O  O      . GLY A 1 100 ? 24.82900  5.03000   47.28200  1.000 99.49000  ? 91  GLY A O      1 
ATOM   643   N  N      . ILE A 1 101 ? 23.61300  6.76800   48.02900  1.000 106.16000 ? 92  ILE A N      1 
ATOM   644   C  CA     . ILE A 1 101 ? 24.77300  7.65500   48.07800  1.000 98.31000  ? 92  ILE A CA     1 
ATOM   645   C  C      . ILE A 1 101 ? 25.80000  7.13700   49.07600  1.000 93.16000  ? 92  ILE A C      1 
ATOM   646   O  O      . ILE A 1 101 ? 27.01000  7.13200   48.80400  1.000 89.25000  ? 92  ILE A O      1 
ATOM   647   C  CB     . ILE A 1 101 ? 24.33100  9.09100   48.41800  1.000 84.78000  ? 92  ILE A CB     1 
ATOM   648   C  CG1    . ILE A 1 101 ? 23.37700  9.62400   47.34700  1.000 96.96000  ? 92  ILE A CG1    1 
ATOM   649   C  CG2    . ILE A 1 101 ? 25.53800  10.00300  48.56800  1.000 79.18000  ? 92  ILE A CG2    1 
ATOM   650   C  CD1    . ILE A 1 101 ? 22.74500  10.95600  47.70100  1.000 105.55000 ? 92  ILE A CD1    1 
ATOM   651   N  N      . VAL A 1 102 ? 25.33800  6.70400   50.25200  1.000 85.41000  ? 93  VAL A N      1 
ATOM   652   C  CA     . VAL A 1 102 ? 26.25500  6.19100   51.26500  1.000 86.94000  ? 93  VAL A CA     1 
ATOM   653   C  C      . VAL A 1 102 ? 26.98500  4.96700   50.73400  1.000 90.36000  ? 93  VAL A C      1 
ATOM   654   O  O      . VAL A 1 102 ? 28.21500  4.85600   50.83900  1.000 92.04000  ? 93  VAL A O      1 
ATOM   655   C  CB     . VAL A 1 102 ? 25.49500  5.87800   52.56600  1.000 79.28000  ? 93  VAL A CB     1 
ATOM   656   C  CG1    . VAL A 1 102 ? 26.36900  5.06600   53.51000  1.000 89.28000  ? 93  VAL A CG1    1 
ATOM   657   C  CG2    . VAL A 1 102 ? 25.03000  7.16300   53.22900  1.000 72.86000  ? 93  VAL A CG2    1 
ATOM   658   N  N      . GLY A 1 103 ? 26.23400  4.02600   50.15700  1.000 86.71000  ? 94  GLY A N      1 
ATOM   659   C  CA     . GLY A 1 103 ? 26.85600  2.83300   49.61800  1.000 73.74000  ? 94  GLY A CA     1 
ATOM   660   C  C      . GLY A 1 103 ? 27.86900  3.15700   48.54000  1.000 80.08000  ? 94  GLY A C      1 
ATOM   661   O  O      . GLY A 1 103 ? 28.94600  2.56100   48.48900  1.000 78.93000  ? 94  GLY A O      1 
ATOM   662   N  N      . MET A 1 104 ? 27.53800  4.10700   47.66300  1.000 77.35000  ? 95  MET A N      1 
ATOM   663   C  CA     . MET A 1 104 ? 28.43700  4.43300   46.56400  1.000 85.12000  ? 95  MET A CA     1 
ATOM   664   C  C      . MET A 1 104 ? 29.72200  5.07100   47.07400  1.000 88.83000  ? 95  MET A C      1 
ATOM   665   O  O      . MET A 1 104 ? 30.81300  4.74200   46.59400  1.000 91.52000  ? 95  MET A O      1 
ATOM   666   C  CB     . MET A 1 104 ? 27.73400  5.35200   45.56700  1.000 92.83000  ? 95  MET A CB     1 
ATOM   667   C  CG     . MET A 1 104 ? 28.54900  5.64700   44.31900  1.000 100.66000 ? 95  MET A CG     1 
ATOM   668   S  SD     . MET A 1 104 ? 28.88400  4.14200   43.37900  1.000 93.84000  ? 95  MET A SD     1 
ATOM   669   C  CE     . MET A 1 104 ? 27.24200  3.72600   42.79800  1.000 83.05000  ? 95  MET A CE     1 
ATOM   670   N  N      . LYS A 1 105 ? 29.62300  5.99000   48.03900  1.000 89.87000  ? 96  LYS A N      1 
ATOM   671   C  CA     . LYS A 1 105 ? 30.83600  6.57200   48.60900  1.000 82.04000  ? 96  LYS A CA     1 
ATOM   672   C  C      . LYS A 1 105 ? 31.68900  5.48700   49.25800  1.000 80.71000  ? 96  LYS A C      1 
ATOM   673   O  O      . LYS A 1 105 ? 32.90700  5.39900   49.02400  1.000 94.10000  ? 96  LYS A O      1 
ATOM   674   C  CB     . LYS A 1 105 ? 30.47500  7.66800   49.61600  1.000 65.81000  ? 96  LYS A CB     1 
ATOM   675   N  N      . MET A 1 106 ? 31.04300  4.61300   50.03700  1.000 79.41000  ? 97  MET A N      1 
ATOM   676   C  CA     . MET A 1 106 ? 31.75200  3.52500   50.69900  1.000 80.82000  ? 97  MET A CA     1 
ATOM   677   C  C      . MET A 1 106 ? 32.46600  2.63700   49.69300  1.000 75.49000  ? 97  MET A C      1 
ATOM   678   O  O      . MET A 1 106 ? 33.62700  2.26600   49.89700  1.000 65.00000  ? 97  MET A O      1 
ATOM   679   C  CB     . MET A 1 106 ? 30.76300  2.70300   51.52500  1.000 100.60000 ? 97  MET A CB     1 
ATOM   680   C  CG     . MET A 1 106 ? 31.40100  1.64900   52.40000  1.000 91.30000  ? 97  MET A CG     1 
ATOM   681   S  SD     . MET A 1 106 ? 32.84200  2.19700   53.32000  1.000 110.10000 ? 97  MET A SD     1 
ATOM   682   C  CE     . MET A 1 106 ? 33.90300  0.77800   53.07500  1.000 125.61000 ? 97  MET A CE     1 
ATOM   683   N  N      . ALA A 1 107 ? 31.79700  2.29600   48.59200  1.000 83.97000  ? 98  ALA A N      1 
ATOM   684   C  CA     . ALA A 1 107 ? 32.40100  1.39600   47.61800  1.000 86.48000  ? 98  ALA A CA     1 
ATOM   685   C  C      . ALA A 1 107 ? 33.53600  2.08000   46.86500  1.000 86.51000  ? 98  ALA A C      1 
ATOM   686   O  O      . ALA A 1 107 ? 34.61100  1.49600   46.68600  1.000 105.86000 ? 98  ALA A O      1 
ATOM   687   C  CB     . ALA A 1 107 ? 31.33800  0.88300   46.64600  1.000 92.45000  ? 98  ALA A CB     1 
ATOM   688   N  N      . THR A 1 108 ? 33.32100  3.32300   46.41600  1.000 76.48000  ? 99  THR A N      1 
ATOM   689   C  CA     . THR A 1 108 ? 34.35800  4.01500   45.65500  1.000 74.24000  ? 99  THR A CA     1 
ATOM   690   C  C      . THR A 1 108 ? 35.62900  4.17100   46.47400  1.000 94.42000  ? 99  THR A C      1 
ATOM   691   O  O      . THR A 1 108 ? 36.73700  4.07400   45.93200  1.000 95.08000  ? 99  THR A O      1 
ATOM   692   C  CB     . THR A 1 108 ? 33.87100  5.38700   45.18100  1.000 76.49000  ? 99  THR A CB     1 
ATOM   693   O  OG1    . THR A 1 108 ? 33.38000  6.13800   46.29700  1.000 88.57000  ? 99  THR A OG1    1 
ATOM   694   C  CG2    . THR A 1 108 ? 32.77800  5.23600   44.14100  1.000 88.01000  ? 99  THR A CG2    1 
ATOM   695   N  N      . ARG A 1 109 ? 35.49200  4.41700   47.77900  1.000 106.41000 ? 100 ARG A N      1 
ATOM   696   C  CA     . ARG A 1 109 ? 36.64700  4.59500   48.65400  1.000 101.21000 ? 100 ARG A CA     1 
ATOM   697   C  C      . ARG A 1 109 ? 37.12100  3.32200   49.35800  1.000 105.16000 ? 100 ARG A C      1 
ATOM   698   O  O      . ARG A 1 109 ? 37.93000  3.42800   50.28200  1.000 129.29000 ? 100 ARG A O      1 
ATOM   699   C  CB     . ARG A 1 109 ? 36.36500  5.71100   49.67100  1.000 89.50000  ? 100 ARG A CB     1 
ATOM   700   C  CG     . ARG A 1 109 ? 36.70200  7.07800   49.09400  1.000 91.80000  ? 100 ARG A CG     1 
ATOM   701   C  CD     . ARG A 1 109 ? 35.82600  8.22100   49.61600  1.000 104.87000 ? 100 ARG A CD     1 
ATOM   702   N  NE     . ARG A 1 109 ? 34.76300  8.56300   48.67400  1.000 119.60000 ? 100 ARG A NE     1 
ATOM   703   C  CZ     . ARG A 1 109 ? 33.94800  9.60200   48.80000  1.000 127.18000 ? 100 ARG A CZ     1 
ATOM   704   N  NH1    . ARG A 1 109 ? 34.05700  10.44800  49.81200  1.000 136.43000 ? 100 ARG A NH1    1 
ATOM   705   N  NH2    . ARG A 1 109 ? 33.02500  9.82200   47.86600  1.000 118.29000 ? 100 ARG A NH2    1 
ATOM   706   N  N      . ALA A 1 110 ? 36.60200  2.13900   49.01200  1.000 96.88000  ? 101 ALA A N      1 
ATOM   707   C  CA     . ALA A 1 110 ? 36.92400  0.92400   49.75900  1.000 85.58000  ? 101 ALA A CA     1 
ATOM   708   C  C      . ALA A 1 110 ? 37.79100  -0.08000  48.99400  1.000 95.97000  ? 101 ALA A C      1 
ATOM   709   O  O      . ALA A 1 110 ? 38.29200  -1.02800  49.61200  1.000 101.56000 ? 101 ALA A O      1 
ATOM   710   C  CB     . ALA A 1 110 ? 35.62900  0.25000   50.21600  1.000 99.66000  ? 101 ALA A CB     1 
ATOM   711   N  N      . ASN A 1 111 ? 37.92600  0.05200   47.67100  1.000 101.98000 ? 102 ASN A N      1 
ATOM   712   C  CA     . ASN A 1 111 ? 38.70000  -0.91500  46.88600  1.000 117.73000 ? 102 ASN A CA     1 
ATOM   713   C  C      . ASN A 1 111 ? 40.18100  -0.85800  47.27100  1.000 133.29000 ? 102 ASN A C      1 
ATOM   714   O  O      . ASN A 1 111 ? 40.82300  -1.90000  47.50600  1.000 131.51000 ? 102 ASN A O      1 
ATOM   715   C  CB     . ASN A 1 111 ? 38.50700  -0.61900  45.39800  1.000 116.21000 ? 102 ASN A CB     1 
ATOM   716   C  CG     . ASN A 1 111 ? 39.06700  0.73600   45.00100  1.000 115.55000 ? 102 ASN A CG     1 
ATOM   717   O  OD1    . ASN A 1 111 ? 40.07300  1.18700   45.54500  1.000 118.75000 ? 102 ASN A OD1    1 
ATOM   718   N  ND2    . ASN A 1 111 ? 38.41500  1.39100   44.05000  1.000 118.22000 ? 102 ASN A ND2    1 
ATOM   719   N  N      . VAL A 1 112 ? 40.73000  0.35200   47.39800  1.000 136.00000 ? 103 VAL A N      1 
ATOM   720   C  CA     . VAL A 1 112 ? 42.15400  0.46900   47.68200  1.000 122.19000 ? 103 VAL A CA     1 
ATOM   721   C  C      . VAL A 1 112 ? 42.50100  -0.11100  49.04500  1.000 119.64000 ? 103 VAL A C      1 
ATOM   722   O  O      . VAL A 1 112 ? 43.57700  -0.69400  49.22400  1.000 136.68000 ? 103 VAL A O      1 
ATOM   723   C  CB     . VAL A 1 112 ? 42.59800  1.93800   47.51700  1.000 125.32000 ? 103 VAL A CB     1 
ATOM   724   C  CG1    . VAL A 1 112 ? 42.42000  2.40000   46.06900  1.000 123.39000 ? 103 VAL A CG1    1 
ATOM   725   C  CG2    . VAL A 1 112 ? 41.84400  2.85000   48.47100  1.000 122.84000 ? 103 VAL A CG2    1 
ATOM   726   N  N      . ARG A 1 113 ? 41.60900  0.03900   50.02600  1.000 121.60000 ? 104 ARG A N      1 
ATOM   727   C  CA     . ARG A 1 113 ? 41.84800  -0.57900  51.32400  1.000 132.78000 ? 104 ARG A CA     1 
ATOM   728   C  C      . ARG A 1 113 ? 42.05900  -2.08500  51.24000  1.000 131.87000 ? 104 ARG A C      1 
ATOM   729   O  O      . ARG A 1 113 ? 42.97800  -2.62600  51.86200  1.000 140.91000 ? 104 ARG A O      1 
ATOM   730   C  CB     . ARG A 1 113 ? 40.67900  -0.25200  52.25600  1.000 146.57000 ? 104 ARG A CB     1 
ATOM   731   C  CG     . ARG A 1 113 ? 40.16000  1.18100   52.15100  1.000 141.67000 ? 104 ARG A CG     1 
ATOM   732   C  CD     . ARG A 1 113 ? 41.15200  2.18100   52.73200  1.000 135.76000 ? 104 ARG A CD     1 
ATOM   733   N  NE     . ARG A 1 113 ? 40.49200  3.36800   53.26500  1.000 124.38000 ? 104 ARG A NE     1 
ATOM   734   C  CZ     . ARG A 1 113 ? 40.25100  4.46600   52.56300  1.000 123.14000 ? 104 ARG A CZ     1 
ATOM   735   N  NH1    . ARG A 1 113 ? 40.61400  4.56700   51.29500  1.000 136.51000 ? 104 ARG A NH1    1 
ATOM   736   N  NH2    . ARG A 1 113 ? 39.63500  5.48900   53.14900  1.000 103.90000 ? 104 ARG A NH2    1 
ATOM   737   N  N      . VAL A 1 114 ? 41.22500  -2.77800  50.46200  1.000 127.99000 ? 105 VAL A N      1 
ATOM   738   C  CA     . VAL A 1 114 ? 41.35900  -4.22600  50.34300  1.000 133.97000 ? 105 VAL A CA     1 
ATOM   739   C  C      . VAL A 1 114 ? 42.65800  -4.59700  49.63400  1.000 151.91000 ? 105 VAL A C      1 
ATOM   740   O  O      . VAL A 1 114 ? 43.36600  -5.52100  50.05400  1.000 154.83000 ? 105 VAL A O      1 
ATOM   741   C  CB     . VAL A 1 114 ? 40.12400  -4.81000  49.63200  1.000 125.28000 ? 105 VAL A CB     1 
ATOM   742   C  CG1    . VAL A 1 114 ? 40.21200  -6.32700  49.54800  1.000 121.41000 ? 105 VAL A CG1    1 
ATOM   743   C  CG2    . VAL A 1 114 ? 38.85400  -4.38900  50.36000  1.000 103.82000 ? 105 VAL A CG2    1 
ATOM   744   N  N      . ALA A 1 115 ? 43.01000  -3.87800  48.56200  1.000 148.69000 ? 106 ALA A N      1 
ATOM   745   C  CA     . ALA A 1 115 ? 44.24800  -4.21100  47.85400  1.000 137.61000 ? 106 ALA A CA     1 
ATOM   746   C  C      . ALA A 1 115 ? 45.47600  -4.02000  48.74400  1.000 146.35000 ? 106 ALA A C      1 
ATOM   747   O  O      . ALA A 1 115 ? 46.33600  -4.91100  48.86200  1.000 150.33000 ? 106 ALA A O      1 
ATOM   748   C  CB     . ALA A 1 115 ? 44.36700  -3.36500  46.58600  1.000 114.28000 ? 106 ALA A CB     1 
ATOM   749   N  N      . GLU A 1 116 ? 45.57100  -2.85800  49.38900  1.000 143.56000 ? 107 GLU A N      1 
ATOM   750   C  CA     . GLU A 1 116 ? 46.69300  -2.61000  50.27900  1.000 136.11000 ? 107 GLU A CA     1 
ATOM   751   C  C      . GLU A 1 116 ? 46.68100  -3.55500  51.47400  1.000 142.14000 ? 107 GLU A C      1 
ATOM   752   O  O      . GLU A 1 116 ? 47.74600  -3.89800  51.99000  1.000 151.72000 ? 107 GLU A O      1 
ATOM   753   C  CB     . GLU A 1 116 ? 46.69800  -1.15100  50.72700  1.000 126.46000 ? 107 GLU A CB     1 
ATOM   754   C  CG     . GLU A 1 116 ? 47.88100  -0.80800  51.60100  1.000 138.40000 ? 107 GLU A CG     1 
ATOM   755   C  CD     . GLU A 1 116 ? 49.20100  -1.10300  50.91300  1.000 130.02000 ? 107 GLU A CD     1 
ATOM   756   O  OE1    . GLU A 1 116 ? 49.27400  -0.96400  49.67400  1.000 127.11000 ? 107 GLU A OE1    1 
ATOM   757   O  OE2    . GLU A 1 116 ? 50.16200  -1.49200  51.60800  1.000 124.96000 ? 107 GLU A OE2    1 
ATOM   758   N  N      . ALA A 1 117 ? 45.50000  -3.97900  51.93800  1.000 135.94000 ? 108 ALA A N      1 
ATOM   759   C  CA     . ALA A 1 117 ? 45.44400  -4.97800  52.99900  1.000 133.35000 ? 108 ALA A CA     1 
ATOM   760   C  C      . ALA A 1 117 ? 46.01500  -6.30600  52.52500  1.000 131.48000 ? 108 ALA A C      1 
ATOM   761   O  O      . ALA A 1 117 ? 46.69300  -7.00700  53.28500  1.000 128.61000 ? 108 ALA A O      1 
ATOM   762   C  CB     . ALA A 1 117 ? 44.00600  -5.15000  53.48600  1.000 135.90000 ? 108 ALA A CB     1 
ATOM   763   N  N      . ALA A 1 118 ? 45.73900  -6.67500  51.27200  1.000 135.78000 ? 109 ALA A N      1 
ATOM   764   C  CA     . ALA A 1 118 ? 46.31500  -7.90000  50.73000  1.000 132.75000 ? 109 ALA A CA     1 
ATOM   765   C  C      . ALA A 1 118 ? 47.83300  -7.81100  50.70900  1.000 138.69000 ? 109 ALA A C      1 
ATOM   766   O  O      . ALA A 1 118 ? 48.52700  -8.78400  51.02800  1.000 123.91000 ? 109 ALA A O      1 
ATOM   767   C  CB     . ALA A 1 118 ? 45.76900  -8.17600  49.32800  1.000 139.14000 ? 109 ALA A CB     1 
ATOM   768   N  N      . ARG A 1 119 ? 48.37200  -6.65000  50.33300  1.000 146.24000 ? 110 ARG A N      1 
ATOM   769   C  CA     . ARG A 1 119 ? 49.82900  -6.52200  50.33900  1.000 112.61000 ? 110 ARG A CA     1 
ATOM   770   C  C      . ARG A 1 119 ? 50.39700  -6.49100  51.75900  1.000 113.42000 ? 110 ARG A C      1 
ATOM   771   O  O      . ARG A 1 119 ? 51.41000  -7.14200  52.03700  1.000 111.25000 ? 110 ARG A O      1 
ATOM   772   C  CB     . ARG A 1 119 ? 50.26900  -5.28800  49.55700  1.000 90.17000  ? 110 ARG A CB     1 
ATOM   773   C  CG     . ARG A 1 119 ? 51.78900  -5.17400  49.41700  1.000 103.92000 ? 110 ARG A CG     1 
ATOM   774   C  CD     . ARG A 1 119 ? 52.41700  -6.40100  48.74400  1.000 119.93000 ? 110 ARG A CD     1 
ATOM   775   N  NE     . ARG A 1 119 ? 53.87300  -6.30300  48.66000  1.000 133.29000 ? 110 ARG A NE     1 
ATOM   776   C  CZ     . ARG A 1 119 ? 54.72400  -6.76100  49.56900  1.000 128.75000 ? 110 ARG A CZ     1 
ATOM   777   N  NH1    . ARG A 1 119 ? 54.30400  -7.37200  50.66400  1.000 133.94000 ? 110 ARG A NH1    1 
ATOM   778   N  NH2    . ARG A 1 119 ? 56.03000  -6.60100  49.37400  1.000 114.98000 ? 110 ARG A NH2    1 
ATOM   779   N  N      . THR A 1 120 ? 49.75000  -5.75800  52.67100  1.000 129.11000 ? 111 THR A N      1 
ATOM   780   C  CA     . THR A 1 120 ? 50.27600  -5.56100  54.02200  1.000 134.61000 ? 111 THR A CA     1 
ATOM   781   C  C      . THR A 1 120 ? 50.20400  -6.82900  54.86500  1.000 133.45000 ? 111 THR A C      1 
ATOM   782   O  O      . THR A 1 120 ? 51.13100  -7.12400  55.62900  1.000 152.13000 ? 111 THR A O      1 
ATOM   783   C  CB     . THR A 1 120 ? 49.50600  -4.43000  54.70600  1.000 137.15000 ? 111 THR A CB     1 
ATOM   784   O  OG1    . THR A 1 120 ? 49.65700  -3.22400  53.94800  1.000 140.86000 ? 111 THR A OG1    1 
ATOM   785   C  CG2    . THR A 1 120 ? 50.00400  -4.20500  56.12500  1.000 146.37000 ? 111 THR A CG2    1 
ATOM   786   N  N      . THR A 1 121 ? 49.11200  -7.57900  54.76100  1.000 123.00000 ? 112 THR A N      1 
ATOM   787   C  CA     . THR A 1 121 ? 48.95100  -8.80300  55.52700  1.000 119.01000 ? 112 THR A CA     1 
ATOM   788   C  C      . THR A 1 121 ? 49.36100  -10.03700 54.74000  1.000 118.69000 ? 112 THR A C      1 
ATOM   789   O  O      . THR A 1 121 ? 49.37900  -11.13700 55.30000  1.000 119.80000 ? 112 THR A O      1 
ATOM   790   C  CB     . THR A 1 121 ? 47.49700  -8.94000  56.00400  1.000 110.59000 ? 112 THR A CB     1 
ATOM   791   O  OG1    . THR A 1 121 ? 46.62400  -9.04500  54.87100  1.000 113.21000 ? 112 THR A OG1    1 
ATOM   792   C  CG2    . THR A 1 121 ? 47.09200  -7.74500  56.85000  1.000 103.33000 ? 112 THR A CG2    1 
ATOM   793   N  N      . LYS A 1 122 ? 49.71200  -9.87500  53.46200  1.000 111.59000 ? 113 LYS A N      1 
ATOM   794   C  CA     . LYS A 1 122 ? 50.17700  -10.98500 52.63000  1.000 108.89000 ? 113 LYS A CA     1 
ATOM   795   C  C      . LYS A 1 122 ? 49.17500  -12.13500 52.63300  1.000 113.21000 ? 113 LYS A C      1 
ATOM   796   O  O      . LYS A 1 122 ? 49.54800  -13.30200 52.49200  1.000 116.69000 ? 113 LYS A O      1 
ATOM   797   C  CB     . LYS A 1 122 ? 51.55800  -11.46500 53.08200  1.000 131.39000 ? 113 LYS A CB     1 
ATOM   798   C  CG     . LYS A 1 122 ? 52.64200  -10.39600 53.01100  1.000 129.45000 ? 113 LYS A CG     1 
ATOM   799   C  CD     . LYS A 1 122 ? 53.68300  -10.72300 51.94900  1.000 121.52000 ? 113 LYS A CD     1 
ATOM   800   C  CE     . LYS A 1 122 ? 53.07400  -10.73300 50.56900  1.000 121.86000 ? 113 LYS A CE     1 
ATOM   801   N  NZ     . LYS A 1 122 ? 54.09300  -10.92700 49.50500  1.000 123.74000 ? 113 LYS A NZ     1 
ATOM   802   N  N      . LYS A 1 123 ? 47.89500  -11.81100 52.80200  1.000 110.33000 ? 114 LYS A N      1 
ATOM   803   C  CA     . LYS A 1 123 ? 46.85000  -12.81500 52.93000  1.000 114.52000 ? 114 LYS A CA     1 
ATOM   804   C  C      . LYS A 1 123 ? 45.53400  -12.23400 52.43700  1.000 116.35000 ? 114 LYS A C      1 
ATOM   805   O  O      . LYS A 1 123 ? 45.32200  -11.01900 52.47500  1.000 124.43000 ? 114 LYS A O      1 
ATOM   806   C  CB     . LYS A 1 123 ? 46.69700  -13.29400 54.37900  1.000 120.22000 ? 114 LYS A CB     1 
ATOM   807   N  N      . ILE A 1 124 ? 44.64600  -13.12100 51.99000  1.000 132.21000 ? 115 ILE A N      1 
ATOM   808   C  CA     . ILE A 1 124 ? 43.37200  -12.69100 51.42500  1.000 129.09000 ? 115 ILE A CA     1 
ATOM   809   C  C      . ILE A 1 124 ? 42.36900  -12.37300 52.52800  1.000 130.28000 ? 115 ILE A C      1 
ATOM   810   O  O      . ILE A 1 124 ? 41.56400  -11.44600 52.39500  1.000 127.50000 ? 115 ILE A O      1 
ATOM   811   C  CB     . ILE A 1 124 ? 42.84700  -13.76900 50.46100  1.000 123.11000 ? 115 ILE A CB     1 
ATOM   812   C  CG1    . ILE A 1 124 ? 41.50500  -13.35600 49.85400  1.000 130.00000 ? 115 ILE A CG1    1 
ATOM   813   C  CG2    . ILE A 1 124 ? 42.73800  -15.11200 51.18300  1.000 123.30000 ? 115 ILE A CG2    1 
ATOM   814   C  CD1    . ILE A 1 124 ? 41.01000  -14.30200 48.79000  1.000 135.25000 ? 115 ILE A CD1    1 
ATOM   815   N  N      . GLY A 1 125 ? 42.41700  -13.12200 53.63000  1.000 137.77000 ? 116 GLY A N      1 
ATOM   816   C  CA     . GLY A 1 125 ? 41.53400  -12.95500 54.76400  1.000 133.76000 ? 116 GLY A CA     1 
ATOM   817   C  C      . GLY A 1 125 ? 41.36300  -11.51900 55.22400  1.000 140.37000 ? 116 GLY A C      1 
ATOM   818   O  O      . GLY A 1 125 ? 40.25100  -10.97000 55.25600  1.000 152.40000 ? 116 GLY A O      1 
ATOM   819   N  N      . PRO A 1 126 ? 42.46000  -10.92500 55.70100  1.000 128.62000 ? 117 PRO A N      1 
ATOM   820   C  CA     . PRO A 1 126 ? 42.37100  -9.56000  56.24600  1.000 126.19000 ? 117 PRO A CA     1 
ATOM   821   C  C      . PRO A 1 126 ? 41.84000  -8.54000  55.25000  1.000 125.19000 ? 117 PRO A C      1 
ATOM   822   O  O      . PRO A 1 126 ? 41.07400  -7.64900  55.63800  1.000 134.85000 ? 117 PRO A O      1 
ATOM   823   C  CB     . PRO A 1 126 ? 43.82800  -9.26500  56.63500  1.000 116.08000 ? 117 PRO A CB     1 
ATOM   824   C  CG     . PRO A 1 126 ? 44.40800  -10.63200 56.92300  1.000 117.75000 ? 117 PRO A CG     1 
ATOM   825   C  CD     . PRO A 1 126 ? 43.80900  -11.49700 55.85500  1.000 125.94000 ? 117 PRO A CD     1 
ATOM   826   N  N      . ALA A 1 127 ? 42.23300  -8.63300  53.97600  1.000 114.33000 ? 118 ALA A N      1 
ATOM   827   C  CA     . ALA A 1 127 ? 41.68500  -7.73000  52.96500  1.000 119.69000 ? 118 ALA A CA     1 
ATOM   828   C  C      . ALA A 1 127 ? 40.19100  -7.96800  52.76200  1.000 135.41000 ? 118 ALA A C      1 
ATOM   829   O  O      . ALA A 1 127 ? 39.42100  -7.02200  52.53800  1.000 129.14000 ? 118 ALA A O      1 
ATOM   830   C  CB     . ALA A 1 127 ? 42.44700  -7.89100  51.65200  1.000 119.42000 ? 118 ALA A CB     1 
ATOM   831   N  N      . LEU A 1 128 ? 39.76800  -9.23300  52.81400  1.000 145.57000 ? 119 LEU A N      1 
ATOM   832   C  CA     . LEU A 1 128 ? 38.35500  -9.54700  52.65500  1.000 129.36000 ? 119 LEU A CA     1 
ATOM   833   C  C      . LEU A 1 128 ? 37.52800  -8.97100  53.78900  1.000 127.40000 ? 119 LEU A C      1 
ATOM   834   O  O      . LEU A 1 128 ? 36.36600  -8.60900  53.58200  1.000 129.65000 ? 119 LEU A O      1 
ATOM   835   C  CB     . LEU A 1 128 ? 38.14500  -11.05300 52.56700  1.000 123.92000 ? 119 LEU A CB     1 
ATOM   836   C  CG     . LEU A 1 128 ? 36.67300  -11.46300 52.63400  1.000 118.24000 ? 119 LEU A CG     1 
ATOM   837   C  CD1    . LEU A 1 128 ? 35.88200  -10.85800 51.47300  1.000 119.10000 ? 119 LEU A CD1    1 
ATOM   838   C  CD2    . LEU A 1 128 ? 36.52500  -12.96900 52.66200  1.000 123.61000 ? 119 LEU A CD2    1 
ATOM   839   N  N      . LYS A 1 129 ? 38.08100  -8.93300  55.00300  1.000 130.71000 ? 120 LYS A N      1 
ATOM   840   C  CA     . LYS A 1 129 ? 37.34700  -8.28900  56.09000  1.000 117.13000 ? 120 LYS A CA     1 
ATOM   841   C  C      . LYS A 1 129 ? 37.00700  -6.84700  55.72600  1.000 128.77000 ? 120 LYS A C      1 
ATOM   842   O  O      . LYS A 1 129 ? 35.88500  -6.38200  55.96300  1.000 133.50000 ? 120 LYS A O      1 
ATOM   843   C  CB     . LYS A 1 129 ? 38.14000  -8.34700  57.39800  1.000 116.28000 ? 120 LYS A CB     1 
ATOM   844   C  CG     . LYS A 1 129 ? 38.05800  -9.68800  58.12100  1.000 116.19000 ? 120 LYS A CG     1 
ATOM   845   C  CD     . LYS A 1 129 ? 39.20700  -9.87200  59.11000  1.000 128.97000 ? 120 LYS A CD     1 
ATOM   846   C  CE     . LYS A 1 129 ? 39.33500  -8.68400  60.05600  1.000 134.00000 ? 120 LYS A CE     1 
ATOM   847   N  NZ     . LYS A 1 129 ? 38.30800  -8.69600  61.13400  1.000 121.54000 ? 120 LYS A NZ     1 
ATOM   848   N  N      . VAL A 1 130 ? 37.95800  -6.13600  55.11300  1.000 129.18000 ? 121 VAL A N      1 
ATOM   849   C  CA     . VAL A 1 130 ? 37.72000  -4.76100  54.68600  1.000 122.56000 ? 121 VAL A CA     1 
ATOM   850   C  C      . VAL A 1 130 ? 36.68300  -4.71700  53.57100  1.000 123.58000 ? 121 VAL A C      1 
ATOM   851   O  O      . VAL A 1 130 ? 35.78000  -3.87200  53.57500  1.000 124.46000 ? 121 VAL A O      1 
ATOM   852   C  CB     . VAL A 1 130 ? 39.04300  -4.10100  54.25100  1.000 128.43000 ? 121 VAL A CB     1 
ATOM   853   C  CG1    . VAL A 1 130 ? 38.79000  -2.70200  53.70600  1.000 133.98000 ? 121 VAL A CG1    1 
ATOM   854   C  CG2    . VAL A 1 130 ? 40.03100  -4.06300  55.40900  1.000 124.86000 ? 121 VAL A CG2    1 
ATOM   855   N  N      . ALA A 1 131 ? 36.80100  -5.61700  52.59100  1.000 116.28000 ? 122 ALA A N      1 
ATOM   856   C  CA     . ALA A 1 131 ? 35.86300  -5.59500  51.46900  1.000 112.85000 ? 122 ALA A CA     1 
ATOM   857   C  C      . ALA A 1 131 ? 34.43200  -5.85400  51.93700  1.000 121.15000 ? 122 ALA A C      1 
ATOM   858   O  O      . ALA A 1 131 ? 33.48000  -5.22200  51.45300  1.000 114.39000 ? 122 ALA A O      1 
ATOM   859   C  CB     . ALA A 1 131 ? 36.28000  -6.62000  50.41600  1.000 105.61000 ? 122 ALA A CB     1 
ATOM   860   N  N      . TYR A 1 132 ? 34.26100  -6.78000  52.88500  1.000 131.37000 ? 123 TYR A N      1 
ATOM   861   C  CA     . TYR A 1 132 ? 32.92900  -7.07700  53.39800  1.000 119.86000 ? 123 TYR A CA     1 
ATOM   862   C  C      . TYR A 1 132 ? 32.41900  -5.95500  54.29100  1.000 120.01000 ? 123 TYR A C      1 
ATOM   863   O  O      . TYR A 1 132 ? 31.22200  -5.65000  54.28100  1.000 123.08000 ? 123 TYR A O      1 
ATOM   864   C  CB     . TYR A 1 132 ? 32.92100  -8.40200  54.15800  1.000 113.49000 ? 123 TYR A CB     1 
ATOM   865   C  CG     . TYR A 1 132 ? 31.53100  -8.84700  54.55900  1.000 115.34000 ? 123 TYR A CG     1 
ATOM   866   C  CD1    . TYR A 1 132 ? 30.64300  -9.34800  53.61600  1.000 134.99000 ? 123 TYR A CD1    1 
ATOM   867   C  CD2    . TYR A 1 132 ? 31.10200  -8.75800  55.87800  1.000 130.94000 ? 123 TYR A CD2    1 
ATOM   868   C  CE1    . TYR A 1 132 ? 29.36900  -9.75400  53.97400  1.000 143.90000 ? 123 TYR A CE1    1 
ATOM   869   C  CE2    . TYR A 1 132 ? 29.82600  -9.16300  56.24600  1.000 150.02000 ? 123 TYR A CE2    1 
ATOM   870   C  CZ     . TYR A 1 132 ? 28.96500  -9.65900  55.28900  1.000 141.08000 ? 123 TYR A CZ     1 
ATOM   871   O  OH     . TYR A 1 132 ? 27.69800  -10.06400 55.64600  1.000 113.13000 ? 123 TYR A OH     1 
ATOM   872   N  N      . GLN A 1 133 ? 33.30200  -5.33500  55.08200  1.000 124.87000 ? 124 GLN A N      1 
ATOM   873   C  CA     . GLN A 1 133 ? 32.89100  -4.15600  55.83500  1.000 129.72000 ? 124 GLN A CA     1 
ATOM   874   C  C      . GLN A 1 133 ? 32.46000  -3.03400  54.90100  1.000 125.77000 ? 124 GLN A C      1 
ATOM   875   O  O      . GLN A 1 133 ? 31.62800  -2.20000  55.27100  1.000 138.22000 ? 124 GLN A O      1 
ATOM   876   C  CB     . GLN A 1 133 ? 34.02600  -3.68800  56.74700  1.000 131.88000 ? 124 GLN A CB     1 
ATOM   877   C  CG     . GLN A 1 133 ? 33.55600  -2.93000  57.97800  1.000 132.08000 ? 124 GLN A CG     1 
ATOM   878   C  CD     . GLN A 1 133 ? 34.61700  -2.85600  59.05800  1.000 149.09000 ? 124 GLN A CD     1 
ATOM   879   O  OE1    . GLN A 1 133 ? 35.40200  -1.91000  59.10800  1.000 145.96000 ? 124 GLN A OE1    1 
ATOM   880   N  NE2    . GLN A 1 133 ? 34.64500  -3.85900  59.93100  1.000 157.10000 ? 124 GLN A NE2    1 
ATOM   881   N  N      . GLY A 1 134 ? 33.01800  -2.99600  53.69400  1.000 112.81000 ? 125 GLY A N      1 
ATOM   882   C  CA     . GLY A 1 134 ? 32.57400  -2.05700  52.68400  1.000 101.18000 ? 125 GLY A CA     1 
ATOM   883   C  C      . GLY A 1 134 ? 31.18100  -2.36600  52.17700  1.000 97.48000  ? 125 GLY A C      1 
ATOM   884   O  O      . GLY A 1 134 ? 30.27900  -1.52700  52.26200  1.000 100.73000 ? 125 GLY A O      1 
ATOM   885   N  N      . GLY A 1 135 ? 30.99700  -3.57400  51.63800  1.000 103.51000 ? 126 GLY A N      1 
ATOM   886   C  CA     . GLY A 1 135 ? 29.68200  -3.95600  51.13700  1.000 104.54000 ? 126 GLY A CA     1 
ATOM   887   C  C      . GLY A 1 135 ? 28.58500  -3.86200  52.18300  1.000 106.68000 ? 126 GLY A C      1 
ATOM   888   O  O      . GLY A 1 135 ? 27.42800  -3.54300  51.86200  1.000 93.34000  ? 126 GLY A O      1 
ATOM   889   N  N      . SER A 1 136 ? 28.92900  -4.12800  53.44800  1.000 118.76000 ? 127 SER A N      1 
ATOM   890   C  CA     . SER A 1 136 ? 27.94400  -4.06000  54.51800  1.000 106.92000 ? 127 SER A CA     1 
ATOM   891   C  C      . SER A 1 136 ? 27.41300  -2.65000  54.68500  1.000 92.04000  ? 127 SER A C      1 
ATOM   892   O  O      . SER A 1 136 ? 26.28000  -2.46800  55.13200  1.000 89.11000  ? 127 SER A O      1 
ATOM   893   C  CB     . SER A 1 136 ? 28.54600  -4.55900  55.83100  1.000 94.06000  ? 127 SER A CB     1 
ATOM   894   O  OG     . SER A 1 136 ? 29.65900  -3.77100  56.21200  1.000 107.79000 ? 127 SER A OG     1 
ATOM   895   N  N      . VAL A 1 137 ? 28.20900  -1.64000  54.33600  1.000 83.27000  ? 128 VAL A N      1 
ATOM   896   C  CA     . VAL A 1 137 ? 27.71400  -0.27100  54.41200  1.000 91.93000  ? 128 VAL A CA     1 
ATOM   897   C  C      . VAL A 1 137 ? 26.47700  -0.11900  53.54200  1.000 100.49000 ? 128 VAL A C      1 
ATOM   898   O  O      . VAL A 1 137 ? 25.42000  0.31600   54.00800  1.000 105.04000 ? 128 VAL A O      1 
ATOM   899   C  CB     . VAL A 1 137 ? 28.81200  0.72700   54.00900  1.000 106.13000 ? 128 VAL A CB     1 
ATOM   900   C  CG1    . VAL A 1 137 ? 28.22500  2.12000   53.86000  1.000 105.00000 ? 128 VAL A CG1    1 
ATOM   901   C  CG2    . VAL A 1 137 ? 29.92500  0.72800   55.04100  1.000 119.70000 ? 128 VAL A CG2    1 
ATOM   902   N  N      . MET A 1 138 ? 26.57700  -0.52000  52.27300  1.000 96.86000  ? 129 MET A N      1 
ATOM   903   C  CA     . MET A 1 138 ? 25.43000  -0.40700  51.37900  1.000 79.06000  ? 129 MET A CA     1 
ATOM   904   C  C      . MET A 1 138 ? 24.28600  -1.31000  51.82400  1.000 70.72000  ? 129 MET A C      1 
ATOM   905   O  O      . MET A 1 138 ? 23.12000  -0.89300  51.81300  1.000 61.43000  ? 129 MET A O      1 
ATOM   906   C  CB     . MET A 1 138 ? 25.84600  -0.73600  49.94600  1.000 80.95000  ? 129 MET A CB     1 
ATOM   907   C  CG     . MET A 1 138 ? 24.72800  -0.58400  48.93300  1.000 90.85000  ? 129 MET A CG     1 
ATOM   908   S  SD     . MET A 1 138 ? 23.89000  1.00500   49.07900  1.000 85.44000  ? 129 MET A SD     1 
ATOM   909   C  CE     . MET A 1 138 ? 22.66600  0.85900   47.77800  1.000 89.23000  ? 129 MET A CE     1 
ATOM   910   N  N      . GLY A 1 139 ? 24.59400  -2.55100  52.21100  1.000 81.93000  ? 130 GLY A N      1 
ATOM   911   C  CA     . GLY A 1 139 ? 23.53200  -3.45600  52.63600  1.000 84.27000  ? 130 GLY A CA     1 
ATOM   912   C  C      . GLY A 1 139 ? 22.75400  -2.92500  53.82600  1.000 75.65000  ? 130 GLY A C      1 
ATOM   913   O  O      . GLY A 1 139 ? 21.51800  -2.84600  53.80400  1.000 71.05000  ? 130 GLY A O      1 
ATOM   914   N  N      . LEU A 1 140 ? 23.47200  -2.57000  54.89300  1.000 84.27000  ? 131 LEU A N      1 
ATOM   915   C  CA     . LEU A 1 140 ? 22.85100  -2.02900  56.09100  1.000 102.30000 ? 131 LEU A CA     1 
ATOM   916   C  C      . LEU A 1 140 ? 22.18100  -0.69400  55.81900  1.000 102.71000 ? 131 LEU A C      1 
ATOM   917   O  O      . LEU A 1 140 ? 21.16600  -0.38200  56.44000  1.000 85.69000  ? 131 LEU A O      1 
ATOM   918   C  CB     . LEU A 1 140 ? 23.90400  -1.87800  57.18300  1.000 95.11000  ? 131 LEU A CB     1 
ATOM   919   C  CG     . LEU A 1 140 ? 24.50000  -3.20400  57.64300  1.000 98.27000  ? 131 LEU A CG     1 
ATOM   920   C  CD1    . LEU A 1 140 ? 25.88200  -2.96900  58.20000  1.000 116.88000 ? 131 LEU A CD1    1 
ATOM   921   C  CD2    . LEU A 1 140 ? 23.60100  -3.85300  58.68100  1.000 104.56000 ? 131 LEU A CD2    1 
ATOM   922   N  N      . SER A 1 141 ? 22.72100  0.10500   54.89700  1.000 100.37000 ? 132 SER A N      1 
ATOM   923   C  CA     . SER A 1 141 ? 22.07800  1.36400   54.54900  1.000 81.09000  ? 132 SER A CA     1 
ATOM   924   C  C      . SER A 1 141 ? 20.71400  1.11000   53.93100  1.000 85.96000  ? 132 SER A C      1 
ATOM   925   O  O      . SER A 1 141 ? 19.70500  1.68500   54.35400  1.000 85.40000  ? 132 SER A O      1 
ATOM   926   C  CB     . SER A 1 141 ? 22.97000  2.15100   53.59100  1.000 70.10000  ? 132 SER A CB     1 
ATOM   927   O  OG     . SER A 1 141 ? 22.46600  3.45400   53.38300  1.000 72.33000  ? 132 SER A OG     1 
ATOM   928   N  N      . VAL A 1 142 ? 20.66800  0.23800   52.92300  1.000 92.36000  ? 133 VAL A N      1 
ATOM   929   C  CA     . VAL A 1 142 ? 19.39200  -0.17400  52.34200  1.000 93.52000  ? 133 VAL A CA     1 
ATOM   930   C  C      . VAL A 1 142 ? 18.43100  -0.60300  53.44400  1.000 89.29000  ? 133 VAL A C      1 
ATOM   931   O  O      . VAL A 1 142 ? 17.33900  -0.04000  53.60600  1.000 79.57000  ? 133 VAL A O      1 
ATOM   932   C  CB     . VAL A 1 142 ? 19.61200  -1.30200  51.31900  1.000 83.44000  ? 133 VAL A CB     1 
ATOM   933   C  CG1    . VAL A 1 142 ? 18.31600  -2.05100  51.05900  1.000 84.26000  ? 133 VAL A CG1    1 
ATOM   934   C  CG2    . VAL A 1 142 ? 20.18900  -0.74400  50.02800  1.000 83.37000  ? 133 VAL A CG2    1 
ATOM   935   N  N      . GLY A 1 143 ? 18.83700  -1.60800  54.22500  1.000 90.00000  ? 134 GLY A N      1 
ATOM   936   C  CA     . GLY A 1 143 ? 17.93300  -2.16100  55.22400  1.000 86.09000  ? 134 GLY A CA     1 
ATOM   937   C  C      . GLY A 1 143 ? 17.45200  -1.12400  56.22100  1.000 80.68000  ? 134 GLY A C      1 
ATOM   938   O  O      . GLY A 1 143 ? 16.24800  -0.97900  56.46000  1.000 83.95000  ? 134 GLY A O      1 
ATOM   939   N  N      . GLY A 1 144 ? 18.39000  -0.39100  56.82200  1.000 77.57000  ? 135 GLY A N      1 
ATOM   940   C  CA     . GLY A 1 144 ? 18.03400  0.56200   57.85400  1.000 94.09000  ? 135 GLY A CA     1 
ATOM   941   C  C      . GLY A 1 144 ? 17.18800  1.70500   57.33800  1.000 85.33000  ? 135 GLY A C      1 
ATOM   942   O  O      . GLY A 1 144 ? 16.21400  2.09300   57.97900  1.000 98.41000  ? 135 GLY A O      1 
ATOM   943   N  N      . PHE A 1 145 ? 17.54400  2.26900   56.18100  1.000 70.40000  ? 136 PHE A N      1 
ATOM   944   C  CA     . PHE A 1 145 ? 16.74300  3.35700   55.63600  1.000 71.71000  ? 136 PHE A CA     1 
ATOM   945   C  C      . PHE A 1 145 ? 15.33300  2.88800   55.31100  1.000 94.80000  ? 136 PHE A C      1 
ATOM   946   O  O      . PHE A 1 145 ? 14.35300  3.58100   55.61600  1.000 85.26000  ? 136 PHE A O      1 
ATOM   947   C  CB     . PHE A 1 145 ? 17.42000  3.93500   54.39600  1.000 67.21000  ? 136 PHE A CB     1 
ATOM   948   C  CG     . PHE A 1 145 ? 18.53000  4.88100   54.71500  1.000 76.72000  ? 136 PHE A CG     1 
ATOM   949   C  CD1    . PHE A 1 145 ? 18.26000  6.10000   55.30800  1.000 93.50000  ? 136 PHE A CD1    1 
ATOM   950   C  CD2    . PHE A 1 145 ? 19.84300  4.55100   54.44000  1.000 80.89000  ? 136 PHE A CD2    1 
ATOM   951   C  CE1    . PHE A 1 145 ? 19.27700  6.97600   55.61400  1.000 92.72000  ? 136 PHE A CE1    1 
ATOM   952   C  CE2    . PHE A 1 145 ? 20.86500  5.42300   54.74500  1.000 88.66000  ? 136 PHE A CE2    1 
ATOM   953   C  CZ     . PHE A 1 145 ? 20.58200  6.63700   55.33200  1.000 84.51000  ? 136 PHE A CZ     1 
ATOM   954   N  N      . ALA A 1 146 ? 15.20700  1.70500   54.70200  1.000 95.68000  ? 137 ALA A N      1 
ATOM   955   C  CA     . ALA A 1 146 ? 13.88200  1.19100   54.37700  1.000 71.72000  ? 137 ALA A CA     1 
ATOM   956   C  C      . ALA A 1 146 ? 13.04800  1.00100   55.63700  1.000 84.93000  ? 137 ALA A C      1 
ATOM   957   O  O      . ALA A 1 146 ? 11.91700  1.50000   55.73300  1.000 101.20000 ? 137 ALA A O      1 
ATOM   958   C  CB     . ALA A 1 146 ? 14.00700  -0.12100  53.60400  1.000 64.50000  ? 137 ALA A CB     1 
ATOM   959   N  N      . LEU A 1 147 ? 13.59400  0.28200   56.62300  1.000 86.54000  ? 138 LEU A N      1 
ATOM   960   C  CA     . LEU A 1 147 ? 12.83400  0.02400   57.84000  1.000 92.18000  ? 138 LEU A CA     1 
ATOM   961   C  C      . LEU A 1 147 ? 12.55800  1.30800   58.61200  1.000 99.37000  ? 138 LEU A C      1 
ATOM   962   O  O      . LEU A 1 147 ? 11.50700  1.43200   59.24900  1.000 107.02000 ? 138 LEU A O      1 
ATOM   963   C  CB     . LEU A 1 147 ? 13.57600  -0.98000  58.72200  1.000 86.77000  ? 138 LEU A CB     1 
ATOM   964   N  N      . LEU A 1 148 ? 13.46300  2.28400   58.54000  1.000 88.53000  ? 139 LEU A N      1 
ATOM   965   C  CA     . LEU A 1 148 ? 13.24700  3.55800   59.21000  1.000 91.00000  ? 139 LEU A CA     1 
ATOM   966   C  C      . LEU A 1 148 ? 12.08100  4.30800   58.58800  1.000 92.00000  ? 139 LEU A C      1 
ATOM   967   O  O      . LEU A 1 148 ? 11.18000  4.77300   59.29600  1.000 100.37000 ? 139 LEU A O      1 
ATOM   968   C  CB     . LEU A 1 148 ? 14.52400  4.39300   59.14500  1.000 97.67000  ? 139 LEU A CB     1 
ATOM   969   C  CG     . LEU A 1 148 ? 14.53300  5.72600   59.88900  1.000 105.29000 ? 139 LEU A CG     1 
ATOM   970   C  CD1    . LEU A 1 148 ? 14.80100  5.51000   61.37200  1.000 120.49000 ? 139 LEU A CD1    1 
ATOM   971   C  CD2    . LEU A 1 148 ? 15.56900  6.65400   59.27800  1.000 87.65000  ? 139 LEU A CD2    1 
ATOM   972   N  N      . GLY A 1 149 ? 12.08700  4.44700   57.26200  1.000 90.45000  ? 140 GLY A N      1 
ATOM   973   C  CA     . GLY A 1 149 ? 10.95600  5.07200   56.59900  1.000 101.04000 ? 140 GLY A CA     1 
ATOM   974   C  C      . GLY A 1 149 ? 9.64700   4.37500   56.91600  1.000 96.67000  ? 140 GLY A C      1 
ATOM   975   O  O      . GLY A 1 149 ? 8.63900   5.02600   57.21400  1.000 88.83000  ? 140 GLY A O      1 
ATOM   976   N  N      . LEU A 1 150 ? 9.64800   3.03900   56.88000  1.000 107.47000 ? 141 LEU A N      1 
ATOM   977   C  CA     . LEU A 1 150 ? 8.40900   2.30700   57.12600  1.000 109.85000 ? 141 LEU A CA     1 
ATOM   978   C  C      . LEU A 1 150 ? 7.92200   2.49700   58.55900  1.000 103.59000 ? 141 LEU A C      1 
ATOM   979   O  O      . LEU A 1 150 ? 6.71900   2.66900   58.79300  1.000 114.19000 ? 141 LEU A O      1 
ATOM   980   C  CB     . LEU A 1 150 ? 8.60100   0.82300   56.80700  1.000 112.45000 ? 141 LEU A CB     1 
ATOM   981   C  CG     . LEU A 1 150 ? 8.66400   0.46600   55.31800  1.000 115.16000 ? 141 LEU A CG     1 
ATOM   982   C  CD1    . LEU A 1 150 ? 8.93700   -1.02100  55.10800  1.000 114.31000 ? 141 LEU A CD1    1 
ATOM   983   C  CD2    . LEU A 1 150 ? 7.38800   0.88800   54.60200  1.000 112.35000 ? 141 LEU A CD2    1 
ATOM   984   N  N      . VAL A 1 151 ? 8.83300   2.47700   59.53300  1.000 91.00000  ? 142 VAL A N      1 
ATOM   985   C  CA     . VAL A 1 151 ? 8.42200   2.65400   60.92000  1.000 98.55000  ? 142 VAL A CA     1 
ATOM   986   C  C      . VAL A 1 151 ? 7.91000   4.07100   61.14900  1.000 100.07000 ? 142 VAL A C      1 
ATOM   987   O  O      . VAL A 1 151 ? 6.92700   4.28300   61.87100  1.000 102.51000 ? 142 VAL A O      1 
ATOM   988   C  CB     . VAL A 1 151 ? 9.58200   2.30700   61.86900  1.000 104.68000 ? 142 VAL A CB     1 
ATOM   989   C  CG1    . VAL A 1 151 ? 9.24400   2.74800   63.27700  1.000 133.24000 ? 142 VAL A CG1    1 
ATOM   990   C  CG2    . VAL A 1 151 ? 9.87900   0.81400   61.82000  1.000 110.27000 ? 142 VAL A CG2    1 
ATOM   991   N  N      . LEU A 1 152 ? 8.56600   5.06400   60.54600  1.000 95.29000  ? 143 LEU A N      1 
ATOM   992   C  CA     . LEU A 1 152 ? 8.08000   6.43400   60.66300  1.000 88.37000  ? 143 LEU A CA     1 
ATOM   993   C  C      . LEU A 1 152 ? 6.68300   6.56900   60.07400  1.000 90.84000  ? 143 LEU A C      1 
ATOM   994   O  O      . LEU A 1 152 ? 5.82800   7.25900   60.63800  1.000 82.97000  ? 143 LEU A O      1 
ATOM   995   C  CB     . LEU A 1 152 ? 9.04500   7.39700   59.97500  1.000 82.31000  ? 143 LEU A CB     1 
ATOM   996   C  CG     . LEU A 1 152 ? 10.50900  7.28400   60.39700  1.000 90.53000  ? 143 LEU A CG     1 
ATOM   997   C  CD1    . LEU A 1 152 ? 11.39200  8.08700   59.46100  1.000 90.64000  ? 143 LEU A CD1    1 
ATOM   998   C  CD2    . LEU A 1 152 ? 10.69200  7.73300   61.83900  1.000 96.88000  ? 143 LEU A CD2    1 
ATOM   999   N  N      . VAL A 1 153 ? 6.43000   5.91400   58.94100  1.000 94.15000  ? 144 VAL A N      1 
ATOM   1000  C  CA     . VAL A 1 153 ? 5.09600   5.97100   58.35400  1.000 80.05000  ? 144 VAL A CA     1 
ATOM   1001  C  C      . VAL A 1 153 ? 4.08200   5.28800   59.26300  1.000 91.63000  ? 144 VAL A C      1 
ATOM   1002  O  O      . VAL A 1 153 ? 2.95300   5.76600   59.42700  1.000 106.47000 ? 144 VAL A O      1 
ATOM   1003  C  CB     . VAL A 1 153 ? 5.10000   5.35400   56.94500  1.000 106.23000 ? 144 VAL A CB     1 
ATOM   1004  C  CG1    . VAL A 1 153 ? 3.67700   5.04000   56.50100  1.000 104.91000 ? 144 VAL A CG1    1 
ATOM   1005  C  CG2    . VAL A 1 153 ? 5.78100   6.29200   55.96100  1.000 103.46000 ? 144 VAL A CG2    1 
ATOM   1006  N  N      . TYR A 1 154 ? 4.46400   4.16100   59.86900  1.000 95.61000  ? 145 TYR A N      1 
ATOM   1007  C  CA     . TYR A 1 154 ? 3.53900   3.43900   60.73700  1.000 113.66000 ? 145 TYR A CA     1 
ATOM   1008  C  C      . TYR A 1 154 ? 3.24400   4.21400   62.01500  1.000 106.90000 ? 145 TYR A C      1 
ATOM   1009  O  O      . TYR A 1 154 ? 2.17100   4.04800   62.60700  1.000 98.94000  ? 145 TYR A O      1 
ATOM   1010  C  CB     . TYR A 1 154 ? 4.11000   2.06000   61.07700  1.000 121.87000 ? 145 TYR A CB     1 
ATOM   1011  C  CG     . TYR A 1 154 ? 3.25100   1.23200   62.01100  1.000 140.16000 ? 145 TYR A CG     1 
ATOM   1012  C  CD1    . TYR A 1 154 ? 1.93700   0.91900   61.68700  1.000 149.09000 ? 145 TYR A CD1    1 
ATOM   1013  C  CD2    . TYR A 1 154 ? 3.75800   0.75700   63.21500  1.000 143.54000 ? 145 TYR A CD2    1 
ATOM   1014  C  CE1    . TYR A 1 154 ? 1.15100   0.15900   62.53500  1.000 139.23000 ? 145 TYR A CE1    1 
ATOM   1015  C  CE2    . TYR A 1 154 ? 2.98000   -0.00400  64.07000  1.000 156.37000 ? 145 TYR A CE2    1 
ATOM   1016  C  CZ     . TYR A 1 154 ? 1.67700   -0.29900  63.72400  1.000 152.97000 ? 145 TYR A CZ     1 
ATOM   1017  O  OH     . TYR A 1 154 ? 0.89800   -1.05500  64.57000  1.000 146.88000 ? 145 TYR A OH     1 
ATOM   1018  N  N      . LEU A 1 155 ? 4.17500   5.05900   62.45300  1.000 102.08000 ? 146 LEU A N      1 
ATOM   1019  C  CA     . LEU A 1 155 ? 3.99800   5.81200   63.70100  1.000 95.63000  ? 146 LEU A CA     1 
ATOM   1020  C  C      . LEU A 1 155 ? 3.35200   7.17200   63.45000  1.000 91.33000  ? 146 LEU A C      1 
ATOM   1021  O  O      . LEU A 1 155 ? 2.20900   7.41000   63.85100  1.000 94.26000  ? 146 LEU A O      1 
ATOM   1022  C  CB     . LEU A 1 155 ? 5.34800   5.96100   64.40600  1.000 96.87000  ? 146 LEU A CB     1 
ATOM   1023  C  CG     . LEU A 1 155 ? 6.06400   4.65200   64.74500  1.000 106.57000 ? 146 LEU A CG     1 
ATOM   1024  C  CD1    . LEU A 1 155 ? 7.27000   4.90700   65.63400  1.000 113.78000 ? 146 LEU A CD1    1 
ATOM   1025  C  CD2    . LEU A 1 155 ? 5.10400   3.67200   65.40400  1.000 117.02000 ? 146 LEU A CD2    1 
ATOM   1026  N  N      . ILE A 1 156 ? 4.07200   8.06400   62.76500  1.000 77.22000  ? 147 ILE A N      1 
ATOM   1027  C  CA     . ILE A 1 156 ? 3.61200   9.44200   62.59700  1.000 79.34000  ? 147 ILE A CA     1 
ATOM   1028  C  C      . ILE A 1 156 ? 2.24600   9.48300   61.92300  1.000 102.37000 ? 147 ILE A C      1 
ATOM   1029  O  O      . ILE A 1 156 ? 1.33900   10.20000  62.36100  1.000 119.50000 ? 147 ILE A O      1 
ATOM   1030  C  CB     . ILE A 1 156 ? 4.64900   10.26100  61.80600  1.000 69.32000  ? 147 ILE A CB     1 
ATOM   1031  C  CG1    . ILE A 1 156 ? 5.96000   10.37800  62.58900  1.000 89.42000  ? 147 ILE A CG1    1 
ATOM   1032  C  CG2    . ILE A 1 156 ? 4.09900   11.64100  61.48300  1.000 73.71000  ? 147 ILE A CG2    1 
ATOM   1033  C  CD1    . ILE A 1 156 ? 6.85400   9.16000   62.48600  1.000 92.34000  ? 147 ILE A CD1    1 
ATOM   1034  N  N      . PHE A 1 157 ? 2.07600   8.71500   60.85000  1.000 94.27000  ? 148 PHE A N      1 
ATOM   1035  C  CA     . PHE A 1 157 ? 0.80800   8.70800   60.13100  1.000 84.29000  ? 148 PHE A CA     1 
ATOM   1036  C  C      . PHE A 1 157 ? -0.13800  7.62800   60.63900  1.000 86.95000  ? 148 PHE A C      1 
ATOM   1037  O  O      . PHE A 1 157 ? -1.33900  7.87700   60.78800  1.000 97.97000  ? 148 PHE A O      1 
ATOM   1038  C  CB     . PHE A 1 157 ? 1.05300   8.52800   58.63000  1.000 89.84000  ? 148 PHE A CB     1 
ATOM   1039  C  CG     . PHE A 1 157 ? 1.71600   9.71000   57.97400  1.000 83.19000  ? 148 PHE A CG     1 
ATOM   1040  C  CD1    . PHE A 1 157 ? 1.08500   10.94300  57.93500  1.000 88.86000  ? 148 PHE A CD1    1 
ATOM   1041  C  CD2    . PHE A 1 157 ? 2.96300   9.58500   57.38600  1.000 92.38000  ? 148 PHE A CD2    1 
ATOM   1042  C  CE1    . PHE A 1 157 ? 1.69000   12.03000  57.32900  1.000 84.47000  ? 148 PHE A CE1    1 
ATOM   1043  C  CE2    . PHE A 1 157 ? 3.57300   10.66700  56.77700  1.000 84.02000  ? 148 PHE A CE2    1 
ATOM   1044  C  CZ     . PHE A 1 157 ? 2.93500   11.89100  56.74900  1.000 79.51000  ? 148 PHE A CZ     1 
ATOM   1045  N  N      . GLY A 1 158 ? 0.37900   6.43300   60.90700  1.000 85.07000  ? 149 GLY A N      1 
ATOM   1046  C  CA     . GLY A 1 158 ? -0.45500  5.32100   61.31100  1.000 101.80000 ? 149 GLY A CA     1 
ATOM   1047  C  C      . GLY A 1 158 ? -1.19400  5.54400   62.61200  1.000 110.17000 ? 149 GLY A C      1 
ATOM   1048  O  O      . GLY A 1 158 ? -2.42700  5.47900   62.65000  1.000 118.43000 ? 149 GLY A O      1 
ATOM   1049  N  N      . LYS A 1 159 ? -0.45500  5.81900   63.68600  1.000 102.91000 ? 150 LYS A N      1 
ATOM   1050  C  CA     . LYS A 1 159 ? -1.05000  5.90600   65.01400  1.000 116.48000 ? 150 LYS A CA     1 
ATOM   1051  C  C      . LYS A 1 159 ? -1.42800  7.33100   65.41500  1.000 122.91000 ? 150 LYS A C      1 
ATOM   1052  O  O      . LYS A 1 159 ? -2.53500  7.55600   65.91500  1.000 135.73000 ? 150 LYS A O      1 
ATOM   1053  C  CB     . LYS A 1 159 ? -0.09200  5.30800   66.04900  1.000 93.96000  ? 150 LYS A CB     1 
ATOM   1054  N  N      . TRP A 1 160 ? -0.53500  8.30100   65.20400  1.000 109.71000 ? 151 TRP A N      1 
ATOM   1055  C  CA     . TRP A 1 160 ? -0.79900  9.66300   65.66500  1.000 120.12000 ? 151 TRP A CA     1 
ATOM   1056  C  C      . TRP A 1 160 ? -2.11500  10.19500  65.10600  1.000 115.78000 ? 151 TRP A C      1 
ATOM   1057  O  O      . TRP A 1 160 ? -3.00900  10.59700  65.85900  1.000 131.20000 ? 151 TRP A O      1 
ATOM   1058  C  CB     . TRP A 1 160 ? 0.36200   10.59100  65.29400  1.000 116.33000 ? 151 TRP A CB     1 
ATOM   1059  C  CG     . TRP A 1 160 ? 0.23800   11.96800  65.90600  1.000 129.27000 ? 151 TRP A CG     1 
ATOM   1060  C  CD1    . TRP A 1 160 ? -0.45700  12.30300  67.03500  1.000 138.33000 ? 151 TRP A CD1    1 
ATOM   1061  C  CD2    . TRP A 1 160 ? 0.82600   13.18600  65.42400  1.000 131.33000 ? 151 TRP A CD2    1 
ATOM   1062  N  NE1    . TRP A 1 160 ? -0.33900  13.65000  67.28300  1.000 132.31000 ? 151 TRP A NE1    1 
ATOM   1063  C  CE2    . TRP A 1 160 ? 0.44300   14.21500  66.31000  1.000 127.43000 ? 151 TRP A CE2    1 
ATOM   1064  C  CE3    . TRP A 1 160 ? 1.63800   13.50600  64.33200  1.000 124.97000 ? 151 TRP A CE3    1 
ATOM   1065  C  CZ2    . TRP A 1 160 ? 0.84300   15.53800  66.13600  1.000 120.93000 ? 151 TRP A CZ2    1 
ATOM   1066  C  CZ3    . TRP A 1 160 ? 2.03400   14.82200  64.16100  1.000 110.35000 ? 151 TRP A CZ3    1 
ATOM   1067  C  CH2    . TRP A 1 160 ? 1.63600   15.82100  65.05900  1.000 111.81000 ? 151 TRP A CH2    1 
ATOM   1068  N  N      . MET A 1 161 ? -2.25100  10.21100  63.78000  1.000 102.25000 ? 152 MET A N      1 
ATOM   1069  C  CA     . MET A 1 161 ? -3.45500  10.74400  63.15400  1.000 101.05000 ? 152 MET A CA     1 
ATOM   1070  C  C      . MET A 1 161 ? -4.60500  9.74700   63.14000  1.000 105.86000 ? 152 MET A C      1 
ATOM   1071  O  O      . MET A 1 161 ? -5.71400  10.10600  62.72800  1.000 92.54000  ? 152 MET A O      1 
ATOM   1072  C  CB     . MET A 1 161 ? -3.14500  11.20000  61.73000  1.000 91.45000  ? 152 MET A CB     1 
ATOM   1073  C  CG     . MET A 1 161 ? -2.05000  12.24500  61.66100  1.000 80.12000  ? 152 MET A CG     1 
ATOM   1074  S  SD     . MET A 1 161 ? -1.48800  12.52400  59.97600  1.000 83.79000  ? 152 MET A SD     1 
ATOM   1075  C  CE     . MET A 1 161 ? 0.03700   13.41800  60.27100  1.000 85.77000  ? 152 MET A CE     1 
ATOM   1076  N  N      . GLY A 1 162 ? -4.36300  8.50800   63.55900  1.000 99.51000  ? 153 GLY A N      1 
ATOM   1077  C  CA     . GLY A 1 162 ? -5.40800  7.50800   63.60000  1.000 112.08000 ? 153 GLY A CA     1 
ATOM   1078  C  C      . GLY A 1 162 ? -5.77900  6.92400   62.25900  1.000 112.89000 ? 153 GLY A C      1 
ATOM   1079  O  O      . GLY A 1 162 ? -6.94200  6.56400   62.04900  1.000 100.13000 ? 153 GLY A O      1 
ATOM   1080  N  N      . GLN A 1 163 ? -4.82200  6.82000   61.33500  1.000 109.09000 ? 154 GLN A N      1 
ATOM   1081  C  CA     . GLN A 1 163 ? -5.11100  6.17300   60.06200  1.000 103.96000 ? 154 GLN A CA     1 
ATOM   1082  C  C      . GLN A 1 163 ? -5.21600  4.66500   60.22600  1.000 114.88000 ? 154 GLN A C      1 
ATOM   1083  O  O      . GLN A 1 163 ? -5.92200  4.00300   59.45400  1.000 115.98000 ? 154 GLN A O      1 
ATOM   1084  C  CB     . GLN A 1 163 ? -4.04900  6.53900   59.03100  1.000 88.61000  ? 154 GLN A CB     1 
ATOM   1085  C  CG     . GLN A 1 163 ? -4.11500  7.99500   58.61100  1.000 88.23000  ? 154 GLN A CG     1 
ATOM   1086  C  CD     . GLN A 1 163 ? -3.05700  8.35400   57.59500  1.000 88.53000  ? 154 GLN A CD     1 
ATOM   1087  O  OE1    . GLN A 1 163 ? -3.22600  8.12500   56.39800  1.000 108.32000 ? 154 GLN A OE1    1 
ATOM   1088  N  NE2    . GLN A 1 163 ? -1.95400  8.92000   58.06700  1.000 86.90000  ? 154 GLN A NE2    1 
ATOM   1089  N  N      . VAL A 1 164 ? -4.51300  4.10300   61.21400  1.000 110.27000 ? 155 VAL A N      1 
ATOM   1090  C  CA     . VAL A 1 164 ? -4.73800  2.71600   61.60400  1.000 117.97000 ? 155 VAL A CA     1 
ATOM   1091  C  C      . VAL A 1 164 ? -5.84600  2.60400   62.64100  1.000 116.47000 ? 155 VAL A C      1 
ATOM   1092  O  O      . VAL A 1 164 ? -6.35000  1.49600   62.88200  1.000 115.70000 ? 155 VAL A O      1 
ATOM   1093  C  CB     . VAL A 1 164 ? -3.44400  2.07500   62.14300  1.000 121.64000 ? 155 VAL A CB     1 
ATOM   1094  C  CG1    . VAL A 1 164 ? -3.03500  2.72900   63.45400  1.000 126.80000 ? 155 VAL A CG1    1 
ATOM   1095  C  CG2    . VAL A 1 164 ? -3.62500  0.57400   62.31800  1.000 125.67000 ? 155 VAL A CG2    1 
ATOM   1096  N  N      . ASP A 1 165 ? -6.24200  3.71800   63.26200  1.000 109.65000 ? 156 ASP A N      1 
ATOM   1097  C  CA     . ASP A 1 165 ? -7.36000  3.71400   64.19800  1.000 106.87000 ? 156 ASP A CA     1 
ATOM   1098  C  C      . ASP A 1 165 ? -8.69300  3.64000   63.46300  1.000 117.34000 ? 156 ASP A C      1 
ATOM   1099  O  O      . ASP A 1 165 ? -9.59500  2.90200   63.87600  1.000 115.53000 ? 156 ASP A O      1 
ATOM   1100  C  CB     . ASP A 1 165 ? -7.30400  4.96300   65.08100  1.000 120.63000 ? 156 ASP A CB     1 
ATOM   1101  C  CG     . ASP A 1 165 ? -8.39800  4.99000   66.13800  1.000 151.47000 ? 156 ASP A CG     1 
ATOM   1102  O  OD1    . ASP A 1 165 ? -9.16700  4.00900   66.23600  1.000 147.31000 ? 156 ASP A OD1    1 
ATOM   1103  O  OD2    . ASP A 1 165 ? -8.49100  5.99900   66.87100  1.000 152.69000 ? 156 ASP A OD2    1 
ATOM   1104  N  N      . ASN A 1 166 ? -8.83100  4.39800   62.37400  1.000 117.36000 ? 157 ASN A N      1 
ATOM   1105  C  CA     . ASN A 1 166 ? -10.08300 4.43100   61.62400  1.000 110.99000 ? 157 ASN A CA     1 
ATOM   1106  C  C      . ASN A 1 166 ? -10.19800 3.23200   60.68600  1.000 118.00000 ? 157 ASN A C      1 
ATOM   1107  O  O      . ASN A 1 166 ? -11.13200 2.42800   60.79800  1.000 114.15000 ? 157 ASN A O      1 
ATOM   1108  C  CB     . ASN A 1 166 ? -10.18700 5.74700   60.84600  1.000 79.40000  ? 157 ASN A CB     1 
ATOM   1109  C  CG     . ASN A 1 166 ? -11.59300 6.02000   60.34400  1.000 95.89000  ? 157 ASN A CG     1 
ATOM   1110  O  OD1    . ASN A 1 166 ? -12.53200 6.15300   61.13000  1.000 101.59000 ? 157 ASN A OD1    1 
ATOM   1111  N  ND2    . ASN A 1 166 ? -11.74300 6.11100   59.02800  1.000 104.79000 ? 157 ASN A ND2    1 
ATOM   1112  N  N      . LEU A 1 167 ? -9.24500  3.08700   59.76500  1.000 112.78000 ? 158 LEU A N      1 
ATOM   1113  C  CA     . LEU A 1 167 ? -9.22200  1.99200   58.79700  1.000 103.27000 ? 158 LEU A CA     1 
ATOM   1114  C  C      . LEU A 1 167 ? -10.48300 1.94100   57.94100  1.000 104.20000 ? 158 LEU A C      1 
ATOM   1115  O  O      . LEU A 1 167 ? -10.82500 0.88600   57.39500  1.000 90.32000  ? 158 LEU A O      1 
ATOM   1116  C  CB     . LEU A 1 167 ? -9.00700  0.64200   59.48900  1.000 105.31000 ? 158 LEU A CB     1 
ATOM   1117  C  CG     . LEU A 1 167 ? -7.56000  0.27600   59.82400  1.000 106.52000 ? 158 LEU A CG     1 
ATOM   1118  C  CD1    . LEU A 1 167 ? -7.50300  -0.99800  60.65400  1.000 100.65000 ? 158 LEU A CD1    1 
ATOM   1119  C  CD2    . LEU A 1 167 ? -6.73600  0.13100   58.55300  1.000 101.01000 ? 158 LEU A CD2    1 
ATOM   1120  N  N      . ASN A 1 168 ? -11.17400 3.06600   57.79400  1.000 102.38000 ? 159 ASN A N      1 
ATOM   1121  C  CA     . ASN A 1 168 ? -12.36700 3.15000   56.96900  1.000 68.38000  ? 159 ASN A CA     1 
ATOM   1122  C  C      . ASN A 1 168 ? -12.09800 4.01500   55.74400  1.000 76.17000  ? 159 ASN A C      1 
ATOM   1123  O  O      . ASN A 1 168 ? -11.11200 4.75400   55.67400  1.000 78.20000  ? 159 ASN A O      1 
ATOM   1124  C  CB     . ASN A 1 168 ? -13.54700 3.71800   57.76400  1.000 69.01000  ? 159 ASN A CB     1 
ATOM   1125  N  N      . ILE A 1 169 ? -12.99500 3.90000   54.76800  1.000 85.42000  ? 160 ILE A N      1 
ATOM   1126  C  CA     . ILE A 1 169 ? -12.83600 4.56100   53.47500  1.000 82.54000  ? 160 ILE A CA     1 
ATOM   1127  C  C      . ILE A 1 169 ? -12.97500 6.07000   53.65900  1.000 76.12000  ? 160 ILE A C      1 
ATOM   1128  O  O      . ILE A 1 169 ? -14.05700 6.56800   53.98000  1.000 83.21000  ? 160 ILE A O      1 
ATOM   1129  C  CB     . ILE A 1 169 ? -13.84600 4.03200   52.45400  1.000 80.10000  ? 160 ILE A CB     1 
ATOM   1130  C  CG1    . ILE A 1 169 ? -13.65300 2.52700   52.26600  1.000 89.80000  ? 160 ILE A CG1    1 
ATOM   1131  C  CG2    . ILE A 1 169 ? -13.70100 4.77200   51.13300  1.000 79.73000  ? 160 ILE A CG2    1 
ATOM   1132  C  CD1    . ILE A 1 169 ? -14.51600 1.68700   53.18900  1.000 96.06000  ? 160 ILE A CD1    1 
ATOM   1133  N  N      . TYR A 1 170 ? -11.88300 6.80000   53.44300  1.000 72.52000  ? 161 TYR A N      1 
ATOM   1134  C  CA     . TYR A 1 170 ? -11.91000 8.25200   53.38300  1.000 90.62000  ? 161 TYR A CA     1 
ATOM   1135  C  C      . TYR A 1 170 ? -12.07300 8.70400   51.93700  1.000 112.09000 ? 161 TYR A C      1 
ATOM   1136  O  O      . TYR A 1 170 ? -11.50200 8.10500   51.01600  1.000 114.40000 ? 161 TYR A O      1 
ATOM   1137  C  CB     . TYR A 1 170 ? -10.62900 8.84500   53.97300  1.000 97.88000  ? 161 TYR A CB     1 
ATOM   1138  C  CG     . TYR A 1 170 ? -10.37800 10.28400  53.57100  1.000 107.61000 ? 161 TYR A CG     1 
ATOM   1139  C  CD1    . TYR A 1 170 ? -11.14000 11.31900  54.09700  1.000 112.23000 ? 161 TYR A CD1    1 
ATOM   1140  C  CD2    . TYR A 1 170 ? -9.38400  10.60400  52.65400  1.000 110.42000 ? 161 TYR A CD2    1 
ATOM   1141  C  CE1    . TYR A 1 170 ? -10.91400 12.63400  53.72700  1.000 111.06000 ? 161 TYR A CE1    1 
ATOM   1142  C  CE2    . TYR A 1 170 ? -9.15200  11.91400  52.27800  1.000 112.31000 ? 161 TYR A CE2    1 
ATOM   1143  C  CZ     . TYR A 1 170 ? -9.91900  12.92600  52.81800  1.000 112.36000 ? 161 TYR A CZ     1 
ATOM   1144  O  OH     . TYR A 1 170 ? -9.69000  14.23100  52.44500  1.000 96.26000  ? 161 TYR A OH     1 
ATOM   1145  N  N      . THR A 1 171 ? -12.86200 9.76000   51.74400  1.000 119.55000 ? 162 THR A N      1 
ATOM   1146  C  CA     . THR A 1 171 ? -13.13500 10.31800  50.42500  1.000 112.77000 ? 162 THR A CA     1 
ATOM   1147  C  C      . THR A 1 171 ? -12.36200 11.62300  50.29300  1.000 110.44000 ? 162 THR A C      1 
ATOM   1148  O  O      . THR A 1 171 ? -12.54700 12.54400  51.09600  1.000 115.37000 ? 162 THR A O      1 
ATOM   1149  C  CB     . THR A 1 171 ? -14.63000 10.55900  50.22400  1.000 112.01000 ? 162 THR A CB     1 
ATOM   1150  O  OG1    . THR A 1 171 ? -15.34300 9.32800   50.39900  1.000 116.74000 ? 162 THR A OG1    1 
ATOM   1151  C  CG2    . THR A 1 171 ? -14.89500 11.10000  48.82600  1.000 103.35000 ? 162 THR A CG2    1 
ATOM   1152  N  N      . ASN A 1 172 ? -11.51200 11.70200  49.27400  1.000 106.81000 ? 163 ASN A N      1 
ATOM   1153  C  CA     . ASN A 1 172 ? -10.69500 12.88300  49.06500  1.000 100.52000 ? 163 ASN A CA     1 
ATOM   1154  C  C      . ASN A 1 172 ? -11.57000 14.08100  48.69400  1.000 99.83000  ? 163 ASN A C      1 
ATOM   1155  O  O      . ASN A 1 172 ? -12.76400 13.95600  48.41000  1.000 93.03000  ? 163 ASN A O      1 
ATOM   1156  C  CB     . ASN A 1 172 ? -9.65000  12.61800  47.98300  1.000 93.11000  ? 163 ASN A CB     1 
ATOM   1157  C  CG     . ASN A 1 172 ? -8.68200  13.76600  47.82300  1.000 104.48000 ? 163 ASN A CG     1 
ATOM   1158  O  OD1    . ASN A 1 172 ? -8.96800  14.89400  48.22800  1.000 109.16000 ? 163 ASN A OD1    1 
ATOM   1159  N  ND2    . ASN A 1 172 ? -7.52100  13.48500  47.24300  1.000 109.20000 ? 163 ASN A ND2    1 
ATOM   1160  N  N      . TRP A 1 173 ? -10.95100 15.26500  48.70100  1.000 99.50000  ? 164 TRP A N      1 
ATOM   1161  C  CA     . TRP A 1 173 ? -11.69100 16.48100  48.38200  1.000 108.53000 ? 164 TRP A CA     1 
ATOM   1162  C  C      . TRP A 1 173 ? -12.21300 16.46300  46.95100  1.000 122.02000 ? 164 TRP A C      1 
ATOM   1163  O  O      . TRP A 1 173 ? -13.31700 16.94900  46.67900  1.000 131.73000 ? 164 TRP A O      1 
ATOM   1164  C  CB     . TRP A 1 173 ? -10.80400 17.70500  48.61500  1.000 98.29000  ? 164 TRP A CB     1 
ATOM   1165  C  CG     . TRP A 1 173 ? -9.74800  17.89300  47.56400  1.000 101.78000 ? 164 TRP A CG     1 
ATOM   1166  C  CD1    . TRP A 1 173 ? -8.50100  17.34000  47.54900  1.000 106.48000 ? 164 TRP A CD1    1 
ATOM   1167  C  CD2    . TRP A 1 173 ? -9.84800  18.68700  46.37400  1.000 103.71000 ? 164 TRP A CD2    1 
ATOM   1168  N  NE1    . TRP A 1 173 ? -7.81800  17.73900  46.42600  1.000 101.31000 ? 164 TRP A NE1    1 
ATOM   1169  C  CE2    . TRP A 1 173 ? -8.62300  18.56600  45.68800  1.000 110.57000 ? 164 TRP A CE2    1 
ATOM   1170  C  CE3    . TRP A 1 173 ? -10.85300 19.48800  45.82200  1.000 112.85000 ? 164 TRP A CE3    1 
ATOM   1171  C  CZ2    . TRP A 1 173 ? -8.37500  19.21600  44.48000  1.000 119.93000 ? 164 TRP A CZ2    1 
ATOM   1172  C  CZ3    . TRP A 1 173 ? -10.60500 20.13200  44.62200  1.000 121.11000 ? 164 TRP A CZ3    1 
ATOM   1173  C  CH2    . TRP A 1 173 ? -9.37600  19.99200  43.96400  1.000 118.20000 ? 164 TRP A CH2    1 
ATOM   1174  N  N      . LEU A 1 174 ? -11.43400 15.90400  46.02000  1.000 113.21000 ? 165 LEU A N      1 
ATOM   1175  C  CA     . LEU A 1 174 ? -11.90700 15.76900  44.64800  1.000 101.82000 ? 165 LEU A CA     1 
ATOM   1176  C  C      . LEU A 1 174 ? -12.97700 14.69500  44.51800  1.000 105.26000 ? 165 LEU A C      1 
ATOM   1177  O  O      . LEU A 1 174 ? -13.74500 14.71400  43.54900  1.000 112.74000 ? 165 LEU A O      1 
ATOM   1178  C  CB     . LEU A 1 174 ? -10.73400 15.45900  43.71600  1.000 89.98000  ? 165 LEU A CB     1 
ATOM   1179  C  CG     . LEU A 1 174 ? -11.00100 15.60300  42.21600  1.000 107.36000 ? 165 LEU A CG     1 
ATOM   1180  C  CD1    . LEU A 1 174 ? -11.06700 17.07000  41.82100  1.000 87.13000  ? 165 LEU A CD1    1 
ATOM   1181  C  CD2    . LEU A 1 174 ? -9.94700  14.86700  41.39900  1.000 127.38000 ? 165 LEU A CD2    1 
ATOM   1182  N  N      . GLY A 1 175 ? -13.04500 13.76900  45.46400  1.000 98.86000  ? 166 GLY A N      1 
ATOM   1183  C  CA     . GLY A 1 175 ? -14.03900 12.72400  45.47000  1.000 112.25000 ? 166 GLY A CA     1 
ATOM   1184  C  C      . GLY A 1 175 ? -13.53300 11.30500  45.25700  1.000 132.20000 ? 166 GLY A C      1 
ATOM   1185  O  O      . GLY A 1 175 ? -14.34000 10.42900  44.92000  1.000 139.13000 ? 166 GLY A O      1 
ATOM   1186  N  N      . ILE A 1 176 ? -12.24200 11.05300  45.44100  1.000 127.22000 ? 167 ILE A N      1 
ATOM   1187  C  CA     . ILE A 1 176 ? -11.68100 9.71700   45.28000  1.000 100.67000 ? 167 ILE A CA     1 
ATOM   1188  C  C      . ILE A 1 176 ? -11.68900 9.02000   46.63300  1.000 107.20000 ? 167 ILE A C      1 
ATOM   1189  O  O      . ILE A 1 176 ? -11.33100 9.61400   47.65700  1.000 120.00000 ? 167 ILE A O      1 
ATOM   1190  C  CB     . ILE A 1 176 ? -10.26600 9.77900   44.67400  1.000 83.58000  ? 167 ILE A CB     1 
ATOM   1191  C  CG1    . ILE A 1 176 ? -9.28700  10.44600  45.63800  1.000 112.01000 ? 167 ILE A CG1    1 
ATOM   1192  C  CG2    . ILE A 1 176 ? -10.29100 10.53100  43.35200  1.000 77.25000  ? 167 ILE A CG2    1 
ATOM   1193  C  CD1    . ILE A 1 176 ? -7.85700  10.44100  45.14200  1.000 111.82000 ? 167 ILE A CD1    1 
ATOM   1194  N  N      . ASN A 1 177 ? -12.10900 7.75800   46.64200  1.000 105.78000 ? 168 ASN A N      1 
ATOM   1195  C  CA     . ASN A 1 177 ? -12.24700 6.97900   47.86500  1.000 103.95000 ? 168 ASN A CA     1 
ATOM   1196  C  C      . ASN A 1 177 ? -11.06600 6.03200   48.04000  1.000 99.85000  ? 168 ASN A C      1 
ATOM   1197  O  O      . ASN A 1 177 ? -10.57500 5.44700   47.06800  1.000 96.37000  ? 168 ASN A O      1 
ATOM   1198  C  CB     . ASN A 1 177 ? -13.55000 6.17700   47.85000  1.000 110.94000 ? 168 ASN A CB     1 
ATOM   1199  C  CG     . ASN A 1 177 ? -14.76300 7.04100   47.57000  1.000 122.21000 ? 168 ASN A CG     1 
ATOM   1200  O  OD1    . ASN A 1 177 ? -14.95000 8.08800   48.18900  1.000 130.07000 ? 168 ASN A OD1    1 
ATOM   1201  N  ND2    . ASN A 1 177 ? -15.60000 6.60300   46.63500  1.000 114.18000 ? 168 ASN A ND2    1 
ATOM   1202  N  N      . PHE A 1 178 ? -10.61300 5.88300   49.28400  1.000 97.78000  ? 169 PHE A N      1 
ATOM   1203  C  CA     . PHE A 1 178 ? -9.53800  4.93900   49.57500  1.000 88.36000  ? 169 PHE A CA     1 
ATOM   1204  C  C      . PHE A 1 178 ? -9.35000  4.84300   51.08200  1.000 82.94000  ? 169 PHE A C      1 
ATOM   1205  O  O      . PHE A 1 178 ? -9.74600  5.73900   51.83100  1.000 99.15000  ? 169 PHE A O      1 
ATOM   1206  C  CB     . PHE A 1 178 ? -8.22400  5.35500   48.90500  1.000 84.92000  ? 169 PHE A CB     1 
ATOM   1207  C  CG     . PHE A 1 178 ? -7.90600  6.81500   49.05100  1.000 77.96000  ? 169 PHE A CG     1 
ATOM   1208  C  CD1    . PHE A 1 178 ? -7.39200  7.30800   50.23900  1.000 70.72000  ? 169 PHE A CD1    1 
ATOM   1209  C  CD2    . PHE A 1 178 ? -8.11300  7.69200   48.00200  1.000 96.08000  ? 169 PHE A CD2    1 
ATOM   1210  C  CE1    . PHE A 1 178 ? -7.09800  8.65000   50.38000  1.000 88.37000  ? 169 PHE A CE1    1 
ATOM   1211  C  CE2    . PHE A 1 178 ? -7.81900  9.03600   48.13600  1.000 109.60000 ? 169 PHE A CE2    1 
ATOM   1212  C  CZ     . PHE A 1 178 ? -7.31200  9.51600   49.32600  1.000 103.32000 ? 169 PHE A CZ     1 
ATOM   1213  N  N      . VAL A 1 179 ? -8.76300  3.73700   51.51700  1.000 61.38000  ? 170 VAL A N      1 
ATOM   1214  C  CA     . VAL A 1 179 ? -8.31800  3.61600   52.90700  1.000 58.67000  ? 170 VAL A CA     1 
ATOM   1215  C  C      . VAL A 1 179 ? -7.03000  4.42100   53.07300  1.000 75.66000  ? 170 VAL A C      1 
ATOM   1216  O  O      . VAL A 1 179 ? -6.08200  4.21900   52.29900  1.000 87.61000  ? 170 VAL A O      1 
ATOM   1217  C  CB     . VAL A 1 179 ? -8.10900  2.15400   53.28600  1.000 73.41000  ? 170 VAL A CB     1 
ATOM   1218  C  CG1    . VAL A 1 179 ? -7.34700  2.04900   54.60200  1.000 88.76000  ? 170 VAL A CG1    1 
ATOM   1219  C  CG2    . VAL A 1 179 ? -9.44900  1.43400   53.38400  1.000 68.61000  ? 170 VAL A CG2    1 
ATOM   1220  N  N      . PRO A 1 180 ? -6.95700  5.33000   54.04800  1.000 93.57000  ? 171 PRO A N      1 
ATOM   1221  C  CA     . PRO A 1 180 ? -5.83500  6.29200   54.06500  1.000 106.63000 ? 171 PRO A CA     1 
ATOM   1222  C  C      . PRO A 1 180 ? -4.46000  5.65400   54.21500  1.000 105.65000 ? 171 PRO A C      1 
ATOM   1223  O  O      . PRO A 1 180 ? -3.52600  6.00700   53.47500  1.000 99.16000  ? 171 PRO A O      1 
ATOM   1224  C  CB     . PRO A 1 180 ? -6.18200  7.19800   55.25700  1.000 109.51000 ? 171 PRO A CB     1 
ATOM   1225  C  CG     . PRO A 1 180 ? -7.07500  6.36200   56.12700  1.000 94.55000  ? 171 PRO A CG     1 
ATOM   1226  C  CD     . PRO A 1 180 ? -7.88000  5.52600   55.17900  1.000 93.63000  ? 171 PRO A CD     1 
ATOM   1227  N  N      . PHE A 1 181 ? -4.30300  4.72200   55.15900  1.000 109.40000 ? 172 PHE A N      1 
ATOM   1228  C  CA     . PHE A 1 181 ? -2.98000  4.16800   55.42900  1.000 107.48000 ? 172 PHE A CA     1 
ATOM   1229  C  C      . PHE A 1 181 ? -2.44700  3.40000   54.22600  1.000 97.60000  ? 172 PHE A C      1 
ATOM   1230  O  O      . PHE A 1 181 ? -1.24000  3.42800   53.94200  1.000 101.00000 ? 172 PHE A O      1 
ATOM   1231  C  CB     . PHE A 1 181 ? -3.03200  3.26600   56.66300  1.000 115.76000 ? 172 PHE A CB     1 
ATOM   1232  C  CG     . PHE A 1 181 ? -1.68100  2.93200   57.22700  1.000 108.86000 ? 172 PHE A CG     1 
ATOM   1233  C  CD1    . PHE A 1 181 ? -0.79800  3.93700   57.57900  1.000 118.27000 ? 172 PHE A CD1    1 
ATOM   1234  C  CD2    . PHE A 1 181 ? -1.29600  1.61400   57.41000  1.000 108.01000 ? 172 PHE A CD2    1 
ATOM   1235  C  CE1    . PHE A 1 181 ? 0.44700   3.63700   58.09700  1.000 102.29000 ? 172 PHE A CE1    1 
ATOM   1236  C  CE2    . PHE A 1 181 ? -0.05200  1.30800   57.92900  1.000 111.47000 ? 172 PHE A CE2    1 
ATOM   1237  C  CZ     . PHE A 1 181 ? 0.82000   2.32100   58.27400  1.000 104.68000 ? 172 PHE A CZ     1 
ATOM   1238  N  N      . ALA A 1 182 ? -3.33200  2.71100   53.50400  1.000 92.52000  ? 173 ALA A N      1 
ATOM   1239  C  CA     . ALA A 1 182 ? -2.91200  2.04800   52.27700  1.000 90.18000  ? 173 ALA A CA     1 
ATOM   1240  C  C      . ALA A 1 182 ? -2.37200  3.05800   51.27400  1.000 88.21000  ? 173 ALA A C      1 
ATOM   1241  O  O      . ALA A 1 182 ? -1.33000  2.82800   50.64800  1.000 104.68000 ? 173 ALA A O      1 
ATOM   1242  C  CB     . ALA A 1 182 ? -4.07800  1.26000   51.68000  1.000 81.80000  ? 173 ALA A CB     1 
ATOM   1243  N  N      . MET A 1 183 ? -3.05500  4.19500   51.12400  1.000 62.98000  ? 174 MET A N      1 
ATOM   1244  C  CA     . MET A 1 183 ? -2.58100  5.22500   50.20600  1.000 65.72000  ? 174 MET A CA     1 
ATOM   1245  C  C      . MET A 1 183 ? -1.21500  5.75400   50.63100  1.000 94.91000  ? 174 MET A C      1 
ATOM   1246  O  O      . MET A 1 183 ? -0.34400  6.00500   49.78700  1.000 109.88000 ? 174 MET A O      1 
ATOM   1247  C  CB     . MET A 1 183 ? -3.59700  6.36300   50.12900  1.000 74.62000  ? 174 MET A CB     1 
ATOM   1248  C  CG     . MET A 1 183 ? -3.40800  7.28700   48.93600  1.000 99.17000  ? 174 MET A CG     1 
ATOM   1249  S  SD     . MET A 1 183 ? -3.31500  6.40300   47.36600  1.000 84.66000  ? 174 MET A SD     1 
ATOM   1250  C  CE     . MET A 1 183 ? -4.98500  5.76900   47.22500  1.000 92.10000  ? 174 MET A CE     1 
ATOM   1251  N  N      . THR A 1 184 ? -1.00400  5.92000   51.93700  1.000 99.40000  ? 175 THR A N      1 
ATOM   1252  C  CA     . THR A 1 184 ? 0.27700   6.44000   52.41400  1.000 100.45000 ? 175 THR A CA     1 
ATOM   1253  C  C      . THR A 1 184 ? 1.41500   5.46100   52.13000  1.000 93.49000  ? 175 THR A C      1 
ATOM   1254  O  O      . THR A 1 184 ? 2.47700   5.84800   51.61400  1.000 83.33000  ? 175 THR A O      1 
ATOM   1255  C  CB     . THR A 1 184 ? 0.18700   6.74500   53.91000  1.000 101.94000 ? 175 THR A CB     1 
ATOM   1256  O  OG1    . THR A 1 184 ? -1.00300  7.50000   54.17200  1.000 105.53000 ? 175 THR A OG1    1 
ATOM   1257  C  CG2    . THR A 1 184 ? 1.39500   7.55100   54.36200  1.000 105.55000 ? 175 THR A CG2    1 
ATOM   1258  N  N      . VAL A 1 185 ? 1.21400   4.18400   52.46600  1.000 89.53000  ? 176 VAL A N      1 
ATOM   1259  C  CA     . VAL A 1 185 ? 2.24900   3.19200   52.18700  1.000 72.97000  ? 176 VAL A CA     1 
ATOM   1260  C  C      . VAL A 1 185 ? 2.49700   3.09100   50.68800  1.000 81.84000  ? 176 VAL A C      1 
ATOM   1261  O  O      . VAL A 1 185 ? 3.63600   2.86800   50.24900  1.000 88.02000  ? 176 VAL A O      1 
ATOM   1262  C  CB     . VAL A 1 185 ? 1.86800   1.82700   52.79200  1.000 70.86000  ? 176 VAL A CB     1 
ATOM   1263  C  CG1    . VAL A 1 185 ? 1.89700   1.89300   54.31500  1.000 81.18000  ? 176 VAL A CG1    1 
ATOM   1264  C  CG2    . VAL A 1 185 ? 0.50500   1.38300   52.29700  1.000 85.46000  ? 176 VAL A CG2    1 
ATOM   1265  N  N      . SER A 1 186 ? 1.45000   3.27500   49.87700  1.000 82.88000  ? 177 SER A N      1 
ATOM   1266  C  CA     . SER A 1 186 ? 1.63200   3.25300   48.43000  1.000 90.45000  ? 177 SER A CA     1 
ATOM   1267  C  C      . SER A 1 186 ? 2.49000   4.42300   47.96600  1.000 76.80000  ? 177 SER A C      1 
ATOM   1268  O  O      . SER A 1 186 ? 3.32800   4.26700   47.07200  1.000 87.54000  ? 177 SER A O      1 
ATOM   1269  C  CB     . SER A 1 186 ? 0.27300   3.26500   47.72900  1.000 86.62000  ? 177 SER A CB     1 
ATOM   1270  O  OG     . SER A 1 186 ? -0.48800  2.12100   48.08100  1.000 87.34000  ? 177 SER A OG     1 
ATOM   1271  N  N      . GLY A 1 187 ? 2.29400   5.60400   48.55300  1.000 60.28000  ? 178 GLY A N      1 
ATOM   1272  C  CA     . GLY A 1 187 ? 3.16100   6.72500   48.21800  1.000 68.43000  ? 178 GLY A CA     1 
ATOM   1273  C  C      . GLY A 1 187 ? 4.61000   6.45500   48.57900  1.000 87.25000  ? 178 GLY A C      1 
ATOM   1274  O  O      . GLY A 1 187 ? 5.52900   6.78400   47.81900  1.000 99.09000  ? 178 GLY A O      1 
ATOM   1275  N  N      . TYR A 1 188 ? 4.83300   5.85100   49.74800  1.000 83.85000  ? 179 TYR A N      1 
ATOM   1276  C  CA     . TYR A 1 188 ? 6.19300   5.47500   50.13100  1.000 75.70000  ? 179 TYR A CA     1 
ATOM   1277  C  C      . TYR A 1 188 ? 6.81000   4.54700   49.08700  1.000 70.27000  ? 179 TYR A C      1 
ATOM   1278  O  O      . TYR A 1 188 ? 7.94300   4.76200   48.62100  1.000 70.08000  ? 179 TYR A O      1 
ATOM   1279  C  CB     . TYR A 1 188 ? 6.17000   4.81400   51.51300  1.000 91.64000  ? 179 TYR A CB     1 
ATOM   1280  C  CG     . TYR A 1 188 ? 7.53000   4.55700   52.12800  1.000 96.84000  ? 179 TYR A CG     1 
ATOM   1281  C  CD1    . TYR A 1 188 ? 8.18300   5.54500   52.85400  1.000 112.57000 ? 179 TYR A CD1    1 
ATOM   1282  C  CD2    . TYR A 1 188 ? 8.14400   3.31700   52.01200  1.000 101.15000 ? 179 TYR A CD2    1 
ATOM   1283  C  CE1    . TYR A 1 188 ? 9.42000   5.31600   53.42600  1.000 111.56000 ? 179 TYR A CE1    1 
ATOM   1284  C  CE2    . TYR A 1 188 ? 9.38200   3.07700   52.58200  1.000 124.57000 ? 179 TYR A CE2    1 
ATOM   1285  C  CZ     . TYR A 1 188 ? 10.01600  4.08000   53.28800  1.000 121.00000 ? 179 TYR A CZ     1 
ATOM   1286  O  OH     . TYR A 1 188 ? 11.24900  3.84600   53.85700  1.000 114.57000 ? 179 TYR A OH     1 
ATOM   1287  N  N      . ALA A 1 189 ? 6.06000   3.51300   48.69600  1.000 70.32000  ? 180 ALA A N      1 
ATOM   1288  C  CA     . ALA A 1 189 ? 6.54600   2.58300   47.68300  1.000 74.27000  ? 180 ALA A CA     1 
ATOM   1289  C  C      . ALA A 1 189 ? 6.81500   3.29400   46.36200  1.000 81.41000  ? 180 ALA A C      1 
ATOM   1290  O  O      . ALA A 1 189 ? 7.76600   2.95700   45.64900  1.000 92.40000  ? 180 ALA A O      1 
ATOM   1291  C  CB     . ALA A 1 189 ? 5.53900   1.44900   47.49200  1.000 74.65000  ? 180 ALA A CB     1 
ATOM   1292  N  N      . LEU A 1 190 ? 5.99200   4.28700   46.02100  1.000 77.81000  ? 181 LEU A N      1 
ATOM   1293  C  CA     . LEU A 1 190 ? 6.19000   5.02400   44.77700  1.000 69.45000  ? 181 LEU A CA     1 
ATOM   1294  C  C      . LEU A 1 190 ? 7.49400   5.80100   44.80000  1.000 81.41000  ? 181 LEU A C      1 
ATOM   1295  O  O      . LEU A 1 190 ? 8.23000   5.83200   43.80600  1.000 89.56000  ? 181 LEU A O      1 
ATOM   1296  C  CB     . LEU A 1 190 ? 5.01800   5.97200   44.53800  1.000 57.22000  ? 181 LEU A CB     1 
ATOM   1297  C  CG     . LEU A 1 190 ? 5.05900   6.74300   43.22100  1.000 49.42000  ? 181 LEU A CG     1 
ATOM   1298  C  CD1    . LEU A 1 190 ? 5.04200   5.77700   42.04500  1.000 59.63000  ? 181 LEU A CD1    1 
ATOM   1299  C  CD2    . LEU A 1 190 ? 3.89100   7.71000   43.14000  1.000 80.59000  ? 181 LEU A CD2    1 
ATOM   1300  N  N      . GLY A 1 191 ? 7.78500   6.45700   45.91900  1.000 88.75000  ? 182 GLY A N      1 
ATOM   1301  C  CA     . GLY A 1 191 ? 9.05900   7.14700   46.02400  1.000 89.31000  ? 182 GLY A CA     1 
ATOM   1302  C  C      . GLY A 1 191 ? 10.22800  6.19600   45.86200  1.000 80.84000  ? 182 GLY A C      1 
ATOM   1303  O  O      . GLY A 1 191 ? 11.16900  6.45600   45.09400  1.000 78.96000  ? 182 GLY A O      1 
ATOM   1304  N  N      . CYS A 1 192 ? 10.18500  5.07400   46.58700  1.000 74.34000  ? 183 CYS A N      1 
ATOM   1305  C  CA     . CYS A 1 192 ? 11.25800  4.09700   46.44300  1.000 70.71000  ? 183 CYS A CA     1 
ATOM   1306  C  C      . CYS A 1 192 ? 11.39400  3.66000   44.99400  1.000 91.57000  ? 183 CYS A C      1 
ATOM   1307  O  O      . CYS A 1 192 ? 12.50900  3.53800   44.47500  1.000 104.00000 ? 183 CYS A O      1 
ATOM   1308  C  CB     . CYS A 1 192 ? 11.02000  2.88700   47.34600  1.000 67.49000  ? 183 CYS A CB     1 
ATOM   1309  S  SG     . CYS A 1 192 ? 10.89900  3.24200   49.11300  1.000 91.30000  ? 183 CYS A SG     1 
ATOM   1310  N  N      . SER A 1 193 ? 10.26500  3.43500   44.32100  1.000 91.33000  ? 184 SER A N      1 
ATOM   1311  C  CA     . SER A 1 193 ? 10.29400  2.96500   42.94200  1.000 82.17000  ? 184 SER A CA     1 
ATOM   1312  C  C      . SER A 1 193 ? 10.89600  4.00700   42.01000  1.000 88.11000  ? 184 SER A C      1 
ATOM   1313  O  O      . SER A 1 193 ? 11.59700  3.65700   41.06100  1.000 90.03000  ? 184 SER A O      1 
ATOM   1314  C  CB     . SER A 1 193 ? 8.88600   2.58600   42.49200  1.000 74.44000  ? 184 SER A CB     1 
ATOM   1315  O  OG     . SER A 1 193 ? 8.16600   3.72900   42.07200  1.000 96.98000  ? 184 SER A OG     1 
ATOM   1316  N  N      . ILE A 1 194 ? 10.59400  5.28700   42.22900  1.000 88.70000  ? 185 ILE A N      1 
ATOM   1317  C  CA     . ILE A 1 194 ? 11.15700  6.32900   41.37000  1.000 84.96000  ? 185 ILE A CA     1 
ATOM   1318  C  C      . ILE A 1 194 ? 12.66900  6.38300   41.53100  1.000 90.75000  ? 185 ILE A C      1 
ATOM   1319  O  O      . ILE A 1 194 ? 13.42200  6.45100   40.54600  1.000 82.02000  ? 185 ILE A O      1 
ATOM   1320  C  CB     . ILE A 1 194 ? 10.51200  7.69200   41.66700  1.000 65.58000  ? 185 ILE A CB     1 
ATOM   1321  C  CG1    . ILE A 1 194 ? 9.01900   7.64600   41.34200  1.000 88.36000  ? 185 ILE A CG1    1 
ATOM   1322  C  CG2    . ILE A 1 194 ? 11.23300  8.79300   40.88500  1.000 68.32000  ? 185 ILE A CG2    1 
ATOM   1323  C  CD1    . ILE A 1 194 ? 8.40600   9.00300   41.13800  1.000 86.10000  ? 185 ILE A CD1    1 
ATOM   1324  N  N      . ILE A 1 195 ? 13.13900  6.36400   42.77900  1.000 98.08000  ? 186 ILE A N      1 
ATOM   1325  C  CA     . ILE A 1 195 ? 14.58400  6.40000   42.98500  1.000 92.72000  ? 186 ILE A CA     1 
ATOM   1326  C  C      . ILE A 1 195 ? 15.23100  5.16200   42.38400  1.000 82.15000  ? 186 ILE A C      1 
ATOM   1327  O  O      . ILE A 1 195 ? 16.30100  5.23800   41.76600  1.000 80.56000  ? 186 ILE A O      1 
ATOM   1328  C  CB     . ILE A 1 195 ? 14.92600  6.55200   44.47700  1.000 92.78000  ? 186 ILE A CB     1 
ATOM   1329  C  CG1    . ILE A 1 195 ? 14.29300  7.82800   45.04000  1.000 112.26000 ? 186 ILE A CG1    1 
ATOM   1330  C  CG2    . ILE A 1 195 ? 16.43600  6.55800   44.66300  1.000 80.44000  ? 186 ILE A CG2    1 
ATOM   1331  C  CD1    . ILE A 1 195 ? 14.73300  9.09100   44.33000  1.000 109.82000 ? 186 ILE A CD1    1 
ATOM   1332  N  N      . ALA A 1 196 ? 14.58800  4.00400   42.54400  1.000 96.18000  ? 187 ALA A N      1 
ATOM   1333  C  CA     . ALA A 1 196 ? 15.12600  2.77100   41.98900  1.000 100.00000 ? 187 ALA A CA     1 
ATOM   1334  C  C      . ALA A 1 196 ? 15.14400  2.81400   40.46800  1.000 86.12000  ? 187 ALA A C      1 
ATOM   1335  O  O      . ALA A 1 196 ? 16.07700  2.31100   39.84100  1.000 102.33000 ? 187 ALA A O      1 
ATOM   1336  C  CB     . ALA A 1 196 ? 14.32100  1.57500   42.49400  1.000 91.39000  ? 187 ALA A CB     1 
ATOM   1337  N  N      . MET A 1 197 ? 14.10900  3.39100   39.85500  1.000 72.52000  ? 188 MET A N      1 
ATOM   1338  C  CA     . MET A 1 197 ? 14.08600  3.50700   38.40200  1.000 91.53000  ? 188 MET A CA     1 
ATOM   1339  C  C      . MET A 1 197 ? 15.23000  4.37100   37.92300  1.000 87.78000  ? 188 MET A C      1 
ATOM   1340  O  O      . MET A 1 197 ? 15.96600  3.99900   37.00300  1.000 83.21000  ? 188 MET A O      1 
ATOM   1341  C  CB     . MET A 1 197 ? 12.76000  4.09800   37.92600  1.000 96.87000  ? 188 MET A CB     1 
ATOM   1342  C  CG     . MET A 1 197 ? 12.63300  4.12700   36.40300  1.000 67.75000  ? 188 MET A CG     1 
ATOM   1343  S  SD     . MET A 1 197 ? 11.01700  4.62000   35.77900  1.000 104.12000 ? 188 MET A SD     1 
ATOM   1344  C  CE     . MET A 1 197 ? 10.76800  6.15200   36.66700  1.000 114.28000 ? 188 MET A CE     1 
ATOM   1345  N  N      . PHE A 1 198 ? 15.41600  5.52300   38.55500  1.000 88.04000  ? 189 PHE A N      1 
ATOM   1346  C  CA     . PHE A 1 198 ? 16.51400  6.35800   38.10900  1.000 99.18000  ? 189 PHE A CA     1 
ATOM   1347  C  C      . PHE A 1 198 ? 17.81300  5.58700   38.24200  1.000 95.97000  ? 189 PHE A C      1 
ATOM   1348  O  O      . PHE A 1 198 ? 18.51200  5.35100   37.24800  1.000 88.86000  ? 189 PHE A O      1 
ATOM   1349  C  CB     . PHE A 1 198 ? 16.55800  7.65600   38.91400  1.000 96.95000  ? 189 PHE A CB     1 
ATOM   1350  N  N      . ASP A 1 199 ? 18.05900  5.03500   39.43100  1.000 96.41000  ? 190 ASP A N      1 
ATOM   1351  C  CA     . ASP A 1 199 ? 19.31600  4.34200   39.65900  1.000 90.50000  ? 190 ASP A CA     1 
ATOM   1352  C  C      . ASP A 1 199 ? 19.51800  3.24900   38.62700  1.000 94.66000  ? 190 ASP A C      1 
ATOM   1353  O  O      . ASP A 1 199 ? 20.45900  3.30800   37.84000  1.000 88.99000  ? 190 ASP A O      1 
ATOM   1354  C  CB     . ASP A 1 199 ? 19.34800  3.74500   41.06800  1.000 84.56000  ? 190 ASP A CB     1 
ATOM   1355  C  CG     . ASP A 1 199 ? 19.99600  4.66900   42.09100  1.000 97.71000  ? 190 ASP A CG     1 
ATOM   1356  O  OD1    . ASP A 1 199 ? 21.24400  4.75500   42.12600  1.000 110.89000 ? 190 ASP A OD1    1 
ATOM   1357  O  OD2    . ASP A 1 199 ? 19.25900  5.26900   42.90300  1.000 103.53000 ? 190 ASP A OD2    1 
ATOM   1358  N  N      . ARG A 1 200 ? 18.54200  2.36000   38.47800  1.000 100.32000 ? 191 ARG A N      1 
ATOM   1359  C  CA     . ARG A 1 200 ? 18.79600  1.15500   37.70500  1.000 83.91000  ? 191 ARG A CA     1 
ATOM   1360  C  C      . ARG A 1 200 ? 18.73400  1.43100   36.21400  1.000 82.22000  ? 191 ARG A C      1 
ATOM   1361  O  O      . ARG A 1 200 ? 19.67800  1.12100   35.49000  1.000 98.86000  ? 191 ARG A O      1 
ATOM   1362  C  CB     . ARG A 1 200 ? 17.79400  0.05900   38.08900  1.000 67.98000  ? 191 ARG A CB     1 
ATOM   1363  N  N      . VAL A 1 201 ? 17.67000  2.07300   35.74000  1.000 66.34000  ? 192 VAL A N      1 
ATOM   1364  C  CA     . VAL A 1 201 ? 17.57000  2.34000   34.31300  1.000 66.03000  ? 192 VAL A CA     1 
ATOM   1365  C  C      . VAL A 1 201 ? 18.72700  3.22500   33.86800  1.000 90.47000  ? 192 VAL A C      1 
ATOM   1366  O  O      . VAL A 1 201 ? 19.52800  2.84200   33.00500  1.000 91.70000  ? 192 VAL A O      1 
ATOM   1367  C  CB     . VAL A 1 201 ? 16.20700  2.97000   33.98500  1.000 65.39000  ? 192 VAL A CB     1 
ATOM   1368  C  CG1    . VAL A 1 201 ? 16.14100  3.37600   32.53000  1.000 80.27000  ? 192 VAL A CG1    1 
ATOM   1369  C  CG2    . VAL A 1 201 ? 15.07900  2.00200   34.33800  1.000 68.94000  ? 192 VAL A CG2    1 
ATOM   1370  N  N      . GLY A 1 202 ? 18.87800  4.39500   34.49400  1.000 94.93000  ? 193 GLY A N      1 
ATOM   1371  C  CA     . GLY A 1 202 ? 19.91400  5.30500   34.04600  1.000 84.20000  ? 193 GLY A CA     1 
ATOM   1372  C  C      . GLY A 1 202 ? 21.30800  4.75000   34.27100  1.000 76.29000  ? 193 GLY A C      1 
ATOM   1373  O  O      . GLY A 1 202 ? 22.14900  4.78000   33.36700  1.000 86.69000  ? 193 GLY A O      1 
ATOM   1374  N  N      . GLY A 1 203 ? 21.56900  4.21800   35.46900  1.000 71.53000  ? 194 GLY A N      1 
ATOM   1375  C  CA     . GLY A 1 203 ? 22.88100  3.68600   35.76600  1.000 80.90000  ? 194 GLY A CA     1 
ATOM   1376  C  C      . GLY A 1 203 ? 23.24700  2.49900   34.90400  1.000 87.68000  ? 194 GLY A C      1 
ATOM   1377  O  O      . GLY A 1 203 ? 24.40800  2.32400   34.55600  1.000 101.39000 ? 194 GLY A O      1 
ATOM   1378  N  N      . GLY A 1 204 ? 22.27600  1.64500   34.58000  1.000 82.74000  ? 195 GLY A N      1 
ATOM   1379  C  CA     . GLY A 1 204 ? 22.54900  0.54400   33.67700  1.000 87.29000  ? 195 GLY A CA     1 
ATOM   1380  C  C      . GLY A 1 204 ? 22.84400  1.01000   32.26800  1.000 90.27000  ? 195 GLY A C      1 
ATOM   1381  O  O      . GLY A 1 204 ? 23.76700  0.50500   31.62000  1.000 101.76000 ? 195 GLY A O      1 
ATOM   1382  N  N      . VAL A 1 205 ? 22.07000  1.98000   31.77100  1.000 68.88000  ? 196 VAL A N      1 
ATOM   1383  C  CA     . VAL A 1 205 ? 22.36600  2.53100   30.45300  1.000 70.49000  ? 196 VAL A CA     1 
ATOM   1384  C  C      . VAL A 1 205 ? 23.79100  3.06900   30.43300  1.000 91.69000  ? 196 VAL A C      1 
ATOM   1385  O  O      . VAL A 1 205 ? 24.58500  2.74100   29.54400  1.000 101.33000 ? 196 VAL A O      1 
ATOM   1386  C  CB     . VAL A 1 205 ? 21.34300  3.61800   30.07200  1.000 85.11000  ? 196 VAL A CB     1 
ATOM   1387  C  CG1    . VAL A 1 205 ? 21.83100  4.40000   28.85600  1.000 99.02000  ? 196 VAL A CG1    1 
ATOM   1388  C  CG2    . VAL A 1 205 ? 19.97500  3.00900   29.79900  1.000 82.50000  ? 196 VAL A CG2    1 
ATOM   1389  N  N      . TYR A 1 206 ? 24.15200  3.85200   31.45500  1.000 96.79000  ? 197 TYR A N      1 
ATOM   1390  C  CA     . TYR A 1 206 ? 25.49700  4.41900   31.53200  1.000 95.57000  ? 197 TYR A CA     1 
ATOM   1391  C  C      . TYR A 1 206 ? 26.55600  3.34300   31.73500  1.000 95.98000  ? 197 TYR A C      1 
ATOM   1392  O  O      . TYR A 1 206 ? 27.63500  3.40900   31.14100  1.000 107.74000 ? 197 TYR A O      1 
ATOM   1393  C  CB     . TYR A 1 206 ? 25.57400  5.44600   32.66000  1.000 99.44000  ? 197 TYR A CB     1 
ATOM   1394  C  CG     . TYR A 1 206 ? 26.97600  5.62500   33.20700  1.000 109.90000 ? 197 TYR A CG     1 
ATOM   1395  C  CD1    . TYR A 1 206 ? 27.94000  6.34300   32.50300  1.000 113.64000 ? 197 TYR A CD1    1 
ATOM   1396  C  CD2    . TYR A 1 206 ? 27.34200  5.05700   34.42000  1.000 102.06000 ? 197 TYR A CD2    1 
ATOM   1397  C  CE1    . TYR A 1 206 ? 29.23000  6.50300   33.00600  1.000 98.15000  ? 197 TYR A CE1    1 
ATOM   1398  C  CE2    . TYR A 1 206 ? 28.62100  5.20800   34.92600  1.000 105.27000 ? 197 TYR A CE2    1 
ATOM   1399  C  CZ     . TYR A 1 206 ? 29.56200  5.93100   34.21700  1.000 102.87000 ? 197 TYR A CZ     1 
ATOM   1400  O  OH     . TYR A 1 206 ? 30.83600  6.07800   34.72600  1.000 120.74000 ? 197 TYR A OH     1 
ATOM   1401  N  N      . THR A 1 207 ? 26.27100  2.35300   32.57800  1.000 89.88000  ? 198 THR A N      1 
ATOM   1402  C  CA     . THR A 1 207 ? 27.23300  1.30300   32.88500  1.000 93.33000  ? 198 THR A CA     1 
ATOM   1403  C  C      . THR A 1 207 ? 27.58200  0.51200   31.63900  1.000 101.49000 ? 198 THR A C      1 
ATOM   1404  O  O      . THR A 1 207 ? 28.75900  0.26300   31.35100  1.000 106.58000 ? 198 THR A O      1 
ATOM   1405  C  CB     . THR A 1 207 ? 26.66700  0.37700   33.96400  1.000 84.04000  ? 198 THR A CB     1 
ATOM   1406  O  OG1    . THR A 1 207 ? 26.46100  1.11400   35.17400  1.000 102.03000 ? 198 THR A OG1    1 
ATOM   1407  C  CG2    . THR A 1 207 ? 27.62500  -0.76300  34.24500  1.000 97.02000  ? 198 THR A CG2    1 
ATOM   1408  N  N      . LYS A 1 208 ? 26.56900  0.09100   30.89000  1.000 84.54000  ? 199 LYS A N      1 
ATOM   1409  C  CA     . LYS A 1 208 ? 26.85100  -0.69200  29.70200  1.000 73.00000  ? 199 LYS A CA     1 
ATOM   1410  C  C      . LYS A 1 208 ? 27.30700  0.17400   28.53900  1.000 78.13000  ? 199 LYS A C      1 
ATOM   1411  O  O      . LYS A 1 208 ? 28.02400  -0.32300  27.66800  1.000 85.03000  ? 199 LYS A O      1 
ATOM   1412  C  CB     . LYS A 1 208 ? 25.62500  -1.52300  29.31900  1.000 78.23000  ? 199 LYS A CB     1 
ATOM   1413  C  CG     . LYS A 1 208 ? 25.26500  -2.56800  30.37600  1.000 84.56000  ? 199 LYS A CG     1 
ATOM   1414  C  CD     . LYS A 1 208 ? 26.38900  -3.58500  30.49600  1.000 76.68000  ? 199 LYS A CD     1 
ATOM   1415  C  CE     . LYS A 1 208 ? 27.37500  -3.18300  31.57900  1.000 72.03000  ? 199 LYS A CE     1 
ATOM   1416  N  NZ     . LYS A 1 208 ? 28.46800  -4.17400  31.76600  1.000 87.20000  ? 199 LYS A NZ     1 
ATOM   1417  N  N      . ALA A 1 209 ? 26.98600  1.46900   28.54200  1.000 72.78000  ? 200 ALA A N      1 
ATOM   1418  C  CA     . ALA A 1 209 ? 27.60200  2.36200   27.57000  1.000 69.51000  ? 200 ALA A CA     1 
ATOM   1419  C  C      . ALA A 1 209 ? 29.08700  2.53400   27.85500  1.000 76.58000  ? 200 ALA A C      1 
ATOM   1420  O  O      . ALA A 1 209 ? 29.89700  2.62900   26.92900  1.000 80.90000  ? 200 ALA A O      1 
ATOM   1421  C  CB     . ALA A 1 209 ? 26.88700  3.71100   27.57400  1.000 76.23000  ? 200 ALA A CB     1 
ATOM   1422  N  N      . ALA A 1 210 ? 29.46700  2.53600   29.13300  1.000 83.41000  ? 201 ALA A N      1 
ATOM   1423  C  CA     . ALA A 1 210 ? 30.87800  2.63200   29.48700  1.000 84.98000  ? 201 ALA A CA     1 
ATOM   1424  C  C      . ALA A 1 210 ? 31.59900  1.32200   29.20500  1.000 84.32000  ? 201 ALA A C      1 
ATOM   1425  O  O      . ALA A 1 210 ? 32.76200  1.32200   28.78800  1.000 92.32000  ? 201 ALA A O      1 
ATOM   1426  C  CB     . ALA A 1 210 ? 31.02600  3.02500   30.95700  1.000 82.53000  ? 201 ALA A CB     1 
ATOM   1427  N  N      . ASP A 1 211 ? 30.92600  0.19600   29.44100  1.000 78.29000  ? 202 ASP A N      1 
ATOM   1428  C  CA     . ASP A 1 211 ? 31.51100  -1.09400  29.09500  1.000 88.44000  ? 202 ASP A CA     1 
ATOM   1429  C  C      . ASP A 1 211 ? 31.71300  -1.21000  27.58900  1.000 84.29000  ? 202 ASP A C      1 
ATOM   1430  O  O      . ASP A 1 211 ? 32.75600  -1.68900  27.13000  1.000 97.03000  ? 202 ASP A O      1 
ATOM   1431  C  CB     . ASP A 1 211 ? 30.62700  -2.23000  29.61400  1.000 93.09000  ? 202 ASP A CB     1 
ATOM   1432  C  CG     . ASP A 1 211 ? 31.23400  -3.60400  29.36800  1.000 83.05000  ? 202 ASP A CG     1 
ATOM   1433  O  OD1    . ASP A 1 211 ? 32.09300  -4.03000  30.16800  1.000 82.02000  ? 202 ASP A OD1    1 
ATOM   1434  O  OD2    . ASP A 1 211 ? 30.85700  -4.25600  28.37100  1.000 70.48000  ? 202 ASP A OD2    1 
ATOM   1435  N  N      . MET A 1 212 ? 30.72100  -0.77900  26.80400  1.000 74.38000  ? 203 MET A N      1 
ATOM   1436  C  CA     . MET A 1 212 ? 30.84100  -0.81100  25.35000  1.000 79.75000  ? 203 MET A CA     1 
ATOM   1437  C  C      . MET A 1 212 ? 31.91200  0.16000   24.86700  1.000 89.50000  ? 203 MET A C      1 
ATOM   1438  O  O      . MET A 1 212 ? 32.64900  -0.13900  23.92100  1.000 112.97000 ? 203 MET A O      1 
ATOM   1439  C  CB     . MET A 1 212 ? 29.49000  -0.50400  24.70600  1.000 83.21000  ? 203 MET A CB     1 
ATOM   1440  C  CG     . MET A 1 212 ? 29.47700  -0.65300  23.19300  1.000 92.50000  ? 203 MET A CG     1 
ATOM   1441  S  SD     . MET A 1 212 ? 27.81100  -0.63600  22.49600  1.000 113.20000 ? 203 MET A SD     1 
ATOM   1442  C  CE     . MET A 1 212 ? 27.15300  -2.17300  23.13800  1.000 92.55000  ? 203 MET A CE     1 
ATOM   1443  N  N      . ALA A 1 213 ? 31.99700  1.34000   25.48000  1.000 71.51000  ? 204 ALA A N      1 
ATOM   1444  C  CA     . ALA A 1 213 ? 33.03700  2.29000   25.11500  1.000 77.83000  ? 204 ALA A CA     1 
ATOM   1445  C  C      . ALA A 1 213 ? 34.42400  1.76800   25.46600  1.000 90.00000  ? 204 ALA A C      1 
ATOM   1446  O  O      . ALA A 1 213 ? 35.39100  2.05900   24.75300  1.000 99.64000  ? 204 ALA A O      1 
ATOM   1447  C  CB     . ALA A 1 213 ? 32.78200  3.63000   25.79800  1.000 86.25000  ? 204 ALA A CB     1 
ATOM   1448  N  N      . ALA A 1 214 ? 34.54800  1.01200   26.56100  1.000 92.30000  ? 205 ALA A N      1 
ATOM   1449  C  CA     . ALA A 1 214 ? 35.85600  0.51000   26.96800  1.000 97.92000  ? 205 ALA A CA     1 
ATOM   1450  C  C      . ALA A 1 214 ? 36.44400  -0.39600  25.89400  1.000 114.93000 ? 205 ALA A C      1 
ATOM   1451  O  O      . ALA A 1 214 ? 37.57100  -0.17800  25.43200  1.000 129.07000 ? 205 ALA A O      1 
ATOM   1452  C  CB     . ALA A 1 214 ? 35.74400  -0.22500  28.30600  1.000 95.30000  ? 205 ALA A CB     1 
ATOM   1453  N  N      . ASP A 1 215 ? 35.69100  -1.41900  25.47400  1.000 115.15000 ? 206 ASP A N      1 
ATOM   1454  C  CA     . ASP A 1 215 ? 36.17600  -2.28300  24.40100  1.000 114.38000 ? 206 ASP A CA     1 
ATOM   1455  C  C      . ASP A 1 215 ? 36.06200  -1.70400  22.99000  1.000 104.95000 ? 206 ASP A C      1 
ATOM   1456  O  O      . ASP A 1 215 ? 36.72100  -2.20000  22.06800  1.000 116.01000 ? 206 ASP A O      1 
ATOM   1457  C  CB     . ASP A 1 215 ? 35.39800  -3.60500  24.35800  1.000 123.87000 ? 206 ASP A CB     1 
ATOM   1458  C  CG     . ASP A 1 215 ? 33.90100  -3.42300  24.50300  1.000 123.56000 ? 206 ASP A CG     1 
ATOM   1459  O  OD1    . ASP A 1 215 ? 33.44600  -2.27400  24.63000  1.000 120.89000 ? 206 ASP A OD1    1 
ATOM   1460  O  OD2    . ASP A 1 215 ? 33.17400  -4.43900  24.48200  1.000 116.74000 ? 206 ASP A OD2    1 
ATOM   1461  N  N      . LEU A 1 216 ? 35.21300  -0.69800  22.79200  1.000 91.19000  ? 207 LEU A N      1 
ATOM   1462  C  CA     . LEU A 1 216 ? 35.12900  0.01300   21.51300  1.000 96.12000  ? 207 LEU A CA     1 
ATOM   1463  C  C      . LEU A 1 216 ? 36.19800  1.10300   21.39400  1.000 96.51000  ? 207 LEU A C      1 
ATOM   1464  O  O      . LEU A 1 216 ? 37.35000  0.85500   21.02600  1.000 83.32000  ? 207 LEU A O      1 
ATOM   1465  C  CB     . LEU A 1 216 ? 33.73300  0.61600   21.31100  1.000 100.67000 ? 207 LEU A CB     1 
ATOM   1466  C  CG     . LEU A 1 216 ? 33.45200  1.22200   19.93300  1.000 106.77000 ? 207 LEU A CG     1 
ATOM   1467  C  CD1    . LEU A 1 216 ? 31.98500  1.05300   19.52300  1.000 122.78000 ? 207 LEU A CD1    1 
ATOM   1468  C  CD2    . LEU A 1 216 ? 33.87000  2.68700   19.90600  1.000 85.15000  ? 207 LEU A CD2    1 
ATOM   1469  N  N      . PRO A 1 225 ? 45.35500  -7.38500  29.27100  1.000 130.76000 ? 216 PRO A N      1 
ATOM   1470  C  CA     . PRO A 1 225 ? 44.45000  -8.20900  28.45700  1.000 122.87000 ? 216 PRO A CA     1 
ATOM   1471  C  C      . PRO A 1 225 ? 42.98700  -7.99100  28.86700  1.000 124.97000 ? 216 PRO A C      1 
ATOM   1472  O  O      . PRO A 1 225 ? 42.12400  -8.58300  28.25000  1.000 126.64000 ? 216 PRO A O      1 
ATOM   1473  C  CB     . PRO A 1 225 ? 44.90600  -9.63500  28.77400  1.000 105.71000 ? 216 PRO A CB     1 
ATOM   1474  C  CG     . PRO A 1 225 ? 46.38900  -9.49000  29.03500  1.000 119.14000 ? 216 PRO A CG     1 
ATOM   1475  C  CD     . PRO A 1 225 ? 46.55400  -8.13200  29.69100  1.000 132.31000 ? 216 PRO A CD     1 
ATOM   1476  N  N      . GLU A 1 226 ? 42.75100  -7.18800  29.91500  1.000 127.12000 ? 217 GLU A N      1 
ATOM   1477  C  CA     . GLU A 1 226 ? 41.40400  -6.87500  30.37700  1.000 132.65000 ? 217 GLU A CA     1 
ATOM   1478  C  C      . GLU A 1 226 ? 40.89200  -5.50400  29.94500  1.000 132.90000 ? 217 GLU A C      1 
ATOM   1479  O  O      . GLU A 1 226 ? 39.76000  -5.40300  29.46000  1.000 121.39000 ? 217 GLU A O      1 
ATOM   1480  C  CB     . GLU A 1 226 ? 41.32800  -6.99800  31.90200  1.000 121.35000 ? 217 GLU A CB     1 
ATOM   1481  C  CG     . GLU A 1 226 ? 39.93800  -6.78700  32.45800  1.000 110.25000 ? 217 GLU A CG     1 
ATOM   1482  C  CD     . GLU A 1 226 ? 38.97000  -7.86000  32.00400  1.000 110.77000 ? 217 GLU A CD     1 
ATOM   1483  O  OE1    . GLU A 1 226 ? 39.42600  -8.89100  31.46500  1.000 120.17000 ? 217 GLU A OE1    1 
ATOM   1484  O  OE2    . GLU A 1 226 ? 37.74900  -7.66800  32.17800  1.000 118.57000 ? 217 GLU A OE2    1 
ATOM   1485  N  N      . ASP A 1 227 ? 41.68000  -4.44000  30.12300  1.000 129.70000 ? 218 ASP A N      1 
ATOM   1486  C  CA     . ASP A 1 227 ? 41.24700  -3.08600  29.79300  1.000 114.72000 ? 218 ASP A CA     1 
ATOM   1487  C  C      . ASP A 1 227 ? 42.29700  -2.37200  28.95000  1.000 125.64000 ? 218 ASP A C      1 
ATOM   1488  O  O      . ASP A 1 227 ? 43.46600  -2.76400  28.91400  1.000 142.28000 ? 218 ASP A O      1 
ATOM   1489  C  CB     . ASP A 1 227 ? 40.95100  -2.25700  31.05400  1.000 103.20000 ? 218 ASP A CB     1 
ATOM   1490  C  CG     . ASP A 1 227 ? 42.20100  -1.93000  31.84200  1.000 123.92000 ? 218 ASP A CG     1 
ATOM   1491  O  OD1    . ASP A 1 227 ? 42.86600  -2.88100  32.29800  1.000 147.93000 ? 218 ASP A OD1    1 
ATOM   1492  O  OD2    . ASP A 1 227 ? 42.51200  -0.73000  32.01500  1.000 126.99000 ? 218 ASP A OD2    1 
ATOM   1493  N  N      . ASP A 1 228 ? 41.85800  -1.30500  28.27600  1.000 127.37000 ? 219 ASP A N      1 
ATOM   1494  C  CA     . ASP A 1 228 ? 42.71800  -0.44500  27.47500  1.000 132.82000 ? 219 ASP A CA     1 
ATOM   1495  C  C      . ASP A 1 228 ? 43.56200  0.46500   28.36300  1.000 129.75000 ? 219 ASP A C      1 
ATOM   1496  O  O      . ASP A 1 228 ? 43.19100  0.76700   29.50200  1.000 122.53000 ? 219 ASP A O      1 
ATOM   1497  C  CB     . ASP A 1 228 ? 41.87900  0.38100   26.50000  1.000 133.53000 ? 219 ASP A CB     1 
ATOM   1498  C  CG     . ASP A 1 228 ? 41.70000  -0.30800  25.14600  1.000 135.02000 ? 219 ASP A CG     1 
ATOM   1499  O  OD1    . ASP A 1 228 ? 42.41600  -1.29700  24.87900  1.000 145.00000 ? 219 ASP A OD1    1 
ATOM   1500  O  OD2    . ASP A 1 228 ? 40.83300  0.12600   24.35300  1.000 126.72000 ? 219 ASP A OD2    1 
ATOM   1501  N  N      . PRO A 1 229 ? 44.71500  0.90700   27.86000  1.000 129.44000 ? 220 PRO A N      1 
ATOM   1502  C  CA     . PRO A 1 229 ? 45.62200  1.72100   28.67900  1.000 126.95000 ? 220 PRO A CA     1 
ATOM   1503  C  C      . PRO A 1 229 ? 45.11900  3.13700   28.92400  1.000 130.42000 ? 220 PRO A C      1 
ATOM   1504  O  O      . PRO A 1 229 ? 45.02700  3.95200   27.99900  1.000 136.37000 ? 220 PRO A O      1 
ATOM   1505  C  CB     . PRO A 1 229 ? 46.92400  1.72300   27.85900  1.000 122.71000 ? 220 PRO A CB     1 
ATOM   1506  C  CG     . PRO A 1 229 ? 46.72600  0.67700   26.78000  1.000 118.46000 ? 220 PRO A CG     1 
ATOM   1507  C  CD     . PRO A 1 229 ? 45.26800  0.65000   26.52200  1.000 115.70000 ? 220 PRO A CD     1 
ATOM   1508  N  N      . ARG A 1 230 ? 44.78500  3.44000   30.17900  1.000 119.58000 ? 221 ARG A N      1 
ATOM   1509  C  CA     . ARG A 1 230 ? 44.33400  4.77800   30.55900  1.000 105.23000 ? 221 ARG A CA     1 
ATOM   1510  C  C      . ARG A 1 230 ? 43.15600  5.25600   29.71700  1.000 110.83000 ? 221 ARG A C      1 
ATOM   1511  O  O      . ARG A 1 230 ? 42.92400  6.46100   29.57400  1.000 107.15000 ? 221 ARG A O      1 
ATOM   1512  C  CB     . ARG A 1 230 ? 45.48500  5.78300   30.52700  1.000 105.67000 ? 221 ARG A CB     1 
ATOM   1513  C  CG     . ARG A 1 230 ? 45.14100  7.08700   31.21100  1.000 111.03000 ? 221 ARG A CG     1 
ATOM   1514  C  CD     . ARG A 1 230 ? 44.33200  6.87200   32.48000  1.000 102.25000 ? 221 ARG A CD     1 
ATOM   1515  N  NE     . ARG A 1 230 ? 44.92600  5.88800   33.37200  1.000 120.36000 ? 221 ARG A NE     1 
ATOM   1516  C  CZ     . ARG A 1 230 ? 44.22100  4.98400   34.03500  1.000 111.42000 ? 221 ARG A CZ     1 
ATOM   1517  N  NH1    . ARG A 1 230 ? 42.90500  4.91800   33.91900  1.000 120.85000 ? 221 ARG A NH1    1 
ATOM   1518  N  NH2    . ARG A 1 230 ? 44.85100  4.11300   34.81800  1.000 83.57000  ? 221 ARG A NH2    1 
ATOM   1519  N  N      . ASN A 1 231 ? 42.41600  4.33100   29.13700  1.000 114.71000 ? 222 ASN A N      1 
ATOM   1520  C  CA     . ASN A 1 231 ? 41.22400  4.70900   28.40500  1.000 112.38000 ? 222 ASN A CA     1 
ATOM   1521  C  C      . ASN A 1 231 ? 40.28100  5.48500   29.31900  1.000 99.22000  ? 222 ASN A C      1 
ATOM   1522  O  O      . ASN A 1 231 ? 40.02500  5.04800   30.44900  1.000 88.87000  ? 222 ASN A O      1 
ATOM   1523  C  CB     . ASN A 1 231 ? 40.52200  3.46200   27.87600  1.000 110.23000 ? 222 ASN A CB     1 
ATOM   1524  C  CG     . ASN A 1 231 ? 39.67300  3.74700   26.66300  1.000 118.32000 ? 222 ASN A CG     1 
ATOM   1525  O  OD1    . ASN A 1 231 ? 38.74400  4.55600   26.71700  1.000 121.00000 ? 222 ASN A OD1    1 
ATOM   1526  N  ND2    . ASN A 1 231 ? 39.97200  3.07300   25.56300  1.000 121.08000 ? 222 ASN A ND2    1 
ATOM   1527  N  N      . PRO A 1 232 ? 39.76400  6.64000   28.88700  1.000 98.66000  ? 223 PRO A N      1 
ATOM   1528  C  CA     . PRO A 1 232 ? 38.77800  7.33000   29.72900  1.000 108.82000 ? 223 PRO A CA     1 
ATOM   1529  C  C      . PRO A 1 232 ? 37.62300  6.41400   30.06100  1.000 115.21000 ? 223 PRO A C      1 
ATOM   1530  O  O      . PRO A 1 232 ? 37.11100  6.41800   31.18800  1.000 115.47000 ? 223 PRO A O      1 
ATOM   1531  C  CB     . PRO A 1 232 ? 38.34700  8.51500   28.85500  1.000 95.39000  ? 223 PRO A CB     1 
ATOM   1532  C  CG     . PRO A 1 232 ? 39.54200  8.78200   28.02200  1.000 99.85000  ? 223 PRO A CG     1 
ATOM   1533  C  CD     . PRO A 1 232 ? 40.08100  7.41700   27.67800  1.000 96.47000  ? 223 PRO A CD     1 
ATOM   1534  N  N      . ALA A 1 233 ? 37.21500  5.60200   29.08800  1.000 112.47000 ? 224 ALA A N      1 
ATOM   1535  C  CA     . ALA A 1 233 ? 36.20300  4.59000   29.33100  1.000 107.00000 ? 224 ALA A CA     1 
ATOM   1536  C  C      . ALA A 1 233 ? 36.67200  3.55000   30.33200  1.000 111.89000 ? 224 ALA A C      1 
ATOM   1537  O  O      . ALA A 1 233 ? 35.83600  2.88200   30.93600  1.000 113.45000 ? 224 ALA A O      1 
ATOM   1538  C  CB     . ALA A 1 233 ? 35.81000  3.91500   28.02700  1.000 102.85000 ? 224 ALA A CB     1 
ATOM   1539  N  N      . THR A 1 234 ? 37.98200  3.38700   30.52100  1.000 102.67000 ? 225 THR A N      1 
ATOM   1540  C  CA     . THR A 1 234 ? 38.45200  2.48700   31.56800  1.000 103.81000 ? 225 THR A CA     1 
ATOM   1541  C  C      . THR A 1 234 ? 38.03000  2.99700   32.94000  1.000 106.18000 ? 225 THR A C      1 
ATOM   1542  O  O      . THR A 1 234 ? 37.45000  2.25800   33.74800  1.000 112.13000 ? 225 THR A O      1 
ATOM   1543  C  CB     . THR A 1 234 ? 39.97300  2.34500   31.48900  1.000 107.18000 ? 225 THR A CB     1 
ATOM   1544  O  OG1    . THR A 1 234 ? 40.32000  1.39300   30.47500  1.000 112.81000 ? 225 THR A OG1    1 
ATOM   1545  C  CG2    . THR A 1 234 ? 40.54200  1.88600   32.82100  1.000 100.68000 ? 225 THR A CG2    1 
ATOM   1546  N  N      . ILE A 1 235 ? 38.28600  4.27900   33.20300  1.000 109.03000 ? 226 ILE A N      1 
ATOM   1547  C  CA     . ILE A 1 235 ? 37.82200  4.89600   34.44000  1.000 121.99000 ? 226 ILE A CA     1 
ATOM   1548  C  C      . ILE A 1 235 ? 36.30100  4.86700   34.50500  1.000 119.51000 ? 226 ILE A C      1 
ATOM   1549  O  O      . ILE A 1 235 ? 35.70900  4.60400   35.56200  1.000 113.92000 ? 226 ILE A O      1 
ATOM   1550  C  CB     . ILE A 1 235 ? 38.37300  6.33000   34.55600  1.000 127.03000 ? 226 ILE A CB     1 
ATOM   1551  C  CG1    . ILE A 1 235 ? 39.85200  6.37000   34.15800  1.000 122.15000 ? 226 ILE A CG1    1 
ATOM   1552  C  CG2    . ILE A 1 235 ? 38.18300  6.86800   35.96900  1.000 117.56000 ? 226 ILE A CG2    1 
ATOM   1553  C  CD1    . ILE A 1 235 ? 40.44700  7.76700   34.13900  1.000 112.67000 ? 226 ILE A CD1    1 
ATOM   1554  N  N      . ALA A 1 236 ? 35.64400  5.14500   33.37900  1.000 115.36000 ? 227 ALA A N      1 
ATOM   1555  C  CA     . ALA A 1 236 ? 34.18700  5.12700   33.36500  1.000 102.64000 ? 227 ALA A CA     1 
ATOM   1556  C  C      . ALA A 1 236 ? 33.64500  3.75100   33.72800  1.000 94.69000  ? 227 ALA A C      1 
ATOM   1557  O  O      . ALA A 1 236 ? 32.66900  3.64100   34.47100  1.000 86.75000  ? 227 ALA A O      1 
ATOM   1558  C  CB     . ALA A 1 236 ? 33.67400  5.56300   31.99600  1.000 94.96000  ? 227 ALA A CB     1 
ATOM   1559  N  N      . ASP A 1 237 ? 34.26900  2.68900   33.21700  1.000 102.51000 ? 228 ASP A N      1 
ATOM   1560  C  CA     . ASP A 1 237 ? 33.82300  1.33400   33.51600  1.000 112.71000 ? 228 ASP A CA     1 
ATOM   1561  C  C      . ASP A 1 237 ? 34.07100  0.98700   34.97400  1.000 104.03000 ? 228 ASP A C      1 
ATOM   1562  O  O      . ASP A 1 237 ? 33.24600  0.32100   35.61400  1.000 104.99000 ? 228 ASP A O      1 
ATOM   1563  C  CB     . ASP A 1 237 ? 34.53000  0.33500   32.59900  1.000 116.73000 ? 228 ASP A CB     1 
ATOM   1564  C  CG     . ASP A 1 237 ? 33.98900  -1.07600  32.74200  1.000 114.58000 ? 228 ASP A CG     1 
ATOM   1565  O  OD1    . ASP A 1 237 ? 32.86800  -1.23000  33.27000  1.000 124.53000 ? 228 ASP A OD1    1 
ATOM   1566  O  OD2    . ASP A 1 237 ? 34.68600  -2.03000  32.33000  1.000 101.77000 ? 228 ASP A OD2    1 
ATOM   1567  N  N      . ASN A 1 238 ? 35.21700  1.40900   35.51100  1.000 103.40000 ? 229 ASN A N      1 
ATOM   1568  C  CA     . ASN A 1 238 ? 35.45400  1.20800   36.93400  1.000 112.27000 ? 229 ASN A CA     1 
ATOM   1569  C  C      . ASN A 1 238 ? 34.35900  1.87000   37.75900  1.000 101.07000 ? 229 ASN A C      1 
ATOM   1570  O  O      . ASN A 1 238 ? 33.88800  1.30400   38.75200  1.000 92.48000  ? 229 ASN A O      1 
ATOM   1571  C  CB     . ASN A 1 238 ? 36.83300  1.74400   37.31600  1.000 128.23000 ? 229 ASN A CB     1 
ATOM   1572  C  CG     . ASN A 1 238 ? 37.94900  1.07000   36.53800  1.000 126.03000 ? 229 ASN A CG     1 
ATOM   1573  O  OD1    . ASN A 1 238 ? 38.98300  1.67600   36.25100  1.000 131.71000 ? 229 ASN A OD1    1 
ATOM   1574  N  ND2    . ASN A 1 238 ? 37.74100  -0.19600  36.19200  1.000 121.09000 ? 229 ASN A ND2    1 
ATOM   1575  N  N      . VAL A 1 239 ? 33.93000  3.06600   37.35100  1.000 96.33000  ? 230 VAL A N      1 
ATOM   1576  C  CA     . VAL A 1 239 ? 32.84200  3.74200   38.05400  1.000 98.29000  ? 230 VAL A CA     1 
ATOM   1577  C  C      . VAL A 1 239 ? 31.52000  3.00100   37.85200  1.000 91.57000  ? 230 VAL A C      1 
ATOM   1578  O  O      . VAL A 1 239 ? 30.70600  2.88200   38.77700  1.000 79.63000  ? 230 VAL A O      1 
ATOM   1579  C  CB     . VAL A 1 239 ? 32.75000  5.20900   37.59900  1.000 110.75000 ? 230 VAL A CB     1 
ATOM   1580  C  CG1    . VAL A 1 239 ? 31.49800  5.86100   38.16700  1.000 93.96000  ? 230 VAL A CG1    1 
ATOM   1581  C  CG2    . VAL A 1 239 ? 33.99700  5.97000   38.01200  1.000 128.58000 ? 230 VAL A CG2    1 
ATOM   1582  N  N      . GLY A 1 240 ? 31.28700  2.49200   36.64200  1.000 95.52000  ? 231 GLY A N      1 
ATOM   1583  C  CA     . GLY A 1 240 ? 30.01800  1.84500   36.34600  1.000 86.23000  ? 231 GLY A CA     1 
ATOM   1584  C  C      . GLY A 1 240 ? 29.82000  0.54600   37.10100  1.000 75.20000  ? 231 GLY A C      1 
ATOM   1585  O  O      . GLY A 1 240 ? 28.70100  0.22100   37.50800  1.000 79.67000  ? 231 GLY A O      1 
ATOM   1586  N  N      . ASP A 1 241 ? 30.89600  -0.22600  37.28400  1.000 82.79000  ? 232 ASP A N      1 
ATOM   1587  C  CA     . ASP A 1 241 ? 30.78800  -1.44400  38.08500  1.000 90.25000  ? 232 ASP A CA     1 
ATOM   1588  C  C      . ASP A 1 241 ? 30.25300  -1.13100  39.47900  1.000 85.67000  ? 232 ASP A C      1 
ATOM   1589  O  O      . ASP A 1 241 ? 29.42900  -1.87700  40.02300  1.000 79.91000  ? 232 ASP A O      1 
ATOM   1590  C  CB     . ASP A 1 241 ? 32.14100  -2.15500  38.17200  1.000 97.16000  ? 232 ASP A CB     1 
ATOM   1591  C  CG     . ASP A 1 241 ? 32.57700  -2.74800  36.84100  1.000 109.03000 ? 232 ASP A CG     1 
ATOM   1592  O  OD1    . ASP A 1 241 ? 31.69400  -3.16000  36.05900  1.000 109.69000 ? 232 ASP A OD1    1 
ATOM   1593  O  OD2    . ASP A 1 241 ? 33.79900  -2.80200  36.57600  1.000 113.76000 ? 232 ASP A OD2    1 
ATOM   1594  N  N      . ASN A 1 242 ? 30.72200  -0.03600  40.07800  1.000 91.29000  ? 233 ASN A N      1 
ATOM   1595  C  CA     . ASN A 1 242 ? 30.18200  0.39700   41.36300  1.000 81.11000  ? 233 ASN A CA     1 
ATOM   1596  C  C      . ASN A 1 242 ? 28.74600  0.87600   41.21700  1.000 86.77000  ? 233 ASN A C      1 
ATOM   1597  O  O      . ASN A 1 242 ? 27.90400  0.61600   42.08500  1.000 86.70000  ? 233 ASN A O      1 
ATOM   1598  C  CB     . ASN A 1 242 ? 31.05500  1.50300   41.94700  1.000 75.93000  ? 233 ASN A CB     1 
ATOM   1599  C  CG     . ASN A 1 242 ? 32.49200  1.07400   42.11000  1.000 98.42000  ? 233 ASN A CG     1 
ATOM   1600  O  OD1    . ASN A 1 242 ? 32.80600  -0.11500  42.04700  1.000 116.44000 ? 233 ASN A OD1    1 
ATOM   1601  N  ND2    . ASN A 1 242 ? 33.38100  2.04100   42.29700  1.000 113.93000 ? 233 ASN A ND2    1 
ATOM   1602  N  N      . VAL A 1 243 ? 28.45600  1.58900   40.12700  1.000 86.78000  ? 234 VAL A N      1 
ATOM   1603  C  CA     . VAL A 1 243 ? 27.11500  2.12300   39.90900  1.000 85.84000  ? 234 VAL A CA     1 
ATOM   1604  C  C      . VAL A 1 243 ? 26.07900  1.00900   39.82400  1.000 84.17000  ? 234 VAL A C      1 
ATOM   1605  O  O      . VAL A 1 243 ? 24.92200  1.19500   40.22000  1.000 77.41000  ? 234 VAL A O      1 
ATOM   1606  C  CB     . VAL A 1 243 ? 27.09700  2.99300   38.63800  1.000 75.88000  ? 234 VAL A CB     1 
ATOM   1607  C  CG1    . VAL A 1 243 ? 25.66900  3.35900   38.26400  1.000 75.53000  ? 234 VAL A CG1    1 
ATOM   1608  C  CG2    . VAL A 1 243 ? 27.95000  4.22900   38.83100  1.000 95.86000  ? 234 VAL A CG2    1 
ATOM   1609  N  N      . GLY A 1 244 ? 26.46200  -0.15700  39.31300  1.000 86.13000  ? 235 GLY A N      1 
ATOM   1610  C  CA     . GLY A 1 244 ? 25.47900  -1.19100  39.06100  1.000 74.40000  ? 235 GLY A CA     1 
ATOM   1611  C  C      . GLY A 1 244 ? 25.14900  -2.11400  40.21700  1.000 73.33000  ? 235 GLY A C      1 
ATOM   1612  O  O      . GLY A 1 244 ? 24.00000  -2.15000  40.66600  1.000 88.09000  ? 235 GLY A O      1 
ATOM   1613  N  N      . ASP A 1 245 ? 26.13200  -2.85500  40.72100  1.000 62.87000  ? 236 ASP A N      1 
ATOM   1614  C  CA     . ASP A 1 245 ? 25.84900  -3.88700  41.71100  1.000 80.34000  ? 236 ASP A CA     1 
ATOM   1615  C  C      . ASP A 1 245 ? 25.84600  -3.36600  43.14000  1.000 78.64000  ? 236 ASP A C      1 
ATOM   1616  O  O      . ASP A 1 245 ? 25.42800  -4.09300  44.04800  1.000 76.75000  ? 236 ASP A O      1 
ATOM   1617  C  CB     . ASP A 1 245 ? 26.84700  -5.04000  41.58100  1.000 93.41000  ? 236 ASP A CB     1 
ATOM   1618  C  CG     . ASP A 1 245 ? 26.60100  -5.87900  40.34800  1.000 113.90000 ? 236 ASP A CG     1 
ATOM   1619  O  OD1    . ASP A 1 245 ? 25.59600  -6.61900  40.32700  1.000 100.97000 ? 236 ASP A OD1    1 
ATOM   1620  O  OD2    . ASP A 1 245 ? 27.41200  -5.79900  39.40200  1.000 140.99000 ? 236 ASP A OD2    1 
ATOM   1621  N  N      . VAL A 1 246 ? 26.28100  -2.12900  43.36300  1.000 82.09000  ? 237 VAL A N      1 
ATOM   1622  C  CA     . VAL A 1 246 ? 26.24500  -1.54600  44.69700  1.000 79.13000  ? 237 VAL A CA     1 
ATOM   1623  C  C      . VAL A 1 246 ? 24.99400  -0.68800  44.82000  1.000 79.20000  ? 237 VAL A C      1 
ATOM   1624  O  O      . VAL A 1 246 ? 24.15300  -0.92000  45.69600  1.000 91.83000  ? 237 VAL A O      1 
ATOM   1625  C  CB     . VAL A 1 246 ? 27.51300  -0.72500  44.98900  1.000 78.16000  ? 237 VAL A CB     1 
ATOM   1626  C  CG1    . VAL A 1 246 ? 27.36400  0.03300   46.29600  1.000 76.04000  ? 237 VAL A CG1    1 
ATOM   1627  C  CG2    . VAL A 1 246 ? 28.72700  -1.63700  45.03800  1.000 92.30000  ? 237 VAL A CG2    1 
ATOM   1628  N  N      . ALA A 1 247 ? 24.86300  0.30800   43.94400  1.000 70.91000  ? 238 ALA A N      1 
ATOM   1629  C  CA     . ALA A 1 247 ? 23.71500  1.20600   44.00600  1.000 79.23000  ? 238 ALA A CA     1 
ATOM   1630  C  C      . ALA A 1 247 ? 22.47800  0.58800   43.35900  1.000 93.49000  ? 238 ALA A C      1 
ATOM   1631  O  O      . ALA A 1 247 ? 21.42600  0.47000   43.99500  1.000 96.14000  ? 238 ALA A O      1 
ATOM   1632  C  CB     . ALA A 1 247 ? 24.05900  2.54100   43.34000  1.000 95.27000  ? 238 ALA A CB     1 
ATOM   1633  N  N      . GLY A 1 248 ? 22.58800  0.18100   42.09300  1.000 86.38000  ? 239 GLY A N      1 
ATOM   1634  C  CA     . GLY A 1 248 ? 21.41200  -0.29300  41.37700  1.000 78.32000  ? 239 GLY A CA     1 
ATOM   1635  C  C      . GLY A 1 248 ? 20.80900  -1.55100  41.97400  1.000 66.81000  ? 239 GLY A C      1 
ATOM   1636  O  O      . GLY A 1 248 ? 19.61800  -1.59200  42.29200  1.000 74.74000  ? 239 GLY A O      1 
ATOM   1637  N  N      . LEU A 1 249 ? 21.62100  -2.59800  42.12800  1.000 62.61000  ? 240 LEU A N      1 
ATOM   1638  C  CA     . LEU A 1 249 ? 21.09100  -3.86000  42.63200  1.000 50.94000  ? 240 LEU A CA     1 
ATOM   1639  C  C      . LEU A 1 249 ? 20.61600  -3.72200  44.07300  1.000 63.74000  ? 240 LEU A C      1 
ATOM   1640  O  O      . LEU A 1 249 ? 19.58900  -4.29900  44.45500  1.000 75.86000  ? 240 LEU A O      1 
ATOM   1641  C  CB     . LEU A 1 249 ? 22.15000  -4.95300  42.51100  1.000 47.26000  ? 240 LEU A CB     1 
ATOM   1642  C  CG     . LEU A 1 249 ? 21.77200  -6.32200  43.06900  1.000 64.61000  ? 240 LEU A CG     1 
ATOM   1643  C  CD1    . LEU A 1 249 ? 20.46300  -6.79100  42.46100  1.000 84.15000  ? 240 LEU A CD1    1 
ATOM   1644  C  CD2    . LEU A 1 249 ? 22.88000  -7.31500  42.77700  1.000 82.49000  ? 240 LEU A CD2    1 
ATOM   1645  N  N      . GLY A 1 250 ? 21.35200  -2.96200  44.88600  1.000 65.57000  ? 241 GLY A N      1 
ATOM   1646  C  CA     . GLY A 1 250 ? 20.90800  -2.71500  46.24600  1.000 75.05000  ? 241 GLY A CA     1 
ATOM   1647  C  C      . GLY A 1 250 ? 19.57300  -2.00100  46.29300  1.000 76.94000  ? 241 GLY A C      1 
ATOM   1648  O  O      . GLY A 1 250 ? 18.68300  -2.37400  47.06300  1.000 87.82000  ? 241 GLY A O      1 
ATOM   1649  N  N      . ALA A 1 251 ? 19.40800  -0.97200  45.45900  1.000 59.08000  ? 242 ALA A N      1 
ATOM   1650  C  CA     . ALA A 1 251 ? 18.13800  -0.26000  45.40900  1.000 75.40000  ? 242 ALA A CA     1 
ATOM   1651  C  C      . ALA A 1 251 ? 17.01600  -1.17100  44.93000  1.000 72.50000  ? 242 ALA A C      1 
ATOM   1652  O  O      . ALA A 1 251 ? 15.88300  -1.07400  45.41100  1.000 69.62000  ? 242 ALA A O      1 
ATOM   1653  C  CB     . ALA A 1 251 ? 18.25800  0.96700   44.50500  1.000 74.88000  ? 242 ALA A CB     1 
ATOM   1654  N  N      . ASP A 1 252 ? 17.31500  -2.07900  43.99800  1.000 79.00000  ? 243 ASP A N      1 
ATOM   1655  C  CA     . ASP A 1 252 ? 16.28900  -2.99600  43.50400  1.000 73.39000  ? 243 ASP A CA     1 
ATOM   1656  C  C      . ASP A 1 252 ? 15.83100  -3.94600  44.60300  1.000 71.16000  ? 243 ASP A C      1 
ATOM   1657  O  O      . ASP A 1 252 ? 14.62600  -4.17000  44.79000  1.000 68.44000  ? 243 ASP A O      1 
ATOM   1658  C  CB     . ASP A 1 252 ? 16.81800  -3.77900  42.29800  1.000 76.27000  ? 243 ASP A CB     1 
ATOM   1659  C  CG     . ASP A 1 252 ? 15.78900  -4.75100  41.72700  1.000 76.06000  ? 243 ASP A CG     1 
ATOM   1660  O  OD1    . ASP A 1 252 ? 14.59900  -4.65900  42.09900  1.000 59.53000  ? 243 ASP A OD1    1 
ATOM   1661  O  OD2    . ASP A 1 252 ? 16.17300  -5.61000  40.90400  1.000 78.16000  ? 243 ASP A OD2    1 
ATOM   1662  N  N      . LEU A 1 253 ? 16.78300  -4.52400  45.33900  1.000 63.05000  ? 244 LEU A N      1 
ATOM   1663  C  CA     . LEU A 1 253 ? 16.41300  -5.40700  46.43900  1.000 61.08000  ? 244 LEU A CA     1 
ATOM   1664  C  C      . LEU A 1 253 ? 15.63700  -4.65000  47.51100  1.000 61.67000  ? 244 LEU A C      1 
ATOM   1665  O  O      . LEU A 1 253 ? 14.63700  -5.15400  48.04400  1.000 57.91000  ? 244 LEU A O      1 
ATOM   1666  C  CB     . LEU A 1 253 ? 17.66600  -6.05500  47.02700  1.000 63.18000  ? 244 LEU A CB     1 
ATOM   1667  C  CG     . LEU A 1 253 ? 18.31300  -7.12900  46.14800  1.000 49.89000  ? 244 LEU A CG     1 
ATOM   1668  C  CD1    . LEU A 1 253 ? 19.75100  -7.38100  46.57200  1.000 73.16000  ? 244 LEU A CD1    1 
ATOM   1669  C  CD2    . LEU A 1 253 ? 17.50600  -8.41700  46.18900  1.000 69.13000  ? 244 LEU A CD2    1 
ATOM   1670  N  N      . LEU A 1 254 ? 16.07400  -3.42600  47.82600  1.000 63.82000  ? 245 LEU A N      1 
ATOM   1671  C  CA     . LEU A 1 254 ? 15.33800  -2.59400  48.77200  1.000 86.32000  ? 245 LEU A CA     1 
ATOM   1672  C  C      . LEU A 1 254 ? 13.90600  -2.37700  48.30500  1.000 82.71000  ? 245 LEU A C      1 
ATOM   1673  O  O      . LEU A 1 254 ? 12.96000  -2.47900  49.09700  1.000 73.19000  ? 245 LEU A O      1 
ATOM   1674  C  CB     . LEU A 1 254 ? 16.05500  -1.25300  48.94900  1.000 82.51000  ? 245 LEU A CB     1 
ATOM   1675  C  CG     . LEU A 1 254 ? 15.62100  -0.33600  50.09700  1.000 86.70000  ? 245 LEU A CG     1 
ATOM   1676  C  CD1    . LEU A 1 254 ? 16.72000  0.66300   50.44700  1.000 87.00000  ? 245 LEU A CD1    1 
ATOM   1677  C  CD2    . LEU A 1 254 ? 14.33100  0.38900   49.75000  1.000 73.55000  ? 245 LEU A CD2    1 
ATOM   1678  N  N      . GLU A 1 255 ? 13.73200  -2.06800  47.02000  1.000 93.51000  ? 246 GLU A N      1 
ATOM   1679  C  CA     . GLU A 1 255 ? 12.40100  -1.82500  46.48400  1.000 78.56000  ? 246 GLU A CA     1 
ATOM   1680  C  C      . GLU A 1 255 ? 11.53000  -3.06500  46.59900  1.000 70.61000  ? 246 GLU A C      1 
ATOM   1681  O  O      . GLU A 1 255 ? 10.36600  -2.97400  46.99600  1.000 62.06000  ? 246 GLU A O      1 
ATOM   1682  C  CB     . GLU A 1 255 ? 12.49700  -1.37200  45.02900  1.000 84.39000  ? 246 GLU A CB     1 
ATOM   1683  C  CG     . GLU A 1 255 ? 11.17500  -0.92300  44.43800  1.000 91.89000  ? 246 GLU A CG     1 
ATOM   1684  C  CD     . GLU A 1 255 ? 11.14600  -1.03800  42.92900  1.000 118.20000 ? 246 GLU A CD     1 
ATOM   1685  O  OE1    . GLU A 1 255 ? 12.09000  -1.62700  42.35900  1.000 115.27000 ? 246 GLU A OE1    1 
ATOM   1686  O  OE2    . GLU A 1 255 ? 10.18300  -0.53700  42.31100  1.000 129.39000 ? 246 GLU A OE2    1 
ATOM   1687  N  N      . SER A 1 256 ? 12.07400  -4.23400  46.25800  1.000 77.56000  ? 247 SER A N      1 
ATOM   1688  C  CA     . SER A 1 256 ? 11.27500  -5.45400  46.34400  1.000 81.60000  ? 247 SER A CA     1 
ATOM   1689  C  C      . SER A 1 256 ? 10.85100  -5.73100  47.78200  1.000 78.06000  ? 247 SER A C      1 
ATOM   1690  O  O      . SER A 1 256 ? 9.69400   -6.08600  48.04400  1.000 62.64000  ? 247 SER A O      1 
ATOM   1691  C  CB     . SER A 1 256 ? 12.05600  -6.64100  45.77600  1.000 87.13000  ? 247 SER A CB     1 
ATOM   1692  O  OG     . SER A 1 256 ? 12.46100  -6.40400  44.43900  1.000 84.92000  ? 247 SER A OG     1 
ATOM   1693  N  N      . PHE A 1 257 ? 11.77500  -5.56500  48.73000  1.000 84.87000  ? 248 PHE A N      1 
ATOM   1694  C  CA     . PHE A 1 257 ? 11.46700  -5.82500  50.13400  1.000 92.85000  ? 248 PHE A CA     1 
ATOM   1695  C  C      . PHE A 1 257 ? 10.39700  -4.86100  50.65500  1.000 92.70000  ? 248 PHE A C      1 
ATOM   1696  O  O      . PHE A 1 257 ? 9.38500   -5.28100  51.24700  1.000 96.45000  ? 248 PHE A O      1 
ATOM   1697  C  CB     . PHE A 1 257 ? 12.77300  -5.74200  50.93100  1.000 87.67000  ? 248 PHE A CB     1 
ATOM   1698  C  CG     . PHE A 1 257 ? 12.61500  -5.32900  52.36100  1.000 104.21000 ? 248 PHE A CG     1 
ATOM   1699  C  CD1    . PHE A 1 257 ? 12.23900  -6.24800  53.32500  1.000 117.65000 ? 248 PHE A CD1    1 
ATOM   1700  C  CD2    . PHE A 1 257 ? 12.90200  -4.03200  52.75300  1.000 94.38000  ? 248 PHE A CD2    1 
ATOM   1701  C  CE1    . PHE A 1 257 ? 12.11800  -5.87200  54.64700  1.000 120.40000 ? 248 PHE A CE1    1 
ATOM   1702  C  CE2    . PHE A 1 257 ? 12.78300  -3.65000  54.07300  1.000 111.98000 ? 248 PHE A CE2    1 
ATOM   1703  C  CZ     . PHE A 1 257 ? 12.39200  -4.57100  55.02200  1.000 122.17000 ? 248 PHE A CZ     1 
ATOM   1704  N  N      . VAL A 1 258 ? 10.59300  -3.56200  50.41400  1.000 92.22000  ? 249 VAL A N      1 
ATOM   1705  C  CA     . VAL A 1 258 ? 9.59800   -2.56600  50.80400  1.000 92.06000  ? 249 VAL A CA     1 
ATOM   1706  C  C      . VAL A 1 258 ? 8.25500   -2.86300  50.14600  1.000 90.14000  ? 249 VAL A C      1 
ATOM   1707  O  O      . VAL A 1 258 ? 7.19700   -2.68700  50.76000  1.000 86.33000  ? 249 VAL A O      1 
ATOM   1708  C  CB     . VAL A 1 258 ? 10.09700  -1.15000  50.45800  1.000 99.12000  ? 249 VAL A CB     1 
ATOM   1709  C  CG1    . VAL A 1 258 ? 9.03300   -0.11100  50.79600  1.000 82.53000  ? 249 VAL A CG1    1 
ATOM   1710  C  CG2    . VAL A 1 258 ? 11.40200  -0.85800  51.18300  1.000 111.83000 ? 249 VAL A CG2    1 
ATOM   1711  N  N      . GLY A 1 259 ? 8.27400   -3.28900  48.88100  1.000 78.90000  ? 250 GLY A N      1 
ATOM   1712  C  CA     . GLY A 1 259 ? 7.03400   -3.59500  48.19200  1.000 63.41000  ? 250 GLY A CA     1 
ATOM   1713  C  C      . GLY A 1 259 ? 6.29600   -4.76300  48.81200  1.000 45.25000  ? 250 GLY A C      1 
ATOM   1714  O  O      . GLY A 1 259 ? 5.07300   -4.73700  48.93500  1.000 46.66000  ? 250 GLY A O      1 
ATOM   1715  N  N      . ALA A 1 260 ? 7.02700   -5.80600  49.20600  1.000 45.75000  ? 251 ALA A N      1 
ATOM   1716  C  CA     . ALA A 1 260 ? 6.38600   -6.91800  49.90200  1.000 62.05000  ? 251 ALA A CA     1 
ATOM   1717  C  C      . ALA A 1 260 ? 5.70200   -6.42900  51.17300  1.000 69.72000  ? 251 ALA A C      1 
ATOM   1718  O  O      . ALA A 1 260 ? 4.53600   -6.76500  51.44600  1.000 68.08000  ? 251 ALA A O      1 
ATOM   1719  C  CB     . ALA A 1 260 ? 7.41300   -8.00700  50.22300  1.000 61.53000  ? 251 ALA A CB     1 
ATOM   1720  N  N      . ILE A 1 261 ? 6.41500   -5.62000  51.96300  1.000 73.04000  ? 252 ILE A N      1 
ATOM   1721  C  CA     . ILE A 1 261 ? 5.82500   -5.11100  53.20200  1.000 71.33000  ? 252 ILE A CA     1 
ATOM   1722  C  C      . ILE A 1 261 ? 4.58100   -4.27800  52.90600  1.000 61.91000  ? 252 ILE A C      1 
ATOM   1723  O  O      . ILE A 1 261 ? 3.53900   -4.42300  53.56500  1.000 59.19000  ? 252 ILE A O      1 
ATOM   1724  C  CB     . ILE A 1 261 ? 6.86600   -4.30500  53.99800  1.000 68.46000  ? 252 ILE A CB     1 
ATOM   1725  C  CG1    . ILE A 1 261 ? 8.06300   -5.18800  54.35000  1.000 73.52000  ? 252 ILE A CG1    1 
ATOM   1726  C  CG2    . ILE A 1 261 ? 6.23500   -3.72200  55.25100  1.000 90.42000  ? 252 ILE A CG2    1 
ATOM   1727  C  CD1    . ILE A 1 261 ? 9.21900   -4.42700  54.93500  1.000 71.87000  ? 252 ILE A CD1    1 
ATOM   1728  N  N      . VAL A 1 262 ? 4.66800   -3.39600  51.90900  1.000 52.94000  ? 253 VAL A N      1 
ATOM   1729  C  CA     . VAL A 1 262 ? 3.54600   -2.52200  51.59200  1.000 55.17000  ? 253 VAL A CA     1 
ATOM   1730  C  C      . VAL A 1 262 ? 2.36800   -3.33000  51.07300  1.000 56.26000  ? 253 VAL A C      1 
ATOM   1731  O  O      . VAL A 1 262 ? 1.21100   -2.98500  51.33100  1.000 54.59000  ? 253 VAL A O      1 
ATOM   1732  C  CB     . VAL A 1 262 ? 3.97500   -1.44400  50.57900  1.000 49.24000  ? 253 VAL A CB     1 
ATOM   1733  C  CG1    . VAL A 1 262 ? 2.75700   -0.70800  50.03600  1.000 38.88000  ? 253 VAL A CG1    1 
ATOM   1734  C  CG2    . VAL A 1 262 ? 4.95500   -0.47200  51.21700  1.000 65.35000  ? 253 VAL A CG2    1 
ATOM   1735  N  N      . SER A 1 263 ? 2.63300   -4.41200  50.34200  1.000 53.46000  ? 254 SER A N      1 
ATOM   1736  C  CA     . SER A 1 263 ? 1.54900   -5.26500  49.87500  1.000 52.61000  ? 254 SER A CA     1 
ATOM   1737  C  C      . SER A 1 263 ? 0.83700   -5.91700  51.04600  1.000 58.84000  ? 254 SER A C      1 
ATOM   1738  O  O      . SER A 1 263 ? -0.39900  -5.94700  51.09300  1.000 71.14000  ? 254 SER A O      1 
ATOM   1739  C  CB     . SER A 1 263 ? 2.08700   -6.32600  48.91500  1.000 58.54000  ? 254 SER A CB     1 
ATOM   1740  O  OG     . SER A 1 263 ? 2.65900   -5.73100  47.76400  1.000 63.73000  ? 254 SER A OG     1 
ATOM   1741  N  N      . SER A 1 264 ? 1.59900   -6.43800  52.00800  1.000 48.46000  ? 255 SER A N      1 
ATOM   1742  C  CA     . SER A 1 264 ? 0.97200   -6.99200  53.20400  1.000 59.76000  ? 255 SER A CA     1 
ATOM   1743  C  C      . SER A 1 264 ? 0.09500   -5.94800  53.89300  1.000 66.83000  ? 255 SER A C      1 
ATOM   1744  O  O      . SER A 1 264 ? -1.05900  -6.22100  54.26000  1.000 62.10000  ? 255 SER A O      1 
ATOM   1745  C  CB     . SER A 1 264 ? 2.04400   -7.51700  54.15800  1.000 80.43000  ? 255 SER A CB     1 
ATOM   1746  O  OG     . SER A 1 264 ? 2.79100   -8.55800  53.55300  1.000 85.89000  ? 255 SER A OG     1 
ATOM   1747  N  N      . ILE A 1 265 ? 0.62300   -4.73200  54.05000  1.000 68.38000  ? 256 ILE A N      1 
ATOM   1748  C  CA     . ILE A 1 265 ? -0.11000  -3.69800  54.77700  1.000 67.47000  ? 256 ILE A CA     1 
ATOM   1749  C  C      . ILE A 1 265 ? -1.37800  -3.29800  54.03000  1.000 68.66000  ? 256 ILE A C      1 
ATOM   1750  O  O      . ILE A 1 265 ? -2.45000  -3.15700  54.63200  1.000 87.49000  ? 256 ILE A O      1 
ATOM   1751  C  CB     . ILE A 1 265 ? 0.80000   -2.48600  55.03700  1.000 79.37000  ? 256 ILE A CB     1 
ATOM   1752  C  CG1    . ILE A 1 265 ? 1.85100   -2.83200  56.09300  1.000 90.54000  ? 256 ILE A CG1    1 
ATOM   1753  C  CG2    . ILE A 1 265 ? -0.02400  -1.27800  55.45900  1.000 76.68000  ? 256 ILE A CG2    1 
ATOM   1754  C  CD1    . ILE A 1 265 ? 2.88100   -1.74900  56.30300  1.000 94.29000  ? 256 ILE A CD1    1 
ATOM   1755  N  N      . ILE A 1 266 ? -1.27600  -3.09200  52.71500  1.000 61.16000  ? 257 ILE A N      1 
ATOM   1756  C  CA     . ILE A 1 266 ? -2.44800  -2.74700  51.91700  1.000 69.41000  ? 257 ILE A CA     1 
ATOM   1757  C  C      . ILE A 1 266 ? -3.48800  -3.85200  52.00100  1.000 54.12000  ? 257 ILE A C      1 
ATOM   1758  O  O      . ILE A 1 266 ? -4.69100  -3.58900  52.14500  1.000 58.05000  ? 257 ILE A O      1 
ATOM   1759  C  CB     . ILE A 1 266 ? -2.04500  -2.47200  50.45800  1.000 70.42000  ? 257 ILE A CB     1 
ATOM   1760  C  CG1    . ILE A 1 266 ? -1.17600  -1.21900  50.36900  1.000 82.71000  ? 257 ILE A CG1    1 
ATOM   1761  C  CG2    . ILE A 1 266 ? -3.28400  -2.32800  49.58600  1.000 67.37000  ? 257 ILE A CG2    1 
ATOM   1762  C  CD1    . ILE A 1 266 ? -0.61300  -0.97800  48.99100  1.000 79.30000  ? 257 ILE A CD1    1 
ATOM   1763  N  N      . LEU A 1 267 ? -3.04800  -5.10600  51.89000  1.000 44.80000  ? 258 LEU A N      1 
ATOM   1764  C  CA     . LEU A 1 267 ? -3.98400  -6.21700  51.95500  1.000 58.60000  ? 258 LEU A CA     1 
ATOM   1765  C  C      . LEU A 1 267 ? -4.75000  -6.19600  53.26800  1.000 61.96000  ? 258 LEU A C      1 
ATOM   1766  O  O      . LEU A 1 267 ? -5.97100  -6.36400  53.28500  1.000 68.64000  ? 258 LEU A O      1 
ATOM   1767  C  CB     . LEU A 1 267 ? -3.24300  -7.54100  51.76800  1.000 76.25000  ? 258 LEU A CB     1 
ATOM   1768  C  CG     . LEU A 1 267 ? -2.75100  -7.82000  50.34500  1.000 57.06000  ? 258 LEU A CG     1 
ATOM   1769  C  CD1    . LEU A 1 267 ? -1.79700  -9.00200  50.32900  1.000 61.50000  ? 258 LEU A CD1    1 
ATOM   1770  C  CD2    . LEU A 1 267 ? -3.92400  -8.05600  49.40300  1.000 59.30000  ? 258 LEU A CD2    1 
ATOM   1771  N  N      . ALA A 1 268 ? -4.05000  -5.97300  54.38300  1.000 56.24000  ? 259 ALA A N      1 
ATOM   1772  C  CA     . ALA A 1 268 ? -4.73900  -5.90700  55.67300  1.000 68.50000  ? 259 ALA A CA     1 
ATOM   1773  C  C      . ALA A 1 268 ? -5.72000  -4.73600  55.71900  1.000 67.82000  ? 259 ALA A C      1 
ATOM   1774  O  O      . ALA A 1 268 ? -6.88300  -4.88600  56.13600  1.000 74.17000  ? 259 ALA A O      1 
ATOM   1775  C  CB     . ALA A 1 268 ? -3.71800  -5.80300  56.80600  1.000 81.13000  ? 259 ALA A CB     1 
ATOM   1776  N  N      . SER A 1 269 ? -5.25800  -3.55100  55.31100  1.000 60.04000  ? 260 SER A N      1 
ATOM   1777  C  CA     . SER A 1 269 ? -6.09300  -2.35700  55.39000  1.000 72.37000  ? 260 SER A CA     1 
ATOM   1778  C  C      . SER A 1 269 ? -7.38200  -2.52600  54.60100  1.000 81.35000  ? 260 SER A C      1 
ATOM   1779  O  O      . SER A 1 269 ? -8.45200  -2.09300  55.04500  1.000 85.94000  ? 260 SER A O      1 
ATOM   1780  C  CB     . SER A 1 269 ? -5.31700  -1.14100  54.88900  1.000 73.13000  ? 260 SER A CB     1 
ATOM   1781  O  OG     . SER A 1 269 ? -4.08700  -1.00400  55.57600  1.000 85.60000  ? 260 SER A OG     1 
ATOM   1782  N  N      . TYR A 1 270 ? -7.30300  -3.14200  53.42100  1.000 81.28000  ? 261 TYR A N      1 
ATOM   1783  C  CA     . TYR A 1 270 ? -8.49800  -3.32800  52.60700  1.000 79.50000  ? 261 TYR A CA     1 
ATOM   1784  C  C      . TYR A 1 270 ? -9.29000  -4.57800  52.96000  1.000 78.20000  ? 261 TYR A C      1 
ATOM   1785  O  O      . TYR A 1 270 ? -10.48100 -4.64300  52.64000  1.000 77.57000  ? 261 TYR A O      1 
ATOM   1786  C  CB     . TYR A 1 270 ? -8.13300  -3.36000  51.12000  1.000 68.12000  ? 261 TYR A CB     1 
ATOM   1787  C  CG     . TYR A 1 270 ? -7.90600  -1.98500  50.53500  1.000 66.13000  ? 261 TYR A CG     1 
ATOM   1788  C  CD1    . TYR A 1 270 ? -8.96000  -1.09500  50.39800  1.000 65.40000  ? 261 TYR A CD1    1 
ATOM   1789  C  CD2    . TYR A 1 270 ? -6.64400  -1.57600  50.12100  1.000 73.84000  ? 261 TYR A CD2    1 
ATOM   1790  C  CE1    . TYR A 1 270 ? -8.76900  0.16400   49.86900  1.000 66.35000  ? 261 TYR A CE1    1 
ATOM   1791  C  CE2    . TYR A 1 270 ? -6.44300  -0.31700  49.58800  1.000 77.86000  ? 261 TYR A CE2    1 
ATOM   1792  C  CZ     . TYR A 1 270 ? -7.51100  0.54900   49.46400  1.000 72.43000  ? 261 TYR A CZ     1 
ATOM   1793  O  OH     . TYR A 1 270 ? -7.32500  1.80600   48.93500  1.000 70.49000  ? 261 TYR A OH     1 
ATOM   1794  N  N      . MET A 1 271 ? -8.67800  -5.56200  53.62300  1.000 82.37000  ? 262 MET A N      1 
ATOM   1795  C  CA     . MET A 1 271 ? -9.44900  -6.68100  54.14500  1.000 90.79000  ? 262 MET A CA     1 
ATOM   1796  C  C      . MET A 1 271 ? -10.28600 -6.26700  55.34100  1.000 96.24000  ? 262 MET A C      1 
ATOM   1797  O  O      . MET A 1 271 ? -11.29300 -6.92000  55.63900  1.000 97.51000  ? 262 MET A O      1 
ATOM   1798  C  CB     . MET A 1 271 ? -8.51900  -7.83600  54.52500  1.000 106.00000 ? 262 MET A CB     1 
ATOM   1799  C  CG     . MET A 1 271 ? -7.79400  -8.46600  53.34400  1.000 93.17000  ? 262 MET A CG     1 
ATOM   1800  S  SD     . MET A 1 271 ? -6.73700  -9.84000  53.84000  1.000 112.65000 ? 262 MET A SD     1 
ATOM   1801  C  CE     . MET A 1 271 ? -7.94700  -11.13800 54.09200  1.000 128.20000 ? 262 MET A CE     1 
ATOM   1802  N  N      . PHE A 1 272 ? -9.90300  -5.18900  56.02300  1.000 89.79000  ? 263 PHE A N      1 
ATOM   1803  C  CA     . PHE A 1 272 ? -10.79200 -4.66400  57.05700  1.000 100.26000 ? 263 PHE A CA     1 
ATOM   1804  C  C      . PHE A 1 272 ? -12.16300 -4.29700  56.50500  1.000 96.73000  ? 263 PHE A C      1 
ATOM   1805  O  O      . PHE A 1 272 ? -13.17300 -4.79800  57.03000  1.000 91.45000  ? 263 PHE A O      1 
ATOM   1806  C  CB     . PHE A 1 272 ? -10.15900 -3.45700  57.75300  1.000 100.83000 ? 263 PHE A CB     1 
ATOM   1807  C  CG     . PHE A 1 272 ? -11.07800 -2.79200  58.74300  1.000 108.34000 ? 263 PHE A CG     1 
ATOM   1808  C  CD1    . PHE A 1 272 ? -11.23600 -3.30600  60.01900  1.000 104.87000 ? 263 PHE A CD1    1 
ATOM   1809  C  CD2    . PHE A 1 272 ? -11.80000 -1.66400  58.38800  1.000 106.80000 ? 263 PHE A CD2    1 
ATOM   1810  C  CE1    . PHE A 1 272 ? -12.08700 -2.69900  60.92700  1.000 107.72000 ? 263 PHE A CE1    1 
ATOM   1811  C  CE2    . PHE A 1 272 ? -12.65000 -1.05200  59.29000  1.000 104.96000 ? 263 PHE A CE2    1 
ATOM   1812  C  CZ     . PHE A 1 272 ? -12.79400 -1.56900  60.56000  1.000 110.47000 ? 263 PHE A CZ     1 
ATOM   1813  N  N      . PRO A 1 273 ? -12.28000 -3.45800  55.47500  1.000 88.15000  ? 264 PRO A N      1 
ATOM   1814  C  CA     . PRO A 1 273 ? -13.60800 -3.02800  55.01200  1.000 92.14000  ? 264 PRO A CA     1 
ATOM   1815  C  C      . PRO A 1 273 ? -14.31800 -4.03700  54.11900  1.000 93.87000  ? 264 PRO A C      1 
ATOM   1816  O  O      . PRO A 1 273 ? -15.55200 -4.05600  54.07100  1.000 92.58000  ? 264 PRO A O      1 
ATOM   1817  C  CB     . PRO A 1 273 ? -13.30500 -1.73300  54.24100  1.000 93.02000  ? 264 PRO A CB     1 
ATOM   1818  C  CG     . PRO A 1 273 ? -11.86700 -1.38200  54.57600  1.000 80.43000  ? 264 PRO A CG     1 
ATOM   1819  C  CD     . PRO A 1 273 ? -11.20400 -2.68500  54.84000  1.000 72.82000  ? 264 PRO A CD     1 
ATOM   1820  N  N      . ILE A 1 274 ? -13.55900 -4.88600  53.42000  1.000 107.90000 ? 265 ILE A N      1 
ATOM   1821  C  CA     . ILE A 1 274 ? -14.16300 -5.78100  52.43300  1.000 104.24000 ? 265 ILE A CA     1 
ATOM   1822  C  C      . ILE A 1 274 ? -15.01400 -6.85300  53.09900  1.000 94.48000  ? 265 ILE A C      1 
ATOM   1823  O  O      . ILE A 1 274 ? -16.00800 -7.31100  52.52300  1.000 89.10000  ? 265 ILE A O      1 
ATOM   1824  C  CB     . ILE A 1 274 ? -13.08000 -6.41300  51.53500  1.000 93.05000  ? 265 ILE A CB     1 
ATOM   1825  C  CG1    . ILE A 1 274 ? -12.10100 -7.24600  52.36900  1.000 92.43000  ? 265 ILE A CG1    1 
ATOM   1826  C  CG2    . ILE A 1 274 ? -12.36600 -5.34900  50.71400  1.000 96.62000  ? 265 ILE A CG2    1 
ATOM   1827  C  CD1    . ILE A 1 274 ? -11.15800 -8.09300  51.53900  1.000 81.66000  ? 265 ILE A CD1    1 
ATOM   1828  N  N      . TYR A 1 275 ? -14.65000 -7.27300  54.30800  1.000 91.92000  ? 266 TYR A N      1 
ATOM   1829  C  CA     . TYR A 1 275 ? -15.38300 -8.31600  55.02100  1.000 87.25000  ? 266 TYR A CA     1 
ATOM   1830  C  C      . TYR A 1 275 ? -16.35700 -7.65100  55.98800  1.000 111.08000 ? 266 TYR A C      1 
ATOM   1831  O  O      . TYR A 1 275 ? -16.07600 -7.45100  57.16900  1.000 125.51000 ? 266 TYR A O      1 
ATOM   1832  C  CB     . TYR A 1 275 ? -14.42300 -9.26600  55.72400  1.000 96.59000  ? 266 TYR A CB     1 
ATOM   1833  C  CG     . TYR A 1 275 ? -13.55000 -10.03500 54.76400  1.000 87.74000  ? 266 TYR A CG     1 
ATOM   1834  C  CD1    . TYR A 1 275 ? -14.10400 -10.71500 53.68600  1.000 89.71000  ? 266 TYR A CD1    1 
ATOM   1835  C  CD2    . TYR A 1 275 ? -12.17300 -10.07700 54.92700  1.000 85.96000  ? 266 TYR A CD2    1 
ATOM   1836  C  CE1    . TYR A 1 275 ? -13.31200 -11.41800 52.80100  1.000 96.79000  ? 266 TYR A CE1    1 
ATOM   1837  C  CE2    . TYR A 1 275 ? -11.37200 -10.77900 54.04700  1.000 92.87000  ? 266 TYR A CE2    1 
ATOM   1838  C  CZ     . TYR A 1 275 ? -11.94600 -11.44700 52.98600  1.000 91.93000  ? 266 TYR A CZ     1 
ATOM   1839  O  OH     . TYR A 1 275 ? -11.15400 -12.14700 52.10600  1.000 98.06000  ? 266 TYR A OH     1 
ATOM   1840  N  N      . VAL A 1 276 ? -17.52300 -7.29000  55.45500  1.000 112.62000 ? 267 VAL A N      1 
ATOM   1841  C  CA     . VAL A 1 276 ? -18.59900 -6.71000  56.24600  1.000 102.53000 ? 267 VAL A CA     1 
ATOM   1842  C  C      . VAL A 1 276 ? -19.89300 -7.42700  55.89000  1.000 99.25000  ? 267 VAL A C      1 
ATOM   1843  O  O      . VAL A 1 276 ? -20.05900 -7.93900  54.77800  1.000 108.38000 ? 267 VAL A O      1 
ATOM   1844  C  CB     . VAL A 1 276 ? -18.73300 -5.18800  56.01400  1.000 96.84000  ? 267 VAL A CB     1 
ATOM   1845  C  CG1    . VAL A 1 276 ? -17.48300 -4.46500  56.49500  1.000 115.44000 ? 267 VAL A CG1    1 
ATOM   1846  C  CG2    . VAL A 1 276 ? -18.99600 -4.89300  54.54600  1.000 85.89000  ? 267 VAL A CG2    1 
ATOM   1847  N  N      . GLN A 1 277 ? -20.81400 -7.45900  56.85000  1.000 113.48000 ? 268 GLN A N      1 
ATOM   1848  C  CA     . GLN A 1 277 ? -22.07200 -8.18300  56.71100  1.000 122.37000 ? 268 GLN A CA     1 
ATOM   1849  C  C      . GLN A 1 277 ? -23.18700 -7.40200  57.38600  1.000 141.24000 ? 268 GLN A C      1 
ATOM   1850  O  O      . GLN A 1 277 ? -23.03200 -6.97100  58.53000  1.000 146.17000 ? 268 GLN A O      1 
ATOM   1851  C  CB     . GLN A 1 277 ? -21.97600 -9.59000  57.31600  1.000 110.82000 ? 268 GLN A CB     1 
ATOM   1852  N  N      . LYS A 1 278 ? -24.30500 -7.21300  56.68900  1.000 150.06000 ? 269 LYS A N      1 
ATOM   1853  C  CA     . LYS A 1 278 ? -25.43300 -6.52400  57.30200  1.000 147.80000 ? 269 LYS A CA     1 
ATOM   1854  C  C      . LYS A 1 278 ? -26.29900 -7.46700  58.12900  1.000 146.06000 ? 269 LYS A C      1 
ATOM   1855  O  O      . LYS A 1 278 ? -27.37400 -7.06800  58.59000  1.000 135.59000 ? 269 LYS A O      1 
ATOM   1856  C  CB     . LYS A 1 278 ? -26.28400 -5.83200  56.23100  1.000 137.85000 ? 269 LYS A CB     1 
ATOM   1857  C  CG     . LYS A 1 278 ? -27.39500 -4.94100  56.78300  1.000 131.37000 ? 269 LYS A CG     1 
ATOM   1858  C  CD     . LYS A 1 278 ? -26.84100 -3.77000  57.58200  1.000 139.16000 ? 269 LYS A CD     1 
ATOM   1859  C  CE     . LYS A 1 278 ? -27.96100 -2.96900  58.22900  1.000 139.43000 ? 269 LYS A CE     1 
ATOM   1860  N  NZ     . LYS A 1 278 ? -27.43700 -1.84700  59.05500  1.000 117.33000 ? 269 LYS A NZ     1 
ATOM   1861  N  N      . ILE A 1 279 ? -25.83900 -8.70500  58.32900  1.000 144.13000 ? 270 ILE A N      1 
ATOM   1862  C  CA     . ILE A 1 279 ? -26.51000 -9.60600  59.24900  1.000 151.67000 ? 270 ILE A CA     1 
ATOM   1863  C  C      . ILE A 1 279 ? -26.43900 -9.02700  60.65900  1.000 165.39000 ? 270 ILE A C      1 
ATOM   1864  O  O      . ILE A 1 279 ? -25.66000 -8.11000  60.95200  1.000 162.99000 ? 270 ILE A O      1 
ATOM   1865  C  CB     . ILE A 1 279 ? -25.89300 -11.01200 59.19800  1.000 154.24000 ? 270 ILE A CB     1 
ATOM   1866  C  CG1    . ILE A 1 279 ? -26.79500 -12.02400 59.91100  1.000 152.75000 ? 270 ILE A CG1    1 
ATOM   1867  C  CG2    . ILE A 1 279 ? -24.49600 -10.99900 59.80500  1.000 157.96000 ? 270 ILE A CG2    1 
ATOM   1868  C  CD1    . ILE A 1 279 ? -28.23100 -12.01100 59.43400  1.000 153.51000 ? 270 ILE A CD1    1 
ATOM   1869  N  N      . GLY A 1 280 ? -27.25200 -9.58600  61.54900  1.000 176.03000 ? 271 GLY A N      1 
ATOM   1870  C  CA     . GLY A 1 280 ? -27.30300 -9.06700  62.89700  1.000 167.96000 ? 271 GLY A CA     1 
ATOM   1871  C  C      . GLY A 1 280 ? -28.00100 -7.73400  63.02300  1.000 171.33000 ? 271 GLY A C      1 
ATOM   1872  O  O      . GLY A 1 280 ? -27.99700 -7.15000  64.11100  1.000 166.26000 ? 271 GLY A O      1 
ATOM   1873  N  N      . GLU A 1 281 ? -28.59000 -7.22900  61.93600  1.000 173.09000 ? 272 GLU A N      1 
ATOM   1874  C  CA     . GLU A 1 281 ? -29.40300 -6.01700  61.92100  1.000 167.05000 ? 272 GLU A CA     1 
ATOM   1875  C  C      . GLU A 1 281 ? -28.57100 -4.74500  61.90400  1.000 163.35000 ? 272 GLU A C      1 
ATOM   1876  O  O      . GLU A 1 281 ? -29.04700 -3.68400  62.31900  1.000 168.46000 ? 272 GLU A O      1 
ATOM   1877  C  CB     . GLU A 1 281 ? -30.36200 -5.96800  63.11100  1.000 164.32000 ? 272 GLU A CB     1 
ATOM   1878  C  CG     . GLU A 1 281 ? -31.68800 -6.67000  62.89200  1.000 189.29000 ? 272 GLU A CG     1 
ATOM   1879  C  CD     . GLU A 1 281 ? -31.53900 -8.13300  62.51000  1.000 198.06000 ? 272 GLU A CD     1 
ATOM   1880  O  OE1    . GLU A 1 281 ? -32.25000 -8.57700  61.58300  1.000 201.34000 ? 272 GLU A OE1    1 
ATOM   1881  O  OE2    . GLU A 1 281 ? -30.72300 -8.84100  63.13800  1.000 201.42000 ? 272 GLU A OE2    1 
ATOM   1882  N  N      . ASN A 1 282 ? -27.33000 -4.82700  61.44300  1.000 156.55000 ? 273 ASN A N      1 
ATOM   1883  C  CA     . ASN A 1 282 ? -26.46500 -3.66300  61.35700  1.000 155.16000 ? 273 ASN A CA     1 
ATOM   1884  C  C      . ASN A 1 282 ? -25.16000 -4.11200  60.71700  1.000 160.02000 ? 273 ASN A C      1 
ATOM   1885  O  O      . ASN A 1 282 ? -24.77500 -5.28500  60.80800  1.000 155.81000 ? 273 ASN A O      1 
ATOM   1886  C  CB     . ASN A 1 282 ? -26.21300 -3.03200  62.73900  1.000 153.89000 ? 273 ASN A CB     1 
ATOM   1887  C  CG     . ASN A 1 282 ? -26.20100 -1.50600  62.70600  1.000 152.72000 ? 273 ASN A CG     1 
ATOM   1888  O  OD1    . ASN A 1 282 ? -26.45800 -0.88500  61.67300  1.000 148.62000 ? 273 ASN A OD1    1 
ATOM   1889  N  ND2    . ASN A 1 282 ? -25.87200 -0.89900  63.84200  1.000 157.62000 ? 273 ASN A ND2    1 
ATOM   1890  N  N      . LEU A 1 283 ? -24.49900 -3.16600  60.05700  1.000 157.37000 ? 274 LEU A N      1 
ATOM   1891  C  CA     . LEU A 1 283 ? -23.22900 -3.42700  59.39900  1.000 129.31000 ? 274 LEU A CA     1 
ATOM   1892  C  C      . LEU A 1 283 ? -22.18200 -3.87800  60.40500  1.000 114.04000 ? 274 LEU A C      1 
ATOM   1893  O  O      . LEU A 1 283 ? -21.76000 -3.10300  61.26900  1.000 113.11000 ? 274 LEU A O      1 
ATOM   1894  C  CB     . LEU A 1 283 ? -22.73600 -2.17500  58.67500  1.000 127.50000 ? 274 LEU A CB     1 
ATOM   1895  C  CG     . LEU A 1 283 ? -23.16600 -1.96500  57.22800  1.000 113.65000 ? 274 LEU A CG     1 
ATOM   1896  C  CD1    . LEU A 1 283 ? -22.55900 -0.67600  56.66400  1.000 79.08000  ? 274 LEU A CD1    1 
ATOM   1897  C  CD2    . LEU A 1 283 ? -22.77200 -3.16900  56.39400  1.000 121.95000 ? 274 LEU A CD2    1 
ATOM   1898  N  N      . VAL A 1 284 ? -21.75600 -5.13000  60.28500  1.000 118.87000 ? 275 VAL A N      1 
ATOM   1899  C  CA     . VAL A 1 284 ? -20.81700 -5.76600  61.19400  1.000 141.31000 ? 275 VAL A CA     1 
ATOM   1900  C  C      . VAL A 1 284 ? -19.54000 -6.05400  60.42400  1.000 138.25000 ? 275 VAL A C      1 
ATOM   1901  O  O      . VAL A 1 284 ? -19.57300 -6.75500  59.40300  1.000 127.83000 ? 275 VAL A O      1 
ATOM   1902  C  CB     . VAL A 1 284 ? -21.40700 -7.05400  61.78400  1.000 138.41000 ? 275 VAL A CB     1 
ATOM   1903  C  CG1    . VAL A 1 284 ? -20.31100 -7.93900  62.32400  1.000 131.73000 ? 275 VAL A CG1    1 
ATOM   1904  C  CG2    . VAL A 1 284 ? -22.42500 -6.71600  62.86500  1.000 146.29000 ? 275 VAL A CG2    1 
ATOM   1905  N  N      . HIS A 1 285 ? -18.42800 -5.48800  60.88400  1.000 136.86000 ? 276 HIS A N      1 
ATOM   1906  C  CA     . HIS A 1 285 ? -17.13300 -5.80700  60.30200  1.000 130.59000 ? 276 HIS A CA     1 
ATOM   1907  C  C      . HIS A 1 285 ? -16.76000 -7.23300  60.68900  1.000 140.34000 ? 276 HIS A C      1 
ATOM   1908  O  O      . HIS A 1 285 ? -16.59200 -7.53900  61.87500  1.000 137.22000 ? 276 HIS A O      1 
ATOM   1909  C  CB     . HIS A 1 285 ? -16.07200 -4.82000  60.78000  1.000 126.98000 ? 276 HIS A CB     1 
ATOM   1910  C  CG     . HIS A 1 285 ? -15.98900 -3.57300  59.95500  1.000 123.65000 ? 276 HIS A CG     1 
ATOM   1911  N  ND1    . HIS A 1 285 ? -16.66400 -2.41600  60.28000  1.000 131.57000 ? 276 HIS A ND1    1 
ATOM   1912  C  CD2    . HIS A 1 285 ? -15.30500 -3.30300  58.81800  1.000 115.59000 ? 276 HIS A CD2    1 
ATOM   1913  C  CE1    . HIS A 1 285 ? -16.39800 -1.48700  59.37900  1.000 131.21000 ? 276 HIS A CE1    1 
ATOM   1914  N  NE2    . HIS A 1 285 ? -15.57700 -2.00000  58.48100  1.000 118.98000 ? 276 HIS A NE2    1 
ATOM   1915  N  N      . GLN A 1 286 ? -16.63500 -8.10800  59.68900  1.000 143.52000 ? 277 GLN A N      1 
ATOM   1916  C  CA     . GLN A 1 286 ? -16.34400 -9.51300  59.95900  1.000 139.64000 ? 277 GLN A CA     1 
ATOM   1917  C  C      . GLN A 1 286 ? -14.92600 -9.72000  60.48300  1.000 139.57000 ? 277 GLN A C      1 
ATOM   1918  O  O      . GLN A 1 286 ? -14.68300 -10.66100 61.24800  1.000 137.20000 ? 277 GLN A O      1 
ATOM   1919  C  CB     . GLN A 1 286 ? -16.58200 -10.33900 58.69600  1.000 121.66000 ? 277 GLN A CB     1 
ATOM   1920  C  CG     . GLN A 1 286 ? -18.04400 -10.36900 58.26500  1.000 109.50000 ? 277 GLN A CG     1 
ATOM   1921  C  CD     . GLN A 1 286 ? -18.26200 -11.11600 56.96500  1.000 109.14000 ? 277 GLN A CD     1 
ATOM   1922  O  OE1    . GLN A 1 286 ? -17.46400 -11.00900 56.03300  1.000 102.56000 ? 277 GLN A OE1    1 
ATOM   1923  N  NE2    . GLN A 1 286 ? -19.35200 -11.87400 56.89400  1.000 107.17000 ? 277 GLN A NE2    1 
ATOM   1924  N  N      . VAL A 1 287 ? -13.98700 -8.87100  60.08900  1.000 138.23000 ? 278 VAL A N      1 
ATOM   1925  C  CA     . VAL A 1 287 ? -12.62100 -8.88500  60.60400  1.000 131.93000 ? 278 VAL A CA     1 
ATOM   1926  C  C      . VAL A 1 287 ? -12.46100 -7.68600  61.53200  1.000 135.83000 ? 278 VAL A C      1 
ATOM   1927  O  O      . VAL A 1 287 ? -12.54100 -6.54000  61.06900  1.000 134.08000 ? 278 VAL A O      1 
ATOM   1928  C  CB     . VAL A 1 287 ? -11.58400 -8.85300  59.47100  1.000 132.59000 ? 278 VAL A CB     1 
ATOM   1929  C  CG1    . VAL A 1 287 ? -10.17900 -9.01200  60.03600  1.000 126.34000 ? 278 VAL A CG1    1 
ATOM   1930  C  CG2    . VAL A 1 287 ? -11.88000 -9.94500  58.45400  1.000 124.47000 ? 278 VAL A CG2    1 
ATOM   1931  N  N      . PRO A 1 288 ? -12.23300 -7.89100  62.82900  1.000 126.63000 ? 279 PRO A N      1 
ATOM   1932  C  CA     . PRO A 1 288 ? -12.20400 -6.75600  63.75800  1.000 115.53000 ? 279 PRO A CA     1 
ATOM   1933  C  C      . PRO A 1 288 ? -11.09000 -5.77800  63.41900  1.000 110.23000 ? 279 PRO A C      1 
ATOM   1934  O  O      . PRO A 1 288 ? -10.07500 -6.12700  62.81300  1.000 117.08000 ? 279 PRO A O      1 
ATOM   1935  C  CB     . PRO A 1 288 ? -11.96500 -7.41500  65.12400  1.000 111.50000 ? 279 PRO A CB     1 
ATOM   1936  C  CG     . PRO A 1 288 ? -12.32700 -8.85400  64.93500  1.000 117.44000 ? 279 PRO A CG     1 
ATOM   1937  C  CD     . PRO A 1 288 ? -12.00100 -9.17400  63.51200  1.000 120.54000 ? 279 PRO A CD     1 
ATOM   1938  N  N      . LYS A 1 289 ? -11.29500 -4.52800  63.83900  1.000 103.85000 ? 280 LYS A N      1 
ATOM   1939  C  CA     . LYS A 1 289 ? -10.29900 -3.49400  63.58600  1.000 112.33000 ? 280 LYS A CA     1 
ATOM   1940  C  C      . LYS A 1 289 ? -8.98500  -3.79800  64.29300  1.000 114.79000 ? 280 LYS A C      1 
ATOM   1941  O  O      . LYS A 1 289 ? -7.91200  -3.45300  63.78400  1.000 113.45000 ? 280 LYS A O      1 
ATOM   1942  C  CB     . LYS A 1 289 ? -10.84200 -2.13300  64.02100  1.000 106.23000 ? 280 LYS A CB     1 
ATOM   1943  C  CG     . LYS A 1 289 ? -10.13700 -0.95000  63.38700  1.000 102.36000 ? 280 LYS A CG     1 
ATOM   1944  C  CD     . LYS A 1 289 ? -10.96200 0.31500   63.54400  1.000 94.96000  ? 280 LYS A CD     1 
ATOM   1945  C  CE     . LYS A 1 289 ? -11.21500 0.62100   65.01000  1.000 111.31000 ? 280 LYS A CE     1 
ATOM   1946  N  NZ     . LYS A 1 289 ? -9.94200  0.84100   65.75300  1.000 120.50000 ? 280 LYS A NZ     1 
ATOM   1947  N  N      . GLU A 1 290 ? -9.04600  -4.44800  65.45700  1.000 105.81000 ? 281 GLU A N      1 
ATOM   1948  C  CA     . GLU A 1 290 ? -7.82100  -4.82100  66.15600  1.000 107.26000 ? 281 GLU A CA     1 
ATOM   1949  C  C      . GLU A 1 290 ? -7.01600  -5.82700  65.34400  1.000 111.05000 ? 281 GLU A C      1 
ATOM   1950  O  O      . GLU A 1 290 ? -5.78900  -5.71000  65.23300  1.000 119.07000 ? 281 GLU A O      1 
ATOM   1951  C  CB     . GLU A 1 290 ? -8.15500  -5.38600  67.53600  1.000 103.67000 ? 281 GLU A CB     1 
ATOM   1952  N  N      . THR A 1 291 ? -7.69100  -6.82700  64.77400  1.000 98.41000  ? 282 THR A N      1 
ATOM   1953  C  CA     . THR A 1 291 ? -6.99600  -7.80100  63.94000  1.000 89.68000  ? 282 THR A CA     1 
ATOM   1954  C  C      . THR A 1 291 ? -6.37900  -7.13100  62.72200  1.000 93.86000  ? 282 THR A C      1 
ATOM   1955  O  O      . THR A 1 291 ? -5.25200  -7.45300  62.33000  1.000 108.41000 ? 282 THR A O      1 
ATOM   1956  C  CB     . THR A 1 291 ? -7.95700  -8.90900  63.51100  1.000 97.78000  ? 282 THR A CB     1 
ATOM   1957  O  OG1    . THR A 1 291 ? -8.52800  -9.52400  64.67200  1.000 121.55000 ? 282 THR A OG1    1 
ATOM   1958  C  CG2    . THR A 1 291 ? -7.22300  -9.96100  62.69500  1.000 105.98000 ? 282 THR A CG2    1 
ATOM   1959  N  N      . ILE A 1 292 ? -7.10300  -6.19400  62.10800  1.000 90.33000  ? 283 ILE A N      1 
ATOM   1960  C  CA     . ILE A 1 292 ? -6.56900  -5.49800  60.94200  1.000 99.41000  ? 283 ILE A CA     1 
ATOM   1961  C  C      . ILE A 1 292 ? -5.34500  -4.68100  61.32900  1.000 99.31000  ? 283 ILE A C      1 
ATOM   1962  O  O      . ILE A 1 292 ? -4.35700  -4.62500  60.58900  1.000 104.53000 ? 283 ILE A O      1 
ATOM   1963  C  CB     . ILE A 1 292 ? -7.65900  -4.62300  60.29600  1.000 105.93000 ? 283 ILE A CB     1 
ATOM   1964  C  CG1    . ILE A 1 292 ? -8.80300  -5.50000  59.78300  1.000 108.46000 ? 283 ILE A CG1    1 
ATOM   1965  C  CG2    . ILE A 1 292 ? -7.07200  -3.78500  59.17300  1.000 100.68000 ? 283 ILE A CG2    1 
ATOM   1966  C  CD1    . ILE A 1 292 ? -8.38400  -6.48600  58.71300  1.000 100.30000 ? 283 ILE A CD1    1 
ATOM   1967  N  N      . GLN A 1 293 ? -5.38200  -4.04900  62.50300  1.000 97.52000  ? 284 GLN A N      1 
ATOM   1968  C  CA     . GLN A 1 293 ? -4.23000  -3.28700  62.97600  1.000 107.10000 ? 284 GLN A CA     1 
ATOM   1969  C  C      . GLN A 1 293 ? -3.02900  -4.20000  63.19200  1.000 98.65000  ? 284 GLN A C      1 
ATOM   1970  O  O      . GLN A 1 293 ? -1.90500  -3.88800  62.77400  1.000 103.87000 ? 284 GLN A O      1 
ATOM   1971  C  CB     . GLN A 1 293 ? -4.59300  -2.56000  64.26900  1.000 113.86000 ? 284 GLN A CB     1 
ATOM   1972  C  CG     . GLN A 1 293 ? -5.58000  -1.42300  64.08500  1.000 115.39000 ? 284 GLN A CG     1 
ATOM   1973  C  CD     . GLN A 1 293 ? -6.26500  -1.03800  65.38000  1.000 118.45000 ? 284 GLN A CD     1 
ATOM   1974  O  OE1    . GLN A 1 293 ? -6.07400  -1.68500  66.41000  1.000 106.36000 ? 284 GLN A OE1    1 
ATOM   1975  N  NE2    . GLN A 1 293 ? -7.07200  0.01700   65.33400  1.000 121.20000 ? 284 GLN A NE2    1 
ATOM   1976  N  N      . ALA A 1 294 ? -3.25300  -5.33800  63.85000  1.000 96.73000  ? 285 ALA A N      1 
ATOM   1977  C  CA     . ALA A 1 294 ? -2.16400  -6.27700  64.09800  1.000 106.05000 ? 285 ALA A CA     1 
ATOM   1978  C  C      . ALA A 1 294 ? -1.58000  -6.79800  62.79100  1.000 110.00000 ? 285 ALA A C      1 
ATOM   1979  O  O      . ALA A 1 294 ? -0.36200  -6.97200  62.67300  1.000 107.34000 ? 285 ALA A O      1 
ATOM   1980  C  CB     . ALA A 1 294 ? -2.65700  -7.43200  64.96900  1.000 114.47000 ? 285 ALA A CB     1 
ATOM   1981  N  N      . LEU A 1 295 ? -2.43400  -7.05400  61.79700  1.000 106.13000 ? 286 LEU A N      1 
ATOM   1982  C  CA     . LEU A 1 295 ? -1.94800  -7.54200  60.51100  1.000 92.00000  ? 286 LEU A CA     1 
ATOM   1983  C  C      . LEU A 1 295 ? -1.22200  -6.45100  59.73800  1.000 88.06000  ? 286 LEU A C      1 
ATOM   1984  O  O      . LEU A 1 295 ? -0.29900  -6.74400  58.96900  1.000 92.00000  ? 286 LEU A O      1 
ATOM   1985  C  CB     . LEU A 1 295 ? -3.11300  -8.09600  59.69200  1.000 82.54000  ? 286 LEU A CB     1 
ATOM   1986  C  CG     . LEU A 1 295 ? -3.76300  -9.35600  60.26700  1.000 92.85000  ? 286 LEU A CG     1 
ATOM   1987  C  CD1    . LEU A 1 295 ? -5.17900  -9.51300  59.74500  1.000 116.06000 ? 286 LEU A CD1    1 
ATOM   1988  C  CD2    . LEU A 1 295 ? -2.93300  -10.58400 59.93300  1.000 95.24000  ? 286 LEU A CD2    1 
ATOM   1989  N  N      . ILE A 1 296 ? -1.62300  -5.19400  59.92300  1.000 88.23000  ? 287 ILE A N      1 
ATOM   1990  C  CA     . ILE A 1 296 ? -0.89600  -4.08900  59.31400  1.000 93.34000  ? 287 ILE A CA     1 
ATOM   1991  C  C      . ILE A 1 296 ? 0.48100   -3.95200  59.94400  1.000 101.62000 ? 287 ILE A C      1 
ATOM   1992  O  O      . ILE A 1 296 ? 1.45000   -3.58400  59.26800  1.000 104.23000 ? 287 ILE A O      1 
ATOM   1993  C  CB     . ILE A 1 296 ? -1.70600  -2.78700  59.44400  1.000 90.12000  ? 287 ILE A CB     1 
ATOM   1994  C  CG1    . ILE A 1 296 ? -2.91900  -2.81500  58.51300  1.000 83.23000  ? 287 ILE A CG1    1 
ATOM   1995  C  CG2    . ILE A 1 296 ? -0.82600  -1.58400  59.14900  1.000 94.15000  ? 287 ILE A CG2    1 
ATOM   1996  C  CD1    . ILE A 1 296 ? -3.85600  -1.64100  58.69700  1.000 81.65000  ? 287 ILE A CD1    1 
ATOM   1997  N  N      . SER A 1 297 ? 0.59600   -4.24400  61.24100  1.000 100.77000 ? 288 SER A N      1 
ATOM   1998  C  CA     . SER A 1 297 ? 1.87200   -4.06400  61.92500  1.000 90.54000  ? 288 SER A CA     1 
ATOM   1999  C  C      . SER A 1 297 ? 2.80300   -5.26100  61.75600  1.000 93.82000  ? 288 SER A C      1 
ATOM   2000  O  O      . SER A 1 297 ? 4.02700   -5.09100  61.77400  1.000 96.76000  ? 288 SER A O      1 
ATOM   2001  C  CB     . SER A 1 297 ? 1.63500   -3.79600  63.41200  1.000 103.17000 ? 288 SER A CB     1 
ATOM   2002  O  OG     . SER A 1 297 ? 0.87800   -4.83800  64.00400  1.000 114.66000 ? 288 SER A OG     1 
ATOM   2003  N  N      . TYR A 1 298 ? 2.25200   -6.46500  61.58300  1.000 95.75000  ? 289 TYR A N      1 
ATOM   2004  C  CA     . TYR A 1 298 ? 3.08100   -7.67100  61.60100  1.000 87.52000  ? 289 TYR A CA     1 
ATOM   2005  C  C      . TYR A 1 298 ? 4.16900   -7.67100  60.53900  1.000 96.29000  ? 289 TYR A C      1 
ATOM   2006  O  O      . TYR A 1 298 ? 5.30700   -8.05700  60.85700  1.000 96.64000  ? 289 TYR A O      1 
ATOM   2007  C  CB     . TYR A 1 298 ? 2.19600   -8.91100  61.45500  1.000 83.43000  ? 289 TYR A CB     1 
ATOM   2008  C  CG     . TYR A 1 298 ? 2.97500   -10.19300 61.22900  1.000 91.99000  ? 289 TYR A CG     1 
ATOM   2009  C  CD1    . TYR A 1 298 ? 3.83100   -10.69100 62.20300  1.000 107.59000 ? 289 TYR A CD1    1 
ATOM   2010  C  CD2    . TYR A 1 298 ? 2.85500   -10.90300 60.04000  1.000 103.24000 ? 289 TYR A CD2    1 
ATOM   2011  C  CE1    . TYR A 1 298 ? 4.54300   -11.86100 62.00200  1.000 100.45000 ? 289 TYR A CE1    1 
ATOM   2012  C  CE2    . TYR A 1 298 ? 3.56400   -12.07500 59.83000  1.000 95.80000  ? 289 TYR A CE2    1 
ATOM   2013  C  CZ     . TYR A 1 298 ? 4.40600   -12.54800 60.81500  1.000 85.72000  ? 289 TYR A CZ     1 
ATOM   2014  O  OH     . TYR A 1 298 ? 5.11500   -13.71100 60.61300  1.000 84.84000  ? 289 TYR A OH     1 
ATOM   2015  N  N      . PRO A 1 299 ? 3.90500   -7.30900  59.28100  1.000 107.48000 ? 290 PRO A N      1 
ATOM   2016  C  CA     . PRO A 1 299 ? 4.99400   -7.33200  58.29000  1.000 99.54000  ? 290 PRO A CA     1 
ATOM   2017  C  C      . PRO A 1 299 ? 6.13800   -6.40200  58.65000  1.000 95.51000  ? 290 PRO A C      1 
ATOM   2018  O  O      . PRO A 1 299 ? 7.30600   -6.74200  58.42200  1.000 106.56000 ? 290 PRO A O      1 
ATOM   2019  C  CB     . PRO A 1 299 ? 4.29500   -6.90800  56.98800  1.000 93.57000  ? 290 PRO A CB     1 
ATOM   2020  C  CG     . PRO A 1 299 ? 3.03900   -6.22200  57.42400  1.000 99.24000  ? 290 PRO A CG     1 
ATOM   2021  C  CD     . PRO A 1 299 ? 2.62000   -6.91600  58.67900  1.000 115.04000 ? 290 PRO A CD     1 
ATOM   2022  N  N      . ILE A 1 300 ? 5.83300   -5.23500  59.22100  1.000 79.00000  ? 291 ILE A N      1 
ATOM   2023  C  CA     . ILE A 1 300 ? 6.88600   -4.30300  59.61200  1.000 75.68000  ? 291 ILE A CA     1 
ATOM   2024  C  C      . ILE A 1 300 ? 7.78400   -4.93200  60.67100  1.000 96.44000  ? 291 ILE A C      1 
ATOM   2025  O  O      . ILE A 1 300 ? 9.01600   -4.86200  60.59100  1.000 103.60000 ? 291 ILE A O      1 
ATOM   2026  C  CB     . ILE A 1 300 ? 6.27100   -2.98400  60.11100  1.000 81.65000  ? 291 ILE A CB     1 
ATOM   2027  C  CG1    . ILE A 1 300 ? 5.15500   -2.53200  59.17000  1.000 94.98000  ? 291 ILE A CG1    1 
ATOM   2028  C  CG2    . ILE A 1 300 ? 7.33600   -1.90900  60.20900  1.000 90.20000  ? 291 ILE A CG2    1 
ATOM   2029  C  CD1    . ILE A 1 300 ? 4.41800   -1.30000  59.64200  1.000 99.11000  ? 291 ILE A CD1    1 
ATOM   2030  N  N      . PHE A 1 301 ? 7.17500   -5.54900  61.68600  1.000 97.21000  ? 292 PHE A N      1 
ATOM   2031  C  CA     . PHE A 1 301 ? 7.95800   -6.19400  62.73600  1.000 92.25000  ? 292 PHE A CA     1 
ATOM   2032  C  C      . PHE A 1 301 ? 8.74000   -7.38400  62.19200  1.000 96.74000  ? 292 PHE A C      1 
ATOM   2033  O  O      . PHE A 1 301 ? 9.86600   -7.64500  62.63100  1.000 111.47000 ? 292 PHE A O      1 
ATOM   2034  C  CB     . PHE A 1 301 ? 7.04500   -6.60900  63.88600  1.000 83.33000  ? 292 PHE A CB     1 
ATOM   2035  C  CG     . PHE A 1 301 ? 6.57200   -5.45100  64.71500  1.000 92.63000  ? 292 PHE A CG     1 
ATOM   2036  C  CD1    . PHE A 1 301 ? 7.47000   -4.49800  65.16700  1.000 104.04000 ? 292 PHE A CD1    1 
ATOM   2037  C  CD2    . PHE A 1 301 ? 5.23200   -5.30300  65.02800  1.000 109.90000 ? 292 PHE A CD2    1 
ATOM   2038  C  CE1    . PHE A 1 301 ? 7.04300   -3.42600  65.92300  1.000 125.39000 ? 292 PHE A CE1    1 
ATOM   2039  C  CE2    . PHE A 1 301 ? 4.79800   -4.23200  65.78500  1.000 128.45000 ? 292 PHE A CE2    1 
ATOM   2040  C  CZ     . PHE A 1 301 ? 5.70600   -3.29200  66.23300  1.000 141.02000 ? 292 PHE A CZ     1 
ATOM   2041  N  N      . PHE A 1 302 ? 8.15600   -8.12400  61.24800  1.000 81.11000  ? 293 PHE A N      1 
ATOM   2042  C  CA     . PHE A 1 302 ? 8.88500   -9.22500  60.62600  1.000 92.71000  ? 293 PHE A CA     1 
ATOM   2043  C  C      . PHE A 1 302 ? 10.12300  -8.71100  59.90200  1.000 98.92000  ? 293 PHE A C      1 
ATOM   2044  O  O      . PHE A 1 302 ? 11.20800  -9.29300  60.01400  1.000 109.47000 ? 293 PHE A O      1 
ATOM   2045  C  CB     . PHE A 1 302 ? 7.97400   -9.98300  59.65800  1.000 91.14000  ? 293 PHE A CB     1 
ATOM   2046  C  CG     . PHE A 1 302 ? 8.57100   -11.26500 59.14400  1.000 84.44000  ? 293 PHE A CG     1 
ATOM   2047  C  CD1    . PHE A 1 302 ? 9.56200   -11.24500 58.17600  1.000 83.11000  ? 293 PHE A CD1    1 
ATOM   2048  C  CD2    . PHE A 1 302 ? 8.13900   -12.48800 59.62600  1.000 84.00000  ? 293 PHE A CD2    1 
ATOM   2049  C  CE1    . PHE A 1 302 ? 10.11500  -12.41700 57.70400  1.000 82.28000  ? 293 PHE A CE1    1 
ATOM   2050  C  CE2    . PHE A 1 302 ? 8.68500   -13.66400 59.15300  1.000 89.81000  ? 293 PHE A CE2    1 
ATOM   2051  C  CZ     . PHE A 1 302 ? 9.67800   -13.62600 58.19400  1.000 81.27000  ? 293 PHE A CZ     1 
ATOM   2052  N  N      . ALA A 1 303 ? 9.97400   -7.62200  59.14600  1.000 93.73000  ? 294 ALA A N      1 
ATOM   2053  C  CA     . ALA A 1 303 ? 11.11500  -7.05100  58.43900  1.000 97.58000  ? 294 ALA A CA     1 
ATOM   2054  C  C      . ALA A 1 303 ? 12.16200  -6.53000  59.41600  1.000 114.43000 ? 294 ALA A C      1 
ATOM   2055  O  O      . ALA A 1 303 ? 13.36800  -6.64100  59.16600  1.000 129.31000 ? 294 ALA A O      1 
ATOM   2056  C  CB     . ALA A 1 303 ? 10.64800  -5.93800  57.50300  1.000 101.44000 ? 294 ALA A CB     1 
ATOM   2057  N  N      . LEU A 1 304 ? 11.71900  -5.94900  60.53300  1.000 104.17000 ? 295 LEU A N      1 
ATOM   2058  C  CA     . LEU A 1 304 ? 12.66300  -5.47200  61.54000  1.000 94.69000  ? 295 LEU A CA     1 
ATOM   2059  C  C      . LEU A 1 304 ? 13.44400  -6.62800  62.15200  1.000 103.85000 ? 295 LEU A C      1 
ATOM   2060  O  O      . LEU A 1 304 ? 14.66100  -6.53200  62.35700  1.000 114.31000 ? 295 LEU A O      1 
ATOM   2061  C  CB     . LEU A 1 304 ? 11.92000  -4.69100  62.62200  1.000 90.36000  ? 295 LEU A CB     1 
ATOM   2062  C  CG     . LEU A 1 304 ? 11.24300  -3.40200  62.15700  1.000 92.55000  ? 295 LEU A CG     1 
ATOM   2063  C  CD1    . LEU A 1 304 ? 10.24900  -2.91100  63.19900  1.000 106.19000 ? 295 LEU A CD1    1 
ATOM   2064  C  CD2    . LEU A 1 304 ? 12.28000  -2.33200  61.84700  1.000 98.32000  ? 295 LEU A CD2    1 
ATOM   2065  N  N      . VAL A 1 305 ? 12.75400  -7.72600  62.46700  1.000 102.29000 ? 296 VAL A N      1 
ATOM   2066  C  CA     . VAL A 1 305 ? 13.42900  -8.92200  62.96400  1.000 111.87000 ? 296 VAL A CA     1 
ATOM   2067  C  C      . VAL A 1 305 ? 14.43300  -9.43000  61.93600  1.000 124.78000 ? 296 VAL A C      1 
ATOM   2068  O  O      . VAL A 1 305 ? 15.54700  -9.84700  62.28100  1.000 126.14000 ? 296 VAL A O      1 
ATOM   2069  C  CB     . VAL A 1 305 ? 12.39200  -10.00200 63.33000  1.000 102.76000 ? 296 VAL A CB     1 
ATOM   2070  C  CG1    . VAL A 1 305 ? 13.08000  -11.32100 63.65000  1.000 108.44000 ? 296 VAL A CG1    1 
ATOM   2071  C  CG2    . VAL A 1 305 ? 11.53100  -9.53700  64.49700  1.000 99.53000  ? 296 VAL A CG2    1 
ATOM   2072  N  N      . GLY A 1 306 ? 14.04700  -9.42300  60.65800  1.000 126.73000 ? 297 GLY A N      1 
ATOM   2073  C  CA     . GLY A 1 306 ? 14.97200  -9.83600  59.61500  1.000 118.25000 ? 297 GLY A CA     1 
ATOM   2074  C  C      . GLY A 1 306 ? 16.21700  -8.97200  59.56400  1.000 132.55000 ? 297 GLY A C      1 
ATOM   2075  O  O      . GLY A 1 306 ? 17.33300  -9.48000  59.43100  1.000 140.34000 ? 297 GLY A O      1 
ATOM   2076  N  N      . LEU A 1 307 ? 16.04300  -7.65100  59.65500  1.000 138.91000 ? 298 LEU A N      1 
ATOM   2077  C  CA     . LEU A 1 307 ? 17.19000  -6.74600  59.66300  1.000 138.06000 ? 298 LEU A CA     1 
ATOM   2078  C  C      . LEU A 1 307 ? 18.09000  -7.01400  60.86500  1.000 140.53000 ? 298 LEU A C      1 
ATOM   2079  O  O      . LEU A 1 307 ? 19.32300  -6.99700  60.74900  1.000 147.67000 ? 298 LEU A O      1 
ATOM   2080  C  CB     . LEU A 1 307 ? 16.71500  -5.29200  59.65400  1.000 122.70000 ? 298 LEU A CB     1 
ATOM   2081  C  CG     . LEU A 1 307 ? 17.78100  -4.22000  59.41100  1.000 111.57000 ? 298 LEU A CG     1 
ATOM   2082  C  CD1    . LEU A 1 307 ? 18.46200  -4.43000  58.06700  1.000 116.78000 ? 298 LEU A CD1    1 
ATOM   2083  C  CD2    . LEU A 1 307 ? 17.17700  -2.82400  59.49700  1.000 100.82000 ? 298 LEU A CD2    1 
ATOM   2084  N  N      . GLY A 1 308 ? 17.48800  -7.24700  62.03300  1.000 134.74000 ? 299 GLY A N      1 
ATOM   2085  C  CA     . GLY A 1 308 ? 18.28000  -7.58400  63.20700  1.000 130.85000 ? 299 GLY A CA     1 
ATOM   2086  C  C      . GLY A 1 308 ? 19.09800  -8.84600  63.00900  1.000 126.32000 ? 299 GLY A C      1 
ATOM   2087  O  O      . GLY A 1 308 ? 20.29000  -8.88900  63.33200  1.000 119.78000 ? 299 GLY A O      1 
ATOM   2088  N  N      . CYS A 1 309 ? 18.46000  -9.90300  62.49600  1.000 120.32000 ? 300 CYS A N      1 
ATOM   2089  C  CA     . CYS A 1 309 ? 19.17800  -11.15000 62.24400  1.000 122.11000 ? 300 CYS A CA     1 
ATOM   2090  C  C      . CYS A 1 309 ? 20.29500  -10.94800 61.22500  1.000 122.84000 ? 300 CYS A C      1 
ATOM   2091  O  O      . CYS A 1 309 ? 21.37300  -11.54000 61.34900  1.000 120.36000 ? 300 CYS A O      1 
ATOM   2092  C  CB     . CYS A 1 309 ? 18.21400  -12.24000 61.77000  1.000 118.24000 ? 300 CYS A CB     1 
ATOM   2093  S  SG     . CYS A 1 309 ? 16.82300  -12.58100 62.87600  1.000 132.47000 ? 300 CYS A SG     1 
ATOM   2094  N  N      . SER A 1 310 ? 20.04900  -10.12800 60.20000  1.000 129.20000 ? 301 SER A N      1 
ATOM   2095  C  CA     . SER A 1 310 ? 21.08900  -9.84800  59.21500  1.000 129.11000 ? 301 SER A CA     1 
ATOM   2096  C  C      . SER A 1 310 ? 22.28000  -9.14800  59.85800  1.000 133.34000 ? 301 SER A C      1 
ATOM   2097  O  O      . SER A 1 310 ? 23.43700  -9.48100  59.56900  1.000 140.93000 ? 301 SER A O      1 
ATOM   2098  C  CB     . SER A 1 310 ? 20.52700  -8.99600  58.07500  1.000 128.24000 ? 301 SER A CB     1 
ATOM   2099  O  OG     . SER A 1 310 ? 19.49400  -9.66900  57.37700  1.000 136.58000 ? 301 SER A OG     1 
ATOM   2100  N  N      . MET A 1 311 ? 22.01500  -8.16000  60.71700  1.000 131.49000 ? 302 MET A N      1 
ATOM   2101  C  CA     . MET A 1 311 ? 23.10600  -7.48800  61.41900  1.000 129.62000 ? 302 MET A CA     1 
ATOM   2102  C  C      . MET A 1 311 ? 23.87000  -8.46400  62.30700  1.000 125.66000 ? 302 MET A C      1 
ATOM   2103  O  O      . MET A 1 311 ? 25.10400  -8.42900  62.36400  1.000 120.01000 ? 302 MET A O      1 
ATOM   2104  C  CB     . MET A 1 311 ? 22.57200  -6.31200  62.23900  1.000 124.03000 ? 302 MET A CB     1 
ATOM   2105  C  CG     . MET A 1 311 ? 22.08100  -5.13800  61.40200  1.000 121.15000 ? 302 MET A CG     1 
ATOM   2106  S  SD     . MET A 1 311 ? 21.62600  -3.69500  62.39100  1.000 106.61000 ? 302 MET A SD     1 
ATOM   2107  C  CE     . MET A 1 311 ? 20.05400  -4.22500  63.06800  1.000 115.84000 ? 302 MET A CE     1 
ATOM   2108  N  N      . LEU A 1 312 ? 23.15400  -9.34700  63.00700  1.000 110.59000 ? 303 LEU A N      1 
ATOM   2109  C  CA     . LEU A 1 312 ? 23.82300  -10.33700 63.84800  1.000 93.00000  ? 303 LEU A CA     1 
ATOM   2110  C  C      . LEU A 1 312 ? 24.72000  -11.24600 63.01300  1.000 97.22000  ? 303 LEU A C      1 
ATOM   2111  O  O      . LEU A 1 312 ? 25.86100  -11.54100 63.39400  1.000 112.18000 ? 303 LEU A O      1 
ATOM   2112  C  CB     . LEU A 1 312 ? 22.78800  -11.15800 64.61800  1.000 79.11000  ? 303 LEU A CB     1 
ATOM   2113  N  N      . GLY A 1 313 ? 24.21000  -11.71500 61.87400  1.000 99.42000  ? 304 GLY A N      1 
ATOM   2114  C  CA     . GLY A 1 313 ? 25.01100  -12.56800 61.01300  1.000 98.47000  ? 304 GLY A CA     1 
ATOM   2115  C  C      . GLY A 1 313 ? 26.24500  -11.86600 60.48000  1.000 100.15000 ? 304 GLY A C      1 
ATOM   2116  O  O      . GLY A 1 313 ? 27.33900  -12.43700 60.47100  1.000 120.37000 ? 304 GLY A O      1 
ATOM   2117  N  N      . ILE A 1 314 ? 26.09000  -10.62000 60.02600  1.000 92.97000  ? 305 ILE A N      1 
ATOM   2118  C  CA     . ILE A 1 314 ? 27.24600  -9.87900  59.52600  1.000 105.26000 ? 305 ILE A CA     1 
ATOM   2119  C  C      . ILE A 1 314 ? 28.26000  -9.66200  60.64400  1.000 123.17000 ? 305 ILE A C      1 
ATOM   2120  O  O      . ILE A 1 314 ? 29.47800  -9.70600  60.41800  1.000 126.61000 ? 305 ILE A O      1 
ATOM   2121  C  CB     . ILE A 1 314 ? 26.80500  -8.55000  58.88200  1.000 103.93000 ? 305 ILE A CB     1 
ATOM   2122  C  CG1    . ILE A 1 314 ? 26.15200  -7.63100  59.91200  1.000 103.01000 ? 305 ILE A CG1    1 
ATOM   2123  C  CG2    . ILE A 1 314 ? 25.85600  -8.81000  57.72100  1.000 111.01000 ? 305 ILE A CG2    1 
ATOM   2124  C  CD1    . ILE A 1 314 ? 25.72000  -6.30100  59.34200  1.000 101.21000 ? 305 ILE A CD1    1 
ATOM   2125  N  N      . LEU A 1 315 ? 27.77900  -9.41900  61.86600  1.000 125.01000 ? 306 LEU A N      1 
ATOM   2126  C  CA     . LEU A 1 315 ? 28.68300  -9.25400  63.00000  1.000 119.96000 ? 306 LEU A CA     1 
ATOM   2127  C  C      . LEU A 1 315 ? 29.47700  -10.52900 63.25300  1.000 112.90000 ? 306 LEU A C      1 
ATOM   2128  O  O      . LEU A 1 315 ? 30.69400  -10.48600 63.46300  1.000 123.68000 ? 306 LEU A O      1 
ATOM   2129  C  CB     . LEU A 1 315 ? 27.89400  -8.85200  64.24700  1.000 113.39000 ? 306 LEU A CB     1 
ATOM   2130  N  N      . TYR A 1 316 ? 28.80100  -11.68100 63.23900  1.000 105.12000 ? 307 TYR A N      1 
ATOM   2131  C  CA     . TYR A 1 316 ? 29.51900  -12.94000 63.41900  1.000 114.11000 ? 307 TYR A CA     1 
ATOM   2132  C  C      . TYR A 1 316 ? 30.52800  -13.16300 62.29800  1.000 126.06000 ? 307 TYR A C      1 
ATOM   2133  O  O      . TYR A 1 316 ? 31.60700  -13.72400 62.52500  1.000 140.07000 ? 307 TYR A O      1 
ATOM   2134  C  CB     . TYR A 1 316 ? 28.54500  -14.11600 63.49700  1.000 132.52000 ? 307 TYR A CB     1 
ATOM   2135  C  CG     . TYR A 1 316 ? 29.23800  -15.44900 63.70900  1.000 137.76000 ? 307 TYR A CG     1 
ATOM   2136  C  CD1    . TYR A 1 316 ? 29.55000  -15.90000 64.98500  1.000 152.92000 ? 307 TYR A CD1    1 
ATOM   2137  C  CD2    . TYR A 1 316 ? 29.59400  -16.24900 62.62900  1.000 129.51000 ? 307 TYR A CD2    1 
ATOM   2138  C  CE1    . TYR A 1 316 ? 30.19000  -17.11300 65.18100  1.000 158.51000 ? 307 TYR A CE1    1 
ATOM   2139  C  CE2    . TYR A 1 316 ? 30.23300  -17.46200 62.81500  1.000 133.97000 ? 307 TYR A CE2    1 
ATOM   2140  C  CZ     . TYR A 1 316 ? 30.52800  -17.88900 64.09300  1.000 149.92000 ? 307 TYR A CZ     1 
ATOM   2141  O  OH     . TYR A 1 316 ? 31.16400  -19.09500 64.28300  1.000 147.88000 ? 307 TYR A OH     1 
ATOM   2142  N  N      . VAL A 1 317 ? 30.18900  -12.74500 61.07700  1.000 122.59000 ? 308 VAL A N      1 
ATOM   2143  C  CA     . VAL A 1 317 ? 31.09000  -12.95400 59.94600  1.000 126.51000 ? 308 VAL A CA     1 
ATOM   2144  C  C      . VAL A 1 317 ? 32.34600  -12.10000 60.08600  1.000 139.77000 ? 308 VAL A C      1 
ATOM   2145  O  O      . VAL A 1 317 ? 33.46500  -12.57500 59.85600  1.000 145.79000 ? 308 VAL A O      1 
ATOM   2146  C  CB     . VAL A 1 317 ? 30.36100  -12.67800 58.61900  1.000 117.05000 ? 308 VAL A CB     1 
ATOM   2147  C  CG1    . VAL A 1 317 ? 31.29000  -12.92200 57.44100  1.000 92.72000  ? 308 VAL A CG1    1 
ATOM   2148  C  CG2    . VAL A 1 317 ? 29.12400  -13.55200 58.51100  1.000 128.33000 ? 308 VAL A CG2    1 
ATOM   2149  N  N      . ILE A 1 318 ? 32.18400  -10.82800 60.46000  1.000 138.66000 ? 309 ILE A N      1 
ATOM   2150  C  CA     . ILE A 1 318 ? 33.31300  -9.90100  60.48400  1.000 131.47000 ? 309 ILE A CA     1 
ATOM   2151  C  C      . ILE A 1 318 ? 34.27500  -10.17200 61.63600  1.000 127.80000 ? 309 ILE A C      1 
ATOM   2152  O  O      . ILE A 1 318 ? 35.44700  -9.78500  61.55500  1.000 114.53000 ? 309 ILE A O      1 
ATOM   2153  C  CB     . ILE A 1 318 ? 32.82000  -8.44300  60.53700  1.000 131.56000 ? 309 ILE A CB     1 
ATOM   2154  C  CG1    . ILE A 1 318 ? 31.95600  -8.21500  61.77700  1.000 141.66000 ? 309 ILE A CG1    1 
ATOM   2155  C  CG2    . ILE A 1 318 ? 32.05500  -8.09000  59.26800  1.000 120.14000 ? 309 ILE A CG2    1 
ATOM   2156  C  CD1    . ILE A 1 318 ? 31.57400  -6.76700  61.99000  1.000 145.24000 ? 309 ILE A CD1    1 
ATOM   2157  N  N      . VAL A 1 319 ? 33.82100  -10.81800 62.71300  1.000 140.08000 ? 310 VAL A N      1 
ATOM   2158  C  CA     . VAL A 1 319 ? 34.65800  -10.93900 63.90500  1.000 143.74000 ? 310 VAL A CA     1 
ATOM   2159  C  C      . VAL A 1 319 ? 35.80000  -11.92100 63.66900  1.000 144.78000 ? 310 VAL A C      1 
ATOM   2160  O  O      . VAL A 1 319 ? 36.97000  -11.60000 63.90900  1.000 154.80000 ? 310 VAL A O      1 
ATOM   2161  C  CB     . VAL A 1 319 ? 33.80400  -11.35300 65.11800  1.000 135.52000 ? 310 VAL A CB     1 
ATOM   2162  C  CG1    . VAL A 1 319 ? 34.69100  -11.68400 66.30800  1.000 153.34000 ? 310 VAL A CG1    1 
ATOM   2163  C  CG2    . VAL A 1 319 ? 32.81800  -10.25400 65.47600  1.000 105.15000 ? 310 VAL A CG2    1 
ATOM   2164  N  N      . LYS A 1 320 ? 35.49200  -13.12700 63.20100  1.000 131.64000 ? 311 LYS A N      1 
ATOM   2165  C  CA     . LYS A 1 320 ? 36.55200  -14.11100 63.04700  1.000 135.75000 ? 311 LYS A CA     1 
ATOM   2166  C  C      . LYS A 1 320 ? 37.44100  -13.73900 61.86500  1.000 129.95000 ? 311 LYS A C      1 
ATOM   2167  O  O      . LYS A 1 320 ? 36.98500  -13.15900 60.87600  1.000 130.96000 ? 311 LYS A O      1 
ATOM   2168  C  CB     . LYS A 1 320 ? 35.96500  -15.50900 62.84500  1.000 134.58000 ? 311 LYS A CB     1 
ATOM   2169  C  CG     . LYS A 1 320 ? 35.22500  -16.05900 64.05500  1.000 137.91000 ? 311 LYS A CG     1 
ATOM   2170  C  CD     . LYS A 1 320 ? 34.77600  -17.49400 63.82700  1.000 140.37000 ? 311 LYS A CD     1 
ATOM   2171  N  N      . LYS A 1 321 ? 38.72200  -14.07200 61.97200  1.000 121.03000 ? 312 LYS A N      1 
ATOM   2172  C  CA     . LYS A 1 321 ? 39.64400  -13.82600 60.86900  1.000 117.23000 ? 312 LYS A CA     1 
ATOM   2173  C  C      . LYS A 1 321 ? 39.27500  -14.67400 59.65700  1.000 101.12000 ? 312 LYS A C      1 
ATOM   2174  O  O      . LYS A 1 321 ? 39.08400  -15.88400 59.77600  1.000 75.09000  ? 312 LYS A O      1 
ATOM   2175  C  CB     . LYS A 1 321 ? 41.09000  -14.07400 61.29500  1.000 116.98000 ? 312 LYS A CB     1 
ATOM   2176  C  CG     . LYS A 1 321 ? 41.64000  -12.95300 62.15700  1.000 123.09000 ? 312 LYS A CG     1 
ATOM   2177  C  CD     . LYS A 1 321 ? 41.77800  -11.68100 61.32900  1.000 109.97000 ? 312 LYS A CD     1 
ATOM   2178  C  CE     . LYS A 1 321 ? 42.53000  -10.59400 62.07500  1.000 127.71000 ? 312 LYS A CE     1 
ATOM   2179  N  NZ     . LYS A 1 321 ? 43.95100  -10.96100 62.31100  1.000 105.73000 ? 312 LYS A NZ     1 
ATOM   2180  N  N      . ASN A 1 325 ? 38.59000  -19.96300 52.12600  1.000 179.73000 ? 316 ASN A N      1 
ATOM   2181  C  CA     . ASN A 1 325 ? 37.65100  -19.83700 51.01600  1.000 180.99000 ? 316 ASN A CA     1 
ATOM   2182  C  C      . ASN A 1 325 ? 36.61400  -18.76200 51.32100  1.000 178.22000 ? 316 ASN A C      1 
ATOM   2183  O  O      . ASN A 1 325 ? 35.79600  -18.92100 52.22800  1.000 174.29000 ? 316 ASN A O      1 
ATOM   2184  C  CB     . ASN A 1 325 ? 36.96900  -21.17500 50.72600  1.000 173.76000 ? 316 ASN A CB     1 
ATOM   2185  C  CG     . ASN A 1 325 ? 36.23900  -21.17900 49.39700  1.000 163.80000 ? 316 ASN A CG     1 
ATOM   2186  O  OD1    . ASN A 1 325 ? 35.01400  -21.07700 49.34900  1.000 163.61000 ? 316 ASN A OD1    1 
ATOM   2187  N  ND2    . ASN A 1 325 ? 36.99200  -21.29600 48.30800  1.000 163.84000 ? 316 ASN A ND2    1 
ATOM   2188  N  N      . PRO A 1 326 ? 36.64900  -17.66400 50.56100  1.000 177.88000 ? 317 PRO A N      1 
ATOM   2189  C  CA     . PRO A 1 326 ? 35.73800  -16.54800 50.86800  1.000 169.19000 ? 317 PRO A CA     1 
ATOM   2190  C  C      . PRO A 1 326 ? 34.27200  -16.87100 50.63100  1.000 162.40000 ? 317 PRO A C      1 
ATOM   2191  O  O      . PRO A 1 326 ? 33.42300  -16.45000 51.42700  1.000 161.62000 ? 317 PRO A O      1 
ATOM   2192  C  CB     . PRO A 1 326 ? 36.23100  -15.42800 49.93800  1.000 163.23000 ? 317 PRO A CB     1 
ATOM   2193  C  CG     . PRO A 1 326 ? 37.62700  -15.82400 49.55000  1.000 161.74000 ? 317 PRO A CG     1 
ATOM   2194  C  CD     . PRO A 1 326 ? 37.62700  -17.31700 49.51700  1.000 164.21000 ? 317 PRO A CD     1 
ATOM   2195  N  N      . GLN A 1 327 ? 33.94200  -17.60100 49.56100  1.000 157.11000 ? 318 GLN A N      1 
ATOM   2196  C  CA     . GLN A 1 327 ? 32.53400  -17.84000 49.25000  1.000 151.07000 ? 318 GLN A CA     1 
ATOM   2197  C  C      . GLN A 1 327 ? 31.84100  -18.60400 50.37200  1.000 155.66000 ? 318 GLN A C      1 
ATOM   2198  O  O      . GLN A 1 327 ? 30.69000  -18.30900 50.71300  1.000 168.77000 ? 318 GLN A O      1 
ATOM   2199  C  CB     . GLN A 1 327 ? 32.39000  -18.59300 47.92700  1.000 160.50000 ? 318 GLN A CB     1 
ATOM   2200  C  CG     . GLN A 1 327 ? 30.93600  -18.89300 47.56200  1.000 151.18000 ? 318 GLN A CG     1 
ATOM   2201  C  CD     . GLN A 1 327 ? 30.77700  -19.51200 46.18400  1.000 150.20000 ? 318 GLN A CD     1 
ATOM   2202  O  OE1    . GLN A 1 327 ? 31.71700  -19.53800 45.39000  1.000 141.28000 ? 318 GLN A OE1    1 
ATOM   2203  N  NE2    . GLN A 1 327 ? 29.58000  -20.01400 45.89500  1.000 142.79000 ? 318 GLN A NE2    1 
ATOM   2204  N  N      . ARG A 1 328 ? 32.52000  -19.59600 50.95400  1.000 149.15000 ? 319 ARG A N      1 
ATOM   2205  C  CA     . ARG A 1 328 ? 31.91900  -20.34300 52.05400  1.000 141.97000 ? 319 ARG A CA     1 
ATOM   2206  C  C      . ARG A 1 328 ? 31.58600  -19.42200 53.22200  1.000 158.90000 ? 319 ARG A C      1 
ATOM   2207  O  O      . ARG A 1 328 ? 30.58300  -19.62300 53.91700  1.000 167.65000 ? 319 ARG A O      1 
ATOM   2208  C  CB     . ARG A 1 328 ? 32.85500  -21.46700 52.49800  1.000 119.29000 ? 319 ARG A CB     1 
ATOM   2209  N  N      . GLU A 1 329 ? 32.41900  -18.40500 53.45300  1.000 155.08000 ? 320 GLU A N      1 
ATOM   2210  C  CA     . GLU A 1 329 ? 32.17800  -17.46700 54.54600  1.000 149.91000 ? 320 GLU A CA     1 
ATOM   2211  C  C      . GLU A 1 329 ? 30.95200  -16.60100 54.26900  1.000 143.86000 ? 320 GLU A C      1 
ATOM   2212  O  O      . GLU A 1 329 ? 30.09200  -16.42400 55.14100  1.000 143.02000 ? 320 GLU A O      1 
ATOM   2213  C  CB     . GLU A 1 329 ? 33.42300  -16.60800 54.77700  1.000 162.26000 ? 320 GLU A CB     1 
ATOM   2214  C  CG     . GLU A 1 329 ? 34.70000  -17.42700 54.93800  1.000 164.18000 ? 320 GLU A CG     1 
ATOM   2215  C  CD     . GLU A 1 329 ? 35.95600  -16.65600 54.57100  1.000 169.26000 ? 320 GLU A CD     1 
ATOM   2216  O  OE1    . GLU A 1 329 ? 35.83900  -15.58900 53.93200  1.000 154.66000 ? 320 GLU A OE1    1 
ATOM   2217  O  OE2    . GLU A 1 329 ? 37.06200  -17.12200 54.92000  1.000 176.22000 ? 320 GLU A OE2    1 
ATOM   2218  N  N      . LEU A 1 330 ? 30.86000  -16.04200 53.06000  1.000 145.14000 ? 321 LEU A N      1 
ATOM   2219  C  CA     . LEU A 1 330 ? 29.70300  -15.22300 52.71100  1.000 138.95000 ? 321 LEU A CA     1 
ATOM   2220  C  C      . LEU A 1 330 ? 28.42900  -16.06200 52.66700  1.000 133.87000 ? 321 LEU A C      1 
ATOM   2221  O  O      . LEU A 1 330 ? 27.35600  -15.60300 53.08400  1.000 141.09000 ? 321 LEU A O      1 
ATOM   2222  C  CB     . LEU A 1 330 ? 29.94500  -14.53300 51.36800  1.000 131.40000 ? 321 LEU A CB     1 
ATOM   2223  C  CG     . LEU A 1 330 ? 30.90000  -13.33600 51.37700  1.000 112.28000 ? 321 LEU A CG     1 
ATOM   2224  C  CD1    . LEU A 1 330 ? 30.76000  -12.51200 50.10400  1.000 103.14000 ? 321 LEU A CD1    1 
ATOM   2225  C  CD2    . LEU A 1 330 ? 30.67200  -12.47000 52.60700  1.000 121.30000 ? 321 LEU A CD2    1 
ATOM   2226  N  N      . ASN A 1 331 ? 28.53100  -17.29700 52.16700  1.000 132.43000 ? 322 ASN A N      1 
ATOM   2227  C  CA     . ASN A 1 331 ? 27.38400  -18.19900 52.18600  1.000 144.44000 ? 322 ASN A CA     1 
ATOM   2228  C  C      . ASN A 1 331 ? 26.93200  -18.46300 53.61500  1.000 148.86000 ? 322 ASN A C      1 
ATOM   2229  O  O      . ASN A 1 331 ? 25.73000  -18.54000 53.89200  1.000 151.20000 ? 322 ASN A O      1 
ATOM   2230  C  CB     . ASN A 1 331 ? 27.73200  -19.51100 51.47600  1.000 156.97000 ? 322 ASN A CB     1 
ATOM   2231  C  CG     . ASN A 1 331 ? 26.56600  -20.48900 51.44000  1.000 158.13000 ? 322 ASN A CG     1 
ATOM   2232  O  OD1    . ASN A 1 331 ? 25.42800  -20.10900 51.16600  1.000 159.45000 ? 322 ASN A OD1    1 
ATOM   2233  N  ND2    . ASN A 1 331 ? 26.85000  -21.75900 51.71600  1.000 142.14000 ? 322 ASN A ND2    1 
ATOM   2234  N  N      . ILE A 1 332 ? 27.88500  -18.59300 54.54100  1.000 150.76000 ? 323 ILE A N      1 
ATOM   2235  C  CA     . ILE A 1 332 ? 27.52500  -18.80400 55.93800  1.000 149.84000 ? 323 ILE A CA     1 
ATOM   2236  C  C      . ILE A 1 332 ? 26.90500  -17.54900 56.53700  1.000 133.40000 ? 323 ILE A C      1 
ATOM   2237  O  O      . ILE A 1 332 ? 26.00800  -17.64100 57.37700  1.000 136.24000 ? 323 ILE A O      1 
ATOM   2238  C  CB     . ILE A 1 332 ? 28.74800  -19.27100 56.74700  1.000 159.35000 ? 323 ILE A CB     1 
ATOM   2239  C  CG1    . ILE A 1 332 ? 29.14200  -20.69600 56.34400  1.000 173.20000 ? 323 ILE A CG1    1 
ATOM   2240  C  CG2    . ILE A 1 332 ? 28.46000  -19.19100 58.23800  1.000 161.78000 ? 323 ILE A CG2    1 
ATOM   2241  C  CD1    . ILE A 1 332 ? 28.04200  -21.72000 56.54900  1.000 148.86000 ? 323 ILE A CD1    1 
ATOM   2242  N  N      . SER A 1 333 ? 27.35800  -16.36300 56.12500  1.000 116.38000 ? 324 SER A N      1 
ATOM   2243  C  CA     . SER A 1 333 ? 26.68700  -15.13400 56.54500  1.000 123.19000 ? 324 SER A CA     1 
ATOM   2244  C  C      . SER A 1 333 ? 25.22300  -15.14100 56.11500  1.000 140.97000 ? 324 SER A C      1 
ATOM   2245  O  O      . SER A 1 333 ? 24.31800  -14.86200 56.91700  1.000 141.47000 ? 324 SER A O      1 
ATOM   2246  C  CB     . SER A 1 333 ? 27.41100  -13.91700 55.96700  1.000 117.32000 ? 324 SER A CB     1 
ATOM   2247  O  OG     . SER A 1 333 ? 26.77300  -12.71000 56.34900  1.000 105.38000 ? 324 SER A OG     1 
ATOM   2248  N  N      . LEU A 1 334 ? 24.97700  -15.44600 54.83900  1.000 134.01000 ? 325 LEU A N      1 
ATOM   2249  C  CA     . LEU A 1 334 ? 23.60600  -15.50600 54.33900  1.000 105.19000 ? 325 LEU A CA     1 
ATOM   2250  C  C      . LEU A 1 334 ? 22.78500  -16.53600 55.10900  1.000 119.18000 ? 325 LEU A C      1 
ATOM   2251  O  O      . LEU A 1 334 ? 21.65000  -16.26200 55.51800  1.000 136.37000 ? 325 LEU A O      1 
ATOM   2252  C  CB     . LEU A 1 334 ? 23.59900  -15.82100 52.84200  1.000 107.23000 ? 325 LEU A CB     1 
ATOM   2253  C  CG     . LEU A 1 334 ? 23.98400  -14.69100 51.88300  1.000 110.48000 ? 325 LEU A CG     1 
ATOM   2254  C  CD1    . LEU A 1 334 ? 24.12900  -15.22200 50.46400  1.000 131.57000 ? 325 LEU A CD1    1 
ATOM   2255  C  CD2    . LEU A 1 334 ? 22.96500  -13.56300 51.93400  1.000 116.33000 ? 325 LEU A CD2    1 
ATOM   2256  N  N      . TRP A 1 335 ? 23.33900  -17.73700 55.30100  1.000 119.07000 ? 326 TRP A N      1 
ATOM   2257  C  CA     . TRP A 1 335 ? 22.61400  -18.78400 56.01600  1.000 121.67000 ? 326 TRP A CA     1 
ATOM   2258  C  C      . TRP A 1 335 ? 22.30500  -18.36800 57.44900  1.000 126.00000 ? 326 TRP A C      1 
ATOM   2259  O  O      . TRP A 1 335 ? 21.19500  -18.59600 57.94200  1.000 122.26000 ? 326 TRP A O      1 
ATOM   2260  C  CB     . TRP A 1 335 ? 23.40800  -20.09200 55.99700  1.000 102.79000 ? 326 TRP A CB     1 
ATOM   2261  C  CG     . TRP A 1 335 ? 23.20100  -20.90700 54.75700  1.000 128.58000 ? 326 TRP A CG     1 
ATOM   2262  C  CD1    . TRP A 1 335 ? 23.94600  -20.86800 53.61600  1.000 142.04000 ? 326 TRP A CD1    1 
ATOM   2263  C  CD2    . TRP A 1 335 ? 22.17400  -21.88200 54.53100  1.000 144.54000 ? 326 TRP A CD2    1 
ATOM   2264  N  NE1    . TRP A 1 335 ? 23.45100  -21.75900 52.69400  1.000 150.59000 ? 326 TRP A NE1    1 
ATOM   2265  C  CE2    . TRP A 1 335 ? 22.36200  -22.39400 53.23200  1.000 163.43000 ? 326 TRP A CE2    1 
ATOM   2266  C  CE3    . TRP A 1 335 ? 21.11400  -22.37100 55.30200  1.000 133.50000 ? 326 TRP A CE3    1 
ATOM   2267  C  CZ2    . TRP A 1 335 ? 21.53200  -23.37100 52.68600  1.000 160.16000 ? 326 TRP A CZ2    1 
ATOM   2268  C  CZ3    . TRP A 1 335 ? 20.29100  -23.34000 54.75900  1.000 120.25000 ? 326 TRP A CZ3    1 
ATOM   2269  C  CH2    . TRP A 1 335 ? 20.50400  -23.83000 53.46300  1.000 130.67000 ? 326 TRP A CH2    1 
ATOM   2270  N  N      . THR A 1 336 ? 23.28200  -17.78000 58.14300  1.000 129.30000 ? 327 THR A N      1 
ATOM   2271  C  CA     . THR A 1 336 ? 23.05300  -17.31400 59.50500  1.000 117.94000 ? 327 THR A CA     1 
ATOM   2272  C  C      . THR A 1 336 ? 21.90000  -16.32400 59.54500  1.000 107.25000 ? 327 THR A C      1 
ATOM   2273  O  O      . THR A 1 336 ? 20.93600  -16.50200 60.29600  1.000 111.81000 ? 327 THR A O      1 
ATOM   2274  C  CB     . THR A 1 336 ? 24.32400  -16.67500 60.07200  1.000 102.30000 ? 327 THR A CB     1 
ATOM   2275  O  OG1    . THR A 1 336 ? 24.86700  -15.75400 59.11900  1.000 101.21000 ? 327 THR A OG1    1 
ATOM   2276  C  CG2    . THR A 1 336 ? 25.36300  -17.73900 60.38300  1.000 112.81000 ? 327 THR A CG2    1 
ATOM   2277  N  N      . SER A 1 337 ? 21.98800  -15.26200 58.74100  1.000 97.34000  ? 328 SER A N      1 
ATOM   2278  C  CA     . SER A 1 337 ? 20.91500  -14.27400 58.72300  1.000 84.58000  ? 328 SER A CA     1 
ATOM   2279  C  C      . SER A 1 337 ? 19.56600  -14.93700 58.45600  1.000 88.15000  ? 328 SER A C      1 
ATOM   2280  O  O      . SER A 1 337 ? 18.59900  -14.73200 59.20100  1.000 102.12000 ? 328 SER A O      1 
ATOM   2281  C  CB     . SER A 1 337 ? 21.21100  -13.19400 57.68000  1.000 87.03000  ? 328 SER A CB     1 
ATOM   2282  O  OG     . SER A 1 337 ? 21.27300  -13.74400 56.37600  1.000 123.77000 ? 328 SER A OG     1 
ATOM   2283  N  N      . ALA A 1 338 ? 19.49400  -15.75900 57.40600  1.000 87.47000  ? 329 ALA A N      1 
ATOM   2284  C  CA     . ALA A 1 338 ? 18.21800  -16.33600 56.99100  1.000 100.64000 ? 329 ALA A CA     1 
ATOM   2285  C  C      . ALA A 1 338 ? 17.62800  -17.22500 58.07900  1.000 100.70000 ? 329 ALA A C      1 
ATOM   2286  O  O      . ALA A 1 338 ? 16.46700  -17.06000 58.46900  1.000 100.29000 ? 329 ALA A O      1 
ATOM   2287  C  CB     . ALA A 1 338 ? 18.39600  -17.12000 55.69000  1.000 107.54000 ? 329 ALA A CB     1 
ATOM   2288  N  N      . LEU A 1 339 ? 18.40900  -18.18800 58.57200  1.000 92.41000  ? 330 LEU A N      1 
ATOM   2289  C  CA     . LEU A 1 339 ? 17.87200  -19.13300 59.54300  1.000 98.79000  ? 330 LEU A CA     1 
ATOM   2290  C  C      . LEU A 1 339 ? 17.59500  -18.46600 60.88500  1.000 103.75000 ? 330 LEU A C      1 
ATOM   2291  O  O      . LEU A 1 339 ? 16.65700  -18.86500 61.58800  1.000 104.75000 ? 330 LEU A O      1 
ATOM   2292  C  CB     . LEU A 1 339 ? 18.82600  -20.31500 59.70800  1.000 83.15000  ? 330 LEU A CB     1 
ATOM   2293  C  CG     . LEU A 1 339 ? 18.57600  -21.45000 58.71200  1.000 79.07000  ? 330 LEU A CG     1 
ATOM   2294  C  CD1    . LEU A 1 339 ? 18.80700  -20.97700 57.28400  1.000 87.18000  ? 330 LEU A CD1    1 
ATOM   2295  C  CD2    . LEU A 1 339 ? 19.45000  -22.64900 59.03000  1.000 113.01000 ? 330 LEU A CD2    1 
ATOM   2296  N  N      . LEU A 1 340 ? 18.37400  -17.44700 61.25600  1.000 93.69000  ? 331 LEU A N      1 
ATOM   2297  C  CA     . LEU A 1 340 ? 18.07700  -16.71200 62.47800  1.000 89.91000  ? 331 LEU A CA     1 
ATOM   2298  C  C      . LEU A 1 340 ? 16.74800  -15.98200 62.35100  1.000 94.29000  ? 331 LEU A C      1 
ATOM   2299  O  O      . LEU A 1 340 ? 15.91200  -16.02900 63.26200  1.000 106.89000 ? 331 LEU A O      1 
ATOM   2300  C  CB     . LEU A 1 340 ? 19.20600  -15.73000 62.79000  1.000 95.24000  ? 331 LEU A CB     1 
ATOM   2301  C  CG     . LEU A 1 340 ? 20.46000  -16.31400 63.44500  1.000 95.38000  ? 331 LEU A CG     1 
ATOM   2302  C  CD1    . LEU A 1 340 ? 21.48300  -15.22000 63.72700  1.000 71.74000  ? 331 LEU A CD1    1 
ATOM   2303  C  CD2    . LEU A 1 340 ? 20.11000  -17.08000 64.71400  1.000 106.09000 ? 331 LEU A CD2    1 
ATOM   2304  N  N      . THR A 1 341 ? 16.53500  -15.30000 61.22200  1.000 84.67000  ? 332 THR A N      1 
ATOM   2305  C  CA     . THR A 1 341 ? 15.23100  -14.69600 60.97100  1.000 82.69000  ? 332 THR A CA     1 
ATOM   2306  C  C      . THR A 1 341 ? 14.12700  -15.74000 61.04100  1.000 89.77000  ? 332 THR A C      1 
ATOM   2307  O  O      . THR A 1 341 ? 13.07300  -15.50100 61.63800  1.000 87.59000  ? 332 THR A O      1 
ATOM   2308  C  CB     . THR A 1 341 ? 15.21900  -14.00500 59.60800  1.000 91.25000  ? 332 THR A CB     1 
ATOM   2309  O  OG1    . THR A 1 341 ? 16.33600  -13.11400 59.51000  1.000 109.50000 ? 332 THR A OG1    1 
ATOM   2310  C  CG2    . THR A 1 341 ? 13.92600  -13.22100 59.42100  1.000 100.41000 ? 332 THR A CG2    1 
ATOM   2311  N  N      . VAL A 1 342 ? 14.35000  -16.90300 60.42900  1.000 85.99000  ? 333 VAL A N      1 
ATOM   2312  C  CA     . VAL A 1 342 ? 13.36400  -17.98200 60.47400  1.000 91.31000  ? 333 VAL A CA     1 
ATOM   2313  C  C      . VAL A 1 342 ? 12.98600  -18.29300 61.91600  1.000 97.30000  ? 333 VAL A C      1 
ATOM   2314  O  O      . VAL A 1 342 ? 11.82200  -18.17500 62.32200  1.000 99.40000  ? 333 VAL A O      1 
ATOM   2315  C  CB     . VAL A 1 342 ? 13.90400  -19.23200 59.76000  1.000 76.22000  ? 333 VAL A CB     1 
ATOM   2316  C  CG1    . VAL A 1 342 ? 13.03000  -20.43600 60.06700  1.000 98.11000  ? 333 VAL A CG1    1 
ATOM   2317  C  CG2    . VAL A 1 342 ? 13.99500  -18.99100 58.26000  1.000 80.46000  ? 333 VAL A CG2    1 
ATOM   2318  N  N      . VAL A 1 343 ? 13.98100  -18.68000 62.71500  1.000 101.84000 ? 334 VAL A N      1 
ATOM   2319  C  CA     . VAL A 1 343 ? 13.71800  -19.17700 64.06200  1.000 111.81000 ? 334 VAL A CA     1 
ATOM   2320  C  C      . VAL A 1 343 ? 13.15900  -18.08000 64.95800  1.000 106.13000 ? 334 VAL A C      1 
ATOM   2321  O  O      . VAL A 1 343 ? 12.42000  -18.36400 65.90900  1.000 98.31000  ? 334 VAL A O      1 
ATOM   2322  C  CB     . VAL A 1 343 ? 14.99600  -19.79300 64.66000  1.000 106.28000 ? 334 VAL A CB     1 
ATOM   2323  C  CG1    . VAL A 1 343 ? 15.40700  -21.02600 63.87200  1.000 101.50000 ? 334 VAL A CG1    1 
ATOM   2324  C  CG2    . VAL A 1 343 ? 16.12000  -18.77000 64.67100  1.000 98.30000  ? 334 VAL A CG2    1 
ATOM   2325  N  N      . LEU A 1 344 ? 13.48700  -16.81800 64.68200  1.000 104.05000 ? 335 LEU A N      1 
ATOM   2326  C  CA     . LEU A 1 344 ? 13.01200  -15.74400 65.54600  1.000 108.27000 ? 335 LEU A CA     1 
ATOM   2327  C  C      . LEU A 1 344 ? 11.59600  -15.32300 65.16700  1.000 106.75000 ? 335 LEU A C      1 
ATOM   2328  O  O      . LEU A 1 344 ? 10.70600  -15.24700 66.02400  1.000 117.64000 ? 335 LEU A O      1 
ATOM   2329  C  CB     . LEU A 1 344 ? 13.97400  -14.55800 65.47000  1.000 109.25000 ? 335 LEU A CB     1 
ATOM   2330  C  CG     . LEU A 1 344 ? 13.88900  -13.53000 66.59500  1.000 117.34000 ? 335 LEU A CG     1 
ATOM   2331  C  CD1    . LEU A 1 344 ? 14.37000  -14.14300 67.89900  1.000 126.01000 ? 335 LEU A CD1    1 
ATOM   2332  C  CD2    . LEU A 1 344 ? 14.71200  -12.30200 66.24400  1.000 115.74000 ? 335 LEU A CD2    1 
ATOM   2333  N  N      . THR A 1 345 ? 11.36300  -15.05800 63.88300  1.000 92.41000  ? 336 THR A N      1 
ATOM   2334  C  CA     . THR A 1 345 ? 10.00300  -14.84000 63.42300  1.000 95.73000  ? 336 THR A CA     1 
ATOM   2335  C  C      . THR A 1 345 ? 9.09600   -16.01200 63.76100  1.000 102.34000 ? 336 THR A C      1 
ATOM   2336  O  O      . THR A 1 345 ? 7.87800   -15.83600 63.80700  1.000 109.07000 ? 336 THR A O      1 
ATOM   2337  C  CB     . THR A 1 345 ? 9.99700   -14.59200 61.91600  1.000 102.77000 ? 336 THR A CB     1 
ATOM   2338  O  OG1    . THR A 1 345 ? 10.67400  -15.66800 61.25300  1.000 98.05000  ? 336 THR A OG1    1 
ATOM   2339  C  CG2    . THR A 1 345 ? 10.70700  -13.28700 61.59500  1.000 100.60000 ? 336 THR A CG2    1 
ATOM   2340  N  N      . ALA A 1 346 ? 9.65700   -17.19600 64.02400  1.000 104.42000 ? 337 ALA A N      1 
ATOM   2341  C  CA     . ALA A 1 346 ? 8.85100   -18.28600 64.56400  1.000 102.05000 ? 337 ALA A CA     1 
ATOM   2342  C  C      . ALA A 1 346 ? 8.07700   -17.83800 65.79900  1.000 94.69000  ? 337 ALA A C      1 
ATOM   2343  O  O      . ALA A 1 346 ? 6.84000   -17.80500 65.80100  1.000 87.33000  ? 337 ALA A O      1 
ATOM   2344  C  CB     . ALA A 1 346 ? 9.74400   -19.48500 64.89100  1.000 99.99000  ? 337 ALA A CB     1 
ATOM   2345  N  N      . PHE A 1 347 ? 8.79600   -17.46600 66.86200  1.000 99.30000  ? 338 PHE A N      1 
ATOM   2346  C  CA     . PHE A 1 347 ? 8.11800   -17.00800 68.06900  1.000 102.28000 ? 338 PHE A CA     1 
ATOM   2347  C  C      . PHE A 1 347 ? 7.36600   -15.71200 67.80300  1.000 102.12000 ? 338 PHE A C      1 
ATOM   2348  O  O      . PHE A 1 347 ? 6.28400   -15.48900 68.36200  1.000 114.00000 ? 338 PHE A O      1 
ATOM   2349  C  CB     . PHE A 1 347 ? 9.11800   -16.84600 69.22100  1.000 109.73000 ? 338 PHE A CB     1 
ATOM   2350  C  CG     . PHE A 1 347 ? 9.66000   -15.44800 69.38300  1.000 122.56000 ? 338 PHE A CG     1 
ATOM   2351  C  CD1    . PHE A 1 347 ? 8.95900   -14.49500 70.11100  1.000 124.53000 ? 338 PHE A CD1    1 
ATOM   2352  C  CD2    . PHE A 1 347 ? 10.87700  -15.09200 68.83000  1.000 132.87000 ? 338 PHE A CD2    1 
ATOM   2353  C  CE1    . PHE A 1 347 ? 9.45300   -13.21300 70.26400  1.000 127.72000 ? 338 PHE A CE1    1 
ATOM   2354  C  CE2    . PHE A 1 347 ? 11.37700  -13.80800 68.98200  1.000 136.22000 ? 338 PHE A CE2    1 
ATOM   2355  C  CZ     . PHE A 1 347 ? 10.66400  -12.87000 69.70000  1.000 138.69000 ? 338 PHE A CZ     1 
ATOM   2356  N  N      . LEU A 1 348 ? 7.92600   -14.84000 66.96100  1.000 91.17000  ? 339 LEU A N      1 
ATOM   2357  C  CA     . LEU A 1 348 ? 7.23800   -13.59400 66.63700  1.000 101.74000 ? 339 LEU A CA     1 
ATOM   2358  C  C      . LEU A 1 348 ? 5.85900   -13.95300 66.09800  1.000 102.46000 ? 339 LEU A C      1 
ATOM   2359  O  O      . LEU A 1 348 ? 4.84000   -13.42100 66.55100  1.000 103.45000 ? 339 LEU A O      1 
ATOM   2360  C  CB     . LEU A 1 348 ? 8.00900   -12.81900 65.56700  1.000 102.96000 ? 339 LEU A CB     1 
ATOM   2361  C  CG     . LEU A 1 348 ? 7.19600   -11.74400 64.83500  1.000 101.03000 ? 339 LEU A CG     1 
ATOM   2362  C  CD1    . LEU A 1 348 ? 6.77700   -10.62400 65.78100  1.000 93.26000  ? 339 LEU A CD1    1 
ATOM   2363  C  CD2    . LEU A 1 348 ? 7.98200   -11.18200 63.66300  1.000 94.52000  ? 339 LEU A CD2    1 
ATOM   2364  N  N      . THR A 1 349 ? 5.81200   -14.86700 65.13000  1.000 105.24000 ? 340 THR A N      1 
ATOM   2365  C  CA     . THR A 1 349 ? 4.54000   -15.27500 64.55200  1.000 109.01000 ? 340 THR A CA     1 
ATOM   2366  C  C      . THR A 1 349 ? 3.63900   -16.00900 65.55200  1.000 115.55000 ? 340 THR A C      1 
ATOM   2367  O  O      . THR A 1 349 ? 2.42800   -15.76700 65.61900  1.000 128.48000 ? 340 THR A O      1 
ATOM   2368  C  CB     . THR A 1 349 ? 4.80000   -16.09200 63.28700  1.000 108.31000 ? 340 THR A CB     1 
ATOM   2369  O  OG1    . THR A 1 349 ? 5.54000   -15.29800 62.35100  1.000 108.92000 ? 340 THR A OG1    1 
ATOM   2370  C  CG2    . THR A 1 349 ? 3.49000   -16.52000 62.65100  1.000 112.99000 ? 340 THR A CG2    1 
ATOM   2371  N  N      . TYR A 1 350 ? 4.23100   -16.88400 66.37100  1.000 105.74000 ? 341 TYR A N      1 
ATOM   2372  C  CA     . TYR A 1 350 ? 3.41900   -17.59700 67.35200  1.000 114.25000 ? 341 TYR A CA     1 
ATOM   2373  C  C      . TYR A 1 350 ? 2.75800   -16.76500 68.44400  1.000 114.74000 ? 341 TYR A C      1 
ATOM   2374  O  O      . TYR A 1 350 ? 1.63700   -17.06800 68.86900  1.000 119.04000 ? 341 TYR A O      1 
ATOM   2375  C  CB     . TYR A 1 350 ? 4.30000   -18.68000 67.97200  1.000 120.15000 ? 341 TYR A CB     1 
ATOM   2376  C  CG     . TYR A 1 350 ? 3.48600   -19.72500 68.71200  1.000 138.03000 ? 341 TYR A CG     1 
ATOM   2377  C  CD1    . TYR A 1 350 ? 2.82100   -20.73300 68.02200  1.000 151.69000 ? 341 TYR A CD1    1 
ATOM   2378  C  CD2    . TYR A 1 350 ? 3.35900   -19.68900 70.09600  1.000 144.79000 ? 341 TYR A CD2    1 
ATOM   2379  C  CE1    . TYR A 1 350 ? 2.07000   -21.68400 68.69000  1.000 169.37000 ? 341 TYR A CE1    1 
ATOM   2380  C  CE2    . TYR A 1 350 ? 2.60900   -20.63600 70.77200  1.000 154.07000 ? 341 TYR A CE2    1 
ATOM   2381  C  CZ     . TYR A 1 350 ? 1.96800   -21.63000 70.06500  1.000 170.65000 ? 341 TYR A CZ     1 
ATOM   2382  O  OH     . TYR A 1 350 ? 1.22200   -22.57400 70.73500  1.000 160.70000 ? 341 TYR A OH     1 
ATOM   2383  N  N      . PHE A 1 351 ? 3.42200   -15.70300 68.89700  1.000 109.11000 ? 342 PHE A N      1 
ATOM   2384  C  CA     . PHE A 1 351 ? 2.85800   -14.90100 69.97700  1.000 116.72000 ? 342 PHE A CA     1 
ATOM   2385  C  C      . PHE A 1 351 ? 2.06900   -13.69700 69.47100  1.000 117.44000 ? 342 PHE A C      1 
ATOM   2386  O  O      . PHE A 1 351 ? 0.96200   -13.43900 69.95700  1.000 122.28000 ? 342 PHE A O      1 
ATOM   2387  C  CB     . PHE A 1 351 ? 3.96700   -14.43200 70.92400  1.000 120.91000 ? 342 PHE A CB     1 
ATOM   2388  C  CG     . PHE A 1 351 ? 4.83100   -15.54300 71.45400  1.000 126.56000 ? 342 PHE A CG     1 
ATOM   2389  C  CD1    . PHE A 1 351 ? 4.29300   -16.79000 71.72800  1.000 124.55000 ? 342 PHE A CD1    1 
ATOM   2390  C  CD2    . PHE A 1 351 ? 6.17800   -15.33400 71.69100  1.000 130.01000 ? 342 PHE A CD2    1 
ATOM   2391  C  CE1    . PHE A 1 351 ? 5.08900   -17.81300 72.21800  1.000 120.87000 ? 342 PHE A CE1    1 
ATOM   2392  C  CE2    . PHE A 1 351 ? 6.97700   -16.35000 72.18200  1.000 136.60000 ? 342 PHE A CE2    1 
ATOM   2393  C  CZ     . PHE A 1 351 ? 6.43200   -17.59100 72.44500  1.000 124.78000 ? 342 PHE A CZ     1 
ATOM   2394  N  N      . TYR A 1 352 ? 2.60300   -12.95900 68.49700  1.000 117.46000 ? 343 TYR A N      1 
ATOM   2395  C  CA     . TYR A 1 352 ? 1.93000   -11.74500 68.04700  1.000 119.10000 ? 343 TYR A CA     1 
ATOM   2396  C  C      . TYR A 1 352 ? 0.53900   -12.05100 67.50500  1.000 115.63000 ? 343 TYR A C      1 
ATOM   2397  O  O      . TYR A 1 352 ? -0.41700  -11.31200 67.77100  1.000 100.34000 ? 343 TYR A O      1 
ATOM   2398  C  CB     . TYR A 1 352 ? 2.77800   -11.04600 66.98500  1.000 118.99000 ? 343 TYR A CB     1 
ATOM   2399  C  CG     . TYR A 1 352 ? 2.47500   -9.57400  66.82300  1.000 120.54000 ? 343 TYR A CG     1 
ATOM   2400  C  CD1    . TYR A 1 352 ? 3.09700   -8.62500  67.62300  1.000 137.09000 ? 343 TYR A CD1    1 
ATOM   2401  C  CD2    . TYR A 1 352 ? 1.56700   -9.13400  65.87000  1.000 112.18000 ? 343 TYR A CD2    1 
ATOM   2402  C  CE1    . TYR A 1 352 ? 2.82400   -7.27800  67.47800  1.000 131.36000 ? 343 TYR A CE1    1 
ATOM   2403  C  CE2    . TYR A 1 352 ? 1.28700   -7.79100  65.71800  1.000 112.34000 ? 343 TYR A CE2    1 
ATOM   2404  C  CZ     . TYR A 1 352 ? 1.91800   -6.86700  66.52400  1.000 117.65000 ? 343 TYR A CZ     1 
ATOM   2405  O  OH     . TYR A 1 352 ? 1.64100   -5.52700  66.37500  1.000 115.00000 ? 343 TYR A OH     1 
ATOM   2406  N  N      . LEU A 1 353 ? 0.40500   -13.14100 66.75200  1.000 128.48000 ? 344 LEU A N      1 
ATOM   2407  C  CA     . LEU A 1 353 ? -0.84100  -13.48700 66.08200  1.000 131.06000 ? 344 LEU A CA     1 
ATOM   2408  C  C      . LEU A 1 353 ? -1.63800  -14.55900 66.81600  1.000 128.57000 ? 344 LEU A C      1 
ATOM   2409  O  O      . LEU A 1 353 ? -2.61000  -15.08000 66.25900  1.000 129.89000 ? 344 LEU A O      1 
ATOM   2410  C  CB     . LEU A 1 353 ? -0.55500  -13.94100 64.64900  1.000 124.92000 ? 344 LEU A CB     1 
ATOM   2411  C  CG     . LEU A 1 353 ? -0.01500  -12.86900 63.69900  1.000 102.48000 ? 344 LEU A CG     1 
ATOM   2412  C  CD1    . LEU A 1 353 ? 1.48500   -12.68000 63.89700  1.000 97.99000  ? 344 LEU A CD1    1 
ATOM   2413  C  CD2    . LEU A 1 353 ? -0.33400  -13.20700 62.25000  1.000 106.72000 ? 344 LEU A CD2    1 
ATOM   2414  N  N      . LYS A 1 354 ? -1.25300  -14.90800 68.04500  1.000 118.50000 ? 345 LYS A N      1 
ATOM   2415  C  CA     . LYS A 1 354 ? -1.99000  -15.93900 68.76800  1.000 118.14000 ? 345 LYS A CA     1 
ATOM   2416  C  C      . LYS A 1 354 ? -3.36600  -15.43800 69.18900  1.000 137.37000 ? 345 LYS A C      1 
ATOM   2417  O  O      . LYS A 1 354 ? -4.33600  -16.20500 69.20000  1.000 132.99000 ? 345 LYS A O      1 
ATOM   2418  C  CB     . LYS A 1 354 ? -1.18900  -16.40300 69.98400  1.000 113.71000 ? 345 LYS A CB     1 
ATOM   2419  N  N      . ASP A 1 355 ? -3.46900  -14.15700 69.53900  1.000 144.20000 ? 346 ASP A N      1 
ATOM   2420  C  CA     . ASP A 1 355 ? -4.71300  -13.56600 70.01500  1.000 138.34000 ? 346 ASP A CA     1 
ATOM   2421  C  C      . ASP A 1 355 ? -5.57800  -12.99100 68.90000  1.000 140.84000 ? 346 ASP A C      1 
ATOM   2422  O  O      . ASP A 1 355 ? -6.71400  -12.58600 69.17000  1.000 129.03000 ? 346 ASP A O      1 
ATOM   2423  C  CB     . ASP A 1 355 ? -4.41700  -12.46800 71.04100  1.000 130.05000 ? 346 ASP A CB     1 
ATOM   2424  C  CG     . ASP A 1 355 ? -3.63900  -12.98200 72.23500  1.000 149.95000 ? 346 ASP A CG     1 
ATOM   2425  O  OD1    . ASP A 1 355 ? -3.60100  -14.21500 72.43500  1.000 158.00000 ? 346 ASP A OD1    1 
ATOM   2426  O  OD2    . ASP A 1 355 ? -3.06900  -12.15300 72.97500  1.000 159.39000 ? 346 ASP A OD2    1 
ATOM   2427  N  N      . LEU A 1 356 ? -5.07700  -12.94000 67.66700  1.000 148.64000 ? 347 LEU A N      1 
ATOM   2428  C  CA     . LEU A 1 356 ? -5.82600  -12.32400 66.58000  1.000 138.09000 ? 347 LEU A CA     1 
ATOM   2429  C  C      . LEU A 1 356 ? -7.12900  -13.07400 66.32600  1.000 140.75000 ? 347 LEU A C      1 
ATOM   2430  O  O      . LEU A 1 356 ? -7.23900  -14.28000 66.56500  1.000 146.98000 ? 347 LEU A O      1 
ATOM   2431  C  CB     . LEU A 1 356 ? -4.98100  -12.28800 65.30600  1.000 133.25000 ? 347 LEU A CB     1 
ATOM   2432  N  N      . GLN A 1 357 ? -8.12600  -12.34100 65.83300  1.000 134.78000 ? 348 GLN A N      1 
ATOM   2433  C  CA     . GLN A 1 357 ? -9.46100  -12.87200 65.58800  1.000 134.48000 ? 348 GLN A CA     1 
ATOM   2434  C  C      . GLN A 1 357 ? -9.83200  -12.69900 64.12200  1.000 134.87000 ? 348 GLN A C      1 
ATOM   2435  O  O      . GLN A 1 357 ? -9.62000  -11.62600 63.54600  1.000 132.34000 ? 348 GLN A O      1 
ATOM   2436  C  CB     . GLN A 1 357 ? -10.49700 -12.17800 66.47800  1.000 113.98000 ? 348 GLN A CB     1 
ATOM   2437  N  N      . GLY A 1 358 ? -10.38700 -13.75000 63.52900  1.000 146.59000 ? 349 GLY A N      1 
ATOM   2438  C  CA     . GLY A 1 358 ? -10.85100 -13.70600 62.15900  1.000 147.33000 ? 349 GLY A CA     1 
ATOM   2439  C  C      . GLY A 1 358 ? -9.89800  -14.23900 61.11200  1.000 155.52000 ? 349 GLY A C      1 
ATOM   2440  O  O      . GLY A 1 358 ? -10.08800 -13.94200 59.92600  1.000 143.79000 ? 349 GLY A O      1 
ATOM   2441  N  N      . LEU A 1 359 ? -8.88700  -15.01800 61.50500  1.000 159.14000 ? 350 LEU A N      1 
ATOM   2442  C  CA     . LEU A 1 359 ? -7.92700  -15.52800 60.53400  1.000 144.08000 ? 350 LEU A CA     1 
ATOM   2443  C  C      . LEU A 1 359 ? -8.54200  -16.55500 59.59200  1.000 127.00000 ? 350 LEU A C      1 
ATOM   2444  O  O      . LEU A 1 359 ? -7.99100  -16.79100 58.51200  1.000 130.08000 ? 350 LEU A O      1 
ATOM   2445  C  CB     . LEU A 1 359 ? -6.72100  -16.13500 61.25200  1.000 138.88000 ? 350 LEU A CB     1 
ATOM   2446  C  CG     . LEU A 1 359 ? -5.94600  -15.19200 62.17500  1.000 138.91000 ? 350 LEU A CG     1 
ATOM   2447  C  CD1    . LEU A 1 359 ? -4.88400  -15.95200 62.96100  1.000 144.94000 ? 350 LEU A CD1    1 
ATOM   2448  C  CD2    . LEU A 1 359 ? -5.32500  -14.04900 61.38400  1.000 116.15000 ? 350 LEU A CD2    1 
ATOM   2449  N  N      . ASP A 1 360 ? -9.66400  -17.17000 59.97400  1.000 108.70000 ? 351 ASP A N      1 
ATOM   2450  C  CA     . ASP A 1 360 ? -10.33300 -18.09300 59.06400  1.000 110.60000 ? 351 ASP A CA     1 
ATOM   2451  C  C      . ASP A 1 360 ? -10.94300 -17.35700 57.88000  1.000 115.32000 ? 351 ASP A C      1 
ATOM   2452  O  O      . ASP A 1 360 ? -11.11200 -17.94500 56.80600  1.000 122.54000 ? 351 ASP A O      1 
ATOM   2453  C  CB     . ASP A 1 360 ? -11.40500 -18.88700 59.81000  1.000 108.24000 ? 351 ASP A CB     1 
ATOM   2454  N  N      . VAL A 1 361 ? -11.28500 -16.07900 58.05500  1.000 113.61000 ? 352 VAL A N      1 
ATOM   2455  C  CA     . VAL A 1 361 ? -11.80200 -15.28700 56.94500  1.000 117.08000 ? 352 VAL A CA     1 
ATOM   2456  C  C      . VAL A 1 361 ? -10.67100 -14.85800 56.01800  1.000 125.03000 ? 352 VAL A C      1 
ATOM   2457  O  O      . VAL A 1 361 ? -10.85000 -14.77800 54.79700  1.000 132.21000 ? 352 VAL A O      1 
ATOM   2458  C  CB     . VAL A 1 361 ? -12.59200 -14.07700 57.47500  1.000 109.78000 ? 352 VAL A CB     1 
ATOM   2459  C  CG1    . VAL A 1 361 ? -13.21000 -13.30200 56.32200  1.000 88.34000  ? 352 VAL A CG1    1 
ATOM   2460  C  CG2    . VAL A 1 361 ? -13.66400 -14.53100 58.45500  1.000 113.05000 ? 352 VAL A CG2    1 
ATOM   2461  N  N      . LEU A 1 362 ? -9.49400  -14.56900 56.58000  1.000 123.69000 ? 353 LEU A N      1 
ATOM   2462  C  CA     . LEU A 1 362 ? -8.34200  -14.20100 55.76400  1.000 118.83000 ? 353 LEU A CA     1 
ATOM   2463  C  C      . LEU A 1 362 ? -7.78900  -15.37800 54.97200  1.000 127.02000 ? 353 LEU A C      1 
ATOM   2464  O  O      . LEU A 1 362 ? -7.11700  -15.16400 53.95700  1.000 133.73000 ? 353 LEU A O      1 
ATOM   2465  C  CB     . LEU A 1 362 ? -7.24100  -13.61200 56.64400  1.000 102.04000 ? 353 LEU A CB     1 
ATOM   2466  C  CG     . LEU A 1 362 ? -7.44200  -12.16400 57.09000  1.000 129.14000 ? 353 LEU A CG     1 
ATOM   2467  C  CD1    . LEU A 1 362 ? -8.52700  -12.05800 58.15400  1.000 115.60000 ? 353 LEU A CD1    1 
ATOM   2468  C  CD2    . LEU A 1 362 ? -6.12900  -11.58800 57.59000  1.000 150.71000 ? 353 LEU A CD2    1 
ATOM   2469  N  N      . GLY A 1 363 ? -8.04600  -16.60000 55.41200  1.000 135.14000 ? 354 GLY A N      1 
ATOM   2470  C  CA     . GLY A 1 363 ? -7.56100  -17.78800 54.75400  1.000 123.62000 ? 354 GLY A CA     1 
ATOM   2471  C  C      . GLY A 1 363 ? -6.42900  -18.52300 55.45100  1.000 112.06000 ? 354 GLY A C      1 
ATOM   2472  O  O      . GLY A 1 363 ? -5.72300  -19.29400 54.78800  1.000 112.38000 ? 354 GLY A O      1 
ATOM   2473  N  N      . PHE A 1 364 ? -6.23500  -18.31400 56.75100  1.000 114.72000 ? 355 PHE A N      1 
ATOM   2474  C  CA     . PHE A 1 364 ? -5.18300  -19.00400 57.49200  1.000 108.88000 ? 355 PHE A CA     1 
ATOM   2475  C  C      . PHE A 1 364 ? -5.67700  -20.39800 57.86100  1.000 96.90000  ? 355 PHE A C      1 
ATOM   2476  O  O      . PHE A 1 364 ? -6.62300  -20.54300 58.64300  1.000 110.69000 ? 355 PHE A O      1 
ATOM   2477  C  CB     . PHE A 1 364 ? -4.79200  -18.21100 58.73700  1.000 117.15000 ? 355 PHE A CB     1 
ATOM   2478  C  CG     . PHE A 1 364 ? -4.07600  -16.91500 58.44400  1.000 115.91000 ? 355 PHE A CG     1 
ATOM   2479  C  CD1    . PHE A 1 364 ? -3.89200  -16.47900 57.14200  1.000 114.63000 ? 355 PHE A CD1    1 
ATOM   2480  C  CD2    . PHE A 1 364 ? -3.58100  -16.13700 59.47800  1.000 112.83000 ? 355 PHE A CD2    1 
ATOM   2481  C  CE1    . PHE A 1 364 ? -3.23400  -15.28800 56.87900  1.000 110.47000 ? 355 PHE A CE1    1 
ATOM   2482  C  CE2    . PHE A 1 364 ? -2.92100  -14.94800 59.22100  1.000 103.20000 ? 355 PHE A CE2    1 
ATOM   2483  C  CZ     . PHE A 1 364 ? -2.74700  -14.52400 57.92000  1.000 98.35000  ? 355 PHE A CZ     1 
ATOM   2484  N  N      . ARG A 1 365 ? -5.04100  -21.42400 57.30400  1.000 95.64000  ? 356 ARG A N      1 
ATOM   2485  C  CA     . ARG A 1 365 ? -5.39900  -22.80900 57.58000  1.000 100.70000 ? 356 ARG A CA     1 
ATOM   2486  C  C      . ARG A 1 365 ? -4.68400  -23.37500 58.80000  1.000 115.74000 ? 356 ARG A C      1 
ATOM   2487  O  O      . ARG A 1 365 ? -4.86900  -24.55500 59.11700  1.000 123.99000 ? 356 ARG A O      1 
ATOM   2488  C  CB     . ARG A 1 365 ? -5.11900  -23.68100 56.35200  1.000 102.77000 ? 356 ARG A CB     1 
ATOM   2489  C  CG     . ARG A 1 365 ? -6.06500  -23.39800 55.19500  1.000 121.40000 ? 356 ARG A CG     1 
ATOM   2490  C  CD     . ARG A 1 365 ? -5.70800  -24.19500 53.95300  1.000 111.05000 ? 356 ARG A CD     1 
ATOM   2491  N  NE     . ARG A 1 365 ? -6.68700  -23.99500 52.89000  1.000 134.76000 ? 356 ARG A NE     1 
ATOM   2492  C  CZ     . ARG A 1 365 ? -6.77200  -22.90000 52.14500  1.000 137.59000 ? 356 ARG A CZ     1 
ATOM   2493  N  NH1    . ARG A 1 365 ? -5.94600  -21.88000 52.31800  1.000 101.28000 ? 356 ARG A NH1    1 
ATOM   2494  N  NH2    . ARG A 1 365 ? -7.70800  -22.82600 51.20300  1.000 147.86000 ? 356 ARG A NH2    1 
ATOM   2495  N  N      . PHE A 1 366 ? -3.87000  -22.57000 59.48700  1.000 113.38000 ? 357 PHE A N      1 
ATOM   2496  C  CA     . PHE A 1 366 ? -3.17000  -23.04300 60.67400  1.000 106.11000 ? 357 PHE A CA     1 
ATOM   2497  C  C      . PHE A 1 366 ? -3.22900  -22.04400 61.82400  1.000 106.10000 ? 357 PHE A C      1 
ATOM   2498  O  O      . PHE A 1 366 ? -2.58800  -22.27300 62.85700  1.000 110.48000 ? 357 PHE A O      1 
ATOM   2499  C  CB     . PHE A 1 366 ? -1.71700  -23.37700 60.33200  1.000 106.48000 ? 357 PHE A CB     1 
ATOM   2500  C  CG     . PHE A 1 366 ? -1.57800  -24.57800 59.44900  1.000 108.90000 ? 357 PHE A CG     1 
ATOM   2501  C  CD1    . PHE A 1 366 ? -1.81400  -25.84700 59.94800  1.000 113.27000 ? 357 PHE A CD1    1 
ATOM   2502  C  CD2    . PHE A 1 366 ? -1.23200  -24.44000 58.11600  1.000 113.08000 ? 357 PHE A CD2    1 
ATOM   2503  C  CE1    . PHE A 1 366 ? -1.69600  -26.95800 59.13900  1.000 127.85000 ? 357 PHE A CE1    1 
ATOM   2504  C  CE2    . PHE A 1 366 ? -1.11300  -25.54800 57.30100  1.000 120.68000 ? 357 PHE A CE2    1 
ATOM   2505  C  CZ     . PHE A 1 366 ? -1.34500  -26.80800 57.81300  1.000 124.64000 ? 357 PHE A CZ     1 
ATOM   2506  N  N      . GLY A 1 367 ? -3.97700  -20.95500 61.67900  1.000 102.78000 ? 358 GLY A N      1 
ATOM   2507  C  CA     . GLY A 1 367 ? -4.15400  -19.98100 62.73700  1.000 104.59000 ? 358 GLY A CA     1 
ATOM   2508  C  C      . GLY A 1 367 ? -3.04100  -18.97000 62.92500  1.000 110.75000 ? 358 GLY A C      1 
ATOM   2509  O  O      . GLY A 1 367 ? -2.78600  -18.14600 62.04100  1.000 105.25000 ? 358 GLY A O      1 
ATOM   2510  N  N      . ALA A 1 368 ? -2.35600  -19.03400 64.06900  1.000 115.16000 ? 359 ALA A N      1 
ATOM   2511  C  CA     . ALA A 1 368 ? -1.39300  -17.99200 64.41200  1.000 113.21000 ? 359 ALA A CA     1 
ATOM   2512  C  C      . ALA A 1 368 ? -0.10100  -18.11800 63.61400  1.000 118.40000 ? 359 ALA A C      1 
ATOM   2513  O  O      . ALA A 1 368 ? 0.34600   -17.14800 62.99100  1.000 121.27000 ? 359 ALA A O      1 
ATOM   2514  C  CB     . ALA A 1 368 ? -1.10000  -18.02600 65.91400  1.000 123.59000 ? 359 ALA A CB     1 
ATOM   2515  N  N      . ILE A 1 369 ? 0.51600   -19.30500 63.61400  1.000 132.56000 ? 360 ILE A N      1 
ATOM   2516  C  CA     . ILE A 1 369 ? 1.82300   -19.46800 62.97900  1.000 124.35000 ? 360 ILE A CA     1 
ATOM   2517  C  C      . ILE A 1 369 ? 1.72800   -19.68400 61.48000  1.000 111.58000 ? 360 ILE A C      1 
ATOM   2518  O  O      . ILE A 1 369 ? 2.76700   -19.75100 60.80800  1.000 117.21000 ? 360 ILE A O      1 
ATOM   2519  C  CB     . ILE A 1 369 ? 2.60200   -20.64000 63.60700  1.000 124.46000 ? 360 ILE A CB     1 
ATOM   2520  C  CG1    . ILE A 1 369 ? 4.08500   -20.55500 63.23700  1.000 121.21000 ? 360 ILE A CG1    1 
ATOM   2521  C  CG2    . ILE A 1 369 ? 2.01200   -21.97100 63.16400  1.000 113.02000 ? 360 ILE A CG2    1 
ATOM   2522  C  CD1    . ILE A 1 369 ? 4.82200   -19.41300 63.91200  1.000 121.51000 ? 360 ILE A CD1    1 
ATOM   2523  N  N      . SER A 1 370 ? 0.51800   -19.76800 60.93200  1.000 102.29000 ? 361 SER A N      1 
ATOM   2524  C  CA     . SER A 1 370 ? 0.30300   -20.04300 59.51900  1.000 98.78000  ? 361 SER A CA     1 
ATOM   2525  C  C      . SER A 1 370 ? 1.18400   -19.14300 58.65600  1.000 86.44000  ? 361 SER A C      1 
ATOM   2526  O  O      . SER A 1 370 ? 2.04900   -19.64400 57.92400  1.000 87.02000  ? 361 SER A O      1 
ATOM   2527  C  CB     . SER A 1 370 ? -1.17600  -19.86400 59.16700  1.000 108.15000 ? 361 SER A CB     1 
ATOM   2528  O  OG     . SER A 1 370 ? -1.46400  -20.38100 57.88000  1.000 120.47000 ? 361 SER A OG     1 
ATOM   2529  N  N      . PRO A 1 371 ? 1.03300   -17.81800 58.73500  1.000 71.16000  ? 362 PRO A N      1 
ATOM   2530  C  CA     . PRO A 1 371 ? 1.81600   -16.95500 57.83800  1.000 72.67000  ? 362 PRO A CA     1 
ATOM   2531  C  C      . PRO A 1 371 ? 3.31200   -17.10600 58.02600  1.000 92.93000  ? 362 PRO A C      1 
ATOM   2532  O  O      . PRO A 1 371 ? 4.07100   -16.89200 57.07100  1.000 96.23000  ? 362 PRO A O      1 
ATOM   2533  C  CB     . PRO A 1 371 ? 1.33900   -15.54200 58.19900  1.000 66.65000  ? 362 PRO A CB     1 
ATOM   2534  C  CG     . PRO A 1 371 ? 0.85600   -15.65400 59.60000  1.000 89.21000  ? 362 PRO A CG     1 
ATOM   2535  C  CD     . PRO A 1 371 ? 0.29100   -17.04200 59.74500  1.000 90.40000  ? 362 PRO A CD     1 
ATOM   2536  N  N      . TRP A 1 372 ? 3.76500   -17.50100 59.21900  1.000 103.24000 ? 363 TRP A N      1 
ATOM   2537  C  CA     . TRP A 1 372 ? 5.19600   -17.70100 59.41100  1.000 99.29000  ? 363 TRP A CA     1 
ATOM   2538  C  C      . TRP A 1 372 ? 5.73100   -18.71500 58.41200  1.000 85.21000  ? 363 TRP A C      1 
ATOM   2539  O  O      . TRP A 1 372 ? 6.80300   -18.51700 57.82500  1.000 86.57000  ? 363 TRP A O      1 
ATOM   2540  C  CB     . TRP A 1 372 ? 5.48900   -18.14200 60.84500  1.000 104.65000 ? 363 TRP A CB     1 
ATOM   2541  C  CG     . TRP A 1 372 ? 6.92300   -18.52700 61.07100  1.000 112.16000 ? 363 TRP A CG     1 
ATOM   2542  C  CD1    . TRP A 1 372 ? 8.00200   -17.69000 61.10700  1.000 103.89000 ? 363 TRP A CD1    1 
ATOM   2543  C  CD2    . TRP A 1 372 ? 7.43300   -19.84700 61.29800  1.000 113.63000 ? 363 TRP A CD2    1 
ATOM   2544  N  NE1    . TRP A 1 372 ? 9.15200   -18.40800 61.33700  1.000 101.72000 ? 363 TRP A NE1    1 
ATOM   2545  C  CE2    . TRP A 1 372 ? 8.82900   -19.73400 61.45900  1.000 109.13000 ? 363 TRP A CE2    1 
ATOM   2546  C  CE3    . TRP A 1 372 ? 6.84500   -21.11300 61.37700  1.000 106.99000 ? 363 TRP A CE3    1 
ATOM   2547  C  CZ2    . TRP A 1 372 ? 9.64400   -20.83900 61.69700  1.000 105.11000 ? 363 TRP A CZ2    1 
ATOM   2548  C  CZ3    . TRP A 1 372 ? 7.65600   -22.20800 61.61400  1.000 101.09000 ? 363 TRP A CZ3    1 
ATOM   2549  C  CH2    . TRP A 1 372 ? 9.04000   -22.06400 61.77100  1.000 93.26000  ? 363 TRP A CH2    1 
ATOM   2550  N  N      . PHE A 1 373 ? 4.96900   -19.78300 58.16200  1.000 82.09000  ? 364 PHE A N      1 
ATOM   2551  C  CA     . PHE A 1 373 ? 5.38400   -20.74500 57.15000  1.000 77.61000  ? 364 PHE A CA     1 
ATOM   2552  C  C      . PHE A 1 373 ? 5.62400   -20.04200 55.82300  1.000 89.22000  ? 364 PHE A C      1 
ATOM   2553  O  O      . PHE A 1 373 ? 6.69000   -20.18800 55.21200  1.000 100.22000 ? 364 PHE A O      1 
ATOM   2554  C  CB     . PHE A 1 373 ? 4.32800   -21.84200 56.99300  1.000 78.74000  ? 364 PHE A CB     1 
ATOM   2555  C  CG     . PHE A 1 373 ? 4.02600   -22.58800 58.26400  1.000 99.29000  ? 364 PHE A CG     1 
ATOM   2556  C  CD1    . PHE A 1 373 ? 4.90500   -23.54000 58.75300  1.000 89.02000  ? 364 PHE A CD1    1 
ATOM   2557  C  CD2    . PHE A 1 373 ? 2.84600   -22.35600 58.95500  1.000 111.63000 ? 364 PHE A CD2    1 
ATOM   2558  C  CE1    . PHE A 1 373 ? 4.62300   -24.23100 59.91700  1.000 85.29000  ? 364 PHE A CE1    1 
ATOM   2559  C  CE2    . PHE A 1 373 ? 2.55900   -23.04500 60.11700  1.000 97.52000  ? 364 PHE A CE2    1 
ATOM   2560  C  CZ     . PHE A 1 373 ? 3.44900   -23.98300 60.59800  1.000 100.09000 ? 364 PHE A CZ     1 
ATOM   2561  N  N      . SER A 1 374 ? 4.66600   -19.21600 55.39400  1.000 94.20000  ? 365 SER A N      1 
ATOM   2562  C  CA     . SER A 1 374 ? 4.84800   -18.45700 54.16200  1.000 95.84000  ? 365 SER A CA     1 
ATOM   2563  C  C      . SER A 1 374 ? 6.19000   -17.74100 54.16800  1.000 89.11000  ? 365 SER A C      1 
ATOM   2564  O  O      . SER A 1 374 ? 6.96400   -17.83400 53.20700  1.000 87.83000  ? 365 SER A O      1 
ATOM   2565  C  CB     . SER A 1 374 ? 3.70400   -17.45600 53.97900  1.000 95.96000  ? 365 SER A CB     1 
ATOM   2566  O  OG     . SER A 1 374 ? 2.43900   -18.09200 54.05100  1.000 103.02000 ? 365 SER A OG     1 
ATOM   2567  N  N      . ALA A 1 375 ? 6.50900   -17.06700 55.27500  1.000 84.74000  ? 366 ALA A N      1 
ATOM   2568  C  CA     . ALA A 1 375 ? 7.77300   -16.34500 55.34600  1.000 84.93000  ? 366 ALA A CA     1 
ATOM   2569  C  C      . ALA A 1 375 ? 8.93700   -17.27600 55.04200  1.000 86.63000  ? 366 ALA A C      1 
ATOM   2570  O  O      . ALA A 1 375 ? 9.74800   -17.00600 54.14600  1.000 79.65000  ? 366 ALA A O      1 
ATOM   2571  C  CB     . ALA A 1 375 ? 7.93300   -15.70400 56.72300  1.000 82.92000  ? 366 ALA A CB     1 
ATOM   2572  N  N      . ILE A 1 376 ? 9.00300   -18.41100 55.74000  1.000 92.27000  ? 367 ILE A N      1 
ATOM   2573  C  CA     . ILE A 1 376 ? 10.11500  -19.32500 55.51100  1.000 80.33000  ? 367 ILE A CA     1 
ATOM   2574  C  C      . ILE A 1 376 ? 10.05300  -19.85700 54.09000  1.000 79.04000  ? 367 ILE A C      1 
ATOM   2575  O  O      . ILE A 1 376 ? 11.08400  -20.01700 53.42300  1.000 88.11000  ? 367 ILE A O      1 
ATOM   2576  C  CB     . ILE A 1 376 ? 10.11500  -20.46500 56.54700  1.000 83.34000  ? 367 ILE A CB     1 
ATOM   2577  C  CG1    . ILE A 1 376 ? 8.87200   -21.34000 56.39300  1.000 68.34000  ? 367 ILE A CG1    1 
ATOM   2578  C  CG2    . ILE A 1 376 ? 10.19700  -19.90400 57.96100  1.000 90.62000  ? 367 ILE A CG2    1 
ATOM   2579  C  CD1    . ILE A 1 376 ? 8.91200   -22.60100 57.22200  1.000 75.39000  ? 367 ILE A CD1    1 
ATOM   2580  N  N      . ILE A 1 377 ? 8.83800   -20.08600 53.58300  1.000 76.53000  ? 368 ILE A N      1 
ATOM   2581  C  CA     . ILE A 1 377 ? 8.70000   -20.58500 52.22000  1.000 78.89000  ? 368 ILE A CA     1 
ATOM   2582  C  C      . ILE A 1 377 ? 9.30000   -19.59300 51.24000  1.000 74.39000  ? 368 ILE A C      1 
ATOM   2583  O  O      . ILE A 1 377 ? 9.85900   -19.98700 50.20800  1.000 69.81000  ? 368 ILE A O      1 
ATOM   2584  C  CB     . ILE A 1 377 ? 7.22100   -20.87300 51.89600  1.000 69.86000  ? 368 ILE A CB     1 
ATOM   2585  C  CG1    . ILE A 1 377 ? 6.68300   -21.99200 52.78900  1.000 82.03000  ? 368 ILE A CG1    1 
ATOM   2586  C  CG2    . ILE A 1 377 ? 7.06200   -21.25200 50.43400  1.000 63.57000  ? 368 ILE A CG2    1 
ATOM   2587  C  CD1    . ILE A 1 377 ? 7.33900   -23.33000 52.54500  1.000 105.94000 ? 368 ILE A CD1    1 
ATOM   2588  N  N      . GLY A 1 378 ? 9.21400   -18.29800 51.54200  1.000 64.85000  ? 369 GLY A N      1 
ATOM   2589  C  CA     . GLY A 1 378 ? 9.91400   -17.33200 50.71700  1.000 64.57000  ? 369 GLY A CA     1 
ATOM   2590  C  C      . GLY A 1 378 ? 11.41900  -17.44400 50.86700  1.000 81.76000  ? 369 GLY A C      1 
ATOM   2591  O  O      . GLY A 1 378 ? 12.14900  -17.53600 49.87400  1.000 92.65000  ? 369 GLY A O      1 
ATOM   2592  N  N      . ILE A 1 379 ? 11.89700  -17.51700 52.11200  1.000 83.30000  ? 370 ILE A N      1 
ATOM   2593  C  CA     . ILE A 1 379 ? 13.33700  -17.56700 52.36000  1.000 83.06000  ? 370 ILE A CA     1 
ATOM   2594  C  C      . ILE A 1 379 ? 13.96600  -18.72900 51.60200  1.000 74.94000  ? 370 ILE A C      1 
ATOM   2595  O  O      . ILE A 1 379 ? 14.80700  -18.53700 50.71400  1.000 84.50000  ? 370 ILE A O      1 
ATOM   2596  C  CB     . ILE A 1 379 ? 13.61900  -17.66200 53.86900  1.000 75.11000  ? 370 ILE A CB     1 
ATOM   2597  C  CG1    . ILE A 1 379 ? 13.03200  -16.45100 54.59700  1.000 68.22000  ? 370 ILE A CG1    1 
ATOM   2598  C  CG2    . ILE A 1 379 ? 15.11500  -17.77300 54.12300  1.000 78.07000  ? 370 ILE A CG2    1 
ATOM   2599  C  CD1    . ILE A 1 379 ? 12.96800  -16.61100 56.10000  1.000 67.98000  ? 370 ILE A CD1    1 
ATOM   2600  N  N      . PHE A 1 380 ? 13.52900  -19.95100 51.91000  1.000 61.76000  ? 371 PHE A N      1 
ATOM   2601  C  CA     . PHE A 1 380 ? 14.09000  -21.11400 51.23500  1.000 76.90000  ? 371 PHE A CA     1 
ATOM   2602  C  C      . PHE A 1 380 ? 13.91100  -21.09100 49.72700  1.000 75.23000  ? 371 PHE A C      1 
ATOM   2603  O  O      . PHE A 1 380 ? 14.72600  -21.66700 48.99600  1.000 84.39000  ? 371 PHE A O      1 
ATOM   2604  C  CB     . PHE A 1 380 ? 13.49900  -22.39600 51.81900  1.000 81.31000  ? 371 PHE A CB     1 
ATOM   2605  C  CG     . PHE A 1 380 ? 13.60200  -22.47800 53.31400  1.000 102.29000 ? 371 PHE A CG     1 
ATOM   2606  C  CD1    . PHE A 1 380 ? 14.80400  -22.21500 53.95000  1.000 110.58000 ? 371 PHE A CD1    1 
ATOM   2607  C  CD2    . PHE A 1 380 ? 12.49900  -22.80300 54.08500  1.000 115.68000 ? 371 PHE A CD2    1 
ATOM   2608  C  CE1    . PHE A 1 380 ? 14.90800  -22.28200 55.32500  1.000 108.09000 ? 371 PHE A CE1    1 
ATOM   2609  C  CE2    . PHE A 1 380 ? 12.59600  -22.87100 55.46200  1.000 127.29000 ? 371 PHE A CE2    1 
ATOM   2610  C  CZ     . PHE A 1 380 ? 13.80200  -22.61000 56.08200  1.000 106.87000 ? 371 PHE A CZ     1 
ATOM   2611  N  N      . SER A 1 381 ? 12.85900  -20.43200 49.24000  1.000 59.70000  ? 372 SER A N      1 
ATOM   2612  C  CA     . SER A 1 381 ? 12.71200  -20.27400 47.79900  1.000 60.15000  ? 372 SER A CA     1 
ATOM   2613  C  C      . SER A 1 381 ? 13.79100  -19.36300 47.22600  1.000 76.61000  ? 372 SER A C      1 
ATOM   2614  O  O      . SER A 1 381 ? 14.47600  -19.71800 46.25600  1.000 70.16000  ? 372 SER A O      1 
ATOM   2615  C  CB     . SER A 1 381 ? 11.33700  -19.69300 47.47600  1.000 57.47000  ? 372 SER A CB     1 
ATOM   2616  O  OG     . SER A 1 381 ? 10.30900  -20.59900 47.82600  1.000 55.57000  ? 372 SER A OG     1 
ATOM   2617  N  N      . GLY A 1 382 ? 14.01400  -18.21600 47.87300  1.000 88.03000  ? 373 GLY A N      1 
ATOM   2618  C  CA     . GLY A 1 382 ? 15.02000  -17.29200 47.37800  1.000 75.50000  ? 373 GLY A CA     1 
ATOM   2619  C  C      . GLY A 1 382 ? 16.34300  -18.01100 47.24700  1.000 86.72000  ? 373 GLY A C      1 
ATOM   2620  O  O      . GLY A 1 382 ? 16.95900  -18.02100 46.17700  1.000 91.31000  ? 373 GLY A O      1 
ATOM   2621  N  N      . ILE A 1 383 ? 16.76700  -18.68300 48.32000  1.000 87.60000  ? 374 ILE A N      1 
ATOM   2622  C  CA     . ILE A 1 383 ? 17.99900  -19.46100 48.26100  1.000 85.26000  ? 374 ILE A CA     1 
ATOM   2623  C  C      . ILE A 1 383 ? 17.98100  -20.35400 47.03200  1.000 76.62000  ? 374 ILE A C      1 
ATOM   2624  O  O      . ILE A 1 383 ? 18.86900  -20.28200 46.17300  1.000 84.84000  ? 374 ILE A O      1 
ATOM   2625  C  CB     . ILE A 1 383 ? 18.18000  -20.28400 49.54900  1.000 84.53000  ? 374 ILE A CB     1 
ATOM   2626  C  CG1    . ILE A 1 383 ? 18.39400  -19.35700 50.74800  1.000 101.28000 ? 374 ILE A CG1    1 
ATOM   2627  C  CG2    . ILE A 1 383 ? 19.33400  -21.26600 49.39600  1.000 85.60000  ? 374 ILE A CG2    1 
ATOM   2628  C  CD1    . ILE A 1 383 ? 17.98800  -19.96700 52.07300  1.000 107.18000 ? 374 ILE A CD1    1 
ATOM   2629  N  N      . LEU A 1 384 ? 16.92300  -21.15500 46.89000  1.000 62.64000  ? 375 LEU A N      1 
ATOM   2630  C  CA     . LEU A 1 384 ? 16.86900  -22.07100 45.76100  1.000 79.77000  ? 375 LEU A CA     1 
ATOM   2631  C  C      . LEU A 1 384 ? 16.97900  -21.30400 44.45300  1.000 81.05000  ? 375 LEU A C      1 
ATOM   2632  O  O      . LEU A 1 384 ? 17.81300  -21.62700 43.59600  1.000 80.73000  ? 375 LEU A O      1 
ATOM   2633  C  CB     . LEU A 1 384 ? 15.57800  -22.89000 45.80500  1.000 54.84000  ? 375 LEU A CB     1 
ATOM   2634  C  CG     . LEU A 1 384 ? 15.48200  -23.94200 46.91200  1.000 71.65000  ? 375 LEU A CG     1 
ATOM   2635  C  CD1    . LEU A 1 384 ? 14.23900  -24.79600 46.73200  1.000 37.44000  ? 375 LEU A CD1    1 
ATOM   2636  C  CD2    . LEU A 1 384 ? 16.73000  -24.80800 46.93400  1.000 91.86000  ? 375 LEU A CD2    1 
ATOM   2637  N  N      . ILE A 1 385 ? 16.21500  -20.21700 44.32700  1.000 81.98000  ? 376 ILE A N      1 
ATOM   2638  C  CA     . ILE A 1 385 ? 16.26000  -19.45300 43.08800  1.000 77.82000  ? 376 ILE A CA     1 
ATOM   2639  C  C      . ILE A 1 385 ? 17.67300  -18.95800 42.84200  1.000 84.16000  ? 376 ILE A C      1 
ATOM   2640  O  O      . ILE A 1 385 ? 18.20700  -19.08600 41.73200  1.000 97.37000  ? 376 ILE A O      1 
ATOM   2641  C  CB     . ILE A 1 385 ? 15.24600  -18.29500 43.13200  1.000 76.57000  ? 376 ILE A CB     1 
ATOM   2642  C  CG1    . ILE A 1 385 ? 13.82000  -18.83100 42.97500  1.000 72.92000  ? 376 ILE A CG1    1 
ATOM   2643  C  CG2    . ILE A 1 385 ? 15.56400  -17.27000 42.05200  1.000 67.91000  ? 376 ILE A CG2    1 
ATOM   2644  C  CD1    . ILE A 1 385 ? 12.74500  -17.86400 43.42800  1.000 57.70000  ? 376 ILE A CD1    1 
ATOM   2645  N  N      . GLY A 1 386 ? 18.33400  -18.46200 43.89000  1.000 81.33000  ? 377 GLY A N      1 
ATOM   2646  C  CA     . GLY A 1 386 ? 19.72400  -18.07600 43.73500  1.000 78.71000  ? 377 GLY A CA     1 
ATOM   2647  C  C      . GLY A 1 386 ? 20.55500  -19.21100 43.18100  1.000 77.44000  ? 377 GLY A C      1 
ATOM   2648  O  O      . GLY A 1 386 ? 21.17700  -19.08500 42.12000  1.000 76.93000  ? 377 GLY A O      1 
ATOM   2649  N  N      . PHE A 1 387 ? 20.50000  -20.37100 43.84200  1.000 71.21000  ? 378 PHE A N      1 
ATOM   2650  C  CA     . PHE A 1 387 ? 21.26300  -21.51400 43.36100  1.000 64.29000  ? 378 PHE A CA     1 
ATOM   2651  C  C      . PHE A 1 387 ? 20.95000  -21.78200 41.89900  1.000 73.08000  ? 378 PHE A C      1 
ATOM   2652  O  O      . PHE A 1 387 ? 21.85800  -22.02400 41.09300  1.000 66.66000  ? 378 PHE A O      1 
ATOM   2653  C  CB     . PHE A 1 387 ? 20.96500  -22.74800 44.21500  1.000 46.90000  ? 378 PHE A CB     1 
ATOM   2654  N  N      . TRP A 1 388 ? 19.67700  -21.65100 41.51800  1.000 88.39000  ? 379 TRP A N      1 
ATOM   2655  C  CA     . TRP A 1 388 ? 19.30500  -21.94400 40.14000  1.000 82.45000  ? 379 TRP A CA     1 
ATOM   2656  C  C      . TRP A 1 388 ? 20.06300  -21.04700 39.17700  1.000 70.08000  ? 379 TRP A C      1 
ATOM   2657  O  O      . TRP A 1 388 ? 20.68000  -21.52900 38.21800  1.000 67.74000  ? 379 TRP A O      1 
ATOM   2658  C  CB     . TRP A 1 388 ? 17.79700  -21.79600 39.94600  1.000 75.94000  ? 379 TRP A CB     1 
ATOM   2659  C  CG     . TRP A 1 388 ? 17.06400  -23.05500 40.24600  1.000 72.22000  ? 379 TRP A CG     1 
ATOM   2660  C  CD1    . TRP A 1 388 ? 16.09000  -23.24100 41.18200  1.000 61.38000  ? 379 TRP A CD1    1 
ATOM   2661  C  CD2    . TRP A 1 388 ? 17.28500  -24.33000 39.63400  1.000 69.09000  ? 379 TRP A CD2    1 
ATOM   2662  N  NE1    . TRP A 1 388 ? 15.66900  -24.55000 41.17100  1.000 59.79000  ? 379 TRP A NE1    1 
ATOM   2663  C  CE2    . TRP A 1 388 ? 16.39100  -25.23900 40.23200  1.000 70.35000  ? 379 TRP A CE2    1 
ATOM   2664  C  CE3    . TRP A 1 388 ? 18.14600  -24.78700 38.63000  1.000 55.56000  ? 379 TRP A CE3    1 
ATOM   2665  C  CZ2    . TRP A 1 388 ? 16.33300  -26.58000 39.85900  1.000 88.52000  ? 379 TRP A CZ2    1 
ATOM   2666  C  CZ3    . TRP A 1 388 ? 18.08700  -26.11400 38.26100  1.000 47.62000  ? 379 TRP A CZ3    1 
ATOM   2667  C  CH2    . TRP A 1 388 ? 17.18700  -26.99700 38.87400  1.000 64.93000  ? 379 TRP A CH2    1 
ATOM   2668  N  N      . ALA A 1 389 ? 20.05900  -19.73700 39.43400  1.000 70.27000  ? 380 ALA A N      1 
ATOM   2669  C  CA     . ALA A 1 389 ? 20.83600  -18.84100 38.59000  1.000 74.77000  ? 380 ALA A CA     1 
ATOM   2670  C  C      . ALA A 1 389 ? 22.26200  -19.35400 38.45800  1.000 79.47000  ? 380 ALA A C      1 
ATOM   2671  O  O      . ALA A 1 389 ? 22.77200  -19.54500 37.34500  1.000 86.29000  ? 380 ALA A O      1 
ATOM   2672  C  CB     . ALA A 1 389 ? 20.81300  -17.42300 39.16300  1.000 74.35000  ? 380 ALA A CB     1 
ATOM   2673  N  N      . GLU A 1 390 ? 22.88400  -19.67900 39.59300  1.000 79.81000  ? 381 GLU A N      1 
ATOM   2674  C  CA     . GLU A 1 390 ? 24.24900  -20.18500 39.56700  1.000 85.11000  ? 381 GLU A CA     1 
ATOM   2675  C  C      . GLU A 1 390 ? 24.36600  -21.34400 38.59200  1.000 78.80000  ? 381 GLU A C      1 
ATOM   2676  O  O      . GLU A 1 390 ? 25.19600  -21.32200 37.67400  1.000 71.59000  ? 381 GLU A O      1 
ATOM   2677  C  CB     . GLU A 1 390 ? 24.67000  -20.61300 40.97400  1.000 87.41000  ? 381 GLU A CB     1 
ATOM   2678  C  CG     . GLU A 1 390 ? 26.13100  -21.00200 41.11000  1.000 66.96000  ? 381 GLU A CG     1 
ATOM   2679  C  CD     . GLU A 1 390 ? 26.45700  -21.54400 42.48800  1.000 89.64000  ? 381 GLU A CD     1 
ATOM   2680  O  OE1    . GLU A 1 390 ? 25.74600  -21.18800 43.45200  1.000 99.61000  ? 381 GLU A OE1    1 
ATOM   2681  O  OE2    . GLU A 1 390 ? 27.42300  -22.32800 42.60800  1.000 96.21000  ? 381 GLU A OE2    1 
ATOM   2682  N  N      . TYR A 1 391 ? 23.48000  -22.33400 38.73100  1.000 81.30000  ? 382 TYR A N      1 
ATOM   2683  C  CA     . TYR A 1 391 ? 23.59500  -23.53800 37.91900  1.000 78.70000  ? 382 TYR A CA     1 
ATOM   2684  C  C      . TYR A 1 391 ? 23.63600  -23.19900 36.43500  1.000 76.56000  ? 382 TYR A C      1 
ATOM   2685  O  O      . TYR A 1 391 ? 24.39700  -23.80700 35.67300  1.000 81.01000  ? 382 TYR A O      1 
ATOM   2686  C  CB     . TYR A 1 391 ? 22.44100  -24.49500 38.22700  1.000 78.11000  ? 382 TYR A CB     1 
ATOM   2687  C  CG     . TYR A 1 391 ? 22.43100  -25.72700 37.35200  1.000 77.77000  ? 382 TYR A CG     1 
ATOM   2688  C  CD1    . TYR A 1 391 ? 23.52100  -26.58600 37.31900  1.000 93.10000  ? 382 TYR A CD1    1 
ATOM   2689  C  CD2    . TYR A 1 391 ? 21.33700  -26.02800 36.55300  1.000 88.43000  ? 382 TYR A CD2    1 
ATOM   2690  C  CE1    . TYR A 1 391 ? 23.52100  -27.71400 36.51900  1.000 86.57000  ? 382 TYR A CE1    1 
ATOM   2691  C  CE2    . TYR A 1 391 ? 21.32800  -27.15300 35.74900  1.000 87.80000  ? 382 TYR A CE2    1 
ATOM   2692  C  CZ     . TYR A 1 391 ? 22.42300  -27.99200 35.73600  1.000 70.83000  ? 382 TYR A CZ     1 
ATOM   2693  O  OH     . TYR A 1 391 ? 22.42200  -29.11500 34.94000  1.000 78.74000  ? 382 TYR A OH     1 
ATOM   2694  N  N      . TYR A 1 392 ? 22.83300  -22.22800 36.00400  1.000 82.38000  ? 383 TYR A N      1 
ATOM   2695  C  CA     . TYR A 1 392 ? 22.76100  -21.91600 34.58400  1.000 70.71000  ? 383 TYR A CA     1 
ATOM   2696  C  C      . TYR A 1 392 ? 23.77600  -20.87500 34.13800  1.000 78.06000  ? 383 TYR A C      1 
ATOM   2697  O  O      . TYR A 1 392 ? 23.98000  -20.71500 32.93000  1.000 68.96000  ? 383 TYR A O      1 
ATOM   2698  C  CB     . TYR A 1 392 ? 21.35600  -21.43500 34.21000  1.000 75.22000  ? 383 TYR A CB     1 
ATOM   2699  C  CG     . TYR A 1 392 ? 20.41500  -22.53400 33.76900  1.000 70.06000  ? 383 TYR A CG     1 
ATOM   2700  C  CD1    . TYR A 1 392 ? 20.40200  -22.97400 32.45000  1.000 55.48000  ? 383 TYR A CD1    1 
ATOM   2701  C  CD2    . TYR A 1 392 ? 19.52200  -23.11400 34.66200  1.000 73.41000  ? 383 TYR A CD2    1 
ATOM   2702  C  CE1    . TYR A 1 392 ? 19.53700  -23.97200 32.03700  1.000 46.42000  ? 383 TYR A CE1    1 
ATOM   2703  C  CE2    . TYR A 1 392 ? 18.65100  -24.11400 34.25700  1.000 62.87000  ? 383 TYR A CE2    1 
ATOM   2704  C  CZ     . TYR A 1 392 ? 18.66300  -24.53700 32.94400  1.000 49.06000  ? 383 TYR A CZ     1 
ATOM   2705  O  OH     . TYR A 1 392 ? 17.80200  -25.52800 32.53500  1.000 46.68000  ? 383 TYR A OH     1 
ATOM   2706  N  N      . THR A 1 393 ? 24.42400  -20.17100 35.06500  1.000 80.28000  ? 384 THR A N      1 
ATOM   2707  C  CA     . THR A 1 393 ? 25.23700  -19.02800 34.68200  1.000 82.48000  ? 384 THR A CA     1 
ATOM   2708  C  C      . THR A 1 393 ? 26.72200  -19.19300 34.97500  1.000 81.03000  ? 384 THR A C      1 
ATOM   2709  O  O      . THR A 1 393 ? 27.49800  -18.27800 34.67300  1.000 74.74000  ? 384 THR A O      1 
ATOM   2710  C  CB     . THR A 1 393 ? 24.70800  -17.76100 35.37400  1.000 79.02000  ? 384 THR A CB     1 
ATOM   2711  O  OG1    . THR A 1 393 ? 25.27600  -16.59500 34.76400  1.000 77.23000  ? 384 THR A OG1    1 
ATOM   2712  C  CG2    . THR A 1 393 ? 25.05700  -17.77400 36.85300  1.000 82.90000  ? 384 THR A CG2    1 
ATOM   2713  N  N      . SER A 1 394 ? 27.15000  -20.32500 35.53000  1.000 89.23000  ? 385 SER A N      1 
ATOM   2714  C  CA     . SER A 1 394 ? 28.54500  -20.51900 35.89300  1.000 97.61000  ? 385 SER A CA     1 
ATOM   2715  C  C      . SER A 1 394 ? 29.13400  -21.67100 35.09100  1.000 95.91000  ? 385 SER A C      1 
ATOM   2716  O  O      . SER A 1 394 ? 28.43500  -22.62800 34.74200  1.000 95.96000  ? 385 SER A O      1 
ATOM   2717  C  CB     . SER A 1 394 ? 28.71300  -20.79500 37.39900  1.000 92.70000  ? 385 SER A CB     1 
ATOM   2718  O  OG     . SER A 1 394 ? 28.04900  -21.98200 37.79700  1.000 94.71000  ? 385 SER A OG     1 
ATOM   2719  N  N      . TYR A 1 395 ? 30.43400  -21.57000 34.80200  1.000 90.15000  ? 386 TYR A N      1 
ATOM   2720  C  CA     . TYR A 1 395 ? 31.12500  -22.63000 34.07800  1.000 96.83000  ? 386 TYR A CA     1 
ATOM   2721  C  C      . TYR A 1 395 ? 31.48400  -23.80700 34.97300  1.000 104.07000 ? 386 TYR A C      1 
ATOM   2722  O  O      . TYR A 1 395 ? 31.93500  -24.84000 34.46500  1.000 109.70000 ? 386 TYR A O      1 
ATOM   2723  C  CB     . TYR A 1 395 ? 32.36800  -22.08400 33.36400  1.000 80.91000  ? 386 TYR A CB     1 
ATOM   2724  C  CG     . TYR A 1 395 ? 33.63300  -21.97200 34.18700  1.000 71.58000  ? 386 TYR A CG     1 
ATOM   2725  C  CD1    . TYR A 1 395 ? 33.86700  -20.86900 34.99600  1.000 88.80000  ? 386 TYR A CD1    1 
ATOM   2726  C  CD2    . TYR A 1 395 ? 34.61100  -22.95500 34.12500  1.000 86.51000  ? 386 TYR A CD2    1 
ATOM   2727  C  CE1    . TYR A 1 395 ? 35.03400  -20.75900 35.73300  1.000 89.09000  ? 386 TYR A CE1    1 
ATOM   2728  C  CE2    . TYR A 1 395 ? 35.77800  -22.85400 34.85600  1.000 99.65000  ? 386 TYR A CE2    1 
ATOM   2729  C  CZ     . TYR A 1 395 ? 35.98400  -21.75500 35.65900  1.000 98.14000  ? 386 TYR A CZ     1 
ATOM   2730  O  OH     . TYR A 1 395 ? 37.14500  -21.65200 36.39000  1.000 96.49000  ? 386 TYR A OH     1 
ATOM   2731  N  N      . ARG A 1 396 ? 31.30000  -23.67400 36.28500  1.000 90.21000  ? 387 ARG A N      1 
ATOM   2732  C  CA     . ARG A 1 396 ? 31.50100  -24.79800 37.18600  1.000 87.13000  ? 387 ARG A CA     1 
ATOM   2733  C  C      . ARG A 1 396 ? 30.39900  -25.84200 37.07600  1.000 98.04000  ? 387 ARG A C      1 
ATOM   2734  O  O      . ARG A 1 396 ? 30.45300  -26.84100 37.79700  1.000 105.87000 ? 387 ARG A O      1 
ATOM   2735  C  CB     . ARG A 1 396 ? 31.59000  -24.30700 38.63000  1.000 84.36000  ? 387 ARG A CB     1 
ATOM   2736  N  N      . TYR A 1 397 ? 29.40500  -25.63600 36.21900  1.000 101.76000 ? 388 TYR A N      1 
ATOM   2737  C  CA     . TYR A 1 397 ? 28.32600  -26.58500 35.99500  1.000 82.47000  ? 388 TYR A CA     1 
ATOM   2738  C  C      . TYR A 1 397 ? 28.20000  -26.86500 34.50000  1.000 78.69000  ? 388 TYR A C      1 
ATOM   2739  O  O      . TYR A 1 397 ? 28.89100  -26.26800 33.66900  1.000 94.45000  ? 388 TYR A O      1 
ATOM   2740  C  CB     . TYR A 1 397 ? 27.00600  -26.07900 36.58900  1.000 68.25000  ? 388 TYR A CB     1 
ATOM   2741  C  CG     . TYR A 1 397 ? 26.93400  -26.16500 38.10300  1.000 69.46000  ? 388 TYR A CG     1 
ATOM   2742  C  CD1    . TYR A 1 397 ? 27.36100  -25.12300 38.91800  1.000 81.21000  ? 388 TYR A CD1    1 
ATOM   2743  C  CD2    . TYR A 1 397 ? 26.42300  -27.30300 38.71300  1.000 77.28000  ? 388 TYR A CD2    1 
ATOM   2744  C  CE1    . TYR A 1 397 ? 27.27900  -25.22100 40.29600  1.000 81.37000  ? 388 TYR A CE1    1 
ATOM   2745  C  CE2    . TYR A 1 397 ? 26.33700  -27.40900 40.08200  1.000 88.31000  ? 388 TYR A CE2    1 
ATOM   2746  C  CZ     . TYR A 1 397 ? 26.76500  -26.36700 40.87300  1.000 87.32000  ? 388 TYR A CZ     1 
ATOM   2747  O  OH     . TYR A 1 397 ? 26.68100  -26.47000 42.24500  1.000 81.16000  ? 388 TYR A OH     1 
ATOM   2748  N  N      . LYS A 1 398 ? 27.28900  -27.77400 34.14700  1.000 72.17000  ? 389 LYS A N      1 
ATOM   2749  C  CA     . LYS A 1 398 ? 27.30900  -28.30400 32.78200  1.000 62.00000  ? 389 LYS A CA     1 
ATOM   2750  C  C      . LYS A 1 398 ? 26.96900  -27.26300 31.71000  1.000 76.95000  ? 389 LYS A C      1 
ATOM   2751  O  O      . LYS A 1 398 ? 27.68600  -27.21900 30.69300  1.000 86.79000  ? 389 LYS A O      1 
ATOM   2752  C  CB     . LYS A 1 398 ? 26.42000  -29.55300 32.68700  1.000 24.78000  ? 389 LYS A CB     1 
ATOM   2753  N  N      . PRO A 1 399 ? 25.93800  -26.40100 31.84500  1.000 75.06000  ? 390 PRO A N      1 
ATOM   2754  C  CA     . PRO A 1 399 ? 25.54800  -25.57300 30.67500  1.000 75.12000  ? 390 PRO A CA     1 
ATOM   2755  C  C      . PRO A 1 399 ? 26.64600  -24.65600 30.16400  1.000 86.15000  ? 390 PRO A C      1 
ATOM   2756  O  O      . PRO A 1 399 ? 26.88800  -24.59700 28.94500  1.000 89.89000  ? 390 PRO A O      1 
ATOM   2757  C  CB     . PRO A 1 399 ? 24.34100  -24.76600 31.18300  1.000 62.07000  ? 390 PRO A CB     1 
ATOM   2758  C  CG     . PRO A 1 399 ? 24.42800  -24.80400 32.64900  1.000 68.08000  ? 390 PRO A CG     1 
ATOM   2759  C  CD     . PRO A 1 399 ? 25.04700  -26.14300 32.99100  1.000 65.15000  ? 390 PRO A CD     1 
ATOM   2760  N  N      . THR A 1 400 ? 27.31000  -23.92100 31.05900  1.000 87.33000  ? 391 THR A N      1 
ATOM   2761  C  CA     . THR A 1 400 ? 28.38700  -23.03200 30.62900  1.000 86.29000  ? 391 THR A CA     1 
ATOM   2762  C  C      . THR A 1 400 ? 29.54000  -23.81200 30.01000  1.000 79.58000  ? 391 THR A C      1 
ATOM   2763  O  O      . THR A 1 400 ? 30.20500  -23.32200 29.08500  1.000 88.25000  ? 391 THR A O      1 
ATOM   2764  C  CB     . THR A 1 400 ? 28.87600  -22.19000 31.81000  1.000 87.18000  ? 391 THR A CB     1 
ATOM   2765  O  OG1    . THR A 1 400 ? 27.78300  -21.43300 32.34700  1.000 88.42000  ? 391 THR A OG1    1 
ATOM   2766  C  CG2    . THR A 1 400 ? 29.97900  -21.23100 31.38100  1.000 94.64000  ? 391 THR A CG2    1 
ATOM   2767  N  N      . GLN A 1 401 ? 29.79400  -25.02300 30.50900  1.000 77.66000  ? 392 GLN A N      1 
ATOM   2768  C  CA     . GLN A 1 401 ? 30.82700  -25.86300 29.91900  1.000 76.39000  ? 392 GLN A CA     1 
ATOM   2769  C  C      . GLN A 1 401 ? 30.46900  -26.23800 28.48900  1.000 77.69000  ? 392 GLN A C      1 
ATOM   2770  O  O      . GLN A 1 401 ? 31.32600  -26.20600 27.59500  1.000 83.47000  ? 392 GLN A O      1 
ATOM   2771  C  CB     . GLN A 1 401 ? 31.02100  -27.12500 30.76100  1.000 91.73000  ? 392 GLN A CB     1 
ATOM   2772  C  CG     . GLN A 1 401 ? 31.60400  -26.88300 32.14500  1.000 76.18000  ? 392 GLN A CG     1 
ATOM   2773  C  CD     . GLN A 1 401 ? 31.60700  -28.14300 32.99900  1.000 90.02000  ? 392 GLN A CD     1 
ATOM   2774  O  OE1    . GLN A 1 401 ? 31.40500  -29.25200 32.49800  1.000 84.16000  ? 392 GLN A OE1    1 
ATOM   2775  N  NE2    . GLN A 1 401 ? 31.83100  -27.97500 34.29600  1.000 107.81000 ? 392 GLN A NE2    1 
ATOM   2776  N  N      . PHE A 1 402 ? 29.20500  -26.60000 28.24900  1.000 68.80000  ? 393 PHE A N      1 
ATOM   2777  C  CA     . PHE A 1 402 ? 28.79900  -26.90500 26.88200  1.000 71.86000  ? 393 PHE A CA     1 
ATOM   2778  C  C      . PHE A 1 402 ? 28.96200  -25.68700 25.98500  1.000 74.76000  ? 393 PHE A C      1 
ATOM   2779  O  O      . PHE A 1 402 ? 29.37100  -25.81400 24.82800  1.000 77.22000  ? 393 PHE A O      1 
ATOM   2780  C  CB     . PHE A 1 402 ? 27.36200  -27.41900 26.82200  1.000 69.85000  ? 393 PHE A CB     1 
ATOM   2781  C  CG     . PHE A 1 402 ? 26.82100  -27.51800 25.41800  1.000 82.51000  ? 393 PHE A CG     1 
ATOM   2782  C  CD1    . PHE A 1 402 ? 27.38900  -28.39100 24.49900  1.000 87.75000  ? 393 PHE A CD1    1 
ATOM   2783  C  CD2    . PHE A 1 402 ? 25.75700  -26.73000 25.01100  1.000 122.50000 ? 393 PHE A CD2    1 
ATOM   2784  C  CE1    . PHE A 1 402 ? 26.89800  -28.48200 23.20700  1.000 103.08000 ? 393 PHE A CE1    1 
ATOM   2785  C  CE2    . PHE A 1 402 ? 25.26100  -26.81800 23.71800  1.000 123.36000 ? 393 PHE A CE2    1 
ATOM   2786  C  CZ     . PHE A 1 402 ? 25.83400  -27.69500 22.81700  1.000 100.40000 ? 393 PHE A CZ     1 
ATOM   2787  N  N      . LEU A 1 403 ? 28.61700  -24.50100 26.48800  1.000 78.37000  ? 394 LEU A N      1 
ATOM   2788  C  CA     . LEU A 1 403 ? 28.78400  -23.29800 25.67100  1.000 73.82000  ? 394 LEU A CA     1 
ATOM   2789  C  C      . LEU A 1 403 ? 30.25400  -23.08100 25.31600  1.000 73.69000  ? 394 LEU A C      1 
ATOM   2790  O  O      . LEU A 1 403 ? 30.61000  -22.83600 24.14900  1.000 81.08000  ? 394 LEU A O      1 
ATOM   2791  C  CB     . LEU A 1 403 ? 28.20900  -22.08800 26.40900  1.000 59.88000  ? 394 LEU A CB     1 
ATOM   2792  C  CG     . LEU A 1 403 ? 28.06700  -20.76200 25.66200  1.000 54.77000  ? 394 LEU A CG     1 
ATOM   2793  C  CD1    . LEU A 1 403 ? 27.32900  -20.97400 24.34900  1.000 71.00000  ? 394 LEU A CD1    1 
ATOM   2794  C  CD2    . LEU A 1 403 ? 27.32000  -19.75900 26.53400  1.000 42.70000  ? 394 LEU A CD2    1 
ATOM   2795  N  N      . GLY A 1 404 ? 31.13000  -23.19900 26.31400  1.000 79.17000  ? 395 GLY A N      1 
ATOM   2796  C  CA     . GLY A 1 404 ? 32.54600  -23.02400 26.05500  1.000 81.06000  ? 395 GLY A CA     1 
ATOM   2797  C  C      . GLY A 1 404 ? 33.04800  -24.01200 25.02400  1.000 72.83000  ? 395 GLY A C      1 
ATOM   2798  O  O      . GLY A 1 404 ? 33.82400  -23.65700 24.13300  1.000 76.94000  ? 395 GLY A O      1 
ATOM   2799  N  N      . LYS A 1 405 ? 32.58900  -25.26200 25.11200  1.000 52.46000  ? 396 LYS A N      1 
ATOM   2800  C  CA     . LYS A 1 405 ? 32.98800  -26.24300 24.11200  1.000 51.21000  ? 396 LYS A CA     1 
ATOM   2801  C  C      . LYS A 1 405 ? 32.41900  -25.94300 22.72900  1.000 74.67000  ? 396 LYS A C      1 
ATOM   2802  O  O      . LYS A 1 405 ? 33.08600  -26.19800 21.72100  1.000 82.32000  ? 396 LYS A O      1 
ATOM   2803  C  CB     . LYS A 1 405 ? 32.57900  -27.64700 24.56000  1.000 51.68000  ? 396 LYS A CB     1 
ATOM   2804  N  N      . SER A 1 406 ? 31.21500  -25.37100 22.65700  1.000 81.77000  ? 397 SER A N      1 
ATOM   2805  C  CA     . SER A 1 406 ? 30.63800  -25.01400 21.36700  1.000 75.09000  ? 397 SER A CA     1 
ATOM   2806  C  C      . SER A 1 406 ? 31.39000  -23.86400 20.73400  1.000 80.26000  ? 397 SER A C      1 
ATOM   2807  O  O      . SER A 1 406 ? 31.21400  -23.58400 19.54100  1.000 86.71000  ? 397 SER A O      1 
ATOM   2808  C  CB     . SER A 1 406 ? 29.17600  -24.59800 21.53600  1.000 78.19000  ? 397 SER A CB     1 
ATOM   2809  O  OG     . SER A 1 406 ? 29.07200  -23.42500 22.33000  1.000 66.93000  ? 397 SER A OG     1 
ATOM   2810  N  N      . SER A 1 407 ? 32.20700  -23.17900 21.52800  1.000 78.10000  ? 398 SER A N      1 
ATOM   2811  C  CA     . SER A 1 407 ? 33.02400  -22.11600 20.96200  1.000 79.32000  ? 398 SER A CA     1 
ATOM   2812  C  C      . SER A 1 407 ? 33.78300  -22.64400 19.74800  1.000 87.00000  ? 398 SER A C      1 
ATOM   2813  O  O      . SER A 1 407 ? 34.02200  -21.89700 18.79200  1.000 91.10000  ? 398 SER A O      1 
ATOM   2814  C  CB     . SER A 1 407 ? 34.00800  -21.57900 22.00000  1.000 62.88000  ? 398 SER A CB     1 
ATOM   2815  O  OG     . SER A 1 407 ? 35.01900  -22.53600 22.25700  1.000 71.89000  ? 398 SER A OG     1 
ATOM   2816  N  N      . ILE A 1 408 ? 34.14300  -23.93300 19.75000  1.000 92.12000  ? 399 ILE A N      1 
ATOM   2817  C  CA     . ILE A 1 408 ? 34.93200  -24.48800 18.65000  1.000 89.37000  ? 399 ILE A CA     1 
ATOM   2818  C  C      . ILE A 1 408 ? 34.13000  -24.55200 17.35400  1.000 100.33000 ? 399 ILE A C      1 
ATOM   2819  O  O      . ILE A 1 408 ? 34.67800  -24.34200 16.26600  1.000 84.11000  ? 399 ILE A O      1 
ATOM   2820  C  CB     . ILE A 1 408 ? 35.47900  -25.87700 19.02600  1.000 78.56000  ? 399 ILE A CB     1 
ATOM   2821  C  CG1    . ILE A 1 408 ? 35.90600  -25.90900 20.49700  1.000 79.69000  ? 399 ILE A CG1    1 
ATOM   2822  C  CG2    . ILE A 1 408 ? 36.61500  -26.26600 18.08000  1.000 89.79000  ? 399 ILE A CG2    1 
ATOM   2823  C  CD1    . ILE A 1 408 ? 36.86000  -24.79400 20.89000  1.000 75.66000  ? 399 ILE A CD1    1 
ATOM   2824  N  N      . GLU A 1 409 ? 32.83000  -24.84500 17.43500  1.000 118.42000 ? 400 GLU A N      1 
ATOM   2825  C  CA     . GLU A 1 409 ? 32.06900  -25.09500 16.21200  1.000 125.15000 ? 400 GLU A CA     1 
ATOM   2826  C  C      . GLU A 1 409 ? 31.81400  -23.81700 15.42100  1.000 114.67000 ? 400 GLU A C      1 
ATOM   2827  O  O      . GLU A 1 409 ? 31.76300  -23.86000 14.18600  1.000 111.53000 ? 400 GLU A O      1 
ATOM   2828  C  CB     . GLU A 1 409 ? 30.75900  -25.81300 16.54500  1.000 122.88000 ? 400 GLU A CB     1 
ATOM   2829  C  CG     . GLU A 1 409 ? 29.82200  -25.03800 17.45300  1.000 119.24000 ? 400 GLU A CG     1 
ATOM   2830  C  CD     . GLU A 1 409 ? 28.75100  -25.91200 18.08200  1.000 111.28000 ? 400 GLU A CD     1 
ATOM   2831  O  OE1    . GLU A 1 409 ? 28.82700  -27.15000 17.94300  1.000 119.89000 ? 400 GLU A OE1    1 
ATOM   2832  O  OE2    . GLU A 1 409 ? 27.83200  -25.35700 18.72000  1.000 95.54000  ? 400 GLU A OE2    1 
ATOM   2833  N  N      . GLY A 1 410 ? 31.62900  -22.69000 16.09700  1.000 103.32000 ? 401 GLY A N      1 
ATOM   2834  C  CA     . GLY A 1 410 ? 31.42100  -21.43200 15.40600  1.000 96.63000  ? 401 GLY A CA     1 
ATOM   2835  C  C      . GLY A 1 410 ? 30.96200  -20.36300 16.37000  1.000 92.03000  ? 401 GLY A C      1 
ATOM   2836  O  O      . GLY A 1 410 ? 30.61700  -20.62900 17.52400  1.000 99.80000  ? 401 GLY A O      1 
ATOM   2837  N  N      . THR A 1 411 ? 30.96100  -19.12800 15.86600  1.000 95.28000  ? 402 THR A N      1 
ATOM   2838  C  CA     . THR A 1 411 ? 30.47500  -17.99600 16.65100  1.000 93.98000  ? 402 THR A CA     1 
ATOM   2839  C  C      . THR A 1 411 ? 28.95100  -17.94100 16.67900  1.000 83.21000  ? 402 THR A C      1 
ATOM   2840  O  O      . THR A 1 411 ? 28.34400  -17.77600 17.74600  1.000 70.42000  ? 402 THR A O      1 
ATOM   2841  C  CB     . THR A 1 411 ? 31.04300  -16.69200 16.08900  1.000 90.90000  ? 402 THR A CB     1 
ATOM   2842  O  OG1    . THR A 1 411 ? 30.38700  -16.37500 14.85500  1.000 105.51000 ? 402 THR A OG1    1 
ATOM   2843  C  CG2    . THR A 1 411 ? 32.52700  -16.85100 15.81900  1.000 93.12000  ? 402 THR A CG2    1 
ATOM   2844  N  N      . GLY A 1 412 ? 28.31500  -18.06900 15.51500  1.000 82.91000  ? 403 GLY A N      1 
ATOM   2845  C  CA     . GLY A 1 412 ? 26.86500  -18.12500 15.49200  1.000 75.49000  ? 403 GLY A CA     1 
ATOM   2846  C  C      . GLY A 1 412 ? 26.33000  -19.26300 16.33700  1.000 75.88000  ? 403 GLY A C      1 
ATOM   2847  O  O      . GLY A 1 412 ? 25.28000  -19.13800 16.97100  1.000 77.06000  ? 403 GLY A O      1 
ATOM   2848  N  N      . MET A 1 413 ? 27.04900  -20.38800 16.36400  1.000 79.68000  ? 404 MET A N      1 
ATOM   2849  C  CA     . MET A 1 413 ? 26.65500  -21.47100 17.25600  1.000 76.80000  ? 404 MET A CA     1 
ATOM   2850  C  C      . MET A 1 413 ? 26.73000  -21.03500 18.70900  1.000 65.71000  ? 404 MET A C      1 
ATOM   2851  O  O      . MET A 1 413 ? 25.86700  -21.39400 19.51500  1.000 67.30000  ? 404 MET A O      1 
ATOM   2852  C  CB     . MET A 1 413 ? 27.51600  -22.70900 17.02100  1.000 84.06000  ? 404 MET A CB     1 
ATOM   2853  C  CG     . MET A 1 413 ? 27.26300  -23.35600 15.68300  1.000 81.72000  ? 404 MET A CG     1 
ATOM   2854  S  SD     . MET A 1 413 ? 25.59100  -24.03100 15.61500  1.000 83.20000  ? 404 MET A SD     1 
ATOM   2855  C  CE     . MET A 1 413 ? 25.60900  -25.20100 16.97100  1.000 77.62000  ? 404 MET A CE     1 
ATOM   2856  N  N      . VAL A 1 414 ? 27.75000  -20.25300 19.06100  1.000 59.45000  ? 405 VAL A N      1 
ATOM   2857  C  CA     . VAL A 1 414 ? 27.84700  -19.74300 20.42400  1.000 60.55000  ? 405 VAL A CA     1 
ATOM   2858  C  C      . VAL A 1 414 ? 26.64600  -18.86500 20.74500  1.000 61.25000  ? 405 VAL A C      1 
ATOM   2859  O  O      . VAL A 1 414 ? 26.02000  -19.00400 21.80200  1.000 67.28000  ? 405 VAL A O      1 
ATOM   2860  C  CB     . VAL A 1 414 ? 29.17500  -18.99100 20.61600  1.000 61.72000  ? 405 VAL A CB     1 
ATOM   2861  C  CG1    . VAL A 1 414 ? 29.16600  -18.21400 21.92000  1.000 52.58000  ? 405 VAL A CG1    1 
ATOM   2862  C  CG2    . VAL A 1 414 ? 30.33400  -19.97500 20.58300  1.000 77.16000  ? 405 VAL A CG2    1 
ATOM   2863  N  N      . ILE A 1 415 ? 26.28900  -17.96700 19.82700  1.000 55.46000  ? 406 ILE A N      1 
ATOM   2864  C  CA     . ILE A 1 415 ? 25.16100  -17.07200 20.07500  1.000 66.20000  ? 406 ILE A CA     1 
ATOM   2865  C  C      . ILE A 1 415 ? 23.87200  -17.87100 20.23600  1.000 65.01000  ? 406 ILE A C      1 
ATOM   2866  O  O      . ILE A 1 415 ? 23.08800  -17.64800 21.17200  1.000 53.68000  ? 406 ILE A O      1 
ATOM   2867  C  CB     . ILE A 1 415 ? 25.04100  -16.03400 18.94500  1.000 62.01000  ? 406 ILE A CB     1 
ATOM   2868  C  CG1    . ILE A 1 415 ? 26.30400  -15.17300 18.87300  1.000 55.67000  ? 406 ILE A CG1    1 
ATOM   2869  C  CG2    . ILE A 1 415 ? 23.78300  -15.19300 19.12600  1.000 45.43000  ? 406 ILE A CG2    1 
ATOM   2870  C  CD1    . ILE A 1 415 ? 26.59200  -14.41000 20.14700  1.000 59.01000  ? 406 ILE A CD1    1 
ATOM   2871  N  N      . SER A 1 416 ? 23.63400  -18.81700 19.32300  1.000 69.05000  ? 407 SER A N      1 
ATOM   2872  C  CA     . SER A 1 416 ? 22.40600  -19.60000 19.37800  1.000 56.12000  ? 407 SER A CA     1 
ATOM   2873  C  C      . SER A 1 416 ? 22.34900  -20.42700 20.65300  1.000 56.98000  ? 407 SER A C      1 
ATOM   2874  O  O      . SER A 1 416 ? 21.29500  -20.52200 21.29300  1.000 63.63000  ? 407 SER A O      1 
ATOM   2875  C  CB     . SER A 1 416 ? 22.29700  -20.50200 18.14600  1.000 54.38000  ? 407 SER A CB     1 
ATOM   2876  O  OG     . SER A 1 416 ? 22.15700  -19.73600 16.96200  1.000 64.99000  ? 407 SER A OG     1 
ATOM   2877  N  N      . ASN A 1 417 ? 23.47800  -21.01800 21.05000  1.000 50.09000  ? 408 ASN A N      1 
ATOM   2878  C  CA     . ASN A 1 417 ? 23.50000  -21.82800 22.26000  1.000 54.61000  ? 408 ASN A CA     1 
ATOM   2879  C  C      . ASN A 1 417 ? 23.26900  -20.96800 23.49500  1.000 53.05000  ? 408 ASN A C      1 
ATOM   2880  O  O      . ASN A 1 417 ? 22.60400  -21.39900 24.44100  1.000 81.62000  ? 408 ASN A O      1 
ATOM   2881  C  CB     . ASN A 1 417 ? 24.82600  -22.58800 22.35400  1.000 67.16000  ? 408 ASN A CB     1 
ATOM   2882  C  CG     . ASN A 1 417 ? 24.92300  -23.72800 21.35300  1.000 79.37000  ? 408 ASN A CG     1 
ATOM   2883  O  OD1    . ASN A 1 417 ? 23.91600  -24.32400 20.96800  1.000 82.87000  ? 408 ASN A OD1    1 
ATOM   2884  N  ND2    . ASN A 1 417 ? 26.14200  -24.02900 20.92000  1.000 66.19000  ? 408 ASN A ND2    1 
ATOM   2885  N  N      . GLY A 1 418 ? 23.77900  -19.73700 23.49800  1.000 38.46000  ? 409 GLY A N      1 
ATOM   2886  C  CA     . GLY A 1 418 ? 23.50300  -18.85400 24.62100  1.000 53.03000  ? 409 GLY A CA     1 
ATOM   2887  C  C      . GLY A 1 418 ? 22.03200  -18.49600 24.72900  1.000 59.30000  ? 409 GLY A C      1 
ATOM   2888  O  O      . GLY A 1 418 ? 21.43600  -18.54300 25.81500  1.000 55.67000  ? 409 GLY A O      1 
ATOM   2889  N  N      . LEU A 1 419 ? 21.42000  -18.13600 23.59900  1.000 51.84000  ? 410 LEU A N      1 
ATOM   2890  C  CA     . LEU A 1 419 ? 19.99800  -17.80900 23.62600  1.000 36.12000  ? 410 LEU A CA     1 
ATOM   2891  C  C      . LEU A 1 419 ? 19.17000  -19.00700 24.07300  1.000 59.81000  ? 410 LEU A C      1 
ATOM   2892  O  O      . LEU A 1 419 ? 18.25400  -18.87000 24.89900  1.000 66.50000  ? 410 LEU A O      1 
ATOM   2893  C  CB     . LEU A 1 419 ? 19.54600  -17.31800 22.25200  1.000 33.43000  ? 410 LEU A CB     1 
ATOM   2894  C  CG     . LEU A 1 419 ? 20.09600  -15.95000 21.85300  1.000 34.73000  ? 410 LEU A CG     1 
ATOM   2895  C  CD1    . LEU A 1 419 ? 19.81000  -15.68800 20.39100  1.000 35.01000  ? 410 LEU A CD1    1 
ATOM   2896  C  CD2    . LEU A 1 419 ? 19.48500  -14.86600 22.72400  1.000 32.22000  ? 410 LEU A CD2    1 
ATOM   2897  N  N      . SER A 1 420 ? 19.49200  -20.19500 23.55000  1.000 66.41000  ? 411 SER A N      1 
ATOM   2898  C  CA     . SER A 1 420 ? 18.77400  -21.40300 23.94000  1.000 61.62000  ? 411 SER A CA     1 
ATOM   2899  C  C      . SER A 1 420 ? 18.96000  -21.69000 25.42400  1.000 54.36000  ? 411 SER A C      1 
ATOM   2900  O  O      . SER A 1 420 ? 18.01200  -22.09300 26.11100  1.000 61.10000  ? 411 SER A O      1 
ATOM   2901  C  CB     . SER A 1 420 ? 19.24100  -22.58300 23.08300  1.000 50.54000  ? 411 SER A CB     1 
ATOM   2902  O  OG     . SER A 1 420 ? 18.83500  -23.82600 23.62600  1.000 70.19000  ? 411 SER A OG     1 
ATOM   2903  N  N      . LEU A 1 421 ? 20.17200  -21.47500 25.94200  1.000 43.87000  ? 412 LEU A N      1 
ATOM   2904  C  CA     . LEU A 1 421 ? 20.42000  -21.71200 27.35800  1.000 50.41000  ? 412 LEU A CA     1 
ATOM   2905  C  C      . LEU A 1 421 ? 19.56600  -20.80000 28.22100  1.000 57.70000  ? 412 LEU A C      1 
ATOM   2906  O  O      . LEU A 1 421 ? 18.99500  -21.24400 29.22000  1.000 72.09000  ? 412 LEU A O      1 
ATOM   2907  C  CB     . LEU A 1 421 ? 21.90400  -21.52500 27.68100  1.000 60.34000  ? 412 LEU A CB     1 
ATOM   2908  C  CG     . LEU A 1 421 ? 22.33700  -21.84300 29.11900  1.000 52.10000  ? 412 LEU A CG     1 
ATOM   2909  C  CD1    . LEU A 1 421 ? 23.78000  -22.34100 29.16800  1.000 77.02000  ? 412 LEU A CD1    1 
ATOM   2910  C  CD2    . LEU A 1 421 ? 22.15700  -20.63400 30.03200  1.000 63.06000  ? 412 LEU A CD2    1 
ATOM   2911  N  N      . GLY A 1 422 ? 19.46300  -19.52100 27.86000  1.000 48.21000  ? 413 GLY A N      1 
ATOM   2912  C  CA     . GLY A 1 422 ? 18.61100  -18.63500 28.64200  1.000 58.10000  ? 413 GLY A CA     1 
ATOM   2913  C  C      . GLY A 1 422 ? 17.15000  -19.04400 28.58000  1.000 55.47000  ? 413 GLY A C      1 
ATOM   2914  O  O      . GLY A 1 422 ? 16.45900  -19.14300 29.61100  1.000 51.02000  ? 413 GLY A O      1 
ATOM   2915  N  N      . MET A 1 423 ? 16.66400  -19.31600 27.36600  1.000 48.95000  ? 414 MET A N      1 
ATOM   2916  C  CA     . MET A 1 423 ? 15.26700  -19.69500 27.21100  1.000 47.16000  ? 414 MET A CA     1 
ATOM   2917  C  C      . MET A 1 423 ? 14.94700  -20.93100 28.04000  1.000 62.16000  ? 414 MET A C      1 
ATOM   2918  O  O      . MET A 1 423 ? 13.88400  -21.00800 28.66900  1.000 66.94000  ? 414 MET A O      1 
ATOM   2919  C  CB     . MET A 1 423 ? 14.93900  -19.93200 25.73700  1.000 41.90000  ? 414 MET A CB     1 
ATOM   2920  C  CG     . MET A 1 423 ? 14.86900  -18.66800 24.89700  1.000 35.64000  ? 414 MET A CG     1 
ATOM   2921  S  SD     . MET A 1 423 ? 14.82100  -19.03700 23.13200  1.000 52.03000  ? 414 MET A SD     1 
ATOM   2922  C  CE     . MET A 1 423 ? 14.27600  -17.46000 22.47900  1.000 26.26000  ? 414 MET A CE     1 
ATOM   2923  N  N      . LYS A 1 424 ? 15.86200  -21.90200 28.07300  1.000 63.00000  ? 415 LYS A N      1 
ATOM   2924  C  CA     . LYS A 1 424 ? 15.63000  -23.09200 28.88600  1.000 53.54000  ? 415 LYS A CA     1 
ATOM   2925  C  C      . LYS A 1 424 ? 15.80600  -22.81500 30.37700  1.000 50.59000  ? 415 LYS A C      1 
ATOM   2926  O  O      . LYS A 1 424 ? 15.11600  -23.42500 31.20100  1.000 62.90000  ? 415 LYS A O      1 
ATOM   2927  C  CB     . LYS A 1 424 ? 16.55000  -24.22800 28.43900  1.000 48.02000  ? 415 LYS A CB     1 
ATOM   2928  C  CG     . LYS A 1 424 ? 16.40200  -24.59300 26.96700  1.000 50.27000  ? 415 LYS A CG     1 
ATOM   2929  C  CD     . LYS A 1 424 ? 17.52000  -25.51200 26.50200  1.000 70.10000  ? 415 LYS A CD     1 
ATOM   2930  C  CE     . LYS A 1 424 ? 17.48100  -26.85100 27.23300  1.000 93.60000  ? 415 LYS A CE     1 
ATOM   2931  N  NZ     . LYS A 1 424 ? 16.29900  -27.69300 26.86400  1.000 102.26000 ? 415 LYS A NZ     1 
ATOM   2932  N  N      . SER A 1 425 ? 16.73400  -21.92500 30.74100  1.000 47.32000  ? 416 SER A N      1 
ATOM   2933  C  CA     . SER A 1 425 ? 16.99900  -21.61200 32.13900  1.000 58.04000  ? 416 SER A CA     1 
ATOM   2934  C  C      . SER A 1 425 ? 15.81400  -20.95000 32.81000  1.000 47.20000  ? 416 SER A C      1 
ATOM   2935  O  O      . SER A 1 425 ? 15.70500  -20.99800 34.04200  1.000 37.97000  ? 416 SER A O      1 
ATOM   2936  C  CB     . SER A 1 425 ? 18.22600  -20.70800 32.24100  1.000 59.57000  ? 416 SER A CB     1 
ATOM   2937  O  OG     . SER A 1 425 ? 17.84600  -19.34500 32.28300  1.000 64.27000  ? 416 SER A OG     1 
ATOM   2938  N  N      . VAL A 1 426 ? 14.94200  -20.31900 32.02400  1.000 39.52000  ? 417 VAL A N      1 
ATOM   2939  C  CA     . VAL A 1 426 ? 13.75800  -19.69600 32.61500  1.000 41.36000  ? 417 VAL A CA     1 
ATOM   2940  C  C      . VAL A 1 426 ? 13.00800  -20.68000 33.51300  1.000 40.66000  ? 417 VAL A C      1 
ATOM   2941  O  O      . VAL A 1 426 ? 12.53500  -20.31200 34.59400  1.000 36.22000  ? 417 VAL A O      1 
ATOM   2942  C  CB     . VAL A 1 426 ? 12.83900  -19.12400 31.51800  1.000 48.78000  ? 417 VAL A CB     1 
ATOM   2943  C  CG1    . VAL A 1 426 ? 11.57000  -18.56100 32.14000  1.000 70.52000  ? 417 VAL A CG1    1 
ATOM   2944  C  CG2    . VAL A 1 426 ? 13.55300  -18.02900 30.76200  1.000 57.84000  ? 417 VAL A CG2    1 
ATOM   2945  N  N      . PHE A 1 427 ? 12.93700  -21.96100 33.10800  1.000 64.04000  ? 418 PHE A N      1 
ATOM   2946  C  CA     . PHE A 1 427 ? 11.98500  -22.88500 33.73200  1.000 67.85000  ? 418 PHE A CA     1 
ATOM   2947  C  C      . PHE A 1 427 ? 12.28900  -23.19800 35.19200  1.000 57.39000  ? 418 PHE A C      1 
ATOM   2948  O  O      . PHE A 1 427 ? 11.35800  -23.15200 36.01300  1.000 64.27000  ? 418 PHE A O      1 
ATOM   2949  C  CB     . PHE A 1 427 ? 11.89100  -24.17500 32.91200  1.000 51.83000  ? 418 PHE A CB     1 
ATOM   2950  C  CG     . PHE A 1 427 ? 10.79700  -25.11100 33.36900  1.000 60.03000  ? 418 PHE A CG     1 
ATOM   2951  C  CD1    . PHE A 1 427 ? 9.49800   -24.96600 32.90600  1.000 72.58000  ? 418 PHE A CD1    1 
ATOM   2952  C  CD2    . PHE A 1 427 ? 11.07000  -26.13500 34.26400  1.000 56.49000  ? 418 PHE A CD2    1 
ATOM   2953  C  CE1    . PHE A 1 427 ? 8.49100   -25.83100 33.32000  1.000 53.41000  ? 418 PHE A CE1    1 
ATOM   2954  C  CE2    . PHE A 1 427 ? 10.06400  -27.00300 34.68400  1.000 38.97000  ? 418 PHE A CE2    1 
ATOM   2955  C  CZ     . PHE A 1 427 ? 8.77400   -26.84800 34.20900  1.000 32.66000  ? 418 PHE A CZ     1 
ATOM   2956  N  N      . PRO A 1 428 ? 13.49900  -23.59200 35.57500  1.000 42.49000  ? 419 PRO A N      1 
ATOM   2957  C  CA     . PRO A 1 428 ? 13.72100  -24.07100 36.95200  1.000 47.38000  ? 419 PRO A CA     1 
ATOM   2958  C  C      . PRO A 1 428 ? 13.30900  -23.03300 37.98300  1.000 49.92000  ? 419 PRO A C      1 
ATOM   2959  O  O      . PRO A 1 428 ? 12.51400  -23.32500 38.89400  1.000 52.84000  ? 419 PRO A O      1 
ATOM   2960  C  CB     . PRO A 1 428 ? 15.23400  -24.33700 36.98400  1.000 55.07000  ? 419 PRO A CB     1 
ATOM   2961  C  CG     . PRO A 1 428 ? 15.54400  -24.69600 35.54700  1.000 49.18000  ? 419 PRO A CG     1 
ATOM   2962  C  CD     . PRO A 1 428 ? 14.71200  -23.72500 34.75000  1.000 47.99000  ? 419 PRO A CD     1 
ATOM   2963  N  N      . PRO A 1 429 ? 13.81200  -21.80200 37.87000  1.000 47.82000  ? 420 PRO A N      1 
ATOM   2964  C  CA     . PRO A 1 429 ? 13.41400  -20.77700 38.84800  1.000 41.88000  ? 420 PRO A CA     1 
ATOM   2965  C  C      . PRO A 1 429 ? 11.93100  -20.45300 38.79700  1.000 52.42000  ? 420 PRO A C      1 
ATOM   2966  O  O      . PRO A 1 429 ? 11.31800  -20.20300 39.84300  1.000 64.82000  ? 420 PRO A O      1 
ATOM   2967  C  CB     . PRO A 1 429 ? 14.28000  -19.56900 38.45600  1.000 38.56000  ? 420 PRO A CB     1 
ATOM   2968  C  CG     . PRO A 1 429 ? 14.59900  -19.79000 37.01300  1.000 51.28000  ? 420 PRO A CG     1 
ATOM   2969  C  CD     . PRO A 1 429 ? 14.76800  -21.27700 36.87900  1.000 47.05000  ? 420 PRO A CD     1 
ATOM   2970  N  N      . THR A 1 430 ? 11.32900  -20.45200 37.60300  1.000 45.57000  ? 421 THR A N      1 
ATOM   2971  C  CA     . THR A 1 430 ? 9.89800   -20.18100 37.50700  1.000 26.93000  ? 421 THR A CA     1 
ATOM   2972  C  C      . THR A 1 430 ? 9.08500   -21.26300 38.20000  1.000 34.55000  ? 421 THR A C      1 
ATOM   2973  O  O      . THR A 1 430 ? 8.08100   -20.97000 38.85700  1.000 49.30000  ? 421 THR A O      1 
ATOM   2974  C  CB     . THR A 1 430 ? 9.47600   -20.05200 36.04400  1.000 34.13000  ? 421 THR A CB     1 
ATOM   2975  O  OG1    . THR A 1 430 ? 10.20300  -18.98000 35.43100  1.000 53.96000  ? 421 THR A OG1    1 
ATOM   2976  C  CG2    . THR A 1 430 ? 7.98500   -19.77300 35.94700  1.000 39.75000  ? 421 THR A CG2    1 
ATOM   2977  N  N      . LEU A 1 431 ? 9.50500   -22.52000 38.06600  1.000 35.27000  ? 422 LEU A N      1 
ATOM   2978  C  CA     . LEU A 1 431 ? 8.83100   -23.60300 38.76900  1.000 41.21000  ? 422 LEU A CA     1 
ATOM   2979  C  C      . LEU A 1 431 ? 8.97800   -23.43600 40.26900  1.000 47.78000  ? 422 LEU A C      1 
ATOM   2980  O  O      . LEU A 1 431 ? 8.02400   -23.65700 41.02800  1.000 42.55000  ? 422 LEU A O      1 
ATOM   2981  C  CB     . LEU A 1 431 ? 9.39100   -24.95100 38.32000  1.000 32.21000  ? 422 LEU A CB     1 
ATOM   2982  C  CG     . LEU A 1 431 ? 8.71900   -26.16100 38.96400  1.000 21.17000  ? 422 LEU A CG     1 
ATOM   2983  C  CD1    . LEU A 1 431 ? 7.22400   -26.10200 38.73000  1.000 10.09000  ? 422 LEU A CD1    1 
ATOM   2984  C  CD2    . LEU A 1 431 ? 9.30100   -27.45100 38.41100  1.000 35.12000  ? 422 LEU A CD2    1 
ATOM   2985  N  N      . THR A 1 432 ? 10.16800  -23.03000 40.71500  1.000 40.13000  ? 423 THR A N      1 
ATOM   2986  C  CA     . THR A 1 432 ? 10.34900  -22.74800 42.13400  1.000 36.99000  ? 423 THR A CA     1 
ATOM   2987  C  C      . THR A 1 432 ? 9.36200   -21.68300 42.60400  1.000 45.86000  ? 423 THR A C      1 
ATOM   2988  O  O      . THR A 1 432 ? 8.69000   -21.84600 43.63100  1.000 45.04000  ? 423 THR A O      1 
ATOM   2989  C  CB     . THR A 1 432 ? 11.78800  -22.31300 42.40600  1.000 35.42000  ? 423 THR A CB     1 
ATOM   2990  O  OG1    . THR A 1 432 ? 12.69500  -23.26200 41.82800  1.000 63.72000  ? 423 THR A OG1    1 
ATOM   2991  C  CG2    . THR A 1 432 ? 12.03500  -22.22000 43.90900  1.000 59.37000  ? 423 THR A CG2    1 
ATOM   2992  N  N      . LEU A 1 433 ? 9.24700   -20.59300 41.84400  1.000 44.75000  ? 424 LEU A N      1 
ATOM   2993  C  CA     . LEU A 1 433 ? 8.34400   -19.50700 42.21800  1.000 39.13000  ? 424 LEU A CA     1 
ATOM   2994  C  C      . LEU A 1 433 ? 6.88800   -19.95900 42.20600  1.000 47.51000  ? 424 LEU A C      1 
ATOM   2995  O  O      . LEU A 1 433 ? 6.09900   -19.56500 43.07200  1.000 49.95000  ? 424 LEU A O      1 
ATOM   2996  C  CB     . LEU A 1 433 ? 8.55100   -18.32200 41.27700  1.000 18.60000  ? 424 LEU A CB     1 
ATOM   2997  C  CG     . LEU A 1 433 ? 9.60200   -17.29900 41.70400  1.000 39.84000  ? 424 LEU A CG     1 
ATOM   2998  C  CD1    . LEU A 1 433 ? 9.79800   -16.26700 40.61500  1.000 37.80000  ? 424 LEU A CD1    1 
ATOM   2999  C  CD2    . LEU A 1 433 ? 9.18000   -16.62100 42.99600  1.000 60.64000  ? 424 LEU A CD2    1 
ATOM   3000  N  N      . VAL A 1 434 ? 6.51300   -20.78100 41.22800  1.000 39.42000  ? 425 VAL A N      1 
ATOM   3001  C  CA     . VAL A 1 434 ? 5.13700   -21.25900 41.12500  1.000 45.92000  ? 425 VAL A CA     1 
ATOM   3002  C  C      . VAL A 1 434 ? 4.78300   -22.12300 42.32800  1.000 52.54000  ? 425 VAL A C      1 
ATOM   3003  O  O      . VAL A 1 434 ? 3.73200   -21.94700 42.95900  1.000 60.08000  ? 425 VAL A O      1 
ATOM   3004  C  CB     . VAL A 1 434 ? 4.94100   -22.01600 39.79900  1.000 42.98000  ? 425 VAL A CB     1 
ATOM   3005  C  CG1    . VAL A 1 434 ? 3.73100   -22.93200 39.86400  1.000 44.14000  ? 425 VAL A CG1    1 
ATOM   3006  C  CG2    . VAL A 1 434 ? 4.81200   -21.02400 38.65200  1.000 40.97000  ? 425 VAL A CG2    1 
ATOM   3007  N  N      . LEU A 1 435 ? 5.65800   -23.07000 42.66500  1.000 44.10000  ? 426 LEU A N      1 
ATOM   3008  C  CA     . LEU A 1 435 ? 5.38400   -23.93200 43.80800  1.000 46.30000  ? 426 LEU A CA     1 
ATOM   3009  C  C      . LEU A 1 435 ? 5.34500   -23.12200 45.09500  1.000 43.94000  ? 426 LEU A C      1 
ATOM   3010  O  O      . LEU A 1 435 ? 4.48900   -23.35000 45.96300  1.000 58.09000  ? 426 LEU A O      1 
ATOM   3011  C  CB     . LEU A 1 435 ? 6.43500   -25.03800 43.89000  1.000 33.32000  ? 426 LEU A CB     1 
ATOM   3012  C  CG     . LEU A 1 435 ? 6.27600   -26.15400 42.85500  1.000 22.16000  ? 426 LEU A CG     1 
ATOM   3013  C  CD1    . LEU A 1 435 ? 7.42700   -27.14400 42.94900  1.000 11.24000  ? 426 LEU A CD1    1 
ATOM   3014  C  CD2    . LEU A 1 435 ? 4.93600   -26.85600 43.01600  1.000 13.32000  ? 426 LEU A CD2    1 
ATOM   3015  N  N      . GLY A 1 436 ? 6.25800   -22.15800 45.23300  1.000 21.68000  ? 427 GLY A N      1 
ATOM   3016  C  CA     . GLY A 1 436 ? 6.23500   -21.31200 46.40900  1.000 34.28000  ? 427 GLY A CA     1 
ATOM   3017  C  C      . GLY A 1 436 ? 4.94100   -20.53500 46.53300  1.000 42.89000  ? 427 GLY A C      1 
ATOM   3018  O  O      . GLY A 1 436 ? 4.33800   -20.48400 47.60600  1.000 52.48000  ? 427 GLY A O      1 
ATOM   3019  N  N      . ILE A 1 437 ? 4.48500   -19.93400 45.43200  1.000 37.07000  ? 428 ILE A N      1 
ATOM   3020  C  CA     . ILE A 1 437 ? 3.23300   -19.18500 45.46900  1.000 54.63000  ? 428 ILE A CA     1 
ATOM   3021  C  C      . ILE A 1 437 ? 2.07800   -20.09900 45.83900  1.000 54.05000  ? 428 ILE A C      1 
ATOM   3022  O  O      . ILE A 1 437 ? 1.21500   -19.73800 46.64700  1.000 54.67000  ? 428 ILE A O      1 
ATOM   3023  C  CB     . ILE A 1 437 ? 2.98100   -18.48500 44.12200  1.000 55.41000  ? 428 ILE A CB     1 
ATOM   3024  C  CG1    . ILE A 1 437 ? 4.09300   -17.48100 43.82800  1.000 65.28000  ? 428 ILE A CG1    1 
ATOM   3025  C  CG2    . ILE A 1 437 ? 1.61400   -17.81600 44.12200  1.000 44.14000  ? 428 ILE A CG2    1 
ATOM   3026  C  CD1    . ILE A 1 437 ? 3.97600   -16.83200 42.47300  1.000 45.57000  ? 428 ILE A CD1    1 
ATOM   3027  N  N      . LEU A 1 438 ? 2.03500   -21.29300 45.24700  1.000 57.62000  ? 429 LEU A N      1 
ATOM   3028  C  CA     . LEU A 1 438 ? 0.92600   -22.20200 45.51600  1.000 50.46000  ? 429 LEU A CA     1 
ATOM   3029  C  C      . LEU A 1 438 ? 0.88400   -22.57800 46.99200  1.000 59.05000  ? 429 LEU A C      1 
ATOM   3030  O  O      . LEU A 1 438 ? -0.17700  -22.53000 47.63200  1.000 64.60000  ? 429 LEU A O      1 
ATOM   3031  C  CB     . LEU A 1 438 ? 1.04500   -23.44400 44.63300  1.000 34.65000  ? 429 LEU A CB     1 
ATOM   3032  C  CG     . LEU A 1 438 ? 0.73500   -23.22700 43.15000  1.000 29.29000  ? 429 LEU A CG     1 
ATOM   3033  C  CD1    . LEU A 1 438 ? 1.13800   -24.44900 42.34100  1.000 47.70000  ? 429 LEU A CD1    1 
ATOM   3034  C  CD2    . LEU A 1 438 ? -0.73600  -22.89900 42.94100  1.000 41.41000  ? 429 LEU A CD2    1 
ATOM   3035  N  N      . PHE A 1 439 ? 2.04100   -22.93000 47.55800  1.000 55.35000  ? 430 PHE A N      1 
ATOM   3036  C  CA     . PHE A 1 439 ? 2.06900   -23.33600 48.95800  1.000 53.05000  ? 430 PHE A CA     1 
ATOM   3037  C  C      . PHE A 1 439 ? 1.76600   -22.15800 49.87700  1.000 64.20000  ? 430 PHE A C      1 
ATOM   3038  O  O      . PHE A 1 439 ? 1.06500   -22.31400 50.88500  1.000 88.06000  ? 430 PHE A O      1 
ATOM   3039  C  CB     . PHE A 1 439 ? 3.42500   -23.95600 49.29400  1.000 45.63000  ? 430 PHE A CB     1 
ATOM   3040  C  CG     . PHE A 1 439 ? 3.69800   -25.24800 48.56900  1.000 46.39000  ? 430 PHE A CG     1 
ATOM   3041  C  CD1    . PHE A 1 439 ? 2.70100   -26.20100 48.41700  1.000 36.63000  ? 430 PHE A CD1    1 
ATOM   3042  C  CD2    . PHE A 1 439 ? 4.95100   -25.50700 48.03500  1.000 34.16000  ? 430 PHE A CD2    1 
ATOM   3043  C  CE1    . PHE A 1 439 ? 2.95300   -27.39000 47.75100  1.000 29.83000  ? 430 PHE A CE1    1 
ATOM   3044  C  CE2    . PHE A 1 439 ? 5.20600   -26.69200 47.36700  1.000 33.96000  ? 430 PHE A CE2    1 
ATOM   3045  C  CZ     . PHE A 1 439 ? 4.20600   -27.63400 47.22700  1.000 39.93000  ? 430 PHE A CZ     1 
ATOM   3046  N  N      . ALA A 1 440 ? 2.25600   -20.96600 49.53400  1.000 49.88000  ? 431 ALA A N      1 
ATOM   3047  C  CA     . ALA A 1 440 ? 1.96600   -19.79100 50.34600  1.000 65.98000  ? 431 ALA A CA     1 
ATOM   3048  C  C      . ALA A 1 440 ? 0.47800   -19.47500 50.34400  1.000 86.22000  ? 431 ALA A C      1 
ATOM   3049  O  O      . ALA A 1 440 ? -0.08900  -19.09400 51.37800  1.000 107.65000 ? 431 ALA A O      1 
ATOM   3050  C  CB     . ALA A 1 440 ? 2.76700   -18.59400 49.84100  1.000 70.43000  ? 431 ALA A CB     1 
ATOM   3051  N  N      . ASP A 1 441 ? -0.17000  -19.60400 49.18400  1.000 79.19000  ? 432 ASP A N      1 
ATOM   3052  C  CA     . ASP A 1 441 ? -1.61200  -19.41800 49.14600  1.000 71.88000  ? 432 ASP A CA     1 
ATOM   3053  C  C      . ASP A 1 441 ? -2.30200  -20.44500 50.03000  1.000 84.65000  ? 432 ASP A C      1 
ATOM   3054  O  O      . ASP A 1 441 ? -3.05000  -20.07900 50.94000  1.000 90.07000  ? 432 ASP A O      1 
ATOM   3055  C  CB     . ASP A 1 441 ? -2.13300  -19.49200 47.71300  1.000 70.18000  ? 432 ASP A CB     1 
ATOM   3056  C  CG     . ASP A 1 441 ? -3.64000  -19.43400 47.65200  1.000 76.72000  ? 432 ASP A CG     1 
ATOM   3057  O  OD1    . ASP A 1 441 ? -4.20200  -18.37400 48.00300  1.000 89.13000  ? 432 ASP A OD1    1 
ATOM   3058  O  OD2    . ASP A 1 441 ? -4.25900  -20.44400 47.25900  1.000 82.49000  ? 432 ASP A OD2    1 
ATOM   3059  N  N      . TYR A 1 442 ? -1.97800  -21.72800 49.84300  1.000 87.43000  ? 433 TYR A N      1 
ATOM   3060  C  CA     . TYR A 1 442 ? -2.57900  -22.76700 50.67500  1.000 89.76000  ? 433 TYR A CA     1 
ATOM   3061  C  C      . TYR A 1 442 ? -2.45000  -22.44900 52.16000  1.000 90.81000  ? 433 TYR A C      1 
ATOM   3062  O  O      . TYR A 1 442 ? -3.38400  -22.68100 52.93500  1.000 89.53000  ? 433 TYR A O      1 
ATOM   3063  C  CB     . TYR A 1 442 ? -1.94100  -24.12000 50.36400  1.000 81.41000  ? 433 TYR A CB     1 
ATOM   3064  C  CG     . TYR A 1 442 ? -2.11600  -25.14400 51.46200  1.000 86.17000  ? 433 TYR A CG     1 
ATOM   3065  C  CD1    . TYR A 1 442 ? -3.35200  -25.72600 51.71000  1.000 115.67000 ? 433 TYR A CD1    1 
ATOM   3066  C  CD2    . TYR A 1 442 ? -1.04100  -25.52500 52.25400  1.000 104.29000 ? 433 TYR A CD2    1 
ATOM   3067  C  CE1    . TYR A 1 442 ? -3.51400  -26.66400 52.71100  1.000 138.01000 ? 433 TYR A CE1    1 
ATOM   3068  C  CE2    . TYR A 1 442 ? -1.19400  -26.46100 53.26000  1.000 132.99000 ? 433 TYR A CE2    1 
ATOM   3069  C  CZ     . TYR A 1 442 ? -2.43400  -27.02800 53.48300  1.000 155.47000 ? 433 TYR A CZ     1 
ATOM   3070  O  OH     . TYR A 1 442 ? -2.59900  -27.96100 54.48100  1.000 188.70000 ? 433 TYR A OH     1 
ATOM   3071  N  N      . PHE A 1 443 ? -1.29800  -21.92300 52.57800  1.000 102.33000 ? 434 PHE A N      1 
ATOM   3072  C  CA     . PHE A 1 443 ? -1.09700  -21.62800 53.99500  1.000 98.89000  ? 434 PHE A CA     1 
ATOM   3073  C  C      . PHE A 1 443 ? -1.94200  -20.44100 54.44800  1.000 99.55000  ? 434 PHE A C      1 
ATOM   3074  O  O      . PHE A 1 443 ? -2.73000  -20.55200 55.39600  1.000 111.93000 ? 434 PHE A O      1 
ATOM   3075  C  CB     . PHE A 1 443 ? 0.38700   -21.37900 54.28100  1.000 90.64000  ? 434 PHE A CB     1 
ATOM   3076  C  CG     . PHE A 1 443 ? 1.21100   -22.63300 54.36600  1.000 91.06000  ? 434 PHE A CG     1 
ATOM   3077  C  CD1    . PHE A 1 443 ? 0.95300   -23.57500 55.34800  1.000 96.13000  ? 434 PHE A CD1    1 
ATOM   3078  C  CD2    . PHE A 1 443 ? 2.23700   -22.87500 53.46700  1.000 86.02000  ? 434 PHE A CD2    1 
ATOM   3079  C  CE1    . PHE A 1 443 ? 1.70600   -24.73400 55.44000  1.000 100.60000 ? 434 PHE A CE1    1 
ATOM   3080  C  CE2    . PHE A 1 443 ? 2.99600   -24.04000 53.55200  1.000 82.10000  ? 434 PHE A CE2    1 
ATOM   3081  C  CZ     . PHE A 1 443 ? 2.72600   -24.96800 54.54200  1.000 98.55000  ? 434 PHE A CZ     1 
ATOM   3082  N  N      . ALA A 1 444 ? -1.78400  -19.28500 53.80000  1.000 97.49000  ? 435 ALA A N      1 
ATOM   3083  C  CA     . ALA A 1 444 ? -2.35300  -18.06900 54.37500  1.000 102.31000 ? 435 ALA A CA     1 
ATOM   3084  C  C      . ALA A 1 444 ? -2.80900  -17.08200 53.31300  1.000 109.05000 ? 435 ALA A C      1 
ATOM   3085  O  O      . ALA A 1 444 ? -2.55900  -15.88100 53.43600  1.000 100.27000 ? 435 ALA A O      1 
ATOM   3086  C  CB     . ALA A 1 444 ? -1.36700  -17.36800 55.31000  1.000 95.09000  ? 435 ALA A CB     1 
ATOM   3087  N  N      . GLY A 1 445 ? -3.41400  -17.56400 52.23400  1.000 102.17000 ? 436 GLY A N      1 
ATOM   3088  C  CA     . GLY A 1 445 ? -3.95200  -16.64100 51.25200  1.000 85.04000  ? 436 GLY A CA     1 
ATOM   3089  C  C      . GLY A 1 445 ? -2.95600  -15.67500 50.60800  1.000 72.23000  ? 436 GLY A C      1 
ATOM   3090  O  O      . GLY A 1 445 ? -1.72800  -15.85700 50.60200  1.000 81.95000  ? 436 GLY A O      1 
ATOM   3091  N  N      . LEU A 1 446 ? -3.53700  -14.59600 50.08200  1.000 69.61000  ? 437 LEU A N      1 
ATOM   3092  C  CA     . LEU A 1 446 ? -2.76200  -13.57200 49.39200  1.000 80.57000  ? 437 LEU A CA     1 
ATOM   3093  C  C      . LEU A 1 446 ? -1.89800  -12.80900 50.38600  1.000 76.61000  ? 437 LEU A C      1 
ATOM   3094  O  O      . LEU A 1 446 ? -0.75400  -12.43400 50.08300  1.000 85.98000  ? 437 LEU A O      1 
ATOM   3095  C  CB     . LEU A 1 446 ? -3.72600  -12.63400 48.66500  1.000 83.98000  ? 437 LEU A CB     1 
ATOM   3096  C  CG     . LEU A 1 446 ? -4.55700  -13.26500 47.53900  1.000 58.29000  ? 437 LEU A CG     1 
ATOM   3097  C  CD1    . LEU A 1 446 ? -5.53700  -12.25800 46.96300  1.000 44.64000  ? 437 LEU A CD1    1 
ATOM   3098  C  CD2    . LEU A 1 446 ? -3.67400  -13.83400 46.44100  1.000 55.74000  ? 437 LEU A CD2    1 
ATOM   3099  N  N      . TYR A 1 447 ? -2.43100  -12.59300 51.59100  1.000 74.43000  ? 438 TYR A N      1 
ATOM   3100  C  CA     . TYR A 1 447 ? -1.63400  -11.99200 52.65100  1.000 83.78000  ? 438 TYR A CA     1 
ATOM   3101  C  C      . TYR A 1 447 ? -0.37700  -12.81100 52.91200  1.000 78.09000  ? 438 TYR A C      1 
ATOM   3102  O  O      . TYR A 1 447 ? 0.70900   -12.25300 53.10400  1.000 85.59000  ? 438 TYR A O      1 
ATOM   3103  C  CB     . TYR A 1 447 ? -2.46800  -11.84500 53.92900  1.000 93.38000  ? 438 TYR A CB     1 
ATOM   3104  C  CG     . TYR A 1 447 ? -1.69200  -11.22500 55.07300  1.000 92.84000  ? 438 TYR A CG     1 
ATOM   3105  C  CD1    . TYR A 1 447 ? -1.28800  -9.89300  55.02300  1.000 78.36000  ? 438 TYR A CD1    1 
ATOM   3106  C  CD2    . TYR A 1 447 ? -1.35300  -11.96900 56.19600  1.000 85.73000  ? 438 TYR A CD2    1 
ATOM   3107  C  CE1    . TYR A 1 447 ? -0.56600  -9.31700  56.06100  1.000 80.50000  ? 438 TYR A CE1    1 
ATOM   3108  C  CE2    . TYR A 1 447 ? -0.63200  -11.40200 57.24000  1.000 88.18000  ? 438 TYR A CE2    1 
ATOM   3109  C  CZ     . TYR A 1 447 ? -0.24100  -10.07600 57.16700  1.000 86.95000  ? 438 TYR A CZ     1 
ATOM   3110  O  OH     . TYR A 1 447 ? 0.47500   -9.51400  58.20300  1.000 92.55000  ? 438 TYR A OH     1 
ATOM   3111  N  N      . GLY A 1 448 ? -0.49300  -14.13900 52.88300  1.000 76.91000  ? 439 GLY A N      1 
ATOM   3112  C  CA     . GLY A 1 448 ? 0.65900   -14.99100 53.09200  1.000 84.61000  ? 439 GLY A CA     1 
ATOM   3113  C  C      . GLY A 1 448 ? 1.60900   -14.99600 51.92100  1.000 86.08000  ? 439 GLY A C      1 
ATOM   3114  O  O      . GLY A 1 448 ? 2.81400   -15.17000 52.10100  1.000 92.47000  ? 439 GLY A O      1 
ATOM   3115  N  N      . VAL A 1 449 ? 1.08800   -14.82500 50.70700  1.000 89.80000  ? 440 VAL A N      1 
ATOM   3116  C  CA     . VAL A 1 449 ? 1.98500   -14.64100 49.56700  1.000 74.81000  ? 440 VAL A CA     1 
ATOM   3117  C  C      . VAL A 1 449 ? 2.84900   -13.39900 49.77700  1.000 74.92000  ? 440 VAL A C      1 
ATOM   3118  O  O      . VAL A 1 449 ? 4.07700   -13.43100 49.59700  1.000 72.87000  ? 440 VAL A O      1 
ATOM   3119  C  CB     . VAL A 1 449 ? 1.17900   -14.57200 48.25600  1.000 50.61000  ? 440 VAL A CB     1 
ATOM   3120  C  CG1    . VAL A 1 449 ? 2.07800   -14.21900 47.08700  1.000 46.32000  ? 440 VAL A CG1    1 
ATOM   3121  C  CG2    . VAL A 1 449 ? 0.47500   -15.90100 48.01000  1.000 55.54000  ? 440 VAL A CG2    1 
ATOM   3122  N  N      . ALA A 1 450 ? 2.23000   -12.29800 50.20600  1.000 55.43000  ? 441 ALA A N      1 
ATOM   3123  C  CA     . ALA A 1 450 ? 3.00700   -11.08900 50.47300  1.000 62.19000  ? 441 ALA A CA     1 
ATOM   3124  C  C      . ALA A 1 450 ? 3.97900   -11.29700 51.63200  1.000 67.17000  ? 441 ALA A C      1 
ATOM   3125  O  O      . ALA A 1 450 ? 5.12100   -10.81700 51.59500  1.000 80.44000  ? 441 ALA A O      1 
ATOM   3126  C  CB     . ALA A 1 450 ? 2.07300   -9.91600  50.75900  1.000 66.19000  ? 441 ALA A CB     1 
ATOM   3127  N  N      . ILE A 1 451 ? 3.54200   -12.01100 52.67000  1.000 55.84000  ? 442 ILE A N      1 
ATOM   3128  C  CA     . ILE A 1 451 ? 4.41700   -12.29300 53.80400  1.000 58.53000  ? 442 ILE A CA     1 
ATOM   3129  C  C      . ILE A 1 451 ? 5.61000   -13.13200 53.36000  1.000 80.31000  ? 442 ILE A C      1 
ATOM   3130  O  O      . ILE A 1 451 ? 6.72500   -12.98100 53.87500  1.000 93.61000  ? 442 ILE A O      1 
ATOM   3131  C  CB     . ILE A 1 451 ? 3.62300   -12.98600 54.92700  1.000 61.22000  ? 442 ILE A CB     1 
ATOM   3132  C  CG1    . ILE A 1 451 ? 2.69200   -11.98800 55.62300  1.000 80.15000  ? 442 ILE A CG1    1 
ATOM   3133  C  CG2    . ILE A 1 451 ? 4.56600   -13.63600 55.92400  1.000 82.75000  ? 442 ILE A CG2    1 
ATOM   3134  C  CD1    . ILE A 1 451 ? 3.41000   -10.83500 56.29200  1.000 93.22000  ? 442 ILE A CD1    1 
ATOM   3135  N  N      . ALA A 1 452 ? 5.39500   -14.03200 52.40100  1.000 79.16000  ? 443 ALA A N      1 
ATOM   3136  C  CA     . ALA A 1 452 ? 6.49100   -14.83700 51.87700  1.000 70.15000  ? 443 ALA A CA     1 
ATOM   3137  C  C      . ALA A 1 452 ? 7.46000   -13.98400 51.07300  1.000 60.11000  ? 443 ALA A C      1 
ATOM   3138  O  O      . ALA A 1 452 ? 8.67300   -14.20400 51.12300  1.000 57.88000  ? 443 ALA A O      1 
ATOM   3139  C  CB     . ALA A 1 452 ? 5.94800   -15.98500 51.02900  1.000 78.23000  ? 443 ALA A CB     1 
ATOM   3140  N  N      . ALA A 1 453 ? 6.94600   -13.01800 50.30900  1.000 64.56000  ? 444 ALA A N      1 
ATOM   3141  C  CA     . ALA A 1 453 ? 7.84800   -12.07600 49.65000  1.000 59.53000  ? 444 ALA A CA     1 
ATOM   3142  C  C      . ALA A 1 453 ? 8.70500   -11.34900 50.68100  1.000 65.73000  ? 444 ALA A C      1 
ATOM   3143  O  O      . ALA A 1 453 ? 9.93300   -11.24700 50.53700  1.000 85.68000  ? 444 ALA A O      1 
ATOM   3144  C  CB     . ALA A 1 453 ? 7.05600   -11.07800 48.80400  1.000 59.74000  ? 444 ALA A CB     1 
ATOM   3145  N  N      . LEU A 1 454 ? 8.07300   -10.87800 51.75800  1.000 72.16000  ? 445 LEU A N      1 
ATOM   3146  C  CA     . LEU A 1 454 ? 8.81600   -10.20000 52.81800  1.000 69.92000  ? 445 LEU A CA     1 
ATOM   3147  C  C      . LEU A 1 454 ? 9.89700   -11.10400 53.40400  1.000 78.03000  ? 445 LEU A C      1 
ATOM   3148  O  O      . LEU A 1 454 ? 11.04600  -10.68300 53.58400  1.000 72.04000  ? 445 LEU A O      1 
ATOM   3149  C  CB     . LEU A 1 454 ? 7.85600   -9.73400  53.91400  1.000 65.97000  ? 445 LEU A CB     1 
ATOM   3150  C  CG     . LEU A 1 454 ? 8.51700   -9.44300  55.26400  1.000 65.02000  ? 445 LEU A CG     1 
ATOM   3151  C  CD1    . LEU A 1 454 ? 9.54900   -8.33100  55.14600  1.000 77.19000  ? 445 LEU A CD1    1 
ATOM   3152  C  CD2    . LEU A 1 454 ? 7.47000   -9.10300  56.31200  1.000 98.13000  ? 445 LEU A CD2    1 
ATOM   3153  N  N      . GLY A 1 455 ? 9.54100   -12.35500 53.70800  1.000 76.19000  ? 446 GLY A N      1 
ATOM   3154  C  CA     . GLY A 1 455 ? 10.51800  -13.28700 54.25400  1.000 78.22000  ? 446 GLY A CA     1 
ATOM   3155  C  C      . GLY A 1 455 ? 11.66800  -13.55500 53.30300  1.000 77.32000  ? 446 GLY A C      1 
ATOM   3156  O  O      . GLY A 1 455 ? 12.83400  -13.58100 53.70600  1.000 79.19000  ? 446 GLY A O      1 
ATOM   3157  N  N      . MET A 1 456 ? 11.35000  -13.77600 52.02500  1.000 74.49000  ? 447 MET A N      1 
ATOM   3158  C  CA     . MET A 1 456 ? 12.38100  -13.91400 51.00400  1.000 62.23000  ? 447 MET A CA     1 
ATOM   3159  C  C      . MET A 1 456 ? 13.34600  -12.74200 51.03300  1.000 70.63000  ? 447 MET A C      1 
ATOM   3160  O  O      . MET A 1 456 ? 14.56500  -12.92600 50.93200  1.000 78.79000  ? 447 MET A O      1 
ATOM   3161  C  CB     . MET A 1 456 ? 11.73700  -14.02900 49.62100  1.000 65.19000  ? 447 MET A CB     1 
ATOM   3162  C  CG     . MET A 1 456 ? 12.73400  -14.21600 48.48700  1.000 74.94000  ? 447 MET A CG     1 
ATOM   3163  S  SD     . MET A 1 456 ? 11.94700  -14.45800 46.88000  1.000 54.19000  ? 447 MET A SD     1 
ATOM   3164  C  CE     . MET A 1 456 ? 10.91100  -15.87700 47.23600  1.000 72.07000  ? 447 MET A CE     1 
ATOM   3165  N  N      . LEU A 1 457 ? 12.82500  -11.52700 51.18600  1.000 70.29000  ? 448 LEU A N      1 
ATOM   3166  C  CA     . LEU A 1 457 ? 13.68200  -10.35300 51.22500  1.000 78.74000  ? 448 LEU A CA     1 
ATOM   3167  C  C      . LEU A 1 457 ? 13.92600  -9.85700  52.64300  1.000 77.22000  ? 448 LEU A C      1 
ATOM   3168  O  O      . LEU A 1 457 ? 14.32700  -8.70400  52.83200  1.000 82.05000  ? 448 LEU A O      1 
ATOM   3169  C  CB     . LEU A 1 457 ? 13.10200  -9.24100  50.35400  1.000 80.59000  ? 448 LEU A CB     1 
ATOM   3170  C  CG     . LEU A 1 457 ? 13.13500  -9.55500  48.85500  1.000 70.31000  ? 448 LEU A CG     1 
ATOM   3171  C  CD1    . LEU A 1 457 ? 12.00400  -8.84900  48.12800  1.000 79.71000  ? 448 LEU A CD1    1 
ATOM   3172  C  CD2    . LEU A 1 457 ? 14.48500  -9.19200  48.24700  1.000 67.45000  ? 448 LEU A CD2    1 
ATOM   3173  N  N      . SER A 1 458 ? 13.70100  -10.71400 53.64000  1.000 72.05000  ? 449 SER A N      1 
ATOM   3174  C  CA     . SER A 1 458 ? 13.98500  -10.34200 55.02100  1.000 80.16000  ? 449 SER A CA     1 
ATOM   3175  C  C      . SER A 1 458 ? 15.46400  -10.02100 55.21900  1.000 86.50000  ? 449 SER A C      1 
ATOM   3176  O  O      . SER A 1 458 ? 15.80800  -9.03800  55.88700  1.000 84.05000  ? 449 SER A O      1 
ATOM   3177  C  CB     . SER A 1 458 ? 13.53500  -11.46200 55.96100  1.000 69.01000  ? 449 SER A CB     1 
ATOM   3178  O  OG     . SER A 1 458 ? 14.41300  -12.57300 55.90300  1.000 79.46000  ? 449 SER A OG     1 
ATOM   3179  N  N      . PHE A 1 459 ? 16.35600  -10.82800 54.64500  1.000 82.42000  ? 450 PHE A N      1 
ATOM   3180  C  CA     . PHE A 1 459 ? 17.79400  -10.57300 54.75100  1.000 77.46000  ? 450 PHE A CA     1 
ATOM   3181  C  C      . PHE A 1 459 ? 18.30200  -9.71100  53.60900  1.000 79.83000  ? 450 PHE A C      1 
ATOM   3182  O  O      . PHE A 1 459 ? 19.36700  -9.97000  53.04100  1.000 77.50000  ? 450 PHE A O      1 
ATOM   3183  C  CB     . PHE A 1 459 ? 18.56600  -11.88900 54.81100  1.000 74.80000  ? 450 PHE A CB     1 
ATOM   3184  C  CG     . PHE A 1 459 ? 18.12400  -12.90400 53.79600  1.000 73.33000  ? 450 PHE A CG     1 
ATOM   3185  C  CD1    . PHE A 1 459 ? 17.03500  -13.72200 54.04100  1.000 90.06000  ? 450 PHE A CD1    1 
ATOM   3186  C  CD2    . PHE A 1 459 ? 18.80300  -13.04500 52.59600  1.000 67.12000  ? 450 PHE A CD2    1 
ATOM   3187  C  CE1    . PHE A 1 459 ? 16.62700  -14.65900 53.10900  1.000 99.32000  ? 450 PHE A CE1    1 
ATOM   3188  C  CE2    . PHE A 1 459 ? 18.40000  -13.98000 51.65900  1.000 87.99000  ? 450 PHE A CE2    1 
ATOM   3189  C  CZ     . PHE A 1 459 ? 17.31000  -14.78800 51.91700  1.000 97.31000  ? 450 PHE A CZ     1 
ATOM   3190  N  N      . VAL A 1 460 ? 17.54700  -8.67300  53.24800  1.000 73.54000  ? 451 VAL A N      1 
ATOM   3191  C  CA     . VAL A 1 460 ? 17.94500  -7.82800  52.13100  1.000 68.76000  ? 451 VAL A CA     1 
ATOM   3192  C  C      . VAL A 1 460 ? 19.28000  -7.16200  52.40900  1.000 86.66000  ? 451 VAL A C      1 
ATOM   3193  O  O      . VAL A 1 460 ? 20.05700  -6.90500  51.48400  1.000 86.47000  ? 451 VAL A O      1 
ATOM   3194  C  CB     . VAL A 1 460 ? 16.85400  -6.78500  51.83700  1.000 72.66000  ? 451 VAL A CB     1 
ATOM   3195  C  CG1    . VAL A 1 460 ? 16.53300  -5.99800  53.09900  1.000 101.05000 ? 451 VAL A CG1    1 
ATOM   3196  C  CG2    . VAL A 1 460 ? 17.29800  -5.86100  50.71700  1.000 65.33000  ? 451 VAL A CG2    1 
ATOM   3197  N  N      . ALA A 1 461 ? 19.57200  -6.86500  53.67600  1.000 107.95000 ? 452 ALA A N      1 
ATOM   3198  C  CA     . ALA A 1 461 ? 20.83400  -6.21100  53.99700  1.000 100.73000 ? 452 ALA A CA     1 
ATOM   3199  C  C      . ALA A 1 461 ? 22.01700  -7.10000  53.63300  1.000 93.90000  ? 452 ALA A C      1 
ATOM   3200  O  O      . ALA A 1 461 ? 22.98200  -6.64300  53.01500  1.000 73.53000  ? 452 ALA A O      1 
ATOM   3201  C  CB     . ALA A 1 461 ? 20.87000  -5.83000  55.47700  1.000 81.88000  ? 452 ALA A CB     1 
ATOM   3202  N  N      . THR A 1 462 ? 21.95600  -8.38200  54.00400  1.000 103.62000 ? 453 THR A N      1 
ATOM   3203  C  CA     . THR A 1 462 ? 23.04300  -9.30200  53.68000  1.000 95.37000  ? 453 THR A CA     1 
ATOM   3204  C  C      . THR A 1 462 ? 23.17200  -9.51600  52.17400  1.000 96.07000  ? 453 THR A C      1 
ATOM   3205  O  O      . THR A 1 462 ? 24.28900  -9.56100  51.63600  1.000 106.77000 ? 453 THR A O      1 
ATOM   3206  C  CB     . THR A 1 462 ? 22.82400  -10.63800 54.39200  1.000 99.05000  ? 453 THR A CB     1 
ATOM   3207  O  OG1    . THR A 1 462 ? 22.52000  -10.40300 55.77300  1.000 104.90000 ? 453 THR A OG1    1 
ATOM   3208  C  CG2    . THR A 1 462 ? 24.06600  -11.50600 54.29400  1.000 105.92000 ? 453 THR A CG2    1 
ATOM   3209  N  N      . SER A 1 463 ? 22.04200  -9.66700  51.47800  1.000 84.98000  ? 454 SER A N      1 
ATOM   3210  C  CA     . SER A 1 463 ? 22.08600  -9.85200  50.03200  1.000 79.08000  ? 454 SER A CA     1 
ATOM   3211  C  C      . SER A 1 463 ? 22.71900  -8.64300  49.35600  1.000 82.28000  ? 454 SER A C      1 
ATOM   3212  O  O      . SER A 1 463 ? 23.61800  -8.77900  48.51600  1.000 94.37000  ? 454 SER A O      1 
ATOM   3213  C  CB     . SER A 1 463 ? 20.67500  -10.10300 49.49500  1.000 81.44000  ? 454 SER A CB     1 
ATOM   3214  O  OG     . SER A 1 463 ? 20.12300  -11.28600 50.05000  1.000 87.50000  ? 454 SER A OG     1 
ATOM   3215  N  N      . VAL A 1 464 ? 22.26900  -7.44500  49.72800  1.000 66.34000  ? 455 VAL A N      1 
ATOM   3216  C  CA     . VAL A 1 464 ? 22.82400  -6.22400  49.15800  1.000 69.81000  ? 455 VAL A CA     1 
ATOM   3217  C  C      . VAL A 1 464 ? 24.28900  -6.07800  49.53400  1.000 91.49000  ? 455 VAL A C      1 
ATOM   3218  O  O      . VAL A 1 464 ? 25.08200  -5.52600  48.76600  1.000 98.66000  ? 455 VAL A O      1 
ATOM   3219  C  CB     . VAL A 1 464 ? 22.00300  -5.00100  49.60300  1.000 78.11000  ? 455 VAL A CB     1 
ATOM   3220  C  CG1    . VAL A 1 464 ? 22.70300  -3.71700  49.17500  1.000 86.28000  ? 455 VAL A CG1    1 
ATOM   3221  C  CG2    . VAL A 1 464 ? 20.59400  -5.07300  49.03800  1.000 64.46000  ? 455 VAL A CG2    1 
ATOM   3222  N  N      . SER A 1 465 ? 24.67200  -6.54600  50.72100  1.000 95.19000  ? 456 SER A N      1 
ATOM   3223  C  CA     . SER A 1 465 ? 26.06000  -6.42900  51.14900  1.000 96.83000  ? 456 SER A CA     1 
ATOM   3224  C  C      . SER A 1 465 ? 26.97600  -7.28600  50.28700  1.000 97.71000  ? 456 SER A C      1 
ATOM   3225  O  O      . SER A 1 465 ? 28.02000  -6.81800  49.82000  1.000 109.02000 ? 456 SER A O      1 
ATOM   3226  C  CB     . SER A 1 465 ? 26.17500  -6.81300  52.62300  1.000 101.47000 ? 456 SER A CB     1 
ATOM   3227  O  OG     . SER A 1 465 ? 25.64400  -5.79000  53.44800  1.000 124.20000 ? 456 SER A OG     1 
ATOM   3228  N  N      . VAL A 1 466 ? 26.60300  -8.54700  50.06500  1.000 87.17000  ? 457 VAL A N      1 
ATOM   3229  C  CA     . VAL A 1 466 ? 27.40900  -9.40000  49.19200  1.000 88.75000  ? 457 VAL A CA     1 
ATOM   3230  C  C      . VAL A 1 466 ? 27.41500  -8.84400  47.77100  1.000 105.33000 ? 457 VAL A C      1 
ATOM   3231  O  O      . VAL A 1 466 ? 28.45800  -8.81700  47.08700  1.000 120.30000 ? 457 VAL A O      1 
ATOM   3232  C  CB     . VAL A 1 466 ? 26.88300  -10.84600 49.24100  1.000 87.20000  ? 457 VAL A CB     1 
ATOM   3233  C  CG1    . VAL A 1 466 ? 27.67900  -11.73800 48.30500  1.000 115.82000 ? 457 VAL A CG1    1 
ATOM   3234  C  CG2    . VAL A 1 466 ? 26.93200  -11.37500 50.67000  1.000 83.01000  ? 457 VAL A CG2    1 
ATOM   3235  N  N      . ASP A 1 467 ? 26.26900  -8.31300  47.33600  1.000 91.28000  ? 458 ASP A N      1 
ATOM   3236  C  CA     . ASP A 1 467 ? 26.17900  -7.76000  45.99500  1.000 87.61000  ? 458 ASP A CA     1 
ATOM   3237  C  C      . ASP A 1 467 ? 27.11600  -6.57000  45.84000  1.000 107.26000 ? 458 ASP A C      1 
ATOM   3238  O  O      . ASP A 1 467 ? 27.75300  -6.40700  44.79600  1.000 119.09000 ? 458 ASP A O      1 
ATOM   3239  C  CB     . ASP A 1 467 ? 24.73300  -7.35800  45.69900  1.000 87.98000  ? 458 ASP A CB     1 
ATOM   3240  C  CG     . ASP A 1 467 ? 23.79800  -8.55800  45.58600  1.000 107.55000 ? 458 ASP A CG     1 
ATOM   3241  O  OD1    . ASP A 1 467 ? 24.29000  -9.69900  45.45700  1.000 126.51000 ? 458 ASP A OD1    1 
ATOM   3242  O  OD2    . ASP A 1 467 ? 22.56500  -8.35700  45.62900  1.000 98.95000  ? 458 ASP A OD2    1 
ATOM   3243  N  N      . SER A 1 468 ? 27.19700  -5.71700  46.86600  1.000 107.55000 ? 459 SER A N      1 
ATOM   3244  C  CA     . SER A 1 468 ? 28.12500  -4.59000  46.83700  1.000 95.04000  ? 459 SER A CA     1 
ATOM   3245  C  C      . SER A 1 468 ? 29.57400  -5.05500  46.93900  1.000 92.43000  ? 459 SER A C      1 
ATOM   3246  O  O      . SER A 1 468 ? 30.46600  -4.45900  46.32500  1.000 94.40000  ? 459 SER A O      1 
ATOM   3247  C  CB     . SER A 1 468 ? 27.79600  -3.61700  47.97000  1.000 89.04000  ? 459 SER A CB     1 
ATOM   3248  O  OG     . SER A 1 468 ? 26.48600  -3.09500  47.82800  1.000 88.35000  ? 459 SER A OG     1 
ATOM   3249  N  N      . TYR A 1 469 ? 29.83000  -6.11200  47.71700  1.000 94.88000  ? 460 TYR A N      1 
ATOM   3250  C  CA     . TYR A 1 469 ? 31.18300  -6.65500  47.79300  1.000 95.51000  ? 460 TYR A CA     1 
ATOM   3251  C  C      . TYR A 1 469 ? 31.70400  -6.97200  46.40400  1.000 111.56000 ? 460 TYR A C      1 
ATOM   3252  O  O      . TYR A 1 469 ? 32.86800  -6.69900  46.08800  1.000 133.49000 ? 460 TYR A O      1 
ATOM   3253  C  CB     . TYR A 1 469 ? 31.22500  -7.91200  48.66400  1.000 97.58000  ? 460 TYR A CB     1 
ATOM   3254  C  CG     . TYR A 1 469 ? 32.26400  -8.92300  48.20300  1.000 114.81000 ? 460 TYR A CG     1 
ATOM   3255  C  CD1    . TYR A 1 469 ? 33.59300  -8.81100  48.59900  1.000 129.08000 ? 460 TYR A CD1    1 
ATOM   3256  C  CD2    . TYR A 1 469 ? 31.91800  -9.98500  47.37500  1.000 128.21000 ? 460 TYR A CD2    1 
ATOM   3257  C  CE1    . TYR A 1 469 ? 34.54600  -9.72400  48.18200  1.000 134.00000 ? 460 TYR A CE1    1 
ATOM   3258  C  CE2    . TYR A 1 469 ? 32.86800  -10.90500 46.95200  1.000 128.31000 ? 460 TYR A CE2    1 
ATOM   3259  C  CZ     . TYR A 1 469 ? 34.18100  -10.76900 47.36000  1.000 125.54000 ? 460 TYR A CZ     1 
ATOM   3260  O  OH     . TYR A 1 469 ? 35.13900  -11.67300 46.95300  1.000 114.53000 ? 460 TYR A OH     1 
ATOM   3261  N  N      . GLY A 1 470 ? 30.85600  -7.56100  45.56500  1.000 111.28000 ? 461 GLY A N      1 
ATOM   3262  C  CA     . GLY A 1 470 ? 31.28500  -7.95700  44.24000  1.000 115.07000 ? 461 GLY A CA     1 
ATOM   3263  C  C      . GLY A 1 470 ? 32.14700  -7.02800  43.38800  1.000 118.17000 ? 461 GLY A C      1 
ATOM   3264  O  O      . GLY A 1 470 ? 33.30000  -7.34200  43.05400  1.000 119.63000 ? 461 GLY A O      1 
ATOM   3265  N  N      . PRO A 1 471 ? 31.60500  -5.85900  43.01900  1.000 115.55000 ? 462 PRO A N      1 
ATOM   3266  C  CA     . PRO A 1 471 ? 32.46100  -4.89600  42.28000  1.000 110.25000 ? 462 PRO A CA     1 
ATOM   3267  C  C      . PRO A 1 471 ? 33.54500  -4.07600  43.05900  1.000 111.73000 ? 462 PRO A C      1 
ATOM   3268  O  O      . PRO A 1 471 ? 34.50000  -3.48800  42.53400  1.000 113.96000 ? 462 PRO A O      1 
ATOM   3269  C  CB     . PRO A 1 471 ? 31.45900  -3.80700  41.87600  1.000 101.86000 ? 462 PRO A CB     1 
ATOM   3270  C  CG     . PRO A 1 471 ? 30.43800  -3.83000  42.94800  1.000 118.68000 ? 462 PRO A CG     1 
ATOM   3271  C  CD     . PRO A 1 471 ? 30.25700  -5.27300  43.32100  1.000 121.68000 ? 462 PRO A CD     1 
ATOM   3272  N  N      . ILE A 1 472 ? 33.38600  -4.13600  44.38200  1.000 124.55000 ? 463 ILE A N      1 
ATOM   3273  C  CA     . ILE A 1 472 ? 34.39200  -3.54500  45.25500  1.000 121.08000 ? 463 ILE A CA     1 
ATOM   3274  C  C      . ILE A 1 472 ? 35.58100  -4.42000  44.89500  1.000 109.96000 ? 463 ILE A C      1 
ATOM   3275  O  O      . ILE A 1 472 ? 36.67600  -3.92200  44.61800  1.000 112.47000 ? 463 ILE A O      1 
ATOM   3276  C  CB     . ILE A 1 472 ? 34.16400  -3.50100  46.77800  1.000 109.46000 ? 463 ILE A CB     1 
ATOM   3277  C  CG1    . ILE A 1 472 ? 33.02600  -2.54100  47.13800  1.000 109.89000 ? 463 ILE A CG1    1 
ATOM   3278  C  CG2    . ILE A 1 472 ? 35.45300  -3.11700  47.50300  1.000 93.52000  ? 463 ILE A CG2    1 
ATOM   3279  C  CD1    . ILE A 1 472 ? 32.75900  -2.47700  48.62900  1.000 92.80000  ? 463 ILE A CD1    1 
ATOM   3280  N  N      . ALA A 1 473 ? 35.37000  -5.73500  44.84900  1.000 100.75000 ? 464 ALA A N      1 
ATOM   3281  C  CA     . ALA A 1 473 ? 36.44100  -6.64900  44.47400  1.000 102.23000 ? 464 ALA A CA     1 
ATOM   3282  C  C      . ALA A 1 473 ? 36.84700  -6.47900  43.01600  1.000 124.02000 ? 464 ALA A C      1 
ATOM   3283  O  O      . ALA A 1 473 ? 38.03900  -6.52400  42.69800  1.000 134.31000 ? 464 ALA A O      1 
ATOM   3284  C  CB     . ALA A 1 473 ? 36.01500  -8.08900  44.74800  1.000 113.41000 ? 464 ALA A CB     1 
ATOM   3285  N  N      . ASP A 1 474 ? 35.87800  -6.30100  42.11000  1.000 123.41000 ? 465 ASP A N      1 
ATOM   3286  C  CA     . ASP A 1 474 ? 36.22800  -6.14300  40.69800  1.000 124.57000 ? 465 ASP A CA     1 
ATOM   3287  C  C      . ASP A 1 474 ? 37.11100  -4.93700  40.39700  1.000 122.58000 ? 465 ASP A C      1 
ATOM   3288  O  O      . ASP A 1 474 ? 38.16200  -5.05500  39.75000  1.000 132.36000 ? 465 ASP A O      1 
ATOM   3289  C  CB     . ASP A 1 474 ? 34.95900  -6.11900  39.84100  1.000 129.31000 ? 465 ASP A CB     1 
ATOM   3290  C  CG     . ASP A 1 474 ? 35.25700  -6.05300  38.35600  1.000 120.75000 ? 465 ASP A CG     1 
ATOM   3291  O  OD1    . ASP A 1 474 ? 35.76200  -5.01200  37.88800  1.000 115.61000 ? 465 ASP A OD1    1 
ATOM   3292  O  OD2    . ASP A 1 474 ? 34.98700  -7.05300  37.66000  1.000 112.19000 ? 465 ASP A OD2    1 
ATOM   3293  N  N      . ASN A 1 475 ? 36.70900  -3.76300  40.88000  1.000 112.96000 ? 466 ASN A N      1 
ATOM   3294  C  CA     . ASN A 1 475 ? 37.54500  -2.58900  40.66800  1.000 107.89000 ? 466 ASN A CA     1 
ATOM   3295  C  C      . ASN A 1 475 ? 38.81400  -2.59800  41.52300  1.000 120.07000 ? 466 ASN A C      1 
ATOM   3296  O  O      . ASN A 1 475 ? 39.81400  -1.99000  41.14900  1.000 121.74000 ? 466 ASN A O      1 
ATOM   3297  C  CB     . ASN A 1 475 ? 36.76300  -1.31500  40.97200  1.000 113.74000 ? 466 ASN A CB     1 
ATOM   3298  C  CG     . ASN A 1 475 ? 35.71600  -1.02600  39.91700  1.000 112.42000 ? 466 ASN A CG     1 
ATOM   3299  O  OD1    . ASN A 1 475 ? 35.82700  -1.49000  38.78200  1.000 110.73000 ? 466 ASN A OD1    1 
ATOM   3300  N  ND2    . ASN A 1 475 ? 34.69800  -0.25500  40.28000  1.000 102.36000 ? 466 ASN A ND2    1 
ATOM   3301  N  N      . ALA A 1 476 ? 38.80000  -3.30700  42.65600  1.000 118.25000 ? 467 ALA A N      1 
ATOM   3302  C  CA     . ALA A 1 476 ? 40.00800  -3.42000  43.46700  1.000 119.03000 ? 467 ALA A CA     1 
ATOM   3303  C  C      . ALA A 1 476 ? 41.00500  -4.23700  42.65500  1.000 125.84000 ? 467 ALA A C      1 
ATOM   3304  O  O      . ALA A 1 476 ? 42.19900  -3.91800  42.61500  1.000 128.14000 ? 467 ALA A O      1 
ATOM   3305  C  CB     . ALA A 1 476 ? 39.77000  -4.05200  44.83800  1.000 106.04000 ? 467 ALA A CB     1 
ATOM   3306  N  N      . GLY A 1 477 ? 40.53600  -5.30900  42.01500  1.000 129.98000 ? 468 GLY A N      1 
ATOM   3307  C  CA     . GLY A 1 477 ? 41.39300  -6.05200  41.10900  1.000 123.70000 ? 468 GLY A CA     1 
ATOM   3308  C  C      . GLY A 1 477 ? 41.87300  -5.18300  39.96800  1.000 120.22000 ? 468 GLY A C      1 
ATOM   3309  O  O      . GLY A 1 477 ? 43.02800  -5.27400  39.54200  1.000 135.45000 ? 468 GLY A O      1 
ATOM   3310  N  N      . GLY A 1 478 ? 40.99100  -4.32800  39.45500  1.000 115.67000 ? 469 GLY A N      1 
ATOM   3311  C  CA     . GLY A 1 478 ? 41.44600  -3.34000  38.49800  1.000 118.43000 ? 469 GLY A CA     1 
ATOM   3312  C  C      . GLY A 1 478 ? 42.46200  -2.43700  39.17500  1.000 138.92000 ? 469 GLY A C      1 
ATOM   3313  O  O      . GLY A 1 478 ? 43.48100  -2.08500  38.57700  1.000 152.91000 ? 469 GLY A O      1 
ATOM   3314  N  N      . ILE A 1 479 ? 42.22700  -2.09400  40.44900  1.000 139.71000 ? 470 ILE A N      1 
ATOM   3315  C  CA     . ILE A 1 479 ? 43.17200  -1.25500  41.18900  1.000 149.12000 ? 470 ILE A CA     1 
ATOM   3316  C  C      . ILE A 1 479 ? 44.51800  -1.96500  41.33900  1.000 146.10000 ? 470 ILE A C      1 
ATOM   3317  O  O      . ILE A 1 479 ? 45.58600  -1.36600  41.16100  1.000 154.31000 ? 470 ILE A O      1 
ATOM   3318  C  CB     . ILE A 1 479 ? 42.59300  -0.76900  42.54100  1.000 138.83000 ? 470 ILE A CB     1 
ATOM   3319  C  CG1    . ILE A 1 479 ? 41.26600  -0.02000  42.37600  1.000 149.36000 ? 470 ILE A CG1    1 
ATOM   3320  C  CG2    . ILE A 1 479 ? 43.62300  0.02100   43.37600  1.000 116.97000 ? 470 ILE A CG2    1 
ATOM   3321  C  CD1    . ILE A 1 479 ? 41.36000  1.21000   41.48600  1.000 147.31000 ? 470 ILE A CD1    1 
ATOM   3322  N  N      . SER A 1 480 ? 44.48000  -3.25200  41.69900  1.000 126.04000 ? 471 SER A N      1 
ATOM   3323  C  CA     . SER A 1 480 ? 45.71000  -4.03500  41.72300  1.000 112.52000 ? 471 SER A CA     1 
ATOM   3324  C  C      . SER A 1 480 ? 46.44600  -4.08000  40.39500  1.000 131.19000 ? 471 SER A C      1 
ATOM   3325  O  O      . SER A 1 480 ? 47.68100  -4.03800  40.35700  1.000 155.23000 ? 471 SER A O      1 
ATOM   3326  C  CB     . SER A 1 480 ? 45.35100  -5.44400  42.20100  1.000 114.13000 ? 471 SER A CB     1 
ATOM   3327  O  OG     . SER A 1 480 ? 46.44800  -6.33300  42.07100  1.000 127.60000 ? 471 SER A OG     1 
ATOM   3328  N  N      . GLU A 1 481 ? 45.69900  -4.19300  39.29300  1.000 131.90000 ? 472 GLU A N      1 
ATOM   3329  C  CA     . GLU A 1 481 ? 46.30700  -4.12400  37.97400  1.000 138.50000 ? 472 GLU A CA     1 
ATOM   3330  C  C      . GLU A 1 481 ? 46.58600  -2.69400  37.54100  1.000 147.59000 ? 472 GLU A C      1 
ATOM   3331  O  O      . GLU A 1 481 ? 47.39900  -2.49700  36.63300  1.000 157.50000 ? 472 GLU A O      1 
ATOM   3332  C  CB     . GLU A 1 481 ? 45.44900  -4.83200  36.92100  1.000 147.75000 ? 472 GLU A CB     1 
ATOM   3333  C  CG     . GLU A 1 481 ? 46.22600  -5.12500  35.62700  1.000 138.41000 ? 472 GLU A CG     1 
ATOM   3334  C  CD     . GLU A 1 481 ? 45.45200  -5.99600  34.65700  1.000 143.60000 ? 472 GLU A CD     1 
ATOM   3335  O  OE1    . GLU A 1 481 ? 44.52200  -6.69300  35.11300  1.000 140.09000 ? 472 GLU A OE1    1 
ATOM   3336  O  OE2    . GLU A 1 481 ? 45.79800  -6.02700  33.45600  1.000 146.48000 ? 472 GLU A OE2    1 
ATOM   3337  N  N      . MET A 1 482 ? 45.91900  -1.69400  38.12800  1.000 147.92000 ? 473 MET A N      1 
ATOM   3338  C  CA     . MET A 1 482 ? 46.31700  -0.32600  37.82700  1.000 168.09000 ? 473 MET A CA     1 
ATOM   3339  C  C      . MET A 1 482 ? 47.80000  -0.25100  38.13600  1.000 176.69000 ? 473 MET A C      1 
ATOM   3340  O  O      . MET A 1 482 ? 48.36200  -1.15700  38.75900  1.000 182.60000 ? 473 MET A O      1 
ATOM   3341  C  CB     . MET A 1 482 ? 45.67700  0.69000   38.76900  1.000 165.62000 ? 473 MET A CB     1 
ATOM   3342  C  CG     . MET A 1 482 ? 44.17800  0.65800   38.84200  1.000 167.02000 ? 473 MET A CG     1 
ATOM   3343  S  SD     . MET A 1 482 ? 43.26200  0.90700   37.30900  1.000 178.44000 ? 473 MET A SD     1 
ATOM   3344  C  CE     . MET A 1 482 ? 41.63900  0.75100   38.03200  1.000 148.50000 ? 473 MET A CE     1 
ATOM   3345  N  N      . CYS A 1 483 ? 48.42900  0.84200   37.70900  1.000 181.90000 ? 474 CYS A N      1 
ATOM   3346  C  CA     . CYS A 1 483 ? 49.89900  0.90700   37.68800  1.000 191.12000 ? 474 CYS A CA     1 
ATOM   3347  C  C      . CYS A 1 483 ? 50.46700  -0.41300  37.17100  1.000 194.94000 ? 474 CYS A C      1 
ATOM   3348  O  O      . CYS A 1 483 ? 50.06700  -0.86500  36.08800  1.000 193.07000 ? 474 CYS A O      1 
ATOM   3349  C  CB     . CYS A 1 483 ? 50.47300  1.35600   39.05900  1.000 200.02000 ? 474 CYS A CB     1 
ATOM   3350  S  SG     . CYS A 1 483 ? 50.07500  0.49400   40.62400  1.000 226.15000 ? 474 CYS A SG     1 
ATOM   3351  N  N      . GLU A 1 484 ? 51.34700  -1.05600  37.92900  1.000 200.53000 ? 475 GLU A N      1 
ATOM   3352  C  CA     . GLU A 1 484 ? 51.77700  -2.42200  37.68400  1.000 182.94000 ? 475 GLU A CA     1 
ATOM   3353  C  C      . GLU A 1 484 ? 51.81300  -2.87900  39.13000  1.000 177.52000 ? 475 GLU A C      1 
ATOM   3354  O  O      . GLU A 1 484 ? 51.87500  -2.06000  40.04900  1.000 199.57000 ? 475 GLU A O      1 
ATOM   3355  C  CB     . GLU A 1 484 ? 53.16300  -2.51500  37.03900  1.000 184.55000 ? 475 GLU A CB     1 
ATOM   3356  C  CG     . GLU A 1 484 ? 53.24100  -1.80500  35.70000  1.000 186.54000 ? 475 GLU A CG     1 
ATOM   3357  C  CD     . GLU A 1 484 ? 54.63800  -1.81800  35.13600  1.000 180.83000 ? 475 GLU A CD     1 
ATOM   3358  O  OE1    . GLU A 1 484 ? 54.90400  -1.05300  34.18400  1.000 176.31000 ? 475 GLU A OE1    1 
ATOM   3359  O  OE2    . GLU A 1 484 ? 55.47500  -2.58000  35.66900  1.000 170.05000 ? 475 GLU A OE2    1 
ATOM   3360  N  N      . LEU A 1 485 ? 51.75400  -4.19300  39.32900  1.000 152.65000 ? 476 LEU A N      1 
ATOM   3361  C  CA     . LEU A 1 485 ? 51.76800  -4.77400  40.66300  1.000 153.47000 ? 476 LEU A CA     1 
ATOM   3362  C  C      . LEU A 1 485 ? 52.31500  -6.18900  40.58900  1.000 154.88000 ? 476 LEU A C      1 
ATOM   3363  O  O      . LEU A 1 485 ? 52.34200  -6.81100  39.52400  1.000 155.76000 ? 476 LEU A O      1 
ATOM   3364  C  CB     . LEU A 1 485 ? 50.37200  -4.77000  41.29700  1.000 145.64000 ? 476 LEU A CB     1 
ATOM   3365  C  CG     . LEU A 1 485 ? 50.32600  -5.10800  42.78700  1.000 140.64000 ? 476 LEU A CG     1 
ATOM   3366  C  CD1    . LEU A 1 485 ? 51.28500  -4.25500  43.56300  1.000 142.79000 ? 476 LEU A CD1    1 
ATOM   3367  C  CD2    . LEU A 1 485 ? 48.90900  -4.95200  43.33400  1.000 143.65000 ? 476 LEU A CD2    1 
ATOM   3368  N  N      . ASP A 1 486 ? 52.73500  -6.69200  41.74400  1.000 152.13000 ? 477 ASP A N      1 
ATOM   3369  C  CA     . ASP A 1 486 ? 53.34000  -8.01400  41.81700  1.000 144.81000 ? 477 ASP A CA     1 
ATOM   3370  C  C      . ASP A 1 486 ? 52.39000  -9.07400  41.26300  1.000 130.58000 ? 477 ASP A C      1 
ATOM   3371  O  O      . ASP A 1 486 ? 51.19200  -9.05800  41.57500  1.000 130.53000 ? 477 ASP A O      1 
ATOM   3372  C  CB     . ASP A 1 486 ? 53.70300  -8.36300  43.26200  1.000 147.65000 ? 477 ASP A CB     1 
ATOM   3373  C  CG     . ASP A 1 486 ? 54.77400  -7.46100  43.83400  1.000 144.75000 ? 477 ASP A CG     1 
ATOM   3374  O  OD1    . ASP A 1 486 ? 55.50700  -6.82800  43.04600  1.000 152.96000 ? 477 ASP A OD1    1 
ATOM   3375  O  OD2    . ASP A 1 486 ? 54.88100  -7.38700  45.07600  1.000 121.49000 ? 477 ASP A OD2    1 
ATOM   3376  N  N      . PRO A 1 487 ? 52.88500  -10.01200 40.44500  1.000 128.24000 ? 478 PRO A N      1 
ATOM   3377  C  CA     . PRO A 1 487 ? 51.99200  -11.06700 39.93500  1.000 127.24000 ? 478 PRO A CA     1 
ATOM   3378  C  C      . PRO A 1 487 ? 51.37600  -11.89000 41.05200  1.000 135.88000 ? 478 PRO A C      1 
ATOM   3379  O  O      . PRO A 1 487 ? 50.18700  -12.22300 40.99100  1.000 148.85000 ? 478 PRO A O      1 
ATOM   3380  C  CB     . PRO A 1 487 ? 52.91300  -11.91100 39.04100  1.000 128.66000 ? 478 PRO A CB     1 
ATOM   3381  C  CG     . PRO A 1 487 ? 54.03100  -11.00100 38.68000  1.000 143.34000 ? 478 PRO A CG     1 
ATOM   3382  C  CD     . PRO A 1 487 ? 54.24200  -10.12300 39.88200  1.000 135.28000 ? 478 PRO A CD     1 
ATOM   3383  N  N      . GLU A 1 488 ? 52.16400  -12.24100 42.07100  1.000 130.94000 ? 479 GLU A N      1 
ATOM   3384  C  CA     . GLU A 1 488 ? 51.61200  -12.95100 43.21900  1.000 128.56000 ? 479 GLU A CA     1 
ATOM   3385  C  C      . GLU A 1 488 ? 50.55400  -12.11300 43.92400  1.000 133.28000 ? 479 GLU A C      1 
ATOM   3386  O  O      . GLU A 1 488 ? 49.50700  -12.63200 44.33100  1.000 131.36000 ? 479 GLU A O      1 
ATOM   3387  C  CB     . GLU A 1 488 ? 52.73400  -13.32400 44.18600  1.000 132.93000 ? 479 GLU A CB     1 
ATOM   3388  C  CG     . GLU A 1 488 ? 52.24700  -13.77400 45.55100  1.000 150.03000 ? 479 GLU A CG     1 
ATOM   3389  C  CD     . GLU A 1 488 ? 52.34700  -12.67800 46.59200  1.000 156.22000 ? 479 GLU A CD     1 
ATOM   3390  O  OE1    . GLU A 1 488 ? 53.01700  -11.65700 46.32400  1.000 149.62000 ? 479 GLU A OE1    1 
ATOM   3391  O  OE2    . GLU A 1 488 ? 51.75000  -12.83500 47.67700  1.000 156.05000 ? 479 GLU A OE2    1 
ATOM   3392  N  N      . VAL A 1 489 ? 50.81300  -10.81400 44.08500  1.000 141.85000 ? 480 VAL A N      1 
ATOM   3393  C  CA     . VAL A 1 489 ? 49.82500  -9.92900  44.69700  1.000 145.30000 ? 480 VAL A CA     1 
ATOM   3394  C  C      . VAL A 1 489 ? 48.57800  -9.84500  43.82500  1.000 140.58000 ? 480 VAL A C      1 
ATOM   3395  O  O      . VAL A 1 489 ? 47.44900  -9.80900  44.32900  1.000 135.25000 ? 480 VAL A O      1 
ATOM   3396  C  CB     . VAL A 1 489 ? 50.43600  -8.54000  44.95800  1.000 140.36000 ? 480 VAL A CB     1 
ATOM   3397  C  CG1    . VAL A 1 489 ? 49.37400  -7.58800  45.48700  1.000 133.82000 ? 480 VAL A CG1    1 
ATOM   3398  C  CG2    . VAL A 1 489 ? 51.59400  -8.65200  45.93700  1.000 140.74000 ? 480 VAL A CG2    1 
ATOM   3399  N  N      . ARG A 1 490 ? 48.76400  -9.80000  42.50300  1.000 135.57000 ? 481 ARG A N      1 
ATOM   3400  C  CA     . ARG A 1 490 ? 47.62700  -9.71300  41.59100  1.000 118.87000 ? 481 ARG A CA     1 
ATOM   3401  C  C      . ARG A 1 490 ? 46.73400  -10.94300 41.69600  1.000 122.93000 ? 481 ARG A C      1 
ATOM   3402  O  O      . ARG A 1 490 ? 45.50600  -10.83600 41.60000  1.000 144.61000 ? 481 ARG A O      1 
ATOM   3403  C  CB     . ARG A 1 490 ? 48.11400  -9.52400  40.15300  1.000 114.48000 ? 481 ARG A CB     1 
ATOM   3404  C  CG     . ARG A 1 490 ? 48.38900  -8.07400  39.76700  1.000 133.90000 ? 481 ARG A CG     1 
ATOM   3405  C  CD     . ARG A 1 490 ? 48.86400  -7.96200  38.32200  1.000 145.59000 ? 481 ARG A CD     1 
ATOM   3406  N  NE     . ARG A 1 490 ? 50.13800  -8.63900  38.10700  1.000 156.15000 ? 481 ARG A NE     1 
ATOM   3407  C  CZ     . ARG A 1 490 ? 50.79300  -8.65800  36.95400  1.000 138.77000 ? 481 ARG A CZ     1 
ATOM   3408  N  NH1    . ARG A 1 490 ? 51.94900  -9.28800  36.82700  1.000 129.55000 ? 481 ARG A NH1    1 
ATOM   3409  N  NH2    . ARG A 1 490 ? 50.27500  -8.02800  35.90300  1.000 117.08000 ? 481 ARG A NH2    1 
ATOM   3410  N  N      . LYS A 1 491 ? 47.32800  -12.12300 41.88800  1.000 115.83000 ? 482 LYS A N      1 
ATOM   3411  C  CA     . LYS A 1 491 ? 46.52700  -13.34200 41.95400  1.000 124.08000 ? 482 LYS A CA     1 
ATOM   3412  C  C      . LYS A 1 491 ? 45.56300  -13.32500 43.13600  1.000 129.35000 ? 482 LYS A C      1 
ATOM   3413  O  O      . LYS A 1 491 ? 44.40900  -13.75000 43.00500  1.000 133.45000 ? 482 LYS A O      1 
ATOM   3414  C  CB     . LYS A 1 491 ? 47.43400  -14.56900 42.02400  1.000 121.63000 ? 482 LYS A CB     1 
ATOM   3415  C  CG     . LYS A 1 491 ? 46.67800  -15.88200 41.91000  1.000 104.69000 ? 482 LYS A CG     1 
ATOM   3416  C  CD     . LYS A 1 491 ? 47.60100  -17.03100 41.56500  1.000 110.64000 ? 482 LYS A CD     1 
ATOM   3417  C  CE     . LYS A 1 491 ? 46.80700  -18.20800 41.02700  1.000 122.27000 ? 482 LYS A CE     1 
ATOM   3418  N  NZ     . LYS A 1 491 ? 45.99200  -17.82700 39.83800  1.000 88.58000  ? 482 LYS A NZ     1 
ATOM   3419  N  N      . ILE A 1 492 ? 46.01400  -12.85700 44.30300  1.000 131.05000 ? 483 ILE A N      1 
ATOM   3420  C  CA     . ILE A 1 492 ? 45.13700  -12.86600 45.47200  1.000 123.60000 ? 483 ILE A CA     1 
ATOM   3421  C  C      . ILE A 1 492 ? 43.96600  -11.91100 45.27100  1.000 126.02000 ? 483 ILE A C      1 
ATOM   3422  O  O      . ILE A 1 492 ? 42.81400  -12.25000 45.56800  1.000 133.23000 ? 483 ILE A O      1 
ATOM   3423  C  CB     . ILE A 1 492 ? 45.92900  -12.54000 46.75400  1.000 123.96000 ? 483 ILE A CB     1 
ATOM   3424  C  CG1    . ILE A 1 492 ? 46.47200  -11.10900 46.71800  1.000 129.22000 ? 483 ILE A CG1    1 
ATOM   3425  C  CG2    . ILE A 1 492 ? 47.06000  -13.53800 46.95400  1.000 129.94000 ? 483 ILE A CG2    1 
ATOM   3426  C  CD1    . ILE A 1 492 ? 47.57100  -10.85300 47.73100  1.000 122.51000 ? 483 ILE A CD1    1 
ATOM   3427  N  N      . THR A 1 493 ? 44.23400  -10.70400 44.76600  1.000 121.97000 ? 484 THR A N      1 
ATOM   3428  C  CA     . THR A 1 493 ? 43.14400  -9.77600  44.47800  1.000 117.95000 ? 484 THR A CA     1 
ATOM   3429  C  C      . THR A 1 493 ? 42.28400  -10.27200 43.32100  1.000 131.39000 ? 484 THR A C      1 
ATOM   3430  O  O      . THR A 1 493 ? 41.06000  -10.09400 43.33100  1.000 138.63000 ? 484 THR A O      1 
ATOM   3431  C  CB     . THR A 1 493 ? 43.69600  -8.38200  44.18200  1.000 112.06000 ? 484 THR A CB     1 
ATOM   3432  O  OG1    . THR A 1 493 ? 44.35600  -8.38200  42.91000  1.000 131.40000 ? 484 THR A OG1    1 
ATOM   3433  C  CG2    . THR A 1 493 ? 44.68400  -7.96700  45.26400  1.000 115.00000 ? 484 THR A CG2    1 
ATOM   3434  N  N      . ASP A 1 494 ? 42.90700  -10.89300 42.31400  1.000 139.26000 ? 485 ASP A N      1 
ATOM   3435  C  CA     . ASP A 1 494 ? 42.15200  -11.41000 41.17400  1.000 145.22000 ? 485 ASP A CA     1 
ATOM   3436  C  C      . ASP A 1 494 ? 41.18700  -12.50900 41.60200  1.000 156.21000 ? 485 ASP A C      1 
ATOM   3437  O  O      . ASP A 1 494 ? 40.07300  -12.60800 41.07400  1.000 176.87000 ? 485 ASP A O      1 
ATOM   3438  C  CB     . ASP A 1 494 ? 43.10800  -11.91600 40.09200  1.000 119.87000 ? 485 ASP A CB     1 
ATOM   3439  C  CG     . ASP A 1 494 ? 42.51600  -11.81800 38.69400  1.000 125.46000 ? 485 ASP A CG     1 
ATOM   3440  O  OD1    . ASP A 1 494 ? 41.42100  -11.23400 38.54300  1.000 133.18000 ? 485 ASP A OD1    1 
ATOM   3441  O  OD2    . ASP A 1 494 ? 43.15300  -12.32000 37.74500  1.000 130.77000 ? 485 ASP A OD2    1 
ATOM   3442  N  N      . HIS A 1 495 ? 41.60000  -13.35200 42.55100  1.000 140.33000 ? 486 HIS A N      1 
ATOM   3443  C  CA     . HIS A 1 495 ? 40.71000  -14.40000 43.03900  1.000 128.90000 ? 486 HIS A CA     1 
ATOM   3444  C  C      . HIS A 1 495 ? 39.47600  -13.80100 43.70000  1.000 140.98000 ? 486 HIS A C      1 
ATOM   3445  O  O      . HIS A 1 495 ? 38.37600  -14.35500 43.59700  1.000 157.06000 ? 486 HIS A O      1 
ATOM   3446  C  CB     . HIS A 1 495 ? 41.45900  -15.31600 44.01000  1.000 145.51000 ? 486 HIS A CB     1 
ATOM   3447  C  CG     . HIS A 1 495 ? 40.58000  -16.29100 44.73500  1.000 157.93000 ? 486 HIS A CG     1 
ATOM   3448  N  ND1    . HIS A 1 495 ? 40.11200  -17.45100 44.15400  1.000 164.72000 ? 486 HIS A ND1    1 
ATOM   3449  C  CD2    . HIS A 1 495 ? 40.09400  -16.28200 45.99800  1.000 149.63000 ? 486 HIS A CD2    1 
ATOM   3450  C  CE1    . HIS A 1 495 ? 39.37300  -18.11100 45.02700  1.000 152.59000 ? 486 HIS A CE1    1 
ATOM   3451  N  NE2    . HIS A 1 495 ? 39.34500  -17.42300 46.15400  1.000 141.46000 ? 486 HIS A NE2    1 
ATOM   3452  N  N      . LEU A 1 496 ? 39.63900  -12.66900 44.38500  1.000 131.80000 ? 487 LEU A N      1 
ATOM   3453  C  CA     . LEU A 1 496 ? 38.49600  -12.01100 45.01000  1.000 135.44000 ? 487 LEU A CA     1 
ATOM   3454  C  C      . LEU A 1 496 ? 37.48000  -11.54200 43.97100  1.000 139.26000 ? 487 LEU A C      1 
ATOM   3455  O  O      . LEU A 1 496 ? 36.26800  -11.59600 44.21100  1.000 155.09000 ? 487 LEU A O      1 
ATOM   3456  C  CB     . LEU A 1 496 ? 38.97800  -10.84000 45.86900  1.000 132.48000 ? 487 LEU A CB     1 
ATOM   3457  C  CG     . LEU A 1 496 ? 39.47700  -11.15600 47.28400  1.000 130.86000 ? 487 LEU A CG     1 
ATOM   3458  C  CD1    . LEU A 1 496 ? 39.96100  -9.89300  47.99100  1.000 113.61000 ? 487 LEU A CD1    1 
ATOM   3459  C  CD2    . LEU A 1 496 ? 38.39900  -11.84400 48.10200  1.000 122.33000 ? 487 LEU A CD2    1 
ATOM   3460  N  N      . ASP A 1 497 ? 37.95300  -11.06700 42.81500  1.000 137.31000 ? 488 ASP A N      1 
ATOM   3461  C  CA     . ASP A 1 497 ? 37.04600  -10.55000 41.79000  1.000 141.74000 ? 488 ASP A CA     1 
ATOM   3462  C  C      . ASP A 1 497 ? 36.14800  -11.64200 41.20800  1.000 149.41000 ? 488 ASP A C      1 
ATOM   3463  O  O      . ASP A 1 497 ? 34.96100  -11.40200 40.96000  1.000 162.36000 ? 488 ASP A O      1 
ATOM   3464  C  CB     . ASP A 1 497 ? 37.85000  -9.86400  40.68500  1.000 148.34000 ? 488 ASP A CB     1 
ATOM   3465  C  CG     . ASP A 1 497 ? 37.04600  -9.66100  39.41300  1.000 147.20000 ? 488 ASP A CG     1 
ATOM   3466  O  OD1    . ASP A 1 497 ? 35.90700  -9.15600  39.50300  1.000 130.81000 ? 488 ASP A OD1    1 
ATOM   3467  O  OD2    . ASP A 1 497 ? 37.55400  -10.00100 38.32400  1.000 158.33000 ? 488 ASP A OD2    1 
ATOM   3468  N  N      . ALA A 1 498 ? 36.69200  -12.84000 40.96700  1.000 142.88000 ? 489 ALA A N      1 
ATOM   3469  C  CA     . ALA A 1 498 ? 35.88500  -13.92200 40.40200  1.000 151.25000 ? 489 ALA A CA     1 
ATOM   3470  C  C      . ALA A 1 498 ? 34.78300  -14.35400 41.36400  1.000 167.51000 ? 489 ALA A C      1 
ATOM   3471  O  O      . ALA A 1 498 ? 33.63900  -14.60200 40.94900  1.000 171.59000 ? 489 ALA A O      1 
ATOM   3472  C  CB     . ALA A 1 498 ? 36.77400  -15.11100 40.03900  1.000 138.16000 ? 489 ALA A CB     1 
ATOM   3473  N  N      . VAL A 1 499 ? 35.11900  -14.47800 42.64900  1.000 168.40000 ? 490 VAL A N      1 
ATOM   3474  C  CA     . VAL A 1 499 ? 34.10400  -14.78500 43.64900  1.000 156.95000 ? 490 VAL A CA     1 
ATOM   3475  C  C      . VAL A 1 499 ? 33.01200  -13.72800 43.61500  1.000 153.63000 ? 490 VAL A C      1 
ATOM   3476  O  O      . VAL A 1 499 ? 31.81700  -14.03600 43.72200  1.000 160.76000 ? 490 VAL A O      1 
ATOM   3477  C  CB     . VAL A 1 499 ? 34.74700  -14.89000 45.04500  1.000 148.52000 ? 490 VAL A CB     1 
ATOM   3478  C  CG1    . VAL A 1 499 ? 33.67400  -14.97600 46.11400  1.000 158.31000 ? 490 VAL A CG1    1 
ATOM   3479  C  CG2    . VAL A 1 499 ? 35.68300  -16.09100 45.11800  1.000 152.25000 ? 490 VAL A CG2    1 
ATOM   3480  N  N      . GLY A 1 500 ? 33.41000  -12.46400 43.45100  1.000 152.11000 ? 491 GLY A N      1 
ATOM   3481  C  CA     . GLY A 1 500 ? 32.43600  -11.39400 43.34200  1.000 136.59000 ? 491 GLY A CA     1 
ATOM   3482  C  C      . GLY A 1 500 ? 31.54700  -11.53000 42.12300  1.000 157.38000 ? 491 GLY A C      1 
ATOM   3483  O  O      . GLY A 1 500 ? 30.34800  -11.26500 42.19100  1.000 172.85000 ? 491 GLY A O      1 
ATOM   3484  N  N      . ASN A 1 501 ? 32.11700  -11.94600 40.99000  1.000 154.33000 ? 492 ASN A N      1 
ATOM   3485  C  CA     . ASN A 1 501 ? 31.30200  -12.10800 39.78800  1.000 146.24000 ? 492 ASN A CA     1 
ATOM   3486  C  C      . ASN A 1 501 ? 30.26100  -13.20800 39.97800  1.000 142.93000 ? 492 ASN A C      1 
ATOM   3487  O  O      . ASN A 1 501 ? 29.07300  -13.01900 39.67800  1.000 146.96000 ? 492 ASN A O      1 
ATOM   3488  C  CB     . ASN A 1 501 ? 32.20000  -12.40100 38.58100  1.000 126.06000 ? 492 ASN A CB     1 
ATOM   3489  C  CG     . ASN A 1 501 ? 32.85200  -11.14500 38.01100  1.000 135.09000 ? 492 ASN A CG     1 
ATOM   3490  O  OD1    . ASN A 1 501 ? 32.67400  -10.04300 38.53100  1.000 138.18000 ? 492 ASN A OD1    1 
ATOM   3491  N  ND2    . ASN A 1 501 ? 33.63400  -11.31700 36.95200  1.000 128.92000 ? 492 ASN A ND2    1 
ATOM   3492  N  N      . THR A 1 502 ? 30.68000  -14.35500 40.51700  1.000 135.32000 ? 493 THR A N      1 
ATOM   3493  C  CA     . THR A 1 502 ? 29.72100  -15.43600 40.75100  1.000 131.64000 ? 493 THR A CA     1 
ATOM   3494  C  C      . THR A 1 502 ? 28.63400  -15.01100 41.73500  1.000 138.34000 ? 493 THR A C      1 
ATOM   3495  O  O      . THR A 1 502 ? 27.43400  -15.22800 41.49500  1.000 140.05000 ? 493 THR A O      1 
ATOM   3496  C  CB     . THR A 1 502 ? 30.44200  -16.69400 41.24000  1.000 128.71000 ? 493 THR A CB     1 
ATOM   3497  O  OG1    . THR A 1 502 ? 31.26000  -17.21500 40.18500  1.000 141.60000 ? 493 THR A OG1    1 
ATOM   3498  C  CG2    . THR A 1 502 ? 29.43500  -17.75900 41.65200  1.000 114.51000 ? 493 THR A CG2    1 
ATOM   3499  N  N      . THR A 1 503 ? 29.03400  -14.39300 42.85000  1.000 143.02000 ? 494 THR A N      1 
ATOM   3500  C  CA     . THR A 1 503 ? 28.05200  -13.94800 43.83200  1.000 129.72000 ? 494 THR A CA     1 
ATOM   3501  C  C      . THR A 1 503 ? 27.11600  -12.90000 43.24200  1.000 128.26000 ? 494 THR A C      1 
ATOM   3502  O  O      . THR A 1 503 ? 25.93200  -12.85200 43.58900  1.000 134.28000 ? 494 THR A O      1 
ATOM   3503  C  CB     . THR A 1 503 ? 28.76200  -13.41200 45.07200  1.000 125.62000 ? 494 THR A CB     1 
ATOM   3504  O  OG1    . THR A 1 503 ? 29.57000  -12.28800 44.70500  1.000 143.33000 ? 494 THR A OG1    1 
ATOM   3505  C  CG2    . THR A 1 503 ? 29.64900  -14.49400 45.67900  1.000 125.48000 ? 494 THR A CG2    1 
ATOM   3506  N  N      . ALA A 1 504 ? 27.62900  -12.03800 42.36200  1.000 129.74000 ? 495 ALA A N      1 
ATOM   3507  C  CA     . ALA A 1 504 ? 26.78500  -11.02600 41.73700  1.000 127.40000 ? 495 ALA A CA     1 
ATOM   3508  C  C      . ALA A 1 504 ? 25.76100  -11.66000 40.80700  1.000 122.23000 ? 495 ALA A C      1 
ATOM   3509  O  O      . ALA A 1 504 ? 24.61900  -11.19400 40.72400  1.000 127.91000 ? 495 ALA A O      1 
ATOM   3510  C  CB     . ALA A 1 504 ? 27.64600  -10.01100 40.98800  1.000 128.67000 ? 495 ALA A CB     1 
ATOM   3511  N  N      . ALA A 1 505 ? 26.15100  -12.70600 40.07900  1.000 114.20000 ? 496 ALA A N      1 
ATOM   3512  C  CA     . ALA A 1 505 ? 25.16400  -13.41600 39.27100  1.000 108.70000 ? 496 ALA A CA     1 
ATOM   3513  C  C      . ALA A 1 505 ? 24.06800  -13.99900 40.15700  1.000 102.08000 ? 496 ALA A C      1 
ATOM   3514  O  O      . ALA A 1 505 ? 22.86800  -13.86800 39.86400  1.000 88.51000  ? 496 ALA A O      1 
ATOM   3515  C  CB     . ALA A 1 505 ? 25.83700  -14.51300 38.44700  1.000 114.97000 ? 496 ALA A CB     1 
ATOM   3516  N  N      . ILE A 1 506 ? 24.46600  -14.63300 41.26500  1.000 105.87000 ? 497 ILE A N      1 
ATOM   3517  C  CA     . ILE A 1 506 ? 23.46700  -15.17400 42.18600  1.000 85.61000  ? 497 ILE A CA     1 
ATOM   3518  C  C      . ILE A 1 506 ? 22.55900  -14.06500 42.70500  1.000 87.19000  ? 497 ILE A C      1 
ATOM   3519  O  O      . ILE A 1 506 ? 21.34200  -14.24800 42.84500  1.000 98.76000  ? 497 ILE A O      1 
ATOM   3520  C  CB     . ILE A 1 506 ? 24.14400  -15.93600 43.33800  1.000 92.35000  ? 497 ILE A CB     1 
ATOM   3521  C  CG1    . ILE A 1 506 ? 25.15800  -16.94200 42.79200  1.000 100.51000 ? 497 ILE A CG1    1 
ATOM   3522  C  CG2    . ILE A 1 506 ? 23.09500  -16.62700 44.19800  1.000 95.45000  ? 497 ILE A CG2    1 
ATOM   3523  C  CD1    . ILE A 1 506 ? 25.98900  -17.60400 43.86300  1.000 101.50000 ? 497 ILE A CD1    1 
ATOM   3524  N  N      . GLY A 1 507 ? 23.13900  -12.90400 43.01300  1.000 90.08000  ? 498 GLY A N      1 
ATOM   3525  C  CA     . GLY A 1 507 ? 22.34800  -11.79200 43.51100  1.000 85.71000  ? 498 GLY A CA     1 
ATOM   3526  C  C      . GLY A 1 507 ? 21.36800  -11.26700 42.48200  1.000 87.57000  ? 498 GLY A C      1 
ATOM   3527  O  O      . GLY A 1 507 ? 20.24800  -10.88400 42.81900  1.000 90.92000  ? 498 GLY A O      1 
ATOM   3528  N  N      . LYS A 1 508 ? 21.78600  -11.21200 41.21600  1.000 98.86000  ? 499 LYS A N      1 
ATOM   3529  C  CA     . LYS A 1 508 ? 20.86400  -10.80700 40.15900  1.000 98.34000  ? 499 LYS A CA     1 
ATOM   3530  C  C      . LYS A 1 508 ? 19.69500  -11.77700 40.06800  1.000 83.76000  ? 499 LYS A C      1 
ATOM   3531  O  O      . LYS A 1 508 ? 18.53800  -11.36100 39.91100  1.000 72.32000  ? 499 LYS A O      1 
ATOM   3532  C  CB     . LYS A 1 508 ? 21.59200  -10.71600 38.81700  1.000 98.89000  ? 499 LYS A CB     1 
ATOM   3533  C  CG     . LYS A 1 508 ? 22.81100  -9.80100  38.81900  1.000 102.18000 ? 499 LYS A CG     1 
ATOM   3534  C  CD     . LYS A 1 508 ? 22.45800  -8.40200  39.29700  1.000 97.70000  ? 499 LYS A CD     1 
ATOM   3535  N  N      . GLY A 1 509 ? 19.97600  -13.07700 40.17200  1.000 78.35000  ? 500 GLY A N      1 
ATOM   3536  C  CA     . GLY A 1 509 ? 18.89000  -14.04600 40.16500  1.000 86.97000  ? 500 GLY A CA     1 
ATOM   3537  C  C      . GLY A 1 509 ? 17.93900  -13.84300 41.33000  1.000 85.53000  ? 500 GLY A C      1 
ATOM   3538  O  O      . GLY A 1 509 ? 16.71300  -13.82400 41.16200  1.000 91.05000  ? 500 GLY A O      1 
ATOM   3539  N  N      . PHE A 1 510 ? 18.50000  -13.67500 42.53200  1.000 72.87000  ? 501 PHE A N      1 
ATOM   3540  C  CA     . PHE A 1 510 ? 17.68500  -13.44700 43.72200  1.000 73.45000  ? 501 PHE A CA     1 
ATOM   3541  C  C      . PHE A 1 510 ? 16.84100  -12.19000 43.57700  1.000 69.69000  ? 501 PHE A C      1 
ATOM   3542  O  O      . PHE A 1 510 ? 15.66000  -12.18000 43.94300  1.000 76.92000  ? 501 PHE A O      1 
ATOM   3543  C  CB     . PHE A 1 510 ? 18.59300  -13.34500 44.95000  1.000 89.04000  ? 501 PHE A CB     1 
ATOM   3544  C  CG     . PHE A 1 510 ? 17.87000  -13.03100 46.23400  1.000 93.77000  ? 501 PHE A CG     1 
ATOM   3545  C  CD1    . PHE A 1 510 ? 17.25500  -14.03300 46.96700  1.000 102.91000 ? 501 PHE A CD1    1 
ATOM   3546  C  CD2    . PHE A 1 510 ? 17.82700  -11.73200 46.72100  1.000 95.89000  ? 501 PHE A CD2    1 
ATOM   3547  C  CE1    . PHE A 1 510 ? 16.60200  -13.74500 48.15500  1.000 117.37000 ? 501 PHE A CE1    1 
ATOM   3548  C  CE2    . PHE A 1 510 ? 17.17500  -11.43800 47.90700  1.000 94.72000  ? 501 PHE A CE2    1 
ATOM   3549  C  CZ     . PHE A 1 510 ? 16.56200  -12.44700 48.62400  1.000 113.28000 ? 501 PHE A CZ     1 
ATOM   3550  N  N      . ALA A 1 511 ? 17.42700  -11.12700 43.02600  1.000 69.77000  ? 502 ALA A N      1 
ATOM   3551  C  CA     . ALA A 1 511 ? 16.69900  -9.87800  42.85200  1.000 67.71000  ? 502 ALA A CA     1 
ATOM   3552  C  C      . ALA A 1 511 ? 15.56400  -10.03600 41.85400  1.000 70.94000  ? 502 ALA A C      1 
ATOM   3553  O  O      . ALA A 1 511 ? 14.45500  -9.55000  42.09200  1.000 73.62000  ? 502 ALA A O      1 
ATOM   3554  C  CB     . ALA A 1 511 ? 17.65600  -8.77100  42.41200  1.000 76.11000  ? 502 ALA A CB     1 
ATOM   3555  N  N      . ILE A 1 512 ? 15.81300  -10.72000 40.73500  1.000 64.02000  ? 503 ILE A N      1 
ATOM   3556  C  CA     . ILE A 1 512 ? 14.75800  -10.91300 39.74300  1.000 56.46000  ? 503 ILE A CA     1 
ATOM   3557  C  C      . ILE A 1 512 ? 13.61300  -11.72200 40.34000  1.000 45.71000  ? 503 ILE A C      1 
ATOM   3558  O  O      . ILE A 1 512 ? 12.43300  -11.37500 40.18700  1.000 46.13000  ? 503 ILE A O      1 
ATOM   3559  C  CB     . ILE A 1 512 ? 15.32300  -11.58500 38.48000  1.000 64.71000  ? 503 ILE A CB     1 
ATOM   3560  C  CG1    . ILE A 1 512 ? 16.32000  -10.65900 37.78100  1.000 71.76000  ? 503 ILE A CG1    1 
ATOM   3561  C  CG2    . ILE A 1 512 ? 14.19500  -11.96200 37.53300  1.000 59.32000  ? 503 ILE A CG2    1 
ATOM   3562  C  CD1    . ILE A 1 512 ? 16.95500  -11.26800 36.54800  1.000 46.28000  ? 503 ILE A CD1    1 
ATOM   3563  N  N      . GLY A 1 513 ? 13.94600  -12.80300 41.04700  1.000 43.57000  ? 504 GLY A N      1 
ATOM   3564  C  CA     . GLY A 1 513 ? 12.90200  -13.62400 41.64000  1.000 57.10000  ? 504 GLY A CA     1 
ATOM   3565  C  C      . GLY A 1 513 ? 12.08800  -12.87000 42.67500  1.000 57.68000  ? 504 GLY A C      1 
ATOM   3566  O  O      . GLY A 1 513 ? 10.85100  -12.88500 42.65000  1.000 55.01000  ? 504 GLY A O      1 
ATOM   3567  N  N      . SER A 1 514 ? 12.77400  -12.18800 43.59700  1.000 58.82000  ? 505 SER A N      1 
ATOM   3568  C  CA     . SER A 1 514 ? 12.06900  -11.40700 44.60400  1.000 73.38000  ? 505 SER A CA     1 
ATOM   3569  C  C      . SER A 1 514 ? 11.24800  -10.29500 43.97300  1.000 77.91000  ? 505 SER A C      1 
ATOM   3570  O  O      . SER A 1 514 ? 10.16900  -9.96800  44.47200  1.000 87.37000  ? 505 SER A O      1 
ATOM   3571  C  CB     . SER A 1 514 ? 13.05300  -10.82300 45.62000  1.000 72.33000  ? 505 SER A CB     1 
ATOM   3572  O  OG     . SER A 1 514 ? 13.71400  -11.83500 46.36000  1.000 81.00000  ? 505 SER A OG     1 
ATOM   3573  N  N      . ALA A 1 515 ? 11.73100  -9.70100  42.88100  1.000 56.27000  ? 506 ALA A N      1 
ATOM   3574  C  CA     . ALA A 1 515 ? 10.96500  -8.64700  42.23000  1.000 57.57000  ? 506 ALA A CA     1 
ATOM   3575  C  C      . ALA A 1 515 ? 9.69500   -9.20000  41.60400  1.000 61.49000  ? 506 ALA A C      1 
ATOM   3576  O  O      . ALA A 1 515 ? 8.63600   -8.57300  41.68300  1.000 65.57000  ? 506 ALA A O      1 
ATOM   3577  C  CB     . ALA A 1 515 ? 11.82000  -7.94300  41.17900  1.000 65.83000  ? 506 ALA A CB     1 
ATOM   3578  N  N      . ILE A 1 516 ? 9.77900   -10.37000 40.97500  1.000 52.92000  ? 507 ILE A N      1 
ATOM   3579  C  CA     . ILE A 1 516 ? 8.57000   -10.99400 40.44600  1.000 51.51000  ? 507 ILE A CA     1 
ATOM   3580  C  C      . ILE A 1 516 ? 7.58700   -11.28200 41.57400  1.000 53.66000  ? 507 ILE A C      1 
ATOM   3581  O  O      . ILE A 1 516 ? 6.38800   -10.98500 41.46900  1.000 55.39000  ? 507 ILE A O      1 
ATOM   3582  C  CB     . ILE A 1 516 ? 8.92800   -12.26800 39.66100  1.000 59.39000  ? 507 ILE A CB     1 
ATOM   3583  C  CG1    . ILE A 1 516 ? 9.84700   -11.92000 38.48800  1.000 46.70000  ? 507 ILE A CG1    1 
ATOM   3584  C  CG2    . ILE A 1 516 ? 7.67200   -12.97800 39.18100  1.000 48.97000  ? 507 ILE A CG2    1 
ATOM   3585  C  CD1    . ILE A 1 516 ? 10.58300  -13.10800 37.90600  1.000 37.76000  ? 507 ILE A CD1    1 
ATOM   3586  N  N      . PHE A 1 517 ? 8.08400   -11.83700 42.68200  1.000 43.47000  ? 508 PHE A N      1 
ATOM   3587  C  CA     . PHE A 1 517 ? 7.20800   -12.16600 43.80200  1.000 55.92000  ? 508 PHE A CA     1 
ATOM   3588  C  C      . PHE A 1 517 ? 6.55100   -10.91100 44.37100  1.000 58.15000  ? 508 PHE A C      1 
ATOM   3589  O  O      . PHE A 1 517 ? 5.33700   -10.88500 44.62700  1.000 56.45000  ? 508 PHE A O      1 
ATOM   3590  C  CB     . PHE A 1 517 ? 8.01500   -12.90100 44.87200  1.000 66.47000  ? 508 PHE A CB     1 
ATOM   3591  C  CG     . PHE A 1 517 ? 7.19900   -13.81200 45.73400  1.000 68.86000  ? 508 PHE A CG     1 
ATOM   3592  C  CD1    . PHE A 1 517 ? 6.16600   -14.55600 45.19400  1.000 73.25000  ? 508 PHE A CD1    1 
ATOM   3593  C  CD2    . PHE A 1 517 ? 7.49200   -13.95900 47.07700  1.000 76.28000  ? 508 PHE A CD2    1 
ATOM   3594  C  CE1    . PHE A 1 517 ? 5.42200   -15.40500 45.98600  1.000 93.52000  ? 508 PHE A CE1    1 
ATOM   3595  C  CE2    . PHE A 1 517 ? 6.75300   -14.80900 47.87100  1.000 66.55000  ? 508 PHE A CE2    1 
ATOM   3596  C  CZ     . PHE A 1 517 ? 5.71700   -15.53200 47.32600  1.000 78.09000  ? 508 PHE A CZ     1 
ATOM   3597  N  N      . ALA A 1 518 ? 7.33700   -9.85000  44.54600  1.000 41.17000  ? 509 ALA A N      1 
ATOM   3598  C  CA     . ALA A 1 518 ? 6.81000   -8.60300  45.08000  1.000 40.37000  ? 509 ALA A CA     1 
ATOM   3599  C  C      . ALA A 1 518 ? 5.81500   -7.96900  44.11800  1.000 41.55000  ? 509 ALA A C      1 
ATOM   3600  O  O      . ALA A 1 518 ? 4.79300   -7.42700  44.54700  1.000 40.71000  ? 509 ALA A O      1 
ATOM   3601  C  CB     . ALA A 1 518 ? 7.95700   -7.64300  45.38500  1.000 37.12000  ? 509 ALA A CB     1 
ATOM   3602  N  N      . ALA A 1 519 ? 6.08900   -8.02700  42.81400  1.000 41.87000  ? 510 ALA A N      1 
ATOM   3603  C  CA     . ALA A 1 519 ? 5.15500   -7.47500  41.84200  1.000 35.90000  ? 510 ALA A CA     1 
ATOM   3604  C  C      . ALA A 1 519 ? 3.84000   -8.24000  41.86000  1.000 34.09000  ? 510 ALA A C      1 
ATOM   3605  O  O      . ALA A 1 519 ? 2.76800   -7.65500  41.67200  1.000 43.50000  ? 510 ALA A O      1 
ATOM   3606  C  CB     . ALA A 1 519 ? 5.77500   -7.48900  40.44600  1.000 47.55000  ? 510 ALA A CB     1 
ATOM   3607  N  N      . LEU A 1 520 ? 3.90100   -9.55500  42.07900  1.000 25.42000  ? 511 LEU A N      1 
ATOM   3608  C  CA     . LEU A 1 520 ? 2.66700   -10.32000 42.21300  1.000 26.78000  ? 511 LEU A CA     1 
ATOM   3609  C  C      . LEU A 1 520 ? 1.89100   -9.88500  43.45000  1.000 41.97000  ? 511 LEU A C      1 
ATOM   3610  O  O      . LEU A 1 520 ? 0.66400   -9.69100  43.40000  1.000 46.96000  ? 511 LEU A O      1 
ATOM   3611  C  CB     . LEU A 1 520 ? 2.98300   -11.81300 42.27100  1.000 33.24000  ? 511 LEU A CB     1 
ATOM   3612  C  CG     . LEU A 1 520 ? 3.56400   -12.38100 40.97600  1.000 45.24000  ? 511 LEU A CG     1 
ATOM   3613  C  CD1    . LEU A 1 520 ? 4.06700   -13.80200 41.18900  1.000 34.63000  ? 511 LEU A CD1    1 
ATOM   3614  C  CD2    . LEU A 1 520 ? 2.54200   -12.32000 39.84900  1.000 42.36000  ? 511 LEU A CD2    1 
ATOM   3615  N  N      . SER A 1 521 ? 2.59500   -9.70400  44.57000  1.000 47.29000  ? 512 SER A N      1 
ATOM   3616  C  CA     . SER A 1 521 ? 1.93300   -9.20100  45.76900  1.000 43.28000  ? 512 SER A CA     1 
ATOM   3617  C  C      . SER A 1 521 ? 1.31000   -7.83300  45.50700  1.000 53.68000  ? 512 SER A C      1 
ATOM   3618  O  O      . SER A 1 521 ? 0.21200   -7.53200  45.99300  1.000 62.99000  ? 512 SER A O      1 
ATOM   3619  C  CB     . SER A 1 521 ? 2.92700   -9.13600  46.92800  1.000 40.07000  ? 512 SER A CB     1 
ATOM   3620  O  OG     . SER A 1 521 ? 3.54500   -10.39500 47.14100  1.000 58.93000  ? 512 SER A OG     1 
ATOM   3621  N  N      . LEU A 1 522 ? 1.98500   -7.00500  44.70700  1.000 46.43000  ? 513 LEU A N      1 
ATOM   3622  C  CA     . LEU A 1 522 ? 1.48100   -5.67100  44.39300  1.000 41.66000  ? 513 LEU A CA     1 
ATOM   3623  C  C      . LEU A 1 522 ? 0.26500   -5.72100  43.47600  1.000 57.44000  ? 513 LEU A C      1 
ATOM   3624  O  O      . LEU A 1 522 ? -0.60500  -4.85100  43.55800  1.000 54.50000  ? 513 LEU A O      1 
ATOM   3625  C  CB     . LEU A 1 522 ? 2.58900   -4.83200  43.76100  1.000 37.95000  ? 513 LEU A CB     1 
ATOM   3626  C  CG     . LEU A 1 522 ? 3.64900   -4.30700  44.73100  1.000 48.54000  ? 513 LEU A CG     1 
ATOM   3627  C  CD1    . LEU A 1 522 ? 4.89500   -3.87000  43.97700  1.000 49.21000  ? 513 LEU A CD1    1 
ATOM   3628  C  CD2    . LEU A 1 522 ? 3.10200   -3.16400  45.57200  1.000 47.02000  ? 513 LEU A CD2    1 
ATOM   3629  N  N      . PHE A 1 523 ? 0.19500   -6.70800  42.58400  1.000 44.49000  ? 514 PHE A N      1 
ATOM   3630  C  CA     . PHE A 1 523 ? -1.02100  -6.89400  41.79700  1.000 41.08000  ? 514 PHE A CA     1 
ATOM   3631  C  C      . PHE A 1 523 ? -2.18900  -7.29700  42.69000  1.000 52.87000  ? 514 PHE A C      1 
ATOM   3632  O  O      . PHE A 1 523 ? -3.32200  -6.82200  42.51100  1.000 56.69000  ? 514 PHE A O      1 
ATOM   3633  C  CB     . PHE A 1 523 ? -0.78700  -7.93800  40.70700  1.000 31.84000  ? 514 PHE A CB     1 
ATOM   3634  C  CG     . PHE A 1 523 ? -2.04400  -8.39700  40.03000  1.000 36.73000  ? 514 PHE A CG     1 
ATOM   3635  C  CD1    . PHE A 1 523 ? -2.73900  -7.54700  39.18700  1.000 43.33000  ? 514 PHE A CD1    1 
ATOM   3636  C  CD2    . PHE A 1 523 ? -2.53300  -9.67600  40.23800  1.000 36.40000  ? 514 PHE A CD2    1 
ATOM   3637  C  CE1    . PHE A 1 523 ? -3.89500  -7.96300  38.56200  1.000 41.47000  ? 514 PHE A CE1    1 
ATOM   3638  C  CE2    . PHE A 1 523 ? -3.68900  -10.09600 39.61700  1.000 56.18000  ? 514 PHE A CE2    1 
ATOM   3639  C  CZ     . PHE A 1 523 ? -4.37200  -9.23800  38.77800  1.000 48.23000  ? 514 PHE A CZ     1 
ATOM   3640  N  N      . ALA A 1 524 ? -1.93200  -8.18000  43.65800  1.000 47.83000  ? 515 ALA A N      1 
ATOM   3641  C  CA     . ALA A 1 524 ? -2.98100  -8.52300  44.61300  1.000 43.54000  ? 515 ALA A CA     1 
ATOM   3642  C  C      . ALA A 1 524 ? -3.44400  -7.28400  45.36900  1.000 65.04000  ? 515 ALA A C      1 
ATOM   3643  O  O      . ALA A 1 524 ? -4.64900  -7.07400  45.57700  1.000 69.56000  ? 515 ALA A O      1 
ATOM   3644  C  CB     . ALA A 1 524 ? -2.48000  -9.59100  45.58100  1.000 35.17000  ? 515 ALA A CB     1 
ATOM   3645  N  N      . SER A 1 525 ? -2.49200  -6.44300  45.77400  1.000 65.29000  ? 516 SER A N      1 
ATOM   3646  C  CA     . SER A 1 525 ? -2.83200  -5.18800  46.43100  1.000 62.55000  ? 516 SER A CA     1 
ATOM   3647  C  C      . SER A 1 525 ? -3.60800  -4.26700  45.49900  1.000 60.53000  ? 516 SER A C      1 
ATOM   3648  O  O      . SER A 1 525 ? -4.47300  -3.51800  45.95200  1.000 70.90000  ? 516 SER A O      1 
ATOM   3649  C  CB     . SER A 1 525 ? -1.56300  -4.50200  46.93000  1.000 64.12000  ? 516 SER A CB     1 
ATOM   3650  O  OG     . SER A 1 525 ? -0.89900  -5.29700  47.89900  1.000 65.42000  ? 516 SER A OG     1 
ATOM   3651  N  N      . TYR A 1 526 ? -3.29500  -4.28900  44.20400  1.000 47.94000  ? 517 TYR A N      1 
ATOM   3652  C  CA     . TYR A 1 526 ? -4.05700  -3.51200  43.23100  1.000 58.68000  ? 517 TYR A CA     1 
ATOM   3653  C  C      . TYR A 1 526 ? -5.52000  -3.94100  43.21900  1.000 58.79000  ? 517 TYR A C      1 
ATOM   3654  O  O      . TYR A 1 526 ? -6.43200  -3.10500  43.28500  1.000 66.23000  ? 517 TYR A O      1 
ATOM   3655  C  CB     . TYR A 1 526 ? -3.43500  -3.67600  41.84400  1.000 42.85000  ? 517 TYR A CB     1 
ATOM   3656  C  CG     . TYR A 1 526 ? -4.30300  -3.19600  40.70100  1.000 44.52000  ? 517 TYR A CG     1 
ATOM   3657  C  CD1    . TYR A 1 526 ? -4.30300  -1.86300  40.31100  1.000 49.05000  ? 517 TYR A CD1    1 
ATOM   3658  C  CD2    . TYR A 1 526 ? -5.10200  -4.08300  39.99300  1.000 49.17000  ? 517 TYR A CD2    1 
ATOM   3659  C  CE1    . TYR A 1 526 ? -5.08700  -1.42400  39.26100  1.000 60.87000  ? 517 TYR A CE1    1 
ATOM   3660  C  CE2    . TYR A 1 526 ? -5.89200  -3.65400  38.94300  1.000 60.37000  ? 517 TYR A CE2    1 
ATOM   3661  C  CZ     . TYR A 1 526 ? -5.88000  -2.32300  38.57900  1.000 62.40000  ? 517 TYR A CZ     1 
ATOM   3662  O  OH     . TYR A 1 526 ? -6.66100  -1.88200  37.53400  1.000 76.95000  ? 517 TYR A OH     1 
ATOM   3663  N  N      . MET A 1 527 ? -5.76000  -5.25100  43.14800  1.000 55.30000  ? 518 MET A N      1 
ATOM   3664  C  CA     . MET A 1 527 ? -7.13600  -5.74400  43.17700  1.000 54.81000  ? 518 MET A CA     1 
ATOM   3665  C  C      . MET A 1 527 ? -7.83700  -5.37700  44.47900  1.000 53.92000  ? 518 MET A C      1 
ATOM   3666  O  O      . MET A 1 527 ? -9.02600  -5.03400  44.47300  1.000 53.73000  ? 518 MET A O      1 
ATOM   3667  C  CB     . MET A 1 527 ? -7.17300  -7.25400  42.94700  1.000 65.86000  ? 518 MET A CB     1 
ATOM   3668  C  CG     . MET A 1 527 ? -6.57000  -7.68400  41.62700  1.000 62.45000  ? 518 MET A CG     1 
ATOM   3669  S  SD     . MET A 1 527 ? -7.43000  -6.87200  40.26000  1.000 61.64000  ? 518 MET A SD     1 
ATOM   3670  C  CE     . MET A 1 527 ? -9.13700  -7.28400  40.61600  1.000 77.83000  ? 518 MET A CE     1 
ATOM   3671  N  N      . PHE A 1 528 ? -7.12100  -5.42700  45.60500  1.000 54.88000  ? 519 PHE A N      1 
ATOM   3672  C  CA     . PHE A 1 528 ? -7.74600  -5.01800  46.86200  1.000 60.16000  ? 519 PHE A CA     1 
ATOM   3673  C  C      . PHE A 1 528 ? -8.00000  -3.51400  46.90700  1.000 70.15000  ? 519 PHE A C      1 
ATOM   3674  O  O      . PHE A 1 528 ? -8.98800  -3.07200  47.50400  1.000 70.97000  ? 519 PHE A O      1 
ATOM   3675  C  CB     . PHE A 1 528 ? -6.89700  -5.46800  48.04900  1.000 57.77000  ? 519 PHE A CB     1 
ATOM   3676  C  CG     . PHE A 1 528 ? -7.09600  -6.90800  48.41500  1.000 61.95000  ? 519 PHE A CG     1 
ATOM   3677  C  CD1    . PHE A 1 528 ? -6.77400  -7.91500  47.52400  1.000 60.42000  ? 519 PHE A CD1    1 
ATOM   3678  C  CD2    . PHE A 1 528 ? -7.61700  -7.25200  49.65000  1.000 73.76000  ? 519 PHE A CD2    1 
ATOM   3679  C  CE1    . PHE A 1 528 ? -6.96500  -9.23800  47.85900  1.000 61.84000  ? 519 PHE A CE1    1 
ATOM   3680  C  CE2    . PHE A 1 528 ? -7.80900  -8.57200  49.99200  1.000 69.81000  ? 519 PHE A CE2    1 
ATOM   3681  C  CZ     . PHE A 1 528 ? -7.48200  -9.56800  49.09400  1.000 63.00000  ? 519 PHE A CZ     1 
ATOM   3682  N  N      . SER A 1 529 ? -7.12400  -2.71600  46.29300  1.000 65.80000  ? 520 SER A N      1 
ATOM   3683  C  CA     . SER A 1 529 ? -7.34500  -1.28000  46.19000  1.000 66.74000  ? 520 SER A CA     1 
ATOM   3684  C  C      . SER A 1 529 ? -8.51000  -0.96600  45.27100  1.000 67.48000  ? 520 SER A C      1 
ATOM   3685  O  O      . SER A 1 529 ? -9.07400  0.13000   45.35300  1.000 80.30000  ? 520 SER A O      1 
ATOM   3686  C  CB     . SER A 1 529 ? -6.08500  -0.57400  45.68300  1.000 76.98000  ? 520 SER A CB     1 
ATOM   3687  O  OG     . SER A 1 529 ? -4.97400  -0.81800  46.52700  1.000 92.37000  ? 520 SER A OG     1 
ATOM   3688  N  N      . GLN A 1 530 ? -8.88400  -1.90800  44.40500  1.000 71.60000  ? 521 GLN A N      1 
ATOM   3689  C  CA     . GLN A 1 530 ? -10.01700 -1.69600  43.51400  1.000 74.11000  ? 521 GLN A CA     1 
ATOM   3690  C  C      . GLN A 1 530 ? -11.34400 -1.70200  44.25800  1.000 82.23000  ? 521 GLN A C      1 
ATOM   3691  O  O      . GLN A 1 530 ? -12.39300 -1.53600  43.62400  1.000 76.97000  ? 521 GLN A O      1 
ATOM   3692  C  CB     . GLN A 1 530 ? -10.01800 -2.77000  42.42100  1.000 67.22000  ? 521 GLN A CB     1 
ATOM   3693  C  CG     . GLN A 1 530 ? -10.73300 -2.36700  41.13600  1.000 95.17000  ? 521 GLN A CG     1 
ATOM   3694  C  CD     . GLN A 1 530 ? -10.36400 -3.25800  39.96100  1.000 78.68000  ? 521 GLN A CD     1 
ATOM   3695  O  OE1    . GLN A 1 530 ? -9.21200  -3.66500  39.81700  1.000 74.47000  ? 521 GLN A OE1    1 
ATOM   3696  N  NE2    . GLN A 1 530 ? -11.34600 -3.57300  39.12200  1.000 87.09000  ? 521 GLN A NE2    1 
ATOM   3697  N  N      . ILE A 1 531 ? -11.32000 -1.88500  45.58100  1.000 88.32000  ? 522 ILE A N      1 
ATOM   3698  C  CA     . ILE A 1 531 ? -12.53700 -1.82700  46.37800  1.000 88.55000  ? 522 ILE A CA     1 
ATOM   3699  C  C      . ILE A 1 531 ? -13.11800 -0.42000  46.33600  1.000 91.54000  ? 522 ILE A C      1 
ATOM   3700  O  O      . ILE A 1 531 ? -12.38700 0.57900   46.33200  1.000 91.88000  ? 522 ILE A O      1 
ATOM   3701  C  CB     . ILE A 1 531 ? -12.25600 -2.27300  47.82300  1.000 81.72000  ? 522 ILE A CB     1 
ATOM   3702  C  CG1    . ILE A 1 531 ? -12.46600 -3.78400  47.96100  1.000 74.85000  ? 522 ILE A CG1    1 
ATOM   3703  C  CG2    . ILE A 1 531 ? -13.13300 -1.50600  48.79800  1.000 76.37000  ? 522 ILE A CG2    1 
ATOM   3704  C  CD1    . ILE A 1 531 ? -11.37700 -4.63100  47.33300  1.000 82.97000  ? 522 ILE A CD1    1 
ATOM   3705  N  N      . SER A 1 532 ? -14.43800 -0.33700  46.30900  1.000 99.25000  ? 523 SER A N      1 
ATOM   3706  C  CA     . SER A 1 532 ? -15.17300 0.91600   46.29900  1.000 101.62000 ? 523 SER A CA     1 
ATOM   3707  C  C      . SER A 1 532 ? -16.23500 0.86700   47.38200  1.000 113.34000 ? 523 SER A C      1 
ATOM   3708  O  O      . SER A 1 532 ? -16.63800 -0.21900  47.81500  1.000 123.75000 ? 523 SER A O      1 
ATOM   3709  C  CB     . SER A 1 532 ? -15.82200 1.17100   44.93000  1.000 108.36000 ? 523 SER A CB     1 
ATOM   3710  O  OG     . SER A 1 532 ? -17.08000 0.52800   44.83000  1.000 112.35000 ? 523 SER A OG     1 
ATOM   3711  N  N      . PRO A 1 533 ? -16.70200 2.02200   47.85900  1.000 113.84000 ? 524 PRO A N      1 
ATOM   3712  C  CA     . PRO A 1 533 ? -17.74000 1.98000   48.89600  1.000 115.08000 ? 524 PRO A CA     1 
ATOM   3713  C  C      . PRO A 1 533 ? -18.98500 1.25400   48.43500  1.000 127.54000 ? 524 PRO A C      1 
ATOM   3714  O  O      . PRO A 1 533 ? -19.55400 0.47500   49.20900  1.000 128.59000 ? 524 PRO A O      1 
ATOM   3715  C  CB     . PRO A 1 533 ? -18.01600 3.46300   49.17200  1.000 104.90000 ? 524 PRO A CB     1 
ATOM   3716  C  CG     . PRO A 1 533 ? -16.73400 4.13800   48.81400  1.000 109.20000 ? 524 PRO A CG     1 
ATOM   3717  C  CD     . PRO A 1 533 ? -16.23000 3.39500   47.61000  1.000 118.20000 ? 524 PRO A CD     1 
ATOM   3718  N  N      . SER A 1 534 ? -19.35800 1.38800   47.16200  1.000 123.87000 ? 525 SER A N      1 
ATOM   3719  C  CA     . SER A 1 534 ? -20.52200 0.66300   46.67500  1.000 121.70000 ? 525 SER A CA     1 
ATOM   3720  C  C      . SER A 1 534 ? -20.23700 -0.82200  46.59400  1.000 114.58000 ? 525 SER A C      1 
ATOM   3721  O  O      . SER A 1 534 ? -21.13900 -1.63700  46.81000  1.000 99.35000  ? 525 SER A O      1 
ATOM   3722  C  CB     . SER A 1 534 ? -20.94700 1.19800   45.31200  1.000 122.26000 ? 525 SER A CB     1 
ATOM   3723  O  OG     . SER A 1 534 ? -19.87600 1.13000   44.38600  1.000 124.07000 ? 525 SER A OG     1 
ATOM   3724  N  N      . ASP A 1 535 ? -18.99400 -1.18900  46.29100  1.000 129.29000 ? 526 ASP A N      1 
ATOM   3725  C  CA     . ASP A 1 535 ? -18.63100 -2.59300  46.31700  1.000 124.29000 ? 526 ASP A CA     1 
ATOM   3726  C  C      . ASP A 1 535 ? -18.54100 -3.13100  47.73100  1.000 134.08000 ? 526 ASP A C      1 
ATOM   3727  O  O      . ASP A 1 535 ? -18.27100 -4.32400  47.89300  1.000 141.91000 ? 526 ASP A O      1 
ATOM   3728  C  CB     . ASP A 1 535 ? -17.29300 -2.81200  45.60700  1.000 116.97000 ? 526 ASP A CB     1 
ATOM   3729  C  CG     . ASP A 1 535 ? -17.36600 -2.54200  44.12000  1.000 111.26000 ? 526 ASP A CG     1 
ATOM   3730  O  OD1    . ASP A 1 535 ? -18.48800 -2.38100  43.59100  1.000 125.55000 ? 526 ASP A OD1    1 
ATOM   3731  O  OD2    . ASP A 1 535 ? -16.29300 -2.47300  43.48400  1.000 93.63000  ? 526 ASP A OD2    1 
ATOM   3732  N  N      . ILE A 1 536 ? -18.75300 -2.29400  48.75200  1.000 140.11000 ? 527 ILE A N      1 
ATOM   3733  C  CA     . ILE A 1 536 ? -18.67900 -2.77900  50.12700  1.000 156.39000 ? 527 ILE A CA     1 
ATOM   3734  C  C      . ILE A 1 536 ? -19.80300 -3.77200  50.39900  1.000 156.25000 ? 527 ILE A C      1 
ATOM   3735  O  O      . ILE A 1 536 ? -19.60400 -4.78700  51.07600  1.000 150.49000 ? 527 ILE A O      1 
ATOM   3736  C  CB     . ILE A 1 536 ? -18.69800 -1.60400  51.12300  1.000 149.17000 ? 527 ILE A CB     1 
ATOM   3737  C  CG1    . ILE A 1 536 ? -17.47500 -0.70100  50.91900  1.000 134.95000 ? 527 ILE A CG1    1 
ATOM   3738  C  CG2    . ILE A 1 536 ? -18.74900 -2.12600  52.55500  1.000 141.25000 ? 527 ILE A CG2    1 
ATOM   3739  C  CD1    . ILE A 1 536 ? -16.13800 -1.40800  51.09300  1.000 139.91000 ? 527 ILE A CD1    1 
ATOM   3740  N  N      . GLY A 1 537 ? -21.00400 -3.49100  49.88600  1.000 147.81000 ? 528 GLY A N      1 
ATOM   3741  C  CA     . GLY A 1 537 ? -22.11900 -4.41200  50.02400  1.000 154.74000 ? 528 GLY A CA     1 
ATOM   3742  C  C      . GLY A 1 537 ? -21.97900 -5.67800  49.20500  1.000 153.95000 ? 528 GLY A C      1 
ATOM   3743  O  O      . GLY A 1 537 ? -22.61600 -6.68700  49.52800  1.000 166.53000 ? 528 GLY A O      1 
ATOM   3744  N  N      . LYS A 1 538 ? -21.15500 -5.65400  48.16000  1.000 144.44000 ? 529 LYS A N      1 
ATOM   3745  C  CA     . LYS A 1 538 ? -21.01500 -6.80800  47.29100  1.000 141.03000 ? 529 LYS A CA     1 
ATOM   3746  C  C      . LYS A 1 538 ? -20.26100 -7.92600  48.00700  1.000 131.99000 ? 529 LYS A C      1 
ATOM   3747  O  O      . LYS A 1 538 ? -19.54500 -7.68400  48.98300  1.000 136.12000 ? 529 LYS A O      1 
ATOM   3748  C  CB     . LYS A 1 538 ? -20.29600 -6.42400  46.00000  1.000 131.40000 ? 529 LYS A CB     1 
ATOM   3749  N  N      . PRO A 1 539 ? -20.43300 -9.16600  47.56000  1.000 115.08000 ? 530 PRO A N      1 
ATOM   3750  C  CA     . PRO A 1 539 ? -19.77900 -10.29800 48.22900  1.000 113.99000 ? 530 PRO A CA     1 
ATOM   3751  C  C      . PRO A 1 539 ? -18.27100 -10.24000 48.06300  1.000 123.73000 ? 530 PRO A C      1 
ATOM   3752  O  O      . PRO A 1 539 ? -17.76000 -9.57100  47.15200  1.000 126.43000 ? 530 PRO A O      1 
ATOM   3753  C  CB     . PRO A 1 539 ? -20.37800 -11.52100 47.51400  1.000 107.92000 ? 530 PRO A CB     1 
ATOM   3754  C  CG     . PRO A 1 539 ? -21.62800 -11.00500 46.84800  1.000 130.86000 ? 530 PRO A CG     1 
ATOM   3755  C  CD     . PRO A 1 539 ? -21.29700 -9.60500  46.45400  1.000 113.17000 ? 530 PRO A CD     1 
ATOM   3756  N  N      . PRO A 1 540 ? -17.51900 -10.93400 48.92300  1.000 124.41000 ? 531 PRO A N      1 
ATOM   3757  C  CA     . PRO A 1 540 ? -16.05300 -10.88400 48.79400  1.000 101.09000 ? 531 PRO A CA     1 
ATOM   3758  C  C      . PRO A 1 540 ? -15.54800 -11.43400 47.47600  1.000 91.14000  ? 531 PRO A C      1 
ATOM   3759  O  O      . PRO A 1 540 ? -14.59900 -10.88500 46.90200  1.000 100.23000 ? 531 PRO A O      1 
ATOM   3760  C  CB     . PRO A 1 540 ? -15.57500 -11.73200 49.98300  1.000 92.65000  ? 531 PRO A CB     1 
ATOM   3761  C  CG     . PRO A 1 540 ? -16.68300 -11.63100 50.97800  1.000 102.91000 ? 531 PRO A CG     1 
ATOM   3762  C  CD     . PRO A 1 540 ? -17.94400 -11.60900 50.16100  1.000 128.23000 ? 531 PRO A CD     1 
ATOM   3763  N  N      . SER A 1 541 ? -16.17600 -12.49400 46.96400  1.000 92.05000  ? 532 SER A N      1 
ATOM   3764  C  CA     . SER A 1 541 ? -15.70200 -13.10100 45.72700  1.000 106.23000 ? 532 SER A CA     1 
ATOM   3765  C  C      . SER A 1 541 ? -15.91400 -12.17800 44.53200  1.000 102.91000 ? 532 SER A C      1 
ATOM   3766  O  O      . SER A 1 541 ? -15.10900 -12.18000 43.59400  1.000 102.02000 ? 532 SER A O      1 
ATOM   3767  C  CB     . SER A 1 541 ? -16.39400 -14.44900 45.50900  1.000 112.21000 ? 532 SER A CB     1 
ATOM   3768  O  OG     . SER A 1 541 ? -17.79800 -14.34200 45.68000  1.000 120.40000 ? 532 SER A OG     1 
ATOM   3769  N  N      . LEU A 1 542 ? -16.97500 -11.37400 44.55300  1.000 103.49000 ? 533 LEU A N      1 
ATOM   3770  C  CA     . LEU A 1 542 ? -17.27300 -10.50700 43.41900  1.000 103.79000 ? 533 LEU A CA     1 
ATOM   3771  C  C      . LEU A 1 542 ? -16.34900 -9.29600  43.36400  1.000 96.94000  ? 533 LEU A C      1 
ATOM   3772  O  O      . LEU A 1 542 ? -15.99300 -8.84200  42.27100  1.000 104.53000 ? 533 LEU A O      1 
ATOM   3773  C  CB     . LEU A 1 542 ? -18.73400 -10.06100 43.47200  1.000 111.45000 ? 533 LEU A CB     1 
ATOM   3774  C  CG     . LEU A 1 542 ? -19.75200 -11.05400 42.90600  1.000 120.70000 ? 533 LEU A CG     1 
ATOM   3775  C  CD1    . LEU A 1 542 ? -19.88900 -12.27200 43.81400  1.000 129.24000 ? 533 LEU A CD1    1 
ATOM   3776  C  CD2    . LEU A 1 542 ? -21.09200 -10.37500 42.71500  1.000 126.79000 ? 533 LEU A CD2    1 
ATOM   3777  N  N      . VAL A 1 543 ? -15.95200 -8.76100  44.51700  1.000 88.85000  ? 534 VAL A N      1 
ATOM   3778  C  CA     . VAL A 1 543 ? -15.13900 -7.54900  44.53000  1.000 93.57000  ? 534 VAL A CA     1 
ATOM   3779  C  C      . VAL A 1 543 ? -13.71700 -7.85200  44.06700  1.000 97.76000  ? 534 VAL A C      1 
ATOM   3780  O  O      . VAL A 1 543 ? -13.13500 -7.11200  43.26400  1.000 97.05000  ? 534 VAL A O      1 
ATOM   3781  C  CB     . VAL A 1 543 ? -15.15500 -6.91600  45.93200  1.000 100.35000 ? 534 VAL A CB     1 
ATOM   3782  C  CG1    . VAL A 1 543 ? -14.02000 -5.91600  46.07100  1.000 101.28000 ? 534 VAL A CG1    1 
ATOM   3783  C  CG2    . VAL A 1 543 ? -16.50000 -6.25700  46.20200  1.000 105.72000 ? 534 VAL A CG2    1 
ATOM   3784  N  N      . LEU A 1 544 ? -13.12800 -8.93100  44.58700  1.000 90.40000  ? 535 LEU A N      1 
ATOM   3785  C  CA     . LEU A 1 544 ? -11.75800 -9.32800  44.25100  1.000 86.04000  ? 535 LEU A CA     1 
ATOM   3786  C  C      . LEU A 1 544 ? -11.79300 -10.25300 43.03500  1.000 75.93000  ? 535 LEU A C      1 
ATOM   3787  O  O      . LEU A 1 544 ? -11.65000 -11.47300 43.13300  1.000 64.34000  ? 535 LEU A O      1 
ATOM   3788  C  CB     . LEU A 1 544 ? -11.09600 -10.00000 45.44800  1.000 84.08000  ? 535 LEU A CB     1 
ATOM   3789  C  CG     . LEU A 1 544 ? -11.27600 -9.29800  46.79600  1.000 68.45000  ? 535 LEU A CG     1 
ATOM   3790  C  CD1    . LEU A 1 544 ? -10.82100 -10.19800 47.93500  1.000 60.52000  ? 535 LEU A CD1    1 
ATOM   3791  C  CD2    . LEU A 1 544 ? -10.52400 -7.97400  46.82200  1.000 67.27000  ? 535 LEU A CD2    1 
ATOM   3792  N  N      . LEU A 1 545 ? -11.96500 -9.65100  41.85900  1.000 68.51000  ? 536 LEU A N      1 
ATOM   3793  C  CA     . LEU A 1 545 ? -12.12900 -10.43100 40.63800  1.000 66.22000  ? 536 LEU A CA     1 
ATOM   3794  C  C      . LEU A 1 545 ? -11.52800 -9.70500  39.44500  1.000 72.24000  ? 536 LEU A C      1 
ATOM   3795  O  O      . LEU A 1 545 ? -11.80600 -8.52000  39.23200  1.000 80.26000  ? 536 LEU A O      1 
ATOM   3796  C  CB     . LEU A 1 545 ? -13.60800 -10.72600 40.36200  1.000 73.73000  ? 536 LEU A CB     1 
ATOM   3797  C  CG     . LEU A 1 545 ? -13.86000 -11.63500 39.15800  1.000 65.93000  ? 536 LEU A CG     1 
ATOM   3798  C  CD1    . LEU A 1 545 ? -13.74800 -13.09600 39.56400  1.000 84.92000  ? 536 LEU A CD1    1 
ATOM   3799  C  CD2    . LEU A 1 545 ? -15.21800 -11.34800 38.52400  1.000 67.38000  ? 536 LEU A CD2    1 
ATOM   3800  N  N      . LEU A 1 546 ? -10.71800 -10.43000 38.66700  1.000 72.31000  ? 537 LEU A N      1 
ATOM   3801  C  CA     . LEU A 1 546 ? -10.19800 -9.97100  37.37600  1.000 56.74000  ? 537 LEU A CA     1 
ATOM   3802  C  C      . LEU A 1 546 ? -10.38600 -11.09900 36.35900  1.000 67.62000  ? 537 LEU A C      1 
ATOM   3803  O  O      . LEU A 1 546 ? -9.47100  -11.89200 36.11800  1.000 71.73000  ? 537 LEU A O      1 
ATOM   3804  C  CB     . LEU A 1 546 ? -8.73400  -9.55400  37.47800  1.000 42.04000  ? 537 LEU A CB     1 
ATOM   3805  C  CG     . LEU A 1 546 ? -8.16300  -8.82600  36.25800  1.000 51.77000  ? 537 LEU A CG     1 
ATOM   3806  C  CD1    . LEU A 1 546 ? -8.64900  -7.37600  36.22300  1.000 79.08000  ? 537 LEU A CD1    1 
ATOM   3807  C  CD2    . LEU A 1 546 ? -6.64600  -8.89800  36.23300  1.000 66.88000  ? 537 LEU A CD2    1 
ATOM   3808  N  N      . ASN A 1 547 ? -11.57100 -11.16800 35.75500  1.000 69.40000  ? 538 ASN A N      1 
ATOM   3809  C  CA     . ASN A 1 547 ? -11.85400 -12.23100 34.79900  1.000 54.15000  ? 538 ASN A CA     1 
ATOM   3810  C  C      . ASN A 1 547 ? -10.93100 -12.13200 33.59300  1.000 55.52000  ? 538 ASN A C      1 
ATOM   3811  O  O      . ASN A 1 547 ? -10.74000 -11.05100 33.02800  1.000 70.22000  ? 538 ASN A O      1 
ATOM   3812  C  CB     . ASN A 1 547 ? -13.31200 -12.16600 34.34900  1.000 67.41000  ? 538 ASN A CB     1 
ATOM   3813  C  CG     . ASN A 1 547 ? -13.74100 -13.41000 33.59500  1.000 67.59000  ? 538 ASN A CG     1 
ATOM   3814  O  OD1    . ASN A 1 547 ? -12.96900 -14.35700 33.44800  1.000 75.15000  ? 538 ASN A OD1    1 
ATOM   3815  N  ND2    . ASN A 1 547 ? -14.97800 -13.41500 33.11500  1.000 70.57000  ? 538 ASN A ND2    1 
ATOM   3816  N  N      . MET A 1 548 ? -10.36300 -13.27000 33.19300  1.000 38.96000  ? 539 MET A N      1 
ATOM   3817  C  CA     . MET A 1 548 ? -9.46800  -13.31400 32.04600  1.000 40.05000  ? 539 MET A CA     1 
ATOM   3818  C  C      . MET A 1 548 ? -10.21100 -13.50400 30.73400  1.000 40.56000  ? 539 MET A C      1 
ATOM   3819  O  O      . MET A 1 548 ? -9.59200  -13.41300 29.66800  1.000 40.88000  ? 539 MET A O      1 
ATOM   3820  C  CB     . MET A 1 548 ? -8.43400  -14.43200 32.21500  1.000 51.10000  ? 539 MET A CB     1 
ATOM   3821  C  CG     . MET A 1 548 ? -7.15900  -14.20800 31.41600  1.000 49.96000  ? 539 MET A CG     1 
ATOM   3822  S  SD     . MET A 1 548 ? -6.16900  -12.87100 32.11000  1.000 54.05000  ? 539 MET A SD     1 
ATOM   3823  C  CE     . MET A 1 548 ? -4.86100  -12.70800 30.89200  1.000 76.89000  ? 539 MET A CE     1 
ATOM   3824  N  N      . LEU A 1 549 ? -11.51400 -13.75900 30.78900  1.000 45.18000  ? 540 LEU A N      1 
ATOM   3825  C  CA     . LEU A 1 549 ? -12.33700 -13.88400 29.59800  1.000 44.53000  ? 540 LEU A CA     1 
ATOM   3826  C  C      . LEU A 1 549 ? -12.85000 -12.53800 29.10200  1.000 51.99000  ? 540 LEU A C      1 
ATOM   3827  O  O      . LEU A 1 549 ? -13.43600 -12.47800 28.01600  1.000 58.33000  ? 540 LEU A O      1 
ATOM   3828  C  CB     . LEU A 1 549 ? -13.51500 -14.82900 29.87700  1.000 43.98000  ? 540 LEU A CB     1 
ATOM   3829  C  CG     . LEU A 1 549 ? -14.15300 -15.59900 28.71500  1.000 41.48000  ? 540 LEU A CG     1 
ATOM   3830  C  CD1    . LEU A 1 549 ? -13.09100 -16.30600 27.88600  1.000 38.91000  ? 540 LEU A CD1    1 
ATOM   3831  C  CD2    . LEU A 1 549 ? -15.16900 -16.60400 29.24400  1.000 57.92000  ? 540 LEU A CD2    1 
ATOM   3832  N  N      . ASP A 1 550 ? -12.64700 -11.46600 29.86800  1.000 60.03000  ? 541 ASP A N      1 
ATOM   3833  C  CA     . ASP A 1 550 ? -13.01900 -10.13100 29.41700  1.000 49.67000  ? 541 ASP A CA     1 
ATOM   3834  C  C      . ASP A 1 550 ? -12.03800 -9.65600  28.35400  1.000 48.98000  ? 541 ASP A C      1 
ATOM   3835  O  O      . ASP A 1 550 ? -10.82200 -9.66500  28.56800  1.000 48.93000  ? 541 ASP A O      1 
ATOM   3836  C  CB     . ASP A 1 550 ? -13.03300 -9.15400  30.59500  1.000 38.34000  ? 541 ASP A CB     1 
ATOM   3837  C  CG     . ASP A 1 550 ? -13.78700 -7.87300  30.28500  1.000 39.01000  ? 541 ASP A CG     1 
ATOM   3838  O  OD1    . ASP A 1 550 ? -14.79400 -7.93400  29.54800  1.000 57.46000  ? 541 ASP A OD1    1 
ATOM   3839  O  OD2    . ASP A 1 550 ? -13.37000 -6.80300  30.77300  1.000 54.46000  ? 541 ASP A OD2    1 
ATOM   3840  N  N      . ALA A 1 551 ? -12.57000 -9.24100  27.20200  1.000 58.60000  ? 542 ALA A N      1 
ATOM   3841  C  CA     . ALA A 1 551 ? -11.70400 -8.85300  26.09200  1.000 71.58000  ? 542 ALA A CA     1 
ATOM   3842  C  C      . ALA A 1 551 ? -10.79300 -7.69700  26.48400  1.000 67.23000  ? 542 ALA A C      1 
ATOM   3843  O  O      . ALA A 1 551 ? -9.64000  -7.62400  26.03800  1.000 60.50000  ? 542 ALA A O      1 
ATOM   3844  C  CB     . ALA A 1 551 ? -12.54700 -8.48900  24.87000  1.000 79.35000  ? 542 ALA A CB     1 
ATOM   3845  N  N      . ARG A 1 552 ? -11.29400 -6.77700  27.31100  1.000 44.67000  ? 543 ARG A N      1 
ATOM   3846  C  CA     . ARG A 1 552 ? -10.45400 -5.68300  27.78000  1.000 33.32000  ? 543 ARG A CA     1 
ATOM   3847  C  C      . ARG A 1 552 ? -9.22100  -6.22200  28.48800  1.000 57.01000  ? 543 ARG A C      1 
ATOM   3848  O  O      . ARG A 1 552 ? -8.10000  -5.75200  28.25600  1.000 56.37000  ? 543 ARG A O      1 
ATOM   3849  C  CB     . ARG A 1 552 ? -11.25200 -4.77900  28.71800  1.000 35.90000  ? 543 ARG A CB     1 
ATOM   3850  C  CG     . ARG A 1 552 ? -12.37500 -4.02200  28.04400  1.000 47.45000  ? 543 ARG A CG     1 
ATOM   3851  C  CD     . ARG A 1 552 ? -13.14800 -3.18500  29.05400  1.000 59.59000  ? 543 ARG A CD     1 
ATOM   3852  N  NE     . ARG A 1 552 ? -13.99500 -2.17700  28.42300  1.000 86.25000  ? 543 ARG A NE     1 
ATOM   3853  C  CZ     . ARG A 1 552 ? -13.62500 -0.92900  28.16700  1.000 81.57000  ? 543 ARG A CZ     1 
ATOM   3854  N  NH1    . ARG A 1 552 ? -12.41400 -0.49000  28.46800  1.000 83.89000  ? 543 ARG A NH1    1 
ATOM   3855  N  NH2    . ARG A 1 552 ? -14.49800 -0.09500  27.60600  1.000 87.56000  ? 543 ARG A NH2    1 
ATOM   3856  N  N      . VAL A 1 553 ? -9.41100  -7.23400  29.33500  1.000 54.29000  ? 544 VAL A N      1 
ATOM   3857  C  CA     . VAL A 1 553 ? -8.30700  -7.80000  30.09900  1.000 46.74000  ? 544 VAL A CA     1 
ATOM   3858  C  C      . VAL A 1 553 ? -7.30200  -8.48000  29.17700  1.000 58.87000  ? 544 VAL A C      1 
ATOM   3859  O  O      . VAL A 1 553 ? -6.08400  -8.32000  29.33300  1.000 60.82000  ? 544 VAL A O      1 
ATOM   3860  C  CB     . VAL A 1 553 ? -8.86200  -8.77200  31.15500  1.000 35.16000  ? 544 VAL A CB     1 
ATOM   3861  C  CG1    . VAL A 1 553 ? -7.73200  -9.38100  31.97400  1.000 47.84000  ? 544 VAL A CG1    1 
ATOM   3862  C  CG2    . VAL A 1 553 ? -9.87300  -8.05400  32.04100  1.000 42.14000  ? 544 VAL A CG2    1 
ATOM   3863  N  N      . ILE A 1 554 ? -7.79100  -9.24000  28.19700  1.000 60.89000  ? 545 ILE A N      1 
ATOM   3864  C  CA     . ILE A 1 554 ? -6.89500  -9.95100  27.29200  1.000 54.31000  ? 545 ILE A CA     1 
ATOM   3865  C  C      . ILE A 1 554 ? -6.08700  -8.95900  26.46200  1.000 59.74000  ? 545 ILE A C      1 
ATOM   3866  O  O      . ILE A 1 554 ? -4.86500  -9.09800  26.30100  1.000 64.03000  ? 545 ILE A O      1 
ATOM   3867  C  CB     . ILE A 1 554 ? -7.70000  -10.91800 26.40700  1.000 37.69000  ? 545 ILE A CB     1 
ATOM   3868  C  CG1    . ILE A 1 554 ? -8.42600  -11.94900 27.27600  1.000 44.86000  ? 545 ILE A CG1    1 
ATOM   3869  C  CG2    . ILE A 1 554 ? -6.78100  -11.62000 25.42900  1.000 41.67000  ? 545 ILE A CG2    1 
ATOM   3870  C  CD1    . ILE A 1 554 ? -9.27100  -12.94900 26.49300  1.000 38.80000  ? 545 ILE A CD1    1 
ATOM   3871  N  N      . ALA A 1 555 ? -6.75900  -7.94100  25.92300  1.000 50.69000  ? 546 ALA A N      1 
ATOM   3872  C  CA     . ALA A 1 555 ? -6.04800  -6.92600  25.15800  1.000 45.51000  ? 546 ALA A CA     1 
ATOM   3873  C  C      . ALA A 1 555 ? -5.02500  -6.21400  26.03000  1.000 44.50000  ? 546 ALA A C      1 
ATOM   3874  O  O      . ALA A 1 555 ? -3.91700  -5.90800  25.57500  1.000 58.50000  ? 546 ALA A O      1 
ATOM   3875  C  CB     . ALA A 1 555 ? -7.03600  -5.92700  24.55700  1.000 60.36000  ? 546 ALA A CB     1 
ATOM   3876  N  N      . GLY A 1 556 ? -5.37200  -5.96000  27.29400  1.000 44.57000  ? 547 GLY A N      1 
ATOM   3877  C  CA     . GLY A 1 556 ? -4.42200  -5.33200  28.19500  1.000 57.78000  ? 547 GLY A CA     1 
ATOM   3878  C  C      . GLY A 1 556 ? -3.20000  -6.19300  28.43900  1.000 45.66000  ? 547 GLY A C      1 
ATOM   3879  O  O      . GLY A 1 556 ? -2.07900  -5.69000  28.51400  1.000 47.30000  ? 547 GLY A O      1 
ATOM   3880  N  N      . ALA A 1 557 ? -3.39800  -7.50500  28.56200  1.000 41.31000  ? 548 ALA A N      1 
ATOM   3881  C  CA     . ALA A 1 557 ? -2.25900  -8.40100  28.72700  1.000 48.35000  ? 548 ALA A CA     1 
ATOM   3882  C  C      . ALA A 1 557 ? -1.36000  -8.36500  27.49600  1.000 49.14000  ? 548 ALA A C      1 
ATOM   3883  O  O      . ALA A 1 557 ? -0.12800  -8.26800  27.60800  1.000 58.15000  ? 548 ALA A O      1 
ATOM   3884  C  CB     . ALA A 1 557 ? -2.74400  -9.82400  29.00500  1.000 39.88000  ? 548 ALA A CB     1 
ATOM   3885  N  N      . LEU A 1 558 ? -1.96200  -8.43700  26.30600  1.000 43.03000  ? 549 LEU A N      1 
ATOM   3886  C  CA     . LEU A 1 558 ? -1.15600  -8.37600  25.09000  1.000 42.93000  ? 549 LEU A CA     1 
ATOM   3887  C  C      . LEU A 1 558 ? -0.38100  -7.06700  25.01700  1.000 48.23000  ? 549 LEU A C      1 
ATOM   3888  O  O      . LEU A 1 558 ? 0.81600   -7.05700  24.69700  1.000 59.25000  ? 549 LEU A O      1 
ATOM   3889  C  CB     . LEU A 1 558 ? -2.03600  -8.55400  23.85500  1.000 36.79000  ? 549 LEU A CB     1 
ATOM   3890  C  CG     . LEU A 1 558 ? -2.64000  -9.94700  23.69800  1.000 27.02000  ? 549 LEU A CG     1 
ATOM   3891  C  CD1    . LEU A 1 558 ? -3.73100  -9.93200  22.65000  1.000 36.39000  ? 549 LEU A CD1    1 
ATOM   3892  C  CD2    . LEU A 1 558 ? -1.55400  -10.94100 23.32700  1.000 26.86000  ? 549 LEU A CD2    1 
ATOM   3893  N  N      . LEU A 1 559 ? -1.04600  -5.95600  25.33500  1.000 45.50000  ? 550 LEU A N      1 
ATOM   3894  C  CA     . LEU A 1 559 ? -0.39200  -4.65600  25.29200  1.000 62.84000  ? 550 LEU A CA     1 
ATOM   3895  C  C      . LEU A 1 559 ? 0.75000   -4.57800  26.29500  1.000 72.83000  ? 550 LEU A C      1 
ATOM   3896  O  O      . LEU A 1 559 ? 1.81400   -4.02700  25.99100  1.000 83.59000  ? 550 LEU A O      1 
ATOM   3897  C  CB     . LEU A 1 559 ? -1.41500  -3.55300  25.55300  1.000 50.28000  ? 550 LEU A CB     1 
ATOM   3898  C  CG     . LEU A 1 559 ? -0.89600  -2.12000  25.49900  1.000 46.60000  ? 550 LEU A CG     1 
ATOM   3899  C  CD1    . LEU A 1 559 ? -0.61900  -1.72000  24.05300  1.000 53.81000  ? 550 LEU A CD1    1 
ATOM   3900  C  CD2    . LEU A 1 559 ? -1.89700  -1.17900  26.14200  1.000 53.28000  ? 550 LEU A CD2    1 
ATOM   3901  N  N      . GLY A 1 560 ? 0.54800   -5.11100  27.50200  1.000 55.89000  ? 551 GLY A N      1 
ATOM   3902  C  CA     . GLY A 1 560 ? 1.60700   -5.07800  28.49500  1.000 40.39000  ? 551 GLY A CA     1 
ATOM   3903  C  C      . GLY A 1 560 ? 2.81600   -5.88800  28.07300  1.000 45.36000  ? 551 GLY A C      1 
ATOM   3904  O  O      . GLY A 1 560 ? 3.96000   -5.45700  28.24700  1.000 54.71000  ? 551 GLY A O      1 
ATOM   3905  N  N      . ALA A 1 561 ? 2.58300   -7.07100  27.50300  1.000 41.59000  ? 552 ALA A N      1 
ATOM   3906  C  CA     . ALA A 1 561 ? 3.71100   -7.86300  27.02600  1.000 51.54000  ? 552 ALA A CA     1 
ATOM   3907  C  C      . ALA A 1 561 ? 4.45400   -7.13100  25.91600  1.000 56.39000  ? 552 ALA A C      1 
ATOM   3908  O  O      . ALA A 1 561 ? 5.69600   -7.07700  25.90900  1.000 57.20000  ? 552 ALA A O      1 
ATOM   3909  C  CB     . ALA A 1 561 ? 3.23300   -9.23300  26.54900  1.000 45.81000  ? 552 ALA A CB     1 
ATOM   3910  N  N      . ALA A 1 562 ? 3.70900   -6.54400  24.97600  1.000 49.68000  ? 553 ALA A N      1 
ATOM   3911  C  CA     . ALA A 1 562 ? 4.35400   -5.79000  23.91000  1.000 52.90000  ? 553 ALA A CA     1 
ATOM   3912  C  C      . ALA A 1 562 ? 5.17500   -4.64100  24.47900  1.000 64.70000  ? 553 ALA A C      1 
ATOM   3913  O  O      . ALA A 1 562 ? 6.29000   -4.37200  24.01300  1.000 65.68000  ? 553 ALA A O      1 
ATOM   3914  C  CB     . ALA A 1 562 ? 3.30600   -5.27200  22.92600  1.000 37.96000  ? 553 ALA A CB     1 
ATOM   3915  N  N      . ILE A 1 563 ? 4.64900   -3.96400  25.50200  1.000 66.30000  ? 554 ILE A N      1 
ATOM   3916  C  CA     . ILE A 1 563 ? 5.37100   -2.84900  26.10400  1.000 55.94000  ? 554 ILE A CA     1 
ATOM   3917  C  C      . ILE A 1 563 ? 6.64500   -3.33400  26.77300  1.000 51.07000  ? 554 ILE A C      1 
ATOM   3918  O  O      . ILE A 1 563 ? 7.67800   -2.66100  26.72800  1.000 48.76000  ? 554 ILE A O      1 
ATOM   3919  C  CB     . ILE A 1 563 ? 4.46800   -2.10100  27.09500  1.000 38.65000  ? 554 ILE A CB     1 
ATOM   3920  C  CG1    . ILE A 1 563 ? 3.26400   -1.53300  26.35200  1.000 44.01000  ? 554 ILE A CG1    1 
ATOM   3921  C  CG2    . ILE A 1 563 ? 5.26200   -1.01300  27.80800  1.000 29.37000  ? 554 ILE A CG2    1 
ATOM   3922  C  CD1    . ILE A 1 563 ? 2.18300   -1.02700  27.25500  1.000 67.99000  ? 554 ILE A CD1    1 
ATOM   3923  N  N      . THR A 1 564 ? 6.59400   -4.49900  27.41500  1.000 53.74000  ? 555 THR A N      1 
ATOM   3924  C  CA     . THR A 1 564 ? 7.80200   -5.02800  28.03900  1.000 57.86000  ? 555 THR A CA     1 
ATOM   3925  C  C      . THR A 1 564 ? 8.88100   -5.29800  26.99600  1.000 63.37000  ? 555 THR A C      1 
ATOM   3926  O  O      . THR A 1 564 ? 10.04700  -4.90400  27.16300  1.000 55.91000  ? 555 THR A O      1 
ATOM   3927  C  CB     . THR A 1 564 ? 7.47800   -6.30200  28.81800  1.000 54.71000  ? 555 THR A CB     1 
ATOM   3928  O  OG1    . THR A 1 564 ? 6.61200   -5.98800  29.91600  1.000 57.86000  ? 555 THR A OG1    1 
ATOM   3929  C  CG2    . THR A 1 564 ? 8.75400   -6.93400  29.34600  1.000 55.31000  ? 555 THR A CG2    1 
ATOM   3930  N  N      . TYR A 1 565 ? 8.50300   -5.95500  25.89700  1.000 55.87000  ? 556 TYR A N      1 
ATOM   3931  C  CA     . TYR A 1 565 ? 9.48800   -6.23100  24.85400  1.000 47.29000  ? 556 TYR A CA     1 
ATOM   3932  C  C      . TYR A 1 565 ? 10.05000  -4.94100  24.26800  1.000 57.27000  ? 556 TYR A C      1 
ATOM   3933  O  O      . TYR A 1 565 ? 11.26600  -4.82100  24.04800  1.000 53.95000  ? 556 TYR A O      1 
ATOM   3934  C  CB     . TYR A 1 565 ? 8.86800   -7.09700  23.76200  1.000 44.94000  ? 556 TYR A CB     1 
ATOM   3935  C  CG     . TYR A 1 565 ? 8.89600   -8.57100  24.08500  1.000 55.32000  ? 556 TYR A CG     1 
ATOM   3936  C  CD1    . TYR A 1 565 ? 8.10400   -9.09600  25.09700  1.000 57.17000  ? 556 TYR A CD1    1 
ATOM   3937  C  CD2    . TYR A 1 565 ? 9.70400   -9.44400  23.36600  1.000 63.41000  ? 556 TYR A CD2    1 
ATOM   3938  C  CE1    . TYR A 1 565 ? 8.12600   -10.44400 25.39200  1.000 46.64000  ? 556 TYR A CE1    1 
ATOM   3939  C  CE2    . TYR A 1 565 ? 9.73000   -10.79400 23.65400  1.000 40.98000  ? 556 TYR A CE2    1 
ATOM   3940  C  CZ     . TYR A 1 565 ? 8.93900   -11.28700 24.66600  1.000 35.49000  ? 556 TYR A CZ     1 
ATOM   3941  O  OH     . TYR A 1 565 ? 8.96000   -12.63000 24.95500  1.000 55.32000  ? 556 TYR A OH     1 
ATOM   3942  N  N      . TYR A 1 566 ? 9.18000   -3.95700  24.02500  1.000 55.30000  ? 557 TYR A N      1 
ATOM   3943  C  CA     . TYR A 1 566 ? 9.63000   -2.68600  23.46900  1.000 52.80000  ? 557 TYR A CA     1 
ATOM   3944  C  C      . TYR A 1 566 ? 10.57700  -1.98000  24.42900  1.000 61.33000  ? 557 TYR A C      1 
ATOM   3945  O  O      . TYR A 1 566 ? 11.56200  -1.36400  24.00900  1.000 80.44000  ? 557 TYR A O      1 
ATOM   3946  C  CB     . TYR A 1 566 ? 8.42300   -1.80600  23.14600  1.000 34.70000  ? 557 TYR A CB     1 
ATOM   3947  C  CG     . TYR A 1 566 ? 8.71900   -0.65000  22.21900  1.000 55.30000  ? 557 TYR A CG     1 
ATOM   3948  C  CD1    . TYR A 1 566 ? 8.64700   -0.80500  20.83900  1.000 63.58000  ? 557 TYR A CD1    1 
ATOM   3949  C  CD2    . TYR A 1 566 ? 9.05600   0.60000   22.72100  1.000 81.43000  ? 557 TYR A CD2    1 
ATOM   3950  C  CE1    . TYR A 1 566 ? 8.91200   0.25300   19.98500  1.000 90.48000  ? 557 TYR A CE1    1 
ATOM   3951  C  CE2    . TYR A 1 566 ? 9.32300   1.66400   21.87500  1.000 93.11000  ? 557 TYR A CE2    1 
ATOM   3952  C  CZ     . TYR A 1 566 ? 9.24900   1.48500   20.50900  1.000 106.45000 ? 557 TYR A CZ     1 
ATOM   3953  O  OH     . TYR A 1 566 ? 9.51400   2.54100   19.66500  1.000 110.41000 ? 557 TYR A OH     1 
ATOM   3954  N  N      . PHE A 1 567 ? 10.27600  -2.04800  25.72400  1.000 46.95000  ? 558 PHE A N      1 
ATOM   3955  C  CA     . PHE A 1 567 ? 11.13500  -1.46100  26.74300  1.000 34.22000  ? 558 PHE A CA     1 
ATOM   3956  C  C      . PHE A 1 567 ? 12.52700  -2.07100  26.68000  1.000 46.05000  ? 558 PHE A C      1 
ATOM   3957  O  O      . PHE A 1 567 ? 13.54100  -1.35900  26.71200  1.000 51.23000  ? 558 PHE A O      1 
ATOM   3958  C  CB     . PHE A 1 567 ? 10.48800  -1.69300  28.10600  1.000 28.75000  ? 558 PHE A CB     1 
ATOM   3959  C  CG     . PHE A 1 567 ? 11.26600  -1.16100  29.25900  1.000 19.70000  ? 558 PHE A CG     1 
ATOM   3960  C  CD1    . PHE A 1 567 ? 11.06100  0.13200   29.70500  1.000 28.96000  ? 558 PHE A CD1    1 
ATOM   3961  C  CD2    . PHE A 1 567 ? 12.14600  -1.97100  29.94600  1.000 28.31000  ? 558 PHE A CD2    1 
ATOM   3962  C  CE1    . PHE A 1 567 ? 11.75100  0.62000   30.78400  1.000 53.14000  ? 558 PHE A CE1    1 
ATOM   3963  C  CE2    . PHE A 1 567 ? 12.84200  -1.49100  31.02600  1.000 42.07000  ? 558 PHE A CE2    1 
ATOM   3964  C  CZ     . PHE A 1 567 ? 12.64600  -0.19200  31.44800  1.000 68.68000  ? 558 PHE A CZ     1 
ATOM   3965  N  N      . SER A 1 568 ? 12.59200  -3.40100  26.59600  1.000 50.63000  ? 559 SER A N      1 
ATOM   3966  C  CA     . SER A 1 568 ? 13.89100  -4.06500  26.53100  1.000 59.90000  ? 559 SER A CA     1 
ATOM   3967  C  C      . SER A 1 568 ? 14.65900  -3.65100  25.27800  1.000 67.07000  ? 559 SER A C      1 
ATOM   3968  O  O      . SER A 1 568 ? 15.86600  -3.35800  25.33900  1.000 66.98000  ? 559 SER A O      1 
ATOM   3969  C  CB     . SER A 1 568 ? 13.69900  -5.57900  26.57700  1.000 45.64000  ? 559 SER A CB     1 
ATOM   3970  O  OG     . SER A 1 568 ? 12.92400  -5.94400  27.70500  1.000 32.01000  ? 559 SER A OG     1 
ATOM   3971  N  N      . GLY A 1 569 ? 13.96800  -3.58800  24.13500  1.000 50.26000  ? 560 GLY A N      1 
ATOM   3972  C  CA     . GLY A 1 569 ? 14.64400  -3.19000  22.90900  1.000 53.28000  ? 560 GLY A CA     1 
ATOM   3973  C  C      . GLY A 1 569 ? 15.15600  -1.76300  22.97100  1.000 54.14000  ? 560 GLY A C      1 
ATOM   3974  O  O      . GLY A 1 569 ? 16.26900  -1.46500  22.51700  1.000 63.41000  ? 560 GLY A O      1 
ATOM   3975  N  N      . TYR A 1 570 ? 14.36300  -0.86400  23.55700  1.000 56.57000  ? 561 TYR A N      1 
ATOM   3976  C  CA     . TYR A 1 570 ? 14.80900  0.51600   23.69800  1.000 80.66000  ? 561 TYR A CA     1 
ATOM   3977  C  C      . TYR A 1 570 ? 16.01900  0.59900   24.61100  1.000 82.12000  ? 561 TYR A C      1 
ATOM   3978  O  O      . TYR A 1 570 ? 16.92000  1.41100   24.38200  1.000 86.46000  ? 561 TYR A O      1 
ATOM   3979  C  CB     . TYR A 1 570 ? 13.67800  1.39800   24.23200  1.000 82.53000  ? 561 TYR A CB     1 
ATOM   3980  C  CG     . TYR A 1 570 ? 14.04700  2.86600   24.32600  1.000 75.17000  ? 561 TYR A CG     1 
ATOM   3981  C  CD1    . TYR A 1 570 ? 14.66100  3.37800   25.46300  1.000 80.34000  ? 561 TYR A CD1    1 
ATOM   3982  C  CD2    . TYR A 1 570 ? 13.78200  3.73800   23.27800  1.000 94.16000  ? 561 TYR A CD2    1 
ATOM   3983  C  CE1    . TYR A 1 570 ? 15.00300  4.71600   25.55000  1.000 103.46000 ? 561 TYR A CE1    1 
ATOM   3984  C  CE2    . TYR A 1 570 ? 14.11900  5.08000   23.35700  1.000 112.78000 ? 561 TYR A CE2    1 
ATOM   3985  C  CZ     . TYR A 1 570 ? 14.72800  5.56400   24.49500  1.000 110.38000 ? 561 TYR A CZ     1 
ATOM   3986  O  OH     . TYR A 1 570 ? 15.06400  6.89900   24.57600  1.000 111.34000 ? 561 TYR A OH     1 
ATOM   3987  N  N      . LEU A 1 571 ? 16.04700  -0.21500  25.66600  1.000 66.86000  ? 562 LEU A N      1 
ATOM   3988  C  CA     . LEU A 1 571 ? 17.20700  -0.20000  26.55000  1.000 60.04000  ? 562 LEU A CA     1 
ATOM   3989  C  C      . LEU A 1 571 ? 18.46100  -0.63600  25.80400  1.000 78.28000  ? 562 LEU A C      1 
ATOM   3990  O  O      . LEU A 1 571 ? 19.54500  -0.05700  25.98400  1.000 77.25000  ? 562 LEU A O      1 
ATOM   3991  C  CB     . LEU A 1 571 ? 16.94700  -1.09800  27.75400  1.000 43.86000  ? 562 LEU A CB     1 
ATOM   3992  C  CG     . LEU A 1 571 ? 15.83600  -0.59200  28.67100  1.000 45.87000  ? 562 LEU A CG     1 
ATOM   3993  C  CD1    . LEU A 1 571 ? 15.82400  -1.41200  29.93900  1.000 54.28000  ? 562 LEU A CD1    1 
ATOM   3994  C  CD2    . LEU A 1 571 ? 16.02900  0.88800   28.98300  1.000 60.21000  ? 562 LEU A CD2    1 
ATOM   3995  N  N      . ILE A 1 572 ? 18.32500  -1.64300  24.94100  1.000 69.37000  ? 563 ILE A N      1 
ATOM   3996  C  CA     . ILE A 1 572 ? 19.46900  -2.07600  24.14200  1.000 61.57000  ? 563 ILE A CA     1 
ATOM   3997  C  C      . ILE A 1 572 ? 19.96100  -0.92900  23.26300  1.000 70.50000  ? 563 ILE A C      1 
ATOM   3998  O  O      . ILE A 1 572 ? 21.15400  -0.57800  23.25800  1.000 87.59000  ? 563 ILE A O      1 
ATOM   3999  C  CB     . ILE A 1 572 ? 19.09900  -3.31400  23.30700  1.000 52.80000  ? 563 ILE A CB     1 
ATOM   4000  C  CG1    . ILE A 1 572 ? 18.58800  -4.42900  24.22400  1.000 59.30000  ? 563 ILE A CG1    1 
ATOM   4001  C  CG2    . ILE A 1 572 ? 20.30100  -3.77900  22.48700  1.000 73.39000  ? 563 ILE A CG2    1 
ATOM   4002  C  CD1    . ILE A 1 572 ? 18.16800  -5.67700  23.49300  1.000 63.76000  ? 563 ILE A CD1    1 
ATOM   4003  N  N      . SER A 1 573 ? 19.03800  -0.31500  22.52000  1.000 66.61000  ? 564 SER A N      1 
ATOM   4004  C  CA     . SER A 1 573 ? 19.43800  0.76000   21.61900  1.000 67.30000  ? 564 SER A CA     1 
ATOM   4005  C  C      . SER A 1 573 ? 20.03000  1.94200   22.37600  1.000 85.47000  ? 564 SER A C      1 
ATOM   4006  O  O      . SER A 1 573 ? 20.95000  2.59700   21.87700  1.000 106.80000 ? 564 SER A O      1 
ATOM   4007  C  CB     . SER A 1 573 ? 18.25200  1.20800   20.77000  1.000 85.93000  ? 564 SER A CB     1 
ATOM   4008  O  OG     . SER A 1 573 ? 18.68500  2.01700   19.69400  1.000 107.43000 ? 564 SER A OG     1 
ATOM   4009  N  N      . ALA A 1 574 ? 19.52700  2.22400   23.57900  1.000 75.46000  ? 565 ALA A N      1 
ATOM   4010  C  CA     . ALA A 1 574 ? 20.05500  3.32900   24.37200  1.000 78.14000  ? 565 ALA A CA     1 
ATOM   4011  C  C      . ALA A 1 574 ? 21.47700  3.05100   24.83200  1.000 84.34000  ? 565 ALA A C      1 
ATOM   4012  O  O      . ALA A 1 574 ? 22.32700  3.95200   24.83000  1.000 103.05000 ? 565 ALA A O      1 
ATOM   4013  C  CB     . ALA A 1 574 ? 19.14900  3.59700   25.57000  1.000 85.83000  ? 565 ALA A CB     1 
ATOM   4014  N  N      . VAL A 1 575 ? 21.75000  1.81600   25.25600  1.000 74.98000  ? 566 VAL A N      1 
ATOM   4015  C  CA     . VAL A 1 575 ? 23.12000  1.47400   25.61800  1.000 87.46000  ? 566 VAL A CA     1 
ATOM   4016  C  C      . VAL A 1 575 ? 24.03900  1.69900   24.42600  1.000 92.41000  ? 566 VAL A C      1 
ATOM   4017  O  O      . VAL A 1 575 ? 25.10200  2.33000   24.54600  1.000 105.45000 ? 566 VAL A O      1 
ATOM   4018  C  CB     . VAL A 1 575 ? 23.18300  0.02300   26.13300  1.000 91.08000  ? 566 VAL A CB     1 
ATOM   4019  C  CG1    . VAL A 1 575 ? 24.61200  -0.48600  26.15000  1.000 90.52000  ? 566 VAL A CG1    1 
ATOM   4020  C  CG2    . VAL A 1 575 ? 22.55400  -0.06800  27.51500  1.000 88.33000  ? 566 VAL A CG2    1 
ATOM   4021  N  N      . THR A 1 576 ? 23.61600  1.24300   23.24300  1.000 95.77000  ? 567 THR A N      1 
ATOM   4022  C  CA     . THR A 1 576 ? 24.46600  1.41300   22.06600  1.000 91.30000  ? 567 THR A CA     1 
ATOM   4023  C  C      . THR A 1 576 ? 24.69100  2.89200   21.75300  1.000 88.14000  ? 567 THR A C      1 
ATOM   4024  O  O      . THR A 1 576 ? 25.81800  3.31000   21.44900  1.000 101.48000 ? 567 THR A O      1 
ATOM   4025  C  CB     . THR A 1 576 ? 23.86100  0.68500   20.86500  1.000 90.37000  ? 567 THR A CB     1 
ATOM   4026  O  OG1    . THR A 1 576 ? 22.76000  1.44100   20.34700  1.000 90.63000  ? 567 THR A OG1    1 
ATOM   4027  C  CG2    . THR A 1 576 ? 23.37900  -0.70500  21.27500  1.000 78.57000  ? 567 THR A CG2    1 
ATOM   4028  N  N      . LYS A 1 577 ? 23.63200  3.70200   21.82900  1.000 83.90000  ? 568 LYS A N      1 
ATOM   4029  C  CA     . LYS A 1 577 ? 23.76000  5.11700   21.49600  1.000 83.53000  ? 568 LYS A CA     1 
ATOM   4030  C  C      . LYS A 1 577 ? 24.68400  5.83600   22.47400  1.000 83.22000  ? 568 LYS A C      1 
ATOM   4031  O  O      . LYS A 1 577 ? 25.51400  6.66000   22.06800  1.000 99.36000  ? 568 LYS A O      1 
ATOM   4032  C  CB     . LYS A 1 577 ? 22.38000  5.77300   21.47700  1.000 83.94000  ? 568 LYS A CB     1 
ATOM   4033  C  CG     . LYS A 1 577 ? 21.51400  5.34800   20.30500  1.000 94.21000  ? 568 LYS A CG     1 
ATOM   4034  N  N      . ALA A 1 578 ? 24.54700  5.55000   23.76900  1.000 75.39000  ? 569 ALA A N      1 
ATOM   4035  C  CA     . ALA A 1 578 ? 25.42300  6.18700   24.74600  1.000 80.51000  ? 569 ALA A CA     1 
ATOM   4036  C  C      . ALA A 1 578 ? 26.87600  5.78100   24.52900  1.000 98.66000  ? 569 ALA A C      1 
ATOM   4037  O  O      . ALA A 1 578 ? 27.78900  6.60900   24.66500  1.000 106.31000 ? 569 ALA A O      1 
ATOM   4038  C  CB     . ALA A 1 578 ? 24.97000  5.84500   26.16300  1.000 91.21000  ? 569 ALA A CB     1 
ATOM   4039  N  N      . ALA A 1 579 ? 27.11500  4.50900   24.20000  1.000 97.95000  ? 570 ALA A N      1 
ATOM   4040  C  CA     . ALA A 1 579 ? 28.48400  4.09200   23.91500  1.000 84.54000  ? 570 ALA A CA     1 
ATOM   4041  C  C      . ALA A 1 579 ? 29.04200  4.83300   22.70700  1.000 93.19000  ? 570 ALA A C      1 
ATOM   4042  O  O      . ALA A 1 579 ? 30.20400  5.26100   22.71200  1.000 95.88000  ? 570 ALA A O      1 
ATOM   4043  C  CB     . ALA A 1 579 ? 28.54300  2.58200   23.69500  1.000 79.24000  ? 570 ALA A CB     1 
ATOM   4044  N  N      . MET A 1 580 ? 28.22500  5.01000   21.66500  1.000 94.85000  ? 571 MET A N      1 
ATOM   4045  C  CA     . MET A 1 580 ? 28.69600  5.74800   20.49800  1.000 77.50000  ? 571 MET A CA     1 
ATOM   4046  C  C      . MET A 1 580 ? 29.01300  7.19400   20.85300  1.000 86.05000  ? 571 MET A C      1 
ATOM   4047  O  O      . MET A 1 580 ? 30.00400  7.75800   20.37100  1.000 101.87000 ? 571 MET A O      1 
ATOM   4048  C  CB     . MET A 1 580 ? 27.66100  5.68600   19.37400  1.000 91.49000  ? 571 MET A CB     1 
ATOM   4049  C  CG     . MET A 1 580 ? 27.41100  4.28200   18.83400  1.000 110.36000 ? 571 MET A CG     1 
ATOM   4050  S  SD     . MET A 1 580 ? 28.71900  3.72000   17.72500  1.000 141.29000 ? 571 MET A SD     1 
ATOM   4051  C  CE     . MET A 1 580 ? 30.04900  3.39900   18.88700  1.000 89.94000  ? 571 MET A CE     1 
ATOM   4052  N  N      . LYS A 1 581 ? 28.18400  7.80900   21.70000  1.000 92.08000  ? 572 LYS A N      1 
ATOM   4053  C  CA     . LYS A 1 581 ? 28.45000  9.18300   22.11900  1.000 97.23000  ? 572 LYS A CA     1 
ATOM   4054  C  C      . LYS A 1 581 ? 29.76400  9.28300   22.88600  1.000 103.02000 ? 572 LYS A C      1 
ATOM   4055  O  O      . LYS A 1 581 ? 30.55700  10.20800  22.65700  1.000 100.24000 ? 572 LYS A O      1 
ATOM   4056  C  CB     . LYS A 1 581 ? 27.28700  9.71600   22.95800  1.000 80.75000  ? 572 LYS A CB     1 
ATOM   4057  N  N      . MET A 1 582 ? 30.02100  8.33700   23.79500  1.000 105.86000 ? 573 MET A N      1 
ATOM   4058  C  CA     . MET A 1 582 ? 31.29500  8.36400   24.51100  1.000 107.96000 ? 573 MET A CA     1 
ATOM   4059  C  C      . MET A 1 582 ? 32.46700  8.15600   23.56000  1.000 108.05000 ? 573 MET A C      1 
ATOM   4060  O  O      . MET A 1 582 ? 33.52200  8.77300   23.72900  1.000 115.80000 ? 573 MET A O      1 
ATOM   4061  C  CB     . MET A 1 582 ? 31.34100  7.32500   25.63100  1.000 107.54000 ? 573 MET A CB     1 
ATOM   4062  C  CG     . MET A 1 582 ? 32.71300  7.31600   26.32600  1.000 92.96000  ? 573 MET A CG     1 
ATOM   4063  S  SD     . MET A 1 582 ? 32.93300  6.16900   27.70400  1.000 93.58000  ? 573 MET A SD     1 
ATOM   4064  C  CE     . MET A 1 582 ? 31.92400  6.94100   28.96500  1.000 112.11000 ? 573 MET A CE     1 
ATOM   4065  N  N      . VAL A 1 583 ? 32.30900  7.28800   22.55800  1.000 102.29000 ? 574 VAL A N      1 
ATOM   4066  C  CA     . VAL A 1 583 ? 33.40500  7.07200   21.61400  1.000 91.57000  ? 574 VAL A CA     1 
ATOM   4067  C  C      . VAL A 1 583 ? 33.69300  8.34800   20.83200  1.000 107.47000 ? 574 VAL A C      1 
ATOM   4068  O  O      . VAL A 1 583 ? 34.85500  8.72800   20.63500  1.000 115.38000 ? 574 VAL A O      1 
ATOM   4069  C  CB     . VAL A 1 583 ? 33.08300  5.89100   20.68100  1.000 84.73000  ? 574 VAL A CB     1 
ATOM   4070  C  CG1    . VAL A 1 583 ? 34.07900  5.83600   19.53700  1.000 84.31000  ? 574 VAL A CG1    1 
ATOM   4071  C  CG2    . VAL A 1 583 ? 33.09000  4.58900   21.46900  1.000 81.76000  ? 574 VAL A CG2    1 
ATOM   4072  N  N      . ASP A 1 584 ? 32.64100  9.03800   20.38700  1.000 106.63000 ? 575 ASP A N      1 
ATOM   4073  C  CA     . ASP A 1 584 ? 32.83200  10.28400  19.65000  1.000 115.08000 ? 575 ASP A CA     1 
ATOM   4074  C  C      . ASP A 1 584 ? 33.47600  11.35700  20.52300  1.000 118.05000 ? 575 ASP A C      1 
ATOM   4075  O  O      . ASP A 1 584 ? 34.34200  12.10700  20.05700  1.000 116.82000 ? 575 ASP A O      1 
ATOM   4076  C  CB     . ASP A 1 584 ? 31.50600  10.77500  19.07000  1.000 115.34000 ? 575 ASP A CB     1 
ATOM   4077  C  CG     . ASP A 1 584 ? 30.97100  9.86100   17.98100  1.000 113.78000 ? 575 ASP A CG     1 
ATOM   4078  O  OD1    . ASP A 1 584 ? 31.73600  8.99700   17.50100  1.000 124.58000 ? 575 ASP A OD1    1 
ATOM   4079  O  OD2    . ASP A 1 584 ? 29.79100  10.00900  17.60100  1.000 98.78000  ? 575 ASP A OD2    1 
ATOM   4080  N  N      . GLU A 1 585 ? 33.07400  11.44700  21.79500  1.000 111.02000 ? 576 GLU A N      1 
ATOM   4081  C  CA     . GLU A 1 585 ? 33.72600  12.40600  22.68600  1.000 113.45000 ? 576 GLU A CA     1 
ATOM   4082  C  C      . GLU A 1 585 ? 35.17900  12.02800  22.94900  1.000 123.08000 ? 576 GLU A C      1 
ATOM   4083  O  O      . GLU A 1 585 ? 36.03900  12.90700  23.07800  1.000 137.43000 ? 576 GLU A O      1 
ATOM   4084  C  CB     . GLU A 1 585 ? 32.96200  12.52400  24.00400  1.000 122.06000 ? 576 GLU A CB     1 
ATOM   4085  C  CG     . GLU A 1 585 ? 33.27800  13.80100  24.78300  1.000 110.37000 ? 576 GLU A CG     1 
ATOM   4086  C  CD     . GLU A 1 585 ? 34.46400  13.64700  25.72400  1.000 105.61000 ? 576 GLU A CD     1 
ATOM   4087  O  OE1    . GLU A 1 585 ? 34.95000  14.67500  26.24100  1.000 100.92000 ? 576 GLU A OE1    1 
ATOM   4088  O  OE2    . GLU A 1 585 ? 34.91400  12.50300  25.94600  1.000 101.45000 ? 576 GLU A OE2    1 
ATOM   4089  N  N      . ILE A 1 586 ? 35.47500  10.73000  23.04600  1.000 121.12000 ? 577 ILE A N      1 
ATOM   4090  C  CA     . ILE A 1 586 ? 36.85500  10.30800  23.25100  1.000 125.60000 ? 577 ILE A CA     1 
ATOM   4091  C  C      . ILE A 1 586 ? 37.68700  10.67200  22.03700  1.000 132.24000 ? 577 ILE A C      1 
ATOM   4092  O  O      . ILE A 1 586 ? 38.87500  10.99500  22.15900  1.000 141.21000 ? 577 ILE A O      1 
ATOM   4093  C  CB     . ILE A 1 586 ? 36.93000  8.79700   23.54900  1.000 127.68000 ? 577 ILE A CB     1 
ATOM   4094  C  CG1    . ILE A 1 586 ? 36.78800  8.51900   25.05100  1.000 97.76000  ? 577 ILE A CG1    1 
ATOM   4095  C  CG2    . ILE A 1 586 ? 38.22900  8.21600   23.01200  1.000 143.30000 ? 577 ILE A CG2    1 
ATOM   4096  C  CD1    . ILE A 1 586 ? 35.71100  9.31600   25.73800  1.000 117.13000 ? 577 ILE A CD1    1 
ATOM   4097  N  N      . ARG A 1 587 ? 37.08500  10.62400  20.84700  1.000 126.54000 ? 578 ARG A N      1 
ATOM   4098  C  CA     . ARG A 1 587 ? 37.78600  11.08900  19.65600  1.000 134.60000 ? 578 ARG A CA     1 
ATOM   4099  C  C      . ARG A 1 587 ? 38.21500  12.54400  19.80900  1.000 138.43000 ? 578 ARG A C      1 
ATOM   4100  O  O      . ARG A 1 587 ? 39.33200  12.91300  19.42700  1.000 152.37000 ? 578 ARG A O      1 
ATOM   4101  C  CB     . ARG A 1 587 ? 36.90000  10.91300  18.42300  1.000 133.61000 ? 578 ARG A CB     1 
ATOM   4102  C  CG     . ARG A 1 587 ? 36.61800  9.46400   18.05000  1.000 133.77000 ? 578 ARG A CG     1 
ATOM   4103  C  CD     . ARG A 1 587 ? 37.84400  8.77300   17.45400  1.000 175.74000 ? 578 ARG A CD     1 
ATOM   4104  N  NE     . ARG A 1 587 ? 38.92000  8.59300   18.42300  1.000 172.04000 ? 578 ARG A NE     1 
ATOM   4105  C  CZ     . ARG A 1 587 ? 40.15200  8.20800   18.11500  1.000 188.39000 ? 578 ARG A CZ     1 
ATOM   4106  N  NH1    . ARG A 1 587 ? 40.50300  7.94400   16.86600  1.000 193.51000 ? 578 ARG A NH1    1 
ATOM   4107  N  NH2    . ARG A 1 587 ? 41.05200  8.07700   19.08500  1.000 192.32000 ? 578 ARG A NH2    1 
ATOM   4108  N  N      . ARG A 1 588 ? 37.34300  13.38300  20.37600  1.000 130.73000 ? 579 ARG A N      1 
ATOM   4109  C  CA     . ARG A 1 588 ? 37.70400  14.77700  20.61700  1.000 127.65000 ? 579 ARG A CA     1 
ATOM   4110  C  C      . ARG A 1 588 ? 38.91800  14.88300  21.53200  1.000 135.16000 ? 579 ARG A C      1 
ATOM   4111  O  O      . ARG A 1 588 ? 39.82800  15.68200  21.28200  1.000 145.88000 ? 579 ARG A O      1 
ATOM   4112  C  CB     . ARG A 1 588 ? 36.51500  15.52800  21.21800  1.000 119.92000 ? 579 ARG A CB     1 
ATOM   4113  C  CG     . ARG A 1 588 ? 35.28800  15.58600  20.31900  1.000 120.96000 ? 579 ARG A CG     1 
ATOM   4114  C  CD     . ARG A 1 588 ? 35.57200  16.34600  19.03000  1.000 121.93000 ? 579 ARG A CD     1 
ATOM   4115  N  NE     . ARG A 1 588 ? 36.11700  17.67400  19.28800  1.000 121.09000 ? 579 ARG A NE     1 
ATOM   4116  C  CZ     . ARG A 1 588 ? 35.38200  18.75600  19.50700  1.000 109.21000 ? 579 ARG A CZ     1 
ATOM   4117  N  NH1    . ARG A 1 588 ? 34.06000  18.69900  19.54000  1.000 85.83000  ? 579 ARG A NH1    1 
ATOM   4118  N  NH2    . ARG A 1 588 ? 35.98900  19.92300  19.70700  1.000 100.51000 ? 579 ARG A NH2    1 
ATOM   4119  N  N      . GLN A 1 589 ? 38.95000  14.08100  22.59400  1.000 132.07000 ? 580 GLN A N      1 
ATOM   4120  C  CA     . GLN A 1 589 ? 40.05900  14.11500  23.53600  1.000 137.19000 ? 580 GLN A CA     1 
ATOM   4121  C  C      . GLN A 1 589 ? 41.35900  13.73400  22.83700  1.000 139.69000 ? 580 GLN A C      1 
ATOM   4122  O  O      . GLN A 1 589 ? 41.37900  12.91000  21.91800  1.000 153.68000 ? 580 GLN A O      1 
ATOM   4123  C  CB     . GLN A 1 589 ? 39.78500  13.16400  24.70300  1.000 134.53000 ? 580 GLN A CB     1 
ATOM   4124  C  CG     . GLN A 1 589 ? 38.61300  13.57700  25.58400  1.000 129.88000 ? 580 GLN A CG     1 
ATOM   4125  C  CD     . GLN A 1 589 ? 39.05100  14.12000  26.92800  1.000 123.50000 ? 580 GLN A CD     1 
ATOM   4126  O  OE1    . GLN A 1 589 ? 40.22000  14.02500  27.30000  1.000 120.79000 ? 580 GLN A OE1    1 
ATOM   4127  N  NE2    . GLN A 1 589 ? 38.10700  14.68500  27.67100  1.000 108.87000 ? 580 GLN A NE2    1 
ATOM   4128  N  N      . ALA A 1 590 ? 42.45400  14.34700  23.27500  1.000 133.13000 ? 581 ALA A N      1 
ATOM   4129  C  CA     . ALA A 1 590 ? 43.76100  14.10000  22.67300  1.000 128.58000 ? 581 ALA A CA     1 
ATOM   4130  C  C      . ALA A 1 590 ? 44.88600  14.34900  23.67100  1.000 112.06000 ? 581 ALA A C      1 
ATOM   4131  O  O      . ALA A 1 590 ? 46.02800  14.60300  23.28600  1.000 93.62000  ? 581 ALA A O      1 
ATOM   4132  C  CB     . ALA A 1 590 ? 43.94700  14.97100  21.43500  1.000 137.24000 ? 581 ALA A CB     1 
ATOM   4133  N  N      . TYR A 1 605 ? 39.16800  13.22000  31.35800  1.000 85.90000  ? 596 TYR A N      1 
ATOM   4134  C  CA     . TYR A 1 605 ? 38.99700  13.42200  32.79100  1.000 104.58000 ? 596 TYR A CA     1 
ATOM   4135  C  C      . TYR A 1 605 ? 37.63400  12.93400  33.27000  1.000 124.72000 ? 596 TYR A C      1 
ATOM   4136  O  O      . TYR A 1 605 ? 37.35700  11.73000  33.28300  1.000 125.42000 ? 596 TYR A O      1 
ATOM   4137  C  CB     . TYR A 1 605 ? 39.17900  14.89900  33.14100  1.000 111.29000 ? 596 TYR A CB     1 
ATOM   4138  C  CG     . TYR A 1 605 ? 40.54000  15.21300  33.70700  1.000 116.76000 ? 596 TYR A CG     1 
ATOM   4139  C  CD1    . TYR A 1 605 ? 41.67900  15.12900  32.91800  1.000 126.76000 ? 596 TYR A CD1    1 
ATOM   4140  C  CD2    . TYR A 1 605 ? 40.69000  15.56500  35.04100  1.000 117.21000 ? 596 TYR A CD2    1 
ATOM   4141  C  CE1    . TYR A 1 605 ? 42.93000  15.40400  33.44000  1.000 137.81000 ? 596 TYR A CE1    1 
ATOM   4142  C  CE2    . TYR A 1 605 ? 41.93100  15.84300  35.57000  1.000 132.75000 ? 596 TYR A CE2    1 
ATOM   4143  C  CZ     . TYR A 1 605 ? 43.05000  15.76100  34.76800  1.000 138.70000 ? 596 TYR A CZ     1 
ATOM   4144  O  OH     . TYR A 1 605 ? 44.29100  16.03700  35.29800  1.000 124.40000 ? 596 TYR A OH     1 
ATOM   4145  N  N      . ASN A 1 606 ? 36.78600  13.88600  33.65200  1.000 129.98000 ? 597 ASN A N      1 
ATOM   4146  C  CA     . ASN A 1 606 ? 35.41300  13.61000  34.04800  1.000 117.09000 ? 597 ASN A CA     1 
ATOM   4147  C  C      . ASN A 1 606 ? 34.42100  14.14100  33.03200  1.000 127.93000 ? 597 ASN A C      1 
ATOM   4148  O  O      . ASN A 1 606 ? 33.20800  14.02600  33.24300  1.000 135.97000 ? 597 ASN A O      1 
ATOM   4149  C  CB     . ASN A 1 606 ? 35.10400  14.22300  35.42100  1.000 97.03000  ? 597 ASN A CB     1 
ATOM   4150  C  CG     . ASN A 1 606 ? 35.74500  13.46300  36.56500  1.000 99.37000  ? 597 ASN A CG     1 
ATOM   4151  O  OD1    . ASN A 1 606 ? 36.43100  12.46500  36.35500  1.000 111.80000 ? 597 ASN A OD1    1 
ATOM   4152  N  ND2    . ASN A 1 606 ? 35.50900  13.92600  37.78900  1.000 85.67000  ? 597 ASN A ND2    1 
ATOM   4153  N  N      . ARG A 1 607 ? 34.91500  14.71500  31.93500  1.000 123.42000 ? 598 ARG A N      1 
ATOM   4154  C  CA     . ARG A 1 607 ? 34.02900  15.23600  30.90400  1.000 117.86000 ? 598 ARG A CA     1 
ATOM   4155  C  C      . ARG A 1 607 ? 33.31200  14.10800  30.17700  1.000 127.12000 ? 598 ARG A C      1 
ATOM   4156  O  O      . ARG A 1 607 ? 32.13600  14.24200  29.82200  1.000 133.49000 ? 598 ARG A O      1 
ATOM   4157  C  CB     . ARG A 1 607 ? 34.82300  16.09200  29.91900  1.000 100.96000 ? 598 ARG A CB     1 
ATOM   4158  C  CG     . ARG A 1 607 ? 33.95200  16.90500  28.98500  1.000 90.93000  ? 598 ARG A CG     1 
ATOM   4159  C  CD     . ARG A 1 607 ? 32.92600  17.69600  29.77400  1.000 105.10000 ? 598 ARG A CD     1 
ATOM   4160  N  NE     . ARG A 1 607 ? 31.76800  18.06600  28.97000  1.000 120.60000 ? 598 ARG A NE     1 
ATOM   4161  C  CZ     . ARG A 1 607 ? 30.68400  18.65700  29.45300  1.000 121.18000 ? 598 ARG A CZ     1 
ATOM   4162  N  NH1    . ARG A 1 607 ? 30.58900  18.98700  30.73100  1.000 115.03000 ? 598 ARG A NH1    1 
ATOM   4163  N  NH2    . ARG A 1 607 ? 29.67200  18.92800  28.63300  1.000 116.50000 ? 598 ARG A NH2    1 
ATOM   4164  N  N      . CYS A 1 608 ? 34.00400  12.99100  29.93700  1.000 124.80000 ? 599 CYS A N      1 
ATOM   4165  C  CA     . CYS A 1 608 ? 33.36300  11.88800  29.23000  1.000 116.88000 ? 599 CYS A CA     1 
ATOM   4166  C  C      . CYS A 1 608 ? 32.26200  11.24800  30.06800  1.000 126.27000 ? 599 CYS A C      1 
ATOM   4167  O  O      . CYS A 1 608 ? 31.22700  10.83900  29.52800  1.000 127.78000 ? 599 CYS A O      1 
ATOM   4168  C  CB     . CYS A 1 608 ? 34.41100  10.84700  28.83800  1.000 111.73000 ? 599 CYS A CB     1 
ATOM   4169  S  SG     . CYS A 1 608 ? 35.54100  10.37500  30.17100  1.000 122.81000 ? 599 CYS A SG     1 
ATOM   4170  N  N      . ILE A 1 609 ? 32.45600  11.15600  31.38600  1.000 129.16000 ? 600 ILE A N      1 
ATOM   4171  C  CA     . ILE A 1 609 ? 31.42500  10.58000  32.24700  1.000 113.10000 ? 600 ILE A CA     1 
ATOM   4172  C  C      . ILE A 1 609 ? 30.15400  11.42000  32.18500  1.000 113.19000 ? 600 ILE A C      1 
ATOM   4173  O  O      . ILE A 1 609 ? 29.04000  10.89500  32.06400  1.000 114.28000 ? 600 ILE A O      1 
ATOM   4174  C  CB     . ILE A 1 609 ? 31.94100  10.42800  33.68900  1.000 97.96000  ? 600 ILE A CB     1 
ATOM   4175  C  CG1    . ILE A 1 609 ? 33.14800  9.48600   33.72300  1.000 104.79000 ? 600 ILE A CG1    1 
ATOM   4176  C  CG2    . ILE A 1 609 ? 30.83500  9.92700   34.60500  1.000 103.79000 ? 600 ILE A CG2    1 
ATOM   4177  C  CD1    . ILE A 1 609 ? 33.45100  8.93300   35.10300  1.000 103.89000 ? 600 ILE A CD1    1 
ATOM   4178  N  N      . GLU A 1 610 ? 30.30700  12.74200  32.28400  1.000 121.51000 ? 601 GLU A N      1 
ATOM   4179  C  CA     . GLU A 1 610 ? 29.15400  13.63600  32.25300  1.000 116.53000 ? 601 GLU A CA     1 
ATOM   4180  C  C      . GLU A 1 610 ? 28.37100  13.49100  30.95400  1.000 119.78000 ? 601 GLU A C      1 
ATOM   4181  O  O      . GLU A 1 610 ? 27.13600  13.45700  30.96800  1.000 129.87000 ? 601 GLU A O      1 
ATOM   4182  C  CB     . GLU A 1 610 ? 29.60800  15.08100  32.45300  1.000 120.65000 ? 601 GLU A CB     1 
ATOM   4183  N  N      . ILE A 1 611 ? 29.07200  13.44100  29.81900  1.000 120.41000 ? 602 ILE A N      1 
ATOM   4184  C  CA     . ILE A 1 611 ? 28.40600  13.29300  28.52600  1.000 129.07000 ? 602 ILE A CA     1 
ATOM   4185  C  C      . ILE A 1 611 ? 27.52300  12.05000  28.52700  1.000 131.04000 ? 602 ILE A C      1 
ATOM   4186  O  O      . ILE A 1 611 ? 26.35000  12.08700  28.11900  1.000 123.23000 ? 602 ILE A O      1 
ATOM   4187  C  CB     . ILE A 1 611 ? 29.45100  13.23500  27.39600  1.000 111.85000 ? 602 ILE A CB     1 
ATOM   4188  C  CG1    . ILE A 1 611 ? 30.18400  14.57300  27.26500  1.000 115.98000 ? 602 ILE A CG1    1 
ATOM   4189  C  CG2    . ILE A 1 611 ? 28.79100  12.86200  26.07900  1.000 101.61000 ? 602 ILE A CG2    1 
ATOM   4190  C  CD1    . ILE A 1 611 ? 29.28200  15.73900  26.96100  1.000 126.86000 ? 602 ILE A CD1    1 
ATOM   4191  N  N      . THR A 1 612 ? 28.06600  10.93800  29.02900  1.000 129.81000 ? 603 THR A N      1 
ATOM   4192  C  CA     . THR A 1 612 ? 27.29600  9.70400   29.10000  1.000 122.76000 ? 603 THR A CA     1 
ATOM   4193  C  C      . THR A 1 612 ? 26.11700  9.85800   30.04700  1.000 119.14000 ? 603 THR A C      1 
ATOM   4194  O  O      . THR A 1 612 ? 25.02400  9.36600   29.76300  1.000 125.17000 ? 603 THR A O      1 
ATOM   4195  C  CB     . THR A 1 612 ? 28.18600  8.53500   29.53100  1.000 115.25000 ? 603 THR A CB     1 
ATOM   4196  O  OG1    . THR A 1 612 ? 28.90500  8.87700   30.72300  1.000 122.96000 ? 603 THR A OG1    1 
ATOM   4197  C  CG2    . THR A 1 612 ? 29.16900  8.16900   28.41700  1.000 110.22000 ? 603 THR A CG2    1 
ATOM   4198  N  N      . SER A 1 613 ? 26.32700  10.49900  31.19900  1.000 114.24000 ? 604 SER A N      1 
ATOM   4199  C  CA     . SER A 1 613 ? 25.23500  10.66800  32.15400  1.000 105.77000 ? 604 SER A CA     1 
ATOM   4200  C  C      . SER A 1 613 ? 24.08100  11.44600  31.53100  1.000 112.99000 ? 604 SER A C      1 
ATOM   4201  O  O      . SER A 1 613 ? 22.91100  11.07200  31.67300  1.000 116.22000 ? 604 SER A O      1 
ATOM   4202  C  CB     . SER A 1 613 ? 25.73400  11.37000  33.41800  1.000 99.01000  ? 604 SER A CB     1 
ATOM   4203  O  OG     . SER A 1 613 ? 26.82800  10.68500  34.00200  1.000 112.73000 ? 604 SER A OG     1 
ATOM   4204  N  N      . ASP A 1 614 ? 24.39400  12.55900  30.86700  1.000 119.31000 ? 605 ASP A N      1 
ATOM   4205  C  CA     . ASP A 1 614 ? 23.36100  13.35100  30.20700  1.000 111.59000 ? 605 ASP A CA     1 
ATOM   4206  C  C      . ASP A 1 614 ? 22.61600  12.53100  29.16000  1.000 122.75000 ? 605 ASP A C      1 
ATOM   4207  O  O      . ASP A 1 614 ? 21.37500  12.48700  29.15200  1.000 131.19000 ? 605 ASP A O      1 
ATOM   4208  C  CB     . ASP A 1 614 ? 23.99200  14.59300  29.57600  1.000 108.18000 ? 605 ASP A CB     1 
ATOM   4209  C  CG     . ASP A 1 614 ? 22.96300  15.56200  29.04100  1.000 103.11000 ? 605 ASP A CG     1 
ATOM   4210  O  OD1    . ASP A 1 614 ? 21.79300  15.48400  29.46700  1.000 113.84000 ? 605 ASP A OD1    1 
ATOM   4211  O  OD2    . ASP A 1 614 ? 23.32900  16.41000  28.19900  1.000 97.34000  ? 605 ASP A OD2    1 
ATOM   4212  N  N      . ASN A 1 615 ? 23.35800  11.86100  28.27000  1.000 127.48000 ? 606 ASN A N      1 
ATOM   4213  C  CA     . ASN A 1 615 ? 22.70100  11.05400  27.24400  1.000 124.89000 ? 606 ASN A CA     1 
ATOM   4214  C  C      . ASN A 1 615 ? 21.82700  9.97300   27.87000  1.000 113.64000 ? 606 ASN A C      1 
ATOM   4215  O  O      . ASN A 1 615 ? 20.70500  9.72500   27.41200  1.000 108.33000 ? 606 ASN A O      1 
ATOM   4216  C  CB     . ASN A 1 615 ? 23.73900  10.43700  26.30700  1.000 109.51000 ? 606 ASN A CB     1 
ATOM   4217  C  CG     . ASN A 1 615 ? 23.18700  10.17700  24.91700  1.000 105.76000 ? 606 ASN A CG     1 
ATOM   4218  O  OD1    . ASN A 1 615 ? 22.20300  10.79100  24.49900  1.000 108.60000 ? 606 ASN A OD1    1 
ATOM   4219  N  ND2    . ASN A 1 615 ? 23.81700  9.25800   24.19600  1.000 101.22000 ? 606 ASN A ND2    1 
ATOM   4220  N  N      . ALA A 1 616 ? 22.32800  9.31200   28.91200  1.000 102.95000 ? 607 ALA A N      1 
ATOM   4221  C  CA     . ALA A 1 616 ? 21.57700  8.25000   29.56800  1.000 98.63000  ? 607 ALA A CA     1 
ATOM   4222  C  C      . ALA A 1 616 ? 20.29900  8.77100   30.21100  1.000 104.89000 ? 607 ALA A C      1 
ATOM   4223  O  O      . ALA A 1 616 ? 19.26100  8.10800   30.15300  1.000 117.57000 ? 607 ALA A O      1 
ATOM   4224  C  CB     . ALA A 1 616 ? 22.45400  7.56000   30.60800  1.000 96.24000  ? 607 ALA A CB     1 
ATOM   4225  N  N      . LEU A 1 617 ? 20.36700  9.91700   30.89300  1.000 105.09000 ? 608 LEU A N      1 
ATOM   4226  C  CA     . LEU A 1 617 ? 19.16600  10.45400  31.53000  1.000 99.20000  ? 608 LEU A CA     1 
ATOM   4227  C  C      . LEU A 1 617 ? 18.11900  10.82700  30.48200  1.000 105.59000 ? 608 LEU A C      1 
ATOM   4228  O  O      . LEU A 1 617 ? 16.92200  10.51500  30.63100  1.000 127.45000 ? 608 LEU A O      1 
ATOM   4229  C  CB     . LEU A 1 617 ? 19.54300  11.66400  32.39600  1.000 103.05000 ? 608 LEU A CB     1 
ATOM   4230  C  CG     . LEU A 1 617 ? 20.33500  11.34900  33.67800  1.000 110.55000 ? 608 LEU A CG     1 
ATOM   4231  C  CD1    . LEU A 1 617 ? 20.80200  12.62200  34.37700  1.000 132.32000 ? 608 LEU A CD1    1 
ATOM   4232  C  CD2    . LEU A 1 617 ? 19.51400  10.49300  34.63100  1.000 100.54000 ? 608 LEU A CD2    1 
ATOM   4233  N  N      . LYS A 1 618 ? 18.57000  11.38700  29.35700  1.000 99.89000  ? 609 LYS A N      1 
ATOM   4234  C  CA     . LYS A 1 618 ? 17.62700  11.69300  28.29000  1.000 102.82000 ? 609 LYS A CA     1 
ATOM   4235  C  C      . LYS A 1 618 ? 17.02500  10.41200  27.73700  1.000 107.48000 ? 609 LYS A C      1 
ATOM   4236  O  O      . LYS A 1 618 ? 15.82700  10.35800  27.43400  1.000 116.54000 ? 609 LYS A O      1 
ATOM   4237  C  CB     . LYS A 1 618 ? 18.31900  12.48800  27.18600  1.000 121.43000 ? 609 LYS A CB     1 
ATOM   4238  N  N      . GLN A 1 619 ? 17.84300  9.36800   27.60500  1.000 104.29000 ? 610 GLN A N      1 
ATOM   4239  C  CA     . GLN A 1 619 ? 17.34800  8.10200   27.08300  1.000 103.68000 ? 610 GLN A CA     1 
ATOM   4240  C  C      . GLN A 1 619 ? 16.36700  7.45500   28.05400  1.000 103.36000 ? 610 GLN A C      1 
ATOM   4241  O  O      . GLN A 1 619 ? 15.37700  6.84800   27.63300  1.000 109.98000 ? 610 GLN A O      1 
ATOM   4242  C  CB     . GLN A 1 619 ? 18.52600  7.16700   26.81200  1.000 105.29000 ? 610 GLN A CB     1 
ATOM   4243  C  CG     . GLN A 1 619 ? 19.38800  7.56400   25.62300  1.000 115.15000 ? 610 GLN A CG     1 
ATOM   4244  C  CD     . GLN A 1 619 ? 18.86100  7.01200   24.31100  1.000 115.49000 ? 610 GLN A CD     1 
ATOM   4245  O  OE1    . GLN A 1 619 ? 17.84200  6.32200   24.28200  1.000 107.18000 ? 610 GLN A OE1    1 
ATOM   4246  N  NE2    . GLN A 1 619 ? 19.56200  7.30400   23.21900  1.000 119.30000 ? 610 GLN A NE2    1 
ATOM   4247  N  N      . MET A 1 620 ? 16.60800  7.59600   29.35900  1.000 103.42000 ? 611 MET A N      1 
ATOM   4248  C  CA     . MET A 1 620 ? 15.70300  7.02300   30.34600  1.000 99.54000  ? 611 MET A CA     1 
ATOM   4249  C  C      . MET A 1 620 ? 14.40200  7.79700   30.44400  1.000 86.54000  ? 611 MET A C      1 
ATOM   4250  O  O      . MET A 1 620 ? 13.43700  7.29400   31.03100  1.000 85.20000  ? 611 MET A O      1 
ATOM   4251  C  CB     . MET A 1 620 ? 16.35900  6.97400   31.72500  1.000 99.91000  ? 611 MET A CB     1 
ATOM   4252  C  CG     . MET A 1 620 ? 16.09300  8.21300   32.56300  1.000 112.23000 ? 611 MET A CG     1 
ATOM   4253  S  SD     . MET A 1 620 ? 16.47400  8.00400   34.31100  1.000 146.10000 ? 611 MET A SD     1 
ATOM   4254  C  CE     . MET A 1 620 ? 15.31400  6.71300   34.75000  1.000 89.43000  ? 611 MET A CE     1 
ATOM   4255  N  N      . GLY A 1 621 ? 14.35600  9.00500   29.88600  1.000 94.13000  ? 612 GLY A N      1 
ATOM   4256  C  CA     . GLY A 1 621 ? 13.09400  9.72600   29.87800  1.000 101.23000 ? 612 GLY A CA     1 
ATOM   4257  C  C      . GLY A 1 621 ? 11.98000  8.92200   29.22700  1.000 96.32000  ? 612 GLY A C      1 
ATOM   4258  O  O      . GLY A 1 621 ? 10.87900  8.80400   29.77400  1.000 92.93000  ? 612 GLY A O      1 
ATOM   4259  N  N      . TYR A 1 622 ? 12.26000  8.33800   28.05200  1.000 101.92000 ? 613 TYR A N      1 
ATOM   4260  C  CA     . TYR A 1 622 ? 11.20600  7.65800   27.29600  1.000 105.77000 ? 613 TYR A CA     1 
ATOM   4261  C  C      . TYR A 1 622 ? 10.75600  6.35600   27.94300  1.000 88.35000  ? 613 TYR A C      1 
ATOM   4262  O  O      . TYR A 1 622 ? 9.54100   6.17600   28.14200  1.000 88.21000  ? 613 TYR A O      1 
ATOM   4263  C  CB     . TYR A 1 622 ? 11.67300  7.42500   25.85600  1.000 124.97000 ? 613 TYR A CB     1 
ATOM   4264  C  CG     . TYR A 1 622 ? 12.06400  8.68300   25.10500  1.000 155.13000 ? 613 TYR A CG     1 
ATOM   4265  C  CD1    . TYR A 1 622 ? 13.30100  9.28600   25.30600  1.000 150.33000 ? 613 TYR A CD1    1 
ATOM   4266  C  CD2    . TYR A 1 622 ? 11.19500  9.26300   24.18900  1.000 169.59000 ? 613 TYR A CD2    1 
ATOM   4267  C  CE1    . TYR A 1 622 ? 13.65600  10.43200  24.61900  1.000 163.32000 ? 613 TYR A CE1    1 
ATOM   4268  C  CE2    . TYR A 1 622 ? 11.54300  10.40900  23.49700  1.000 175.33000 ? 613 TYR A CE2    1 
ATOM   4269  C  CZ     . TYR A 1 622 ? 12.77400  10.98900  23.71600  1.000 179.14000 ? 613 TYR A CZ     1 
ATOM   4270  O  OH     . TYR A 1 622 ? 13.12300  12.12900  23.02900  1.000 184.49000 ? 613 TYR A OH     1 
ATOM   4271  N  N      . PRO A 1 623 ? 11.64500  5.41700   28.28700  1.000 85.03000  ? 614 PRO A N      1 
ATOM   4272  C  CA     . PRO A 1 623 ? 11.17400  4.18900   28.95000  1.000 66.15000  ? 614 PRO A CA     1 
ATOM   4273  C  C      . PRO A 1 623 ? 10.51100  4.46200   30.28400  1.000 75.30000  ? 614 PRO A C      1 
ATOM   4274  O  O      . PRO A 1 623 ? 9.51600   3.81200   30.62900  1.000 81.02000  ? 614 PRO A O      1 
ATOM   4275  C  CB     . PRO A 1 623 ? 12.45200  3.34800   29.09300  1.000 49.27000  ? 614 PRO A CB     1 
ATOM   4276  C  CG     . PRO A 1 623 ? 13.58500  4.31300   28.94200  1.000 76.54000  ? 614 PRO A CG     1 
ATOM   4277  C  CD     . PRO A 1 623 ? 13.09200  5.38600   28.01900  1.000 95.34000  ? 614 PRO A CD     1 
ATOM   4278  N  N      . ALA A 1 624 ? 11.06700  5.38600   31.06900  1.000 71.03000  ? 615 ALA A N      1 
ATOM   4279  C  CA     . ALA A 1 624 ? 10.42700  5.75600   32.32300  1.000 60.77000  ? 615 ALA A CA     1 
ATOM   4280  C  C      . ALA A 1 624 ? 9.03300   6.31100   32.08000  1.000 72.64000  ? 615 ALA A C      1 
ATOM   4281  O  O      . ALA A 1 624 ? 8.08600   5.95800   32.79000  1.000 67.22000  ? 615 ALA A O      1 
ATOM   4282  C  CB     . ALA A 1 624 ? 11.28400  6.77200   33.07000  1.000 72.11000  ? 615 ALA A CB     1 
ATOM   4283  N  N      . PHE A 1 625 ? 8.89000   7.20500   31.09900  1.000 72.79000  ? 616 PHE A N      1 
ATOM   4284  C  CA     . PHE A 1 625 ? 7.56500   7.72000   30.78000  1.000 64.33000  ? 616 PHE A CA     1 
ATOM   4285  C  C      . PHE A 1 625 ? 6.62500   6.59600   30.37700  1.000 59.09000  ? 616 PHE A C      1 
ATOM   4286  O  O      . PHE A 1 625 ? 5.44900   6.59900   30.75300  1.000 66.23000  ? 616 PHE A O      1 
ATOM   4287  C  CB     . PHE A 1 625 ? 7.65600   8.77000   29.67800  1.000 86.05000  ? 616 PHE A CB     1 
ATOM   4288  C  CG     . PHE A 1 625 ? 8.21800   10.08300  30.14400  1.000 103.37000 ? 616 PHE A CG     1 
ATOM   4289  C  CD1    . PHE A 1 625 ? 8.25900   10.39600  31.49500  1.000 97.99000  ? 616 PHE A CD1    1 
ATOM   4290  C  CD2    . PHE A 1 625 ? 8.70700   11.00300  29.23400  1.000 117.12000 ? 616 PHE A CD2    1 
ATOM   4291  C  CE1    . PHE A 1 625 ? 8.78200   11.59900  31.92300  1.000 115.86000 ? 616 PHE A CE1    1 
ATOM   4292  C  CE2    . PHE A 1 625 ? 9.22700   12.20700  29.65800  1.000 120.02000 ? 616 PHE A CE2    1 
ATOM   4293  C  CZ     . PHE A 1 625 ? 9.26500   12.50500  31.00300  1.000 123.81000 ? 616 PHE A CZ     1 
ATOM   4294  N  N      . ILE A 1 626 ? 7.13000   5.60100   29.64700  1.000 63.21000  ? 617 ILE A N      1 
ATOM   4295  C  CA     . ILE A 1 626 ? 6.30900   4.43200   29.35000  1.000 56.69000  ? 617 ILE A CA     1 
ATOM   4296  C  C      . ILE A 1 626 ? 5.83400   3.80400   30.65200  1.000 56.93000  ? 617 ILE A C      1 
ATOM   4297  O  O      . ILE A 1 626 ? 4.63100   3.71300   30.92800  1.000 55.49000  ? 617 ILE A O      1 
ATOM   4298  C  CB     . ILE A 1 626 ? 7.08800   3.41900   28.49100  1.000 32.99000  ? 617 ILE A CB     1 
ATOM   4299  C  CG1    . ILE A 1 626 ? 7.37700   3.97100   27.09100  1.000 66.57000  ? 617 ILE A CG1    1 
ATOM   4300  C  CG2    . ILE A 1 626 ? 6.33400   2.09900   28.39800  1.000 26.60000  ? 617 ILE A CG2    1 
ATOM   4301  C  CD1    . ILE A 1 626 ? 8.33100   3.09800   26.28900  1.000 59.47000  ? 617 ILE A CD1    1 
ATOM   4302  N  N      . ALA A 1 627 ? 6.78800   3.40100   31.49000  1.000 54.68000  ? 618 ALA A N      1 
ATOM   4303  C  CA     . ALA A 1 627 ? 6.46000   2.65100   32.69600  1.000 54.51000  ? 618 ALA A CA     1 
ATOM   4304  C  C      . ALA A 1 627 ? 5.48800   3.41900   33.58200  1.000 57.35000  ? 618 ALA A C      1 
ATOM   4305  O  O      . ALA A 1 627 ? 4.61800   2.82100   34.22600  1.000 54.05000  ? 618 ALA A O      1 
ATOM   4306  C  CB     . ALA A 1 627 ? 7.73600   2.31800   33.46800  1.000 46.55000  ? 618 ALA A CB     1 
ATOM   4307  N  N      . ILE A 1 628 ? 5.62200   4.74200   33.62800  1.000 71.16000  ? 619 ILE A N      1 
ATOM   4308  C  CA     . ILE A 1 628 ? 4.81000   5.53800   34.53900  1.000 59.61000  ? 619 ILE A CA     1 
ATOM   4309  C  C      . ILE A 1 628 ? 3.42800   5.79700   33.95800  1.000 52.03000  ? 619 ILE A C      1 
ATOM   4310  O  O      . ILE A 1 628 ? 2.41300   5.62500   34.64100  1.000 61.27000  ? 619 ILE A O      1 
ATOM   4311  C  CB     . ILE A 1 628 ? 5.53000   6.85600   34.86800  1.000 61.10000  ? 619 ILE A CB     1 
ATOM   4312  C  CG1    . ILE A 1 628 ? 6.92000   6.57000   35.44400  1.000 79.15000  ? 619 ILE A CG1    1 
ATOM   4313  C  CG2    . ILE A 1 628 ? 4.68200   7.68700   35.82100  1.000 59.01000  ? 619 ILE A CG2    1 
ATOM   4314  C  CD1    . ILE A 1 628 ? 7.83800   7.77600   35.47500  1.000 79.28000  ? 619 ILE A CD1    1 
ATOM   4315  N  N      . LEU A 1 629 ? 3.35500   6.19200   32.68800  1.000 50.59000  ? 620 LEU A N      1 
ATOM   4316  C  CA     . LEU A 1 629 ? 2.10400   6.69100   32.14000  1.000 55.10000  ? 620 LEU A CA     1 
ATOM   4317  C  C      . LEU A 1 629 ? 1.28000   5.60400   31.47000  1.000 44.84000  ? 620 LEU A C      1 
ATOM   4318  O  O      . LEU A 1 629 ? 0.10700   5.84500   31.16500  1.000 50.89000  ? 620 LEU A O      1 
ATOM   4319  C  CB     . LEU A 1 629 ? 2.37500   7.83100   31.15300  1.000 51.05000  ? 620 LEU A CB     1 
ATOM   4320  C  CG     . LEU A 1 629 ? 3.24100   8.96500   31.70000  1.000 44.99000  ? 620 LEU A CG     1 
ATOM   4321  C  CD1    . LEU A 1 629 ? 3.65200   9.91800   30.58300  1.000 79.32000  ? 620 LEU A CD1    1 
ATOM   4322  C  CD2    . LEU A 1 629 ? 2.48900   9.69900   32.79800  1.000 38.97000  ? 620 LEU A CD2    1 
ATOM   4323  N  N      . THR A 1 630 ? 1.84500   4.42300   31.23100  1.000 41.78000  ? 621 THR A N      1 
ATOM   4324  C  CA     . THR A 1 630 ? 1.04200   3.35800   30.63800  1.000 50.60000  ? 621 THR A CA     1 
ATOM   4325  C  C      . THR A 1 630 ? -0.16000  3.01800   31.50200  1.000 60.24000  ? 621 THR A C      1 
ATOM   4326  O  O      . THR A 1 630 ? -1.27600  2.92400   30.96000  1.000 68.08000  ? 621 THR A O      1 
ATOM   4327  C  CB     . THR A 1 630 ? 1.92000   2.13300   30.37300  1.000 40.15000  ? 621 THR A CB     1 
ATOM   4328  O  OG1    . THR A 1 630 ? 2.96300   2.48500   29.45700  1.000 39.99000  ? 621 THR A OG1    1 
ATOM   4329  C  CG2    . THR A 1 630 ? 1.08500   1.01800   29.77100  1.000 37.68000  ? 621 THR A CG2    1 
ATOM   4330  N  N      . PRO A 1 631 ? -0.03000  2.84400   32.82300  1.000 55.21000  ? 622 PRO A N      1 
ATOM   4331  C  CA     . PRO A 1 631 ? -1.23100  2.56600   33.62400  1.000 57.48000  ? 622 PRO A CA     1 
ATOM   4332  C  C      . PRO A 1 631 ? -2.25700  3.67500   33.54700  1.000 58.53000  ? 622 PRO A C      1 
ATOM   4333  O  O      . PRO A 1 631 ? -3.44800  3.40000   33.37800  1.000 52.54000  ? 622 PRO A O      1 
ATOM   4334  C  CB     . PRO A 1 631 ? -0.65900  2.41900   35.04000  1.000 52.67000  ? 622 PRO A CB     1 
ATOM   4335  C  CG     . PRO A 1 631 ? 0.76000   2.02300   34.83000  1.000 63.62000  ? 622 PRO A CG     1 
ATOM   4336  C  CD     . PRO A 1 631 ? 1.19400   2.79600   33.61200  1.000 62.08000  ? 622 PRO A CD     1 
ATOM   4337  N  N      . LEU A 1 632 ? -1.81100  4.92900   33.60900  1.000 59.01000  ? 623 LEU A N      1 
ATOM   4338  C  CA     . LEU A 1 632 ? -2.73600  6.05700   33.59800  1.000 48.00000  ? 623 LEU A CA     1 
ATOM   4339  C  C      . LEU A 1 632 ? -3.48900  6.12500   32.27700  1.000 53.13000  ? 623 LEU A C      1 
ATOM   4340  O  O      . LEU A 1 632 ? -4.72200  6.21200   32.25400  1.000 64.40000  ? 623 LEU A O      1 
ATOM   4341  C  CB     . LEU A 1 632 ? -1.97000  7.35200   33.85300  1.000 42.96000  ? 623 LEU A CB     1 
ATOM   4342  C  CG     . LEU A 1 632 ? -1.50900  7.57400   35.29200  1.000 35.41000  ? 623 LEU A CG     1 
ATOM   4343  C  CD1    . LEU A 1 632 ? -0.45300  6.55300   35.68100  1.000 45.32000  ? 623 LEU A CD1    1 
ATOM   4344  C  CD2    . LEU A 1 632 ? -0.95400  8.97800   35.43400  1.000 55.30000  ? 623 LEU A CD2    1 
ATOM   4345  N  N      . VAL A 1 633 ? -2.75700  6.12800   31.16400  1.000 48.12000  ? 624 VAL A N      1 
ATOM   4346  C  CA     . VAL A 1 633 ? -3.39500  6.21500   29.85400  1.000 53.28000  ? 624 VAL A CA     1 
ATOM   4347  C  C      . VAL A 1 633 ? -4.34400  5.03900   29.64700  1.000 61.45000  ? 624 VAL A C      1 
ATOM   4348  O  O      . VAL A 1 633 ? -5.51100  5.21900   29.28100  1.000 55.65000  ? 624 VAL A O      1 
ATOM   4349  C  CB     . VAL A 1 633 ? -2.33500  6.30100   28.74000  1.000 42.18000  ? 624 VAL A CB     1 
ATOM   4350  C  CG1    . VAL A 1 633 ? -1.35900  5.14200   28.83100  1.000 70.27000  ? 624 VAL A CG1    1 
ATOM   4351  C  CG2    . VAL A 1 633 ? -3.00700  6.33400   27.37100  1.000 38.35000  ? 624 VAL A CG2    1 
ATOM   4352  N  N      . THR A 1 634 ? -3.85200  3.81600   29.86800  1.000 46.38000  ? 625 THR A N      1 
ATOM   4353  C  CA     . THR A 1 634 ? -4.67900  2.63800   29.63700  1.000 41.65000  ? 625 THR A CA     1 
ATOM   4354  C  C      . THR A 1 634 ? -5.88900  2.58600   30.56500  1.000 61.17000  ? 625 THR A C      1 
ATOM   4355  O  O      . THR A 1 634 ? -6.93700  2.05700   30.17900  1.000 71.28000  ? 625 THR A O      1 
ATOM   4356  C  CB     . THR A 1 634 ? -3.83700  1.37500   29.80000  1.000 50.14000  ? 625 THR A CB     1 
ATOM   4357  O  OG1    . THR A 1 634 ? -3.36200  1.28800   31.14900  1.000 67.15000  ? 625 THR A OG1    1 
ATOM   4358  C  CG2    . THR A 1 634 ? -2.64000  1.41600   28.85400  1.000 48.82000  ? 625 THR A CG2    1 
ATOM   4359  N  N      . GLY A 1 635 ? -5.77800  3.12200   31.77800  1.000 61.26000  ? 626 GLY A N      1 
ATOM   4360  C  CA     . GLY A 1 635 ? -6.89800  3.11800   32.69600  1.000 67.45000  ? 626 GLY A CA     1 
ATOM   4361  C  C      . GLY A 1 635 ? -7.93800  4.17700   32.40500  1.000 63.43000  ? 626 GLY A C      1 
ATOM   4362  O  O      . GLY A 1 635 ? -9.14300  3.91800   32.48800  1.000 53.17000  ? 626 GLY A O      1 
ATOM   4363  N  N      . PHE A 1 636 ? -7.48100  5.37600   32.04200  1.000 56.43000  ? 627 PHE A N      1 
ATOM   4364  C  CA     . PHE A 1 636 ? -8.40600  6.45800   31.74200  1.000 56.91000  ? 627 PHE A CA     1 
ATOM   4365  C  C      . PHE A 1 636 ? -9.06300  6.26500   30.38400  1.000 65.48000  ? 627 PHE A C      1 
ATOM   4366  O  O      . PHE A 1 636 ? -10.20600 6.69200   30.18100  1.000 64.21000  ? 627 PHE A O      1 
ATOM   4367  C  CB     . PHE A 1 636 ? -7.66300  7.79300   31.79500  1.000 48.29000  ? 627 PHE A CB     1 
ATOM   4368  C  CG     . PHE A 1 636 ? -7.51700  8.34600   33.18200  1.000 60.73000  ? 627 PHE A CG     1 
ATOM   4369  C  CD1    . PHE A 1 636 ? -8.63300  8.66900   33.92700  1.000 65.53000  ? 627 PHE A CD1    1 
ATOM   4370  C  CD2    . PHE A 1 636 ? -6.26200  8.54300   33.74100  1.000 72.61000  ? 627 PHE A CD2    1 
ATOM   4371  C  CE1    . PHE A 1 636 ? -8.50800  9.17500   35.20100  1.000 78.49000  ? 627 PHE A CE1    1 
ATOM   4372  C  CE2    . PHE A 1 636 ? -6.13000  9.05400   35.02000  1.000 54.91000  ? 627 PHE A CE2    1 
ATOM   4373  C  CZ     . PHE A 1 636 ? -7.25800  9.37000   35.75000  1.000 63.13000  ? 627 PHE A CZ     1 
ATOM   4374  N  N      . LEU A 1 637 ? -8.36800  5.61300   29.45400  1.000 60.34000  ? 628 LEU A N      1 
ATOM   4375  C  CA     . LEU A 1 637 ? -8.96300  5.29900   28.16300  1.000 60.90000  ? 628 LEU A CA     1 
ATOM   4376  C  C      . LEU A 1 637 ? -9.93600  4.13300   28.27400  1.000 71.08000  ? 628 LEU A C      1 
ATOM   4377  O  O      . LEU A 1 637 ? -11.08300 4.22800   27.82600  1.000 75.32000  ? 628 LEU A O      1 
ATOM   4378  C  CB     . LEU A 1 637 ? -7.86700  4.99800   27.13800  1.000 44.96000  ? 628 LEU A CB     1 
ATOM   4379  C  CG     . LEU A 1 637 ? -7.16800  6.22900   26.55900  1.000 51.13000  ? 628 LEU A CG     1 
ATOM   4380  C  CD1    . LEU A 1 637 ? -6.05300  5.83500   25.60000  1.000 58.98000  ? 628 LEU A CD1    1 
ATOM   4381  C  CD2    . LEU A 1 637 ? -8.17600  7.13900   25.87200  1.000 45.39000  ? 628 LEU A CD2    1 
ATOM   4382  N  N      . LEU A 1 638 ? -9.50600  3.03000   28.88400  1.000 59.57000  ? 629 LEU A N      1 
ATOM   4383  C  CA     . LEU A 1 638 ? -10.28500 1.79900   28.87200  1.000 56.51000  ? 629 LEU A CA     1 
ATOM   4384  C  C      . LEU A 1 638 ? -10.83400 1.39700   30.23400  1.000 68.30000  ? 629 LEU A C      1 
ATOM   4385  O  O      . LEU A 1 638 ? -12.01900 1.06700   30.33900  1.000 87.71000  ? 629 LEU A O      1 
ATOM   4386  C  CB     . LEU A 1 638 ? -9.43700  0.66400   28.28400  1.000 58.20000  ? 629 LEU A CB     1 
ATOM   4387  C  CG     . LEU A 1 638 ? -9.27100  0.73000   26.76100  1.000 62.34000  ? 629 LEU A CG     1 
ATOM   4388  C  CD1    . LEU A 1 638 ? -8.00500  1.48400   26.37500  1.000 73.87000  ? 629 LEU A CD1    1 
ATOM   4389  C  CD2    . LEU A 1 638 ? -9.27400  -0.66500  26.14900  1.000 63.63000  ? 629 LEU A CD2    1 
ATOM   4390  N  N      . GLY A 1 639 ? -10.03200 1.41100   31.28700  1.000 52.11000  ? 630 GLY A N      1 
ATOM   4391  C  CA     . GLY A 1 639 ? -10.59000 1.14700   32.59300  1.000 63.73000  ? 630 GLY A CA     1 
ATOM   4392  C  C      . GLY A 1 639 ? -9.67100  0.29300   33.43500  1.000 61.64000  ? 630 GLY A C      1 
ATOM   4393  O  O      . GLY A 1 639 ? -8.52200  0.03300   33.08200  1.000 66.21000  ? 630 GLY A O      1 
ATOM   4394  N  N      . ALA A 1 640 ? -10.20500 -0.14000  34.58000  1.000 62.32000  ? 631 ALA A N      1 
ATOM   4395  C  CA     . ALA A 1 640 ? -9.41100  -0.85800  35.57000  1.000 54.03000  ? 631 ALA A CA     1 
ATOM   4396  C  C      . ALA A 1 640 ? -9.15400  -2.31400  35.19700  1.000 67.09000  ? 631 ALA A C      1 
ATOM   4397  O  O      . ALA A 1 640 ? -8.10400  -2.85900  35.55800  1.000 79.40000  ? 631 ALA A O      1 
ATOM   4398  C  CB     . ALA A 1 640 ? -10.09600 -0.78200  36.93300  1.000 58.33000  ? 631 ALA A CB     1 
ATOM   4399  N  N      . GLU A 1 641 ? -10.08700 -2.97300  34.50700  1.000 62.99000  ? 632 GLU A N      1 
ATOM   4400  C  CA     . GLU A 1 641 ? -9.84800  -4.36200  34.12600  1.000 40.94000  ? 632 GLU A CA     1 
ATOM   4401  C  C      . GLU A 1 641 ? -8.75200  -4.44800  33.07200  1.000 55.07000  ? 632 GLU A C      1 
ATOM   4402  O  O      . GLU A 1 641 ? -7.88000  -5.32600  33.13400  1.000 59.97000  ? 632 GLU A O      1 
ATOM   4403  C  CB     . GLU A 1 641 ? -11.14000 -4.99700  33.62000  1.000 27.42000  ? 632 GLU A CB     1 
ATOM   4404  C  CG     . GLU A 1 641 ? -12.05900 -5.49800  34.72600  1.000 57.01000  ? 632 GLU A CG     1 
ATOM   4405  C  CD     . GLU A 1 641 ? -12.84300 -4.37800  35.38900  1.000 94.17000  ? 632 GLU A CD     1 
ATOM   4406  O  OE1    . GLU A 1 641 ? -13.09500 -3.35200  34.72200  1.000 98.69000  ? 632 GLU A OE1    1 
ATOM   4407  O  OE2    . GLU A 1 641 ? -13.21900 -4.53000  36.57100  1.000 106.91000 ? 632 GLU A OE2    1 
ATOM   4408  N  N      . PHE A 1 642 ? -8.77200  -3.52500  32.10900  1.000 56.02000  ? 633 PHE A N      1 
ATOM   4409  C  CA     . PHE A 1 642 ? -7.70100  -3.45400  31.12400  1.000 36.74000  ? 633 PHE A CA     1 
ATOM   4410  C  C      . PHE A 1 642 ? -6.36500  -3.17900  31.80100  1.000 51.88000  ? 633 PHE A C      1 
ATOM   4411  O  O      . PHE A 1 642 ? -5.32900  -3.71600  31.39200  1.000 55.39000  ? 633 PHE A O      1 
ATOM   4412  C  CB     . PHE A 1 642 ? -8.03200  -2.38000  30.08700  1.000 41.68000  ? 633 PHE A CB     1 
ATOM   4413  C  CG     . PHE A 1 642 ? -7.07600  -2.32500  28.92800  1.000 55.28000  ? 633 PHE A CG     1 
ATOM   4414  C  CD1    . PHE A 1 642 ? -5.87100  -1.64800  29.03000  1.000 57.57000  ? 633 PHE A CD1    1 
ATOM   4415  C  CD2    . PHE A 1 642 ? -7.39000  -2.94400  27.72800  1.000 64.69000  ? 633 PHE A CD2    1 
ATOM   4416  C  CE1    . PHE A 1 642 ? -4.99700  -1.59200  27.95500  1.000 60.33000  ? 633 PHE A CE1    1 
ATOM   4417  C  CE2    . PHE A 1 642 ? -6.51900  -2.89200  26.65300  1.000 62.50000  ? 633 PHE A CE2    1 
ATOM   4418  C  CZ     . PHE A 1 642 ? -5.32300  -2.21600  26.76800  1.000 58.95000  ? 633 PHE A CZ     1 
ATOM   4419  N  N      . VAL A 1 643 ? -6.36800  -2.34800  32.84500  1.000 57.77000  ? 634 VAL A N      1 
ATOM   4420  C  CA     . VAL A 1 643 ? -5.12500  -2.05400  33.55100  1.000 59.38000  ? 634 VAL A CA     1 
ATOM   4421  C  C      . VAL A 1 643 ? -4.62800  -3.28500  34.30300  1.000 60.50000  ? 634 VAL A C      1 
ATOM   4422  O  O      . VAL A 1 643 ? -3.42300  -3.56600  34.33000  1.000 80.37000  ? 634 VAL A O      1 
ATOM   4423  C  CB     . VAL A 1 643 ? -5.31600  -0.84500  34.48600  1.000 56.96000  ? 634 VAL A CB     1 
ATOM   4424  C  CG1    . VAL A 1 643 ? -4.18500  -0.76900  35.49400  1.000 57.17000  ? 634 VAL A CG1    1 
ATOM   4425  C  CG2    . VAL A 1 643 ? -5.38200  0.43900   33.67200  1.000 65.80000  ? 634 VAL A CG2    1 
ATOM   4426  N  N      . GLY A 1 644 ? -5.53800  -4.04400  34.91800  1.000 42.63000  ? 635 GLY A N      1 
ATOM   4427  C  CA     . GLY A 1 644 ? -5.12800  -5.28700  35.55500  1.000 39.65000  ? 635 GLY A CA     1 
ATOM   4428  C  C      . GLY A 1 644 ? -4.52600  -6.26600  34.56500  1.000 58.01000  ? 635 GLY A C      1 
ATOM   4429  O  O      . GLY A 1 644 ? -3.52400  -6.93200  34.85700  1.000 72.50000  ? 635 GLY A O      1 
ATOM   4430  N  N      . GLY A 1 645 ? -5.13100  -6.36900  33.38000  1.000 61.42000  ? 636 GLY A N      1 
ATOM   4431  C  CA     . GLY A 1 645 ? -4.56100  -7.21900  32.34700  1.000 65.65000  ? 636 GLY A CA     1 
ATOM   4432  C  C      . GLY A 1 645 ? -3.18700  -6.75200  31.90400  1.000 58.28000  ? 636 GLY A C      1 
ATOM   4433  O  O      . GLY A 1 645 ? -2.27100  -7.56100  31.72200  1.000 57.81000  ? 636 GLY A O      1 
ATOM   4434  N  N      . VAL A 1 646 ? -3.02700  -5.44000  31.71700  1.000 49.15000  ? 637 VAL A N      1 
ATOM   4435  C  CA     . VAL A 1 646 ? -1.71600  -4.90100  31.37400  1.000 48.73000  ? 637 VAL A CA     1 
ATOM   4436  C  C      . VAL A 1 646 ? -0.70100  -5.28800  32.43600  1.000 57.71000  ? 637 VAL A C      1 
ATOM   4437  O  O      . VAL A 1 646 ? 0.42500   -5.68900  32.12300  1.000 77.78000  ? 637 VAL A O      1 
ATOM   4438  C  CB     . VAL A 1 646 ? -1.78300  -3.37300  31.20200  1.000 43.49000  ? 637 VAL A CB     1 
ATOM   4439  C  CG1    . VAL A 1 646 ? -0.38500  -2.81300  31.00500  1.000 38.47000  ? 637 VAL A CG1    1 
ATOM   4440  C  CG2    . VAL A 1 646 ? -2.67600  -3.00400  30.03000  1.000 54.16000  ? 637 VAL A CG2    1 
ATOM   4441  N  N      . LEU A 1 647 ? -1.09100  -5.18900  33.70700  1.000 51.70000  ? 638 LEU A N      1 
ATOM   4442  C  CA     . LEU A 1 647 ? -0.17300  -5.52000  34.79100  1.000 54.16000  ? 638 LEU A CA     1 
ATOM   4443  C  C      . LEU A 1 647 ? 0.23900   -6.98700  34.74200  1.000 60.11000  ? 638 LEU A C      1 
ATOM   4444  O  O      . LEU A 1 647 ? 1.42800   -7.31200  34.84600  1.000 44.07000  ? 638 LEU A O      1 
ATOM   4445  C  CB     . LEU A 1 647 ? -0.80200  -5.17300  36.14100  1.000 42.83000  ? 638 LEU A CB     1 
ATOM   4446  C  CG     . LEU A 1 647 ? -1.23900  -3.72300  36.35000  1.000 48.58000  ? 638 LEU A CG     1 
ATOM   4447  C  CD1    . LEU A 1 647 ? -2.00300  -3.56800  37.65800  1.000 44.99000  ? 638 LEU A CD1    1 
ATOM   4448  C  CD2    . LEU A 1 647 ? -0.02400  -2.81500  36.33300  1.000 53.11000  ? 638 LEU A CD2    1 
ATOM   4449  N  N      . ILE A 1 648 ? -0.73000  -7.89100  34.58500  1.000 63.43000  ? 639 ILE A N      1 
ATOM   4450  C  CA     . ILE A 1 648 ? -0.38400  -9.31100  34.60000  1.000 56.65000  ? 639 ILE A CA     1 
ATOM   4451  C  C      . ILE A 1 648 ? 0.48400   -9.66600  33.39800  1.000 58.75000  ? 639 ILE A C      1 
ATOM   4452  O  O      . ILE A 1 648 ? 1.49300   -10.37500 33.53100  1.000 73.44000  ? 639 ILE A O      1 
ATOM   4453  C  CB     . ILE A 1 648 ? -1.65300  -10.18100 34.67700  1.000 43.24000  ? 639 ILE A CB     1 
ATOM   4454  C  CG1    . ILE A 1 648 ? -2.68100  -9.72700  33.64200  1.000 73.29000  ? 639 ILE A CG1    1 
ATOM   4455  C  CG2    . ILE A 1 648 ? -2.23500  -10.16100 36.08400  1.000 59.58000  ? 639 ILE A CG2    1 
ATOM   4456  C  CD1    . ILE A 1 648 ? -4.06400  -10.29700 33.88100  1.000 78.51000  ? 639 ILE A CD1    1 
ATOM   4457  N  N      . GLY A 1 649 ? 0.12700   -9.16400  32.21300  1.000 47.97000  ? 640 GLY A N      1 
ATOM   4458  C  CA     . GLY A 1 649 ? 0.93700   -9.44700  31.04000  1.000 46.63000  ? 640 GLY A CA     1 
ATOM   4459  C  C      . GLY A 1 649 ? 2.34600   -8.90300  31.16900  1.000 45.16000  ? 640 GLY A C      1 
ATOM   4460  O  O      . GLY A 1 649 ? 3.32100   -9.57800  30.81800  1.000 43.45000  ? 640 GLY A O      1 
ATOM   4461  N  N      . THR A 1 650 ? 2.47400   -7.67800  31.68600  1.000 42.16000  ? 641 THR A N      1 
ATOM   4462  C  CA     . THR A 1 650 ? 3.79400   -7.09700  31.87800  1.000 43.12000  ? 641 THR A CA     1 
ATOM   4463  C  C      . THR A 1 650 ? 4.60300   -7.91000  32.87500  1.000 44.88000  ? 641 THR A C      1 
ATOM   4464  O  O      . THR A 1 650 ? 5.78900   -8.15600  32.65800  1.000 47.38000  ? 641 THR A O      1 
ATOM   4465  C  CB     . THR A 1 650 ? 3.66900   -5.64400  32.33800  1.000 37.06000  ? 641 THR A CB     1 
ATOM   4466  O  OG1    . THR A 1 650 ? 3.27400   -4.82300  31.23000  1.000 41.87000  ? 641 THR A OG1    1 
ATOM   4467  C  CG2    . THR A 1 650 ? 4.99000   -5.14000  32.89800  1.000 39.06000  ? 641 THR A CG2    1 
ATOM   4468  N  N      . VAL A 1 651 ? 3.97700   -8.35700  33.96400  1.000 48.99000  ? 642 VAL A N      1 
ATOM   4469  C  CA     . VAL A 1 651 ? 4.70600   -9.15700  34.94400  1.000 44.01000  ? 642 VAL A CA     1 
ATOM   4470  C  C      . VAL A 1 651 ? 5.22100   -10.43700 34.30000  1.000 37.72000  ? 642 VAL A C      1 
ATOM   4471  O  O      . VAL A 1 651 ? 6.39000   -10.80400 34.45600  1.000 47.11000  ? 642 VAL A O      1 
ATOM   4472  C  CB     . VAL A 1 651 ? 3.82300   -9.45400  36.16900  1.000 34.38000  ? 642 VAL A CB     1 
ATOM   4473  C  CG1    . VAL A 1 651 ? 4.47200   -10.51000 37.04700  1.000 20.23000  ? 642 VAL A CG1    1 
ATOM   4474  C  CG2    . VAL A 1 651 ? 3.59600   -8.18100  36.96700  1.000 37.71000  ? 642 VAL A CG2    1 
ATOM   4475  N  N      . LEU A 1 652 ? 4.36000   -11.12700 33.55200  1.000 32.22000  ? 643 LEU A N      1 
ATOM   4476  C  CA     . LEU A 1 652 ? 4.78400   -12.38000 32.93300  1.000 29.84000  ? 643 LEU A CA     1 
ATOM   4477  C  C      . LEU A 1 652 ? 5.93500   -12.14700 31.96000  1.000 42.45000  ? 643 LEU A C      1 
ATOM   4478  O  O      . LEU A 1 652 ? 7.00500   -12.76900 32.07400  1.000 60.79000  ? 643 LEU A O      1 
ATOM   4479  C  CB     . LEU A 1 652 ? 3.60100   -13.03300 32.22000  1.000 35.08000  ? 643 LEU A CB     1 
ATOM   4480  C  CG     . LEU A 1 652 ? 2.43900   -13.50000 33.09600  1.000 31.03000  ? 643 LEU A CG     1 
ATOM   4481  C  CD1    . LEU A 1 652 ? 1.34500   -14.11200 32.23800  1.000 21.43000  ? 643 LEU A CD1    1 
ATOM   4482  C  CD2    . LEU A 1 652 ? 2.93300   -14.50700 34.12000  1.000 51.38000  ? 643 LEU A CD2    1 
ATOM   4483  N  N      . SER A 1 653 ? 5.73900   -11.22900 31.00900  1.000 40.57000  ? 644 SER A N      1 
ATOM   4484  C  CA     . SER A 1 653 ? 6.75600   -10.99200 29.99300  1.000 39.99000  ? 644 SER A CA     1 
ATOM   4485  C  C      . SER A 1 653 ? 8.04900   -10.49100 30.61300  1.000 40.40000  ? 644 SER A C      1 
ATOM   4486  O  O      . SER A 1 653 ? 9.13900   -10.90300 30.20300  1.000 34.29000  ? 644 SER A O      1 
ATOM   4487  C  CB     . SER A 1 653 ? 6.24100   -9.99400  28.95600  1.000 44.27000  ? 644 SER A CB     1 
ATOM   4488  O  OG     . SER A 1 653 ? 5.22700   -10.56700 28.15000  1.000 56.84000  ? 644 SER A OG     1 
ATOM   4489  N  N      . GLY A 1 654 ? 7.95300   -9.61500  31.61400  1.000 40.22000  ? 645 GLY A N      1 
ATOM   4490  C  CA     . GLY A 1 654 ? 9.14900   -9.08400  32.23600  1.000 39.10000  ? 645 GLY A CA     1 
ATOM   4491  C  C      . GLY A 1 654 ? 9.90200   -10.13300 33.02100  1.000 43.59000  ? 645 GLY A C      1 
ATOM   4492  O  O      . GLY A 1 654 ? 11.12700  -10.21200 32.94000  1.000 44.13000  ? 645 GLY A O      1 
ATOM   4493  N  N      . ALA A 1 655 ? 9.18800   -10.95900 33.78500  1.000 39.39000  ? 646 ALA A N      1 
ATOM   4494  C  CA     . ALA A 1 655 ? 9.85800   -12.04000 34.49300  1.000 38.87000  ? 646 ALA A CA     1 
ATOM   4495  C  C      . ALA A 1 655 ? 10.61700  -12.91800 33.51400  1.000 53.63000  ? 646 ALA A C      1 
ATOM   4496  O  O      . ALA A 1 655 ? 11.81800  -13.17300 33.68600  1.000 71.30000  ? 646 ALA A O      1 
ATOM   4497  C  CB     . ALA A 1 655 ? 8.83900   -12.86000 35.28300  1.000 25.94000  ? 646 ALA A CB     1 
ATOM   4498  N  N      . MET A 1 656 ? 9.94200   -13.34500 32.44300  1.000 35.49000  ? 647 MET A N      1 
ATOM   4499  C  CA     . MET A 1 656 ? 10.58600  -14.25000 31.49700  1.000 44.23000  ? 647 MET A CA     1 
ATOM   4500  C  C      . MET A 1 656 ? 11.78100  -13.58300 30.82500  1.000 53.62000  ? 647 MET A C      1 
ATOM   4501  O  O      . MET A 1 656 ? 12.87400  -14.16200 30.75700  1.000 52.12000  ? 647 MET A O      1 
ATOM   4502  C  CB     . MET A 1 656 ? 9.57100   -14.73300 30.46300  1.000 47.99000  ? 647 MET A CB     1 
ATOM   4503  C  CG     . MET A 1 656 ? 8.33800   -15.37600 31.07600  1.000 63.27000  ? 647 MET A CG     1 
ATOM   4504  S  SD     . MET A 1 656 ? 8.75900   -16.59200 32.34100  1.000 72.15000  ? 647 MET A SD     1 
ATOM   4505  C  CE     . MET A 1 656 ? 7.22900   -16.67600 33.27200  1.000 71.87000  ? 647 MET A CE     1 
ATOM   4506  N  N      . LEU A 1 657 ? 11.59900  -12.35100 30.34100  1.000 35.22000  ? 648 LEU A N      1 
ATOM   4507  C  CA     . LEU A 1 657 ? 12.66600  -11.66800 29.62100  1.000 30.05000  ? 648 LEU A CA     1 
ATOM   4508  C  C      . LEU A 1 657 ? 13.84500  -11.35800 30.53000  1.000 42.40000  ? 648 LEU A C      1 
ATOM   4509  O  O      . LEU A 1 657 ? 15.00200  -11.48000 30.11400  1.000 47.23000  ? 648 LEU A O      1 
ATOM   4510  C  CB     . LEU A 1 657 ? 12.13100  -10.38600 28.99000  1.000 19.41000  ? 648 LEU A CB     1 
ATOM   4511  C  CG     . LEU A 1 657 ? 11.49400  -10.54600 27.61200  1.000 47.61000  ? 648 LEU A CG     1 
ATOM   4512  C  CD1    . LEU A 1 657 ? 10.86600  -9.24000  27.15600  1.000 69.65000  ? 648 LEU A CD1    1 
ATOM   4513  C  CD2    . LEU A 1 657 ? 12.54000  -11.01200 26.61800  1.000 47.09000  ? 648 LEU A CD2    1 
ATOM   4514  N  N      . ALA A 1 658 ? 13.57800  -10.94500 31.76900  1.000 37.10000  ? 649 ALA A N      1 
ATOM   4515  C  CA     . ALA A 1 658 ? 14.66000  -10.66200 32.69900  1.000 39.85000  ? 649 ALA A CA     1 
ATOM   4516  C  C      . ALA A 1 658 ? 15.45100  -11.92400 32.99600  1.000 45.66000  ? 649 ALA A C      1 
ATOM   4517  O  O      . ALA A 1 658 ? 16.68700  -11.92000 32.95700  1.000 49.01000  ? 649 ALA A O      1 
ATOM   4518  C  CB     . ALA A 1 658 ? 14.10200  -10.05900 33.98700  1.000 39.60000  ? 649 ALA A CB     1 
ATOM   4519  N  N      . ILE A 1 659 ? 14.75500  -13.02500 33.28300  1.000 35.53000  ? 650 ILE A N      1 
ATOM   4520  C  CA     . ILE A 1 659 ? 15.46400  -14.27400 33.52900  1.000 46.06000  ? 650 ILE A CA     1 
ATOM   4521  C  C      . ILE A 1 659 ? 16.33200  -14.62500 32.32700  1.000 48.17000  ? 650 ILE A C      1 
ATOM   4522  O  O      . ILE A 1 659 ? 17.53600  -14.88800 32.46100  1.000 55.79000  ? 650 ILE A O      1 
ATOM   4523  C  CB     . ILE A 1 659 ? 14.47100  -15.40000 33.86200  1.000 50.56000  ? 650 ILE A CB     1 
ATOM   4524  C  CG1    . ILE A 1 659 ? 13.71500  -15.06500 35.15000  1.000 54.90000  ? 650 ILE A CG1    1 
ATOM   4525  C  CG2    . ILE A 1 659 ? 15.20800  -16.72700 33.99600  1.000 58.15000  ? 650 ILE A CG2    1 
ATOM   4526  C  CD1    . ILE A 1 659 ? 12.62900  -16.05600 35.49800  1.000 62.43000  ? 650 ILE A CD1    1 
ATOM   4527  N  N      . LEU A 1 660 ? 15.74100  -14.59300 31.12900  1.000 43.21000  ? 651 LEU A N      1 
ATOM   4528  C  CA     . LEU A 1 660 ? 16.48000  -14.96400 29.92600  1.000 41.06000  ? 651 LEU A CA     1 
ATOM   4529  C  C      . LEU A 1 660 ? 17.71800  -14.09600 29.75200  1.000 46.80000  ? 651 LEU A C      1 
ATOM   4530  O  O      . LEU A 1 660 ? 18.82800  -14.60900 29.58400  1.000 56.93000  ? 651 LEU A O      1 
ATOM   4531  C  CB     . LEU A 1 660 ? 15.57300  -14.86100 28.69800  1.000 44.95000  ? 651 LEU A CB     1 
ATOM   4532  C  CG     . LEU A 1 660 ? 16.07300  -15.49800 27.39900  1.000 35.83000  ? 651 LEU A CG     1 
ATOM   4533  C  CD1    . LEU A 1 660 ? 14.90800  -15.78200 26.47000  1.000 13.62000  ? 651 LEU A CD1    1 
ATOM   4534  C  CD2    . LEU A 1 660 ? 17.09000  -14.59800 26.70800  1.000 50.79000  ? 651 LEU A CD2    1 
ATOM   4535  N  N      . THR A 1 661 ? 17.54700  -12.77400 29.79400  1.000 48.65000  ? 652 THR A N      1 
ATOM   4536  C  CA     . THR A 1 661 ? 18.66500  -11.87900 29.51900  1.000 50.27000  ? 652 THR A CA     1 
ATOM   4537  C  C      . THR A 1 661 ? 19.76000  -12.02900 30.56600  1.000 54.12000  ? 652 THR A C      1 
ATOM   4538  O  O      . THR A 1 661 ? 20.94200  -12.18300 30.22800  1.000 67.41000  ? 652 THR A O      1 
ATOM   4539  C  CB     . THR A 1 661 ? 18.17200  -10.43300 29.45300  1.000 41.31000  ? 652 THR A CB     1 
ATOM   4540  O  OG1    . THR A 1 661 ? 17.55000  -10.08400 30.69500  1.000 48.08000  ? 652 THR A OG1    1 
ATOM   4541  C  CG2    . THR A 1 661 ? 17.15400  -10.26800 28.32700  1.000 34.42000  ? 652 THR A CG2    1 
ATOM   4542  N  N      . ALA A 1 662 ? 19.38600  -12.00600 31.84800  1.000 41.12000  ? 653 ALA A N      1 
ATOM   4543  C  CA     . ALA A 1 662 ? 20.38900  -12.09000 32.90200  1.000 36.47000  ? 653 ALA A CA     1 
ATOM   4544  C  C      . ALA A 1 662 ? 21.16900  -13.39200 32.81000  1.000 43.49000  ? 653 ALA A C      1 
ATOM   4545  O  O      . ALA A 1 662 ? 22.40900  -13.39000 32.81700  1.000 52.78000  ? 653 ALA A O      1 
ATOM   4546  C  CB     . ALA A 1 662 ? 19.72300  -11.95400 34.27000  1.000 36.92000  ? 653 ALA A CB     1 
ATOM   4547  N  N      . ASN A 1 663 ? 20.46100  -14.52000 32.70200  1.000 42.57000  ? 654 ASN A N      1 
ATOM   4548  C  CA     . ASN A 1 663 ? 21.15400  -15.80100 32.67600  1.000 44.32000  ? 654 ASN A CA     1 
ATOM   4549  C  C      . ASN A 1 663 ? 21.99700  -15.95200 31.41800  1.000 48.87000  ? 654 ASN A C      1 
ATOM   4550  O  O      . ASN A 1 663 ? 23.12000  -16.46100 31.48400  1.000 60.70000  ? 654 ASN A O      1 
ATOM   4551  C  CB     . ASN A 1 663 ? 20.15300  -16.94600 32.80800  1.000 28.15000  ? 654 ASN A CB     1 
ATOM   4552  C  CG     . ASN A 1 663 ? 19.75800  -17.19700 34.25000  1.000 49.04000  ? 654 ASN A CG     1 
ATOM   4553  O  OD1    . ASN A 1 663 ? 20.49900  -16.85200 35.17500  1.000 49.54000  ? 654 ASN A OD1    1 
ATOM   4554  N  ND2    . ASN A 1 663 ? 18.58300  -17.78200 34.45400  1.000 84.33000  ? 654 ASN A ND2    1 
ATOM   4555  N  N      . SER A 1 664 ? 21.49300  -15.50400 30.26600  1.000 42.62000  ? 655 SER A N      1 
ATOM   4556  C  CA     . SER A 1 664 ? 22.27300  -15.62200 29.04100  1.000 46.26000  ? 655 SER A CA     1 
ATOM   4557  C  C      . SER A 1 664 ? 23.56200  -14.82000 29.14100  1.000 58.32000  ? 655 SER A C      1 
ATOM   4558  O  O      . SER A 1 664 ? 24.64900  -15.32700 28.83400  1.000 73.01000  ? 655 SER A O      1 
ATOM   4559  C  CB     . SER A 1 664 ? 21.44100  -15.17300 27.83800  1.000 58.05000  ? 655 SER A CB     1 
ATOM   4560  O  OG     . SER A 1 664 ? 20.35800  -16.05600 27.59900  1.000 62.05000  ? 655 SER A OG     1 
ATOM   4561  N  N      . GLY A 1 665 ? 23.46600  -13.56600 29.59300  1.000 55.29000  ? 656 GLY A N      1 
ATOM   4562  C  CA     . GLY A 1 665 ? 24.66200  -12.74600 29.69600  1.000 48.80000  ? 656 GLY A CA     1 
ATOM   4563  C  C      . GLY A 1 665 ? 25.66700  -13.31700 30.67800  1.000 54.00000  ? 656 GLY A C      1 
ATOM   4564  O  O      . GLY A 1 665 ? 26.86200  -13.43200 30.37300  1.000 72.82000  ? 656 GLY A O      1 
ATOM   4565  N  N      . GLY A 1 666 ? 25.19400  -13.70300 31.86700  1.000 49.09000  ? 657 GLY A N      1 
ATOM   4566  C  CA     . GLY A 1 666 ? 26.10000  -14.26800 32.85300  1.000 62.00000  ? 657 GLY A CA     1 
ATOM   4567  C  C      . GLY A 1 666 ? 26.76700  -15.54200 32.37100  1.000 71.68000  ? 657 GLY A C      1 
ATOM   4568  O  O      . GLY A 1 666 ? 27.97000  -15.74500 32.57400  1.000 88.38000  ? 657 GLY A O      1 
ATOM   4569  N  N      . ALA A 1 667 ? 26.00100  -16.41600 31.71700  1.000 61.84000  ? 658 ALA A N      1 
ATOM   4570  C  CA     . ALA A 1 667 ? 26.57000  -17.65800 31.21700  1.000 73.08000  ? 658 ALA A CA     1 
ATOM   4571  C  C      . ALA A 1 667 ? 27.59900  -17.39200 30.12800  1.000 69.18000  ? 658 ALA A C      1 
ATOM   4572  O  O      . ALA A 1 667 ? 28.64000  -18.05500 30.07900  1.000 88.89000  ? 658 ALA A O      1 
ATOM   4573  C  CB     . ALA A 1 667 ? 25.46100  -18.57600 30.71000  1.000 81.47000  ? 658 ALA A CB     1 
ATOM   4574  N  N      . TRP A 1 668 ? 27.31700  -16.44600 29.22700  1.000 51.10000  ? 659 TRP A N      1 
ATOM   4575  C  CA     . TRP A 1 668 ? 28.30600  -16.09600 28.21100  1.000 66.09000  ? 659 TRP A CA     1 
ATOM   4576  C  C      . TRP A 1 668 ? 29.59800  -15.61400 28.86100  1.000 83.99000  ? 659 TRP A C      1 
ATOM   4577  O  O      . TRP A 1 668 ? 30.70100  -15.99500 28.43900  1.000 88.29000  ? 659 TRP A O      1 
ATOM   4578  C  CB     . TRP A 1 668 ? 27.74400  -15.02100 27.27700  1.000 73.00000  ? 659 TRP A CB     1 
ATOM   4579  C  CG     . TRP A 1 668 ? 27.13400  -15.55000 26.00000  1.000 71.95000  ? 659 TRP A CG     1 
ATOM   4580  C  CD1    . TRP A 1 668 ? 27.53600  -16.64000 25.28000  1.000 81.95000  ? 659 TRP A CD1    1 
ATOM   4581  C  CD2    . TRP A 1 668 ? 26.00600  -15.00600 25.30200  1.000 75.05000  ? 659 TRP A CD2    1 
ATOM   4582  N  NE1    . TRP A 1 668 ? 26.73200  -16.80400 24.17600  1.000 77.55000  ? 659 TRP A NE1    1 
ATOM   4583  C  CE2    . TRP A 1 668 ? 25.78400  -15.81400 24.16800  1.000 71.93000  ? 659 TRP A CE2    1 
ATOM   4584  C  CE3    . TRP A 1 668 ? 25.16300  -13.91200 25.52600  1.000 82.96000  ? 659 TRP A CE3    1 
ATOM   4585  C  CZ2    . TRP A 1 668 ? 24.75400  -15.56300 23.26300  1.000 68.27000  ? 659 TRP A CZ2    1 
ATOM   4586  C  CZ3    . TRP A 1 668 ? 24.14300  -13.66400 24.62700  1.000 66.04000  ? 659 TRP A CZ3    1 
ATOM   4587  C  CH2    . TRP A 1 668 ? 23.94600  -14.48500 23.51100  1.000 58.95000  ? 659 TRP A CH2    1 
ATOM   4588  N  N      . ASP A 1 669 ? 29.47700  -14.79700 29.91100  1.000 83.67000  ? 660 ASP A N      1 
ATOM   4589  C  CA     . ASP A 1 669 ? 30.66300  -14.27600 30.58500  1.000 84.00000  ? 660 ASP A CA     1 
ATOM   4590  C  C      . ASP A 1 669 ? 31.47600  -15.41300 31.19800  1.000 84.70000  ? 660 ASP A C      1 
ATOM   4591  O  O      . ASP A 1 669 ? 32.70200  -15.49100 31.02600  1.000 106.87000 ? 660 ASP A O      1 
ATOM   4592  C  CB     . ASP A 1 669 ? 30.24700  -13.25300 31.64600  1.000 73.20000  ? 660 ASP A CB     1 
ATOM   4593  C  CG     . ASP A 1 669 ? 31.42900  -12.64600 32.37600  1.000 86.66000  ? 660 ASP A CG     1 
ATOM   4594  O  OD1    . ASP A 1 669 ? 32.23500  -11.94400 31.73200  1.000 110.28000 ? 660 ASP A OD1    1 
ATOM   4595  O  OD2    . ASP A 1 669 ? 31.53900  -12.85100 33.60200  1.000 84.03000  ? 660 ASP A OD2    1 
ATOM   4596  N  N      . ASN A 1 670 ? 30.80200  -16.32500 31.90000  1.000 68.58000  ? 661 ASN A N      1 
ATOM   4597  C  CA     . ASN A 1 670 ? 31.52700  -17.41000 32.55400  1.000 66.11000  ? 661 ASN A CA     1 
ATOM   4598  C  C      . ASN A 1 670 ? 32.11000  -18.40100 31.54800  1.000 74.91000  ? 661 ASN A C      1 
ATOM   4599  O  O      . ASN A 1 670 ? 33.15700  -18.99900 31.81300  1.000 92.69000  ? 661 ASN A O      1 
ATOM   4600  C  CB     . ASN A 1 670 ? 30.62700  -18.11300 33.56800  1.000 83.49000  ? 661 ASN A CB     1 
ATOM   4601  C  CG     . ASN A 1 670 ? 30.43400  -17.29500 34.83100  1.000 87.58000  ? 661 ASN A CG     1 
ATOM   4602  O  OD1    . ASN A 1 670 ? 30.13900  -17.83900 35.89800  1.000 86.29000  ? 661 ASN A OD1    1 
ATOM   4603  N  ND2    . ASN A 1 670 ? 30.58200  -15.98300 34.71500  1.000 107.11000 ? 661 ASN A ND2    1 
ATOM   4604  N  N      . ALA A 1 671 ? 31.45400  -18.60700 30.40300  1.000 60.70000  ? 662 ALA A N      1 
ATOM   4605  C  CA     . ALA A 1 671 ? 32.03300  -19.46700 29.37100  1.000 72.35000  ? 662 ALA A CA     1 
ATOM   4606  C  C      . ALA A 1 671 ? 33.28200  -18.83200 28.77100  1.000 92.86000  ? 662 ALA A C      1 
ATOM   4607  O  O      . ALA A 1 671 ? 34.27100  -19.52500 28.47800  1.000 100.58000 ? 662 ALA A O      1 
ATOM   4608  C  CB     . ALA A 1 671 ? 30.99900  -19.75900 28.28500  1.000 75.38000  ? 662 ALA A CB     1 
ATOM   4609  N  N      . LYS A 1 672 ? 33.24800  -17.51500 28.55900  1.000 89.67000  ? 663 LYS A N      1 
ATOM   4610  C  CA     . LYS A 1 672 ? 34.45900  -16.83600 28.12300  1.000 73.83000  ? 663 LYS A CA     1 
ATOM   4611  C  C      . LYS A 1 672 ? 35.57100  -17.03600 29.14000  1.000 73.27000  ? 663 LYS A C      1 
ATOM   4612  O  O      . LYS A 1 672 ? 36.73300  -17.24100 28.77200  1.000 84.16000  ? 663 LYS A O      1 
ATOM   4613  C  CB     . LYS A 1 672 ? 34.18400  -15.34900 27.91700  1.000 81.83000  ? 663 LYS A CB     1 
ATOM   4614  C  CG     . LYS A 1 672 ? 35.32800  -14.60600 27.24300  1.000 97.28000  ? 663 LYS A CG     1 
ATOM   4615  C  CD     . LYS A 1 672 ? 35.10700  -13.10300 27.26100  1.000 80.38000  ? 663 LYS A CD     1 
ATOM   4616  C  CE     . LYS A 1 672 ? 35.05700  -12.58700 28.68700  1.000 69.41000  ? 663 LYS A CE     1 
ATOM   4617  N  NZ     . LYS A 1 672 ? 34.87000  -11.11200 28.77500  1.000 93.66000  ? 663 LYS A NZ     1 
ATOM   4618  N  N      . LYS A 1 673 ? 35.22600  -16.98400 30.42900  1.000 73.29000  ? 664 LYS A N      1 
ATOM   4619  C  CA     . LYS A 1 673 ? 36.21000  -17.27100 31.47100  1.000 71.81000  ? 664 LYS A CA     1 
ATOM   4620  C  C      . LYS A 1 673 ? 36.72000  -18.70600 31.37200  1.000 78.97000  ? 664 LYS A C      1 
ATOM   4621  O  O      . LYS A 1 673 ? 37.90800  -18.97300 31.59600  1.000 84.05000  ? 664 LYS A O      1 
ATOM   4622  C  CB     . LYS A 1 673 ? 35.60700  -17.00000 32.84600  1.000 61.42000  ? 664 LYS A CB     1 
ATOM   4623  C  CG     . LYS A 1 673 ? 35.45600  -15.51200 33.15700  1.000 66.95000  ? 664 LYS A CG     1 
ATOM   4624  C  CD     . LYS A 1 673 ? 34.84000  -15.28800 34.53000  1.000 97.48000  ? 664 LYS A CD     1 
ATOM   4625  C  CE     . LYS A 1 673 ? 35.12100  -13.88000 35.03600  1.000 88.36000  ? 664 LYS A CE     1 
ATOM   4626  N  NZ     . LYS A 1 673 ? 34.64600  -12.81800 34.10500  1.000 93.34000  ? 664 LYS A NZ     1 
ATOM   4627  N  N      . TYR A 1 674 ? 35.82600  -19.64100 31.04800  1.000 72.11000  ? 665 TYR A N      1 
ATOM   4628  C  CA     . TYR A 1 674 ? 36.21300  -21.03800 30.88400  1.000 77.68000  ? 665 TYR A CA     1 
ATOM   4629  C  C      . TYR A 1 674 ? 37.28800  -21.17600 29.82100  1.000 74.90000  ? 665 TYR A C      1 
ATOM   4630  O  O      . TYR A 1 674 ? 38.28900  -21.87600 30.01500  1.000 82.52000  ? 665 TYR A O      1 
ATOM   4631  C  CB     . TYR A 1 674 ? 34.98400  -21.87200 30.51100  1.000 81.95000  ? 665 TYR A CB     1 
ATOM   4632  C  CG     . TYR A 1 674 ? 35.23500  -23.35400 30.29300  1.000 71.86000  ? 665 TYR A CG     1 
ATOM   4633  C  CD1    . TYR A 1 674 ? 35.64200  -23.83300 29.05400  1.000 77.53000  ? 665 TYR A CD1    1 
ATOM   4634  C  CD2    . TYR A 1 674 ? 35.03200  -24.27300 31.31300  1.000 77.31000  ? 665 TYR A CD2    1 
ATOM   4635  C  CE1    . TYR A 1 674 ? 35.86100  -25.18400 28.84700  1.000 102.80000 ? 665 TYR A CE1    1 
ATOM   4636  C  CE2    . TYR A 1 674 ? 35.24700  -25.62400 31.11700  1.000 94.93000  ? 665 TYR A CE2    1 
ATOM   4637  C  CZ     . TYR A 1 674 ? 35.66100  -26.07600 29.88500  1.000 113.10000 ? 665 TYR A CZ     1 
ATOM   4638  O  OH     . TYR A 1 674 ? 35.87400  -27.42500 29.69600  1.000 107.21000 ? 665 TYR A OH     1 
ATOM   4639  N  N      . LEU A 1 675 ? 37.09700  -20.50900 28.68300  1.000 72.01000  ? 666 LEU A N      1 
ATOM   4640  C  CA     . LEU A 1 675 ? 38.13200  -20.55500 27.65400  1.000 60.18000  ? 666 LEU A CA     1 
ATOM   4641  C  C      . LEU A 1 675 ? 39.39500  -19.82700 28.10300  1.000 67.54000  ? 666 LEU A C      1 
ATOM   4642  O  O      . LEU A 1 675 ? 40.50900  -20.30900 27.87000  1.000 73.48000  ? 666 LEU A O      1 
ATOM   4643  C  CB     . LEU A 1 675 ? 37.61500  -19.96600 26.34400  1.000 48.64000  ? 666 LEU A CB     1 
ATOM   4644  C  CG     . LEU A 1 675 ? 38.52500  -20.22800 25.14100  1.000 55.46000  ? 666 LEU A CG     1 
ATOM   4645  C  CD1    . LEU A 1 675 ? 37.71400  -20.32300 23.85700  1.000 65.00000  ? 666 LEU A CD1    1 
ATOM   4646  C  CD2    . LEU A 1 675 ? 39.60500  -19.15600 25.02200  1.000 71.27000  ? 666 LEU A CD2    1 
ATOM   4647  N  N      . GLU A 1 676 ? 39.24400  -18.66600 28.74300  1.000 71.36000  ? 667 GLU A N      1 
ATOM   4648  C  CA     . GLU A 1 676 ? 40.40800  -17.92300 29.21900  1.000 76.79000  ? 667 GLU A CA     1 
ATOM   4649  C  C      . GLU A 1 676 ? 41.15200  -18.68200 30.30800  1.000 83.10000  ? 667 GLU A C      1 
ATOM   4650  O  O      . GLU A 1 676 ? 42.38800  -18.70500 30.33000  1.000 88.04000  ? 667 GLU A O      1 
ATOM   4651  C  CB     . GLU A 1 676 ? 39.99500  -16.54400 29.72700  1.000 83.90000  ? 667 GLU A CB     1 
ATOM   4652  C  CG     . GLU A 1 676 ? 39.50900  -15.59600 28.65500  1.000 74.79000  ? 667 GLU A CG     1 
ATOM   4653  C  CD     . GLU A 1 676 ? 39.23100  -14.21800 29.21000  1.000 79.83000  ? 667 GLU A CD     1 
ATOM   4654  O  OE1    . GLU A 1 676 ? 39.42900  -14.02200 30.42900  1.000 76.12000  ? 667 GLU A OE1    1 
ATOM   4655  O  OE2    . GLU A 1 676 ? 38.83400  -13.32800 28.43000  1.000 85.07000  ? 667 GLU A OE2    1 
ATOM   4656  N  N      . ALA A 1 677 ? 40.40900  -19.31400 31.22000  1.000 85.07000  ? 668 ALA A N      1 
ATOM   4657  C  CA     . ALA A 1 677 ? 41.00600  -20.04800 32.32900  1.000 85.70000  ? 668 ALA A CA     1 
ATOM   4658  C  C      . ALA A 1 677 ? 41.88100  -21.20100 31.87200  1.000 93.52000  ? 668 ALA A C      1 
ATOM   4659  O  O      . ALA A 1 677 ? 42.66600  -21.72200 32.67200  1.000 100.87000 ? 668 ALA A O      1 
ATOM   4660  C  CB     . ALA A 1 677 ? 39.92100  -20.58300 33.25800  1.000 98.17000  ? 668 ALA A CB     1 
ATOM   4661  N  N      . GLY A 1 678 ? 41.76200  -21.61900 30.62000  1.000 90.36000  ? 669 GLY A N      1 
ATOM   4662  C  CA     . GLY A 1 678 ? 42.49000  -22.76700 30.13800  1.000 91.51000  ? 669 GLY A CA     1 
ATOM   4663  C  C      . GLY A 1 678 ? 41.82600  -24.09200 30.41400  1.000 92.70000  ? 669 GLY A C      1 
ATOM   4664  O  O      . GLY A 1 678 ? 42.44900  -25.13800 30.19100  1.000 106.79000 ? 669 GLY A O      1 
ATOM   4665  N  N      . ASN A 1 679 ? 40.58500  -24.08800 30.91100  1.000 101.85000 ? 670 ASN A N      1 
ATOM   4666  C  CA     . ASN A 1 679 ? 39.88400  -25.35200 31.09100  1.000 109.18000 ? 670 ASN A CA     1 
ATOM   4667  C  C      . ASN A 1 679 ? 39.70700  -26.03100 29.74400  1.000 108.54000 ? 670 ASN A C      1 
ATOM   4668  O  O      . ASN A 1 679 ? 39.83200  -27.25600 29.63100  1.000 123.82000 ? 670 ASN A O      1 
ATOM   4669  C  CB     . ASN A 1 679 ? 38.53500  -25.13100 31.77600  1.000 96.70000  ? 670 ASN A CB     1 
ATOM   4670  C  CG     . ASN A 1 679 ? 38.62100  -24.16200 32.94000  1.000 91.64000  ? 670 ASN A CG     1 
ATOM   4671  O  OD1    . ASN A 1 679 ? 38.09700  -23.04900 32.88000  1.000 72.75000  ? 670 ASN A OD1    1 
ATOM   4672  N  ND2    . ASN A 1 679 ? 39.27700  -24.58700 34.01400  1.000 100.89000 ? 670 ASN A ND2    1 
ATOM   4673  N  N      . LEU A 1 680 ? 39.41400  -25.24700 28.71300  1.000 92.74000  ? 671 LEU A N      1 
ATOM   4674  C  CA     . LEU A 1 680 ? 39.42700  -25.74400 27.35000  1.000 89.19000  ? 671 LEU A CA     1 
ATOM   4675  C  C      . LEU A 1 680 ? 40.87700  -25.90100 26.91700  1.000 97.34000  ? 671 LEU A C      1 
ATOM   4676  O  O      . LEU A 1 680 ? 41.71300  -25.03300 27.18300  1.000 100.34000 ? 671 LEU A O      1 
ATOM   4677  C  CB     . LEU A 1 680 ? 38.69800  -24.77700 26.42600  1.000 80.42000  ? 671 LEU A CB     1 
ATOM   4678  C  CG     . LEU A 1 680 ? 38.45000  -25.22700 24.99100  1.000 91.41000  ? 671 LEU A CG     1 
ATOM   4679  C  CD1    . LEU A 1 680 ? 37.75100  -26.57000 24.97000  1.000 85.95000  ? 671 LEU A CD1    1 
ATOM   4680  C  CD2    . LEU A 1 680 ? 37.64700  -24.18200 24.22900  1.000 68.12000  ? 671 LEU A CD2    1 
ATOM   4681  N  N      . GLU A 1 681 ? 41.17500  -26.99900 26.23200  1.000 102.49000 ? 672 GLU A N      1 
ATOM   4682  C  CA     . GLU A 1 681 ? 42.54100  -27.31700 25.83500  1.000 95.56000  ? 672 GLU A CA     1 
ATOM   4683  C  C      . GLU A 1 681 ? 42.73000  -27.17200 24.33300  1.000 84.61000  ? 672 GLU A C      1 
ATOM   4684  O  O      . GLU A 1 681 ? 41.82900  -27.47800 23.54500  1.000 81.97000  ? 672 GLU A O      1 
ATOM   4685  C  CB     . GLU A 1 681 ? 42.93800  -28.72600 26.28600  1.000 96.30000  ? 672 GLU A CB     1 
ATOM   4686  C  CG     . GLU A 1 681 ? 43.30100  -28.78400 27.75500  1.000 96.80000  ? 672 GLU A CG     1 
ATOM   4687  C  CD     . GLU A 1 681 ? 42.14600  -29.20300 28.63300  1.000 124.75000 ? 672 GLU A CD     1 
ATOM   4688  O  OE1    . GLU A 1 681 ? 41.06700  -29.52900 28.09100  1.000 140.84000 ? 672 GLU A OE1    1 
ATOM   4689  O  OE2    . GLU A 1 681 ? 42.31900  -29.19400 29.87100  1.000 104.41000 ? 672 GLU A OE2    1 
ATOM   4690  N  N      . GLY A 1 682 ? 43.90900  -26.67900 23.94900  1.000 85.25000  ? 673 GLY A N      1 
ATOM   4691  C  CA     . GLY A 1 682 ? 44.20800  -26.37000 22.57800  1.000 100.41000 ? 673 GLY A CA     1 
ATOM   4692  C  C      . GLY A 1 682 ? 43.91800  -24.93300 22.21700  1.000 98.94000  ? 673 GLY A C      1 
ATOM   4693  O  O      . GLY A 1 682 ? 44.48800  -24.41300 21.25100  1.000 100.26000 ? 673 GLY A O      1 
ATOM   4694  N  N      . TYR A 1 683 ? 42.99000  -24.30400 22.93200  1.000 104.59000 ? 674 TYR A N      1 
ATOM   4695  C  CA     . TYR A 1 683 ? 42.55800  -22.94200 22.66300  1.000 107.41000 ? 674 TYR A CA     1 
ATOM   4696  C  C      . TYR A 1 683 ? 42.89400  -22.03600 23.84400  1.000 96.59000  ? 674 TYR A C      1 
ATOM   4697  O  O      . TYR A 1 683 ? 42.48200  -22.30800 24.97600  1.000 90.65000  ? 674 TYR A O      1 
ATOM   4698  C  CB     . TYR A 1 683 ? 41.05700  -22.93900 22.37600  1.000 95.31000  ? 674 TYR A CB     1 
ATOM   4699  C  CG     . TYR A 1 683 ? 40.64600  -24.05700 21.43200  1.000 106.93000 ? 674 TYR A CG     1 
ATOM   4700  C  CD1    . TYR A 1 683 ? 40.81300  -23.93200 20.05800  1.000 107.01000 ? 674 TYR A CD1    1 
ATOM   4701  C  CD2    . TYR A 1 683 ? 40.12400  -25.25400 21.92000  1.000 107.90000 ? 674 TYR A CD2    1 
ATOM   4702  C  CE1    . TYR A 1 683 ? 40.44700  -24.95300 19.18900  1.000 85.70000  ? 674 TYR A CE1    1 
ATOM   4703  C  CE2    . TYR A 1 683 ? 39.75600  -26.28100 21.05800  1.000 104.84000 ? 674 TYR A CE2    1 
ATOM   4704  C  CZ     . TYR A 1 683 ? 39.92100  -26.12300 19.69500  1.000 99.73000  ? 674 TYR A CZ     1 
ATOM   4705  O  OH     . TYR A 1 683 ? 39.55600  -27.14000 18.84200  1.000 110.17000 ? 674 TYR A OH     1 
ATOM   4706  N  N      . GLY A 1 684 ? 43.66400  -20.97800 23.58900  1.000 101.51000 ? 675 GLY A N      1 
ATOM   4707  C  CA     . GLY A 1 684 ? 43.97500  -19.98700 24.59300  1.000 94.38000  ? 675 GLY A CA     1 
ATOM   4708  C  C      . GLY A 1 684 ? 43.42000  -18.62800 24.20600  1.000 96.95000  ? 675 GLY A C      1 
ATOM   4709  O  O      . GLY A 1 684 ? 42.81100  -18.45300 23.14700  1.000 88.18000  ? 675 GLY A O      1 
ATOM   4710  N  N      . LYS A 1 685 ? 43.65400  -17.66100 25.08800  1.000 89.08000  ? 676 LYS A N      1 
ATOM   4711  C  CA     . LYS A 1 685 ? 43.16700  -16.31100 24.84600  1.000 86.49000  ? 676 LYS A CA     1 
ATOM   4712  C  C      . LYS A 1 685 ? 43.59800  -15.83200 23.46500  1.000 86.24000  ? 676 LYS A C      1 
ATOM   4713  O  O      . LYS A 1 685 ? 44.71600  -16.09800 23.01700  1.000 115.32000 ? 676 LYS A O      1 
ATOM   4714  C  CB     . LYS A 1 685 ? 43.67900  -15.35800 25.92700  1.000 81.18000  ? 676 LYS A CB     1 
ATOM   4715  C  CG     . LYS A 1 685 ? 42.98000  -14.00400 25.91000  1.000 76.12000  ? 676 LYS A CG     1 
ATOM   4716  C  CD     . LYS A 1 685 ? 43.38000  -13.12300 27.08500  1.000 58.72000  ? 676 LYS A CD     1 
ATOM   4717  C  CE     . LYS A 1 685 ? 43.10000  -13.79100 28.41300  1.000 41.52000  ? 676 LYS A CE     1 
ATOM   4718  N  NZ     . LYS A 1 685 ? 43.56700  -12.94500 29.53900  1.000 40.93000  ? 676 LYS A NZ     1 
ATOM   4719  N  N      . GLY A 1 686 ? 42.69700  -15.11600 22.79400  1.000 93.48000  ? 677 GLY A N      1 
ATOM   4720  C  CA     . GLY A 1 686 ? 42.92500  -14.63300 21.44700  1.000 98.54000  ? 677 GLY A CA     1 
ATOM   4721  C  C      . GLY A 1 686 ? 42.72500  -15.64500 20.34300  1.000 89.54000  ? 677 GLY A C      1 
ATOM   4722  O  O      . GLY A 1 686 ? 43.07300  -15.35500 19.19200  1.000 106.68000 ? 677 GLY A O      1 
ATOM   4723  N  N      . SER A 1 687 ? 42.16200  -16.81300 20.64200  1.000 63.49000  ? 678 SER A N      1 
ATOM   4724  C  CA     . SER A 1 687 ? 41.91000  -17.81200 19.61600  1.000 76.98000  ? 678 SER A CA     1 
ATOM   4725  C  C      . SER A 1 687 ? 40.54800  -17.56700 18.96600  1.000 101.13000 ? 678 SER A C      1 
ATOM   4726  O  O      . SER A 1 687 ? 39.75900  -16.73300 19.41600  1.000 121.91000 ? 678 SER A O      1 
ATOM   4727  C  CB     . SER A 1 687 ? 41.97900  -19.21900 20.20400  1.000 86.37000  ? 678 SER A CB     1 
ATOM   4728  O  OG     . SER A 1 687 ? 40.89500  -19.45700 21.08300  1.000 110.85000 ? 678 SER A OG     1 
ATOM   4729  N  N      . GLU A 1 688 ? 40.27100  -18.31000 17.89200  1.000 92.28000  ? 679 GLU A N      1 
ATOM   4730  C  CA     . GLU A 1 688 ? 38.98500  -18.15300 17.21400  1.000 94.64000  ? 679 GLU A CA     1 
ATOM   4731  C  C      . GLU A 1 688 ? 37.80900  -18.54600 18.09600  1.000 114.83000 ? 679 GLU A C      1 
ATOM   4732  O  O      . GLU A 1 688 ? 36.84000  -17.76700 18.18600  1.000 126.89000 ? 679 GLU A O      1 
ATOM   4733  C  CB     . GLU A 1 688 ? 38.99300  -18.94800 15.90400  1.000 76.69000  ? 679 GLU A CB     1 
ATOM   4734  N  N      . PRO A 1 689 ? 37.82200  -19.69500 18.78300  1.000 107.84000 ? 680 PRO A N      1 
ATOM   4735  C  CA     . PRO A 1 689 ? 36.73500  -19.97100 19.73600  1.000 106.71000 ? 680 PRO A CA     1 
ATOM   4736  C  C      . PRO A 1 689 ? 36.57500  -18.87100 20.77000  1.000 104.15000 ? 680 PRO A C      1 
ATOM   4737  O  O      . PRO A 1 689 ? 35.44200  -18.49900 21.11300  1.000 110.99000 ? 680 PRO A O      1 
ATOM   4738  C  CB     . PRO A 1 689 ? 37.15400  -21.31000 20.36400  1.000 97.01000  ? 680 PRO A CB     1 
ATOM   4739  C  CG     . PRO A 1 689 ? 38.05000  -21.93900 19.34200  1.000 100.85000 ? 680 PRO A CG     1 
ATOM   4740  C  CD     . PRO A 1 689 ? 38.81500  -20.78400 18.75600  1.000 112.72000 ? 680 PRO A CD     1 
ATOM   4741  N  N      . HIS A 1 690 ? 37.68900  -18.35400 21.29700  1.000 87.39000  ? 681 HIS A N      1 
ATOM   4742  C  CA     . HIS A 1 690 ? 37.61200  -17.24700 22.24100  1.000 77.85000  ? 681 HIS A CA     1 
ATOM   4743  C  C      . HIS A 1 690 ? 37.00200  -16.01400 21.59000  1.000 92.87000  ? 681 HIS A C      1 
ATOM   4744  O  O      . HIS A 1 690 ? 36.30900  -15.24000 22.25600  1.000 106.39000 ? 681 HIS A O      1 
ATOM   4745  C  CB     . HIS A 1 690 ? 38.99700  -16.93100 22.80000  1.000 88.08000  ? 681 HIS A CB     1 
ATOM   4746  C  CG     . HIS A 1 690 ? 39.02500  -15.74000 23.70600  1.000 98.72000  ? 681 HIS A CG     1 
ATOM   4747  N  ND1    . HIS A 1 690 ? 38.67700  -15.81100 25.03800  1.000 95.77000  ? 681 HIS A ND1    1 
ATOM   4748  C  CD2    . HIS A 1 690 ? 39.35500  -14.44800 23.47300  1.000 98.27000  ? 681 HIS A CD2    1 
ATOM   4749  C  CE1    . HIS A 1 690 ? 38.79000  -14.61400 25.58600  1.000 69.48000  ? 681 HIS A CE1    1 
ATOM   4750  N  NE2    . HIS A 1 690 ? 39.20100  -13.77000 24.65800  1.000 80.02000  ? 681 HIS A NE2    1 
ATOM   4751  N  N      . LYS A 1 691 ? 37.25900  -15.80400 20.29700  1.000 98.31000  ? 682 LYS A N      1 
ATOM   4752  C  CA     . LYS A 1 691 ? 36.64100  -14.67800 19.60500  1.000 102.45000 ? 682 LYS A CA     1 
ATOM   4753  C  C      . LYS A 1 691 ? 35.12500  -14.83500 19.58300  1.000 106.69000 ? 682 LYS A C      1 
ATOM   4754  O  O      . LYS A 1 691 ? 34.37800  -13.89100 19.88200  1.000 107.04000 ? 682 LYS A O      1 
ATOM   4755  C  CB     . LYS A 1 691 ? 37.18400  -14.56800 18.17700  1.000 106.19000 ? 682 LYS A CB     1 
ATOM   4756  C  CG     . LYS A 1 691 ? 38.69700  -14.41400 18.04000  1.000 122.04000 ? 682 LYS A CG     1 
ATOM   4757  C  CD     . LYS A 1 691 ? 39.05800  -14.07400 16.59100  1.000 104.75000 ? 682 LYS A CD     1 
ATOM   4758  C  CE     . LYS A 1 691 ? 40.56100  -14.08800 16.35900  1.000 99.91000  ? 682 LYS A CE     1 
ATOM   4759  N  NZ     . LYS A 1 691 ? 41.12400  -15.46800 16.38800  1.000 116.74000 ? 682 LYS A NZ     1 
ATOM   4760  N  N      . ALA A 1 692 ? 34.65200  -16.03600 19.24300  1.000 109.02000 ? 683 ALA A N      1 
ATOM   4761  C  CA     . ALA A 1 692 ? 33.21500  -16.28700 19.26100  1.000 108.49000 ? 683 ALA A CA     1 
ATOM   4762  C  C      . ALA A 1 692 ? 32.63800  -16.03100 20.64700  1.000 98.65000  ? 683 ALA A C      1 
ATOM   4763  O  O      . ALA A 1 692 ? 31.60900  -15.35500 20.79600  1.000 117.51000 ? 683 ALA A O      1 
ATOM   4764  C  CB     . ALA A 1 692 ? 32.92600  -17.71900 18.80900  1.000 98.19000  ? 683 ALA A CB     1 
ATOM   4765  N  N      . LEU A 1 693 ? 33.30600  -16.54700 21.68100  1.000 85.48000  ? 684 LEU A N      1 
ATOM   4766  C  CA     . LEU A 1 693 ? 32.79200  -16.39000 23.03800  1.000 90.56000  ? 684 LEU A CA     1 
ATOM   4767  C  C      . LEU A 1 693 ? 32.76500  -14.92300 23.46300  1.000 99.11000  ? 684 LEU A C      1 
ATOM   4768  O  O      . LEU A 1 693 ? 31.80900  -14.47100 24.10600  1.000 109.05000 ? 684 LEU A O      1 
ATOM   4769  C  CB     . LEU A 1 693 ? 33.61600  -17.23300 24.01300  1.000 82.22000  ? 684 LEU A CB     1 
ATOM   4770  C  CG     . LEU A 1 693 ? 33.45800  -18.75100 23.87800  1.000 80.25000  ? 684 LEU A CG     1 
ATOM   4771  C  CD1    . LEU A 1 693 ? 34.44200  -19.49400 24.77500  1.000 81.49000  ? 684 LEU A CD1    1 
ATOM   4772  C  CD2    . LEU A 1 693 ? 32.03200  -19.16900 24.18800  1.000 81.71000  ? 684 LEU A CD2    1 
ATOM   4773  N  N      . VAL A 1 694 ? 33.80200  -14.15900 23.11200  1.000 82.84000  ? 685 VAL A N      1 
ATOM   4774  C  CA     . VAL A 1 694 ? 33.86300  -12.75900 23.51900  1.000 81.33000  ? 685 VAL A CA     1 
ATOM   4775  C  C      . VAL A 1 694 ? 32.81100  -11.94100 22.78600  1.000 85.90000  ? 685 VAL A C      1 
ATOM   4776  O  O      . VAL A 1 694 ? 32.23800  -11.00100 23.34500  1.000 89.58000  ? 685 VAL A O      1 
ATOM   4777  C  CB     . VAL A 1 694 ? 35.27500  -12.19500 23.28900  1.000 90.31000  ? 685 VAL A CB     1 
ATOM   4778  C  CG1    . VAL A 1 694 ? 35.59800  -12.15500 21.80200  1.000 109.85000 ? 685 VAL A CG1    1 
ATOM   4779  C  CG2    . VAL A 1 694 ? 35.41700  -10.81800 23.92100  1.000 100.70000 ? 685 VAL A CG2    1 
ATOM   4780  N  N      . ILE A 1 695 ? 32.54800  -12.26400 21.52000  1.000 88.24000  ? 686 ILE A N      1 
ATOM   4781  C  CA     . ILE A 1 695 ? 31.49600  -11.54600 20.80800  1.000 94.64000  ? 686 ILE A CA     1 
ATOM   4782  C  C      . ILE A 1 695 ? 30.14800  -11.83300 21.45000  1.000 82.07000  ? 686 ILE A C      1 
ATOM   4783  O  O      . ILE A 1 695 ? 29.33300  -10.92200 21.68400  1.000 73.87000  ? 686 ILE A O      1 
ATOM   4784  C  CB     . ILE A 1 695 ? 31.50800  -11.92700 19.31800  1.000 111.79000 ? 686 ILE A CB     1 
ATOM   4785  C  CG1    . ILE A 1 695 ? 32.76900  -11.38800 18.64600  1.000 117.21000 ? 686 ILE A CG1    1 
ATOM   4786  C  CG2    . ILE A 1 695 ? 30.26300  -11.40100 18.61700  1.000 119.67000 ? 686 ILE A CG2    1 
ATOM   4787  C  CD1    . ILE A 1 695 ? 32.94100  -11.85200 17.21900  1.000 126.55000 ? 686 ILE A CD1    1 
ATOM   4788  N  N      . GLY A 1 696 ? 29.90800  -13.09900 21.78800  1.000 78.27000  ? 687 GLY A N      1 
ATOM   4789  C  CA     . GLY A 1 696 ? 28.67000  -13.42500 22.45900  1.000 77.14000  ? 687 GLY A CA     1 
ATOM   4790  C  C      . GLY A 1 696 ? 28.55600  -12.73500 23.80100  1.000 88.67000  ? 687 GLY A C      1 
ATOM   4791  O  O      . GLY A 1 696 ? 27.46100  -12.35100 24.21500  1.000 94.02000  ? 687 GLY A O      1 
ATOM   4792  N  N      . ASP A 1 697 ? 29.69000  -12.51000 24.46800  1.000 89.96000  ? 688 ASP A N      1 
ATOM   4793  C  CA     . ASP A 1 697 ? 29.66900  -11.81000 25.74900  1.000 80.62000  ? 688 ASP A CA     1 
ATOM   4794  C  C      . ASP A 1 697 ? 29.37700  -10.32300 25.58800  1.000 78.75000  ? 688 ASP A C      1 
ATOM   4795  O  O      . ASP A 1 697 ? 28.67700  -9.73300  26.41600  1.000 87.30000  ? 688 ASP A O      1 
ATOM   4796  C  CB     . ASP A 1 697 ? 30.99300  -12.02000 26.47700  1.000 85.07000  ? 688 ASP A CB     1 
ATOM   4797  C  CG     . ASP A 1 697 ? 31.00500  -11.40600 27.86600  1.000 83.02000  ? 688 ASP A CG     1 
ATOM   4798  O  OD1    . ASP A 1 697 ? 29.97900  -10.83600 28.29100  1.000 80.41000  ? 688 ASP A OD1    1 
ATOM   4799  O  OD2    . ASP A 1 697 ? 32.05300  -11.49100 28.53700  1.000 106.13000 ? 688 ASP A OD2    1 
ATOM   4800  N  N      . THR A 1 698 ? 29.94100  -9.69000  24.55900  1.000 81.00000  ? 689 THR A N      1 
ATOM   4801  C  CA     . THR A 1 698 ? 29.58500  -8.30200  24.29100  1.000 81.15000  ? 689 THR A CA     1 
ATOM   4802  C  C      . THR A 1 698 ? 28.10100  -8.17300  23.99100  1.000 82.19000  ? 689 THR A C      1 
ATOM   4803  O  O      . THR A 1 698 ? 27.48900  -7.14300  24.29800  1.000 82.93000  ? 689 THR A O      1 
ATOM   4804  C  CB     . THR A 1 698 ? 30.40500  -7.74600  23.12600  1.000 92.14000  ? 689 THR A CB     1 
ATOM   4805  O  OG1    . THR A 1 698 ? 31.80100  -7.78300  23.45300  1.000 94.99000  ? 689 THR A OG1    1 
ATOM   4806  C  CG2    . THR A 1 698 ? 29.98300  -6.31900  22.81400  1.000 100.42000 ? 689 THR A CG2    1 
ATOM   4807  N  N      . VAL A 1 699 ? 27.49800  -9.21200  23.40900  1.000 78.78000  ? 690 VAL A N      1 
ATOM   4808  C  CA     . VAL A 1 699 ? 26.05400  -9.15700  23.20300  1.000 54.35000  ? 690 VAL A CA     1 
ATOM   4809  C  C      . VAL A 1 699 ? 25.33800  -9.36200  24.53400  1.000 49.05000  ? 690 VAL A C      1 
ATOM   4810  O  O      . VAL A 1 699 ? 24.32200  -8.71600  24.81100  1.000 61.92000  ? 690 VAL A O      1 
ATOM   4811  C  CB     . VAL A 1 699 ? 25.57900  -10.17600 22.15500  1.000 53.91000  ? 690 VAL A CB     1 
ATOM   4812  C  CG1    . VAL A 1 699 ? 24.07200  -10.09400 22.02600  1.000 36.38000  ? 690 VAL A CG1    1 
ATOM   4813  C  CG2    . VAL A 1 699 ? 26.23800  -9.91100  20.81900  1.000 79.84000  ? 690 VAL A CG2    1 
ATOM   4814  N  N      . GLY A 1 700 ? 25.85600  -10.25800 25.37600  1.000 54.71000  ? 691 GLY A N      1 
ATOM   4815  C  CA     . GLY A 1 700 ? 25.18500  -10.57500 26.62500  1.000 64.01000  ? 691 GLY A CA     1 
ATOM   4816  C  C      . GLY A 1 700 ? 25.23600  -9.46500  27.65800  1.000 77.80000  ? 691 GLY A C      1 
ATOM   4817  O  O      . GLY A 1 700 ? 24.30600  -9.31800  28.45500  1.000 85.67000  ? 691 GLY A O      1 
ATOM   4818  N  N      . ASP A 1 701 ? 26.31800  -8.68000  27.66600  1.000 78.95000  ? 692 ASP A N      1 
ATOM   4819  C  CA     . ASP A 1 701 ? 26.54700  -7.64800  28.67600  1.000 77.83000  ? 692 ASP A CA     1 
ATOM   4820  C  C      . ASP A 1 701 ? 25.35500  -6.71000  28.81300  1.000 76.55000  ? 692 ASP A C      1 
ATOM   4821  O  O      . ASP A 1 701 ? 24.76300  -6.60400  29.89700  1.000 83.36000  ? 692 ASP A O      1 
ATOM   4822  C  CB     . ASP A 1 701 ? 27.79300  -6.82900  28.33600  1.000 85.21000  ? 692 ASP A CB     1 
ATOM   4823  C  CG     . ASP A 1 701 ? 29.05400  -7.43600  28.89400  1.000 88.27000  ? 692 ASP A CG     1 
ATOM   4824  O  OD1    . ASP A 1 701 ? 29.34000  -7.19400  30.08500  1.000 82.67000  ? 692 ASP A OD1    1 
ATOM   4825  O  OD2    . ASP A 1 701 ? 29.77000  -8.14000  28.14800  1.000 108.01000 ? 692 ASP A OD2    1 
ATOM   4826  N  N      . PRO A 1 702 ? 24.98800  -5.99500  27.75100  1.000 68.83000  ? 693 PRO A N      1 
ATOM   4827  C  CA     . PRO A 1 702 ? 23.85800  -5.06600  27.87300  1.000 72.60000  ? 693 PRO A CA     1 
ATOM   4828  C  C      . PRO A 1 702 ? 22.57300  -5.76600  28.25700  1.000 74.58000  ? 693 PRO A C      1 
ATOM   4829  O  O      . PRO A 1 702 ? 21.72800  -5.16900  28.93600  1.000 76.37000  ? 693 PRO A O      1 
ATOM   4830  C  CB     . PRO A 1 702 ? 23.78100  -4.43000  26.47700  1.000 80.88000  ? 693 PRO A CB     1 
ATOM   4831  C  CG     . PRO A 1 702 ? 25.16200  -4.61000  25.91000  1.000 75.72000  ? 693 PRO A CG     1 
ATOM   4832  C  CD     . PRO A 1 702 ? 25.59100  -5.95200  26.41000  1.000 69.78000  ? 693 PRO A CD     1 
ATOM   4833  N  N      . LEU A 1 703 ? 22.41500  -7.03100  27.87100  1.000 61.94000  ? 694 LEU A N      1 
ATOM   4834  C  CA     . LEU A 1 703 ? 21.18200  -7.73900  28.18500  1.000 69.05000  ? 694 LEU A CA     1 
ATOM   4835  C  C      . LEU A 1 703 ? 21.11900  -8.09500  29.66400  1.000 71.03000  ? 694 LEU A C      1 
ATOM   4836  O  O      . LEU A 1 703 ? 20.06200  -7.97800  30.29600  1.000 77.90000  ? 694 LEU A O      1 
ATOM   4837  C  CB     . LEU A 1 703 ? 21.06400  -8.99100  27.31700  1.000 54.41000  ? 694 LEU A CB     1 
ATOM   4838  C  CG     . LEU A 1 703 ? 20.97400  -8.75800  25.80700  1.000 52.93000  ? 694 LEU A CG     1 
ATOM   4839  C  CD1    . LEU A 1 703 ? 20.84800  -10.07800 25.05700  1.000 34.58000  ? 694 LEU A CD1    1 
ATOM   4840  C  CD2    . LEU A 1 703 ? 19.81000  -7.83200  25.48000  1.000 65.53000  ? 694 LEU A CD2    1 
ATOM   4841  N  N      . LYS A 1 704 ? 22.24200  -8.50800  30.24100  1.000 56.92000  ? 695 LYS A N      1 
ATOM   4842  C  CA     . LYS A 1 704 ? 22.22600  -8.97100  31.62000  1.000 62.30000  ? 695 LYS A CA     1 
ATOM   4843  C  C      . LYS A 1 704 ? 22.36900  -7.84000  32.62900  1.000 71.54000  ? 695 LYS A C      1 
ATOM   4844  O  O      . LYS A 1 704 ? 21.87000  -7.96100  33.75400  1.000 73.64000  ? 695 LYS A O      1 
ATOM   4845  C  CB     . LYS A 1 704 ? 23.34900  -9.98700  31.83800  1.000 78.21000  ? 695 LYS A CB     1 
ATOM   4846  C  CG     . LYS A 1 704 ? 24.74200  -9.40400  31.66500  1.000 74.19000  ? 695 LYS A CG     1 
ATOM   4847  C  CD     . LYS A 1 704 ? 25.79600  -10.29800 32.29600  1.000 70.02000  ? 695 LYS A CD     1 
ATOM   4848  C  CE     . LYS A 1 704 ? 27.17600  -10.05700 31.70100  1.000 81.47000  ? 695 LYS A CE     1 
ATOM   4849  N  NZ     . LYS A 1 704 ? 27.70700  -8.70600  32.03600  1.000 80.33000  ? 695 LYS A NZ     1 
ATOM   4850  N  N      . ASP A 1 705 ? 23.00500  -6.73000  32.25000  1.000 70.93000  ? 696 ASP A N      1 
ATOM   4851  C  CA     . ASP A 1 705 ? 23.25300  -5.64800  33.19200  1.000 73.38000  ? 696 ASP A CA     1 
ATOM   4852  C  C      . ASP A 1 705 ? 22.31900  -4.45800  33.01500  1.000 60.42000  ? 696 ASP A C      1 
ATOM   4853  O  O      . ASP A 1 705 ? 22.32300  -3.56100  33.86400  1.000 76.46000  ? 696 ASP A O      1 
ATOM   4854  C  CB     . ASP A 1 705 ? 24.71400  -5.17500  33.09500  1.000 88.25000  ? 696 ASP A CB     1 
ATOM   4855  C  CG     . ASP A 1 705 ? 25.70400  -6.26700  33.46500  1.000 97.41000  ? 696 ASP A CG     1 
ATOM   4856  O  OD1    . ASP A 1 705 ? 25.32900  -7.16400  34.25000  1.000 117.26000 ? 696 ASP A OD1    1 
ATOM   4857  O  OD2    . ASP A 1 705 ? 26.85700  -6.22400  32.98500  1.000 95.11000  ? 696 ASP A OD2    1 
ATOM   4858  N  N      . THR A 1 706 ? 21.52500  -4.42300  31.94700  1.000 51.76000  ? 697 THR A N      1 
ATOM   4859  C  CA     . THR A 1 706 ? 20.57500  -3.33900  31.72100  1.000 65.63000  ? 697 THR A CA     1 
ATOM   4860  C  C      . THR A 1 706 ? 19.16500  -3.86500  31.49600  1.000 63.65000  ? 697 THR A C      1 
ATOM   4861  O  O      . THR A 1 706 ? 18.24300  -3.47200  32.22000  1.000 54.14000  ? 697 THR A O      1 
ATOM   4862  C  CB     . THR A 1 706 ? 21.04800  -2.47300  30.54500  1.000 71.71000  ? 697 THR A CB     1 
ATOM   4863  O  OG1    . THR A 1 706 ? 22.35900  -1.97300  30.82700  1.000 68.42000  ? 697 THR A OG1    1 
ATOM   4864  C  CG2    . THR A 1 706 ? 20.10900  -1.30800  30.30200  1.000 80.29000  ? 697 THR A CG2    1 
ATOM   4865  N  N      . VAL A 1 707 ? 18.96800  -4.75300  30.51900  1.000 54.07000  ? 698 VAL A N      1 
ATOM   4866  C  CA     . VAL A 1 707 ? 17.61600  -5.17800  30.16300  1.000 51.20000  ? 698 VAL A CA     1 
ATOM   4867  C  C      . VAL A 1 707 ? 16.94300  -5.87700  31.34200  1.000 64.52000  ? 698 VAL A C      1 
ATOM   4868  O  O      . VAL A 1 707 ? 15.83700  -5.50800  31.74800  1.000 82.30000  ? 698 VAL A O      1 
ATOM   4869  C  CB     . VAL A 1 707 ? 17.64400  -6.05600  28.89700  1.000 51.40000  ? 698 VAL A CB     1 
ATOM   4870  C  CG1    . VAL A 1 707 ? 16.28500  -6.68700  28.63400  1.000 55.44000  ? 698 VAL A CG1    1 
ATOM   4871  C  CG2    . VAL A 1 707 ? 18.10000  -5.21800  27.70300  1.000 60.29000  ? 698 VAL A CG2    1 
ATOM   4872  N  N      . GLY A 1 708 ? 17.60300  -6.87900  31.92400  1.000 53.31000  ? 699 GLY A N      1 
ATOM   4873  C  CA     . GLY A 1 708 ? 17.02900  -7.62000  33.02700  1.000 55.48000  ? 699 GLY A CA     1 
ATOM   4874  C  C      . GLY A 1 708 ? 16.65900  -6.78200  34.24100  1.000 67.29000  ? 699 GLY A C      1 
ATOM   4875  O  O      . GLY A 1 708 ? 15.50400  -6.77000  34.69500  1.000 85.72000  ? 699 GLY A O      1 
ATOM   4876  N  N      . PRO A 1 709 ? 17.64100  -6.09100  34.81900  1.000 56.77000  ? 700 PRO A N      1 
ATOM   4877  C  CA     . PRO A 1 709 ? 17.33700  -5.30900  36.02700  1.000 70.17000  ? 700 PRO A CA     1 
ATOM   4878  C  C      . PRO A 1 709 ? 16.31900  -4.21700  35.76800  1.000 68.06000  ? 700 PRO A C      1 
ATOM   4879  O  O      . PRO A 1 709 ? 15.43500  -3.96800  36.60700  1.000 88.02000  ? 700 PRO A O      1 
ATOM   4880  C  CB     . PRO A 1 709 ? 18.70300  -4.72600  36.40900  1.000 87.83000  ? 700 PRO A CB     1 
ATOM   4881  C  CG     . PRO A 1 709 ? 19.68400  -5.71600  35.85100  1.000 88.14000  ? 700 PRO A CG     1 
ATOM   4882  C  CD     . PRO A 1 709 ? 19.08600  -6.15300  34.54300  1.000 60.31000  ? 700 PRO A CD     1 
ATOM   4883  N  N      . SER A 1 710 ? 16.32000  -3.66400  34.56000  1.000 55.97000  ? 701 SER A N      1 
ATOM   4884  C  CA     . SER A 1 710 ? 15.35000  -2.63100  34.25500  1.000 53.13000  ? 701 SER A CA     1 
ATOM   4885  C  C      . SER A 1 710 ? 13.97800  -3.24100  34.06600  1.000 54.78000  ? 701 SER A C      1 
ATOM   4886  O  O      . SER A 1 710 ? 12.96800  -2.58500  34.32500  1.000 54.14000  ? 701 SER A O      1 
ATOM   4887  C  CB     . SER A 1 710 ? 15.77500  -1.86600  33.00300  1.000 40.10000  ? 701 SER A CB     1 
ATOM   4888  O  OG     . SER A 1 710 ? 17.08900  -1.34400  33.12300  1.000 71.64000  ? 701 SER A OG     1 
ATOM   4889  N  N      . LEU A 1 711 ? 13.92500  -4.49300  33.62600  1.000 50.18000  ? 702 LEU A N      1 
ATOM   4890  C  CA     . LEU A 1 711 ? 12.64200  -5.16800  33.53000  1.000 42.84000  ? 702 LEU A CA     1 
ATOM   4891  C  C      . LEU A 1 711 ? 12.07200  -5.41400  34.92100  1.000 58.01000  ? 702 LEU A C      1 
ATOM   4892  O  O      . LEU A 1 711 ? 10.86000  -5.27100  35.14000  1.000 67.72000  ? 702 LEU A O      1 
ATOM   4893  C  CB     . LEU A 1 711 ? 12.79600  -6.46300  32.73900  1.000 35.55000  ? 702 LEU A CB     1 
ATOM   4894  C  CG     . LEU A 1 711 ? 12.78200  -6.26900  31.22000  1.000 39.16000  ? 702 LEU A CG     1 
ATOM   4895  C  CD1    . LEU A 1 711 ? 12.93100  -7.60400  30.52500  1.000 74.05000  ? 702 LEU A CD1    1 
ATOM   4896  C  CD2    . LEU A 1 711 ? 11.50900  -5.56900  30.75300  1.000 38.80000  ? 702 LEU A CD2    1 
ATOM   4897  N  N      . ASP A 1 712 ? 12.93500  -5.76800  35.87900  1.000 52.65000  ? 703 ASP A N      1 
ATOM   4898  C  CA     . ASP A 1 712 ? 12.45100  -5.93100  37.25100  1.000 48.72000  ? 703 ASP A CA     1 
ATOM   4899  C  C      . ASP A 1 712 ? 11.83200  -4.63100  37.74000  1.000 68.80000  ? 703 ASP A C      1 
ATOM   4900  O  O      . ASP A 1 712 ? 10.68700  -4.60100  38.23400  1.000 83.23000  ? 703 ASP A O      1 
ATOM   4901  C  CB     . ASP A 1 712 ? 13.59800  -6.32000  38.18800  1.000 43.15000  ? 703 ASP A CB     1 
ATOM   4902  C  CG     . ASP A 1 712 ? 14.45000  -7.43700  37.64300  1.000 71.93000  ? 703 ASP A CG     1 
ATOM   4903  O  OD1    . ASP A 1 712 ? 13.95900  -8.18100  36.76900  1.000 104.21000 ? 703 ASP A OD1    1 
ATOM   4904  O  OD2    . ASP A 1 712 ? 15.62200  -7.55400  38.06900  1.000 80.36000  ? 703 ASP A OD2    1 
ATOM   4905  N  N      . ILE A 1 713 ? 12.56000  -3.53000  37.52900  1.000 69.47000  ? 704 ILE A N      1 
ATOM   4906  C  CA     . ILE A 1 713 ? 12.07400  -2.21400  37.93000  1.000 61.40000  ? 704 ILE A CA     1 
ATOM   4907  C  C      . ILE A 1 713 ? 10.76500  -1.88700  37.22400  1.000 71.70000  ? 704 ILE A C      1 
ATOM   4908  O  O      . ILE A 1 713 ? 9.82200   -1.37400  37.84000  1.000 81.63000  ? 704 ILE A O      1 
ATOM   4909  C  CB     . ILE A 1 713 ? 13.14900  -1.14700  37.64800  1.000 61.74000  ? 704 ILE A CB     1 
ATOM   4910  C  CG1    . ILE A 1 713 ? 14.46000  -1.49400  38.35900  1.000 90.54000  ? 704 ILE A CG1    1 
ATOM   4911  C  CG2    . ILE A 1 713 ? 12.65600  0.23000   38.05400  1.000 82.25000  ? 704 ILE A CG2    1 
ATOM   4912  C  CD1    . ILE A 1 713 ? 14.35100  -1.52700  39.86700  1.000 104.94000 ? 704 ILE A CD1    1 
ATOM   4913  N  N      . LEU A 1 714 ? 10.69000  -2.16200  35.92000  1.000 66.14000  ? 705 LEU A N      1 
ATOM   4914  C  CA     . LEU A 1 714 ? 9.47900   -1.87300  35.16000  1.000 48.48000  ? 705 LEU A CA     1 
ATOM   4915  C  C      . LEU A 1 714 ? 8.27400   -2.57400  35.76600  1.000 38.36000  ? 705 LEU A C      1 
ATOM   4916  O  O      . LEU A 1 714 ? 7.25000   -1.94000  36.05000  1.000 52.13000  ? 705 LEU A O      1 
ATOM   4917  C  CB     . LEU A 1 714 ? 9.66500   -2.27400  33.69300  1.000 47.05000  ? 705 LEU A CB     1 
ATOM   4918  C  CG     . LEU A 1 714 ? 8.61300   -1.79100  32.68000  1.000 44.15000  ? 705 LEU A CG     1 
ATOM   4919  C  CD1    . LEU A 1 714 ? 9.03800   -2.11400  31.25500  1.000 37.26000  ? 705 LEU A CD1    1 
ATOM   4920  C  CD2    . LEU A 1 714 ? 7.22400   -2.35900  32.94500  1.000 48.62000  ? 705 LEU A CD2    1 
ATOM   4921  N  N      . ILE A 1 715 ? 8.37400   -3.88700  35.97300  1.000 44.45000  ? 706 ILE A N      1 
ATOM   4922  C  CA     . ILE A 1 715 ? 7.20500   -4.62600  36.44200  1.000 53.89000  ? 706 ILE A CA     1 
ATOM   4923  C  C      . ILE A 1 715 ? 6.74900   -4.07700  37.78700  1.000 59.31000  ? 706 ILE A C      1 
ATOM   4924  O  O      . ILE A 1 715 ? 5.56400   -3.75800  37.98400  1.000 64.37000  ? 706 ILE A O      1 
ATOM   4925  C  CB     . ILE A 1 715 ? 7.49600   -6.13800  36.50100  1.000 51.82000  ? 706 ILE A CB     1 
ATOM   4926  C  CG1    . ILE A 1 715 ? 8.55300   -6.45600  37.56000  1.000 64.95000  ? 706 ILE A CG1    1 
ATOM   4927  C  CG2    . ILE A 1 715 ? 7.92900   -6.65900  35.14200  1.000 49.43000  ? 706 ILE A CG2    1 
ATOM   4928  C  CD1    . ILE A 1 715 ? 9.09400   -7.87100  37.47600  1.000 67.72000  ? 706 ILE A CD1    1 
ATOM   4929  N  N      . LYS A 1 716 ? 7.69500   -3.88000  38.71000  1.000 57.57000  ? 707 LYS A N      1 
ATOM   4930  C  CA     . LYS A 1 716 ? 7.27600   -3.46300  40.04400  1.000 71.97000  ? 707 LYS A CA     1 
ATOM   4931  C  C      . LYS A 1 716 ? 6.69100   -2.04600  40.03100  1.000 84.11000  ? 707 LYS A C      1 
ATOM   4932  O  O      . LYS A 1 716 ? 5.64300   -1.79000  40.64900  1.000 72.89000  ? 707 LYS A O      1 
ATOM   4933  C  CB     . LYS A 1 716 ? 8.45000   -3.58400  41.01300  1.000 73.10000  ? 707 LYS A CB     1 
ATOM   4934  C  CG     . LYS A 1 716 ? 8.90100   -5.02700  41.20400  1.000 74.36000  ? 707 LYS A CG     1 
ATOM   4935  C  CD     . LYS A 1 716 ? 9.57800   -5.23600  42.54600  1.000 89.73000  ? 707 LYS A CD     1 
ATOM   4936  C  CE     . LYS A 1 716 ? 10.80900  -4.36100  42.69600  1.000 92.33000  ? 707 LYS A CE     1 
ATOM   4937  N  NZ     . LYS A 1 716 ? 11.71400  -4.47400  41.52300  1.000 97.04000  ? 707 LYS A NZ     1 
ATOM   4938  N  N      . ILE A 1 717 ? 7.32500   -1.11900  39.30600  1.000 83.94000  ? 708 ILE A N      1 
ATOM   4939  C  CA     . ILE A 1 717 ? 6.84700   0.26000   39.30100  1.000 68.82000  ? 708 ILE A CA     1 
ATOM   4940  C  C      . ILE A 1 717 ? 5.49400   0.36900   38.61400  1.000 72.31000  ? 708 ILE A C      1 
ATOM   4941  O  O      . ILE A 1 717 ? 4.65100   1.18300   39.00900  1.000 77.81000  ? 708 ILE A O      1 
ATOM   4942  C  CB     . ILE A 1 717 ? 7.87600   1.19400   38.64400  1.000 60.19000  ? 708 ILE A CB     1 
ATOM   4943  C  CG1    . ILE A 1 717 ? 7.45500   2.64800   38.87000  1.000 70.29000  ? 708 ILE A CG1    1 
ATOM   4944  C  CG2    . ILE A 1 717 ? 7.97900   0.89800   37.16000  1.000 56.16000  ? 708 ILE A CG2    1 
ATOM   4945  C  CD1    . ILE A 1 717 ? 8.44600   3.66900   38.36700  1.000 95.37000  ? 708 ILE A CD1    1 
ATOM   4946  N  N      . MET A 1 718 ? 5.27100   -0.40700  37.55100  1.000 80.53000  ? 709 MET A N      1 
ATOM   4947  C  CA     . MET A 1 718 ? 3.95800   -0.37400  36.92100  1.000 65.94000  ? 709 MET A CA     1 
ATOM   4948  C  C      . MET A 1 718 ? 2.89700   -0.89500  37.88000  1.000 73.17000  ? 709 MET A C      1 
ATOM   4949  O  O      . MET A 1 718 ? 1.80200   -0.32100  37.98000  1.000 67.22000  ? 709 MET A O      1 
ATOM   4950  C  CB     . MET A 1 718 ? 3.97100   -1.16800  35.61200  1.000 60.04000  ? 709 MET A CB     1 
ATOM   4951  C  CG     . MET A 1 718 ? 2.75100   -0.92500  34.72800  1.000 61.54000  ? 709 MET A CG     1 
ATOM   4952  S  SD     . MET A 1 718 ? 2.92400   -1.59400  33.05900  1.000 68.31000  ? 709 MET A SD     1 
ATOM   4953  C  CE     . MET A 1 718 ? 4.29900   -0.62200  32.44200  1.000 58.94000  ? 709 MET A CE     1 
ATOM   4954  N  N      . SER A 1 719 ? 3.21800   -1.95600  38.63400  1.000 69.29000  ? 710 SER A N      1 
ATOM   4955  C  CA     . SER A 1 719 ? 2.27300   -2.42600  39.64400  1.000 59.55000  ? 710 SER A CA     1 
ATOM   4956  C  C      . SER A 1 719 ? 1.92700   -1.31300  40.62400  1.000 66.36000  ? 710 SER A C      1 
ATOM   4957  O  O      . SER A 1 719 ? 0.75100   -1.10000  40.94900  1.000 68.19000  ? 710 SER A O      1 
ATOM   4958  C  CB     . SER A 1 719 ? 2.83900   -3.63400  40.39400  1.000 47.40000  ? 710 SER A CB     1 
ATOM   4959  O  OG     . SER A 1 719 ? 2.98900   -4.76000  39.54700  1.000 62.34000  ? 710 SER A OG     1 
ATOM   4960  N  N      . VAL A 1 720 ? 2.93600   -0.57100  41.08100  1.000 70.35000  ? 711 VAL A N      1 
ATOM   4961  C  CA     . VAL A 1 720 ? 2.69200   0.46800   42.08300  1.000 69.29000  ? 711 VAL A CA     1 
ATOM   4962  C  C      . VAL A 1 720 ? 1.84500   1.59700   41.50200  1.000 66.94000  ? 711 VAL A C      1 
ATOM   4963  O  O      . VAL A 1 720 ? 0.85600   2.03400   42.11000  1.000 66.66000  ? 711 VAL A O      1 
ATOM   4964  C  CB     . VAL A 1 720 ? 4.02400   0.99900   42.63900  1.000 71.66000  ? 711 VAL A CB     1 
ATOM   4965  C  CG1    . VAL A 1 720 ? 3.78100   2.21100   43.52600  1.000 59.74000  ? 711 VAL A CG1    1 
ATOM   4966  C  CG2    . VAL A 1 720 ? 4.74400   -0.09100  43.40900  1.000 102.61000 ? 711 VAL A CG2    1 
ATOM   4967  N  N      . VAL A 1 721 ? 2.23700   2.10300   40.33000  1.000 63.46000  ? 712 VAL A N      1 
ATOM   4968  C  CA     . VAL A 1 721 ? 1.51200   3.20900   39.70800  1.000 57.79000  ? 712 VAL A CA     1 
ATOM   4969  C  C      . VAL A 1 721 ? 0.05600   2.83500   39.47300  1.000 68.61000  ? 712 VAL A C      1 
ATOM   4970  O  O      . VAL A 1 721 ? -0.85200  3.65000   39.68600  1.000 67.15000  ? 712 VAL A O      1 
ATOM   4971  C  CB     . VAL A 1 721 ? 2.20500   3.63000   38.40100  1.000 55.74000  ? 712 VAL A CB     1 
ATOM   4972  C  CG1    . VAL A 1 721 ? 1.33500   4.60800   37.62800  1.000 60.24000  ? 712 VAL A CG1    1 
ATOM   4973  C  CG2    . VAL A 1 721 ? 3.56100   4.24100   38.70200  1.000 64.51000  ? 712 VAL A CG2    1 
ATOM   4974  N  N      . SER A 1 722 ? -0.19500  1.60200   39.02700  1.000 69.76000  ? 713 SER A N      1 
ATOM   4975  C  CA     . SER A 1 722 ? -1.57600  1.18400   38.82700  1.000 48.23000  ? 713 SER A CA     1 
ATOM   4976  C  C      . SER A 1 722 ? -2.31400  1.09300   40.15600  1.000 55.98000  ? 713 SER A C      1 
ATOM   4977  O  O      . SER A 1 722 ? -3.46600  1.53300   40.26300  1.000 64.41000  ? 713 SER A O      1 
ATOM   4978  C  CB     . SER A 1 722 ? -1.61700  -0.15200  38.08700  1.000 54.52000  ? 713 SER A CB     1 
ATOM   4979  O  OG     . SER A 1 722 ? -0.78400  -1.10500  38.72100  1.000 74.22000  ? 713 SER A OG     1 
ATOM   4980  N  N      . VAL A 1 723 ? -1.66300  0.54200   41.18500  1.000 56.87000  ? 714 VAL A N      1 
ATOM   4981  C  CA     . VAL A 1 723 ? -2.30500  0.44600   42.49300  1.000 64.61000  ? 714 VAL A CA     1 
ATOM   4982  C  C      . VAL A 1 723 ? -2.74000  1.82200   42.97600  1.000 70.66000  ? 714 VAL A C      1 
ATOM   4983  O  O      . VAL A 1 723 ? -3.79100  1.97100   43.61200  1.000 66.38000  ? 714 VAL A O      1 
ATOM   4984  C  CB     . VAL A 1 723 ? -1.36500  -0.23400  43.50500  1.000 53.46000  ? 714 VAL A CB     1 
ATOM   4985  C  CG1    . VAL A 1 723 ? -1.90100  -0.05900  44.91800  1.000 65.78000  ? 714 VAL A CG1    1 
ATOM   4986  C  CG2    . VAL A 1 723 ? -1.21500  -1.70700  43.17400  1.000 69.82000  ? 714 VAL A CG2    1 
ATOM   4987  N  N      . ILE A 1 724 ? -1.94400  2.84700   42.68100  1.000 70.78000  ? 715 ILE A N      1 
ATOM   4988  C  CA     . ILE A 1 724 ? -2.30000  4.19100   43.13000  1.000 58.05000  ? 715 ILE A CA     1 
ATOM   4989  C  C      . ILE A 1 724 ? -3.41900  4.77600   42.27500  1.000 58.38000  ? 715 ILE A C      1 
ATOM   4990  O  O      . ILE A 1 724 ? -4.44000  5.23900   42.79700  1.000 58.97000  ? 715 ILE A O      1 
ATOM   4991  C  CB     . ILE A 1 724 ? -1.06300  5.10700   43.14000  1.000 55.26000  ? 715 ILE A CB     1 
ATOM   4992  C  CG1    . ILE A 1 724 ? -0.08100  4.66100   44.22800  1.000 52.46000  ? 715 ILE A CG1    1 
ATOM   4993  C  CG2    . ILE A 1 724 ? -1.48500  6.55500   43.34100  1.000 50.16000  ? 715 ILE A CG2    1 
ATOM   4994  C  CD1    . ILE A 1 724 ? 1.22200   5.42900   44.23100  1.000 46.29000  ? 715 ILE A CD1    1 
ATOM   4995  N  N      . ALA A 1 725 ? -3.25700  4.75500   40.95000  1.000 75.30000  ? 716 ALA A N      1 
ATOM   4996  C  CA     . ALA A 1 725 ? -4.18000  5.45700   40.06300  1.000 75.69000  ? 716 ALA A CA     1 
ATOM   4997  C  C      . ALA A 1 725 ? -5.51700  4.74400   39.87800  1.000 75.98000  ? 716 ALA A C      1 
ATOM   4998  O  O      . ALA A 1 725 ? -6.45400  5.35400   39.33900  1.000 84.53000  ? 716 ALA A O      1 
ATOM   4999  C  CB     . ALA A 1 725 ? -3.52200  5.68100   38.69900  1.000 59.65000  ? 716 ALA A CB     1 
ATOM   5000  N  N      . VAL A 1 726 ? -5.63900  3.48300   40.30300  1.000 70.80000  ? 717 VAL A N      1 
ATOM   5001  C  CA     . VAL A 1 726 ? -6.92400  2.80300   40.20600  1.000 74.77000  ? 717 VAL A CA     1 
ATOM   5002  C  C      . VAL A 1 726 ? -7.97700  3.48800   41.06300  1.000 83.04000  ? 717 VAL A C      1 
ATOM   5003  O  O      . VAL A 1 726 ? -9.17300  3.39300   40.76900  1.000 79.82000  ? 717 VAL A O      1 
ATOM   5004  C  CB     . VAL A 1 726 ? -6.77800  1.31600   40.59800  1.000 65.26000  ? 717 VAL A CB     1 
ATOM   5005  C  CG1    . VAL A 1 726 ? -6.51000  1.18100   42.09100  1.000 68.23000  ? 717 VAL A CG1    1 
ATOM   5006  C  CG2    . VAL A 1 726 ? -8.02100  0.53100   40.19700  1.000 64.15000  ? 717 VAL A CG2    1 
ATOM   5007  N  N      . SER A 1 727 ? -7.56000  4.20000   42.11400  1.000 86.70000  ? 718 SER A N      1 
ATOM   5008  C  CA     . SER A 1 727 ? -8.51600  4.95700   42.91400  1.000 89.81000  ? 718 SER A CA     1 
ATOM   5009  C  C      . SER A 1 727 ? -9.21000  6.03400   42.09100  1.000 81.33000  ? 718 SER A C      1 
ATOM   5010  O  O      . SER A 1 727 ? -10.37000 6.36700   42.35800  1.000 82.88000  ? 718 SER A O      1 
ATOM   5011  C  CB     . SER A 1 727 ? -7.81400  5.58100   44.12100  1.000 90.92000  ? 718 SER A CB     1 
ATOM   5012  O  OG     . SER A 1 727 ? -7.17100  4.59100   44.90500  1.000 80.41000  ? 718 SER A OG     1 
ATOM   5013  N  N      . ILE A 1 728 ? -8.52800  6.58400   41.09000  1.000 77.79000  ? 719 ILE A N      1 
ATOM   5014  C  CA     . ILE A 1 728 ? -9.06900  7.67600   40.29300  1.000 70.48000  ? 719 ILE A CA     1 
ATOM   5015  C  C      . ILE A 1 728 ? -9.72200  7.17500   39.01000  1.000 81.50000  ? 719 ILE A C      1 
ATOM   5016  O  O      . ILE A 1 728 ? -10.81300 7.62400   38.66000  1.000 92.36000  ? 719 ILE A O      1 
ATOM   5017  C  CB     . ILE A 1 728 ? -7.97600  8.72600   39.99400  1.000 82.97000  ? 719 ILE A CB     1 
ATOM   5018  C  CG1    . ILE A 1 728 ? -6.95900  8.19200   38.98400  1.000 97.78000  ? 719 ILE A CG1    1 
ATOM   5019  C  CG2    . ILE A 1 728 ? -7.27900  9.15100   41.28100  1.000 101.24000 ? 719 ILE A CG2    1 
ATOM   5020  C  CD1    . ILE A 1 728 ? -5.87500  9.18800   38.62700  1.000 85.50000  ? 719 ILE A CD1    1 
ATOM   5021  N  N      . PHE A 1 729 ? -9.08600  6.24900   38.28800  1.000 93.72000  ? 720 PHE A N      1 
ATOM   5022  C  CA     . PHE A 1 729 ? -9.66100  5.77600   37.03200  1.000 89.44000  ? 720 PHE A CA     1 
ATOM   5023  C  C      . PHE A 1 729 ? -10.39100 4.44200   37.17700  1.000 85.63000  ? 720 PHE A C      1 
ATOM   5024  O  O      . PHE A 1 729 ? -10.69500 3.80100   36.16500  1.000 85.01000  ? 720 PHE A O      1 
ATOM   5025  C  CB     . PHE A 1 729 ? -8.59600  5.69900   35.92700  1.000 73.02000  ? 720 PHE A CB     1 
ATOM   5026  C  CG     . PHE A 1 729 ? -7.53700  4.65200   36.14400  1.000 65.83000  ? 720 PHE A CG     1 
ATOM   5027  C  CD1    . PHE A 1 729 ? -7.81900  3.30600   35.96700  1.000 74.53000  ? 720 PHE A CD1    1 
ATOM   5028  C  CD2    . PHE A 1 729 ? -6.24600  5.01900   36.47500  1.000 62.51000  ? 720 PHE A CD2    1 
ATOM   5029  C  CE1    . PHE A 1 729 ? -6.84200  2.34800   36.15200  1.000 79.50000  ? 720 PHE A CE1    1 
ATOM   5030  C  CE2    . PHE A 1 729 ? -5.26500  4.06500   36.65800  1.000 68.26000  ? 720 PHE A CE2    1 
ATOM   5031  C  CZ     . PHE A 1 729 ? -5.56300  2.72800   36.49700  1.000 72.30000  ? 720 PHE A CZ     1 
ATOM   5032  N  N      . LYS A 1 730 ? -10.68800 4.01800   38.40700  1.000 78.45000  ? 721 LYS A N      1 
ATOM   5033  C  CA     . LYS A 1 730 ? -11.52100 2.83400   38.60400  1.000 74.63000  ? 721 LYS A CA     1 
ATOM   5034  C  C      . LYS A 1 730 ? -12.85900 2.98900   37.89500  1.000 75.84000  ? 721 LYS A C      1 
ATOM   5035  O  O      . LYS A 1 730 ? -13.28600 2.10500   37.14200  1.000 73.52000  ? 721 LYS A O      1 
ATOM   5036  C  CB     . LYS A 1 730 ? -11.73400 2.59800   40.09900  1.000 84.39000  ? 721 LYS A CB     1 
ATOM   5037  C  CG     . LYS A 1 730 ? -12.53100 1.35700   40.45000  1.000 77.78000  ? 721 LYS A CG     1 
ATOM   5038  C  CD     . LYS A 1 730 ? -12.49100 1.12000   41.95000  1.000 77.34000  ? 721 LYS A CD     1 
ATOM   5039  C  CE     . LYS A 1 730 ? -12.86100 2.39000   42.70500  1.000 88.26000  ? 721 LYS A CE     1 
ATOM   5040  N  NZ     . LYS A 1 730 ? -12.61300 2.28100   44.16900  1.000 91.76000  ? 721 LYS A NZ     1 
ATOM   5041  N  N      . HIS A 1 731 ? -13.53500 4.11200   38.12800  1.000 90.52000  ? 722 HIS A N      1 
ATOM   5042  C  CA     . HIS A 1 731 ? -14.78200 4.43600   37.45700  1.000 102.85000 ? 722 HIS A CA     1 
ATOM   5043  C  C      . HIS A 1 731 ? -14.61700 5.51900   36.40200  1.000 108.21000 ? 722 HIS A C      1 
ATOM   5044  O  O      . HIS A 1 731 ? -15.54900 5.75200   35.62400  1.000 105.72000 ? 722 HIS A O      1 
ATOM   5045  C  CB     . HIS A 1 731 ? -15.83100 4.89000   38.48200  1.000 94.58000  ? 722 HIS A CB     1 
ATOM   5046  C  CG     . HIS A 1 731 ? -15.37700 6.03200   39.33600  1.000 100.63000 ? 722 HIS A CG     1 
ATOM   5047  N  ND1    . HIS A 1 731 ? -14.57500 5.86000   40.44400  1.000 101.82000 ? 722 HIS A ND1    1 
ATOM   5048  C  CD2    . HIS A 1 731 ? -15.60800 7.36300   39.24300  1.000 104.26000 ? 722 HIS A CD2    1 
ATOM   5049  C  CE1    . HIS A 1 731 ? -14.33300 7.03500   40.99700  1.000 101.69000 ? 722 HIS A CE1    1 
ATOM   5050  N  NE2    . HIS A 1 731 ? -14.94900 7.96400   40.28700  1.000 108.61000 ? 722 HIS A NE2    1 
ATOM   5051  N  N      . VAL A 1 732 ? -13.46500 6.18800   36.36200  1.000 101.32000 ? 723 VAL A N      1 
ATOM   5052  C  CA     . VAL A 1 732 ? -13.20200 7.23100   35.37900  1.000 85.90000  ? 723 VAL A CA     1 
ATOM   5053  C  C      . VAL A 1 732 ? -12.38200 6.66400   34.23000  1.000 86.08000  ? 723 VAL A C      1 
ATOM   5054  O  O      . VAL A 1 732 ? -11.16100 6.85000   34.17000  1.000 84.54000  ? 723 VAL A O      1 
ATOM   5055  C  CB     . VAL A 1 732 ? -12.48500 8.43300   36.01600  1.000 86.28000  ? 723 VAL A CB     1 
ATOM   5056  C  CG1    . VAL A 1 732 ? -12.25300 9.52100   34.97400  1.000 76.88000  ? 723 VAL A CG1    1 
ATOM   5057  C  CG2    . VAL A 1 732 ? -13.29200 8.97100   37.18600  1.000 99.74000  ? 723 VAL A CG2    1 
ATOM   5058  N  N      . HIS A 1 733 ? -13.04600 5.97200   33.31100  1.000 78.49000  ? 724 HIS A N      1 
ATOM   5059  C  CA     . HIS A 1 733 ? -12.42100 5.47800   32.09200  1.000 73.93000  ? 724 HIS A CA     1 
ATOM   5060  C  C      . HIS A 1 733 ? -13.22200 6.03200   30.92600  1.000 79.32000  ? 724 HIS A C      1 
ATOM   5061  O  O      . HIS A 1 733 ? -14.42900 5.78800   30.82200  1.000 86.63000  ? 724 HIS A O      1 
ATOM   5062  C  CB     . HIS A 1 733 ? -12.37000 3.95000   32.06600  1.000 73.85000  ? 724 HIS A CB     1 
ATOM   5063  C  CG     . HIS A 1 733 ? -13.67800 3.29600   32.37900  1.000 63.94000  ? 724 HIS A CG     1 
ATOM   5064  N  ND1    . HIS A 1 733 ? -14.64100 3.06300   31.42200  1.000 76.89000  ? 724 HIS A ND1    1 
ATOM   5065  C  CD2    . HIS A 1 733 ? -14.17900 2.81900   33.54200  1.000 69.24000  ? 724 HIS A CD2    1 
ATOM   5066  C  CE1    . HIS A 1 733 ? -15.68100 2.47200   31.98300  1.000 94.86000  ? 724 HIS A CE1    1 
ATOM   5067  N  NE2    . HIS A 1 733 ? -15.42600 2.31300   33.26900  1.000 89.26000  ? 724 HIS A NE2    1 
ATOM   5068  N  N      . LEU A 1 734 ? -12.54500 6.77900   30.05700  1.000 79.42000  ? 725 LEU A N      1 
ATOM   5069  C  CA     . LEU A 1 734 ? -13.21500 7.62900   29.08500  1.000 88.06000  ? 725 LEU A CA     1 
ATOM   5070  C  C      . LEU A 1 734 ? -13.67500 6.89500   27.83200  1.000 101.79000 ? 725 LEU A C      1 
ATOM   5071  O  O      . LEU A 1 734 ? -14.47700 7.45200   27.07600  1.000 126.93000 ? 725 LEU A O      1 
ATOM   5072  C  CB     . LEU A 1 734 ? -12.29800 8.79700   28.71400  1.000 94.64000  ? 725 LEU A CB     1 
ATOM   5073  C  CG     . LEU A 1 734 ? -11.86800 9.61100   29.94200  1.000 95.28000  ? 725 LEU A CG     1 
ATOM   5074  C  CD1    . LEU A 1 734 ? -10.68900 10.53000  29.63100  1.000 72.82000  ? 725 LEU A CD1    1 
ATOM   5075  C  CD2    . LEU A 1 734 ? -13.04100 10.39300  30.52600  1.000 75.41000  ? 725 LEU A CD2    1 
ATOM   5076  N  N      . PHE A 1 735 ? -13.20700 5.67600   27.58800  1.000 97.33000  ? 726 PHE A N      1 
ATOM   5077  C  CA     . PHE A 1 735 ? -13.66000 4.94000   26.41300  1.000 94.62000  ? 726 PHE A CA     1 
ATOM   5078  C  C      . PHE A 1 735 ? -14.29900 3.61400   26.81400  1.000 84.19000  ? 726 PHE A C      1 
ATOM   5079  O  O      . PHE A 1 735 ? -14.26100 3.21700   27.97900  1.000 83.68000  ? 726 PHE A O      1 
ATOM   5080  C  CB     . PHE A 1 735 ? -12.49200 4.70600   25.44700  1.000 106.88000 ? 726 PHE A CB     1 
ATOM   5081  C  CG     . PHE A 1 735 ? -12.90800 4.52500   24.01000  1.000 112.87000 ? 726 PHE A CG     1 
ATOM   5082  C  CD1    . PHE A 1 735 ? -13.09500 5.62000   23.18200  1.000 100.40000 ? 726 PHE A CD1    1 
ATOM   5083  C  CD2    . PHE A 1 735 ? -13.08700 3.25600   23.48100  1.000 130.67000 ? 726 PHE A CD2    1 
ATOM   5084  C  CE1    . PHE A 1 735 ? -13.47100 5.45400   21.85800  1.000 112.37000 ? 726 PHE A CE1    1 
ATOM   5085  C  CE2    . PHE A 1 735 ? -13.46000 3.08400   22.15800  1.000 120.47000 ? 726 PHE A CE2    1 
ATOM   5086  C  CZ     . PHE A 1 735 ? -13.65300 4.18400   21.34700  1.000 114.78000 ? 726 PHE A CZ     1 
ATOM   5087  O  OXT    . PHE A 1 735 ? -14.88000 2.90900   25.98800  1.000 88.92000  ? 726 PHE A OXT    1 
ATOM   5088  N  N      . VAL B 1 12  ? -29.93200 -24.68400 -1.60800  1.000 116.39000 ? 3   VAL B N      1 
ATOM   5089  C  CA     . VAL B 1 12  ? -28.77500 -23.81000 -1.75600  1.000 123.03000 ? 3   VAL B CA     1 
ATOM   5090  C  C      . VAL B 1 12  ? -27.61200 -24.32000 -0.91400  1.000 127.25000 ? 3   VAL B C      1 
ATOM   5091  O  O      . VAL B 1 12  ? -26.44700 -24.20000 -1.30500  1.000 112.49000 ? 3   VAL B O      1 
ATOM   5092  C  CB     . VAL B 1 12  ? -29.12000 -22.36100 -1.37600  1.000 111.46000 ? 3   VAL B CB     1 
ATOM   5093  C  CG1    . VAL B 1 12  ? -27.87600 -21.48700 -1.44000  1.000 94.47000  ? 3   VAL B CG1    1 
ATOM   5094  C  CG2    . VAL B 1 12  ? -30.21700 -21.81800 -2.28100  1.000 106.98000 ? 3   VAL B CG2    1 
ATOM   5095  N  N      . ALA B 1 13  ? -27.92900 -24.87800 0.25800   1.000 145.44000 ? 4   ALA B N      1 
ATOM   5096  C  CA     . ALA B 1 13  ? -26.87800 -25.45700 1.08400   1.000 144.45000 ? 4   ALA B CA     1 
ATOM   5097  C  C      . ALA B 1 13  ? -26.18800 -26.60900 0.36900   1.000 142.28000 ? 4   ALA B C      1 
ATOM   5098  O  O      . ALA B 1 13  ? -25.00000 -26.86200 0.60100   1.000 143.77000 ? 4   ALA B O      1 
ATOM   5099  C  CB     . ALA B 1 13  ? -27.45400 -25.92200 2.42200   1.000 155.86000 ? 4   ALA B CB     1 
ATOM   5100  N  N      . ALA B 1 14  ? -26.91200 -27.32000 -0.50000  1.000 138.43000 ? 5   ALA B N      1 
ATOM   5101  C  CA     . ALA B 1 14  ? -26.28000 -28.34600 -1.31800  1.000 142.02000 ? 5   ALA B CA     1 
ATOM   5102  C  C      . ALA B 1 14  ? -25.34500 -27.74000 -2.35600  1.000 140.81000 ? 5   ALA B C      1 
ATOM   5103  O  O      . ALA B 1 14  ? -24.42900 -28.42300 -2.82500  1.000 134.26000 ? 5   ALA B O      1 
ATOM   5104  C  CB     . ALA B 1 14  ? -27.34100 -29.20900 -2.00200  1.000 159.47000 ? 5   ALA B CB     1 
ATOM   5105  N  N      . LEU B 1 15  ? -25.56500 -26.47500 -2.72500  1.000 140.78000 ? 6   LEU B N      1 
ATOM   5106  C  CA     . LEU B 1 15  ? -24.67900 -25.76100 -3.63400  1.000 134.40000 ? 6   LEU B CA     1 
ATOM   5107  C  C      . LEU B 1 15  ? -23.52100 -25.08900 -2.91200  1.000 141.79000 ? 6   LEU B C      1 
ATOM   5108  O  O      . LEU B 1 15  ? -22.53200 -24.72100 -3.55800  1.000 132.81000 ? 6   LEU B O      1 
ATOM   5109  C  CB     . LEU B 1 15  ? -25.46600 -24.71400 -4.42900  1.000 134.61000 ? 6   LEU B CB     1 
ATOM   5110  C  CG     . LEU B 1 15  ? -26.47300 -25.28700 -5.42900  1.000 137.96000 ? 6   LEU B CG     1 
ATOM   5111  C  CD1    . LEU B 1 15  ? -27.40500 -24.20200 -5.95000  1.000 120.35000 ? 6   LEU B CD1    1 
ATOM   5112  C  CD2    . LEU B 1 15  ? -25.75100 -25.98000 -6.57400  1.000 109.40000 ? 6   LEU B CD2    1 
ATOM   5113  N  N      . PHE B 1 16  ? -23.62400 -24.92000 -1.59300  1.000 153.41000 ? 7   PHE B N      1 
ATOM   5114  C  CA     . PHE B 1 16  ? -22.46200 -24.51900 -0.80700  1.000 140.16000 ? 7   PHE B CA     1 
ATOM   5115  C  C      . PHE B 1 16  ? -21.59500 -25.72500 -0.46700  1.000 131.04000 ? 7   PHE B C      1 
ATOM   5116  O  O      . PHE B 1 16  ? -20.36400 -25.65200 -0.55300  1.000 131.75000 ? 7   PHE B O      1 
ATOM   5117  C  CB     . PHE B 1 16  ? -22.90300 -23.80400 0.47300   1.000 124.50000 ? 7   PHE B CB     1 
ATOM   5118  C  CG     . PHE B 1 16  ? -23.50800 -22.44900 0.24100   1.000 129.98000 ? 7   PHE B CG     1 
ATOM   5119  C  CD1    . PHE B 1 16  ? -23.40600 -21.82900 -0.99300  1.000 148.41000 ? 7   PHE B CD1    1 
ATOM   5120  C  CD2    . PHE B 1 16  ? -24.17500 -21.79100 1.26200   1.000 132.95000 ? 7   PHE B CD2    1 
ATOM   5121  C  CE1    . PHE B 1 16  ? -23.96100 -20.58000 -1.20500  1.000 153.64000 ? 7   PHE B CE1    1 
ATOM   5122  C  CE2    . PHE B 1 16  ? -24.73300 -20.54100 1.05600   1.000 142.63000 ? 7   PHE B CE2    1 
ATOM   5123  C  CZ     . PHE B 1 16  ? -24.62500 -19.93600 -0.18000  1.000 141.58000 ? 7   PHE B CZ     1 
ATOM   5124  N  N      . PHE B 1 17  ? -22.22200 -26.84200 -0.08500  1.000 133.79000 ? 8   PHE B N      1 
ATOM   5125  C  CA     . PHE B 1 17  ? -21.48800 -28.08600 0.11800   1.000 147.29000 ? 8   PHE B CA     1 
ATOM   5126  C  C      . PHE B 1 17  ? -20.65900 -28.46100 -1.10300  1.000 143.27000 ? 8   PHE B C      1 
ATOM   5127  O  O      . PHE B 1 17  ? -19.69200 -29.22400 -0.98100  1.000 137.33000 ? 8   PHE B O      1 
ATOM   5128  C  CB     . PHE B 1 17  ? -22.45900 -29.21700 0.46900   1.000 152.53000 ? 8   PHE B CB     1 
ATOM   5129  N  N      . LEU B 1 18  ? -21.01800 -27.94500 -2.28000  1.000 135.53000 ? 9   LEU B N      1 
ATOM   5130  C  CA     . LEU B 1 18  ? -20.29700 -28.26300 -3.50400  1.000 125.82000 ? 9   LEU B CA     1 
ATOM   5131  C  C      . LEU B 1 18  ? -18.99400 -27.48900 -3.62600  1.000 127.09000 ? 9   LEU B C      1 
ATOM   5132  O  O      . LEU B 1 18  ? -18.13000 -27.87600 -4.42000  1.000 129.50000 ? 9   LEU B O      1 
ATOM   5133  C  CB     . LEU B 1 18  ? -21.18500 -27.97500 -4.71800  1.000 125.04000 ? 9   LEU B CB     1 
ATOM   5134  C  CG     . LEU B 1 18  ? -20.72000 -28.45300 -6.09400  1.000 145.77000 ? 9   LEU B CG     1 
ATOM   5135  C  CD1    . LEU B 1 18  ? -20.58200 -29.96800 -6.10400  1.000 156.45000 ? 9   LEU B CD1    1 
ATOM   5136  C  CD2    . LEU B 1 18  ? -21.69100 -27.99300 -7.17400  1.000 147.57000 ? 9   LEU B CD2    1 
ATOM   5137  N  N      . ILE B 1 19  ? -18.83800 -26.40700 -2.85600  1.000 131.32000 ? 10  ILE B N      1 
ATOM   5138  C  CA     . ILE B 1 19  ? -17.62300 -25.59700 -2.97000  1.000 122.35000 ? 10  ILE B CA     1 
ATOM   5139  C  C      . ILE B 1 19  ? -16.39300 -26.40200 -2.61100  1.000 118.21000 ? 10  ILE B C      1 
ATOM   5140  O  O      . ILE B 1 19  ? -15.36700 -26.26600 -3.29600  1.000 113.55000 ? 10  ILE B O      1 
ATOM   5141  C  CB     . ILE B 1 19  ? -17.77200 -24.31000 -2.13600  1.000 111.82000 ? 10  ILE B CB     1 
ATOM   5142  C  CG1    . ILE B 1 19  ? -19.02400 -23.53600 -2.55700  1.000 123.18000 ? 10  ILE B CG1    1 
ATOM   5143  C  CG2    . ILE B 1 19  ? -16.53000 -23.44000 -2.28400  1.000 104.36000 ? 10  ILE B CG2    1 
ATOM   5144  C  CD1    . ILE B 1 19  ? -19.09900 -23.23300 -4.04300  1.000 128.31000 ? 10  ILE B CD1    1 
ATOM   5145  N  N      . PRO B 1 20  ? -16.38400 -27.22800 -1.55900  1.000 117.51000 ? 11  PRO B N      1 
ATOM   5146  C  CA     . PRO B 1 20  ? -15.17100 -28.01100 -1.26600  1.000 119.85000 ? 11  PRO B CA     1 
ATOM   5147  C  C      . PRO B 1 20  ? -14.78300 -28.95800 -2.38700  1.000 121.48000 ? 11  PRO B C      1 
ATOM   5148  O  O      . PRO B 1 20  ? -13.60100 -29.04300 -2.74600  1.000 122.51000 ? 11  PRO B O      1 
ATOM   5149  C  CB     . PRO B 1 20  ? -15.55500 -28.76300 0.01300   1.000 116.17000 ? 11  PRO B CB     1 
ATOM   5150  C  CG     . PRO B 1 20  ? -16.53800 -27.86400 0.67600   1.000 118.52000 ? 11  PRO B CG     1 
ATOM   5151  C  CD     . PRO B 1 20  ? -17.35200 -27.27900 -0.44900  1.000 119.10000 ? 11  PRO B CD     1 
ATOM   5152  N  N      . LEU B 1 21  ? -15.75300 -29.68900 -2.94200  1.000 125.28000 ? 12  LEU B N      1 
ATOM   5153  C  CA     . LEU B 1 21  ? -15.46300 -30.58200 -4.05900  1.000 122.97000 ? 12  LEU B CA     1 
ATOM   5154  C  C      . LEU B 1 21  ? -15.01700 -29.79900 -5.28800  1.000 123.03000 ? 12  LEU B C      1 
ATOM   5155  O  O      . LEU B 1 21  ? -14.11700 -30.23200 -6.01700  1.000 122.27000 ? 12  LEU B O      1 
ATOM   5156  C  CB     . LEU B 1 21  ? -16.69500 -31.43100 -4.37100  1.000 120.37000 ? 12  LEU B CB     1 
ATOM   5157  C  CG     . LEU B 1 21  ? -17.30700 -32.17300 -3.17900  1.000 116.39000 ? 12  LEU B CG     1 
ATOM   5158  C  CD1    . LEU B 1 21  ? -18.62200 -32.82900 -3.57000  1.000 117.28000 ? 12  LEU B CD1    1 
ATOM   5159  C  CD2    . LEU B 1 21  ? -16.33500 -33.20400 -2.62800  1.000 100.57000 ? 12  LEU B CD2    1 
ATOM   5160  N  N      . VAL B 1 22  ? -15.63000 -28.63700 -5.53000  1.000 120.17000 ? 13  VAL B N      1 
ATOM   5161  C  CA     . VAL B 1 22  ? -15.20800 -27.79300 -6.64500  1.000 104.25000 ? 13  VAL B CA     1 
ATOM   5162  C  C      . VAL B 1 22  ? -13.75400 -27.37900 -6.47100  1.000 107.31000 ? 13  VAL B C      1 
ATOM   5163  O  O      . VAL B 1 22  ? -12.95200 -27.45500 -7.40700  1.000 112.11000 ? 13  VAL B O      1 
ATOM   5164  C  CB     . VAL B 1 22  ? -16.12400 -26.56300 -6.77200  1.000 109.56000 ? 13  VAL B CB     1 
ATOM   5165  C  CG1    . VAL B 1 22  ? -15.43400 -25.48000 -7.58400  1.000 98.33000  ? 13  VAL B CG1    1 
ATOM   5166  C  CG2    . VAL B 1 22  ? -17.45400 -26.94900 -7.40400  1.000 125.95000 ? 13  VAL B CG2    1 
ATOM   5167  N  N      . ALA B 1 23  ? -13.39900 -26.92600 -5.26800  1.000 112.02000 ? 14  ALA B N      1 
ATOM   5168  C  CA     . ALA B 1 23  ? -12.03100 -26.49300 -5.00800  1.000 110.63000 ? 14  ALA B CA     1 
ATOM   5169  C  C      . ALA B 1 23  ? -11.05100 -27.65100 -5.13700  1.000 100.60000 ? 14  ALA B C      1 
ATOM   5170  O  O      . ALA B 1 23  ? -9.96400  -27.49300 -5.70200  1.000 110.02000 ? 14  ALA B O      1 
ATOM   5171  C  CB     . ALA B 1 23  ? -11.94000 -25.86000 -3.62100  1.000 105.58000 ? 14  ALA B CB     1 
ATOM   5172  N  N      . LEU B 1 24  ? -11.41800 -28.82400 -4.62000  1.000 92.07000  ? 15  LEU B N      1 
ATOM   5173  C  CA     . LEU B 1 24  ? -10.53300 -29.97900 -4.71700  1.000 101.87000 ? 15  LEU B CA     1 
ATOM   5174  C  C      . LEU B 1 24  ? -10.31100 -30.36400 -6.17300  1.000 110.44000 ? 15  LEU B C      1 
ATOM   5175  O  O      . LEU B 1 24  ? -9.17700  -30.61100 -6.60000  1.000 111.30000 ? 15  LEU B O      1 
ATOM   5176  C  CB     . LEU B 1 24  ? -11.11300 -31.15100 -3.92400  1.000 104.97000 ? 15  LEU B CB     1 
ATOM   5177  C  CG     . LEU B 1 24  ? -11.19700 -30.96100 -2.40800  1.000 97.22000  ? 15  LEU B CG     1 
ATOM   5178  C  CD1    . LEU B 1 24  ? -11.97800 -32.09800 -1.77200  1.000 101.83000 ? 15  LEU B CD1    1 
ATOM   5179  C  CD2    . LEU B 1 24  ? -9.80600  -30.85700 -1.80000  1.000 89.76000  ? 15  LEU B CD2    1 
ATOM   5180  N  N      . GLY B 1 25  ? -11.39200 -30.41000 -6.95400  1.000 115.77000 ? 16  GLY B N      1 
ATOM   5181  C  CA     . GLY B 1 25  ? -11.26300 -30.73200 -8.36300  1.000 113.49000 ? 16  GLY B CA     1 
ATOM   5182  C  C      . GLY B 1 25  ? -10.45900 -29.70300 -9.12900  1.000 102.92000 ? 16  GLY B C      1 
ATOM   5183  O  O      . GLY B 1 25  ? -9.67100  -30.05100 -10.00800 1.000 100.22000 ? 16  GLY B O      1 
ATOM   5184  N  N      . PHE B 1 26  ? -10.64000 -28.42300 -8.80100  1.000 100.31000 ? 17  PHE B N      1 
ATOM   5185  C  CA     . PHE B 1 26  ? -9.91200  -27.37200 -9.50200  1.000 102.04000 ? 17  PHE B CA     1 
ATOM   5186  C  C      . PHE B 1 26  ? -8.43100  -27.40300 -9.14800  1.000 104.76000 ? 17  PHE B C      1 
ATOM   5187  O  O      . PHE B 1 26  ? -7.57600  -27.16300 -10.00700 1.000 109.13000 ? 17  PHE B O      1 
ATOM   5188  C  CB     . PHE B 1 26  ? -10.53300 -26.01400 -9.17200  1.000 103.00000 ? 17  PHE B CB     1 
ATOM   5189  C  CG     . PHE B 1 26  ? -9.78300  -24.84500 -9.73600  1.000 111.12000 ? 17  PHE B CG     1 
ATOM   5190  C  CD1    . PHE B 1 26  ? -9.52700  -24.75000 -11.09400 1.000 132.06000 ? 17  PHE B CD1    1 
ATOM   5191  C  CD2    . PHE B 1 26  ? -9.33500  -23.83500 -8.90300  1.000 115.03000 ? 17  PHE B CD2    1 
ATOM   5192  C  CE1    . PHE B 1 26  ? -8.83700  -23.66600 -11.60900 1.000 145.68000 ? 17  PHE B CE1    1 
ATOM   5193  C  CE2    . PHE B 1 26  ? -8.64400  -22.75200 -9.41100  1.000 114.83000 ? 17  PHE B CE2    1 
ATOM   5194  C  CZ     . PHE B 1 26  ? -8.39500  -22.66700 -10.76600 1.000 106.60000 ? 17  PHE B CZ     1 
ATOM   5195  N  N      . ALA B 1 27  ? -8.10400  -27.72500 -7.89400  1.000 106.91000 ? 18  ALA B N      1 
ATOM   5196  C  CA     . ALA B 1 27  ? -6.70500  -27.89300 -7.51700  1.000 114.33000 ? 18  ALA B CA     1 
ATOM   5197  C  C      . ALA B 1 27  ? -6.08700  -29.10200 -8.21100  1.000 120.04000 ? 18  ALA B C      1 
ATOM   5198  O  O      . ALA B 1 27  ? -4.94800  -29.03800 -8.68900  1.000 109.54000 ? 18  ALA B O      1 
ATOM   5199  C  CB     . ALA B 1 27  ? -6.58000  -28.01300 -5.99900  1.000 114.57000 ? 18  ALA B CB     1 
ATOM   5200  N  N      . ALA B 1 28  ? -6.81800  -30.21700 -8.26800  1.000 121.26000 ? 19  ALA B N      1 
ATOM   5201  C  CA     . ALA B 1 28  ? -6.32100  -31.38500 -8.98900  1.000 125.14000 ? 19  ALA B CA     1 
ATOM   5202  C  C      . ALA B 1 28  ? -6.11400  -31.07500 -10.46800 1.000 129.03000 ? 19  ALA B C      1 
ATOM   5203  O  O      . ALA B 1 28  ? -5.13800  -31.52900 -11.07800 1.000 130.67000 ? 19  ALA B O      1 
ATOM   5204  C  CB     . ALA B 1 28  ? -7.28900  -32.55200 -8.81400  1.000 114.37000 ? 19  ALA B CB     1 
ATOM   5205  N  N      . ALA B 1 29  ? -7.03100  -30.30900 -11.06300 1.000 119.22000 ? 20  ALA B N      1 
ATOM   5206  C  CA     . ALA B 1 29  ? -6.89500  -29.92100 -12.46200 1.000 112.63000 ? 20  ALA B CA     1 
ATOM   5207  C  C      . ALA B 1 29  ? -5.69300  -29.01000 -12.66700 1.000 117.97000 ? 20  ALA B C      1 
ATOM   5208  O  O      . ALA B 1 29  ? -4.99500  -29.11900 -13.67900 1.000 129.04000 ? 20  ALA B O      1 
ATOM   5209  C  CB     . ALA B 1 29  ? -8.17500  -29.24200 -12.94700 1.000 119.61000 ? 20  ALA B CB     1 
ATOM   5210  N  N      . ASN B 1 30  ? -5.45300  -28.08700 -11.73300 1.000 115.54000 ? 21  ASN B N      1 
ATOM   5211  C  CA     . ASN B 1 30  ? -4.25300  -27.26000 -11.81200 1.000 109.65000 ? 21  ASN B CA     1 
ATOM   5212  C  C      . ASN B 1 30  ? -3.00000  -28.11700 -11.72100 1.000 126.27000 ? 21  ASN B C      1 
ATOM   5213  O  O      . ASN B 1 30  ? -2.01400  -27.86400 -12.42100 1.000 131.72000 ? 21  ASN B O      1 
ATOM   5214  C  CB     . ASN B 1 30  ? -4.26600  -26.20600 -10.70800 1.000 99.43000  ? 21  ASN B CB     1 
ATOM   5215  C  CG     . ASN B 1 30  ? -5.41600  -25.23600 -10.85500 1.000 118.83000 ? 21  ASN B CG     1 
ATOM   5216  O  OD1    . ASN B 1 30  ? -5.94200  -25.04600 -11.95200 1.000 131.82000 ? 21  ASN B OD1    1 
ATOM   5217  N  ND2    . ASN B 1 30  ? -5.82200  -24.62500 -9.74900  1.000 122.23000 ? 21  ASN B ND2    1 
ATOM   5218  N  N      . PHE B 1 31  ? -3.01900  -29.13100 -10.85400 1.000 126.85000 ? 22  PHE B N      1 
ATOM   5219  C  CA     . PHE B 1 31  ? -1.89200  -30.05400 -10.76500 1.000 129.84000 ? 22  PHE B CA     1 
ATOM   5220  C  C      . PHE B 1 31  ? -1.66200  -30.74800 -12.10100 1.000 144.20000 ? 22  PHE B C      1 
ATOM   5221  O  O      . PHE B 1 31  ? -0.52400  -30.87800 -12.56400 1.000 141.23000 ? 22  PHE B O      1 
ATOM   5222  C  CB     . PHE B 1 31  ? -2.14800  -31.10500 -9.68800  1.000 113.90000 ? 22  PHE B CB     1 
ATOM   5223  C  CG     . PHE B 1 31  ? -1.42000  -32.39300 -9.93400  1.000 123.59000 ? 22  PHE B CG     1 
ATOM   5224  C  CD1    . PHE B 1 31  ? -0.09900  -32.54300 -9.54200  1.000 128.03000 ? 22  PHE B CD1    1 
ATOM   5225  C  CD2    . PHE B 1 31  ? -2.01600  -33.41000 -10.66300 1.000 141.55000 ? 22  PHE B CD2    1 
ATOM   5226  C  CE1    . PHE B 1 31  ? 0.58300   -33.72100 -9.78900  1.000 147.47000 ? 22  PHE B CE1    1 
ATOM   5227  C  CE2    . PHE B 1 31  ? -1.32900  -34.58300 -10.94100 1.000 143.71000 ? 22  PHE B CE2    1 
ATOM   5228  C  CZ     . PHE B 1 31  ? -0.03100  -34.74200 -10.49200 1.000 142.07000 ? 22  PHE B CZ     1 
ATOM   5229  N  N      . ALA B 1 32  ? -2.74000  -31.24200 -12.71600 1.000 146.69000 ? 23  ALA B N      1 
ATOM   5230  C  CA     . ALA B 1 32  ? -2.61100  -31.94100 -13.99300 1.000 134.27000 ? 23  ALA B CA     1 
ATOM   5231  C  C      . ALA B 1 32  ? -2.09700  -31.00600 -15.08100 1.000 128.40000 ? 23  ALA B C      1 
ATOM   5232  O  O      . ALA B 1 32  ? -1.24900  -31.39200 -15.89300 1.000 130.12000 ? 23  ALA B O      1 
ATOM   5233  C  CB     . ALA B 1 32  ? -3.95000  -32.55900 -14.39500 1.000 115.82000 ? 23  ALA B CB     1 
ATOM   5234  N  N      . ALA B 1 33  ? -2.61000  -29.77400 -15.12300 1.000 113.73000 ? 24  ALA B N      1 
ATOM   5235  C  CA     . ALA B 1 33  ? -2.13800  -28.80300 -16.10300 1.000 109.53000 ? 24  ALA B CA     1 
ATOM   5236  C  C      . ALA B 1 33  ? -0.66800  -28.42700 -15.99900 1.000 130.96000 ? 24  ALA B C      1 
ATOM   5237  O  O      . ALA B 1 33  ? -0.00800  -28.19900 -17.02100 1.000 135.20000 ? 24  ALA B O      1 
ATOM   5238  C  CB     . ALA B 1 33  ? -3.00100  -27.54200 -16.05900 1.000 94.15000  ? 24  ALA B CB     1 
ATOM   5239  N  N      . VAL B 1 34  ? -0.13800  -28.35400 -14.77700 1.000 139.18000 ? 25  VAL B N      1 
ATOM   5240  C  CA     . VAL B 1 34  ? 1.28700   -28.09500 -14.60200 1.000 151.77000 ? 25  VAL B CA     1 
ATOM   5241  C  C      . VAL B 1 34  ? 2.12500   -29.34000 -14.90500 1.000 161.34000 ? 25  VAL B C      1 
ATOM   5242  O  O      . VAL B 1 34  ? 3.28300   -29.25900 -15.33100 1.000 169.34000 ? 25  VAL B O      1 
ATOM   5243  C  CB     . VAL B 1 34  ? 1.57000   -27.66400 -13.15100 1.000 140.55000 ? 25  VAL B CB     1 
ATOM   5244  C  CG1    . VAL B 1 34  ? 3.06800   -27.51400 -12.92100 1.000 144.30000 ? 25  VAL B CG1    1 
ATOM   5245  C  CG2    . VAL B 1 34  ? 0.83700   -26.37300 -12.82800 1.000 123.75000 ? 25  VAL B CG2    1 
ATOM   5246  N  N      . VAL B 1 35  ? 1.52500   -30.51400 -14.70800 1.000 150.94000 ? 26  VAL B N      1 
ATOM   5247  C  CA     . VAL B 1 35  ? 2.18300   -31.75400 -15.10500 1.000 143.30000 ? 26  VAL B CA     1 
ATOM   5248  C  C      . VAL B 1 35  ? 2.29600   -31.66400 -16.61900 1.000 146.20000 ? 26  VAL B C      1 
ATOM   5249  O  O      . VAL B 1 35  ? 3.29000   -32.09500 -17.21400 1.000 144.06000 ? 26  VAL B O      1 
ATOM   5250  C  CB     . VAL B 1 35  ? 1.45100   -33.03700 -14.67300 1.000 133.22000 ? 26  VAL B CB     1 
ATOM   5251  C  CG1    . VAL B 1 35  ? 2.00600   -34.23600 -15.42100 1.000 131.61000 ? 26  VAL B CG1    1 
ATOM   5252  C  CG2    . VAL B 1 35  ? 1.54900   -33.23000 -13.16900 1.000 129.96000 ? 26  VAL B CG2    1 
ATOM   5253  N  N      . ARG B 1 36  ? 1.27300   -31.10300 -17.26400 1.000 144.14000 ? 27  ARG B N      1 
ATOM   5254  C  CA     . ARG B 1 36  ? 1.33400   -30.87400 -18.70000 1.000 139.38000 ? 27  ARG B CA     1 
ATOM   5255  C  C      . ARG B 1 36  ? 2.41500   -29.86300 -19.05400 1.000 133.83000 ? 27  ARG B C      1 
ATOM   5256  O  O      . ARG B 1 36  ? 3.02000   -29.95700 -20.12700 1.000 134.36000 ? 27  ARG B O      1 
ATOM   5257  C  CB     . ARG B 1 36  ? -0.02800  -30.41200 -19.21400 1.000 133.27000 ? 27  ARG B CB     1 
ATOM   5258  N  N      . LYS B 1 37  ? 2.67500   -28.90200 -18.17200 1.000 133.05000 ? 28  LYS B N      1 
ATOM   5259  C  CA     . LYS B 1 37  ? 3.66400   -27.88000 -18.47200 1.000 145.26000 ? 28  LYS B CA     1 
ATOM   5260  C  C      . LYS B 1 37  ? 5.02600   -28.53600 -18.69100 1.000 150.25000 ? 28  LYS B C      1 
ATOM   5261  O  O      . LYS B 1 37  ? 5.38400   -29.48000 -17.97600 1.000 139.81000 ? 28  LYS B O      1 
ATOM   5262  C  CB     . LYS B 1 37  ? 3.74000   -26.85400 -17.34000 1.000 140.35000 ? 28  LYS B CB     1 
ATOM   5263  C  CG     . LYS B 1 37  ? 2.43700   -26.10800 -17.11300 1.000 120.15000 ? 28  LYS B CG     1 
ATOM   5264  C  CD     . LYS B 1 37  ? 1.92200   -25.46800 -18.39400 1.000 98.03000  ? 28  LYS B CD     1 
ATOM   5265  C  CE     . LYS B 1 37  ? 0.65000   -24.67100 -18.13300 1.000 116.51000 ? 28  LYS B CE     1 
ATOM   5266  N  NZ     . LYS B 1 37  ? -0.47500  -25.53800 -17.67300 1.000 106.42000 ? 28  LYS B NZ     1 
ATOM   5267  N  N      . PRO B 1 38  ? 5.81000   -28.06700 -19.65800 1.000 155.85000 ? 29  PRO B N      1 
ATOM   5268  C  CA     . PRO B 1 38  ? 7.07400   -28.74200 -19.96700 1.000 157.44000 ? 29  PRO B CA     1 
ATOM   5269  C  C      . PRO B 1 38  ? 8.15600   -28.46100 -18.93700 1.000 150.50000 ? 29  PRO B C      1 
ATOM   5270  O  O      . PRO B 1 38  ? 8.16200   -27.43000 -18.26100 1.000 150.35000 ? 29  PRO B O      1 
ATOM   5271  C  CB     . PRO B 1 38  ? 7.45700   -28.15600 -21.33100 1.000 168.81000 ? 29  PRO B CB     1 
ATOM   5272  C  CG     . PRO B 1 38  ? 6.82600   -26.80400 -21.33600 1.000 157.55000 ? 29  PRO B CG     1 
ATOM   5273  C  CD     . PRO B 1 38  ? 5.51900   -26.97700 -20.60700 1.000 141.89000 ? 29  PRO B CD     1 
ATOM   5274  N  N      . GLU B 1 39  ? 9.08400   -29.40800 -18.83500 1.000 144.27000 ? 30  GLU B N      1 
ATOM   5275  C  CA     . GLU B 1 39  ? 10.21800  -29.30400 -17.92100 1.000 134.44000 ? 30  GLU B CA     1 
ATOM   5276  C  C      . GLU B 1 39  ? 11.50600  -28.95000 -18.66000 1.000 119.35000 ? 30  GLU B C      1 
ATOM   5277  O  O      . GLU B 1 39  ? 11.47600  -28.35200 -19.73600 1.000 133.56000 ? 30  GLU B O      1 
ATOM   5278  C  CB     . GLU B 1 39  ? 10.38600  -30.60700 -17.13600 1.000 118.86000 ? 30  GLU B CB     1 
ATOM   5279  C  CG     . GLU B 1 39  ? 9.47200   -30.70500 -15.92700 1.000 137.01000 ? 30  GLU B CG     1 
ATOM   5280  C  CD     . GLU B 1 39  ? 8.01700   -30.90100 -16.30700 1.000 143.98000 ? 30  GLU B CD     1 
ATOM   5281  O  OE1    . GLU B 1 39  ? 7.74900   -31.56300 -17.33300 1.000 141.01000 ? 30  GLU B OE1    1 
ATOM   5282  O  OE2    . GLU B 1 39  ? 7.14200   -30.38200 -15.58100 1.000 131.86000 ? 30  GLU B OE2    1 
ATOM   5283  N  N      . GLU B 1 42  ? 17.31500  -31.31000 -20.60800 1.000 145.59000 ? 33  GLU B N      1 
ATOM   5284  C  CA     . GLU B 1 42  ? 17.16800  -32.62700 -20.00000 1.000 152.19000 ? 33  GLU B CA     1 
ATOM   5285  C  C      . GLU B 1 42  ? 17.96900  -32.71000 -18.70600 1.000 178.67000 ? 33  GLU B C      1 
ATOM   5286  O  O      . GLU B 1 42  ? 17.54800  -33.33800 -17.73600 1.000 190.04000 ? 33  GLU B O      1 
ATOM   5287  C  CB     . GLU B 1 42  ? 17.61600  -33.72000 -20.97100 1.000 129.62000 ? 33  GLU B CB     1 
ATOM   5288  N  N      . ARG B 1 43  ? 19.13800  -32.07200 -18.70400 1.000 179.16000 ? 34  ARG B N      1 
ATOM   5289  C  CA     . ARG B 1 43  ? 19.98900  -32.10100 -17.52000 1.000 175.64000 ? 34  ARG B CA     1 
ATOM   5290  C  C      . ARG B 1 43  ? 19.29000  -31.47000 -16.32100 1.000 185.59000 ? 34  ARG B C      1 
ATOM   5291  O  O      . ARG B 1 43  ? 19.41500  -31.95700 -15.19300 1.000 188.57000 ? 34  ARG B O      1 
ATOM   5292  C  CB     . ARG B 1 43  ? 21.31500  -31.39800 -17.80600 1.000 165.93000 ? 34  ARG B CB     1 
ATOM   5293  N  N      . MET B 1 44  ? 18.55400  -30.37900 -16.54600 1.000 183.26000 ? 35  MET B N      1 
ATOM   5294  C  CA     . MET B 1 44  ? 17.86000  -29.70900 -15.44800 1.000 186.08000 ? 35  MET B CA     1 
ATOM   5295  C  C      . MET B 1 44  ? 16.77800  -30.58900 -14.82300 1.000 190.02000 ? 35  MET B C      1 
ATOM   5296  O  O      . MET B 1 44  ? 16.58800  -30.56800 -13.60200 1.000 198.15000 ? 35  MET B O      1 
ATOM   5297  C  CB     . MET B 1 44  ? 17.26200  -28.39100 -15.93900 1.000 167.55000 ? 35  MET B CB     1 
ATOM   5298  N  N      . LYS B 1 45  ? 16.05900  -31.37100 -15.63600 1.000 183.20000 ? 36  LYS B N      1 
ATOM   5299  C  CA     . LYS B 1 45  ? 14.95300  -32.17600 -15.11300 1.000 183.75000 ? 36  LYS B CA     1 
ATOM   5300  C  C      . LYS B 1 45  ? 15.41400  -33.16600 -14.04800 1.000 197.31000 ? 36  LYS B C      1 
ATOM   5301  O  O      . LYS B 1 45  ? 14.66300  -33.46700 -13.10600 1.000 210.15000 ? 36  LYS B O      1 
ATOM   5302  C  CB     . LYS B 1 45  ? 14.25700  -32.91500 -16.25400 1.000 161.61000 ? 36  LYS B CB     1 
ATOM   5303  N  N      . GLU B 1 46  ? 16.63800  -33.68100 -14.17600 1.000 190.24000 ? 37  GLU B N      1 
ATOM   5304  C  CA     . GLU B 1 46  ? 17.11300  -34.69300 -13.24000 1.000 181.67000 ? 37  GLU B CA     1 
ATOM   5305  C  C      . GLU B 1 46  ? 17.10600  -34.18000 -11.80800 1.000 184.37000 ? 37  GLU B C      1 
ATOM   5306  O  O      . GLU B 1 46  ? 16.65100  -34.88000 -10.89700 1.000 187.71000 ? 37  GLU B O      1 
ATOM   5307  C  CB     . GLU B 1 46  ? 18.51700  -35.14800 -13.63500 1.000 172.57000 ? 37  GLU B CB     1 
ATOM   5308  N  N      . ILE B 1 47  ? 17.58800  -32.95400 -11.59200 1.000 183.65000 ? 38  ILE B N      1 
ATOM   5309  C  CA     . ILE B 1 47  ? 17.64500  -32.40300 -10.24100 1.000 167.89000 ? 38  ILE B CA     1 
ATOM   5310  C  C      . ILE B 1 47  ? 16.24600  -32.27100 -9.65700  1.000 171.71000 ? 38  ILE B C      1 
ATOM   5311  O  O      . ILE B 1 47  ? 16.02500  -32.52200 -8.46300  1.000 164.82000 ? 38  ILE B O      1 
ATOM   5312  C  CB     . ILE B 1 47  ? 18.38700  -31.05400 -10.25000 1.000 144.20000 ? 38  ILE B CB     1 
ATOM   5313  N  N      . SER B 1 48  ? 15.27900  -31.86000 -10.47900 1.000 177.06000 ? 39  SER B N      1 
ATOM   5314  C  CA     . SER B 1 48  ? 13.90800  -31.80100 -9.99500  1.000 164.15000 ? 39  SER B CA     1 
ATOM   5315  C  C      . SER B 1 48  ? 13.43800  -33.18500 -9.57100  1.000 176.41000 ? 39  SER B C      1 
ATOM   5316  O  O      . SER B 1 48  ? 12.74100  -33.33200 -8.55800  1.000 169.94000 ? 39  SER B O      1 
ATOM   5317  C  CB     . SER B 1 48  ? 12.98900  -31.21600 -11.06800 1.000 153.26000 ? 39  SER B CB     1 
ATOM   5318  O  OG     . SER B 1 48  ? 11.62500  -31.39400 -10.73100 1.000 151.36000 ? 39  SER B OG     1 
ATOM   5319  N  N      . SER B 1 49  ? 13.81400  -34.21600 -10.33100 1.000 189.18000 ? 40  SER B N      1 
ATOM   5320  C  CA     . SER B 1 49  ? 13.45000  -35.57000 -9.92600  1.000 183.41000 ? 40  SER B CA     1 
ATOM   5321  C  C      . SER B 1 49  ? 14.17800  -35.87100 -8.61800  1.000 170.84000 ? 40  SER B C      1 
ATOM   5322  O  O      . SER B 1 49  ? 13.60900  -36.49400 -7.70900  1.000 176.06000 ? 40  SER B O      1 
ATOM   5323  C  CB     . SER B 1 49  ? 13.83900  -36.57000 -11.01600 1.000 200.48000 ? 40  SER B CB     1 
ATOM   5324  O  OG     . SER B 1 49  ? 13.65300  -37.91000 -10.59000 1.000 227.33000 ? 40  SER B OG     1 
ATOM   5325  N  N      . TYR B 1 50  ? 15.43300  -35.42500 -8.49700  1.000 167.92000 ? 41  TYR B N      1 
ATOM   5326  C  CA     . TYR B 1 50  ? 16.17900  -35.66400 -7.25800  1.000 158.18000 ? 41  TYR B CA     1 
ATOM   5327  C  C      . TYR B 1 50  ? 15.39500  -35.13600 -6.05700  1.000 158.25000 ? 41  TYR B C      1 
ATOM   5328  O  O      . TYR B 1 50  ? 15.11200  -35.85800 -5.08700  1.000 155.51000 ? 41  TYR B O      1 
ATOM   5329  C  CB     . TYR B 1 50  ? 17.58200  -35.04200 -7.31300  1.000 159.36000 ? 41  TYR B CB     1 
ATOM   5330  C  CG     . TYR B 1 50  ? 18.54300  -35.56600 -8.36600  1.000 171.82000 ? 41  TYR B CG     1 
ATOM   5331  C  CD1    . TYR B 1 50  ? 18.64700  -36.92600 -8.64100  1.000 180.37000 ? 41  TYR B CD1    1 
ATOM   5332  C  CD2    . TYR B 1 50  ? 19.41200  -34.70700 -9.01500  1.000 166.42000 ? 41  TYR B CD2    1 
ATOM   5333  C  CE1    . TYR B 1 50  ? 19.55200  -37.39800 -9.58700  1.000 166.62000 ? 41  TYR B CE1    1 
ATOM   5334  C  CE2    . TYR B 1 50  ? 20.30900  -35.16200 -9.95700  1.000 164.64000 ? 41  TYR B CE2    1 
ATOM   5335  C  CZ     . TYR B 1 50  ? 20.38100  -36.50800 -10.24000 1.000 167.86000 ? 41  TYR B CZ     1 
ATOM   5336  O  OH     . TYR B 1 50  ? 21.28600  -36.95600 -11.17700 1.000 177.12000 ? 41  TYR B OH     1 
ATOM   5337  N  N      . ILE B 1 51  ? 15.01700  -33.85800 -6.13400  1.000 161.62000 ? 42  ILE B N      1 
ATOM   5338  C  CA     . ILE B 1 51  ? 14.27300  -33.23000 -5.04900  1.000 155.08000 ? 42  ILE B CA     1 
ATOM   5339  C  C      . ILE B 1 51  ? 12.90800  -33.84100 -4.76500  1.000 160.30000 ? 42  ILE B C      1 
ATOM   5340  O  O      . ILE B 1 51  ? 12.50600  -33.98700 -3.60200  1.000 164.65000 ? 42  ILE B O      1 
ATOM   5341  C  CB     . ILE B 1 51  ? 14.16300  -31.73700 -5.40800  1.000 133.78000 ? 42  ILE B CB     1 
ATOM   5342  N  N      . ARG B 1 52  ? 12.16800  -34.20100 -5.81900  1.000 165.77000 ? 43  ARG B N      1 
ATOM   5343  C  CA     . ARG B 1 52  ? 10.85900  -34.81300 -5.61200  1.000 159.51000 ? 43  ARG B CA     1 
ATOM   5344  C  C      . ARG B 1 52  ? 10.98300  -36.11700 -4.83200  1.000 145.36000 ? 43  ARG B C      1 
ATOM   5345  O  O      . ARG B 1 52  ? 10.19400  -36.37900 -3.91400  1.000 139.55000 ? 43  ARG B O      1 
ATOM   5346  C  CB     . ARG B 1 52  ? 10.16200  -35.04400 -6.95400  1.000 152.47000 ? 43  ARG B CB     1 
ATOM   5347  N  N      . SER B 1 53  ? 11.97600  -36.94500 -5.17500  1.000 147.25000 ? 44  SER B N      1 
ATOM   5348  C  CA     . SER B 1 53  ? 12.13200  -38.22500 -4.48700  1.000 157.02000 ? 44  SER B CA     1 
ATOM   5349  C  C      . SER B 1 53  ? 12.50000  -38.02500 -3.02100  1.000 146.93000 ? 44  SER B C      1 
ATOM   5350  O  O      . SER B 1 53  ? 11.97800  -38.72500 -2.14000  1.000 147.52000 ? 44  SER B O      1 
ATOM   5351  C  CB     . SER B 1 53  ? 13.18400  -39.08100 -5.19200  1.000 173.75000 ? 44  SER B CB     1 
ATOM   5352  O  OG     . SER B 1 53  ? 13.26700  -40.37100 -4.60800  1.000 177.19000 ? 44  SER B OG     1 
ATOM   5353  N  N      . GLY B 1 54  ? 13.40800  -37.08700 -2.74000  1.000 143.36000 ? 45  GLY B N      1 
ATOM   5354  C  CA     . GLY B 1 54  ? 13.74800  -36.81200 -1.35200  1.000 139.99000 ? 45  GLY B CA     1 
ATOM   5355  C  C      . GLY B 1 54  ? 12.54700  -36.33800 -0.55400  1.000 143.42000 ? 45  GLY B C      1 
ATOM   5356  O  O      . GLY B 1 54  ? 12.31900  -36.78000 0.58100   1.000 135.22000 ? 45  GLY B O      1 
ATOM   5357  N  N      . ALA B 1 55  ? 11.76200  -35.43000 -1.13800  1.000 153.21000 ? 46  ALA B N      1 
ATOM   5358  C  CA     . ALA B 1 55  ? 10.56700  -34.95300 -0.45600  1.000 133.04000 ? 46  ALA B CA     1 
ATOM   5359  C  C      . ALA B 1 55  ? 9.59600   -36.09700 -0.20100  1.000 130.37000 ? 46  ALA B C      1 
ATOM   5360  O  O      . ALA B 1 55  ? 8.96100   -36.15400 0.85600   1.000 125.07000 ? 46  ALA B O      1 
ATOM   5361  C  CB     . ALA B 1 55  ? 9.90000   -33.84500 -1.26900  1.000 101.95000 ? 46  ALA B CB     1 
ATOM   5362  N  N      . ASP B 1 56  ? 9.46800   -37.02200 -1.15700  1.000 140.16000 ? 47  ASP B N      1 
ATOM   5363  C  CA     . ASP B 1 56  ? 8.56100   -38.15000 -0.95900  1.000 136.98000 ? 47  ASP B CA     1 
ATOM   5364  C  C      . ASP B 1 56  ? 9.03900   -39.06000 0.16600   1.000 135.77000 ? 47  ASP B C      1 
ATOM   5365  O  O      . ASP B 1 56  ? 8.22400   -39.56600 0.94500   1.000 128.99000 ? 47  ASP B O      1 
ATOM   5366  C  CB     . ASP B 1 56  ? 8.39800   -38.94100 -2.25600  1.000 136.48000 ? 47  ASP B CB     1 
ATOM   5367  C  CG     . ASP B 1 56  ? 7.65500   -38.16200 -3.31700  1.000 144.67000 ? 47  ASP B CG     1 
ATOM   5368  O  OD1    . ASP B 1 56  ? 6.97700   -37.17800 -2.95400  1.000 151.72000 ? 47  ASP B OD1    1 
ATOM   5369  O  OD2    . ASP B 1 56  ? 7.74700   -38.53000 -4.50700  1.000 163.23000 ? 47  ASP B OD2    1 
ATOM   5370  N  N      . SER B 1 57  ? 10.35100  -39.28200 0.27200   1.000 134.58000 ? 48  SER B N      1 
ATOM   5371  C  CA     . SER B 1 57  ? 10.86200  -40.09000 1.37900   1.000 123.77000 ? 48  SER B CA     1 
ATOM   5372  C  C      . SER B 1 57  ? 10.56900  -39.42700 2.72000   1.000 126.18000 ? 48  SER B C      1 
ATOM   5373  O  O      . SER B 1 57  ? 10.11800  -40.08100 3.67400   1.000 128.13000 ? 48  SER B O      1 
ATOM   5374  C  CB     . SER B 1 57  ? 12.36400  -40.31900 1.22100   1.000 128.67000 ? 48  SER B CB     1 
ATOM   5375  O  OG     . SER B 1 57  ? 12.88600  -41.05200 2.31700   1.000 131.35000 ? 48  SER B OG     1 
ATOM   5376  N  N      . PHE B 1 58  ? 10.83900  -38.12200 2.81400   1.000 122.48000 ? 49  PHE B N      1 
ATOM   5377  C  CA     . PHE B 1 58  ? 10.53900  -37.40500 4.04800   1.000 113.99000 ? 49  PHE B CA     1 
ATOM   5378  C  C      . PHE B 1 58  ? 9.05400   -37.49200 4.38000   1.000 112.38000 ? 49  PHE B C      1 
ATOM   5379  O  O      . PHE B 1 58  ? 8.67500   -37.74600 5.53300   1.000 115.25000 ? 49  PHE B O      1 
ATOM   5380  C  CB     . PHE B 1 58  ? 10.99000  -35.94900 3.92400   1.000 108.28000 ? 49  PHE B CB     1 
ATOM   5381  C  CG     . PHE B 1 58  ? 10.33100  -35.02200 4.90100   1.000 111.83000 ? 49  PHE B CG     1 
ATOM   5382  C  CD1    . PHE B 1 58  ? 10.72400  -34.99800 6.22800   1.000 121.34000 ? 49  PHE B CD1    1 
ATOM   5383  C  CD2    . PHE B 1 58  ? 9.33100   -34.15900 4.48600   1.000 101.10000 ? 49  PHE B CD2    1 
ATOM   5384  C  CE1    . PHE B 1 58  ? 10.11800  -34.14000 7.12700   1.000 114.07000 ? 49  PHE B CE1    1 
ATOM   5385  C  CE2    . PHE B 1 58  ? 8.72500   -33.30000 5.37800   1.000 97.02000  ? 49  PHE B CE2    1 
ATOM   5386  C  CZ     . PHE B 1 58  ? 9.11800   -33.29000 6.70000   1.000 99.75000  ? 49  PHE B CZ     1 
ATOM   5387  N  N      . LEU B 1 59  ? 8.20000   -37.30800 3.37000   1.000 107.00000 ? 50  LEU B N      1 
ATOM   5388  C  CA     . LEU B 1 59  ? 6.75900   -37.36300 3.58200   1.000 92.45000  ? 50  LEU B CA     1 
ATOM   5389  C  C      . LEU B 1 59  ? 6.32100   -38.74300 4.04500   1.000 100.96000 ? 50  LEU B C      1 
ATOM   5390  O  O      . LEU B 1 59  ? 5.43700   -38.86200 4.89500   1.000 104.59000 ? 50  LEU B O      1 
ATOM   5391  C  CB     . LEU B 1 59  ? 6.02100   -36.97300 2.30100   1.000 75.04000  ? 50  LEU B CB     1 
ATOM   5392  C  CG     . LEU B 1 59  ? 6.05100   -35.49600 1.90200   1.000 87.22000  ? 50  LEU B CG     1 
ATOM   5393  C  CD1    . LEU B 1 59  ? 5.31700   -35.27200 0.58300   1.000 98.24000  ? 50  LEU B CD1    1 
ATOM   5394  C  CD2    . LEU B 1 59  ? 5.46400   -34.62800 3.00500   1.000 102.23000 ? 50  LEU B CD2    1 
ATOM   5395  N  N      . ALA B 1 60  ? 6.91600   -39.79800 3.48900   1.000 100.51000 ? 51  ALA B N      1 
ATOM   5396  C  CA     . ALA B 1 60  ? 6.53400   -41.14900 3.88500   1.000 98.89000  ? 51  ALA B CA     1 
ATOM   5397  C  C      . ALA B 1 60  ? 6.91300   -41.41800 5.33400   1.000 104.74000 ? 51  ALA B C      1 
ATOM   5398  O  O      . ALA B 1 60  ? 6.10600   -41.95000 6.11000   1.000 111.00000 ? 51  ALA B O      1 
ATOM   5399  C  CB     . ALA B 1 60  ? 7.18200   -42.17300 2.95500   1.000 103.84000 ? 51  ALA B CB     1 
ATOM   5400  N  N      . HIS B 1 61  ? 8.14100   -41.06000 5.71900   1.000 100.55000 ? 52  HIS B N      1 
ATOM   5401  C  CA     . HIS B 1 61  ? 8.54800   -41.25300 7.10800   1.000 92.84000  ? 52  HIS B CA     1 
ATOM   5402  C  C      . HIS B 1 61  ? 7.60900   -40.50600 8.04900   1.000 99.02000  ? 52  HIS B C      1 
ATOM   5403  O  O      . HIS B 1 61  ? 7.04800   -41.08600 8.99800   1.000 111.03000 ? 52  HIS B O      1 
ATOM   5404  C  CB     . HIS B 1 61  ? 9.98900   -40.77600 7.29700   1.000 95.81000  ? 52  HIS B CB     1 
ATOM   5405  C  CG     . HIS B 1 61  ? 11.01500  -41.71600 6.74500   1.000 116.10000 ? 52  HIS B CG     1 
ATOM   5406  N  ND1    . HIS B 1 61  ? 11.86000  -41.36900 5.71300   1.000 112.94000 ? 52  HIS B ND1    1 
ATOM   5407  C  CD2    . HIS B 1 61  ? 11.33500  -42.98800 7.08200   1.000 127.76000 ? 52  HIS B CD2    1 
ATOM   5408  C  CE1    . HIS B 1 61  ? 12.65200  -42.38800 5.43300   1.000 128.70000 ? 52  HIS B CE1    1 
ATOM   5409  N  NE2    . HIS B 1 61  ? 12.35500  -43.38300 6.25000   1.000 147.55000 ? 52  HIS B NE2    1 
ATOM   5410  N  N      . GLU B 1 62  ? 7.39100   -39.21700 7.76400   1.000 91.36000  ? 53  GLU B N      1 
ATOM   5411  C  CA     . GLU B 1 62  ? 6.52800   -38.40100 8.60700   1.000 89.34000  ? 53  GLU B CA     1 
ATOM   5412  C  C      . GLU B 1 62  ? 5.12500   -38.98300 8.67600   1.000 95.55000  ? 53  GLU B C      1 
ATOM   5413  O  O      . GLU B 1 62  ? 4.52200   -39.04000 9.75000   1.000 105.55000 ? 53  GLU B O      1 
ATOM   5414  C  CB     . GLU B 1 62  ? 6.48800   -36.96100 8.09000   1.000 98.61000  ? 53  GLU B CB     1 
ATOM   5415  C  CG     . GLU B 1 62  ? 5.49200   -36.06400 8.82300   1.000 113.37000 ? 53  GLU B CG     1 
ATOM   5416  C  CD     . GLU B 1 62  ? 5.25500   -34.74300 8.10800   1.000 107.94000 ? 53  GLU B CD     1 
ATOM   5417  O  OE1    . GLU B 1 62  ? 4.44200   -33.93300 8.60600   1.000 103.60000 ? 53  GLU B OE1    1 
ATOM   5418  O  OE2    . GLU B 1 62  ? 5.88300   -34.51400 7.05100   1.000 104.02000 ? 53  GLU B OE2    1 
ATOM   5419  N  N      . THR B 1 63  ? 4.57500   -39.38900 7.52900   1.000 96.57000  ? 54  THR B N      1 
ATOM   5420  C  CA     . THR B 1 63  ? 3.21000   -39.89500 7.48500   1.000 98.34000  ? 54  THR B CA     1 
ATOM   5421  C  C      . THR B 1 63  ? 3.06800   -41.16700 8.30300   1.000 89.05000  ? 54  THR B C      1 
ATOM   5422  O  O      . THR B 1 63  ? 2.07700   -41.34400 9.01900   1.000 102.15000 ? 54  THR B O      1 
ATOM   5423  C  CB     . THR B 1 63  ? 2.79300   -40.13900 6.03400   1.000 87.83000  ? 54  THR B CB     1 
ATOM   5424  O  OG1    . THR B 1 63  ? 2.61300   -38.88300 5.37000   1.000 66.54000  ? 54  THR B OG1    1 
ATOM   5425  C  CG2    . THR B 1 63  ? 1.49400   -40.91300 5.97500   1.000 82.99000  ? 54  THR B CG2    1 
ATOM   5426  N  N      . LYS B 1 64  ? 4.04200   -42.07200 8.20300   1.000 79.81000  ? 55  LYS B N      1 
ATOM   5427  C  CA     . LYS B 1 64  ? 3.98300   -43.27800 9.01900   1.000 94.38000  ? 55  LYS B CA     1 
ATOM   5428  C  C      . LYS B 1 64  ? 3.93500   -42.91400 10.49600  1.000 93.60000  ? 55  LYS B C      1 
ATOM   5429  O  O      . LYS B 1 64  ? 3.05300   -43.37500 11.23900  1.000 102.05000 ? 55  LYS B O      1 
ATOM   5430  C  CB     . LYS B 1 64  ? 5.18000   -44.18200 8.71500   1.000 97.43000  ? 55  LYS B CB     1 
ATOM   5431  N  N      . ALA B 1 65  ? 4.85800   -42.05300 10.93400  1.000 87.33000  ? 56  ALA B N      1 
ATOM   5432  C  CA     . ALA B 1 65  ? 4.88400   -41.69500 12.35000  1.000 87.67000  ? 56  ALA B CA     1 
ATOM   5433  C  C      . ALA B 1 65  ? 3.57800   -41.02300 12.77100  1.000 96.59000  ? 56  ALA B C      1 
ATOM   5434  O  O      . ALA B 1 65  ? 2.99600   -41.35600 13.81500  1.000 108.93000 ? 56  ALA B O      1 
ATOM   5435  C  CB     . ALA B 1 65  ? 6.08000   -40.78900 12.64500  1.000 81.47000  ? 56  ALA B CB     1 
ATOM   5436  N  N      . ILE B 1 66  ? 3.09500   -40.08300 11.95600  1.000 97.54000  ? 57  ILE B N      1 
ATOM   5437  C  CA     . ILE B 1 66  ? 1.92000   -39.29900 12.31700  1.000 96.67000  ? 57  ILE B CA     1 
ATOM   5438  C  C      . ILE B 1 66  ? 0.68300   -40.18100 12.37500  1.000 85.92000  ? 57  ILE B C      1 
ATOM   5439  O  O      . ILE B 1 66  ? -0.18000  -39.99300 13.23400  1.000 90.03000  ? 57  ILE B O      1 
ATOM   5440  C  CB     . ILE B 1 66  ? 1.72500   -38.12000 11.34500  1.000 105.49000 ? 57  ILE B CB     1 
ATOM   5441  C  CG1    . ILE B 1 66  ? 1.33100   -38.62200 9.95300   1.000 110.89000 ? 57  ILE B CG1    1 
ATOM   5442  C  CG2    . ILE B 1 66  ? 2.97400   -37.24800 11.29300  1.000 103.06000 ? 57  ILE B CG2    1 
ATOM   5443  C  CD1    . ILE B 1 66  ? 1.18400   -37.51400 8.91900   1.000 100.39000 ? 57  ILE B CD1    1 
ATOM   5444  N  N      . PHE B 1 67  ? 0.55900   -41.14300 11.46000  1.000 91.56000  ? 58  PHE B N      1 
ATOM   5445  C  CA     . PHE B 1 67  ? -0.62300  -41.99600 11.48600  1.000 100.95000 ? 58  PHE B CA     1 
ATOM   5446  C  C      . PHE B 1 67  ? -0.57400  -43.00100 12.63100  1.000 87.79000  ? 58  PHE B C      1 
ATOM   5447  O  O      . PHE B 1 67  ? -1.62200  -43.33900 13.19000  1.000 98.66000  ? 58  PHE B O      1 
ATOM   5448  C  CB     . PHE B 1 67  ? -0.81900  -42.68200 10.13400  1.000 110.80000 ? 58  PHE B CB     1 
ATOM   5449  C  CG     . PHE B 1 67  ? -1.52400  -41.81500 9.11600   1.000 119.76000 ? 58  PHE B CG     1 
ATOM   5450  C  CD1    . PHE B 1 67  ? -2.67400  -41.11800 9.46100   1.000 102.15000 ? 58  PHE B CD1    1 
ATOM   5451  C  CD2    . PHE B 1 67  ? -1.04300  -41.69500 7.82300   1.000 119.42000 ? 58  PHE B CD2    1 
ATOM   5452  C  CE1    . PHE B 1 67  ? -3.33000  -40.31800 8.53800   1.000 75.96000  ? 58  PHE B CE1    1 
ATOM   5453  C  CE2    . PHE B 1 67  ? -1.69600  -40.89500 6.89400   1.000 108.91000 ? 58  PHE B CE2    1 
ATOM   5454  C  CZ     . PHE B 1 67  ? -2.84100  -40.20700 7.25600   1.000 94.22000  ? 58  PHE B CZ     1 
ATOM   5455  N  N      . LYS B 1 68  ? 0.61100   -43.47900 13.02000  1.000 78.36000  ? 59  LYS B N      1 
ATOM   5456  C  CA     . LYS B 1 68  ? 0.67200   -44.27800 14.24400  1.000 78.52000  ? 59  LYS B CA     1 
ATOM   5457  C  C      . LYS B 1 68  ? 0.19900   -43.45800 15.44400  1.000 91.54000  ? 59  LYS B C      1 
ATOM   5458  O  O      . LYS B 1 68  ? -0.64600  -43.90400 16.24400  1.000 97.66000  ? 59  LYS B O      1 
ATOM   5459  C  CB     . LYS B 1 68  ? 2.09200   -44.79900 14.46800  1.000 75.26000  ? 59  LYS B CB     1 
ATOM   5460  N  N      . VAL B 1 69  ? 0.71900   -42.23300 15.56600  1.000 91.26000  ? 60  VAL B N      1 
ATOM   5461  C  CA     . VAL B 1 69  ? 0.33200   -41.37100 16.67900  1.000 83.98000  ? 60  VAL B CA     1 
ATOM   5462  C  C      . VAL B 1 69  ? -1.16500  -41.08200 16.63500  1.000 85.00000  ? 60  VAL B C      1 
ATOM   5463  O  O      . VAL B 1 69  ? -1.83700  -41.04400 17.67200  1.000 94.02000  ? 60  VAL B O      1 
ATOM   5464  C  CB     . VAL B 1 69  ? 1.16600   -40.07800 16.66200  1.000 80.37000  ? 60  VAL B CB     1 
ATOM   5465  C  CG1    . VAL B 1 69  ? 0.52900   -39.03000 17.54600  1.000 97.69000  ? 60  VAL B CG1    1 
ATOM   5466  C  CG2    . VAL B 1 69  ? 2.59700   -40.36300 17.10200  1.000 94.49000  ? 60  VAL B CG2    1 
ATOM   5467  N  N      . ALA B 1 70  ? -1.70900  -40.87500 15.43500  1.000 83.20000  ? 61  ALA B N      1 
ATOM   5468  C  CA     . ALA B 1 70  ? -3.13400  -40.61200 15.28000  1.000 73.26000  ? 61  ALA B CA     1 
ATOM   5469  C  C      . ALA B 1 70  ? -3.97100  -41.82700 15.64400  1.000 75.03000  ? 61  ALA B C      1 
ATOM   5470  O  O      . ALA B 1 70  ? -5.08200  -41.67800 16.16000  1.000 81.95000  ? 61  ALA B O      1 
ATOM   5471  C  CB     . ALA B 1 70  ? -3.43000  -40.16900 13.85100  1.000 64.69000  ? 61  ALA B CB     1 
ATOM   5472  N  N      . ILE B 1 71  ? -3.47300  -43.03000 15.37100  1.000 83.61000  ? 62  ILE B N      1 
ATOM   5473  C  CA     . ILE B 1 71  ? -4.18200  -44.22600 15.80800  1.000 86.15000  ? 62  ILE B CA     1 
ATOM   5474  C  C      . ILE B 1 71  ? -4.30300  -44.22200 17.32400  1.000 83.66000  ? 62  ILE B C      1 
ATOM   5475  O  O      . ILE B 1 71  ? -5.38800  -44.43300 17.88800  1.000 88.37000  ? 62  ILE B O      1 
ATOM   5476  C  CB     . ILE B 1 71  ? -3.46400  -45.49000 15.30600  1.000 91.35000  ? 62  ILE B CB     1 
ATOM   5477  C  CG1    . ILE B 1 71  ? -3.57100  -45.60200 13.78500  1.000 99.20000  ? 62  ILE B CG1    1 
ATOM   5478  C  CG2    . ILE B 1 71  ? -4.03500  -46.73400 15.98500  1.000 98.56000  ? 62  ILE B CG2    1 
ATOM   5479  C  CD1    . ILE B 1 71  ? -2.71000  -46.70200 13.20800  1.000 98.73000  ? 62  ILE B CD1    1 
ATOM   5480  N  N      . VAL B 1 72  ? -3.18500  -43.96100 18.00700  1.000 76.67000  ? 63  VAL B N      1 
ATOM   5481  C  CA     . VAL B 1 72  ? -3.23400  -43.92600 19.46900  1.000 70.60000  ? 63  VAL B CA     1 
ATOM   5482  C  C      . VAL B 1 72  ? -4.19000  -42.83400 19.94600  1.000 81.47000  ? 63  VAL B C      1 
ATOM   5483  O  O      . VAL B 1 72  ? -4.97600  -43.03700 20.88400  1.000 85.75000  ? 63  VAL B O      1 
ATOM   5484  C  CB     . VAL B 1 72  ? -1.82500  -43.74300 20.06000  1.000 70.38000  ? 63  VAL B CB     1 
ATOM   5485  C  CG1    . VAL B 1 72  ? -1.87500  -43.93200 21.56600  1.000 55.98000  ? 63  VAL B CG1    1 
ATOM   5486  C  CG2    . VAL B 1 72  ? -0.85100  -44.72800 19.43100  1.000 101.40000 ? 63  VAL B CG2    1 
ATOM   5487  N  N      . ILE B 1 73  ? -4.14000  -41.66300 19.30500  1.000 85.24000  ? 64  ILE B N      1 
ATOM   5488  C  CA     . ILE B 1 73  ? -4.98400  -40.53800 19.71000  1.000 68.23000  ? 64  ILE B CA     1 
ATOM   5489  C  C      . ILE B 1 73  ? -6.46000  -40.88700 19.55500  1.000 76.72000  ? 64  ILE B C      1 
ATOM   5490  O  O      . ILE B 1 73  ? -7.27700  -40.60800 20.44000  1.000 97.87000  ? 64  ILE B O      1 
ATOM   5491  C  CB     . ILE B 1 73  ? -4.62000  -39.27700 18.90300  1.000 72.19000  ? 64  ILE B CB     1 
ATOM   5492  C  CG1    . ILE B 1 73  ? -3.19900  -38.81400 19.23600  1.000 77.97000  ? 64  ILE B CG1    1 
ATOM   5493  C  CG2    . ILE B 1 73  ? -5.63900  -38.17200 19.14500  1.000 65.25000  ? 64  ILE B CG2    1 
ATOM   5494  C  CD1    . ILE B 1 73  ? -2.98900  -38.48800 20.69700  1.000 74.99000  ? 64  ILE B CD1    1 
ATOM   5495  N  N      . ALA B 1 74  ? -6.82700  -41.48800 18.42200  1.000 69.69000  ? 65  ALA B N      1 
ATOM   5496  C  CA     . ALA B 1 74  ? -8.22400  -41.83400 18.18500  1.000 67.80000  ? 65  ALA B CA     1 
ATOM   5497  C  C      . ALA B 1 74  ? -8.70100  -42.90300 19.15800  1.000 82.27000  ? 65  ALA B C      1 
ATOM   5498  O  O      . ALA B 1 74  ? -9.84500  -42.85500 19.63200  1.000 95.91000  ? 65  ALA B O      1 
ATOM   5499  C  CB     . ALA B 1 74  ? -8.41300  -42.28900 16.73800  1.000 53.97000  ? 65  ALA B CB     1 
ATOM   5500  N  N      . ILE B 1 75  ? -7.84300  -43.88000 19.47000  1.000 85.16000  ? 66  ILE B N      1 
ATOM   5501  C  CA     . ILE B 1 75  ? -8.22000  -44.89900 20.44700  1.000 87.62000  ? 66  ILE B CA     1 
ATOM   5502  C  C      . ILE B 1 75  ? -8.49400  -44.25700 21.80300  1.000 88.01000  ? 66  ILE B C      1 
ATOM   5503  O  O      . ILE B 1 75  ? -9.51600  -44.53200 22.44700  1.000 100.52000 ? 66  ILE B O      1 
ATOM   5504  C  CB     . ILE B 1 75  ? -7.13700  -45.98900 20.53900  1.000 84.48000  ? 66  ILE B CB     1 
ATOM   5505  C  CG1    . ILE B 1 75  ? -7.04100  -46.75000 19.21400  1.000 78.49000  ? 66  ILE B CG1    1 
ATOM   5506  C  CG2    . ILE B 1 75  ? -7.42800  -46.93800 21.69600  1.000 61.07000  ? 66  ILE B CG2    1 
ATOM   5507  C  CD1    . ILE B 1 75  ? -8.37100  -47.26000 18.69500  1.000 73.89000  ? 66  ILE B CD1    1 
ATOM   5508  N  N      . LEU B 1 76  ? -7.58400  -43.39000 22.25700  1.000 84.33000  ? 67  LEU B N      1 
ATOM   5509  C  CA     . LEU B 1 76  ? -7.78500  -42.72600 23.54200  1.000 71.80000  ? 67  LEU B CA     1 
ATOM   5510  C  C      . LEU B 1 76  ? -9.04700  -41.87000 23.52700  1.000 76.70000  ? 67  LEU B C      1 
ATOM   5511  O  O      . LEU B 1 76  ? -9.79200  -41.82900 24.51500  1.000 82.55000  ? 67  LEU B O      1 
ATOM   5512  C  CB     . LEU B 1 76  ? -6.56100  -41.88000 23.89500  1.000 44.58000  ? 67  LEU B CB     1 
ATOM   5513  C  CG     . LEU B 1 76  ? -5.28600  -42.65100 24.24400  1.000 44.72000  ? 67  LEU B CG     1 
ATOM   5514  C  CD1    . LEU B 1 76  ? -4.13700  -41.70500 24.54400  1.000 40.82000  ? 67  LEU B CD1    1 
ATOM   5515  C  CD2    . LEU B 1 76  ? -5.54200  -43.56700 25.42800  1.000 67.27000  ? 67  LEU B CD2    1 
ATOM   5516  N  N      . LEU B 1 77  ? -9.30700  -41.18800 22.40900  1.000 74.85000  ? 68  LEU B N      1 
ATOM   5517  C  CA     . LEU B 1 77  ? -10.48500 -40.33300 22.31200  1.000 73.12000  ? 68  LEU B CA     1 
ATOM   5518  C  C      . LEU B 1 77  ? -11.76100 -41.15300 22.44200  1.000 85.55000  ? 68  LEU B C      1 
ATOM   5519  O  O      . LEU B 1 77  ? -12.66500 -40.80600 23.21100  1.000 92.38000  ? 68  LEU B O      1 
ATOM   5520  C  CB     . LEU B 1 77  ? -10.46700 -39.57100 20.98300  1.000 74.33000  ? 68  LEU B CB     1 
ATOM   5521  C  CG     . LEU B 1 77  ? -9.49000  -38.40000 20.82400  1.000 81.71000  ? 68  LEU B CG     1 
ATOM   5522  C  CD1    . LEU B 1 77  ? -9.56300  -37.81500 19.41500  1.000 95.53000  ? 68  LEU B CD1    1 
ATOM   5523  C  CD2    . LEU B 1 77  ? -9.74800  -37.32000 21.86400  1.000 80.28000  ? 68  LEU B CD2    1 
ATOM   5524  N  N      . MET B 1 78  ? -11.85100 -42.25300 21.69300  1.000 89.30000  ? 69  MET B N      1 
ATOM   5525  C  CA     . MET B 1 78  ? -13.05300 -43.07700 21.75200  1.000 80.44000  ? 69  MET B CA     1 
ATOM   5526  C  C      . MET B 1 78  ? -13.22100 -43.72200 23.12300  1.000 78.69000  ? 69  MET B C      1 
ATOM   5527  O  O      . MET B 1 78  ? -14.34700 -43.84600 23.62000  1.000 91.37000  ? 69  MET B O      1 
ATOM   5528  C  CB     . MET B 1 78  ? -13.00700 -44.14200 20.65900  1.000 80.98000  ? 69  MET B CB     1 
ATOM   5529  C  CG     . MET B 1 78  ? -13.03900 -43.58000 19.24900  1.000 90.09000  ? 69  MET B CG     1 
ATOM   5530  S  SD     . MET B 1 78  ? -13.27100 -44.87200 18.01400  1.000 90.30000  ? 69  MET B SD     1 
ATOM   5531  C  CE     . MET B 1 78  ? -13.24500 -43.90800 16.50300  1.000 96.22000  ? 69  MET B CE     1 
ATOM   5532  N  N      . ILE B 1 79  ? -12.11900 -44.12600 23.76000  1.000 68.97000  ? 70  ILE B N      1 
ATOM   5533  C  CA     . ILE B 1 79  ? -12.22400 -44.75900 25.07300  1.000 76.06000  ? 70  ILE B CA     1 
ATOM   5534  C  C      . ILE B 1 79  ? -12.70000 -43.75800 26.12300  1.000 96.38000  ? 70  ILE B C      1 
ATOM   5535  O  O      . ILE B 1 79  ? -13.61900 -44.04300 26.89900  1.000 116.65000 ? 70  ILE B O      1 
ATOM   5536  C  CB     . ILE B 1 79  ? -10.88700 -45.40900 25.47300  1.000 91.81000  ? 70  ILE B CB     1 
ATOM   5537  C  CG1    . ILE B 1 79  ? -10.58800 -46.61700 24.57800  1.000 110.31000 ? 70  ILE B CG1    1 
ATOM   5538  C  CG2    . ILE B 1 79  ? -10.91700 -45.82700 26.93700  1.000 98.98000  ? 70  ILE B CG2    1 
ATOM   5539  C  CD1    . ILE B 1 79  ? -9.30500  -47.35100 24.93300  1.000 100.34000 ? 70  ILE B CD1    1 
ATOM   5540  N  N      . PHE B 1 80  ? -12.08400 -42.57600 26.16900  1.000 87.11000  ? 71  PHE B N      1 
ATOM   5541  C  CA     . PHE B 1 80  ? -12.36900 -41.61400 27.22900  1.000 77.32000  ? 71  PHE B CA     1 
ATOM   5542  C  C      . PHE B 1 80  ? -13.47200 -40.61800 26.88100  1.000 78.78000  ? 71  PHE B C      1 
ATOM   5543  O  O      . PHE B 1 80  ? -13.93000 -39.89100 27.77000  1.000 87.87000  ? 71  PHE B O      1 
ATOM   5544  C  CB     . PHE B 1 80  ? -11.08800 -40.85200 27.59200  1.000 70.29000  ? 71  PHE B CB     1 
ATOM   5545  C  CG     . PHE B 1 80  ? -10.05500 -41.69200 28.29900  1.000 61.86000  ? 71  PHE B CG     1 
ATOM   5546  C  CD1    . PHE B 1 80  ? -10.18500 -41.99300 29.64500  1.000 69.29000  ? 71  PHE B CD1    1 
ATOM   5547  C  CD2    . PHE B 1 80  ? -8.94800  -42.17000 27.61700  1.000 70.31000  ? 71  PHE B CD2    1 
ATOM   5548  C  CE1    . PHE B 1 80  ? -9.23400  -42.75800 30.29500  1.000 84.68000  ? 71  PHE B CE1    1 
ATOM   5549  C  CE2    . PHE B 1 80  ? -7.99400  -42.93600 28.26200  1.000 88.49000  ? 71  PHE B CE2    1 
ATOM   5550  C  CZ     . PHE B 1 80  ? -8.13800  -43.23000 29.60200  1.000 97.12000  ? 71  PHE B CZ     1 
ATOM   5551  N  N      . THR B 1 81  ? -13.91200 -40.56100 25.62800  1.000 77.43000  ? 72  THR B N      1 
ATOM   5552  C  CA     . THR B 1 81  ? -14.97300 -39.64800 25.21800  1.000 81.50000  ? 72  THR B CA     1 
ATOM   5553  C  C      . THR B 1 81  ? -15.86400 -40.47900 24.30600  1.000 95.59000  ? 72  THR B C      1 
ATOM   5554  O  O      . THR B 1 81  ? -15.67000 -41.68800 24.14700  1.000 101.30000 ? 72  THR B O      1 
ATOM   5555  C  CB     . THR B 1 81  ? -14.41100 -38.36000 24.60000  1.000 65.00000  ? 72  THR B CB     1 
ATOM   5556  O  OG1    . THR B 1 81  ? -14.04900 -38.60000 23.23400  1.000 68.35000  ? 72  THR B OG1    1 
ATOM   5557  C  CG2    . THR B 1 81  ? -13.19400 -37.88500 25.36900  1.000 88.22000  ? 72  THR B CG2    1 
ATOM   5558  N  N      . THR B 1 82  ? -16.86400 -39.83100 23.72000  1.000 91.92000  ? 73  THR B N      1 
ATOM   5559  C  CA     . THR B 1 82  ? -17.71600 -40.53400 22.76900  1.000 100.78000 ? 73  THR B CA     1 
ATOM   5560  C  C      . THR B 1 82  ? -16.93200 -40.75700 21.48200  1.000 101.39000 ? 73  THR B C      1 
ATOM   5561  O  O      . THR B 1 82  ? -16.09100 -39.93500 21.10500  1.000 103.61000 ? 73  THR B O      1 
ATOM   5562  C  CB     . THR B 1 82  ? -19.00100 -39.73600 22.53600  1.000 106.13000 ? 73  THR B CB     1 
ATOM   5563  O  OG1    . THR B 1 82  ? -19.91600 -40.51000 21.75200  1.000 141.82000 ? 73  THR B OG1    1 
ATOM   5564  C  CG2    . THR B 1 82  ? -18.69800 -38.43400 21.81700  1.000 94.11000  ? 73  THR B CG2    1 
ATOM   5565  N  N      . TRP B 1 83  ? -17.19800 -41.88400 20.81500  1.000 91.28000  ? 74  TRP B N      1 
ATOM   5566  C  CA     . TRP B 1 83  ? -16.42500 -42.28200 19.63800  1.000 96.76000  ? 74  TRP B CA     1 
ATOM   5567  C  C      . TRP B 1 83  ? -16.44100 -41.38100 18.40500  1.000 96.18000  ? 74  TRP B C      1 
ATOM   5568  O  O      . TRP B 1 83  ? -15.45200 -41.32900 17.65400  1.000 105.50000 ? 74  TRP B O      1 
ATOM   5569  C  CB     . TRP B 1 83  ? -16.95100 -43.67600 19.29400  1.000 108.54000 ? 74  TRP B CB     1 
ATOM   5570  C  CG     . TRP B 1 83  ? -18.35700 -43.68300 18.76000  1.000 117.77000 ? 74  TRP B CG     1 
ATOM   5571  C  CD1    . TRP B 1 83  ? -19.50800 -43.83500 19.48300  1.000 119.30000 ? 74  TRP B CD1    1 
ATOM   5572  C  CD2    . TRP B 1 83  ? -18.75800 -43.57200 17.38900  1.000 111.84000 ? 74  TRP B CD2    1 
ATOM   5573  N  NE1    . TRP B 1 83  ? -20.59900 -43.80400 18.64900  1.000 115.47000 ? 74  TRP B NE1    1 
ATOM   5574  C  CE2    . TRP B 1 83  ? -20.16600 -43.64700 17.35800  1.000 112.82000 ? 74  TRP B CE2    1 
ATOM   5575  C  CE3    . TRP B 1 83  ? -18.06500 -43.40900 16.18600  1.000 102.88000 ? 74  TRP B CE3    1 
ATOM   5576  C  CZ2    . TRP B 1 83  ? -20.89100 -43.56300 16.17100  1.000 114.42000 ? 74  TRP B CZ2    1 
ATOM   5577  C  CZ3    . TRP B 1 83  ? -18.78600 -43.32600 15.01000  1.000 102.04000 ? 74  TRP B CZ3    1 
ATOM   5578  C  CH2    . TRP B 1 83  ? -20.18400 -43.40400 15.01000  1.000 101.24000 ? 74  TRP B CH2    1 
ATOM   5579  N  N      . GLN B 1 84  ? -17.54900 -40.67100 18.17500  1.000 90.94000  ? 75  GLN B N      1 
ATOM   5580  C  CA     . GLN B 1 84  ? -17.63500 -39.80600 17.00500  1.000 83.28000  ? 75  GLN B CA     1 
ATOM   5581  C  C      . GLN B 1 84  ? -16.49800 -38.79500 16.97000  1.000 93.95000  ? 75  GLN B C      1 
ATOM   5582  O  O      . GLN B 1 84  ? -16.04600 -38.40200 15.88900  1.000 98.30000  ? 75  GLN B O      1 
ATOM   5583  C  CB     . GLN B 1 84  ? -18.97900 -39.07700 16.98300  1.000 79.68000  ? 75  GLN B CB     1 
ATOM   5584  C  CG     . GLN B 1 84  ? -20.17600 -40.00000 16.80600  1.000 91.46000  ? 75  GLN B CG     1 
ATOM   5585  C  CD     . GLN B 1 84  ? -20.66400 -40.59300 18.11400  1.000 106.49000 ? 75  GLN B CD     1 
ATOM   5586  O  OE1    . GLN B 1 84  ? -20.11100 -40.32000 19.17800  1.000 121.11000 ? 75  GLN B OE1    1 
ATOM   5587  N  NE2    . GLN B 1 84  ? -21.70700 -41.41200 18.04000  1.000 125.84000 ? 75  GLN B NE2    1 
ATOM   5588  N  N      . THR B 1 85  ? -16.01700 -38.37100 18.14000  1.000 96.04000  ? 76  THR B N      1 
ATOM   5589  C  CA     . THR B 1 85  ? -14.90800 -37.42600 18.17300  1.000 97.91000  ? 76  THR B CA     1 
ATOM   5590  C  C      . THR B 1 85  ? -13.65400 -38.08600 17.61400  1.000 100.87000 ? 76  THR B C      1 
ATOM   5591  O  O      . THR B 1 85  ? -12.90000 -37.45800 16.86500  1.000 99.89000  ? 76  THR B O      1 
ATOM   5592  C  CB     . THR B 1 85  ? -14.66700 -36.89000 19.58400  1.000 87.41000  ? 76  THR B CB     1 
ATOM   5593  O  OG1    . THR B 1 85  ? -14.00000 -37.88300 20.37300  1.000 100.23000 ? 76  THR B OG1    1 
ATOM   5594  C  CG2    . THR B 1 85  ? -15.99100 -36.51000 20.23600  1.000 85.20000  ? 76  THR B CG2    1 
ATOM   5595  N  N      . GLY B 1 86  ? -13.40700 -39.35000 17.96300  1.000 93.94000  ? 77  GLY B N      1 
ATOM   5596  C  CA     . GLY B 1 86  ? -12.27400 -40.04600 17.37600  1.000 81.76000  ? 77  GLY B CA     1 
ATOM   5597  C  C      . GLY B 1 86  ? -12.41400 -40.20400 15.87400  1.000 82.75000  ? 77  GLY B C      1 
ATOM   5598  O  O      . GLY B 1 86  ? -11.45200 -40.00600 15.12000  1.000 90.24000  ? 77  GLY B O      1 
ATOM   5599  N  N      . VAL B 1 87  ? -13.62000 -40.54700 15.41300  1.000 83.36000  ? 78  VAL B N      1 
ATOM   5600  C  CA     . VAL B 1 87  ? -13.82300 -40.67800 13.97100  1.000 80.89000  ? 78  VAL B CA     1 
ATOM   5601  C  C      . VAL B 1 87  ? -13.56300 -39.34500 13.27400  1.000 88.61000  ? 78  VAL B C      1 
ATOM   5602  O  O      . VAL B 1 87  ? -12.89900 -39.28700 12.22800  1.000 95.72000  ? 78  VAL B O      1 
ATOM   5603  C  CB     . VAL B 1 87  ? -15.23400 -41.21900 13.66900  1.000 74.93000  ? 78  VAL B CB     1 
ATOM   5604  C  CG1    . VAL B 1 87  ? -15.51900 -41.14900 12.17800  1.000 53.32000  ? 78  VAL B CG1    1 
ATOM   5605  C  CG2    . VAL B 1 87  ? -15.36700 -42.65400 14.16500  1.000 72.51000  ? 78  VAL B CG2    1 
ATOM   5606  N  N      . ALA B 1 88  ? -14.06000 -38.25000 13.85400  1.000 84.06000  ? 79  ALA B N      1 
ATOM   5607  C  CA     . ALA B 1 88  ? -13.83800 -36.93200 13.26600  1.000 86.47000  ? 79  ALA B CA     1 
ATOM   5608  C  C      . ALA B 1 88  ? -12.36200 -36.55200 13.30200  1.000 91.44000  ? 79  ALA B C      1 
ATOM   5609  O  O      . ALA B 1 88  ? -11.86500 -35.87300 12.39500  1.000 93.82000  ? 79  ALA B O      1 
ATOM   5610  C  CB     . ALA B 1 88  ? -14.68700 -35.88900 13.99000  1.000 80.48000  ? 79  ALA B CB     1 
ATOM   5611  N  N      . PHE B 1 89  ? -11.65200 -36.96700 14.35200  1.000 88.66000  ? 80  PHE B N      1 
ATOM   5612  C  CA     . PHE B 1 89  ? -10.21400 -36.73900 14.41600  1.000 83.04000  ? 80  PHE B CA     1 
ATOM   5613  C  C      . PHE B 1 89  ? -9.51900  -37.39700 13.23600  1.000 84.83000  ? 80  PHE B C      1 
ATOM   5614  O  O      . PHE B 1 89  ? -8.67000  -36.78700 12.57300  1.000 79.45000  ? 80  PHE B O      1 
ATOM   5615  C  CB     . PHE B 1 89  ? -9.66300  -37.27300 15.74200  1.000 77.04000  ? 80  PHE B CB     1 
ATOM   5616  C  CG     . PHE B 1 89  ? -8.16000  -37.37900 15.78500  1.000 72.08000  ? 80  PHE B CG     1 
ATOM   5617  C  CD1    . PHE B 1 89  ? -7.51500  -38.52100 15.33100  1.000 83.00000  ? 80  PHE B CD1    1 
ATOM   5618  C  CD2    . PHE B 1 89  ? -7.39500  -36.34800 16.30300  1.000 74.38000  ? 80  PHE B CD2    1 
ATOM   5619  C  CE1    . PHE B 1 89  ? -6.13800  -38.62200 15.37500  1.000 82.51000  ? 80  PHE B CE1    1 
ATOM   5620  C  CE2    . PHE B 1 89  ? -6.01700  -36.44500 16.35100  1.000 75.13000  ? 80  PHE B CE2    1 
ATOM   5621  C  CZ     . PHE B 1 89  ? -5.38800  -37.58200 15.88600  1.000 78.68000  ? 80  PHE B CZ     1 
ATOM   5622  N  N      . LEU B 1 90  ? -9.87600  -38.65200 12.96000  1.000 86.80000  ? 81  LEU B N      1 
ATOM   5623  C  CA     . LEU B 1 90  ? -9.27600  -39.34100 11.82300  1.000 71.54000  ? 81  LEU B CA     1 
ATOM   5624  C  C      . LEU B 1 90  ? -9.60800  -38.62800 10.52100  1.000 72.50000  ? 81  LEU B C      1 
ATOM   5625  O  O      . LEU B 1 90  ? -8.73900  -38.46100 9.65200   1.000 77.74000  ? 81  LEU B O      1 
ATOM   5626  C  CB     . LEU B 1 90  ? -9.74900  -40.79300 11.77700  1.000 61.46000  ? 81  LEU B CB     1 
ATOM   5627  C  CG     . LEU B 1 90  ? -9.38800  -41.64200 12.99500  1.000 61.99000  ? 81  LEU B CG     1 
ATOM   5628  C  CD1    . LEU B 1 90  ? -9.80500  -43.08700 12.77200  1.000 75.96000  ? 81  LEU B CD1    1 
ATOM   5629  C  CD2    . LEU B 1 90  ? -7.90200  -41.54000 13.29500  1.000 72.04000  ? 81  LEU B CD2    1 
ATOM   5630  N  N      . LEU B 1 91  ? -10.85600 -38.17700 10.38300  1.000 66.48000  ? 82  LEU B N      1 
ATOM   5631  C  CA     . LEU B 1 91  ? -11.25100 -37.44700 9.18200   1.000 66.79000  ? 82  LEU B CA     1 
ATOM   5632  C  C      . LEU B 1 91  ? -10.38400 -36.21000 8.97500   1.000 71.62000  ? 82  LEU B C      1 
ATOM   5633  O  O      . LEU B 1 91  ? -9.83900  -35.99100 7.88600   1.000 87.27000  ? 82  LEU B O      1 
ATOM   5634  C  CB     . LEU B 1 91  ? -12.72900 -37.06300 9.26700   1.000 59.95000  ? 82  LEU B CB     1 
ATOM   5635  C  CG     . LEU B 1 91  ? -13.16500 -35.88600 8.38900   1.000 65.30000  ? 82  LEU B CG     1 
ATOM   5636  C  CD1    . LEU B 1 91  ? -12.89700 -36.15300 6.91500   1.000 68.39000  ? 82  LEU B CD1    1 
ATOM   5637  C  CD2    . LEU B 1 91  ? -14.63700 -35.56200 8.61400   1.000 72.14000  ? 82  LEU B CD2    1 
ATOM   5638  N  N      . GLY B 1 92  ? -10.24400 -35.38900 10.01600  1.000 66.81000  ? 83  GLY B N      1 
ATOM   5639  C  CA     . GLY B 1 92  ? -9.47300  -34.16400 9.87700   1.000 76.23000  ? 83  GLY B CA     1 
ATOM   5640  C  C      . GLY B 1 92  ? -8.00100  -34.41900 9.61900   1.000 81.56000  ? 83  GLY B C      1 
ATOM   5641  O  O      . GLY B 1 92  ? -7.37100  -33.73000 8.80500   1.000 86.36000  ? 83  GLY B O      1 
ATOM   5642  N  N      . ALA B 1 93  ? -7.42300  -35.39600 10.32000  1.000 74.82000  ? 84  ALA B N      1 
ATOM   5643  C  CA     . ALA B 1 93  ? -6.02000  -35.71500 10.09500  1.000 79.73000  ? 84  ALA B CA     1 
ATOM   5644  C  C      . ALA B 1 93  ? -5.79400  -36.15700 8.65900   1.000 87.00000  ? 84  ALA B C      1 
ATOM   5645  O  O      . ALA B 1 93  ? -4.82100  -35.73900 8.01600   1.000 92.53000  ? 84  ALA B O      1 
ATOM   5646  C  CB     . ALA B 1 93  ? -5.56000  -36.79700 11.07100  1.000 88.02000  ? 84  ALA B CB     1 
ATOM   5647  N  N      . VAL B 1 94  ? -6.68900  -36.99500 8.13300   1.000 80.56000  ? 85  VAL B N      1 
ATOM   5648  C  CA     . VAL B 1 94  ? -6.54800  -37.43100 6.75100   1.000 80.48000  ? 85  VAL B CA     1 
ATOM   5649  C  C      . VAL B 1 94  ? -6.67600  -36.24300 5.80800   1.000 93.19000  ? 85  VAL B C      1 
ATOM   5650  O  O      . VAL B 1 94  ? -5.94000  -36.13600 4.82000   1.000 93.59000  ? 85  VAL B O      1 
ATOM   5651  C  CB     . VAL B 1 94  ? -7.57800  -38.52600 6.42500   1.000 74.91000  ? 85  VAL B CB     1 
ATOM   5652  C  CG1    . VAL B 1 94  ? -7.68000  -38.71500 4.91600   1.000 95.70000  ? 85  VAL B CG1    1 
ATOM   5653  C  CG2    . VAL B 1 94  ? -7.20800  -39.82700 7.12300   1.000 82.80000  ? 85  VAL B CG2    1 
ATOM   5654  N  N      . MET B 1 95  ? -7.60200  -35.32700 6.09900   1.000 95.06000  ? 86  MET B N      1 
ATOM   5655  C  CA     . MET B 1 95  ? -7.76400  -34.14900 5.25100   1.000 92.82000  ? 86  MET B CA     1 
ATOM   5656  C  C      . MET B 1 95  ? -6.47100  -33.34600 5.18100   1.000 94.10000  ? 86  MET B C      1 
ATOM   5657  O  O      . MET B 1 95  ? -5.99200  -32.99200 4.09300   1.000 101.21000 ? 86  MET B O      1 
ATOM   5658  C  CB     . MET B 1 95  ? -8.90400  -33.27700 5.78000   1.000 80.63000  ? 86  MET B CB     1 
ATOM   5659  C  CG     . MET B 1 95  ? -10.28100 -33.90500 5.66700   1.000 87.37000  ? 86  MET B CG     1 
ATOM   5660  S  SD     . MET B 1 95  ? -10.85900 -33.92600 3.96500   1.000 90.37000  ? 86  MET B SD     1 
ATOM   5661  C  CE     . MET B 1 95  ? -10.03100 -35.39500 3.36200   1.000 92.72000  ? 86  MET B CE     1 
ATOM   5662  N  N      . SER B 1 96  ? -5.89100  -33.04900 6.34500   1.000 84.83000  ? 87  SER B N      1 
ATOM   5663  C  CA     . SER B 1 96  ? -4.68500  -32.23000 6.37300   1.000 95.68000  ? 87  SER B CA     1 
ATOM   5664  C  C      . SER B 1 96  ? -3.52300  -32.94300 5.69300   1.000 90.05000  ? 87  SER B C      1 
ATOM   5665  O  O      . SER B 1 96  ? -2.76300  -32.32600 4.93200   1.000 95.71000  ? 87  SER B O      1 
ATOM   5666  C  CB     . SER B 1 96  ? -4.33100  -31.86500 7.81400   1.000 100.03000 ? 87  SER B CB     1 
ATOM   5667  O  OG     . SER B 1 96  ? -5.39300  -31.17300 8.45200   1.000 106.38000 ? 87  SER B OG     1 
ATOM   5668  N  N      . ALA B 1 97  ? -3.37300  -34.24500 5.94600   1.000 83.39000  ? 88  ALA B N      1 
ATOM   5669  C  CA     . ALA B 1 97  ? -2.29700  -34.98700 5.30500   1.000 83.82000  ? 88  ALA B CA     1 
ATOM   5670  C  C      . ALA B 1 97  ? -2.46000  -34.97900 3.79300   1.000 91.88000  ? 88  ALA B C      1 
ATOM   5671  O  O      . ALA B 1 97  ? -1.47700  -34.84200 3.05300   1.000 102.37000 ? 88  ALA B O      1 
ATOM   5672  C  CB     . ALA B 1 97  ? -2.25700  -36.41800 5.84000   1.000 68.44000  ? 88  ALA B CB     1 
ATOM   5673  N  N      . SER B 1 98  ? -3.69900  -35.11800 3.31500   1.000 72.34000  ? 89  SER B N      1 
ATOM   5674  C  CA     . SER B 1 98  ? -3.95500  -35.08800 1.88000   1.000 89.67000  ? 89  SER B CA     1 
ATOM   5675  C  C      . SER B 1 98  ? -3.57100  -33.74100 1.28400   1.000 95.76000  ? 89  SER B C      1 
ATOM   5676  O  O      . SER B 1 98  ? -2.91800  -33.67400 0.23600   1.000 107.47000 ? 89  SER B O      1 
ATOM   5677  C  CB     . SER B 1 98  ? -5.42700  -35.39700 1.60900   1.000 90.18000  ? 89  SER B CB     1 
ATOM   5678  O  OG     . SER B 1 98  ? -5.72200  -36.75700 1.87800   1.000 108.99000 ? 89  SER B OG     1 
ATOM   5679  N  N      . ALA B 1 99  ? -3.98100  -32.65100 1.93700   1.000 88.25000  ? 90  ALA B N      1 
ATOM   5680  C  CA     . ALA B 1 99  ? -3.63600  -31.32600 1.42900   1.000 97.09000  ? 90  ALA B CA     1 
ATOM   5681  C  C      . ALA B 1 99  ? -2.12500  -31.15800 1.33400   1.000 95.66000  ? 90  ALA B C      1 
ATOM   5682  O  O      . ALA B 1 99  ? -1.59600  -30.71900 0.30100   1.000 95.25000  ? 90  ALA B O      1 
ATOM   5683  C  CB     . ALA B 1 99  ? -4.24400  -30.24400 2.32200   1.000 101.11000 ? 90  ALA B CB     1 
ATOM   5684  N  N      . GLY B 1 100 ? -1.41100  -31.52800 2.40000   1.000 98.71000  ? 91  GLY B N      1 
ATOM   5685  C  CA     . GLY B 1 100 ? 0.03400   -31.36400 2.39600   1.000 101.80000 ? 91  GLY B CA     1 
ATOM   5686  C  C      . GLY B 1 100 ? 0.70700   -32.18800 1.31600   1.000 100.13000 ? 91  GLY B C      1 
ATOM   5687  O  O      . GLY B 1 100 ? 1.56900   -31.69300 0.57900   1.000 106.15000 ? 91  GLY B O      1 
ATOM   5688  N  N      . ILE B 1 101 ? 0.32500   -33.46300 1.20800   1.000 89.06000  ? 92  ILE B N      1 
ATOM   5689  C  CA     . ILE B 1 101 ? 0.94400   -34.33000 0.21400   1.000 84.68000  ? 92  ILE B CA     1 
ATOM   5690  C  C      . ILE B 1 101 ? 0.67100   -33.80500 -1.18600  1.000 87.76000  ? 92  ILE B C      1 
ATOM   5691  O  O      . ILE B 1 101 ? 1.56200   -33.79300 -2.04300  1.000 97.66000  ? 92  ILE B O      1 
ATOM   5692  C  CB     . ILE B 1 101 ? 0.45300   -35.77900 0.38200   1.000 87.66000  ? 92  ILE B CB     1 
ATOM   5693  C  CG1    . ILE B 1 101 ? 0.86800   -36.32500 1.74900   1.000 82.65000  ? 92  ILE B CG1    1 
ATOM   5694  C  CG2    . ILE B 1 101 ? 0.99600   -36.65800 -0.73200  1.000 103.26000 ? 92  ILE B CG2    1 
ATOM   5695  C  CD1    . ILE B 1 101 ? 0.52100   -37.78200 1.94300   1.000 97.20000  ? 92  ILE B CD1    1 
ATOM   5696  N  N      . VAL B 1 102 ? -0.56200  -33.36500 -1.44400  1.000 78.43000  ? 93  VAL B N      1 
ATOM   5697  C  CA     . VAL B 1 102 ? -0.89800  -32.85500 -2.77000  1.000 93.58000  ? 93  VAL B CA     1 
ATOM   5698  C  C      . VAL B 1 102 ? -0.03200  -31.65100 -3.10500  1.000 101.12000 ? 93  VAL B C      1 
ATOM   5699  O  O      . VAL B 1 102 ? 0.57700   -31.57800 -4.18200  1.000 110.20000 ? 93  VAL B O      1 
ATOM   5700  C  CB     . VAL B 1 102 ? -2.39500  -32.50300 -2.84700  1.000 91.94000  ? 93  VAL B CB     1 
ATOM   5701  C  CG1    . VAL B 1 102 ? -2.65600  -31.55900 -4.01300  1.000 71.58000  ? 93  VAL B CG1    1 
ATOM   5702  C  CG2    . VAL B 1 102 ? -3.23200  -33.76300 -2.97900  1.000 112.93000 ? 93  VAL B CG2    1 
ATOM   5703  N  N      . GLY B 1 103 ? 0.04200   -30.68900 -2.18200  1.000 94.95000  ? 94  GLY B N      1 
ATOM   5704  C  CA     . GLY B 1 103 ? 0.82600   -29.49800 -2.45800  1.000 84.45000  ? 94  GLY B CA     1 
ATOM   5705  C  C      . GLY B 1 103 ? 2.28800   -29.81400 -2.70900  1.000 87.78000  ? 94  GLY B C      1 
ATOM   5706  O  O      . GLY B 1 103 ? 2.88300   -29.33900 -3.68300  1.000 93.56000  ? 94  GLY B O      1 
ATOM   5707  N  N      . MET B 1 104 ? 2.87600   -30.66300 -1.86200  1.000 93.51000  ? 95  MET B N      1 
ATOM   5708  C  CA     . MET B 1 104 ? 4.29700   -30.96200 -2.01900  1.000 103.19000 ? 95  MET B CA     1 
ATOM   5709  C  C      . MET B 1 104 ? 4.56300   -31.74700 -3.29800  1.000 106.35000 ? 95  MET B C      1 
ATOM   5710  O  O      . MET B 1 104 ? 5.55300   -31.49000 -3.99500  1.000 107.10000 ? 95  MET B O      1 
ATOM   5711  C  CB     . MET B 1 104 ? 4.82800   -31.71200 -0.79800  1.000 105.97000 ? 95  MET B CB     1 
ATOM   5712  C  CG     . MET B 1 104 ? 4.87400   -30.87400 0.47200   1.000 107.56000 ? 95  MET B CG     1 
ATOM   5713  S  SD     . MET B 1 104 ? 6.17400   -31.38200 1.62000   1.000 107.76000 ? 95  MET B SD     1 
ATOM   5714  C  CE     . MET B 1 104 ? 7.64200   -30.89800 0.71300   1.000 92.53000  ? 95  MET B CE     1 
ATOM   5715  N  N      . LYS B 1 105 ? 3.70200   -32.71600 -3.61900  1.000 104.97000 ? 96  LYS B N      1 
ATOM   5716  C  CA     . LYS B 1 105 ? 3.88200   -33.48300 -4.84500  1.000 108.91000 ? 96  LYS B CA     1 
ATOM   5717  C  C      . LYS B 1 105 ? 3.69700   -32.49800 -5.99100  1.000 116.70000 ? 96  LYS B C      1 
ATOM   5718  O  O      . LYS B 1 105 ? 4.47500   -32.49600 -6.95100  1.000 128.70000 ? 96  LYS B O      1 
ATOM   5719  C  CB     . LYS B 1 105 ? 2.82700   -34.58600 -4.93600  1.000 87.78000  ? 96  LYS B CB     1 
ATOM   5720  N  N      . MET B 1 106 ? 2.67400   -31.64600 -5.90700  1.000 106.27000 ? 97  MET B N      1 
ATOM   5721  C  CA     . MET B 1 106 ? 2.50500   -30.65000 -6.96600  1.000 101.38000 ? 97  MET B CA     1 
ATOM   5722  C  C      . MET B 1 106 ? 3.79000   -29.82700 -7.21100  1.000 108.25000 ? 97  MET B C      1 
ATOM   5723  O  O      . MET B 1 106 ? 4.32300   -29.74300 -8.32300  1.000 117.01000 ? 97  MET B O      1 
ATOM   5724  C  CB     . MET B 1 106 ? 1.26900   -29.78800 -6.69000  1.000 105.61000 ? 97  MET B CB     1 
ATOM   5725  C  CG     . MET B 1 106 ? 0.99500   -28.67900 -7.72100  1.000 85.62000  ? 97  MET B CG     1 
ATOM   5726  S  SD     . MET B 1 106 ? 0.52600   -29.17300 -9.38600  1.000 99.78000  ? 97  MET B SD     1 
ATOM   5727  C  CE     . MET B 1 106 ? 0.35200   -27.57800 -10.19300 1.000 128.93000 ? 97  MET B CE     1 
ATOM   5728  N  N      . ALA B 1 107 ? 4.32400   -29.26200 -6.12100  1.000 108.45000 ? 98  ALA B N      1 
ATOM   5729  C  CA     . ALA B 1 107 ? 5.52400   -28.43300 -6.21900  1.000 112.32000 ? 98  ALA B CA     1 
ATOM   5730  C  C      . ALA B 1 107 ? 6.84800   -29.06800 -6.63200  1.000 116.09000 ? 98  ALA B C      1 
ATOM   5731  O  O      . ALA B 1 107 ? 7.62000   -28.46400 -7.38700  1.000 121.77000 ? 98  ALA B O      1 
ATOM   5732  C  CB     . ALA B 1 107 ? 5.66100   -27.78600 -4.84000  1.000 125.01000 ? 98  ALA B CB     1 
ATOM   5733  N  N      . THR B 1 108 ? 7.14300   -30.27300 -6.13600  1.000 111.18000 ? 99  THR B N      1 
ATOM   5734  C  CA     . THR B 1 108 ? 8.43200   -30.89100 -6.43900  1.000 120.44000 ? 99  THR B CA     1 
ATOM   5735  C  C      . THR B 1 108 ? 8.63700   -31.02600 -7.94100  1.000 134.63000 ? 99  THR B C      1 
ATOM   5736  O  O      . THR B 1 108 ? 9.75400   -30.84300 -8.44400  1.000 133.17000 ? 99  THR B O      1 
ATOM   5737  C  CB     . THR B 1 108 ? 8.52600   -32.25500 -5.76700  1.000 129.78000 ? 99  THR B CB     1 
ATOM   5738  O  OG1    . THR B 1 108 ? 7.35500   -33.00700 -6.09600  1.000 138.86000 ? 99  THR B OG1    1 
ATOM   5739  C  CG2    . THR B 1 108 ? 8.59400   -32.09100 -4.26200  1.000 136.60000 ? 99  THR B CG2    1 
ATOM   5740  N  N      . ARG B 1 109 ? 7.57000   -31.32900 -8.67400  1.000 136.31000 ? 100 ARG B N      1 
ATOM   5741  C  CA     . ARG B 1 109 ? 7.64200   -31.40400 -10.12200 1.000 128.52000 ? 100 ARG B CA     1 
ATOM   5742  C  C      . ARG B 1 109 ? 7.30400   -30.07000 -10.79300 1.000 136.07000 ? 100 ARG B C      1 
ATOM   5743  O  O      . ARG B 1 109 ? 7.35800   -29.98100 -12.02400 1.000 148.32000 ? 100 ARG B O      1 
ATOM   5744  C  CB     . ARG B 1 109 ? 6.72700   -32.53300 -10.63100 1.000 105.32000 ? 100 ARG B CB     1 
ATOM   5745  N  N      . ALA B 1 110 ? 7.02200   -29.01300 -10.02400 1.000 128.89000 ? 101 ALA B N      1 
ATOM   5746  C  CA     . ALA B 1 110 ? 6.61800   -27.74500 -10.61200 1.000 123.45000 ? 101 ALA B CA     1 
ATOM   5747  C  C      . ALA B 1 110 ? 7.79400   -26.79000 -10.49700 1.000 126.18000 ? 101 ALA B C      1 
ATOM   5748  O  O      . ALA B 1 110 ? 7.80000   -25.75200 -11.16600 1.000 129.48000 ? 101 ALA B O      1 
ATOM   5749  C  CB     . ALA B 1 110 ? 5.36900   -27.20200 -9.90200  1.000 107.93000 ? 101 ALA B CB     1 
ATOM   5750  N  N      . ASN B 1 111 ? 8.79400   -27.12800 -9.68200  1.000 114.79000 ? 102 ASN B N      1 
ATOM   5751  C  CA     . ASN B 1 111 ? 9.92700   -26.22900 -9.49700  1.000 116.92000 ? 102 ASN B CA     1 
ATOM   5752  C  C      . ASN B 1 111 ? 10.64600  -25.92100 -10.82400 1.000 145.86000 ? 102 ASN B C      1 
ATOM   5753  O  O      . ASN B 1 111 ? 10.85900  -24.76100 -11.19500 1.000 143.15000 ? 102 ASN B O      1 
ATOM   5754  C  CB     . ASN B 1 111 ? 10.84200  -26.78400 -8.40500  1.000 122.14000 ? 102 ASN B CB     1 
ATOM   5755  C  CG     . ASN B 1 111 ? 11.48600  -28.10100 -8.78600  1.000 140.09000 ? 102 ASN B CG     1 
ATOM   5756  O  OD1    . ASN B 1 111 ? 11.09300  -28.74800 -9.75800  1.000 141.80000 ? 102 ASN B OD1    1 
ATOM   5757  N  ND2    . ASN B 1 111 ? 12.47900  -28.51300 -8.00700  1.000 135.64000 ? 102 ASN B ND2    1 
ATOM   5758  N  N      . VAL B 1 112 ? 11.01200  -26.97400 -11.55600 1.000 156.52000 ? 103 VAL B N      1 
ATOM   5759  C  CA     . VAL B 1 112 ? 11.64300  -26.80000 -12.86300 1.000 152.60000 ? 103 VAL B CA     1 
ATOM   5760  C  C      . VAL B 1 112 ? 10.75300  -26.31700 -14.00600 1.000 151.58000 ? 103 VAL B C      1 
ATOM   5761  O  O      . VAL B 1 112 ? 11.22700  -25.64800 -14.93700 1.000 151.51000 ? 103 VAL B O      1 
ATOM   5762  C  CB     . VAL B 1 112 ? 12.25300  -28.17800 -13.15600 1.000 141.81000 ? 103 VAL B CB     1 
ATOM   5763  C  CG1    . VAL B 1 112 ? 11.14900  -29.19400 -13.33100 1.000 127.59000 ? 103 VAL B CG1    1 
ATOM   5764  C  CG2    . VAL B 1 112 ? 13.11700  -28.12900 -14.39800 1.000 152.81000 ? 103 VAL B CG2    1 
ATOM   5765  N  N      . ARG B 1 113 ? 9.46400   -26.65900 -13.96000 1.000 148.48000 ? 104 ARG B N      1 
ATOM   5766  C  CA     . ARG B 1 113 ? 8.53900   -26.24300 -15.00500 1.000 150.47000 ? 104 ARG B CA     1 
ATOM   5767  C  C      . ARG B 1 113 ? 8.51100   -24.72900 -15.15400 1.000 153.50000 ? 104 ARG B C      1 
ATOM   5768  O  O      . ARG B 1 113 ? 8.52000   -24.20900 -16.27600 1.000 163.58000 ? 104 ARG B O      1 
ATOM   5769  C  CB     . ARG B 1 113 ? 7.14200   -26.78000 -14.70200 1.000 141.90000 ? 104 ARG B CB     1 
ATOM   5770  N  N      . VAL B 1 114 ? 8.47300   -24.00200 -14.03500 1.000 145.48000 ? 105 VAL B N      1 
ATOM   5771  C  CA     . VAL B 1 114 ? 8.43600   -22.54500 -14.10500 1.000 150.48000 ? 105 VAL B CA     1 
ATOM   5772  C  C      . VAL B 1 114 ? 9.71800   -22.02500 -14.73900 1.000 167.13000 ? 105 VAL B C      1 
ATOM   5773  O  O      . VAL B 1 114 ? 9.70100   -21.06300 -15.51800 1.000 169.98000 ? 105 VAL B O      1 
ATOM   5774  C  CB     . VAL B 1 114 ? 8.19800   -21.94100 -12.70800 1.000 143.72000 ? 105 VAL B CB     1 
ATOM   5775  C  CG1    . VAL B 1 114 ? 6.89000   -22.46300 -12.12000 1.000 132.41000 ? 105 VAL B CG1    1 
ATOM   5776  C  CG2    . VAL B 1 114 ? 9.36200   -22.25400 -11.78500 1.000 150.98000 ? 105 VAL B CG2    1 
ATOM   5777  N  N      . ALA B 1 115 ? 10.85300  -22.64900 -14.41500 1.000 168.91000 ? 106 ALA B N      1 
ATOM   5778  C  CA     . ALA B 1 115 ? 12.11500  -22.24800 -15.02600 1.000 159.98000 ? 106 ALA B CA     1 
ATOM   5779  C  C      . ALA B 1 115 ? 12.05500  -22.42200 -16.53700 1.000 163.73000 ? 106 ALA B C      1 
ATOM   5780  O  O      . ALA B 1 115 ? 12.47400  -21.53800 -17.29500 1.000 160.62000 ? 106 ALA B O      1 
ATOM   5781  C  CB     . ALA B 1 115 ? 13.27100  -23.05000 -14.42900 1.000 140.08000 ? 106 ALA B CB     1 
ATOM   5782  N  N      . GLU B 1 116 ? 11.55000  -23.57000 -16.99700 1.000 164.68000 ? 107 GLU B N      1 
ATOM   5783  C  CA     . GLU B 1 116 ? 11.37300  -23.75600 -18.43200 1.000 156.33000 ? 107 GLU B CA     1 
ATOM   5784  C  C      . GLU B 1 116 ? 10.38300  -22.74900 -18.99900 1.000 149.46000 ? 107 GLU B C      1 
ATOM   5785  O  O      . GLU B 1 116 ? 10.52400  -22.32100 -20.15000 1.000 149.84000 ? 107 GLU B O      1 
ATOM   5786  C  CB     . GLU B 1 116 ? 10.90700  -25.18100 -18.73000 1.000 158.08000 ? 107 GLU B CB     1 
ATOM   5787  C  CG     . GLU B 1 116 ? 10.20000  -25.33200 -20.07300 1.000 157.29000 ? 107 GLU B CG     1 
ATOM   5788  C  CD     . GLU B 1 116 ? 11.15000  -25.26700 -21.25600 1.000 167.13000 ? 107 GLU B CD     1 
ATOM   5789  O  OE1    . GLU B 1 116 ? 11.33300  -26.30300 -21.93000 1.000 163.34000 ? 107 GLU B OE1    1 
ATOM   5790  O  OE2    . GLU B 1 116 ? 11.71600  -24.18300 -21.51300 1.000 164.67000 ? 107 GLU B OE2    1 
ATOM   5791  N  N      . ALA B 1 117 ? 9.37500   -22.36500 -18.21400 1.000 151.45000 ? 108 ALA B N      1 
ATOM   5792  C  CA     . ALA B 1 117 ? 8.46100   -21.31300 -18.64400 1.000 154.07000 ? 108 ALA B CA     1 
ATOM   5793  C  C      . ALA B 1 117 ? 9.17100   -19.96800 -18.74600 1.000 166.83000 ? 108 ALA B C      1 
ATOM   5794  O  O      . ALA B 1 117 ? 8.89400   -19.18100 -19.65900 1.000 179.44000 ? 108 ALA B O      1 
ATOM   5795  C  CB     . ALA B 1 117 ? 7.27200   -21.22400 -17.68800 1.000 134.41000 ? 108 ALA B CB     1 
ATOM   5796  N  N      . ALA B 1 118 ? 10.08200  -19.68200 -17.81200 1.000 156.29000 ? 109 ALA B N      1 
ATOM   5797  C  CA     . ALA B 1 118 ? 10.80100  -18.41100 -17.83700 1.000 148.60000 ? 109 ALA B CA     1 
ATOM   5798  C  C      . ALA B 1 118 ? 11.64200  -18.26400 -19.09900 1.000 159.65000 ? 109 ALA B C      1 
ATOM   5799  O  O      . ALA B 1 118 ? 11.68000  -17.18600 -19.70400 1.000 157.02000 ? 109 ALA B O      1 
ATOM   5800  C  CB     . ALA B 1 118 ? 11.67500  -18.27900 -16.59000 1.000 142.65000 ? 109 ALA B CB     1 
ATOM   5801  N  N      . ARG B 1 119 ? 12.33600  -19.33000 -19.50500 1.000 168.66000 ? 110 ARG B N      1 
ATOM   5802  C  CA     . ARG B 1 119 ? 13.14300  -19.26500 -20.71900 1.000 153.34000 ? 110 ARG B CA     1 
ATOM   5803  C  C      . ARG B 1 119 ? 12.27000  -19.21900 -21.96800 1.000 163.04000 ? 110 ARG B C      1 
ATOM   5804  O  O      . ARG B 1 119 ? 12.53900  -18.43900 -22.88900 1.000 169.96000 ? 110 ARG B O      1 
ATOM   5805  C  CB     . ARG B 1 119 ? 14.09800  -20.45400 -20.77800 1.000 129.65000 ? 110 ARG B CB     1 
ATOM   5806  C  CG     . ARG B 1 119 ? 14.55500  -20.80400 -22.18300 1.000 141.51000 ? 110 ARG B CG     1 
ATOM   5807  C  CD     . ARG B 1 119 ? 15.44600  -22.03600 -22.18200 1.000 166.32000 ? 110 ARG B CD     1 
ATOM   5808  N  NE     . ARG B 1 119 ? 14.71400  -23.24500 -21.82500 1.000 166.06000 ? 110 ARG B NE     1 
ATOM   5809  C  CZ     . ARG B 1 119 ? 14.74700  -23.81500 -20.62800 1.000 158.86000 ? 110 ARG B CZ     1 
ATOM   5810  N  NH1    . ARG B 1 119 ? 15.46300  -23.30500 -19.63900 1.000 156.83000 ? 110 ARG B NH1    1 
ATOM   5811  N  NH2    . ARG B 1 119 ? 14.04800  -24.92700 -20.41900 1.000 153.36000 ? 110 ARG B NH2    1 
ATOM   5812  N  N      . THR B 1 120 ? 11.22600  -20.05100 -22.02500 1.000 165.84000 ? 111 THR B N      1 
ATOM   5813  C  CA     . THR B 1 120 ? 10.37600  -20.08200 -23.21400 1.000 164.43000 ? 111 THR B CA     1 
ATOM   5814  C  C      . THR B 1 120 ? 9.54300   -18.81200 -23.32900 1.000 166.62000 ? 111 THR B C      1 
ATOM   5815  O  O      . THR B 1 120 ? 9.30500   -18.31700 -24.43700 1.000 172.17000 ? 111 THR B O      1 
ATOM   5816  C  CB     . THR B 1 120 ? 9.47300   -21.31800 -23.20800 1.000 163.99000 ? 111 THR B CB     1 
ATOM   5817  O  OG1    . THR B 1 120 ? 9.01300   -21.57900 -24.54100 1.000 147.77000 ? 111 THR B OG1    1 
ATOM   5818  C  CG2    . THR B 1 120 ? 8.27300   -21.12200 -22.29300 1.000 169.00000 ? 111 THR B CG2    1 
ATOM   5819  N  N      . THR B 1 121 ? 9.07300   -18.28800 -22.20200 1.000 165.68000 ? 112 THR B N      1 
ATOM   5820  C  CA     . THR B 1 121 ? 8.27400   -17.07200 -22.16200 1.000 167.22000 ? 112 THR B CA     1 
ATOM   5821  C  C      . THR B 1 121 ? 9.10700   -15.82700 -21.88500 1.000 158.69000 ? 112 THR B C      1 
ATOM   5822  O  O      . THR B 1 121 ? 8.55200   -14.72500 -21.83200 1.000 149.43000 ? 112 THR B O      1 
ATOM   5823  C  CB     . THR B 1 121 ? 7.17200   -17.19800 -21.10500 1.000 161.45000 ? 112 THR B CB     1 
ATOM   5824  O  OG1    . THR B 1 121 ? 7.74400   -17.07600 -19.79500 1.000 168.07000 ? 112 THR B OG1    1 
ATOM   5825  C  CG2    . THR B 1 121 ? 6.45900   -18.54600 -21.22700 1.000 163.79000 ? 112 THR B CG2    1 
ATOM   5826  N  N      . LYS B 1 122 ? 10.41500  -15.97900 -21.70100 1.000 156.36000 ? 113 LYS B N      1 
ATOM   5827  C  CA     . LYS B 1 122 ? 11.30400  -14.85000 -21.44900 1.000 154.86000 ? 113 LYS B CA     1 
ATOM   5828  C  C      . LYS B 1 122 ? 10.86200  -14.05500 -20.22500 1.000 157.17000 ? 113 LYS B C      1 
ATOM   5829  O  O      . LYS B 1 122 ? 11.49200  -14.12300 -19.16900 1.000 147.56000 ? 113 LYS B O      1 
ATOM   5830  C  CB     . LYS B 1 122 ? 11.36500  -13.93500 -22.67200 1.000 124.82000 ? 113 LYS B CB     1 
ATOM   5831  N  N      . ILE B 1 124 ? 10.20600  -14.27200 -16.88000 1.000 138.49000 ? 115 ILE B N      1 
ATOM   5832  C  CA     . ILE B 1 124 ? 9.39100   -13.08000 -16.66000 1.000 155.89000 ? 115 ILE B CA     1 
ATOM   5833  C  C      . ILE B 1 124 ? 8.05500   -13.18100 -17.39400 1.000 147.79000 ? 115 ILE B C      1 
ATOM   5834  O  O      . ILE B 1 124 ? 7.97300   -13.78900 -18.46000 1.000 156.03000 ? 115 ILE B O      1 
ATOM   5835  C  CB     . ILE B 1 124 ? 10.14300  -11.81000 -17.09400 1.000 142.51000 ? 115 ILE B CB     1 
ATOM   5836  C  CG1    . ILE B 1 124 ? 9.74800   -10.62700 -16.20800 1.000 132.47000 ? 115 ILE B CG1    1 
ATOM   5837  C  CG2    . ILE B 1 124 ? 9.88200   -11.51300 -18.56700 1.000 154.39000 ? 115 ILE B CG2    1 
ATOM   5838  C  CD1    . ILE B 1 124 ? 10.54000  -9.37000  -16.48200 1.000 115.13000 ? 115 ILE B CD1    1 
ATOM   5839  N  N      . GLY B 1 125 ? 7.01400   -12.58400 -16.81300 1.000 124.95000 ? 116 GLY B N      1 
ATOM   5840  C  CA     . GLY B 1 125 ? 5.68700   -12.59300 -17.38500 1.000 123.31000 ? 116 GLY B CA     1 
ATOM   5841  C  C      . GLY B 1 125 ? 4.96100   -13.92600 -17.31000 1.000 145.90000 ? 116 GLY B C      1 
ATOM   5842  O  O      . GLY B 1 125 ? 4.41000   -14.29700 -16.27000 1.000 157.45000 ? 116 GLY B O      1 
ATOM   5843  N  N      . PRO B 1 126 ? 4.93700   -14.66700 -18.42400 1.000 147.12000 ? 117 PRO B N      1 
ATOM   5844  C  CA     . PRO B 1 126 ? 4.17400   -15.93200 -18.46100 1.000 153.90000 ? 117 PRO B CA     1 
ATOM   5845  C  C      . PRO B 1 126 ? 4.65800   -16.99400 -17.48600 1.000 145.92000 ? 117 PRO B C      1 
ATOM   5846  O  O      . PRO B 1 126 ? 3.84400   -17.78400 -16.99000 1.000 141.20000 ? 117 PRO B O      1 
ATOM   5847  C  CB     . PRO B 1 126 ? 4.33600   -16.39200 -19.91800 1.000 158.37000 ? 117 PRO B CB     1 
ATOM   5848  C  CG     . PRO B 1 126 ? 4.65100   -15.13200 -20.67300 1.000 158.15000 ? 117 PRO B CG     1 
ATOM   5849  C  CD     . PRO B 1 126 ? 5.52700   -14.35400 -19.73600 1.000 148.45000 ? 117 PRO B CD     1 
ATOM   5850  N  N      . ALA B 1 127 ? 5.96400   -17.05900 -17.21500 1.000 140.05000 ? 118 ALA B N      1 
ATOM   5851  C  CA     . ALA B 1 127 ? 6.47800   -18.07100 -16.29700 1.000 122.76000 ? 118 ALA B CA     1 
ATOM   5852  C  C      . ALA B 1 127 ? 5.83500   -17.95300 -14.92200 1.000 126.70000 ? 118 ALA B C      1 
ATOM   5853  O  O      . ALA B 1 127 ? 5.60000   -18.96500 -14.25100 1.000 125.77000 ? 118 ALA B O      1 
ATOM   5854  C  CB     . ALA B 1 127 ? 7.99800   -17.96300 -16.19000 1.000 119.14000 ? 118 ALA B CB     1 
ATOM   5855  N  N      . LEU B 1 128 ? 5.54300   -16.72700 -14.48200 1.000 137.52000 ? 119 LEU B N      1 
ATOM   5856  C  CA     . LEU B 1 128 ? 4.91500   -16.54100 -13.17700 1.000 142.35000 ? 119 LEU B CA     1 
ATOM   5857  C  C      . LEU B 1 128 ? 3.53900   -17.19200 -13.11400 1.000 139.52000 ? 119 LEU B C      1 
ATOM   5858  O  O      . LEU B 1 128 ? 3.13700   -17.69400 -12.05600 1.000 131.22000 ? 119 LEU B O      1 
ATOM   5859  C  CB     . LEU B 1 128 ? 4.81200   -15.05300 -12.85300 1.000 132.78000 ? 119 LEU B CB     1 
ATOM   5860  N  N      . LYS B 1 129 ? 2.80200   -17.18700 -14.22800 1.000 140.60000 ? 120 LYS B N      1 
ATOM   5861  C  CA     . LYS B 1 129 ? 1.50300   -17.85100 -14.25800 1.000 127.16000 ? 120 LYS B CA     1 
ATOM   5862  C  C      . LYS B 1 129 ? 1.62200   -19.32000 -13.87000 1.000 137.07000 ? 120 LYS B C      1 
ATOM   5863  O  O      . LYS B 1 129 ? 0.77400   -19.84500 -13.14100 1.000 145.55000 ? 120 LYS B O      1 
ATOM   5864  C  CB     . LYS B 1 129 ? 0.86800   -17.70700 -15.64200 1.000 115.59000 ? 120 LYS B CB     1 
ATOM   5865  C  CG     . LYS B 1 129 ? -0.41900  -18.50300 -15.82200 1.000 118.86000 ? 120 LYS B CG     1 
ATOM   5866  C  CD     . LYS B 1 129 ? -0.98900  -18.34100 -17.22600 1.000 133.42000 ? 120 LYS B CD     1 
ATOM   5867  C  CE     . LYS B 1 129 ? -1.14500  -16.87100 -17.58900 1.000 128.30000 ? 120 LYS B CE     1 
ATOM   5868  N  NZ     . LYS B 1 129 ? -2.13200  -16.67100 -18.68500 1.000 124.07000 ? 120 LYS B NZ     1 
ATOM   5869  N  N      . VAL B 1 130 ? 2.67300   -19.99800 -14.33800 1.000 137.74000 ? 121 VAL B N      1 
ATOM   5870  C  CA     . VAL B 1 130 ? 2.85800   -21.40900 -14.00800 1.000 133.33000 ? 121 VAL B CA     1 
ATOM   5871  C  C      . VAL B 1 130 ? 3.09800   -21.58400 -12.51200 1.000 148.63000 ? 121 VAL B C      1 
ATOM   5872  O  O      . VAL B 1 130 ? 2.51300   -22.46500 -11.86700 1.000 150.82000 ? 121 VAL B O      1 
ATOM   5873  C  CB     . VAL B 1 130 ? 4.01400   -22.00200 -14.83500 1.000 115.50000 ? 121 VAL B CB     1 
ATOM   5874  C  CG1    . VAL B 1 130 ? 4.20600   -23.47000 -14.50200 1.000 130.54000 ? 121 VAL B CG1    1 
ATOM   5875  C  CG2    . VAL B 1 130 ? 3.75600   -21.81600 -16.32600 1.000 119.52000 ? 121 VAL B CG2    1 
ATOM   5876  N  N      . ALA B 1 131 ? 3.96300   -20.74800 -11.93700 1.000 145.13000 ? 122 ALA B N      1 
ATOM   5877  C  CA     . ALA B 1 131 ? 4.26900   -20.86700 -10.51500 1.000 143.28000 ? 122 ALA B CA     1 
ATOM   5878  C  C      . ALA B 1 131 ? 3.03700   -20.59800 -9.66000  1.000 143.53000 ? 122 ALA B C      1 
ATOM   5879  O  O      . ALA B 1 131 ? 2.82200   -21.25900 -8.63300  1.000 136.26000 ? 122 ALA B O      1 
ATOM   5880  C  CB     . ALA B 1 131 ? 5.40400   -19.91400 -10.14300 1.000 130.07000 ? 122 ALA B CB     1 
ATOM   5881  N  N      . TYR B 1 132 ? 2.21600   -19.62400 -10.06000 1.000 136.35000 ? 123 TYR B N      1 
ATOM   5882  C  CA     . TYR B 1 132 ? 1.02300   -19.32100 -9.27900  1.000 128.33000 ? 123 TYR B CA     1 
ATOM   5883  C  C      . TYR B 1 132 ? -0.03000  -20.41100 -9.43800  1.000 127.52000 ? 123 TYR B C      1 
ATOM   5884  O  O      . TYR B 1 132 ? -0.72400  -20.75200 -8.47400  1.000 124.55000 ? 123 TYR B O      1 
ATOM   5885  C  CB     . TYR B 1 132 ? 0.45500   -17.96000 -9.68000  1.000 145.53000 ? 123 TYR B CB     1 
ATOM   5886  C  CG     . TYR B 1 132 ? -0.73800  -17.53300 -8.85100  1.000 140.60000 ? 123 TYR B CG     1 
ATOM   5887  C  CD1    . TYR B 1 132 ? -0.57600  -17.11100 -7.53700  1.000 137.88000 ? 123 TYR B CD1    1 
ATOM   5888  C  CD2    . TYR B 1 132 ? -2.02200  -17.55500 -9.37800  1.000 140.31000 ? 123 TYR B CD2    1 
ATOM   5889  C  CE1    . TYR B 1 132 ? -1.65900  -16.71900 -6.77400  1.000 147.56000 ? 123 TYR B CE1    1 
ATOM   5890  C  CE2    . TYR B 1 132 ? -3.11300  -17.16500 -8.62200  1.000 151.44000 ? 123 TYR B CE2    1 
ATOM   5891  C  CZ     . TYR B 1 132 ? -2.92600  -16.74900 -7.32000  1.000 155.54000 ? 123 TYR B CZ     1 
ATOM   5892  O  OH     . TYR B 1 132 ? -4.00600  -16.35900 -6.56100  1.000 148.77000 ? 123 TYR B OH     1 
ATOM   5893  N  N      . GLN B 1 133 ? -0.16800  -20.97300 -10.64600 1.000 134.44000 ? 124 GLN B N      1 
ATOM   5894  C  CA     . GLN B 1 133 ? -1.05000  -22.12100 -10.82200 1.000 128.11000 ? 124 GLN B CA     1 
ATOM   5895  C  C      . GLN B 1 133 ? -0.58300  -23.30200 -9.98500  1.000 137.34000 ? 124 GLN B C      1 
ATOM   5896  O  O      . GLN B 1 133 ? -1.39900  -24.13100 -9.56400  1.000 138.10000 ? 124 GLN B O      1 
ATOM   5897  C  CB     . GLN B 1 133 ? -1.12300  -22.51400 -12.30000 1.000 107.51000 ? 124 GLN B CB     1 
ATOM   5898  N  N      . GLY B 1 134 ? 0.71900   -23.39400 -9.73400  1.000 133.48000 ? 125 GLY B N      1 
ATOM   5899  C  CA     . GLY B 1 134 ? 1.23500   -24.39600 -8.82400  1.000 129.86000 ? 125 GLY B CA     1 
ATOM   5900  C  C      . GLY B 1 134 ? 0.82300   -24.13500 -7.38900  1.000 125.08000 ? 125 GLY B C      1 
ATOM   5901  O  O      . GLY B 1 134 ? 0.18900   -24.98100 -6.74900  1.000 123.77000 ? 125 GLY B O      1 
ATOM   5902  N  N      . GLY B 1 135 ? 1.18100   -22.95600 -6.87400  1.000 122.26000 ? 126 GLY B N      1 
ATOM   5903  C  CA     . GLY B 1 135 ? 0.82800   -22.61600 -5.50100  1.000 119.58000 ? 126 GLY B CA     1 
ATOM   5904  C  C      . GLY B 1 135 ? -0.66200  -22.70100 -5.22100  1.000 117.51000 ? 126 GLY B C      1 
ATOM   5905  O  O      . GLY B 1 135 ? -1.07700  -23.02700 -4.09700  1.000 117.44000 ? 126 GLY B O      1 
ATOM   5906  N  N      . SER B 1 136 ? -1.48700  -22.41000 -6.23000  1.000 116.09000 ? 127 SER B N      1 
ATOM   5907  C  CA     . SER B 1 136 ? -2.92800  -22.47900 -6.04200  1.000 113.62000 ? 127 SER B CA     1 
ATOM   5908  C  C      . SER B 1 136 ? -3.33700  -23.90800 -5.73000  1.000 107.24000 ? 127 SER B C      1 
ATOM   5909  O  O      . SER B 1 136 ? -4.32700  -24.12900 -5.02900  1.000 117.35000 ? 127 SER B O      1 
ATOM   5910  C  CB     . SER B 1 136 ? -3.64800  -21.96800 -7.29100  1.000 107.44000 ? 127 SER B CB     1 
ATOM   5911  O  OG     . SER B 1 136 ? -3.30400  -22.74000 -8.42900  1.000 111.33000 ? 127 SER B OG     1 
ATOM   5912  N  N      . VAL B 1 137 ? -2.57500  -24.88800 -6.22100  1.000 96.39000  ? 128 VAL B N      1 
ATOM   5913  C  CA     . VAL B 1 137 ? -2.87800  -26.28100 -5.90900  1.000 101.68000 ? 128 VAL B CA     1 
ATOM   5914  C  C      . VAL B 1 137 ? -2.87400  -26.48700 -4.40000  1.000 99.74000  ? 128 VAL B C      1 
ATOM   5915  O  O      . VAL B 1 137 ? -3.86000  -26.95100 -3.81900  1.000 99.15000  ? 128 VAL B O      1 
ATOM   5916  C  CB     . VAL B 1 137 ? -1.89500  -27.22500 -6.62400  1.000 108.09000 ? 128 VAL B CB     1 
ATOM   5917  C  CG1    . VAL B 1 137 ? -2.14700  -28.66200 -6.19800  1.000 100.70000 ? 128 VAL B CG1    1 
ATOM   5918  C  CG2    . VAL B 1 137 ? -2.03100  -27.08700 -8.13000  1.000 120.19000 ? 128 VAL B CG2    1 
ATOM   5919  N  N      . MET B 1 138 ? -1.77500  -26.11300 -3.74100  1.000 109.25000 ? 129 MET B N      1 
ATOM   5920  C  CA     . MET B 1 138 ? -1.69400  -26.28100 -2.29300  1.000 108.84000 ? 129 MET B CA     1 
ATOM   5921  C  C      . MET B 1 138 ? -2.70700  -25.42800 -1.54000  1.000 98.80000  ? 129 MET B C      1 
ATOM   5922  O  O      . MET B 1 138 ? -3.32200  -25.89300 -0.57100  1.000 99.38000  ? 129 MET B O      1 
ATOM   5923  C  CB     . MET B 1 138 ? -0.27500  -25.95100 -1.83400  1.000 102.48000 ? 129 MET B CB     1 
ATOM   5924  C  CG     . MET B 1 138 ? -0.06800  -26.13800 -0.34100  1.000 94.24000  ? 129 MET B CG     1 
ATOM   5925  S  SD     . MET B 1 138 ? -0.67300  -27.73400 0.24600   1.000 91.87000  ? 129 MET B SD     1 
ATOM   5926  C  CE     . MET B 1 138 ? -0.29200  -27.61600 1.99200   1.000 109.53000 ? 129 MET B CE     1 
ATOM   5927  N  N      . GLY B 1 139 ? -2.88500  -24.17100 -1.95700  1.000 106.62000 ? 130 GLY B N      1 
ATOM   5928  C  CA     . GLY B 1 139 ? -3.84100  -23.31700 -1.26100  1.000 106.02000 ? 130 GLY B CA     1 
ATOM   5929  C  C      . GLY B 1 139 ? -5.25000  -23.88200 -1.28500  1.000 93.75000  ? 130 GLY B C      1 
ATOM   5930  O  O      . GLY B 1 139 ? -5.90100  -24.03600 -0.24000  1.000 82.30000  ? 130 GLY B O      1 
ATOM   5931  N  N      . LEU B 1 140 ? -5.74600  -24.19000 -2.48500  1.000 92.52000  ? 131 LEU B N      1 
ATOM   5932  C  CA     . LEU B 1 140 ? -7.07900  -24.75300 -2.62200  1.000 80.37000  ? 131 LEU B CA     1 
ATOM   5933  C  C      . LEU B 1 140 ? -7.17800  -26.11700 -1.95900  1.000 95.39000  ? 131 LEU B C      1 
ATOM   5934  O  O      . LEU B 1 140 ? -8.24000  -26.46900 -1.44600  1.000 110.64000 ? 131 LEU B O      1 
ATOM   5935  C  CB     . LEU B 1 140 ? -7.45400  -24.84700 -4.10000  1.000 81.16000  ? 131 LEU B CB     1 
ATOM   5936  C  CG     . LEU B 1 140 ? -7.59400  -23.51000 -4.82900  1.000 79.60000  ? 131 LEU B CG     1 
ATOM   5937  C  CD1    . LEU B 1 140 ? -7.36900  -23.69400 -6.31900  1.000 112.37000 ? 131 LEU B CD1    1 
ATOM   5938  C  CD2    . LEU B 1 140 ? -8.96000  -22.89900 -4.56600  1.000 87.32000  ? 131 LEU B CD2    1 
ATOM   5939  N  N      . SER B 1 141 ? -6.09200  -26.89200 -1.94100  1.000 86.63000  ? 132 SER B N      1 
ATOM   5940  C  CA     . SER B 1 141 ? -6.12600  -28.18100 -1.26000  1.000 83.49000  ? 132 SER B CA     1 
ATOM   5941  C  C      . SER B 1 141 ? -6.35700  -27.99400 0.23200   1.000 95.15000  ? 132 SER B C      1 
ATOM   5942  O  O      . SER B 1 141 ? -7.25400  -28.61100 0.81700   1.000 94.78000  ? 132 SER B O      1 
ATOM   5943  C  CB     . SER B 1 141 ? -4.82500  -28.94100 -1.51800  1.000 79.30000  ? 132 SER B CB     1 
ATOM   5944  O  OG     . SER B 1 141 ? -4.89600  -30.26600 -1.02400  1.000 75.21000  ? 132 SER B OG     1 
ATOM   5945  N  N      . VAL B 1 142 ? -5.55500  -27.13500 0.86400   1.000 94.42000  ? 133 VAL B N      1 
ATOM   5946  C  CA     . VAL B 1 142 ? -5.77400  -26.80200 2.27200   1.000 83.79000  ? 133 VAL B CA     1 
ATOM   5947  C  C      . VAL B 1 142 ? -7.22800  -26.40600 2.49800   1.000 81.82000  ? 133 VAL B C      1 
ATOM   5948  O  O      . VAL B 1 142 ? -7.94600  -27.01200 3.30700   1.000 89.35000  ? 133 VAL B O      1 
ATOM   5949  C  CB     . VAL B 1 142 ? -4.81700  -25.68400 2.72000   1.000 83.33000  ? 133 VAL B CB     1 
ATOM   5950  C  CG1    . VAL B 1 142 ? -5.33900  -25.01800 3.98300   1.000 77.81000  ? 133 VAL B CG1    1 
ATOM   5951  C  CG2    . VAL B 1 142 ? -3.42000  -26.23900 2.94400   1.000 100.93000 ? 133 VAL B CG2    1 
ATOM   5952  N  N      . GLY B 1 143 ? -7.67700  -25.37000 1.78400   1.000 75.93000  ? 134 GLY B N      1 
ATOM   5953  C  CA     . GLY B 1 143 ? -9.01600  -24.85200 2.02700   1.000 73.54000  ? 134 GLY B CA     1 
ATOM   5954  C  C      . GLY B 1 143 ? -10.09300 -25.90500 1.84000   1.000 78.81000  ? 134 GLY B C      1 
ATOM   5955  O  O      . GLY B 1 143 ? -10.94400 -26.11200 2.71400   1.000 105.84000 ? 134 GLY B O      1 
ATOM   5956  N  N      . GLY B 1 144 ? -10.06700 -26.58700 0.69400   1.000 73.27000  ? 135 GLY B N      1 
ATOM   5957  C  CA     . GLY B 1 144 ? -11.10100 -27.55100 0.38400   1.000 75.72000  ? 135 GLY B CA     1 
ATOM   5958  C  C      . GLY B 1 144 ? -11.10900 -28.73200 1.33000   1.000 77.12000  ? 135 GLY B C      1 
ATOM   5959  O  O      . GLY B 1 144 ? -12.16900 -29.16900 1.76800   1.000 90.67000  ? 135 GLY B O      1 
ATOM   5960  N  N      . PHE B 1 145 ? -9.93100  -29.27400 1.65500   1.000 76.42000  ? 136 PHE B N      1 
ATOM   5961  C  CA     . PHE B 1 145 ? -9.88500  -30.40300 2.57700   1.000 88.12000  ? 136 PHE B CA     1 
ATOM   5962  C  C      . PHE B 1 145 ? -10.40300 -30.01500 3.95600   1.000 84.23000  ? 136 PHE B C      1 
ATOM   5963  O  O      . PHE B 1 145 ? -11.17900 -30.76200 4.56900   1.000 85.46000  ? 136 PHE B O      1 
ATOM   5964  C  CB     . PHE B 1 145 ? -8.46100  -30.95100 2.67200   1.000 91.10000  ? 136 PHE B CB     1 
ATOM   5965  C  CG     . PHE B 1 145 ? -8.09200  -31.86500 1.54200   1.000 87.62000  ? 136 PHE B CG     1 
ATOM   5966  C  CD1    . PHE B 1 145 ? -8.71700  -33.09100 1.40100   1.000 90.16000  ? 136 PHE B CD1    1 
ATOM   5967  C  CD2    . PHE B 1 145 ? -7.11500  -31.50700 0.63000   1.000 76.73000  ? 136 PHE B CD2    1 
ATOM   5968  C  CE1    . PHE B 1 145 ? -8.38400  -33.93800 0.36500   1.000 106.13000 ? 136 PHE B CE1    1 
ATOM   5969  C  CE2    . PHE B 1 145 ? -6.77600  -32.35300 -0.40700  1.000 86.72000  ? 136 PHE B CE2    1 
ATOM   5970  C  CZ     . PHE B 1 145 ? -7.41000  -33.57000 -0.54000  1.000 105.14000 ? 136 PHE B CZ     1 
ATOM   5971  N  N      . ALA B 1 146 ? -9.99500  -28.84700 4.46200   1.000 76.30000  ? 137 ALA B N      1 
ATOM   5972  C  CA     . ALA B 1 146 ? -10.46900 -28.42300 5.77500   1.000 66.64000  ? 137 ALA B CA     1 
ATOM   5973  C  C      . ALA B 1 146 ? -11.98500 -28.27300 5.78400   1.000 75.54000  ? 137 ALA B C      1 
ATOM   5974  O  O      . ALA B 1 146 ? -12.67800 -28.85200 6.63500   1.000 74.11000  ? 137 ALA B O      1 
ATOM   5975  C  CB     . ALA B 1 146 ? -9.79200  -27.11300 6.17800   1.000 73.68000  ? 137 ALA B CB     1 
ATOM   5976  N  N      . LEU B 1 147 ? -12.52200 -27.50000 4.83400   1.000 88.81000  ? 138 LEU B N      1 
ATOM   5977  C  CA     . LEU B 1 147 ? -13.96300 -27.27700 4.81100   1.000 76.12000  ? 138 LEU B CA     1 
ATOM   5978  C  C      . LEU B 1 147 ? -14.73100 -28.56000 4.51500   1.000 71.75000  ? 138 LEU B C      1 
ATOM   5979  O  O      . LEU B 1 147 ? -15.85300 -28.73100 5.00000   1.000 61.82000  ? 138 LEU B O      1 
ATOM   5980  C  CB     . LEU B 1 147 ? -14.31300 -26.19000 3.79600   1.000 64.65000  ? 138 LEU B CB     1 
ATOM   5981  C  CG     . LEU B 1 147 ? -14.26800 -24.77500 4.37800   1.000 85.30000  ? 138 LEU B CG     1 
ATOM   5982  C  CD1    . LEU B 1 147 ? -14.60100 -23.72300 3.32400   1.000 101.99000 ? 138 LEU B CD1    1 
ATOM   5983  C  CD2    . LEU B 1 147 ? -15.20300 -24.66600 5.57500   1.000 90.19000  ? 138 LEU B CD2    1 
ATOM   5984  N  N      . LEU B 1 148 ? -14.14500 -29.47700 3.74500   1.000 82.72000  ? 139 LEU B N      1 
ATOM   5985  C  CA     . LEU B 1 148 ? -14.79300 -30.75300 3.48000   1.000 89.39000  ? 139 LEU B CA     1 
ATOM   5986  C  C      . LEU B 1 148 ? -14.91100 -31.56900 4.75600   1.000 88.76000  ? 139 LEU B C      1 
ATOM   5987  O  O      . LEU B 1 148 ? -15.98200 -32.10200 5.06600   1.000 95.24000  ? 139 LEU B O      1 
ATOM   5988  C  CB     . LEU B 1 148 ? -14.01000 -31.52200 2.41500   1.000 93.53000  ? 139 LEU B CB     1 
ATOM   5989  C  CG     . LEU B 1 148 ? -14.60600 -32.84000 1.92300   1.000 80.28000  ? 139 LEU B CG     1 
ATOM   5990  C  CD1    . LEU B 1 148 ? -15.68700 -32.57900 0.88700   1.000 86.02000  ? 139 LEU B CD1    1 
ATOM   5991  C  CD2    . LEU B 1 148 ? -13.51500 -33.73300 1.35600   1.000 100.06000 ? 139 LEU B CD2    1 
ATOM   5992  N  N      . GLY B 1 149 ? -13.81300 -31.69400 5.50200   1.000 79.75000  ? 140 GLY B N      1 
ATOM   5993  C  CA     . GLY B 1 149 ? -13.89100 -32.37200 6.78300   1.000 76.28000  ? 140 GLY B CA     1 
ATOM   5994  C  C      . GLY B 1 149 ? -14.93500 -31.75300 7.69300   1.000 72.82000  ? 140 GLY B C      1 
ATOM   5995  O  O      . GLY B 1 149 ? -15.73500 -32.46300 8.31200   1.000 64.69000  ? 140 GLY B O      1 
ATOM   5996  N  N      . LEU B 1 150 ? -14.96300 -30.41900 7.76200   1.000 77.35000  ? 141 LEU B N      1 
ATOM   5997  C  CA     . LEU B 1 150 ? -15.91500 -29.76200 8.65500   1.000 80.45000  ? 141 LEU B CA     1 
ATOM   5998  C  C      . LEU B 1 150 ? -17.35800 -29.99700 8.21500   1.000 74.95000  ? 141 LEU B C      1 
ATOM   5999  O  O      . LEU B 1 150 ? -18.23400 -30.25100 9.05000   1.000 80.14000  ? 141 LEU B O      1 
ATOM   6000  C  CB     . LEU B 1 150 ? -15.61400 -28.26500 8.73700   1.000 80.68000  ? 141 LEU B CB     1 
ATOM   6001  C  CG     . LEU B 1 150 ? -14.39500 -27.87600 9.57700   1.000 91.38000  ? 141 LEU B CG     1 
ATOM   6002  C  CD1    . LEU B 1 150 ? -14.14400 -26.37500 9.51800   1.000 84.01000  ? 141 LEU B CD1    1 
ATOM   6003  C  CD2    . LEU B 1 150 ? -14.56700 -28.33700 11.01500  1.000 106.52000 ? 141 LEU B CD2    1 
ATOM   6004  N  N      . VAL B 1 151 ? -17.62500 -29.92500 6.91000   1.000 71.06000  ? 142 VAL B N      1 
ATOM   6005  C  CA     . VAL B 1 151 ? -18.98300 -30.12900 6.42000   1.000 77.26000  ? 142 VAL B CA     1 
ATOM   6006  C  C      . VAL B 1 151 ? -19.41700 -31.57100 6.63800   1.000 78.18000  ? 142 VAL B C      1 
ATOM   6007  O  O      . VAL B 1 151 ? -20.56300 -31.83800 7.01900   1.000 81.29000  ? 142 VAL B O      1 
ATOM   6008  C  CB     . VAL B 1 151 ? -19.08100 -29.72800 4.93800   1.000 84.53000  ? 142 VAL B CB     1 
ATOM   6009  C  CG1    . VAL B 1 151 ? -20.38800 -30.22800 4.33700   1.000 92.92000  ? 142 VAL B CG1    1 
ATOM   6010  C  CG2    . VAL B 1 151 ? -18.95600 -28.22100 4.79000   1.000 86.49000  ? 142 VAL B CG2    1 
ATOM   6011  N  N      . LEU B 1 152 ? -18.51300 -32.52200 6.40300   1.000 78.97000  ? 143 LEU B N      1 
ATOM   6012  C  CA     . LEU B 1 152 ? -18.83400 -33.91900 6.66500   1.000 83.56000  ? 143 LEU B CA     1 
ATOM   6013  C  C      . LEU B 1 152 ? -19.15100 -34.13200 8.13800   1.000 86.91000  ? 143 LEU B C      1 
ATOM   6014  O  O      . LEU B 1 152 ? -20.08700 -34.86400 8.48100   1.000 91.82000  ? 143 LEU B O      1 
ATOM   6015  C  CB     . LEU B 1 152 ? -17.67400 -34.81200 6.22800   1.000 94.42000  ? 143 LEU B CB     1 
ATOM   6016  C  CG     . LEU B 1 152 ? -17.20100 -34.59700 4.78900   1.000 83.14000  ? 143 LEU B CG     1 
ATOM   6017  C  CD1    . LEU B 1 152 ? -15.88400 -35.31400 4.53000   1.000 86.75000  ? 143 LEU B CD1    1 
ATOM   6018  C  CD2    . LEU B 1 152 ? -18.26800 -35.04300 3.80100   1.000 99.50000  ? 143 LEU B CD2    1 
ATOM   6019  N  N      . VAL B 1 153 ? -18.39600 -33.48200 9.02500   1.000 83.96000  ? 144 VAL B N      1 
ATOM   6020  C  CA     . VAL B 1 153 ? -18.67500 -33.61200 10.45000  1.000 71.64000  ? 144 VAL B CA     1 
ATOM   6021  C  C      . VAL B 1 153 ? -20.03600 -33.01500 10.78200  1.000 74.95000  ? 144 VAL B C      1 
ATOM   6022  O  O      . VAL B 1 153 ? -20.80700 -33.58800 11.56100  1.000 83.74000  ? 144 VAL B O      1 
ATOM   6023  C  CB     . VAL B 1 153 ? -17.55100 -32.95800 11.27400  1.000 65.82000  ? 144 VAL B CB     1 
ATOM   6024  C  CG1    . VAL B 1 153 ? -18.01000 -32.72500 12.70500  1.000 64.51000  ? 144 VAL B CG1    1 
ATOM   6025  C  CG2    . VAL B 1 153 ? -16.30300 -33.82300 11.23900  1.000 74.75000  ? 144 VAL B CG2    1 
ATOM   6026  N  N      . TYR B 1 154 ? -20.36300 -31.86600 10.18700  1.000 77.24000  ? 145 TYR B N      1 
ATOM   6027  C  CA     . TYR B 1 154 ? -21.64300 -31.23500 10.48900  1.000 77.94000  ? 145 TYR B CA     1 
ATOM   6028  C  C      . TYR B 1 154 ? -22.81700 -32.02300 9.92100   1.000 79.54000  ? 145 TYR B C      1 
ATOM   6029  O  O      . TYR B 1 154 ? -23.92500 -31.95300 10.46200  1.000 80.76000  ? 145 TYR B O      1 
ATOM   6030  C  CB     . TYR B 1 154 ? -21.67800 -29.80100 9.96400   1.000 72.29000  ? 145 TYR B CB     1 
ATOM   6031  C  CG     . TYR B 1 154 ? -22.95700 -29.08400 10.33200  1.000 94.93000  ? 145 TYR B CG     1 
ATOM   6032  C  CD1    . TYR B 1 154 ? -23.34300 -28.96500 11.66000  1.000 115.02000 ? 145 TYR B CD1    1 
ATOM   6033  C  CD2    . TYR B 1 154 ? -23.78300 -28.53700 9.36000   1.000 104.70000 ? 145 TYR B CD2    1 
ATOM   6034  C  CE1    . TYR B 1 154 ? -24.50900 -28.32000 12.01400  1.000 110.33000 ? 145 TYR B CE1    1 
ATOM   6035  C  CE2    . TYR B 1 154 ? -24.95700 -27.88500 9.70600   1.000 134.75000 ? 145 TYR B CE2    1 
ATOM   6036  C  CZ     . TYR B 1 154 ? -25.31200 -27.78100 11.03700  1.000 106.51000 ? 145 TYR B CZ     1 
ATOM   6037  O  OH     . TYR B 1 154 ? -26.47400 -27.13700 11.39700  1.000 88.34000  ? 145 TYR B OH     1 
ATOM   6038  N  N      . LEU B 1 155 ? -22.60300 -32.77300 8.84400   1.000 81.65000  ? 146 LEU B N      1 
ATOM   6039  C  CA     . LEU B 1 155 ? -23.69500 -33.52300 8.21100   1.000 88.26000  ? 146 LEU B CA     1 
ATOM   6040  C  C      . LEU B 1 155 ? -23.79300 -34.92000 8.81600   1.000 92.39000  ? 146 LEU B C      1 
ATOM   6041  O  O      . LEU B 1 155 ? -24.78300 -35.25200 9.47300   1.000 102.00000 ? 146 LEU B O      1 
ATOM   6042  C  CB     . LEU B 1 155 ? -23.49800 -33.58200 6.69500   1.000 83.54000  ? 146 LEU B CB     1 
ATOM   6043  C  CG     . LEU B 1 155 ? -23.46300 -32.23500 5.97500   1.000 68.94000  ? 146 LEU B CG     1 
ATOM   6044  C  CD1    . LEU B 1 155 ? -23.49500 -32.43400 4.46800   1.000 63.73000  ? 146 LEU B CD1    1 
ATOM   6045  C  CD2    . LEU B 1 155 ? -24.62800 -31.37300 6.42800   1.000 59.14000  ? 146 LEU B CD2    1 
ATOM   6046  N  N      . ILE B 1 156 ? -22.76600 -35.74400 8.60200   1.000 85.88000  ? 147 ILE B N      1 
ATOM   6047  C  CA     . ILE B 1 156 ? -22.81800 -37.12800 9.06700   1.000 88.01000  ? 147 ILE B CA     1 
ATOM   6048  C  C      . ILE B 1 156 ? -23.06300 -37.17000 10.56900  1.000 88.82000  ? 147 ILE B C      1 
ATOM   6049  O  O      . ILE B 1 156 ? -23.87500 -37.96000 11.06400  1.000 93.03000  ? 147 ILE B O      1 
ATOM   6050  C  CB     . ILE B 1 156 ? -21.52800 -37.87500 8.68400   1.000 106.13000 ? 147 ILE B CB     1 
ATOM   6051  C  CG1    . ILE B 1 156 ? -21.38000 -37.93800 7.16200   1.000 106.52000 ? 147 ILE B CG1    1 
ATOM   6052  C  CG2    . ILE B 1 156 ? -21.52000 -39.26900 9.29700   1.000 108.54000 ? 147 ILE B CG2    1 
ATOM   6053  C  CD1    . ILE B 1 156 ? -22.62400 -38.40900 6.44200   1.000 106.21000 ? 147 ILE B CD1    1 
ATOM   6054  N  N      . PHE B 1 157 ? -22.35100 -36.33300 11.32100  1.000 84.41000  ? 148 PHE B N      1 
ATOM   6055  C  CA     . PHE B 1 157 ? -22.54000 -36.30000 12.76400  1.000 80.29000  ? 148 PHE B CA     1 
ATOM   6056  C  C      . PHE B 1 157 ? -23.55400 -35.23900 13.18000  1.000 82.92000  ? 148 PHE B C      1 
ATOM   6057  O  O      . PHE B 1 157 ? -24.45300 -35.51700 13.97800  1.000 92.99000  ? 148 PHE B O      1 
ATOM   6058  C  CB     . PHE B 1 157 ? -21.20000 -36.05200 13.46200  1.000 85.38000  ? 148 PHE B CB     1 
ATOM   6059  C  CG     . PHE B 1 157 ? -20.21300 -37.17000 13.29200  1.000 94.77000  ? 148 PHE B CG     1 
ATOM   6060  C  CD1    . PHE B 1 157 ? -20.45300 -38.41500 13.84700  1.000 99.08000  ? 148 PHE B CD1    1 
ATOM   6061  C  CD2    . PHE B 1 157 ? -19.04000 -36.97300 12.58300  1.000 97.11000  ? 148 PHE B CD2    1 
ATOM   6062  C  CE1    . PHE B 1 157 ? -19.54400 -39.44500 13.69300  1.000 95.71000  ? 148 PHE B CE1    1 
ATOM   6063  C  CE2    . PHE B 1 157 ? -18.12700 -37.99700 12.42700  1.000 94.17000  ? 148 PHE B CE2    1 
ATOM   6064  C  CZ     . PHE B 1 157 ? -18.37900 -39.23500 12.98300  1.000 91.18000  ? 148 PHE B CZ     1 
ATOM   6065  N  N      . GLY B 1 158 ? -23.44600 -34.03400 12.62400  1.000 74.26000  ? 149 GLY B N      1 
ATOM   6066  C  CA     . GLY B 1 158 ? -24.30600 -32.93900 13.03000  1.000 77.43000  ? 149 GLY B CA     1 
ATOM   6067  C  C      . GLY B 1 158 ? -25.77600 -33.15800 12.74200  1.000 84.73000  ? 149 GLY B C      1 
ATOM   6068  O  O      . GLY B 1 158 ? -26.60300 -33.15200 13.65900  1.000 81.82000  ? 149 GLY B O      1 
ATOM   6069  N  N      . LYS B 1 159 ? -26.11500 -33.35000 11.46800  1.000 93.56000  ? 150 LYS B N      1 
ATOM   6070  C  CA     . LYS B 1 159 ? -27.50200 -33.48500 11.04000  1.000 89.25000  ? 150 LYS B CA     1 
ATOM   6071  C  C      . LYS B 1 159 ? -27.93200 -34.94300 10.93800  1.000 102.83000 ? 150 LYS B C      1 
ATOM   6072  O  O      . LYS B 1 159 ? -29.00900 -35.30700 11.41900  1.000 108.15000 ? 150 LYS B O      1 
ATOM   6073  C  CB     . LYS B 1 159 ? -27.71000 -32.78800 9.69500   1.000 30.00000  ? 150 LYS B CB     1 
ATOM   6074  C  CG     . LYS B 1 159 ? -27.37900 -31.30300 9.70600   1.000 30.00000  ? 150 LYS B CG     1 
ATOM   6075  C  CD     . LYS B 1 159 ? -28.22400 -30.55600 10.72400  1.000 30.00000  ? 150 LYS B CD     1 
ATOM   6076  C  CE     . LYS B 1 159 ? -29.67800 -30.48300 10.28900  1.000 30.00000  ? 150 LYS B CE     1 
ATOM   6077  N  NZ     . LYS B 1 159 ? -30.48400 -29.61400 11.18900  1.000 30.00000  ? 150 LYS B NZ     1 
ATOM   6078  N  N      . TRP B 1 160 ? -27.10400 -35.78700 10.31800  1.000 105.14000 ? 151 TRP B N      1 
ATOM   6079  C  CA     . TRP B 1 160 ? -27.44500 -37.19700 10.15700  1.000 107.46000 ? 151 TRP B CA     1 
ATOM   6080  C  C      . TRP B 1 160 ? -27.74900 -37.83400 11.50800  1.000 97.28000  ? 151 TRP B C      1 
ATOM   6081  O  O      . TRP B 1 160 ? -28.83100 -38.39200 11.72300  1.000 98.88000  ? 151 TRP B O      1 
ATOM   6082  C  CB     . TRP B 1 160 ? -26.29500 -37.93200 9.45800   1.000 132.80000 ? 151 TRP B CB     1 
ATOM   6083  C  CG     . TRP B 1 160 ? -26.57000 -39.37900 9.10000   1.000 139.54000 ? 151 TRP B CG     1 
ATOM   6084  C  CD1    . TRP B 1 160 ? -26.71600 -40.42600 9.96500   1.000 126.90000 ? 151 TRP B CD1    1 
ATOM   6085  C  CD2    . TRP B 1 160 ? -26.67200 -39.93600 7.78000   1.000 139.26000 ? 151 TRP B CD2    1 
ATOM   6086  N  NE1    . TRP B 1 160 ? -26.93200 -41.59100 9.26900   1.000 122.69000 ? 151 TRP B NE1    1 
ATOM   6087  C  CE2    . TRP B 1 160 ? -26.90600 -41.31900 7.92700   1.000 136.96000 ? 151 TRP B CE2    1 
ATOM   6088  C  CE3    . TRP B 1 160 ? -26.60000 -39.39800 6.49000   1.000 128.07000 ? 151 TRP B CE3    1 
ATOM   6089  C  CZ2    . TRP B 1 160 ? -27.07000 -42.16900 6.83400   1.000 150.21000 ? 151 TRP B CZ2    1 
ATOM   6090  C  CZ3    . TRP B 1 160 ? -26.76200 -40.24500 5.40700   1.000 122.73000 ? 151 TRP B CZ3    1 
ATOM   6091  C  CH2    . TRP B 1 160 ? -26.99400 -41.61400 5.58600   1.000 147.68000 ? 151 TRP B CH2    1 
ATOM   6092  N  N      . MET B 1 161 ? -26.79200 -37.75600 12.43400  1.000 95.93000  ? 152 MET B N      1 
ATOM   6093  C  CA     . MET B 1 161 ? -26.91900 -38.36100 13.75400  1.000 100.67000 ? 152 MET B CA     1 
ATOM   6094  C  C      . MET B 1 161 ? -27.70800 -37.50900 14.74000  1.000 95.15000  ? 152 MET B C      1 
ATOM   6095  O  O      . MET B 1 161 ? -28.00400 -37.98500 15.84200  1.000 79.89000  ? 152 MET B O      1 
ATOM   6096  C  CB     . MET B 1 161 ? -25.52700 -38.64100 14.32500  1.000 97.17000  ? 152 MET B CB     1 
ATOM   6097  C  CG     . MET B 1 161 ? -25.51800 -39.47200 15.59400  1.000 95.22000  ? 152 MET B CG     1 
ATOM   6098  S  SD     . MET B 1 161 ? -23.85400 -40.01800 16.02500  1.000 101.96000 ? 152 MET B SD     1 
ATOM   6099  C  CE     . MET B 1 161 ? -23.36500 -40.83900 14.51000  1.000 93.20000  ? 152 MET B CE     1 
ATOM   6100  N  N      . GLY B 1 162 ? -28.05700 -36.27700 14.38600  1.000 93.82000  ? 153 GLY B N      1 
ATOM   6101  C  CA     . GLY B 1 162 ? -28.80400 -35.44000 15.30500  1.000 100.63000 ? 153 GLY B CA     1 
ATOM   6102  C  C      . GLY B 1 162 ? -27.96900 -34.84900 16.41900  1.000 116.66000 ? 153 GLY B C      1 
ATOM   6103  O  O      . GLY B 1 162 ? -28.46300 -34.69500 17.54400  1.000 117.12000 ? 153 GLY B O      1 
ATOM   6104  N  N      . GLN B 1 163 ? -26.70600 -34.51500 16.13900  1.000 118.68000 ? 154 GLN B N      1 
ATOM   6105  C  CA     . GLN B 1 163 ? -25.86000 -33.89300 17.15200  1.000 111.36000 ? 154 GLN B CA     1 
ATOM   6106  C  C      . GLN B 1 163 ? -26.29200 -32.46200 17.43900  1.000 104.17000 ? 154 GLN B C      1 
ATOM   6107  O  O      . GLN B 1 163 ? -26.07100 -31.95900 18.54600  1.000 112.01000 ? 154 GLN B O      1 
ATOM   6108  C  CB     . GLN B 1 163 ? -24.39900 -33.92000 16.70000  1.000 103.64000 ? 154 GLN B CB     1 
ATOM   6109  C  CG     . GLN B 1 163 ? -23.78700 -35.31000 16.64500  1.000 102.56000 ? 154 GLN B CG     1 
ATOM   6110  C  CD     . GLN B 1 163 ? -23.67500 -35.95600 18.00800  1.000 121.78000 ? 154 GLN B CD     1 
ATOM   6111  O  OE1    . GLN B 1 163 ? -22.84800 -35.56300 18.83200  1.000 132.48000 ? 154 GLN B OE1    1 
ATOM   6112  N  NE2    . GLN B 1 163 ? -24.52800 -36.93800 18.26400  1.000 128.41000 ? 154 GLN B NE2    1 
ATOM   6113  N  N      . VAL B 1 164 ? -26.89800 -31.79200 16.45500  1.000 81.57000  ? 155 VAL B N      1 
ATOM   6114  C  CA     . VAL B 1 164 ? -27.51900 -30.48900 16.67800  1.000 87.27000  ? 155 VAL B CA     1 
ATOM   6115  C  C      . VAL B 1 164 ? -28.96400 -30.59500 17.14700  1.000 110.84000 ? 155 VAL B C      1 
ATOM   6116  O  O      . VAL B 1 164 ? -29.54500 -29.58100 17.56300  1.000 127.13000 ? 155 VAL B O      1 
ATOM   6117  C  CB     . VAL B 1 164 ? -27.45600 -29.62600 15.40300  1.000 71.25000  ? 155 VAL B CB     1 
ATOM   6118  C  CG1    . VAL B 1 164 ? -26.01000 -29.37400 15.01100  1.000 78.57000  ? 155 VAL B CG1    1 
ATOM   6119  C  CG2    . VAL B 1 164 ? -28.21300 -30.29800 14.27000  1.000 104.19000 ? 155 VAL B CG2    1 
ATOM   6120  N  N      . ASP B 1 165 ? -29.56700 -31.78600 17.09100  1.000 108.52000 ? 156 ASP B N      1 
ATOM   6121  C  CA     . ASP B 1 165 ? -30.94400 -31.94000 17.55100  1.000 101.28000 ? 156 ASP B CA     1 
ATOM   6122  C  C      . ASP B 1 165 ? -30.97000 -31.93400 19.07600  1.000 129.65000 ? 156 ASP B C      1 
ATOM   6123  O  O      . ASP B 1 165 ? -31.86600 -31.33500 19.68100  1.000 136.82000 ? 156 ASP B O      1 
ATOM   6124  C  CB     . ASP B 1 165 ? -31.52900 -33.25000 17.02400  1.000 95.04000  ? 156 ASP B CB     1 
ATOM   6125  N  N      . ASN B 1 166 ? -30.00500 -32.59800 19.71500  1.000 125.77000 ? 157 ASN B N      1 
ATOM   6126  C  CA     . ASN B 1 166 ? -29.98500 -32.65200 21.17400  1.000 126.23000 ? 157 ASN B CA     1 
ATOM   6127  C  C      . ASN B 1 166 ? -29.52900 -31.32300 21.77700  1.000 126.61000 ? 157 ASN B C      1 
ATOM   6128  O  O      . ASN B 1 166 ? -30.29800 -30.63800 22.46100  1.000 142.14000 ? 157 ASN B O      1 
ATOM   6129  C  CB     . ASN B 1 166 ? -29.11500 -33.83000 21.63500  1.000 128.54000 ? 157 ASN B CB     1 
ATOM   6130  C  CG     . ASN B 1 166 ? -27.64700 -33.66100 21.27400  1.000 137.67000 ? 157 ASN B CG     1 
ATOM   6131  O  OD1    . ASN B 1 166 ? -27.12000 -32.54800 21.26500  1.000 124.77000 ? 157 ASN B OD1    1 
ATOM   6132  N  ND2    . ASN B 1 166 ? -26.98000 -34.77100 20.97400  1.000 143.95000 ? 157 ASN B ND2    1 
ATOM   6133  N  N      . LEU B 1 167 ? -28.27800 -30.94300 21.52000  1.000 122.22000 ? 158 LEU B N      1 
ATOM   6134  C  CA     . LEU B 1 167 ? -27.69800 -29.69000 21.99900  1.000 110.58000 ? 158 LEU B CA     1 
ATOM   6135  C  C      . LEU B 1 167 ? -27.73800 -29.56500 23.51600  1.000 119.46000 ? 158 LEU B C      1 
ATOM   6136  O  O      . LEU B 1 167 ? -27.60900 -28.46200 24.05700  1.000 120.57000 ? 158 LEU B O      1 
ATOM   6137  C  CB     . LEU B 1 167 ? -28.30500 -28.44000 21.35400  1.000 98.11000  ? 158 LEU B CB     1 
ATOM   6138  C  CG     . LEU B 1 167 ? -27.78100 -28.10400 19.95800  1.000 90.47000  ? 158 LEU B CG     1 
ATOM   6139  C  CD1    . LEU B 1 167 ? -28.55100 -26.93900 19.35600  1.000 87.34000  ? 158 LEU B CD1    1 
ATOM   6140  C  CD2    . LEU B 1 167 ? -26.29000 -27.80300 20.00500  1.000 81.72000  ? 158 LEU B CD2    1 
ATOM   6141  N  N      . ASN B 1 168 ? -27.91500 -30.67800 24.21400  1.000 118.73000 ? 159 ASN B N      1 
ATOM   6142  C  CA     . ASN B 1 168 ? -27.90600 -30.70800 25.66500  1.000 110.70000 ? 159 ASN B CA     1 
ATOM   6143  C  C      . ASN B 1 168 ? -26.70100 -31.50600 26.14300  1.000 104.63000 ? 159 ASN B C      1 
ATOM   6144  O  O      . ASN B 1 168 ? -26.06900 -32.24100 25.38000  1.000 99.17000  ? 159 ASN B O      1 
ATOM   6145  C  CB     . ASN B 1 168 ? -29.21100 -31.30400 26.20500  1.000 125.45000 ? 159 ASN B CB     1 
ATOM   6146  C  CG     . ASN B 1 168 ? -29.65800 -30.65000 27.49600  1.000 122.13000 ? 159 ASN B CG     1 
ATOM   6147  O  OD1    . ASN B 1 168 ? -28.83600 -30.17600 28.28300  1.000 110.21000 ? 159 ASN B OD1    1 
ATOM   6148  N  ND2    . ASN B 1 168 ? -30.96700 -30.61000 27.71700  1.000 111.49000 ? 159 ASN B ND2    1 
ATOM   6149  N  N      . ILE B 1 169 ? -26.38600 -31.35900 27.42700  1.000 115.85000 ? 160 ILE B N      1 
ATOM   6150  C  CA     . ILE B 1 169 ? -25.18900 -31.99100 27.97300  1.000 112.42000 ? 160 ILE B CA     1 
ATOM   6151  C  C      . ILE B 1 169 ? -25.38200 -33.50200 27.91600  1.000 105.91000 ? 160 ILE B C      1 
ATOM   6152  O  O      . ILE B 1 169 ? -26.22800 -34.05800 28.62300  1.000 115.96000 ? 160 ILE B O      1 
ATOM   6153  C  CB     . ILE B 1 169 ? -24.90100 -31.52100 29.40300  1.000 112.68000 ? 160 ILE B CB     1 
ATOM   6154  C  CG1    . ILE B 1 169 ? -24.68200 -30.00700 29.43600  1.000 103.04000 ? 160 ILE B CG1    1 
ATOM   6155  C  CG2    . ILE B 1 169 ? -23.69400 -32.25300 29.97100  1.000 101.12000 ? 160 ILE B CG2    1 
ATOM   6156  C  CD1    . ILE B 1 169 ? -25.94000 -29.22000 29.72300  1.000 131.56000 ? 160 ILE B CD1    1 
ATOM   6157  N  N      . TYR B 1 170 ? -24.59600 -34.16900 27.07600  1.000 89.03000  ? 161 TYR B N      1 
ATOM   6158  C  CA     . TYR B 1 170 ? -24.54100 -35.61800 27.04200  1.000 87.11000  ? 161 TYR B CA     1 
ATOM   6159  C  C      . TYR B 1 170 ? -23.42000 -36.09200 27.95700  1.000 81.95000  ? 161 TYR B C      1 
ATOM   6160  O  O      . TYR B 1 170 ? -22.34700 -35.48000 28.01900  1.000 90.07000  ? 161 TYR B O      1 
ATOM   6161  C  CB     . TYR B 1 170 ? -24.31600 -36.10800 25.61000  1.000 73.41000  ? 161 TYR B CB     1 
ATOM   6162  C  CG     . TYR B 1 170 ? -23.85200 -37.54000 25.49800  1.000 72.88000  ? 161 TYR B CG     1 
ATOM   6163  C  CD1    . TYR B 1 170 ? -24.70800 -38.59400 25.78700  1.000 83.41000  ? 161 TYR B CD1    1 
ATOM   6164  C  CD2    . TYR B 1 170 ? -22.56000 -37.83800 25.09200  1.000 86.30000  ? 161 TYR B CD2    1 
ATOM   6165  C  CE1    . TYR B 1 170 ? -24.28500 -39.90600 25.68200  1.000 89.39000  ? 161 TYR B CE1    1 
ATOM   6166  C  CE2    . TYR B 1 170 ? -22.12800 -39.14400 24.98300  1.000 86.90000  ? 161 TYR B CE2    1 
ATOM   6167  C  CZ     . TYR B 1 170 ? -22.99300 -40.17400 25.27800  1.000 87.96000  ? 161 TYR B CZ     1 
ATOM   6168  O  OH     . TYR B 1 170 ? -22.56000 -41.47500 25.16800  1.000 89.90000  ? 161 TYR B OH     1 
ATOM   6169  N  N      . THR B 1 171 ? -23.68800 -37.17400 28.68200  1.000 79.06000  ? 162 THR B N      1 
ATOM   6170  C  CA     . THR B 1 171 ? -22.75500 -37.74100 29.64500  1.000 91.40000  ? 162 THR B CA     1 
ATOM   6171  C  C      . THR B 1 171 ? -22.16900 -39.03700 29.10400  1.000 96.08000  ? 162 THR B C      1 
ATOM   6172  O  O      . THR B 1 171 ? -22.91100 -39.95500 28.73500  1.000 101.29000 ? 162 THR B O      1 
ATOM   6173  C  CB     . THR B 1 171 ? -23.44000 -37.99400 30.98800  1.000 100.18000 ? 162 THR B CB     1 
ATOM   6174  O  OG1    . THR B 1 171 ? -24.00000 -36.77000 31.47800  1.000 78.05000  ? 162 THR B OG1    1 
ATOM   6175  C  CG2    . THR B 1 171 ? -22.44000 -38.53300 32.00100  1.000 91.53000  ? 162 THR B CG2    1 
ATOM   6176  N  N      . ASN B 1 172 ? -20.84200 -39.10700 29.05800  1.000 105.19000 ? 163 ASN B N      1 
ATOM   6177  C  CA     . ASN B 1 172 ? -20.16800 -40.29600 28.56500  1.000 105.66000 ? 163 ASN B CA     1 
ATOM   6178  C  C      . ASN B 1 172 ? -20.43800 -41.47400 29.50500  1.000 109.80000 ? 163 ASN B C      1 
ATOM   6179  O  O      . ASN B 1 172 ? -20.94100 -41.31200 30.62000  1.000 106.86000 ? 163 ASN B O      1 
ATOM   6180  C  CB     . ASN B 1 172 ? -18.66900 -40.02800 28.43400  1.000 89.80000  ? 163 ASN B CB     1 
ATOM   6181  C  CG     . ASN B 1 172 ? -17.94800 -41.10900 27.66200  1.000 98.31000  ? 163 ASN B CG     1 
ATOM   6182  O  OD1    . ASN B 1 172 ? -18.51600 -41.73400 26.76600  1.000 124.24000 ? 163 ASN B OD1    1 
ATOM   6183  N  ND2    . ASN B 1 172 ? -16.68500 -41.33300 28.00000  1.000 83.07000  ? 163 ASN B ND2    1 
ATOM   6184  N  N      . TRP B 1 173 ? -20.09400 -42.68000 29.04200  1.000 112.50000 ? 164 TRP B N      1 
ATOM   6185  C  CA     . TRP B 1 173 ? -20.34800 -43.86800 29.85500  1.000 116.28000 ? 164 TRP B CA     1 
ATOM   6186  C  C      . TRP B 1 173 ? -19.52000 -43.85000 31.13600  1.000 110.38000 ? 164 TRP B C      1 
ATOM   6187  O  O      . TRP B 1 173 ? -19.98500 -44.30500 32.18800  1.000 114.17000 ? 164 TRP B O      1 
ATOM   6188  C  CB     . TRP B 1 173 ? -20.09300 -45.14300 29.04300  1.000 133.15000 ? 164 TRP B CB     1 
ATOM   6189  C  CG     . TRP B 1 173 ? -18.65200 -45.43800 28.69100  1.000 125.45000 ? 164 TRP B CG     1 
ATOM   6190  C  CD1    . TRP B 1 173 ? -17.64400 -45.77900 29.55000  1.000 126.23000 ? 164 TRP B CD1    1 
ATOM   6191  C  CD2    . TRP B 1 173 ? -18.07900 -45.45500 27.37700  1.000 121.66000 ? 164 TRP B CD2    1 
ATOM   6192  N  NE1    . TRP B 1 173 ? -16.47700 -45.98500 28.85300  1.000 126.07000 ? 164 TRP B NE1    1 
ATOM   6193  C  CE2    . TRP B 1 173 ? -16.71800 -45.79400 27.51800  1.000 122.91000 ? 164 TRP B CE2    1 
ATOM   6194  C  CE3    . TRP B 1 173 ? -18.58200 -45.20800 26.09600  1.000 125.20000 ? 164 TRP B CE3    1 
ATOM   6195  C  CZ2    . TRP B 1 173 ? -15.85600 -45.89300 26.42700  1.000 123.15000 ? 164 TRP B CZ2    1 
ATOM   6196  C  CZ3    . TRP B 1 173 ? -17.72400 -45.30500 25.01400  1.000 132.68000 ? 164 TRP B CZ3    1 
ATOM   6197  C  CH2    . TRP B 1 173 ? -16.37700 -45.64500 25.18700  1.000 124.08000 ? 164 TRP B CH2    1 
ATOM   6198  N  N      . LEU B 1 174 ? -18.29300 -43.33200 31.06800  1.000 115.17000 ? 165 LEU B N      1 
ATOM   6199  C  CA     . LEU B 1 174 ? -17.47800 -43.19200 32.26700  1.000 106.95000 ? 165 LEU B CA     1 
ATOM   6200  C  C      . LEU B 1 174 ? -17.99000 -42.08500 33.17800  1.000 103.04000 ? 165 LEU B C      1 
ATOM   6201  O  O      . LEU B 1 174 ? -17.64500 -42.06600 34.36500  1.000 90.65000  ? 165 LEU B O      1 
ATOM   6202  C  CB     . LEU B 1 174 ? -16.02000 -42.92700 31.88600  1.000 82.82000  ? 165 LEU B CB     1 
ATOM   6203  N  N      . GLY B 1 175 ? -18.80000 -41.17400 32.65600  1.000 106.19000 ? 166 GLY B N      1 
ATOM   6204  C  CA     . GLY B 1 175 ? -19.33900 -40.07900 33.42500  1.000 102.83000 ? 166 GLY B CA     1 
ATOM   6205  C  C      . GLY B 1 175 ? -18.88100 -38.68800 33.01100  1.000 106.47000 ? 166 GLY B C      1 
ATOM   6206  O  O      . GLY B 1 175 ? -18.95700 -37.76700 33.83500  1.000 108.63000 ? 166 GLY B O      1 
ATOM   6207  N  N      . ILE B 1 176 ? -18.41300 -38.50900 31.77700  1.000 112.02000 ? 167 ILE B N      1 
ATOM   6208  C  CA     . ILE B 1 176 ? -17.92400 -37.21800 31.30400  1.000 101.15000 ? 167 ILE B CA     1 
ATOM   6209  C  C      . ILE B 1 176 ? -19.07700 -36.43800 30.69000  1.000 101.68000 ? 167 ILE B C      1 
ATOM   6210  O  O      . ILE B 1 176 ? -19.85500 -36.98100 29.89600  1.000 112.83000 ? 167 ILE B O      1 
ATOM   6211  C  CB     . ILE B 1 176 ? -16.78900 -37.40000 30.28200  1.000 100.46000 ? 167 ILE B CB     1 
ATOM   6212  C  CG1    . ILE B 1 176 ? -15.62500 -38.18900 30.88700  1.000 104.74000 ? 167 ILE B CG1    1 
ATOM   6213  C  CG2    . ILE B 1 176 ? -16.31800 -36.04900 29.76400  1.000 99.06000  ? 167 ILE B CG2    1 
ATOM   6214  C  CD1    . ILE B 1 176 ? -15.79800 -39.69400 30.81500  1.000 105.25000 ? 167 ILE B CD1    1 
ATOM   6215  N  N      . ASN B 1 177 ? -19.18400 -35.16100 31.04800  1.000 96.46000  ? 168 ASN B N      1 
ATOM   6216  C  CA     . ASN B 1 177 ? -20.24900 -34.29400 30.56300  1.000 92.81000  ? 168 ASN B CA     1 
ATOM   6217  C  C      . ASN B 1 177 ? -19.71700 -33.38300 29.46700  1.000 75.36000  ? 168 ASN B C      1 
ATOM   6218  O  O      . ASN B 1 177 ? -18.61000 -32.84600 29.57700  1.000 74.44000  ? 168 ASN B O      1 
ATOM   6219  C  CB     . ASN B 1 177 ? -20.82500 -33.44400 31.69700  1.000 88.45000  ? 168 ASN B CB     1 
ATOM   6220  C  CG     . ASN B 1 177 ? -21.28300 -34.27700 32.87500  1.000 113.69000 ? 168 ASN B CG     1 
ATOM   6221  O  OD1    . ASN B 1 177 ? -22.00900 -35.25800 32.71200  1.000 123.46000 ? 168 ASN B OD1    1 
ATOM   6222  N  ND2    . ASN B 1 177 ? -20.85600 -33.89100 34.07300  1.000 119.72000 ? 168 ASN B ND2    1 
ATOM   6223  N  N      . PHE B 1 178 ? -20.51100 -33.19800 28.41700  1.000 68.52000  ? 169 PHE B N      1 
ATOM   6224  C  CA     . PHE B 1 178 ? -20.11200 -32.26800 27.36800  1.000 66.95000  ? 169 PHE B CA     1 
ATOM   6225  C  C      . PHE B 1 178 ? -21.24900 -32.13500 26.36900  1.000 79.82000  ? 169 PHE B C      1 
ATOM   6226  O  O      . PHE B 1 178 ? -22.10800 -33.01100 26.26400  1.000 78.65000  ? 169 PHE B O      1 
ATOM   6227  C  CB     . PHE B 1 178 ? -18.82900 -32.72500 26.66200  1.000 75.51000  ? 169 PHE B CB     1 
ATOM   6228  C  CG     . PHE B 1 178 ? -18.80200 -34.19000 26.33800  1.000 47.15000  ? 169 PHE B CG     1 
ATOM   6229  C  CD1    . PHE B 1 178 ? -19.49100 -34.68200 25.24400  1.000 50.14000  ? 169 PHE B CD1    1 
ATOM   6230  C  CD2    . PHE B 1 178 ? -18.08400 -35.07400 27.12200  1.000 51.99000  ? 169 PHE B CD2    1 
ATOM   6231  C  CE1    . PHE B 1 178 ? -19.46900 -36.02900 24.94100  1.000 66.20000  ? 169 PHE B CE1    1 
ATOM   6232  C  CE2    . PHE B 1 178 ? -18.05700 -36.42300 26.82600  1.000 59.90000  ? 169 PHE B CE2    1 
ATOM   6233  C  CZ     . PHE B 1 178 ? -18.75000 -36.90300 25.73400  1.000 62.23000  ? 169 PHE B CZ     1 
ATOM   6234  N  N      . VAL B 1 179 ? -21.24500 -31.02500 25.63800  1.000 85.71000  ? 170 VAL B N      1 
ATOM   6235  C  CA     . VAL B 1 179 ? -22.13700 -30.89700 24.49100  1.000 81.47000  ? 170 VAL B CA     1 
ATOM   6236  C  C      . VAL B 1 179 ? -21.52900 -31.75200 23.38800  1.000 81.77000  ? 170 VAL B C      1 
ATOM   6237  O  O      . VAL B 1 179 ? -20.35700 -31.56000 23.03200  1.000 94.21000  ? 170 VAL B O      1 
ATOM   6238  C  CB     . VAL B 1 179 ? -22.31100 -29.43400 24.05900  1.000 82.87000  ? 170 VAL B CB     1 
ATOM   6239  C  CG1    . VAL B 1 179 ? -22.94600 -29.36300 22.67700  1.000 86.78000  ? 170 VAL B CG1    1 
ATOM   6240  C  CG2    . VAL B 1 179 ? -23.15700 -28.68200 25.07800  1.000 87.22000  ? 170 VAL B CG2    1 
ATOM   6241  N  N      . PRO B 1 180 ? -22.27700 -32.69900 22.82200  1.000 77.20000  ? 171 PRO B N      1 
ATOM   6242  C  CA     . PRO B 1 180 ? -21.63600 -33.69600 21.94400  1.000 90.39000  ? 171 PRO B CA     1 
ATOM   6243  C  C      . PRO B 1 180 ? -20.99800 -33.09100 20.70400  1.000 96.08000  ? 171 PRO B C      1 
ATOM   6244  O  O      . PRO B 1 180 ? -19.84300 -33.41100 20.37600  1.000 93.85000  ? 171 PRO B O      1 
ATOM   6245  C  CB     . PRO B 1 180 ? -22.79700 -34.64200 21.60400  1.000 111.35000 ? 171 PRO B CB     1 
ATOM   6246  C  CG     . PRO B 1 180 ? -24.03700 -33.82200 21.81200  1.000 98.47000  ? 171 PRO B CG     1 
ATOM   6247  C  CD     . PRO B 1 180 ? -23.72600 -32.92200 22.96300  1.000 92.28000  ? 171 PRO B CD     1 
ATOM   6248  N  N      . PHE B 1 181 ? -21.71800 -32.21500 20.00100  1.000 87.41000  ? 172 PHE B N      1 
ATOM   6249  C  CA     . PHE B 1 181 ? -21.19500 -31.68100 18.75000  1.000 80.22000  ? 172 PHE B CA     1 
ATOM   6250  C  C      . PHE B 1 181 ? -19.96000 -30.82200 18.99100  1.000 73.87000  ? 172 PHE B C      1 
ATOM   6251  O  O      . PHE B 1 181 ? -19.03200 -30.80800 18.17100  1.000 78.73000  ? 172 PHE B O      1 
ATOM   6252  C  CB     . PHE B 1 181 ? -22.27900 -30.88600 18.02500  1.000 81.15000  ? 172 PHE B CB     1 
ATOM   6253  C  CG     . PHE B 1 181 ? -21.97600 -30.64000 16.57700  1.000 69.69000  ? 172 PHE B CG     1 
ATOM   6254  C  CD1    . PHE B 1 181 ? -21.69900 -31.70100 15.73000  1.000 81.12000  ? 172 PHE B CD1    1 
ATOM   6255  C  CD2    . PHE B 1 181 ? -21.97400 -29.35700 16.06000  1.000 61.47000  ? 172 PHE B CD2    1 
ATOM   6256  C  CE1    . PHE B 1 181 ? -21.41800 -31.48600 14.39600  1.000 76.79000  ? 172 PHE B CE1    1 
ATOM   6257  C  CE2    . PHE B 1 181 ? -21.69500 -29.13700 14.72500  1.000 68.41000  ? 172 PHE B CE2    1 
ATOM   6258  C  CZ     . PHE B 1 181 ? -21.41600 -30.20200 13.89400  1.000 69.90000  ? 172 PHE B CZ     1 
ATOM   6259  N  N      . ALA B 1 182 ? -19.93100 -30.09200 20.10700  1.000 74.09000  ? 173 ALA B N      1 
ATOM   6260  C  CA     . ALA B 1 182 ? -18.72700 -29.34800 20.45700  1.000 74.70000  ? 173 ALA B CA     1 
ATOM   6261  C  C      . ALA B 1 182 ? -17.54500 -30.29000 20.62600  1.000 83.35000  ? 173 ALA B C      1 
ATOM   6262  O  O      . ALA B 1 182 ? -16.44100 -30.01000 20.14500  1.000 92.63000  ? 173 ALA B O      1 
ATOM   6263  C  CB     . ALA B 1 182 ? -18.95800 -28.53800 21.73200  1.000 76.75000  ? 173 ALA B CB     1 
ATOM   6264  N  N      . MET B 1 183 ? -17.76500 -31.42500 21.29300  1.000 79.61000  ? 174 MET B N      1 
ATOM   6265  C  CA     . MET B 1 183 ? -16.69800 -32.40200 21.46800  1.000 69.91000  ? 174 MET B CA     1 
ATOM   6266  C  C      . MET B 1 183 ? -16.21800 -32.93100 20.12100  1.000 77.04000  ? 174 MET B C      1 
ATOM   6267  O  O      . MET B 1 183 ? -15.01300 -33.12000 19.90800  1.000 78.30000  ? 174 MET B O      1 
ATOM   6268  C  CB     . MET B 1 183 ? -17.19100 -33.54900 22.35000  1.000 65.18000  ? 174 MET B CB     1 
ATOM   6269  C  CG     . MET B 1 183 ? -16.09800 -34.42900 22.92400  1.000 67.60000  ? 174 MET B CG     1 
ATOM   6270  S  SD     . MET B 1 183 ? -14.83600 -33.46300 23.76800  1.000 60.75000  ? 174 MET B SD     1 
ATOM   6271  C  CE     . MET B 1 183 ? -15.77500 -32.83900 25.15900  1.000 63.45000  ? 174 MET B CE     1 
ATOM   6272  N  N      . THR B 1 184 ? -17.14800 -33.16200 19.19100  1.000 73.41000  ? 175 THR B N      1 
ATOM   6273  C  CA     . THR B 1 184 ? -16.76900 -33.68100 17.87800  1.000 80.82000  ? 175 THR B CA     1 
ATOM   6274  C  C      . THR B 1 184 ? -15.93400 -32.66600 17.10000  1.000 78.55000  ? 175 THR B C      1 
ATOM   6275  O  O      . THR B 1 184 ? -14.88400 -33.00600 16.53100  1.000 83.45000  ? 175 THR B O      1 
ATOM   6276  C  CB     . THR B 1 184 ? -18.02000 -34.06900 17.08900  1.000 93.60000  ? 175 THR B CB     1 
ATOM   6277  O  OG1    . THR B 1 184 ? -18.87900 -34.86800 17.91200  1.000 109.43000 ? 175 THR B OG1    1 
ATOM   6278  C  CG2    . THR B 1 184 ? -17.64400 -34.86000 15.84200  1.000 92.42000  ? 175 THR B CG2    1 
ATOM   6279  N  N      . VAL B 1 185 ? -16.39000 -31.41100 17.05300  1.000 62.64000  ? 176 VAL B N      1 
ATOM   6280  C  CA     . VAL B 1 185 ? -15.61800 -30.38500 16.35800  1.000 63.15000  ? 176 VAL B CA     1 
ATOM   6281  C  C      . VAL B 1 185 ? -14.26000 -30.21000 17.01900  1.000 67.35000  ? 176 VAL B C      1 
ATOM   6282  O  O      . VAL B 1 185 ? -13.25500 -29.94600 16.34300  1.000 72.08000  ? 176 VAL B O      1 
ATOM   6283  C  CB     . VAL B 1 185 ? -16.39400 -29.05400 16.30900  1.000 71.64000  ? 176 VAL B CB     1 
ATOM   6284  C  CG1    . VAL B 1 185 ? -17.60900 -29.18200 15.40400  1.000 72.15000  ? 176 VAL B CG1    1 
ATOM   6285  C  CG2    . VAL B 1 185 ? -16.80800 -28.62100 17.70400  1.000 69.88000  ? 176 VAL B CG2    1 
ATOM   6286  N  N      . SER B 1 186 ? -14.19800 -30.37800 18.34200  1.000 64.28000  ? 177 SER B N      1 
ATOM   6287  C  CA     . SER B 1 186 ? -12.91700 -30.29200 19.03100  1.000 66.17000  ? 177 SER B CA     1 
ATOM   6288  C  C      . SER B 1 186 ? -11.99300 -31.42200 18.60300  1.000 53.25000  ? 177 SER B C      1 
ATOM   6289  O  O      . SER B 1 186 ? -10.79200 -31.21000 18.41500  1.000 44.77000  ? 177 SER B O      1 
ATOM   6290  C  CB     . SER B 1 186 ? -13.13800 -30.31500 20.54300  1.000 60.74000  ? 177 SER B CB     1 
ATOM   6291  O  OG     . SER B 1 186 ? -13.93800 -29.21700 20.95100  1.000 58.83000  ? 177 SER B OG     1 
ATOM   6292  N  N      . GLY B 1 187 ? -12.53700 -32.62800 18.43700  1.000 55.29000  ? 178 GLY B N      1 
ATOM   6293  C  CA     . GLY B 1 187 ? -11.72200 -33.72600 17.93900  1.000 63.89000  ? 178 GLY B CA     1 
ATOM   6294  C  C      . GLY B 1 187 ? -11.18800 -33.46300 16.54300  1.000 66.91000  ? 178 GLY B C      1 
ATOM   6295  O  O      . GLY B 1 187 ? -10.03100 -33.77100 16.23600  1.000 81.06000  ? 178 GLY B O      1 
ATOM   6296  N  N      . TYR B 1 188 ? -12.03100 -32.90400 15.67200  1.000 56.16000  ? 179 TYR B N      1 
ATOM   6297  C  CA     . TYR B 1 188 ? -11.56800 -32.53200 14.33400  1.000 60.56000  ? 179 TYR B CA     1 
ATOM   6298  C  C      . TYR B 1 188 ? -10.41700 -31.52800 14.41200  1.000 68.51000  ? 179 TYR B C      1 
ATOM   6299  O  O      . TYR B 1 188 ? -9.37600  -31.68800 13.75000  1.000 78.84000  ? 179 TYR B O      1 
ATOM   6300  C  CB     . TYR B 1 188 ? -12.73400 -31.97200 13.51500  1.000 64.42000  ? 179 TYR B CB     1 
ATOM   6301  C  CG     . TYR B 1 188 ? -12.42100 -31.73200 12.05000  1.000 68.71000  ? 179 TYR B CG     1 
ATOM   6302  C  CD1    . TYR B 1 188 ? -12.53400 -32.75500 11.11400  1.000 66.38000  ? 179 TYR B CD1    1 
ATOM   6303  C  CD2    . TYR B 1 188 ? -12.02300 -30.47900 11.60300  1.000 88.45000  ? 179 TYR B CD2    1 
ATOM   6304  C  CE1    . TYR B 1 188 ? -12.25400 -32.53600 9.77400   1.000 74.36000  ? 179 TYR B CE1    1 
ATOM   6305  C  CE2    . TYR B 1 188 ? -11.74000 -30.25200 10.26700  1.000 87.82000  ? 179 TYR B CE2    1 
ATOM   6306  C  CZ     . TYR B 1 188 ? -11.85700 -31.28100 9.35800   1.000 76.79000  ? 179 TYR B CZ     1 
ATOM   6307  O  OH     . TYR B 1 188 ? -11.57300 -31.04700 8.03200   1.000 75.99000  ? 179 TYR B OH     1 
ATOM   6308  N  N      . ALA B 1 189 ? -10.59300 -30.47700 15.22000  1.000 57.27000  ? 180 ALA B N      1 
ATOM   6309  C  CA     . ALA B 1 189 ? -9.53100  -29.49100 15.38400  1.000 59.59000  ? 180 ALA B CA     1 
ATOM   6310  C  C      . ALA B 1 189 ? -8.27000  -30.13900 15.94100  1.000 61.73000  ? 180 ALA B C      1 
ATOM   6311  O  O      . ALA B 1 189 ? -7.15200  -29.76100 15.57300  1.000 66.50000  ? 180 ALA B O      1 
ATOM   6312  C  CB     . ALA B 1 189 ? -10.00600 -28.35000 16.28700  1.000 61.54000  ? 180 ALA B CB     1 
ATOM   6313  N  N      . LEU B 1 190 ? -8.42900  -31.12900 16.82000  1.000 61.11000  ? 181 LEU B N      1 
ATOM   6314  C  CA     . LEU B 1 190 ? -7.26900  -31.81800 17.37600  1.000 59.63000  ? 181 LEU B CA     1 
ATOM   6315  C  C      . LEU B 1 190 ? -6.51400  -32.58600 16.30200  1.000 54.55000  ? 181 LEU B C      1 
ATOM   6316  O  O      . LEU B 1 190 ? -5.27800  -32.60800 16.29900  1.000 51.09000  ? 181 LEU B O      1 
ATOM   6317  C  CB     . LEU B 1 190 ? -7.69600  -32.75700 18.50200  1.000 59.68000  ? 181 LEU B CB     1 
ATOM   6318  C  CG     . LEU B 1 190 ? -6.53300  -33.50400 19.16700  1.000 52.33000  ? 181 LEU B CG     1 
ATOM   6319  C  CD1    . LEU B 1 190 ? -5.57600  -32.54400 19.86700  1.000 44.06000  ? 181 LEU B CD1    1 
ATOM   6320  C  CD2    . LEU B 1 190 ? -7.03800  -34.55600 20.14800  1.000 78.86000  ? 181 LEU B CD2    1 
ATOM   6321  N  N      . GLY B 1 191 ? -7.23800  -33.26100 15.41100  1.000 61.57000  ? 182 GLY B N      1 
ATOM   6322  C  CA     . GLY B 1 191 ? -6.56700  -33.93900 14.31200  1.000 78.36000  ? 182 GLY B CA     1 
ATOM   6323  C  C      . GLY B 1 191 ? -5.77800  -32.97400 13.44700  1.000 85.20000  ? 182 GLY B C      1 
ATOM   6324  O  O      . GLY B 1 191 ? -4.60300  -33.21400 13.11500  1.000 103.83000 ? 182 GLY B O      1 
ATOM   6325  N  N      . CYS B 1 192 ? -6.41800  -31.86700 13.05700  1.000 68.90000  ? 183 CYS B N      1 
ATOM   6326  C  CA     . CYS B 1 192 ? -5.69400  -30.87300 12.27300  1.000 62.46000  ? 183 CYS B CA     1 
ATOM   6327  C  C      . CYS B 1 192 ? -4.45300  -30.40900 13.02100  1.000 74.10000  ? 183 CYS B C      1 
ATOM   6328  O  O      . CYS B 1 192 ? -3.37600  -30.26600 12.43100  1.000 89.66000  ? 183 CYS B O      1 
ATOM   6329  C  CB     . CYS B 1 192 ? -6.59300  -29.68400 11.92900  1.000 67.36000  ? 183 CYS B CB     1 
ATOM   6330  S  SG     . CYS B 1 192 ? -8.15100  -30.08600 11.09700  1.000 82.04000  ? 183 CYS B SG     1 
ATOM   6331  N  N      . SER B 1 193 ? -4.58300  -30.19400 14.33200  1.000 70.34000  ? 184 SER B N      1 
ATOM   6332  C  CA     . SER B 1 193 ? -3.46100  -29.70600 15.12300  1.000 64.31000  ? 184 SER B CA     1 
ATOM   6333  C  C      . SER B 1 193 ? -2.33300  -30.72500 15.18300  1.000 74.20000  ? 184 SER B C      1 
ATOM   6334  O  O      . SER B 1 193 ? -1.16000  -30.35100 15.16100  1.000 77.18000  ? 184 SER B O      1 
ATOM   6335  C  CB     . SER B 1 193 ? -3.92500  -29.34000 16.53100  1.000 56.69000  ? 184 SER B CB     1 
ATOM   6336  O  OG     . SER B 1 193 ? -4.31500  -30.49100 17.25600  1.000 79.67000  ? 184 SER B OG     1 
ATOM   6337  N  N      . ILE B 1 194 ? -2.66100  -32.01300 15.30100  1.000 72.13000  ? 185 ILE B N      1 
ATOM   6338  C  CA     . ILE B 1 194 ? -1.61600  -33.03500 15.36500  1.000 73.27000  ? 185 ILE B CA     1 
ATOM   6339  C  C      . ILE B 1 194 ? -0.82900  -33.06500 14.06300  1.000 76.61000  ? 185 ILE B C      1 
ATOM   6340  O  O      . ILE B 1 194 ? 0.41200   -33.08200 14.06200  1.000 85.40000  ? 185 ILE B O      1 
ATOM   6341  C  CB     . ILE B 1 194 ? -2.21700  -34.41500 15.68900  1.000 61.00000  ? 185 ILE B CB     1 
ATOM   6342  C  CG1    . ILE B 1 194 ? -2.84300  -34.41400 17.08300  1.000 74.55000  ? 185 ILE B CG1    1 
ATOM   6343  C  CG2    . ILE B 1 194 ? -1.15000  -35.49600 15.59100  1.000 48.43000  ? 185 ILE B CG2    1 
ATOM   6344  C  CD1    . ILE B 1 194 ? -1.85500  -34.15600 18.19700  1.000 66.72000  ? 185 ILE B CD1    1 
ATOM   6345  N  N      . ILE B 1 195 ? -1.53500  -33.07200 12.93100  1.000 74.60000  ? 186 ILE B N      1 
ATOM   6346  C  CA     . ILE B 1 195 ? -0.80900  -33.11300 11.66300  1.000 78.71000  ? 186 ILE B CA     1 
ATOM   6347  C  C      . ILE B 1 195 ? 0.01400   -31.84400 11.48000  1.000 75.35000  ? 186 ILE B C      1 
ATOM   6348  O  O      . ILE B 1 195 ? 1.16100   -31.89300 11.01600  1.000 66.86000  ? 186 ILE B O      1 
ATOM   6349  C  CB     . ILE B 1 195 ? -1.76600  -33.34700 10.48000  1.000 89.27000  ? 186 ILE B CB     1 
ATOM   6350  C  CG1    . ILE B 1 195 ? -0.99000  -33.33100 9.15900   1.000 98.40000  ? 186 ILE B CG1    1 
ATOM   6351  C  CG2    . ILE B 1 195 ? -2.84900  -32.29400 10.45100  1.000 87.21000  ? 186 ILE B CG2    1 
ATOM   6352  C  CD1    . ILE B 1 195 ? 0.01900   -34.45400 9.02400   1.000 128.74000 ? 186 ILE B CD1    1 
ATOM   6353  N  N      . ALA B 1 196 ? -0.55300  -30.68800 11.84200  1.000 85.98000  ? 187 ALA B N      1 
ATOM   6354  C  CA     . ALA B 1 196 ? 0.17400   -29.43300 11.68900  1.000 85.26000  ? 187 ALA B CA     1 
ATOM   6355  C  C      . ALA B 1 196 ? 1.39500   -29.39100 12.59600  1.000 86.05000  ? 187 ALA B C      1 
ATOM   6356  O  O      . ALA B 1 196 ? 2.45900   -28.91000 12.19100  1.000 94.10000  ? 187 ALA B O      1 
ATOM   6357  C  CB     . ALA B 1 196 ? -0.75100  -28.24800 11.96700  1.000 68.46000  ? 187 ALA B CB     1 
ATOM   6358  N  N      . MET B 1 197 ? 1.26700   -29.89100 13.82600  1.000 73.44000  ? 188 MET B N      1 
ATOM   6359  C  CA     . MET B 1 197 ? 2.41100   -29.92100 14.72700  1.000 69.49000  ? 188 MET B CA     1 
ATOM   6360  C  C      . MET B 1 197 ? 3.50900   -30.79800 14.16500  1.000 76.67000  ? 188 MET B C      1 
ATOM   6361  O  O      . MET B 1 197 ? 4.67400   -30.39700 14.12000  1.000 69.04000  ? 188 MET B O      1 
ATOM   6362  C  CB     . MET B 1 197 ? 2.01400   -30.43800 16.10600  1.000 78.52000  ? 188 MET B CB     1 
ATOM   6363  C  CG     . MET B 1 197 ? 3.22200   -30.57700 17.03600  1.000 69.52000  ? 188 MET B CG     1 
ATOM   6364  S  SD     . MET B 1 197 ? 2.88900   -31.45800 18.56800  1.000 86.95000  ? 188 MET B SD     1 
ATOM   6365  C  CE     . MET B 1 197 ? 2.11700   -32.94100 17.92100  1.000 81.83000  ? 188 MET B CE     1 
ATOM   6366  N  N      . PHE B 1 198 ? 3.16100   -32.00200 13.71300  1.000 90.61000  ? 189 PHE B N      1 
ATOM   6367  C  CA     . PHE B 1 198 ? 4.20600   -32.85500 13.16800  1.000 89.74000  ? 189 PHE B CA     1 
ATOM   6368  C  C      . PHE B 1 198 ? 4.87200   -32.17000 11.99100  1.000 80.98000  ? 189 PHE B C      1 
ATOM   6369  O  O      . PHE B 1 198 ? 6.08800   -31.94300 11.99800  1.000 88.67000  ? 189 PHE B O      1 
ATOM   6370  C  CB     . PHE B 1 198 ? 3.63600   -34.21100 12.76300  1.000 87.21000  ? 189 PHE B CB     1 
ATOM   6371  C  CG     . PHE B 1 198 ? 3.76000   -35.26400 13.83000  1.000 91.24000  ? 189 PHE B CG     1 
ATOM   6372  C  CD1    . PHE B 1 198 ? 4.89000   -36.06600 13.89300  1.000 96.26000  ? 189 PHE B CD1    1 
ATOM   6373  C  CD2    . PHE B 1 198 ? 2.76500   -35.44600 14.77500  1.000 89.76000  ? 189 PHE B CD2    1 
ATOM   6374  C  CE1    . PHE B 1 198 ? 5.02000   -37.03700 14.86100  1.000 113.05000 ? 189 PHE B CE1    1 
ATOM   6375  C  CE2    . PHE B 1 198 ? 2.89400   -36.41700 15.75000  1.000 96.89000  ? 189 PHE B CE2    1 
ATOM   6376  C  CZ     . PHE B 1 198 ? 4.02200   -37.21200 15.79200  1.000 109.44000 ? 189 PHE B CZ     1 
ATOM   6377  N  N      . ASP B 1 199 ? 4.06600   -31.70700 11.03500  1.000 69.92000  ? 190 ASP B N      1 
ATOM   6378  C  CA     . ASP B 1 199 ? 4.62800   -31.09100 9.84400   1.000 73.07000  ? 190 ASP B CA     1 
ATOM   6379  C  C      . ASP B 1 199 ? 5.54800   -29.94300 10.21500  1.000 83.74000  ? 190 ASP B C      1 
ATOM   6380  O  O      . ASP B 1 199 ? 6.73700   -29.98200 9.90600   1.000 99.13000  ? 190 ASP B O      1 
ATOM   6381  C  CB     . ASP B 1 199 ? 3.50200   -30.61100 8.92800   1.000 82.06000  ? 190 ASP B CB     1 
ATOM   6382  C  CG     . ASP B 1 199 ? 3.85000   -30.70900 7.45300   1.000 93.53000  ? 190 ASP B CG     1 
ATOM   6383  O  OD1    . ASP B 1 199 ? 4.96800   -31.14100 7.11100   1.000 111.71000 ? 190 ASP B OD1    1 
ATOM   6384  O  OD2    . ASP B 1 199 ? 2.97600   -30.35800 6.63100   1.000 101.26000 ? 190 ASP B OD2    1 
ATOM   6385  N  N      . ARG B 1 200 ? 5.07300   -29.00100 11.02300  1.000 82.59000  ? 191 ARG B N      1 
ATOM   6386  C  CA     . ARG B 1 200 ? 5.86700   -27.79600 11.21700  1.000 87.60000  ? 191 ARG B CA     1 
ATOM   6387  C  C      . ARG B 1 200 ? 7.01900   -28.02300 12.18500  1.000 86.51000  ? 191 ARG B C      1 
ATOM   6388  O  O      . ARG B 1 200 ? 8.15600   -27.68300 11.87000  1.000 82.73000  ? 191 ARG B O      1 
ATOM   6389  C  CB     . ARG B 1 200 ? 4.98800   -26.63300 11.67500  1.000 81.20000  ? 191 ARG B CB     1 
ATOM   6390  C  CG     . ARG B 1 200 ? 4.82100   -25.59500 10.58400  1.000 81.26000  ? 191 ARG B CG     1 
ATOM   6391  C  CD     . ARG B 1 200 ? 6.02000   -24.65300 10.60500  1.000 106.13000 ? 191 ARG B CD     1 
ATOM   6392  N  NE     . ARG B 1 200 ? 6.10600   -23.80100 9.42300   1.000 127.20000 ? 191 ARG B NE     1 
ATOM   6393  C  CZ     . ARG B 1 200 ? 5.41800   -22.68300 9.23900   1.000 113.21000 ? 191 ARG B CZ     1 
ATOM   6394  N  NH1    . ARG B 1 200 ? 4.54900   -22.24800 10.13600  1.000 101.75000 ? 191 ARG B NH1    1 
ATOM   6395  N  NH2    . ARG B 1 200 ? 5.60500   -21.98300 8.12300   1.000 104.35000 ? 191 ARG B NH2    1 
ATOM   6396  N  N      . VAL B 1 201 ? 6.77600   -28.63500 13.34100  1.000 80.42000  ? 192 VAL B N      1 
ATOM   6397  C  CA     . VAL B 1 201 ? 7.87100   -28.84600 14.28000  1.000 72.03000  ? 192 VAL B CA     1 
ATOM   6398  C  C      . VAL B 1 201 ? 8.94800   -29.72100 13.65100  1.000 86.24000  ? 192 VAL B C      1 
ATOM   6399  O  O      . VAL B 1 201 ? 10.12000  -29.32900 13.56700  1.000 84.06000  ? 192 VAL B O      1 
ATOM   6400  C  CB     . VAL B 1 201 ? 7.34400   -29.45000 15.59200  1.000 52.63000  ? 192 VAL B CB     1 
ATOM   6401  C  CG1    . VAL B 1 201 ? 8.48500   -29.69900 16.54800  1.000 55.90000  ? 192 VAL B CG1    1 
ATOM   6402  C  CG2    . VAL B 1 201 ? 6.31200   -28.52500 16.22600  1.000 60.29000  ? 192 VAL B CG2    1 
ATOM   6403  N  N      . GLY B 1 202 ? 8.57000   -30.91000 13.17400  1.000 73.27000  ? 193 GLY B N      1 
ATOM   6404  C  CA     . GLY B 1 202 ? 9.57500   -31.80200 12.63100  1.000 69.62000  ? 193 GLY B CA     1 
ATOM   6405  C  C      . GLY B 1 202 ? 10.20800  -31.24800 11.37000  1.000 81.60000  ? 193 GLY B C      1 
ATOM   6406  O  O      . GLY B 1 202 ? 11.43600  -31.25700 11.22400  1.000 100.74000 ? 193 GLY B O      1 
ATOM   6407  N  N      . GLY B 1 203 ? 9.38200   -30.74400 10.44600  1.000 75.10000  ? 194 GLY B N      1 
ATOM   6408  C  CA     . GLY B 1 203 ? 9.90400   -30.21300 9.20500   1.000 81.39000  ? 194 GLY B CA     1 
ATOM   6409  C  C      . GLY B 1 203 ? 10.77900  -28.99600 9.40400   1.000 86.26000  ? 194 GLY B C      1 
ATOM   6410  O  O      . GLY B 1 203 ? 11.75100  -28.81000 8.68400   1.000 100.68000 ? 194 GLY B O      1 
ATOM   6411  N  N      . GLY B 1 204 ? 10.43100  -28.13400 10.35800  1.000 78.84000  ? 195 GLY B N      1 
ATOM   6412  C  CA     . GLY B 1 204 ? 11.28200  -27.00100 10.66100  1.000 87.76000  ? 195 GLY B CA     1 
ATOM   6413  C  C      . GLY B 1 204 ? 12.60000  -27.42200 11.27100  1.000 83.81000  ? 195 GLY B C      1 
ATOM   6414  O  O      . GLY B 1 204 ? 13.65600  -26.88700 10.91900  1.000 90.03000  ? 195 GLY B O      1 
ATOM   6415  N  N      . VAL B 1 205 ? 12.56300  -28.38500 12.19600  1.000 65.77000  ? 196 VAL B N      1 
ATOM   6416  C  CA     . VAL B 1 205 ? 13.81300  -28.89500 12.74200  1.000 73.17000  ? 196 VAL B CA     1 
ATOM   6417  C  C      . VAL B 1 205 ? 14.69100  -29.39800 11.60700  1.000 75.83000  ? 196 VAL B C      1 
ATOM   6418  O  O      . VAL B 1 205 ? 15.86600  -29.03100 11.49300  1.000 86.23000  ? 196 VAL B O      1 
ATOM   6419  C  CB     . VAL B 1 205 ? 13.54000  -29.99500 13.78300  1.000 77.10000  ? 196 VAL B CB     1 
ATOM   6420  C  CG1    . VAL B 1 205 ? 14.81000  -30.78800 14.06400  1.000 82.21000  ? 196 VAL B CG1    1 
ATOM   6421  C  CG2    . VAL B 1 205 ? 12.98700  -29.39300 15.06200  1.000 67.42000  ? 196 VAL B CG2    1 
ATOM   6422  N  N      . TYR B 1 206 ? 14.10300  -30.18500 10.70500  1.000 67.06000  ? 197 TYR B N      1 
ATOM   6423  C  CA     . TYR B 1 206 ? 14.84900  -30.71600 9.57100   1.000 68.34000  ? 197 TYR B CA     1 
ATOM   6424  C  C      . TYR B 1 206 ? 15.29500  -29.60800 8.62500   1.000 95.36000  ? 197 TYR B C      1 
ATOM   6425  O  O      . TYR B 1 206 ? 16.41500  -29.64000 8.11200   1.000 126.04000 ? 197 TYR B O      1 
ATOM   6426  C  CB     . TYR B 1 206 ? 13.99500  -31.74600 8.83800   1.000 76.22000  ? 197 TYR B CB     1 
ATOM   6427  C  CG     . TYR B 1 206 ? 14.28300  -31.85000 7.36100   1.000 87.33000  ? 197 TYR B CG     1 
ATOM   6428  C  CD1    . TYR B 1 206 ? 15.40100  -32.53100 6.89100   1.000 88.62000  ? 197 TYR B CD1    1 
ATOM   6429  C  CD2    . TYR B 1 206 ? 13.43600  -31.26100 6.43300   1.000 88.18000  ? 197 TYR B CD2    1 
ATOM   6430  C  CE1    . TYR B 1 206 ? 15.66100  -32.62600 5.53100   1.000 79.30000  ? 197 TYR B CE1    1 
ATOM   6431  C  CE2    . TYR B 1 206 ? 13.68800  -31.35000 5.08100   1.000 97.50000  ? 197 TYR B CE2    1 
ATOM   6432  C  CZ     . TYR B 1 206 ? 14.80100  -32.03200 4.63300   1.000 92.44000  ? 197 TYR B CZ     1 
ATOM   6433  O  OH     . TYR B 1 206 ? 15.05000  -32.11900 3.28100   1.000 103.95000 ? 197 TYR B OH     1 
ATOM   6434  N  N      . THR B 1 207 ? 14.43600  -28.61800 8.39100   1.000 90.71000  ? 198 THR B N      1 
ATOM   6435  C  CA     . THR B 1 207 ? 14.73500  -27.54100 7.45600   1.000 94.97000  ? 198 THR B CA     1 
ATOM   6436  C  C      . THR B 1 207 ? 15.94200  -26.74200 7.91400   1.000 100.79000 ? 198 THR B C      1 
ATOM   6437  O  O      . THR B 1 207 ? 16.88200  -26.50500 7.14400   1.000 107.18000 ? 198 THR B O      1 
ATOM   6438  C  CB     . THR B 1 207 ? 13.51000  -26.63300 7.31600   1.000 89.88000  ? 198 THR B CB     1 
ATOM   6439  O  OG1    . THR B 1 207 ? 12.52300  -27.28700 6.51200   1.000 114.99000 ? 198 THR B OG1    1 
ATOM   6440  C  CG2    . THR B 1 207 ? 13.87600  -25.31000 6.66500   1.000 95.58000  ? 198 THR B CG2    1 
ATOM   6441  N  N      . LYS B 1 208 ? 15.93900  -26.32000 9.17400   1.000 90.15000  ? 199 LYS B N      1 
ATOM   6442  C  CA     . LYS B 1 208 ? 17.05400  -25.51700 9.63700   1.000 86.65000  ? 199 LYS B CA     1 
ATOM   6443  C  C      . LYS B 1 208 ? 18.27100  -26.36600 9.95600   1.000 94.61000  ? 199 LYS B C      1 
ATOM   6444  O  O      . LYS B 1 208 ? 19.39500  -25.86600 9.84700   1.000 104.84000 ? 199 LYS B O      1 
ATOM   6445  C  CB     . LYS B 1 208 ? 16.63500  -24.67700 10.84000  1.000 81.41000  ? 199 LYS B CB     1 
ATOM   6446  C  CG     . LYS B 1 208 ? 15.90000  -23.41000 10.41100  1.000 90.52000  ? 199 LYS B CG     1 
ATOM   6447  C  CD     . LYS B 1 208 ? 16.58000  -22.76000 9.20000   1.000 105.00000 ? 199 LYS B CD     1 
ATOM   6448  C  CE     . LYS B 1 208 ? 15.70000  -22.81800 7.94500   1.000 92.53000  ? 199 LYS B CE     1 
ATOM   6449  N  NZ     . LYS B 1 208 ? 16.42000  -22.43200 6.69200   1.000 92.94000  ? 199 LYS B NZ     1 
ATOM   6450  N  N      . ALA B 1 209 ? 18.08600  -27.66000 10.23300  1.000 85.73000  ? 200 ALA B N      1 
ATOM   6451  C  CA     . ALA B 1 209 ? 19.23700  -28.54600 10.29800  1.000 82.40000  ? 200 ALA B CA     1 
ATOM   6452  C  C      . ALA B 1 209 ? 19.87700  -28.69800 8.93200   1.000 86.02000  ? 200 ALA B C      1 
ATOM   6453  O  O      . ALA B 1 209 ? 21.10300  -28.75900 8.83500   1.000 90.04000  ? 200 ALA B O      1 
ATOM   6454  C  CB     . ALA B 1 209 ? 18.83100  -29.91900 10.83300  1.000 74.58000  ? 200 ALA B CB     1 
ATOM   6455  N  N      . ALA B 1 210 ? 19.06600  -28.69800 7.86800   1.000 82.79000  ? 201 ALA B N      1 
ATOM   6456  C  CA     . ALA B 1 210 ? 19.59500  -28.80900 6.51400   1.000 91.85000  ? 201 ALA B CA     1 
ATOM   6457  C  C      . ALA B 1 210 ? 20.28100  -27.52100 6.08400   1.000 94.86000  ? 201 ALA B C      1 
ATOM   6458  O  O      . ALA B 1 210 ? 21.35200  -27.56000 5.47400   1.000 94.91000  ? 201 ALA B O      1 
ATOM   6459  C  CB     . ALA B 1 210 ? 18.47100  -29.16900 5.53900   1.000 90.83000  ? 201 ALA B CB     1 
ATOM   6460  N  N      . ASP B 1 211 ? 19.71000  -26.36900 6.43400   1.000 90.31000  ? 202 ASP B N      1 
ATOM   6461  C  CA     . ASP B 1 211 ? 20.39200  -25.11300 6.13400   1.000 89.66000  ? 202 ASP B CA     1 
ATOM   6462  C  C      . ASP B 1 211 ? 21.70500  -25.00700 6.90000   1.000 91.52000  ? 202 ASP B C      1 
ATOM   6463  O  O      . ASP B 1 211 ? 22.73700  -24.62100 6.33400   1.000 105.13000 ? 202 ASP B O      1 
ATOM   6464  C  CB     . ASP B 1 211 ? 19.49200  -23.92100 6.45500   1.000 98.67000  ? 202 ASP B CB     1 
ATOM   6465  C  CG     . ASP B 1 211 ? 19.97200  -22.63900 5.80100   1.000 100.24000 ? 202 ASP B CG     1 
ATOM   6466  O  OD1    . ASP B 1 211 ? 19.69500  -22.43800 4.59900   1.000 90.35000  ? 202 ASP B OD1    1 
ATOM   6467  O  OD2    . ASP B 1 211 ? 20.63500  -21.83900 6.49200   1.000 85.56000  ? 202 ASP B OD2    1 
ATOM   6468  N  N      . MET B 1 212 ? 21.69200  -25.36700 8.18600   1.000 86.52000  ? 203 MET B N      1 
ATOM   6469  C  CA     . MET B 1 212 ? 22.90500  -25.30100 8.98700   1.000 89.78000  ? 203 MET B CA     1 
ATOM   6470  C  C      . MET B 1 212 ? 23.94800  -26.28900 8.48600   1.000 103.02000 ? 203 MET B C      1 
ATOM   6471  O  O      . MET B 1 212 ? 25.12500  -25.94000 8.35700   1.000 108.58000 ? 203 MET B O      1 
ATOM   6472  C  CB     . MET B 1 212 ? 22.56500  -25.56300 10.45400  1.000 74.96000  ? 203 MET B CB     1 
ATOM   6473  C  CG     . MET B 1 212 ? 23.74500  -25.48700 11.38800  1.000 77.13000  ? 203 MET B CG     1 
ATOM   6474  S  SD     . MET B 1 212 ? 23.25700  -25.71700 13.10700  1.000 108.67000 ? 203 MET B SD     1 
ATOM   6475  C  CE     . MET B 1 212 ? 22.13600  -24.33700 13.33200  1.000 85.70000  ? 203 MET B CE     1 
ATOM   6476  N  N      . ALA B 1 213 ? 23.53400  -27.51100 8.15200   1.000 101.51000 ? 204 ALA B N      1 
ATOM   6477  C  CA     . ALA B 1 213 ? 24.48600  -28.48900 7.65000   1.000 89.09000  ? 204 ALA B CA     1 
ATOM   6478  C  C      . ALA B 1 213 ? 25.03000  -28.08400 6.29000   1.000 96.29000  ? 204 ALA B C      1 
ATOM   6479  O  O      . ALA B 1 213 ? 26.21900  -28.25700 6.02900   1.000 107.50000 ? 204 ALA B O      1 
ATOM   6480  C  CB     . ALA B 1 213 ? 23.83700  -29.86700 7.58500   1.000 80.24000  ? 204 ALA B CB     1 
ATOM   6481  N  N      . ALA B 1 214 ? 24.18900  -27.52300 5.41700   1.000 92.26000  ? 205 ALA B N      1 
ATOM   6482  C  CA     . ALA B 1 214 ? 24.65500  -27.09100 4.10200   1.000 98.86000  ? 205 ALA B CA     1 
ATOM   6483  C  C      . ALA B 1 214 ? 25.65600  -25.94700 4.21900   1.000 105.09000 ? 205 ALA B C      1 
ATOM   6484  O  O      . ALA B 1 214 ? 26.76600  -26.02100 3.67600   1.000 112.49000 ? 205 ALA B O      1 
ATOM   6485  C  CB     . ALA B 1 214 ? 23.46800  -26.68200 3.22700   1.000 101.53000 ? 205 ALA B CB     1 
ATOM   6486  N  N      . ASP B 1 215 ? 25.29100  -24.89100 4.95100   1.000 95.15000  ? 206 ASP B N      1 
ATOM   6487  C  CA     . ASP B 1 215 ? 26.17800  -23.74700 5.10100   1.000 98.34000  ? 206 ASP B CA     1 
ATOM   6488  C  C      . ASP B 1 215 ? 27.42200  -24.07800 5.90700   1.000 103.87000 ? 206 ASP B C      1 
ATOM   6489  O  O      . ASP B 1 215 ? 28.45700  -23.43600 5.70700   1.000 99.31000  ? 206 ASP B O      1 
ATOM   6490  C  CB     . ASP B 1 215 ? 25.41600  -22.59600 5.75100   1.000 102.81000 ? 206 ASP B CB     1 
ATOM   6491  C  CG     . ASP B 1 215 ? 25.06300  -21.50100 4.76300   1.000 119.23000 ? 206 ASP B CG     1 
ATOM   6492  O  OD1    . ASP B 1 215 ? 25.53600  -21.56200 3.60500   1.000 117.13000 ? 206 ASP B OD1    1 
ATOM   6493  O  OD2    . ASP B 1 215 ? 24.27500  -20.60400 5.13300   1.000 114.39000 ? 206 ASP B OD2    1 
ATOM   6494  N  N      . LEU B 1 216 ? 27.36300  -25.08600 6.77900   1.000 104.73000 ? 207 LEU B N      1 
ATOM   6495  C  CA     . LEU B 1 216 ? 28.55200  -25.49000 7.51300   1.000 114.02000 ? 207 LEU B CA     1 
ATOM   6496  C  C      . LEU B 1 216 ? 29.43300  -26.41100 6.68100   1.000 119.80000 ? 207 LEU B C      1 
ATOM   6497  O  O      . LEU B 1 216 ? 30.66300  -26.32200 6.74800   1.000 129.95000 ? 207 LEU B O      1 
ATOM   6498  C  CB     . LEU B 1 216 ? 28.13900  -26.17300 8.81500   1.000 102.10000 ? 207 LEU B CB     1 
ATOM   6499  C  CG     . LEU B 1 216 ? 29.23400  -26.67500 9.75000   1.000 119.26000 ? 207 LEU B CG     1 
ATOM   6500  C  CD1    . LEU B 1 216 ? 30.18100  -25.54700 10.13700  1.000 110.10000 ? 207 LEU B CD1    1 
ATOM   6501  C  CD2    . LEU B 1 216 ? 28.59900  -27.29400 10.99000  1.000 106.95000 ? 207 LEU B CD2    1 
ATOM   6502  N  N      . VAL B 1 217 ? 28.82600  -27.30100 5.89600   1.000 112.22000 ? 208 VAL B N      1 
ATOM   6503  C  CA     . VAL B 1 217 ? 29.59000  -28.21800 5.06200   1.000 121.91000 ? 208 VAL B CA     1 
ATOM   6504  C  C      . VAL B 1 217 ? 30.30100  -27.45500 3.95800   1.000 128.93000 ? 208 VAL B C      1 
ATOM   6505  O  O      . VAL B 1 217 ? 31.43500  -27.78300 3.58700   1.000 132.29000 ? 208 VAL B O      1 
ATOM   6506  C  CB     . VAL B 1 217 ? 28.66600  -29.31000 4.49500   1.000 118.65000 ? 208 VAL B CB     1 
ATOM   6507  C  CG1    . VAL B 1 217 ? 29.23900  -29.85500 3.20000   1.000 132.62000 ? 208 VAL B CG1    1 
ATOM   6508  C  CG2    . VAL B 1 217 ? 28.46400  -30.42500 5.51700   1.000 92.75000  ? 208 VAL B CG2    1 
ATOM   6509  N  N      . GLY B 1 218 ? 29.64600  -26.43200 3.40700   1.000 120.04000 ? 209 GLY B N      1 
ATOM   6510  C  CA     . GLY B 1 218 ? 30.34700  -25.53300 2.51000   1.000 123.51000 ? 209 GLY B CA     1 
ATOM   6511  C  C      . GLY B 1 218 ? 31.60900  -24.98600 3.14100   1.000 127.31000 ? 209 GLY B C      1 
ATOM   6512  O  O      . GLY B 1 218 ? 32.65200  -24.89300 2.49200   1.000 125.47000 ? 209 GLY B O      1 
ATOM   6513  N  N      . LYS B 1 219 ? 31.53300  -24.63400 4.42700   1.000 127.99000 ? 210 LYS B N      1 
ATOM   6514  C  CA     . LYS B 1 219 ? 32.70000  -24.19900 5.18100   1.000 124.06000 ? 210 LYS B CA     1 
ATOM   6515  C  C      . LYS B 1 219 ? 33.54500  -25.35400 5.69900   1.000 135.66000 ? 210 LYS B C      1 
ATOM   6516  O  O      . LYS B 1 219 ? 34.74100  -25.16700 5.94500   1.000 152.88000 ? 210 LYS B O      1 
ATOM   6517  C  CB     . LYS B 1 219 ? 32.26800  -23.33800 6.36900   1.000 124.02000 ? 210 LYS B CB     1 
ATOM   6518  C  CG     . LYS B 1 219 ? 31.08900  -22.42600 6.08900   1.000 129.03000 ? 210 LYS B CG     1 
ATOM   6519  C  CD     . LYS B 1 219 ? 31.38500  -21.44500 4.96600   1.000 123.30000 ? 210 LYS B CD     1 
ATOM   6520  C  CE     . LYS B 1 219 ? 30.14700  -20.62600 4.64100   1.000 116.23000 ? 210 LYS B CE     1 
ATOM   6521  N  NZ     . LYS B 1 219 ? 30.42200  -19.51700 3.68800   1.000 114.42000 ? 210 LYS B NZ     1 
ATOM   6522  N  N      . THR B 1 220 ? 32.94900  -26.53800 5.86400   1.000 140.68000 ? 211 THR B N      1 
ATOM   6523  C  CA     . THR B 1 220 ? 33.66600  -27.66100 6.46200   1.000 143.25000 ? 211 THR B CA     1 
ATOM   6524  C  C      . THR B 1 220 ? 34.84600  -28.09300 5.60000   1.000 135.26000 ? 211 THR B C      1 
ATOM   6525  O  O      . THR B 1 220 ? 35.96700  -28.25700 6.09600   1.000 129.77000 ? 211 THR B O      1 
ATOM   6526  C  CB     . THR B 1 220 ? 32.71300  -28.83900 6.68300   1.000 132.88000 ? 211 THR B CB     1 
ATOM   6527  O  OG1    . THR B 1 220 ? 31.66500  -28.45000 7.58200   1.000 123.22000 ? 211 THR B OG1    1 
ATOM   6528  C  CG2    . THR B 1 220 ? 33.46100  -30.03100 7.27100   1.000 128.74000 ? 211 THR B CG2    1 
ATOM   6529  N  N      . GLU B 1 221 ? 34.61400  -28.29000 4.30700   1.000 125.26000 ? 212 GLU B N      1 
ATOM   6530  C  CA     . GLU B 1 221 ? 35.67500  -28.74900 3.41900   1.000 131.23000 ? 212 GLU B CA     1 
ATOM   6531  C  C      . GLU B 1 221 ? 35.71600  -27.92100 2.13800   1.000 125.05000 ? 212 GLU B C      1 
ATOM   6532  O  O      . GLU B 1 221 ? 35.26600  -26.77600 2.11400   1.000 119.52000 ? 212 GLU B O      1 
ATOM   6533  C  CB     . GLU B 1 221 ? 35.50600  -30.23300 3.08400   1.000 129.36000 ? 212 GLU B CB     1 
ATOM   6534  C  CG     . GLU B 1 221 ? 36.75600  -30.88700 2.51500   1.000 125.10000 ? 212 GLU B CG     1 
ATOM   6535  C  CD     . GLU B 1 221 ? 37.86200  -31.01700 3.54800   1.000 128.37000 ? 212 GLU B CD     1 
ATOM   6536  O  OE1    . GLU B 1 221 ? 37.54400  -31.06200 4.75500   1.000 130.51000 ? 212 GLU B OE1    1 
ATOM   6537  O  OE2    . GLU B 1 221 ? 39.04600  -31.07300 3.15500   1.000 124.73000 ? 212 GLU B OE2    1 
ATOM   6538  N  N      . PRO B 1 225 ? 33.53200  -22.03100 0.31400   1.000 151.54000 ? 216 PRO B N      1 
ATOM   6539  C  CA     . PRO B 1 225 ? 32.65000  -22.57200 -0.72700  1.000 154.63000 ? 216 PRO B CA     1 
ATOM   6540  C  C      . PRO B 1 225 ? 31.16300  -22.34500 -0.43600  1.000 152.51000 ? 216 PRO B C      1 
ATOM   6541  O  O      . PRO B 1 225 ? 30.33500  -22.52500 -1.33400  1.000 155.43000 ? 216 PRO B O      1 
ATOM   6542  C  CB     . PRO B 1 225 ? 32.97800  -24.06700 -0.71400  1.000 142.43000 ? 216 PRO B CB     1 
ATOM   6543  C  CG     . PRO B 1 225 ? 34.37800  -24.13800 -0.20200  1.000 138.84000 ? 216 PRO B CG     1 
ATOM   6544  C  CD     . PRO B 1 225 ? 34.49500  -23.03200 0.80500   1.000 147.85000 ? 216 PRO B CD     1 
ATOM   6545  N  N      . GLU B 1 226 ? 30.84900  -21.92400 0.79300   1.000 138.65000 ? 217 GLU B N      1 
ATOM   6546  C  CA     . GLU B 1 226 ? 29.49000  -21.59500 1.21400   1.000 142.28000 ? 217 GLU B CA     1 
ATOM   6547  C  C      . GLU B 1 226 ? 28.48300  -22.62200 0.69800   1.000 143.11000 ? 217 GLU B C      1 
ATOM   6548  O  O      . GLU B 1 226 ? 28.66600  -23.82500 0.90800   1.000 139.41000 ? 217 GLU B O      1 
ATOM   6549  C  CB     . GLU B 1 226 ? 29.14300  -20.17400 0.75300   1.000 152.11000 ? 217 GLU B CB     1 
ATOM   6550  C  CG     . GLU B 1 226 ? 27.87800  -19.60800 1.37800   1.000 155.10000 ? 217 GLU B CG     1 
ATOM   6551  C  CD     . GLU B 1 226 ? 27.27900  -18.46400 0.57300   1.000 148.44000 ? 217 GLU B CD     1 
ATOM   6552  O  OE1    . GLU B 1 226 ? 26.19300  -17.97200 0.94800   1.000 131.58000 ? 217 GLU B OE1    1 
ATOM   6553  O  OE2    . GLU B 1 226 ? 27.89700  -18.05100 -0.43200  1.000 140.94000 ? 217 GLU B OE2    1 
ATOM   6554  N  N      . ASP B 1 227 ? 27.43300  -22.17000 0.01000   1.000 142.40000 ? 218 ASP B N      1 
ATOM   6555  C  CA     . ASP B 1 227 ? 26.37700  -23.04800 -0.49500  1.000 133.71000 ? 218 ASP B CA     1 
ATOM   6556  C  C      . ASP B 1 227 ? 26.85600  -23.71400 -1.77600  1.000 132.95000 ? 218 ASP B C      1 
ATOM   6557  O  O      . ASP B 1 227 ? 26.72300  -23.17200 -2.87500  1.000 132.60000 ? 218 ASP B O      1 
ATOM   6558  C  CB     . ASP B 1 227 ? 25.09500  -22.26000 -0.73400  1.000 123.05000 ? 218 ASP B CB     1 
ATOM   6559  C  CG     . ASP B 1 227 ? 24.27300  -22.08800 0.52200   1.000 125.88000 ? 218 ASP B CG     1 
ATOM   6560  O  OD1    . ASP B 1 227 ? 24.64200  -22.68200 1.55900   1.000 118.82000 ? 218 ASP B OD1    1 
ATOM   6561  O  OD2    . ASP B 1 227 ? 23.26200  -21.35500 0.47000   1.000 123.55000 ? 218 ASP B OD2    1 
ATOM   6562  N  N      . ASP B 1 228 ? 27.42900  -24.90800 -1.63500  1.000 141.53000 ? 219 ASP B N      1 
ATOM   6563  C  CA     . ASP B 1 228 ? 27.80700  -25.61700 -2.84300  1.000 148.87000 ? 219 ASP B CA     1 
ATOM   6564  C  C      . ASP B 1 228 ? 26.56300  -26.19000 -3.51500  1.000 140.49000 ? 219 ASP B C      1 
ATOM   6565  O  O      . ASP B 1 228 ? 25.58300  -26.52600 -2.84300  1.000 132.32000 ? 219 ASP B O      1 
ATOM   6566  C  CB     . ASP B 1 228 ? 28.78300  -26.74600 -2.52500  1.000 146.61000 ? 219 ASP B CB     1 
ATOM   6567  C  CG     . ASP B 1 228 ? 30.09000  -26.24400 -1.94600  1.000 152.05000 ? 219 ASP B CG     1 
ATOM   6568  O  OD1    . ASP B 1 228 ? 30.42100  -25.06000 -2.16600  1.000 162.79000 ? 219 ASP B OD1    1 
ATOM   6569  O  OD2    . ASP B 1 228 ? 30.78600  -27.03300 -1.26900  1.000 128.30000 ? 219 ASP B OD2    1 
ATOM   6570  N  N      . PRO B 1 229 ? 26.57500  -26.30300 -4.83800  1.000 142.49000 ? 220 PRO B N      1 
ATOM   6571  C  CA     . PRO B 1 229 ? 25.40000  -26.84200 -5.53200  1.000 139.09000 ? 220 PRO B CA     1 
ATOM   6572  C  C      . PRO B 1 229 ? 25.29000  -28.34400 -5.34400  1.000 134.37000 ? 220 PRO B C      1 
ATOM   6573  O  O      . PRO B 1 229 ? 24.21900  -28.86200 -5.00800  1.000 130.89000 ? 220 PRO B O      1 
ATOM   6574  C  CB     . PRO B 1 229 ? 25.65100  -26.46900 -6.99900  1.000 144.29000 ? 220 PRO B CB     1 
ATOM   6575  C  CG     . PRO B 1 229 ? 26.63100  -25.32900 -6.94100  1.000 134.94000 ? 220 PRO B CG     1 
ATOM   6576  C  CD     . PRO B 1 229 ? 27.50600  -25.64000 -5.76500  1.000 142.64000 ? 220 PRO B CD     1 
ATOM   6577  N  N      . ARG B 1 230 ? 26.40800  -29.04700 -5.53000  1.000 133.10000 ? 221 ARG B N      1 
ATOM   6578  C  CA     . ARG B 1 230 ? 26.45100  -30.49500 -5.38100  1.000 126.40000 ? 221 ARG B CA     1 
ATOM   6579  C  C      . ARG B 1 230 ? 26.46300  -30.94400 -3.92800  1.000 117.79000 ? 221 ARG B C      1 
ATOM   6580  O  O      . ARG B 1 230 ? 26.65300  -32.13700 -3.66400  1.000 114.13000 ? 221 ARG B O      1 
ATOM   6581  C  CB     . ARG B 1 230 ? 27.69500  -31.04100 -6.08900  1.000 144.96000 ? 221 ARG B CB     1 
ATOM   6582  C  CG     . ARG B 1 230 ? 27.73700  -30.79700 -7.59000  1.000 144.69000 ? 221 ARG B CG     1 
ATOM   6583  C  CD     . ARG B 1 230 ? 29.08200  -31.21300 -8.17700  1.000 138.87000 ? 221 ARG B CD     1 
ATOM   6584  N  NE     . ARG B 1 230 ? 29.55600  -32.46800 -7.60600  1.000 110.48000 ? 221 ARG B NE     1 
ATOM   6585  C  CZ     . ARG B 1 230 ? 29.28100  -33.67100 -8.09000  1.000 113.08000 ? 221 ARG B CZ     1 
ATOM   6586  N  NH1    . ARG B 1 230 ? 28.54400  -33.82800 -9.17800  1.000 109.72000 ? 221 ARG B NH1    1 
ATOM   6587  N  NH2    . ARG B 1 230 ? 29.75100  -34.74500 -7.46200  1.000 118.62000 ? 221 ARG B NH2    1 
ATOM   6588  N  N      . ASN B 1 231 ? 26.26600  -30.03400 -2.98900  1.000 114.28000 ? 222 ASN B N      1 
ATOM   6589  C  CA     . ASN B 1 231 ? 26.12400  -30.43400 -1.60000  1.000 114.64000 ? 222 ASN B CA     1 
ATOM   6590  C  C      . ASN B 1 231 ? 24.81200  -31.19100 -1.42900  1.000 123.71000 ? 222 ASN B C      1 
ATOM   6591  O  O      . ASN B 1 231 ? 23.76100  -30.70000 -1.86100  1.000 119.06000 ? 222 ASN B O      1 
ATOM   6592  C  CB     . ASN B 1 231 ? 26.17500  -29.21400 -0.68900  1.000 114.59000 ? 222 ASN B CB     1 
ATOM   6593  C  CG     . ASN B 1 231 ? 26.34000  -29.58400 0.77000   1.000 113.69000 ? 222 ASN B CG     1 
ATOM   6594  O  OD1    . ASN B 1 231 ? 26.84900  -30.65700 1.10100   1.000 99.61000  ? 222 ASN B OD1    1 
ATOM   6595  N  ND2    . ASN B 1 231 ? 25.91900  -28.68900 1.65300   1.000 116.78000 ? 222 ASN B ND2    1 
ATOM   6596  N  N      . PRO B 1 232 ? 24.82200  -32.38100 -0.82400  1.000 120.22000 ? 223 PRO B N      1 
ATOM   6597  C  CA     . PRO B 1 232 ? 23.54000  -33.06300 -0.57000  1.000 123.61000 ? 223 PRO B CA     1 
ATOM   6598  C  C      . PRO B 1 232 ? 22.60500  -32.23900 0.29900   1.000 130.58000 ? 223 PRO B C      1 
ATOM   6599  O  O      . PRO B 1 232 ? 21.38700  -32.20100 0.06200   1.000 124.53000 ? 223 PRO B O      1 
ATOM   6600  C  CB     . PRO B 1 232 ? 23.97100  -34.37000 0.11600   1.000 103.76000 ? 223 PRO B CB     1 
ATOM   6601  C  CG     . PRO B 1 232 ? 25.36700  -34.09300 0.64300   1.000 91.36000  ? 223 PRO B CG     1 
ATOM   6602  C  CD     . PRO B 1 232 ? 25.97600  -33.17900 -0.37600  1.000 103.35000 ? 223 PRO B CD     1 
ATOM   6603  N  N      . ALA B 1 233 ? 23.15700  -31.56400 1.30700   1.000 132.52000 ? 224 ALA B N      1 
ATOM   6604  C  CA     . ALA B 1 233 ? 22.35300  -30.70700 2.15900   1.000 116.79000 ? 224 ALA B CA     1 
ATOM   6605  C  C      . ALA B 1 233 ? 21.75000  -29.53800 1.40400   1.000 125.88000 ? 224 ALA B C      1 
ATOM   6606  O  O      . ALA B 1 233 ? 20.74500  -28.99600 1.85600   1.000 139.48000 ? 224 ALA B O      1 
ATOM   6607  C  CB     . ALA B 1 233 ? 23.18800  -30.19900 3.32300   1.000 107.32000 ? 224 ALA B CB     1 
ATOM   6608  N  N      . THR B 1 234 ? 22.33100  -29.13400 0.27300   1.000 117.33000 ? 225 THR B N      1 
ATOM   6609  C  CA     . THR B 1 234 ? 21.71200  -28.09400 -0.54700  1.000 112.62000 ? 225 THR B CA     1 
ATOM   6610  C  C      . THR B 1 234 ? 20.38700  -28.57700 -1.13100  1.000 119.69000 ? 225 THR B C      1 
ATOM   6611  O  O      . THR B 1 234 ? 19.36800  -27.86800 -1.09200  1.000 114.88000 ? 225 THR B O      1 
ATOM   6612  C  CB     . THR B 1 234 ? 22.67900  -27.66200 -1.65100  1.000 104.57000 ? 225 THR B CB     1 
ATOM   6613  O  OG1    . THR B 1 234 ? 23.77700  -26.94900 -1.06800  1.000 122.54000 ? 225 THR B OG1    1 
ATOM   6614  C  CG2    . THR B 1 234 ? 21.98000  -26.76500 -2.66100  1.000 90.55000  ? 225 THR B CG2    1 
ATOM   6615  N  N      . ILE B 1 235 ? 20.38800  -29.79100 -1.68400  1.000 121.15000 ? 226 ILE B N      1 
ATOM   6616  C  CA     . ILE B 1 235 ? 19.15000  -30.39200 -2.16200  1.000 123.82000 ? 226 ILE B CA     1 
ATOM   6617  C  C      . ILE B 1 235 ? 18.17500  -30.53100 -1.00500  1.000 120.22000 ? 226 ILE B C      1 
ATOM   6618  O  O      . ILE B 1 235 ? 16.97900  -30.22400 -1.12500  1.000 114.89000 ? 226 ILE B O      1 
ATOM   6619  C  CB     . ILE B 1 235 ? 19.45600  -31.75200 -2.81600  1.000 113.80000 ? 226 ILE B CB     1 
ATOM   6620  C  CG1    . ILE B 1 235 ? 20.70400  -31.64900 -3.69900  1.000 111.48000 ? 226 ILE B CG1    1 
ATOM   6621  C  CG2    . ILE B 1 235 ? 18.27300  -32.23200 -3.63300  1.000 130.50000 ? 226 ILE B CG2    1 
ATOM   6622  C  CD1    . ILE B 1 235 ? 21.16300  -32.97200 -4.28100  1.000 123.02000 ? 226 ILE B CD1    1 
ATOM   6623  N  N      . ALA B 1 236 ? 18.68400  -30.96700 0.14700   1.000 118.73000 ? 227 ALA B N      1 
ATOM   6624  C  CA     . ALA B 1 236 ? 17.84100  -31.07200 1.33000   1.000 113.92000 ? 227 ALA B CA     1 
ATOM   6625  C  C      . ALA B 1 236 ? 17.26100  -29.71400 1.71200   1.000 117.36000 ? 227 ALA B C      1 
ATOM   6626  O  O      . ALA B 1 236 ? 16.14500  -29.63600 2.22600   1.000 118.26000 ? 227 ALA B O      1 
ATOM   6627  C  CB     . ALA B 1 236 ? 18.63300  -31.67300 2.48600   1.000 107.46000 ? 227 ALA B CB     1 
ATOM   6628  N  N      . ASP B 1 237 ? 18.03300  -28.64000 1.52200   1.000 118.91000 ? 228 ASP B N      1 
ATOM   6629  C  CA     . ASP B 1 237 ? 17.57900  -27.29100 1.85000   1.000 130.57000 ? 228 ASP B CA     1 
ATOM   6630  C  C      . ASP B 1 237 ? 16.44700  -26.84400 0.93700   1.000 130.86000 ? 228 ASP B C      1 
ATOM   6631  O  O      . ASP B 1 237 ? 15.48600  -26.21400 1.39300   1.000 134.25000 ? 228 ASP B O      1 
ATOM   6632  C  CB     . ASP B 1 237 ? 18.76000  -26.31800 1.76200   1.000 126.64000 ? 228 ASP B CB     1 
ATOM   6633  C  CG     . ASP B 1 237 ? 18.45300  -24.95100 2.35300   1.000 116.51000 ? 228 ASP B CG     1 
ATOM   6634  O  OD1    . ASP B 1 237 ? 17.44300  -24.82100 3.07300   1.000 131.06000 ? 228 ASP B OD1    1 
ATOM   6635  O  OD2    . ASP B 1 237 ? 19.23500  -24.00500 2.10500   1.000 90.31000  ? 228 ASP B OD2    1 
ATOM   6636  N  N      . ASN B 1 238 ? 16.55300  -27.13300 -0.36000  1.000 112.44000 ? 229 ASN B N      1 
ATOM   6637  C  CA     . ASN B 1 238 ? 15.42300  -26.84300 -1.24000  1.000 108.33000 ? 229 ASN B CA     1 
ATOM   6638  C  C      . ASN B 1 238 ? 14.19000  -27.62000 -0.78700  1.000 109.72000 ? 229 ASN B C      1 
ATOM   6639  O  O      . ASN B 1 238 ? 13.07600  -27.06600 -0.68500  1.000 117.58000 ? 229 ASN B O      1 
ATOM   6640  C  CB     . ASN B 1 238 ? 15.78300  -27.18100 -2.68800  1.000 114.00000 ? 229 ASN B CB     1 
ATOM   6641  C  CG     . ASN B 1 238 ? 17.09700  -26.54400 -3.12500  1.000 120.85000 ? 229 ASN B CG     1 
ATOM   6642  O  OD1    . ASN B 1 238 ? 17.45500  -25.45800 -2.66900  1.000 124.02000 ? 229 ASN B OD1    1 
ATOM   6643  N  ND2    . ASN B 1 238 ? 17.83300  -27.23200 -3.99500  1.000 109.23000 ? 229 ASN B ND2    1 
ATOM   6644  N  N      . VAL B 1 239 ? 14.39900  -28.88500 -0.41000  1.000 105.29000 ? 230 VAL B N      1 
ATOM   6645  C  CA     . VAL B 1 239 ? 13.29100  -29.70500 0.06600   1.000 105.92000 ? 230 VAL B CA     1 
ATOM   6646  C  C      . VAL B 1 239 ? 12.70900  -29.10800 1.33800   1.000 101.32000 ? 230 VAL B C      1 
ATOM   6647  O  O      . VAL B 1 239 ? 11.49600  -29.14300 1.55800   1.000 96.11000  ? 230 VAL B O      1 
ATOM   6648  C  CB     . VAL B 1 239 ? 13.74800  -31.15900 0.28200   1.000 106.13000 ? 230 VAL B CB     1 
ATOM   6649  C  CG1    . VAL B 1 239 ? 12.63600  -31.96000 0.93300   1.000 114.54000 ? 230 VAL B CG1    1 
ATOM   6650  C  CG2    . VAL B 1 239 ? 14.15700  -31.78700 -1.03800  1.000 127.59000 ? 230 VAL B CG2    1 
ATOM   6651  N  N      . GLY B 1 240 ? 13.56700  -28.57400 2.20500   1.000 102.95000 ? 231 GLY B N      1 
ATOM   6652  C  CA     . GLY B 1 240 ? 13.09100  -27.99100 3.44600   1.000 110.20000 ? 231 GLY B CA     1 
ATOM   6653  C  C      . GLY B 1 240 ? 12.31000  -26.71200 3.22400   1.000 113.25000 ? 231 GLY B C      1 
ATOM   6654  O  O      . GLY B 1 240 ? 11.32400  -26.45300 3.91500   1.000 110.63000 ? 231 GLY B O      1 
ATOM   6655  N  N      . ASP B 1 241 ? 12.74400  -25.88400 2.27000   1.000 121.10000 ? 232 ASP B N      1 
ATOM   6656  C  CA     . ASP B 1 241 ? 11.95500  -24.70100 1.94100   1.000 120.96000 ? 232 ASP B CA     1 
ATOM   6657  C  C      . ASP B 1 241 ? 10.54500  -25.10700 1.54700   1.000 116.12000 ? 232 ASP B C      1 
ATOM   6658  O  O      . ASP B 1 241 ? 9.56000   -24.52500 2.03000   1.000 116.03000 ? 232 ASP B O      1 
ATOM   6659  C  CB     . ASP B 1 241 ? 12.61200  -23.89600 0.81500   1.000 121.26000 ? 232 ASP B CB     1 
ATOM   6660  C  CG     . ASP B 1 241 ? 14.07100  -23.59000 1.08700   1.000 125.37000 ? 232 ASP B CG     1 
ATOM   6661  O  OD1    . ASP B 1 241 ? 14.45200  -23.55100 2.27500   1.000 134.30000 ? 232 ASP B OD1    1 
ATOM   6662  O  OD2    . ASP B 1 241 ? 14.83600  -23.39900 0.11500   1.000 117.42000 ? 232 ASP B OD2    1 
ATOM   6663  N  N      . ASN B 1 242 ? 10.42400  -26.15800 0.72600   1.000 117.62000 ? 233 ASN B N      1 
ATOM   6664  C  CA     . ASN B 1 242 ? 9.08100   -26.62400 0.37800   1.000 116.92000 ? 233 ASN B CA     1 
ATOM   6665  C  C      . ASN B 1 242 ? 8.35200   -27.21900 1.58100   1.000 111.74000 ? 233 ASN B C      1 
ATOM   6666  O  O      . ASN B 1 242 ? 7.15500   -26.97600 1.76700   1.000 112.93000 ? 233 ASN B O      1 
ATOM   6667  C  CB     . ASN B 1 242 ? 9.13500   -27.64000 -0.76000  1.000 122.81000 ? 233 ASN B CB     1 
ATOM   6668  C  CG     . ASN B 1 242 ? 9.52700   -27.01300 -2.07900  1.000 141.98000 ? 233 ASN B CG     1 
ATOM   6669  O  OD1    . ASN B 1 242 ? 9.55300   -25.78800 -2.21300  1.000 137.23000 ? 233 ASN B OD1    1 
ATOM   6670  N  ND2    . ASN B 1 242 ? 9.82200   -27.84900 -3.06800  1.000 158.32000 ? 233 ASN B ND2    1 
ATOM   6671  N  N      . VAL B 1 243 ? 9.05100   -28.00200 2.40500   1.000 102.22000 ? 234 VAL B N      1 
ATOM   6672  C  CA     . VAL B 1 243 ? 8.41800   -28.63400 3.56000   1.000 100.53000 ? 234 VAL B CA     1 
ATOM   6673  C  C      . VAL B 1 243 ? 7.89400   -27.58700 4.53000   1.000 87.94000  ? 234 VAL B C      1 
ATOM   6674  O  O      . VAL B 1 243 ? 6.87900   -27.79800 5.20600   1.000 80.96000  ? 234 VAL B O      1 
ATOM   6675  C  CB     . VAL B 1 243 ? 9.41500   -29.58400 4.25100   1.000 96.83000  ? 234 VAL B CB     1 
ATOM   6676  C  CG1    . VAL B 1 243 ? 8.86500   -30.05100 5.58600   1.000 94.28000  ? 234 VAL B CG1    1 
ATOM   6677  C  CG2    . VAL B 1 243 ? 9.72900   -30.76900 3.35300   1.000 83.42000  ? 234 VAL B CG2    1 
ATOM   6678  N  N      . GLY B 1 244 ? 8.57500   -26.45200 4.61700   1.000 90.94000  ? 235 GLY B N      1 
ATOM   6679  C  CA     . GLY B 1 244 ? 8.26000   -25.43900 5.59600   1.000 93.89000  ? 235 GLY B CA     1 
ATOM   6680  C  C      . GLY B 1 244 ? 7.20200   -24.46700 5.12500   1.000 102.35000 ? 235 GLY B C      1 
ATOM   6681  O  O      . GLY B 1 244 ? 6.14000   -24.36500 5.74700   1.000 102.14000 ? 235 GLY B O      1 
ATOM   6682  N  N      . ASP B 1 245 ? 7.45800   -23.75500 4.02500   1.000 107.89000 ? 236 ASP B N      1 
ATOM   6683  C  CA     . ASP B 1 245 ? 6.54200   -22.68900 3.63200   1.000 101.68000 ? 236 ASP B CA     1 
ATOM   6684  C  C      . ASP B 1 245 ? 5.39500   -23.15700 2.74200   1.000 103.42000 ? 236 ASP B C      1 
ATOM   6685  O  O      . ASP B 1 245 ? 4.44200   -22.39600 2.54300   1.000 106.49000 ? 236 ASP B O      1 
ATOM   6686  C  CB     . ASP B 1 245 ? 7.30800   -21.55900 2.93800   1.000 103.12000 ? 236 ASP B CB     1 
ATOM   6687  C  CG     . ASP B 1 245 ? 8.01100   -20.65200 3.92600   1.000 117.71000 ? 236 ASP B CG     1 
ATOM   6688  O  OD1    . ASP B 1 245 ? 7.79300   -20.82900 5.14300   1.000 121.85000 ? 236 ASP B OD1    1 
ATOM   6689  O  OD2    . ASP B 1 245 ? 8.78300   -19.77000 3.49300   1.000 133.58000 ? 236 ASP B OD2    1 
ATOM   6690  N  N      . VAL B 1 246 ? 5.45300   -24.37700 2.20900   1.000 106.31000 ? 237 VAL B N      1 
ATOM   6691  C  CA     . VAL B 1 246 ? 4.35800   -24.91800 1.41000   1.000 103.35000 ? 237 VAL B CA     1 
ATOM   6692  C  C      . VAL B 1 246 ? 3.52100   -25.88200 2.24100   1.000 95.44000  ? 237 VAL B C      1 
ATOM   6693  O  O      . VAL B 1 246 ? 2.32100   -25.66600 2.44700   1.000 99.89000  ? 237 VAL B O      1 
ATOM   6694  C  CB     . VAL B 1 246 ? 4.89000   -25.60800 0.14000   1.000 119.22000 ? 237 VAL B CB     1 
ATOM   6695  C  CG1    . VAL B 1 246 ? 3.76600   -26.33200 -0.58200  1.000 126.43000 ? 237 VAL B CG1    1 
ATOM   6696  C  CG2    . VAL B 1 246 ? 5.53600   -24.58800 -0.78000  1.000 121.70000 ? 237 VAL B CG2    1 
ATOM   6697  N  N      . ALA B 1 247 ? 4.15100   -26.95200 2.73000   1.000 86.03000  ? 238 ALA B N      1 
ATOM   6698  C  CA     . ALA B 1 247 ? 3.42500   -27.95800 3.49800   1.000 68.05000  ? 238 ALA B CA     1 
ATOM   6699  C  C      . ALA B 1 247 ? 3.20200   -27.50000 4.93300   1.000 91.22000  ? 238 ALA B C      1 
ATOM   6700  O  O      . ALA B 1 247 ? 2.06300   -27.46900 5.41300   1.000 100.95000 ? 238 ALA B O      1 
ATOM   6701  C  CB     . ALA B 1 247 ? 4.17700   -29.28900 3.46600   1.000 67.10000  ? 238 ALA B CB     1 
ATOM   6702  N  N      . GLY B 1 248 ? 4.27800   -27.13700 5.63200   1.000 94.43000  ? 239 GLY B N      1 
ATOM   6703  C  CA     . GLY B 1 248 ? 4.14200   -26.76100 7.02900   1.000 85.30000  ? 239 GLY B CA     1 
ATOM   6704  C  C      . GLY B 1 248 ? 3.25800   -25.54400 7.21200   1.000 79.80000  ? 239 GLY B C      1 
ATOM   6705  O  O      . GLY B 1 248 ? 2.31100   -25.55900 8.00200   1.000 85.06000  ? 239 GLY B O      1 
ATOM   6706  N  N      . LEU B 1 249 ? 3.55100   -24.47100 6.47400   1.000 72.43000  ? 240 LEU B N      1 
ATOM   6707  C  CA     . LEU B 1 249 ? 2.77900   -23.24300 6.62400   1.000 77.00000  ? 240 LEU B CA     1 
ATOM   6708  C  C      . LEU B 1 249 ? 1.32700   -23.45000 6.21300   1.000 76.37000  ? 240 LEU B C      1 
ATOM   6709  O  O      . LEU B 1 249 ? 0.41300   -22.88600 6.83000   1.000 87.76000  ? 240 LEU B O      1 
ATOM   6710  C  CB     . LEU B 1 249 ? 3.41400   -22.12300 5.80200   1.000 87.66000  ? 240 LEU B CB     1 
ATOM   6711  C  CG     . LEU B 1 249 ? 2.63300   -20.81000 5.77800   1.000 87.58000  ? 240 LEU B CG     1 
ATOM   6712  C  CD1    . LEU B 1 249 ? 2.34800   -20.33900 7.19500   1.000 91.94000  ? 240 LEU B CD1    1 
ATOM   6713  C  CD2    . LEU B 1 249 ? 3.40300   -19.75300 5.00600   1.000 116.92000 ? 240 LEU B CD2    1 
ATOM   6714  N  N      . GLY B 1 250 ? 1.09300   -24.24100 5.16400   1.000 72.68000  ? 241 GLY B N      1 
ATOM   6715  C  CA     . GLY B 1 250 ? -0.27500  -24.54400 4.77900   1.000 62.81000  ? 241 GLY B CA     1 
ATOM   6716  C  C      . GLY B 1 250 ? -1.03100  -25.25400 5.88300   1.000 60.32000  ? 241 GLY B C      1 
ATOM   6717  O  O      . GLY B 1 250 ? -2.17300  -24.90900 6.19600   1.000 60.14000  ? 241 GLY B O      1 
ATOM   6718  N  N      . ALA B 1 251 ? -0.39100  -26.24900 6.50400   1.000 70.74000  ? 242 ALA B N      1 
ATOM   6719  C  CA     . ALA B 1 251 ? -1.02500  -26.95100 7.61500   1.000 85.15000  ? 242 ALA B CA     1 
ATOM   6720  C  C      . ALA B 1 251 ? -1.26100  -26.02100 8.79900   1.000 77.62000  ? 242 ALA B C      1 
ATOM   6721  O  O      . ALA B 1 251 ? -2.27200  -26.13900 9.49700   1.000 70.04000  ? 242 ALA B O      1 
ATOM   6722  C  CB     . ALA B 1 251 ? -0.17100  -28.14900 8.03600   1.000 93.61000  ? 242 ALA B CB     1 
ATOM   6723  N  N      . ASP B 1 252 ? -0.34300  -25.08100 9.03700   1.000 71.94000  ? 243 ASP B N      1 
ATOM   6724  C  CA     . ASP B 1 252 ? -0.50000  -24.14700 10.14900  1.000 78.65000  ? 243 ASP B CA     1 
ATOM   6725  C  C      . ASP B 1 252 ? -1.69200  -23.22100 9.92400   1.000 70.61000  ? 243 ASP B C      1 
ATOM   6726  O  O      . ASP B 1 252 ? -2.50500  -22.99700 10.83200  1.000 77.21000  ? 243 ASP B O      1 
ATOM   6727  C  CB     . ASP B 1 252 ? 0.79300   -23.35000 10.34100  1.000 79.30000  ? 243 ASP B CB     1 
ATOM   6728  C  CG     . ASP B 1 252 ? 0.72000   -22.37200 11.50100  1.000 85.11000  ? 243 ASP B CG     1 
ATOM   6729  O  OD1    . ASP B 1 252 ? -0.23800  -22.45600 12.29900  1.000 103.35000 ? 243 ASP B OD1    1 
ATOM   6730  O  OD2    . ASP B 1 252 ? 1.63400   -21.52800 11.62000  1.000 85.43000  ? 243 ASP B OD2    1 
ATOM   6731  N  N      . LEU B 1 253 ? -1.80800  -22.66300 8.71800   1.000 51.78000  ? 244 LEU B N      1 
ATOM   6732  C  CA     . LEU B 1 253 ? -2.96600  -21.83100 8.41100   1.000 45.49000  ? 244 LEU B CA     1 
ATOM   6733  C  C      . LEU B 1 253 ? -4.25300  -22.64200 8.48300   1.000 61.49000  ? 244 LEU B C      1 
ATOM   6734  O  O      . LEU B 1 253 ? -5.27600  -22.15800 8.98500   1.000 55.42000  ? 244 LEU B O      1 
ATOM   6735  C  CB     . LEU B 1 253 ? -2.81100  -21.18900 7.03500   1.000 39.33000  ? 244 LEU B CB     1 
ATOM   6736  C  CG     . LEU B 1 253 ? -1.82900  -20.02100 6.98700   1.000 53.63000  ? 244 LEU B CG     1 
ATOM   6737  C  CD1    . LEU B 1 253 ? -1.41300  -19.73700 5.55700   1.000 93.11000  ? 244 LEU B CD1    1 
ATOM   6738  C  CD2    . LEU B 1 253 ? -2.44800  -18.78800 7.62300   1.000 73.68000  ? 244 LEU B CD2    1 
ATOM   6739  N  N      . LEU B 1 254 ? -4.22200  -23.88100 7.98600   1.000 72.47000  ? 245 LEU B N      1 
ATOM   6740  C  CA     . LEU B 1 254 ? -5.38300  -24.75300 8.10600   1.000 67.10000  ? 245 LEU B CA     1 
ATOM   6741  C  C      . LEU B 1 254 ? -5.77300  -24.92800 9.56500   1.000 66.57000  ? 245 LEU B C      1 
ATOM   6742  O  O      . LEU B 1 254 ? -6.95400  -24.85100 9.91900   1.000 78.27000  ? 245 LEU B O      1 
ATOM   6743  C  CB     . LEU B 1 254 ? -5.08800  -26.10900 7.46200   1.000 68.88000  ? 245 LEU B CB     1 
ATOM   6744  C  CG     . LEU B 1 254 ? -6.27400  -27.04600 7.21700   1.000 66.09000  ? 245 LEU B CG     1 
ATOM   6745  C  CD1    . LEU B 1 254 ? -5.93400  -28.06100 6.13500   1.000 78.80000  ? 245 LEU B CD1    1 
ATOM   6746  C  CD2    . LEU B 1 254 ? -6.69200  -27.75300 8.50000   1.000 54.34000  ? 245 LEU B CD2    1 
ATOM   6747  N  N      . GLU B 1 255 ? -4.78500  -25.16900 10.42900  1.000 61.56000  ? 246 GLU B N      1 
ATOM   6748  C  CA     . GLU B 1 255 ? -5.07800  -25.36100 11.84300  1.000 64.40000  ? 246 GLU B CA     1 
ATOM   6749  C  C      . GLU B 1 255 ? -5.69600  -24.11400 12.44800  1.000 61.96000  ? 246 GLU B C      1 
ATOM   6750  O  O      . GLU B 1 255 ? -6.68300  -24.19900 13.18000  1.000 57.16000  ? 246 GLU B O      1 
ATOM   6751  C  CB     . GLU B 1 255 ? -3.81200  -25.73700 12.61100  1.000 73.06000  ? 246 GLU B CB     1 
ATOM   6752  C  CG     . GLU B 1 255 ? -4.08800  -26.10200 14.06600  1.000 75.88000  ? 246 GLU B CG     1 
ATOM   6753  C  CD     . GLU B 1 255 ? -2.90000  -25.86100 14.97500  1.000 84.13000  ? 246 GLU B CD     1 
ATOM   6754  O  OE1    . GLU B 1 255 ? -1.91500  -25.24000 14.52200  1.000 92.30000  ? 246 GLU B OE1    1 
ATOM   6755  O  OE2    . GLU B 1 255 ? -2.95300  -26.29600 16.14600  1.000 86.93000  ? 246 GLU B OE2    1 
ATOM   6756  N  N      . SER B 1 256 ? -5.13300  -22.94300 12.14800  1.000 59.79000  ? 247 SER B N      1 
ATOM   6757  C  CA     . SER B 1 256 ? -5.66900  -21.71200 12.72200  1.000 66.16000  ? 247 SER B CA     1 
ATOM   6758  C  C      . SER B 1 256 ? -7.10100  -21.46700 12.26300  1.000 64.70000  ? 247 SER B C      1 
ATOM   6759  O  O      . SER B 1 256 ? -7.97200  -21.10700 13.06600  1.000 63.02000  ? 247 SER B O      1 
ATOM   6760  C  CB     . SER B 1 256 ? -4.77400  -20.53100 12.35000  1.000 73.69000  ? 247 SER B CB     1 
ATOM   6761  O  OG     . SER B 1 256 ? -3.43400  -20.76800 12.74700  1.000 79.70000  ? 247 SER B OG     1 
ATOM   6762  N  N      . PHE B 1 257 ? -7.36200  -21.66800 10.97300  1.000 65.59000  ? 248 PHE B N      1 
ATOM   6763  C  CA     . PHE B 1 257 ? -8.69600  -21.45000 10.42500  1.000 61.30000  ? 248 PHE B CA     1 
ATOM   6764  C  C      . PHE B 1 257 ? -9.70700  -22.42600 11.02800  1.000 53.34000  ? 248 PHE B C      1 
ATOM   6765  O  O      . PHE B 1 257 ? -10.77600 -22.02100 11.51900  1.000 52.11000  ? 248 PHE B O      1 
ATOM   6766  C  CB     . PHE B 1 257 ? -8.60200  -21.56900 8.90200   1.000 74.24000  ? 248 PHE B CB     1 
ATOM   6767  C  CG     . PHE B 1 257 ? -9.85400  -22.02900 8.22800   1.000 96.51000  ? 248 PHE B CG     1 
ATOM   6768  C  CD1    . PHE B 1 257 ? -10.86900 -21.13600 7.93600   1.000 116.41000 ? 248 PHE B CD1    1 
ATOM   6769  C  CD2    . PHE B 1 257 ? -9.99600  -23.35100 7.84100   1.000 102.00000 ? 248 PHE B CD2    1 
ATOM   6770  C  CE1    . PHE B 1 257 ? -12.01100 -21.55600 7.29100   1.000 112.56000 ? 248 PHE B CE1    1 
ATOM   6771  C  CE2    . PHE B 1 257 ? -11.13700 -23.77900 7.19900   1.000 113.12000 ? 248 PHE B CE2    1 
ATOM   6772  C  CZ     . PHE B 1 257 ? -12.14700 -22.88100 6.92300   1.000 125.85000 ? 248 PHE B CZ     1 
ATOM   6773  N  N      . VAL B 1 258 ? -9.37200  -23.71800 11.02000  1.000 53.70000  ? 249 VAL B N      1 
ATOM   6774  C  CA     . VAL B 1 258 ? -10.23400 -24.72000 11.63500  1.000 50.76000  ? 249 VAL B CA     1 
ATOM   6775  C  C      . VAL B 1 258 ? -10.45900 -24.40000 13.10500  1.000 54.44000  ? 249 VAL B C      1 
ATOM   6776  O  O      . VAL B 1 258 ? -11.56200 -24.57900 13.62800  1.000 49.24000  ? 249 VAL B O      1 
ATOM   6777  C  CB     . VAL B 1 258 ? -9.63800  -26.12800 11.44800  1.000 57.17000  ? 249 VAL B CB     1 
ATOM   6778  C  CG1    . VAL B 1 258 ? -10.49500 -27.16700 12.16200  1.000 49.64000  ? 249 VAL B CG1    1 
ATOM   6779  C  CG2    . VAL B 1 258 ? -9.49900  -26.45700 9.96900   1.000 67.38000  ? 249 VAL B CG2    1 
ATOM   6780  N  N      . GLY B 1 259 ? -9.41400  -23.94300 13.80100  1.000 52.94000  ? 250 GLY B N      1 
ATOM   6781  C  CA     . GLY B 1 259 ? -9.55500  -23.61600 15.20800  1.000 47.91000  ? 250 GLY B CA     1 
ATOM   6782  C  C      . GLY B 1 259 ? -10.50300 -22.46000 15.44700  1.000 49.69000  ? 250 GLY B C      1 
ATOM   6783  O  O      . GLY B 1 259 ? -11.30600 -22.49100 16.37900  1.000 61.10000  ? 250 GLY B O      1 
ATOM   6784  N  N      . ALA B 1 260 ? -10.42500 -21.42400 14.61100  1.000 42.35000  ? 251 ALA B N      1 
ATOM   6785  C  CA     . ALA B 1 260 ? -11.37900 -20.32500 14.72700  1.000 45.42000  ? 251 ALA B CA     1 
ATOM   6786  C  C      . ALA B 1 260 ? -12.80500 -20.82800 14.54900  1.000 38.68000  ? 251 ALA B C      1 
ATOM   6787  O  O      . ALA B 1 260 ? -13.69800 -20.51700 15.35200  1.000 46.04000  ? 251 ALA B O      1 
ATOM   6788  C  CB     . ALA B 1 260 ? -11.06100 -19.23500 13.70200  1.000 65.42000  ? 251 ALA B CB     1 
ATOM   6789  N  N      . ILE B 1 261 ? -13.03700 -21.62000 13.50000  1.000 39.47000  ? 252 ILE B N      1 
ATOM   6790  C  CA     . ILE B 1 261 ? -14.38800 -22.12800 13.26400  1.000 54.70000  ? 252 ILE B CA     1 
ATOM   6791  C  C      . ILE B 1 261 ? -14.85500 -22.99700 14.42700  1.000 48.79000  ? 252 ILE B C      1 
ATOM   6792  O  O      . ILE B 1 261 ? -15.99400 -22.87500 14.89900  1.000 58.58000  ? 252 ILE B O      1 
ATOM   6793  C  CB     . ILE B 1 261 ? -14.45900 -22.88400 11.92700  1.000 43.38000  ? 252 ILE B CB     1 
ATOM   6794  C  CG1    . ILE B 1 261 ? -14.15000 -21.93200 10.77100  1.000 54.05000  ? 252 ILE B CG1    1 
ATOM   6795  C  CG2    . ILE B 1 261 ? -15.81800 -23.54800 11.76500  1.000 37.57000  ? 252 ILE B CG2    1 
ATOM   6796  C  CD1    . ILE B 1 261 ? -14.02900 -22.62200 9.45100   1.000 57.14000  ? 252 ILE B CD1    1 
ATOM   6797  N  N      . VAL B 1 262 ? -13.98800 -23.88900 14.90400  1.000 42.58000  ? 253 VAL B N      1 
ATOM   6798  C  CA     . VAL B 1 262 ? -14.37300 -24.79200 15.97900  1.000 46.56000  ? 253 VAL B CA     1 
ATOM   6799  C  C      . VAL B 1 262 ? -14.63300 -24.01600 17.25700  1.000 44.09000  ? 253 VAL B C      1 
ATOM   6800  O  O      . VAL B 1 262 ? -15.50900 -24.38400 18.04300  1.000 47.65000  ? 253 VAL B O      1 
ATOM   6801  C  CB     . VAL B 1 262 ? -13.29100 -25.86800 16.18500  1.000 66.14000  ? 253 VAL B CB     1 
ATOM   6802  C  CG1    . VAL B 1 262 ? -13.52700 -26.61200 17.48700  1.000 58.42000  ? 253 VAL B CG1    1 
ATOM   6803  C  CG2    . VAL B 1 262 ? -13.26900 -26.83200 15.00800  1.000 70.33000  ? 253 VAL B CG2    1 
ATOM   6804  N  N      . SER B 1 263 ? -13.88700 -22.93600 17.49100  1.000 41.55000  ? 254 SER B N      1 
ATOM   6805  C  CA     . SER B 1 263 ? -14.14400 -22.10200 18.65800  1.000 45.67000  ? 254 SER B CA     1 
ATOM   6806  C  C      . SER B 1 263 ? -15.50600 -21.43400 18.55800  1.000 50.54000  ? 254 SER B C      1 
ATOM   6807  O  O      . SER B 1 263 ? -16.25800 -21.39400 19.53900  1.000 56.23000  ? 254 SER B O      1 
ATOM   6808  C  CB     . SER B 1 263 ? -13.03900 -21.05800 18.80900  1.000 50.53000  ? 254 SER B CB     1 
ATOM   6809  O  OG     . SER B 1 263 ? -13.31600 -20.18500 19.88900  1.000 58.63000  ? 254 SER B OG     1 
ATOM   6810  N  N      . SER B 1 264 ? -15.83900 -20.89900 17.38200  1.000 48.74000  ? 255 SER B N      1 
ATOM   6811  C  CA     . SER B 1 264 ? -17.16900 -20.32900 17.18500  1.000 47.64000  ? 255 SER B CA     1 
ATOM   6812  C  C      . SER B 1 264 ? -18.25400 -21.36500 17.47300  1.000 48.20000  ? 255 SER B C      1 
ATOM   6813  O  O      . SER B 1 264 ? -19.24200 -21.08200 18.16800  1.000 46.78000  ? 255 SER B O      1 
ATOM   6814  C  CB     . SER B 1 264 ? -17.29200 -19.79100 15.76000  1.000 61.65000  ? 255 SER B CB     1 
ATOM   6815  O  OG     . SER B 1 264 ? -16.34300 -18.76300 15.53000  1.000 67.10000  ? 255 SER B OG     1 
ATOM   6816  N  N      . ILE B 1 265 ? -18.07700 -22.58000 16.95000  1.000 52.81000  ? 256 ILE B N      1 
ATOM   6817  C  CA     . ILE B 1 265 ? -19.08900 -23.62100 17.11800  1.000 52.84000  ? 256 ILE B CA     1 
ATOM   6818  C  C      . ILE B 1 265 ? -19.21300 -24.02900 18.58300  1.000 50.85000  ? 256 ILE B C      1 
ATOM   6819  O  O      . ILE B 1 265 ? -20.32300 -24.20300 19.10200  1.000 42.44000  ? 256 ILE B O      1 
ATOM   6820  C  CB     . ILE B 1 265 ? -18.76600 -24.82900 16.22200  1.000 58.10000  ? 256 ILE B CB     1 
ATOM   6821  C  CG1    . ILE B 1 265 ? -19.07900 -24.50900 14.76000  1.000 55.59000  ? 256 ILE B CG1    1 
ATOM   6822  C  CG2    . ILE B 1 265 ? -19.52100 -26.06400 16.69400  1.000 71.28000  ? 256 ILE B CG2    1 
ATOM   6823  C  CD1    . ILE B 1 265 ? -18.66600 -25.60400 13.80400  1.000 69.83000  ? 256 ILE B CD1    1 
ATOM   6824  N  N      . ILE B 1 266 ? -18.08000 -24.21500 19.26300  1.000 46.92000  ? 257 ILE B N      1 
ATOM   6825  C  CA     . ILE B 1 266 ? -18.10100 -24.55900 20.68100  1.000 43.97000  ? 257 ILE B CA     1 
ATOM   6826  C  C      . ILE B 1 266 ? -18.81400 -23.47300 21.47000  1.000 47.70000  ? 257 ILE B C      1 
ATOM   6827  O  O      . ILE B 1 266 ? -19.64700 -23.75400 22.34000  1.000 50.92000  ? 257 ILE B O      1 
ATOM   6828  C  CB     . ILE B 1 266 ? -16.66700 -24.77200 21.20200  1.000 50.67000  ? 257 ILE B CB     1 
ATOM   6829  C  CG1    . ILE B 1 266 ? -16.03200 -26.00700 20.56300  1.000 76.78000  ? 257 ILE B CG1    1 
ATOM   6830  C  CG2    . ILE B 1 266 ? -16.65000 -24.87100 22.72400  1.000 45.42000  ? 257 ILE B CG2    1 
ATOM   6831  C  CD1    . ILE B 1 266 ? -14.56800 -26.17300 20.90900  1.000 53.05000  ? 257 ILE B CD1    1 
ATOM   6832  N  N      . LEU B 1 267 ? -18.49100 -22.21100 21.18100  1.000 38.24000  ? 258 LEU B N      1 
ATOM   6833  C  CA     . LEU B 1 267 ? -19.11500 -21.10600 21.89600  1.000 32.39000  ? 258 LEU B CA     1 
ATOM   6834  C  C      . LEU B 1 267 ? -20.62700 -21.12700 21.72100  1.000 55.67000  ? 258 LEU B C      1 
ATOM   6835  O  O      . LEU B 1 267 ? -21.37100 -20.96200 22.69000  1.000 74.71000  ? 258 LEU B O      1 
ATOM   6836  C  CB     . LEU B 1 267 ? -18.52700 -19.77700 21.42600  1.000 46.83000  ? 258 LEU B CB     1 
ATOM   6837  C  CG     . LEU B 1 267 ? -17.09200 -19.49500 21.87300  1.000 58.29000  ? 258 LEU B CG     1 
ATOM   6838  C  CD1    . LEU B 1 267 ? -16.51200 -18.31800 21.10200  1.000 58.57000  ? 258 LEU B CD1    1 
ATOM   6839  C  CD2    . LEU B 1 267 ? -17.03300 -19.24100 23.37300  1.000 52.58000  ? 258 LEU B CD2    1 
ATOM   6840  N  N      . ALA B 1 268 ? -21.10500 -21.33400 20.49200  1.000 45.38000  ? 259 ALA B N      1 
ATOM   6841  C  CA     . ALA B 1 268 ? -22.55200 -21.39100 20.28800  1.000 41.34000  ? 259 ALA B CA     1 
ATOM   6842  C  C      . ALA B 1 268 ? -23.16600 -22.57000 21.03800  1.000 45.72000  ? 259 ALA B C      1 
ATOM   6843  O  O      . ALA B 1 268 ? -24.15200 -22.42000 21.78000  1.000 51.46000  ? 259 ALA B O      1 
ATOM   6844  C  CB     . ALA B 1 268 ? -22.87200 -21.47700 18.79600  1.000 53.86000  ? 259 ALA B CB     1 
ATOM   6845  N  N      . SER B 1 269 ? -22.58300 -23.75700 20.86200  1.000 45.25000  ? 260 SER B N      1 
ATOM   6846  C  CA     . SER B 1 269 ? -23.13900 -24.95500 21.47500  1.000 60.58000  ? 260 SER B CA     1 
ATOM   6847  C  C      . SER B 1 269 ? -23.22300 -24.81200 22.98800  1.000 63.89000  ? 260 SER B C      1 
ATOM   6848  O  O      . SER B 1 269 ? -24.20500 -25.23900 23.60600  1.000 64.56000  ? 260 SER B O      1 
ATOM   6849  C  CB     . SER B 1 269 ? -22.30200 -26.17100 21.08200  1.000 55.45000  ? 260 SER B CB     1 
ATOM   6850  O  OG     . SER B 1 269 ? -22.17200 -26.25500 19.67300  1.000 36.29000  ? 260 SER B OG     1 
ATOM   6851  N  N      . TYR B 1 270 ? -22.20900 -24.20000 23.60300  1.000 56.81000  ? 261 TYR B N      1 
ATOM   6852  C  CA     . TYR B 1 270 ? -22.21700 -24.04400 25.05000  1.000 59.85000  ? 261 TYR B CA     1 
ATOM   6853  C  C      . TYR B 1 270 ? -22.99200 -22.81600 25.50800  1.000 61.63000  ? 261 TYR B C      1 
ATOM   6854  O  O      . TYR B 1 270 ? -23.37400 -22.75000 26.68000  1.000 69.84000  ? 261 TYR B O      1 
ATOM   6855  C  CB     . TYR B 1 270 ? -20.78500 -23.99100 25.58500  1.000 57.03000  ? 261 TYR B CB     1 
ATOM   6856  C  CG     . TYR B 1 270 ? -20.11800 -25.34800 25.59400  1.000 61.20000  ? 261 TYR B CG     1 
ATOM   6857  C  CD1    . TYR B 1 270 ? -20.55100 -26.34900 26.45200  1.000 66.91000  ? 261 TYR B CD1    1 
ATOM   6858  C  CD2    . TYR B 1 270 ? -19.05800 -25.62800 24.74300  1.000 66.64000  ? 261 TYR B CD2    1 
ATOM   6859  C  CE1    . TYR B 1 270 ? -19.94900 -27.59500 26.46100  1.000 78.94000  ? 261 TYR B CE1    1 
ATOM   6860  C  CE2    . TYR B 1 270 ? -18.45000 -26.86600 24.74500  1.000 82.97000  ? 261 TYR B CE2    1 
ATOM   6861  C  CZ     . TYR B 1 270 ? -18.89700 -27.84700 25.60400  1.000 91.91000  ? 261 TYR B CZ     1 
ATOM   6862  O  OH     . TYR B 1 270 ? -18.28500 -29.08200 25.60100  1.000 98.13000  ? 261 TYR B OH     1 
ATOM   6863  N  N      . MET B 1 271 ? -23.23200 -21.84400 24.62700  1.000 51.93000  ? 262 MET B N      1 
ATOM   6864  C  CA     . MET B 1 271 ? -24.16100 -20.77800 24.96000  1.000 51.78000  ? 262 MET B CA     1 
ATOM   6865  C  C      . MET B 1 271 ? -25.58100 -21.30700 24.97600  1.000 69.70000  ? 262 MET B C      1 
ATOM   6866  O  O      . MET B 1 271 ? -26.46100 -20.69300 25.59000  1.000 78.81000  ? 262 MET B O      1 
ATOM   6867  C  CB     . MET B 1 271 ? -24.02600 -19.61600 23.97100  1.000 34.53000  ? 262 MET B CB     1 
ATOM   6868  N  N      . PHE B 1 272 ? -25.81800 -22.43500 24.30800  1.000 70.18000  ? 263 PHE B N      1 
ATOM   6869  C  CA     . PHE B 1 272 ? -27.11600 -23.09500 24.44900  1.000 73.38000  ? 263 PHE B CA     1 
ATOM   6870  C  C      . PHE B 1 272 ? -27.41900 -23.43700 25.90300  1.000 72.61000  ? 263 PHE B C      1 
ATOM   6871  O  O      . PHE B 1 272 ? -28.48800 -23.04500 26.40400  1.000 76.96000  ? 263 PHE B O      1 
ATOM   6872  C  CB     . PHE B 1 272 ? -27.16600 -24.33400 23.55400  1.000 68.57000  ? 263 PHE B CB     1 
ATOM   6873  N  N      . PRO B 1 273 ? -26.55100 -24.16600 26.63500  1.000 74.00000  ? 264 PRO B N      1 
ATOM   6874  C  CA     . PRO B 1 273 ? -26.88200 -24.53400 28.02000  1.000 66.46000  ? 264 PRO B CA     1 
ATOM   6875  C  C      . PRO B 1 273 ? -26.62300 -23.42600 29.03000  1.000 78.07000  ? 264 PRO B C      1 
ATOM   6876  O  O      . PRO B 1 273 ? -27.29000 -23.36700 30.06800  1.000 81.68000  ? 264 PRO B O      1 
ATOM   6877  C  CB     . PRO B 1 273 ? -25.96700 -25.73900 28.29400  1.000 52.80000  ? 264 PRO B CB     1 
ATOM   6878  C  CG     . PRO B 1 273 ? -25.41100 -26.14600 26.95800  1.000 58.88000  ? 264 PRO B CG     1 
ATOM   6879  C  CD     . PRO B 1 273 ? -25.36300 -24.88900 26.15600  1.000 74.39000  ? 264 PRO B CD     1 
ATOM   6880  N  N      . ILE B 1 274 ? -25.66200 -22.54400 28.74200  1.000 88.33000  ? 265 ILE B N      1 
ATOM   6881  C  CA     . ILE B 1 274 ? -25.29100 -21.52900 29.72500  1.000 89.42000  ? 265 ILE B CA     1 
ATOM   6882  C  C      . ILE B 1 274 ? -26.39000 -20.48600 29.86700  1.000 87.98000  ? 265 ILE B C      1 
ATOM   6883  O  O      . ILE B 1 274 ? -26.60300 -19.94500 30.95900  1.000 94.03000  ? 265 ILE B O      1 
ATOM   6884  C  CB     . ILE B 1 274 ? -23.94200 -20.87700 29.36000  1.000 86.46000  ? 265 ILE B CB     1 
ATOM   6885  C  CG1    . ILE B 1 274 ? -24.04100 -20.14100 28.02200  1.000 91.89000  ? 265 ILE B CG1    1 
ATOM   6886  C  CG2    . ILE B 1 274 ? -22.81900 -21.91200 29.34300  1.000 84.21000  ? 265 ILE B CG2    1 
ATOM   6887  C  CD1    . ILE B 1 274 ? -22.84200 -19.27100 27.71700  1.000 86.75000  ? 265 ILE B CD1    1 
ATOM   6888  N  N      . TYR B 1 275 ? -27.10900 -20.18800 28.78400  1.000 82.39000  ? 266 TYR B N      1 
ATOM   6889  C  CA     . TYR B 1 275 ? -28.18300 -19.19900 28.82200  1.000 74.64000  ? 266 TYR B CA     1 
ATOM   6890  C  C      . TYR B 1 275 ? -29.50800 -19.94000 28.97700  1.000 75.87000  ? 266 TYR B C      1 
ATOM   6891  O  O      . TYR B 1 275 ? -30.26100 -20.14900 28.02600  1.000 86.15000  ? 266 TYR B O      1 
ATOM   6892  C  CB     . TYR B 1 275 ? -28.15100 -18.32500 27.57500  1.000 80.71000  ? 266 TYR B CB     1 
ATOM   6893  C  CG     . TYR B 1 275 ? -26.93400 -17.43500 27.51000  1.000 69.78000  ? 266 TYR B CG     1 
ATOM   6894  C  CD1    . TYR B 1 275 ? -26.59100 -16.62000 28.58000  1.000 78.95000  ? 266 TYR B CD1    1 
ATOM   6895  C  CD2    . TYR B 1 275 ? -26.12200 -17.41900 26.38700  1.000 69.09000  ? 266 TYR B CD2    1 
ATOM   6896  C  CE1    . TYR B 1 275 ? -25.47500 -15.80900 28.52900  1.000 85.93000  ? 266 TYR B CE1    1 
ATOM   6897  C  CE2    . TYR B 1 275 ? -25.00400 -16.61200 26.32600  1.000 75.86000  ? 266 TYR B CE2    1 
ATOM   6898  C  CZ     . TYR B 1 275 ? -24.68600 -15.80900 27.39900  1.000 76.14000  ? 266 TYR B CZ     1 
ATOM   6899  O  OH     . TYR B 1 275 ? -23.57400 -15.00200 27.34100  1.000 82.28000  ? 266 TYR B OH     1 
ATOM   6900  N  N      . VAL B 1 276 ? -29.77800 -20.34700 30.21700  1.000 82.45000  ? 267 VAL B N      1 
ATOM   6901  C  CA     . VAL B 1 276 ? -31.02600 -20.99200 30.60100  1.000 96.69000  ? 267 VAL B CA     1 
ATOM   6902  C  C      . VAL B 1 276 ? -31.46700 -20.39500 31.92900  1.000 91.52000  ? 267 VAL B C      1 
ATOM   6903  O  O      . VAL B 1 276 ? -30.65600 -19.87700 32.69900  1.000 97.60000  ? 267 VAL B O      1 
ATOM   6904  C  CB     . VAL B 1 276 ? -30.89500 -22.52800 30.71500  1.000 96.13000  ? 267 VAL B CB     1 
ATOM   6905  C  CG1    . VAL B 1 276 ? -30.59800 -23.14200 29.35400  1.000 89.20000  ? 267 VAL B CG1    1 
ATOM   6906  C  CG2    . VAL B 1 276 ? -29.81400 -22.89400 31.71700  1.000 102.35000 ? 267 VAL B CG2    1 
ATOM   6907  N  N      . GLN B 1 277 ? -32.77000 -20.46700 32.19500  1.000 93.52000  ? 268 GLN B N      1 
ATOM   6908  C  CA     . GLN B 1 277 ? -33.31900 -19.89200 33.41900  1.000 107.35000 ? 268 GLN B CA     1 
ATOM   6909  C  C      . GLN B 1 277 ? -34.37900 -20.82700 33.97800  1.000 115.12000 ? 268 GLN B C      1 
ATOM   6910  O  O      . GLN B 1 277 ? -35.37800 -21.11300 33.31100  1.000 110.31000 ? 268 GLN B O      1 
ATOM   6911  C  CB     . GLN B 1 277 ? -33.91100 -18.50600 33.14700  1.000 101.18000 ? 268 GLN B CB     1 
ATOM   6912  C  CG     . GLN B 1 277 ? -34.46800 -17.80600 34.37100  1.000 100.12000 ? 268 GLN B CG     1 
ATOM   6913  C  CD     . GLN B 1 277 ? -35.01200 -16.42800 34.04700  1.000 120.61000 ? 268 GLN B CD     1 
ATOM   6914  O  OE1    . GLN B 1 277 ? -34.87000 -15.94100 32.92400  1.000 115.19000 ? 268 GLN B OE1    1 
ATOM   6915  N  NE2    . GLN B 1 277 ? -35.64300 -15.79400 35.02800  1.000 149.74000 ? 268 GLN B NE2    1 
ATOM   6916  N  N      . LYS B 1 278 ? -34.15000 -21.29700 35.20600  1.000 125.81000 ? 269 LYS B N      1 
ATOM   6917  C  CA     . LYS B 1 278 ? -35.08500 -22.16000 35.92400  1.000 129.03000 ? 269 LYS B CA     1 
ATOM   6918  C  C      . LYS B 1 278 ? -35.95600 -21.29700 36.83600  1.000 136.06000 ? 269 LYS B C      1 
ATOM   6919  O  O      . LYS B 1 278 ? -35.72600 -21.18900 38.04200  1.000 137.53000 ? 269 LYS B O      1 
ATOM   6920  C  CB     . LYS B 1 278 ? -34.32500 -23.23000 36.70400  1.000 107.33000 ? 269 LYS B CB     1 
ATOM   6921  C  CG     . LYS B 1 278 ? -34.89800 -24.63100 36.56300  1.000 109.74000 ? 269 LYS B CG     1 
ATOM   6922  C  CD     . LYS B 1 278 ? -33.99000 -25.67000 37.20300  1.000 101.49000 ? 269 LYS B CD     1 
ATOM   6923  N  N      . ILE B 1 279 ? -36.97300 -20.66600 36.24800  1.000 122.73000 ? 270 ILE B N      1 
ATOM   6924  C  CA     . ILE B 1 279 ? -37.93500 -19.93200 37.06600  1.000 116.00000 ? 270 ILE B CA     1 
ATOM   6925  C  C      . ILE B 1 279 ? -38.67200 -20.88700 37.99700  1.000 108.07000 ? 270 ILE B C      1 
ATOM   6926  O  O      . ILE B 1 279 ? -38.97000 -20.55200 39.15000  1.000 109.65000 ? 270 ILE B O      1 
ATOM   6927  C  CB     . ILE B 1 279 ? -38.90500 -19.13700 36.17700  1.000 113.27000 ? 270 ILE B CB     1 
ATOM   6928  C  CG1    . ILE B 1 279 ? -39.68100 -20.08200 35.26400  1.000 106.84000 ? 270 ILE B CG1    1 
ATOM   6929  C  CG2    . ILE B 1 279 ? -38.15600 -18.09100 35.36500  1.000 121.45000 ? 270 ILE B CG2    1 
ATOM   6930  C  CD1    . ILE B 1 279 ? -40.72100 -19.37700 34.45200  1.000 114.25000 ? 270 ILE B CD1    1 
ATOM   6931  N  N      . GLY B 1 280 ? -38.97800 -22.08700 37.51100  1.000 90.35000  ? 271 GLY B N      1 
ATOM   6932  C  CA     . GLY B 1 280 ? -39.66600 -23.09500 38.29200  1.000 102.95000 ? 271 GLY B CA     1 
ATOM   6933  C  C      . GLY B 1 280 ? -38.99300 -24.43600 38.09400  1.000 116.00000 ? 271 GLY B C      1 
ATOM   6934  O  O      . GLY B 1 280 ? -37.81700 -24.47900 37.72100  1.000 133.96000 ? 271 GLY B O      1 
ATOM   6935  N  N      . GLU B 1 281 ? -39.70700 -25.53900 38.34100  1.000 116.19000 ? 272 GLU B N      1 
ATOM   6936  C  CA     . GLU B 1 281 ? -39.14100 -26.84800 38.03000  1.000 138.79000 ? 272 GLU B CA     1 
ATOM   6937  C  C      . GLU B 1 281 ? -38.67500 -26.99700 36.59000  1.000 135.95000 ? 272 GLU B C      1 
ATOM   6938  O  O      . GLU B 1 281 ? -37.63300 -27.60500 36.32000  1.000 138.95000 ? 272 GLU B O      1 
ATOM   6939  C  CB     . GLU B 1 281 ? -40.15200 -27.95700 38.32800  1.000 146.98000 ? 272 GLU B CB     1 
ATOM   6940  C  CG     . GLU B 1 281 ? -40.37500 -28.25100 39.79700  1.000 154.03000 ? 272 GLU B CG     1 
ATOM   6941  C  CD     . GLU B 1 281 ? -41.23400 -29.48500 40.00700  1.000 158.82000 ? 272 GLU B CD     1 
ATOM   6942  O  OE1    . GLU B 1 281 ? -41.75400 -30.02500 39.00700  1.000 136.38000 ? 272 GLU B OE1    1 
ATOM   6943  O  OE2    . GLU B 1 281 ? -41.38400 -29.91800 41.16900  1.000 170.25000 ? 272 GLU B OE2    1 
ATOM   6944  N  N      . ASN B 1 282 ? -39.43400 -26.43800 35.65500  1.000 130.36000 ? 273 ASN B N      1 
ATOM   6945  C  CA     . ASN B 1 282 ? -39.04200 -26.48000 34.25300  1.000 122.90000 ? 273 ASN B CA     1 
ATOM   6946  C  C      . ASN B 1 282 ? -37.89600 -25.51100 34.01300  1.000 114.95000 ? 273 ASN B C      1 
ATOM   6947  O  O      . ASN B 1 282 ? -37.72000 -24.53200 34.74200  1.000 117.34000 ? 273 ASN B O      1 
ATOM   6948  C  CB     . ASN B 1 282 ? -40.24600 -26.14600 33.37100  1.000 120.42000 ? 273 ASN B CB     1 
ATOM   6949  C  CG     . ASN B 1 282 ? -41.35400 -27.17600 33.49000  1.000 120.63000 ? 273 ASN B CG     1 
ATOM   6950  O  OD1    . ASN B 1 282 ? -42.52200 -26.82800 33.66500  1.000 127.55000 ? 273 ASN B OD1    1 
ATOM   6951  N  ND2    . ASN B 1 282 ? -40.99500 -28.44800 33.39500  1.000 101.61000 ? 273 ASN B ND2    1 
ATOM   6952  N  N      . LEU B 1 283 ? -37.10300 -25.79900 32.98600  1.000 112.63000 ? 274 LEU B N      1 
ATOM   6953  C  CA     . LEU B 1 283 ? -35.97000 -24.96900 32.59700  1.000 89.51000  ? 274 LEU B CA     1 
ATOM   6954  C  C      . LEU B 1 283 ? -36.20800 -24.42600 31.19800  1.000 86.35000  ? 274 LEU B C      1 
ATOM   6955  O  O      . LEU B 1 283 ? -36.38100 -25.20100 30.25000  1.000 107.72000 ? 274 LEU B O      1 
ATOM   6956  C  CB     . LEU B 1 283 ? -34.72900 -25.86200 32.63400  1.000 103.84000 ? 274 LEU B CB     1 
ATOM   6957  C  CG     . LEU B 1 283 ? -33.42100 -25.17000 32.25300  1.000 130.64000 ? 274 LEU B CG     1 
ATOM   6958  C  CD1    . LEU B 1 283 ? -33.04200 -24.14300 33.30600  1.000 125.57000 ? 274 LEU B CD1    1 
ATOM   6959  C  CD2    . LEU B 1 283 ? -32.31000 -26.18900 32.06400  1.000 140.89000 ? 274 LEU B CD2    1 
ATOM   6960  N  N      . VAL B 1 284 ? -36.20800 -23.10500 31.06500  1.000 73.81000  ? 275 VAL B N      1 
ATOM   6961  C  CA     . VAL B 1 284 ? -36.51600 -22.44500 29.80300  1.000 79.85000  ? 275 VAL B CA     1 
ATOM   6962  C  C      . VAL B 1 284 ? -35.21700 -21.88300 29.24700  1.000 83.30000  ? 275 VAL B C      1 
ATOM   6963  O  O      . VAL B 1 284 ? -34.56300 -21.04900 29.88700  1.000 84.63000  ? 275 VAL B O      1 
ATOM   6964  C  CB     . VAL B 1 284 ? -37.57500 -21.34400 29.98000  1.000 74.62000  ? 275 VAL B CB     1 
ATOM   6965  C  CG1    . VAL B 1 284 ? -37.13000 -20.33400 31.02700  1.000 83.91000  ? 275 VAL B CG1    1 
ATOM   6966  C  CG2    . VAL B 1 284 ? -37.85400 -20.65600 28.65400  1.000 80.73000  ? 275 VAL B CG2    1 
ATOM   6967  N  N      . HIS B 1 285 ? -34.84600 -22.34500 28.05600  1.000 90.09000  ? 276 HIS B N      1 
ATOM   6968  C  CA     . HIS B 1 285 ? -33.64000 -21.87500 27.39000  1.000 89.07000  ? 276 HIS B CA     1 
ATOM   6969  C  C      . HIS B 1 285 ? -33.82200 -20.43000 26.94600  1.000 86.77000  ? 276 HIS B C      1 
ATOM   6970  O  O      . HIS B 1 285 ? -34.70000 -20.13200 26.12900  1.000 98.13000  ? 276 HIS B O      1 
ATOM   6971  C  CB     . HIS B 1 285 ? -33.32300 -22.76500 26.18900  1.000 98.14000  ? 276 HIS B CB     1 
ATOM   6972  C  CG     . HIS B 1 285 ? -32.58700 -24.02200 26.53800  1.000 93.30000  ? 276 HIS B CG     1 
ATOM   6973  N  ND1    . HIS B 1 285 ? -31.41700 -24.39500 25.91200  1.000 98.35000  ? 276 HIS B ND1    1 
ATOM   6974  C  CD2    . HIS B 1 285 ? -32.85600 -24.99400 27.44100  1.000 94.01000  ? 276 HIS B CD2    1 
ATOM   6975  C  CE1    . HIS B 1 285 ? -30.99600 -25.54100 26.41500  1.000 108.00000 ? 276 HIS B CE1    1 
ATOM   6976  N  NE2    . HIS B 1 285 ? -31.85200 -25.92700 27.34500  1.000 101.80000 ? 276 HIS B NE2    1 
ATOM   6977  N  N      . GLN B 1 286 ? -32.99700 -19.53000 27.48700  1.000 98.10000  ? 277 GLN B N      1 
ATOM   6978  C  CA     . GLN B 1 286 ? -33.11400 -18.12500 27.11500  1.000 98.86000  ? 277 GLN B CA     1 
ATOM   6979  C  C      . GLN B 1 286 ? -32.70900 -17.91100 25.66400  1.000 105.98000 ? 277 GLN B C      1 
ATOM   6980  O  O      . GLN B 1 286 ? -33.21500 -16.99400 25.00700  1.000 107.10000 ? 277 GLN B O      1 
ATOM   6981  C  CB     . GLN B 1 286 ? -32.26400 -17.25700 28.04400  1.000 95.14000  ? 277 GLN B CB     1 
ATOM   6982  C  CG     . GLN B 1 286 ? -32.77000 -17.20900 29.47700  1.000 93.41000  ? 277 GLN B CG     1 
ATOM   6983  C  CD     . GLN B 1 286 ? -31.88100 -16.38100 30.38500  1.000 101.80000 ? 277 GLN B CD     1 
ATOM   6984  O  OE1    . GLN B 1 286 ? -30.65300 -16.43200 30.28900  1.000 112.96000 ? 277 GLN B OE1    1 
ATOM   6985  N  NE2    . GLN B 1 286 ? -32.50000 -15.60600 31.27100  1.000 88.11000  ? 277 GLN B NE2    1 
ATOM   6986  N  N      . VAL B 1 287 ? -31.80100 -18.73600 25.15600  1.000 110.17000 ? 278 VAL B N      1 
ATOM   6987  C  CA     . VAL B 1 287 ? -31.43600 -18.76300 23.74600  1.000 100.21000 ? 278 VAL B CA     1 
ATOM   6988  C  C      . VAL B 1 287 ? -32.03000 -20.03800 23.14900  1.000 100.93000 ? 278 VAL B C      1 
ATOM   6989  O  O      . VAL B 1 287 ? -31.61300 -21.14600 23.52100  1.000 99.88000  ? 278 VAL B O      1 
ATOM   6990  C  CB     . VAL B 1 287 ? -29.91600 -18.70900 23.54900  1.000 88.97000  ? 278 VAL B CB     1 
ATOM   6991  C  CG1    . VAL B 1 287 ? -29.57900 -18.60400 22.06900  1.000 86.13000  ? 278 VAL B CG1    1 
ATOM   6992  C  CG2    . VAL B 1 287 ? -29.32300 -17.53800 24.32000  1.000 86.58000  ? 278 VAL B CG2    1 
ATOM   6993  N  N      . PRO B 1 288 ? -32.99800 -19.93900 22.24000  1.000 95.42000  ? 279 PRO B N      1 
ATOM   6994  C  CA     . PRO B 1 288 ? -33.65400 -21.14500 21.72400  1.000 85.47000  ? 279 PRO B CA     1 
ATOM   6995  C  C      . PRO B 1 288 ? -32.67800 -22.03900 20.97300  1.000 81.36000  ? 279 PRO B C      1 
ATOM   6996  O  O      . PRO B 1 288 ? -31.63400 -21.60100 20.48600  1.000 89.94000  ? 279 PRO B O      1 
ATOM   6997  C  CB     . PRO B 1 288 ? -34.73700 -20.59100 20.79100  1.000 96.54000  ? 279 PRO B CB     1 
ATOM   6998  C  CG     . PRO B 1 288 ? -34.24900 -19.22500 20.41500  1.000 90.44000  ? 279 PRO B CG     1 
ATOM   6999  C  CD     . PRO B 1 288 ? -33.52300 -18.71000 21.62100  1.000 92.07000  ? 279 PRO B CD     1 
ATOM   7000  N  N      . LYS B 1 289 ? -33.04400 -23.32000 20.87300  1.000 76.49000  ? 280 LYS B N      1 
ATOM   7001  C  CA     . LYS B 1 289 ? -32.19500 -24.27300 20.16700  1.000 76.30000  ? 280 LYS B CA     1 
ATOM   7002  C  C      . LYS B 1 289 ? -31.99800 -23.86700 18.71300  1.000 83.25000  ? 280 LYS B C      1 
ATOM   7003  O  O      . LYS B 1 289 ? -30.96100 -24.17700 18.11500  1.000 94.35000  ? 280 LYS B O      1 
ATOM   7004  C  CB     . LYS B 1 289 ? -32.79200 -25.67900 20.25100  1.000 66.66000  ? 280 LYS B CB     1 
ATOM   7005  N  N      . GLU B 1 290 ? -32.98100 -23.17800 18.12900  1.000 94.23000  ? 281 GLU B N      1 
ATOM   7006  C  CA     . GLU B 1 290 ? -32.83900 -22.70000 16.75900  1.000 102.92000 ? 281 GLU B CA     1 
ATOM   7007  C  C      . GLU B 1 290 ? -31.70500 -21.68700 16.64300  1.000 92.71000  ? 281 GLU B C      1 
ATOM   7008  O  O      . GLU B 1 290 ? -30.90100 -21.74600 15.70400  1.000 100.36000 ? 281 GLU B O      1 
ATOM   7009  C  CB     . GLU B 1 290 ? -34.15900 -22.09000 16.28700  1.000 96.54000  ? 281 GLU B CB     1 
ATOM   7010  C  CG     . GLU B 1 290 ? -34.34400 -22.06900 14.78100  1.000 120.84000 ? 281 GLU B CG     1 
ATOM   7011  C  CD     . GLU B 1 290 ? -35.67500 -21.46600 14.37200  1.000 149.03000 ? 281 GLU B CD     1 
ATOM   7012  O  OE1    . GLU B 1 290 ? -36.27500 -20.74100 15.19400  1.000 146.59000 ? 281 GLU B OE1    1 
ATOM   7013  O  OE2    . GLU B 1 290 ? -36.12300 -21.71800 13.23300  1.000 162.59000 ? 281 GLU B OE2    1 
ATOM   7014  N  N      . THR B 1 291 ? -31.62500 -20.74800 17.58900  1.000 79.56000  ? 282 THR B N      1 
ATOM   7015  C  CA     . THR B 1 291 ? -30.54400 -19.76700 17.56700  1.000 83.18000  ? 282 THR B CA     1 
ATOM   7016  C  C      . THR B 1 291 ? -29.18600 -20.44000 17.72500  1.000 85.05000  ? 282 THR B C      1 
ATOM   7017  O  O      . THR B 1 291 ? -28.21900 -20.07400 17.04600  1.000 86.12000  ? 282 THR B O      1 
ATOM   7018  C  CB     . THR B 1 291 ? -30.75200 -18.72500 18.66700  1.000 84.40000  ? 282 THR B CB     1 
ATOM   7019  O  OG1    . THR B 1 291 ? -32.03600 -18.10800 18.51100  1.000 97.71000  ? 282 THR B OG1    1 
ATOM   7020  C  CG2    . THR B 1 291 ? -29.67200 -17.65400 18.59900  1.000 79.07000  ? 282 THR B CG2    1 
ATOM   7021  N  N      . ILE B 1 292 ? -29.09600 -21.42800 18.61900  1.000 85.51000  ? 283 ILE B N      1 
ATOM   7022  C  CA     . ILE B 1 292 ? -27.83200 -22.12800 18.82800  1.000 76.94000  ? 283 ILE B CA     1 
ATOM   7023  C  C      . ILE B 1 292 ? -27.43200 -22.89400 17.57300  1.000 88.17000  ? 283 ILE B C      1 
ATOM   7024  O  O      . ILE B 1 292 ? -26.25500 -22.93000 17.19800  1.000 92.32000  ? 283 ILE B O      1 
ATOM   7025  C  CB     . ILE B 1 292 ? -27.93300 -23.05700 20.05200  1.000 64.50000  ? 283 ILE B CB     1 
ATOM   7026  C  CG1    . ILE B 1 292 ? -28.20900 -22.24000 21.31700  1.000 75.59000  ? 283 ILE B CG1    1 
ATOM   7027  C  CG2    . ILE B 1 292 ? -26.66100 -23.87200 20.20600  1.000 76.88000  ? 283 ILE B CG2    1 
ATOM   7028  C  CD1    . ILE B 1 292 ? -27.12700 -21.23900 21.65000  1.000 87.71000  ? 283 ILE B CD1    1 
ATOM   7029  N  N      . GLN B 1 293 ? -28.40600 -23.50800 16.89700  1.000 82.23000  ? 284 GLN B N      1 
ATOM   7030  C  CA     . GLN B 1 293 ? -28.12000 -24.22000 15.65500  1.000 73.23000  ? 284 GLN B CA     1 
ATOM   7031  C  C      . GLN B 1 293 ? -27.62000 -23.26300 14.57800  1.000 73.07000  ? 284 GLN B C      1 
ATOM   7032  O  O      . GLN B 1 293 ? -26.63200 -23.54200 13.88500  1.000 87.45000  ? 284 GLN B O      1 
ATOM   7033  C  CB     . GLN B 1 293 ? -29.37600 -24.95600 15.18600  1.000 87.25000  ? 284 GLN B CB     1 
ATOM   7034  C  CG     . GLN B 1 293 ? -29.76600 -26.13700 16.06500  1.000 89.37000  ? 284 GLN B CG     1 
ATOM   7035  C  CD     . GLN B 1 293 ? -31.21200 -26.55300 15.87200  1.000 88.56000  ? 284 GLN B CD     1 
ATOM   7036  O  OE1    . GLN B 1 293 ? -31.96000 -25.91400 15.13100  1.000 98.06000  ? 284 GLN B OE1    1 
ATOM   7037  N  NE2    . GLN B 1 293 ? -31.61400 -27.62700 16.54200  1.000 106.30000 ? 284 GLN B NE2    1 
ATOM   7038  N  N      . ALA B 1 294 ? -28.30000 -22.12500 14.42000  1.000 63.11000  ? 285 ALA B N      1 
ATOM   7039  C  CA     . ALA B 1 294 ? -27.88200 -21.15100 13.41500  1.000 75.26000  ? 285 ALA B CA     1 
ATOM   7040  C  C      . ALA B 1 294 ? -26.48700 -20.61400 13.71000  1.000 87.30000  ? 285 ALA B C      1 
ATOM   7041  O  O      . ALA B 1 294 ? -25.67800 -20.42100 12.79200  1.000 88.80000  ? 285 ALA B O      1 
ATOM   7042  C  CB     . ALA B 1 294 ? -28.89300 -20.00700 13.34200  1.000 94.28000  ? 285 ALA B CB     1 
ATOM   7043  N  N      . LEU B 1 295 ? -26.18100 -20.37500 14.98800  1.000 93.97000  ? 286 LEU B N      1 
ATOM   7044  C  CA     . LEU B 1 295 ? -24.86000 -19.87100 15.34100  1.000 83.20000  ? 286 LEU B CA     1 
ATOM   7045  C  C      . LEU B 1 295 ? -23.79300 -20.94200 15.16700  1.000 69.84000  ? 286 LEU B C      1 
ATOM   7046  O  O      . LEU B 1 295 ? -22.64400 -20.62400 14.83900  1.000 76.50000  ? 286 LEU B O      1 
ATOM   7047  C  CB     . LEU B 1 295 ? -24.86700 -19.35100 16.77800  1.000 71.54000  ? 286 LEU B CB     1 
ATOM   7048  C  CG     . LEU B 1 295 ? -25.74300 -18.11900 17.01200  1.000 76.62000  ? 286 LEU B CG     1 
ATOM   7049  C  CD1    . LEU B 1 295 ? -26.10800 -17.99600 18.48100  1.000 97.59000  ? 286 LEU B CD1    1 
ATOM   7050  C  CD2    . LEU B 1 295 ? -25.04800 -16.86000 16.51800  1.000 77.77000  ? 286 LEU B CD2    1 
ATOM   7051  N  N      . ILE B 1 296 ? -24.15400 -22.21000 15.36800  1.000 58.02000  ? 287 ILE B N      1 
ATOM   7052  C  CA     . ILE B 1 296 ? -23.21900 -23.29600 15.11200  1.000 72.54000  ? 287 ILE B CA     1 
ATOM   7053  C  C      . ILE B 1 296 ? -22.93000 -23.41300 13.62400  1.000 84.58000  ? 287 ILE B C      1 
ATOM   7054  O  O      . ILE B 1 296 ? -21.81400 -23.77000 13.22600  1.000 101.00000 ? 287 ILE B O      1 
ATOM   7055  C  CB     . ILE B 1 296 ? -23.77300 -24.61700 15.67800  1.000 67.11000  ? 287 ILE B CB     1 
ATOM   7056  C  CG1    . ILE B 1 296 ? -23.71300 -24.61900 17.20700  1.000 66.10000  ? 287 ILE B CG1    1 
ATOM   7057  C  CG2    . ILE B 1 296 ? -23.00600 -25.80000 15.11000  1.000 79.29000  ? 287 ILE B CG2    1 
ATOM   7058  C  CD1    . ILE B 1 296 ? -24.37700 -25.82600 17.83800  1.000 48.43000  ? 287 ILE B CD1    1 
ATOM   7059  N  N      . SER B 1 297 ? -23.92200 -23.12300 12.77900  1.000 93.62000  ? 288 SER B N      1 
ATOM   7060  C  CA     . SER B 1 297 ? -23.74500 -23.30100 11.34000  1.000 101.32000 ? 288 SER B CA     1 
ATOM   7061  C  C      . SER B 1 297 ? -23.09000 -22.10000 10.65700  1.000 91.70000  ? 288 SER B C      1 
ATOM   7062  O  O      . SER B 1 297 ? -22.39500 -22.27500 9.64900   1.000 77.70000  ? 288 SER B O      1 
ATOM   7063  C  CB     . SER B 1 297 ? -25.09500 -23.59700 10.68600  1.000 106.26000 ? 288 SER B CB     1 
ATOM   7064  O  OG     . SER B 1 297 ? -26.03800 -22.58100 10.98400  1.000 113.29000 ? 288 SER B OG     1 
ATOM   7065  N  N      . TYR B 1 298 ? -23.27700 -20.89100 11.18700  1.000 87.97000  ? 289 TYR B N      1 
ATOM   7066  C  CA     . TYR B 1 298 ? -22.86100 -19.69300 10.45800  1.000 89.19000  ? 289 TYR B CA     1 
ATOM   7067  C  C      . TYR B 1 298 ? -21.37700 -19.65200 10.10100  1.000 102.27000 ? 289 TYR B C      1 
ATOM   7068  O  O      . TYR B 1 298 ? -21.05600 -19.28900 8.95300   1.000 107.70000 ? 289 TYR B O      1 
ATOM   7069  C  CB     . TYR B 1 298 ? -23.25700 -18.45300 11.26900  1.000 83.78000  ? 289 TYR B CB     1 
ATOM   7070  C  CG     . TYR B 1 298 ? -22.64900 -17.16000 10.77600  1.000 91.03000  ? 289 TYR B CG     1 
ATOM   7071  C  CD1    . TYR B 1 298 ? -22.94700 -16.66200 9.51400   1.000 83.43000  ? 289 TYR B CD1    1 
ATOM   7072  C  CD2    . TYR B 1 298 ? -21.78200 -16.43200 11.58000  1.000 97.70000  ? 289 TYR B CD2    1 
ATOM   7073  C  CE1    . TYR B 1 298 ? -22.39500 -15.47700 9.06700   1.000 80.14000  ? 289 TYR B CE1    1 
ATOM   7074  C  CE2    . TYR B 1 298 ? -21.22500 -15.24800 11.14200  1.000 97.05000  ? 289 TYR B CE2    1 
ATOM   7075  C  CZ     . TYR B 1 298 ? -21.53300 -14.77600 9.88600   1.000 89.38000  ? 289 TYR B CZ     1 
ATOM   7076  O  OH     . TYR B 1 298 ? -20.97800 -13.59500 9.45000   1.000 93.38000  ? 289 TYR B OH     1 
ATOM   7077  N  N      . PRO B 1 299 ? -20.44000 -19.99000 10.99400  1.000 97.50000  ? 290 PRO B N      1 
ATOM   7078  C  CA     . PRO B 1 299 ? -19.01900 -19.89500 10.61300  1.000 91.98000  ? 290 PRO B CA     1 
ATOM   7079  C  C      . PRO B 1 299 ? -18.66100 -20.75300 9.41300   1.000 90.54000  ? 290 PRO B C      1 
ATOM   7080  O  O      . PRO B 1 299 ? -17.81500 -20.35600 8.60000   1.000 85.95000  ? 290 PRO B O      1 
ATOM   7081  C  CB     . PRO B 1 299 ? -18.28300 -20.35200 11.88300  1.000 82.89000  ? 290 PRO B CB     1 
ATOM   7082  C  CG     . PRO B 1 299 ? -19.30000 -21.11000 12.67300  1.000 80.05000  ? 290 PRO B CG     1 
ATOM   7083  C  CD     . PRO B 1 299 ? -20.61300 -20.45400 12.37900  1.000 85.99000  ? 290 PRO B CD     1 
ATOM   7084  N  N      . ILE B 1 300 ? -19.27200 -21.93300 9.28700   1.000 83.19000  ? 291 ILE B N      1 
ATOM   7085  C  CA     . ILE B 1 300 ? -19.00700 -22.78300 8.13000   1.000 93.63000  ? 291 ILE B CA     1 
ATOM   7086  C  C      . ILE B 1 300 ? -19.41800 -22.07100 6.84700   1.000 98.77000  ? 291 ILE B C      1 
ATOM   7087  O  O      . ILE B 1 300 ? -18.69100 -22.09300 5.84300   1.000 99.58000  ? 291 ILE B O      1 
ATOM   7088  C  CB     . ILE B 1 300 ? -19.71900 -24.13900 8.28900   1.000 77.19000  ? 291 ILE B CB     1 
ATOM   7089  C  CG1    . ILE B 1 300 ? -19.46000 -24.71000 9.68500   1.000 51.90000  ? 291 ILE B CG1    1 
ATOM   7090  C  CG2    . ILE B 1 300 ? -19.25200 -25.11400 7.22500   1.000 81.52000  ? 291 ILE B CG2    1 
ATOM   7091  C  CD1    . ILE B 1 300 ? -20.20500 -25.99600 9.97100   1.000 78.54000  ? 291 ILE B CD1    1 
ATOM   7092  N  N      . PHE B 1 301 ? -20.59000 -21.43000 6.85700   1.000 85.16000  ? 292 PHE B N      1 
ATOM   7093  C  CA     . PHE B 1 301 ? -21.03400 -20.69300 5.67900   1.000 90.67000  ? 292 PHE B CA     1 
ATOM   7094  C  C      . PHE B 1 301 ? -20.07600 -19.55400 5.37000   1.000 96.73000  ? 292 PHE B C      1 
ATOM   7095  O  O      . PHE B 1 301 ? -19.77900 -19.27200 4.20100   1.000 99.91000  ? 292 PHE B O      1 
ATOM   7096  C  CB     . PHE B 1 301 ? -22.44200 -20.14100 5.90700   1.000 102.94000 ? 292 PHE B CB     1 
ATOM   7097  C  CG     . PHE B 1 301 ? -23.52700 -21.17800 5.83800   1.000 110.50000 ? 292 PHE B CG     1 
ATOM   7098  C  CD1    . PHE B 1 301 ? -23.82900 -21.95300 6.94600   1.000 110.26000 ? 292 PHE B CD1    1 
ATOM   7099  C  CD2    . PHE B 1 301 ? -24.25700 -21.36500 4.67700   1.000 100.78000 ? 292 PHE B CD2    1 
ATOM   7100  C  CE1    . PHE B 1 301 ? -24.82900 -22.90400 6.89300   1.000 104.69000 ? 292 PHE B CE1    1 
ATOM   7101  C  CE2    . PHE B 1 301 ? -25.25900 -22.31500 4.61800   1.000 114.84000 ? 292 PHE B CE2    1 
ATOM   7102  C  CZ     . PHE B 1 301 ? -25.54500 -23.08500 5.72800   1.000 118.43000 ? 292 PHE B CZ     1 
ATOM   7103  N  N      . PHE B 1 302 ? -19.56700 -18.89900 6.41400   1.000 100.37000 ? 293 PHE B N      1 
ATOM   7104  C  CA     . PHE B 1 302 ? -18.60300 -17.82200 6.21700   1.000 100.15000 ? 293 PHE B CA     1 
ATOM   7105  C  C      . PHE B 1 302 ? -17.33400 -18.33300 5.54100   1.000 100.25000 ? 293 PHE B C      1 
ATOM   7106  O  O      . PHE B 1 302 ? -16.83200 -17.72600 4.58300   1.000 107.63000 ? 293 PHE B O      1 
ATOM   7107  C  CB     . PHE B 1 302 ? -18.29000 -17.18100 7.56800   1.000 88.59000  ? 293 PHE B CB     1 
ATOM   7108  C  CG     . PHE B 1 302 ? -17.54500 -15.89000 7.46800   1.000 93.78000  ? 293 PHE B CG     1 
ATOM   7109  C  CD1    . PHE B 1 302 ? -17.35500 -15.27500 6.24700   1.000 81.01000  ? 293 PHE B CD1    1 
ATOM   7110  C  CD2    . PHE B 1 302 ? -17.03900 -15.28800 8.60200   1.000 118.47000 ? 293 PHE B CD2    1 
ATOM   7111  C  CE1    . PHE B 1 302 ? -16.66800 -14.08600 6.15500   1.000 91.00000  ? 293 PHE B CE1    1 
ATOM   7112  C  CE2    . PHE B 1 302 ? -16.35200 -14.10300 8.51800   1.000 132.86000 ? 293 PHE B CE2    1 
ATOM   7113  C  CZ     . PHE B 1 302 ? -16.16700 -13.49600 7.29300   1.000 126.87000 ? 293 PHE B CZ     1 
ATOM   7114  N  N      . ALA B 1 303 ? -16.80800 -19.46200 6.01900   1.000 87.25000  ? 294 ALA B N      1 
ATOM   7115  C  CA     . ALA B 1 303 ? -15.59300 -20.02100 5.43200   1.000 93.78000  ? 294 ALA B CA     1 
ATOM   7116  C  C      . ALA B 1 303 ? -15.82100 -20.46000 3.99000   1.000 102.88000 ? 294 ALA B C      1 
ATOM   7117  O  O      . ALA B 1 303 ? -14.94200 -20.29500 3.13300   1.000 91.99000  ? 294 ALA B O      1 
ATOM   7118  C  CB     . ALA B 1 303 ? -15.09500 -21.19100 6.27900   1.000 84.61000  ? 294 ALA B CB     1 
ATOM   7119  N  N      . LEU B 1 304 ? -16.99700 -21.02300 3.70400   1.000 108.10000 ? 295 LEU B N      1 
ATOM   7120  C  CA     . LEU B 1 304 ? -17.30600 -21.43500 2.33800   1.000 94.11000  ? 295 LEU B CA     1 
ATOM   7121  C  C      . LEU B 1 304 ? -17.37800 -20.23300 1.40300   1.000 91.45000  ? 295 LEU B C      1 
ATOM   7122  O  O      . LEU B 1 304 ? -16.86500 -20.27700 0.27600   1.000 105.82000 ? 295 LEU B O      1 
ATOM   7123  C  CB     . LEU B 1 304 ? -18.61600 -22.21900 2.32300   1.000 93.41000  ? 295 LEU B CB     1 
ATOM   7124  C  CG     . LEU B 1 304 ? -18.58200 -23.52100 3.12800   1.000 77.41000  ? 295 LEU B CG     1 
ATOM   7125  C  CD1    . LEU B 1 304 ? -19.98600 -24.04800 3.38600   1.000 82.21000  ? 295 LEU B CD1    1 
ATOM   7126  C  CD2    . LEU B 1 304 ? -17.73200 -24.57000 2.42100   1.000 99.33000  ? 295 LEU B CD2    1 
ATOM   7127  N  N      . VAL B 1 305 ? -18.02300 -19.15100 1.85000   1.000 85.41000  ? 296 VAL B N      1 
ATOM   7128  C  CA     . VAL B 1 305 ? -18.05400 -17.92700 1.05400   1.000 102.17000 ? 296 VAL B CA     1 
ATOM   7129  C  C      . VAL B 1 305 ? -16.63800 -17.42800 0.79700   1.000 110.34000 ? 296 VAL B C      1 
ATOM   7130  O  O      . VAL B 1 305 ? -16.30400 -16.98600 -0.31300  1.000 107.26000 ? 296 VAL B O      1 
ATOM   7131  C  CB     . VAL B 1 305 ? -18.91100 -16.85600 1.75500   1.000 103.11000 ? 296 VAL B CB     1 
ATOM   7132  C  CG1    . VAL B 1 305 ? -18.79200 -15.52100 1.03100   1.000 111.90000 ? 296 VAL B CG1    1 
ATOM   7133  C  CG2    . VAL B 1 305 ? -20.36300 -17.30600 1.84500   1.000 105.68000 ? 296 VAL B CG2    1 
ATOM   7134  N  N      . GLY B 1 306 ? -15.78700 -17.47800 1.82400   1.000 109.04000 ? 297 GLY B N      1 
ATOM   7135  C  CA     . GLY B 1 306 ? -14.40400 -17.07200 1.63700   1.000 102.01000 ? 297 GLY B CA     1 
ATOM   7136  C  C      . GLY B 1 306 ? -13.69600 -17.90000 0.58300   1.000 108.93000 ? 297 GLY B C      1 
ATOM   7137  O  O      . GLY B 1 306 ? -12.97500 -17.36300 -0.26200  1.000 118.32000 ? 297 GLY B O      1 
ATOM   7138  N  N      . LEU B 1 307 ? -13.89100 -19.22000 0.61900   1.000 117.53000 ? 298 LEU B N      1 
ATOM   7139  C  CA     . LEU B 1 307 ? -13.27300 -20.08800 -0.38200  1.000 123.99000 ? 298 LEU B CA     1 
ATOM   7140  C  C      . LEU B 1 307 ? -13.76200 -19.74900 -1.78800  1.000 116.11000 ? 298 LEU B C      1 
ATOM   7141  O  O      . LEU B 1 307 ? -12.97000 -19.71900 -2.74000  1.000 118.56000 ? 298 LEU B O      1 
ATOM   7142  C  CB     . LEU B 1 307 ? -13.55500 -21.55500 -0.05400  1.000 116.59000 ? 298 LEU B CB     1 
ATOM   7143  C  CG     . LEU B 1 307 ? -13.03200 -22.58700 -1.05800  1.000 121.45000 ? 298 LEU B CG     1 
ATOM   7144  C  CD1    . LEU B 1 307 ? -11.51200 -22.54800 -1.14100  1.000 114.58000 ? 298 LEU B CD1    1 
ATOM   7145  C  CD2    . LEU B 1 307 ? -13.51800 -23.98400 -0.70100  1.000 127.08000 ? 298 LEU B CD2    1 
ATOM   7146  N  N      . GLY B 1 308 ? -15.06500 -19.50300 -1.94000  1.000 112.17000 ? 299 GLY B N      1 
ATOM   7147  C  CA     . GLY B 1 308 ? -15.58800 -19.12500 -3.24700  1.000 91.97000  ? 299 GLY B CA     1 
ATOM   7148  C  C      . GLY B 1 308 ? -14.97200 -17.84200 -3.77700  1.000 119.69000 ? 299 GLY B C      1 
ATOM   7149  O  O      . GLY B 1 308 ? -14.54200 -17.77000 -4.93700  1.000 133.59000 ? 299 GLY B O      1 
ATOM   7150  N  N      . CYS B 1 309 ? -14.93200 -16.80200 -2.93700  1.000 124.72000 ? 300 CYS B N      1 
ATOM   7151  C  CA     . CYS B 1 309 ? -14.33700 -15.53700 -3.36700  1.000 124.14000 ? 300 CYS B CA     1 
ATOM   7152  C  C      . CYS B 1 309 ? -12.86000 -15.70800 -3.70900  1.000 136.45000 ? 300 CYS B C      1 
ATOM   7153  O  O      . CYS B 1 309 ? -12.36100 -15.10800 -4.67200  1.000 137.48000 ? 300 CYS B O      1 
ATOM   7154  C  CB     . CYS B 1 309 ? -14.51900 -14.46600 -2.28800  1.000 124.94000 ? 300 CYS B CB     1 
ATOM   7155  S  SG     . CYS B 1 309 ? -16.17000 -14.37800 -1.54700  1.000 112.43000 ? 300 CYS B SG     1 
ATOM   7156  N  N      . SER B 1 310 ? -12.14200 -16.51900 -2.92700  1.000 137.39000 ? 301 SER B N      1 
ATOM   7157  C  CA     . SER B 1 310 ? -10.73200 -16.76300 -3.21500  1.000 131.62000 ? 301 SER B CA     1 
ATOM   7158  C  C      . SER B 1 310 ? -10.55100 -17.45500 -4.56000  1.000 144.50000 ? 301 SER B C      1 
ATOM   7159  O  O      . SER B 1 310 ? -9.64800  -17.10300 -5.32900  1.000 152.44000 ? 301 SER B O      1 
ATOM   7160  C  CB     . SER B 1 310 ? -10.10200 -17.59100 -2.09600  1.000 121.14000 ? 301 SER B CB     1 
ATOM   7161  O  OG     . SER B 1 310 ? -10.03500 -16.85000 -0.89000  1.000 121.46000 ? 301 SER B OG     1 
ATOM   7162  N  N      . MET B 1 311 ? -11.38400 -18.45700 -4.85400  1.000 148.71000 ? 302 MET B N      1 
ATOM   7163  C  CA     . MET B 1 311 ? -11.29700 -19.11300 -6.15500  1.000 141.22000 ? 302 MET B CA     1 
ATOM   7164  C  C      . MET B 1 311 ? -11.56500 -18.12800 -7.28400  1.000 140.65000 ? 302 MET B C      1 
ATOM   7165  O  O      . MET B 1 311 ? -10.87700 -18.14800 -8.31100  1.000 148.59000 ? 302 MET B O      1 
ATOM   7166  C  CB     . MET B 1 311 ? -12.27100 -20.29000 -6.23500  1.000 141.41000 ? 302 MET B CB     1 
ATOM   7167  C  CG     . MET B 1 311 ? -11.80000 -21.54700 -5.52000  1.000 146.12000 ? 302 MET B CG     1 
ATOM   7168  S  SD     . MET B 1 311 ? -12.89100 -22.96600 -5.77500  1.000 129.64000 ? 302 MET B SD     1 
ATOM   7169  C  CE     . MET B 1 311 ? -14.19000 -22.62000 -4.58900  1.000 118.24000 ? 302 MET B CE     1 
ATOM   7170  N  N      . LEU B 1 312 ? -12.56000 -17.25500 -7.11200  1.000 143.05000 ? 303 LEU B N      1 
ATOM   7171  C  CA     . LEU B 1 312 ? -12.84700 -16.26600 -8.15000  1.000 147.07000 ? 303 LEU B CA     1 
ATOM   7172  C  C      . LEU B 1 312 ? -11.64800 -15.35200 -8.38300  1.000 148.06000 ? 303 LEU B C      1 
ATOM   7173  O  O      . LEU B 1 312 ? -11.26100 -15.08500 -9.53100  1.000 151.98000 ? 303 LEU B O      1 
ATOM   7174  C  CB     . LEU B 1 312 ? -14.08400 -15.45100 -7.76900  1.000 143.71000 ? 303 LEU B CB     1 
ATOM   7175  N  N      . GLY B 1 313 ? -11.04400 -14.86300 -7.29800  1.000 148.34000 ? 304 GLY B N      1 
ATOM   7176  C  CA     . GLY B 1 313 ? -9.88000  -14.00400 -7.44100  1.000 150.04000 ? 304 GLY B CA     1 
ATOM   7177  C  C      . GLY B 1 313 ? -8.71500  -14.70800 -8.11100  1.000 152.87000 ? 304 GLY B C      1 
ATOM   7178  O  O      . GLY B 1 313 ? -8.05200  -14.14200 -8.98600  1.000 158.27000 ? 304 GLY B O      1 
ATOM   7179  N  N      . ILE B 1 314 ? -8.45100  -15.95500 -7.71000  1.000 146.81000 ? 305 ILE B N      1 
ATOM   7180  C  CA     . ILE B 1 314 ? -7.35900  -16.71700 -8.30800  1.000 143.50000 ? 305 ILE B CA     1 
ATOM   7181  C  C      . ILE B 1 314 ? -7.61400  -16.93800 -9.79300  1.000 145.44000 ? 305 ILE B C      1 
ATOM   7182  O  O      . ILE B 1 314 ? -6.69000  -16.87800 -10.61500 1.000 148.63000 ? 305 ILE B O      1 
ATOM   7183  C  CB     . ILE B 1 314 ? -7.17300  -18.05300 -7.56300  1.000 142.63000 ? 305 ILE B CB     1 
ATOM   7184  C  CG1    . ILE B 1 314 ? -6.76600  -17.81100 -6.10900  1.000 117.55000 ? 305 ILE B CG1    1 
ATOM   7185  C  CG2    . ILE B 1 314 ? -6.13100  -18.91400 -8.25600  1.000 158.27000 ? 305 ILE B CG2    1 
ATOM   7186  C  CD1    . ILE B 1 314 ? -6.72500  -19.07500 -5.27300  1.000 91.20000  ? 305 ILE B CD1    1 
ATOM   7187  N  N      . LEU B 1 315 ? -8.87100  -17.19700 -10.16200 1.000 144.71000 ? 306 LEU B N      1 
ATOM   7188  C  CA     . LEU B 1 315 ? -9.20600  -17.37900 -11.56900 1.000 142.99000 ? 306 LEU B CA     1 
ATOM   7189  C  C      . LEU B 1 315 ? -8.93900  -16.10700 -12.36000 1.000 140.30000 ? 306 LEU B C      1 
ATOM   7190  O  O      . LEU B 1 315 ? -8.35500  -16.15100 -13.45000 1.000 140.79000 ? 306 LEU B O      1 
ATOM   7191  C  CB     . LEU B 1 315 ? -10.66600 -17.80900 -11.71200 1.000 142.34000 ? 306 LEU B CB     1 
ATOM   7192  N  N      . TYR B 1 316 ? -9.36100  -14.95700 -11.82800 1.000 144.32000 ? 307 TYR B N      1 
ATOM   7193  C  CA     . TYR B 1 316 ? -9.08500  -13.70800 -12.53300 1.000 143.71000 ? 307 TYR B CA     1 
ATOM   7194  C  C      . TYR B 1 316 ? -7.58400  -13.46600 -12.65000 1.000 146.17000 ? 307 TYR B C      1 
ATOM   7195  O  O      . TYR B 1 316 ? -7.10800  -12.94300 -13.66500 1.000 146.03000 ? 307 TYR B O      1 
ATOM   7196  C  CB     . TYR B 1 316 ? -9.75600  -12.52400 -11.83600 1.000 146.25000 ? 307 TYR B CB     1 
ATOM   7197  C  CG     . TYR B 1 316 ? -9.08000  -11.20100 -12.14200 1.000 154.55000 ? 307 TYR B CG     1 
ATOM   7198  C  CD1    . TYR B 1 316 ? -9.28600  -10.56000 -13.35900 1.000 153.53000 ? 307 TYR B CD1    1 
ATOM   7199  C  CD2    . TYR B 1 316 ? -8.22700  -10.60000 -11.22500 1.000 166.52000 ? 307 TYR B CD2    1 
ATOM   7200  C  CE1    . TYR B 1 316 ? -8.66800  -9.35600  -13.64800 1.000 162.41000 ? 307 TYR B CE1    1 
ATOM   7201  C  CE2    . TYR B 1 316 ? -7.60400  -9.39500  -11.50700 1.000 160.47000 ? 307 TYR B CE2    1 
ATOM   7202  C  CZ     . TYR B 1 316 ? -7.82800  -8.77800  -12.71900 1.000 156.44000 ? 307 TYR B CZ     1 
ATOM   7203  O  OH     . TYR B 1 316 ? -7.21300  -7.58100  -13.00500 1.000 172.23000 ? 307 TYR B OH     1 
ATOM   7204  N  N      . VAL B 1 317 ? -6.82000  -13.83800 -11.61900 1.000 146.34000 ? 308 VAL B N      1 
ATOM   7205  C  CA     . VAL B 1 317 ? -5.37900  -13.59000 -11.63700 1.000 151.28000 ? 308 VAL B CA     1 
ATOM   7206  C  C      . VAL B 1 317 ? -4.69200  -14.46000 -12.68600 1.000 158.21000 ? 308 VAL B C      1 
ATOM   7207  O  O      . VAL B 1 317 ? -3.86100  -13.97800 -13.46500 1.000 167.61000 ? 308 VAL B O      1 
ATOM   7208  C  CB     . VAL B 1 317 ? -4.77500  -13.81100 -10.23900 1.000 140.93000 ? 308 VAL B CB     1 
ATOM   7209  C  CG1    . VAL B 1 317 ? -3.25400  -13.81000 -10.31200 1.000 126.36000 ? 308 VAL B CG1    1 
ATOM   7210  C  CG2    . VAL B 1 317 ? -5.26500  -12.74200 -9.27300  1.000 141.42000 ? 308 VAL B CG2    1 
ATOM   7211  N  N      . ILE B 1 318 ? -5.02300  -15.75300 -12.72200 1.000 150.85000 ? 309 ILE B N      1 
ATOM   7212  C  CA     . ILE B 1 318 ? -4.29800  -16.66400 -13.60500 1.000 142.82000 ? 309 ILE B CA     1 
ATOM   7213  C  C      . ILE B 1 318 ? -4.69800  -16.45800 -15.06300 1.000 151.26000 ? 309 ILE B C      1 
ATOM   7214  O  O      . ILE B 1 318 ? -3.89100  -16.68700 -15.97400 1.000 149.14000 ? 309 ILE B O      1 
ATOM   7215  C  CB     . ILE B 1 318 ? -4.52700  -18.12100 -13.15700 1.000 126.62000 ? 309 ILE B CB     1 
ATOM   7216  C  CG1    . ILE B 1 318 ? -3.33700  -19.00200 -13.54000 1.000 131.63000 ? 309 ILE B CG1    1 
ATOM   7217  C  CG2    . ILE B 1 318 ? -5.81400  -18.67300 -13.75200 1.000 123.96000 ? 309 ILE B CG2    1 
ATOM   7218  C  CD1    . ILE B 1 318 ? -3.19600  -20.23000 -12.66900 1.000 120.29000 ? 309 ILE B CD1    1 
ATOM   7219  N  N      . VAL B 1 319 ? -5.93500  -16.02900 -15.31000 1.000 153.15000 ? 310 VAL B N      1 
ATOM   7220  C  CA     . VAL B 1 319 ? -6.44500  -15.90900 -16.67400 1.000 145.81000 ? 310 VAL B CA     1 
ATOM   7221  C  C      . VAL B 1 319 ? -5.92100  -14.64700 -17.35000 1.000 164.48000 ? 310 VAL B C      1 
ATOM   7222  O  O      . VAL B 1 319 ? -5.45000  -14.68100 -18.49200 1.000 184.59000 ? 310 VAL B O      1 
ATOM   7223  C  CB     . VAL B 1 319 ? -7.98500  -15.94900 -16.67100 1.000 120.61000 ? 310 VAL B CB     1 
ATOM   7224  N  N      . LYS B 1 320 ? -5.98800  -13.51900 -16.64800 1.000 161.81000 ? 311 LYS B N      1 
ATOM   7225  C  CA     . LYS B 1 320 ? -5.71500  -12.20900 -17.22200 1.000 162.98000 ? 311 LYS B CA     1 
ATOM   7226  C  C      . LYS B 1 320 ? -4.24400  -12.04500 -17.60600 1.000 154.17000 ? 311 LYS B C      1 
ATOM   7227  O  O      . LYS B 1 320 ? -3.35700  -12.76000 -17.13100 1.000 143.95000 ? 311 LYS B O      1 
ATOM   7228  C  CB     . LYS B 1 320 ? -6.13300  -11.10700 -16.24900 1.000 160.51000 ? 311 LYS B CB     1 
ATOM   7229  C  CG     . LYS B 1 320 ? -6.66500  -9.85600  -16.93500 1.000 167.18000 ? 311 LYS B CG     1 
ATOM   7230  C  CD     . LYS B 1 320 ? -7.65100  -10.20700 -18.04600 1.000 158.88000 ? 311 LYS B CD     1 
ATOM   7231  C  CE     . LYS B 1 320 ? -8.97700  -10.70300 -17.48800 1.000 152.93000 ? 311 LYS B CE     1 
ATOM   7232  N  NZ     . LYS B 1 320 ? -9.91600  -11.12800 -18.56600 1.000 124.15000 ? 311 LYS B NZ     1 
ATOM   7233  N  N      . LYS B 1 321 ? -4.00300  -11.07600 -18.49500 1.000 148.33000 ? 312 LYS B N      1 
ATOM   7234  C  CA     . LYS B 1 321 ? -2.69000  -10.73100 -19.02800 1.000 130.45000 ? 312 LYS B CA     1 
ATOM   7235  C  C      . LYS B 1 321 ? -1.71100  -10.43800 -17.89700 1.000 136.82000 ? 312 LYS B C      1 
ATOM   7236  O  O      . LYS B 1 321 ? -1.83600  -9.41500  -17.21100 1.000 136.85000 ? 312 LYS B O      1 
ATOM   7237  C  CB     . LYS B 1 321 ? -2.80800  -9.50700  -19.94200 1.000 122.84000 ? 312 LYS B CB     1 
ATOM   7238  C  CG     . LYS B 1 321 ? -3.63300  -9.71500  -21.20500 1.000 121.67000 ? 312 LYS B CG     1 
ATOM   7239  C  CD     . LYS B 1 321 ? -2.90700  -10.58700 -22.21100 1.000 129.29000 ? 312 LYS B CD     1 
ATOM   7240  C  CE     . LYS B 1 321 ? -1.61200  -9.92500  -22.65400 1.000 115.49000 ? 312 LYS B CE     1 
ATOM   7241  N  NZ     . LYS B 1 321 ? -0.82500  -10.77500 -23.58400 1.000 108.09000 ? 312 LYS B NZ     1 
ATOM   7242  N  N      . PRO B 1 322 ? -0.72000  -11.30500 -17.68000 1.000 145.57000 ? 313 PRO B N      1 
ATOM   7243  C  CA     . PRO B 1 322 ? 0.20500   -11.12500 -16.54800 1.000 139.23000 ? 313 PRO B CA     1 
ATOM   7244  C  C      . PRO B 1 322 ? 1.08500   -9.89800  -16.73900 1.000 135.35000 ? 313 PRO B C      1 
ATOM   7245  O  O      . PRO B 1 322 ? 1.82400   -9.79500  -17.72100 1.000 151.14000 ? 313 PRO B O      1 
ATOM   7246  C  CB     . PRO B 1 322 ? 1.03400   -12.41800 -16.55600 1.000 129.15000 ? 313 PRO B CB     1 
ATOM   7247  C  CG     . PRO B 1 322 ? 0.26700   -13.38100 -17.41600 1.000 144.55000 ? 313 PRO B CG     1 
ATOM   7248  C  CD     . PRO B 1 322 ? -0.44500  -12.54200 -18.42700 1.000 145.70000 ? 313 PRO B CD     1 
ATOM   7249  N  N      . SER B 1 323 ? 1.01100   -8.97100  -15.78800 1.000 126.11000 ? 314 SER B N      1 
ATOM   7250  C  CA     . SER B 1 323 ? 1.89700   -7.82000  -15.80400 1.000 138.12000 ? 314 SER B CA     1 
ATOM   7251  C  C      . SER B 1 323 ? 3.31100   -8.24200  -15.40100 1.000 136.51000 ? 314 SER B C      1 
ATOM   7252  O  O      . SER B 1 323 ? 3.56000   -9.37700  -14.98300 1.000 137.69000 ? 314 SER B O      1 
ATOM   7253  C  CB     . SER B 1 323 ? 1.37100   -6.72300  -14.87700 1.000 147.22000 ? 314 SER B CB     1 
ATOM   7254  O  OG     . SER B 1 323 ? 1.99800   -6.76800  -13.60700 1.000 150.86000 ? 314 SER B OG     1 
ATOM   7255  N  N      . ASP B 1 324 ? 4.25300   -7.30700  -15.54200 1.000 133.44000 ? 315 ASP B N      1 
ATOM   7256  C  CA     . ASP B 1 324 ? 5.63900   -7.61400  -15.20700 1.000 130.90000 ? 315 ASP B CA     1 
ATOM   7257  C  C      . ASP B 1 324 ? 5.83500   -7.70200  -13.69700 1.000 143.06000 ? 315 ASP B C      1 
ATOM   7258  O  O      . ASP B 1 324 ? 6.56400   -8.57500  -13.21100 1.000 148.22000 ? 315 ASP B O      1 
ATOM   7259  C  CB     . ASP B 1 324 ? 6.57400   -6.56700  -15.81800 1.000 147.01000 ? 315 ASP B CB     1 
ATOM   7260  C  CG     . ASP B 1 324 ? 8.04600   -6.89300  -15.60200 1.000 143.83000 ? 315 ASP B CG     1 
ATOM   7261  O  OD1    . ASP B 1 324 ? 8.35000   -7.94700  -15.00300 1.000 140.14000 ? 315 ASP B OD1    1 
ATOM   7262  O  OD2    . ASP B 1 324 ? 8.90200   -6.08900  -16.02900 1.000 136.35000 ? 315 ASP B OD2    1 
ATOM   7263  N  N      . ASN B 1 325 ? 5.18400   -6.81700  -12.93600 1.000 146.18000 ? 316 ASN B N      1 
ATOM   7264  C  CA     . ASN B 1 325 ? 5.34600   -6.80600  -11.48700 1.000 136.49000 ? 316 ASN B CA     1 
ATOM   7265  C  C      . ASN B 1 325 ? 4.55100   -7.94000  -10.85200 1.000 139.90000 ? 316 ASN B C      1 
ATOM   7266  O  O      . ASN B 1 325 ? 3.31400   -7.89500  -10.81900 1.000 146.42000 ? 316 ASN B O      1 
ATOM   7267  C  CB     . ASN B 1 325 ? 4.90500   -5.46100  -10.90600 1.000 118.68000 ? 316 ASN B CB     1 
ATOM   7268  N  N      . PRO B 1 326 ? 5.22500   -8.96700  -10.32600 1.000 125.81000 ? 317 PRO B N      1 
ATOM   7269  C  CA     . PRO B 1 326 ? 4.48200   -10.10500 -9.75900  1.000 113.71000 ? 317 PRO B CA     1 
ATOM   7270  C  C      . PRO B 1 326 ? 3.77600   -9.77200  -8.46000  1.000 115.77000 ? 317 PRO B C      1 
ATOM   7271  O  O      . PRO B 1 326 ? 2.65000   -10.23400 -8.23400  1.000 122.69000 ? 317 PRO B O      1 
ATOM   7272  C  CB     . PRO B 1 326 ? 5.57400   -11.16300 -9.56200  1.000 122.94000 ? 317 PRO B CB     1 
ATOM   7273  C  CG     . PRO B 1 326 ? 6.81100   -10.36400 -9.33200  1.000 131.67000 ? 317 PRO B CG     1 
ATOM   7274  C  CD     . PRO B 1 326 ? 6.68300   -9.13700  -10.19800 1.000 121.21000 ? 317 PRO B CD     1 
ATOM   7275  N  N      . GLN B 1 327 ? 4.41300   -8.98200  -7.59200  1.000 113.31000 ? 318 GLN B N      1 
ATOM   7276  C  CA     . GLN B 1 327 ? 3.85200   -8.72800  -6.26900  1.000 106.95000 ? 318 GLN B CA     1 
ATOM   7277  C  C      . GLN B 1 327 ? 2.48800   -8.05800  -6.36200  1.000 121.21000 ? 318 GLN B C      1 
ATOM   7278  O  O      . GLN B 1 327 ? 1.57300   -8.39000  -5.59800  1.000 131.54000 ? 318 GLN B O      1 
ATOM   7279  C  CB     . GLN B 1 327 ? 4.81600   -7.87300  -5.44700  1.000 67.17000  ? 318 GLN B CB     1 
ATOM   7280  N  N      . ARG B 1 328 ? 2.33100   -7.10600  -7.28400  1.000 122.13000 ? 319 ARG B N      1 
ATOM   7281  C  CA     . ARG B 1 328 ? 1.04100   -6.44100  -7.42900  1.000 131.96000 ? 319 ARG B CA     1 
ATOM   7282  C  C      . ARG B 1 328 ? -0.06200  -7.42900  -7.78900  1.000 145.70000 ? 319 ARG B C      1 
ATOM   7283  O  O      . ARG B 1 328 ? -1.19700  -7.28200  -7.32500  1.000 155.41000 ? 319 ARG B O      1 
ATOM   7284  C  CB     . ARG B 1 328 ? 1.13100   -5.32800  -8.47500  1.000 135.62000 ? 319 ARG B CB     1 
ATOM   7285  C  CG     . ARG B 1 328 ? 0.04800   -4.26200  -8.33300  1.000 136.85000 ? 319 ARG B CG     1 
ATOM   7286  C  CD     . ARG B 1 328 ? 0.27900   -3.37700  -7.11300  1.000 117.44000 ? 319 ARG B CD     1 
ATOM   7287  N  NE     . ARG B 1 328 ? 1.52200   -2.61900  -7.20400  1.000 124.25000 ? 319 ARG B NE     1 
ATOM   7288  C  CZ     . ARG B 1 328 ? 1.61600   -1.38900  -7.69000  1.000 114.58000 ? 319 ARG B CZ     1 
ATOM   7289  N  NH1    . ARG B 1 328 ? 0.55400   -0.73900  -8.13700  1.000 93.51000  ? 319 ARG B NH1    1 
ATOM   7290  N  NH2    . ARG B 1 328 ? 2.80600   -0.79600  -7.73100  1.000 111.34000 ? 319 ARG B NH2    1 
ATOM   7291  N  N      . GLU B 1 329 ? 0.25600   -8.46300  -8.57200  1.000 142.13000 ? 320 GLU B N      1 
ATOM   7292  C  CA     . GLU B 1 329 ? -0.76900  -9.42100  -8.98000  1.000 140.72000 ? 320 GLU B CA     1 
ATOM   7293  C  C      . GLU B 1 329 ? -1.28600  -10.21900 -7.78700  1.000 133.82000 ? 320 GLU B C      1 
ATOM   7294  O  O      . GLU B 1 329 ? -2.50100  -10.33500 -7.58100  1.000 132.98000 ? 320 GLU B O      1 
ATOM   7295  C  CB     . GLU B 1 329 ? -0.20900  -10.36100 -10.05100 1.000 127.87000 ? 320 GLU B CB     1 
ATOM   7296  C  CG     . GLU B 1 329 ? 0.55600   -9.67000  -11.17500 1.000 118.00000 ? 320 GLU B CG     1 
ATOM   7297  C  CD     . GLU B 1 329 ? -0.23500  -8.55800  -11.84000 1.000 148.92000 ? 320 GLU B CD     1 
ATOM   7298  O  OE1    . GLU B 1 329 ? -1.10300  -8.86600  -12.68400 1.000 153.59000 ? 320 GLU B OE1    1 
ATOM   7299  O  OE2    . GLU B 1 329 ? 0.01400   -7.37600  -11.52100 1.000 157.78000 ? 320 GLU B OE2    1 
ATOM   7300  N  N      . LEU B 1 330 ? -0.37700  -10.77400 -6.98300  1.000 121.46000 ? 321 LEU B N      1 
ATOM   7301  C  CA     . LEU B 1 330 ? -0.79800  -11.53400 -5.81000  1.000 120.63000 ? 321 LEU B CA     1 
ATOM   7302  C  C      . LEU B 1 330 ? -1.46200  -10.63200 -4.77500  1.000 132.32000 ? 321 LEU B C      1 
ATOM   7303  O  O      . LEU B 1 330 ? -2.42100  -11.04300 -4.10900  1.000 134.46000 ? 321 LEU B O      1 
ATOM   7304  C  CB     . LEU B 1 330 ? 0.39600   -12.27300 -5.20600  1.000 117.35000 ? 321 LEU B CB     1 
ATOM   7305  C  CG     . LEU B 1 330 ? 0.82300   -13.57200 -5.89600  1.000 119.66000 ? 321 LEU B CG     1 
ATOM   7306  C  CD1    . LEU B 1 330 ? 0.96700   -13.37900 -7.39800  1.000 114.14000 ? 321 LEU B CD1    1 
ATOM   7307  C  CD2    . LEU B 1 330 ? 2.12000   -14.10100 -5.29900  1.000 125.23000 ? 321 LEU B CD2    1 
ATOM   7308  N  N      . ASN B 1 331 ? -0.96100  -9.40400  -4.61500  1.000 132.44000 ? 322 ASN B N      1 
ATOM   7309  C  CA     . ASN B 1 331 ? -1.59800  -8.46300  -3.69700  1.000 133.14000 ? 322 ASN B CA     1 
ATOM   7310  C  C      . ASN B 1 331 ? -3.02600  -8.15200  -4.12800  1.000 145.65000 ? 322 ASN B C      1 
ATOM   7311  O  O      . ASN B 1 331 ? -3.92800  -8.04700  -3.28700  1.000 144.74000 ? 322 ASN B O      1 
ATOM   7312  C  CB     . ASN B 1 331 ? -0.77100  -7.18000  -3.60300  1.000 117.36000 ? 322 ASN B CB     1 
ATOM   7313  N  N      . ILE B 1 332 ? -3.25600  -8.00600  -5.43500  1.000 149.51000 ? 323 ILE B N      1 
ATOM   7314  C  CA     . ILE B 1 332 ? -4.60900  -7.75300  -5.91400  1.000 147.21000 ? 323 ILE B CA     1 
ATOM   7315  C  C      . ILE B 1 332 ? -5.47600  -8.99200  -5.75500  1.000 138.24000 ? 323 ILE B C      1 
ATOM   7316  O  O      . ILE B 1 332 ? -6.67400  -8.88400  -5.48300  1.000 142.45000 ? 323 ILE B O      1 
ATOM   7317  C  CB     . ILE B 1 332 ? -4.58400  -7.26400  -7.37300  1.000 156.63000 ? 323 ILE B CB     1 
ATOM   7318  C  CG1    . ILE B 1 332 ? -3.91200  -5.89200  -7.45800  1.000 172.07000 ? 323 ILE B CG1    1 
ATOM   7319  C  CG2    . ILE B 1 332 ? -5.99600  -7.21100  -7.93800  1.000 168.63000 ? 323 ILE B CG2    1 
ATOM   7320  C  CD1    . ILE B 1 332 ? -3.60600  -5.44700  -8.87100  1.000 169.52000 ? 323 ILE B CD1    1 
ATOM   7321  N  N      . SER B 1 333 ? -4.89800  -10.18300 -5.92000  1.000 130.86000 ? 324 SER B N      1 
ATOM   7322  C  CA     . SER B 1 333 ? -5.63900  -11.40500 -5.61900  1.000 134.51000 ? 324 SER B CA     1 
ATOM   7323  C  C      . SER B 1 333 ? -6.11000  -11.41000 -4.16800  1.000 140.45000 ? 324 SER B C      1 
ATOM   7324  O  O      . SER B 1 333 ? -7.28000  -11.69500 -3.87900  1.000 143.92000 ? 324 SER B O      1 
ATOM   7325  C  CB     . SER B 1 333 ? -4.77200  -12.63000 -5.91300  1.000 135.47000 ? 324 SER B CB     1 
ATOM   7326  O  OG     . SER B 1 333 ? -5.46600  -13.83000 -5.62000  1.000 131.01000 ? 324 SER B OG     1 
ATOM   7327  N  N      . LEU B 1 334 ? -5.19700  -11.11400 -3.23900  1.000 138.15000 ? 325 LEU B N      1 
ATOM   7328  C  CA     . LEU B 1 334 ? -5.55100  -11.06000 -1.82300  1.000 133.04000 ? 325 LEU B CA     1 
ATOM   7329  C  C      . LEU B 1 334 ? -6.63800  -10.02200 -1.56400  1.000 124.52000 ? 325 LEU B C      1 
ATOM   7330  O  O      . LEU B 1 334 ? -7.61300  -10.29000 -0.85100  1.000 111.12000 ? 325 LEU B O      1 
ATOM   7331  C  CB     . LEU B 1 334 ? -4.31000  -10.75500 -0.98100  1.000 114.20000 ? 325 LEU B CB     1 
ATOM   7332  C  CG     . LEU B 1 334 ? -3.31100  -11.88800 -0.74200  1.000 99.77000  ? 325 LEU B CG     1 
ATOM   7333  C  CD1    . LEU B 1 334 ? -2.04800  -11.35500 -0.08100  1.000 76.96000  ? 325 LEU B CD1    1 
ATOM   7334  C  CD2    . LEU B 1 334 ? -3.93500  -12.98900 0.10000   1.000 98.71000  ? 325 LEU B CD2    1 
ATOM   7335  N  N      . TRP B 1 335 ? -6.47400  -8.81800  -2.12200  1.000 128.22000 ? 326 TRP B N      1 
ATOM   7336  C  CA     . TRP B 1 335 ? -7.46100  -7.76300  -1.91200  1.000 124.77000 ? 326 TRP B CA     1 
ATOM   7337  C  C      . TRP B 1 335 ? -8.82400  -8.17500  -2.45100  1.000 127.08000 ? 326 TRP B C      1 
ATOM   7338  O  O      . TRP B 1 335 ? -9.85100  -7.95500  -1.80000  1.000 122.11000 ? 326 TRP B O      1 
ATOM   7339  C  CB     . TRP B 1 335 ? -6.99800  -6.46700  -2.57900  1.000 133.03000 ? 326 TRP B CB     1 
ATOM   7340  C  CG     . TRP B 1 335 ? -5.90000  -5.75800  -1.84900  1.000 133.35000 ? 326 TRP B CG     1 
ATOM   7341  C  CD1    . TRP B 1 335 ? -5.47500  -5.99500  -0.57400  1.000 124.29000 ? 326 TRP B CD1    1 
ATOM   7342  C  CD2    . TRP B 1 335 ? -5.07800  -4.69900  -2.35600  1.000 137.30000 ? 326 TRP B CD2    1 
ATOM   7343  N  NE1    . TRP B 1 335 ? -4.44200  -5.14700  -0.25500  1.000 128.60000 ? 326 TRP B NE1    1 
ATOM   7344  C  CE2    . TRP B 1 335 ? -4.17900  -4.34200  -1.33200  1.000 144.75000 ? 326 TRP B CE2    1 
ATOM   7345  C  CE3    . TRP B 1 335 ? -5.01500  -4.01700  -3.57600  1.000 131.57000 ? 326 TRP B CE3    1 
ATOM   7346  C  CZ2    . TRP B 1 335 ? -3.22900  -3.33300  -1.48900  1.000 149.01000 ? 326 TRP B CZ2    1 
ATOM   7347  C  CZ3    . TRP B 1 335 ? -4.07200  -3.01600  -3.73000  1.000 130.40000 ? 326 TRP B CZ3    1 
ATOM   7348  C  CH2    . TRP B 1 335 ? -3.19200  -2.68400  -2.69300  1.000 141.40000 ? 326 TRP B CH2    1 
ATOM   7349  N  N      . THR B 1 336 ? -8.85300  -8.75500  -3.65400  1.000 142.71000 ? 327 THR B N      1 
ATOM   7350  C  CA     . THR B 1 336 ? -10.10400 -9.23200  -4.22900  1.000 145.09000 ? 327 THR B CA     1 
ATOM   7351  C  C      . THR B 1 336 ? -10.76800 -10.24400 -3.31100  1.000 122.55000 ? 327 THR B C      1 
ATOM   7352  O  O      . THR B 1 336 ? -11.93600 -10.09100 -2.94300  1.000 116.77000 ? 327 THR B O      1 
ATOM   7353  C  CB     . THR B 1 336 ? -9.85800  -9.84500  -5.60900  1.000 148.05000 ? 327 THR B CB     1 
ATOM   7354  O  OG1    . THR B 1 336 ? -8.74500  -10.74600 -5.54500  1.000 138.51000 ? 327 THR B OG1    1 
ATOM   7355  C  CG2    . THR B 1 336 ? -9.56800  -8.76000  -6.63200  1.000 158.26000 ? 327 THR B CG2    1 
ATOM   7356  N  N      . SER B 1 337 ? -10.04000 -11.29900 -2.94200  1.000 116.16000 ? 328 SER B N      1 
ATOM   7357  C  CA     . SER B 1 337 ? -10.61700 -12.30700 -2.06000  1.000 108.81000 ? 328 SER B CA     1 
ATOM   7358  C  C      . SER B 1 337 ? -11.18100 -11.66600 -0.80000  1.000 111.82000 ? 328 SER B C      1 
ATOM   7359  O  O      . SER B 1 337 ? -12.34500 -11.88300 -0.44300  1.000 109.95000 ? 328 SER B O      1 
ATOM   7360  C  CB     . SER B 1 337 ? -9.56600  -13.36200 -1.70700  1.000 116.87000 ? 328 SER B CB     1 
ATOM   7361  O  OG     . SER B 1 337 ? -9.14500  -14.06900 -2.86000  1.000 110.32000 ? 328 SER B OG     1 
ATOM   7362  N  N      . ALA B 1 338 ? -10.37400 -10.84100 -0.12800  1.000 115.74000 ? 329 ALA B N      1 
ATOM   7363  C  CA     . ALA B 1 338 ? -10.78400 -10.28700 1.15700   1.000 122.97000 ? 329 ALA B CA     1 
ATOM   7364  C  C      . ALA B 1 338 ? -12.01900 -9.40700  1.01600   1.000 109.15000 ? 329 ALA B C      1 
ATOM   7365  O  O      . ALA B 1 338 ? -13.02800 -9.62200  1.69500   1.000 107.22000 ? 329 ALA B O      1 
ATOM   7366  C  CB     . ALA B 1 338 ? -9.63000  -9.50000  1.77900   1.000 131.46000 ? 329 ALA B CB     1 
ATOM   7367  N  N      . LEU B 1 339 ? -11.96400 -8.40900  0.13100   1.000 96.56000  ? 330 LEU B N      1 
ATOM   7368  C  CA     . LEU B 1 339 ? -13.06600 -7.46000  0.04000   1.000 96.81000  ? 330 LEU B CA     1 
ATOM   7369  C  C      . LEU B 1 339 ? -14.31500 -8.09400  -0.56200  1.000 96.30000  ? 330 LEU B C      1 
ATOM   7370  O  O      . LEU B 1 339 ? -15.43500 -7.73200  -0.18000  1.000 91.83000  ? 330 LEU B O      1 
ATOM   7371  C  CB     . LEU B 1 339 ? -12.62900 -6.23700  -0.76900  1.000 113.39000 ? 330 LEU B CB     1 
ATOM   7372  C  CG     . LEU B 1 339 ? -11.92800 -5.14100  0.04200   1.000 109.11000 ? 330 LEU B CG     1 
ATOM   7373  C  CD1    . LEU B 1 339 ? -10.62500 -5.65500  0.64100   1.000 105.44000 ? 330 LEU B CD1    1 
ATOM   7374  C  CD2    . LEU B 1 339 ? -11.67200 -3.90900  -0.81200  1.000 95.97000  ? 330 LEU B CD2    1 
ATOM   7375  N  N      . LEU B 1 340 ? -14.15300 -9.05200  -1.47800  1.000 97.20000  ? 331 LEU B N      1 
ATOM   7376  C  CA     . LEU B 1 340 ? -15.30200 -9.76300  -2.02100  1.000 101.27000 ? 331 LEU B CA     1 
ATOM   7377  C  C      . LEU B 1 340 ? -15.98100 -10.59900 -0.94600  1.000 99.41000  ? 331 LEU B C      1 
ATOM   7378  O  O      . LEU B 1 340 ? -17.21200 -10.59700 -0.82900  1.000 97.24000  ? 331 LEU B O      1 
ATOM   7379  C  CB     . LEU B 1 340 ? -14.85900 -10.64300 -3.18900  1.000 108.09000 ? 331 LEU B CB     1 
ATOM   7380  C  CG     . LEU B 1 340 ? -15.92200 -11.00200 -4.22700  1.000 120.66000 ? 331 LEU B CG     1 
ATOM   7381  C  CD1    . LEU B 1 340 ? -15.26000 -11.46900 -5.51500  1.000 116.53000 ? 331 LEU B CD1    1 
ATOM   7382  C  CD2    . LEU B 1 340 ? -16.88300 -12.05300 -3.69100  1.000 121.80000 ? 331 LEU B CD2    1 
ATOM   7383  N  N      . THR B 1 341 ? -15.19200 -11.34100 -0.16100  1.000 94.30000  ? 332 THR B N      1 
ATOM   7384  C  CA     . THR B 1 341 ? -15.75700 -12.04200 0.98400   1.000 99.26000  ? 332 THR B CA     1 
ATOM   7385  C  C      . THR B 1 341 ? -16.46900 -11.06900 1.91000   1.000 101.21000 ? 332 THR B C      1 
ATOM   7386  O  O      . THR B 1 341 ? -17.57700 -11.34400 2.37800   1.000 87.80000  ? 332 THR B O      1 
ATOM   7387  C  CB     . THR B 1 341 ? -14.65900 -12.79100 1.73800   1.000 106.04000 ? 332 THR B CB     1 
ATOM   7388  O  OG1    . THR B 1 341 ? -13.91600 -13.60400 0.82100   1.000 103.47000 ? 332 THR B OG1    1 
ATOM   7389  C  CG2    . THR B 1 341 ? -15.26300 -13.67500 2.81900   1.000 110.23000 ? 332 THR B CG2    1 
ATOM   7390  N  N      . VAL B 1 342 ? -15.85100 -9.91800  2.17700   1.000 101.37000 ? 333 VAL B N      1 
ATOM   7391  C  CA     . VAL B 1 342 ? -16.48500 -8.90400  3.01500   1.000 92.35000  ? 333 VAL B CA     1 
ATOM   7392  C  C      . VAL B 1 342 ? -17.87900 -8.59100  2.48700   1.000 88.37000  ? 333 VAL B C      1 
ATOM   7393  O  O      . VAL B 1 342 ? -18.88500 -8.76300  3.18300   1.000 82.97000  ? 333 VAL B O      1 
ATOM   7394  C  CB     . VAL B 1 342 ? -15.61500 -7.63700  3.08000   1.000 88.89000  ? 333 VAL B CB     1 
ATOM   7395  C  CG1    . VAL B 1 342 ? -16.40000 -6.48000  3.68100   1.000 95.79000  ? 333 VAL B CG1    1 
ATOM   7396  C  CG2    . VAL B 1 342 ? -14.35100 -7.90600  3.87900   1.000 94.59000  ? 333 VAL B CG2    1 
ATOM   7397  N  N      . VAL B 1 343 ? -17.95200 -8.14800  1.23100   1.000 97.45000  ? 334 VAL B N      1 
ATOM   7398  C  CA     . VAL B 1 343 ? -19.21200 -7.65100  0.68700   1.000 97.29000  ? 334 VAL B CA     1 
ATOM   7399  C  C      . VAL B 1 343 ? -20.24800 -8.76400  0.54700   1.000 90.81000  ? 334 VAL B C      1 
ATOM   7400  O  O      . VAL B 1 343 ? -21.45200 -8.50900  0.65800   1.000 85.75000  ? 334 VAL B O      1 
ATOM   7401  C  CB     . VAL B 1 343 ? -18.96000 -6.94700  -0.65800  1.000 94.34000  ? 334 VAL B CB     1 
ATOM   7402  C  CG1    . VAL B 1 343 ? -18.08600 -5.72300  -0.45200  1.000 91.71000  ? 334 VAL B CG1    1 
ATOM   7403  C  CG2    . VAL B 1 343 ? -18.31600 -7.90900  -1.64600  1.000 108.14000 ? 334 VAL B CG2    1 
ATOM   7404  N  N      . LEU B 1 344 ? -19.81800 -10.00600 0.32500   1.000 91.00000  ? 335 LEU B N      1 
ATOM   7405  C  CA     . LEU B 1 344 ? -20.78800 -11.07800 0.12200   1.000 89.62000  ? 335 LEU B CA     1 
ATOM   7406  C  C      . LEU B 1 344 ? -21.32700 -11.65300 1.42700   1.000 91.86000  ? 335 LEU B C      1 
ATOM   7407  O  O      . LEU B 1 344 ? -22.54600 -11.73900 1.63200   1.000 93.13000  ? 335 LEU B O      1 
ATOM   7408  C  CB     . LEU B 1 344 ? -20.16900 -12.17700 -0.74500  1.000 106.75000 ? 335 LEU B CB     1 
ATOM   7409  C  CG     . LEU B 1 344 ? -21.11300 -13.21400 -1.35700  1.000 108.58000 ? 335 LEU B CG     1 
ATOM   7410  C  CD1    . LEU B 1 344 ? -20.43400 -13.90900 -2.52600  1.000 91.73000  ? 335 LEU B CD1    1 
ATOM   7411  C  CD2    . LEU B 1 344 ? -21.57300 -14.22700 -0.31800  1.000 101.82000 ? 335 LEU B CD2    1 
ATOM   7412  N  N      . THR B 1 345 ? -20.43500 -12.05400 2.33000   1.000 90.62000  ? 336 THR B N      1 
ATOM   7413  C  CA     . THR B 1 345 ? -20.86700 -12.40900 3.67100   1.000 86.68000  ? 336 THR B CA     1 
ATOM   7414  C  C      . THR B 1 345 ? -21.56600 -11.24500 4.36100   1.000 98.79000  ? 336 THR B C      1 
ATOM   7415  O  O      . THR B 1 345 ? -22.21200 -11.44200 5.39200   1.000 96.67000  ? 336 THR B O      1 
ATOM   7416  C  CB     . THR B 1 345 ? -19.66200 -12.84100 4.49700   1.000 96.45000  ? 336 THR B CB     1 
ATOM   7417  O  OG1    . THR B 1 345 ? -18.71200 -11.77100 4.54300   1.000 91.06000  ? 336 THR B OG1    1 
ATOM   7418  C  CG2    . THR B 1 345 ? -19.01400 -14.03800 3.84100   1.000 104.74000 ? 336 THR B CG2    1 
ATOM   7419  N  N      . ALA B 1 346 ? -21.45600 -10.03500 3.80500   1.000 102.57000 ? 337 ALA B N      1 
ATOM   7420  C  CA     . ALA B 1 346 ? -22.30500 -8.94100  4.25200   1.000 95.10000  ? 337 ALA B CA     1 
ATOM   7421  C  C      . ALA B 1 346 ? -23.74600 -9.42600  4.18000   1.000 86.83000  ? 337 ALA B C      1 
ATOM   7422  O  O      . ALA B 1 346 ? -24.44200 -9.49500  5.19500   1.000 71.73000  ? 337 ALA B O      1 
ATOM   7423  C  CB     . ALA B 1 346 ? -22.10300 -7.69400  3.38800   1.000 90.56000  ? 337 ALA B CB     1 
ATOM   7424  N  N      . PHE B 1 347 ? -24.19900 -9.79300  2.97900   1.000 96.42000  ? 338 PHE B N      1 
ATOM   7425  C  CA     . PHE B 1 347 ? -25.55600 -10.31100 2.83300   1.000 103.77000 ? 338 PHE B CA     1 
ATOM   7426  C  C      . PHE B 1 347 ? -25.79100 -11.61700 3.58100   1.000 87.34000  ? 338 PHE B C      1 
ATOM   7427  O  O      . PHE B 1 347 ? -26.85800 -11.82200 4.17300   1.000 83.12000  ? 338 PHE B O      1 
ATOM   7428  C  CB     . PHE B 1 347 ? -25.89200 -10.50100 1.35200   1.000 104.28000 ? 338 PHE B CB     1 
ATOM   7429  C  CG     . PHE B 1 347 ? -25.65000 -9.28200  0.50700   1.000 110.87000 ? 338 PHE B CG     1 
ATOM   7430  C  CD1    . PHE B 1 347 ? -26.47300 -8.17400  0.60900   1.000 105.62000 ? 338 PHE B CD1    1 
ATOM   7431  C  CD2    . PHE B 1 347 ? -24.60400 -9.25100  -0.40100  1.000 120.20000 ? 338 PHE B CD2    1 
ATOM   7432  C  CE1    . PHE B 1 347 ? -26.25200 -7.05300  -0.17200  1.000 103.72000 ? 338 PHE B CE1    1 
ATOM   7433  C  CE2    . PHE B 1 347 ? -24.37900 -8.13300  -1.18600  1.000 117.40000 ? 338 PHE B CE2    1 
ATOM   7434  C  CZ     . PHE B 1 347 ? -25.20300 -7.03300  -1.07100  1.000 84.95000  ? 338 PHE B CZ     1 
ATOM   7435  N  N      . LEU B 1 348 ? -24.80100 -12.51300 3.56900   1.000 88.08000  ? 339 LEU B N      1 
ATOM   7436  C  CA     . LEU B 1 348 ? -24.95500 -13.78300 4.27700   1.000 88.59000  ? 339 LEU B CA     1 
ATOM   7437  C  C      . LEU B 1 348 ? -25.19400 -13.50400 5.75900   1.000 80.74000  ? 339 LEU B C      1 
ATOM   7438  O  O      . LEU B 1 348 ? -26.11900 -14.04700 6.37200   1.000 80.00000  ? 339 LEU B O      1 
ATOM   7439  C  CB     . LEU B 1 348 ? -23.67100 -14.60600 4.17100   1.000 99.69000  ? 339 LEU B CB     1 
ATOM   7440  C  CG     . LEU B 1 348 ? -23.71300 -15.92000 4.95600   1.000 93.86000  ? 339 LEU B CG     1 
ATOM   7441  C  CD1    . LEU B 1 348 ? -24.79300 -16.84200 4.41000   1.000 73.31000  ? 339 LEU B CD1    1 
ATOM   7442  C  CD2    . LEU B 1 348 ? -22.35900 -16.60000 4.91800   1.000 102.99000 ? 339 LEU B CD2    1 
ATOM   7443  N  N      . THR B 1 349 ? -24.37000 -12.63600 6.34100   1.000 88.99000  ? 340 THR B N      1 
ATOM   7444  C  CA     . THR B 1 349 ? -24.52400 -12.26100 7.74200   1.000 94.94000  ? 340 THR B CA     1 
ATOM   7445  C  C      . THR B 1 349 ? -25.84200 -11.49800 7.94300   1.000 99.19000  ? 340 THR B C      1 
ATOM   7446  O  O      . THR B 1 349 ? -26.57100 -11.71300 8.91700   1.000 100.96000 ? 340 THR B O      1 
ATOM   7447  C  CB     . THR B 1 349 ? -23.30700 -11.50200 8.26700   1.000 91.29000  ? 340 THR B CB     1 
ATOM   7448  O  OG1    . THR B 1 349 ? -22.14100 -12.32000 8.12600   1.000 84.19000  ? 340 THR B OG1    1 
ATOM   7449  C  CG2    . THR B 1 349 ? -23.48300 -11.17200 9.72900   1.000 87.27000  ? 340 THR B CG2    1 
ATOM   7450  N  N      . TYR B 1 350 ? -26.16200 -10.62900 6.98000   1.000 95.88000  ? 341 TYR B N      1 
ATOM   7451  C  CA     . TYR B 1 350 ? -27.37400 -9.82300  7.03600   1.000 102.94000 ? 341 TYR B CA     1 
ATOM   7452  C  C      . TYR B 1 350 ? -28.70100 -10.56700 7.04100   1.000 83.02000  ? 341 TYR B C      1 
ATOM   7453  O  O      . TYR B 1 350 ? -29.64900 -10.16100 7.72300   1.000 59.14000  ? 341 TYR B O      1 
ATOM   7454  C  CB     . TYR B 1 350 ? -27.28000 -8.89100  5.82300   1.000 106.04000 ? 341 TYR B CB     1 
ATOM   7455  C  CG     . TYR B 1 350 ? -28.07100 -7.60000  5.88200   1.000 124.39000 ? 341 TYR B CG     1 
ATOM   7456  C  CD1    . TYR B 1 350 ? -27.59900 -6.50400  6.59500   1.000 139.07000 ? 341 TYR B CD1    1 
ATOM   7457  C  CD2    . TYR B 1 350 ? -29.26400 -7.46100  5.18400   1.000 134.48000 ? 341 TYR B CD2    1 
ATOM   7458  C  CE1    . TYR B 1 350 ? -28.30900 -5.31600  6.63200   1.000 155.72000 ? 341 TYR B CE1    1 
ATOM   7459  C  CE2    . TYR B 1 350 ? -29.98100 -6.27700  5.21600   1.000 148.08000 ? 341 TYR B CE2    1 
ATOM   7460  C  CZ     . TYR B 1 350 ? -29.49800 -5.20800  5.94200   1.000 163.44000 ? 341 TYR B CZ     1 
ATOM   7461  O  OH     . TYR B 1 350 ? -30.20600 -4.02600  5.97900   1.000 160.89000 ? 341 TYR B OH     1 
ATOM   7462  N  N      . PHE B 1 351 ? -28.78000 -11.66000 6.28900   1.000 85.26000  ? 342 PHE B N      1 
ATOM   7463  C  CA     . PHE B 1 351 ? -29.99800 -12.45300 6.19400   1.000 102.87000 ? 342 PHE B CA     1 
ATOM   7464  C  C      . PHE B 1 351 ? -29.99500 -13.66700 7.11100   1.000 98.90000  ? 342 PHE B C      1 
ATOM   7465  O  O      . PHE B 1 351 ? -31.00300 -13.94000 7.77000   1.000 89.16000  ? 342 PHE B O      1 
ATOM   7466  C  CB     . PHE B 1 351 ? -30.22200 -12.90200 4.74700   1.000 111.27000 ? 342 PHE B CB     1 
ATOM   7467  C  CG     . PHE B 1 351 ? -30.13200 -11.78400 3.74900   1.000 100.50000 ? 342 PHE B CG     1 
ATOM   7468  C  CD1    . PHE B 1 351 ? -30.94200 -10.66800 3.87100   1.000 97.62000  ? 342 PHE B CD1    1 
ATOM   7469  C  CD2    . PHE B 1 351 ? -29.23800 -11.84600 2.69400   1.000 101.60000 ? 342 PHE B CD2    1 
ATOM   7470  C  CE1    . PHE B 1 351 ? -30.86300 -9.63400  2.95900   1.000 96.73000  ? 342 PHE B CE1    1 
ATOM   7471  C  CE2    . PHE B 1 351 ? -29.15400 -10.81300 1.77800   1.000 118.98000 ? 342 PHE B CE2    1 
ATOM   7472  C  CZ     . PHE B 1 351 ? -29.96800 -9.70600  1.91200   1.000 110.13000 ? 342 PHE B CZ     1 
ATOM   7473  N  N      . TYR B 1 352 ? -28.87800 -14.39800 7.17800   1.000 101.64000 ? 343 TYR B N      1 
ATOM   7474  C  CA     . TYR B 1 352 ? -28.85800 -15.64800 7.92900   1.000 105.93000 ? 343 TYR B CA     1 
ATOM   7475  C  C      . TYR B 1 352 ? -29.20800 -15.42500 9.39400   1.000 107.20000 ? 343 TYR B C      1 
ATOM   7476  O  O      . TYR B 1 352 ? -29.92900 -16.22900 9.99600   1.000 118.28000 ? 343 TYR B O      1 
ATOM   7477  C  CB     . TYR B 1 352 ? -27.48900 -16.31400 7.80200   1.000 111.01000 ? 343 TYR B CB     1 
ATOM   7478  C  CG     . TYR B 1 352 ? -27.53000 -17.80300 8.04300   1.000 130.94000 ? 343 TYR B CG     1 
ATOM   7479  C  CD1    . TYR B 1 352 ? -27.59900 -18.31700 9.33200   1.000 140.70000 ? 343 TYR B CD1    1 
ATOM   7480  C  CD2    . TYR B 1 352 ? -27.50500 -18.69800 6.98100   1.000 121.10000 ? 343 TYR B CD2    1 
ATOM   7481  C  CE1    . TYR B 1 352 ? -27.64200 -19.68000 9.55600   1.000 134.90000 ? 343 TYR B CE1    1 
ATOM   7482  C  CE2    . TYR B 1 352 ? -27.54600 -20.06300 7.19600   1.000 125.15000 ? 343 TYR B CE2    1 
ATOM   7483  C  CZ     . TYR B 1 352 ? -27.61500 -20.54900 8.48600   1.000 129.39000 ? 343 TYR B CZ     1 
ATOM   7484  O  OH     . TYR B 1 352 ? -27.65700 -21.90600 8.70600   1.000 130.97000 ? 343 TYR B OH     1 
ATOM   7485  N  N      . LEU B 1 353 ? -28.72000 -14.33800 9.98300   1.000 104.10000 ? 344 LEU B N      1 
ATOM   7486  C  CA     . LEU B 1 353 ? -28.92200 -14.08000 11.40100  1.000 114.10000 ? 344 LEU B CA     1 
ATOM   7487  C  C      . LEU B 1 353 ? -30.06900 -13.11100 11.66100  1.000 110.59000 ? 344 LEU B C      1 
ATOM   7488  O  O      . LEU B 1 353 ? -30.25200 -12.67200 12.80000  1.000 106.31000 ? 344 LEU B O      1 
ATOM   7489  C  CB     . LEU B 1 353 ? -27.63200 -13.53900 12.02100  1.000 111.42000 ? 344 LEU B CB     1 
ATOM   7490  C  CG     . LEU B 1 353 ? -26.43300 -14.48800 12.02800  1.000 94.17000  ? 344 LEU B CG     1 
ATOM   7491  C  CD1    . LEU B 1 353 ? -25.74600 -14.48800 10.67000  1.000 83.56000  ? 344 LEU B CD1    1 
ATOM   7492  C  CD2    . LEU B 1 353 ? -25.45400 -14.10500 13.12700  1.000 107.54000 ? 344 LEU B CD2    1 
ATOM   7493  N  N      . LYS B 1 354 ? -30.85400 -12.78200 10.63300  1.000 98.45000  ? 345 LYS B N      1 
ATOM   7494  C  CA     . LYS B 1 354 ? -31.94800 -11.83500 10.80400  1.000 95.91000  ? 345 LYS B CA     1 
ATOM   7495  C  C      . LYS B 1 354 ? -33.09600 -12.42300 11.61400  1.000 102.11000 ? 345 LYS B C      1 
ATOM   7496  O  O      . LYS B 1 354 ? -33.74900 -11.69900 12.37400  1.000 99.26000  ? 345 LYS B O      1 
ATOM   7497  C  CB     . LYS B 1 354 ? -32.44600 -11.36500 9.43800   1.000 100.99000 ? 345 LYS B CB     1 
ATOM   7498  N  N      . ASP B 1 355 ? -33.35700 -13.72100 11.47300  1.000 111.89000 ? 346 ASP B N      1 
ATOM   7499  C  CA     . ASP B 1 355 ? -34.49600 -14.34800 12.12800  1.000 121.41000 ? 346 ASP B CA     1 
ATOM   7500  C  C      . ASP B 1 355 ? -34.18900 -14.86000 13.52900  1.000 120.88000 ? 346 ASP B C      1 
ATOM   7501  O  O      . ASP B 1 355 ? -35.12100 -15.24900 14.24100  1.000 108.66000 ? 346 ASP B O      1 
ATOM   7502  C  CB     . ASP B 1 355 ? -35.01600 -15.50700 11.27200  1.000 129.51000 ? 346 ASP B CB     1 
ATOM   7503  C  CG     . ASP B 1 355 ? -35.43900 -15.06100 9.88300   1.000 129.31000 ? 346 ASP B CG     1 
ATOM   7504  O  OD1    . ASP B 1 355 ? -35.63600 -13.84300 9.68000   1.000 121.97000 ? 346 ASP B OD1    1 
ATOM   7505  O  OD2    . ASP B 1 355 ? -35.57100 -15.92900 8.99300   1.000 121.41000 ? 346 ASP B OD2    1 
ATOM   7506  N  N      . LEU B 1 356 ? -32.92300 -14.87100 13.94000  1.000 124.47000 ? 347 LEU B N      1 
ATOM   7507  C  CA     . LEU B 1 356 ? -32.57000 -15.39800 15.25100  1.000 116.44000 ? 347 LEU B CA     1 
ATOM   7508  C  C      . LEU B 1 356 ? -33.18300 -14.54900 16.35900  1.000 107.13000 ? 347 LEU B C      1 
ATOM   7509  O  O      . LEU B 1 356 ? -33.41000 -13.34600 16.20100  1.000 96.10000  ? 347 LEU B O      1 
ATOM   7510  C  CB     . LEU B 1 356 ? -31.05200 -15.45400 15.41400  1.000 117.01000 ? 347 LEU B CB     1 
ATOM   7511  C  CG     . LEU B 1 356 ? -30.38600 -16.73800 14.91900  1.000 113.41000 ? 347 LEU B CG     1 
ATOM   7512  C  CD1    . LEU B 1 356 ? -30.68500 -16.96300 13.44500  1.000 108.93000 ? 347 LEU B CD1    1 
ATOM   7513  C  CD2    . LEU B 1 356 ? -28.88700 -16.70200 15.17400  1.000 122.08000 ? 347 LEU B CD2    1 
ATOM   7514  N  N      . GLN B 1 357 ? -33.44600 -15.19100 17.49500  1.000 103.93000 ? 348 GLN B N      1 
ATOM   7515  C  CA     . GLN B 1 357 ? -34.05800 -14.54300 18.64700  1.000 112.93000 ? 348 GLN B CA     1 
ATOM   7516  C  C      . GLN B 1 357 ? -33.12800 -14.66900 19.84500  1.000 101.00000 ? 348 GLN B C      1 
ATOM   7517  O  O      . GLN B 1 357 ? -32.62200 -15.76000 20.13100  1.000 97.24000  ? 348 GLN B O      1 
ATOM   7518  C  CB     . GLN B 1 357 ? -35.42300 -15.16000 18.96500  1.000 112.03000 ? 348 GLN B CB     1 
ATOM   7519  N  N      . GLY B 1 358 ? -32.91700 -13.56000 20.54400  1.000 108.45000 ? 349 GLY B N      1 
ATOM   7520  C  CA     . GLY B 1 358 ? -32.09400 -13.54400 21.73400  1.000 107.75000 ? 349 GLY B CA     1 
ATOM   7521  C  C      . GLY B 1 358 ? -30.65100 -13.13800 21.52700  1.000 102.99000 ? 349 GLY B C      1 
ATOM   7522  O  O      . GLY B 1 358 ? -29.82600 -13.39100 22.41200  1.000 105.26000 ? 349 GLY B O      1 
ATOM   7523  N  N      . LEU B 1 359 ? -30.32200 -12.50800 20.39700  1.000 94.20000  ? 350 LEU B N      1 
ATOM   7524  C  CA     . LEU B 1 359 ? -28.94100 -12.13200 20.12000  1.000 79.51000  ? 350 LEU B CA     1 
ATOM   7525  C  C      . LEU B 1 359 ? -28.44000 -11.03300 21.04700  1.000 90.48000  ? 350 LEU B C      1 
ATOM   7526  O  O      . LEU B 1 359 ? -27.22400 -10.84900 21.17000  1.000 89.09000  ? 350 LEU B O      1 
ATOM   7527  C  CB     . LEU B 1 359 ? -28.80000 -11.69400 18.66100  1.000 76.12000  ? 350 LEU B CB     1 
ATOM   7528  C  CG     . LEU B 1 359 ? -29.19600 -12.73700 17.61000  1.000 80.99000  ? 350 LEU B CG     1 
ATOM   7529  C  CD1    . LEU B 1 359 ? -29.17700 -12.14000 16.20800  1.000 92.65000  ? 350 LEU B CD1    1 
ATOM   7530  C  CD2    . LEU B 1 359 ? -28.29900 -13.96300 17.68800  1.000 90.91000  ? 350 LEU B CD2    1 
ATOM   7531  N  N      . ASP B 1 360 ? -29.34500 -10.29100 21.68900  1.000 103.96000 ? 351 ASP B N      1 
ATOM   7532  C  CA     . ASP B 1 360 ? -28.92500 -9.27000  22.64300  1.000 103.34000 ? 351 ASP B CA     1 
ATOM   7533  C  C      . ASP B 1 360 ? -28.31300 -9.88900  23.89300  1.000 98.46000  ? 351 ASP B C      1 
ATOM   7534  O  O      . ASP B 1 360 ? -27.50500 -9.24300  24.57000  1.000 102.09000 ? 351 ASP B O      1 
ATOM   7535  C  CB     . ASP B 1 360 ? -30.10900 -8.38000  23.01900  1.000 93.35000  ? 351 ASP B CB     1 
ATOM   7536  C  CG     . ASP B 1 360 ? -31.13200 -9.10200  23.87600  1.000 98.72000  ? 351 ASP B CG     1 
ATOM   7537  O  OD1    . ASP B 1 360 ? -31.67200 -10.13600 23.42600  1.000 96.43000  ? 351 ASP B OD1    1 
ATOM   7538  O  OD2    . ASP B 1 360 ? -31.39700 -8.63100  25.00200  1.000 106.41000 ? 351 ASP B OD2    1 
ATOM   7539  N  N      . VAL B 1 361 ? -28.68200 -11.12900 24.21600  1.000 87.19000  ? 352 VAL B N      1 
ATOM   7540  C  CA     . VAL B 1 361 ? -28.09400 -11.80500 25.36900  1.000 87.13000  ? 352 VAL B CA     1 
ATOM   7541  C  C      . VAL B 1 361 ? -26.67400 -12.26500 25.05500  1.000 99.56000  ? 352 VAL B C      1 
ATOM   7542  O  O      . VAL B 1 361 ? -25.80200 -12.26500 25.93200  1.000 87.78000  ? 352 VAL B O      1 
ATOM   7543  C  CB     . VAL B 1 361 ? -28.99000 -12.97700 25.81100  1.000 72.10000  ? 352 VAL B CB     1 
ATOM   7544  C  CG1    . VAL B 1 361 ? -28.44400 -13.61900 27.07900  1.000 67.52000  ? 352 VAL B CG1    1 
ATOM   7545  C  CG2    . VAL B 1 361 ? -30.42300 -12.50400 26.01600  1.000 79.02000  ? 352 VAL B CG2    1 
ATOM   7546  N  N      . LEU B 1 362 ? -26.42200 -12.67100 23.80700  1.000 103.23000 ? 353 LEU B N      1 
ATOM   7547  C  CA     . LEU B 1 362 ? -25.08000 -13.06800 23.39300  1.000 83.39000  ? 353 LEU B CA     1 
ATOM   7548  C  C      . LEU B 1 362 ? -24.12000 -11.88900 23.30300  1.000 95.86000  ? 353 LEU B C      1 
ATOM   7549  O  O      . LEU B 1 362 ? -22.90300 -12.09200 23.36100  1.000 111.65000 ? 353 LEU B O      1 
ATOM   7550  C  CB     . LEU B 1 362 ? -25.12900 -13.78800 22.04400  1.000 72.20000  ? 353 LEU B CB     1 
ATOM   7551  C  CG     . LEU B 1 362 ? -25.56700 -15.25500 22.05300  1.000 101.80000 ? 353 LEU B CG     1 
ATOM   7552  C  CD1    . LEU B 1 362 ? -27.06300 -15.38400 22.30300  1.000 112.79000 ? 353 LEU B CD1    1 
ATOM   7553  C  CD2    . LEU B 1 362 ? -25.17300 -15.94100 20.75100  1.000 84.35000  ? 353 LEU B CD2    1 
ATOM   7554  N  N      . GLY B 1 363 ? -24.62900 -10.67700 23.14900  1.000 101.86000 ? 354 GLY B N      1 
ATOM   7555  C  CA     . GLY B 1 363 ? -23.80300 -9.50300  23.01400  1.000 92.77000  ? 354 GLY B CA     1 
ATOM   7556  C  C      . GLY B 1 363 ? -23.74200 -8.91500  21.62100  1.000 82.17000  ? 354 GLY B C      1 
ATOM   7557  O  O      . GLY B 1 363 ? -22.78500 -8.19000  21.32000  1.000 87.25000  ? 354 GLY B O      1 
ATOM   7558  N  N      . PHE B 1 364 ? -24.72300 -9.20000  20.76900  1.000 75.52000  ? 355 PHE B N      1 
ATOM   7559  C  CA     . PHE B 1 364 ? -24.74800 -8.67000  19.41200  1.000 81.68000  ? 355 PHE B CA     1 
ATOM   7560  C  C      . PHE B 1 364 ? -25.25500 -7.23400  19.43700  1.000 90.95000  ? 355 PHE B C      1 
ATOM   7561  O  O      . PHE B 1 364 ? -26.39900 -6.97900  19.82800  1.000 80.37000  ? 355 PHE B O      1 
ATOM   7562  C  CB     . PHE B 1 364 ? -25.62400 -9.54200  18.51600  1.000 88.96000  ? 355 PHE B CB     1 
ATOM   7563  C  CG     . PHE B 1 364 ? -24.97200 -10.83100 18.09200  1.000 98.31000  ? 355 PHE B CG     1 
ATOM   7564  C  CD1    . PHE B 1 364 ? -24.47300 -11.71800 19.03200  1.000 97.19000  ? 355 PHE B CD1    1 
ATOM   7565  C  CD2    . PHE B 1 364 ? -24.86700 -11.15900 16.74900  1.000 89.67000  ? 355 PHE B CD2    1 
ATOM   7566  C  CE1    . PHE B 1 364 ? -23.87600 -12.90300 18.64100  1.000 86.43000  ? 355 PHE B CE1    1 
ATOM   7567  C  CE2    . PHE B 1 364 ? -24.27400 -12.34300 16.35300  1.000 69.62000  ? 355 PHE B CE2    1 
ATOM   7568  C  CZ     . PHE B 1 364 ? -23.77800 -13.21500 17.30000  1.000 71.42000  ? 355 PHE B CZ     1 
ATOM   7569  N  N      . ARG B 1 365 ? -24.39600 -6.29800  19.03500  1.000 109.99000 ? 356 ARG B N      1 
ATOM   7570  C  CA     . ARG B 1 365 ? -24.73700 -4.88300  18.98700  1.000 105.97000 ? 356 ARG B CA     1 
ATOM   7571  C  C      . ARG B 1 365 ? -25.40700 -4.48100  17.67900  1.000 103.65000 ? 356 ARG B C      1 
ATOM   7572  O  O      . ARG B 1 365 ? -25.73700 -3.30400  17.50700  1.000 97.36000  ? 356 ARG B O      1 
ATOM   7573  C  CB     . ARG B 1 365 ? -23.47800 -4.03100  19.18700  1.000 106.05000 ? 356 ARG B CB     1 
ATOM   7574  C  CG     . ARG B 1 365 ? -22.82600 -4.15400  20.55700  1.000 97.52000  ? 356 ARG B CG     1 
ATOM   7575  C  CD     . ARG B 1 365 ? -23.51400 -3.29400  21.60100  1.000 105.05000 ? 356 ARG B CD     1 
ATOM   7576  N  NE     . ARG B 1 365 ? -22.77400 -3.28200  22.85800  1.000 104.22000 ? 356 ARG B NE     1 
ATOM   7577  C  CZ     . ARG B 1 365 ? -23.26300 -2.84800  24.01200  1.000 141.50000 ? 356 ARG B CZ     1 
ATOM   7578  N  NH1    . ARG B 1 365 ? -24.49800 -2.38400  24.10900  1.000 154.98000 ? 356 ARG B NH1    1 
ATOM   7579  N  NH2    . ARG B 1 365 ? -22.49300 -2.88100  25.09600  1.000 150.55000 ? 356 ARG B NH2    1 
ATOM   7580  N  N      . PHE B 1 366 ? -25.60300 -5.42100  16.75100  1.000 115.96000 ? 357 PHE B N      1 
ATOM   7581  C  CA     . PHE B 1 366 ? -26.25300 -5.11600  15.48400  1.000 114.77000 ? 357 PHE B CA     1 
ATOM   7582  C  C      . PHE B 1 366 ? -27.26900 -6.15900  15.04200  1.000 99.82000  ? 357 PHE B C      1 
ATOM   7583  O  O      . PHE B 1 366 ? -27.80900 -6.03300  13.93900  1.000 98.11000  ? 357 PHE B O      1 
ATOM   7584  C  CB     . PHE B 1 366 ? -25.20500 -4.94300  14.36800  1.000 118.65000 ? 357 PHE B CB     1 
ATOM   7585  C  CG     . PHE B 1 366 ? -24.36000 -3.70800  14.50900  1.000 115.90000 ? 357 PHE B CG     1 
ATOM   7586  C  CD1    . PHE B 1 366 ? -24.90900 -2.45100  14.31300  1.000 113.16000 ? 357 PHE B CD1    1 
ATOM   7587  C  CD2    . PHE B 1 366 ? -23.01500 -3.80300  14.82400  1.000 109.01000 ? 357 PHE B CD2    1 
ATOM   7588  C  CE1    . PHE B 1 366 ? -24.13400 -1.31300  14.43800  1.000 112.68000 ? 357 PHE B CE1    1 
ATOM   7589  C  CE2    . PHE B 1 366 ? -22.23700 -2.66800  14.94900  1.000 114.87000 ? 357 PHE B CE2    1 
ATOM   7590  C  CZ     . PHE B 1 366 ? -22.79600 -1.42200  14.75600  1.000 109.11000 ? 357 PHE B CZ     1 
ATOM   7591  N  N      . GLY B 1 367 ? -27.55000 -7.17800  15.84900  1.000 100.76000 ? 358 GLY B N      1 
ATOM   7592  C  CA     . GLY B 1 367 ? -28.52400 -8.17100  15.44700  1.000 81.14000  ? 358 GLY B CA     1 
ATOM   7593  C  C      . GLY B 1 367 ? -27.92900 -9.16100  14.46900  1.000 82.17000  ? 358 GLY B C      1 
ATOM   7594  O  O      . GLY B 1 367 ? -27.06900 -9.97100  14.83100  1.000 98.22000  ? 358 GLY B O      1 
ATOM   7595  N  N      . ALA B 1 368 ? -28.38900 -9.10400  13.21800  1.000 72.52000  ? 359 ALA B N      1 
ATOM   7596  C  CA     . ALA B 1 368 ? -27.96000 -10.07500 12.21700  1.000 91.87000  ? 359 ALA B CA     1 
ATOM   7597  C  C      . ALA B 1 368 ? -26.53900 -9.78900  11.73800  1.000 92.53000  ? 359 ALA B C      1 
ATOM   7598  O  O      . ALA B 1 368 ? -25.69900 -10.69400 11.68500  1.000 87.25000  ? 359 ALA B O      1 
ATOM   7599  C  CB     . ALA B 1 368 ? -28.93700 -10.08200 11.04100  1.000 97.30000  ? 359 ALA B CB     1 
ATOM   7600  N  N      . ILE B 1 369 ? -26.25600 -8.53300  11.37200  1.000 78.37000  ? 360 ILE B N      1 
ATOM   7601  C  CA     . ILE B 1 369 ? -24.97100 -8.18200  10.76700  1.000 82.96000  ? 360 ILE B CA     1 
ATOM   7602  C  C      . ILE B 1 369 ? -23.86000 -7.98000  11.78300  1.000 100.91000 ? 360 ILE B C      1 
ATOM   7603  O  O      . ILE B 1 369 ? -22.71800 -7.70800  11.38700  1.000 102.60000 ? 360 ILE B O      1 
ATOM   7604  C  CB     . ILE B 1 369 ? -25.09800 -6.90200  9.91700   1.000 73.16000  ? 360 ILE B CB     1 
ATOM   7605  C  CG1    . ILE B 1 369 ? -23.90300 -6.76100  8.97000   1.000 85.17000  ? 360 ILE B CG1    1 
ATOM   7606  C  CG2    . ILE B 1 369 ? -25.20800 -5.68100  10.81500  1.000 71.71000  ? 360 ILE B CG2    1 
ATOM   7607  C  CD1    . ILE B 1 369 ? -23.89300 -7.77000  7.83700   1.000 95.90000  ? 360 ILE B CD1    1 
ATOM   7608  N  N      . SER B 1 370 ? -24.15200 -8.09800  13.07600  1.000 93.00000  ? 361 SER B N      1 
ATOM   7609  C  CA     . SER B 1 370 ? -23.16900 -7.85800  14.12500  1.000 85.32000  ? 361 SER B CA     1 
ATOM   7610  C  C      . SER B 1 370 ? -21.85900 -8.58900  13.84600  1.000 81.30000  ? 361 SER B C      1 
ATOM   7611  O  O      . SER B 1 370 ? -20.81100 -7.94400  13.69900  1.000 89.38000  ? 361 SER B O      1 
ATOM   7612  C  CB     . SER B 1 370 ? -23.73100 -8.28000  15.48400  1.000 81.28000  ? 361 SER B CB     1 
ATOM   7613  O  OG     . SER B 1 370 ? -22.90000 -7.82900  16.53900  1.000 100.72000 ? 361 SER B OG     1 
ATOM   7614  N  N      . PRO B 1 371 ? -21.87000 -9.92200  13.75400  1.000 64.31000  ? 362 PRO B N      1 
ATOM   7615  C  CA     . PRO B 1 371 ? -20.60000 -10.64500 13.58100  1.000 70.15000  ? 362 PRO B CA     1 
ATOM   7616  C  C      . PRO B 1 371 ? -19.87000 -10.28900 12.30100  1.000 85.79000  ? 362 PRO B C      1 
ATOM   7617  O  O      . PRO B 1 371 ? -18.64300 -10.43900 12.24200  1.000 88.58000  ? 362 PRO B O      1 
ATOM   7618  C  CB     . PRO B 1 371 ? -21.03000 -12.11700 13.59400  1.000 61.00000  ? 362 PRO B CB     1 
ATOM   7619  C  CG     . PRO B 1 371 ? -22.44000 -12.10000 13.13300  1.000 68.01000  ? 362 PRO B CG     1 
ATOM   7620  C  CD     . PRO B 1 371 ? -23.03600 -10.81300 13.63500  1.000 80.61000  ? 362 PRO B CD     1 
ATOM   7621  N  N      . TRP B 1 372 ? -20.58400 -9.83800  11.26700  1.000 80.42000  ? 363 TRP B N      1 
ATOM   7622  C  CA     . TRP B 1 372 ? -19.92200 -9.45700  10.02300  1.000 86.46000  ? 363 TRP B CA     1 
ATOM   7623  C  C      . TRP B 1 372 ? -18.89000 -8.36000  10.26000  1.000 80.09000  ? 363 TRP B C      1 
ATOM   7624  O  O      . TRP B 1 372 ? -17.80300 -8.37800  9.66700   1.000 82.71000  ? 363 TRP B O      1 
ATOM   7625  C  CB     . TRP B 1 372 ? -20.96100 -9.00600  8.99700   1.000 76.72000  ? 363 TRP B CB     1 
ATOM   7626  C  CG     . TRP B 1 372 ? -20.36700 -8.57100  7.69800   1.000 85.66000  ? 363 TRP B CG     1 
ATOM   7627  C  CD1    . TRP B 1 372 ? -19.88900 -9.37800  6.70700   1.000 95.36000  ? 363 TRP B CD1    1 
ATOM   7628  C  CD2    . TRP B 1 372 ? -20.17000 -7.22500  7.25000   1.000 90.38000  ? 363 TRP B CD2    1 
ATOM   7629  N  NE1    . TRP B 1 372 ? -19.41800 -8.61800  5.66400   1.000 101.37000 ? 363 TRP B NE1    1 
ATOM   7630  C  CE2    . TRP B 1 372 ? -19.57700 -7.29300  5.97300   1.000 93.05000  ? 363 TRP B CE2    1 
ATOM   7631  C  CE3    . TRP B 1 372 ? -20.44000 -5.96900  7.80200   1.000 90.80000  ? 363 TRP B CE3    1 
ATOM   7632  C  CZ2    . TRP B 1 372 ? -19.25100 -6.15500  5.24000   1.000 92.73000  ? 363 TRP B CZ2    1 
ATOM   7633  C  CZ3    . TRP B 1 372 ? -20.11500 -4.84000  7.07100   1.000 86.45000  ? 363 TRP B CZ3    1 
ATOM   7634  C  CH2    . TRP B 1 372 ? -19.52700 -4.94100  5.80400   1.000 88.82000  ? 363 TRP B CH2    1 
ATOM   7635  N  N      . PHE B 1 373 ? -19.22500 -7.37700  11.09700  1.000 73.25000  ? 364 PHE B N      1 
ATOM   7636  C  CA     . PHE B 1 373 ? -18.25600 -6.34800  11.45800  1.000 79.08000  ? 364 PHE B CA     1 
ATOM   7637  C  C      . PHE B 1 373 ? -17.01700 -6.95700  12.09600  1.000 77.59000  ? 364 PHE B C      1 
ATOM   7638  O  O      . PHE B 1 373 ? -15.88700 -6.58900  11.75600  1.000 74.34000  ? 364 PHE B O      1 
ATOM   7639  C  CB     . PHE B 1 373 ? -18.89900 -5.32300  12.38900  1.000 80.62000  ? 364 PHE B CB     1 
ATOM   7640  C  CG     . PHE B 1 373 ? -19.86000 -4.41400  11.69700  1.000 79.01000  ? 364 PHE B CG     1 
ATOM   7641  C  CD1    . PHE B 1 373 ? -19.39800 -3.33200  10.96900  1.000 81.04000  ? 364 PHE B CD1    1 
ATOM   7642  C  CD2    . PHE B 1 373 ? -21.22100 -4.64900  11.75400  1.000 77.42000  ? 364 PHE B CD2    1 
ATOM   7643  C  CE1    . PHE B 1 373 ? -20.27400 -2.49300  10.32100  1.000 73.96000  ? 364 PHE B CE1    1 
ATOM   7644  C  CE2    . PHE B 1 373 ? -22.10500 -3.81200  11.10600  1.000 91.26000  ? 364 PHE B CE2    1 
ATOM   7645  C  CZ     . PHE B 1 373 ? -21.63000 -2.73200  10.38800  1.000 86.79000  ? 364 PHE B CZ     1 
ATOM   7646  N  N      . SER B 1 374 ? -17.21100 -7.84500  13.07400  1.000 71.83000  ? 365 SER B N      1 
ATOM   7647  C  CA     . SER B 1 374 ? -16.08000 -8.54300  13.67600  1.000 76.48000  ? 365 SER B CA     1 
ATOM   7648  C  C      . SER B 1 374 ? -15.22100 -9.19900  12.60500  1.000 82.06000  ? 365 SER B C      1 
ATOM   7649  O  O      . SER B 1 374 ? -13.99000 -9.09100  12.61700  1.000 83.85000  ? 365 SER B O      1 
ATOM   7650  C  CB     . SER B 1 374 ? -16.58300 -9.58700  14.67400  1.000 73.68000  ? 365 SER B CB     1 
ATOM   7651  O  OG     . SER B 1 374 ? -17.46700 -9.01000  15.61800  1.000 80.00000  ? 365 SER B OG     1 
ATOM   7652  N  N      . ALA B 1 375 ? -15.86700 -9.90100  11.67500  1.000 76.13000  ? 366 ALA B N      1 
ATOM   7653  C  CA     . ALA B 1 375 ? -15.15000 -10.57800 10.60000  1.000 69.11000  ? 366 ALA B CA     1 
ATOM   7654  C  C      . ALA B 1 375 ? -14.30300 -9.60100  9.79400   1.000 77.77000  ? 366 ALA B C      1 
ATOM   7655  O  O      . ALA B 1 375 ? -13.11400 -9.84000  9.55100   1.000 86.75000  ? 366 ALA B O      1 
ATOM   7656  C  CB     . ALA B 1 375 ? -16.14500 -11.29700 9.69600   1.000 64.95000  ? 366 ALA B CB     1 
ATOM   7657  N  N      . ILE B 1 376 ? -14.91100 -8.50200  9.34700   1.000 66.52000  ? 367 ILE B N      1 
ATOM   7658  C  CA     . ILE B 1 376 ? -14.19200 -7.55800  8.49700   1.000 68.57000  ? 367 ILE B CA     1 
ATOM   7659  C  C      . ILE B 1 376 ? -13.05100 -6.90000  9.26200   1.000 71.19000  ? 367 ILE B C      1 
ATOM   7660  O  O      . ILE B 1 376 ? -11.96500 -6.66800  8.71000   1.000 86.60000  ? 367 ILE B O      1 
ATOM   7661  C  CB     . ILE B 1 376 ? -15.16400 -6.51200  7.92300   1.000 88.47000  ? 367 ILE B CB     1 
ATOM   7662  C  CG1    . ILE B 1 376 ? -15.76000 -5.66300  9.04700   1.000 78.34000  ? 367 ILE B CG1    1 
ATOM   7663  C  CG2    . ILE B 1 376 ? -16.27100 -7.19200  7.12800   1.000 95.68000  ? 367 ILE B CG2    1 
ATOM   7664  C  CD1    . ILE B 1 376 ? -16.54800 -4.47100  8.55800   1.000 84.68000  ? 367 ILE B CD1    1 
ATOM   7665  N  N      . ILE B 1 377 ? -13.27900 -6.56700  10.53500  1.000 67.62000  ? 368 ILE B N      1 
ATOM   7666  C  CA     . ILE B 1 377 ? -12.21800 -5.96500  11.33300  1.000 73.25000  ? 368 ILE B CA     1 
ATOM   7667  C  C      . ILE B 1 377 ? -11.08200 -6.95600  11.54400  1.000 61.57000  ? 368 ILE B C      1 
ATOM   7668  O  O      . ILE B 1 377 ? -9.91000  -6.56900  11.55400  1.000 43.27000  ? 368 ILE B O      1 
ATOM   7669  C  CB     . ILE B 1 377 ? -12.77700 -5.42900  12.66400  1.000 63.89000  ? 368 ILE B CB     1 
ATOM   7670  C  CG1    . ILE B 1 377 ? -13.10500 -6.57300  13.62100  1.000 80.14000  ? 368 ILE B CG1    1 
ATOM   7671  C  CG2    . ILE B 1 377 ? -14.00400 -4.56500  12.41500  1.000 72.31000  ? 368 ILE B CG2    1 
ATOM   7672  C  CD1    . ILE B 1 377 ? -13.28200 -6.11800  15.04700  1.000 77.75000  ? 368 ILE B CD1    1 
ATOM   7673  N  N      . GLY B 1 378 ? -11.39400 -8.24700  11.65400  1.000 49.35000  ? 369 GLY B N      1 
ATOM   7674  C  CA     . GLY B 1 378 ? -10.33900 -9.24500  11.69900  1.000 60.28000  ? 369 GLY B CA     1 
ATOM   7675  C  C      . GLY B 1 378 ? -9.56700  -9.29600  10.39600  1.000 70.82000  ? 369 GLY B C      1 
ATOM   7676  O  O      . GLY B 1 378 ? -8.34000  -9.43900  10.39100  1.000 68.04000  ? 369 GLY B O      1 
ATOM   7677  N  N      . ILE B 1 379 ? -10.28100 -9.22400  9.27300   1.000 75.01000  ? 370 ILE B N      1 
ATOM   7678  C  CA     . ILE B 1 379 ? -9.62800  -9.21000  7.96500   1.000 73.78000  ? 370 ILE B CA     1 
ATOM   7679  C  C      . ILE B 1 379 ? -8.60600  -8.08100  7.91300   1.000 71.97000  ? 370 ILE B C      1 
ATOM   7680  O  O      . ILE B 1 379 ? -7.41700  -8.29300  7.63000   1.000 71.27000  ? 370 ILE B O      1 
ATOM   7681  C  CB     . ILE B 1 379 ? -10.67200 -9.06700  6.84400   1.000 67.66000  ? 370 ILE B CB     1 
ATOM   7682  C  CG1    . ILE B 1 379 ? -11.67900 -10.21600 6.89900   1.000 89.58000  ? 370 ILE B CG1    1 
ATOM   7683  C  CG2    . ILE B 1 379 ? -9.99500  -9.02300  5.48400   1.000 78.18000  ? 370 ILE B CG2    1 
ATOM   7684  C  CD1    . ILE B 1 379 ? -12.91600 -9.98000  6.06200   1.000 101.95000 ? 370 ILE B CD1    1 
ATOM   7685  N  N      . PHE B 1 380 ? -9.07300  -6.85300  8.15800   1.000 74.31000  ? 371 PHE B N      1 
ATOM   7686  C  CA     . PHE B 1 380 ? -8.17800  -5.69900  8.12500   1.000 71.96000  ? 371 PHE B CA     1 
ATOM   7687  C  C      . PHE B 1 380 ? -7.08200  -5.80200  9.17700   1.000 77.26000  ? 371 PHE B C      1 
ATOM   7688  O  O      . PHE B 1 380 ? -5.97500  -5.29600  8.96700   1.000 62.55000  ? 371 PHE B O      1 
ATOM   7689  C  CB     . PHE B 1 380 ? -8.96900  -4.40700  8.31100   1.000 57.41000  ? 371 PHE B CB     1 
ATOM   7690  C  CG     . PHE B 1 380 ? -10.14000 -4.28200  7.38800   1.000 79.09000  ? 371 PHE B CG     1 
ATOM   7691  C  CD1    . PHE B 1 380 ? -10.00300 -4.55300  6.03700   1.000 86.88000  ? 371 PHE B CD1    1 
ATOM   7692  C  CD2    . PHE B 1 380 ? -11.37900 -3.89200  7.86700   1.000 87.59000  ? 371 PHE B CD2    1 
ATOM   7693  C  CE1    . PHE B 1 380 ? -11.08000 -4.44200  5.18200   1.000 98.16000  ? 371 PHE B CE1    1 
ATOM   7694  C  CE2    . PHE B 1 380 ? -12.46000 -3.77800  7.01700   1.000 95.22000  ? 371 PHE B CE2    1 
ATOM   7695  C  CZ     . PHE B 1 380 ? -12.31000 -4.05300  5.67300   1.000 119.58000 ? 371 PHE B CZ     1 
ATOM   7696  N  N      . SER B 1 381 ? -7.35300  -6.47400  10.29700  1.000 77.53000  ? 372 SER B N      1 
ATOM   7697  C  CA     . SER B 1 381 ? -6.31400  -6.69900  11.29300  1.000 63.86000  ? 372 SER B CA     1 
ATOM   7698  C  C      . SER B 1 381 ? -5.20200  -7.55700  10.71200  1.000 63.79000  ? 372 SER B C      1 
ATOM   7699  O  O      . SER B 1 381 ? -4.01700  -7.24600  10.86400  1.000 73.29000  ? 372 SER B O      1 
ATOM   7700  C  CB     . SER B 1 381 ? -6.91400  -7.35700  12.53500  1.000 65.14000  ? 372 SER B CB     1 
ATOM   7701  O  OG     . SER B 1 381 ? -7.88300  -6.51700  13.13800  1.000 53.19000  ? 372 SER B OG     1 
ATOM   7702  N  N      . GLY B 1 382 ? -5.57100  -8.67500  10.08800  1.000 49.66000  ? 373 GLY B N      1 
ATOM   7703  C  CA     . GLY B 1 382 ? -4.57500  -9.51400  9.44100   1.000 62.84000  ? 373 GLY B CA     1 
ATOM   7704  C  C      . GLY B 1 382 ? -3.77800  -8.75000  8.40100   1.000 73.10000  ? 373 GLY B C      1 
ATOM   7705  O  O      . GLY B 1 382 ? -2.54800  -8.83500  8.34700   1.000 73.99000  ? 373 GLY B O      1 
ATOM   7706  N  N      . ILE B 1 383 ? -4.48100  -8.02300  7.53200   1.000 61.71000  ? 374 ILE B N      1 
ATOM   7707  C  CA     . ILE B 1 383 ? -3.81200  -7.19600  6.52700   1.000 60.46000  ? 374 ILE B CA     1 
ATOM   7708  C  C      . ILE B 1 383 ? -2.78300  -6.28200  7.18300   1.000 66.38000  ? 374 ILE B C      1 
ATOM   7709  O  O      . ILE B 1 383 ? -1.61400  -6.22700  6.77600   1.000 74.02000  ? 374 ILE B O      1 
ATOM   7710  C  CB     . ILE B 1 383 ? -4.85000  -6.39500  5.72400   1.000 70.01000  ? 374 ILE B CB     1 
ATOM   7711  C  CG1    . ILE B 1 383 ? -5.73100  -7.35000  4.91700   1.000 58.27000  ? 374 ILE B CG1    1 
ATOM   7712  C  CG2    . ILE B 1 383 ? -4.16000  -5.38500  4.81800   1.000 63.74000  ? 374 ILE B CG2    1 
ATOM   7713  C  CD1    . ILE B 1 383 ? -7.10100  -6.80500  4.60500   1.000 67.94000  ? 374 ILE B CD1    1 
ATOM   7714  N  N      . LEU B 1 384 ? -3.21900  -5.52200  8.19000   1.000 69.71000  ? 375 LEU B N      1 
ATOM   7715  C  CA     . LEU B 1 384 ? -2.33700  -4.57300  8.85800   1.000 70.84000  ? 375 LEU B CA     1 
ATOM   7716  C  C      . LEU B 1 384 ? -1.13800  -5.26400  9.49400   1.000 78.88000  ? 375 LEU B C      1 
ATOM   7717  O  O      . LEU B 1 384 ? -0.01800  -4.74900  9.43000   1.000 66.87000  ? 375 LEU B O      1 
ATOM   7718  C  CB     . LEU B 1 384 ? -3.11700  -3.78200  9.90500   1.000 63.86000  ? 375 LEU B CB     1 
ATOM   7719  C  CG     . LEU B 1 384 ? -4.12500  -2.79800  9.31800   1.000 89.60000  ? 375 LEU B CG     1 
ATOM   7720  C  CD1    . LEU B 1 384 ? -4.70300  -1.90800  10.40600  1.000 116.88000 ? 375 LEU B CD1    1 
ATOM   7721  C  CD2    . LEU B 1 384 ? -3.47800  -1.97000  8.21700   1.000 102.43000 ? 375 LEU B CD2    1 
ATOM   7722  N  N      . ILE B 1 385 ? -1.35800  -6.39000  10.17500  1.000 84.50000  ? 376 ILE B N      1 
ATOM   7723  C  CA     . ILE B 1 385 ? -0.24100  -7.09100  10.80700  1.000 85.20000  ? 376 ILE B CA     1 
ATOM   7724  C  C      . ILE B 1 385 ? 0.75400   -7.55200  9.75100   1.000 88.17000  ? 376 ILE B C      1 
ATOM   7725  O  O      . ILE B 1 385 ? 1.97400   -7.51100  9.96300   1.000 101.24000 ? 376 ILE B O      1 
ATOM   7726  C  CB     . ILE B 1 385 ? -0.74100  -8.26600  11.66800  1.000 76.83000  ? 376 ILE B CB     1 
ATOM   7727  C  CG1    . ILE B 1 385 ? -1.32900  -9.36600  10.78800  1.000 78.57000  ? 376 ILE B CG1    1 
ATOM   7728  C  CG2    . ILE B 1 385 ? -1.76900  -7.78100  12.68100  1.000 61.77000  ? 376 ILE B CG2    1 
ATOM   7729  C  CD1    . ILE B 1 385 ? -1.52300  -10.67800 11.51000  1.000 91.29000  ? 376 ILE B CD1    1 
ATOM   7730  N  N      . GLY B 1 386 ? 0.25100   -8.04800  8.61900   1.000 68.97000  ? 377 GLY B N      1 
ATOM   7731  C  CA     . GLY B 1 386 ? 1.13600   -8.36500  7.51100   1.000 73.16000  ? 377 GLY B CA     1 
ATOM   7732  C  C      . GLY B 1 386 ? 1.98200   -7.17400  7.10600   1.000 80.32000  ? 377 GLY B C      1 
ATOM   7733  O  O      . GLY B 1 386 ? 3.20500   -7.27600  6.96300   1.000 82.09000  ? 377 GLY B O      1 
ATOM   7734  N  N      . PHE B 1 387 ? 1.32700   -6.03400  6.87300   1.000 83.66000  ? 378 PHE B N      1 
ATOM   7735  C  CA     . PHE B 1 387 ? 2.05400   -4.81300  6.53500   1.000 86.32000  ? 378 PHE B CA     1 
ATOM   7736  C  C      . PHE B 1 387 ? 3.10300   -4.48100  7.59500   1.000 98.13000  ? 378 PHE B C      1 
ATOM   7737  O  O      . PHE B 1 387 ? 4.19900   -4.01400  7.26900   1.000 113.09000 ? 378 PHE B O      1 
ATOM   7738  C  CB     . PHE B 1 387 ? 1.07600   -3.65200  6.35300   1.000 88.29000  ? 378 PHE B CB     1 
ATOM   7739  N  N      . TRP B 1 388 ? 2.76900   -4.68600  8.87200   1.000 97.17000  ? 379 TRP B N      1 
ATOM   7740  C  CA     . TRP B 1 388 ? 3.70200   -4.39400  9.96000   1.000 79.87000  ? 379 TRP B CA     1 
ATOM   7741  C  C      . TRP B 1 388 ? 4.94400   -5.26800  9.86200   1.000 73.50000  ? 379 TRP B C      1 
ATOM   7742  O  O      . TRP B 1 388 ? 6.08200   -4.78200  9.96100   1.000 81.72000  ? 379 TRP B O      1 
ATOM   7743  C  CB     . TRP B 1 388 ? 3.01700   -4.61400  11.30800  1.000 72.43000  ? 379 TRP B CB     1 
ATOM   7744  C  CG     . TRP B 1 388 ? 2.28300   -3.43100  11.80900  1.000 62.35000  ? 379 TRP B CG     1 
ATOM   7745  C  CD1    . TRP B 1 388 ? 0.94600   -3.34500  12.06500  1.000 68.76000  ? 379 TRP B CD1    1 
ATOM   7746  C  CD2    . TRP B 1 388 ? 2.83600   -2.15000  12.12000  1.000 53.27000  ? 379 TRP B CD2    1 
ATOM   7747  N  NE1    . TRP B 1 388 ? 0.63100   -2.08700  12.51800  1.000 81.31000  ? 379 TRP B NE1    1 
ATOM   7748  C  CE2    . TRP B 1 388 ? 1.77500   -1.33400  12.56100  1.000 73.69000  ? 379 TRP B CE2    1 
ATOM   7749  C  CE3    . TRP B 1 388 ? 4.12500   -1.61300  12.06800  1.000 60.17000  ? 379 TRP B CE3    1 
ATOM   7750  C  CZ2    . TRP B 1 388 ? 1.96300   -0.00900  12.94700  1.000 86.76000  ? 379 TRP B CZ2    1 
ATOM   7751  C  CZ3    . TRP B 1 388 ? 4.31000   -0.29700  12.45300  1.000 87.69000  ? 379 TRP B CZ3    1 
ATOM   7752  C  CH2    . TRP B 1 388 ? 3.23500   0.49000   12.88600  1.000 104.07000 ? 379 TRP B CH2    1 
ATOM   7753  N  N      . ALA B 1 389 ? 4.73300   -6.57800  9.73000   1.000 64.08000  ? 380 ALA B N      1 
ATOM   7754  C  CA     . ALA B 1 389 ? 5.84400   -7.49600  9.51600   1.000 72.24000  ? 380 ALA B CA     1 
ATOM   7755  C  C      . ALA B 1 389 ? 6.70600   -7.02400  8.35300   1.000 86.24000  ? 380 ALA B C      1 
ATOM   7756  O  O      . ALA B 1 389 ? 7.93900   -6.99400  8.44600   1.000 93.47000  ? 380 ALA B O      1 
ATOM   7757  C  CB     . ALA B 1 389 ? 5.31700   -8.91100  9.27100   1.000 80.53000  ? 380 ALA B CB     1 
ATOM   7758  N  N      . GLU B 1 390 ? 6.06500   -6.67300  7.23500   1.000 83.46000  ? 381 GLU B N      1 
ATOM   7759  C  CA     . GLU B 1 390 ? 6.80200   -6.16400  6.08200   1.000 83.23000  ? 381 GLU B CA     1 
ATOM   7760  C  C      . GLU B 1 390 ? 7.68300   -4.98200  6.47500   1.000 96.59000  ? 381 GLU B C      1 
ATOM   7761  O  O      . GLU B 1 390 ? 8.88600   -4.96300  6.19000   1.000 111.70000 ? 381 GLU B O      1 
ATOM   7762  C  CB     . GLU B 1 390 ? 5.82900   -5.76700  4.97000   1.000 74.21000  ? 381 GLU B CB     1 
ATOM   7763  N  N      . TYR B 1 391 ? 7.08700   -3.97900  7.12600   1.000 101.50000 ? 382 TYR B N      1 
ATOM   7764  C  CA     . TYR B 1 391 ? 7.82800   -2.77200  7.48600   1.000 93.94000  ? 382 TYR B CA     1 
ATOM   7765  C  C      . TYR B 1 391 ? 9.04400   -3.09500  8.34100   1.000 93.11000  ? 382 TYR B C      1 
ATOM   7766  O  O      . TYR B 1 391 ? 10.11400  -2.50200  8.16200   1.000 103.77000 ? 382 TYR B O      1 
ATOM   7767  C  CB     . TYR B 1 391 ? 6.92200   -1.78300  8.22100   1.000 82.83000  ? 382 TYR B CB     1 
ATOM   7768  C  CG     . TYR B 1 391 ? 7.67600   -0.62100  8.83700   1.000 74.96000  ? 382 TYR B CG     1 
ATOM   7769  C  CD1    . TYR B 1 391 ? 8.24000   0.36700   8.04100   1.000 91.54000  ? 382 TYR B CD1    1 
ATOM   7770  C  CD2    . TYR B 1 391 ? 7.83000   -0.51700  10.21400  1.000 81.54000  ? 382 TYR B CD2    1 
ATOM   7771  C  CE1    . TYR B 1 391 ? 8.93000   1.43000   8.59700   1.000 107.87000 ? 382 TYR B CE1    1 
ATOM   7772  C  CE2    . TYR B 1 391 ? 8.52000   0.54300   10.78000  1.000 83.50000  ? 382 TYR B CE2    1 
ATOM   7773  C  CZ     . TYR B 1 391 ? 9.06800   1.51300   9.96600   1.000 101.01000 ? 382 TYR B CZ     1 
ATOM   7774  O  OH     . TYR B 1 391 ? 9.75500   2.57100   10.51800  1.000 104.26000 ? 382 TYR B OH     1 
ATOM   7775  N  N      . TYR B 1 392 ? 8.90200   -4.02900  9.27900   1.000 82.63000  ? 383 TYR B N      1 
ATOM   7776  C  CA     . TYR B 1 392 ? 9.99700   -4.30600  10.20200  1.000 76.81000  ? 383 TYR B CA     1 
ATOM   7777  C  C      . TYR B 1 392 ? 11.00300  -5.33300  9.68600   1.000 78.54000  ? 383 TYR B C      1 
ATOM   7778  O  O      . TYR B 1 392 ? 12.08900  -5.44900  10.26400  1.000 74.08000  ? 383 TYR B O      1 
ATOM   7779  C  CB     . TYR B 1 392 ? 9.44700   -4.76500  11.55900  1.000 63.47000  ? 383 TYR B CB     1 
ATOM   7780  C  CG     . TYR B 1 392 ? 9.05700   -3.63000  12.48300  1.000 58.50000  ? 383 TYR B CG     1 
ATOM   7781  C  CD1    . TYR B 1 392 ? 10.01300  -2.97900  13.25100  1.000 67.62000  ? 383 TYR B CD1    1 
ATOM   7782  C  CD2    . TYR B 1 392 ? 7.73800   -3.20800  12.58500  1.000 78.31000  ? 383 TYR B CD2    1 
ATOM   7783  C  CE1    . TYR B 1 392 ? 9.66600   -1.94000  14.09900  1.000 73.42000  ? 383 TYR B CE1    1 
ATOM   7784  C  CE2    . TYR B 1 392 ? 7.38000   -2.16800  13.43100  1.000 65.67000  ? 383 TYR B CE2    1 
ATOM   7785  C  CZ     . TYR B 1 392 ? 8.34900   -1.54000  14.18400  1.000 62.95000  ? 383 TYR B CZ     1 
ATOM   7786  O  OH     . TYR B 1 392 ? 8.00000   -0.50800  15.02500  1.000 85.88000  ? 383 TYR B OH     1 
ATOM   7787  N  N      . THR B 1 393 ? 10.69100  -6.07000  8.62000   1.000 92.43000  ? 384 THR B N      1 
ATOM   7788  C  CA     . THR B 1 393 ? 11.54700  -7.16600  8.18000   1.000 91.15000  ? 384 THR B CA     1 
ATOM   7789  C  C      . THR B 1 393 ? 12.15400  -6.97500  6.79600   1.000 111.55000 ? 384 THR B C      1 
ATOM   7790  O  O      . THR B 1 393 ? 12.86400  -7.87300  6.32500   1.000 103.36000 ? 384 THR B O      1 
ATOM   7791  C  CB     . THR B 1 393 ? 10.77200  -8.49100  8.20300   1.000 82.05000  ? 384 THR B CB     1 
ATOM   7792  O  OG1    . THR B 1 393 ? 11.69500  -9.58600  8.23600   1.000 95.38000  ? 384 THR B OG1    1 
ATOM   7793  C  CG2    . THR B 1 393 ? 9.89400   -8.61700  6.96800   1.000 82.66000  ? 384 THR B CG2    1 
ATOM   7794  N  N      . SER B 1 394 ? 11.91800  -5.84400  6.13700   1.000 117.51000 ? 385 SER B N      1 
ATOM   7795  C  CA     . SER B 1 394 ? 12.34500  -5.63900  4.76100   1.000 113.97000 ? 385 SER B CA     1 
ATOM   7796  C  C      . SER B 1 394 ? 13.37300  -4.51900  4.67300   1.000 115.72000 ? 385 SER B C      1 
ATOM   7797  O  O      . SER B 1 394 ? 13.38600  -3.59600  5.49300   1.000 122.22000 ? 385 SER B O      1 
ATOM   7798  C  CB     . SER B 1 394 ? 11.15100  -5.31100  3.85500   1.000 114.84000 ? 385 SER B CB     1 
ATOM   7799  O  OG     . SER B 1 394 ? 10.47400  -4.15300  4.31000   1.000 124.60000 ? 385 SER B OG     1 
ATOM   7800  N  N      . TYR B 1 395 ? 14.24100  -4.61800  3.66200   1.000 120.39000 ? 386 TYR B N      1 
ATOM   7801  C  CA     . TYR B 1 395 ? 15.27400  -3.61800  3.41800   1.000 131.37000 ? 386 TYR B CA     1 
ATOM   7802  C  C      . TYR B 1 395 ? 14.73000  -2.35200  2.76900   1.000 123.96000 ? 386 TYR B C      1 
ATOM   7803  O  O      . TYR B 1 395 ? 15.44400  -1.34400  2.71900   1.000 113.61000 ? 386 TYR B O      1 
ATOM   7804  C  CB     . TYR B 1 395 ? 16.36100  -4.20500  2.51300   1.000 118.14000 ? 386 TYR B CB     1 
ATOM   7805  C  CG     . TYR B 1 395 ? 15.84200  -4.56100  1.13500   1.000 133.18000 ? 386 TYR B CG     1 
ATOM   7806  C  CD1    . TYR B 1 395 ? 15.20900  -5.77500  0.90200   1.000 158.67000 ? 386 TYR B CD1    1 
ATOM   7807  C  CD2    . TYR B 1 395 ? 15.96800  -3.67400  0.07300   1.000 139.32000 ? 386 TYR B CD2    1 
ATOM   7808  C  CE1    . TYR B 1 395 ? 14.72200  -6.09900  -0.35300  1.000 164.08000 ? 386 TYR B CE1    1 
ATOM   7809  C  CE2    . TYR B 1 395 ? 15.48500  -3.99100  -1.18500  1.000 156.96000 ? 386 TYR B CE2    1 
ATOM   7810  C  CZ     . TYR B 1 395 ? 14.86300  -5.20500  -1.39100  1.000 160.09000 ? 386 TYR B CZ     1 
ATOM   7811  O  OH     . TYR B 1 395 ? 14.38200  -5.52300  -2.64100  1.000 156.65000 ? 386 TYR B OH     1 
ATOM   7812  N  N      . ARG B 1 396 ? 13.49700  -2.38200  2.27000   1.000 132.57000 ? 387 ARG B N      1 
ATOM   7813  C  CA     . ARG B 1 396 ? 12.86000  -1.20500  1.69700   1.000 132.19000 ? 387 ARG B CA     1 
ATOM   7814  C  C      . ARG B 1 396 ? 12.36700  -0.21900  2.74700   1.000 129.20000 ? 387 ARG B C      1 
ATOM   7815  O  O      . ARG B 1 396 ? 11.81500  0.82300   2.37700   1.000 146.97000 ? 387 ARG B O      1 
ATOM   7816  C  CB     . ARG B 1 396 ? 11.69200  -1.62300  0.80000   1.000 133.71000 ? 387 ARG B CB     1 
ATOM   7817  N  N      . TYR B 1 397 ? 12.53500  -0.51400  4.03400   1.000 111.19000 ? 388 TYR B N      1 
ATOM   7818  C  CA     . TYR B 1 397 ? 12.08600  0.38100   5.09000   1.000 109.94000 ? 388 TYR B CA     1 
ATOM   7819  C  C      . TYR B 1 397 ? 13.22400  0.66400   6.06700   1.000 113.75000 ? 388 TYR B C      1 
ATOM   7820  O  O      . TYR B 1 397 ? 14.31700  0.09900   5.97000   1.000 111.36000 ? 388 TYR B O      1 
ATOM   7821  C  CB     . TYR B 1 397 ? 10.85800  -0.19900  5.80500   1.000 116.37000 ? 388 TYR B CB     1 
ATOM   7822  C  CG     . TYR B 1 397 ? 9.61500   -0.21000  4.93000   1.000 131.35000 ? 388 TYR B CG     1 
ATOM   7823  C  CD1    . TYR B 1 397 ? 8.80800   0.91700   4.81900   1.000 131.67000 ? 388 TYR B CD1    1 
ATOM   7824  C  CD2    . TYR B 1 397 ? 9.26500   -1.33900  4.19600   1.000 126.07000 ? 388 TYR B CD2    1 
ATOM   7825  C  CE1    . TYR B 1 397 ? 7.67600   0.91600   4.01500   1.000 124.47000 ? 388 TYR B CE1    1 
ATOM   7826  C  CE2    . TYR B 1 397 ? 8.13700   -1.34800  3.38900   1.000 109.49000 ? 388 TYR B CE2    1 
ATOM   7827  C  CZ     . TYR B 1 397 ? 7.34700   -0.21800  3.30300   1.000 112.00000 ? 388 TYR B CZ     1 
ATOM   7828  O  OH     . TYR B 1 397 ? 6.22700   -0.22800  2.50100   1.000 101.76000 ? 388 TYR B OH     1 
ATOM   7829  N  N      . LYS B 1 398 ? 12.94700  1.55300   7.03100   1.000 113.37000 ? 389 LYS B N      1 
ATOM   7830  C  CA     . LYS B 1 398 ? 14.02500  2.14600   7.82500   1.000 126.46000 ? 389 LYS B CA     1 
ATOM   7831  C  C      . LYS B 1 398 ? 14.73000  1.16200   8.75600   1.000 118.88000 ? 389 LYS B C      1 
ATOM   7832  O  O      . LYS B 1 398 ? 15.97400  1.17000   8.79500   1.000 132.02000 ? 389 LYS B O      1 
ATOM   7833  C  CB     . LYS B 1 398 ? 13.48200  3.35100   8.60000   1.000 122.97000 ? 389 LYS B CB     1 
ATOM   7834  N  N      . PRO B 1 399 ? 14.03500  0.32800   9.54100   1.000 100.32000 ? 390 PRO B N      1 
ATOM   7835  C  CA     . PRO B 1 399 ? 14.74900  -0.46100  10.57200  1.000 91.27000  ? 390 PRO B CA     1 
ATOM   7836  C  C      . PRO B 1 399 ? 15.78800  -1.42300  10.01400  1.000 93.94000  ? 390 PRO B C      1 
ATOM   7837  O  O      . PRO B 1 399 ? 16.92800  -1.48700  10.51400  1.000 98.11000  ? 390 PRO B O      1 
ATOM   7838  C  CB     . PRO B 1 399 ? 13.60900  -1.20100  11.28700  1.000 85.64000  ? 390 PRO B CB     1 
ATOM   7839  C  CG     . PRO B 1 399 ? 12.48600  -1.23300  10.28800  1.000 87.15000  ? 390 PRO B CG     1 
ATOM   7840  C  CD     . PRO B 1 399 ? 12.58300  0.07700   9.56600   1.000 91.27000  ? 390 PRO B CD     1 
ATOM   7841  N  N      . THR B 1 400 ? 15.41700  -2.19700  8.99400   1.000 88.25000  ? 391 THR B N      1 
ATOM   7842  C  CA     . THR B 1 400 ? 16.38100  -3.10900  8.39300   1.000 95.01000  ? 391 THR B CA     1 
ATOM   7843  C  C      . THR B 1 400 ? 17.55000  -2.34500  7.78900   1.000 110.18000 ? 391 THR B C      1 
ATOM   7844  O  O      . THR B 1 400 ? 18.68500  -2.83200  7.81100   1.000 119.57000 ? 391 THR B O      1 
ATOM   7845  C  CB     . THR B 1 400 ? 15.69600  -3.98300  7.33900   1.000 100.47000 ? 391 THR B CB     1 
ATOM   7846  O  OG1    . THR B 1 400 ? 14.47900  -4.51700  7.87900   1.000 115.11000 ? 391 THR B OG1    1 
ATOM   7847  C  CG2    . THR B 1 400 ? 16.60200  -5.13500  6.91000   1.000 82.76000  ? 391 THR B CG2    1 
ATOM   7848  N  N      . GLN B 1 401 ? 17.29700  -1.14700  7.25400   1.000 109.30000 ? 392 GLN B N      1 
ATOM   7849  C  CA     . GLN B 1 401 ? 18.38800  -0.32600  6.74100   1.000 103.90000 ? 392 GLN B CA     1 
ATOM   7850  C  C      . GLN B 1 401 ? 19.33500  0.09000   7.85800   1.000 101.99000 ? 392 GLN B C      1 
ATOM   7851  O  O      . GLN B 1 401 ? 20.55900  0.09900   7.67200   1.000 115.75000 ? 392 GLN B O      1 
ATOM   7852  C  CB     . GLN B 1 401 ? 17.84100  0.90400   6.01700   1.000 115.58000 ? 392 GLN B CB     1 
ATOM   7853  C  CG     . GLN B 1 401 ? 17.32600  0.61100   4.61900   1.000 124.53000 ? 392 GLN B CG     1 
ATOM   7854  C  CD     . GLN B 1 401 ? 17.19800  1.85900   3.76400   1.000 143.37000 ? 392 GLN B CD     1 
ATOM   7855  O  OE1    . GLN B 1 401 ? 17.25700  2.98600   4.26200   1.000 147.42000 ? 392 GLN B OE1    1 
ATOM   7856  N  NE2    . GLN B 1 401 ? 17.04000  1.66000   2.46100   1.000 139.84000 ? 392 GLN B NE2    1 
ATOM   7857  N  N      . PHE B 1 402 ? 18.79300  0.46300   9.02100   1.000 98.78000  ? 393 PHE B N      1 
ATOM   7858  C  CA     . PHE B 1 402 ? 19.67300  0.78500   10.13700  1.000 91.73000  ? 393 PHE B CA     1 
ATOM   7859  C  C      . PHE B 1 402 ? 20.53800  -0.40900  10.49200  1.000 88.06000  ? 393 PHE B C      1 
ATOM   7860  O  O      . PHE B 1 402 ? 21.74700  -0.26700  10.69900  1.000 95.17000  ? 393 PHE B O      1 
ATOM   7861  C  CB     . PHE B 1 402 ? 18.87500  1.23400   11.36400  1.000 93.06000  ? 393 PHE B CB     1 
ATOM   7862  C  CG     . PHE B 1 402 ? 19.73700  1.55600   12.57000  1.000 101.39000 ? 393 PHE B CG     1 
ATOM   7863  C  CD1    . PHE B 1 402 ? 21.05000  1.98400   12.41900  1.000 114.08000 ? 393 PHE B CD1    1 
ATOM   7864  C  CD2    . PHE B 1 402 ? 19.23800  1.40200   13.85500  1.000 118.78000 ? 393 PHE B CD2    1 
ATOM   7865  C  CE1    . PHE B 1 402 ? 21.83800  2.27000   13.52600  1.000 123.14000 ? 393 PHE B CE1    1 
ATOM   7866  C  CE2    . PHE B 1 402 ? 20.02300  1.68500   14.96300  1.000 119.66000 ? 393 PHE B CE2    1 
ATOM   7867  C  CZ     . PHE B 1 402 ? 21.32300  2.11900   14.79800  1.000 116.09000 ? 393 PHE B CZ     1 
ATOM   7868  N  N      . LEU B 1 403 ? 19.94600  -1.60100  10.54100  1.000 86.51000  ? 394 LEU B N      1 
ATOM   7869  C  CA     . LEU B 1 403 ? 20.74900  -2.77700  10.87000  1.000 92.64000  ? 394 LEU B CA     1 
ATOM   7870  C  C      . LEU B 1 403 ? 21.82500  -3.02200  9.81400   1.000 93.36000  ? 394 LEU B C      1 
ATOM   7871  O  O      . LEU B 1 403 ? 22.99500  -3.27900  10.13800  1.000 100.54000 ? 394 LEU B O      1 
ATOM   7872  C  CB     . LEU B 1 403 ? 19.85300  -4.00400  11.03600  1.000 88.55000  ? 394 LEU B CB     1 
ATOM   7873  C  CG     . LEU B 1 403 ? 20.59900  -5.25500  11.50700  1.000 81.46000  ? 394 LEU B CG     1 
ATOM   7874  C  CD1    . LEU B 1 403 ? 21.40000  -4.98900  12.78100  1.000 84.09000  ? 394 LEU B CD1    1 
ATOM   7875  C  CD2    . LEU B 1 403 ? 19.62400  -6.39800  11.71700  1.000 86.70000  ? 394 LEU B CD2    1 
ATOM   7876  N  N      . GLY B 1 404 ? 21.44700  -2.94200  8.53900   1.000 95.72000  ? 395 GLY B N      1 
ATOM   7877  C  CA     . GLY B 1 404 ? 22.40600  -3.18600  7.47500   1.000 114.25000 ? 395 GLY B CA     1 
ATOM   7878  C  C      . GLY B 1 404 ? 23.56000  -2.20400  7.47900   1.000 112.50000 ? 395 GLY B C      1 
ATOM   7879  O  O      . GLY B 1 404 ? 24.71800  -2.59100  7.30400   1.000 116.92000 ? 395 GLY B O      1 
ATOM   7880  N  N      . LYS B 1 405 ? 23.26500  -0.91800  7.68000   1.000 98.89000  ? 396 LYS B N      1 
ATOM   7881  C  CA     . LYS B 1 405 ? 24.33700  0.06700   7.74200   1.000 105.92000 ? 396 LYS B CA     1 
ATOM   7882  C  C      . LYS B 1 405 ? 25.16800  -0.08800  9.01100   1.000 114.14000 ? 396 LYS B C      1 
ATOM   7883  O  O      . LYS B 1 405 ? 26.37800  0.16600   8.98900   1.000 123.35000 ? 396 LYS B O      1 
ATOM   7884  C  CB     . LYS B 1 405 ? 23.75800  1.47900   7.62800   1.000 101.38000 ? 396 LYS B CB     1 
ATOM   7885  C  CG     . LYS B 1 405 ? 23.09600  1.75800   6.27800   1.000 99.79000  ? 396 LYS B CG     1 
ATOM   7886  C  CD     . LYS B 1 405 ? 22.75800  3.23000   6.10100   1.000 112.41000 ? 396 LYS B CD     1 
ATOM   7887  C  CE     . LYS B 1 405 ? 24.01900  4.07900   6.06200   1.000 119.41000 ? 396 LYS B CE     1 
ATOM   7888  N  NZ     . LYS B 1 405 ? 23.72500  5.50800   5.76200   1.000 87.39000  ? 396 LYS B NZ     1 
ATOM   7889  N  N      . SER B 1 406 ? 24.54900  -0.50500  10.11900  1.000 95.32000  ? 397 SER B N      1 
ATOM   7890  C  CA     . SER B 1 406 ? 25.28700  -0.75100  11.35100  1.000 97.42000  ? 397 SER B CA     1 
ATOM   7891  C  C      . SER B 1 406 ? 26.18100  -1.97600  11.26300  1.000 99.21000  ? 397 SER B C      1 
ATOM   7892  O  O      . SER B 1 406 ? 27.07300  -2.14000  12.10200  1.000 100.95000 ? 397 SER B O      1 
ATOM   7893  C  CB     . SER B 1 406 ? 24.31400  -0.91100  12.51900  1.000 110.65000 ? 397 SER B CB     1 
ATOM   7894  O  OG     . SER B 1 406 ? 23.79200  -2.22900  12.57800  1.000 96.93000  ? 397 SER B OG     1 
ATOM   7895  N  N      . SER B 1 407 ? 25.94100  -2.84800  10.27800  1.000 97.93000  ? 398 SER B N      1 
ATOM   7896  C  CA     . SER B 1 407 ? 26.78800  -4.02800  10.11000  1.000 97.91000  ? 398 SER B CA     1 
ATOM   7897  C  C      . SER B 1 407 ? 28.27000  -3.67400  10.12700  1.000 89.40000  ? 398 SER B C      1 
ATOM   7898  O  O      . SER B 1 407 ? 29.10300  -4.50100  10.51900  1.000 69.41000  ? 398 SER B O      1 
ATOM   7899  C  CB     . SER B 1 407 ? 26.44500  -4.73900  8.80200   1.000 89.20000  ? 398 SER B CB     1 
ATOM   7900  O  OG     . SER B 1 407 ? 26.73100  -3.91500  7.68600   1.000 92.06000  ? 398 SER B OG     1 
ATOM   7901  N  N      . ILE B 1 408 ? 28.61900  -2.45900  9.69700   1.000 104.60000 ? 399 ILE B N      1 
ATOM   7902  C  CA     . ILE B 1 408 ? 30.01200  -2.02700  9.72400   1.000 96.48000  ? 399 ILE B CA     1 
ATOM   7903  C  C      . ILE B 1 408 ? 30.47600  -1.89400  11.17100  1.000 97.18000  ? 399 ILE B C      1 
ATOM   7904  O  O      . ILE B 1 408 ? 31.66000  -2.09800  11.47000  1.000 98.51000  ? 399 ILE B O      1 
ATOM   7905  C  CB     . ILE B 1 408 ? 30.21500  -0.70700  8.95300   1.000 85.33000  ? 399 ILE B CB     1 
ATOM   7906  C  CG1    . ILE B 1 408 ? 29.23400  0.36000   9.44300   1.000 94.52000  ? 399 ILE B CG1    1 
ATOM   7907  C  CG2    . ILE B 1 408 ? 30.06500  -0.93000  7.45400   1.000 76.06000  ? 399 ILE B CG2    1 
ATOM   7908  C  CD1    . ILE B 1 408 ? 29.39000  1.69300   8.75500   1.000 86.04000  ? 399 ILE B CD1    1 
ATOM   7909  N  N      . GLU B 1 409 ? 29.55900  -1.56400  12.09200  1.000 102.99000 ? 400 GLU B N      1 
ATOM   7910  C  CA     . GLU B 1 409 ? 29.94500  -1.21200  13.45900  1.000 100.74000 ? 400 GLU B CA     1 
ATOM   7911  C  C      . GLU B 1 409 ? 30.47600  -2.41200  14.23700  1.000 97.97000  ? 400 GLU B C      1 
ATOM   7912  O  O      . GLU B 1 409 ? 31.37800  -2.26100  15.07000  1.000 95.83000  ? 400 GLU B O      1 
ATOM   7913  C  CB     . GLU B 1 409 ? 28.75700  -0.60400  14.20500  1.000 103.16000 ? 400 GLU B CB     1 
ATOM   7914  C  CG     . GLU B 1 409 ? 28.09000  0.55500   13.49300  1.000 96.07000  ? 400 GLU B CG     1 
ATOM   7915  C  CD     . GLU B 1 409 ? 28.90200  1.83400   13.56100  1.000 115.81000 ? 400 GLU B CD     1 
ATOM   7916  O  OE1    . GLU B 1 409 ? 29.70600  1.98700   14.50200  1.000 133.80000 ? 400 GLU B OE1    1 
ATOM   7917  O  OE2    . GLU B 1 409 ? 28.73200  2.69100   12.67000  1.000 115.11000 ? 400 GLU B OE2    1 
ATOM   7918  N  N      . GLY B 1 410 ? 29.92400  -3.59700  14.00900  1.000 92.67000  ? 401 GLY B N      1 
ATOM   7919  C  CA     . GLY B 1 410 ? 30.43100  -4.78100  14.67800  1.000 69.40000  ? 401 GLY B CA     1 
ATOM   7920  C  C      . GLY B 1 410 ? 29.50600  -5.95900  14.48300  1.000 89.04000  ? 401 GLY B C      1 
ATOM   7921  O  O      . GLY B 1 410 ? 28.37300  -5.82800  14.00900  1.000 109.93000 ? 401 GLY B O      1 
ATOM   7922  N  N      . THR B 1 411 ? 30.02400  -7.13200  14.84900  1.000 83.33000  ? 402 THR B N      1 
ATOM   7923  C  CA     . THR B 1 411 ? 29.20500  -8.33800  14.83400  1.000 84.77000  ? 402 THR B CA     1 
ATOM   7924  C  C      . THR B 1 411 ? 28.27800  -8.37100  16.04000  1.000 86.49000  ? 402 THR B C      1 
ATOM   7925  O  O      . THR B 1 411 ? 27.07200  -8.61500  15.90400  1.000 98.65000  ? 402 THR B O      1 
ATOM   7926  C  CB     . THR B 1 411 ? 30.09400  -9.58100  14.81100  1.000 97.32000  ? 402 THR B CB     1 
ATOM   7927  O  OG1    . THR B 1 411 ? 31.12600  -9.42000  13.83100  1.000 125.06000 ? 402 THR B OG1    1 
ATOM   7928  C  CG2    . THR B 1 411 ? 29.27800  -10.82100 14.50100  1.000 71.72000  ? 402 THR B CG2    1 
ATOM   7929  N  N      . GLY B 1 412 ? 28.82900  -8.12100  17.22900  1.000 87.52000  ? 403 GLY B N      1 
ATOM   7930  C  CA     . GLY B 1 412 ? 27.98600  -8.00200  18.40300  1.000 84.90000  ? 403 GLY B CA     1 
ATOM   7931  C  C      . GLY B 1 412 ? 26.95700  -6.90200  18.23900  1.000 78.24000  ? 403 GLY B C      1 
ATOM   7932  O  O      . GLY B 1 412 ? 25.82400  -7.02000  18.70900  1.000 75.58000  ? 403 GLY B O      1 
ATOM   7933  N  N      . MET B 1 413 ? 27.33800  -5.82100  17.55400  1.000 89.47000  ? 404 MET B N      1 
ATOM   7934  C  CA     . MET B 1 413 ? 26.37000  -4.78100  17.22800  1.000 91.77000  ? 404 MET B CA     1 
ATOM   7935  C  C      . MET B 1 413 ? 25.26200  -5.32800  16.34300  1.000 89.51000  ? 404 MET B C      1 
ATOM   7936  O  O      . MET B 1 413 ? 24.08700  -5.00900  16.54300  1.000 104.65000 ? 404 MET B O      1 
ATOM   7937  C  CB     . MET B 1 413 ? 27.06400  -3.60400  16.54300  1.000 91.37000  ? 404 MET B CB     1 
ATOM   7938  C  CG     . MET B 1 413 ? 27.59700  -2.55300  17.49400  1.000 94.68000  ? 404 MET B CG     1 
ATOM   7939  S  SD     . MET B 1 413 ? 26.26600  -1.52200  18.13700  1.000 91.45000  ? 404 MET B SD     1 
ATOM   7940  C  CE     . MET B 1 413 ? 25.61800  -0.82600  16.62000  1.000 80.34000  ? 404 MET B CE     1 
ATOM   7941  N  N      . VAL B 1 414 ? 25.60900  -6.18100  15.38000  1.000 73.49000  ? 405 VAL B N      1 
ATOM   7942  C  CA     . VAL B 1 414 ? 24.58800  -6.76500  14.51400  1.000 79.31000  ? 405 VAL B CA     1 
ATOM   7943  C  C      . VAL B 1 414 ? 23.61000  -7.59400  15.33400  1.000 78.66000  ? 405 VAL B C      1 
ATOM   7944  O  O      . VAL B 1 414 ? 22.38800  -7.46200  15.19800  1.000 77.39000  ? 405 VAL B O      1 
ATOM   7945  C  CB     . VAL B 1 414 ? 25.24200  -7.60900  13.40600  1.000 72.53000  ? 405 VAL B CB     1 
ATOM   7946  C  CG1    . VAL B 1 414 ? 24.20300  -8.49400  12.73700  1.000 71.72000  ? 405 VAL B CG1    1 
ATOM   7947  C  CG2    . VAL B 1 414 ? 25.91300  -6.71200  12.38300  1.000 95.79000  ? 405 VAL B CG2    1 
ATOM   7948  N  N      . ILE B 1 415 ? 24.13500  -8.44700  16.21300  1.000 72.72000  ? 406 ILE B N      1 
ATOM   7949  C  CA     . ILE B 1 415 ? 23.26600  -9.32200  16.99700  1.000 63.93000  ? 406 ILE B CA     1 
ATOM   7950  C  C      . ILE B 1 415 ? 22.37900  -8.50200  17.92800  1.000 62.46000  ? 406 ILE B C      1 
ATOM   7951  O  O      . ILE B 1 415 ? 21.16400  -8.73000  18.02300  1.000 68.71000  ? 406 ILE B O      1 
ATOM   7952  C  CB     . ILE B 1 415 ? 24.10000  -10.35200 17.77600  1.000 66.43000  ? 406 ILE B CB     1 
ATOM   7953  C  CG1    . ILE B 1 415 ? 24.83300  -11.28100 16.80400  1.000 62.10000  ? 406 ILE B CG1    1 
ATOM   7954  C  CG2    . ILE B 1 415 ? 23.20900  -11.14000 18.72400  1.000 59.26000  ? 406 ILE B CG2    1 
ATOM   7955  C  CD1    . ILE B 1 415 ? 23.91600  -12.10700 15.93300  1.000 79.76000  ? 406 ILE B CD1    1 
ATOM   7956  N  N      . SER B 1 416 ? 22.97600  -7.54400  18.64100  1.000 65.91000  ? 407 SER B N      1 
ATOM   7957  C  CA     . SER B 1 416 ? 22.20600  -6.73700  19.57900  1.000 59.59000  ? 407 SER B CA     1 
ATOM   7958  C  C      . SER B 1 416 ? 21.15300  -5.91400  18.85400  1.000 61.69000  ? 407 SER B C      1 
ATOM   7959  O  O      . SER B 1 416 ? 20.02200  -5.78000  19.33400  1.000 62.12000  ? 407 SER B O      1 
ATOM   7960  C  CB     . SER B 1 416 ? 23.13600  -5.83200  20.38500  1.000 65.77000  ? 407 SER B CB     1 
ATOM   7961  O  OG     . SER B 1 416 ? 23.90800  -6.58400  21.30500  1.000 79.78000  ? 407 SER B OG     1 
ATOM   7962  N  N      . ASN B 1 417 ? 21.50500  -5.35300  17.69600  1.000 67.75000  ? 408 ASN B N      1 
ATOM   7963  C  CA     . ASN B 1 417 ? 20.54000  -4.56400  16.94700  1.000 86.55000  ? 408 ASN B CA     1 
ATOM   7964  C  C      . ASN B 1 417 ? 19.41200  -5.43900  16.42200  1.000 81.35000  ? 408 ASN B C      1 
ATOM   7965  O  O      . ASN B 1 417 ? 18.25600  -5.01500  16.41000  1.000 88.73000  ? 408 ASN B O      1 
ATOM   7966  C  CB     . ASN B 1 417 ? 21.23700  -3.82200  15.80600  1.000 95.09000  ? 408 ASN B CB     1 
ATOM   7967  C  CG     . ASN B 1 417 ? 21.97900  -2.58300  16.28400  1.000 104.00000 ? 408 ASN B CG     1 
ATOM   7968  O  OD1    . ASN B 1 417 ? 23.20200  -2.48300  16.15500  1.000 103.96000 ? 408 ASN B OD1    1 
ATOM   7969  N  ND2    . ASN B 1 417 ? 21.23900  -1.63300  16.84400  1.000 103.34000 ? 408 ASN B ND2    1 
ATOM   7970  N  N      . GLY B 1 418 ? 19.71400  -6.67500  16.02200  1.000 61.31000  ? 409 GLY B N      1 
ATOM   7971  C  CA     . GLY B 1 418 ? 18.64800  -7.57000  15.59900  1.000 54.41000  ? 409 GLY B CA     1 
ATOM   7972  C  C      . GLY B 1 418 ? 17.69900  -7.91000  16.73300  1.000 58.72000  ? 409 GLY B C      1 
ATOM   7973  O  O      . GLY B 1 418 ? 16.47100  -7.86900  16.57400  1.000 52.36000  ? 409 GLY B O      1 
ATOM   7974  N  N      . LEU B 1 419 ? 18.25400  -8.23900  17.90100  1.000 61.15000  ? 410 LEU B N      1 
ATOM   7975  C  CA     . LEU B 1 419 ? 17.40700  -8.54900  19.04800  1.000 49.29000  ? 410 LEU B CA     1 
ATOM   7976  C  C      . LEU B 1 419 ? 16.55400  -7.35100  19.44000  1.000 69.05000  ? 410 LEU B C      1 
ATOM   7977  O  O      . LEU B 1 419 ? 15.35200  -7.48900  19.70600  1.000 81.31000  ? 410 LEU B O      1 
ATOM   7978  C  CB     . LEU B 1 419 ? 18.26600  -8.99600  20.22900  1.000 36.21000  ? 410 LEU B CB     1 
ATOM   7979  C  CG     . LEU B 1 419 ? 18.87600  -10.38800 20.10700  1.000 24.70000  ? 410 LEU B CG     1 
ATOM   7980  C  CD1    . LEU B 1 419 ? 19.98100  -10.58000 21.13400  1.000 12.99000  ? 410 LEU B CD1    1 
ATOM   7981  C  CD2    . LEU B 1 419 ? 17.78200  -11.42400 20.27000  1.000 15.25000  ? 410 LEU B CD2    1 
ATOM   7982  N  N      . SER B 1 420 ? 17.16100  -6.16300  19.47600  1.000 50.99000  ? 411 SER B N      1 
ATOM   7983  C  CA     . SER B 1 420 ? 16.41100  -4.96000  19.81000  1.000 50.97000  ? 411 SER B CA     1 
ATOM   7984  C  C      . SER B 1 420 ? 15.33200  -4.68200  18.77300  1.000 61.31000  ? 411 SER B C      1 
ATOM   7985  O  O      . SER B 1 420 ? 14.22100  -4.26400  19.11900  1.000 78.46000  ? 411 SER B O      1 
ATOM   7986  C  CB     . SER B 1 420 ? 17.36500  -3.77400  19.93700  1.000 65.17000  ? 411 SER B CB     1 
ATOM   7987  O  OG     . SER B 1 420 ? 18.03300  -3.52400  18.71200  1.000 88.52000  ? 411 SER B OG     1 
ATOM   7988  N  N      . LEU B 1 421 ? 15.64300  -4.89600  17.49400  1.000 57.52000  ? 412 LEU B N      1 
ATOM   7989  C  CA     . LEU B 1 421 ? 14.65700  -4.66300  16.44900  1.000 55.76000  ? 412 LEU B CA     1 
ATOM   7990  C  C      . LEU B 1 421 ? 13.46000  -5.58300  16.62400  1.000 59.85000  ? 412 LEU B C      1 
ATOM   7991  O  O      . LEU B 1 421 ? 12.31100  -5.14800  16.49700  1.000 67.76000  ? 412 LEU B O      1 
ATOM   7992  C  CB     . LEU B 1 421 ? 15.29700  -4.85400  15.07400  1.000 64.95000  ? 412 LEU B CB     1 
ATOM   7993  C  CG     . LEU B 1 421 ? 14.54300  -4.27700  13.87200  1.000 58.82000  ? 412 LEU B CG     1 
ATOM   7994  C  CD1    . LEU B 1 421 ? 15.51300  -3.82500  12.78400  1.000 91.03000  ? 412 LEU B CD1    1 
ATOM   7995  C  CD2    . LEU B 1 421 ? 13.55000  -5.28300  13.31700  1.000 62.08000  ? 412 LEU B CD2    1 
ATOM   7996  N  N      . GLY B 1 422 ? 13.70500  -6.85700  16.92900  1.000 56.37000  ? 413 GLY B N      1 
ATOM   7997  C  CA     . GLY B 1 422 ? 12.59000  -7.76300  17.16200  1.000 59.19000  ? 413 GLY B CA     1 
ATOM   7998  C  C      . GLY B 1 422 ? 11.76500  -7.35400  18.36900  1.000 62.50000  ? 413 GLY B C      1 
ATOM   7999  O  O      . GLY B 1 422 ? 10.52600  -7.33600  18.32700  1.000 65.10000  ? 413 GLY B O      1 
ATOM   8000  N  N      . MET B 1 423 ? 12.44700  -7.02000  19.46700  1.000 54.04000  ? 414 MET B N      1 
ATOM   8001  C  CA     . MET B 1 423 ? 11.74100  -6.61900  20.67700  1.000 46.45000  ? 414 MET B CA     1 
ATOM   8002  C  C      . MET B 1 423 ? 10.86600  -5.39600  20.42400  1.000 51.49000  ? 414 MET B C      1 
ATOM   8003  O  O      . MET B 1 423 ? 9.73400   -5.31900  20.91800  1.000 56.79000  ? 414 MET B O      1 
ATOM   8004  C  CB     . MET B 1 423 ? 12.74400  -6.35500  21.79800  1.000 42.08000  ? 414 MET B CB     1 
ATOM   8005  C  CG     . MET B 1 423 ? 13.26400  -7.61700  22.45800  1.000 30.07000  ? 414 MET B CG     1 
ATOM   8006  S  SD     . MET B 1 423 ? 14.76400  -7.32600  23.40500  1.000 61.21000  ? 414 MET B SD     1 
ATOM   8007  C  CE     . MET B 1 423 ? 14.84600  -8.83500  24.36600  1.000 22.02000  ? 414 MET B CE     1 
ATOM   8008  N  N      . LYS B 1 424 ? 11.36500  -4.43900  19.63900  1.000 58.05000  ? 415 LYS B N      1 
ATOM   8009  C  CA     . LYS B 1 424 ? 10.57600  -3.24900  19.33600  1.000 53.09000  ? 415 LYS B CA     1 
ATOM   8010  C  C      . LYS B 1 424 ? 9.43900   -3.56700  18.37100  1.000 63.08000  ? 415 LYS B C      1 
ATOM   8011  O  O      . LYS B 1 424 ? 8.34600   -2.99800  18.48400  1.000 63.44000  ? 415 LYS B O      1 
ATOM   8012  C  CB     . LYS B 1 424 ? 11.47900  -2.16100  18.75700  1.000 58.05000  ? 415 LYS B CB     1 
ATOM   8013  C  CG     . LYS B 1 424 ? 12.34600  -1.44600  19.78000  1.000 68.01000  ? 415 LYS B CG     1 
ATOM   8014  C  CD     . LYS B 1 424 ? 13.16000  -0.34300  19.12000  1.000 88.50000  ? 415 LYS B CD     1 
ATOM   8015  C  CE     . LYS B 1 424 ? 13.95300  0.46100   20.13800  1.000 93.79000  ? 415 LYS B CE     1 
ATOM   8016  N  NZ     . LYS B 1 424 ? 14.57200  1.66400   19.51000  1.000 114.31000 ? 415 LYS B NZ     1 
ATOM   8017  N  N      . SER B 1 425 ? 9.67800   -4.46600  17.41100  1.000 65.78000  ? 416 SER B N      1 
ATOM   8018  C  CA     . SER B 1 425 ? 8.65300   -4.83600  16.44200  1.000 65.22000  ? 416 SER B CA     1 
ATOM   8019  C  C      . SER B 1 425 ? 7.49200   -5.56200  17.09800  1.000 58.65000  ? 416 SER B C      1 
ATOM   8020  O  O      . SER B 1 425 ? 6.39000   -5.58900  16.53600  1.000 51.59000  ? 416 SER B O      1 
ATOM   8021  C  CB     . SER B 1 425 ? 9.25500   -5.71000  15.34000  1.000 64.42000  ? 416 SER B CB     1 
ATOM   8022  O  OG     . SER B 1 425 ? 9.53400   -7.01500  15.81900  1.000 48.63000  ? 416 SER B OG     1 
ATOM   8023  N  N      . VAL B 1 426 ? 7.73000   -6.17200  18.26000  1.000 62.86000  ? 417 VAL B N      1 
ATOM   8024  C  CA     . VAL B 1 426 ? 6.65100   -6.86500  18.96400  1.000 58.31000  ? 417 VAL B CA     1 
ATOM   8025  C  C      . VAL B 1 426 ? 5.42500   -5.96400  19.10600  1.000 55.89000  ? 417 VAL B C      1 
ATOM   8026  O  O      . VAL B 1 426 ? 4.28200   -6.42200  18.98500  1.000 57.81000  ? 417 VAL B O      1 
ATOM   8027  C  CB     . VAL B 1 426 ? 7.14500   -7.35900  20.33700  1.000 48.91000  ? 417 VAL B CB     1 
ATOM   8028  C  CG1    . VAL B 1 426 ? 5.98500   -7.90000  21.15300  1.000 53.04000  ? 417 VAL B CG1    1 
ATOM   8029  C  CG2    . VAL B 1 426 ? 8.21300   -8.41800  20.16400  1.000 56.06000  ? 417 VAL B CG2    1 
ATOM   8030  N  N      . PHE B 1 427 ? 5.64200   -4.66400  19.34900  1.000 62.64000  ? 418 PHE B N      1 
ATOM   8031  C  CA     . PHE B 1 427 ? 4.53800   -3.80600  19.78000  1.000 59.10000  ? 418 PHE B CA     1 
ATOM   8032  C  C      . PHE B 1 427 ? 3.48700   -3.56000  18.70300  1.000 57.67000  ? 418 PHE B C      1 
ATOM   8033  O  O      . PHE B 1 427 ? 2.29400   -3.78300  18.97500  1.000 61.17000  ? 418 PHE B O      1 
ATOM   8034  C  CB     . PHE B 1 427 ? 5.08800   -2.47900  20.30800  1.000 46.09000  ? 418 PHE B CB     1 
ATOM   8035  C  CG     . PHE B 1 427 ? 4.06300   -1.65400  21.01900  1.000 43.55000  ? 418 PHE B CG     1 
ATOM   8036  C  CD1    . PHE B 1 427 ? 3.71600   -1.93400  22.32900  1.000 57.22000  ? 418 PHE B CD1    1 
ATOM   8037  C  CD2    . PHE B 1 427 ? 3.41000   -0.62800  20.36100  1.000 47.17000  ? 418 PHE B CD2    1 
ATOM   8038  C  CE1    . PHE B 1 427 ? 2.75800   -1.18400  22.98000  1.000 69.20000  ? 418 PHE B CE1    1 
ATOM   8039  C  CE2    . PHE B 1 427 ? 2.44800   0.12500   21.00500  1.000 62.04000  ? 418 PHE B CE2    1 
ATOM   8040  C  CZ     . PHE B 1 427 ? 2.12200   -0.15400  22.31800  1.000 74.71000  ? 418 PHE B CZ     1 
ATOM   8041  N  N      . PRO B 1 428 ? 3.83100   -3.10400  17.50100  1.000 54.20000  ? 419 PRO B N      1 
ATOM   8042  C  CA     . PRO B 1 428 ? 2.80700   -2.63800  16.54300  1.000 57.15000  ? 419 PRO B CA     1 
ATOM   8043  C  C      . PRO B 1 428 ? 1.76800   -3.70500  16.24500  1.000 59.42000  ? 419 PRO B C      1 
ATOM   8044  O  O      . PRO B 1 428 ? 0.55500   -3.44000  16.31600  1.000 43.87000  ? 419 PRO B O      1 
ATOM   8045  C  CB     . PRO B 1 428 ? 3.63100   -2.29600  15.29500  1.000 57.87000  ? 419 PRO B CB     1 
ATOM   8046  C  CG     . PRO B 1 428 ? 4.96100   -1.91700  15.84400  1.000 53.89000  ? 419 PRO B CG     1 
ATOM   8047  C  CD     . PRO B 1 428 ? 5.19400   -2.86000  16.99900  1.000 61.00000  ? 419 PRO B CD     1 
ATOM   8048  N  N      . PRO B 1 429 ? 2.19200   -4.91500  15.87800  1.000 60.66000  ? 420 PRO B N      1 
ATOM   8049  C  CA     . PRO B 1 429 ? 1.19800   -5.96100  15.60300  1.000 47.44000  ? 420 PRO B CA     1 
ATOM   8050  C  C      . PRO B 1 429 ? 0.37800   -6.30800  16.82700  1.000 52.59000  ? 420 PRO B C      1 
ATOM   8051  O  O      . PRO B 1 429 ? -0.81500  -6.60500  16.69900  1.000 64.22000  ? 420 PRO B O      1 
ATOM   8052  C  CB     . PRO B 1 429 ? 2.05300   -7.14200  15.12500  1.000 45.31000  ? 420 PRO B CB     1 
ATOM   8053  C  CG     . PRO B 1 429 ? 3.38300   -6.91300  15.75100  1.000 48.87000  ? 420 PRO B CG     1 
ATOM   8054  C  CD     . PRO B 1 429 ? 3.57100   -5.42600  15.79000  1.000 49.23000  ? 420 PRO B CD     1 
ATOM   8055  N  N      . THR B 1 430 ? 0.98000   -6.27300  18.01900  1.000 50.21000  ? 421 THR B N      1 
ATOM   8056  C  CA     . THR B 1 430 ? 0.21200   -6.53800  19.23100  1.000 54.33000  ? 421 THR B CA     1 
ATOM   8057  C  C      . THR B 1 430 ? -0.86000  -5.47800  19.44200  1.000 68.44000  ? 421 THR B C      1 
ATOM   8058  O  O      . THR B 1 430 ? -1.97400  -5.78900  19.87200  1.000 66.37000  ? 421 THR B O      1 
ATOM   8059  C  CB     . THR B 1 430 ? 1.13700   -6.60800  20.44500  1.000 43.77000  ? 421 THR B CB     1 
ATOM   8060  O  OG1    . THR B 1 430 ? 1.98300   -7.75900  20.33700  1.000 39.22000  ? 421 THR B OG1    1 
ATOM   8061  C  CG2    . THR B 1 430 ? 0.32000   -6.70200  21.72500  1.000 47.05000  ? 421 THR B CG2    1 
ATOM   8062  N  N      . LEU B 1 431 ? -0.54200  -4.21600  19.14900  1.000 65.48000  ? 422 LEU B N      1 
ATOM   8063  C  CA     . LEU B 1 431 ? -1.54900  -3.16500  19.25100  1.000 56.31000  ? 422 LEU B CA     1 
ATOM   8064  C  C      . LEU B 1 431 ? -2.65400  -3.36400  18.22700  1.000 56.23000  ? 422 LEU B C      1 
ATOM   8065  O  O      . LEU B 1 431 ? -3.83800  -3.15900  18.52800  1.000 60.43000  ? 422 LEU B O      1 
ATOM   8066  C  CB     . LEU B 1 431 ? -0.90400  -1.79300  19.07300  1.000 47.28000  ? 422 LEU B CB     1 
ATOM   8067  C  CG     . LEU B 1 431 ? -1.87700  -0.62500  19.22800  1.000 49.24000  ? 422 LEU B CG     1 
ATOM   8068  C  CD1    . LEU B 1 431 ? -2.73800  -0.81700  20.47100  1.000 53.94000  ? 422 LEU B CD1    1 
ATOM   8069  C  CD2    . LEU B 1 431 ? -1.12100  0.68900   19.29400  1.000 80.74000  ? 422 LEU B CD2    1 
ATOM   8070  N  N      . THR B 1 432 ? -2.28300  -3.75600  17.00800  1.000 52.01000  ? 423 THR B N      1 
ATOM   8071  C  CA     . THR B 1 432 ? -3.28800  -4.06200  15.99700  1.000 44.62000  ? 423 THR B CA     1 
ATOM   8072  C  C      . THR B 1 432 ? -4.22700  -5.15400  16.49100  1.000 52.83000  ? 423 THR B C      1 
ATOM   8073  O  O      . THR B 1 432 ? -5.45500  -5.03200  16.39500  1.000 49.29000  ? 423 THR B O      1 
ATOM   8074  C  CB     . THR B 1 432 ? -2.61100  -4.47900  14.69100  1.000 51.45000  ? 423 THR B CB     1 
ATOM   8075  O  OG1    . THR B 1 432 ? -1.61400  -3.51200  14.33700  1.000 64.87000  ? 423 THR B OG1    1 
ATOM   8076  C  CG2    . THR B 1 432 ? -3.63900  -4.58500  13.56800  1.000 78.10000  ? 423 THR B CG2    1 
ATOM   8077  N  N      . LEU B 1 433 ? -3.65700  -6.23000  17.03800  1.000 60.14000  ? 424 LEU B N      1 
ATOM   8078  C  CA     . LEU B 1 433 ? -4.47200  -7.32600  17.54900  1.000 60.35000  ? 424 LEU B CA     1 
ATOM   8079  C  C      . LEU B 1 433 ? -5.32900  -6.87200  18.72200  1.000 53.90000  ? 424 LEU B C      1 
ATOM   8080  O  O      . LEU B 1 433 ? -6.48200  -7.29500  18.85500  1.000 62.50000  ? 424 LEU B O      1 
ATOM   8081  C  CB     . LEU B 1 433 ? -3.58500  -8.50700  17.94300  1.000 29.56000  ? 424 LEU B CB     1 
ATOM   8082  C  CG     . LEU B 1 433 ? -3.07100  -9.34700  16.76700  1.000 36.00000  ? 424 LEU B CG     1 
ATOM   8083  C  CD1    . LEU B 1 433 ? -1.91100  -10.25000 17.16800  1.000 23.27000  ? 424 LEU B CD1    1 
ATOM   8084  C  CD2    . LEU B 1 433 ? -4.20300  -10.16500 16.16600  1.000 26.73000  ? 424 LEU B CD2    1 
ATOM   8085  N  N      . VAL B 1 434 ? -4.78900  -6.00700  19.58000  1.000 42.42000  ? 425 VAL B N      1 
ATOM   8086  C  CA     . VAL B 1 434 ? -5.55400  -5.52800  20.72600  1.000 47.60000  ? 425 VAL B CA     1 
ATOM   8087  C  C      . VAL B 1 434 ? -6.77800  -4.75600  20.25100  1.000 62.79000  ? 425 VAL B C      1 
ATOM   8088  O  O      . VAL B 1 434 ? -7.89800  -4.96900  20.73200  1.000 72.91000  ? 425 VAL B O      1 
ATOM   8089  C  CB     . VAL B 1 434 ? -4.66600  -4.66700  21.64300  1.000 49.18000  ? 425 VAL B CB     1 
ATOM   8090  C  CG1    . VAL B 1 434 ? -5.52500  -3.87600  22.61900  1.000 48.98000  ? 425 VAL B CG1    1 
ATOM   8091  C  CG2    . VAL B 1 434 ? -3.64900  -5.53100  22.37800  1.000 58.55000  ? 425 VAL B CG2    1 
ATOM   8092  N  N      . LEU B 1 435 ? -6.58100  -3.84400  19.29700  1.000 70.94000  ? 426 LEU B N      1 
ATOM   8093  C  CA     . LEU B 1 435 ? -7.70700  -3.06600  18.78900  1.000 75.16000  ? 426 LEU B CA     1 
ATOM   8094  C  C      . LEU B 1 435 ? -8.71700  -3.95900  18.07700  1.000 67.32000  ? 426 LEU B C      1 
ATOM   8095  O  O      . LEU B 1 435 ? -9.93400  -3.78800  18.24000  1.000 70.87000  ? 426 LEU B O      1 
ATOM   8096  C  CB     . LEU B 1 435 ? -7.20900  -1.96300  17.85500  1.000 72.24000  ? 426 LEU B CB     1 
ATOM   8097  C  CG     . LEU B 1 435 ? -6.36500  -0.86800  18.51100  1.000 51.97000  ? 426 LEU B CG     1 
ATOM   8098  C  CD1    . LEU B 1 435 ? -5.86900  0.13100   17.47700  1.000 44.90000  ? 426 LEU B CD1    1 
ATOM   8099  C  CD2    . LEU B 1 435 ? -7.15700  -0.16700  19.60200  1.000 42.33000  ? 426 LEU B CD2    1 
ATOM   8100  N  N      . GLY B 1 436 ? -8.23400  -4.92500  17.29500  1.000 61.55000  ? 427 GLY B N      1 
ATOM   8101  C  CA     . GLY B 1 436 ? -9.15000  -5.83500  16.63000  1.000 63.51000  ? 427 GLY B CA     1 
ATOM   8102  C  C      . GLY B 1 436 ? -9.99200  -6.61600  17.61800  1.000 59.98000  ? 427 GLY B C      1 
ATOM   8103  O  O      . GLY B 1 436 ? -11.21000 -6.72900  17.46300  1.000 55.87000  ? 427 GLY B O      1 
ATOM   8104  N  N      . ILE B 1 437 ? -9.35200  -7.14800  18.66200  1.000 62.74000  ? 428 ILE B N      1 
ATOM   8105  C  CA     . ILE B 1 437 ? -10.07100 -7.89900  19.68600  1.000 73.13000  ? 428 ILE B CA     1 
ATOM   8106  C  C      . ILE B 1 437 ? -11.09100 -7.00900  20.38000  1.000 75.38000  ? 428 ILE B C      1 
ATOM   8107  O  O      . ILE B 1 437 ? -12.23400 -7.41800  20.62000  1.000 76.43000  ? 428 ILE B O      1 
ATOM   8108  C  CB     . ILE B 1 437 ? -9.07700  -8.50300  20.69500  1.000 62.44000  ? 428 ILE B CB     1 
ATOM   8109  C  CG1    . ILE B 1 437 ? -8.28800  -9.65000  20.05900  1.000 65.85000  ? 428 ILE B CG1    1 
ATOM   8110  C  CG2    . ILE B 1 437 ? -9.80400  -8.96400  21.95000  1.000 65.61000  ? 428 ILE B CG2    1 
ATOM   8111  C  CD1    . ILE B 1 437 ? -7.02000  -10.01800 20.81400  1.000 54.54000  ? 428 ILE B CD1    1 
ATOM   8112  N  N      . LEU B 1 438 ? -10.69300 -5.78100  20.71800  1.000 64.05000  ? 429 LEU B N      1 
ATOM   8113  C  CA     . LEU B 1 438 ? -11.58900 -4.88400  21.43700  1.000 52.20000  ? 429 LEU B CA     1 
ATOM   8114  C  C      . LEU B 1 438 ? -12.83300 -4.57900  20.61600  1.000 65.64000  ? 429 LEU B C      1 
ATOM   8115  O  O      . LEU B 1 438 ? -13.95900 -4.64800  21.12200  1.000 58.90000  ? 429 LEU B O      1 
ATOM   8116  C  CB     . LEU B 1 438 ? -10.85000 -3.59600  21.79400  1.000 36.39000  ? 429 LEU B CB     1 
ATOM   8117  C  CG     . LEU B 1 438 ? -9.69700  -3.77100  22.78000  1.000 45.34000  ? 429 LEU B CG     1 
ATOM   8118  C  CD1    . LEU B 1 438 ? -8.71700  -2.60800  22.69100  1.000 47.59000  ? 429 LEU B CD1    1 
ATOM   8119  C  CD2    . LEU B 1 438 ? -10.23900 -3.91700  24.18900  1.000 50.33000  ? 429 LEU B CD2    1 
ATOM   8120  N  N      . PHE B 1 439 ? -12.65000 -4.23700  19.34000  1.000 71.20000  ? 430 PHE B N      1 
ATOM   8121  C  CA     . PHE B 1 439 ? -13.80600 -3.90400  18.51600  1.000 64.65000  ? 430 PHE B CA     1 
ATOM   8122  C  C      . PHE B 1 439 ? -14.65500 -5.13500  18.21400  1.000 73.80000  ? 430 PHE B C      1 
ATOM   8123  O  O      . PHE B 1 439 ? -15.88900 -5.05200  18.20400  1.000 78.51000  ? 430 PHE B O      1 
ATOM   8124  C  CB     . PHE B 1 439 ? -13.35400 -3.20100  17.23800  1.000 68.90000  ? 430 PHE B CB     1 
ATOM   8125  C  CG     . PHE B 1 439 ? -12.63900 -1.90500  17.49600  1.000 70.37000  ? 430 PHE B CG     1 
ATOM   8126  C  CD1    . PHE B 1 439 ? -13.20000 -0.95100  18.33000  1.000 50.66000  ? 430 PHE B CD1    1 
ATOM   8127  C  CD2    . PHE B 1 439 ? -11.41400 -1.63600  16.91000  1.000 88.35000  ? 430 PHE B CD2    1 
ATOM   8128  C  CE1    . PHE B 1 439 ? -12.55200 0.24400   18.57900  1.000 56.04000  ? 430 PHE B CE1    1 
ATOM   8129  C  CE2    . PHE B 1 439 ? -10.76000 -0.44000  17.15400  1.000 78.89000  ? 430 PHE B CE2    1 
ATOM   8130  C  CZ     . PHE B 1 439 ? -11.33200 0.50000   17.99000  1.000 59.12000  ? 430 PHE B CZ     1 
ATOM   8131  N  N      . ALA B 1 440 ? -14.02500 -6.29300  17.99700  1.000 73.78000  ? 431 ALA B N      1 
ATOM   8132  C  CA     . ALA B 1 440 ? -14.80000 -7.50700  17.76600  1.000 71.35000  ? 431 ALA B CA     1 
ATOM   8133  C  C      . ALA B 1 440 ? -15.63900 -7.84800  18.98800  1.000 63.70000  ? 431 ALA B C      1 
ATOM   8134  O  O      . ALA B 1 440 ? -16.79200 -8.28800  18.86400  1.000 75.62000  ? 431 ALA B O      1 
ATOM   8135  C  CB     . ALA B 1 440 ? -13.87100 -8.66600  17.40400  1.000 69.77000  ? 431 ALA B CB     1 
ATOM   8136  N  N      . ASP B 1 441 ? -15.06900 -7.67200  20.18200  1.000 54.66000  ? 432 ASP B N      1 
ATOM   8137  C  CA     . ASP B 1 441 ? -15.84700 -7.85400  21.39900  1.000 73.12000  ? 432 ASP B CA     1 
ATOM   8138  C  C      . ASP B 1 441 ? -16.99400 -6.86200  21.45100  1.000 83.26000  ? 432 ASP B C      1 
ATOM   8139  O  O      . ASP B 1 441 ? -18.15300 -7.25500  21.60100  1.000 83.80000  ? 432 ASP B O      1 
ATOM   8140  C  CB     . ASP B 1 441 ? -14.95700 -7.70700  22.63200  1.000 81.61000  ? 432 ASP B CB     1 
ATOM   8141  C  CG     . ASP B 1 441 ? -15.73400 -7.84700  23.92700  1.000 81.69000  ? 432 ASP B CG     1 
ATOM   8142  O  OD1    . ASP B 1 441 ? -16.15900 -8.97900  24.24400  1.000 75.53000  ? 432 ASP B OD1    1 
ATOM   8143  O  OD2    . ASP B 1 441 ? -15.92100 -6.82600  24.62500  1.000 74.99000  ? 432 ASP B OD2    1 
ATOM   8144  N  N      . TYR B 1 442 ? -16.69600 -5.58000  21.25200  1.000 73.35000  ? 433 TYR B N      1 
ATOM   8145  C  CA     . TYR B 1 442 ? -17.75300 -4.58200  21.26200  1.000 69.42000  ? 433 TYR B CA     1 
ATOM   8146  C  C      . TYR B 1 442 ? -18.89500 -4.99400  20.34400  1.000 79.34000  ? 433 TYR B C      1 
ATOM   8147  O  O      . TYR B 1 442 ? -20.06800 -4.79300  20.67300  1.000 91.16000  ? 433 TYR B O      1 
ATOM   8148  C  CB     . TYR B 1 442 ? -17.19600 -3.22100  20.85000  1.000 81.19000  ? 433 TYR B CB     1 
ATOM   8149  C  CG     . TYR B 1 442 ? -18.26400 -2.26700  20.37600  1.000 86.48000  ? 433 TYR B CG     1 
ATOM   8150  C  CD1    . TYR B 1 442 ? -19.18800 -1.72900  21.26400  1.000 88.85000  ? 433 TYR B CD1    1 
ATOM   8151  C  CD2    . TYR B 1 442 ? -18.36200 -1.91900  19.03700  1.000 98.23000  ? 433 TYR B CD2    1 
ATOM   8152  C  CE1    . TYR B 1 442 ? -20.17300 -0.86500  20.83100  1.000 105.38000 ? 433 TYR B CE1    1 
ATOM   8153  C  CE2    . TYR B 1 442 ? -19.34100 -1.06000  18.59500  1.000 115.87000 ? 433 TYR B CE2    1 
ATOM   8154  C  CZ     . TYR B 1 442 ? -20.24500 -0.53400  19.49500  1.000 128.49000 ? 433 TYR B CZ     1 
ATOM   8155  O  OH     . TYR B 1 442 ? -21.22400 0.32600   19.05300  1.000 173.75000 ? 433 TYR B OH     1 
ATOM   8156  N  N      . PHE B 1 443 ? -18.56700 -5.57800  19.18800  1.000 89.54000  ? 434 PHE B N      1 
ATOM   8157  C  CA     . PHE B 1 443 ? -19.60000 -5.97000  18.23400  1.000 86.05000  ? 434 PHE B CA     1 
ATOM   8158  C  C      . PHE B 1 443 ? -20.41400 -7.16100  18.73900  1.000 73.39000  ? 434 PHE B C      1 
ATOM   8159  O  O      . PHE B 1 443 ? -21.64200 -7.07500  18.86400  1.000 80.55000  ? 434 PHE B O      1 
ATOM   8160  C  CB     . PHE B 1 443 ? -18.97700 -6.28200  16.86900  1.000 82.99000  ? 434 PHE B CB     1 
ATOM   8161  C  CG     . PHE B 1 443 ? -18.55300 -5.06200  16.09400  1.000 77.81000  ? 434 PHE B CG     1 
ATOM   8162  C  CD1    . PHE B 1 443 ? -19.39000 -3.96500  15.98300  1.000 66.62000  ? 434 PHE B CD1    1 
ATOM   8163  C  CD2    . PHE B 1 443 ? -17.33300 -5.03200  15.43800  1.000 86.17000  ? 434 PHE B CD2    1 
ATOM   8164  C  CE1    . PHE B 1 443 ? -19.00900 -2.85000  15.25300  1.000 61.57000  ? 434 PHE B CE1    1 
ATOM   8165  C  CE2    . PHE B 1 443 ? -16.94500 -3.91700  14.70100  1.000 84.14000  ? 434 PHE B CE2    1 
ATOM   8166  C  CZ     . PHE B 1 443 ? -17.78800 -2.82500  14.61000  1.000 65.90000  ? 434 PHE B CZ     1 
ATOM   8167  N  N      . ALA B 1 444 ? -19.75700 -8.28800  19.03100  1.000 78.68000  ? 435 ALA B N      1 
ATOM   8168  C  CA     . ALA B 1 444 ? -20.51600 -9.52100  19.24900  1.000 86.18000  ? 435 ALA B CA     1 
ATOM   8169  C  C      . ALA B 1 444 ? -19.85200 -10.41300 20.28500  1.000 94.78000  ? 435 ALA B C      1 
ATOM   8170  O  O      . ALA B 1 444 ? -19.78800 -11.63300 20.11000  1.000 83.14000  ? 435 ALA B O      1 
ATOM   8171  C  CB     . ALA B 1 444 ? -20.72400 -10.30400 17.94800  1.000 81.32000  ? 435 ALA B CB     1 
ATOM   8172  N  N      . GLY B 1 445 ? -19.29700 -9.82600  21.34000  1.000 88.74000  ? 436 GLY B N      1 
ATOM   8173  C  CA     . GLY B 1 445 ? -18.74600 -10.69100 22.36000  1.000 82.79000  ? 436 GLY B CA     1 
ATOM   8174  C  C      . GLY B 1 445 ? -17.62800 -11.61500 21.88000  1.000 66.09000  ? 436 GLY B C      1 
ATOM   8175  O  O      . GLY B 1 445 ? -16.93700 -11.37800 20.88200  1.000 55.78000  ? 436 GLY B O      1 
ATOM   8176  N  N      . LEU B 1 446 ? -17.46700 -12.70400 22.63300  1.000 72.61000  ? 437 LEU B N      1 
ATOM   8177  C  CA     . LEU B 1 446 ? -16.41500 -13.66800 22.32900  1.000 73.46000  ? 437 LEU B CA     1 
ATOM   8178  C  C      . LEU B 1 446 ? -16.71900 -14.43700 21.05100  1.000 65.84000  ? 437 LEU B C      1 
ATOM   8179  O  O      . LEU B 1 446 ? -15.80100 -14.78700 20.29500  1.000 64.96000  ? 437 LEU B O      1 
ATOM   8180  C  CB     . LEU B 1 446 ? -16.22700 -14.61800 23.50800  1.000 71.04000  ? 437 LEU B CB     1 
ATOM   8181  C  CG     . LEU B 1 446 ? -15.82600 -13.95400 24.82800  1.000 50.61000  ? 437 LEU B CG     1 
ATOM   8182  C  CD1    . LEU B 1 446 ? -15.87900 -14.94700 25.98400  1.000 53.61000  ? 437 LEU B CD1    1 
ATOM   8183  C  CD2    . LEU B 1 446 ? -14.44100 -13.33200 24.70200  1.000 56.64000  ? 437 LEU B CD2    1 
ATOM   8184  N  N      . TYR B 1 447 ? -17.99600 -14.73200 20.80200  1.000 65.01000  ? 438 TYR B N      1 
ATOM   8185  C  CA     . TYR B 1 447 ? -18.36000 -15.34400 19.53000  1.000 73.94000  ? 438 TYR B CA     1 
ATOM   8186  C  C      . TYR B 1 447 ? -17.90100 -14.47700 18.36700  1.000 79.02000  ? 438 TYR B C      1 
ATOM   8187  O  O      . TYR B 1 447 ? -17.38100 -14.98300 17.36600  1.000 77.06000  ? 438 TYR B O      1 
ATOM   8188  C  CB     . TYR B 1 447 ? -19.87000 -15.57000 19.46900  1.000 65.33000  ? 438 TYR B CB     1 
ATOM   8189  C  CG     . TYR B 1 447 ? -20.33800 -16.18800 18.17500  1.000 65.88000  ? 438 TYR B CG     1 
ATOM   8190  C  CD1    . TYR B 1 447 ? -20.20000 -17.55100 17.93500  1.000 70.97000  ? 438 TYR B CD1    1 
ATOM   8191  C  CD2    . TYR B 1 447 ? -20.90800 -15.40300 17.18600  1.000 70.64000  ? 438 TYR B CD2    1 
ATOM   8192  C  CE1    . TYR B 1 447 ? -20.63000 -18.11200 16.74400  1.000 79.29000  ? 438 TYR B CE1    1 
ATOM   8193  C  CE2    . TYR B 1 447 ? -21.33700 -15.95000 15.99700  1.000 73.27000  ? 438 TYR B CE2    1 
ATOM   8194  C  CZ     . TYR B 1 447 ? -21.19800 -17.30400 15.77800  1.000 81.29000  ? 438 TYR B CZ     1 
ATOM   8195  O  OH     . TYR B 1 447 ? -21.62900 -17.84800 14.58900  1.000 82.12000  ? 438 TYR B OH     1 
ATOM   8196  N  N      . GLY B 1 448 ? -18.05300 -13.15900 18.49700  1.000 66.94000  ? 439 GLY B N      1 
ATOM   8197  C  CA     . GLY B 1 448 ? -17.59200 -12.25300 17.46600  1.000 63.73000  ? 439 GLY B CA     1 
ATOM   8198  C  C      . GLY B 1 448 ? -16.08600 -12.13100 17.41000  1.000 76.24000  ? 439 GLY B C      1 
ATOM   8199  O  O      . GLY B 1 448 ? -15.53100 -11.86400 16.34900  1.000 79.10000  ? 439 GLY B O      1 
ATOM   8200  N  N      . VAL B 1 449 ? -15.40600 -12.28400 18.54700  1.000 76.79000  ? 440 VAL B N      1 
ATOM   8201  C  CA     . VAL B 1 449 ? -13.94300 -12.35000 18.51600  1.000 65.19000  ? 440 VAL B CA     1 
ATOM   8202  C  C      . VAL B 1 449 ? -13.49200 -13.53400 17.66300  1.000 69.14000  ? 440 VAL B C      1 
ATOM   8203  O  O      . VAL B 1 449 ? -12.59100 -13.42400 16.81700  1.000 65.93000  ? 440 VAL B O      1 
ATOM   8204  C  CB     . VAL B 1 449 ? -13.37300 -12.43800 19.94300  1.000 34.43000  ? 440 VAL B CB     1 
ATOM   8205  C  CG1    . VAL B 1 449 ? -11.86700 -12.57500 19.89000  1.000 27.40000  ? 440 VAL B CG1    1 
ATOM   8206  C  CG2    . VAL B 1 449 ? -13.76600 -11.21700 20.74900  1.000 46.23000  ? 440 VAL B CG2    1 
ATOM   8207  N  N      . ALA B 1 450 ? -14.12900 -14.68700 17.87100  1.000 70.20000  ? 441 ALA B N      1 
ATOM   8208  C  CA     . ALA B 1 450 ? -13.81300 -15.85900 17.06000  1.000 71.81000  ? 441 ALA B CA     1 
ATOM   8209  C  C      . ALA B 1 450 ? -14.19500 -15.63100 15.60400  1.000 63.85000  ? 441 ALA B C      1 
ATOM   8210  O  O      . ALA B 1 450 ? -13.47800 -16.05400 14.68900  1.000 64.19000  ? 441 ALA B O      1 
ATOM   8211  C  CB     . ALA B 1 450 ? -14.52100 -17.09100 17.62000  1.000 81.62000  ? 441 ALA B CB     1 
ATOM   8212  N  N      . ILE B 1 451 ? -15.33400 -14.97600 15.37200  1.000 61.52000  ? 442 ILE B N      1 
ATOM   8213  C  CA     . ILE B 1 451 ? -15.75400 -14.65500 14.01200  1.000 74.57000  ? 442 ILE B CA     1 
ATOM   8214  C  C      . ILE B 1 451 ? -14.76600 -13.70200 13.35600  1.000 75.10000  ? 442 ILE B C      1 
ATOM   8215  O  O      . ILE B 1 451 ? -14.54500 -13.76200 12.14500  1.000 70.18000  ? 442 ILE B O      1 
ATOM   8216  C  CB     . ILE B 1 451 ? -17.18200 -14.07700 14.01600  1.000 59.76000  ? 442 ILE B CB     1 
ATOM   8217  C  CG1    . ILE B 1 451 ? -18.18600 -15.15400 14.43600  1.000 59.03000  ? 442 ILE B CG1    1 
ATOM   8218  C  CG2    . ILE B 1 451 ? -17.52800 -13.50000 12.65000  1.000 54.45000  ? 442 ILE B CG2    1 
ATOM   8219  C  CD1    . ILE B 1 451 ? -18.11900 -16.41600 13.60300  1.000 71.02000  ? 442 ILE B CD1    1 
ATOM   8220  N  N      . ALA B 1 452 ? -14.17000 -12.79900 14.13400  1.000 69.10000  ? 443 ALA B N      1 
ATOM   8221  C  CA     . ALA B 1 452 ? -13.16800 -11.89400 13.59300  1.000 61.07000  ? 443 ALA B CA     1 
ATOM   8222  C  C      . ALA B 1 452 ? -11.90600 -12.65200 13.22100  1.000 58.76000  ? 443 ALA B C      1 
ATOM   8223  O  O      . ALA B 1 452 ? -11.28300 -12.36600 12.19400  1.000 70.86000  ? 443 ALA B O      1 
ATOM   8224  C  CB     . ALA B 1 452 ? -12.85700 -10.79100 14.60300  1.000 58.99000  ? 443 ALA B CB     1 
ATOM   8225  N  N      . ALA B 1 453 ? -11.51500 -13.62400 14.04700  1.000 54.71000  ? 444 ALA B N      1 
ATOM   8226  C  CA     . ALA B 1 453 ? -10.41100 -14.50100 13.66300  1.000 75.96000  ? 444 ALA B CA     1 
ATOM   8227  C  C      . ALA B 1 453 ? -10.72300 -15.22900 12.36000  1.000 69.87000  ? 444 ALA B C      1 
ATOM   8228  O  O      . ALA B 1 453 ? -9.88300  -15.30000 11.45000  1.000 71.66000  ? 444 ALA B O      1 
ATOM   8229  C  CB     . ALA B 1 453 ? -10.11900 -15.49900 14.78500  1.000 85.95000  ? 444 ALA B CB     1 
ATOM   8230  N  N      . LEU B 1 454 ? -11.93800 -15.76600 12.25200  1.000 71.58000  ? 445 LEU B N      1 
ATOM   8231  C  CA     . LEU B 1 454 ? -12.35900 -16.44400 11.03100  1.000 86.57000  ? 445 LEU B CA     1 
ATOM   8232  C  C      . LEU B 1 454 ? -12.29800 -15.50500 9.83000   1.000 95.95000  ? 445 LEU B C      1 
ATOM   8233  O  O      . LEU B 1 454 ? -11.79800 -15.87400 8.76200   1.000 83.89000  ? 445 LEU B O      1 
ATOM   8234  C  CB     . LEU B 1 454 ? -13.77000 -17.00000 11.21900  1.000 92.00000  ? 445 LEU B CB     1 
ATOM   8235  C  CG     . LEU B 1 454 ? -14.48900 -17.54000 9.98600   1.000 85.69000  ? 445 LEU B CG     1 
ATOM   8236  C  CD1    . LEU B 1 454 ? -13.74600 -18.75000 9.43200   1.000 92.34000  ? 445 LEU B CD1    1 
ATOM   8237  C  CD2    . LEU B 1 454 ? -15.92200 -17.89700 10.33300  1.000 84.64000  ? 445 LEU B CD2    1 
ATOM   8238  N  N      . GLY B 1 455 ? -12.80400 -14.28000 9.99100   1.000 97.58000  ? 446 GLY B N      1 
ATOM   8239  C  CA     . GLY B 1 455 ? -12.74300 -13.31100 8.91000   1.000 84.52000  ? 446 GLY B CA     1 
ATOM   8240  C  C      . GLY B 1 455 ? -11.31600 -13.01600 8.50300   1.000 86.78000  ? 446 GLY B C      1 
ATOM   8241  O  O      . GLY B 1 455 ? -10.99300 -12.96600 7.31300   1.000 89.10000  ? 446 GLY B O      1 
ATOM   8242  N  N      . MET B 1 456 ? -10.43900 -12.83300 9.49100   1.000 88.11000  ? 447 MET B N      1 
ATOM   8243  C  CA     . MET B 1 456 ? -9.01600  -12.70500 9.21900   1.000 73.92000  ? 447 MET B CA     1 
ATOM   8244  C  C      . MET B 1 456 ? -8.53800  -13.85400 8.34800   1.000 84.47000  ? 447 MET B C      1 
ATOM   8245  O  O      . MET B 1 456 ? -7.74400  -13.65900 7.42000   1.000 80.23000  ? 447 MET B O      1 
ATOM   8246  C  CB     . MET B 1 456 ? -8.24500  -12.67200 10.53800  1.000 59.38000  ? 447 MET B CB     1 
ATOM   8247  C  CG     . MET B 1 456 ? -6.74800  -12.52600 10.39200  1.000 80.07000  ? 447 MET B CG     1 
ATOM   8248  S  SD     . MET B 1 456 ? -5.94000  -12.54700 12.00300  1.000 43.40000  ? 447 MET B SD     1 
ATOM   8249  C  CE     . MET B 1 456 ? -4.26700  -12.12600 11.54400  1.000 61.80000  ? 447 MET B CE     1 
ATOM   8250  N  N      . LEU B 1 457 ? -9.01700  -15.06500 8.63300   1.000 90.66000  ? 448 LEU B N      1 
ATOM   8251  C  CA     . LEU B 1 457 ? -8.66900  -16.24900 7.86000   1.000 87.79000  ? 448 LEU B CA     1 
ATOM   8252  C  C      . LEU B 1 457 ? -9.76900  -16.66400 6.88700   1.000 91.36000  ? 448 LEU B C      1 
ATOM   8253  O  O      . LEU B 1 457 ? -9.78900  -17.82000 6.44900   1.000 102.56000 ? 448 LEU B O      1 
ATOM   8254  C  CB     . LEU B 1 457 ? -8.33700  -17.41200 8.79100   1.000 73.50000  ? 448 LEU B CB     1 
ATOM   8255  C  CG     . LEU B 1 457 ? -7.06700  -17.25800 9.62400   1.000 77.20000  ? 448 LEU B CG     1 
ATOM   8256  C  CD1    . LEU B 1 457 ? -7.16200  -18.07200 10.91200  1.000 82.49000  ? 448 LEU B CD1    1 
ATOM   8257  C  CD2    . LEU B 1 457 ? -5.83900  -17.65000 8.81600   1.000 66.22000  ? 448 LEU B CD2    1 
ATOM   8258  N  N      . SER B 1 458 ? -10.68800 -15.75600 6.54600   1.000 83.89000  ? 449 SER B N      1 
ATOM   8259  C  CA     . SER B 1 458 ? -11.72300 -16.10500 5.57800   1.000 107.02000 ? 449 SER B CA     1 
ATOM   8260  C  C      . SER B 1 458 ? -11.10700 -16.50600 4.24600   1.000 110.26000 ? 449 SER B C      1 
ATOM   8261  O  O      . SER B 1 458 ? -11.51400 -17.50200 3.63500   1.000 104.69000 ? 449 SER B O      1 
ATOM   8262  C  CB     . SER B 1 458 ? -12.68600 -14.93500 5.38300   1.000 103.74000 ? 449 SER B CB     1 
ATOM   8263  O  OG     . SER B 1 458 ? -13.34300 -14.60100 6.59000   1.000 109.51000 ? 449 SER B OG     1 
ATOM   8264  N  N      . PHE B 1 459 ? -10.12100 -15.74500 3.78500   1.000 99.18000  ? 450 PHE B N      1 
ATOM   8265  C  CA     . PHE B 1 459 ? -9.39500  -16.05200 2.55700   1.000 94.88000  ? 450 PHE B CA     1 
ATOM   8266  C  C      . PHE B 1 459 ? -8.15700  -16.89100 2.82800   1.000 97.57000  ? 450 PHE B C      1 
ATOM   8267  O  O      . PHE B 1 459 ? -7.08800  -16.64300 2.26300   1.000 112.92000 ? 450 PHE B O      1 
ATOM   8268  C  CB     . PHE B 1 459 ? -9.03600  -14.75700 1.83200   1.000 94.92000  ? 450 PHE B CB     1 
ATOM   8269  C  CG     . PHE B 1 459 ? -8.32900  -13.74900 2.69500   1.000 90.10000  ? 450 PHE B CG     1 
ATOM   8270  C  CD1    . PHE B 1 459 ? -9.03000  -12.98400 3.61600   1.000 99.53000  ? 450 PHE B CD1    1 
ATOM   8271  C  CD2    . PHE B 1 459 ? -6.95900  -13.57400 2.59500   1.000 109.37000 ? 450 PHE B CD2    1 
ATOM   8272  C  CE1    . PHE B 1 459 ? -8.37800  -12.05800 4.41300   1.000 114.29000 ? 450 PHE B CE1    1 
ATOM   8273  C  CE2    . PHE B 1 459 ? -6.30100  -12.65200 3.39100   1.000 117.27000 ? 450 PHE B CE2    1 
ATOM   8274  C  CZ     . PHE B 1 459 ? -7.01200  -11.89300 4.30100   1.000 116.83000 ? 450 PHE B CZ     1 
ATOM   8275  N  N      . VAL B 1 460 ? -8.27800  -17.89600 3.70000   1.000 92.19000  ? 451 VAL B N      1 
ATOM   8276  C  CA     . VAL B 1 460 ? -7.12900  -18.72400 4.05600   1.000 91.86000  ? 451 VAL B CA     1 
ATOM   8277  C  C      . VAL B 1 460 ? -6.58100  -19.45000 2.83600   1.000 107.18000 ? 451 VAL B C      1 
ATOM   8278  O  O      . VAL B 1 460 ? -5.37200  -19.69800 2.74600   1.000 118.84000 ? 451 VAL B O      1 
ATOM   8279  C  CB     . VAL B 1 460 ? -7.50600  -19.70800 5.18300   1.000 80.12000  ? 451 VAL B CB     1 
ATOM   8280  C  CG1    . VAL B 1 460 ? -8.47200  -20.75900 4.67200   1.000 83.01000  ? 451 VAL B CG1    1 
ATOM   8281  C  CG2    . VAL B 1 460 ? -6.25700  -20.36500 5.76000   1.000 69.42000  ? 451 VAL B CG2    1 
ATOM   8282  N  N      . ALA B 1 461 ? -7.44500  -19.80600 1.88200   1.000 101.20000 ? 452 ALA B N      1 
ATOM   8283  C  CA     . ALA B 1 461 ? -6.98200  -20.50700 0.68700   1.000 81.67000  ? 452 ALA B CA     1 
ATOM   8284  C  C      . ALA B 1 461 ? -6.04000  -19.63200 -0.13300  1.000 98.78000  ? 452 ALA B C      1 
ATOM   8285  O  O      . ALA B 1 461 ? -4.96700  -20.07900 -0.56100  1.000 105.51000 ? 452 ALA B O      1 
ATOM   8286  C  CB     . ALA B 1 461 ? -8.17600  -20.95400 -0.15500  1.000 73.50000  ? 452 ALA B CB     1 
ATOM   8287  N  N      . THR B 1 462 ? -6.42400  -18.37300 -0.35700  1.000 95.80000  ? 453 THR B N      1 
ATOM   8288  C  CA     . THR B 1 462 ? -5.57200  -17.46300 -1.11600  1.000 103.33000 ? 453 THR B CA     1 
ATOM   8289  C  C      . THR B 1 462 ? -4.25600  -17.21400 -0.39100  1.000 102.08000 ? 453 THR B C      1 
ATOM   8290  O  O      . THR B 1 462 ? -3.19000  -17.15300 -1.01900  1.000 111.05000 ? 453 THR B O      1 
ATOM   8291  C  CB     . THR B 1 462 ? -6.30500  -16.14400 -1.36500  1.000 112.79000 ? 453 THR B CB     1 
ATOM   8292  N  N      . SER B 1 463 ? -4.31200  -17.05700 0.93300   1.000 100.85000 ? 454 SER B N      1 
ATOM   8293  C  CA     . SER B 1 463 ? -3.09200  -16.86400 1.70800   1.000 104.56000 ? 454 SER B CA     1 
ATOM   8294  C  C      . SER B 1 463 ? -2.16300  -18.06300 1.56100   1.000 104.45000 ? 454 SER B C      1 
ATOM   8295  O  O      . SER B 1 463 ? -0.95900  -17.90600 1.32900   1.000 112.99000 ? 454 SER B O      1 
ATOM   8296  C  CB     . SER B 1 463 ? -3.43600  -16.62100 3.18000   1.000 109.95000 ? 454 SER B CB     1 
ATOM   8297  O  OG     . SER B 1 463 ? -4.22000  -15.45000 3.34300   1.000 106.52000 ? 454 SER B OG     1 
ATOM   8298  N  N      . VAL B 1 464 ? -2.71000  -19.27400 1.69400   1.000 77.80000  ? 455 VAL B N      1 
ATOM   8299  C  CA     . VAL B 1 464 ? -1.88600  -20.47500 1.58600   1.000 75.25000  ? 455 VAL B CA     1 
ATOM   8300  C  C      . VAL B 1 464 ? -1.29200  -20.59600 0.18800   1.000 97.05000  ? 455 VAL B C      1 
ATOM   8301  O  O      . VAL B 1 464 ? -0.14100  -21.01600 0.02400   1.000 100.20000 ? 455 VAL B O      1 
ATOM   8302  C  CB     . VAL B 1 464 ? -2.70900  -21.72100 1.96400   1.000 78.06000  ? 455 VAL B CB     1 
ATOM   8303  C  CG1    . VAL B 1 464 ? -1.87000  -22.98300 1.80300   1.000 93.52000  ? 455 VAL B CG1    1 
ATOM   8304  C  CG2    . VAL B 1 464 ? -3.22800  -21.60000 3.38700   1.000 77.13000  ? 455 VAL B CG2    1 
ATOM   8305  N  N      . SER B 1 465 ? -2.05300  -20.21200 -0.84000  1.000 102.96000 ? 456 SER B N      1 
ATOM   8306  C  CA     . SER B 1 465 ? -1.54400  -20.30800 -2.20700  1.000 106.78000 ? 456 SER B CA     1 
ATOM   8307  C  C      . SER B 1 465 ? -0.39500  -19.33100 -2.43800  1.000 117.05000 ? 456 SER B C      1 
ATOM   8308  O  O      . SER B 1 465 ? 0.65000   -19.69900 -2.99500  1.000 111.44000 ? 456 SER B O      1 
ATOM   8309  C  CB     . SER B 1 465 ? -2.67300  -20.06200 -3.20600  1.000 91.15000  ? 456 SER B CB     1 
ATOM   8310  O  OG     . SER B 1 465 ? -3.15500  -18.73400 -3.11300  1.000 112.77000 ? 456 SER B OG     1 
ATOM   8311  N  N      . VAL B 1 466 ? -0.57000  -18.07700 -2.01500  1.000 126.56000 ? 457 VAL B N      1 
ATOM   8312  C  CA     . VAL B 1 466 ? 0.50100   -17.09400 -2.16600  1.000 114.12000 ? 457 VAL B CA     1 
ATOM   8313  C  C      . VAL B 1 466 ? 1.72400   -17.51500 -1.36100  1.000 106.80000 ? 457 VAL B C      1 
ATOM   8314  O  O      . VAL B 1 466 ? 2.86800   -17.30500 -1.78300  1.000 107.21000 ? 457 VAL B O      1 
ATOM   8315  C  CB     . VAL B 1 466 ? 0.00700   -15.69300 -1.75900  1.000 117.88000 ? 457 VAL B CB     1 
ATOM   8316  C  CG1    . VAL B 1 466 ? 1.16800   -14.70200 -1.75800  1.000 109.47000 ? 457 VAL B CG1    1 
ATOM   8317  C  CG2    . VAL B 1 466 ? -1.09500  -15.22800 -2.69400  1.000 128.37000 ? 457 VAL B CG2    1 
ATOM   8318  N  N      . ASP B 1 467 ? 1.50500   -18.11500 -0.18900  1.000 98.03000  ? 458 ASP B N      1 
ATOM   8319  C  CA     . ASP B 1 467 ? 2.62400   -18.57000 0.62800   1.000 95.29000  ? 458 ASP B CA     1 
ATOM   8320  C  C      . ASP B 1 467 ? 3.36900   -19.71600 -0.04500  1.000 115.65000 ? 458 ASP B C      1 
ATOM   8321  O  O      . ASP B 1 467 ? 4.60500   -19.76100 -0.01900  1.000 125.57000 ? 458 ASP B O      1 
ATOM   8322  C  CB     . ASP B 1 467 ? 2.12100   -18.98500 2.00900   1.000 105.81000 ? 458 ASP B CB     1 
ATOM   8323  C  CG     . ASP B 1 467 ? 1.68000   -17.80000 2.84300   1.000 105.03000 ? 458 ASP B CG     1 
ATOM   8324  O  OD1    . ASP B 1 467 ? 2.02200   -16.65800 2.47300   1.000 97.47000  ? 458 ASP B OD1    1 
ATOM   8325  O  OD2    . ASP B 1 467 ? 0.99000   -18.00900 3.86300   1.000 115.75000 ? 458 ASP B OD2    1 
ATOM   8326  N  N      . SER B 1 468 ? 2.63300   -20.64900 -0.65700  1.000 115.29000 ? 459 SER B N      1 
ATOM   8327  C  CA     . SER B 1 468 ? 3.26700   -21.74900 -1.37600  1.000 110.51000 ? 459 SER B CA     1 
ATOM   8328  C  C      . SER B 1 468 ? 4.03600   -21.24300 -2.58500  1.000 97.80000  ? 459 SER B C      1 
ATOM   8329  O  O      . SER B 1 468 ? 5.04800   -21.83700 -2.97400  1.000 84.74000  ? 459 SER B O      1 
ATOM   8330  C  CB     . SER B 1 468 ? 2.21700   -22.77500 -1.80300  1.000 112.41000 ? 459 SER B CB     1 
ATOM   8331  O  OG     . SER B 1 468 ? 1.48800   -23.24900 -0.68500  1.000 115.45000 ? 459 SER B OG     1 
ATOM   8332  N  N      . TYR B 1 469 ? 3.56300   -20.15800 -3.19800  1.000 100.68000 ? 460 TYR B N      1 
ATOM   8333  C  CA     . TYR B 1 469 ? 4.29800   -19.55000 -4.30200  1.000 102.79000 ? 460 TYR B CA     1 
ATOM   8334  C  C      . TYR B 1 469 ? 5.75900   -19.29700 -3.94400  1.000 107.05000 ? 460 TYR B C      1 
ATOM   8335  O  O      . TYR B 1 469 ? 6.65700   -19.57200 -4.74700  1.000 107.76000 ? 460 TYR B O      1 
ATOM   8336  C  CB     . TYR B 1 469 ? 3.61700   -18.24400 -4.70600  1.000 112.89000 ? 460 TYR B CB     1 
ATOM   8337  C  CG     . TYR B 1 469 ? 4.46500   -17.34800 -5.57800  1.000 112.55000 ? 460 TYR B CG     1 
ATOM   8338  C  CD1    . TYR B 1 469 ? 4.65700   -17.62100 -6.92500  1.000 110.42000 ? 460 TYR B CD1    1 
ATOM   8339  C  CD2    . TYR B 1 469 ? 5.09000   -16.23000 -5.04000  1.000 123.86000 ? 460 TYR B CD2    1 
ATOM   8340  C  CE1    . TYR B 1 469 ? 5.43600   -16.79400 -7.71600  1.000 111.06000 ? 460 TYR B CE1    1 
ATOM   8341  C  CE2    . TYR B 1 469 ? 5.86700   -15.40700 -5.81600  1.000 123.00000 ? 460 TYR B CE2    1 
ATOM   8342  C  CZ     . TYR B 1 469 ? 6.03900   -15.69000 -7.15200  1.000 112.74000 ? 460 TYR B CZ     1 
ATOM   8343  O  OH     . TYR B 1 469 ? 6.81800   -14.85700 -7.91600  1.000 106.89000 ? 460 TYR B OH     1 
ATOM   8344  N  N      . GLY B 1 470 ? 6.01600   -18.78300 -2.74500  1.000 107.29000 ? 461 GLY B N      1 
ATOM   8345  C  CA     . GLY B 1 470 ? 7.35200   -18.40400 -2.34100  1.000 114.50000 ? 461 GLY B CA     1 
ATOM   8346  C  C      . GLY B 1 470 ? 8.39800   -19.48800 -2.51100  1.000 111.27000 ? 461 GLY B C      1 
ATOM   8347  O  O      . GLY B 1 470 ? 9.42800   -19.29600 -3.16800  1.000 113.78000 ? 461 GLY B O      1 
ATOM   8348  N  N      . PRO B 1 471 ? 8.15000   -20.65600 -1.91800  1.000 102.97000 ? 462 PRO B N      1 
ATOM   8349  C  CA     . PRO B 1 471 ? 9.14200   -21.73700 -2.02400  1.000 107.36000 ? 462 PRO B CA     1 
ATOM   8350  C  C      . PRO B 1 471 ? 9.40800   -22.15900 -3.45400  1.000 109.28000 ? 462 PRO B C      1 
ATOM   8351  O  O      . PRO B 1 471 ? 10.55000  -22.48800 -3.79100  1.000 117.36000 ? 462 PRO B O      1 
ATOM   8352  C  CB     . PRO B 1 471 ? 8.51800   -22.86800 -1.19400  1.000 113.58000 ? 462 PRO B CB     1 
ATOM   8353  C  CG     . PRO B 1 471 ? 7.53500   -22.18500 -0.28900  1.000 123.97000 ? 462 PRO B CG     1 
ATOM   8354  C  CD     . PRO B 1 471 ? 7.00000   -21.03900 -1.08400  1.000 105.90000 ? 462 PRO B CD     1 
ATOM   8355  N  N      . ILE B 1 472 ? 8.38800   -22.17100 -4.30900  1.000 102.97000 ? 463 ILE B N      1 
ATOM   8356  C  CA     . ILE B 1 472 ? 8.61700   -22.53400 -5.70300  1.000 104.98000 ? 463 ILE B CA     1 
ATOM   8357  C  C      . ILE B 1 472 ? 9.56100   -21.53200 -6.36400  1.000 103.75000 ? 463 ILE B C      1 
ATOM   8358  O  O      . ILE B 1 472 ? 10.45400  -21.90900 -7.13200  1.000 116.95000 ? 463 ILE B O      1 
ATOM   8359  C  CB     . ILE B 1 472 ? 7.27800   -22.65600 -6.45200  1.000 109.54000 ? 463 ILE B CB     1 
ATOM   8360  C  CG1    . ILE B 1 472 ? 6.34100   -23.61700 -5.71400  1.000 105.51000 ? 463 ILE B CG1    1 
ATOM   8361  C  CG2    . ILE B 1 472 ? 7.50600   -23.15100 -7.87600  1.000 117.85000 ? 463 ILE B CG2    1 
ATOM   8362  C  CD1    . ILE B 1 472 ? 5.04400   -23.88200 -6.45200  1.000 95.50000  ? 463 ILE B CD1    1 
ATOM   8363  N  N      . ALA B 1 473 ? 9.39100   -20.24100 -6.06800  1.000 89.37000  ? 464 ALA B N      1 
ATOM   8364  C  CA     . ALA B 1 473 ? 10.29400  -19.23400 -6.61900  1.000 104.51000 ? 464 ALA B CA     1 
ATOM   8365  C  C      . ALA B 1 473 ? 11.70900  -19.41400 -6.08300  1.000 122.89000 ? 464 ALA B C      1 
ATOM   8366  O  O      . ALA B 1 473 ? 12.68900  -19.24600 -6.82300  1.000 130.80000 ? 464 ALA B O      1 
ATOM   8367  C  CB     . ALA B 1 473 ? 9.77100   -17.83400 -6.31000  1.000 106.60000 ? 464 ALA B CB     1 
ATOM   8368  N  N      . ASP B 1 474 ? 11.83600  -19.73900 -4.79300  1.000 119.63000 ? 465 ASP B N      1 
ATOM   8369  C  CA     . ASP B 1 474 ? 13.15800  -19.98400 -4.22300  1.000 121.66000 ? 465 ASP B CA     1 
ATOM   8370  C  C      . ASP B 1 474 ? 13.82700  -21.15800 -4.92600  1.000 132.92000 ? 465 ASP B C      1 
ATOM   8371  O  O      . ASP B 1 474 ? 15.02300  -21.11200 -5.24400  1.000 139.50000 ? 465 ASP B O      1 
ATOM   8372  C  CB     . ASP B 1 474 ? 13.04400  -20.23800 -2.71700  1.000 114.95000 ? 465 ASP B CB     1 
ATOM   8373  C  CG     . ASP B 1 474 ? 14.34400  -20.71600 -2.10200  1.000 114.77000 ? 465 ASP B CG     1 
ATOM   8374  O  OD1    . ASP B 1 474 ? 14.74700  -21.86800 -2.35900  1.000 122.63000 ? 465 ASP B OD1    1 
ATOM   8375  O  OD2    . ASP B 1 474 ? 14.96800  -19.93000 -1.35800  1.000 115.24000 ? 465 ASP B OD2    1 
ATOM   8376  N  N      . ASN B 1 475 ? 13.06200  -22.22500 -5.16800  1.000 131.45000 ? 466 ASN B N      1 
ATOM   8377  C  CA     . ASN B 1 475 ? 13.58700  -23.38300 -5.87800  1.000 130.17000 ? 466 ASN B CA     1 
ATOM   8378  C  C      . ASN B 1 475 ? 13.96100  -23.03200 -7.31000  1.000 123.17000 ? 466 ASN B C      1 
ATOM   8379  O  O      . ASN B 1 475 ? 14.92000  -23.58100 -7.85600  1.000 137.86000 ? 466 ASN B O      1 
ATOM   8380  C  CB     . ASN B 1 475 ? 12.56800  -24.52300 -5.85600  1.000 135.84000 ? 466 ASN B CB     1 
ATOM   8381  C  CG     . ASN B 1 475 ? 12.66600  -25.37200 -4.60100  1.000 144.74000 ? 466 ASN B CG     1 
ATOM   8382  O  OD1    . ASN B 1 475 ? 12.03800  -26.42800 -4.49600  1.000 143.88000 ? 466 ASN B OD1    1 
ATOM   8383  N  ND2    . ASN B 1 475 ? 13.45300  -24.90800 -3.63800  1.000 144.71000 ? 466 ASN B ND2    1 
ATOM   8384  N  N      . ALA B 1 476 ? 13.21400  -22.12800 -7.94500  1.000 108.17000 ? 467 ALA B N      1 
ATOM   8385  C  CA     . ALA B 1 476 ? 13.57800  -21.71500 -9.29800  1.000 112.06000 ? 467 ALA B CA     1 
ATOM   8386  C  C      . ALA B 1 476 ? 14.89900  -20.95200 -9.30700  1.000 133.59000 ? 467 ALA B C      1 
ATOM   8387  O  O      . ALA B 1 476 ? 15.74900  -21.16800 -10.18200 1.000 134.33000 ? 467 ALA B O      1 
ATOM   8388  C  CB     . ALA B 1 476 ? 12.46300  -20.87100 -9.91100  1.000 118.60000 ? 467 ALA B CB     1 
ATOM   8389  N  N      . GLY B 1 477 ? 15.09400  -20.05500 -8.34000  1.000 135.62000 ? 468 GLY B N      1 
ATOM   8390  C  CA     . GLY B 1 477 ? 16.37800  -19.37500 -8.24700  1.000 135.79000 ? 468 GLY B CA     1 
ATOM   8391  C  C      . GLY B 1 477 ? 17.52400  -20.33500 -7.98200  1.000 135.01000 ? 468 GLY B C      1 
ATOM   8392  O  O      . GLY B 1 477 ? 18.58700  -20.24600 -8.60900  1.000 148.77000 ? 468 GLY B O      1 
ATOM   8393  N  N      . GLY B 1 478 ? 17.30800  -21.29000 -7.07600  1.000 127.95000 ? 469 GLY B N      1 
ATOM   8394  C  CA     . GLY B 1 478 ? 18.30900  -22.31900 -6.84700  1.000 129.09000 ? 469 GLY B CA     1 
ATOM   8395  C  C      . GLY B 1 478 ? 18.59300  -23.13500 -8.09100  1.000 133.46000 ? 469 GLY B C      1 
ATOM   8396  O  O      . GLY B 1 478 ? 19.73600  -23.52300 -8.34400  1.000 139.51000 ? 469 GLY B O      1 
ATOM   8397  N  N      . ILE B 1 479 ? 17.55500  -23.40700 -8.88300  1.000 138.58000 ? 470 ILE B N      1 
ATOM   8398  C  CA     . ILE B 1 479 ? 17.72300  -24.15800 -10.12100 1.000 141.30000 ? 470 ILE B CA     1 
ATOM   8399  C  C      . ILE B 1 479 ? 18.58900  -23.37000 -11.08700 1.000 143.67000 ? 470 ILE B C      1 
ATOM   8400  O  O      . ILE B 1 479 ? 19.43400  -23.93000 -11.79600 1.000 155.71000 ? 470 ILE B O      1 
ATOM   8401  C  CB     . ILE B 1 479 ? 16.34600  -24.46700 -10.73600 1.000 133.76000 ? 470 ILE B CB     1 
ATOM   8402  C  CG1    . ILE B 1 479 ? 15.61500  -25.53500 -9.92500  1.000 126.12000 ? 470 ILE B CG1    1 
ATOM   8403  C  CG2    . ILE B 1 479 ? 16.48700  -24.89300 -12.18600 1.000 122.17000 ? 470 ILE B CG2    1 
ATOM   8404  C  CD1    . ILE B 1 479 ? 14.11300  -25.47700 -10.07200 1.000 124.01000 ? 470 ILE B CD1    1 
ATOM   8405  N  N      . SER B 1 480 ? 18.38000  -22.05600 -11.13700 1.000 139.59000 ? 471 SER B N      1 
ATOM   8406  C  CA     . SER B 1 480 ? 19.26300  -21.20400 -11.92500 1.000 159.39000 ? 471 SER B CA     1 
ATOM   8407  C  C      . SER B 1 480 ? 20.69600  -21.29600 -11.42000 1.000 163.06000 ? 471 SER B C      1 
ATOM   8408  O  O      . SER B 1 480 ? 21.64500  -21.27800 -12.21200 1.000 168.78000 ? 471 SER B O      1 
ATOM   8409  C  CB     . SER B 1 480 ? 18.77900  -19.75500 -11.89900 1.000 171.78000 ? 471 SER B CB     1 
ATOM   8410  O  OG     . SER B 1 480 ? 19.39600  -19.03000 -10.85000 1.000 169.08000 ? 471 SER B OG     1 
ATOM   8411  N  N      . GLU B 1 481 ? 20.87300  -21.40000 -10.09900 1.000 161.32000 ? 472 GLU B N      1 
ATOM   8412  C  CA     . GLU B 1 481 ? 22.22400  -21.49700 -9.55500  1.000 158.90000 ? 472 GLU B CA     1 
ATOM   8413  C  C      . GLU B 1 481 ? 22.86800  -22.85000 -9.84000  1.000 152.51000 ? 472 GLU B C      1 
ATOM   8414  O  O      . GLU B 1 481 ? 24.10100  -22.95000 -9.83400  1.000 150.49000 ? 472 GLU B O      1 
ATOM   8415  C  CB     . GLU B 1 481 ? 22.21200  -21.23300 -8.04900  1.000 153.10000 ? 472 GLU B CB     1 
ATOM   8416  C  CG     . GLU B 1 481 ? 21.49000  -19.96000 -7.62100  1.000 157.51000 ? 472 GLU B CG     1 
ATOM   8417  C  CD     . GLU B 1 481 ? 22.00100  -18.72300 -8.34500  1.000 167.02000 ? 472 GLU B CD     1 
ATOM   8418  O  OE1    . GLU B 1 481 ? 23.22200  -18.63400 -8.59200  1.000 174.91000 ? 472 GLU B OE1    1 
ATOM   8419  O  OE2    . GLU B 1 481 ? 21.18200  -17.83600 -8.66600  1.000 158.89000 ? 472 GLU B OE2    1 
ATOM   8420  N  N      . MET B 1 482 ? 22.07700  -23.88600 -10.11100 1.000 151.34000 ? 473 MET B N      1 
ATOM   8421  C  CA     . MET B 1 482 ? 22.64400  -25.17900 -10.50600 1.000 148.12000 ? 473 MET B CA     1 
ATOM   8422  C  C      . MET B 1 482 ? 22.39700  -25.48800 -11.98500 1.000 134.25000 ? 473 MET B C      1 
ATOM   8423  O  O      . MET B 1 482 ? 21.75500  -26.48000 -12.33000 1.000 120.46000 ? 473 MET B O      1 
ATOM   8424  C  CB     . MET B 1 482 ? 22.09200  -26.30700 -9.62800  1.000 143.79000 ? 473 MET B CB     1 
ATOM   8425  C  CG     . MET B 1 482 ? 22.36100  -26.11600 -8.14100  1.000 149.10000 ? 473 MET B CG     1 
ATOM   8426  S  SD     . MET B 1 482 ? 22.05400  -27.60900 -7.17700  1.000 166.26000 ? 473 MET B SD     1 
ATOM   8427  C  CE     . MET B 1 482 ? 23.10800  -28.78800 -8.01600  1.000 142.96000 ? 473 MET B CE     1 
ATOM   8428  N  N      . ASP B 1 486 ? 21.38500  -20.30100 -18.04200 1.000 175.55000 ? 477 ASP B N      1 
ATOM   8429  C  CA     . ASP B 1 486 ? 21.18400  -19.10800 -18.85500 1.000 189.28000 ? 477 ASP B CA     1 
ATOM   8430  C  C      . ASP B 1 486 ? 21.27000  -17.87300 -17.96400 1.000 204.71000 ? 477 ASP B C      1 
ATOM   8431  O  O      . ASP B 1 486 ? 20.68000  -17.84200 -16.88700 1.000 208.42000 ? 477 ASP B O      1 
ATOM   8432  C  CB     . ASP B 1 486 ? 19.83500  -19.18100 -19.57200 1.000 187.75000 ? 477 ASP B CB     1 
ATOM   8433  C  CG     . ASP B 1 486 ? 19.70600  -18.16900 -20.69300 1.000 203.72000 ? 477 ASP B CG     1 
ATOM   8434  O  OD1    . ASP B 1 486 ? 19.64600  -16.95500 -20.40600 1.000 214.44000 ? 477 ASP B OD1    1 
ATOM   8435  O  OD2    . ASP B 1 486 ? 19.65900  -18.59500 -21.86700 1.000 208.93000 ? 477 ASP B OD2    1 
ATOM   8436  N  N      . PRO B 1 487 ? 22.02000  -16.86000 -18.40200 1.000 207.85000 ? 478 PRO B N      1 
ATOM   8437  C  CA     . PRO B 1 487 ? 22.16400  -15.65700 -17.56000 1.000 198.42000 ? 478 PRO B CA     1 
ATOM   8438  C  C      . PRO B 1 487 ? 20.85200  -14.93300 -17.31100 1.000 201.75000 ? 478 PRO B C      1 
ATOM   8439  O  O      . PRO B 1 487 ? 20.54100  -14.57900 -16.16300 1.000 202.51000 ? 478 PRO B O      1 
ATOM   8440  C  CB     . PRO B 1 487 ? 23.15700  -14.79800 -18.35900 1.000 189.34000 ? 478 PRO B CB     1 
ATOM   8441  C  CG     . PRO B 1 487 ? 23.87600  -15.77300 -19.25300 1.000 190.43000 ? 478 PRO B CG     1 
ATOM   8442  C  CD     . PRO B 1 487 ? 22.85200  -16.79900 -19.61300 1.000 200.12000 ? 478 PRO B CD     1 
ATOM   8443  N  N      . GLU B 1 488 ? 20.05600  -14.72100 -18.36000 1.000 203.16000 ? 479 GLU B N      1 
ATOM   8444  C  CA     . GLU B 1 488 ? 18.75600  -14.08700 -18.18100 1.000 185.12000 ? 479 GLU B CA     1 
ATOM   8445  C  C      . GLU B 1 488 ? 17.85100  -14.94000 -17.30600 1.000 180.92000 ? 479 GLU B C      1 
ATOM   8446  O  O      . GLU B 1 488 ? 17.14200  -14.42100 -16.43700 1.000 180.13000 ? 479 GLU B O      1 
ATOM   8447  C  CB     . GLU B 1 488 ? 18.10700  -13.83500 -19.54000 1.000 172.47000 ? 479 GLU B CB     1 
ATOM   8448  N  N      . VAL B 1 489 ? 17.86300  -16.25600 -17.52400 1.000 186.66000 ? 480 VAL B N      1 
ATOM   8449  C  CA     . VAL B 1 489 ? 17.03900  -17.14500 -16.71400 1.000 179.68000 ? 480 VAL B CA     1 
ATOM   8450  C  C      . VAL B 1 489 ? 17.48800  -17.11200 -15.25900 1.000 187.61000 ? 480 VAL B C      1 
ATOM   8451  O  O      . VAL B 1 489 ? 16.65900  -17.08200 -14.34200 1.000 187.07000 ? 480 VAL B O      1 
ATOM   8452  C  CB     . VAL B 1 489 ? 17.07000  -18.57400 -17.28500 1.000 179.87000 ? 480 VAL B CB     1 
ATOM   8453  C  CG1    . VAL B 1 489 ? 16.48100  -19.55200 -16.28500 1.000 172.24000 ? 480 VAL B CG1    1 
ATOM   8454  C  CG2    . VAL B 1 489 ? 16.32400  -18.63000 -18.60800 1.000 173.30000 ? 480 VAL B CG2    1 
ATOM   8455  N  N      . ARG B 1 490 ? 18.80400  -17.11500 -15.01600 1.000 199.15000 ? 481 ARG B N      1 
ATOM   8456  C  CA     . ARG B 1 490 ? 19.26900  -17.10100 -13.63300 1.000 191.73000 ? 481 ARG B CA     1 
ATOM   8457  C  C      . ARG B 1 490 ? 18.87700  -15.80300 -12.93900 1.000 180.84000 ? 481 ARG B C      1 
ATOM   8458  O  O      . ARG B 1 490 ? 18.40900  -15.82200 -11.79600 1.000 167.09000 ? 481 ARG B O      1 
ATOM   8459  C  CB     . ARG B 1 490 ? 20.78200  -17.31700 -13.56100 1.000 179.53000 ? 481 ARG B CB     1 
ATOM   8460  C  CG     . ARG B 1 490 ? 21.61800  -16.25900 -14.25200 1.000 196.65000 ? 481 ARG B CG     1 
ATOM   8461  C  CD     . ARG B 1 490 ? 23.10000  -16.57300 -14.12300 1.000 202.99000 ? 481 ARG B CD     1 
ATOM   8462  N  NE     . ARG B 1 490 ? 23.93200  -15.67400 -14.91400 1.000 193.99000 ? 481 ARG B NE     1 
ATOM   8463  C  CZ     . ARG B 1 490 ? 24.35100  -14.48500 -14.50200 1.000 173.22000 ? 481 ARG B CZ     1 
ATOM   8464  N  NH1    . ARG B 1 490 ? 24.04000  -14.01800 -13.30400 1.000 164.81000 ? 481 ARG B NH1    1 
ATOM   8465  N  NH2    . ARG B 1 490 ? 25.10000  -13.74400 -15.31400 1.000 163.06000 ? 481 ARG B NH2    1 
ATOM   8466  N  N      . LYS B 1 491 ? 19.02500  -14.66500 -13.62400 1.000 180.43000 ? 482 LYS B N      1 
ATOM   8467  C  CA     . LYS B 1 491 ? 18.63800  -13.40100 -13.00100 1.000 168.58000 ? 482 LYS B CA     1 
ATOM   8468  C  C      . LYS B 1 491 ? 17.13100  -13.32800 -12.76600 1.000 172.92000 ? 482 LYS B C      1 
ATOM   8469  O  O      . LYS B 1 491 ? 16.68500  -12.85100 -11.71400 1.000 172.71000 ? 482 LYS B O      1 
ATOM   8470  C  CB     . LYS B 1 491 ? 19.12300  -12.21700 -13.83500 1.000 168.95000 ? 482 LYS B CB     1 
ATOM   8471  C  CG     . LYS B 1 491 ? 20.56300  -11.83300 -13.53900 1.000 169.44000 ? 482 LYS B CG     1 
ATOM   8472  C  CD     . LYS B 1 491 ? 20.76900  -11.72500 -12.03600 1.000 144.20000 ? 482 LYS B CD     1 
ATOM   8473  C  CE     . LYS B 1 491 ? 22.22100  -11.46300 -11.68000 1.000 135.10000 ? 482 LYS B CE     1 
ATOM   8474  N  NZ     . LYS B 1 491 ? 22.42100  -11.35700 -10.20600 1.000 123.01000 ? 482 LYS B NZ     1 
ATOM   8475  N  N      . ILE B 1 492 ? 16.32700  -13.78200 -13.73200 1.000 175.88000 ? 483 ILE B N      1 
ATOM   8476  C  CA     . ILE B 1 492 ? 14.87800  -13.70700 -13.57200 1.000 165.77000 ? 483 ILE B CA     1 
ATOM   8477  C  C      . ILE B 1 492 ? 14.42200  -14.61000 -12.43300 1.000 152.69000 ? 483 ILE B C      1 
ATOM   8478  O  O      . ILE B 1 492 ? 13.57100  -14.22700 -11.62000 1.000 142.35000 ? 483 ILE B O      1 
ATOM   8479  C  CB     . ILE B 1 492 ? 14.16600  -14.04300 -14.89600 1.000 160.65000 ? 483 ILE B CB     1 
ATOM   8480  C  CG1    . ILE B 1 492 ? 14.45600  -15.48200 -15.32300 1.000 160.22000 ? 483 ILE B CG1    1 
ATOM   8481  C  CG2    . ILE B 1 492 ? 14.57100  -13.06000 -15.98200 1.000 153.97000 ? 483 ILE B CG2    1 
ATOM   8482  C  CD1    . ILE B 1 492 ? 13.95900  -15.81700 -16.71500 1.000 148.93000 ? 483 ILE B CD1    1 
ATOM   8483  N  N      . THR B 1 493 ? 14.98200  -15.81800 -12.34500 1.000 152.89000 ? 484 THR B N      1 
ATOM   8484  C  CA     . THR B 1 493 ? 14.64800  -16.70100 -11.23500 1.000 145.69000 ? 484 THR B CA     1 
ATOM   8485  C  C      . THR B 1 493 ? 15.12100  -16.12000 -9.91100  1.000 149.29000 ? 484 THR B C      1 
ATOM   8486  O  O      . THR B 1 493 ? 14.47000  -16.30500 -8.88000  1.000 144.24000 ? 484 THR B O      1 
ATOM   8487  C  CB     . THR B 1 493 ? 15.24400  -18.08600 -11.46400 1.000 150.52000 ? 484 THR B CB     1 
ATOM   8488  O  OG1    . THR B 1 493 ? 16.67300  -17.99700 -11.45700 1.000 170.48000 ? 484 THR B OG1    1 
ATOM   8489  C  CG2    . THR B 1 493 ? 14.77200  -18.64000 -12.80000 1.000 150.04000 ? 484 THR B CG2    1 
ATOM   8490  N  N      . ASP B 1 494 ? 16.26300  -15.43300 -9.90900  1.000 157.78000 ? 485 ASP B N      1 
ATOM   8491  C  CA     . ASP B 1 494 ? 16.73600  -14.81200 -8.67800  1.000 158.30000 ? 485 ASP B CA     1 
ATOM   8492  C  C      . ASP B 1 494 ? 15.77000  -13.73100 -8.20800  1.000 152.51000 ? 485 ASP B C      1 
ATOM   8493  O  O      . ASP B 1 494 ? 15.44000  -13.64800 -7.01700  1.000 165.89000 ? 485 ASP B O      1 
ATOM   8494  C  CB     . ASP B 1 494 ? 18.13600  -14.24200 -8.91800  1.000 150.53000 ? 485 ASP B CB     1 
ATOM   8495  C  CG     . ASP B 1 494 ? 18.59600  -13.31200 -7.82500  1.000 143.53000 ? 485 ASP B CG     1 
ATOM   8496  O  OD1    . ASP B 1 494 ? 18.74600  -13.76600 -6.67200  1.000 148.19000 ? 485 ASP B OD1    1 
ATOM   8497  O  OD2    . ASP B 1 494 ? 18.83300  -12.12500 -8.13500  1.000 128.35000 ? 485 ASP B OD2    1 
ATOM   8498  N  N      . HIS B 1 495 ? 15.27400  -12.91800 -9.14200  1.000 137.08000 ? 486 HIS B N      1 
ATOM   8499  C  CA     . HIS B 1 495 ? 14.30600  -11.88700 -8.78000  1.000 144.55000 ? 486 HIS B CA     1 
ATOM   8500  C  C      . HIS B 1 495 ? 13.00000  -12.51500 -8.30300  1.000 152.79000 ? 486 HIS B C      1 
ATOM   8501  O  O      . HIS B 1 495 ? 12.37800  -12.03700 -7.34200  1.000 153.23000 ? 486 HIS B O      1 
ATOM   8502  C  CB     . HIS B 1 495 ? 14.07400  -10.96000 -9.97200  1.000 154.15000 ? 486 HIS B CB     1 
ATOM   8503  C  CG     . HIS B 1 495 ? 15.33300  -10.35900 -10.51800 1.000 168.81000 ? 486 HIS B CG     1 
ATOM   8504  N  ND1    . HIS B 1 495 ? 15.53900  -10.16600 -11.86700 1.000 172.34000 ? 486 HIS B ND1    1 
ATOM   8505  C  CD2    . HIS B 1 495 ? 16.45800  -9.92500  -9.90000  1.000 174.00000 ? 486 HIS B CD2    1 
ATOM   8506  C  CE1    . HIS B 1 495 ? 16.73200  -9.63100  -12.05600 1.000 170.88000 ? 486 HIS B CE1    1 
ATOM   8507  N  NE2    . HIS B 1 495 ? 17.31000  -9.47400  -10.87900 1.000 176.89000 ? 486 HIS B NE2    1 
ATOM   8508  N  N      . LEU B 1 496 ? 12.58800  -13.60900 -8.95000  1.000 148.27000 ? 487 LEU B N      1 
ATOM   8509  C  CA     . LEU B 1 496 ? 11.39100  -14.32100 -8.52200  1.000 126.83000 ? 487 LEU B CA     1 
ATOM   8510  C  C      . LEU B 1 496 ? 11.58000  -14.88200 -7.11800  1.000 125.15000 ? 487 LEU B C      1 
ATOM   8511  O  O      . LEU B 1 496 ? 10.64900  -14.88400 -6.30600  1.000 118.85000 ? 487 LEU B O      1 
ATOM   8512  C  CB     . LEU B 1 496 ? 11.07100  -15.43500 -9.51900  1.000 123.87000 ? 487 LEU B CB     1 
ATOM   8513  C  CG     . LEU B 1 496 ? 9.71200   -16.12800 -9.44000  1.000 118.64000 ? 487 LEU B CG     1 
ATOM   8514  C  CD1    . LEU B 1 496 ? 8.63000   -15.20300 -9.96100  1.000 113.10000 ? 487 LEU B CD1    1 
ATOM   8515  C  CD2    . LEU B 1 496 ? 9.72500   -17.43500 -10.22800 1.000 112.72000 ? 487 LEU B CD2    1 
ATOM   8516  N  N      . ASP B 1 497 ? 12.78800  -15.36400 -6.82000  1.000 132.24000 ? 488 ASP B N      1 
ATOM   8517  C  CA     . ASP B 1 497 ? 13.08900  -15.89400 -5.49600  1.000 124.07000 ? 488 ASP B CA     1 
ATOM   8518  C  C      . ASP B 1 497 ? 13.03000  -14.79200 -4.44600  1.000 139.06000 ? 488 ASP B C      1 
ATOM   8519  O  O      . ASP B 1 497 ? 12.55900  -15.01400 -3.32500  1.000 148.46000 ? 488 ASP B O      1 
ATOM   8520  C  CB     . ASP B 1 497 ? 14.46500  -16.56500 -5.50900  1.000 123.76000 ? 488 ASP B CB     1 
ATOM   8521  C  CG     . ASP B 1 497 ? 14.82300  -17.20700 -4.17700  1.000 135.27000 ? 488 ASP B CG     1 
ATOM   8522  O  OD1    . ASP B 1 497 ? 14.00400  -17.15100 -3.23700  1.000 139.96000 ? 488 ASP B OD1    1 
ATOM   8523  O  OD2    . ASP B 1 497 ? 15.93400  -17.77000 -4.06900  1.000 141.92000 ? 488 ASP B OD2    1 
ATOM   8524  N  N      . ALA B 1 498 ? 13.52200  -13.59800 -4.78300  1.000 141.47000 ? 489 ALA B N      1 
ATOM   8525  C  CA     . ALA B 1 498 ? 13.46800  -12.49000 -3.83200  1.000 120.23000 ? 489 ALA B CA     1 
ATOM   8526  C  C      . ALA B 1 498 ? 12.02400  -12.08500 -3.54200  1.000 128.56000 ? 489 ALA B C      1 
ATOM   8527  O  O      . ALA B 1 498 ? 11.64500  -11.86200 -2.37900  1.000 141.57000 ? 489 ALA B O      1 
ATOM   8528  C  CB     . ALA B 1 498 ? 14.27000  -11.30100 -4.36300  1.000 101.23000 ? 489 ALA B CB     1 
ATOM   8529  N  N      . VAL B 1 499 ? 11.20200  -11.97500 -4.59100  1.000 124.15000 ? 490 VAL B N      1 
ATOM   8530  C  CA     . VAL B 1 499 ? 9.78700   -11.67700 -4.37300  1.000 124.57000 ? 490 VAL B CA     1 
ATOM   8531  C  C      . VAL B 1 499 ? 9.13600   -12.77400 -3.53300  1.000 136.20000 ? 490 VAL B C      1 
ATOM   8532  O  O      . VAL B 1 499 ? 8.31900   -12.49500 -2.64300  1.000 132.17000 ? 490 VAL B O      1 
ATOM   8533  C  CB     . VAL B 1 499 ? 9.05500   -11.45700 -5.71400  1.000 114.12000 ? 490 VAL B CB     1 
ATOM   8534  C  CG1    . VAL B 1 499 ? 9.72800   -10.34700 -6.51500  1.000 112.72000 ? 490 VAL B CG1    1 
ATOM   8535  C  CG2    . VAL B 1 499 ? 8.97000   -12.73500 -6.52400  1.000 126.60000 ? 490 VAL B CG2    1 
ATOM   8536  N  N      . GLY B 1 500 ? 9.49700   -14.03400 -3.78900  1.000 140.85000 ? 491 GLY B N      1 
ATOM   8537  C  CA     . GLY B 1 500 ? 8.97300   -15.12300 -2.98100  1.000 124.12000 ? 491 GLY B CA     1 
ATOM   8538  C  C      . GLY B 1 500 ? 9.37500   -15.01300 -1.52300  1.000 136.36000 ? 491 GLY B C      1 
ATOM   8539  O  O      . GLY B 1 500 ? 8.59300   -15.33900 -0.63000  1.000 151.91000 ? 491 GLY B O      1 
ATOM   8540  N  N      . ASN B 1 501 ? 10.60900  -14.57500 -1.26200  1.000 133.91000 ? 492 ASN B N      1 
ATOM   8541  C  CA     . ASN B 1 501 ? 11.06100  -14.40500 0.11700   1.000 129.63000 ? 492 ASN B CA     1 
ATOM   8542  C  C      . ASN B 1 501 ? 10.24700  -13.33700 0.82900   1.000 129.85000 ? 492 ASN B C      1 
ATOM   8543  O  O      . ASN B 1 501 ? 9.84400   -13.51300 1.98900   1.000 134.70000 ? 492 ASN B O      1 
ATOM   8544  C  CB     . ASN B 1 501 ? 12.54500  -14.04700 0.14500   1.000 129.32000 ? 492 ASN B CB     1 
ATOM   8545  C  CG     . ASN B 1 501 ? 13.43100  -15.25800 -0.01000  1.000 134.59000 ? 492 ASN B CG     1 
ATOM   8546  O  OD1    . ASN B 1 501 ? 12.94600  -16.37000 -0.22500  1.000 132.84000 ? 492 ASN B OD1    1 
ATOM   8547  N  ND2    . ASN B 1 501 ? 14.73700  -15.05400 0.09500   1.000 120.52000 ? 492 ASN B ND2    1 
ATOM   8548  N  N      . THR B 1 502 ? 10.00400  -12.21500 0.15300   1.000 126.20000 ? 493 THR B N      1 
ATOM   8549  C  CA     . THR B 1 502 ? 9.16400   -11.18100 0.75100   1.000 126.87000 ? 493 THR B CA     1 
ATOM   8550  C  C      . THR B 1 502 ? 7.76700   -11.72200 1.04600   1.000 125.35000 ? 493 THR B C      1 
ATOM   8551  O  O      . THR B 1 502 ? 7.21200   -11.50200 2.13500   1.000 111.55000 ? 493 THR B O      1 
ATOM   8552  C  CB     . THR B 1 502 ? 9.09100   -9.96700  -0.17200  1.000 119.47000 ? 493 THR B CB     1 
ATOM   8553  O  OG1    . THR B 1 502 ? 8.50300   -10.35400 -1.42000  1.000 128.50000 ? 493 THR B OG1    1 
ATOM   8554  C  CG2    . THR B 1 502 ? 10.48600  -9.41000  -0.42000  1.000 120.95000 ? 493 THR B CG2    1 
ATOM   8555  N  N      . THR B 1 503 ? 7.18400   -12.44300 0.08200   1.000 133.40000 ? 494 THR B N      1 
ATOM   8556  C  CA     . THR B 1 503 ? 5.84800   -12.99200 0.29300   1.000 130.22000 ? 494 THR B CA     1 
ATOM   8557  C  C      . THR B 1 503 ? 5.83900   -13.98700 1.44600   1.000 117.14000 ? 494 THR B C      1 
ATOM   8558  O  O      . THR B 1 503 ? 4.87400   -14.04600 2.21600   1.000 114.95000 ? 494 THR B O      1 
ATOM   8559  C  CB     . THR B 1 503 ? 5.32700   -13.65600 -0.98500  1.000 137.65000 ? 494 THR B CB     1 
ATOM   8560  O  OG1    . THR B 1 503 ? 6.16400   -14.76700 -1.33000  1.000 140.99000 ? 494 THR B OG1    1 
ATOM   8561  C  CG2    . THR B 1 503 ? 5.30600   -12.65900 -2.13600  1.000 142.73000 ? 494 THR B CG2    1 
ATOM   8562  N  N      . ALA B 1 504 ? 6.90900   -14.77100 1.59000   1.000 111.02000 ? 495 ALA B N      1 
ATOM   8563  C  CA     . ALA B 1 504 ? 6.98400   -15.73900 2.67700   1.000 105.14000 ? 495 ALA B CA     1 
ATOM   8564  C  C      . ALA B 1 504 ? 7.06300   -15.04300 4.02700   1.000 112.70000 ? 495 ALA B C      1 
ATOM   8565  O  O      . ALA B 1 504 ? 6.46100   -15.50200 5.00500   1.000 132.32000 ? 495 ALA B O      1 
ATOM   8566  C  CB     . ALA B 1 504 ? 8.18500   -16.66200 2.47800   1.000 118.39000 ? 495 ALA B CB     1 
ATOM   8567  N  N      . ALA B 1 505 ? 7.81000   -13.94100 4.10700   1.000 107.93000 ? 496 ALA B N      1 
ATOM   8568  C  CA     . ALA B 1 505 ? 7.84100   -13.17400 5.35000   1.000 118.80000 ? 496 ALA B CA     1 
ATOM   8569  C  C      . ALA B 1 505 ? 6.45400   -12.64200 5.69900   1.000 113.18000 ? 496 ALA B C      1 
ATOM   8570  O  O      . ALA B 1 505 ? 5.99800   -12.74200 6.85100   1.000 106.51000 ? 496 ALA B O      1 
ATOM   8571  C  CB     . ALA B 1 505 ? 8.84700   -12.02900 5.23400   1.000 132.43000 ? 496 ALA B CB     1 
ATOM   8572  N  N      . ILE B 1 506 ? 5.76400   -12.07400 4.70600   1.000 115.00000 ? 497 ILE B N      1 
ATOM   8573  C  CA     . ILE B 1 506 ? 4.41000   -11.57800 4.94500   1.000 114.31000 ? 497 ILE B CA     1 
ATOM   8574  C  C      . ILE B 1 506 ? 3.50700   -12.71200 5.41500   1.000 118.60000 ? 497 ILE B C      1 
ATOM   8575  O  O      . ILE B 1 506 ? 2.68000   -12.54000 6.32400   1.000 120.61000 ? 497 ILE B O      1 
ATOM   8576  C  CB     . ILE B 1 506 ? 3.85500   -10.89900 3.67800   1.000 117.04000 ? 497 ILE B CB     1 
ATOM   8577  C  CG1    . ILE B 1 506 ? 4.76000   -9.74100  3.25100   1.000 95.08000  ? 497 ILE B CG1    1 
ATOM   8578  C  CG2    . ILE B 1 506 ? 2.43100   -10.40900 3.91100   1.000 119.46000 ? 497 ILE B CG2    1 
ATOM   8579  C  CD1    . ILE B 1 506 ? 4.29300   -9.03700  1.99200   1.000 75.43000  ? 497 ILE B CD1    1 
ATOM   8580  N  N      . GLY B 1 507 ? 3.64900   -13.88800 4.80300   1.000 119.45000 ? 498 GLY B N      1 
ATOM   8581  C  CA     . GLY B 1 507 ? 2.82100   -15.01600 5.18600   1.000 114.87000 ? 498 GLY B CA     1 
ATOM   8582  C  C      . GLY B 1 507 ? 3.09400   -15.48700 6.60000   1.000 99.82000  ? 498 GLY B C      1 
ATOM   8583  O  O      . GLY B 1 507 ? 2.16800   -15.83300 7.33400   1.000 99.35000  ? 498 GLY B O      1 
ATOM   8584  N  N      . LYS B 1 508 ? 4.36500   -15.50700 7.00100   1.000 103.10000 ? 499 LYS B N      1 
ATOM   8585  C  CA     . LYS B 1 508 ? 4.69400   -15.88200 8.37200   1.000 101.68000 ? 499 LYS B CA     1 
ATOM   8586  C  C      . LYS B 1 508 ? 4.07000   -14.91200 9.36700   1.000 95.80000  ? 499 LYS B C      1 
ATOM   8587  O  O      . LYS B 1 508 ? 3.52800   -15.32700 10.40200  1.000 91.57000  ? 499 LYS B O      1 
ATOM   8588  C  CB     . LYS B 1 508 ? 6.21100   -15.94100 8.55200   1.000 98.25000  ? 499 LYS B CB     1 
ATOM   8589  N  N      . GLY B 1 509 ? 4.12600   -13.61300 9.06500   1.000 95.19000  ? 500 GLY B N      1 
ATOM   8590  C  CA     . GLY B 1 509 ? 3.49400   -12.64300 9.95000   1.000 86.99000  ? 500 GLY B CA     1 
ATOM   8591  C  C      . GLY B 1 509 ? 1.99100   -12.84100 10.05900  1.000 86.34000  ? 500 GLY B C      1 
ATOM   8592  O  O      . GLY B 1 509 ? 1.42400   -12.84800 11.16200  1.000 92.15000  ? 500 GLY B O      1 
ATOM   8593  N  N      . PHE B 1 510 ? 1.32300   -13.00300 8.91200   1.000 88.16000  ? 501 PHE B N      1 
ATOM   8594  C  CA     . PHE B 1 510 ? -0.12100  -13.22500 8.92300   1.000 86.82000  ? 501 PHE B CA     1 
ATOM   8595  C  C      . PHE B 1 510 ? -0.47100  -14.49800 9.68300   1.000 85.47000  ? 501 PHE B C      1 
ATOM   8596  O  O      . PHE B 1 510 ? -1.47300  -14.54600 10.40600  1.000 84.05000  ? 501 PHE B O      1 
ATOM   8597  C  CB     . PHE B 1 510 ? -0.66100  -13.27900 7.49300   1.000 94.66000  ? 501 PHE B CB     1 
ATOM   8598  C  CG     . PHE B 1 510 ? -2.16500  -13.26300 7.40500   1.000 85.73000  ? 501 PHE B CG     1 
ATOM   8599  C  CD1    . PHE B 1 510 ? -2.86000  -12.06200 7.37400   1.000 83.75000  ? 501 PHE B CD1    1 
ATOM   8600  C  CD2    . PHE B 1 510 ? -2.88300  -14.44600 7.34300   1.000 98.96000  ? 501 PHE B CD2    1 
ATOM   8601  C  CE1    . PHE B 1 510 ? -4.24300  -12.04500 7.28800   1.000 84.42000  ? 501 PHE B CE1    1 
ATOM   8602  C  CE2    . PHE B 1 510 ? -4.26500  -14.43300 7.25600   1.000 107.87000 ? 501 PHE B CE2    1 
ATOM   8603  C  CZ     . PHE B 1 510 ? -4.94400  -13.23100 7.22800   1.000 90.51000  ? 501 PHE B CZ     1 
ATOM   8604  N  N      . ALA B 1 511 ? 0.34100   -15.54600 9.51800   1.000 85.88000  ? 502 ALA B N      1 
ATOM   8605  C  CA     . ALA B 1 511 ? 0.09200   -16.79800 10.22100  1.000 76.51000  ? 502 ALA B CA     1 
ATOM   8606  C  C      . ALA B 1 511 ? 0.21900   -16.61300 11.72400  1.000 82.41000  ? 502 ALA B C      1 
ATOM   8607  O  O      . ALA B 1 511 ? -0.58800  -17.14800 12.48900  1.000 77.75000  ? 502 ALA B O      1 
ATOM   8608  C  CB     . ALA B 1 511 ? 1.05400   -17.87900 9.73200   1.000 78.48000  ? 502 ALA B CB     1 
ATOM   8609  N  N      . ILE B 1 512 ? 1.22800   -15.86300 12.17000  1.000 94.61000  ? 503 ILE B N      1 
ATOM   8610  C  CA     . ILE B 1 512 ? 1.37500   -15.62300 13.60400  1.000 85.45000  ? 503 ILE B CA     1 
ATOM   8611  C  C      . ILE B 1 512 ? 0.15800   -14.88200 14.14700  1.000 69.23000  ? 503 ILE B C      1 
ATOM   8612  O  O      . ILE B 1 512 ? -0.37500  -15.22200 15.21300  1.000 65.00000  ? 503 ILE B O      1 
ATOM   8613  C  CB     . ILE B 1 512 ? 2.67900   -14.85700 13.89200  1.000 94.72000  ? 503 ILE B CB     1 
ATOM   8614  C  CG1    . ILE B 1 512 ? 3.89400   -15.71700 13.53800  1.000 105.49000 ? 503 ILE B CG1    1 
ATOM   8615  C  CG2    . ILE B 1 512 ? 2.72900   -14.42200 15.35300  1.000 82.11000  ? 503 ILE B CG2    1 
ATOM   8616  C  CD1    . ILE B 1 512 ? 5.22500   -15.00900 13.71700  1.000 85.04000  ? 503 ILE B CD1    1 
ATOM   8617  N  N      . GLY B 1 513 ? -0.30100  -13.85700 13.42400  1.000 63.65000  ? 504 GLY B N      1 
ATOM   8618  C  CA     . GLY B 1 513 ? -1.46300  -13.11200 13.89200  1.000 55.76000  ? 504 GLY B CA     1 
ATOM   8619  C  C      . GLY B 1 513 ? -2.71100  -13.97300 13.96500  1.000 66.46000  ? 504 GLY B C      1 
ATOM   8620  O  O      . GLY B 1 513 ? -3.43700  -13.97100 14.97000  1.000 64.44000  ? 504 GLY B O      1 
ATOM   8621  N  N      . SER B 1 514 ? -2.97600  -14.73000 12.90000  1.000 75.53000  ? 505 SER B N      1 
ATOM   8622  C  CA     . SER B 1 514 ? -4.12500  -15.62500 12.90600  1.000 77.24000  ? 505 SER B CA     1 
ATOM   8623  C  C      . SER B 1 514 ? -4.00100  -16.67500 13.99800  1.000 71.22000  ? 505 SER B C      1 
ATOM   8624  O  O      . SER B 1 514 ? -5.00900  -17.07900 14.58300  1.000 67.95000  ? 505 SER B O      1 
ATOM   8625  C  CB     . SER B 1 514 ? -4.28200  -16.29000 11.54000  1.000 80.88000  ? 505 SER B CB     1 
ATOM   8626  O  OG     . SER B 1 514 ? -4.41800  -15.32200 10.51600  1.000 86.33000  ? 505 SER B OG     1 
ATOM   8627  N  N      . ALA B 1 515 ? -2.77800  -17.12300 14.29000  1.000 51.14000  ? 506 ALA B N      1 
ATOM   8628  C  CA     . ALA B 1 515 ? -2.58200  -18.10900 15.34400  1.000 50.56000  ? 506 ALA B CA     1 
ATOM   8629  C  C      . ALA B 1 515 ? -2.90100  -17.52100 16.70800  1.000 49.85000  ? 506 ALA B C      1 
ATOM   8630  O  O      . ALA B 1 515 ? -3.50900  -18.18800 17.54900  1.000 61.12000  ? 506 ALA B O      1 
ATOM   8631  C  CB     . ALA B 1 515 ? -1.14900  -18.63600 15.30900  1.000 71.90000  ? 506 ALA B CB     1 
ATOM   8632  N  N      . ILE B 1 516 ? -2.49400  -16.27500 16.94900  1.000 44.07000  ? 507 ILE B N      1 
ATOM   8633  C  CA     . ILE B 1 516 ? -2.87300  -15.62300 18.19900  1.000 44.74000  ? 507 ILE B CA     1 
ATOM   8634  C  C      . ILE B 1 516 ? -4.38900  -15.53100 18.30300  1.000 43.52000  ? 507 ILE B C      1 
ATOM   8635  O  O      . ILE B 1 516 ? -4.97600  -15.83600 19.35200  1.000 44.93000  ? 507 ILE B O      1 
ATOM   8636  C  CB     . ILE B 1 516 ? -2.21000  -14.23900 18.31200  1.000 45.48000  ? 507 ILE B CB     1 
ATOM   8637  C  CG1    . ILE B 1 516 ? -0.68800  -14.36600 18.21500  1.000 53.78000  ? 507 ILE B CG1    1 
ATOM   8638  C  CG2    . ILE B 1 516 ? -2.62700  -13.55400 19.61000  1.000 29.89000  ? 507 ILE B CG2    1 
ATOM   8639  C  CD1    . ILE B 1 516 ? 0.01000   -13.06300 17.89900  1.000 73.09000  ? 507 ILE B CD1    1 
ATOM   8640  N  N      . PHE B 1 517 ? -5.05000  -15.13400 17.21000  1.000 46.29000  ? 508 PHE B N      1 
ATOM   8641  C  CA     . PHE B 1 517 ? -6.50900  -15.03100 17.23300  1.000 57.03000  ? 508 PHE B CA     1 
ATOM   8642  C  C      . PHE B 1 517 ? -7.15700  -16.38400 17.51000  1.000 58.59000  ? 508 PHE B C      1 
ATOM   8643  O  O      . PHE B 1 517 ? -8.09200  -16.48600 18.31800  1.000 46.53000  ? 508 PHE B O      1 
ATOM   8644  C  CB     . PHE B 1 517 ? -7.02100  -14.46300 15.90800  1.000 58.50000  ? 508 PHE B CB     1 
ATOM   8645  C  CG     . PHE B 1 517 ? -7.50400  -13.04100 15.99500  1.000 58.26000  ? 508 PHE B CG     1 
ATOM   8646  C  CD1    . PHE B 1 517 ? -8.66500  -12.73500 16.68700  1.000 51.17000  ? 508 PHE B CD1    1 
ATOM   8647  C  CD2    . PHE B 1 517 ? -6.81800  -12.01700 15.36400  1.000 65.37000  ? 508 PHE B CD2    1 
ATOM   8648  C  CE1    . PHE B 1 517 ? -9.12300  -11.43300 16.76400  1.000 57.36000  ? 508 PHE B CE1    1 
ATOM   8649  C  CE2    . PHE B 1 517 ? -7.27400  -10.70900 15.43700  1.000 56.76000  ? 508 PHE B CE2    1 
ATOM   8650  C  CZ     . PHE B 1 517 ? -8.42800  -10.41800 16.13900  1.000 61.82000  ? 508 PHE B CZ     1 
ATOM   8651  N  N      . ALA B 1 518 ? -6.67000  -17.43500 16.85200  1.000 57.09000  ? 509 ALA B N      1 
ATOM   8652  C  CA     . ALA B 1 518 ? -7.24400  -18.76000 17.03500  1.000 55.35000  ? 509 ALA B CA     1 
ATOM   8653  C  C      . ALA B 1 518 ? -7.00600  -19.27900 18.44300  1.000 39.82000  ? 509 ALA B C      1 
ATOM   8654  O  O      . ALA B 1 518 ? -7.90300  -19.87300 19.04500  1.000 35.71000  ? 509 ALA B O      1 
ATOM   8655  C  CB     . ALA B 1 518 ? -6.66300  -19.73000 16.00700  1.000 61.85000  ? 509 ALA B CB     1 
ATOM   8656  N  N      . ALA B 1 519 ? -5.81200  -19.05400 18.99100  1.000 37.60000  ? 510 ALA B N      1 
ATOM   8657  C  CA     . ALA B 1 519 ? -5.52800  -19.51300 20.34400  1.000 42.92000  ? 510 ALA B CA     1 
ATOM   8658  C  C      . ALA B 1 519 ? -6.39300  -18.78500 21.36000  1.000 40.32000  ? 510 ALA B C      1 
ATOM   8659  O  O      . ALA B 1 519 ? -6.85800  -19.38800 22.33300  1.000 42.64000  ? 510 ALA B O      1 
ATOM   8660  C  CB     . ALA B 1 519 ? -4.04600  -19.32500 20.66400  1.000 38.70000  ? 510 ALA B CB     1 
ATOM   8661  N  N      . LEU B 1 520 ? -6.63600  -17.49000 21.14600  1.000 34.69000  ? 511 LEU B N      1 
ATOM   8662  C  CA     . LEU B 1 520 ? -7.53000  -16.76800 22.04300  1.000 42.64000  ? 511 LEU B CA     1 
ATOM   8663  C  C      . LEU B 1 520 ? -8.95800  -17.29600 21.94100  1.000 46.61000  ? 511 LEU B C      1 
ATOM   8664  O  O      . LEU B 1 520 ? -9.62400  -17.51300 22.96300  1.000 47.45000  ? 511 LEU B O      1 
ATOM   8665  C  CB     . LEU B 1 520 ? -7.47600  -15.27100 21.73600  1.000 42.77000  ? 511 LEU B CB     1 
ATOM   8666  C  CG     . LEU B 1 520 ? -6.13300  -14.60500 22.05800  1.000 38.35000  ? 511 LEU B CG     1 
ATOM   8667  C  CD1    . LEU B 1 520 ? -6.07100  -13.17400 21.53700  1.000 29.40000  ? 511 LEU B CD1    1 
ATOM   8668  C  CD2    . LEU B 1 520 ? -5.86100  -14.64900 23.55400  1.000 44.10000  ? 511 LEU B CD2    1 
ATOM   8669  N  N      . SER B 1 521 ? -9.44500  -17.52100 20.71900  1.000 41.43000  ? 512 SER B N      1 
ATOM   8670  C  CA     . SER B 1 521 ? -10.77700 -18.09900 20.56900  1.000 51.84000  ? 512 SER B CA     1 
ATOM   8671  C  C      . SER B 1 521 ? -10.85300 -19.47900 21.21100  1.000 54.36000  ? 512 SER B C      1 
ATOM   8672  O  O      . SER B 1 521 ? -11.87800 -19.84600 21.79600  1.000 61.71000  ? 512 SER B O      1 
ATOM   8673  C  CB     . SER B 1 521 ? -11.16900 -18.15500 19.09400  1.000 56.23000  ? 512 SER B CB     1 
ATOM   8674  O  OG     . SER B 1 521 ? -11.08900 -16.87100 18.49800  1.000 44.35000  ? 512 SER B OG     1 
ATOM   8675  N  N      . LEU B 1 522 ? -9.77700  -20.25900 21.11600  1.000 46.86000  ? 513 LEU B N      1 
ATOM   8676  C  CA     . LEU B 1 522 ? -9.77900  -21.58500 21.72000  1.000 50.98000  ? 513 LEU B CA     1 
ATOM   8677  C  C      . LEU B 1 522 ? -9.73800  -21.50500 23.23700  1.000 51.71000  ? 513 LEU B C      1 
ATOM   8678  O  O      . LEU B 1 522 ? -10.32800 -22.35000 23.91400  1.000 55.37000  ? 513 LEU B O      1 
ATOM   8679  C  CB     . LEU B 1 522 ? -8.60500  -22.41100 21.20000  1.000 38.16000  ? 513 LEU B CB     1 
ATOM   8680  C  CG     . LEU B 1 522 ? -8.69700  -22.74800 19.71300  1.000 38.57000  ? 513 LEU B CG     1 
ATOM   8681  C  CD1    . LEU B 1 522 ? -7.36500  -23.27700 19.20200  1.000 53.92000  ? 513 LEU B CD1    1 
ATOM   8682  C  CD2    . LEU B 1 522 ? -9.82400  -23.73500 19.45300  1.000 28.75000  ? 513 LEU B CD2    1 
ATOM   8683  N  N      . PHE B 1 523 ? -9.06300  -20.49900 23.78900  1.000 32.57000  ? 514 PHE B N      1 
ATOM   8684  C  CA     . PHE B 1 523 ? -9.13800  -20.28400 25.22800  1.000 32.08000  ? 514 PHE B CA     1 
ATOM   8685  C  C      . PHE B 1 523 ? -10.55900 -19.92200 25.64100  1.000 45.25000  ? 514 PHE B C      1 
ATOM   8686  O  O      . PHE B 1 523 ? -11.05700 -20.38600 26.67600  1.000 64.71000  ? 514 PHE B O      1 
ATOM   8687  C  CB     . PHE B 1 523 ? -8.15900  -19.19200 25.65000  1.000 30.14000  ? 514 PHE B CB     1 
ATOM   8688  C  CG     . PHE B 1 523 ? -8.47100  -18.59100 26.98800  1.000 30.90000  ? 514 PHE B CG     1 
ATOM   8689  C  CD1    . PHE B 1 523 ? -8.15100  -19.26300 28.15600  1.000 38.27000  ? 514 PHE B CD1    1 
ATOM   8690  C  CD2    . PHE B 1 523 ? -9.09600  -17.36000 27.08000  1.000 29.90000  ? 514 PHE B CD2    1 
ATOM   8691  C  CE1    . PHE B 1 523 ? -8.44400  -18.71400 29.38800  1.000 40.76000  ? 514 PHE B CE1    1 
ATOM   8692  C  CE2    . PHE B 1 523 ? -9.39200  -16.80700 28.30800  1.000 32.74000  ? 514 PHE B CE2    1 
ATOM   8693  C  CZ     . PHE B 1 523 ? -9.06500  -17.48500 29.46400  1.000 42.11000  ? 514 PHE B CZ     1 
ATOM   8694  N  N      . ALA B 1 524 ? -11.22600 -19.08900 24.84100  1.000 39.84000  ? 515 ALA B N      1 
ATOM   8695  C  CA     . ALA B 1 524 ? -12.62300 -18.76600 25.11600  1.000 35.69000  ? 515 ALA B CA     1 
ATOM   8696  C  C      . ALA B 1 524 ? -13.49700 -20.01400 25.07700  1.000 38.73000  ? 515 ALA B C      1 
ATOM   8697  O  O      . ALA B 1 524 ? -14.38800 -20.18600 25.91600  1.000 35.13000  ? 515 ALA B O      1 
ATOM   8698  C  CB     . ALA B 1 524 ? -13.12700 -17.72400 24.11800  1.000 41.50000  ? 515 ALA B CB     1 
ATOM   8699  N  N      . SER B 1 525 ? -13.26700 -20.88800 24.09500  1.000 43.36000  ? 516 SER B N      1 
ATOM   8700  C  CA     . SER B 1 525 ? -14.01000 -22.14400 24.03000  1.000 43.40000  ? 516 SER B CA     1 
ATOM   8701  C  C      . SER B 1 525 ? -13.69400 -23.03200 25.22600  1.000 46.29000  ? 516 SER B C      1 
ATOM   8702  O  O      . SER B 1 525 ? -14.57100 -23.73800 25.73800  1.000 45.52000  ? 516 SER B O      1 
ATOM   8703  C  CB     . SER B 1 525 ? -13.69500 -22.87500 22.72600  1.000 39.97000  ? 516 SER B CB     1 
ATOM   8704  O  OG     . SER B 1 525 ? -14.35400 -22.27400 21.62700  1.000 45.69000  ? 516 SER B OG     1 
ATOM   8705  N  N      . TYR B 1 526 ? -12.44000 -23.01400 25.67700  1.000 39.85000  ? 517 TYR B N      1 
ATOM   8706  C  CA     . TYR B 1 526 ? -12.06300 -23.76500 26.86700  1.000 40.06000  ? 517 TYR B CA     1 
ATOM   8707  C  C      . TYR B 1 526 ? -12.86200 -23.29800 28.07500  1.000 55.37000  ? 517 TYR B C      1 
ATOM   8708  O  O      . TYR B 1 526 ? -13.40500 -24.11200 28.83100  1.000 75.05000  ? 517 TYR B O      1 
ATOM   8709  C  CB     . TYR B 1 526 ? -10.56200 -23.62000 27.11400  1.000 25.79000  ? 517 TYR B CB     1 
ATOM   8710  C  CG     . TYR B 1 526 ? -10.12300 -24.08800 28.47800  1.000 41.61000  ? 517 TYR B CG     1 
ATOM   8711  C  CD1    . TYR B 1 526 ? -9.85600  -25.42800 28.71900  1.000 55.04000  ? 517 TYR B CD1    1 
ATOM   8712  C  CD2    . TYR B 1 526 ? -9.96600  -23.18900 29.52300  1.000 44.21000  ? 517 TYR B CD2    1 
ATOM   8713  C  CE1    . TYR B 1 526 ? -9.45400  -25.86200 29.96300  1.000 54.56000  ? 517 TYR B CE1    1 
ATOM   8714  C  CE2    . TYR B 1 526 ? -9.56500  -23.61200 30.76900  1.000 55.54000  ? 517 TYR B CE2    1 
ATOM   8715  C  CZ     . TYR B 1 526 ? -9.30900  -24.95000 30.98400  1.000 62.45000  ? 517 TYR B CZ     1 
ATOM   8716  O  OH     . TYR B 1 526 ? -8.90900  -25.37300 32.22800  1.000 83.73000  ? 517 TYR B OH     1 
ATOM   8717  N  N      . MET B 1 527 ? -12.93900 -21.98200 28.27500  1.000 45.08000  ? 518 MET B N      1 
ATOM   8718  C  CA     . MET B 1 527 ? -13.74300 -21.45900 29.37600  1.000 38.45000  ? 518 MET B CA     1 
ATOM   8719  C  C      . MET B 1 527 ? -15.21400 -21.81200 29.19200  1.000 54.04000  ? 518 MET B C      1 
ATOM   8720  O  O      . MET B 1 527 ? -15.91200 -22.12900 30.16300  1.000 59.29000  ? 518 MET B O      1 
ATOM   8721  C  CB     . MET B 1 527 ? -13.56600 -19.94600 29.49100  1.000 36.41000  ? 518 MET B CB     1 
ATOM   8722  C  CG     . MET B 1 527 ? -12.16700 -19.51000 29.89400  1.000 54.79000  ? 518 MET B CG     1 
ATOM   8723  S  SD     . MET B 1 527 ? -11.57900 -20.34700 31.38000  1.000 65.94000  ? 518 MET B SD     1 
ATOM   8724  C  CE     . MET B 1 527 ? -12.97600 -20.12600 32.47700  1.000 77.57000  ? 518 MET B CE     1 
ATOM   8725  N  N      . PHE B 1 528 ? -15.70100 -21.76000 27.95000  1.000 55.57000  ? 519 PHE B N      1 
ATOM   8726  C  CA     . PHE B 1 528 ? -17.08600 -22.12700 27.67700  1.000 53.69000  ? 519 PHE B CA     1 
ATOM   8727  C  C      . PHE B 1 528 ? -17.30300 -23.62800 27.80600  1.000 72.05000  ? 519 PHE B C      1 
ATOM   8728  O  O      . PHE B 1 528 ? -18.36700 -24.07000 28.25600  1.000 86.46000  ? 519 PHE B O      1 
ATOM   8729  C  CB     . PHE B 1 528 ? -17.48500 -21.65500 26.28000  1.000 53.92000  ? 519 PHE B CB     1 
ATOM   8730  C  CG     . PHE B 1 528 ? -18.17800 -20.33200 26.26500  1.000 39.23000  ? 519 PHE B CG     1 
ATOM   8731  C  CD1    . PHE B 1 528 ? -17.50900 -19.18300 26.64300  1.000 44.33000  ? 519 PHE B CD1    1 
ATOM   8732  C  CD2    . PHE B 1 528 ? -19.50200 -20.23400 25.87300  1.000 63.46000  ? 519 PHE B CD2    1 
ATOM   8733  C  CE1    . PHE B 1 528 ? -18.14700 -17.95900 26.63300  1.000 59.94000  ? 519 PHE B CE1    1 
ATOM   8734  C  CE2    . PHE B 1 528 ? -20.14600 -19.01300 25.86000  1.000 75.15000  ? 519 PHE B CE2    1 
ATOM   8735  C  CZ     . PHE B 1 528 ? -19.46700 -17.87300 26.24100  1.000 67.83000  ? 519 PHE B CZ     1 
ATOM   8736  N  N      . SER B 1 529 ? -16.30600 -24.42800 27.42000  1.000 52.10000  ? 520 SER B N      1 
ATOM   8737  C  CA     . SER B 1 529 ? -16.42100 -25.87400 27.55500  1.000 52.88000  ? 520 SER B CA     1 
ATOM   8738  C  C      . SER B 1 529 ? -16.42400 -26.31800 29.01100  1.000 68.55000  ? 520 SER B C      1 
ATOM   8739  O  O      . SER B 1 529 ? -16.88000 -27.42800 29.30600  1.000 90.20000  ? 520 SER B O      1 
ATOM   8740  C  CB     . SER B 1 529 ? -15.28300 -26.55900 26.79700  1.000 54.24000  ? 520 SER B CB     1 
ATOM   8741  O  OG     . SER B 1 529 ? -15.34000 -27.96700 26.94700  1.000 64.83000  ? 520 SER B OG     1 
ATOM   8742  N  N      . GLN B 1 530 ? -15.93000 -25.47800 29.92200  1.000 58.83000  ? 521 GLN B N      1 
ATOM   8743  C  CA     . GLN B 1 530 ? -15.88300 -25.80100 31.34400  1.000 73.19000  ? 521 GLN B CA     1 
ATOM   8744  C  C      . GLN B 1 530 ? -17.25600 -25.76100 32.01400  1.000 100.93000 ? 521 GLN B C      1 
ATOM   8745  O  O      . GLN B 1 530 ? -17.33700 -25.97600 33.22900  1.000 113.75000 ? 521 GLN B O      1 
ATOM   8746  C  CB     . GLN B 1 530 ? -14.90600 -24.85700 32.05300  1.000 65.95000  ? 521 GLN B CB     1 
ATOM   8747  C  CG     . GLN B 1 530 ? -14.62700 -25.21400 33.50800  1.000 88.83000  ? 521 GLN B CG     1 
ATOM   8748  C  CD     . GLN B 1 530 ? -13.48500 -24.40800 34.10200  1.000 109.40000 ? 521 GLN B CD     1 
ATOM   8749  O  OE1    . GLN B 1 530 ? -12.89900 -23.55300 33.43500  1.000 114.66000 ? 521 GLN B OE1    1 
ATOM   8750  N  NE2    . GLN B 1 530 ? -13.16200 -24.67900 35.36200  1.000 110.17000 ? 521 GLN B NE2    1 
ATOM   8751  N  N      . ILE B 1 531 ? -18.32700 -25.49300 31.26300  1.000 109.47000 ? 522 ILE B N      1 
ATOM   8752  C  CA     . ILE B 1 531 ? -19.66900 -25.51100 31.83500  1.000 115.57000 ? 522 ILE B CA     1 
ATOM   8753  C  C      . ILE B 1 531 ? -20.00600 -26.90900 32.33300  1.000 111.67000 ? 522 ILE B C      1 
ATOM   8754  O  O      . ILE B 1 531 ? -19.61400 -27.92000 31.73400  1.000 111.81000 ? 522 ILE B O      1 
ATOM   8755  C  CB     . ILE B 1 531 ? -20.69700 -25.02100 30.80100  1.000 88.03000  ? 522 ILE B CB     1 
ATOM   8756  C  CG1    . ILE B 1 531 ? -22.10000 -24.97800 31.41200  1.000 106.56000 ? 522 ILE B CG1    1 
ATOM   8757  C  CG2    . ILE B 1 531 ? -20.68800 -25.91300 29.57600  1.000 81.37000  ? 522 ILE B CG2    1 
ATOM   8758  C  CD1    . ILE B 1 531 ? -22.25400 -23.99000 32.54100  1.000 115.67000 ? 522 ILE B CD1    1 
ATOM   8759  N  N      . SER B 1 532 ? -20.74600 -26.97200 33.43600  1.000 100.47000 ? 523 SER B N      1 
ATOM   8760  C  CA     . SER B 1 532 ? -21.16000 -28.22700 34.03900  1.000 103.02000 ? 523 SER B CA     1 
ATOM   8761  C  C      . SER B 1 532 ? -22.66400 -28.23100 34.26300  1.000 128.79000 ? 523 SER B C      1 
ATOM   8762  O  O      . SER B 1 532 ? -23.28500 -27.16900 34.37300  1.000 145.71000 ? 523 SER B O      1 
ATOM   8763  C  CB     . SER B 1 532 ? -20.44300 -28.45900 35.37700  1.000 117.38000 ? 523 SER B CB     1 
ATOM   8764  O  OG     . SER B 1 532 ? -20.48100 -27.29800 36.19100  1.000 122.44000 ? 523 SER B OG     1 
ATOM   8765  N  N      . PRO B 1 533 ? -23.27700 -29.41700 34.32500  1.000 129.95000 ? 524 PRO B N      1 
ATOM   8766  C  CA     . PRO B 1 533 ? -24.73300 -29.48200 34.54400  1.000 130.35000 ? 524 PRO B CA     1 
ATOM   8767  C  C      . PRO B 1 533 ? -25.18400 -28.86500 35.85800  1.000 132.09000 ? 524 PRO B C      1 
ATOM   8768  O  O      . PRO B 1 533 ? -26.32000 -28.38000 35.94600  1.000 141.21000 ? 524 PRO B O      1 
ATOM   8769  C  CB     . PRO B 1 533 ? -25.03200 -30.98700 34.48400  1.000 150.34000 ? 524 PRO B CB     1 
ATOM   8770  C  CG     . PRO B 1 533 ? -23.87300 -31.58200 33.74400  1.000 150.31000 ? 524 PRO B CG     1 
ATOM   8771  C  CD     . PRO B 1 533 ? -22.68800 -30.75200 34.12800  1.000 147.48000 ? 524 PRO B CD     1 
ATOM   8772  N  N      . SER B 1 534 ? -24.33300 -28.88300 36.88800  1.000 121.34000 ? 525 SER B N      1 
ATOM   8773  C  CA     . SER B 1 534 ? -24.68600 -28.26800 38.16600  1.000 123.07000 ? 525 SER B CA     1 
ATOM   8774  C  C      . SER B 1 534 ? -24.71600 -26.74400 38.08600  1.000 130.21000 ? 525 SER B C      1 
ATOM   8775  O  O      . SER B 1 534 ? -25.49100 -26.10500 38.80500  1.000 129.29000 ? 525 SER B O      1 
ATOM   8776  C  CB     . SER B 1 534 ? -23.70800 -28.72400 39.24900  1.000 111.95000 ? 525 SER B CB     1 
ATOM   8777  O  OG     . SER B 1 534 ? -22.39700 -28.25200 38.98200  1.000 125.03000 ? 525 SER B OG     1 
ATOM   8778  N  N      . ASP B 1 535 ? -23.87400 -26.14700 37.24000  1.000 134.02000 ? 526 ASP B N      1 
ATOM   8779  C  CA     . ASP B 1 535 ? -23.82300 -24.70300 37.02400  1.000 125.57000 ? 526 ASP B CA     1 
ATOM   8780  C  C      . ASP B 1 535 ? -25.00700 -24.16700 36.22300  1.000 126.61000 ? 526 ASP B C      1 
ATOM   8781  O  O      . ASP B 1 535 ? -25.02600 -22.96800 35.92200  1.000 131.44000 ? 526 ASP B O      1 
ATOM   8782  C  CB     . ASP B 1 535 ? -22.51100 -24.33100 36.32900  1.000 98.95000  ? 526 ASP B CB     1 
ATOM   8783  N  N      . ILE B 1 536 ? -25.97800 -25.01000 35.86200  1.000 125.68000 ? 527 ILE B N      1 
ATOM   8784  C  CA     . ILE B 1 536 ? -27.09700 -24.54700 35.04400  1.000 132.92000 ? 527 ILE B CA     1 
ATOM   8785  C  C      . ILE B 1 536 ? -27.90100 -23.48300 35.77900  1.000 137.75000 ? 527 ILE B C      1 
ATOM   8786  O  O      . ILE B 1 536 ? -28.33400 -22.48900 35.18200  1.000 132.11000 ? 527 ILE B O      1 
ATOM   8787  C  CB     . ILE B 1 536 ? -27.98200 -25.73600 34.62400  1.000 136.90000 ? 527 ILE B CB     1 
ATOM   8788  C  CG1    . ILE B 1 536 ? -27.18900 -26.71800 33.75900  1.000 131.15000 ? 527 ILE B CG1    1 
ATOM   8789  C  CG2    . ILE B 1 536 ? -29.22100 -25.24900 33.88200  1.000 141.60000 ? 527 ILE B CG2    1 
ATOM   8790  C  CD1    . ILE B 1 536 ? -26.61700 -26.08900 32.50500  1.000 110.07000 ? 527 ILE B CD1    1 
ATOM   8791  N  N      . GLY B 1 537 ? -28.11500 -23.67100 37.08400  1.000 137.00000 ? 528 GLY B N      1 
ATOM   8792  C  CA     . GLY B 1 537 ? -28.82700 -22.67800 37.87000  1.000 130.14000 ? 528 GLY B CA     1 
ATOM   8793  C  C      . GLY B 1 537 ? -28.05500 -21.39300 38.09600  1.000 129.08000 ? 528 GLY B C      1 
ATOM   8794  O  O      . GLY B 1 537 ? -28.67000 -20.35300 38.35700  1.000 122.48000 ? 528 GLY B O      1 
ATOM   8795  N  N      . LYS B 1 538 ? -26.72700 -21.44200 37.99800  1.000 130.13000 ? 529 LYS B N      1 
ATOM   8796  C  CA     . LYS B 1 538 ? -25.90600 -20.27200 38.26300  1.000 112.63000 ? 529 LYS B CA     1 
ATOM   8797  C  C      . LYS B 1 538 ? -25.99200 -19.26300 37.11500  1.000 106.63000 ? 529 LYS B C      1 
ATOM   8798  O  O      . LYS B 1 538 ? -26.22200 -19.63400 35.96000  1.000 105.40000 ? 529 LYS B O      1 
ATOM   8799  C  CB     . LYS B 1 538 ? -24.45100 -20.68600 38.47700  1.000 102.97000 ? 529 LYS B CB     1 
ATOM   8800  N  N      . PRO B 1 539 ? -25.79000 -17.98200 37.40700  1.000 99.49000  ? 530 PRO B N      1 
ATOM   8801  C  CA     . PRO B 1 539 ? -25.84100 -16.95400 36.36300  1.000 101.14000 ? 530 PRO B CA     1 
ATOM   8802  C  C      . PRO B 1 539 ? -24.66600 -17.09100 35.41300  1.000 104.87000 ? 530 PRO B C      1 
ATOM   8803  O  O      . PRO B 1 539 ? -23.69600 -17.80400 35.71200  1.000 105.35000 ? 530 PRO B O      1 
ATOM   8804  C  CB     . PRO B 1 539 ? -25.76800 -15.63900 37.15400  1.000 95.16000  ? 530 PRO B CB     1 
ATOM   8805  C  CG     . PRO B 1 539 ? -26.20100 -15.99600 38.53900  1.000 102.35000 ? 530 PRO B CG     1 
ATOM   8806  C  CD     . PRO B 1 539 ? -25.70600 -17.39500 38.75400  1.000 102.30000 ? 530 PRO B CD     1 
ATOM   8807  N  N      . PRO B 1 540 ? -24.72300 -16.43600 34.25100  1.000 110.38000 ? 531 PRO B N      1 
ATOM   8808  C  CA     . PRO B 1 540 ? -23.58700 -16.51100 33.31700  1.000 108.59000 ? 531 PRO B CA     1 
ATOM   8809  C  C      . PRO B 1 540 ? -22.28800 -15.99900 33.91600  1.000 105.39000 ? 531 PRO B C      1 
ATOM   8810  O  O      . PRO B 1 540 ? -21.21300 -16.49500 33.55400  1.000 104.77000 ? 531 PRO B O      1 
ATOM   8811  C  CB     . PRO B 1 540 ? -24.04800 -15.65100 32.13000  1.000 78.39000  ? 531 PRO B CB     1 
ATOM   8812  C  CG     . PRO B 1 540 ? -25.53400 -15.57200 32.25800  1.000 103.83000 ? 531 PRO B CG     1 
ATOM   8813  C  CD     . PRO B 1 540 ? -25.82300 -15.61300 33.72500  1.000 121.36000 ? 531 PRO B CD     1 
ATOM   8814  N  N      . SER B 1 541 ? -22.35300 -15.03400 34.83800  1.000 105.86000 ? 532 SER B N      1 
ATOM   8815  C  CA     . SER B 1 541 ? -21.13600 -14.45600 35.40200  1.000 103.52000 ? 532 SER B CA     1 
ATOM   8816  C  C      . SER B 1 541 ? -20.31500 -15.48100 36.17400  1.000 96.26000  ? 532 SER B C      1 
ATOM   8817  O  O      . SER B 1 541 ? -19.08400 -15.37700 36.21600  1.000 93.10000  ? 532 SER B O      1 
ATOM   8818  C  CB     . SER B 1 541 ? -21.49000 -13.28300 36.31400  1.000 118.60000 ? 532 SER B CB     1 
ATOM   8819  O  OG     . SER B 1 541 ? -22.28900 -13.72300 37.39800  1.000 122.80000 ? 532 SER B OG     1 
ATOM   8820  N  N      . LEU B 1 542 ? -20.96900 -16.46400 36.80400  1.000 107.28000 ? 533 LEU B N      1 
ATOM   8821  C  CA     . LEU B 1 542 ? -20.24800 -17.44600 37.61100  1.000 108.71000 ? 533 LEU B CA     1 
ATOM   8822  C  C      . LEU B 1 542 ? -19.57100 -18.51600 36.76200  1.000 101.13000 ? 533 LEU B C      1 
ATOM   8823  O  O      . LEU B 1 542 ? -18.46500 -18.96000 37.09000  1.000 105.44000 ? 533 LEU B O      1 
ATOM   8824  C  CB     . LEU B 1 542 ? -21.19600 -18.11300 38.60900  1.000 127.21000 ? 533 LEU B CB     1 
ATOM   8825  C  CG     . LEU B 1 542 ? -21.53200 -17.32900 39.87700  1.000 128.36000 ? 533 LEU B CG     1 
ATOM   8826  C  CD1    . LEU B 1 542 ? -22.43500 -16.14600 39.56000  1.000 126.74000 ? 533 LEU B CD1    1 
ATOM   8827  C  CD2    . LEU B 1 542 ? -22.15400 -18.23000 40.94100  1.000 112.30000 ? 533 LEU B CD2    1 
ATOM   8828  N  N      . VAL B 1 543 ? -20.22300 -18.96300 35.68800  1.000 97.78000  ? 534 VAL B N      1 
ATOM   8829  C  CA     . VAL B 1 543 ? -19.68200 -20.06500 34.89800  1.000 105.29000 ? 534 VAL B CA     1 
ATOM   8830  C  C      . VAL B 1 543 ? -18.52600 -19.60200 34.02100  1.000 109.39000 ? 534 VAL B C      1 
ATOM   8831  O  O      . VAL B 1 543 ? -17.46600 -20.23700 33.98000  1.000 113.30000 ? 534 VAL B O      1 
ATOM   8832  C  CB     . VAL B 1 543 ? -20.79000 -20.71900 34.05800  1.000 112.00000 ? 534 VAL B CB     1 
ATOM   8833  C  CG1    . VAL B 1 543 ? -20.19500 -21.81400 33.19900  1.000 115.60000 ? 534 VAL B CG1    1 
ATOM   8834  C  CG2    . VAL B 1 543 ? -21.87300 -21.27200 34.96600  1.000 133.34000 ? 534 VAL B CG2    1 
ATOM   8835  N  N      . LEU B 1 544 ? -18.71000 -18.49400 33.30200  1.000 91.10000  ? 535 LEU B N      1 
ATOM   8836  C  CA     . LEU B 1 544 ? -17.67800 -17.99100 32.39500  1.000 71.51000  ? 535 LEU B CA     1 
ATOM   8837  C  C      . LEU B 1 544 ? -16.75400 -17.06800 33.18500  1.000 81.59000  ? 535 LEU B C      1 
ATOM   8838  O  O      . LEU B 1 544 ? -16.81600 -15.84000 33.09900  1.000 101.70000 ? 535 LEU B O      1 
ATOM   8839  C  CB     . LEU B 1 544 ? -18.30400 -17.28800 31.19400  1.000 81.11000  ? 535 LEU B CB     1 
ATOM   8840  C  CG     . LEU B 1 544 ? -19.53700 -17.91600 30.53100  1.000 79.19000  ? 535 LEU B CG     1 
ATOM   8841  C  CD1    . LEU B 1 544 ? -20.16200 -16.96600 29.51300  1.000 58.25000  ? 535 LEU B CD1    1 
ATOM   8842  C  CD2    . LEU B 1 544 ? -19.18500 -19.24500 29.87800  1.000 92.16000  ? 535 LEU B CD2    1 
ATOM   8843  N  N      . LEU B 1 545 ? -15.87200 -17.68700 33.96900  1.000 90.41000  ? 536 LEU B N      1 
ATOM   8844  C  CA     . LEU B 1 545 ? -14.99100 -16.94400 34.86000  1.000 69.81000  ? 536 LEU B CA     1 
ATOM   8845  C  C      . LEU B 1 545 ? -13.67200 -17.68400 35.02700  1.000 71.11000  ? 536 LEU B C      1 
ATOM   8846  O  O      . LEU B 1 545 ? -13.66100 -18.88000 35.33400  1.000 80.03000  ? 536 LEU B O      1 
ATOM   8847  C  CB     . LEU B 1 545 ? -15.65300 -16.73900 36.22500  1.000 66.77000  ? 536 LEU B CB     1 
ATOM   8848  C  CG     . LEU B 1 545 ? -14.88900 -15.88700 37.23700  1.000 64.98000  ? 536 LEU B CG     1 
ATOM   8849  C  CD1    . LEU B 1 545 ? -15.02300 -14.40900 36.89500  1.000 71.55000  ? 536 LEU B CD1    1 
ATOM   8850  C  CD2    . LEU B 1 545 ? -15.38000 -16.17400 38.64700  1.000 66.59000  ? 536 LEU B CD2    1 
ATOM   8851  N  N      . LEU B 1 546 ? -12.56300 -16.96000 34.83800  1.000 81.82000  ? 537 LEU B N      1 
ATOM   8852  C  CA     . LEU B 1 546 ? -11.20900 -17.43400 35.14400  1.000 68.86000  ? 537 LEU B CA     1 
ATOM   8853  C  C      . LEU B 1 546 ? -10.54400 -16.29900 35.91600  1.000 60.53000  ? 537 LEU B C      1 
ATOM   8854  O  O      . LEU B 1 546 ? -9.86400  -15.44900 35.33400  1.000 51.24000  ? 537 LEU B O      1 
ATOM   8855  C  CB     . LEU B 1 546 ? -10.42500 -17.81800 33.87800  1.000 48.19000  ? 537 LEU B CB     1 
ATOM   8856  C  CG     . LEU B 1 546 ? -9.01500  -18.37200 34.12800  1.000 58.21000  ? 537 LEU B CG     1 
ATOM   8857  C  CD1    . LEU B 1 546 ? -9.07900  -19.84600 34.49000  1.000 99.20000  ? 537 LEU B CD1    1 
ATOM   8858  C  CD2    . LEU B 1 546 ? -8.09900  -18.16200 32.92500  1.000 47.98000  ? 537 LEU B CD2    1 
ATOM   8859  N  N      . ASN B 1 547 ? -10.76900 -16.27700 37.22900  1.000 75.46000  ? 538 ASN B N      1 
ATOM   8860  C  CA     . ASN B 1 547 ? -10.26900 -15.19200 38.06200  1.000 79.94000  ? 538 ASN B CA     1 
ATOM   8861  C  C      . ASN B 1 547 ? -8.74600  -15.16900 38.06600  1.000 73.58000  ? 538 ASN B C      1 
ATOM   8862  O  O      . ASN B 1 547 ? -8.09500  -16.20300 38.24100  1.000 69.41000  ? 538 ASN B O      1 
ATOM   8863  C  CB     . ASN B 1 547 ? -10.79800 -15.33600 39.48800  1.000 76.00000  ? 538 ASN B CB     1 
ATOM   8864  C  CG     . ASN B 1 547 ? -10.62000 -14.06900 40.30500  1.000 65.16000  ? 538 ASN B CG     1 
ATOM   8865  O  OD1    . ASN B 1 547 ? -10.16100 -13.04300 39.79700  1.000 50.15000  ? 538 ASN B OD1    1 
ATOM   8866  N  ND2    . ASN B 1 547 ? -10.98400 -14.13400 41.58000  1.000 65.17000  ? 538 ASN B ND2    1 
ATOM   8867  N  N      . MET B 1 548 ? -8.18200  -13.97900 37.87400  1.000 58.55000  ? 539 MET B N      1 
ATOM   8868  C  CA     . MET B 1 548 ? -6.73900  -13.79800 37.86000  1.000 43.40000  ? 539 MET B CA     1 
ATOM   8869  C  C      . MET B 1 548 ? -6.16500  -13.53500 39.24500  1.000 47.98000  ? 539 MET B C      1 
ATOM   8870  O  O      . MET B 1 548 ? -4.94000  -13.54900 39.40700  1.000 42.09000  ? 539 MET B O      1 
ATOM   8871  C  CB     . MET B 1 548 ? -6.37100  -12.64400 36.91900  1.000 54.85000  ? 539 MET B CB     1 
ATOM   8872  C  CG     . MET B 1 548 ? -4.97600  -12.73400 36.33000  1.000 67.82000  ? 539 MET B CG     1 
ATOM   8873  S  SD     . MET B 1 548 ? -4.79100  -14.18800 35.28600  1.000 69.81000  ? 539 MET B SD     1 
ATOM   8874  C  CE     . MET B 1 548 ? -3.05400  -14.55000 35.53600  1.000 55.66000  ? 539 MET B CE     1 
ATOM   8875  N  N      . LEU B 1 549 ? -7.01300  -13.30800 40.24500  1.000 50.77000  ? 540 LEU B N      1 
ATOM   8876  C  CA     . LEU B 1 549 ? -6.54800  -13.11800 41.60900  1.000 40.22000  ? 540 LEU B CA     1 
ATOM   8877  C  C      . LEU B 1 549 ? -6.37700  -14.43300 42.35500  1.000 54.66000  ? 540 LEU B C      1 
ATOM   8878  O  O      . LEU B 1 549 ? -5.82000  -14.43400 43.45800  1.000 59.52000  ? 540 LEU B O      1 
ATOM   8879  C  CB     . LEU B 1 549 ? -7.51900  -12.21000 42.37300  1.000 33.27000  ? 540 LEU B CB     1 
ATOM   8880  C  CG     . LEU B 1 549 ? -7.00000  -11.51900 43.63400  1.000 41.34000  ? 540 LEU B CG     1 
ATOM   8881  C  CD1    . LEU B 1 549 ? -5.74000  -10.71700 43.34300  1.000 58.06000  ? 540 LEU B CD1    1 
ATOM   8882  C  CD2    . LEU B 1 549 ? -8.08000  -10.62500 44.21800  1.000 66.54000  ? 540 LEU B CD2    1 
ATOM   8883  N  N      . ASP B 1 550 ? -6.84100  -15.54200 41.78300  1.000 64.07000  ? 541 ASP B N      1 
ATOM   8884  C  CA     . ASP B 1 550 ? -6.62300  -16.85200 42.38000  1.000 66.41000  ? 541 ASP B CA     1 
ATOM   8885  C  C      . ASP B 1 550 ? -5.17600  -17.28100 42.17400  1.000 60.40000  ? 541 ASP B C      1 
ATOM   8886  O  O      . ASP B 1 550 ? -4.67300  -17.28300 41.04700  1.000 62.52000  ? 541 ASP B O      1 
ATOM   8887  C  CB     . ASP B 1 550 ? -7.57800  -17.87700 41.77300  1.000 79.27000  ? 541 ASP B CB     1 
ATOM   8888  C  CG     . ASP B 1 550 ? -7.53900  -19.21100 42.49500  1.000 95.75000  ? 541 ASP B CG     1 
ATOM   8889  O  OD1    . ASP B 1 550 ? -6.89700  -19.29400 43.56300  1.000 91.52000  ? 541 ASP B OD1    1 
ATOM   8890  O  OD2    . ASP B 1 550 ? -8.15500  -20.17800 41.99800  1.000 109.61000 ? 541 ASP B OD2    1 
ATOM   8891  N  N      . ALA B 1 551 ? -4.50800  -17.65500 43.26800  1.000 63.96000  ? 542 ALA B N      1 
ATOM   8892  C  CA     . ALA B 1 551 ? -3.08800  -17.98100 43.19000  1.000 64.31000  ? 542 ALA B CA     1 
ATOM   8893  C  C      . ALA B 1 551 ? -2.82900  -19.12200 42.21400  1.000 65.41000  ? 542 ALA B C      1 
ATOM   8894  O  O      . ALA B 1 551 ? -1.80500  -19.13400 41.51900  1.000 70.14000  ? 542 ALA B O      1 
ATOM   8895  C  CB     . ALA B 1 551 ? -2.55500  -18.33500 44.57900  1.000 51.92000  ? 542 ALA B CB     1 
ATOM   8896  N  N      . ARG B 1 552 ? -3.74400  -20.09100 42.14600  1.000 54.28000  ? 543 ARG B N      1 
ATOM   8897  C  CA     . ARG B 1 552 ? -3.57700  -21.18800 41.19900  1.000 45.44000  ? 543 ARG B CA     1 
ATOM   8898  C  C      . ARG B 1 552 ? -3.44400  -20.66600 39.77600  1.000 65.84000  ? 543 ARG B C      1 
ATOM   8899  O  O      . ARG B 1 552 ? -2.58000  -21.12200 39.01800  1.000 81.00000  ? 543 ARG B O      1 
ATOM   8900  C  CB     . ARG B 1 552 ? -4.75100  -22.15800 41.30400  1.000 61.54000  ? 543 ARG B CB     1 
ATOM   8901  C  CG     . ARG B 1 552 ? -4.77500  -22.96500 42.58700  1.000 67.72000  ? 543 ARG B CG     1 
ATOM   8902  C  CD     . ARG B 1 552 ? -5.91600  -23.96800 42.57600  1.000 71.76000  ? 543 ARG B CD     1 
ATOM   8903  N  NE     . ARG B 1 552 ? -5.91100  -24.80200 43.77100  1.000 71.63000  ? 543 ARG B NE     1 
ATOM   8904  C  CZ     . ARG B 1 552 ? -5.40400  -26.02500 43.82600  1.000 80.55000  ? 543 ARG B CZ     1 
ATOM   8905  N  NH1    . ARG B 1 552 ? -4.85100  -26.59300 42.76600  1.000 73.40000  ? 543 ARG B NH1    1 
ATOM   8906  N  NH2    . ARG B 1 552 ? -5.44900  -26.69500 44.97400  1.000 115.15000 ? 543 ARG B NH2    1 
ATOM   8907  N  N      . VAL B 1 553 ? -4.27900  -19.69400 39.40100  1.000 64.75000  ? 544 VAL B N      1 
ATOM   8908  C  CA     . VAL B 1 553 ? -4.23900  -19.16300 38.04100  1.000 55.95000  ? 544 VAL B CA     1 
ATOM   8909  C  C      . VAL B 1 553 ? -2.90600  -18.47100 37.77600  1.000 63.86000  ? 544 VAL B C      1 
ATOM   8910  O  O      . VAL B 1 553 ? -2.32800  -18.60100 36.69000  1.000 61.48000  ? 544 VAL B O      1 
ATOM   8911  C  CB     . VAL B 1 553 ? -5.43000  -18.21800 37.80200  1.000 63.02000  ? 544 VAL B CB     1 
ATOM   8912  C  CG1    . VAL B 1 553 ? -5.47100  -17.77700 36.34700  1.000 71.78000  ? 544 VAL B CG1    1 
ATOM   8913  C  CG2    . VAL B 1 553 ? -6.73400  -18.89800 38.20300  1.000 79.50000  ? 544 VAL B CG2    1 
ATOM   8914  N  N      . ILE B 1 554 ? -2.40300  -17.71800 38.75600  1.000 70.50000  ? 545 ILE B N      1 
ATOM   8915  C  CA     . ILE B 1 554 ? -1.13800  -17.00700 38.57500  1.000 65.20000  ? 545 ILE B CA     1 
ATOM   8916  C  C      . ILE B 1 554 ? 0.00600   -18.00000 38.39900  1.000 61.44000  ? 545 ILE B C      1 
ATOM   8917  O  O      . ILE B 1 554 ? 0.87600   -17.83900 37.52800  1.000 60.84000  ? 545 ILE B O      1 
ATOM   8918  C  CB     . ILE B 1 554 ? -0.88600  -16.05600 39.75800  1.000 42.22000  ? 545 ILE B CB     1 
ATOM   8919  C  CG1    . ILE B 1 554 ? -1.95600  -14.96200 39.79500  1.000 41.20000  ? 545 ILE B CG1    1 
ATOM   8920  C  CG2    . ILE B 1 554 ? 0.50300   -15.44700 39.66400  1.000 60.69000  ? 545 ILE B CG2    1 
ATOM   8921  C  CD1    . ILE B 1 554 ? -1.78400  -13.96700 40.92600  1.000 34.97000  ? 545 ILE B CD1    1 
ATOM   8922  N  N      . ALA B 1 555 ? 0.03400   -19.03400 39.24100  1.000 57.80000  ? 546 ALA B N      1 
ATOM   8923  C  CA     . ALA B 1 555 ? 1.07100   -20.04800 39.10500  1.000 53.64000  ? 546 ALA B CA     1 
ATOM   8924  C  C      . ALA B 1 555 ? 0.97200   -20.74200 37.75500  1.000 55.72000  ? 546 ALA B C      1 
ATOM   8925  O  O      . ALA B 1 555 ? 1.99300   -21.02200 37.11500  1.000 63.95000  ? 546 ALA B O      1 
ATOM   8926  C  CB     . ALA B 1 555 ? 0.97000   -21.06200 40.24500  1.000 53.90000  ? 546 ALA B CB     1 
ATOM   8927  N  N      . GLY B 1 556 ? -0.25300  -21.00400 37.29300  1.000 56.50000  ? 547 GLY B N      1 
ATOM   8928  C  CA     . GLY B 1 556 ? -0.42200  -21.63200 35.99500  1.000 59.57000  ? 547 GLY B CA     1 
ATOM   8929  C  C      . GLY B 1 556 ? 0.07300   -20.76300 34.85700  1.000 59.87000  ? 547 GLY B C      1 
ATOM   8930  O  O      . GLY B 1 556 ? 0.67600   -21.25700 33.90300  1.000 69.99000  ? 547 GLY B O      1 
ATOM   8931  N  N      . ALA B 1 557 ? -0.17500  -19.45500 34.94200  1.000 64.61000  ? 548 ALA B N      1 
ATOM   8932  C  CA     . ALA B 1 557 ? 0.32000   -18.53700 33.92000  1.000 75.61000  ? 548 ALA B CA     1 
ATOM   8933  C  C      . ALA B 1 557 ? 1.84400   -18.51400 33.89600  1.000 70.29000  ? 548 ALA B C      1 
ATOM   8934  O  O      . ALA B 1 557 ? 2.46600   -18.55900 32.82400  1.000 68.45000  ? 548 ALA B O      1 
ATOM   8935  C  CB     . ALA B 1 557 ? -0.23800  -17.13400 34.15800  1.000 84.94000  ? 548 ALA B CB     1 
ATOM   8936  N  N      . LEU B 1 558 ? 2.46700   -18.42600 35.07400  1.000 61.40000  ? 549 LEU B N      1 
ATOM   8937  C  CA     . LEU B 1 558 ? 3.92600   -18.44300 35.12100  1.000 52.50000  ? 549 LEU B CA     1 
ATOM   8938  C  C      . LEU B 1 558 ? 4.47000   -19.73500 34.52600  1.000 40.28000  ? 549 LEU B C      1 
ATOM   8939  O  O      . LEU B 1 558 ? 5.42900   -19.71600 33.74200  1.000 49.03000  ? 549 LEU B O      1 
ATOM   8940  C  CB     . LEU B 1 558 ? 4.41500   -18.26000 36.55900  1.000 47.86000  ? 549 LEU B CB     1 
ATOM   8941  C  CG     . LEU B 1 558 ? 4.33400   -16.85100 37.15400  1.000 40.74000  ? 549 LEU B CG     1 
ATOM   8942  C  CD1    . LEU B 1 558 ? 4.62000   -16.86900 38.64600  1.000 39.34000  ? 549 LEU B CD1    1 
ATOM   8943  C  CD2    . LEU B 1 558 ? 5.30800   -15.93000 36.44300  1.000 36.72000  ? 549 LEU B CD2    1 
ATOM   8944  N  N      . LEU B 1 559 ? 3.85800   -20.86700 34.87800  1.000 38.19000  ? 550 LEU B N      1 
ATOM   8945  C  CA     . LEU B 1 559 ? 4.31900   -22.14800 34.35900  1.000 44.63000  ? 550 LEU B CA     1 
ATOM   8946  C  C      . LEU B 1 559 ? 4.16000   -22.21700 32.84600  1.000 45.71000  ? 550 LEU B C      1 
ATOM   8947  O  O      . LEU B 1 559 ? 5.04900   -22.71000 32.14500  1.000 59.18000  ? 550 LEU B O      1 
ATOM   8948  C  CB     . LEU B 1 559 ? 3.55800   -23.28500 35.04000  1.000 49.83000  ? 550 LEU B CB     1 
ATOM   8949  C  CG     . LEU B 1 559 ? 4.08400   -24.70000 34.81000  1.000 45.49000  ? 550 LEU B CG     1 
ATOM   8950  C  CD1    . LEU B 1 559 ? 5.38600   -24.90500 35.56900  1.000 47.21000  ? 550 LEU B CD1    1 
ATOM   8951  C  CD2    . LEU B 1 559 ? 3.04700   -25.72300 35.23900  1.000 66.71000  ? 550 LEU B CD2    1 
ATOM   8952  N  N      . GLY B 1 560 ? 3.03500   -21.72700 32.32100  1.000 49.53000  ? 551 GLY B N      1 
ATOM   8953  C  CA     . GLY B 1 560 ? 2.83100   -21.75800 30.88200  1.000 47.70000  ? 551 GLY B CA     1 
ATOM   8954  C  C      . GLY B 1 560 ? 3.82400   -20.89300 30.13200  1.000 52.45000  ? 551 GLY B C      1 
ATOM   8955  O  O      . GLY B 1 560 ? 4.35000   -21.29100 29.08800  1.000 53.69000  ? 551 GLY B O      1 
ATOM   8956  N  N      . ALA B 1 561 ? 4.10000   -19.69700 30.65400  1.000 52.19000  ? 552 ALA B N      1 
ATOM   8957  C  CA     . ALA B 1 561 ? 5.09000   -18.83800 30.01300  1.000 51.83000  ? 552 ALA B CA     1 
ATOM   8958  C  C      . ALA B 1 561 ? 6.47200   -19.48000 30.03800  1.000 50.65000  ? 552 ALA B C      1 
ATOM   8959  O  O      . ALA B 1 561 ? 7.19000   -19.48100 29.02600  1.000 49.39000  ? 552 ALA B O      1 
ATOM   8960  C  CB     . ALA B 1 561 ? 5.11800   -17.47200 30.69700  1.000 57.46000  ? 552 ALA B CB     1 
ATOM   8961  N  N      . ALA B 1 562 ? 6.86100   -20.03600 31.18600  1.000 57.53000  ? 553 ALA B N      1 
ATOM   8962  C  CA     . ALA B 1 562 ? 8.15300   -20.70500 31.26600  1.000 51.39000  ? 553 ALA B CA     1 
ATOM   8963  C  C      . ALA B 1 562 ? 8.22200   -21.87700 30.29700  1.000 53.70000  ? 553 ALA B C      1 
ATOM   8964  O  O      . ALA B 1 562 ? 9.26000   -22.10800 29.66900  1.000 66.74000  ? 553 ALA B O      1 
ATOM   8965  C  CB     . ALA B 1 562 ? 8.42400   -21.16600 32.69700  1.000 46.84000  ? 553 ALA B CB     1 
ATOM   8966  N  N      . ILE B 1 563 ? 7.12800   -22.63000 30.16100  1.000 50.50000  ? 554 ILE B N      1 
ATOM   8967  C  CA     . ILE B 1 563 ? 7.11700   -23.76900 29.24800  1.000 48.30000  ? 554 ILE B CA     1 
ATOM   8968  C  C      . ILE B 1 563 ? 7.25300   -23.30200 27.80500  1.000 46.70000  ? 554 ILE B C      1 
ATOM   8969  O  O      . ILE B 1 563 ? 7.92100   -23.95000 26.99300  1.000 43.50000  ? 554 ILE B O      1 
ATOM   8970  C  CB     . ILE B 1 563 ? 5.84400   -24.61000 29.45800  1.000 61.29000  ? 554 ILE B CB     1 
ATOM   8971  C  CG1    . ILE B 1 563 ? 5.93200   -25.38000 30.77900  1.000 55.34000  ? 554 ILE B CG1    1 
ATOM   8972  C  CG2    . ILE B 1 563 ? 5.62900   -25.55800 28.28900  1.000 46.89000  ? 554 ILE B CG2    1 
ATOM   8973  C  CD1    . ILE B 1 563 ? 4.59500   -25.86700 31.30400  1.000 48.91000  ? 554 ILE B CD1    1 
ATOM   8974  N  N      . THR B 1 564 ? 6.61300   -22.18300 27.45600  1.000 44.69000  ? 555 THR B N      1 
ATOM   8975  C  CA     . THR B 1 564 ? 6.76100   -21.64000 26.10700  1.000 39.85000  ? 555 THR B CA     1 
ATOM   8976  C  C      . THR B 1 564 ? 8.21000   -21.25100 25.83500  1.000 46.10000  ? 555 THR B C      1 
ATOM   8977  O  O      . THR B 1 564 ? 8.76200   -21.54500 24.76500  1.000 46.05000  ? 555 THR B O      1 
ATOM   8978  C  CB     . THR B 1 564 ? 5.83900   -20.43600 25.91500  1.000 48.20000  ? 555 THR B CB     1 
ATOM   8979  O  OG1    . THR B 1 564 ? 4.49500   -20.80400 26.25200  1.000 64.14000  ? 555 THR B OG1    1 
ATOM   8980  C  CG2    . THR B 1 564 ? 5.88700   -19.95400 24.46700  1.000 40.62000  ? 555 THR B CG2    1 
ATOM   8981  N  N      . TYR B 1 565 ? 8.83800   -20.57400 26.79600  1.000 39.43000  ? 556 TYR B N      1 
ATOM   8982  C  CA     . TYR B 1 565 ? 10.24400  -20.21900 26.63100  1.000 32.09000  ? 556 TYR B CA     1 
ATOM   8983  C  C      . TYR B 1 565 ? 11.10900  -21.46600 26.50600  1.000 43.33000  ? 556 TYR B C      1 
ATOM   8984  O  O      . TYR B 1 565 ? 12.03900  -21.50800 25.69300  1.000 46.99000  ? 556 TYR B O      1 
ATOM   8985  C  CB     . TYR B 1 565 ? 10.71400  -19.35100 27.79700  1.000 40.49000  ? 556 TYR B CB     1 
ATOM   8986  C  CG     . TYR B 1 565 ? 10.53400  -17.86700 27.56800  1.000 52.50000  ? 556 TYR B CG     1 
ATOM   8987  C  CD1    . TYR B 1 565 ? 9.26900   -17.29400 27.55100  1.000 62.82000  ? 556 TYR B CD1    1 
ATOM   8988  C  CD2    . TYR B 1 565 ? 11.62900  -17.04000 27.35800  1.000 53.90000  ? 556 TYR B CD2    1 
ATOM   8989  C  CE1    . TYR B 1 565 ? 9.10100   -15.94100 27.33700  1.000 44.06000  ? 556 TYR B CE1    1 
ATOM   8990  C  CE2    . TYR B 1 565 ? 11.47000  -15.68600 27.14400  1.000 42.29000  ? 556 TYR B CE2    1 
ATOM   8991  C  CZ     . TYR B 1 565 ? 10.20400  -15.14300 27.13400  1.000 42.36000  ? 556 TYR B CZ     1 
ATOM   8992  O  OH     . TYR B 1 565 ? 10.04600  -13.79300 26.92000  1.000 78.92000  ? 556 TYR B OH     1 
ATOM   8993  N  N      . TYR B 1 566 ? 10.81500  -22.49100 27.30900  1.000 51.90000  ? 557 TYR B N      1 
ATOM   8994  C  CA     . TYR B 1 566 ? 11.58500  -23.72900 27.26400  1.000 51.29000  ? 557 TYR B CA     1 
ATOM   8995  C  C      . TYR B 1 566 ? 11.44400  -24.41300 25.91100  1.000 46.71000  ? 557 TYR B C      1 
ATOM   8996  O  O      . TYR B 1 566 ? 12.42900  -24.89000 25.34100  1.000 60.51000  ? 557 TYR B O      1 
ATOM   8997  C  CB     . TYR B 1 566 ? 11.12200  -24.65300 28.39400  1.000 47.07000  ? 557 TYR B CB     1 
ATOM   8998  C  CG     . TYR B 1 566 ? 12.10100  -25.73900 28.79400  1.000 62.84000  ? 557 TYR B CG     1 
ATOM   8999  C  CD1    . TYR B 1 566 ? 13.11500  -25.48000 29.70700  1.000 74.70000  ? 557 TYR B CD1    1 
ATOM   9000  C  CD2    . TYR B 1 566 ? 11.98200  -27.03400 28.29800  1.000 73.32000  ? 557 TYR B CD2    1 
ATOM   9001  C  CE1    . TYR B 1 566 ? 14.00700  -26.46800 30.08900  1.000 86.48000  ? 557 TYR B CE1    1 
ATOM   9002  C  CE2    . TYR B 1 566 ? 12.86900  -28.03100 28.67800  1.000 90.16000  ? 557 TYR B CE2    1 
ATOM   9003  C  CZ     . TYR B 1 566 ? 13.87900  -27.74100 29.57500  1.000 82.55000  ? 557 TYR B CZ     1 
ATOM   9004  O  OH     . TYR B 1 566 ? 14.76800  -28.71800 29.96200  1.000 80.04000  ? 557 TYR B OH     1 
ATOM   9005  N  N      . PHE B 1 567 ? 10.22400  -24.45500 25.37700  1.000 37.55000  ? 558 PHE B N      1 
ATOM   9006  C  CA     . PHE B 1 567 ? 9.98900   -25.02900 24.05600  1.000 42.93000  ? 558 PHE B CA     1 
ATOM   9007  C  C      . PHE B 1 567 ? 10.78000  -24.28100 22.98800  1.000 61.33000  ? 558 PHE B C      1 
ATOM   9008  O  O      . PHE B 1 567 ? 11.49500  -24.88900 22.17400  1.000 63.96000  ? 558 PHE B O      1 
ATOM   9009  C  CB     . PHE B 1 567 ? 8.48300   -24.99800 23.77300  1.000 42.84000  ? 558 PHE B CB     1 
ATOM   9010  C  CG     . PHE B 1 567 ? 8.10500   -25.32400 22.35800  1.000 41.11000  ? 558 PHE B CG     1 
ATOM   9011  C  CD1    . PHE B 1 567 ? 7.92100   -26.63300 21.95400  1.000 52.44000  ? 558 PHE B CD1    1 
ATOM   9012  C  CD2    . PHE B 1 567 ? 7.88500   -24.30900 21.44500  1.000 61.43000  ? 558 PHE B CD2    1 
ATOM   9013  C  CE1    . PHE B 1 567 ? 7.55500   -26.92300 20.65200  1.000 73.31000  ? 558 PHE B CE1    1 
ATOM   9014  C  CE2    . PHE B 1 567 ? 7.52000   -24.59000 20.14900  1.000 61.31000  ? 558 PHE B CE2    1 
ATOM   9015  C  CZ     . PHE B 1 567 ? 7.35500   -25.89800 19.75000  1.000 66.60000  ? 558 PHE B CZ     1 
ATOM   9016  N  N      . SER B 1 568 ? 10.69000  -22.95000 23.00200  1.000 65.24000  ? 559 SER B N      1 
ATOM   9017  C  CA     . SER B 1 568 ? 11.40200  -22.16300 22.00400  1.000 51.91000  ? 559 SER B CA     1 
ATOM   9018  C  C      . SER B 1 568 ? 12.90700  -22.37800 22.10700  1.000 49.23000  ? 559 SER B C      1 
ATOM   9019  O  O      . SER B 1 568 ? 13.59200  -22.51900 21.08700  1.000 62.73000  ? 559 SER B O      1 
ATOM   9020  C  CB     . SER B 1 568 ? 11.04300  -20.68600 22.16000  1.000 43.52000  ? 559 SER B CB     1 
ATOM   9021  O  OG     . SER B 1 568 ? 11.33000  -20.22900 23.47000  1.000 64.25000  ? 559 SER B OG     1 
ATOM   9022  N  N      . GLY B 1 569 ? 13.44100  -22.41100 23.32900  1.000 36.12000  ? 560 GLY B N      1 
ATOM   9023  C  CA     . GLY B 1 569 ? 14.86700  -22.63800 23.49700  1.000 55.70000  ? 560 GLY B CA     1 
ATOM   9024  C  C      . GLY B 1 569 ? 15.29700  -24.02700 23.06400  1.000 51.52000  ? 560 GLY B C      1 
ATOM   9025  O  O      . GLY B 1 569 ? 16.37600  -24.20400 22.49100  1.000 58.68000  ? 560 GLY B O      1 
ATOM   9026  N  N      . TYR B 1 570 ? 14.46600  -25.03200 23.34100  1.000 46.12000  ? 561 TYR B N      1 
ATOM   9027  C  CA     . TYR B 1 570 ? 14.80300  -26.39900 22.96400  1.000 61.31000  ? 561 TYR B CA     1 
ATOM   9028  C  C      . TYR B 1 570 ? 14.84900  -26.55900 21.45000  1.000 60.75000  ? 561 TYR B C      1 
ATOM   9029  O  O      . TYR B 1 570 ? 15.66100  -27.33400 20.92600  1.000 65.14000  ? 561 TYR B O      1 
ATOM   9030  C  CB     . TYR B 1 570 ? 13.79500  -27.37500 23.56900  1.000 70.34000  ? 561 TYR B CB     1 
ATOM   9031  C  CG     . TYR B 1 570 ? 13.99400  -28.80800 23.12600  1.000 68.02000  ? 561 TYR B CG     1 
ATOM   9032  C  CD1    . TYR B 1 570 ? 13.39600  -29.28900 21.97100  1.000 65.72000  ? 561 TYR B CD1    1 
ATOM   9033  C  CD2    . TYR B 1 570 ? 14.74700  -29.69200 23.89000  1.000 89.18000  ? 561 TYR B CD2    1 
ATOM   9034  C  CE1    . TYR B 1 570 ? 13.57400  -30.59500 21.56700  1.000 83.33000  ? 561 TYR B CE1    1 
ATOM   9035  C  CE2    . TYR B 1 570 ? 14.92200  -31.00400 23.49700  1.000 105.24000 ? 561 TYR B CE2    1 
ATOM   9036  C  CZ     . TYR B 1 570 ? 14.33100  -31.45000 22.33300  1.000 90.85000  ? 561 TYR B CZ     1 
ATOM   9037  O  OH     . TYR B 1 570 ? 14.49700  -32.75500 21.93000  1.000 83.40000  ? 561 TYR B OH     1 
ATOM   9038  N  N      . LEU B 1 571 ? 13.96600  -25.86000 20.72900  1.000 58.20000  ? 562 LEU B N      1 
ATOM   9039  C  CA     . LEU B 1 571 ? 13.96800  -25.99300 19.27100  1.000 71.57000  ? 562 LEU B CA     1 
ATOM   9040  C  C      . LEU B 1 571 ? 15.31300  -25.59000 18.66600  1.000 79.15000  ? 562 LEU B C      1 
ATOM   9041  O  O      . LEU B 1 571 ? 15.77200  -26.20200 17.69100  1.000 91.17000  ? 562 LEU B O      1 
ATOM   9042  C  CB     . LEU B 1 571 ? 12.83100  -25.17800 18.64900  1.000 76.97000  ? 562 LEU B CB     1 
ATOM   9043  C  CG     . LEU B 1 571 ? 11.44600  -25.83100 18.57500  1.000 59.96000  ? 562 LEU B CG     1 
ATOM   9044  C  CD1    . LEU B 1 571 ? 11.49800  -27.02700 17.64700  1.000 77.87000  ? 562 LEU B CD1    1 
ATOM   9045  C  CD2    . LEU B 1 571 ? 10.93100  -26.24300 19.93100  1.000 46.65000  ? 562 LEU B CD2    1 
ATOM   9046  N  N      . ILE B 1 572 ? 15.95900  -24.56500 19.22400  1.000 57.97000  ? 563 ILE B N      1 
ATOM   9047  C  CA     . ILE B 1 572 ? 17.25900  -24.13100 18.71300  1.000 56.54000  ? 563 ILE B CA     1 
ATOM   9048  C  C      . ILE B 1 572 ? 18.27900  -25.25900 18.81800  1.000 64.18000  ? 563 ILE B C      1 
ATOM   9049  O  O      . ILE B 1 572 ? 18.96200  -25.60700 17.84100  1.000 66.15000  ? 563 ILE B O      1 
ATOM   9050  C  CB     . ILE B 1 572 ? 17.73000  -22.87800 19.47100  1.000 68.48000  ? 563 ILE B CB     1 
ATOM   9051  C  CG1    . ILE B 1 572 ? 16.68400  -21.76700 19.35600  1.000 47.15000  ? 563 ILE B CG1    1 
ATOM   9052  C  CG2    . ILE B 1 572 ? 19.08200  -22.41500 18.95000  1.000 81.12000  ? 563 ILE B CG2    1 
ATOM   9053  C  CD1    . ILE B 1 572 ? 17.03100  -20.51400 20.12700  1.000 48.78000  ? 563 ILE B CD1    1 
ATOM   9054  N  N      . SER B 1 573 ? 18.40900  -25.83700 20.01400  1.000 73.31000  ? 564 SER B N      1 
ATOM   9055  C  CA     . SER B 1 573 ? 19.37000  -26.91500 20.20700  1.000 82.80000  ? 564 SER B CA     1 
ATOM   9056  C  C      . SER B 1 573 ? 19.01700  -28.12400 19.35600  1.000 80.35000  ? 564 SER B C      1 
ATOM   9057  O  O      . SER B 1 573 ? 19.91200  -28.84200 18.90100  1.000 87.63000  ? 564 SER B O      1 
ATOM   9058  C  CB     . SER B 1 573 ? 19.45000  -27.30100 21.68500  1.000 70.12000  ? 564 SER B CB     1 
ATOM   9059  O  OG     . SER B 1 573 ? 18.24100  -27.88700 22.13300  1.000 77.04000  ? 564 SER B OG     1 
ATOM   9060  N  N      . ALA B 1 574 ? 17.72300  -28.37300 19.13500  1.000 76.39000  ? 565 ALA B N      1 
ATOM   9061  C  CA     . ALA B 1 574 ? 17.33300  -29.50400 18.30000  1.000 79.48000  ? 565 ALA B CA     1 
ATOM   9062  C  C      . ALA B 1 574 ? 17.75600  -29.29500 16.85000  1.000 84.54000  ? 565 ALA B C      1 
ATOM   9063  O  O      . ALA B 1 574 ? 18.26000  -30.22300 16.20300  1.000 93.77000  ? 565 ALA B O      1 
ATOM   9064  C  CB     . ALA B 1 574 ? 15.82400  -29.73100 18.38900  1.000 92.65000  ? 565 ALA B CB     1 
ATOM   9065  N  N      . VAL B 1 575 ? 17.55600  -28.08800 16.32000  1.000 84.50000  ? 566 VAL B N      1 
ATOM   9066  C  CA     . VAL B 1 575 ? 18.01400  -27.80600 14.96200  1.000 64.15000  ? 566 VAL B CA     1 
ATOM   9067  C  C      . VAL B 1 575 ? 19.52400  -27.97500 14.87200  1.000 69.20000  ? 566 VAL B C      1 
ATOM   9068  O  O      . VAL B 1 575 ? 20.03900  -28.58200 13.92300  1.000 80.95000  ? 566 VAL B O      1 
ATOM   9069  C  CB     . VAL B 1 575 ? 17.56800  -26.40300 14.51500  1.000 59.96000  ? 566 VAL B CB     1 
ATOM   9070  C  CG1    . VAL B 1 575 ? 18.30300  -25.99500 13.25100  1.000 56.38000  ? 566 VAL B CG1    1 
ATOM   9071  C  CG2    . VAL B 1 575 ? 16.06400  -26.37400 14.29000  1.000 67.00000  ? 566 VAL B CG2    1 
ATOM   9072  N  N      . THR B 1 576 ? 20.25800  -27.45500 15.86300  1.000 78.33000  ? 567 THR B N      1 
ATOM   9073  C  CA     . THR B 1 576 ? 21.71500  -27.57600 15.82200  1.000 78.87000  ? 567 THR B CA     1 
ATOM   9074  C  C      . THR B 1 576 ? 22.15200  -29.03700 15.87800  1.000 89.75000  ? 567 THR B C      1 
ATOM   9075  O  O      . THR B 1 576 ? 23.06000  -29.45000 15.14700  1.000 94.79000  ? 567 THR B O      1 
ATOM   9076  C  CB     . THR B 1 576 ? 22.36000  -26.77200 16.95400  1.000 74.28000  ? 567 THR B CB     1 
ATOM   9077  O  OG1    . THR B 1 576 ? 22.11900  -27.41800 18.21100  1.000 92.52000  ? 567 THR B OG1    1 
ATOM   9078  C  CG2    . THR B 1 576 ? 21.80900  -25.34400 16.98800  1.000 65.64000  ? 567 THR B CG2    1 
ATOM   9079  N  N      . LYS B 1 577 ? 21.53200  -29.83500 16.75000  1.000 88.71000  ? 568 LYS B N      1 
ATOM   9080  C  CA     . LYS B 1 577 ? 21.92100  -31.23600 16.87200  1.000 80.61000  ? 568 LYS B CA     1 
ATOM   9081  C  C      . LYS B 1 577 ? 21.60300  -32.01700 15.60200  1.000 88.50000  ? 568 LYS B C      1 
ATOM   9082  O  O      . LYS B 1 577 ? 22.40200  -32.85500 15.16800  1.000 99.10000  ? 568 LYS B O      1 
ATOM   9083  C  CB     . LYS B 1 577 ? 21.24200  -31.86900 18.08400  1.000 68.51000  ? 568 LYS B CB     1 
ATOM   9084  N  N      . ALA B 1 578 ? 20.43100  -31.78600 15.00400  1.000 81.73000  ? 569 ALA B N      1 
ATOM   9085  C  CA     . ALA B 1 578 ? 20.11800  -32.47800 13.75900  1.000 76.05000  ? 569 ALA B CA     1 
ATOM   9086  C  C      . ALA B 1 578 ? 21.08300  -32.06900 12.65200  1.000 86.83000  ? 569 ALA B C      1 
ATOM   9087  O  O      . ALA B 1 578 ? 21.51700  -32.90800 11.85000  1.000 102.15000 ? 569 ALA B O      1 
ATOM   9088  C  CB     . ALA B 1 578 ? 18.67200  -32.21100 13.34800  1.000 70.65000  ? 569 ALA B CB     1 
ATOM   9089  N  N      . ALA B 1 579 ? 21.43900  -30.78200 12.59100  1.000 95.74000  ? 570 ALA B N      1 
ATOM   9090  C  CA     . ALA B 1 579 ? 22.42200  -30.35200 11.60500  1.000 95.88000  ? 570 ALA B CA     1 
ATOM   9091  C  C      . ALA B 1 579 ? 23.76500  -31.03200 11.84100  1.000 107.08000 ? 570 ALA B C      1 
ATOM   9092  O  O      . ALA B 1 579 ? 24.44900  -31.41600 10.88600  1.000 115.19000 ? 570 ALA B O      1 
ATOM   9093  C  CB     . ALA B 1 579 ? 22.57100  -28.83200 11.62800  1.000 94.68000  ? 570 ALA B CB     1 
ATOM   9094  N  N      . MET B 1 580 ? 24.16900  -31.17900 13.10700  1.000 111.85000 ? 571 MET B N      1 
ATOM   9095  C  CA     . MET B 1 580 ? 25.41400  -31.88500 13.40400  1.000 107.10000 ? 571 MET B CA     1 
ATOM   9096  C  C      . MET B 1 580 ? 25.33900  -33.35000 12.99300  1.000 113.62000 ? 571 MET B C      1 
ATOM   9097  O  O      . MET B 1 580 ? 26.33700  -33.92500 12.54900  1.000 119.84000 ? 571 MET B O      1 
ATOM   9098  C  CB     . MET B 1 580 ? 25.77200  -31.75500 14.88300  1.000 90.69000  ? 571 MET B CB     1 
ATOM   9099  C  CG     . MET B 1 580 ? 26.61600  -30.53000 15.18300  1.000 92.89000  ? 571 MET B CG     1 
ATOM   9100  S  SD     . MET B 1 580 ? 28.03800  -30.43100 14.07000  1.000 127.73000 ? 571 MET B SD     1 
ATOM   9101  C  CE     . MET B 1 580 ? 28.95900  -31.89600 14.54400  1.000 105.26000 ? 571 MET B CE     1 
ATOM   9102  N  N      . LYS B 1 581 ? 24.17800  -33.98400 13.17200  1.000 108.56000 ? 572 LYS B N      1 
ATOM   9103  C  CA     . LYS B 1 581 ? 24.02200  -35.36100 12.70700  1.000 103.30000 ? 572 LYS B CA     1 
ATOM   9104  C  C      . LYS B 1 581 ? 24.18900  -35.44500 11.19300  1.000 113.27000 ? 572 LYS B C      1 
ATOM   9105  O  O      . LYS B 1 581 ? 24.83300  -36.36800 10.68100  1.000 125.26000 ? 572 LYS B O      1 
ATOM   9106  C  CB     . LYS B 1 581 ? 22.66600  -35.92600 13.13900  1.000 103.37000 ? 572 LYS B CB     1 
ATOM   9107  C  CG     . LYS B 1 581 ? 22.66800  -36.62900 14.49400  1.000 120.69000 ? 572 LYS B CG     1 
ATOM   9108  C  CD     . LYS B 1 581 ? 23.53500  -37.87800 14.43400  1.000 142.19000 ? 572 LYS B CD     1 
ATOM   9109  C  CE     . LYS B 1 581 ? 23.41800  -38.70800 15.70200  1.000 138.49000 ? 572 LYS B CE     1 
ATOM   9110  N  NZ     . LYS B 1 581 ? 24.25300  -39.94500 15.65600  1.000 106.14000 ? 572 LYS B NZ     1 
ATOM   9111  N  N      . MET B 1 582 ? 23.61000  -34.48900 10.46100  1.000 109.66000 ? 573 MET B N      1 
ATOM   9112  C  CA     . MET B 1 582 ? 23.81400  -34.45300 9.01400   1.000 95.24000  ? 573 MET B CA     1 
ATOM   9113  C  C      . MET B 1 582 ? 25.28300  -34.22900 8.66700   1.000 101.81000 ? 573 MET B C      1 
ATOM   9114  O  O      . MET B 1 582 ? 25.79500  -34.79700 7.69600   1.000 120.22000 ? 573 MET B O      1 
ATOM   9115  C  CB     . MET B 1 582 ? 22.95300  -33.36300 8.37800   1.000 83.97000  ? 573 MET B CB     1 
ATOM   9116  C  CG     . MET B 1 582 ? 22.86700  -33.47000 6.85800   1.000 66.03000  ? 573 MET B CG     1 
ATOM   9117  S  SD     . MET B 1 582 ? 21.52800  -32.51100 6.12000   1.000 100.47000 ? 573 MET B SD     1 
ATOM   9118  C  CE     . MET B 1 582 ? 21.23100  -33.45200 4.62700   1.000 91.13000  ? 573 MET B CE     1 
ATOM   9119  N  N      . VAL B 1 583 ? 25.96900  -33.38800 9.44200   1.000 93.56000  ? 574 VAL B N      1 
ATOM   9120  C  CA     . VAL B 1 583 ? 27.39100  -33.14000 9.21100   1.000 92.79000  ? 574 VAL B CA     1 
ATOM   9121  C  C      . VAL B 1 583 ? 28.20000  -34.40900 9.44000   1.000 97.54000  ? 574 VAL B C      1 
ATOM   9122  O  O      . VAL B 1 583 ? 29.15800  -34.69200 8.70900   1.000 116.64000 ? 574 VAL B O      1 
ATOM   9123  C  CB     . VAL B 1 583 ? 27.89100  -31.98700 10.10100  1.000 103.76000 ? 574 VAL B CB     1 
ATOM   9124  C  CG1    . VAL B 1 583 ? 29.40500  -31.91600 10.07400  1.000 84.67000  ? 574 VAL B CG1    1 
ATOM   9125  C  CG2    . VAL B 1 583 ? 27.30000  -30.66600 9.63500   1.000 107.28000 ? 574 VAL B CG2    1 
ATOM   9126  N  N      . ASP B 1 584 ? 27.83100  -35.19100 10.45600  1.000 99.57000  ? 575 ASP B N      1 
ATOM   9127  C  CA     . ASP B 1 584 ? 28.58300  -36.40200 10.76400  1.000 116.87000 ? 575 ASP B CA     1 
ATOM   9128  C  C      . ASP B 1 584 ? 28.56400  -37.36100 9.58100   1.000 114.95000 ? 575 ASP B C      1 
ATOM   9129  O  O      . ASP B 1 584 ? 29.59900  -37.92400 9.20800   1.000 144.62000 ? 575 ASP B O      1 
ATOM   9130  C  CB     . ASP B 1 584 ? 28.00600  -37.07000 12.01300  1.000 114.41000 ? 575 ASP B CB     1 
ATOM   9131  C  CG     . ASP B 1 584 ? 28.32400  -36.30500 13.29000  1.000 132.00000 ? 575 ASP B CG     1 
ATOM   9132  O  OD1    . ASP B 1 584 ? 29.16800  -35.38100 13.25500  1.000 111.77000 ? 575 ASP B OD1    1 
ATOM   9133  O  OD2    . ASP B 1 584 ? 27.72100  -36.63000 14.33400  1.000 142.57000 ? 575 ASP B OD2    1 
ATOM   9134  N  N      . GLU B 1 585 ? 27.39600  -37.57200 8.98300   1.000 100.78000 ? 576 GLU B N      1 
ATOM   9135  C  CA     . GLU B 1 585 ? 27.35100  -38.27200 7.70900   1.000 105.06000 ? 576 GLU B CA     1 
ATOM   9136  C  C      . GLU B 1 585 ? 27.87400  -37.33300 6.63100   1.000 112.84000 ? 576 GLU B C      1 
ATOM   9137  O  O      . GLU B 1 585 ? 27.59000  -36.13200 6.64600   1.000 114.75000 ? 576 GLU B O      1 
ATOM   9138  C  CB     . GLU B 1 585 ? 25.93100  -38.74000 7.38700   1.000 95.69000  ? 576 GLU B CB     1 
ATOM   9139  C  CG     . GLU B 1 585 ? 25.86300  -39.91000 6.40600   1.000 95.99000  ? 576 GLU B CG     1 
ATOM   9140  C  CD     . GLU B 1 585 ? 24.74300  -40.87300 6.73200   1.000 113.98000 ? 576 GLU B CD     1 
ATOM   9141  O  OE1    . GLU B 1 585 ? 24.41500  -41.72200 5.87800   1.000 123.53000 ? 576 GLU B OE1    1 
ATOM   9142  O  OE2    . GLU B 1 585 ? 24.18500  -40.77700 7.84400   1.000 111.84000 ? 576 GLU B OE2    1 
ATOM   9143  N  N      . ILE B 1 586 ? 28.64900  -37.87500 5.70200   1.000 120.60000 ? 577 ILE B N      1 
ATOM   9144  C  CA     . ILE B 1 586 ? 29.22900  -37.05600 4.64800   1.000 111.98000 ? 577 ILE B CA     1 
ATOM   9145  C  C      . ILE B 1 586 ? 30.27100  -36.10300 5.23100   1.000 103.07000 ? 577 ILE B C      1 
ATOM   9146  O  O      . ILE B 1 586 ? 31.01100  -36.44700 6.15600   1.000 80.49000  ? 577 ILE B O      1 
ATOM   9147  C  CB     . ILE B 1 586 ? 28.14500  -36.26800 3.88800   1.000 106.78000 ? 577 ILE B CB     1 
ATOM   9148  C  CG1    . ILE B 1 586 ? 27.04400  -37.21100 3.39200   1.000 117.32000 ? 577 ILE B CG1    1 
ATOM   9149  C  CG2    . ILE B 1 586 ? 28.76700  -35.47000 2.74600   1.000 109.87000 ? 577 ILE B CG2    1 
ATOM   9150  C  CD1    . ILE B 1 586 ? 25.84700  -36.49400 2.80100   1.000 107.73000 ? 577 ILE B CD1    1 
ATOM   9151  N  N      . ALA B 1 601 ? 29.54600  -43.74900 -12.03300 1.000 146.31000 ? 592 ALA B N      1 
ATOM   9152  C  CA     . ALA B 1 601 ? 28.41500  -43.23300 -11.26900 1.000 146.79000 ? 592 ALA B CA     1 
ATOM   9153  C  C      . ALA B 1 601 ? 28.89100  -42.44100 -10.05500 1.000 144.30000 ? 592 ALA B C      1 
ATOM   9154  O  O      . ALA B 1 601 ? 28.72300  -42.87800 -8.91600  1.000 146.94000 ? 592 ALA B O      1 
ATOM   9155  C  CB     . ALA B 1 601 ? 27.50400  -44.37400 -10.83600 1.000 139.92000 ? 592 ALA B CB     1 
ATOM   9156  N  N      . LYS B 1 602 ? 29.48500  -41.27300 -10.30500 1.000 131.96000 ? 593 LYS B N      1 
ATOM   9157  C  CA     . LYS B 1 602 ? 29.99800  -40.45900 -9.20400  1.000 138.59000 ? 593 LYS B CA     1 
ATOM   9158  C  C      . LYS B 1 602 ? 28.89700  -40.02900 -8.24500  1.000 156.24000 ? 593 LYS B C      1 
ATOM   9159  O  O      . LYS B 1 602 ? 29.08500  -40.15800 -7.02200  1.000 163.09000 ? 593 LYS B O      1 
ATOM   9160  C  CB     . LYS B 1 602 ? 30.75300  -39.25000 -9.76700  1.000 115.02000 ? 593 LYS B CB     1 
ATOM   9161  C  CG     . LYS B 1 602 ? 31.55100  -38.47500 -8.72800  1.000 113.79000 ? 593 LYS B CG     1 
ATOM   9162  C  CD     . LYS B 1 602 ? 32.49100  -37.46400 -9.37200  1.000 102.17000 ? 593 LYS B CD     1 
ATOM   9163  C  CE     . LYS B 1 602 ? 33.39500  -36.81100 -8.33200  1.000 90.46000  ? 593 LYS B CE     1 
ATOM   9164  N  NZ     . LYS B 1 602 ? 34.43200  -35.94600 -8.96500  1.000 73.79000  ? 593 LYS B NZ     1 
ATOM   9165  N  N      . PRO B 1 603 ? 27.75200  -39.51600 -8.70400  1.000 149.58000 ? 594 PRO B N      1 
ATOM   9166  C  CA     . PRO B 1 603 ? 26.67500  -39.14300 -7.77400  1.000 143.63000 ? 594 PRO B CA     1 
ATOM   9167  C  C      . PRO B 1 603 ? 25.98900  -40.34100 -7.13600  1.000 140.23000 ? 594 PRO B C      1 
ATOM   9168  O  O      . PRO B 1 603 ? 25.76900  -40.36300 -5.92100  1.000 118.77000 ? 594 PRO B O      1 
ATOM   9169  C  CB     . PRO B 1 603 ? 25.69900  -38.36400 -8.66400  1.000 136.53000 ? 594 PRO B CB     1 
ATOM   9170  C  CG     . PRO B 1 603 ? 25.97400  -38.85100 -10.05600 1.000 138.35000 ? 594 PRO B CG     1 
ATOM   9171  C  CD     . PRO B 1 603 ? 27.44200  -39.15300 -10.09700 1.000 132.19000 ? 594 PRO B CD     1 
ATOM   9172  N  N      . ASP B 1 604 ? 25.63200  -41.33300 -7.95100  1.000 151.63000 ? 595 ASP B N      1 
ATOM   9173  C  CA     . ASP B 1 604 ? 24.94300  -42.55100 -7.49700  1.000 148.51000 ? 595 ASP B CA     1 
ATOM   9174  C  C      . ASP B 1 604 ? 23.66900  -42.11300 -6.76800  1.000 152.77000 ? 595 ASP B C      1 
ATOM   9175  O  O      . ASP B 1 604 ? 22.91500  -41.29500 -7.31300  1.000 145.21000 ? 595 ASP B O      1 
ATOM   9176  C  CB     . ASP B 1 604 ? 25.91100  -43.40300 -6.68600  1.000 138.03000 ? 595 ASP B CB     1 
ATOM   9177  C  CG     . ASP B 1 604 ? 25.63400  -44.88700 -6.81900  1.000 122.62000 ? 595 ASP B CG     1 
ATOM   9178  O  OD1    . ASP B 1 604 ? 24.74900  -45.26200 -7.61500  1.000 118.76000 ? 595 ASP B OD1    1 
ATOM   9179  O  OD2    . ASP B 1 604 ? 26.30500  -45.68100 -6.12600  1.000 121.85000 ? 595 ASP B OD2    1 
ATOM   9180  N  N      . TYR B 1 605 ? 23.39500  -42.60800 -5.55900  1.000 153.60000 ? 596 TYR B N      1 
ATOM   9181  C  CA     . TYR B 1 605 ? 22.17900  -42.26500 -4.82400  1.000 150.66000 ? 596 TYR B CA     1 
ATOM   9182  C  C      . TYR B 1 605 ? 22.53900  -41.80400 -3.41900  1.000 135.73000 ? 596 TYR B C      1 
ATOM   9183  O  O      . TYR B 1 605 ? 22.97500  -42.61200 -2.59200  1.000 134.53000 ? 596 TYR B O      1 
ATOM   9184  C  CB     . TYR B 1 605 ? 21.21600  -43.45300 -4.73800  1.000 146.80000 ? 596 TYR B CB     1 
ATOM   9185  C  CG     . TYR B 1 605 ? 21.17900  -44.33800 -5.95700  1.000 143.97000 ? 596 TYR B CG     1 
ATOM   9186  C  CD1    . TYR B 1 605 ? 20.53600  -43.93000 -7.11600  1.000 145.68000 ? 596 TYR B CD1    1 
ATOM   9187  C  CD2    . TYR B 1 605 ? 21.77500  -45.59100 -5.94200  1.000 139.39000 ? 596 TYR B CD2    1 
ATOM   9188  C  CE1    . TYR B 1 605 ? 20.49200  -44.74200 -8.23100  1.000 153.93000 ? 596 TYR B CE1    1 
ATOM   9189  C  CE2    . TYR B 1 605 ? 21.73700  -46.40900 -7.05100  1.000 147.53000 ? 596 TYR B CE2    1 
ATOM   9190  C  CZ     . TYR B 1 605 ? 21.09500  -45.98100 -8.19300  1.000 153.36000 ? 596 TYR B CZ     1 
ATOM   9191  O  OH     . TYR B 1 605 ? 21.05600  -46.79600 -9.30000  1.000 166.84000 ? 596 TYR B OH     1 
ATOM   9192  N  N      . ASN B 1 606 ? 22.37000  -40.51000 -3.15700  1.000 125.03000 ? 597 ASN B N      1 
ATOM   9193  C  CA     . ASN B 1 606 ? 22.54900  -39.93300 -1.83000  1.000 114.14000 ? 597 ASN B CA     1 
ATOM   9194  C  C      . ASN B 1 606 ? 21.21800  -39.38200 -1.33400  1.000 117.18000 ? 597 ASN B C      1 
ATOM   9195  O  O      . ASN B 1 606 ? 20.66000  -38.46400 -1.94600  1.000 116.43000 ? 597 ASN B O      1 
ATOM   9196  C  CB     . ASN B 1 606 ? 23.62000  -38.84200 -1.86300  1.000 119.36000 ? 597 ASN B CB     1 
ATOM   9197  C  CG     . ASN B 1 606 ? 24.77800  -39.20000 -2.77500  1.000 131.87000 ? 597 ASN B CG     1 
ATOM   9198  O  OD1    . ASN B 1 606 ? 25.62100  -40.02400 -2.42300  1.000 144.73000 ? 597 ASN B OD1    1 
ATOM   9199  N  ND2    . ASN B 1 606 ? 24.81000  -38.60300 -3.96100  1.000 126.98000 ? 597 ASN B ND2    1 
ATOM   9200  N  N      . ARG B 1 607 ? 20.70800  -39.93600 -0.23000  1.000 116.20000 ? 598 ARG B N      1 
ATOM   9201  C  CA     . ARG B 1 607 ? 19.44900  -39.48000 0.36000   1.000 90.47000  ? 598 ARG B CA     1 
ATOM   9202  C  C      . ARG B 1 607 ? 19.58200  -39.45900 1.88600   1.000 104.17000 ? 598 ARG B C      1 
ATOM   9203  O  O      . ARG B 1 607 ? 18.90100  -40.17000 2.62100   1.000 104.74000 ? 598 ARG B O      1 
ATOM   9204  C  CB     . ARG B 1 607 ? 18.27200  -40.34000 -0.09700  1.000 84.59000  ? 598 ARG B CB     1 
ATOM   9205  C  CG     . ARG B 1 607 ? 18.04400  -40.26800 -1.59900  1.000 105.76000 ? 598 ARG B CG     1 
ATOM   9206  C  CD     . ARG B 1 607 ? 16.94000  -41.18900 -2.07800  1.000 130.77000 ? 598 ARG B CD     1 
ATOM   9207  N  NE     . ARG B 1 607 ? 15.62200  -40.77800 -1.61300  1.000 121.16000 ? 598 ARG B NE     1 
ATOM   9208  C  CZ     . ARG B 1 607 ? 14.51700  -41.48900 -1.79100  1.000 135.34000 ? 598 ARG B CZ     1 
ATOM   9209  N  NH1    . ARG B 1 607 ? 14.54600  -42.67300 -2.37900  1.000 162.75000 ? 598 ARG B NH1    1 
ATOM   9210  N  NH2    . ARG B 1 607 ? 13.35100  -40.99000 -1.39300  1.000 123.03000 ? 598 ARG B NH2    1 
ATOM   9211  N  N      . CYS B 1 608 ? 20.49300  -38.60800 2.36100   1.000 116.77000 ? 599 CYS B N      1 
ATOM   9212  C  CA     . CYS B 1 608 ? 20.76200  -38.41600 3.78100   1.000 117.39000 ? 599 CYS B CA     1 
ATOM   9213  C  C      . CYS B 1 608 ? 19.58500  -37.80500 4.52500   1.000 108.72000 ? 599 CYS B C      1 
ATOM   9214  O  O      . CYS B 1 608 ? 19.56600  -37.84600 5.76100   1.000 100.41000 ? 599 CYS B O      1 
ATOM   9215  C  CB     . CYS B 1 608 ? 22.00300  -37.54200 3.97000   1.000 123.91000 ? 599 CYS B CB     1 
ATOM   9216  S  SG     . CYS B 1 608 ? 22.48900  -37.26900 5.69800   1.000 142.20000 ? 599 CYS B SG     1 
ATOM   9217  N  N      . ILE B 1 609 ? 18.62500  -37.21700 3.80700   1.000 104.77000 ? 600 ILE B N      1 
ATOM   9218  C  CA     . ILE B 1 609 ? 17.50800  -36.52200 4.44300   1.000 93.13000  ? 600 ILE B CA     1 
ATOM   9219  C  C      . ILE B 1 609 ? 16.85900  -37.39300 5.51100   1.000 94.26000  ? 600 ILE B C      1 
ATOM   9220  O  O      . ILE B 1 609 ? 16.57300  -36.92700 6.62300   1.000 104.40000 ? 600 ILE B O      1 
ATOM   9221  C  CB     . ILE B 1 609 ? 16.48500  -36.09300 3.37400   1.000 81.57000  ? 600 ILE B CB     1 
ATOM   9222  C  CG1    . ILE B 1 609 ? 16.97100  -34.84100 2.63700   1.000 92.62000  ? 600 ILE B CG1    1 
ATOM   9223  C  CG2    . ILE B 1 609 ? 15.11600  -35.86900 3.99700   1.000 107.00000 ? 600 ILE B CG2    1 
ATOM   9224  C  CD1    . ILE B 1 609 ? 17.96800  -35.12500 1.52200   1.000 86.71000  ? 600 ILE B CD1    1 
ATOM   9225  N  N      . GLU B 1 610 ? 16.64600  -38.67500 5.21000   1.000 92.28000  ? 601 GLU B N      1 
ATOM   9226  C  CA     . GLU B 1 610 ? 15.99300  -39.55000 6.17800   1.000 100.86000 ? 601 GLU B CA     1 
ATOM   9227  C  C      . GLU B 1 610 ? 16.73900  -39.54000 7.50500   1.000 107.02000 ? 601 GLU B C      1 
ATOM   9228  O  O      . GLU B 1 610 ? 16.13200  -39.36900 8.56900   1.000 117.76000 ? 601 GLU B O      1 
ATOM   9229  C  CB     . GLU B 1 610 ? 15.89800  -40.97100 5.62100   1.000 111.39000 ? 601 GLU B CB     1 
ATOM   9230  N  N      . ILE B 1 611 ? 18.07000  -39.65800 7.45400   1.000 101.99000 ? 602 ILE B N      1 
ATOM   9231  C  CA     . ILE B 1 611 ? 18.86800  -39.64100 8.67800   1.000 105.02000 ? 602 ILE B CA     1 
ATOM   9232  C  C      . ILE B 1 611 ? 18.54900  -38.39500 9.49000   1.000 109.85000 ? 602 ILE B C      1 
ATOM   9233  O  O      . ILE B 1 611 ? 18.35600  -38.45400 10.71100  1.000 106.49000 ? 602 ILE B O      1 
ATOM   9234  C  CB     . ILE B 1 611 ? 20.36800  -39.72500 8.34500   1.000 95.56000  ? 602 ILE B CB     1 
ATOM   9235  C  CG1    . ILE B 1 611 ? 20.63000  -40.82500 7.31400   1.000 105.74000 ? 602 ILE B CG1    1 
ATOM   9236  C  CG2    . ILE B 1 611 ? 21.18700  -39.95200 9.61300   1.000 101.61000 ? 602 ILE B CG2    1 
ATOM   9237  C  CD1    . ILE B 1 611 ? 20.38800  -42.22100 7.83400   1.000 119.95000 ? 602 ILE B CD1    1 
ATOM   9238  N  N      . THR B 1 612 ? 18.50100  -37.24000 8.82500   1.000 103.77000 ? 603 THR B N      1 
ATOM   9239  C  CA     . THR B 1 612 ? 18.09200  -36.03100 9.52500   1.000 84.25000  ? 603 THR B CA     1 
ATOM   9240  C  C      . THR B 1 612 ? 16.60600  -36.07900 9.85400   1.000 91.58000  ? 603 THR B C      1 
ATOM   9241  O  O      . THR B 1 612 ? 16.20700  -35.87500 11.00700  1.000 94.78000  ? 603 THR B O      1 
ATOM   9242  C  CB     . THR B 1 612 ? 18.41900  -34.79400 8.68500   1.000 78.38000  ? 603 THR B CB     1 
ATOM   9243  O  OG1    . THR B 1 612 ? 17.63100  -34.79600 7.48800   1.000 89.24000  ? 603 THR B OG1    1 
ATOM   9244  C  CG2    . THR B 1 612 ? 19.89700  -34.77500 8.30800   1.000 89.67000  ? 603 THR B CG2    1 
ATOM   9245  N  N      . SER B 1 613 ? 15.77700  -36.43000 8.86600   1.000 89.58000  ? 604 SER B N      1 
ATOM   9246  C  CA     . SER B 1 613 ? 14.33400  -36.39600 9.08000   1.000 87.93000  ? 604 SER B CA     1 
ATOM   9247  C  C      . SER B 1 613 ? 13.94000  -37.31000 10.22800  1.000 92.99000  ? 604 SER B C      1 
ATOM   9248  O  O      . SER B 1 613 ? 13.26300  -36.88500 11.17300  1.000 108.40000 ? 604 SER B O      1 
ATOM   9249  C  CB     . SER B 1 613 ? 13.60100  -36.78500 7.79600   1.000 92.20000  ? 604 SER B CB     1 
ATOM   9250  O  OG     . SER B 1 613 ? 13.88600  -35.87600 6.74600   1.000 95.60000  ? 604 SER B OG     1 
ATOM   9251  N  N      . ASP B 1 614 ? 14.41400  -38.55500 10.19700  1.000 90.29000  ? 605 ASP B N      1 
ATOM   9252  C  CA     . ASP B 1 614 ? 14.12900  -39.46300 11.29800  1.000 95.66000  ? 605 ASP B CA     1 
ATOM   9253  C  C      . ASP B 1 614 ? 14.60500  -38.84900 12.60300  1.000 103.40000 ? 605 ASP B C      1 
ATOM   9254  O  O      . ASP B 1 614 ? 13.85000  -38.77000 13.58200  1.000 115.10000 ? 605 ASP B O      1 
ATOM   9255  C  CB     . ASP B 1 614 ? 14.79400  -40.81800 11.05100  1.000 104.94000 ? 605 ASP B CB     1 
ATOM   9256  N  N      . ASN B 1 615 ? 15.83900  -38.33500 12.60900  1.000 94.07000  ? 606 ASN B N      1 
ATOM   9257  C  CA     . ASN B 1 615 ? 16.34500  -37.69000 13.81200  1.000 95.34000  ? 606 ASN B CA     1 
ATOM   9258  C  C      . ASN B 1 615 ? 15.42500  -36.55100 14.22100  1.000 95.90000  ? 606 ASN B C      1 
ATOM   9259  O  O      . ASN B 1 615 ? 15.00600  -36.46600 15.38300  1.000 90.98000  ? 606 ASN B O      1 
ATOM   9260  C  CB     . ASN B 1 615 ? 17.77000  -37.18300 13.57700  1.000 102.22000 ? 606 ASN B CB     1 
ATOM   9261  C  CG     . ASN B 1 615 ? 18.40600  -36.61900 14.83600  1.000 119.43000 ? 606 ASN B CG     1 
ATOM   9262  O  OD1    . ASN B 1 615 ? 18.20900  -35.45300 15.17600  1.000 119.94000 ? 606 ASN B OD1    1 
ATOM   9263  N  ND2    . ASN B 1 615 ? 19.18200  -37.44700 15.53100  1.000 116.16000 ? 606 ASN B ND2    1 
ATOM   9264  N  N      . ALA B 1 616 ? 15.01000  -35.72900 13.25500  1.000 99.23000  ? 607 ALA B N      1 
ATOM   9265  C  CA     . ALA B 1 616 ? 14.10800  -34.63600 13.58700  1.000 91.77000  ? 607 ALA B CA     1 
ATOM   9266  C  C      . ALA B 1 616 ? 12.82000  -35.18600 14.17800  1.000 94.33000  ? 607 ALA B C      1 
ATOM   9267  O  O      . ALA B 1 616 ? 12.35300  -34.71200 15.22200  1.000 96.78000  ? 607 ALA B O      1 
ATOM   9268  C  CB     . ALA B 1 616 ? 13.82500  -33.79000 12.34700  1.000 80.73000  ? 607 ALA B CB     1 
ATOM   9269  N  N      . LEU B 1 617 ? 12.27500  -36.24400 13.56600  1.000 104.48000 ? 608 LEU B N      1 
ATOM   9270  C  CA     . LEU B 1 617 ? 11.04200  -36.81900 14.08300  1.000 91.78000  ? 608 LEU B CA     1 
ATOM   9271  C  C      . LEU B 1 617 ? 11.24400  -37.33000 15.49900  1.000 93.33000  ? 608 LEU B C      1 
ATOM   9272  O  O      . LEU B 1 617 ? 10.32500  -37.25900 16.32100  1.000 105.57000 ? 608 LEU B O      1 
ATOM   9273  C  CB     . LEU B 1 617 ? 10.54400  -37.94400 13.17000  1.000 97.10000  ? 608 LEU B CB     1 
ATOM   9274  C  CG     . LEU B 1 617 ? 9.90800   -37.50200 11.85000  1.000 93.07000  ? 608 LEU B CG     1 
ATOM   9275  C  CD1    . LEU B 1 617 ? 9.67000   -38.70100 10.94200  1.000 97.06000  ? 608 LEU B CD1    1 
ATOM   9276  C  CD2    . LEU B 1 617 ? 8.60900   -36.76000 12.11400  1.000 78.76000  ? 608 LEU B CD2    1 
ATOM   9277  N  N      . LYS B 1 618 ? 12.42700  -37.86800 15.80000  1.000 89.13000  ? 609 LYS B N      1 
ATOM   9278  C  CA     . LYS B 1 618 ? 12.70600  -38.24500 17.17900  1.000 82.60000  ? 609 LYS B CA     1 
ATOM   9279  C  C      . LYS B 1 618 ? 12.90700  -37.01300 18.05300  1.000 92.12000  ? 609 LYS B C      1 
ATOM   9280  O  O      . LYS B 1 618 ? 12.35500  -36.93000 19.15800  1.000 94.85000  ? 609 LYS B O      1 
ATOM   9281  C  CB     . LYS B 1 618 ? 13.93400  -39.15200 17.23300  1.000 85.41000  ? 609 LYS B CB     1 
ATOM   9282  N  N      . GLN B 1 619 ? 13.64800  -36.02000 17.55100  1.000 101.57000 ? 610 GLN B N      1 
ATOM   9283  C  CA     . GLN B 1 619 ? 13.97400  -34.86400 18.37900  1.000 114.61000 ? 610 GLN B CA     1 
ATOM   9284  C  C      . GLN B 1 619 ? 12.74400  -34.01900 18.68800  1.000 105.67000 ? 610 GLN B C      1 
ATOM   9285  O  O      . GLN B 1 619 ? 12.65200  -33.43400 19.77300  1.000 89.29000  ? 610 GLN B O      1 
ATOM   9286  C  CB     . GLN B 1 619 ? 15.05700  -34.02500 17.70100  1.000 112.57000 ? 610 GLN B CB     1 
ATOM   9287  C  CG     . GLN B 1 619 ? 15.87800  -33.20500 18.68000  1.000 112.15000 ? 610 GLN B CG     1 
ATOM   9288  C  CD     . GLN B 1 619 ? 17.19400  -32.73700 18.10200  1.000 124.38000 ? 610 GLN B CD     1 
ATOM   9289  O  OE1    . GLN B 1 619 ? 18.05300  -32.23600 18.82700  1.000 140.14000 ? 610 GLN B OE1    1 
ATOM   9290  N  NE2    . GLN B 1 619 ? 17.36600  -32.90400 16.79500  1.000 124.37000 ? 610 GLN B NE2    1 
ATOM   9291  N  N      . MET B 1 620 ? 11.80300  -33.92800 17.74600  1.000 111.05000 ? 611 MET B N      1 
ATOM   9292  C  CA     . MET B 1 620 ? 10.55500  -33.21000 17.97500  1.000 103.09000 ? 611 MET B CA     1 
ATOM   9293  C  C      . MET B 1 620 ? 9.62400   -33.97200 18.90900  1.000 87.72000  ? 611 MET B C      1 
ATOM   9294  O  O      . MET B 1 620 ? 8.61500   -33.41000 19.35000  1.000 87.93000  ? 611 MET B O      1 
ATOM   9295  C  CB     . MET B 1 620 ? 9.86300   -32.91800 16.63500  1.000 105.36000 ? 611 MET B CB     1 
ATOM   9296  C  CG     . MET B 1 620 ? 9.28500   -34.13100 15.90900  1.000 108.42000 ? 611 MET B CG     1 
ATOM   9297  S  SD     . MET B 1 620 ? 7.56300   -34.46900 16.31600  1.000 100.08000 ? 611 MET B SD     1 
ATOM   9298  C  CE     . MET B 1 620 ? 6.73600   -33.09500 15.52400  1.000 81.42000  ? 611 MET B CE     1 
ATOM   9299  N  N      . GLY B 1 621 ? 9.94400   -35.23200 19.22000  1.000 86.79000  ? 612 GLY B N      1 
ATOM   9300  C  CA     . GLY B 1 621 ? 9.10500   -35.99800 20.12700  1.000 71.95000  ? 612 GLY B CA     1 
ATOM   9301  C  C      . GLY B 1 621 ? 8.91900   -35.32600 21.47400  1.000 65.59000  ? 612 GLY B C      1 
ATOM   9302  O  O      . GLY B 1 621 ? 7.80300   -35.24400 21.99200  1.000 69.95000  ? 612 GLY B O      1 
ATOM   9303  N  N      . TYR B 1 622 ? 10.01500  -34.83800 22.06400  1.000 72.47000  ? 613 TYR B N      1 
ATOM   9304  C  CA     . TYR B 1 622 ? 9.92300   -34.28800 23.41700  1.000 84.96000  ? 613 TYR B CA     1 
ATOM   9305  C  C      . TYR B 1 622 ? 9.11800   -32.99700 23.44300  1.000 81.07000  ? 613 TYR B C      1 
ATOM   9306  O  O      . TYR B 1 622 ? 8.24200   -32.85700 24.31500  1.000 78.30000  ? 613 TYR B O      1 
ATOM   9307  C  CB     . TYR B 1 622 ? 11.32500  -34.09600 24.00400  1.000 102.16000 ? 613 TYR B CB     1 
ATOM   9308  C  CG     . TYR B 1 622 ? 11.33500  -33.59100 25.43600  1.000 116.50000 ? 613 TYR B CG     1 
ATOM   9309  C  CD1    . TYR B 1 622 ? 10.64100  -34.26500 26.43400  1.000 122.77000 ? 613 TYR B CD1    1 
ATOM   9310  C  CD2    . TYR B 1 622 ? 12.05500  -32.45600 25.79300  1.000 114.30000 ? 613 TYR B CD2    1 
ATOM   9311  C  CE1    . TYR B 1 622 ? 10.64800  -33.81200 27.74400  1.000 117.66000 ? 613 TYR B CE1    1 
ATOM   9312  C  CE2    . TYR B 1 622 ? 12.07000  -31.99800 27.10200  1.000 105.92000 ? 613 TYR B CE2    1 
ATOM   9313  C  CZ     . TYR B 1 622 ? 11.36500  -32.68000 28.07100  1.000 108.34000 ? 613 TYR B CZ     1 
ATOM   9314  O  OH     . TYR B 1 622 ? 11.37700  -32.22900 29.37200  1.000 113.10000 ? 613 TYR B OH     1 
ATOM   9315  N  N      . PRO B 1 623 ? 9.34700   -32.02700 22.55000  1.000 78.81000  ? 614 PRO B N      1 
ATOM   9316  C  CA     . PRO B 1 623 ? 8.51900   -30.81000 22.58700  1.000 64.50000  ? 614 PRO B CA     1 
ATOM   9317  C  C      . PRO B 1 623 ? 7.04300   -31.09300 22.40300  1.000 74.50000  ? 614 PRO B C      1 
ATOM   9318  O  O      . PRO B 1 623 ? 6.20300   -30.52000 23.11000  1.000 77.10000  ? 614 PRO B O      1 
ATOM   9319  C  CB     . PRO B 1 623 ? 9.06900   -29.98800 21.41500  1.000 50.98000  ? 614 PRO B CB     1 
ATOM   9320  C  CG     . PRO B 1 623 ? 10.47700  -30.41400 21.30600  1.000 63.54000  ? 614 PRO B CG     1 
ATOM   9321  C  CD     . PRO B 1 623 ? 10.47800  -31.88900 21.61600  1.000 83.29000  ? 614 PRO B CD     1 
ATOM   9322  N  N      . ALA B 1 624 ? 6.70500   -31.98400 21.47300  1.000 72.16000  ? 615 ALA B N      1 
ATOM   9323  C  CA     . ALA B 1 624 ? 5.30700   -32.34000 21.28900  1.000 48.69000  ? 615 ALA B CA     1 
ATOM   9324  C  C      . ALA B 1 624 ? 4.72000   -32.87700 22.58400  1.000 52.58000  ? 615 ALA B C      1 
ATOM   9325  O  O      . ALA B 1 624 ? 3.63000   -32.46400 22.99800  1.000 65.17000  ? 615 ALA B O      1 
ATOM   9326  C  CB     . ALA B 1 624 ? 5.17200   -33.36300 20.16500  1.000 64.24000  ? 615 ALA B CB     1 
ATOM   9327  N  N      . PHE B 1 625 ? 5.45800   -33.75300 23.27000  1.000 47.93000  ? 616 PHE B N      1 
ATOM   9328  C  CA     . PHE B 1 625 ? 4.97100   -34.27600 24.54100  1.000 54.85000  ? 616 PHE B CA     1 
ATOM   9329  C  C      . PHE B 1 625 ? 4.64300   -33.14600 25.50400  1.000 59.83000  ? 616 PHE B C      1 
ATOM   9330  O  O      . PHE B 1 625 ? 3.70500   -33.25400 26.30300  1.000 77.92000  ? 616 PHE B O      1 
ATOM   9331  C  CB     . PHE B 1 625 ? 5.99800   -35.22200 25.16100  1.000 66.11000  ? 616 PHE B CB     1 
ATOM   9332  C  CG     . PHE B 1 625 ? 5.98100   -36.61200 24.57700  1.000 75.55000  ? 616 PHE B CG     1 
ATOM   9333  C  CD1    . PHE B 1 625 ? 4.78100   -37.23800 24.28400  1.000 57.56000  ? 616 PHE B CD1    1 
ATOM   9334  C  CD2    . PHE B 1 625 ? 7.16200   -37.29800 24.33400  1.000 82.50000  ? 616 PHE B CD2    1 
ATOM   9335  C  CE1    . PHE B 1 625 ? 4.75500   -38.51800 23.75000  1.000 55.41000  ? 616 PHE B CE1    1 
ATOM   9336  C  CE2    . PHE B 1 625 ? 7.14400   -38.57900 23.79900  1.000 91.51000  ? 616 PHE B CE2    1 
ATOM   9337  C  CZ     . PHE B 1 625 ? 5.94000   -39.19000 23.50600  1.000 91.55000  ? 616 PHE B CZ     1 
ATOM   9338  N  N      . ILE B 1 626 ? 5.42000   -32.06600 25.46700  1.000 60.86000  ? 617 ILE B N      1 
ATOM   9339  C  CA     . ILE B 1 626 ? 5.06400   -30.88700 26.24900  1.000 66.89000  ? 617 ILE B CA     1 
ATOM   9340  C  C      . ILE B 1 626 ? 3.70700   -30.35900 25.80200  1.000 72.72000  ? 617 ILE B C      1 
ATOM   9341  O  O      . ILE B 1 626 ? 2.72100   -30.40700 26.55000  1.000 76.04000  ? 617 ILE B O      1 
ATOM   9342  C  CB     . ILE B 1 626 ? 6.14700   -29.80300 26.11600  1.000 59.09000  ? 617 ILE B CB     1 
ATOM   9343  C  CG1    . ILE B 1 626 ? 7.46000   -30.28200 26.73400  1.000 79.82000  ? 617 ILE B CG1    1 
ATOM   9344  C  CG2    . ILE B 1 626 ? 5.66800   -28.49600 26.76100  1.000 54.57000  ? 617 ILE B CG2    1 
ATOM   9345  C  CD1    . ILE B 1 626 ? 8.67200   -29.54600 26.22800  1.000 68.21000  ? 617 ILE B CD1    1 
ATOM   9346  N  N      . ALA B 1 627 ? 3.62100   -29.95100 24.53000  1.000 66.59000  ? 618 ALA B N      1 
ATOM   9347  C  CA     . ALA B 1 627 ? 2.45300   -29.21600 24.05300  1.000 57.53000  ? 618 ALA B CA     1 
ATOM   9348  C  C      . ALA B 1 627 ? 1.16800   -29.98600 24.30700  1.000 54.55000  ? 618 ALA B C      1 
ATOM   9349  O  O      . ALA B 1 627 ? 0.12800   -29.38800 24.60800  1.000 67.06000  ? 618 ALA B O      1 
ATOM   9350  C  CB     . ALA B 1 627 ? 2.60000   -28.90100 22.56500  1.000 54.05000  ? 618 ALA B CB     1 
ATOM   9351  N  N      . ILE B 1 628 ? 1.21400   -31.31100 24.16900  1.000 53.65000  ? 619 ILE B N      1 
ATOM   9352  C  CA     . ILE B 1 628 ? 0.02000   -32.12500 24.35900  1.000 62.06000  ? 619 ILE B CA     1 
ATOM   9353  C  C      . ILE B 1 628 ? -0.21000  -32.41600 25.83500  1.000 49.28000  ? 619 ILE B C      1 
ATOM   9354  O  O      . ILE B 1 628 ? -1.34600  -32.35900 26.31800  1.000 52.40000  ? 619 ILE B O      1 
ATOM   9355  C  CB     . ILE B 1 628 ? 0.11600   -33.42100 23.53600  1.000 47.68000  ? 619 ILE B CB     1 
ATOM   9356  C  CG1    . ILE B 1 628 ? -0.09000  -33.12100 22.05100  1.000 50.56000  ? 619 ILE B CG1    1 
ATOM   9357  C  CG2    . ILE B 1 628 ? -0.91100  -34.42400 24.02300  1.000 46.15000  ? 619 ILE B CG2    1 
ATOM   9358  C  CD1    . ILE B 1 628 ? 0.24400   -34.27900 21.15100  1.000 49.52000  ? 619 ILE B CD1    1 
ATOM   9359  N  N      . LEU B 1 629 ? 0.85000   -32.73000 26.58000  1.000 44.25000  ? 620 LEU B N      1 
ATOM   9360  C  CA     . LEU B 1 629 ? 0.66400   -33.29200 27.91200  1.000 59.06000  ? 620 LEU B CA     1 
ATOM   9361  C  C      . LEU B 1 629 ? 0.65600   -32.25800 29.02900  1.000 63.32000  ? 620 LEU B C      1 
ATOM   9362  O  O      . LEU B 1 629 ? 0.26300   -32.59100 30.15400  1.000 67.77000  ? 620 LEU B O      1 
ATOM   9363  C  CB     . LEU B 1 629 ? 1.75000   -34.33200 28.19900  1.000 72.04000  ? 620 LEU B CB     1 
ATOM   9364  C  CG     . LEU B 1 629 ? 1.63200   -35.61500 27.37800  1.000 66.45000  ? 620 LEU B CG     1 
ATOM   9365  C  CD1    . LEU B 1 629 ? 2.95500   -36.37000 27.36300  1.000 95.64000  ? 620 LEU B CD1    1 
ATOM   9366  C  CD2    . LEU B 1 629 ? 0.50700   -36.48100 27.93100  1.000 78.96000  ? 620 LEU B CD2    1 
ATOM   9367  N  N      . THR B 1 630 ? 1.06700   -31.02300 28.76000  1.000 52.03000  ? 621 THR B N      1 
ATOM   9368  C  CA     . THR B 1 630 ? 1.04500   -30.01600 29.81500  1.000 57.27000  ? 621 THR B CA     1 
ATOM   9369  C  C      . THR B 1 630 ? -0.35200  -29.79100 30.38100  1.000 62.69000  ? 621 THR B C      1 
ATOM   9370  O  O      . THR B 1 630 ? -0.48400  -29.71400 31.61500  1.000 72.87000  ? 621 THR B O      1 
ATOM   9371  C  CB     . THR B 1 630 ? 1.64300   -28.70000 29.30300  1.000 59.88000  ? 621 THR B CB     1 
ATOM   9372  O  OG1    . THR B 1 630 ? 2.98300   -28.92500 28.84300  1.000 54.57000  ? 621 THR B OG1    1 
ATOM   9373  C  CG2    . THR B 1 630 ? 1.66100   -27.66900 30.42100  1.000 58.44000  ? 621 THR B CG2    1 
ATOM   9374  N  N      . PRO B 1 631 ? -1.41100  -29.67700 29.57500  1.000 54.96000  ? 622 PRO B N      1 
ATOM   9375  C  CA     . PRO B 1 631 ? -2.74800  -29.49200 30.16400  1.000 64.91000  ? 622 PRO B CA     1 
ATOM   9376  C  C      . PRO B 1 631 ? -3.18900  -30.65200 31.03700  1.000 67.22000  ? 622 PRO B C      1 
ATOM   9377  O  O      . PRO B 1 631 ? -3.79600  -30.43000 32.09200  1.000 67.57000  ? 622 PRO B O      1 
ATOM   9378  C  CB     . PRO B 1 631 ? -3.65600  -29.32500 28.93600  1.000 58.64000  ? 622 PRO B CB     1 
ATOM   9379  C  CG     . PRO B 1 631 ? -2.74700  -29.00800 27.80400  1.000 57.84000  ? 622 PRO B CG     1 
ATOM   9380  C  CD     . PRO B 1 631 ? -1.44900  -29.68100 28.10500  1.000 59.39000  ? 622 PRO B CD     1 
ATOM   9381  N  N      . LEU B 1 632 ? -2.91000  -31.88800 30.62500  1.000 71.28000  ? 623 LEU B N      1 
ATOM   9382  C  CA     . LEU B 1 632 ? -3.40300  -33.04200 31.37100  1.000 65.20000  ? 623 LEU B CA     1 
ATOM   9383  C  C      . LEU B 1 632 ? -2.79000  -33.11800 32.76600  1.000 73.00000  ? 623 LEU B C      1 
ATOM   9384  O  O      . LEU B 1 632 ? -3.50600  -33.08500 33.77400  1.000 76.84000  ? 623 LEU B O      1 
ATOM   9385  C  CB     . LEU B 1 632 ? -3.12100  -34.32300 30.58400  1.000 45.84000  ? 623 LEU B CB     1 
ATOM   9386  C  CG     . LEU B 1 632 ? -4.10300  -34.65400 29.45800  1.000 50.96000  ? 623 LEU B CG     1 
ATOM   9387  C  CD1    . LEU B 1 632 ? -4.03600  -33.62600 28.34000  1.000 66.90000  ? 623 LEU B CD1    1 
ATOM   9388  C  CD2    . LEU B 1 632 ? -3.79500  -36.03800 28.91800  1.000 94.68000  ? 623 LEU B CD2    1 
ATOM   9389  N  N      . VAL B 1 633 ? -1.45900  -33.16500 32.85000  1.000 61.81000  ? 624 VAL B N      1 
ATOM   9390  C  CA     . VAL B 1 633 ? -0.81600  -33.36100 34.14800  1.000 63.26000  ? 624 VAL B CA     1 
ATOM   9391  C  C      . VAL B 1 633 ? -1.21700  -32.24700 35.10900  1.000 82.98000  ? 624 VAL B C      1 
ATOM   9392  O  O      . VAL B 1 633 ? -1.82500  -32.49500 36.15900  1.000 89.50000  ? 624 VAL B O      1 
ATOM   9393  C  CB     . VAL B 1 633 ? 0.71200   -33.45500 33.98600  1.000 41.13000  ? 624 VAL B CB     1 
ATOM   9394  C  CG1    . VAL B 1 633 ? 1.26700   -32.23100 33.29500  1.000 53.13000  ? 624 VAL B CG1    1 
ATOM   9395  C  CG2    . VAL B 1 633 ? 1.37500   -33.63000 35.34100  1.000 52.95000  ? 624 VAL B CG2    1 
ATOM   9396  N  N      . THR B 1 634 ? -0.96400  -30.99700 34.71700  1.000 75.83000  ? 625 THR B N      1 
ATOM   9397  C  CA     . THR B 1 634 ? -1.32500  -29.87700 35.57500  1.000 61.75000  ? 625 THR B CA     1 
ATOM   9398  C  C      . THR B 1 634 ? -2.82800  -29.83200 35.80300  1.000 70.85000  ? 625 THR B C      1 
ATOM   9399  O  O      . THR B 1 634 ? -3.28400  -29.33700 36.83900  1.000 70.68000  ? 625 THR B O      1 
ATOM   9400  C  CB     . THR B 1 634 ? -0.83800  -28.56000 34.97200  1.000 43.74000  ? 625 THR B CB     1 
ATOM   9401  O  OG1    . THR B 1 634 ? -1.49000  -28.34100 33.71400  1.000 64.45000  ? 625 THR B OG1    1 
ATOM   9402  C  CG2    . THR B 1 634 ? 0.66800   -28.60100 34.76400  1.000 37.67000  ? 625 THR B CG2    1 
ATOM   9403  N  N      . GLY B 1 635 ? -3.61200  -30.35000 34.85600  1.000 65.57000  ? 626 GLY B N      1 
ATOM   9404  C  CA     . GLY B 1 635 ? -5.04900  -30.38100 35.02800  1.000 73.89000  ? 626 GLY B CA     1 
ATOM   9405  C  C      . GLY B 1 635 ? -5.45100  -31.45900 36.01200  1.000 80.83000  ? 626 GLY B C      1 
ATOM   9406  O  O      . GLY B 1 635 ? -6.35300  -31.25200 36.82800  1.000 93.47000  ? 626 GLY B O      1 
ATOM   9407  N  N      . PHE B 1 636 ? -4.79600  -32.62100 35.94400  1.000 67.89000  ? 627 PHE B N      1 
ATOM   9408  C  CA     . PHE B 1 636 ? -5.10100  -33.68400 36.89400  1.000 71.68000  ? 627 PHE B CA     1 
ATOM   9409  C  C      . PHE B 1 636 ? -4.43500  -33.44700 38.24600  1.000 74.39000  ? 627 PHE B C      1 
ATOM   9410  O  O      . PHE B 1 636 ? -4.93500  -33.92700 39.26900  1.000 83.75000  ? 627 PHE B O      1 
ATOM   9411  C  CB     . PHE B 1 636 ? -4.70900  -35.04100 36.31000  1.000 80.92000  ? 627 PHE B CB     1 
ATOM   9412  C  CG     . PHE B 1 636 ? -5.66900  -35.54800 35.26300  1.000 66.21000  ? 627 PHE B CG     1 
ATOM   9413  C  CD1    . PHE B 1 636 ? -6.99500  -35.79700 35.58300  1.000 70.61000  ? 627 PHE B CD1    1 
ATOM   9414  C  CD2    . PHE B 1 636 ? -5.24300  -35.78500 33.96400  1.000 60.30000  ? 627 PHE B CD2    1 
ATOM   9415  C  CE1    . PHE B 1 636 ? -7.88100  -36.26300 34.62100  1.000 61.87000  ? 627 PHE B CE1    1 
ATOM   9416  C  CE2    . PHE B 1 636 ? -6.12300  -36.25500 33.00300  1.000 43.74000  ? 627 PHE B CE2    1 
ATOM   9417  C  CZ     . PHE B 1 636 ? -7.44300  -36.49200 33.33300  1.000 38.56000  ? 627 PHE B CZ     1 
ATOM   9418  N  N      . LEU B 1 637 ? -3.30800  -32.72700 38.26800  1.000 70.01000  ? 628 LEU B N      1 
ATOM   9419  C  CA     . LEU B 1 637 ? -2.65700  -32.39700 39.53300  1.000 76.91000  ? 628 LEU B CA     1 
ATOM   9420  C  C      . LEU B 1 637 ? -3.42100  -31.30900 40.28000  1.000 90.42000  ? 628 LEU B C      1 
ATOM   9421  O  O      . LEU B 1 637 ? -3.75400  -31.46900 41.46100  1.000 88.03000  ? 628 LEU B O      1 
ATOM   9422  C  CB     . LEU B 1 637 ? -1.21300  -31.95100 39.28100  1.000 56.40000  ? 628 LEU B CB     1 
ATOM   9423  C  CG     . LEU B 1 637 ? -0.22100  -33.02100 38.82100  1.000 58.35000  ? 628 LEU B CG     1 
ATOM   9424  C  CD1    . LEU B 1 637 ? 1.11300   -32.39700 38.43800  1.000 42.61000  ? 628 LEU B CD1    1 
ATOM   9425  C  CD2    . LEU B 1 637 ? -0.03300  -34.05800 39.91500  1.000 95.00000  ? 628 LEU B CD2    1 
ATOM   9426  N  N      . LEU B 1 638 ? -3.72200  -30.19900 39.60400  1.000 88.44000  ? 629 LEU B N      1 
ATOM   9427  C  CA     . LEU B 1 638 ? -4.27500  -29.01600 40.25300  1.000 75.90000  ? 629 LEU B CA     1 
ATOM   9428  C  C      . LEU B 1 638 ? -5.71000  -28.71100 39.84600  1.000 78.39000  ? 629 LEU B C      1 
ATOM   9429  O  O      . LEU B 1 638 ? -6.55100  -28.44300 40.71200  1.000 103.97000 ? 629 LEU B O      1 
ATOM   9430  C  CB     . LEU B 1 638 ? -3.37500  -27.80500 39.96500  1.000 62.33000  ? 629 LEU B CB     1 
ATOM   9431  C  CG     . LEU B 1 638 ? -2.08900  -27.80500 40.79900  1.000 60.42000  ? 629 LEU B CG     1 
ATOM   9432  C  CD1    . LEU B 1 638 ? -1.10100  -28.83900 40.26100  1.000 77.21000  ? 629 LEU B CD1    1 
ATOM   9433  C  CD2    . LEU B 1 638 ? -1.45300  -26.43100 40.85000  1.000 52.28000  ? 629 LEU B CD2    1 
ATOM   9434  N  N      . GLY B 1 639 ? -6.02800  -28.73500 38.55600  1.000 56.40000  ? 630 GLY B N      1 
ATOM   9435  C  CA     . GLY B 1 639 ? -7.40500  -28.59000 38.14200  1.000 78.92000  ? 630 GLY B CA     1 
ATOM   9436  C  C      . GLY B 1 639 ? -7.54100  -27.73200 36.90300  1.000 65.82000  ? 630 GLY B C      1 
ATOM   9437  O  O      . GLY B 1 639 ? -6.56000  -27.36500 36.25800  1.000 63.63000  ? 630 GLY B O      1 
ATOM   9438  N  N      . ALA B 1 640 ? -8.80000  -27.41300 36.58400  1.000 65.57000  ? 631 ALA B N      1 
ATOM   9439  C  CA     . ALA B 1 640 ? -9.13800  -26.68700 35.36600  1.000 52.17000  ? 631 ALA B CA     1 
ATOM   9440  C  C      . ALA B 1 640 ? -8.79000  -25.20600 35.45800  1.000 69.05000  ? 631 ALA B C      1 
ATOM   9441  O  O      . ALA B 1 640 ? -8.47900  -24.58600 34.43600  1.000 80.38000  ? 631 ALA B O      1 
ATOM   9442  C  CB     . ALA B 1 640 ? -10.62600 -26.85300 35.05200  1.000 74.09000  ? 631 ALA B CB     1 
ATOM   9443  N  N      . GLU B 1 641 ? -8.84900  -24.61600 36.65400  1.000 62.98000  ? 632 GLU B N      1 
ATOM   9444  C  CA     . GLU B 1 641 ? -8.50600  -23.20100 36.78000  1.000 71.19000  ? 632 GLU B CA     1 
ATOM   9445  C  C      . GLU B 1 641 ? -7.01800  -22.96600 36.54000  1.000 75.77000  ? 632 GLU B C      1 
ATOM   9446  O  O      . GLU B 1 641 ? -6.63300  -21.98200 35.89500  1.000 76.40000  ? 632 GLU B O      1 
ATOM   9447  C  CB     . GLU B 1 641 ? -8.91900  -22.67500 38.15400  1.000 79.12000  ? 632 GLU B CB     1 
ATOM   9448  C  CG     . GLU B 1 641 ? -10.41400 -22.74000 38.39700  1.000 101.52000 ? 632 GLU B CG     1 
ATOM   9449  C  CD     . GLU B 1 641 ? -11.20700 -22.05200 37.30400  1.000 116.50000 ? 632 GLU B CD     1 
ATOM   9450  O  OE1    . GLU B 1 641 ? -10.72400 -21.03400 36.76700  1.000 112.28000 ? 632 GLU B OE1    1 
ATOM   9451  O  OE2    . GLU B 1 641 ? -12.31200 -22.53400 36.97700  1.000 137.89000 ? 632 GLU B OE2    1 
ATOM   9452  N  N      . PHE B 1 642 ? -6.16600  -23.85500 37.05700  1.000 59.90000  ? 633 PHE B N      1 
ATOM   9453  C  CA     . PHE B 1 642 ? -4.73300  -23.76800 36.79100  1.000 46.16000  ? 633 PHE B CA     1 
ATOM   9454  C  C      . PHE B 1 642 ? -4.43100  -23.91000 35.30200  1.000 49.40000  ? 633 PHE B C      1 
ATOM   9455  O  O      . PHE B 1 642 ? -3.56000  -23.21200 34.76300  1.000 65.99000  ? 633 PHE B O      1 
ATOM   9456  C  CB     . PHE B 1 642 ? -4.00300  -24.84600 37.59500  1.000 57.22000  ? 633 PHE B CB     1 
ATOM   9457  C  CG     . PHE B 1 642 ? -2.51100  -24.66100 37.66400  1.000 63.52000  ? 633 PHE B CG     1 
ATOM   9458  C  CD1    . PHE B 1 642 ? -1.69800  -25.07800 36.62100  1.000 69.90000  ? 633 PHE B CD1    1 
ATOM   9459  C  CD2    . PHE B 1 642 ? -1.92000  -24.08900 38.77900  1.000 69.41000  ? 633 PHE B CD2    1 
ATOM   9460  C  CE1    . PHE B 1 642 ? -0.32400  -24.91800 36.68300  1.000 53.37000  ? 633 PHE B CE1    1 
ATOM   9461  C  CE2    . PHE B 1 642 ? -0.54300  -23.92700 38.84700  1.000 69.02000  ? 633 PHE B CE2    1 
ATOM   9462  C  CZ     . PHE B 1 642 ? 0.25300   -24.34200 37.79600  1.000 60.44000  ? 633 PHE B CZ     1 
ATOM   9463  N  N      . VAL B 1 643 ? -5.16000  -24.79100 34.61300  1.000 52.09000  ? 634 VAL B N      1 
ATOM   9464  C  CA     . VAL B 1 643 ? -4.91900  -25.00600 33.19000  1.000 37.36000  ? 634 VAL B CA     1 
ATOM   9465  C  C      . VAL B 1 643 ? -5.27900  -23.76300 32.38900  1.000 46.20000  ? 634 VAL B C      1 
ATOM   9466  O  O      . VAL B 1 643 ? -4.61900  -23.44100 31.39600  1.000 58.58000  ? 634 VAL B O      1 
ATOM   9467  C  CB     . VAL B 1 643 ? -5.69200  -26.24200 32.69700  1.000 42.67000  ? 634 VAL B CB     1 
ATOM   9468  C  CG1    . VAL B 1 643 ? -5.72300  -26.27100 31.18100  1.000 52.85000  ? 634 VAL B CG1    1 
ATOM   9469  C  CG2    . VAL B 1 643 ? -5.05200  -27.50800 33.24200  1.000 53.18000  ? 634 VAL B CG2    1 
ATOM   9470  N  N      . GLY B 1 644 ? -6.33800  -23.05800 32.78200  1.000 39.68000  ? 635 GLY B N      1 
ATOM   9471  C  CA     . GLY B 1 644 ? -6.66000  -21.81400 32.10200  1.000 51.37000  ? 635 GLY B CA     1 
ATOM   9472  C  C      . GLY B 1 644 ? -5.54100  -20.79500 32.20400  1.000 46.24000  ? 635 GLY B C      1 
ATOM   9473  O  O      . GLY B 1 644 ? -5.20400  -20.12000 31.22300  1.000 57.33000  ? 635 GLY B O      1 
ATOM   9474  N  N      . GLY B 1 645 ? -4.94200  -20.67600 33.38800  1.000 50.90000  ? 636 GLY B N      1 
ATOM   9475  C  CA     . GLY B 1 645 ? -3.80100  -19.79100 33.53700  1.000 69.96000  ? 636 GLY B CA     1 
ATOM   9476  C  C      . GLY B 1 645 ? -2.62300  -20.22600 32.68800  1.000 61.53000  ? 636 GLY B C      1 
ATOM   9477  O  O      . GLY B 1 645 ? -1.94600  -19.39500 32.07200  1.000 66.54000  ? 636 GLY B O      1 
ATOM   9478  N  N      . VAL B 1 646 ? -2.34500  -21.53200 32.66200  1.000 53.94000  ? 637 VAL B N      1 
ATOM   9479  C  CA     . VAL B 1 646 ? -1.27600  -22.02200 31.79900  1.000 42.60000  ? 637 VAL B CA     1 
ATOM   9480  C  C      . VAL B 1 646 ? -1.55800  -21.64100 30.35400  1.000 56.59000  ? 637 VAL B C      1 
ATOM   9481  O  O      . VAL B 1 646 ? -0.66000  -21.21000 29.62300  1.000 74.43000  ? 637 VAL B O      1 
ATOM   9482  C  CB     . VAL B 1 646 ? -1.09700  -23.54200 31.95300  1.000 49.62000  ? 637 VAL B CB     1 
ATOM   9483  C  CG1    . VAL B 1 646 ? -0.29800  -24.08900 30.78300  1.000 31.14000  ? 637 VAL B CG1    1 
ATOM   9484  C  CG2    . VAL B 1 646 ? -0.41300  -23.87100 33.26900  1.000 58.28000  ? 637 VAL B CG2    1 
ATOM   9485  N  N      . LEU B 1 647 ? -2.81600  -21.77400 29.92500  1.000 46.97000  ? 638 LEU B N      1 
ATOM   9486  C  CA     . LEU B 1 647 ? -3.17100  -21.45300 28.54700  1.000 50.59000  ? 638 LEU B CA     1 
ATOM   9487  C  C      . LEU B 1 647 ? -2.92100  -19.98100 28.24300  1.000 54.58000  ? 638 LEU B C      1 
ATOM   9488  O  O      . LEU B 1 647 ? -2.32600  -19.64400 27.21400  1.000 41.70000  ? 638 LEU B O      1 
ATOM   9489  C  CB     . LEU B 1 647 ? -4.63400  -21.81400 28.27300  1.000 31.77000  ? 638 LEU B CB     1 
ATOM   9490  C  CG     . LEU B 1 647 ? -5.05400  -23.28500 28.26500  1.000 34.23000  ? 638 LEU B CG     1 
ATOM   9491  C  CD1    . LEU B 1 647 ? -6.56000  -23.39900 28.06300  1.000 53.28000  ? 638 LEU B CD1    1 
ATOM   9492  C  CD2    . LEU B 1 647 ? -4.31500  -24.06000 27.19200  1.000 16.76000  ? 638 LEU B CD2    1 
ATOM   9493  N  N      . ILE B 1 648 ? -3.37900  -19.08600 29.12100  1.000 51.97000  ? 639 ILE B N      1 
ATOM   9494  C  CA     . ILE B 1 648 ? -3.23600  -17.65900 28.83200  1.000 38.14000  ? 639 ILE B CA     1 
ATOM   9495  C  C      . ILE B 1 648 ? -1.76800  -17.25300 28.84200  1.000 43.40000  ? 639 ILE B C      1 
ATOM   9496  O  O      . ILE B 1 648 ? -1.30700  -16.51000 27.96400  1.000 61.89000  ? 639 ILE B O      1 
ATOM   9497  C  CB     . ILE B 1 648 ? -4.05900  -16.80500 29.81500  1.000 38.35000  ? 639 ILE B CB     1 
ATOM   9498  C  CG1    . ILE B 1 648 ? -3.57000  -17.00200 31.24800  1.000 52.05000  ? 639 ILE B CG1    1 
ATOM   9499  C  CG2    . ILE B 1 648 ? -5.54700  -17.12200 29.69300  1.000 54.87000  ? 639 ILE B CG2    1 
ATOM   9500  C  CD1    . ILE B 1 648 ? -4.16400  -16.01100 32.22400  1.000 68.48000  ? 639 ILE B CD1    1 
ATOM   9501  N  N      . GLY B 1 649 ? -1.00900  -17.72500 29.83200  1.000 35.39000  ? 640 GLY B N      1 
ATOM   9502  C  CA     . GLY B 1 649 ? 0.40300   -17.39200 29.86900  1.000 32.43000  ? 640 GLY B CA     1 
ATOM   9503  C  C      . GLY B 1 649 ? 1.14200   -17.92100 28.65700  1.000 43.53000  ? 640 GLY B C      1 
ATOM   9504  O  O      . GLY B 1 649 ? 1.98000   -17.22600 28.07500  1.000 51.43000  ? 640 GLY B O      1 
ATOM   9505  N  N      . THR B 1 650 ? 0.83600   -19.15600 28.25500  1.000 43.97000  ? 641 THR B N      1 
ATOM   9506  C  CA     . THR B 1 650 ? 1.46800   -19.71700 27.07300  1.000 37.49000  ? 641 THR B CA     1 
ATOM   9507  C  C      . THR B 1 650 ? 1.09200   -18.93000 25.82900  1.000 49.60000  ? 641 THR B C      1 
ATOM   9508  O  O      . THR B 1 650 ? 1.94600   -18.65800 24.98600  1.000 57.79000  ? 641 THR B O      1 
ATOM   9509  C  CB     . THR B 1 650 ? 1.08000   -21.18500 26.91400  1.000 44.57000  ? 641 THR B CB     1 
ATOM   9510  O  OG1    . THR B 1 650 ? 1.76100   -21.96500 27.90400  1.000 48.47000  ? 641 THR B OG1    1 
ATOM   9511  C  CG2    . THR B 1 650 ? 1.46000   -21.68500 25.53000  1.000 54.35000  ? 641 THR B CG2    1 
ATOM   9512  N  N      . VAL B 1 651 ? -0.17500  -18.53600 25.70200  1.000 42.92000  ? 642 VAL B N      1 
ATOM   9513  C  CA     . VAL B 1 651 ? -0.59000  -17.77400 24.52700  1.000 45.91000  ? 642 VAL B CA     1 
ATOM   9514  C  C      . VAL B 1 651 ? 0.18100   -16.46300 24.45200  1.000 35.85000  ? 642 VAL B C      1 
ATOM   9515  O  O      . VAL B 1 651 ? 0.73000   -16.10200 23.40400  1.000 52.83000  ? 642 VAL B O      1 
ATOM   9516  C  CB     . VAL B 1 651 ? -2.11000  -17.53600 24.54600  1.000 40.24000  ? 642 VAL B CB     1 
ATOM   9517  C  CG1    . VAL B 1 651 ? -2.49100  -16.49700 23.51300  1.000 30.03000  ? 642 VAL B CG1    1 
ATOM   9518  C  CG2    . VAL B 1 651 ? -2.86000  -18.83800 24.28700  1.000 42.84000  ? 642 VAL B CG2    1 
ATOM   9519  N  N      . LEU B 1 652 ? 0.25100   -15.74100 25.57200  1.000 25.81000  ? 643 LEU B N      1 
ATOM   9520  C  CA     . LEU B 1 652 ? 0.94600   -14.45600 25.57500  1.000 40.12000  ? 643 LEU B CA     1 
ATOM   9521  C  C      . LEU B 1 652 ? 2.42800   -14.62600 25.25100  1.000 43.28000  ? 643 LEU B C      1 
ATOM   9522  O  O      . LEU B 1 652 ? 2.96800   -13.96700 24.34500  1.000 52.03000  ? 643 LEU B O      1 
ATOM   9523  C  CB     . LEU B 1 652 ? 0.76300   -13.77300 26.93000  1.000 36.96000  ? 643 LEU B CB     1 
ATOM   9524  C  CG     . LEU B 1 652 ? -0.66000  -13.34000 27.28400  1.000 34.23000  ? 643 LEU B CG     1 
ATOM   9525  C  CD1    . LEU B 1 652 ? -0.77000  -13.05200 28.77000  1.000 33.66000  ? 643 LEU B CD1    1 
ATOM   9526  C  CD2    . LEU B 1 652 ? -1.05100  -12.11800 26.47500  1.000 30.88000  ? 643 LEU B CD2    1 
ATOM   9527  N  N      . SER B 1 653 ? 3.10600   -15.50700 25.99100  1.000 23.93000  ? 644 SER B N      1 
ATOM   9528  C  CA     . SER B 1 653 ? 4.53400   -15.69100 25.78100  1.000 31.93000  ? 644 SER B CA     1 
ATOM   9529  C  C      . SER B 1 653 ? 4.82000   -16.19500 24.37600  1.000 46.08000  ? 644 SER B C      1 
ATOM   9530  O  O      . SER B 1 653 ? 5.79800   -15.77800 23.74700  1.000 53.50000  ? 644 SER B O      1 
ATOM   9531  C  CB     . SER B 1 653 ? 5.09900   -16.65000 26.82700  1.000 37.05000  ? 644 SER B CB     1 
ATOM   9532  O  OG     . SER B 1 653 ? 5.24500   -15.99900 28.07600  1.000 47.15000  ? 644 SER B OG     1 
ATOM   9533  N  N      . GLY B 1 654 ? 3.97300   -17.08500 23.85700  1.000 38.13000  ? 645 GLY B N      1 
ATOM   9534  C  CA     . GLY B 1 654 ? 4.20600   -17.61500 22.53000  1.000 43.34000  ? 645 GLY B CA     1 
ATOM   9535  C  C      . GLY B 1 654 ? 4.03000   -16.56500 21.45800  1.000 46.11000  ? 645 GLY B C      1 
ATOM   9536  O  O      . GLY B 1 654 ? 4.85000   -16.46200 20.54500  1.000 64.33000  ? 645 GLY B O      1 
ATOM   9537  N  N      . ALA B 1 655 ? 2.97800   -15.75100 21.56200  1.000 38.75000  ? 646 ALA B N      1 
ATOM   9538  C  CA     . ALA B 1 655 ? 2.81300   -14.66800 20.60100  1.000 42.80000  ? 646 ALA B CA     1 
ATOM   9539  C  C      . ALA B 1 655 ? 4.04000   -13.76600 20.59900  1.000 52.06000  ? 646 ALA B C      1 
ATOM   9540  O  O      . ALA B 1 655 ? 4.61800   -13.48100 19.53900  1.000 63.40000  ? 646 ALA B O      1 
ATOM   9541  C  CB     . ALA B 1 655 ? 1.54800   -13.86700 20.91500  1.000 28.13000  ? 646 ALA B CB     1 
ATOM   9542  N  N      . MET B 1 656 ? 4.47800   -13.33900 21.78700  1.000 49.52000  ? 647 MET B N      1 
ATOM   9543  C  CA     . MET B 1 656 ? 5.60000   -12.40600 21.85300  1.000 52.66000  ? 647 MET B CA     1 
ATOM   9544  C  C      . MET B 1 656 ? 6.88100   -13.03200 21.30100  1.000 54.88000  ? 647 MET B C      1 
ATOM   9545  O  O      . MET B 1 656 ? 7.58300   -12.42400 20.47900  1.000 57.70000  ? 647 MET B O      1 
ATOM   9546  C  CB     . MET B 1 656 ? 5.80200   -11.92800 23.29200  1.000 40.27000  ? 647 MET B CB     1 
ATOM   9547  C  CG     . MET B 1 656 ? 4.54700   -11.37100 23.95800  1.000 40.91000  ? 647 MET B CG     1 
ATOM   9548  S  SD     . MET B 1 656 ? 3.76100   -10.03800 23.02500  1.000 48.00000  ? 647 MET B SD     1 
ATOM   9549  C  CE     . MET B 1 656 ? 2.03000   -10.45100 23.23500  1.000 51.47000  ? 647 MET B CE     1 
ATOM   9550  N  N      . LEU B 1 657 ? 7.19900   -14.25500 21.73400  1.000 46.62000  ? 648 LEU B N      1 
ATOM   9551  C  CA     . LEU B 1 657 ? 8.44200   -14.88700 21.30700  1.000 46.90000  ? 648 LEU B CA     1 
ATOM   9552  C  C      . LEU B 1 657 ? 8.42800   -15.19000 19.81600  1.000 48.76000  ? 648 LEU B C      1 
ATOM   9553  O  O      . LEU B 1 657 ? 9.45000   -15.03200 19.13800  1.000 48.15000  ? 648 LEU B O      1 
ATOM   9554  C  CB     . LEU B 1 657 ? 8.69000   -16.16000 22.11600  1.000 49.54000  ? 648 LEU B CB     1 
ATOM   9555  C  CG     . LEU B 1 657 ? 9.15500   -15.96900 23.56200  1.000 36.79000  ? 648 LEU B CG     1 
ATOM   9556  C  CD1    . LEU B 1 657 ? 9.22800   -17.30200 24.28700  1.000 48.19000  ? 648 LEU B CD1    1 
ATOM   9557  C  CD2    . LEU B 1 657 ? 10.50400  -15.26800 23.60200  1.000 38.88000  ? 648 LEU B CD2    1 
ATOM   9558  N  N      . ALA B 1 658 ? 7.28500   -15.63200 19.28600  1.000 46.22000  ? 649 ALA B N      1 
ATOM   9559  C  CA     . ALA B 1 658 ? 7.19000   -15.91400 17.86000  1.000 64.18000  ? 649 ALA B CA     1 
ATOM   9560  C  C      . ALA B 1 658 ? 7.38900   -14.64600 17.04300  1.000 69.06000  ? 649 ALA B C      1 
ATOM   9561  O  O      . ALA B 1 658 ? 8.14600   -14.63600 16.06300  1.000 75.69000  ? 649 ALA B O      1 
ATOM   9562  C  CB     . ALA B 1 658 ? 5.84000   -16.55700 17.54200  1.000 58.14000  ? 649 ALA B CB     1 
ATOM   9563  N  N      . ILE B 1 659 ? 6.72200   -13.55700 17.43300  1.000 50.74000  ? 650 ILE B N      1 
ATOM   9564  C  CA     . ILE B 1 659 ? 6.92000   -12.29800 16.72000  1.000 46.65000  ? 650 ILE B CA     1 
ATOM   9565  C  C      . ILE B 1 659 ? 8.39500   -11.91700 16.73400  1.000 52.73000  ? 650 ILE B C      1 
ATOM   9566  O  O      . ILE B 1 659 ? 8.99600   -11.63600 15.68500  1.000 59.19000  ? 650 ILE B O      1 
ATOM   9567  C  CB     . ILE B 1 659 ? 6.04200   -11.18900 17.33000  1.000 39.58000  ? 650 ILE B CB     1 
ATOM   9568  C  CG1    . ILE B 1 659 ? 4.55800   -11.54700 17.21900  1.000 46.41000  ? 650 ILE B CG1    1 
ATOM   9569  C  CG2    . ILE B 1 659 ? 6.33700   -9.84400  16.67300  1.000 55.48000  ? 650 ILE B CG2    1 
ATOM   9570  C  CD1    . ILE B 1 659 ? 3.65800   -10.65200 18.05000  1.000 35.02000  ? 650 ILE B CD1    1 
ATOM   9571  N  N      . LEU B 1 660 ? 9.00800   -11.93900 17.92200  1.000 50.34000  ? 651 LEU B N      1 
ATOM   9572  C  CA     . LEU B 1 660 ? 10.40400  -11.52800 18.05400  1.000 50.83000  ? 651 LEU B CA     1 
ATOM   9573  C  C      . LEU B 1 660 ? 11.31700  -12.36400 17.16300  1.000 55.07000  ? 651 LEU B C      1 
ATOM   9574  O  O      . LEU B 1 660 ? 12.11200  -11.82400 16.38100  1.000 57.10000  ? 651 LEU B O      1 
ATOM   9575  C  CB     . LEU B 1 660 ? 10.82800  -11.62300 19.52000  1.000 46.78000  ? 651 LEU B CB     1 
ATOM   9576  C  CG     . LEU B 1 660 ? 12.22900  -11.14500 19.90300  1.000 47.95000  ? 651 LEU B CG     1 
ATOM   9577  C  CD1    . LEU B 1 660 ? 12.26800  -10.72400 21.36600  1.000 40.38000  ? 651 LEU B CD1    1 
ATOM   9578  C  CD2    . LEU B 1 660 ? 13.25100  -12.23500 19.64200  1.000 59.77000  ? 651 LEU B CD2    1 
ATOM   9579  N  N      . THR B 1 661 ? 11.21600  -13.69100 17.26800  1.000 57.85000  ? 652 THR B N      1 
ATOM   9580  C  CA     . THR B 1 661 ? 12.12300  -14.56900 16.53500  1.000 63.25000  ? 652 THR B CA     1 
ATOM   9581  C  C      . THR B 1 661 ? 11.93100  -14.43200 15.02700  1.000 56.82000  ? 652 THR B C      1 
ATOM   9582  O  O      . THR B 1 661 ? 12.90800  -14.30700 14.27100  1.000 74.26000  ? 652 THR B O      1 
ATOM   9583  C  CB     . THR B 1 661 ? 11.91500  -16.01700 16.98600  1.000 63.57000  ? 652 THR B CB     1 
ATOM   9584  O  OG1    . THR B 1 661 ? 10.53800  -16.37900 16.82900  1.000 73.65000  ? 652 THR B OG1    1 
ATOM   9585  C  CG2    . THR B 1 661 ? 12.29900  -16.17500 18.45400  1.000 50.36000  ? 652 THR B CG2    1 
ATOM   9586  N  N      . ALA B 1 662 ? 10.67600  -14.46100 14.56700  1.000 41.95000  ? 653 ALA B N      1 
ATOM   9587  C  CA     . ALA B 1 662 ? 10.41300  -14.37300 13.13500  1.000 49.68000  ? 653 ALA B CA     1 
ATOM   9588  C  C      . ALA B 1 662 ? 10.95600  -13.07200 12.56100  1.000 63.47000  ? 653 ALA B C      1 
ATOM   9589  O  O      . ALA B 1 662 ? 11.63400  -13.06700 11.52100  1.000 72.42000  ? 653 ALA B O      1 
ATOM   9590  C  CB     . ALA B 1 662 ? 8.91300   -14.49600 12.87100  1.000 44.80000  ? 653 ALA B CB     1 
ATOM   9591  N  N      . ASN B 1 663 ? 10.66600  -11.95100 13.22500  1.000 69.43000  ? 654 ASN B N      1 
ATOM   9592  C  CA     . ASN B 1 663 ? 11.12000  -10.67500 12.69300  1.000 67.77000  ? 654 ASN B CA     1 
ATOM   9593  C  C      . ASN B 1 663 ? 12.64100  -10.58100 12.71200  1.000 74.13000  ? 654 ASN B C      1 
ATOM   9594  O  O      . ASN B 1 663 ? 13.24400  -10.07700 11.75800  1.000 87.10000  ? 654 ASN B O      1 
ATOM   9595  C  CB     . ASN B 1 663 ? 10.49000  -9.52600  13.47800  1.000 56.76000  ? 654 ASN B CB     1 
ATOM   9596  C  CG     . ASN B 1 663 ? 9.01800   -9.34100  13.15100  1.000 60.83000  ? 654 ASN B CG     1 
ATOM   9597  O  OD1    . ASN B 1 663 ? 8.56900   -9.66200  12.05000  1.000 72.94000  ? 654 ASN B OD1    1 
ATOM   9598  N  ND2    . ASN B 1 663 ? 8.25800   -8.82600  14.11200  1.000 59.64000  ? 654 ASN B ND2    1 
ATOM   9599  N  N      . SER B 1 664 ? 13.28800  -11.08200 13.77100  1.000 59.70000  ? 655 SER B N      1 
ATOM   9600  C  CA     . SER B 1 664 ? 14.74500  -11.01400 13.82800  1.000 61.62000  ? 655 SER B CA     1 
ATOM   9601  C  C      . SER B 1 664 ? 15.37200  -11.78600 12.67100  1.000 83.16000  ? 655 SER B C      1 
ATOM   9602  O  O      . SER B 1 664 ? 16.28100  -11.28700 11.99000  1.000 102.48000 ? 655 SER B O      1 
ATOM   9603  C  CB     . SER B 1 664 ? 15.24500  -11.55300 15.17000  1.000 73.26000  ? 655 SER B CB     1 
ATOM   9604  O  OG     . SER B 1 664 ? 14.82400  -10.73800 16.25100  1.000 75.60000  ? 655 SER B OG     1 
ATOM   9605  N  N      . GLY B 1 665 ? 14.89200  -13.00900 12.43200  1.000 87.85000  ? 656 GLY B N      1 
ATOM   9606  C  CA     . GLY B 1 665 ? 15.45300  -13.80200 11.34700  1.000 75.64000  ? 656 GLY B CA     1 
ATOM   9607  C  C      . GLY B 1 665 ? 15.24300  -13.15300 9.99300   1.000 68.58000  ? 656 GLY B C      1 
ATOM   9608  O  O      . GLY B 1 665 ? 16.16900  -13.06700 9.17300   1.000 88.19000  ? 656 GLY B O      1 
ATOM   9609  N  N      . GLY B 1 666 ? 14.01800  -12.68200 9.73800   1.000 58.96000  ? 657 GLY B N      1 
ATOM   9610  C  CA     . GLY B 1 666 ? 13.74600  -12.03200 8.46600   1.000 85.02000  ? 657 GLY B CA     1 
ATOM   9611  C  C      . GLY B 1 666 ? 14.59400  -10.79300 8.25000   1.000 79.90000  ? 657 GLY B C      1 
ATOM   9612  O  O      . GLY B 1 666 ? 15.08700  -10.54800 7.14400   1.000 69.58000  ? 657 GLY B O      1 
ATOM   9613  N  N      . ALA B 1 667 ? 14.77400  -9.99200  9.30300   1.000 91.83000  ? 658 ALA B N      1 
ATOM   9614  C  CA     . ALA B 1 667 ? 15.57300  -8.78000  9.17600   1.000 95.16000  ? 658 ALA B CA     1 
ATOM   9615  C  C      . ALA B 1 667 ? 17.03300  -9.10400  8.89300   1.000 88.31000  ? 658 ALA B C      1 
ATOM   9616  O  O      . ALA B 1 667 ? 17.65800  -8.46300  8.04000   1.000 87.58000  ? 658 ALA B O      1 
ATOM   9617  C  CB     . ALA B 1 667 ? 15.44400  -7.93000  10.43900  1.000 83.98000  ? 658 ALA B CB     1 
ATOM   9618  N  N      . TRP B 1 668 ? 17.60400  -10.08900 9.59400   1.000 85.57000  ? 659 TRP B N      1 
ATOM   9619  C  CA     . TRP B 1 668 ? 18.98300  -10.45400 9.28200   1.000 88.53000  ? 659 TRP B CA     1 
ATOM   9620  C  C      . TRP B 1 668 ? 19.11400  -10.90500 7.83400   1.000 94.26000  ? 659 TRP B C      1 
ATOM   9621  O  O      . TRP B 1 668 ? 20.02600  -10.46700 7.12000   1.000 108.22000 ? 659 TRP B O      1 
ATOM   9622  C  CB     . TRP B 1 668 ? 19.49500  -11.54100 10.23400  1.000 101.26000 ? 659 TRP B CB     1 
ATOM   9623  C  CG     . TRP B 1 668 ? 20.09200  -11.01600 11.52400  1.000 110.73000 ? 659 TRP B CG     1 
ATOM   9624  C  CD1    . TRP B 1 668 ? 21.13300  -10.13600 11.64200  1.000 108.25000 ? 659 TRP B CD1    1 
ATOM   9625  C  CD2    . TRP B 1 668 ? 19.70900  -11.36000 12.86700  1.000 108.46000 ? 659 TRP B CD2    1 
ATOM   9626  N  NE1    . TRP B 1 668 ? 21.40900  -9.89800  12.96600  1.000 110.14000 ? 659 TRP B NE1    1 
ATOM   9627  C  CE2    . TRP B 1 668 ? 20.55100  -10.63600 13.73900  1.000 102.87000 ? 659 TRP B CE2    1 
ATOM   9628  C  CE3    . TRP B 1 668 ? 18.73500  -12.20000 13.41600  1.000 88.84000  ? 659 TRP B CE3    1 
ATOM   9629  C  CZ2    . TRP B 1 668 ? 20.44700  -10.72700 15.12500  1.000 80.52000  ? 659 TRP B CZ2    1 
ATOM   9630  C  CZ3    . TRP B 1 668 ? 18.63500  -12.28800 14.79600  1.000 72.02000  ? 659 TRP B CZ3    1 
ATOM   9631  C  CH2    . TRP B 1 668 ? 19.48600  -11.55600 15.63300  1.000 68.22000  ? 659 TRP B CH2    1 
ATOM   9632  N  N      . ASP B 1 669 ? 18.17800  -11.72900 7.35900   1.000 90.53000  ? 660 ASP B N      1 
ATOM   9633  C  CA     . ASP B 1 669 ? 18.28900  -12.22300 5.99000   1.000 92.24000  ? 660 ASP B CA     1 
ATOM   9634  C  C      . ASP B 1 669 ? 18.28800  -11.13700 4.91900   1.000 108.26000 ? 660 ASP B C      1 
ATOM   9635  O  O      . ASP B 1 669 ? 19.17700  -11.09000 4.05700   1.000 127.49000 ? 660 ASP B O      1 
ATOM   9636  C  CB     . ASP B 1 669 ? 17.20800  -13.26800 5.71800   1.000 98.38000  ? 660 ASP B CB     1 
ATOM   9637  C  CG     . ASP B 1 669 ? 17.28900  -13.84600 4.31300   1.000 109.83000 ? 660 ASP B CG     1 
ATOM   9638  O  OD1    . ASP B 1 669 ? 18.29400  -14.52100 3.99000   1.000 117.23000 ? 660 ASP B OD1    1 
ATOM   9639  O  OD2    . ASP B 1 669 ? 16.34100  -13.62700 3.53000   1.000 105.99000 ? 660 ASP B OD2    1 
ATOM   9640  N  N      . ASN B 1 670 ? 17.30600  -10.23500 4.96800   1.000 97.25000  ? 661 ASN B N      1 
ATOM   9641  C  CA     . ASN B 1 670 ? 17.22900  -9.22000  3.92400   1.000 88.06000  ? 661 ASN B CA     1 
ATOM   9642  C  C      . ASN B 1 670 ? 18.27000  -8.09900  4.08000   1.000 100.31000 ? 661 ASN B C      1 
ATOM   9643  O  O      . ASN B 1 670 ? 18.68300  -7.47800  3.09500   1.000 115.92000 ? 661 ASN B O      1 
ATOM   9644  C  CB     . ASN B 1 670 ? 15.84300  -8.57400  3.91800   1.000 89.04000  ? 661 ASN B CB     1 
ATOM   9645  C  CG     . ASN B 1 670 ? 14.76600  -9.51300  3.38900   1.000 102.42000 ? 661 ASN B CG     1 
ATOM   9646  O  OD1    . ASN B 1 670 ? 14.66000  -9.73800  2.18100   1.000 97.74000  ? 661 ASN B OD1    1 
ATOM   9647  N  ND2    . ASN B 1 670 ? 13.97500  -10.08000 4.29400   1.000 122.20000 ? 661 ASN B ND2    1 
ATOM   9648  N  N      . ALA B 1 671 ? 18.75100  -7.87200  5.30600   1.000 92.27000  ? 662 ALA B N      1 
ATOM   9649  C  CA     . ALA B 1 671 ? 19.82600  -6.90400  5.49900   1.000 83.05000  ? 662 ALA B CA     1 
ATOM   9650  C  C      . ALA B 1 671 ? 21.06400  -7.51000  4.85200   1.000 96.72000  ? 662 ALA B C      1 
ATOM   9651  O  O      . ALA B 1 671 ? 21.83400  -6.80800  4.17900   1.000 119.06000 ? 662 ALA B O      1 
ATOM   9652  C  CB     . ALA B 1 671 ? 20.10100  -6.53400  6.95600   1.000 80.01000  ? 662 ALA B CB     1 
ATOM   9653  N  N      . LYS B 1 672 ? 21.28200  -8.81200  5.05300   1.000 93.64000  ? 663 LYS B N      1 
ATOM   9654  C  CA     . LYS B 1 672 ? 22.37300  -9.46700  4.34800   1.000 97.02000  ? 663 LYS B CA     1 
ATOM   9655  C  C      . LYS B 1 672 ? 22.17100  -9.37200  2.84400   1.000 108.38000 ? 663 LYS B C      1 
ATOM   9656  O  O      . LYS B 1 672 ? 23.13600  -9.19600  2.09400   1.000 116.74000 ? 663 LYS B O      1 
ATOM   9657  C  CB     . LYS B 1 672 ? 22.50600  -10.92200 4.79100   1.000 101.83000 ? 663 LYS B CB     1 
ATOM   9658  C  CG     . LYS B 1 672 ? 23.90700  -11.47300 4.55800   1.000 113.57000 ? 663 LYS B CG     1 
ATOM   9659  C  CD     . LYS B 1 672 ? 24.01100  -12.95300 4.88300   1.000 99.54000  ? 663 LYS B CD     1 
ATOM   9660  C  CE     . LYS B 1 672 ? 23.18100  -13.77300 3.91800   1.000 88.66000  ? 663 LYS B CE     1 
ATOM   9661  N  NZ     . LYS B 1 672 ? 23.34500  -15.23900 4.11900   1.000 96.07000  ? 663 LYS B NZ     1 
ATOM   9662  N  N      . LYS B 1 673 ? 20.92500  -9.49700  2.37900   1.000 105.87000 ? 664 LYS B N      1 
ATOM   9663  C  CA     . LYS B 1 673 ? 20.66700  -9.31200  0.95300   1.000 100.91000 ? 664 LYS B CA     1 
ATOM   9664  C  C      . LYS B 1 673 ? 21.02000  -7.89900  0.51100   1.000 97.35000  ? 664 LYS B C      1 
ATOM   9665  O  O      . LYS B 1 673 ? 21.60500  -7.70100  -0.56100  1.000 105.52000 ? 664 LYS B O      1 
ATOM   9666  C  CB     . LYS B 1 673 ? 19.20600  -9.60300  0.62500   1.000 105.88000 ? 664 LYS B CB     1 
ATOM   9667  C  CG     . LYS B 1 673 ? 18.82200  -9.13200  -0.76800  1.000 119.94000 ? 664 LYS B CG     1 
ATOM   9668  C  CD     . LYS B 1 673 ? 17.33000  -9.20700  -0.99400  1.000 128.87000 ? 664 LYS B CD     1 
ATOM   9669  C  CE     . LYS B 1 673 ? 16.94400  -8.56900  -2.31900  1.000 115.02000 ? 664 LYS B CE     1 
ATOM   9670  N  NZ     . LYS B 1 673 ? 17.38600  -7.14700  -2.41300  1.000 106.90000 ? 664 LYS B NZ     1 
ATOM   9671  N  N      . TYR B 1 674 ? 20.68200  -6.90500  1.33200   1.000 98.87000  ? 665 TYR B N      1 
ATOM   9672  C  CA     . TYR B 1 674 ? 21.01200  -5.52500  0.99400   1.000 96.91000  ? 665 TYR B CA     1 
ATOM   9673  C  C      . TYR B 1 674 ? 22.51500  -5.35500  0.83200   1.000 97.86000  ? 665 TYR B C      1 
ATOM   9674  O  O      . TYR B 1 674 ? 22.98000  -4.71700  -0.12100  1.000 97.99000  ? 665 TYR B O      1 
ATOM   9675  C  CB     . TYR B 1 674 ? 20.46900  -4.57700  2.06600   1.000 103.75000 ? 665 TYR B CB     1 
ATOM   9676  C  CG     . TYR B 1 674 ? 20.25400  -3.15500  1.58900   1.000 118.85000 ? 665 TYR B CG     1 
ATOM   9677  C  CD1    . TYR B 1 674 ? 19.55400  -2.88800  0.41800   1.000 135.15000 ? 665 TYR B CD1    1 
ATOM   9678  C  CD2    . TYR B 1 674 ? 20.74800  -2.07700  2.31600   1.000 119.51000 ? 665 TYR B CD2    1 
ATOM   9679  C  CE1    . TYR B 1 674 ? 19.35400  -1.58400  -0.01600  1.000 145.97000 ? 665 TYR B CE1    1 
ATOM   9680  C  CE2    . TYR B 1 674 ? 20.55900  -0.77700  1.88800   1.000 136.99000 ? 665 TYR B CE2    1 
ATOM   9681  C  CZ     . TYR B 1 674 ? 19.86000  -0.53700  0.72200   1.000 145.82000 ? 665 TYR B CZ     1 
ATOM   9682  O  OH     . TYR B 1 674 ? 19.66200  0.75600   0.29800   1.000 154.71000 ? 665 TYR B OH     1 
ATOM   9683  N  N      . LEU B 1 675 ? 23.29000  -5.93300  1.75000   1.000 103.87000 ? 666 LEU B N      1 
ATOM   9684  C  CA     . LEU B 1 675 ? 24.74500  -5.86700  1.63200   1.000 94.38000  ? 666 LEU B CA     1 
ATOM   9685  C  C      . LEU B 1 675 ? 25.23100  -6.63700  0.41300   1.000 93.67000  ? 666 LEU B C      1 
ATOM   9686  O  O      . LEU B 1 675 ? 26.18600  -6.22100  -0.25400  1.000 101.10000 ? 666 LEU B O      1 
ATOM   9687  C  CB     . LEU B 1 675 ? 25.41700  -6.39100  2.89900   1.000 97.95000  ? 666 LEU B CB     1 
ATOM   9688  C  CG     . LEU B 1 675 ? 26.94800  -6.30200  2.85800   1.000 94.09000  ? 666 LEU B CG     1 
ATOM   9689  C  CD1    . LEU B 1 675 ? 27.43300  -4.89800  2.47400   1.000 113.42000 ? 666 LEU B CD1    1 
ATOM   9690  C  CD2    . LEU B 1 675 ? 27.55700  -6.74000  4.17800   1.000 96.94000  ? 666 LEU B CD2    1 
ATOM   9691  N  N      . GLU B 1 676 ? 24.58000  -7.76200  0.10700   1.000 98.92000  ? 667 GLU B N      1 
ATOM   9692  C  CA     . GLU B 1 676 ? 24.95700  -8.55700  -1.05500  1.000 102.37000 ? 667 GLU B CA     1 
ATOM   9693  C  C      . GLU B 1 676 ? 24.85500  -7.73800  -2.32600  1.000 99.80000  ? 667 GLU B C      1 
ATOM   9694  O  O      . GLU B 1 676 ? 25.74700  -7.78900  -3.18000  1.000 116.23000 ? 667 GLU B O      1 
ATOM   9695  C  CB     . GLU B 1 676 ? 24.05100  -9.78700  -1.14800  1.000 108.67000 ? 667 GLU B CB     1 
ATOM   9696  C  CG     . GLU B 1 676 ? 23.96700  -10.44300 -2.51700  1.000 117.84000 ? 667 GLU B CG     1 
ATOM   9697  C  CD     . GLU B 1 676 ? 25.26100  -11.08700 -2.93100  1.000 126.51000 ? 667 GLU B CD     1 
ATOM   9698  O  OE1    . GLU B 1 676 ? 25.51900  -11.17700 -4.15100  1.000 127.51000 ? 667 GLU B OE1    1 
ATOM   9699  O  OE2    . GLU B 1 676 ? 26.02500  -11.49700 -2.02900  1.000 115.14000 ? 667 GLU B OE2    1 
ATOM   9700  N  N      . ALA B 1 677 ? 23.76800  -6.98400  -2.43400  1.000 88.72000  ? 668 ALA B N      1 
ATOM   9701  C  CA     . ALA B 1 677 ? 23.62000  -6.09900  -3.60300  1.000 86.96000  ? 668 ALA B CA     1 
ATOM   9702  C  C      . ALA B 1 677 ? 24.52300  -4.89600  -3.37900  1.000 99.99000  ? 668 ALA B C      1 
ATOM   9703  O  O      . ALA B 1 677 ? 24.92400  -4.24300  -4.35700  1.000 122.18000 ? 668 ALA B O      1 
ATOM   9704  C  CB     . ALA B 1 677 ? 22.18500  -5.67700  -3.74500  1.000 87.02000  ? 668 ALA B CB     1 
ATOM   9705  N  N      . GLY B 1 678 ? 24.83100  -4.61500  -2.11500  1.000 95.87000  ? 669 GLY B N      1 
ATOM   9706  C  CA     . GLY B 1 678 ? 25.62800  -3.41400  -1.81100  1.000 114.79000 ? 669 GLY B CA     1 
ATOM   9707  C  C      . GLY B 1 678 ? 24.79900  -2.20400  -2.17700  1.000 119.10000 ? 669 GLY B C      1 
ATOM   9708  O  O      . GLY B 1 678 ? 25.38700  -1.13100  -2.40400  1.000 135.45000 ? 669 GLY B O      1 
ATOM   9709  N  N      . ASN B 1 679 ? 23.47600  -2.36500  -2.22100  1.000 107.44000 ? 670 ASN B N      1 
ATOM   9710  C  CA     . ASN B 1 679 ? 22.60400  -1.24000  -2.64800  1.000 119.98000 ? 670 ASN B CA     1 
ATOM   9711  C  C      . ASN B 1 679 ? 23.11000  0.02100   -1.95700  1.000 118.99000 ? 670 ASN B C      1 
ATOM   9712  O  O      . ASN B 1 679 ? 23.27500  1.04500   -2.64100  1.000 147.82000 ? 670 ASN B O      1 
ATOM   9713  C  CB     . ASN B 1 679 ? 21.12600  -1.52400  -2.42100  1.000 123.98000 ? 670 ASN B CB     1 
ATOM   9714  C  CG     . ASN B 1 679 ? 20.24900  -0.44100  -3.00100  1.000 143.62000 ? 670 ASN B CG     1 
ATOM   9715  O  OD1    . ASN B 1 679 ? 20.71900  0.67800   -3.23900  1.000 166.78000 ? 670 ASN B OD1    1 
ATOM   9716  N  ND2    . ASN B 1 679 ? 18.98100  -0.74400  -3.23300  1.000 130.43000 ? 670 ASN B ND2    1 
ATOM   9717  N  N      . LEU B 1 680 ? 23.31800  -0.06700  -0.64900  1.000 104.37000 ? 671 LEU B N      1 
ATOM   9718  C  CA     . LEU B 1 680 ? 23.97100  1.04200   0.07600   1.000 124.10000 ? 671 LEU B CA     1 
ATOM   9719  C  C      . LEU B 1 680 ? 25.10200  0.35000   0.83500   1.000 139.37000 ? 671 LEU B C      1 
ATOM   9720  O  O      . LEU B 1 680 ? 25.21900  -0.88300  0.69100   1.000 145.35000 ? 671 LEU B O      1 
ATOM   9721  C  CB     . LEU B 1 680 ? 22.97700  1.75100   0.99200   1.000 109.80000 ? 671 LEU B CB     1 
ATOM   9722  C  CG     . LEU B 1 680 ? 23.54300  2.84300   1.90500   1.000 89.76000  ? 671 LEU B CG     1 
ATOM   9723  C  CD1    . LEU B 1 680 ? 24.12600  4.00000   1.11600   1.000 73.22000  ? 671 LEU B CD1    1 
ATOM   9724  C  CD2    . LEU B 1 680 ? 22.50200  3.33500   2.89300   1.000 101.68000 ? 671 LEU B CD2    1 
ATOM   9725  N  N      . GLU B 1 681 ? 25.91800  1.10200   1.56600   1.000 134.56000 ? 672 GLU B N      1 
ATOM   9726  C  CA     . GLU B 1 681 ? 27.07600  0.48100   2.25100   1.000 136.00000 ? 672 GLU B CA     1 
ATOM   9727  C  C      . GLU B 1 681 ? 27.90600  -0.21400  1.16000   1.000 144.55000 ? 672 GLU B C      1 
ATOM   9728  O  O      . GLU B 1 681 ? 28.90500  0.40000   0.72200   1.000 146.29000 ? 672 GLU B O      1 
ATOM   9729  C  CB     . GLU B 1 681 ? 26.65500  -0.48400  3.35500   1.000 134.33000 ? 672 GLU B CB     1 
ATOM   9730  C  CG     . GLU B 1 681 ? 25.85100  0.19000   4.46100   1.000 133.93000 ? 672 GLU B CG     1 
ATOM   9731  C  CD     . GLU B 1 681 ? 26.72100  0.86200   5.50500   1.000 124.39000 ? 672 GLU B CD     1 
ATOM   9732  O  OE1    . GLU B 1 681 ? 26.63600  2.09800   5.66000   1.000 115.90000 ? 672 GLU B OE1    1 
ATOM   9733  O  OE2    . GLU B 1 681 ? 27.47800  0.13400   6.17600   1.000 116.41000 ? 672 GLU B OE2    1 
ATOM   9734  N  N      . LYS B 1 685 ? 30.76700  -7.25800  -0.61300  1.000 67.00000  ? 676 LYS B N      1 
ATOM   9735  C  CA     . LYS B 1 685 ? 30.55400  -8.71800  -0.46000  1.000 86.06000  ? 676 LYS B CA     1 
ATOM   9736  C  C      . LYS B 1 685 ? 31.82200  -9.36000  0.11400   1.000 112.00000 ? 676 LYS B C      1 
ATOM   9737  O  O      . LYS B 1 685 ? 32.91300  -8.83300  -0.16100  1.000 147.35000 ? 676 LYS B O      1 
ATOM   9738  C  CB     . LYS B 1 685 ? 30.20900  -9.33800  -1.81500  1.000 92.75000  ? 676 LYS B CB     1 
ATOM   9739  C  CG     . LYS B 1 685 ? 28.84200  -8.98200  -2.37800  1.000 95.23000  ? 676 LYS B CG     1 
ATOM   9740  C  CD     . LYS B 1 685 ? 28.68200  -9.41400  -3.83100  1.000 97.23000  ? 676 LYS B CD     1 
ATOM   9741  C  CE     . LYS B 1 685 ? 29.14500  -10.81500 -4.07700  1.000 105.01000 ? 676 LYS B CE     1 
ATOM   9742  N  NZ     . LYS B 1 685 ? 28.36100  -11.80500 -3.33400  1.000 103.70000 ? 676 LYS B NZ     1 
ATOM   9743  N  N      . GLY B 1 686 ? 31.68300  -10.43300 0.89700   1.000 110.65000 ? 677 GLY B N      1 
ATOM   9744  C  CA     . GLY B 1 686 ? 32.84800  -11.15200 1.45400   1.000 102.15000 ? 677 GLY B CA     1 
ATOM   9745  C  C      . GLY B 1 686 ? 33.66000  -10.29600 2.40400   1.000 110.34000 ? 677 GLY B C      1 
ATOM   9746  O  O      . GLY B 1 686 ? 34.82000  -10.66500 2.67100   1.000 106.97000 ? 677 GLY B O      1 
ATOM   9747  N  N      . SER B 1 687 ? 33.07700  -9.21700  2.92900   1.000 115.47000 ? 678 SER B N      1 
ATOM   9748  C  CA     . SER B 1 687 ? 33.82800  -8.27300  3.79600   1.000 118.58000 ? 678 SER B CA     1 
ATOM   9749  C  C      . SER B 1 687 ? 33.74600  -8.70200  5.26100   1.000 117.31000 ? 678 SER B C      1 
ATOM   9750  O  O      . SER B 1 687 ? 33.41400  -9.87500  5.52200   1.000 131.85000 ? 678 SER B O      1 
ATOM   9751  C  CB     . SER B 1 687 ? 33.28800  -6.88300  3.64100   1.000 109.05000 ? 678 SER B CB     1 
ATOM   9752  O  OG     . SER B 1 687 ? 34.06100  -5.95400  4.38700   1.000 141.80000 ? 678 SER B OG     1 
ATOM   9753  N  N      . GLU B 1 688 ? 34.06800  -7.78700  6.17400   1.000 114.42000 ? 679 GLU B N      1 
ATOM   9754  C  CA     . GLU B 1 688 ? 33.89900  -8.09400  7.61700   1.000 129.67000 ? 679 GLU B CA     1 
ATOM   9755  C  C      . GLU B 1 688 ? 32.42300  -7.84200  7.96300   1.000 130.74000 ? 679 GLU B C      1 
ATOM   9756  O  O      . GLU B 1 688 ? 31.77600  -8.77600  8.47000   1.000 137.79000 ? 679 GLU B O      1 
ATOM   9757  C  CB     . GLU B 1 688 ? 34.88800  -7.30600  8.47700   1.000 135.53000 ? 679 GLU B CB     1 
ATOM   9758  C  CG     . GLU B 1 688 ? 34.56400  -7.36100  9.96700   1.000 135.06000 ? 679 GLU B CG     1 
ATOM   9759  C  CD     . GLU B 1 688 ? 35.74800  -7.71800  10.84700  1.000 137.26000 ? 679 GLU B CD     1 
ATOM   9760  O  OE1    . GLU B 1 688 ? 36.84000  -7.96800  10.29600  1.000 117.63000 ? 679 GLU B OE1    1 
ATOM   9761  O  OE2    . GLU B 1 688 ? 35.57700  -7.74200  12.08300  1.000 149.15000 ? 679 GLU B OE2    1 
ATOM   9762  N  N      . PRO B 1 689 ? 31.84500  -6.64400  7.72800   1.000 112.51000 ? 680 PRO B N      1 
ATOM   9763  C  CA     . PRO B 1 689 ? 30.40200  -6.45000  7.93900   1.000 111.91000 ? 680 PRO B CA     1 
ATOM   9764  C  C      . PRO B 1 689 ? 29.57400  -7.60300  7.40000   1.000 124.09000 ? 680 PRO B C      1 
ATOM   9765  O  O      . PRO B 1 689 ? 28.61800  -8.04400  8.05700   1.000 134.27000 ? 680 PRO B O      1 
ATOM   9766  C  CB     . PRO B 1 689 ? 30.12300  -5.14100  7.19300   1.000 100.64000 ? 680 PRO B CB     1 
ATOM   9767  C  CG     . PRO B 1 689 ? 31.39400  -4.36900  7.34700   1.000 115.93000 ? 680 PRO B CG     1 
ATOM   9768  C  CD     . PRO B 1 689 ? 32.51400  -5.39800  7.31000   1.000 115.33000 ? 680 PRO B CD     1 
ATOM   9769  N  N      . HIS B 1 690 ? 29.91100  -8.09600  6.20600   1.000 115.63000 ? 681 HIS B N      1 
ATOM   9770  C  CA     . HIS B 1 690 ? 29.19400  -9.24000  5.65300   1.000 105.27000 ? 681 HIS B CA     1 
ATOM   9771  C  C      . HIS B 1 690 ? 29.37000  -10.47500 6.52900   1.000 104.13000 ? 681 HIS B C      1 
ATOM   9772  O  O      . HIS B 1 690 ? 28.45300  -11.29300 6.64600   1.000 113.33000 ? 681 HIS B O      1 
ATOM   9773  C  CB     . HIS B 1 690 ? 29.65700  -9.51700  4.22300   1.000 105.74000 ? 681 HIS B CB     1 
ATOM   9774  C  CG     . HIS B 1 690 ? 28.92000  -10.63900 3.55800   1.000 101.31000 ? 681 HIS B CG     1 
ATOM   9775  N  ND1    . HIS B 1 690 ? 27.60800  -10.53000 3.14800   1.000 114.69000 ? 681 HIS B ND1    1 
ATOM   9776  C  CD2    . HIS B 1 690 ? 29.31200  -11.89400 3.23500   1.000 101.16000 ? 681 HIS B CD2    1 
ATOM   9777  C  CE1    . HIS B 1 690 ? 27.22400  -11.67000 2.60100   1.000 114.72000 ? 681 HIS B CE1    1 
ATOM   9778  N  NE2    . HIS B 1 690 ? 28.23900  -12.51400 2.64100   1.000 108.55000 ? 681 HIS B NE2    1 
ATOM   9779  N  N      . LYS B 1 691 ? 30.54500  -10.64000 7.13800   1.000 109.05000 ? 682 LYS B N      1 
ATOM   9780  C  CA     . LYS B 1 691 ? 30.73800  -11.77300 8.03900   1.000 115.97000 ? 682 LYS B CA     1 
ATOM   9781  C  C      . LYS B 1 691 ? 29.81500  -11.67000 9.24800   1.000 125.47000 ? 682 LYS B C      1 
ATOM   9782  O  O      . LYS B 1 691 ? 29.18800  -12.66000 9.65300   1.000 134.00000 ? 682 LYS B O      1 
ATOM   9783  C  CB     . LYS B 1 691 ? 32.20100  -11.85600 8.47600   1.000 105.39000 ? 682 LYS B CB     1 
ATOM   9784  N  N      . ALA B 1 692 ? 29.72500  -10.47700 9.84200   1.000 116.72000 ? 683 ALA B N      1 
ATOM   9785  C  CA     . ALA B 1 692 ? 28.79000  -10.29000 10.94600  1.000 107.76000 ? 683 ALA B CA     1 
ATOM   9786  C  C      . ALA B 1 692 ? 27.36900  -10.62000 10.51200  1.000 120.85000 ? 683 ALA B C      1 
ATOM   9787  O  O      . ALA B 1 692 ? 26.63100  -11.31000 11.23000  1.000 144.29000 ? 683 ALA B O      1 
ATOM   9788  C  CB     . ALA B 1 692 ? 28.87300  -8.85800  11.47300  1.000 81.75000  ? 683 ALA B CB     1 
ATOM   9789  N  N      . LEU B 1 693 ? 26.96900  -10.13300 9.33700   1.000 115.29000 ? 684 LEU B N      1 
ATOM   9790  C  CA     . LEU B 1 693 ? 25.61000  -10.37300 8.85900   1.000 109.89000 ? 684 LEU B CA     1 
ATOM   9791  C  C      . LEU B 1 693 ? 25.35700  -11.86200 8.62000   1.000 106.94000 ? 684 LEU B C      1 
ATOM   9792  O  O      . LEU B 1 693 ? 24.26900  -12.37100 8.91500   1.000 104.05000 ? 684 LEU B O      1 
ATOM   9793  C  CB     . LEU B 1 693 ? 25.35200  -9.55300  7.59400   1.000 103.62000 ? 684 LEU B CB     1 
ATOM   9794  C  CG     . LEU B 1 693 ? 25.25100  -8.03100  7.78500   1.000 109.87000 ? 684 LEU B CG     1 
ATOM   9795  C  CD1    . LEU B 1 693 ? 24.57200  -7.35400  6.59700   1.000 108.57000 ? 684 LEU B CD1    1 
ATOM   9796  C  CD2    . LEU B 1 693 ? 24.53000  -7.67600  9.08000   1.000 110.19000 ? 684 LEU B CD2    1 
ATOM   9797  N  N      . VAL B 1 694 ? 26.34300  -12.57600 8.07500   1.000 108.87000 ? 685 VAL B N      1 
ATOM   9798  C  CA     . VAL B 1 694 ? 26.14600  -13.99500 7.80100   1.000 104.95000 ? 685 VAL B CA     1 
ATOM   9799  C  C      . VAL B 1 694 ? 26.05000  -14.78200 9.10100   1.000 106.71000 ? 685 VAL B C      1 
ATOM   9800  O  O      . VAL B 1 694 ? 25.27400  -15.73900 9.20500   1.000 111.51000 ? 685 VAL B O      1 
ATOM   9801  C  CB     . VAL B 1 694 ? 27.25800  -14.53500 6.87900   1.000 101.01000 ? 685 VAL B CB     1 
ATOM   9802  C  CG1    . VAL B 1 694 ? 27.26100  -13.77600 5.55700   1.000 108.53000 ? 685 VAL B CG1    1 
ATOM   9803  C  CG2    . VAL B 1 694 ? 28.62500  -14.45300 7.55300   1.000 100.49000 ? 685 VAL B CG2    1 
ATOM   9804  N  N      . ILE B 1 695 ? 26.82200  -14.39700 10.11900  1.000 102.44000 ? 686 ILE B N      1 
ATOM   9805  C  CA     . ILE B 1 695 ? 26.69200  -15.07400 11.40700  1.000 98.56000  ? 686 ILE B CA     1 
ATOM   9806  C  C      . ILE B 1 695 ? 25.31400  -14.80400 12.00700  1.000 101.85000 ? 686 ILE B C      1 
ATOM   9807  O  O      . ILE B 1 695 ? 24.64700  -15.71600 12.52700  1.000 109.02000 ? 686 ILE B O      1 
ATOM   9808  C  CB     . ILE B 1 695 ? 27.83000  -14.64800 12.35200  1.000 91.47000  ? 686 ILE B CB     1 
ATOM   9809  C  CG1    . ILE B 1 695 ? 29.16800  -15.23600 11.89000  1.000 101.77000 ? 686 ILE B CG1    1 
ATOM   9810  C  CG2    . ILE B 1 695 ? 27.54000  -15.07900 13.77900  1.000 90.12000  ? 686 ILE B CG2    1 
ATOM   9811  C  CD1    . ILE B 1 695 ? 29.08700  -16.66900 11.40100  1.000 117.18000 ? 686 ILE B CD1    1 
ATOM   9812  N  N      . GLY B 1 696 ? 24.85200  -13.55400 11.91600  1.000 103.88000 ? 687 GLY B N      1 
ATOM   9813  C  CA     . GLY B 1 696 ? 23.52900  -13.23900 12.41900  1.000 86.94000  ? 687 GLY B CA     1 
ATOM   9814  C  C      . GLY B 1 696 ? 22.43300  -13.98000 11.68300  1.000 90.45000  ? 687 GLY B C      1 
ATOM   9815  O  O      . GLY B 1 696 ? 21.43300  -14.36600 12.28600  1.000 86.11000  ? 687 GLY B O      1 
ATOM   9816  N  N      . ASP B 1 697 ? 22.62700  -14.23700 10.38400  1.000 104.42000 ? 688 ASP B N      1 
ATOM   9817  C  CA     . ASP B 1 697 ? 21.65300  -15.02600 9.63200   1.000 96.11000  ? 688 ASP B CA     1 
ATOM   9818  C  C      . ASP B 1 697 ? 21.70700  -16.49700 10.02000  1.000 91.38000  ? 688 ASP B C      1 
ATOM   9819  O  O      . ASP B 1 697 ? 20.66600  -17.15500 10.11100  1.000 101.47000 ? 688 ASP B O      1 
ATOM   9820  C  CB     . ASP B 1 697 ? 21.87500  -14.86700 8.12600   1.000 111.84000 ? 688 ASP B CB     1 
ATOM   9821  C  CG     . ASP B 1 697 ? 20.59100  -14.52800 7.37600   1.000 111.61000 ? 688 ASP B CG     1 
ATOM   9822  O  OD1    . ASP B 1 697 ? 19.50100  -14.67700 7.96500   1.000 111.04000 ? 688 ASP B OD1    1 
ATOM   9823  O  OD2    . ASP B 1 697 ? 20.66800  -14.11600 6.19700   1.000 118.32000 ? 688 ASP B OD2    1 
ATOM   9824  N  N      . THR B 1 698 ? 22.90900  -17.03600 10.24200  1.000 97.53000  ? 689 THR B N      1 
ATOM   9825  C  CA     . THR B 1 698 ? 23.00800  -18.41200 10.72000  1.000 85.14000  ? 689 THR B CA     1 
ATOM   9826  C  C      . THR B 1 698 ? 22.28400  -18.58500 12.04500  1.000 80.08000  ? 689 THR B C      1 
ATOM   9827  O  O      . THR B 1 698 ? 21.74100  -19.66300 12.32200  1.000 74.29000  ? 689 THR B O      1 
ATOM   9828  C  CB     . THR B 1 698 ? 24.47200  -18.83000 10.86700  1.000 84.59000  ? 689 THR B CB     1 
ATOM   9829  O  OG1    . THR B 1 698 ? 25.05700  -19.00900 9.57100   1.000 95.17000  ? 689 THR B OG1    1 
ATOM   9830  C  CG2    . THR B 1 698 ? 24.58000  -20.12600 11.65700  1.000 92.65000  ? 689 THR B CG2    1 
ATOM   9831  N  N      . VAL B 1 699 ? 22.27800  -17.54200 12.87800  1.000 91.40000  ? 690 VAL B N      1 
ATOM   9832  C  CA     . VAL B 1 699 ? 21.50100  -17.58900 14.11400  1.000 75.76000  ? 690 VAL B CA     1 
ATOM   9833  C  C      . VAL B 1 699 ? 20.00900  -17.39100 13.84600  1.000 66.89000  ? 690 VAL B C      1 
ATOM   9834  O  O      . VAL B 1 699 ? 19.16800  -18.06500 14.45100  1.000 69.98000  ? 690 VAL B O      1 
ATOM   9835  C  CB     . VAL B 1 699 ? 22.02800  -16.55200 15.12000  1.000 68.27000  ? 690 VAL B CB     1 
ATOM   9836  C  CG1    . VAL B 1 699 ? 21.20100  -16.61300 16.39500  1.000 72.26000  ? 690 VAL B CG1    1 
ATOM   9837  C  CG2    . VAL B 1 699 ? 23.49000  -16.82300 15.42400  1.000 77.64000  ? 690 VAL B CG2    1 
ATOM   9838  N  N      . GLY B 1 700 ? 19.66200  -16.47700 12.93500  1.000 73.55000  ? 691 GLY B N      1 
ATOM   9839  C  CA     . GLY B 1 700 ? 18.26500  -16.12400 12.72700  1.000 78.21000  ? 691 GLY B CA     1 
ATOM   9840  C  C      . GLY B 1 700 ? 17.44000  -17.19000 12.02700  1.000 80.07000  ? 691 GLY B C      1 
ATOM   9841  O  O      . GLY B 1 700 ? 16.25400  -17.35500 12.32800  1.000 85.32000  ? 691 GLY B O      1 
ATOM   9842  N  N      . ASP B 1 701 ? 18.04400  -17.92500 11.08800  1.000 78.60000  ? 692 ASP B N      1 
ATOM   9843  C  CA     . ASP B 1 701 ? 17.30000  -18.92400 10.31900  1.000 73.25000  ? 692 ASP B CA     1 
ATOM   9844  C  C      . ASP B 1 701 ? 16.57300  -19.89600 11.24600  1.000 80.80000  ? 692 ASP B C      1 
ATOM   9845  O  O      . ASP B 1 701 ? 15.34400  -20.03000 11.15900  1.000 86.64000  ? 692 ASP B O      1 
ATOM   9846  C  CB     . ASP B 1 701 ? 18.21200  -19.68700 9.35700   1.000 88.66000  ? 692 ASP B CB     1 
ATOM   9847  C  CG     . ASP B 1 701 ? 18.67800  -18.83200 8.19500   1.000 122.74000 ? 692 ASP B CG     1 
ATOM   9848  O  OD1    . ASP B 1 701 ? 18.08400  -17.75300 7.97100   1.000 117.20000 ? 692 ASP B OD1    1 
ATOM   9849  O  OD2    . ASP B 1 701 ? 19.62200  -19.25400 7.49200   1.000 140.36000 ? 692 ASP B OD2    1 
ATOM   9850  N  N      . PRO B 1 702 ? 17.28100  -20.61500 12.12000  1.000 74.42000  ? 693 PRO B N      1 
ATOM   9851  C  CA     . PRO B 1 702 ? 16.57100  -21.54300 13.01800  1.000 69.85000  ? 693 PRO B CA     1 
ATOM   9852  C  C      . PRO B 1 702 ? 15.56700  -20.84200 13.92100  1.000 78.64000  ? 693 PRO B C      1 
ATOM   9853  O  O      . PRO B 1 702 ? 14.55000  -21.44500 14.29500  1.000 85.50000  ? 693 PRO B O      1 
ATOM   9854  C  CB     . PRO B 1 702 ? 17.71000  -22.19600 13.81900  1.000 50.41000  ? 693 PRO B CB     1 
ATOM   9855  C  CG     . PRO B 1 702 ? 18.83900  -21.21400 13.73700  1.000 76.42000  ? 693 PRO B CG     1 
ATOM   9856  C  CD     . PRO B 1 702 ? 18.73600  -20.62200 12.35500  1.000 93.59000  ? 693 PRO B CD     1 
ATOM   9857  N  N      . LEU B 1 703 ? 15.81900  -19.57400 14.26700  1.000 68.86000  ? 694 LEU B N      1 
ATOM   9858  C  CA     . LEU B 1 703 ? 14.93600  -18.85000 15.17600  1.000 68.17000  ? 694 LEU B CA     1 
ATOM   9859  C  C      . LEU B 1 703 ? 13.63300  -18.45000 14.49400  1.000 71.33000  ? 694 LEU B C      1 
ATOM   9860  O  O      . LEU B 1 703 ? 12.55600  -18.56300 15.09200  1.000 72.14000  ? 694 LEU B O      1 
ATOM   9861  C  CB     . LEU B 1 703 ? 15.65200  -17.61300 15.71500  1.000 62.20000  ? 694 LEU B CB     1 
ATOM   9862  C  CG     . LEU B 1 703 ? 16.33000  -17.76900 17.07700  1.000 63.74000  ? 694 LEU B CG     1 
ATOM   9863  C  CD1    . LEU B 1 703 ? 16.90400  -16.43800 17.54400  1.000 63.74000  ? 694 LEU B CD1    1 
ATOM   9864  C  CD2    . LEU B 1 703 ? 15.37100  -18.34700 18.10800  1.000 70.23000  ? 694 LEU B CD2    1 
ATOM   9865  N  N      . LYS B 1 704 ? 13.70800  -17.97500 13.24700  1.000 66.68000  ? 695 LYS B N      1 
ATOM   9866  C  CA     . LYS B 1 704 ? 12.53400  -17.49500 12.52500  1.000 65.12000  ? 695 LYS B CA     1 
ATOM   9867  C  C      . LYS B 1 704 ? 11.80600  -18.59000 11.76100  1.000 79.01000  ? 695 LYS B C      1 
ATOM   9868  O  O      . LYS B 1 704 ? 10.61200  -18.43800 11.47500  1.000 83.02000  ? 695 LYS B O      1 
ATOM   9869  C  CB     . LYS B 1 704 ? 12.91800  -16.39000 11.53800  1.000 70.62000  ? 695 LYS B CB     1 
ATOM   9870  C  CG     . LYS B 1 704 ? 13.64000  -16.88600 10.28800  1.000 91.30000  ? 695 LYS B CG     1 
ATOM   9871  C  CD     . LYS B 1 704 ? 13.40300  -15.96200 9.10200   1.000 90.42000  ? 695 LYS B CD     1 
ATOM   9872  C  CE     . LYS B 1 704 ? 14.28500  -16.31900 7.91200   1.000 73.38000  ? 695 LYS B CE     1 
ATOM   9873  N  NZ     . LYS B 1 704 ? 15.73500  -16.30000 8.25200   1.000 80.63000  ? 695 LYS B NZ     1 
ATOM   9874  N  N      . ASP B 1 705 ? 12.49300  -19.67100 11.39800  1.000 80.66000  ? 696 ASP B N      1 
ATOM   9875  C  CA     . ASP B 1 705 ? 11.90000  -20.72500 10.58900  1.000 82.59000  ? 696 ASP B CA     1 
ATOM   9876  C  C      . ASP B 1 705 ? 11.53100  -21.96500 11.38800  1.000 69.13000  ? 696 ASP B C      1 
ATOM   9877  O  O      . ASP B 1 705 ? 10.84800  -22.84200 10.85000  1.000 66.01000  ? 696 ASP B O      1 
ATOM   9878  C  CB     . ASP B 1 705 ? 12.85300  -21.12900 9.45500   1.000 98.04000  ? 696 ASP B CB     1 
ATOM   9879  C  CG     . ASP B 1 705 ? 12.98700  -20.05400 8.39000   1.000 103.33000 ? 696 ASP B CG     1 
ATOM   9880  O  OD1    . ASP B 1 705 ? 11.96200  -19.43500 8.03000   1.000 114.35000 ? 696 ASP B OD1    1 
ATOM   9881  O  OD2    . ASP B 1 705 ? 14.11800  -19.82900 7.90700   1.000 106.53000 ? 696 ASP B OD2    1 
ATOM   9882  N  N      . THR B 1 706 ? 11.95300  -22.06000 12.64800  1.000 64.89000  ? 697 THR B N      1 
ATOM   9883  C  CA     . THR B 1 706 ? 11.60500  -23.21200 13.46800  1.000 63.31000  ? 697 THR B CA     1 
ATOM   9884  C  C      . THR B 1 706 ? 10.93300  -22.77800 14.76700  1.000 76.12000  ? 697 THR B C      1 
ATOM   9885  O  O      . THR B 1 706 ? 9.78700   -23.15700 15.02500  1.000 71.81000  ? 697 THR B O      1 
ATOM   9886  C  CB     . THR B 1 706 ? 12.84900  -24.05600 13.75700  1.000 69.98000  ? 697 THR B CB     1 
ATOM   9887  O  OG1    . THR B 1 706 ? 13.64000  -24.15500 12.56700  1.000 80.96000  ? 697 THR B OG1    1 
ATOM   9888  C  CG2    . THR B 1 706 ? 12.45700  -25.45500 14.20800  1.000 79.47000  ? 697 THR B CG2    1 
ATOM   9889  N  N      . VAL B 1 707 ? 11.62000  -21.96500 15.57500  1.000 71.63000  ? 698 VAL B N      1 
ATOM   9890  C  CA     . VAL B 1 707 ? 11.10700  -21.61300 16.90000  1.000 64.92000  ? 698 VAL B CA     1 
ATOM   9891  C  C      . VAL B 1 707 ? 9.80300   -20.82700 16.78200  1.000 74.83000  ? 698 VAL B C      1 
ATOM   9892  O  O      . VAL B 1 707 ? 8.77100   -21.19500 17.36600  1.000 78.29000  ? 698 VAL B O      1 
ATOM   9893  C  CB     . VAL B 1 707 ? 12.16900  -20.82600 17.68800  1.000 52.92000  ? 698 VAL B CB     1 
ATOM   9894  C  CG1    . VAL B 1 707 ? 11.57500  -20.27100 18.96600  1.000 58.03000  ? 698 VAL B CG1    1 
ATOM   9895  C  CG2    . VAL B 1 707 ? 13.39800  -21.69300 17.96700  1.000 73.85000  ? 698 VAL B CG2    1 
ATOM   9896  N  N      . GLY B 1 708 ? 9.82900   -19.74100 16.01100  1.000 69.56000  ? 699 GLY B N      1 
ATOM   9897  C  CA     . GLY B 1 708 ? 8.67700   -18.89200 15.82400  1.000 60.68000  ? 699 GLY B CA     1 
ATOM   9898  C  C      . GLY B 1 708 ? 7.49200   -19.67400 15.29800  1.000 71.34000  ? 699 GLY B C      1 
ATOM   9899  O  O      . GLY B 1 708 ? 6.41300   -19.69200 15.90100  1.000 83.55000  ? 699 GLY B O      1 
ATOM   9900  N  N      . PRO B 1 709 ? 7.67900   -20.34200 14.15700  1.000 62.56000  ? 700 PRO B N      1 
ATOM   9901  C  CA     . PRO B 1 709 ? 6.57700   -21.10700 13.55200  1.000 56.22000  ? 700 PRO B CA     1 
ATOM   9902  C  C      . PRO B 1 709 ? 6.07700   -22.23500 14.43200  1.000 59.80000  ? 700 PRO B C      1 
ATOM   9903  O  O      . PRO B 1 709 ? 4.96400   -22.72600 14.21500  1.000 71.16000  ? 700 PRO B O      1 
ATOM   9904  C  CB     . PRO B 1 709 ? 7.19500   -21.64000 12.25000  1.000 77.72000  ? 700 PRO B CB     1 
ATOM   9905  C  CG     . PRO B 1 709 ? 8.40800   -20.78500 12.02600  1.000 83.75000  ? 700 PRO B CG     1 
ATOM   9906  C  CD     . PRO B 1 709 ? 8.92400   -20.51200 13.39500  1.000 70.56000  ? 700 PRO B CD     1 
ATOM   9907  N  N      . SER B 1 710 ? 6.90100   -22.73100 15.35300  1.000 51.78000  ? 701 SER B N      1 
ATOM   9908  C  CA     . SER B 1 710 ? 6.44800   -23.75800 16.28200  1.000 49.04000  ? 701 SER B CA     1 
ATOM   9909  C  C      . SER B 1 710 ? 5.67400   -23.18900 17.46900  1.000 60.92000  ? 701 SER B C      1 
ATOM   9910  O  O      . SER B 1 710 ? 4.81000   -23.88000 18.02000  1.000 60.44000  ? 701 SER B O      1 
ATOM   9911  C  CB     . SER B 1 710 ? 7.64200   -24.57600 16.76700  1.000 54.56000  ? 701 SER B CB     1 
ATOM   9912  O  OG     . SER B 1 710 ? 8.10600   -25.40300 15.71600  1.000 73.45000  ? 701 SER B OG     1 
ATOM   9913  N  N      . LEU B 1 711 ? 5.94500   -21.93900 17.86400  1.000 62.76000  ? 702 LEU B N      1 
ATOM   9914  C  CA     . LEU B 1 711 ? 5.28900   -21.37900 19.05000  1.000 43.80000  ? 702 LEU B CA     1 
ATOM   9915  C  C      . LEU B 1 711 ? 3.78000   -21.19000 18.86700  1.000 49.86000  ? 702 LEU B C      1 
ATOM   9916  O  O      . LEU B 1 711 ? 2.99700   -21.46000 19.79100  1.000 64.04000  ? 702 LEU B O      1 
ATOM   9917  C  CB     . LEU B 1 711 ? 5.95500   -20.05500 19.41900  1.000 33.00000  ? 702 LEU B CB     1 
ATOM   9918  C  CG     . LEU B 1 711 ? 7.34500   -20.19400 20.04200  1.000 53.73000  ? 702 LEU B CG     1 
ATOM   9919  C  CD1    . LEU B 1 711 ? 8.11500   -18.89800 19.86200  1.000 72.20000  ? 702 LEU B CD1    1 
ATOM   9920  C  CD2    . LEU B 1 711 ? 7.26100   -20.57800 21.51500  1.000 59.49000  ? 702 LEU B CD2    1 
ATOM   9921  N  N      . ASP B 1 712 ? 3.34400   -20.70800 17.70400  1.000 44.93000  ? 703 ASP B N      1 
ATOM   9922  C  CA     . ASP B 1 712 ? 1.90600   -20.56500 17.48800  1.000 47.87000  ? 703 ASP B CA     1 
ATOM   9923  C  C      . ASP B 1 712 ? 1.21200   -21.91900 17.56500  1.000 51.94000  ? 703 ASP B C      1 
ATOM   9924  O  O      . ASP B 1 712 ? 0.12000   -22.04100 18.13700  1.000 72.45000  ? 703 ASP B O      1 
ATOM   9925  C  CB     . ASP B 1 712 ? 1.63200   -19.88500 16.14900  1.000 48.11000  ? 703 ASP B CB     1 
ATOM   9926  C  CG     . ASP B 1 712 ? 2.48800   -20.42400 15.04100  1.000 62.95000  ? 703 ASP B CG     1 
ATOM   9927  O  OD1    . ASP B 1 712 ? 3.16700   -21.44200 15.27300  1.000 75.81000  ? 703 ASP B OD1    1 
ATOM   9928  O  OD2    . ASP B 1 712 ? 2.47900   -19.83300 13.94000  1.000 62.33000  ? 703 ASP B OD2    1 
ATOM   9929  N  N      . ILE B 1 713 ? 1.81500   -22.94300 16.96000  1.000 56.75000  ? 704 ILE B N      1 
ATOM   9930  C  CA     . ILE B 1 713 ? 1.25200   -24.28300 17.07700  1.000 65.14000  ? 704 ILE B CA     1 
ATOM   9931  C  C      . ILE B 1 713 ? 1.19200   -24.68500 18.53800  1.000 58.34000  ? 704 ILE B C      1 
ATOM   9932  O  O      . ILE B 1 713 ? 0.21000   -25.27900 18.99300  1.000 54.34000  ? 704 ILE B O      1 
ATOM   9933  C  CB     . ILE B 1 713 ? 2.05900   -25.29700 16.24800  1.000 67.29000  ? 704 ILE B CB     1 
ATOM   9934  C  CG1    . ILE B 1 713 ? 1.59800   -25.28400 14.79000  1.000 81.49000  ? 704 ILE B CG1    1 
ATOM   9935  C  CG2    . ILE B 1 713 ? 1.93700   -26.69400 16.85100  1.000 50.72000  ? 704 ILE B CG2    1 
ATOM   9936  C  CD1    . ILE B 1 713 ? 2.65500   -25.75000 13.81200  1.000 101.15000 ? 704 ILE B CD1    1 
ATOM   9937  N  N      . LEU B 1 714 ? 2.24500   -24.38200 19.29400  1.000 47.18000  ? 705 LEU B N      1 
ATOM   9938  C  CA     . LEU B 1 714 ? 2.22700   -24.70100 20.71500  1.000 38.35000  ? 705 LEU B CA     1 
ATOM   9939  C  C      . LEU B 1 714 ? 0.98600   -24.11100 21.37000  1.000 44.03000  ? 705 LEU B C      1 
ATOM   9940  O  O      . LEU B 1 714 ? 0.19400   -24.82700 21.99700  1.000 62.16000  ? 705 LEU B O      1 
ATOM   9941  C  CB     . LEU B 1 714 ? 3.49600   -24.17300 21.38300  1.000 44.54000  ? 705 LEU B CB     1 
ATOM   9942  C  CG     . LEU B 1 714 ? 3.59300   -24.36500 22.89600  1.000 36.49000  ? 705 LEU B CG     1 
ATOM   9943  C  CD1    . LEU B 1 714 ? 3.91100   -25.81300 23.24900  1.000 47.71000  ? 705 LEU B CD1    1 
ATOM   9944  C  CD2    . LEU B 1 714 ? 4.63200   -23.42200 23.48300  1.000 54.74000  ? 705 LEU B CD2    1 
ATOM   9945  N  N      . ILE B 1 715 ? 0.76900   -22.81000 21.17600  1.000 40.40000  ? 706 ILE B N      1 
ATOM   9946  C  CA     . ILE B 1 715 ? -0.33500  -22.13900 21.86100  1.000 44.15000  ? 706 ILE B CA     1 
ATOM   9947  C  C      . ILE B 1 715 ? -1.67000  -22.74300 21.43800  1.000 49.03000  ? 706 ILE B C      1 
ATOM   9948  O  O      . ILE B 1 715 ? -2.50900  -23.10000 22.27700  1.000 55.75000  ? 706 ILE B O      1 
ATOM   9949  C  CB     . ILE B 1 715 ? -0.29600  -20.61900 21.60700  1.000 38.13000  ? 706 ILE B CB     1 
ATOM   9950  C  CG1    . ILE B 1 715 ? -0.76100  -20.28200 20.18800  1.000 46.07000  ? 706 ILE B CG1    1 
ATOM   9951  C  CG2    . ILE B 1 715 ? 1.10200   -20.07100 21.83900  1.000 39.68000  ? 706 ILE B CG2    1 
ATOM   9952  C  CD1    . ILE B 1 715 ? -0.79300  -18.80300 19.89000  1.000 40.93000  ? 706 ILE B CD1    1 
ATOM   9953  N  N      . LYS B 1 716 ? -1.87600  -22.90400 20.12900  1.000 46.98000  ? 707 LYS B N      1 
ATOM   9954  C  CA     . LYS B 1 716 ? -3.18600  -23.34400 19.65800  1.000 55.65000  ? 707 LYS B CA     1 
ATOM   9955  C  C      . LYS B 1 716 ? -3.46000  -24.80100 20.01900  1.000 56.26000  ? 707 LYS B C      1 
ATOM   9956  O  O      . LYS B 1 716 ? -4.56500  -25.13700 20.46800  1.000 46.41000  ? 707 LYS B O      1 
ATOM   9957  C  CB     . LYS B 1 716 ? -3.30900  -23.11900 18.15200  1.000 61.74000  ? 707 LYS B CB     1 
ATOM   9958  C  CG     . LYS B 1 716 ? -3.24800  -21.65400 17.75400  1.000 63.12000  ? 707 LYS B CG     1 
ATOM   9959  C  CD     . LYS B 1 716 ? -3.68200  -21.45700 16.31100  1.000 76.39000  ? 707 LYS B CD     1 
ATOM   9960  C  CE     . LYS B 1 716 ? -2.95000  -22.40700 15.37300  1.000 71.81000  ? 707 LYS B CE     1 
ATOM   9961  N  NZ     . LYS B 1 716 ? -1.48600  -22.12600 15.31800  1.000 77.58000  ? 707 LYS B NZ     1 
ATOM   9962  N  N      . ILE B 1 717 ? -2.47900  -25.68600 19.83300  1.000 58.09000  ? 708 ILE B N      1 
ATOM   9963  C  CA     . ILE B 1 717 ? -2.71400  -27.09300 20.12800  1.000 53.93000  ? 708 ILE B CA     1 
ATOM   9964  C  C      . ILE B 1 717 ? -2.90700  -27.29100 21.62200  1.000 50.52000  ? 708 ILE B C      1 
ATOM   9965  O  O      . ILE B 1 717 ? -3.70800  -28.13100 22.04500  1.000 60.50000  ? 708 ILE B O      1 
ATOM   9966  C  CB     . ILE B 1 717 ? -1.57400  -27.97100 19.58500  1.000 54.57000  ? 708 ILE B CB     1 
ATOM   9967  C  CG1    . ILE B 1 717 ? -1.93900  -29.44900 19.73700  1.000 50.43000  ? 708 ILE B CG1    1 
ATOM   9968  C  CG2    . ILE B 1 717 ? -0.28100  -27.68700 20.32600  1.000 63.00000  ? 708 ILE B CG2    1 
ATOM   9969  C  CD1    . ILE B 1 717 ? -1.28200  -30.35800 18.71600  1.000 68.25000  ? 708 ILE B CD1    1 
ATOM   9970  N  N      . MET B 1 718 ? -2.17100  -26.54200 22.44900  1.000 39.80000  ? 709 MET B N      1 
ATOM   9971  C  CA     . MET B 1 718 ? -2.39600  -26.64200 23.88400  1.000 37.41000  ? 709 MET B CA     1 
ATOM   9972  C  C      . MET B 1 718 ? -3.79700  -26.16200 24.24400  1.000 59.02000  ? 709 MET B C      1 
ATOM   9973  O  O      . MET B 1 718 ? -4.47600  -26.77500 25.07800  1.000 64.47000  ? 709 MET B O      1 
ATOM   9974  C  CB     . MET B 1 718 ? -1.33400  -25.84500 24.63700  1.000 31.15000  ? 709 MET B CB     1 
ATOM   9975  C  CG     . MET B 1 718 ? -1.13800  -26.28600 26.07200  1.000 35.12000  ? 709 MET B CG     1 
ATOM   9976  S  SD     . MET B 1 718 ? 0.23600   -25.43300 26.86500  1.000 48.09000  ? 709 MET B SD     1 
ATOM   9977  C  CE     . MET B 1 718 ? 1.63000   -26.18200 26.02200  1.000 43.77000  ? 709 MET B CE     1 
ATOM   9978  N  N      . SER B 1 719 ? -4.25700  -25.07800 23.60700  1.000 43.65000  ? 710 SER B N      1 
ATOM   9979  C  CA     . SER B 1 719 ? -5.63000  -24.63200 23.82300  1.000 42.53000  ? 710 SER B CA     1 
ATOM   9980  C  C      . SER B 1 719 ? -6.62900  -25.72600 23.46600  1.000 56.35000  ? 710 SER B C      1 
ATOM   9981  O  O      . SER B 1 719 ? -7.59200  -25.96100 24.20300  1.000 52.26000  ? 710 SER B O      1 
ATOM   9982  C  CB     . SER B 1 719 ? -5.91000  -23.36300 23.01700  1.000 44.99000  ? 710 SER B CB     1 
ATOM   9983  O  OG     . SER B 1 719 ? -5.13400  -22.27300 23.48500  1.000 41.94000  ? 710 SER B OG     1 
ATOM   9984  N  N      . VAL B 1 720 ? -6.41700  -26.40600 22.33800  1.000 67.01000  ? 711 VAL B N      1 
ATOM   9985  C  CA     . VAL B 1 720 ? -7.36300  -27.43400 21.89800  1.000 58.83000  ? 711 VAL B CA     1 
ATOM   9986  C  C      . VAL B 1 720 ? -7.35300  -28.62000 22.85700  1.000 44.15000  ? 711 VAL B C      1 
ATOM   9987  O  O      . VAL B 1 720 ? -8.40900  -29.10000 23.29400  1.000 54.38000  ? 711 VAL B O      1 
ATOM   9988  C  CB     . VAL B 1 720 ? -7.04900  -27.87500 20.45700  1.000 46.94000  ? 711 VAL B CB     1 
ATOM   9989  C  CG1    . VAL B 1 720 ? -7.88900  -29.08100 20.07800  1.000 30.22000  ? 711 VAL B CG1    1 
ATOM   9990  C  CG2    . VAL B 1 720 ? -7.29900  -26.73200 19.48400  1.000 59.25000  ? 711 VAL B CG2    1 
ATOM   9991  N  N      . VAL B 1 721 ? -6.15900  -29.12500 23.17900  1.000 35.44000  ? 712 VAL B N      1 
ATOM   9992  C  CA     . VAL B 1 721 ? -6.04800  -30.26500 24.08500  1.000 50.21000  ? 712 VAL B CA     1 
ATOM   9993  C  C      . VAL B 1 721 ? -6.69800  -29.94200 25.42000  1.000 57.11000  ? 712 VAL B C      1 
ATOM   9994  O  O      . VAL B 1 721 ? -7.37200  -30.78800 26.02100  1.000 53.95000  ? 712 VAL B O      1 
ATOM   9995  C  CB     . VAL B 1 721 ? -4.57400  -30.67200 24.26700  1.000 53.98000  ? 712 VAL B CB     1 
ATOM   9996  C  CG1    . VAL B 1 721 ? -4.44300  -31.69400 25.38800  1.000 31.65000  ? 712 VAL B CG1    1 
ATOM   9997  C  CG2    . VAL B 1 721 ? -4.00400  -31.22400 22.96800  1.000 59.15000  ? 712 VAL B CG2    1 
ATOM   9998  N  N      . SER B 1 722 ? -6.50000  -28.71700 25.91300  1.000 45.63000  ? 713 SER B N      1 
ATOM   9999  C  CA     . SER B 1 722 ? -7.12700  -28.32400 27.16600  1.000 30.98000  ? 713 SER B CA     1 
ATOM   10000 C  C      . SER B 1 722 ? -8.64100  -28.23700 27.02200  1.000 40.31000  ? 713 SER B C      1 
ATOM   10001 O  O      . SER B 1 722 ? -9.37600  -28.68400 27.90800  1.000 45.68000  ? 713 SER B O      1 
ATOM   10002 C  CB     . SER B 1 722 ? -6.53700  -26.99900 27.64300  1.000 44.35000  ? 713 SER B CB     1 
ATOM   10003 O  OG     . SER B 1 722 ? -6.54700  -26.03800 26.60400  1.000 54.53000  ? 713 SER B OG     1 
ATOM   10004 N  N      . VAL B 1 723 ? -9.12900  -27.67100 25.91500  1.000 38.51000  ? 714 VAL B N      1 
ATOM   10005 C  CA     . VAL B 1 723 ? -10.57100 -27.58600 25.69900  1.000 42.79000  ? 714 VAL B CA     1 
ATOM   10006 C  C      . VAL B 1 723 ? -11.19600 -28.97300 25.74500  1.000 38.27000  ? 714 VAL B C      1 
ATOM   10007 O  O      . VAL B 1 723 ? -12.31900 -29.15300 26.23400  1.000 26.23000  ? 714 VAL B O      1 
ATOM   10008 C  CB     . VAL B 1 723 ? -10.87400 -26.87800 24.36600  1.000 32.47000  ? 714 VAL B CB     1 
ATOM   10009 C  CG1    . VAL B 1 723 ? -12.34600 -27.04500 23.99900  1.000 32.62000  ? 714 VAL B CG1    1 
ATOM   10010 C  CG2    . VAL B 1 723 ? -10.50400 -25.41000 24.45400  1.000 39.91000  ? 714 VAL B CG2    1 
ATOM   10011 N  N      . ILE B 1 724 ? -10.48400 -29.97200 25.23100  1.000 44.69000  ? 715 ILE B N      1 
ATOM   10012 C  CA     . ILE B 1 724 ? -11.02500 -31.32700 25.24000  1.000 45.09000  ? 715 ILE B CA     1 
ATOM   10013 C  C      . ILE B 1 724 ? -10.93300 -31.94200 26.63400  1.000 52.47000  ? 715 ILE B C      1 
ATOM   10014 O  O      . ILE B 1 724 ? -11.92900 -32.43400 27.17600  1.000 62.08000  ? 715 ILE B O      1 
ATOM   10015 C  CB     . ILE B 1 724 ? -10.31800 -32.20100 24.18800  1.000 45.12000  ? 715 ILE B CB     1 
ATOM   10016 C  CG1    . ILE B 1 724 ? -10.70600 -31.75200 22.77800  1.000 44.12000  ? 715 ILE B CG1    1 
ATOM   10017 C  CG2    . ILE B 1 724 ? -10.66200 -33.66800 24.39800  1.000 55.63000  ? 715 ILE B CG2    1 
ATOM   10018 C  CD1    . ILE B 1 724 ? -9.98000  -32.49900 21.68700  1.000 43.07000  ? 715 ILE B CD1    1 
ATOM   10019 N  N      . ALA B 1 725 ? -9.74600  -31.91200 27.24400  1.000 42.69000  ? 716 ALA B N      1 
ATOM   10020 C  CA     . ALA B 1 725 ? -9.51200  -32.62700 28.49400  1.000 44.43000  ? 716 ALA B CA     1 
ATOM   10021 C  C      . ALA B 1 725 ? -10.11900 -31.93900 29.71300  1.000 60.51000  ? 716 ALA B C      1 
ATOM   10022 O  O      . ALA B 1 725 ? -10.17700 -32.55700 30.78600  1.000 76.52000  ? 716 ALA B O      1 
ATOM   10023 C  CB     . ALA B 1 725 ? -8.00900  -32.82100 28.70900  1.000 60.05000  ? 716 ALA B CB     1 
ATOM   10024 N  N      . VAL B 1 726 ? -10.56600 -30.68700 29.58300  1.000 65.79000  ? 717 VAL B N      1 
ATOM   10025 C  CA     . VAL B 1 726 ? -11.22400 -30.01100 30.69200  1.000 70.23000  ? 717 VAL B CA     1 
ATOM   10026 C  C      . VAL B 1 726 ? -12.51100 -30.72100 31.07300  1.000 84.62000  ? 717 VAL B C      1 
ATOM   10027 O  O      . VAL B 1 726 ? -12.96500 -30.61400 32.21800  1.000 78.73000  ? 717 VAL B O      1 
ATOM   10028 C  CB     . VAL B 1 726 ? -11.48400 -28.53200 30.33500  1.000 57.25000  ? 717 VAL B CB     1 
ATOM   10029 C  CG1    . VAL B 1 726 ? -12.55500 -28.42300 29.25900  1.000 53.99000  ? 717 VAL B CG1    1 
ATOM   10030 C  CG2    . VAL B 1 726 ? -11.88000 -27.74900 31.57500  1.000 79.67000  ? 717 VAL B CG2    1 
ATOM   10031 N  N      . SER B 1 727 ? -13.11300 -31.45700 30.13600  1.000 95.05000  ? 718 SER B N      1 
ATOM   10032 C  CA     . SER B 1 727 ? -14.27600 -32.26700 30.47100  1.000 87.14000  ? 718 SER B CA     1 
ATOM   10033 C  C      . SER B 1 727 ? -13.93000 -33.32300 31.51200  1.000 86.83000  ? 718 SER B C      1 
ATOM   10034 O  O      . SER B 1 727 ? -14.78600 -33.70700 32.31600  1.000 104.67000 ? 718 SER B O      1 
ATOM   10035 C  CB     . SER B 1 727 ? -14.84000 -32.92600 29.21000  1.000 69.50000  ? 718 SER B CB     1 
ATOM   10036 O  OG     . SER B 1 727 ? -15.16200 -31.96100 28.22300  1.000 63.47000  ? 718 SER B OG     1 
ATOM   10037 N  N      . ILE B 1 728 ? -12.68500 -33.79200 31.52100  1.000 92.00000  ? 719 ILE B N      1 
ATOM   10038 C  CA     . ILE B 1 728 ? -12.26000 -34.86900 32.40600  1.000 97.22000  ? 719 ILE B CA     1 
ATOM   10039 C  C      . ILE B 1 728 ? -11.62000 -34.34200 33.68500  1.000 87.02000  ? 719 ILE B C      1 
ATOM   10040 O  O      . ILE B 1 728 ? -11.92200 -34.83100 34.77400  1.000 83.26000  ? 719 ILE B O      1 
ATOM   10041 C  CB     . ILE B 1 728 ? -11.30400 -35.82700 31.66300  1.000 87.86000  ? 719 ILE B CB     1 
ATOM   10042 C  CG1    . ILE B 1 728 ? -12.01500 -36.47100 30.47000  1.000 76.87000  ? 719 ILE B CG1    1 
ATOM   10043 C  CG2    . ILE B 1 728 ? -10.75500 -36.88100 32.61800  1.000 81.42000  ? 719 ILE B CG2    1 
ATOM   10044 C  CD1    . ILE B 1 728 ? -11.12500 -37.36000 29.63300  1.000 55.37000  ? 719 ILE B CD1    1 
ATOM   10045 N  N      . PHE B 1 729 ? -10.73200 -33.35300 33.59100  1.000 88.61000  ? 720 PHE B N      1 
ATOM   10046 C  CA     . PHE B 1 729 ? -10.05900 -32.86800 34.79000  1.000 82.02000  ? 720 PHE B CA     1 
ATOM   10047 C  C      . PHE B 1 729 ? -10.68100 -31.59400 35.35400  1.000 85.31000  ? 720 PHE B C      1 
ATOM   10048 O  O      . PHE B 1 729 ? -10.08000 -30.96100 36.22700  1.000 90.59000  ? 720 PHE B O      1 
ATOM   10049 C  CB     . PHE B 1 729 ? -8.55900  -32.66300 34.53000  1.000 75.02000  ? 720 PHE B CB     1 
ATOM   10050 C  CG     . PHE B 1 729 ? -8.24400  -31.61200 33.50200  1.000 61.97000  ? 720 PHE B CG     1 
ATOM   10051 C  CD1    . PHE B 1 729 ? -8.39100  -30.26500 33.79400  1.000 71.06000  ? 720 PHE B CD1    1 
ATOM   10052 C  CD2    . PHE B 1 729 ? -7.76400  -31.97100 32.25500  1.000 50.92000  ? 720 PHE B CD2    1 
ATOM   10053 C  CE1    . PHE B 1 729 ? -8.09300  -29.30000 32.85400  1.000 70.81000  ? 720 PHE B CE1    1 
ATOM   10054 C  CE2    . PHE B 1 729 ? -7.46100  -31.00900 31.31100  1.000 57.80000  ? 720 PHE B CE2    1 
ATOM   10055 C  CZ     . PHE B 1 729 ? -7.62700  -29.67300 31.61000  1.000 67.08000  ? 720 PHE B CZ     1 
ATOM   10056 N  N      . LYS B 1 730 ? -11.87400 -31.21200 34.89200  1.000 91.37000  ? 721 LYS B N      1 
ATOM   10057 C  CA     . LYS B 1 730 ? -12.57900 -30.09900 35.52200  1.000 90.74000  ? 721 LYS B CA     1 
ATOM   10058 C  C      . LYS B 1 730 ? -12.81100 -30.37800 37.00200  1.000 93.58000  ? 721 LYS B C      1 
ATOM   10059 O  O      . LYS B 1 730 ? -12.50000 -29.54600 37.86200  1.000 82.87000  ? 721 LYS B O      1 
ATOM   10060 C  CB     . LYS B 1 730 ? -13.90500 -29.84100 34.80600  1.000 81.90000  ? 721 LYS B CB     1 
ATOM   10061 N  N      . HIS B 1 731 ? -13.35700 -31.55500 37.31500  1.000 109.06000 ? 722 HIS B N      1 
ATOM   10062 C  CA     . HIS B 1 731 ? -13.56200 -31.99000 38.68800  1.000 104.10000 ? 722 HIS B CA     1 
ATOM   10063 C  C      . HIS B 1 731 ? -12.57900 -33.06500 39.12700  1.000 107.98000 ? 722 HIS B C      1 
ATOM   10064 O  O      . HIS B 1 731 ? -12.52400 -33.37600 40.32200  1.000 119.41000 ? 722 HIS B O      1 
ATOM   10065 C  CB     . HIS B 1 731 ? -14.99400 -32.51400 38.87500  1.000 109.09000 ? 722 HIS B CB     1 
ATOM   10066 C  CG     . HIS B 1 731 ? -16.05500 -31.55100 38.44000  1.000 130.21000 ? 722 HIS B CG     1 
ATOM   10067 N  ND1    . HIS B 1 731 ? -16.65100 -31.61100 37.19800  1.000 122.03000 ? 722 HIS B ND1    1 
ATOM   10068 C  CD2    . HIS B 1 731 ? -16.63200 -30.50800 39.08400  1.000 139.32000 ? 722 HIS B CD2    1 
ATOM   10069 C  CE1    . HIS B 1 731 ? -17.54600 -30.64500 37.09500  1.000 120.19000 ? 722 HIS B CE1    1 
ATOM   10070 N  NE2    . HIS B 1 731 ? -17.55500 -29.96200 38.22500  1.000 113.55000 ? 722 HIS B NE2    1 
ATOM   10071 N  N      . VAL B 1 732 ? -11.80900 -33.63800 38.20200  1.000 108.21000 ? 723 VAL B N      1 
ATOM   10072 C  CA     . VAL B 1 732 ? -10.82300 -34.65800 38.53800  1.000 109.01000 ? 723 VAL B CA     1 
ATOM   10073 C  C      . VAL B 1 732 ? -9.45700  -33.99700 38.65800  1.000 104.66000 ? 723 VAL B C      1 
ATOM   10074 O  O      . VAL B 1 732 ? -8.63400  -34.06900 37.74000  1.000 108.42000 ? 723 VAL B O      1 
ATOM   10075 C  CB     . VAL B 1 732 ? -10.80000 -35.78600 37.49100  1.000 84.92000  ? 723 VAL B CB     1 
ATOM   10076 C  CG1    . VAL B 1 732 ? -9.80400  -36.86400 37.89800  1.000 61.24000  ? 723 VAL B CG1    1 
ATOM   10077 C  CG2    . VAL B 1 732 ? -12.19100 -36.37400 37.31400  1.000 89.63000  ? 723 VAL B CG2    1 
ATOM   10078 N  N      . HIS B 1 733 ? -9.21300  -33.35100 39.79300  1.000 96.15000  ? 724 HIS B N      1 
ATOM   10079 C  CA     . HIS B 1 733 ? -7.93300  -32.72900 40.09900  1.000 90.27000  ? 724 HIS B CA     1 
ATOM   10080 C  C      . HIS B 1 733 ? -7.43000  -33.27000 41.42700  1.000 100.62000 ? 724 HIS B C      1 
ATOM   10081 O  O      . HIS B 1 733 ? -8.14500  -33.21800 42.43400  1.000 112.16000 ? 724 HIS B O      1 
ATOM   10082 C  CB     . HIS B 1 733 ? -8.05300  -31.20200 40.13500  1.000 84.67000  ? 724 HIS B CB     1 
ATOM   10083 C  CG     . HIS B 1 733 ? -9.20000  -30.70600 40.96000  1.000 96.35000  ? 724 HIS B CG     1 
ATOM   10084 N  ND1    . HIS B 1 733 ? -9.11000  -30.51300 42.32100  1.000 117.39000 ? 724 HIS B ND1    1 
ATOM   10085 C  CD2    . HIS B 1 733 ? -10.46100 -30.35800 40.61200  1.000 105.20000 ? 724 HIS B CD2    1 
ATOM   10086 C  CE1    . HIS B 1 733 ? -10.26800 -30.06800 42.77800  1.000 123.01000 ? 724 HIS B CE1    1 
ATOM   10087 N  NE2    . HIS B 1 733 ? -11.10500 -29.96500 41.76100  1.000 108.52000 ? 724 HIS B NE2    1 
ATOM   10088 N  N      . LEU B 1 734 ? -6.20600  -33.80100 41.42300  1.000 87.12000  ? 725 LEU B N      1 
ATOM   10089 C  CA     . LEU B 1 734 ? -5.72300  -34.58500 42.55100  1.000 96.99000  ? 725 LEU B CA     1 
ATOM   10090 C  C      . LEU B 1 734 ? -5.26800  -33.71900 43.71600  1.000 114.25000 ? 725 LEU B C      1 
ATOM   10091 O  O      . LEU B 1 734 ? -5.15100  -34.22700 44.83600  1.000 125.43000 ? 725 LEU B O      1 
ATOM   10092 C  CB     . LEU B 1 734 ? -4.57600  -35.49400 42.09200  1.000 109.34000 ? 725 LEU B CB     1 
ATOM   10093 C  CG     . LEU B 1 734 ? -3.88800  -36.44900 43.07200  1.000 113.43000 ? 725 LEU B CG     1 
ATOM   10094 C  CD1    . LEU B 1 734 ? -3.14300  -37.51800 42.29400  1.000 134.37000 ? 725 LEU B CD1    1 
ATOM   10095 C  CD2    . LEU B 1 734 ? -2.92400  -35.71000 43.98400  1.000 88.99000  ? 725 LEU B CD2    1 
ATOM   10096 N  N      . PHE B 1 735 ? -5.03900  -32.43000 43.49000  1.000 103.03000 ? 726 PHE B N      1 
ATOM   10097 C  CA     . PHE B 1 735 ? -4.66000  -31.52700 44.56900  1.000 94.82000  ? 726 PHE B CA     1 
ATOM   10098 C  C      . PHE B 1 735 ? -5.63500  -30.36000 44.66900  1.000 97.60000  ? 726 PHE B C      1 
ATOM   10099 O  O      . PHE B 1 735 ? -6.50900  -30.19300 43.81900  1.000 102.91000 ? 726 PHE B O      1 
ATOM   10100 C  CB     . PHE B 1 735 ? -3.23300  -31.01200 44.37200  1.000 93.56000  ? 726 PHE B CB     1 
ATOM   10101 C  CG     . PHE B 1 735 ? -2.17100  -31.97300 44.83200  1.000 104.62000 ? 726 PHE B CG     1 
ATOM   10102 C  CD1    . PHE B 1 735 ? -2.09100  -32.34500 46.16400  1.000 106.20000 ? 726 PHE B CD1    1 
ATOM   10103 C  CD2    . PHE B 1 735 ? -1.24900  -32.49800 43.93900  1.000 94.85000  ? 726 PHE B CD2    1 
ATOM   10104 C  CE1    . PHE B 1 735 ? -1.11700  -33.22400 46.59800  1.000 116.85000 ? 726 PHE B CE1    1 
ATOM   10105 C  CE2    . PHE B 1 735 ? -0.27000  -33.38000 44.36800  1.000 97.17000  ? 726 PHE B CE2    1 
ATOM   10106 C  CZ     . PHE B 1 735 ? -0.20600  -33.74200 45.70000  1.000 121.53000 ? 726 PHE B CZ     1 
ATOM   10107 O  OXT    . PHE B 1 735 ? -5.57600  -29.55900 45.60200  1.000 112.63000 ? 726 PHE B OXT    1 
HETATM 10108 P  P1     . 911 C 2 .   ? 33.18900  -6.78700  33.65700  1.000 148.31000 ? 801 911 A P1     1 
HETATM 10109 O  O2     . 911 C 2 .   ? 32.34700  -6.32500  32.49000  1.000 104.75000 ? 801 911 A O2     1 
HETATM 10110 O  O3     . 911 C 2 .   ? 34.31000  -5.85800  34.04300  1.000 134.06000 ? 801 911 A O3     1 
HETATM 10111 O  O5     . 911 C 2 .   ? 32.28300  -7.06400  34.91100  1.000 136.81000 ? 801 911 A O5     1 
HETATM 10112 C  C7     . 911 C 2 .   ? 33.90900  -8.42100  33.21800  1.000 131.34000 ? 801 911 A C7     1 
HETATM 10113 P  P8     . 911 C 2 .   ? 34.66900  -8.38900  31.54500  1.000 145.31000 ? 801 911 A P8     1 
HETATM 10114 O  O9     . 911 C 2 .   ? 33.64200  -8.87300  30.55100  1.000 105.19000 ? 801 911 A O9     1 
HETATM 10115 O  O10    . 911 C 2 .   ? 35.21000  -7.00300  31.30700  1.000 133.57000 ? 801 911 A O10    1 
HETATM 10116 O  O12    . 911 C 2 .   ? 35.86500  -9.40300  31.60900  1.000 129.58000 ? 801 911 A O12    1 
HETATM 10117 O  O14    . 911 C 2 .   ? 32.81600  -9.36000  33.15500  1.000 112.11000 ? 801 911 A O14    1 
HETATM 10118 C  C16    . 911 C 2 .   ? 34.93700  -8.87000  34.27000  1.000 115.80000 ? 801 911 A C16    1 
HETATM 10119 H  HO5    . 911 C 2 .   ? 31.34800  -6.74000  34.99200  1.000 165.78000 ? 801 911 A HO5    1 
HETATM 10120 H  HO12   . 911 C 2 .   ? 35.63500  -10.36800 31.55700  1.000 157.10000 ? 801 911 A HO12   1 
HETATM 10121 H  HO14   . 911 C 2 .   ? 33.23600  -10.24900 33.01300  1.000 136.14000 ? 801 911 A HO14   1 
HETATM 10122 H  H16    . 911 C 2 .   ? 35.21600  -9.91600  34.14900  1.000 140.57000 ? 801 911 A H16    1 
HETATM 10123 H  H16A   . 911 C 2 .   ? 35.85800  -8.29200  34.21500  1.000 140.57000 ? 801 911 A H16A   1 
HETATM 10124 H  H16B   . 911 C 2 .   ? 34.55900  -8.76200  35.28500  1.000 140.57000 ? 801 911 A H16B   1 
HETATM 10125 MG MG     . MG  D 3 .   ? 31.77200  -5.96700  28.73000  1.000 85.26000  ? 802 MG  A MG     1 
HETATM 10126 MG MG     . MG  E 3 .   ? 32.31700  -4.32500  33.69400  1.000 91.72000  ? 803 MG  A MG     1 
HETATM 10127 MG MG     . MG  F 3 .   ? 34.69400  -3.50200  34.18000  1.000 98.19000  ? 804 MG  A MG     1 
HETATM 10128 MG MG     . MG  G 3 .   ? 37.22300  -5.48900  30.59300  1.000 102.10000 ? 805 MG  A MG     1 
HETATM 10129 CA CA     . CA  H 4 .   ? 30.54100  -9.13400  32.27000  1.000 89.93000  ? 806 CA  A CA     1 
HETATM 10130 P  P1     . 911 I 2 .   ? 16.91600  -19.58800 2.57400   1.000 158.85000 ? 801 911 B P1     1 
HETATM 10131 O  O2     . 911 I 2 .   ? 17.68600  -20.22200 3.71000   1.000 120.72000 ? 801 911 B O2     1 
HETATM 10132 O  O3     . 911 I 2 .   ? 16.30900  -20.54700 1.58400   1.000 147.59000 ? 801 911 B O3     1 
HETATM 10133 O  O5     . 911 I 2 .   ? 15.78700  -18.64900 3.13100   1.000 137.23000 ? 801 911 B O5     1 
HETATM 10134 C  C7     . 911 I 2 .   ? 18.05300  -18.46500 1.66500   1.000 134.07000 ? 801 911 B C7     1 
HETATM 10135 P  P8     . 911 I 2 .   ? 19.66300  -19.27500 1.30600   1.000 158.56000 ? 801 911 B P8     1 
HETATM 10136 O  O9     . 911 I 2 .   ? 20.62600  -18.94900 2.42100   1.000 147.15000 ? 801 911 B O9     1 
HETATM 10137 O  O10    . 911 I 2 .   ? 19.40900  -20.74400 1.08500   1.000 141.77000 ? 801 911 B O10    1 
HETATM 10138 O  O12    . 911 I 2 .   ? 20.15000  -18.62900 -0.03800  1.000 134.78000 ? 801 911 B O12    1 
HETATM 10139 O  O14    . 911 I 2 .   ? 18.33600  -17.35500 2.54200   1.000 122.63000 ? 801 911 B O14    1 
HETATM 10140 C  C16    . 911 I 2 .   ? 17.40200  -17.95900 0.36700   1.000 121.59000 ? 801 911 B C16    1 
HETATM 10141 H  HO5    . 911 I 2 .   ? 15.91300  -18.04600 3.91000   1.000 166.28000 ? 801 911 B HO5    1 
HETATM 10142 H  HO12   . 911 I 2 .   ? 20.39700  -17.66800 -0.00700  1.000 163.34000 ? 801 911 B HO12   1 
HETATM 10143 H  HO14   . 911 I 2 .   ? 17.49100  -16.83700 2.59900   1.000 148.76000 ? 801 911 B HO14   1 
HETATM 10144 H  H16    . 911 I 2 .   ? 17.96500  -17.14200 -0.08200  1.000 147.51000 ? 801 911 B H16    1 
HETATM 10145 H  H16A   . 911 I 2 .   ? 17.32900  -18.74100 -0.38700  1.000 147.51000 ? 801 911 B H16A   1 
HETATM 10146 H  H16B   . 911 I 2 .   ? 16.39100  -17.58900 0.53300   1.000 147.51000 ? 801 911 B H16B   1 
HETATM 10147 C  C1B    . LMT J 5 .   ? 0.56700   -41.59900 0.75500   1.000 145.27000 ? 802 LMT B C1B    1 
HETATM 10148 C  C2B    . LMT J 5 .   ? 0.67100   -41.49000 -0.77000  1.000 153.04000 ? 802 LMT B C2B    1 
HETATM 10149 C  C3B    . LMT J 5 .   ? 2.05500   -41.59500 -1.33600  1.000 151.21000 ? 802 LMT B C3B    1 
HETATM 10150 C  C4B    . LMT J 5 .   ? 2.99200   -42.44400 -0.56500  1.000 155.02000 ? 802 LMT B C4B    1 
HETATM 10151 C  C5B    . LMT J 5 .   ? 2.85900   -42.27200 0.94500   1.000 146.69000 ? 802 LMT B C5B    1 
HETATM 10152 C  C6B    . LMT J 5 .   ? 4.17400   -41.79200 1.44100   1.000 141.67000 ? 802 LMT B C6B    1 
HETATM 10153 O  O1B    . LMT J 5 .   ? 0.18100   -42.87800 1.03500   1.000 144.66000 ? 802 LMT B O1B    1 
HETATM 10154 O  O2B    . LMT J 5 .   ? -0.08300  -42.54900 -1.39100  1.000 161.30000 ? 802 LMT B O2B    1 
HETATM 10155 O  O3B    . LMT J 5 .   ? 2.59500   -40.23700 -1.48900  1.000 134.06000 ? 802 LMT B O3B    1 
HETATM 10156 O  "O4'"  . LMT J 5 .   ? 2.78000   -43.83400 -0.93100  1.000 149.10000 ? 802 LMT B "O4'"  1 
HETATM 10157 O  O5B    . LMT J 5 .   ? 1.84400   -41.27800 1.37000   1.000 128.24000 ? 802 LMT B O5B    1 
HETATM 10158 O  O6B    . LMT J 5 .   ? 4.33800   -40.49500 0.92600   1.000 149.31000 ? 802 LMT B O6B    1 
HETATM 10159 C  "C1'"  . LMT J 5 .   ? -1.58800  -45.50300 2.16100   1.000 140.23000 ? 802 LMT B "C1'"  1 
HETATM 10160 C  "C2'"  . LMT J 5 .   ? -2.44600  -44.27800 1.85500   1.000 138.70000 ? 802 LMT B "C2'"  1 
HETATM 10161 C  "C3'"  . LMT J 5 .   ? -1.84600  -43.00100 2.32000   1.000 140.45000 ? 802 LMT B "C3'"  1 
HETATM 10162 C  "C4'"  . LMT J 5 .   ? -0.36900  -42.98600 2.36500   1.000 132.96000 ? 802 LMT B "C4'"  1 
HETATM 10163 C  "C5'"  . LMT J 5 .   ? 0.29300   -44.23600 2.94600   1.000 129.57000 ? 802 LMT B "C5'"  1 
HETATM 10164 C  "C6'"  . LMT J 5 .   ? 1.06400   -43.85400 4.15500   1.000 125.97000 ? 802 LMT B "C6'"  1 
HETATM 10165 O  "O1'"  . LMT J 5 .   ? -2.48400  -46.48900 2.48700   1.000 125.93000 ? 802 LMT B "O1'"  1 
HETATM 10166 O  "O2'"  . LMT J 5 .   ? -2.68700  -44.12600 0.44900   1.000 115.86000 ? 802 LMT B "O2'"  1 
HETATM 10167 O  "O3'"  . LMT J 5 .   ? -2.32700  -42.65500 3.66500   1.000 120.21000 ? 802 LMT B "O3'"  1 
HETATM 10168 O  "O5'"  . LMT J 5 .   ? -0.69400  -45.29100 3.29100   1.000 147.54000 ? 802 LMT B "O5'"  1 
HETATM 10169 O  "O6'"  . LMT J 5 .   ? 1.75600   -44.98300 4.60800   1.000 122.84000 ? 802 LMT B "O6'"  1 
HETATM 10170 C  C1     . LMT J 5 .   ? -2.94000  -47.24100 1.40200   1.000 111.24000 ? 802 LMT B C1     1 
HETATM 10171 C  C2     . LMT J 5 .   ? -4.06700  -48.14500 1.89200   1.000 108.64000 ? 802 LMT B C2     1 
HETATM 10172 C  C3     . LMT J 5 .   ? -5.41900  -47.46400 1.71900   1.000 107.00000 ? 802 LMT B C3     1 
HETATM 10173 C  C4     . LMT J 5 .   ? -6.58200  -48.32600 2.19600   1.000 93.20000  ? 802 LMT B C4     1 
HETATM 10174 C  C5     . LMT J 5 .   ? -7.89900  -47.55900 2.10700   1.000 97.29000  ? 802 LMT B C5     1 
HETATM 10175 C  C6     . LMT J 5 .   ? -8.61500  -47.84200 0.79000   1.000 110.05000 ? 802 LMT B C6     1 
HETATM 10176 C  C7     . LMT J 5 .   ? -10.07100 -47.39000 0.79600   1.000 101.74000 ? 802 LMT B C7     1 
HETATM 10177 C  C8     . LMT J 5 .   ? -10.65800 -47.37200 -0.61300  1.000 95.99000  ? 802 LMT B C8     1 
HETATM 10178 C  C9     . LMT J 5 .   ? -12.15100 -47.67600 -0.59700  1.000 100.08000 ? 802 LMT B C9     1 
HETATM 10179 C  C10    . LMT J 5 .   ? -12.84800 -47.33700 -1.91100  1.000 113.15000 ? 802 LMT B C10    1 
HETATM 10180 C  C11    . LMT J 5 .   ? -14.14300 -48.13100 -2.05100  1.000 100.79000 ? 802 LMT B C11    1 
HETATM 10181 C  C12    . LMT J 5 .   ? -15.29200 -47.47300 -1.28800  1.000 89.56000  ? 802 LMT B C12    1 
HETATM 10182 H  H1B    . LMT J 5 .   ? -0.17400  -40.92500 1.16700   1.000 175.92000 ? 802 LMT B H1B    1 
HETATM 10183 H  H2B    . LMT J 5 .   ? 0.26700   -40.51200 -1.00200  1.000 185.25000 ? 802 LMT B H2B    1 
HETATM 10184 H  H3B    . LMT J 5 .   ? 1.97800   -42.06800 -2.30700  1.000 183.06000 ? 802 LMT B H3B    1 
HETATM 10185 H  H4B    . LMT J 5 .   ? 4.00400   -42.16600 -0.83000  1.000 187.63000 ? 802 LMT B H4B    1 
HETATM 10186 H  H5B    . LMT J 5 .   ? 2.57600   -43.22900 1.36600   1.000 177.64000 ? 802 LMT B H5B    1 
HETATM 10187 H  "H6'2" . LMT J 5 .   ? 4.96800   -42.44000 1.08400   1.000 171.61000 ? 802 LMT B "H6'2" 1 
HETATM 10188 H  "H6'1" . LMT J 5 .   ? 4.18000   -41.76800 2.52500   1.000 171.61000 ? 802 LMT B "H6'1" 1 
HETATM 10189 H  H2O1   . LMT J 5 .   ? 0.26400   -43.39600 -1.12500  1.000 195.17000 ? 802 LMT B H2O1   1 
HETATM 10190 H  H3O1   . LMT J 5 .   ? 3.23800   -40.22700 -2.18300  1.000 162.47000 ? 802 LMT B H3O1   1 
HETATM 10191 H  H4O1   . LMT J 5 .   ? 3.58200   -44.32800 -0.82500  1.000 180.52000 ? 802 LMT B H4O1   1 
HETATM 10192 H  H6B    . LMT J 5 .   ? 5.12300   -40.44100 0.40400   1.000 180.78000 ? 802 LMT B H6B    1 
HETATM 10193 H  "H1'"  . LMT J 5 .   ? -0.97500  -45.77300 1.30900   1.000 169.88000 ? 802 LMT B "H1'"  1 
HETATM 10194 H  "H2'"  . LMT J 5 .   ? -3.38600  -44.46400 2.36100   1.000 168.04000 ? 802 LMT B "H2'"  1 
HETATM 10195 H  "H3'"  . LMT J 5 .   ? -2.17800  -42.25900 1.60400   1.000 170.15000 ? 802 LMT B "H3'"  1 
HETATM 10196 H  "H4'"  . LMT J 5 .   ? -0.14200  -42.12500 2.98100   1.000 161.15000 ? 802 LMT B "H4'"  1 
HETATM 10197 H  "H5'"  . LMT J 5 .   ? 0.97700   -44.64500 2.21300   1.000 157.09000 ? 802 LMT B "H5'"  1 
HETATM 10198 H  H6D    . LMT J 5 .   ? 0.38600   -43.50500 4.92700   1.000 152.77000 ? 802 LMT B H6D    1 
HETATM 10199 H  H6E    . LMT J 5 .   ? 1.76900   -43.06800 3.90500   1.000 152.77000 ? 802 LMT B H6E    1 
HETATM 10200 H  H2O2   . LMT J 5 .   ? -1.93900  -43.70800 0.05300   1.000 140.64000 ? 802 LMT B H2O2   1 
HETATM 10201 H  H3O2   . LMT J 5 .   ? -2.28900  -41.71300 3.78200   1.000 145.86000 ? 802 LMT B H3O2   1 
HETATM 10202 H  "H6'"  . LMT J 5 .   ? 2.55900   -45.06900 4.12000   1.000 149.02000 ? 802 LMT B "H6'"  1 
HETATM 10203 H  H12    . LMT J 5 .   ? -2.12900  -47.84500 1.00800   1.000 135.09000 ? 802 LMT B H12    1 
HETATM 10204 H  H11    . LMT J 5 .   ? -3.31200  -46.57800 0.62700   1.000 135.09000 ? 802 LMT B H11    1 
HETATM 10205 H  H22    . LMT J 5 .   ? -3.91300  -48.37400 2.94100   1.000 131.97000 ? 802 LMT B H22    1 
HETATM 10206 H  H21    . LMT J 5 .   ? -4.05600  -49.07100 1.32500   1.000 131.97000 ? 802 LMT B H21    1 
HETATM 10207 H  H32    . LMT J 5 .   ? -5.41700  -46.53700 2.28200   1.000 130.01000 ? 802 LMT B H32    1 
HETATM 10208 H  H31    . LMT J 5 .   ? -5.56200  -47.23600 0.66700   1.000 130.01000 ? 802 LMT B H31    1 
HETATM 10209 H  H42    . LMT J 5 .   ? -6.64500  -49.21600 1.57900   1.000 113.44000 ? 802 LMT B H42    1 
HETATM 10210 H  H41    . LMT J 5 .   ? -6.41000  -48.62200 3.22500   1.000 113.44000 ? 802 LMT B H41    1 
HETATM 10211 H  H52    . LMT J 5 .   ? -7.69800  -46.49600 2.18200   1.000 118.35000 ? 802 LMT B H52    1 
HETATM 10212 H  H51    . LMT J 5 .   ? -8.54000  -47.85500 2.93100   1.000 118.35000 ? 802 LMT B H51    1 
HETATM 10213 H  H62    . LMT J 5 .   ? -8.58200  -48.90900 0.59700   1.000 133.66000 ? 802 LMT B H62    1 
HETATM 10214 H  H61    . LMT J 5 .   ? -8.09300  -47.32400 -0.00800  1.000 133.66000 ? 802 LMT B H61    1 
HETATM 10215 H  H72    . LMT J 5 .   ? -10.13100 -46.39200 1.21800   1.000 123.69000 ? 802 LMT B H72    1 
HETATM 10216 H  H71    . LMT J 5 .   ? -10.65000 -48.06900 1.41300   1.000 123.69000 ? 802 LMT B H71    1 
HETATM 10217 H  H82    . LMT J 5 .   ? -10.15000 -48.11500 -1.21900  1.000 116.80000 ? 802 LMT B H82    1 
HETATM 10218 H  H81    . LMT J 5 .   ? -10.50000 -46.39200 -1.05200  1.000 116.80000 ? 802 LMT B H81    1 
HETATM 10219 H  H92    . LMT J 5 .   ? -12.61400 -47.10300 0.19900   1.000 121.70000 ? 802 LMT B H92    1 
HETATM 10220 H  H91    . LMT J 5 .   ? -12.28800 -48.73400 -0.39500  1.000 121.70000 ? 802 LMT B H91    1 
HETATM 10221 H  H102   . LMT J 5 .   ? -12.18900 -47.57500 -2.73900  1.000 137.39000 ? 802 LMT B H102   1 
HETATM 10222 H  H101   . LMT J 5 .   ? -13.07300 -46.27500 -1.93500  1.000 137.39000 ? 802 LMT B H101   1 
HETATM 10223 H  H112   . LMT J 5 .   ? -13.98800 -49.13300 -1.66400  1.000 122.55000 ? 802 LMT B H112   1 
HETATM 10224 H  H111   . LMT J 5 .   ? -14.40700 -48.19700 -3.10100  1.000 122.55000 ? 802 LMT B H111   1 
HETATM 10225 H  H123   . LMT J 5 .   ? -16.23800 -47.87000 -1.64600  1.000 109.08000 ? 802 LMT B H123   1 
HETATM 10226 H  H122   . LMT J 5 .   ? -15.26600 -46.40000 -1.45000  1.000 109.08000 ? 802 LMT B H122   1 
HETATM 10227 H  H121   . LMT J 5 .   ? -15.18900 -47.68300 -0.22800  1.000 109.08000 ? 802 LMT B H121   1 
HETATM 10228 C  C1B    . LMT K 5 .   ? -6.24000  -42.47800 -8.69400  1.000 164.07000 ? 803 LMT B C1B    1 
HETATM 10229 C  C2B    . LMT K 5 .   ? -7.16700  -41.76700 -9.67600  1.000 146.34000 ? 803 LMT B C2B    1 
HETATM 10230 C  C3B    . LMT K 5 .   ? -8.57300  -41.67300 -9.21000  1.000 144.56000 ? 803 LMT B C3B    1 
HETATM 10231 C  C4B    . LMT K 5 .   ? -8.78400  -41.38500 -7.77300  1.000 150.05000 ? 803 LMT B C4B    1 
HETATM 10232 C  C5B    . LMT K 5 .   ? -7.58800  -41.61200 -6.86500  1.000 156.65000 ? 803 LMT B C5B    1 
HETATM 10233 C  C6B    . LMT K 5 .   ? -7.99600  -42.01200 -5.49700  1.000 148.26000 ? 803 LMT B C6B    1 
HETATM 10234 O  O1B    . LMT K 5 .   ? -5.18300  -41.61400 -8.65900  1.000 170.79000 ? 803 LMT B O1B    1 
HETATM 10235 O  O2B    . LMT K 5 .   ? -6.78900  -40.40000 -9.96500  1.000 132.75000 ? 803 LMT B O2B    1 
HETATM 10236 O  O3B    . LMT K 5 .   ? -9.24200  -42.95500 -9.48000  1.000 138.03000 ? 803 LMT B O3B    1 
HETATM 10237 O  "O4'"  . LMT K 5 .   ? -9.11500  -39.98800 -7.59000  1.000 149.40000 ? 803 LMT B "O4'"  1 
HETATM 10238 O  O5B    . LMT K 5 .   ? -6.73800  -42.71300 -7.35700  1.000 161.95000 ? 803 LMT B O5B    1 
HETATM 10239 O  O6B    . LMT K 5 .   ? -8.35600  -43.36400 -5.56700  1.000 155.62000 ? 803 LMT B O6B    1 
HETATM 10240 C  "C1'"  . LMT K 5 .   ? -2.82200  -39.60800 -7.79800  1.000 141.40000 ? 803 LMT B "C1'"  1 
HETATM 10241 C  "C2'"  . LMT K 5 .   ? -2.47100  -40.44900 -9.02400  1.000 154.45000 ? 803 LMT B "C2'"  1 
HETATM 10242 C  "C3'"  . LMT K 5 .   ? -2.89200  -41.87300 -8.89800  1.000 159.07000 ? 803 LMT B "C3'"  1 
HETATM 10243 C  "C4'"  . LMT K 5 .   ? -4.02600  -42.11700 -7.98300  1.000 164.65000 ? 803 LMT B "C4'"  1 
HETATM 10244 C  "C5'"  . LMT K 5 .   ? -3.89800  -41.45000 -6.62000  1.000 155.58000 ? 803 LMT B "C5'"  1 
HETATM 10245 C  "C6'"  . LMT K 5 .   ? -3.60200  -42.58100 -5.69800  1.000 155.83000 ? 803 LMT B "C6'"  1 
HETATM 10246 O  "O1'"  . LMT K 5 .   ? -1.88900  -38.61900 -7.61600  1.000 143.63000 ? 803 LMT B "O1'"  1 
HETATM 10247 O  "O2'"  . LMT K 5 .   ? -3.13600  -39.89800 -10.17300 1.000 150.16000 ? 803 LMT B "O2'"  1 
HETATM 10248 O  "O3'"  . LMT K 5 .   ? -1.74900  -42.64900 -8.41900  1.000 158.40000 ? 803 LMT B "O3'"  1 
HETATM 10249 O  "O5'"  . LMT K 5 .   ? -2.84700  -40.40700 -6.57200  1.000 146.58000 ? 803 LMT B "O5'"  1 
HETATM 10250 O  "O6'"  . LMT K 5 .   ? -3.23600  -42.03400 -4.47300  1.000 159.83000 ? 803 LMT B "O6'"  1 
HETATM 10251 C  C1     . LMT K 5 .   ? -2.27000  -37.75300 -6.58700  1.000 133.54000 ? 803 LMT B C1     1 
HETATM 10252 C  C2     . LMT K 5 .   ? -2.12900  -36.31900 -7.08500  1.000 119.91000 ? 803 LMT B C2     1 
HETATM 10253 C  C3     . LMT K 5 .   ? -2.96500  -36.05800 -8.33300  1.000 117.42000 ? 803 LMT B C3     1 
HETATM 10254 C  C4     . LMT K 5 .   ? -4.41100  -35.78100 -7.94200  1.000 104.27000 ? 803 LMT B C4     1 
HETATM 10255 C  C5     . LMT K 5 .   ? -5.30900  -35.55100 -9.15300  1.000 113.23000 ? 803 LMT B C5     1 
HETATM 10256 C  C6     . LMT K 5 .   ? -6.04500  -36.82600 -9.55700  1.000 139.23000 ? 803 LMT B C6     1 
HETATM 10257 C  C7     . LMT K 5 .   ? -7.29700  -37.04900 -8.71400  1.000 132.37000 ? 803 LMT B C7     1 
HETATM 10258 C  C8     . LMT K 5 .   ? -8.55000  -37.04500 -9.58300  1.000 120.85000 ? 803 LMT B C8     1 
HETATM 10259 C  C9     . LMT K 5 .   ? -9.78300  -37.52400 -8.82300  1.000 132.14000 ? 803 LMT B C9     1 
HETATM 10260 C  C10    . LMT K 5 .   ? -10.94600 -36.54500 -8.96600  1.000 130.26000 ? 803 LMT B C10    1 
HETATM 10261 C  C11    . LMT K 5 .   ? -10.65700 -35.24100 -8.22200  1.000 108.61000 ? 803 LMT B C11    1 
HETATM 10262 C  C12    . LMT K 5 .   ? -11.14900 -33.99900 -8.96300  1.000 90.23000  ? 803 LMT B C12    1 
HETATM 10263 H  H1B    . LMT K 5 .   ? -6.01400  -43.48300 -9.02900  1.000 198.49000 ? 803 LMT B H1B    1 
HETATM 10264 H  H2B    . LMT K 5 .   ? -7.06400  -42.36300 -10.57300 1.000 177.21000 ? 803 LMT B H2B    1 
HETATM 10265 H  H3B    . LMT K 5 .   ? -9.00000  -40.84900 -9.76800  1.000 175.08000 ? 803 LMT B H3B    1 
HETATM 10266 H  H4B    . LMT K 5 .   ? -9.58900  -42.05200 -7.48900  1.000 181.67000 ? 803 LMT B H4B    1 
HETATM 10267 H  H5B    . LMT K 5 .   ? -7.06100  -40.66600 -6.81900  1.000 189.59000 ? 803 LMT B H5B    1 
HETATM 10268 H  "H6'2" . LMT K 5 .   ? -8.84300  -41.41700 -5.17100  1.000 179.52000 ? 803 LMT B "H6'2" 1 
HETATM 10269 H  "H6'1" . LMT K 5 .   ? -7.17000  -41.88100 -4.80700  1.000 179.52000 ? 803 LMT B "H6'1" 1 
HETATM 10270 H  H2O1   . LMT K 5 .   ? -6.10800  -40.09500 -9.38200  1.000 160.91000 ? 803 LMT B H2O1   1 
HETATM 10271 H  H3O1   . LMT K 5 .   ? -9.94900  -42.85100 -10.09800 1.000 167.24000 ? 803 LMT B H3O1   1 
HETATM 10272 H  H4O1   . LMT K 5 .   ? -9.90500  -39.90400 -7.07900  1.000 180.89000 ? 803 LMT B H4O1   1 
HETATM 10273 H  H6B    . LMT K 5 .   ? -7.94900  -43.77000 -6.31800  1.000 188.34000 ? 803 LMT B H6B    1 
HETATM 10274 H  "H1'"  . LMT K 5 .   ? -3.79100  -39.16100 -7.98100  1.000 171.28000 ? 803 LMT B "H1'"  1 
HETATM 10275 H  "H2'"  . LMT K 5 .   ? -1.39700  -40.41000 -9.15400  1.000 186.95000 ? 803 LMT B "H2'"  1 
HETATM 10276 H  "H3'"  . LMT K 5 .   ? -3.20400  -42.19500 -9.88400  1.000 192.49000 ? 803 LMT B "H3'"  1 
HETATM 10277 H  "H4'"  . LMT K 5 .   ? -4.10600  -43.17800 -7.78000  1.000 199.19000 ? 803 LMT B "H4'"  1 
HETATM 10278 H  "H5'"  . LMT K 5 .   ? -4.80300  -40.93300 -6.32600  1.000 188.30000 ? 803 LMT B "H5'"  1 
HETATM 10279 H  H6D    . LMT K 5 .   ? -2.78700  -43.17800 -6.09500  1.000 188.60000 ? 803 LMT B H6D    1 
HETATM 10280 H  H6E    . LMT K 5 .   ? -4.48400  -43.20100 -5.57800  1.000 188.60000 ? 803 LMT B H6E    1 
HETATM 10281 H  H2O2   . LMT K 5 .   ? -2.89900  -38.99100 -10.29500 1.000 181.79000 ? 803 LMT B H2O2   1 
HETATM 10282 H  H3O2   . LMT K 5 .   ? -1.34900  -42.19600 -7.69100  1.000 191.69000 ? 803 LMT B H3O2   1 
HETATM 10283 H  "H6'"  . LMT K 5 .   ? -2.83300  -41.20100 -4.65100  1.000 193.40000 ? 803 LMT B "H6'"  1 
HETATM 10284 H  H12    . LMT K 5 .   ? -1.62700  -37.90500 -5.72600  1.000 161.85000 ? 803 LMT B H12    1 
HETATM 10285 H  H11    . LMT K 5 .   ? -3.30200  -37.94400 -6.31200  1.000 161.85000 ? 803 LMT B H11    1 
HETATM 10286 H  H22    . LMT K 5 .   ? -1.08600  -36.12600 -7.31400  1.000 145.50000 ? 803 LMT B H22    1 
HETATM 10287 H  H21    . LMT K 5 .   ? -2.44800  -35.64100 -6.30000  1.000 145.50000 ? 803 LMT B H21    1 
HETATM 10288 H  H32    . LMT K 5 .   ? -2.56400  -35.20200 -8.86500  1.000 142.51000 ? 803 LMT B H32    1 
HETATM 10289 H  H31    . LMT K 5 .   ? -2.92600  -36.92700 -8.98200  1.000 142.51000 ? 803 LMT B H31    1 
HETATM 10290 H  H42    . LMT K 5 .   ? -4.79100  -36.62800 -7.38100  1.000 126.73000 ? 803 LMT B H42    1 
HETATM 10291 H  H41    . LMT K 5 .   ? -4.44100  -34.89900 -7.31200  1.000 126.73000 ? 803 LMT B H41    1 
HETATM 10292 H  H52    . LMT K 5 .   ? -4.70200  -35.21300 -9.98600  1.000 137.48000 ? 803 LMT B H52    1 
HETATM 10293 H  H51    . LMT K 5 .   ? -6.03700  -34.78200 -8.91300  1.000 137.48000 ? 803 LMT B H51    1 
HETATM 10294 H  H62    . LMT K 5 .   ? -5.37900  -37.67400 -9.43100  1.000 168.68000 ? 803 LMT B H62    1 
HETATM 10295 H  H61    . LMT K 5 .   ? -6.33000  -36.75400 -10.60100 1.000 168.68000 ? 803 LMT B H61    1 
HETATM 10296 H  H72    . LMT K 5 .   ? -7.22000  -38.00300 -8.20400  1.000 160.45000 ? 803 LMT B H72    1 
HETATM 10297 H  H71    . LMT K 5 .   ? -7.37400  -36.25900 -7.97300  1.000 160.45000 ? 803 LMT B H71    1 
HETATM 10298 H  H82    . LMT K 5 .   ? -8.38800  -37.69500 -10.43600 1.000 146.62000 ? 803 LMT B H82    1 
HETATM 10299 H  H81    . LMT K 5 .   ? -8.72700  -36.03500 -9.93900  1.000 146.62000 ? 803 LMT B H81    1 
HETATM 10300 H  H92    . LMT K 5 .   ? -9.53400  -37.62900 -7.77200  1.000 160.17000 ? 803 LMT B H92    1 
HETATM 10301 H  H91    . LMT K 5 .   ? -10.08500 -38.49200 -9.21100  1.000 160.17000 ? 803 LMT B H91    1 
HETATM 10302 H  H102   . LMT K 5 .   ? -11.84500 -36.99600 -8.56000  1.000 157.92000 ? 803 LMT B H102   1 
HETATM 10303 H  H101   . LMT K 5 .   ? -11.10400 -36.32900 -10.01800 1.000 157.92000 ? 803 LMT B H101   1 
HETATM 10304 H  H112   . LMT K 5 .   ? -11.14200 -35.28000 -7.25200  1.000 131.93000 ? 803 LMT B H112   1 
HETATM 10305 H  H111   . LMT K 5 .   ? -9.58500  -35.15500 -8.07600  1.000 131.93000 ? 803 LMT B H111   1 
HETATM 10306 H  H123   . LMT K 5 .   ? -11.11700 -33.14300 -8.29600  1.000 109.88000 ? 803 LMT B H123   1 
HETATM 10307 H  H122   . LMT K 5 .   ? -12.17000 -34.15800 -9.29800  1.000 109.88000 ? 803 LMT B H122   1 
HETATM 10308 H  H121   . LMT K 5 .   ? -10.51100 -33.81300 -9.82200  1.000 109.88000 ? 803 LMT B H121   1 
HETATM 10309 MG MG     . MG  L 3 .   ? 16.86700  -21.36800 -1.10300  1.000 88.31000  ? 804 MG  B MG     1 
HETATM 10310 MG MG     . MG  M 3 .   ? 19.82800  -19.29200 4.72600   1.000 92.72000  ? 805 MG  B MG     1 
HETATM 10311 MG MG     . MG  N 3 .   ? 14.54700  -20.99000 3.35200   1.000 101.27000 ? 806 MG  B MG     1 
HETATM 10312 MG MG     . MG  O 3 .   ? 22.68900  -19.00200 0.46900   1.000 110.51000 ? 807 MG  B MG     1 
HETATM 10313 MG MG     . MG  P 3 .   ? 18.99900  -21.71600 -1.66500  1.000 88.93000  ? 808 MG  B MG     1 
HETATM 10314 CA CA     . CA  Q 4 .   ? 18.56100  -16.82400 5.21000   1.000 98.35000  ? 809 CA  B CA     1 
HETATM 10315 O  O      . HOH R 6 .   ? 30.97600  -9.26200  30.06600  1.000 87.17000  ? 901 HOH A O      1 
HETATM 10316 O  O      . HOH R 6 .   ? 29.44800  -7.90200  36.23900  1.000 61.57000  ? 902 HOH A O      1 
HETATM 10317 O  O      . HOH S 6 .   ? 14.71200  -17.61800 -1.10300  1.000 118.07000 ? 901 HOH B O      1 
HETATM 10318 O  O      . HOH S 6 .   ? -15.88000 -30.01800 25.81400  1.000 45.99000  ? 902 HOH B O      1 
HETATM 10319 O  O      . HOH S 6 .   ? 12.76900  -18.49100 3.88500   1.000 73.17000  ? 903 HOH B O      1 
HETATM 10320 O  O      . HOH S 6 .   ? 10.90600  -21.36100 5.33700   1.000 61.37000  ? 904 HOH B O      1 
# 
