data_9J6N
# 
_entry.id   9J6N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9J6N         pdb_00009j6n 10.2210/pdb9j6n/pdb 
WWPDB D_1300050469 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-25 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J6N 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              asfushi@mail.ecc.u-tokyo.ac.jp 
_pdbx_contact_author.name_first         Shinya 
_pdbx_contact_author.name_last          Fushinobu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1346-6435 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fujio, N.'     1 0000-0002-7909-1501 
'Yamada, C.'    2 0000-0003-0606-3996 
'Takegawa, K.'  3 0000-0003-3477-7216 
'Fushinobu, S.' 4 0000-0003-1346-6435 
# 
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 
? ? ? ? ? ? ? NE ? ? primary 'Febs Lett.'    FEBLAL 0165 0014-5793 ? ? 598 ? 2866     2875 
;Crystal structure of beta-d-galactofuranosidase from Streptomyces sp. JHA19 in complex with an inhibitor provides insights into substrate specificity.
;
2024 ? 10.1002/1873-3468.15056      39543437 ? ? 
? ? ? ? ? ? ? US ? ? 1       'PLoS One'      ?      ?    1932-6203 ? ? 10  ? e0137230 ?    
'Identification and Characterization of a Novel Galactofuranose-Specific beta-D-Galactofuranosidase from Streptomyces Species.' 
2015 ? 10.1007/s10529-014-1493-6    26340350 ? ? 
? ? ? ? ? ? ? NE ? ? 2       'Carbohydr Res' CRBRAT 0156 1873-426X ? ? 480 ? 35       41   
'Galactofuranosidase from JHA 19 Streptomyces sp.: subcloning and biochemical characterization.' 2019 ? 
10.1016/j.carres.2019.05.011 31174175 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fujio, N.'      1  ? 
primary 'Yamada, C.'     2  ? 
primary 'Kashima, T.'    3  ? 
primary 'Matsunaga, E.'  4  ? 
primary 'Nash, R.J.'     5  ? 
primary 'Takegawa, K.'   6  ? 
primary 'Fushinobu, S.'  7  ? 
1       'Matsunaga, E.'  8  ? 
1       'Higuchi, Y.'    9  ? 
1       'Mori, K.'       10 ? 
1       'Yairo, N.'      11 ? 
1       'Oka, T.'        12 ? 
1       'Shinozuka, S.'  13 ? 
1       'Tashiro, K.'    14 ? 
1       'Izumi, M.'      15 ? 
1       'Kuhara, S.'     16 ? 
1       'Takegawa, K.'   17 ? 
2       'Senicar, M.'    18 ? 
2       'Legentil, L.'   19 ? 
2       'Ferrieres, V.'  20 ? 
2       'Eliseeva, S.V.' 21 ? 
2       'Petoud, S.'     22 ? 
2       'Takegawa, K.'   23 ? 
2       'Lafite, P.'     24 ? 
2       'Daniellou, R.'  25 ? 
# 
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 'Beta-D-galactofuranosidase 2'                                               67070.711 2   ? ? ? ? 
2 non-polymer syn 'HEXAETHYLENE GLYCOL'                                                        282.331   1   ? ? ? ? 
3 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                                              118.174   3   ? ? ? ? 
4 non-polymer syn '(2~{S},3~{S},4~{S})-2-[(1~{S})-1,2-bis(oxidanyl)ethyl]pyrrolidine-3,4-diol' 163.172   2   ? ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                                              24.305    2   ? ? ? ? 
6 non-polymer syn 'TETRAETHYLENE GLYCOL'                                                       194.226   1   ? ? ? ? 
7 water       nat water                                                                        18.015    797 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSAALEVLFQGPAPRAWTPKPSPMTTPWTDQVPVDNPLPEYPRPQLTRPDWANLNGIWDFAVTSANAGQPA
TFPEQIRVPFVAESALSGIQRKITQNDKLWYKRTFTVPSNWNGRRVQLNFGASDWRTTVWVNGRQAGAVHSGGYDAFSYD
VTDLLTAGTNTLVVSVWDPTETGTQAVGKQRIRDVAPHPGGGILYTAASGIWQTVWLEPTAAAHVTRLDLVPDPANSRLK
VTVRGAGISGHQARVTVSTGGTTVGTATGPVGTEFTVPVPNPRLWTPEDPFLYDVRADPLSGGTTVDSVGSYTGMRTIAL
ASVGGHQRPVLNGKFVFQTGTLDQGYWPDGIYTAPTDAALRHDLQKHKDLGFNMVRKHIKVEPQRWFYWADRLGLLVWQD
MPNMERTPDAAARTQWEAEYDRIIDQHRSSPSLVLWVNQNEGWGQYDQARLADKVKAYDPTRLVDNMSGVNCCGAVDGGN
GDVVDHHVYVGPGTTVPSATRAAVLGEFGGLGFKVAGHEWYPGGGFSYEDQPDLAHLNNRFVGLIDAIREVRMPRGLSAS
VYTEITDVENEVNGLLTYDRQVVKVDEARVRAANRALIDASRGTTAPLTLPV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSAALEVLFQGPAPRAWTPKPSPMTTPWTDQVPVDNPLPEYPRPQLTRPDWANLNGIWDFAVTSANAGQPA
TFPEQIRVPFVAESALSGIQRKITQNDKLWYKRTFTVPSNWNGRRVQLNFGASDWRTTVWVNGRQAGAVHSGGYDAFSYD
VTDLLTAGTNTLVVSVWDPTETGTQAVGKQRIRDVAPHPGGGILYTAASGIWQTVWLEPTAAAHVTRLDLVPDPANSRLK
VTVRGAGISGHQARVTVSTGGTTVGTATGPVGTEFTVPVPNPRLWTPEDPFLYDVRADPLSGGTTVDSVGSYTGMRTIAL
ASVGGHQRPVLNGKFVFQTGTLDQGYWPDGIYTAPTDAALRHDLQKHKDLGFNMVRKHIKVEPQRWFYWADRLGLLVWQD
MPNMERTPDAAARTQWEAEYDRIIDQHRSSPSLVLWVNQNEGWGQYDQARLADKVKAYDPTRLVDNMSGVNCCGAVDGGN
GDVVDHHVYVGPGTTVPSATRAAVLGEFGGLGFKVAGHEWYPGGGFSYEDQPDLAHLNNRFVGLIDAIREVRMPRGLSAS
VYTEITDVENEVNGLLTYDRQVVKVDEARVRAANRALIDASRGTTAPLTLPV
;
_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 'HEXAETHYLENE GLYCOL'                                                        P6G   
3 '(4S)-2-METHYL-2,4-PENTANEDIOL'                                              MPD   
4 '(2~{S},3~{S},4~{S})-2-[(1~{S})-1,2-bis(oxidanyl)ethyl]pyrrolidine-3,4-diol' A1L3Z 
5 'MAGNESIUM ION'                                                              MG    
6 'TETRAETHYLENE GLYCOL'                                                       PG4   
7 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   GLY n 
1 3   SER 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  SER n 
1 12  ALA n 
1 13  ALA n 
1 14  LEU n 
1 15  GLU n 
1 16  VAL n 
1 17  LEU n 
1 18  PHE n 
1 19  GLN n 
1 20  GLY n 
1 21  PRO n 
1 22  ALA n 
1 23  PRO n 
1 24  ARG n 
1 25  ALA n 
1 26  TRP n 
1 27  THR n 
1 28  PRO n 
1 29  LYS n 
1 30  PRO n 
1 31  SER n 
1 32  PRO n 
1 33  MET n 
1 34  THR n 
1 35  THR n 
1 36  PRO n 
1 37  TRP n 
1 38  THR n 
1 39  ASP n 
1 40  GLN n 
1 41  VAL n 
1 42  PRO n 
1 43  VAL n 
1 44  ASP n 
1 45  ASN n 
1 46  PRO n 
1 47  LEU n 
1 48  PRO n 
1 49  GLU n 
1 50  TYR n 
1 51  PRO n 
1 52  ARG n 
1 53  PRO n 
1 54  GLN n 
1 55  LEU n 
1 56  THR n 
1 57  ARG n 
1 58  PRO n 
1 59  ASP n 
1 60  TRP n 
1 61  ALA n 
1 62  ASN n 
1 63  LEU n 
1 64  ASN n 
1 65  GLY n 
1 66  ILE n 
1 67  TRP n 
1 68  ASP n 
1 69  PHE n 
1 70  ALA n 
1 71  VAL n 
1 72  THR n 
1 73  SER n 
1 74  ALA n 
1 75  ASN n 
1 76  ALA n 
1 77  GLY n 
1 78  GLN n 
1 79  PRO n 
1 80  ALA n 
1 81  THR n 
1 82  PHE n 
1 83  PRO n 
1 84  GLU n 
1 85  GLN n 
1 86  ILE n 
1 87  ARG n 
1 88  VAL n 
1 89  PRO n 
1 90  PHE n 
1 91  VAL n 
1 92  ALA n 
1 93  GLU n 
1 94  SER n 
1 95  ALA n 
1 96  LEU n 
1 97  SER n 
1 98  GLY n 
1 99  ILE n 
1 100 GLN n 
1 101 ARG n 
1 102 LYS n 
1 103 ILE n 
1 104 THR n 
1 105 GLN n 
1 106 ASN n 
1 107 ASP n 
1 108 LYS n 
1 109 LEU n 
1 110 TRP n 
1 111 TYR n 
1 112 LYS n 
1 113 ARG n 
1 114 THR n 
1 115 PHE n 
1 116 THR n 
1 117 VAL n 
1 118 PRO n 
1 119 SER n 
1 120 ASN n 
1 121 TRP n 
1 122 ASN n 
1 123 GLY n 
1 124 ARG n 
1 125 ARG n 
1 126 VAL n 
1 127 GLN n 
1 128 LEU n 
1 129 ASN n 
1 130 PHE n 
1 131 GLY n 
1 132 ALA n 
1 133 SER n 
1 134 ASP n 
1 135 TRP n 
1 136 ARG n 
1 137 THR n 
1 138 THR n 
1 139 VAL n 
1 140 TRP n 
1 141 VAL n 
1 142 ASN n 
1 143 GLY n 
1 144 ARG n 
1 145 GLN n 
1 146 ALA n 
1 147 GLY n 
1 148 ALA n 
1 149 VAL n 
1 150 HIS n 
1 151 SER n 
1 152 GLY n 
1 153 GLY n 
1 154 TYR n 
1 155 ASP n 
1 156 ALA n 
1 157 PHE n 
1 158 SER n 
1 159 TYR n 
1 160 ASP n 
1 161 VAL n 
1 162 THR n 
1 163 ASP n 
1 164 LEU n 
1 165 LEU n 
1 166 THR n 
1 167 ALA n 
1 168 GLY n 
1 169 THR n 
1 170 ASN n 
1 171 THR n 
1 172 LEU n 
1 173 VAL n 
1 174 VAL n 
1 175 SER n 
1 176 VAL n 
1 177 TRP n 
1 178 ASP n 
1 179 PRO n 
1 180 THR n 
1 181 GLU n 
1 182 THR n 
1 183 GLY n 
1 184 THR n 
1 185 GLN n 
1 186 ALA n 
1 187 VAL n 
1 188 GLY n 
1 189 LYS n 
1 190 GLN n 
1 191 ARG n 
1 192 ILE n 
1 193 ARG n 
1 194 ASP n 
1 195 VAL n 
1 196 ALA n 
1 197 PRO n 
1 198 HIS n 
1 199 PRO n 
1 200 GLY n 
1 201 GLY n 
1 202 GLY n 
1 203 ILE n 
1 204 LEU n 
1 205 TYR n 
1 206 THR n 
1 207 ALA n 
1 208 ALA n 
1 209 SER n 
1 210 GLY n 
1 211 ILE n 
1 212 TRP n 
1 213 GLN n 
1 214 THR n 
1 215 VAL n 
1 216 TRP n 
1 217 LEU n 
1 218 GLU n 
1 219 PRO n 
1 220 THR n 
1 221 ALA n 
1 222 ALA n 
1 223 ALA n 
1 224 HIS n 
1 225 VAL n 
1 226 THR n 
1 227 ARG n 
1 228 LEU n 
1 229 ASP n 
1 230 LEU n 
1 231 VAL n 
1 232 PRO n 
1 233 ASP n 
1 234 PRO n 
1 235 ALA n 
1 236 ASN n 
1 237 SER n 
1 238 ARG n 
1 239 LEU n 
1 240 LYS n 
1 241 VAL n 
1 242 THR n 
1 243 VAL n 
1 244 ARG n 
1 245 GLY n 
1 246 ALA n 
1 247 GLY n 
1 248 ILE n 
1 249 SER n 
1 250 GLY n 
1 251 HIS n 
1 252 GLN n 
1 253 ALA n 
1 254 ARG n 
1 255 VAL n 
1 256 THR n 
1 257 VAL n 
1 258 SER n 
1 259 THR n 
1 260 GLY n 
1 261 GLY n 
1 262 THR n 
1 263 THR n 
1 264 VAL n 
1 265 GLY n 
1 266 THR n 
1 267 ALA n 
1 268 THR n 
1 269 GLY n 
1 270 PRO n 
1 271 VAL n 
1 272 GLY n 
1 273 THR n 
1 274 GLU n 
1 275 PHE n 
1 276 THR n 
1 277 VAL n 
1 278 PRO n 
1 279 VAL n 
1 280 PRO n 
1 281 ASN n 
1 282 PRO n 
1 283 ARG n 
1 284 LEU n 
1 285 TRP n 
1 286 THR n 
1 287 PRO n 
1 288 GLU n 
1 289 ASP n 
1 290 PRO n 
1 291 PHE n 
1 292 LEU n 
1 293 TYR n 
1 294 ASP n 
1 295 VAL n 
1 296 ARG n 
1 297 ALA n 
1 298 ASP n 
1 299 PRO n 
1 300 LEU n 
1 301 SER n 
1 302 GLY n 
1 303 GLY n 
1 304 THR n 
1 305 THR n 
1 306 VAL n 
1 307 ASP n 
1 308 SER n 
1 309 VAL n 
1 310 GLY n 
1 311 SER n 
1 312 TYR n 
1 313 THR n 
1 314 GLY n 
1 315 MET n 
1 316 ARG n 
1 317 THR n 
1 318 ILE n 
1 319 ALA n 
1 320 LEU n 
1 321 ALA n 
1 322 SER n 
1 323 VAL n 
1 324 GLY n 
1 325 GLY n 
1 326 HIS n 
1 327 GLN n 
1 328 ARG n 
1 329 PRO n 
1 330 VAL n 
1 331 LEU n 
1 332 ASN n 
1 333 GLY n 
1 334 LYS n 
1 335 PHE n 
1 336 VAL n 
1 337 PHE n 
1 338 GLN n 
1 339 THR n 
1 340 GLY n 
1 341 THR n 
1 342 LEU n 
1 343 ASP n 
1 344 GLN n 
1 345 GLY n 
1 346 TYR n 
1 347 TRP n 
1 348 PRO n 
1 349 ASP n 
1 350 GLY n 
1 351 ILE n 
1 352 TYR n 
1 353 THR n 
1 354 ALA n 
1 355 PRO n 
1 356 THR n 
1 357 ASP n 
1 358 ALA n 
1 359 ALA n 
1 360 LEU n 
1 361 ARG n 
1 362 HIS n 
1 363 ASP n 
1 364 LEU n 
1 365 GLN n 
1 366 LYS n 
1 367 HIS n 
1 368 LYS n 
1 369 ASP n 
1 370 LEU n 
1 371 GLY n 
1 372 PHE n 
1 373 ASN n 
1 374 MET n 
1 375 VAL n 
1 376 ARG n 
1 377 LYS n 
1 378 HIS n 
1 379 ILE n 
1 380 LYS n 
1 381 VAL n 
1 382 GLU n 
1 383 PRO n 
1 384 GLN n 
1 385 ARG n 
1 386 TRP n 
1 387 PHE n 
1 388 TYR n 
1 389 TRP n 
1 390 ALA n 
1 391 ASP n 
1 392 ARG n 
1 393 LEU n 
1 394 GLY n 
1 395 LEU n 
1 396 LEU n 
1 397 VAL n 
1 398 TRP n 
1 399 GLN n 
1 400 ASP n 
1 401 MET n 
1 402 PRO n 
1 403 ASN n 
1 404 MET n 
1 405 GLU n 
1 406 ARG n 
1 407 THR n 
1 408 PRO n 
1 409 ASP n 
1 410 ALA n 
1 411 ALA n 
1 412 ALA n 
1 413 ARG n 
1 414 THR n 
1 415 GLN n 
1 416 TRP n 
1 417 GLU n 
1 418 ALA n 
1 419 GLU n 
1 420 TYR n 
1 421 ASP n 
1 422 ARG n 
1 423 ILE n 
1 424 ILE n 
1 425 ASP n 
1 426 GLN n 
1 427 HIS n 
1 428 ARG n 
1 429 SER n 
1 430 SER n 
1 431 PRO n 
1 432 SER n 
1 433 LEU n 
1 434 VAL n 
1 435 LEU n 
1 436 TRP n 
1 437 VAL n 
1 438 ASN n 
1 439 GLN n 
1 440 ASN n 
1 441 GLU n 
1 442 GLY n 
1 443 TRP n 
1 444 GLY n 
1 445 GLN n 
1 446 TYR n 
1 447 ASP n 
1 448 GLN n 
1 449 ALA n 
1 450 ARG n 
1 451 LEU n 
1 452 ALA n 
1 453 ASP n 
1 454 LYS n 
1 455 VAL n 
1 456 LYS n 
1 457 ALA n 
1 458 TYR n 
1 459 ASP n 
1 460 PRO n 
1 461 THR n 
1 462 ARG n 
1 463 LEU n 
1 464 VAL n 
1 465 ASP n 
1 466 ASN n 
1 467 MET n 
1 468 SER n 
1 469 GLY n 
1 470 VAL n 
1 471 ASN n 
1 472 CYS n 
1 473 CYS n 
1 474 GLY n 
1 475 ALA n 
1 476 VAL n 
1 477 ASP n 
1 478 GLY n 
1 479 GLY n 
1 480 ASN n 
1 481 GLY n 
1 482 ASP n 
1 483 VAL n 
1 484 VAL n 
1 485 ASP n 
1 486 HIS n 
1 487 HIS n 
1 488 VAL n 
1 489 TYR n 
1 490 VAL n 
1 491 GLY n 
1 492 PRO n 
1 493 GLY n 
1 494 THR n 
1 495 THR n 
1 496 VAL n 
1 497 PRO n 
1 498 SER n 
1 499 ALA n 
1 500 THR n 
1 501 ARG n 
1 502 ALA n 
1 503 ALA n 
1 504 VAL n 
1 505 LEU n 
1 506 GLY n 
1 507 GLU n 
1 508 PHE n 
1 509 GLY n 
1 510 GLY n 
1 511 LEU n 
1 512 GLY n 
1 513 PHE n 
1 514 LYS n 
1 515 VAL n 
1 516 ALA n 
1 517 GLY n 
1 518 HIS n 
1 519 GLU n 
1 520 TRP n 
1 521 TYR n 
1 522 PRO n 
1 523 GLY n 
1 524 GLY n 
1 525 GLY n 
1 526 PHE n 
1 527 SER n 
1 528 TYR n 
1 529 GLU n 
1 530 ASP n 
1 531 GLN n 
1 532 PRO n 
1 533 ASP n 
1 534 LEU n 
1 535 ALA n 
1 536 HIS n 
1 537 LEU n 
1 538 ASN n 
1 539 ASN n 
1 540 ARG n 
1 541 PHE n 
1 542 VAL n 
1 543 GLY n 
1 544 LEU n 
1 545 ILE n 
1 546 ASP n 
1 547 ALA n 
1 548 ILE n 
1 549 ARG n 
1 550 GLU n 
1 551 VAL n 
1 552 ARG n 
1 553 MET n 
1 554 PRO n 
1 555 ARG n 
1 556 GLY n 
1 557 LEU n 
1 558 SER n 
1 559 ALA n 
1 560 SER n 
1 561 VAL n 
1 562 TYR n 
1 563 THR n 
1 564 GLU n 
1 565 ILE n 
1 566 THR n 
1 567 ASP n 
1 568 VAL n 
1 569 GLU n 
1 570 ASN n 
1 571 GLU n 
1 572 VAL n 
1 573 ASN n 
1 574 GLY n 
1 575 LEU n 
1 576 LEU n 
1 577 THR n 
1 578 TYR n 
1 579 ASP n 
1 580 ARG n 
1 581 GLN n 
1 582 VAL n 
1 583 VAL n 
1 584 LYS n 
1 585 VAL n 
1 586 ASP n 
1 587 GLU n 
1 588 ALA n 
1 589 ARG n 
1 590 VAL n 
1 591 ARG n 
1 592 ALA n 
1 593 ALA n 
1 594 ASN n 
1 595 ARG n 
1 596 ALA n 
1 597 LEU n 
1 598 ILE n 
1 599 ASP n 
1 600 ALA n 
1 601 SER n 
1 602 ARG n 
1 603 GLY n 
1 604 THR n 
1 605 THR n 
1 606 ALA n 
1 607 PRO n 
1 608 LEU n 
1 609 THR n 
1 610 LEU n 
1 611 PRO n 
1 612 VAL 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                   612 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Streptomyces sp. JHA19' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1577588 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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              CodonPlus-RIL-X 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET50b 
_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 
A1L3Z non-polymer         . '(2~{S},3~{S},4~{S})-2-[(1~{S})-1,2-bis(oxidanyl)ethyl]pyrrolidine-3,4-diol' ? 'C6 H13 N O4'    
163.172 
ALA   'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'     89.093 
ARG   'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'     75.067 
HIS   'L-peptide linking' y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                        ? 'H2 O'           18.015 
ILE   'L-peptide linking' y ISOLEUCINE                                                                   ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                       ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'  
149.211 
MG    non-polymer         . 'MAGNESIUM ION'                                                              ? 'Mg 2'           24.305 
MPD   non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL'                                              ? 'C6 H14 O2'      
118.174 
P6G   non-polymer         . 'HEXAETHYLENE GLYCOL'                                                        
'POLYETHYLENE GLYCOL PEG400' 'C12 H26 O7'     282.331 
PG4   non-polymer         . 'TETRAETHYLENE GLYCOL'                                                       ? 'C8 H18 O5'      
194.226 
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   24  ?   ?   ?   A . n 
A 1 2   GLY 2   25  ?   ?   ?   A . n 
A 1 3   SER 3   26  ?   ?   ?   A . n 
A 1 4   SER 4   27  ?   ?   ?   A . n 
A 1 5   HIS 5   28  ?   ?   ?   A . n 
A 1 6   HIS 6   29  ?   ?   ?   A . n 
A 1 7   HIS 7   30  ?   ?   ?   A . n 
A 1 8   HIS 8   31  ?   ?   ?   A . n 
A 1 9   HIS 9   32  ?   ?   ?   A . n 
A 1 10  HIS 10  33  ?   ?   ?   A . n 
A 1 11  SER 11  34  ?   ?   ?   A . n 
A 1 12  ALA 12  35  ?   ?   ?   A . n 
A 1 13  ALA 13  36  ?   ?   ?   A . n 
A 1 14  LEU 14  37  ?   ?   ?   A . n 
A 1 15  GLU 15  38  ?   ?   ?   A . n 
A 1 16  VAL 16  39  ?   ?   ?   A . n 
A 1 17  LEU 17  40  ?   ?   ?   A . n 
A 1 18  PHE 18  41  ?   ?   ?   A . n 
A 1 19  GLN 19  42  ?   ?   ?   A . n 
A 1 20  GLY 20  43  ?   ?   ?   A . n 
A 1 21  PRO 21  44  ?   ?   ?   A . n 
A 1 22  ALA 22  45  45  ALA ALA A . n 
A 1 23  PRO 23  46  46  PRO PRO A . n 
A 1 24  ARG 24  47  47  ARG ARG A . n 
A 1 25  ALA 25  48  48  ALA ALA A . n 
A 1 26  TRP 26  49  49  TRP TRP A . n 
A 1 27  THR 27  50  50  THR THR A . n 
A 1 28  PRO 28  51  51  PRO PRO A . n 
A 1 29  LYS 29  52  52  LYS LYS A . n 
A 1 30  PRO 30  53  53  PRO PRO A . n 
A 1 31  SER 31  54  54  SER SER A . n 
A 1 32  PRO 32  55  55  PRO PRO A . n 
A 1 33  MET 33  56  56  MET MET A . n 
A 1 34  THR 34  57  57  THR THR A . n 
A 1 35  THR 35  58  58  THR THR A . n 
A 1 36  PRO 36  59  59  PRO PRO A . n 
A 1 37  TRP 37  60  60  TRP TRP A . n 
A 1 38  THR 38  61  61  THR THR A . n 
A 1 39  ASP 39  62  62  ASP ASP A . n 
A 1 40  GLN 40  63  63  GLN GLN A . n 
A 1 41  VAL 41  64  64  VAL VAL A . n 
A 1 42  PRO 42  65  65  PRO PRO A . n 
A 1 43  VAL 43  66  66  VAL VAL A . n 
A 1 44  ASP 44  67  67  ASP ASP A . n 
A 1 45  ASN 45  68  68  ASN ASN A . n 
A 1 46  PRO 46  69  69  PRO PRO A . n 
A 1 47  LEU 47  70  70  LEU LEU A . n 
A 1 48  PRO 48  71  71  PRO PRO A . n 
A 1 49  GLU 49  72  72  GLU GLU A . n 
A 1 50  TYR 50  73  73  TYR TYR A . n 
A 1 51  PRO 51  74  74  PRO PRO A . n 
A 1 52  ARG 52  75  75  ARG ARG A . n 
A 1 53  PRO 53  76  76  PRO PRO A . n 
A 1 54  GLN 54  77  77  GLN GLN A . n 
A 1 55  LEU 55  78  78  LEU LEU A . n 
A 1 56  THR 56  79  79  THR THR A . n 
A 1 57  ARG 57  80  80  ARG ARG A . n 
A 1 58  PRO 58  81  81  PRO PRO A . n 
A 1 59  ASP 59  82  82  ASP ASP A . n 
A 1 60  TRP 60  83  83  TRP TRP A . n 
A 1 61  ALA 61  84  84  ALA ALA A . n 
A 1 62  ASN 62  85  85  ASN ASN A . n 
A 1 63  LEU 63  86  86  LEU LEU A . n 
A 1 64  ASN 64  87  87  ASN ASN A . n 
A 1 65  GLY 65  88  88  GLY GLY A . n 
A 1 66  ILE 66  89  89  ILE ILE A . n 
A 1 67  TRP 67  90  90  TRP TRP A . n 
A 1 68  ASP 68  91  91  ASP ASP A . n 
A 1 69  PHE 69  92  92  PHE PHE A . n 
A 1 70  ALA 70  93  93  ALA ALA A . n 
A 1 71  VAL 71  94  94  VAL VAL A . n 
A 1 72  THR 72  95  95  THR THR A . n 
A 1 73  SER 73  96  96  SER SER A . n 
A 1 74  ALA 74  97  97  ALA ALA A . n 
A 1 75  ASN 75  98  98  ASN ASN A . n 
A 1 76  ALA 76  99  99  ALA ALA A . n 
A 1 77  GLY 77  100 100 GLY GLY A . n 
A 1 78  GLN 78  101 101 GLN GLN A . n 
A 1 79  PRO 79  102 102 PRO PRO A . n 
A 1 80  ALA 80  103 103 ALA ALA A . n 
A 1 81  THR 81  104 104 THR THR A . n 
A 1 82  PHE 82  105 105 PHE PHE A . n 
A 1 83  PRO 83  106 106 PRO PRO A . n 
A 1 84  GLU 84  107 107 GLU GLU A . n 
A 1 85  GLN 85  108 108 GLN GLN A . n 
A 1 86  ILE 86  109 109 ILE ILE A . n 
A 1 87  ARG 87  110 110 ARG ARG A . n 
A 1 88  VAL 88  111 111 VAL VAL A . n 
A 1 89  PRO 89  112 112 PRO PRO A . n 
A 1 90  PHE 90  113 113 PHE PHE A . n 
A 1 91  VAL 91  114 114 VAL VAL A . n 
A 1 92  ALA 92  115 115 ALA ALA A . n 
A 1 93  GLU 93  116 116 GLU GLU A . n 
A 1 94  SER 94  117 117 SER SER A . n 
A 1 95  ALA 95  118 118 ALA ALA A . n 
A 1 96  LEU 96  119 119 LEU LEU A . n 
A 1 97  SER 97  120 120 SER SER A . n 
A 1 98  GLY 98  121 121 GLY GLY A . n 
A 1 99  ILE 99  122 122 ILE ILE A . n 
A 1 100 GLN 100 123 123 GLN GLN A . n 
A 1 101 ARG 101 124 124 ARG ARG A . n 
A 1 102 LYS 102 125 125 LYS LYS A . n 
A 1 103 ILE 103 126 126 ILE ILE A . n 
A 1 104 THR 104 127 127 THR THR A . n 
A 1 105 GLN 105 128 128 GLN GLN A . n 
A 1 106 ASN 106 129 129 ASN ASN A . n 
A 1 107 ASP 107 130 130 ASP ASP A . n 
A 1 108 LYS 108 131 131 LYS LYS A . n 
A 1 109 LEU 109 132 132 LEU LEU A . n 
A 1 110 TRP 110 133 133 TRP TRP A . n 
A 1 111 TYR 111 134 134 TYR TYR A . n 
A 1 112 LYS 112 135 135 LYS LYS A . n 
A 1 113 ARG 113 136 136 ARG ARG A . n 
A 1 114 THR 114 137 137 THR THR A . n 
A 1 115 PHE 115 138 138 PHE PHE A . n 
A 1 116 THR 116 139 139 THR THR A . n 
A 1 117 VAL 117 140 140 VAL VAL A . n 
A 1 118 PRO 118 141 141 PRO PRO A . n 
A 1 119 SER 119 142 142 SER SER A . n 
A 1 120 ASN 120 143 143 ASN ASN A . n 
A 1 121 TRP 121 144 144 TRP TRP A . n 
A 1 122 ASN 122 145 145 ASN ASN A . n 
A 1 123 GLY 123 146 146 GLY GLY A . n 
A 1 124 ARG 124 147 147 ARG ARG A . n 
A 1 125 ARG 125 148 148 ARG ARG A . n 
A 1 126 VAL 126 149 149 VAL VAL A . n 
A 1 127 GLN 127 150 150 GLN GLN A . n 
A 1 128 LEU 128 151 151 LEU LEU A . n 
A 1 129 ASN 129 152 152 ASN ASN A . n 
A 1 130 PHE 130 153 153 PHE PHE A . n 
A 1 131 GLY 131 154 154 GLY GLY A . n 
A 1 132 ALA 132 155 155 ALA ALA A . n 
A 1 133 SER 133 156 156 SER SER A . n 
A 1 134 ASP 134 157 157 ASP ASP A . n 
A 1 135 TRP 135 158 158 TRP TRP A . n 
A 1 136 ARG 136 159 159 ARG ARG A . n 
A 1 137 THR 137 160 160 THR THR A . n 
A 1 138 THR 138 161 161 THR THR A . n 
A 1 139 VAL 139 162 162 VAL VAL A . n 
A 1 140 TRP 140 163 163 TRP TRP A . n 
A 1 141 VAL 141 164 164 VAL VAL A . n 
A 1 142 ASN 142 165 165 ASN ASN A . n 
A 1 143 GLY 143 166 166 GLY GLY A . n 
A 1 144 ARG 144 167 167 ARG ARG A . n 
A 1 145 GLN 145 168 168 GLN GLN A . n 
A 1 146 ALA 146 169 169 ALA ALA A . n 
A 1 147 GLY 147 170 170 GLY GLY A . n 
A 1 148 ALA 148 171 171 ALA ALA A . n 
A 1 149 VAL 149 172 172 VAL VAL A . n 
A 1 150 HIS 150 173 173 HIS HIS A . n 
A 1 151 SER 151 174 174 SER SER A . n 
A 1 152 GLY 152 175 175 GLY GLY A . n 
A 1 153 GLY 153 176 176 GLY GLY A . n 
A 1 154 TYR 154 177 177 TYR TYR A . n 
A 1 155 ASP 155 178 178 ASP ASP A . n 
A 1 156 ALA 156 179 179 ALA ALA A . n 
A 1 157 PHE 157 180 180 PHE PHE A . n 
A 1 158 SER 158 181 181 SER SER A . n 
A 1 159 TYR 159 182 182 TYR TYR A . n 
A 1 160 ASP 160 183 183 ASP ASP A . n 
A 1 161 VAL 161 184 184 VAL VAL A . n 
A 1 162 THR 162 185 185 THR THR A . n 
A 1 163 ASP 163 186 186 ASP ASP A . n 
A 1 164 LEU 164 187 187 LEU LEU A . n 
A 1 165 LEU 165 188 188 LEU LEU A . n 
A 1 166 THR 166 189 189 THR THR A . n 
A 1 167 ALA 167 190 190 ALA ALA A . n 
A 1 168 GLY 168 191 191 GLY GLY A . n 
A 1 169 THR 169 192 192 THR THR A . n 
A 1 170 ASN 170 193 193 ASN ASN A . n 
A 1 171 THR 171 194 194 THR THR A . n 
A 1 172 LEU 172 195 195 LEU LEU A . n 
A 1 173 VAL 173 196 196 VAL VAL A . n 
A 1 174 VAL 174 197 197 VAL VAL A . n 
A 1 175 SER 175 198 198 SER SER A . n 
A 1 176 VAL 176 199 199 VAL VAL A . n 
A 1 177 TRP 177 200 200 TRP TRP A . n 
A 1 178 ASP 178 201 201 ASP ASP A . n 
A 1 179 PRO 179 202 202 PRO PRO A . n 
A 1 180 THR 180 203 203 THR THR A . n 
A 1 181 GLU 181 204 204 GLU GLU A . n 
A 1 182 THR 182 205 205 THR THR A . n 
A 1 183 GLY 183 206 206 GLY GLY A . n 
A 1 184 THR 184 207 207 THR THR A . n 
A 1 185 GLN 185 208 208 GLN GLN A . n 
A 1 186 ALA 186 209 209 ALA ALA A . n 
A 1 187 VAL 187 210 210 VAL VAL A . n 
A 1 188 GLY 188 211 211 GLY GLY A . n 
A 1 189 LYS 189 212 212 LYS LYS A . n 
A 1 190 GLN 190 213 213 GLN GLN A . n 
A 1 191 ARG 191 214 214 ARG ARG A . n 
A 1 192 ILE 192 215 215 ILE ILE A . n 
A 1 193 ARG 193 216 216 ARG ARG A . n 
A 1 194 ASP 194 217 217 ASP ASP A . n 
A 1 195 VAL 195 218 218 VAL VAL A . n 
A 1 196 ALA 196 219 219 ALA ALA A . n 
A 1 197 PRO 197 220 220 PRO PRO A . n 
A 1 198 HIS 198 221 221 HIS HIS A . n 
A 1 199 PRO 199 222 222 PRO PRO A . n 
A 1 200 GLY 200 223 223 GLY GLY A . n 
A 1 201 GLY 201 224 224 GLY GLY A . n 
A 1 202 GLY 202 225 225 GLY GLY A . n 
A 1 203 ILE 203 226 226 ILE ILE A . n 
A 1 204 LEU 204 227 227 LEU LEU A . n 
A 1 205 TYR 205 228 228 TYR TYR A . n 
A 1 206 THR 206 229 229 THR THR A . n 
A 1 207 ALA 207 230 230 ALA ALA A . n 
A 1 208 ALA 208 231 231 ALA ALA A . n 
A 1 209 SER 209 232 232 SER SER A . n 
A 1 210 GLY 210 233 233 GLY GLY A . n 
A 1 211 ILE 211 234 234 ILE ILE A . n 
A 1 212 TRP 212 235 235 TRP TRP A . n 
A 1 213 GLN 213 236 236 GLN GLN A . n 
A 1 214 THR 214 237 237 THR THR A . n 
A 1 215 VAL 215 238 238 VAL VAL A . n 
A 1 216 TRP 216 239 239 TRP TRP A . n 
A 1 217 LEU 217 240 240 LEU LEU A . n 
A 1 218 GLU 218 241 241 GLU GLU A . n 
A 1 219 PRO 219 242 242 PRO PRO A . n 
A 1 220 THR 220 243 243 THR THR A . n 
A 1 221 ALA 221 244 244 ALA ALA A . n 
A 1 222 ALA 222 245 245 ALA ALA A . n 
A 1 223 ALA 223 246 246 ALA ALA A . n 
A 1 224 HIS 224 247 247 HIS HIS A . n 
A 1 225 VAL 225 248 248 VAL VAL A . n 
A 1 226 THR 226 249 249 THR THR A . n 
A 1 227 ARG 227 250 250 ARG ARG A . n 
A 1 228 LEU 228 251 251 LEU LEU A . n 
A 1 229 ASP 229 252 252 ASP ASP A . n 
A 1 230 LEU 230 253 253 LEU LEU A . n 
A 1 231 VAL 231 254 254 VAL VAL A . n 
A 1 232 PRO 232 255 255 PRO PRO A . n 
A 1 233 ASP 233 256 256 ASP ASP A . n 
A 1 234 PRO 234 257 257 PRO PRO A . n 
A 1 235 ALA 235 258 258 ALA ALA A . n 
A 1 236 ASN 236 259 259 ASN ASN A . n 
A 1 237 SER 237 260 260 SER SER A . n 
A 1 238 ARG 238 261 261 ARG ARG A . n 
A 1 239 LEU 239 262 262 LEU LEU A . n 
A 1 240 LYS 240 263 263 LYS LYS A . n 
A 1 241 VAL 241 264 264 VAL VAL A . n 
A 1 242 THR 242 265 265 THR THR A . n 
A 1 243 VAL 243 266 266 VAL VAL A . n 
A 1 244 ARG 244 267 267 ARG ARG A . n 
A 1 245 GLY 245 268 268 GLY GLY A . n 
A 1 246 ALA 246 269 269 ALA ALA A . n 
A 1 247 GLY 247 270 270 GLY GLY A . n 
A 1 248 ILE 248 271 271 ILE ILE A . n 
A 1 249 SER 249 272 272 SER SER A . n 
A 1 250 GLY 250 273 273 GLY GLY A . n 
A 1 251 HIS 251 274 274 HIS HIS A . n 
A 1 252 GLN 252 275 275 GLN GLN A . n 
A 1 253 ALA 253 276 276 ALA ALA A . n 
A 1 254 ARG 254 277 277 ARG ARG A . n 
A 1 255 VAL 255 278 278 VAL VAL A . n 
A 1 256 THR 256 279 279 THR THR A . n 
A 1 257 VAL 257 280 280 VAL VAL A . n 
A 1 258 SER 258 281 281 SER SER A . n 
A 1 259 THR 259 282 282 THR THR A . n 
A 1 260 GLY 260 283 283 GLY GLY A . n 
A 1 261 GLY 261 284 284 GLY GLY A . n 
A 1 262 THR 262 285 285 THR THR A . n 
A 1 263 THR 263 286 286 THR THR A . n 
A 1 264 VAL 264 287 287 VAL VAL A . n 
A 1 265 GLY 265 288 288 GLY GLY A . n 
A 1 266 THR 266 289 289 THR THR A . n 
A 1 267 ALA 267 290 290 ALA ALA A . n 
A 1 268 THR 268 291 291 THR THR A . n 
A 1 269 GLY 269 292 292 GLY GLY A . n 
A 1 270 PRO 270 293 293 PRO PRO A . n 
A 1 271 VAL 271 294 294 VAL VAL A . n 
A 1 272 GLY 272 295 295 GLY GLY A . n 
A 1 273 THR 273 296 296 THR THR A . n 
A 1 274 GLU 274 297 297 GLU GLU A . n 
A 1 275 PHE 275 298 298 PHE PHE A . n 
A 1 276 THR 276 299 299 THR THR A . n 
A 1 277 VAL 277 300 300 VAL VAL A . n 
A 1 278 PRO 278 301 301 PRO PRO A . n 
A 1 279 VAL 279 302 302 VAL VAL A . n 
A 1 280 PRO 280 303 303 PRO PRO A . n 
A 1 281 ASN 281 304 304 ASN ASN A . n 
A 1 282 PRO 282 305 305 PRO PRO A . n 
A 1 283 ARG 283 306 306 ARG ARG A . n 
A 1 284 LEU 284 307 307 LEU LEU A . n 
A 1 285 TRP 285 308 308 TRP TRP A . n 
A 1 286 THR 286 309 309 THR THR A . n 
A 1 287 PRO 287 310 310 PRO PRO A . n 
A 1 288 GLU 288 311 311 GLU GLU A . n 
A 1 289 ASP 289 312 312 ASP ASP A . n 
A 1 290 PRO 290 313 313 PRO PRO A . n 
A 1 291 PHE 291 314 314 PHE PHE A . n 
A 1 292 LEU 292 315 315 LEU LEU A . n 
A 1 293 TYR 293 316 316 TYR TYR A . n 
A 1 294 ASP 294 317 317 ASP ASP A . n 
A 1 295 VAL 295 318 318 VAL VAL A . n 
A 1 296 ARG 296 319 319 ARG ARG A . n 
A 1 297 ALA 297 320 320 ALA ALA A . n 
A 1 298 ASP 298 321 321 ASP ASP A . n 
A 1 299 PRO 299 322 322 PRO PRO A . n 
A 1 300 LEU 300 323 323 LEU LEU A . n 
A 1 301 SER 301 324 324 SER SER A . n 
A 1 302 GLY 302 325 325 GLY GLY A . n 
A 1 303 GLY 303 326 326 GLY GLY A . n 
A 1 304 THR 304 327 327 THR THR A . n 
A 1 305 THR 305 328 328 THR THR A . n 
A 1 306 VAL 306 329 329 VAL VAL A . n 
A 1 307 ASP 307 330 330 ASP ASP A . n 
A 1 308 SER 308 331 331 SER SER A . n 
A 1 309 VAL 309 332 332 VAL VAL A . n 
A 1 310 GLY 310 333 333 GLY GLY A . n 
A 1 311 SER 311 334 334 SER SER A . n 
A 1 312 TYR 312 335 335 TYR TYR A . n 
A 1 313 THR 313 336 336 THR THR A . n 
A 1 314 GLY 314 337 337 GLY GLY A . n 
A 1 315 MET 315 338 338 MET MET A . n 
A 1 316 ARG 316 339 339 ARG ARG A . n 
A 1 317 THR 317 340 340 THR THR A . n 
A 1 318 ILE 318 341 341 ILE ILE A . n 
A 1 319 ALA 319 342 342 ALA ALA A . n 
A 1 320 LEU 320 343 343 LEU LEU A . n 
A 1 321 ALA 321 344 344 ALA ALA A . n 
A 1 322 SER 322 345 345 SER SER A . n 
A 1 323 VAL 323 346 346 VAL VAL A . n 
A 1 324 GLY 324 347 347 GLY GLY A . n 
A 1 325 GLY 325 348 348 GLY GLY A . n 
A 1 326 HIS 326 349 349 HIS HIS A . n 
A 1 327 GLN 327 350 350 GLN GLN A . n 
A 1 328 ARG 328 351 351 ARG ARG A . n 
A 1 329 PRO 329 352 352 PRO PRO A . n 
A 1 330 VAL 330 353 353 VAL VAL A . n 
A 1 331 LEU 331 354 354 LEU LEU A . n 
A 1 332 ASN 332 355 355 ASN ASN A . n 
A 1 333 GLY 333 356 356 GLY GLY A . n 
A 1 334 LYS 334 357 357 LYS LYS A . n 
A 1 335 PHE 335 358 358 PHE PHE A . n 
A 1 336 VAL 336 359 359 VAL VAL A . n 
A 1 337 PHE 337 360 360 PHE PHE A . n 
A 1 338 GLN 338 361 361 GLN GLN A . n 
A 1 339 THR 339 362 362 THR THR A . n 
A 1 340 GLY 340 363 363 GLY GLY A . n 
A 1 341 THR 341 364 364 THR THR A . n 
A 1 342 LEU 342 365 365 LEU LEU A . n 
A 1 343 ASP 343 366 366 ASP ASP A . n 
A 1 344 GLN 344 367 367 GLN GLN A . n 
A 1 345 GLY 345 368 368 GLY GLY A . n 
A 1 346 TYR 346 369 369 TYR TYR A . n 
A 1 347 TRP 347 370 370 TRP TRP A . n 
A 1 348 PRO 348 371 371 PRO PRO A . n 
A 1 349 ASP 349 372 372 ASP ASP A . n 
A 1 350 GLY 350 373 373 GLY GLY A . n 
A 1 351 ILE 351 374 374 ILE ILE A . n 
A 1 352 TYR 352 375 375 TYR TYR A . n 
A 1 353 THR 353 376 376 THR THR A . n 
A 1 354 ALA 354 377 377 ALA ALA A . n 
A 1 355 PRO 355 378 378 PRO PRO A . n 
A 1 356 THR 356 379 379 THR THR A . n 
A 1 357 ASP 357 380 380 ASP ASP A . n 
A 1 358 ALA 358 381 381 ALA ALA A . n 
A 1 359 ALA 359 382 382 ALA ALA A . n 
A 1 360 LEU 360 383 383 LEU LEU A . n 
A 1 361 ARG 361 384 384 ARG ARG A . n 
A 1 362 HIS 362 385 385 HIS HIS A . n 
A 1 363 ASP 363 386 386 ASP ASP A . n 
A 1 364 LEU 364 387 387 LEU LEU A . n 
A 1 365 GLN 365 388 388 GLN GLN A . n 
A 1 366 LYS 366 389 389 LYS LYS A . n 
A 1 367 HIS 367 390 390 HIS HIS A . n 
A 1 368 LYS 368 391 391 LYS LYS A . n 
A 1 369 ASP 369 392 392 ASP ASP A . n 
A 1 370 LEU 370 393 393 LEU LEU A . n 
A 1 371 GLY 371 394 394 GLY GLY A . n 
A 1 372 PHE 372 395 395 PHE PHE A . n 
A 1 373 ASN 373 396 396 ASN ASN A . n 
A 1 374 MET 374 397 397 MET MET A . n 
A 1 375 VAL 375 398 398 VAL VAL A . n 
A 1 376 ARG 376 399 399 ARG ARG A . n 
A 1 377 LYS 377 400 400 LYS LYS A . n 
A 1 378 HIS 378 401 401 HIS HIS A . n 
A 1 379 ILE 379 402 402 ILE ILE A . n 
A 1 380 LYS 380 403 403 LYS LYS A . n 
A 1 381 VAL 381 404 404 VAL VAL A . n 
A 1 382 GLU 382 405 405 GLU GLU A . n 
A 1 383 PRO 383 406 406 PRO PRO A . n 
A 1 384 GLN 384 407 407 GLN GLN A . n 
A 1 385 ARG 385 408 408 ARG ARG A . n 
A 1 386 TRP 386 409 409 TRP TRP A . n 
A 1 387 PHE 387 410 410 PHE PHE A . n 
A 1 388 TYR 388 411 411 TYR TYR A . n 
A 1 389 TRP 389 412 412 TRP TRP A . n 
A 1 390 ALA 390 413 413 ALA ALA A . n 
A 1 391 ASP 391 414 414 ASP ASP A . n 
A 1 392 ARG 392 415 415 ARG ARG A . n 
A 1 393 LEU 393 416 416 LEU LEU A . n 
A 1 394 GLY 394 417 417 GLY GLY A . n 
A 1 395 LEU 395 418 418 LEU LEU A . n 
A 1 396 LEU 396 419 419 LEU LEU A . n 
A 1 397 VAL 397 420 420 VAL VAL A . n 
A 1 398 TRP 398 421 421 TRP TRP A . n 
A 1 399 GLN 399 422 422 GLN GLN A . n 
A 1 400 ASP 400 423 423 ASP ASP A . n 
A 1 401 MET 401 424 424 MET MET A . n 
A 1 402 PRO 402 425 425 PRO PRO A . n 
A 1 403 ASN 403 426 426 ASN ASN A . n 
A 1 404 MET 404 427 427 MET MET A . n 
A 1 405 GLU 405 428 428 GLU GLU A . n 
A 1 406 ARG 406 429 429 ARG ARG A . n 
A 1 407 THR 407 430 430 THR THR A . n 
A 1 408 PRO 408 431 431 PRO PRO A . n 
A 1 409 ASP 409 432 432 ASP ASP A . n 
A 1 410 ALA 410 433 433 ALA ALA A . n 
A 1 411 ALA 411 434 434 ALA ALA A . n 
A 1 412 ALA 412 435 435 ALA ALA A . n 
A 1 413 ARG 413 436 436 ARG ARG A . n 
A 1 414 THR 414 437 437 THR THR A . n 
A 1 415 GLN 415 438 438 GLN GLN A . n 
A 1 416 TRP 416 439 439 TRP TRP A . n 
A 1 417 GLU 417 440 440 GLU GLU A . n 
A 1 418 ALA 418 441 441 ALA ALA A . n 
A 1 419 GLU 419 442 442 GLU GLU A . n 
A 1 420 TYR 420 443 443 TYR TYR A . n 
A 1 421 ASP 421 444 444 ASP ASP A . n 
A 1 422 ARG 422 445 445 ARG ARG A . n 
A 1 423 ILE 423 446 446 ILE ILE A . n 
A 1 424 ILE 424 447 447 ILE ILE A . n 
A 1 425 ASP 425 448 448 ASP ASP A . n 
A 1 426 GLN 426 449 449 GLN GLN A . n 
A 1 427 HIS 427 450 450 HIS HIS A . n 
A 1 428 ARG 428 451 451 ARG ARG A . n 
A 1 429 SER 429 452 452 SER SER A . n 
A 1 430 SER 430 453 453 SER SER A . n 
A 1 431 PRO 431 454 454 PRO PRO A . n 
A 1 432 SER 432 455 455 SER SER A . n 
A 1 433 LEU 433 456 456 LEU LEU A . n 
A 1 434 VAL 434 457 457 VAL VAL A . n 
A 1 435 LEU 435 458 458 LEU LEU A . n 
A 1 436 TRP 436 459 459 TRP TRP A . n 
A 1 437 VAL 437 460 460 VAL VAL A . n 
A 1 438 ASN 438 461 461 ASN ASN A . n 
A 1 439 GLN 439 462 462 GLN GLN A . n 
A 1 440 ASN 440 463 463 ASN ASN A . n 
A 1 441 GLU 441 464 464 GLU GLU A . n 
A 1 442 GLY 442 465 465 GLY GLY A . n 
A 1 443 TRP 443 466 466 TRP TRP A . n 
A 1 444 GLY 444 467 467 GLY GLY A . n 
A 1 445 GLN 445 468 468 GLN GLN A . n 
A 1 446 TYR 446 469 469 TYR TYR A . n 
A 1 447 ASP 447 470 470 ASP ASP A . n 
A 1 448 GLN 448 471 471 GLN GLN A . n 
A 1 449 ALA 449 472 472 ALA ALA A . n 
A 1 450 ARG 450 473 473 ARG ARG A . n 
A 1 451 LEU 451 474 474 LEU LEU A . n 
A 1 452 ALA 452 475 475 ALA ALA A . n 
A 1 453 ASP 453 476 476 ASP ASP A . n 
A 1 454 LYS 454 477 477 LYS LYS A . n 
A 1 455 VAL 455 478 478 VAL VAL A . n 
A 1 456 LYS 456 479 479 LYS LYS A . n 
A 1 457 ALA 457 480 480 ALA ALA A . n 
A 1 458 TYR 458 481 481 TYR TYR A . n 
A 1 459 ASP 459 482 482 ASP ASP A . n 
A 1 460 PRO 460 483 483 PRO PRO A . n 
A 1 461 THR 461 484 484 THR THR A . n 
A 1 462 ARG 462 485 485 ARG ARG A . n 
A 1 463 LEU 463 486 486 LEU LEU A . n 
A 1 464 VAL 464 487 487 VAL VAL A . n 
A 1 465 ASP 465 488 488 ASP ASP A . n 
A 1 466 ASN 466 489 489 ASN ASN A . n 
A 1 467 MET 467 490 490 MET MET A . n 
A 1 468 SER 468 491 491 SER SER A . n 
A 1 469 GLY 469 492 492 GLY GLY A . n 
A 1 470 VAL 470 493 493 VAL VAL A . n 
A 1 471 ASN 471 494 494 ASN ASN A . n 
A 1 472 CYS 472 495 495 CYS CYS A . n 
A 1 473 CYS 473 496 496 CYS CYS A . n 
A 1 474 GLY 474 497 497 GLY GLY A . n 
A 1 475 ALA 475 498 498 ALA ALA A . n 
A 1 476 VAL 476 499 499 VAL VAL A . n 
A 1 477 ASP 477 500 500 ASP ASP A . n 
A 1 478 GLY 478 501 501 GLY GLY A . n 
A 1 479 GLY 479 502 502 GLY GLY A . n 
A 1 480 ASN 480 503 503 ASN ASN A . n 
A 1 481 GLY 481 504 504 GLY GLY A . n 
A 1 482 ASP 482 505 505 ASP ASP A . n 
A 1 483 VAL 483 506 506 VAL VAL A . n 
A 1 484 VAL 484 507 507 VAL VAL A . n 
A 1 485 ASP 485 508 508 ASP ASP A . n 
A 1 486 HIS 486 509 509 HIS HIS A . n 
A 1 487 HIS 487 510 510 HIS HIS A . n 
A 1 488 VAL 488 511 511 VAL VAL A . n 
A 1 489 TYR 489 512 512 TYR TYR A . n 
A 1 490 VAL 490 513 513 VAL VAL A . n 
A 1 491 GLY 491 514 514 GLY GLY A . n 
A 1 492 PRO 492 515 515 PRO PRO A . n 
A 1 493 GLY 493 516 516 GLY GLY A . n 
A 1 494 THR 494 517 517 THR THR A . n 
A 1 495 THR 495 518 518 THR THR A . n 
A 1 496 VAL 496 519 519 VAL VAL A . n 
A 1 497 PRO 497 520 520 PRO PRO A . n 
A 1 498 SER 498 521 521 SER SER A . n 
A 1 499 ALA 499 522 522 ALA ALA A . n 
A 1 500 THR 500 523 523 THR THR A . n 
A 1 501 ARG 501 524 524 ARG ARG A . n 
A 1 502 ALA 502 525 525 ALA ALA A . n 
A 1 503 ALA 503 526 526 ALA ALA A . n 
A 1 504 VAL 504 527 527 VAL VAL A . n 
A 1 505 LEU 505 528 528 LEU LEU A . n 
A 1 506 GLY 506 529 529 GLY GLY A . n 
A 1 507 GLU 507 530 530 GLU GLU A . n 
A 1 508 PHE 508 531 531 PHE PHE A . n 
A 1 509 GLY 509 532 532 GLY GLY A . n 
A 1 510 GLY 510 533 533 GLY GLY A . n 
A 1 511 LEU 511 534 534 LEU LEU A . n 
A 1 512 GLY 512 535 535 GLY GLY A . n 
A 1 513 PHE 513 536 536 PHE PHE A . n 
A 1 514 LYS 514 537 537 LYS LYS A . n 
A 1 515 VAL 515 538 538 VAL VAL A . n 
A 1 516 ALA 516 539 539 ALA ALA A . n 
A 1 517 GLY 517 540 540 GLY GLY A . n 
A 1 518 HIS 518 541 541 HIS HIS A . n 
A 1 519 GLU 519 542 542 GLU GLU A . n 
A 1 520 TRP 520 543 543 TRP TRP A . n 
A 1 521 TYR 521 544 544 TYR TYR A . n 
A 1 522 PRO 522 545 545 PRO PRO A . n 
A 1 523 GLY 523 546 546 GLY GLY A . n 
A 1 524 GLY 524 547 547 GLY GLY A . n 
A 1 525 GLY 525 548 548 GLY GLY A . n 
A 1 526 PHE 526 549 549 PHE PHE A . n 
A 1 527 SER 527 550 550 SER SER A . n 
A 1 528 TYR 528 551 551 TYR TYR A . n 
A 1 529 GLU 529 552 552 GLU GLU A . n 
A 1 530 ASP 530 553 553 ASP ASP A . n 
A 1 531 GLN 531 554 554 GLN GLN A . n 
A 1 532 PRO 532 555 555 PRO PRO A . n 
A 1 533 ASP 533 556 556 ASP ASP A . n 
A 1 534 LEU 534 557 557 LEU LEU A . n 
A 1 535 ALA 535 558 558 ALA ALA A . n 
A 1 536 HIS 536 559 559 HIS HIS A . n 
A 1 537 LEU 537 560 560 LEU LEU A . n 
A 1 538 ASN 538 561 561 ASN ASN A . n 
A 1 539 ASN 539 562 562 ASN ASN A . n 
A 1 540 ARG 540 563 563 ARG ARG A . n 
A 1 541 PHE 541 564 564 PHE PHE A . n 
A 1 542 VAL 542 565 565 VAL VAL A . n 
A 1 543 GLY 543 566 566 GLY GLY A . n 
A 1 544 LEU 544 567 567 LEU LEU A . n 
A 1 545 ILE 545 568 568 ILE ILE A . n 
A 1 546 ASP 546 569 569 ASP ASP A . n 
A 1 547 ALA 547 570 570 ALA ALA A . n 
A 1 548 ILE 548 571 571 ILE ILE A . n 
A 1 549 ARG 549 572 572 ARG ARG A . n 
A 1 550 GLU 550 573 573 GLU GLU A . n 
A 1 551 VAL 551 574 574 VAL VAL A . n 
A 1 552 ARG 552 575 575 ARG ARG A . n 
A 1 553 MET 553 576 576 MET MET A . n 
A 1 554 PRO 554 577 577 PRO PRO A . n 
A 1 555 ARG 555 578 578 ARG ARG A . n 
A 1 556 GLY 556 579 579 GLY GLY A . n 
A 1 557 LEU 557 580 580 LEU LEU A . n 
A 1 558 SER 558 581 581 SER SER A . n 
A 1 559 ALA 559 582 582 ALA ALA A . n 
A 1 560 SER 560 583 583 SER SER A . n 
A 1 561 VAL 561 584 584 VAL VAL A . n 
A 1 562 TYR 562 585 585 TYR TYR A . n 
A 1 563 THR 563 586 586 THR THR A . n 
A 1 564 GLU 564 587 587 GLU GLU A . n 
A 1 565 ILE 565 588 588 ILE ILE A . n 
A 1 566 THR 566 589 589 THR THR A . n 
A 1 567 ASP 567 590 590 ASP ASP A . n 
A 1 568 VAL 568 591 591 VAL VAL A . n 
A 1 569 GLU 569 592 592 GLU GLU A . n 
A 1 570 ASN 570 593 593 ASN ASN A . n 
A 1 571 GLU 571 594 594 GLU GLU A . n 
A 1 572 VAL 572 595 595 VAL VAL A . n 
A 1 573 ASN 573 596 596 ASN ASN A . n 
A 1 574 GLY 574 597 597 GLY GLY A . n 
A 1 575 LEU 575 598 598 LEU LEU A . n 
A 1 576 LEU 576 599 599 LEU LEU A . n 
A 1 577 THR 577 600 600 THR THR A . n 
A 1 578 TYR 578 601 601 TYR TYR A . n 
A 1 579 ASP 579 602 602 ASP ASP A . n 
A 1 580 ARG 580 603 603 ARG ARG A . n 
A 1 581 GLN 581 604 604 GLN GLN A . n 
A 1 582 VAL 582 605 605 VAL VAL A . n 
A 1 583 VAL 583 606 606 VAL VAL A . n 
A 1 584 LYS 584 607 607 LYS LYS A . n 
A 1 585 VAL 585 608 608 VAL VAL A . n 
A 1 586 ASP 586 609 609 ASP ASP A . n 
A 1 587 GLU 587 610 610 GLU GLU A . n 
A 1 588 ALA 588 611 611 ALA ALA A . n 
A 1 589 ARG 589 612 612 ARG ARG A . n 
A 1 590 VAL 590 613 613 VAL VAL A . n 
A 1 591 ARG 591 614 614 ARG ARG A . n 
A 1 592 ALA 592 615 615 ALA ALA A . n 
A 1 593 ALA 593 616 616 ALA ALA A . n 
A 1 594 ASN 594 617 617 ASN ASN A . n 
A 1 595 ARG 595 618 618 ARG ARG A . n 
A 1 596 ALA 596 619 619 ALA ALA A . n 
A 1 597 LEU 597 620 620 LEU LEU A . n 
A 1 598 ILE 598 621 621 ILE ILE A . n 
A 1 599 ASP 599 622 622 ASP ASP A . n 
A 1 600 ALA 600 623 623 ALA ALA A . n 
A 1 601 SER 601 624 624 SER SER A . n 
A 1 602 ARG 602 625 625 ARG ARG A . n 
A 1 603 GLY 603 626 ?   ?   ?   A . n 
A 1 604 THR 604 627 ?   ?   ?   A . n 
A 1 605 THR 605 628 ?   ?   ?   A . n 
A 1 606 ALA 606 629 ?   ?   ?   A . n 
A 1 607 PRO 607 630 ?   ?   ?   A . n 
A 1 608 LEU 608 631 ?   ?   ?   A . n 
A 1 609 THR 609 632 ?   ?   ?   A . n 
A 1 610 LEU 610 633 ?   ?   ?   A . n 
A 1 611 PRO 611 634 ?   ?   ?   A . n 
A 1 612 VAL 612 635 ?   ?   ?   A . n 
B 1 1   MET 1   24  ?   ?   ?   B . n 
B 1 2   GLY 2   25  ?   ?   ?   B . n 
B 1 3   SER 3   26  ?   ?   ?   B . n 
B 1 4   SER 4   27  ?   ?   ?   B . n 
B 1 5   HIS 5   28  ?   ?   ?   B . n 
B 1 6   HIS 6   29  ?   ?   ?   B . n 
B 1 7   HIS 7   30  ?   ?   ?   B . n 
B 1 8   HIS 8   31  ?   ?   ?   B . n 
B 1 9   HIS 9   32  ?   ?   ?   B . n 
B 1 10  HIS 10  33  ?   ?   ?   B . n 
B 1 11  SER 11  34  ?   ?   ?   B . n 
B 1 12  ALA 12  35  ?   ?   ?   B . n 
B 1 13  ALA 13  36  ?   ?   ?   B . n 
B 1 14  LEU 14  37  ?   ?   ?   B . n 
B 1 15  GLU 15  38  ?   ?   ?   B . n 
B 1 16  VAL 16  39  ?   ?   ?   B . n 
B 1 17  LEU 17  40  ?   ?   ?   B . n 
B 1 18  PHE 18  41  ?   ?   ?   B . n 
B 1 19  GLN 19  42  ?   ?   ?   B . n 
B 1 20  GLY 20  43  ?   ?   ?   B . n 
B 1 21  PRO 21  44  ?   ?   ?   B . n 
B 1 22  ALA 22  45  ?   ?   ?   B . n 
B 1 23  PRO 23  46  46  PRO PRO B . n 
B 1 24  ARG 24  47  47  ARG ARG B . n 
B 1 25  ALA 25  48  48  ALA ALA B . n 
B 1 26  TRP 26  49  49  TRP TRP B . n 
B 1 27  THR 27  50  50  THR THR B . n 
B 1 28  PRO 28  51  51  PRO PRO B . n 
B 1 29  LYS 29  52  52  LYS LYS B . n 
B 1 30  PRO 30  53  53  PRO PRO B . n 
B 1 31  SER 31  54  54  SER SER B . n 
B 1 32  PRO 32  55  55  PRO PRO B . n 
B 1 33  MET 33  56  56  MET MET B . n 
B 1 34  THR 34  57  57  THR THR B . n 
B 1 35  THR 35  58  58  THR THR B . n 
B 1 36  PRO 36  59  59  PRO PRO B . n 
B 1 37  TRP 37  60  60  TRP TRP B . n 
B 1 38  THR 38  61  61  THR THR B . n 
B 1 39  ASP 39  62  62  ASP ASP B . n 
B 1 40  GLN 40  63  63  GLN GLN B . n 
B 1 41  VAL 41  64  64  VAL VAL B . n 
B 1 42  PRO 42  65  65  PRO PRO B . n 
B 1 43  VAL 43  66  66  VAL VAL B . n 
B 1 44  ASP 44  67  67  ASP ASP B . n 
B 1 45  ASN 45  68  68  ASN ASN B . n 
B 1 46  PRO 46  69  69  PRO PRO B . n 
B 1 47  LEU 47  70  70  LEU LEU B . n 
B 1 48  PRO 48  71  71  PRO PRO B . n 
B 1 49  GLU 49  72  72  GLU GLU B . n 
B 1 50  TYR 50  73  73  TYR TYR B . n 
B 1 51  PRO 51  74  74  PRO PRO B . n 
B 1 52  ARG 52  75  75  ARG ARG B . n 
B 1 53  PRO 53  76  76  PRO PRO B . n 
B 1 54  GLN 54  77  77  GLN GLN B . n 
B 1 55  LEU 55  78  78  LEU LEU B . n 
B 1 56  THR 56  79  79  THR THR B . n 
B 1 57  ARG 57  80  80  ARG ARG B . n 
B 1 58  PRO 58  81  81  PRO PRO B . n 
B 1 59  ASP 59  82  82  ASP ASP B . n 
B 1 60  TRP 60  83  83  TRP TRP B . n 
B 1 61  ALA 61  84  84  ALA ALA B . n 
B 1 62  ASN 62  85  85  ASN ASN B . n 
B 1 63  LEU 63  86  86  LEU LEU B . n 
B 1 64  ASN 64  87  87  ASN ASN B . n 
B 1 65  GLY 65  88  88  GLY GLY B . n 
B 1 66  ILE 66  89  89  ILE ILE B . n 
B 1 67  TRP 67  90  90  TRP TRP B . n 
B 1 68  ASP 68  91  91  ASP ASP B . n 
B 1 69  PHE 69  92  92  PHE PHE B . n 
B 1 70  ALA 70  93  93  ALA ALA B . n 
B 1 71  VAL 71  94  94  VAL VAL B . n 
B 1 72  THR 72  95  95  THR THR B . n 
B 1 73  SER 73  96  96  SER SER B . n 
B 1 74  ALA 74  97  97  ALA ALA B . n 
B 1 75  ASN 75  98  98  ASN ASN B . n 
B 1 76  ALA 76  99  99  ALA ALA B . n 
B 1 77  GLY 77  100 100 GLY GLY B . n 
B 1 78  GLN 78  101 101 GLN GLN B . n 
B 1 79  PRO 79  102 102 PRO PRO B . n 
B 1 80  ALA 80  103 103 ALA ALA B . n 
B 1 81  THR 81  104 104 THR THR B . n 
B 1 82  PHE 82  105 105 PHE PHE B . n 
B 1 83  PRO 83  106 106 PRO PRO B . n 
B 1 84  GLU 84  107 107 GLU GLU B . n 
B 1 85  GLN 85  108 108 GLN GLN B . n 
B 1 86  ILE 86  109 109 ILE ILE B . n 
B 1 87  ARG 87  110 110 ARG ARG B . n 
B 1 88  VAL 88  111 111 VAL VAL B . n 
B 1 89  PRO 89  112 112 PRO PRO B . n 
B 1 90  PHE 90  113 113 PHE PHE B . n 
B 1 91  VAL 91  114 114 VAL VAL B . n 
B 1 92  ALA 92  115 115 ALA ALA B . n 
B 1 93  GLU 93  116 116 GLU GLU B . n 
B 1 94  SER 94  117 117 SER SER B . n 
B 1 95  ALA 95  118 118 ALA ALA B . n 
B 1 96  LEU 96  119 119 LEU LEU B . n 
B 1 97  SER 97  120 120 SER SER B . n 
B 1 98  GLY 98  121 121 GLY GLY B . n 
B 1 99  ILE 99  122 122 ILE ILE B . n 
B 1 100 GLN 100 123 123 GLN GLN B . n 
B 1 101 ARG 101 124 124 ARG ARG B . n 
B 1 102 LYS 102 125 125 LYS LYS B . n 
B 1 103 ILE 103 126 126 ILE ILE B . n 
B 1 104 THR 104 127 127 THR THR B . n 
B 1 105 GLN 105 128 128 GLN GLN B . n 
B 1 106 ASN 106 129 129 ASN ASN B . n 
B 1 107 ASP 107 130 130 ASP ASP B . n 
B 1 108 LYS 108 131 131 LYS LYS B . n 
B 1 109 LEU 109 132 132 LEU LEU B . n 
B 1 110 TRP 110 133 133 TRP TRP B . n 
B 1 111 TYR 111 134 134 TYR TYR B . n 
B 1 112 LYS 112 135 135 LYS LYS B . n 
B 1 113 ARG 113 136 136 ARG ARG B . n 
B 1 114 THR 114 137 137 THR THR B . n 
B 1 115 PHE 115 138 138 PHE PHE B . n 
B 1 116 THR 116 139 139 THR THR B . n 
B 1 117 VAL 117 140 140 VAL VAL B . n 
B 1 118 PRO 118 141 141 PRO PRO B . n 
B 1 119 SER 119 142 142 SER SER B . n 
B 1 120 ASN 120 143 143 ASN ASN B . n 
B 1 121 TRP 121 144 144 TRP TRP B . n 
B 1 122 ASN 122 145 145 ASN ASN B . n 
B 1 123 GLY 123 146 146 GLY GLY B . n 
B 1 124 ARG 124 147 147 ARG ARG B . n 
B 1 125 ARG 125 148 148 ARG ARG B . n 
B 1 126 VAL 126 149 149 VAL VAL B . n 
B 1 127 GLN 127 150 150 GLN GLN B . n 
B 1 128 LEU 128 151 151 LEU LEU B . n 
B 1 129 ASN 129 152 152 ASN ASN B . n 
B 1 130 PHE 130 153 153 PHE PHE B . n 
B 1 131 GLY 131 154 154 GLY GLY B . n 
B 1 132 ALA 132 155 155 ALA ALA B . n 
B 1 133 SER 133 156 156 SER SER B . n 
B 1 134 ASP 134 157 157 ASP ASP B . n 
B 1 135 TRP 135 158 158 TRP TRP B . n 
B 1 136 ARG 136 159 159 ARG ARG B . n 
B 1 137 THR 137 160 160 THR THR B . n 
B 1 138 THR 138 161 161 THR THR B . n 
B 1 139 VAL 139 162 162 VAL VAL B . n 
B 1 140 TRP 140 163 163 TRP TRP B . n 
B 1 141 VAL 141 164 164 VAL VAL B . n 
B 1 142 ASN 142 165 165 ASN ASN B . n 
B 1 143 GLY 143 166 166 GLY GLY B . n 
B 1 144 ARG 144 167 167 ARG ARG B . n 
B 1 145 GLN 145 168 168 GLN GLN B . n 
B 1 146 ALA 146 169 169 ALA ALA B . n 
B 1 147 GLY 147 170 170 GLY GLY B . n 
B 1 148 ALA 148 171 171 ALA ALA B . n 
B 1 149 VAL 149 172 172 VAL VAL B . n 
B 1 150 HIS 150 173 173 HIS HIS B . n 
B 1 151 SER 151 174 174 SER SER B . n 
B 1 152 GLY 152 175 175 GLY GLY B . n 
B 1 153 GLY 153 176 176 GLY GLY B . n 
B 1 154 TYR 154 177 177 TYR TYR B . n 
B 1 155 ASP 155 178 178 ASP ASP B . n 
B 1 156 ALA 156 179 179 ALA ALA B . n 
B 1 157 PHE 157 180 180 PHE PHE B . n 
B 1 158 SER 158 181 181 SER SER B . n 
B 1 159 TYR 159 182 182 TYR TYR B . n 
B 1 160 ASP 160 183 183 ASP ASP B . n 
B 1 161 VAL 161 184 184 VAL VAL B . n 
B 1 162 THR 162 185 185 THR THR B . n 
B 1 163 ASP 163 186 186 ASP ASP B . n 
B 1 164 LEU 164 187 187 LEU LEU B . n 
B 1 165 LEU 165 188 188 LEU LEU B . n 
B 1 166 THR 166 189 189 THR THR B . n 
B 1 167 ALA 167 190 190 ALA ALA B . n 
B 1 168 GLY 168 191 191 GLY GLY B . n 
B 1 169 THR 169 192 192 THR THR B . n 
B 1 170 ASN 170 193 193 ASN ASN B . n 
B 1 171 THR 171 194 194 THR THR B . n 
B 1 172 LEU 172 195 195 LEU LEU B . n 
B 1 173 VAL 173 196 196 VAL VAL B . n 
B 1 174 VAL 174 197 197 VAL VAL B . n 
B 1 175 SER 175 198 198 SER SER B . n 
B 1 176 VAL 176 199 199 VAL VAL B . n 
B 1 177 TRP 177 200 200 TRP TRP B . n 
B 1 178 ASP 178 201 201 ASP ASP B . n 
B 1 179 PRO 179 202 202 PRO PRO B . n 
B 1 180 THR 180 203 203 THR THR B . n 
B 1 181 GLU 181 204 204 GLU GLU B . n 
B 1 182 THR 182 205 205 THR THR B . n 
B 1 183 GLY 183 206 206 GLY GLY B . n 
B 1 184 THR 184 207 207 THR THR B . n 
B 1 185 GLN 185 208 208 GLN GLN B . n 
B 1 186 ALA 186 209 209 ALA ALA B . n 
B 1 187 VAL 187 210 210 VAL VAL B . n 
B 1 188 GLY 188 211 211 GLY GLY B . n 
B 1 189 LYS 189 212 212 LYS LYS B . n 
B 1 190 GLN 190 213 213 GLN GLN B . n 
B 1 191 ARG 191 214 214 ARG ARG B . n 
B 1 192 ILE 192 215 215 ILE ILE B . n 
B 1 193 ARG 193 216 216 ARG ARG B . n 
B 1 194 ASP 194 217 217 ASP ASP B . n 
B 1 195 VAL 195 218 218 VAL VAL B . n 
B 1 196 ALA 196 219 219 ALA ALA B . n 
B 1 197 PRO 197 220 220 PRO PRO B . n 
B 1 198 HIS 198 221 221 HIS HIS B . n 
B 1 199 PRO 199 222 222 PRO PRO B . n 
B 1 200 GLY 200 223 223 GLY GLY B . n 
B 1 201 GLY 201 224 224 GLY GLY B . n 
B 1 202 GLY 202 225 225 GLY GLY B . n 
B 1 203 ILE 203 226 226 ILE ILE B . n 
B 1 204 LEU 204 227 227 LEU LEU B . n 
B 1 205 TYR 205 228 228 TYR TYR B . n 
B 1 206 THR 206 229 229 THR THR B . n 
B 1 207 ALA 207 230 230 ALA ALA B . n 
B 1 208 ALA 208 231 231 ALA ALA B . n 
B 1 209 SER 209 232 232 SER SER B . n 
B 1 210 GLY 210 233 233 GLY GLY B . n 
B 1 211 ILE 211 234 234 ILE ILE B . n 
B 1 212 TRP 212 235 235 TRP TRP B . n 
B 1 213 GLN 213 236 236 GLN GLN B . n 
B 1 214 THR 214 237 237 THR THR B . n 
B 1 215 VAL 215 238 238 VAL VAL B . n 
B 1 216 TRP 216 239 239 TRP TRP B . n 
B 1 217 LEU 217 240 240 LEU LEU B . n 
B 1 218 GLU 218 241 241 GLU GLU B . n 
B 1 219 PRO 219 242 242 PRO PRO B . n 
B 1 220 THR 220 243 243 THR THR B . n 
B 1 221 ALA 221 244 244 ALA ALA B . n 
B 1 222 ALA 222 245 245 ALA ALA B . n 
B 1 223 ALA 223 246 246 ALA ALA B . n 
B 1 224 HIS 224 247 247 HIS HIS B . n 
B 1 225 VAL 225 248 248 VAL VAL B . n 
B 1 226 THR 226 249 249 THR THR B . n 
B 1 227 ARG 227 250 250 ARG ARG B . n 
B 1 228 LEU 228 251 251 LEU LEU B . n 
B 1 229 ASP 229 252 252 ASP ASP B . n 
B 1 230 LEU 230 253 253 LEU LEU B . n 
B 1 231 VAL 231 254 254 VAL VAL B . n 
B 1 232 PRO 232 255 255 PRO PRO B . n 
B 1 233 ASP 233 256 256 ASP ASP B . n 
B 1 234 PRO 234 257 257 PRO PRO B . n 
B 1 235 ALA 235 258 258 ALA ALA B . n 
B 1 236 ASN 236 259 259 ASN ASN B . n 
B 1 237 SER 237 260 260 SER SER B . n 
B 1 238 ARG 238 261 261 ARG ARG B . n 
B 1 239 LEU 239 262 262 LEU LEU B . n 
B 1 240 LYS 240 263 263 LYS LYS B . n 
B 1 241 VAL 241 264 264 VAL VAL B . n 
B 1 242 THR 242 265 265 THR THR B . n 
B 1 243 VAL 243 266 266 VAL VAL B . n 
B 1 244 ARG 244 267 267 ARG ARG B . n 
B 1 245 GLY 245 268 268 GLY GLY B . n 
B 1 246 ALA 246 269 269 ALA ALA B . n 
B 1 247 GLY 247 270 270 GLY GLY B . n 
B 1 248 ILE 248 271 271 ILE ILE B . n 
B 1 249 SER 249 272 272 SER SER B . n 
B 1 250 GLY 250 273 273 GLY GLY B . n 
B 1 251 HIS 251 274 274 HIS HIS B . n 
B 1 252 GLN 252 275 275 GLN GLN B . n 
B 1 253 ALA 253 276 276 ALA ALA B . n 
B 1 254 ARG 254 277 277 ARG ARG B . n 
B 1 255 VAL 255 278 278 VAL VAL B . n 
B 1 256 THR 256 279 279 THR THR B . n 
B 1 257 VAL 257 280 280 VAL VAL B . n 
B 1 258 SER 258 281 281 SER SER B . n 
B 1 259 THR 259 282 282 THR THR B . n 
B 1 260 GLY 260 283 283 GLY GLY B . n 
B 1 261 GLY 261 284 284 GLY GLY B . n 
B 1 262 THR 262 285 285 THR THR B . n 
B 1 263 THR 263 286 286 THR THR B . n 
B 1 264 VAL 264 287 287 VAL VAL B . n 
B 1 265 GLY 265 288 288 GLY GLY B . n 
B 1 266 THR 266 289 289 THR THR B . n 
B 1 267 ALA 267 290 290 ALA ALA B . n 
B 1 268 THR 268 291 291 THR THR B . n 
B 1 269 GLY 269 292 292 GLY GLY B . n 
B 1 270 PRO 270 293 293 PRO PRO B . n 
B 1 271 VAL 271 294 294 VAL VAL B . n 
B 1 272 GLY 272 295 295 GLY GLY B . n 
B 1 273 THR 273 296 296 THR THR B . n 
B 1 274 GLU 274 297 297 GLU GLU B . n 
B 1 275 PHE 275 298 298 PHE PHE B . n 
B 1 276 THR 276 299 299 THR THR B . n 
B 1 277 VAL 277 300 300 VAL VAL B . n 
B 1 278 PRO 278 301 301 PRO PRO B . n 
B 1 279 VAL 279 302 302 VAL VAL B . n 
B 1 280 PRO 280 303 303 PRO PRO B . n 
B 1 281 ASN 281 304 304 ASN ASN B . n 
B 1 282 PRO 282 305 305 PRO PRO B . n 
B 1 283 ARG 283 306 306 ARG ARG B . n 
B 1 284 LEU 284 307 307 LEU LEU B . n 
B 1 285 TRP 285 308 308 TRP TRP B . n 
B 1 286 THR 286 309 309 THR THR B . n 
B 1 287 PRO 287 310 310 PRO PRO B . n 
B 1 288 GLU 288 311 311 GLU GLU B . n 
B 1 289 ASP 289 312 312 ASP ASP B . n 
B 1 290 PRO 290 313 313 PRO PRO B . n 
B 1 291 PHE 291 314 314 PHE PHE B . n 
B 1 292 LEU 292 315 315 LEU LEU B . n 
B 1 293 TYR 293 316 316 TYR TYR B . n 
B 1 294 ASP 294 317 317 ASP ASP B . n 
B 1 295 VAL 295 318 318 VAL VAL B . n 
B 1 296 ARG 296 319 319 ARG ARG B . n 
B 1 297 ALA 297 320 320 ALA ALA B . n 
B 1 298 ASP 298 321 321 ASP ASP B . n 
B 1 299 PRO 299 322 322 PRO PRO B . n 
B 1 300 LEU 300 323 323 LEU LEU B . n 
B 1 301 SER 301 324 ?   ?   ?   B . n 
B 1 302 GLY 302 325 ?   ?   ?   B . n 
B 1 303 GLY 303 326 ?   ?   ?   B . n 
B 1 304 THR 304 327 ?   ?   ?   B . n 
B 1 305 THR 305 328 ?   ?   ?   B . n 
B 1 306 VAL 306 329 329 VAL VAL B . n 
B 1 307 ASP 307 330 330 ASP ASP B . n 
B 1 308 SER 308 331 331 SER SER B . n 
B 1 309 VAL 309 332 332 VAL VAL B . n 
B 1 310 GLY 310 333 333 GLY GLY B . n 
B 1 311 SER 311 334 334 SER SER B . n 
B 1 312 TYR 312 335 335 TYR TYR B . n 
B 1 313 THR 313 336 336 THR THR B . n 
B 1 314 GLY 314 337 337 GLY GLY B . n 
B 1 315 MET 315 338 338 MET MET B . n 
B 1 316 ARG 316 339 339 ARG ARG B . n 
B 1 317 THR 317 340 340 THR THR B . n 
B 1 318 ILE 318 341 341 ILE ILE B . n 
B 1 319 ALA 319 342 342 ALA ALA B . n 
B 1 320 LEU 320 343 343 LEU LEU B . n 
B 1 321 ALA 321 344 344 ALA ALA B . n 
B 1 322 SER 322 345 345 SER SER B . n 
B 1 323 VAL 323 346 346 VAL VAL B . n 
B 1 324 GLY 324 347 347 GLY GLY B . n 
B 1 325 GLY 325 348 348 GLY GLY B . n 
B 1 326 HIS 326 349 349 HIS HIS B . n 
B 1 327 GLN 327 350 350 GLN GLN B . n 
B 1 328 ARG 328 351 351 ARG ARG B . n 
B 1 329 PRO 329 352 352 PRO PRO B . n 
B 1 330 VAL 330 353 353 VAL VAL B . n 
B 1 331 LEU 331 354 354 LEU LEU B . n 
B 1 332 ASN 332 355 355 ASN ASN B . n 
B 1 333 GLY 333 356 356 GLY GLY B . n 
B 1 334 LYS 334 357 357 LYS LYS B . n 
B 1 335 PHE 335 358 358 PHE PHE B . n 
B 1 336 VAL 336 359 359 VAL VAL B . n 
B 1 337 PHE 337 360 360 PHE PHE B . n 
B 1 338 GLN 338 361 361 GLN GLN B . n 
B 1 339 THR 339 362 362 THR THR B . n 
B 1 340 GLY 340 363 363 GLY GLY B . n 
B 1 341 THR 341 364 364 THR THR B . n 
B 1 342 LEU 342 365 365 LEU LEU B . n 
B 1 343 ASP 343 366 366 ASP ASP B . n 
B 1 344 GLN 344 367 367 GLN GLN B . n 
B 1 345 GLY 345 368 368 GLY GLY B . n 
B 1 346 TYR 346 369 369 TYR TYR B . n 
B 1 347 TRP 347 370 370 TRP TRP B . n 
B 1 348 PRO 348 371 371 PRO PRO B . n 
B 1 349 ASP 349 372 372 ASP ASP B . n 
B 1 350 GLY 350 373 373 GLY GLY B . n 
B 1 351 ILE 351 374 374 ILE ILE B . n 
B 1 352 TYR 352 375 375 TYR TYR B . n 
B 1 353 THR 353 376 376 THR THR B . n 
B 1 354 ALA 354 377 377 ALA ALA B . n 
B 1 355 PRO 355 378 378 PRO PRO B . n 
B 1 356 THR 356 379 379 THR THR B . n 
B 1 357 ASP 357 380 380 ASP ASP B . n 
B 1 358 ALA 358 381 381 ALA ALA B . n 
B 1 359 ALA 359 382 382 ALA ALA B . n 
B 1 360 LEU 360 383 383 LEU LEU B . n 
B 1 361 ARG 361 384 384 ARG ARG B . n 
B 1 362 HIS 362 385 385 HIS HIS B . n 
B 1 363 ASP 363 386 386 ASP ASP B . n 
B 1 364 LEU 364 387 387 LEU LEU B . n 
B 1 365 GLN 365 388 388 GLN GLN B . n 
B 1 366 LYS 366 389 389 LYS LYS B . n 
B 1 367 HIS 367 390 390 HIS HIS B . n 
B 1 368 LYS 368 391 391 LYS LYS B . n 
B 1 369 ASP 369 392 392 ASP ASP B . n 
B 1 370 LEU 370 393 393 LEU LEU B . n 
B 1 371 GLY 371 394 394 GLY GLY B . n 
B 1 372 PHE 372 395 395 PHE PHE B . n 
B 1 373 ASN 373 396 396 ASN ASN B . n 
B 1 374 MET 374 397 397 MET MET B . n 
B 1 375 VAL 375 398 398 VAL VAL B . n 
B 1 376 ARG 376 399 399 ARG ARG B . n 
B 1 377 LYS 377 400 400 LYS LYS B . n 
B 1 378 HIS 378 401 401 HIS HIS B . n 
B 1 379 ILE 379 402 402 ILE ILE B . n 
B 1 380 LYS 380 403 403 LYS LYS B . n 
B 1 381 VAL 381 404 404 VAL VAL B . n 
B 1 382 GLU 382 405 405 GLU GLU B . n 
B 1 383 PRO 383 406 406 PRO PRO B . n 
B 1 384 GLN 384 407 407 GLN GLN B . n 
B 1 385 ARG 385 408 408 ARG ARG B . n 
B 1 386 TRP 386 409 409 TRP TRP B . n 
B 1 387 PHE 387 410 410 PHE PHE B . n 
B 1 388 TYR 388 411 411 TYR TYR B . n 
B 1 389 TRP 389 412 412 TRP TRP B . n 
B 1 390 ALA 390 413 413 ALA ALA B . n 
B 1 391 ASP 391 414 414 ASP ASP B . n 
B 1 392 ARG 392 415 415 ARG ARG B . n 
B 1 393 LEU 393 416 416 LEU LEU B . n 
B 1 394 GLY 394 417 417 GLY GLY B . n 
B 1 395 LEU 395 418 418 LEU LEU B . n 
B 1 396 LEU 396 419 419 LEU LEU B . n 
B 1 397 VAL 397 420 420 VAL VAL B . n 
B 1 398 TRP 398 421 421 TRP TRP B . n 
B 1 399 GLN 399 422 422 GLN GLN B . n 
B 1 400 ASP 400 423 423 ASP ASP B . n 
B 1 401 MET 401 424 424 MET MET B . n 
B 1 402 PRO 402 425 425 PRO PRO B . n 
B 1 403 ASN 403 426 426 ASN ASN B . n 
B 1 404 MET 404 427 427 MET MET B . n 
B 1 405 GLU 405 428 428 GLU GLU B . n 
B 1 406 ARG 406 429 429 ARG ARG B . n 
B 1 407 THR 407 430 430 THR THR B . n 
B 1 408 PRO 408 431 431 PRO PRO B . n 
B 1 409 ASP 409 432 432 ASP ASP B . n 
B 1 410 ALA 410 433 433 ALA ALA B . n 
B 1 411 ALA 411 434 434 ALA ALA B . n 
B 1 412 ALA 412 435 435 ALA ALA B . n 
B 1 413 ARG 413 436 436 ARG ARG B . n 
B 1 414 THR 414 437 437 THR THR B . n 
B 1 415 GLN 415 438 438 GLN GLN B . n 
B 1 416 TRP 416 439 439 TRP TRP B . n 
B 1 417 GLU 417 440 440 GLU GLU B . n 
B 1 418 ALA 418 441 441 ALA ALA B . n 
B 1 419 GLU 419 442 442 GLU GLU B . n 
B 1 420 TYR 420 443 443 TYR TYR B . n 
B 1 421 ASP 421 444 444 ASP ASP B . n 
B 1 422 ARG 422 445 445 ARG ARG B . n 
B 1 423 ILE 423 446 446 ILE ILE B . n 
B 1 424 ILE 424 447 447 ILE ILE B . n 
B 1 425 ASP 425 448 448 ASP ASP B . n 
B 1 426 GLN 426 449 449 GLN GLN B . n 
B 1 427 HIS 427 450 450 HIS HIS B . n 
B 1 428 ARG 428 451 451 ARG ARG B . n 
B 1 429 SER 429 452 452 SER SER B . n 
B 1 430 SER 430 453 453 SER SER B . n 
B 1 431 PRO 431 454 454 PRO PRO B . n 
B 1 432 SER 432 455 455 SER SER B . n 
B 1 433 LEU 433 456 456 LEU LEU B . n 
B 1 434 VAL 434 457 457 VAL VAL B . n 
B 1 435 LEU 435 458 458 LEU LEU B . n 
B 1 436 TRP 436 459 459 TRP TRP B . n 
B 1 437 VAL 437 460 460 VAL VAL B . n 
B 1 438 ASN 438 461 461 ASN ASN B . n 
B 1 439 GLN 439 462 462 GLN GLN B . n 
B 1 440 ASN 440 463 463 ASN ASN B . n 
B 1 441 GLU 441 464 464 GLU GLU B . n 
B 1 442 GLY 442 465 465 GLY GLY B . n 
B 1 443 TRP 443 466 466 TRP TRP B . n 
B 1 444 GLY 444 467 467 GLY GLY B . n 
B 1 445 GLN 445 468 468 GLN GLN B . n 
B 1 446 TYR 446 469 469 TYR TYR B . n 
B 1 447 ASP 447 470 470 ASP ASP B . n 
B 1 448 GLN 448 471 471 GLN GLN B . n 
B 1 449 ALA 449 472 472 ALA ALA B . n 
B 1 450 ARG 450 473 473 ARG ARG B . n 
B 1 451 LEU 451 474 474 LEU LEU B . n 
B 1 452 ALA 452 475 475 ALA ALA B . n 
B 1 453 ASP 453 476 476 ASP ASP B . n 
B 1 454 LYS 454 477 477 LYS LYS B . n 
B 1 455 VAL 455 478 478 VAL VAL B . n 
B 1 456 LYS 456 479 479 LYS LYS B . n 
B 1 457 ALA 457 480 480 ALA ALA B . n 
B 1 458 TYR 458 481 481 TYR TYR B . n 
B 1 459 ASP 459 482 482 ASP ASP B . n 
B 1 460 PRO 460 483 483 PRO PRO B . n 
B 1 461 THR 461 484 484 THR THR B . n 
B 1 462 ARG 462 485 485 ARG ARG B . n 
B 1 463 LEU 463 486 486 LEU LEU B . n 
B 1 464 VAL 464 487 487 VAL VAL B . n 
B 1 465 ASP 465 488 488 ASP ASP B . n 
B 1 466 ASN 466 489 489 ASN ASN B . n 
B 1 467 MET 467 490 490 MET MET B . n 
B 1 468 SER 468 491 491 SER SER B . n 
B 1 469 GLY 469 492 492 GLY GLY B . n 
B 1 470 VAL 470 493 493 VAL VAL B . n 
B 1 471 ASN 471 494 494 ASN ASN B . n 
B 1 472 CYS 472 495 495 CYS CYS B . n 
B 1 473 CYS 473 496 496 CYS CYS B . n 
B 1 474 GLY 474 497 497 GLY GLY B . n 
B 1 475 ALA 475 498 498 ALA ALA B . n 
B 1 476 VAL 476 499 499 VAL VAL B . n 
B 1 477 ASP 477 500 500 ASP ASP B . n 
B 1 478 GLY 478 501 501 GLY GLY B . n 
B 1 479 GLY 479 502 502 GLY GLY B . n 
B 1 480 ASN 480 503 503 ASN ASN B . n 
B 1 481 GLY 481 504 504 GLY GLY B . n 
B 1 482 ASP 482 505 505 ASP ASP B . n 
B 1 483 VAL 483 506 506 VAL VAL B . n 
B 1 484 VAL 484 507 507 VAL VAL B . n 
B 1 485 ASP 485 508 508 ASP ASP B . n 
B 1 486 HIS 486 509 509 HIS HIS B . n 
B 1 487 HIS 487 510 510 HIS HIS B . n 
B 1 488 VAL 488 511 511 VAL VAL B . n 
B 1 489 TYR 489 512 512 TYR TYR B . n 
B 1 490 VAL 490 513 513 VAL VAL B . n 
B 1 491 GLY 491 514 514 GLY GLY B . n 
B 1 492 PRO 492 515 515 PRO PRO B . n 
B 1 493 GLY 493 516 516 GLY GLY B . n 
B 1 494 THR 494 517 517 THR THR B . n 
B 1 495 THR 495 518 518 THR THR B . n 
B 1 496 VAL 496 519 519 VAL VAL B . n 
B 1 497 PRO 497 520 520 PRO PRO B . n 
B 1 498 SER 498 521 521 SER SER B . n 
B 1 499 ALA 499 522 522 ALA ALA B . n 
B 1 500 THR 500 523 523 THR THR B . n 
B 1 501 ARG 501 524 524 ARG ARG B . n 
B 1 502 ALA 502 525 525 ALA ALA B . n 
B 1 503 ALA 503 526 526 ALA ALA B . n 
B 1 504 VAL 504 527 527 VAL VAL B . n 
B 1 505 LEU 505 528 528 LEU LEU B . n 
B 1 506 GLY 506 529 529 GLY GLY B . n 
B 1 507 GLU 507 530 530 GLU GLU B . n 
B 1 508 PHE 508 531 531 PHE PHE B . n 
B 1 509 GLY 509 532 532 GLY GLY B . n 
B 1 510 GLY 510 533 533 GLY GLY B . n 
B 1 511 LEU 511 534 534 LEU LEU B . n 
B 1 512 GLY 512 535 535 GLY GLY B . n 
B 1 513 PHE 513 536 536 PHE PHE B . n 
B 1 514 LYS 514 537 537 LYS LYS B . n 
B 1 515 VAL 515 538 538 VAL VAL B . n 
B 1 516 ALA 516 539 539 ALA ALA B . n 
B 1 517 GLY 517 540 540 GLY GLY B . n 
B 1 518 HIS 518 541 541 HIS HIS B . n 
B 1 519 GLU 519 542 542 GLU GLU B . n 
B 1 520 TRP 520 543 543 TRP TRP B . n 
B 1 521 TYR 521 544 544 TYR TYR B . n 
B 1 522 PRO 522 545 545 PRO PRO B . n 
B 1 523 GLY 523 546 546 GLY GLY B . n 
B 1 524 GLY 524 547 547 GLY GLY B . n 
B 1 525 GLY 525 548 548 GLY GLY B . n 
B 1 526 PHE 526 549 549 PHE PHE B . n 
B 1 527 SER 527 550 550 SER SER B . n 
B 1 528 TYR 528 551 551 TYR TYR B . n 
B 1 529 GLU 529 552 552 GLU GLU B . n 
B 1 530 ASP 530 553 553 ASP ASP B . n 
B 1 531 GLN 531 554 554 GLN GLN B . n 
B 1 532 PRO 532 555 555 PRO PRO B . n 
B 1 533 ASP 533 556 556 ASP ASP B . n 
B 1 534 LEU 534 557 557 LEU LEU B . n 
B 1 535 ALA 535 558 558 ALA ALA B . n 
B 1 536 HIS 536 559 559 HIS HIS B . n 
B 1 537 LEU 537 560 560 LEU LEU B . n 
B 1 538 ASN 538 561 561 ASN ASN B . n 
B 1 539 ASN 539 562 562 ASN ASN B . n 
B 1 540 ARG 540 563 563 ARG ARG B . n 
B 1 541 PHE 541 564 564 PHE PHE B . n 
B 1 542 VAL 542 565 565 VAL VAL B . n 
B 1 543 GLY 543 566 566 GLY GLY B . n 
B 1 544 LEU 544 567 567 LEU LEU B . n 
B 1 545 ILE 545 568 568 ILE ILE B . n 
B 1 546 ASP 546 569 569 ASP ASP B . n 
B 1 547 ALA 547 570 570 ALA ALA B . n 
B 1 548 ILE 548 571 571 ILE ILE B . n 
B 1 549 ARG 549 572 572 ARG ARG B . n 
B 1 550 GLU 550 573 573 GLU GLU B . n 
B 1 551 VAL 551 574 574 VAL VAL B . n 
B 1 552 ARG 552 575 575 ARG ARG B . n 
B 1 553 MET 553 576 576 MET MET B . n 
B 1 554 PRO 554 577 577 PRO PRO B . n 
B 1 555 ARG 555 578 578 ARG ARG B . n 
B 1 556 GLY 556 579 579 GLY GLY B . n 
B 1 557 LEU 557 580 580 LEU LEU B . n 
B 1 558 SER 558 581 581 SER SER B . n 
B 1 559 ALA 559 582 582 ALA ALA B . n 
B 1 560 SER 560 583 583 SER SER B . n 
B 1 561 VAL 561 584 584 VAL VAL B . n 
B 1 562 TYR 562 585 585 TYR TYR B . n 
B 1 563 THR 563 586 586 THR THR B . n 
B 1 564 GLU 564 587 587 GLU GLU B . n 
B 1 565 ILE 565 588 588 ILE ILE B . n 
B 1 566 THR 566 589 589 THR THR B . n 
B 1 567 ASP 567 590 590 ASP ASP B . n 
B 1 568 VAL 568 591 591 VAL VAL B . n 
B 1 569 GLU 569 592 592 GLU GLU B . n 
B 1 570 ASN 570 593 593 ASN ASN B . n 
B 1 571 GLU 571 594 594 GLU GLU B . n 
B 1 572 VAL 572 595 595 VAL VAL B . n 
B 1 573 ASN 573 596 596 ASN ASN B . n 
B 1 574 GLY 574 597 597 GLY GLY B . n 
B 1 575 LEU 575 598 598 LEU LEU B . n 
B 1 576 LEU 576 599 599 LEU LEU B . n 
B 1 577 THR 577 600 600 THR THR B . n 
B 1 578 TYR 578 601 601 TYR TYR B . n 
B 1 579 ASP 579 602 602 ASP ASP B . n 
B 1 580 ARG 580 603 603 ARG ARG B . n 
B 1 581 GLN 581 604 604 GLN GLN B . n 
B 1 582 VAL 582 605 605 VAL VAL B . n 
B 1 583 VAL 583 606 606 VAL VAL B . n 
B 1 584 LYS 584 607 607 LYS LYS B . n 
B 1 585 VAL 585 608 608 VAL VAL B . n 
B 1 586 ASP 586 609 609 ASP ASP B . n 
B 1 587 GLU 587 610 610 GLU GLU B . n 
B 1 588 ALA 588 611 611 ALA ALA B . n 
B 1 589 ARG 589 612 612 ARG ARG B . n 
B 1 590 VAL 590 613 613 VAL VAL B . n 
B 1 591 ARG 591 614 614 ARG ARG B . n 
B 1 592 ALA 592 615 615 ALA ALA B . n 
B 1 593 ALA 593 616 616 ALA ALA B . n 
B 1 594 ASN 594 617 617 ASN ASN B . n 
B 1 595 ARG 595 618 618 ARG ARG B . n 
B 1 596 ALA 596 619 619 ALA ALA B . n 
B 1 597 LEU 597 620 620 LEU LEU B . n 
B 1 598 ILE 598 621 621 ILE ILE B . n 
B 1 599 ASP 599 622 622 ASP ASP B . n 
B 1 600 ALA 600 623 623 ALA ALA B . n 
B 1 601 SER 601 624 624 SER SER B . n 
B 1 602 ARG 602 625 625 ARG ARG B . n 
B 1 603 GLY 603 626 626 GLY GLY B . n 
B 1 604 THR 604 627 ?   ?   ?   B . n 
B 1 605 THR 605 628 ?   ?   ?   B . n 
B 1 606 ALA 606 629 ?   ?   ?   B . n 
B 1 607 PRO 607 630 ?   ?   ?   B . n 
B 1 608 LEU 608 631 ?   ?   ?   B . n 
B 1 609 THR 609 632 ?   ?   ?   B . n 
B 1 610 LEU 610 633 ?   ?   ?   B . n 
B 1 611 PRO 611 634 ?   ?   ?   B . n 
B 1 612 VAL 612 635 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L3Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L3Z 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 P6G   1   701  646 P6G   P6G A . 
D 3 MPD   1   702  648 MPD   MPD A . 
E 3 MPD   1   703  649 MPD   MPD A . 
F 4 A1L3Z 1   704  650 A1L3Z DRG A . 
G 5 MG    1   705  1   MG    MG  A . 
H 6 PG4   1   701  647 PG4   PG4 B . 
I 3 MPD   1   702  646 MPD   MPD B . 
J 4 A1L3Z 1   703  647 A1L3Z DRG B . 
K 5 MG    1   704  2   MG    MG  B . 
L 7 HOH   1   801  243 HOH   HOH A . 
L 7 HOH   2   802  584 HOH   HOH A . 
L 7 HOH   3   803  361 HOH   HOH A . 
L 7 HOH   4   804  563 HOH   HOH A . 
L 7 HOH   5   805  758 HOH   HOH A . 
L 7 HOH   6   806  171 HOH   HOH A . 
L 7 HOH   7   807  266 HOH   HOH A . 
L 7 HOH   8   808  384 HOH   HOH A . 
L 7 HOH   9   809  599 HOH   HOH A . 
L 7 HOH   10  810  592 HOH   HOH A . 
L 7 HOH   11  811  428 HOH   HOH A . 
L 7 HOH   12  812  567 HOH   HOH A . 
L 7 HOH   13  813  752 HOH   HOH A . 
L 7 HOH   14  814  31  HOH   HOH A . 
L 7 HOH   15  815  773 HOH   HOH A . 
L 7 HOH   16  816  391 HOH   HOH A . 
L 7 HOH   17  817  45  HOH   HOH A . 
L 7 HOH   18  818  226 HOH   HOH A . 
L 7 HOH   19  819  707 HOH   HOH A . 
L 7 HOH   20  820  37  HOH   HOH A . 
L 7 HOH   21  821  389 HOH   HOH A . 
L 7 HOH   22  822  631 HOH   HOH A . 
L 7 HOH   23  823  622 HOH   HOH A . 
L 7 HOH   24  824  191 HOH   HOH A . 
L 7 HOH   25  825  251 HOH   HOH A . 
L 7 HOH   26  826  144 HOH   HOH A . 
L 7 HOH   27  827  138 HOH   HOH A . 
L 7 HOH   28  828  435 HOH   HOH A . 
L 7 HOH   29  829  61  HOH   HOH A . 
L 7 HOH   30  830  588 HOH   HOH A . 
L 7 HOH   31  831  293 HOH   HOH A . 
L 7 HOH   32  832  664 HOH   HOH A . 
L 7 HOH   33  833  233 HOH   HOH A . 
L 7 HOH   34  834  718 HOH   HOH A . 
L 7 HOH   35  835  483 HOH   HOH A . 
L 7 HOH   36  836  767 HOH   HOH A . 
L 7 HOH   37  837  585 HOH   HOH A . 
L 7 HOH   38  838  336 HOH   HOH A . 
L 7 HOH   39  839  362 HOH   HOH A . 
L 7 HOH   40  840  657 HOH   HOH A . 
L 7 HOH   41  841  239 HOH   HOH A . 
L 7 HOH   42  842  241 HOH   HOH A . 
L 7 HOH   43  843  190 HOH   HOH A . 
L 7 HOH   44  844  44  HOH   HOH A . 
L 7 HOH   45  845  200 HOH   HOH A . 
L 7 HOH   46  846  292 HOH   HOH A . 
L 7 HOH   47  847  15  HOH   HOH A . 
L 7 HOH   48  848  76  HOH   HOH A . 
L 7 HOH   49  849  252 HOH   HOH A . 
L 7 HOH   50  850  745 HOH   HOH A . 
L 7 HOH   51  851  777 HOH   HOH A . 
L 7 HOH   52  852  508 HOH   HOH A . 
L 7 HOH   53  853  260 HOH   HOH A . 
L 7 HOH   54  854  794 HOH   HOH A . 
L 7 HOH   55  855  549 HOH   HOH A . 
L 7 HOH   56  856  504 HOH   HOH A . 
L 7 HOH   57  857  60  HOH   HOH A . 
L 7 HOH   58  858  496 HOH   HOH A . 
L 7 HOH   59  859  409 HOH   HOH A . 
L 7 HOH   60  860  610 HOH   HOH A . 
L 7 HOH   61  861  438 HOH   HOH A . 
L 7 HOH   62  862  477 HOH   HOH A . 
L 7 HOH   63  863  704 HOH   HOH A . 
L 7 HOH   64  864  54  HOH   HOH A . 
L 7 HOH   65  865  214 HOH   HOH A . 
L 7 HOH   66  866  774 HOH   HOH A . 
L 7 HOH   67  867  262 HOH   HOH A . 
L 7 HOH   68  868  372 HOH   HOH A . 
L 7 HOH   69  869  176 HOH   HOH A . 
L 7 HOH   70  870  11  HOH   HOH A . 
L 7 HOH   71  871  25  HOH   HOH A . 
L 7 HOH   72  872  90  HOH   HOH A . 
L 7 HOH   73  873  760 HOH   HOH A . 
L 7 HOH   74  874  183 HOH   HOH A . 
L 7 HOH   75  875  611 HOH   HOH A . 
L 7 HOH   76  876  27  HOH   HOH A . 
L 7 HOH   77  877  731 HOH   HOH A . 
L 7 HOH   78  878  204 HOH   HOH A . 
L 7 HOH   79  879  29  HOH   HOH A . 
L 7 HOH   80  880  124 HOH   HOH A . 
L 7 HOH   81  881  359 HOH   HOH A . 
L 7 HOH   82  882  133 HOH   HOH A . 
L 7 HOH   83  883  66  HOH   HOH A . 
L 7 HOH   84  884  206 HOH   HOH A . 
L 7 HOH   85  885  65  HOH   HOH A . 
L 7 HOH   86  886  7   HOH   HOH A . 
L 7 HOH   87  887  30  HOH   HOH A . 
L 7 HOH   88  888  620 HOH   HOH A . 
L 7 HOH   89  889  639 HOH   HOH A . 
L 7 HOH   90  890  502 HOH   HOH A . 
L 7 HOH   91  891  51  HOH   HOH A . 
L 7 HOH   92  892  614 HOH   HOH A . 
L 7 HOH   93  893  673 HOH   HOH A . 
L 7 HOH   94  894  34  HOH   HOH A . 
L 7 HOH   95  895  766 HOH   HOH A . 
L 7 HOH   96  896  488 HOH   HOH A . 
L 7 HOH   97  897  514 HOH   HOH A . 
L 7 HOH   98  898  117 HOH   HOH A . 
L 7 HOH   99  899  609 HOH   HOH A . 
L 7 HOH   100 900  485 HOH   HOH A . 
L 7 HOH   101 901  114 HOH   HOH A . 
L 7 HOH   102 902  40  HOH   HOH A . 
L 7 HOH   103 903  254 HOH   HOH A . 
L 7 HOH   104 904  418 HOH   HOH A . 
L 7 HOH   105 905  245 HOH   HOH A . 
L 7 HOH   106 906  244 HOH   HOH A . 
L 7 HOH   107 907  95  HOH   HOH A . 
L 7 HOH   108 908  137 HOH   HOH A . 
L 7 HOH   109 909  119 HOH   HOH A . 
L 7 HOH   110 910  220 HOH   HOH A . 
L 7 HOH   111 911  199 HOH   HOH A . 
L 7 HOH   112 912  158 HOH   HOH A . 
L 7 HOH   113 913  115 HOH   HOH A . 
L 7 HOH   114 914  505 HOH   HOH A . 
L 7 HOH   115 915  13  HOH   HOH A . 
L 7 HOH   116 916  603 HOH   HOH A . 
L 7 HOH   117 917  425 HOH   HOH A . 
L 7 HOH   118 918  122 HOH   HOH A . 
L 7 HOH   119 919  761 HOH   HOH A . 
L 7 HOH   120 920  557 HOH   HOH A . 
L 7 HOH   121 921  6   HOH   HOH A . 
L 7 HOH   122 922  697 HOH   HOH A . 
L 7 HOH   123 923  471 HOH   HOH A . 
L 7 HOH   124 924  59  HOH   HOH A . 
L 7 HOH   125 925  131 HOH   HOH A . 
L 7 HOH   126 926  132 HOH   HOH A . 
L 7 HOH   127 927  38  HOH   HOH A . 
L 7 HOH   128 928  23  HOH   HOH A . 
L 7 HOH   129 929  442 HOH   HOH A . 
L 7 HOH   130 930  272 HOH   HOH A . 
L 7 HOH   131 931  303 HOH   HOH A . 
L 7 HOH   132 932  100 HOH   HOH A . 
L 7 HOH   133 933  489 HOH   HOH A . 
L 7 HOH   134 934  334 HOH   HOH A . 
L 7 HOH   135 935  198 HOH   HOH A . 
L 7 HOH   136 936  17  HOH   HOH A . 
L 7 HOH   137 937  566 HOH   HOH A . 
L 7 HOH   138 938  680 HOH   HOH A . 
L 7 HOH   139 939  780 HOH   HOH A . 
L 7 HOH   140 940  439 HOH   HOH A . 
L 7 HOH   141 941  217 HOH   HOH A . 
L 7 HOH   142 942  377 HOH   HOH A . 
L 7 HOH   143 943  725 HOH   HOH A . 
L 7 HOH   144 944  2   HOH   HOH A . 
L 7 HOH   145 945  730 HOH   HOH A . 
L 7 HOH   146 946  91  HOH   HOH A . 
L 7 HOH   147 947  9   HOH   HOH A . 
L 7 HOH   148 948  456 HOH   HOH A . 
L 7 HOH   149 949  743 HOH   HOH A . 
L 7 HOH   150 950  619 HOH   HOH A . 
L 7 HOH   151 951  682 HOH   HOH A . 
L 7 HOH   152 952  545 HOH   HOH A . 
L 7 HOH   153 953  24  HOH   HOH A . 
L 7 HOH   154 954  400 HOH   HOH A . 
L 7 HOH   155 955  320 HOH   HOH A . 
L 7 HOH   156 956  295 HOH   HOH A . 
L 7 HOH   157 957  160 HOH   HOH A . 
L 7 HOH   158 958  108 HOH   HOH A . 
L 7 HOH   159 959  317 HOH   HOH A . 
L 7 HOH   160 960  484 HOH   HOH A . 
L 7 HOH   161 961  286 HOH   HOH A . 
L 7 HOH   162 962  75  HOH   HOH A . 
L 7 HOH   163 963  167 HOH   HOH A . 
L 7 HOH   164 964  288 HOH   HOH A . 
L 7 HOH   165 965  49  HOH   HOH A . 
L 7 HOH   166 966  562 HOH   HOH A . 
L 7 HOH   167 967  728 HOH   HOH A . 
L 7 HOH   168 968  791 HOH   HOH A . 
L 7 HOH   169 969  101 HOH   HOH A . 
L 7 HOH   170 970  366 HOH   HOH A . 
L 7 HOH   171 971  71  HOH   HOH A . 
L 7 HOH   172 972  333 HOH   HOH A . 
L 7 HOH   173 973  674 HOH   HOH A . 
L 7 HOH   174 974  169 HOH   HOH A . 
L 7 HOH   175 975  81  HOH   HOH A . 
L 7 HOH   176 976  135 HOH   HOH A . 
L 7 HOH   177 977  72  HOH   HOH A . 
L 7 HOH   178 978  376 HOH   HOH A . 
L 7 HOH   179 979  437 HOH   HOH A . 
L 7 HOH   180 980  77  HOH   HOH A . 
L 7 HOH   181 981  12  HOH   HOH A . 
L 7 HOH   182 982  629 HOH   HOH A . 
L 7 HOH   183 983  22  HOH   HOH A . 
L 7 HOH   184 984  121 HOH   HOH A . 
L 7 HOH   185 985  348 HOH   HOH A . 
L 7 HOH   186 986  104 HOH   HOH A . 
L 7 HOH   187 987  10  HOH   HOH A . 
L 7 HOH   188 988  308 HOH   HOH A . 
L 7 HOH   189 989  242 HOH   HOH A . 
L 7 HOH   190 990  94  HOH   HOH A . 
L 7 HOH   191 991  68  HOH   HOH A . 
L 7 HOH   192 992  649 HOH   HOH A . 
L 7 HOH   193 993  470 HOH   HOH A . 
L 7 HOH   194 994  69  HOH   HOH A . 
L 7 HOH   195 995  145 HOH   HOH A . 
L 7 HOH   196 996  401 HOH   HOH A . 
L 7 HOH   197 997  224 HOH   HOH A . 
L 7 HOH   198 998  457 HOH   HOH A . 
L 7 HOH   199 999  134 HOH   HOH A . 
L 7 HOH   200 1000 70  HOH   HOH A . 
L 7 HOH   201 1001 688 HOH   HOH A . 
L 7 HOH   202 1002 143 HOH   HOH A . 
L 7 HOH   203 1003 338 HOH   HOH A . 
L 7 HOH   204 1004 55  HOH   HOH A . 
L 7 HOH   205 1005 314 HOH   HOH A . 
L 7 HOH   206 1006 540 HOH   HOH A . 
L 7 HOH   207 1007 756 HOH   HOH A . 
L 7 HOH   208 1008 419 HOH   HOH A . 
L 7 HOH   209 1009 67  HOH   HOH A . 
L 7 HOH   210 1010 18  HOH   HOH A . 
L 7 HOH   211 1011 520 HOH   HOH A . 
L 7 HOH   212 1012 594 HOH   HOH A . 
L 7 HOH   213 1013 541 HOH   HOH A . 
L 7 HOH   214 1014 658 HOH   HOH A . 
L 7 HOH   215 1015 776 HOH   HOH A . 
L 7 HOH   216 1016 396 HOH   HOH A . 
L 7 HOH   217 1017 768 HOH   HOH A . 
L 7 HOH   218 1018 670 HOH   HOH A . 
L 7 HOH   219 1019 573 HOH   HOH A . 
L 7 HOH   220 1020 168 HOH   HOH A . 
L 7 HOH   221 1021 737 HOH   HOH A . 
L 7 HOH   222 1022 120 HOH   HOH A . 
L 7 HOH   223 1023 480 HOH   HOH A . 
L 7 HOH   224 1024 265 HOH   HOH A . 
L 7 HOH   225 1025 355 HOH   HOH A . 
L 7 HOH   226 1026 311 HOH   HOH A . 
L 7 HOH   227 1027 219 HOH   HOH A . 
L 7 HOH   228 1028 441 HOH   HOH A . 
L 7 HOH   229 1029 128 HOH   HOH A . 
L 7 HOH   230 1030 769 HOH   HOH A . 
L 7 HOH   231 1031 87  HOH   HOH A . 
L 7 HOH   232 1032 208 HOH   HOH A . 
L 7 HOH   233 1033 19  HOH   HOH A . 
L 7 HOH   234 1034 691 HOH   HOH A . 
L 7 HOH   235 1035 74  HOH   HOH A . 
L 7 HOH   236 1036 748 HOH   HOH A . 
L 7 HOH   237 1037 82  HOH   HOH A . 
L 7 HOH   238 1038 232 HOH   HOH A . 
L 7 HOH   239 1039 98  HOH   HOH A . 
L 7 HOH   240 1040 129 HOH   HOH A . 
L 7 HOH   241 1041 253 HOH   HOH A . 
L 7 HOH   242 1042 255 HOH   HOH A . 
L 7 HOH   243 1043 79  HOH   HOH A . 
L 7 HOH   244 1044 645 HOH   HOH A . 
L 7 HOH   245 1045 112 HOH   HOH A . 
L 7 HOH   246 1046 211 HOH   HOH A . 
L 7 HOH   247 1047 155 HOH   HOH A . 
L 7 HOH   248 1048 276 HOH   HOH A . 
L 7 HOH   249 1049 736 HOH   HOH A . 
L 7 HOH   250 1050 41  HOH   HOH A . 
L 7 HOH   251 1051 747 HOH   HOH A . 
L 7 HOH   252 1052 163 HOH   HOH A . 
L 7 HOH   253 1053 607 HOH   HOH A . 
L 7 HOH   254 1054 350 HOH   HOH A . 
L 7 HOH   255 1055 397 HOH   HOH A . 
L 7 HOH   256 1056 42  HOH   HOH A . 
L 7 HOH   257 1057 512 HOH   HOH A . 
L 7 HOH   258 1058 36  HOH   HOH A . 
L 7 HOH   259 1059 613 HOH   HOH A . 
L 7 HOH   260 1060 33  HOH   HOH A . 
L 7 HOH   261 1061 316 HOH   HOH A . 
L 7 HOH   262 1062 569 HOH   HOH A . 
L 7 HOH   263 1063 331 HOH   HOH A . 
L 7 HOH   264 1064 547 HOH   HOH A . 
L 7 HOH   265 1065 755 HOH   HOH A . 
L 7 HOH   266 1066 513 HOH   HOH A . 
L 7 HOH   267 1067 5   HOH   HOH A . 
L 7 HOH   268 1068 380 HOH   HOH A . 
L 7 HOH   269 1069 4   HOH   HOH A . 
L 7 HOH   270 1070 491 HOH   HOH A . 
L 7 HOH   271 1071 624 HOH   HOH A . 
L 7 HOH   272 1072 479 HOH   HOH A . 
L 7 HOH   273 1073 452 HOH   HOH A . 
L 7 HOH   274 1074 174 HOH   HOH A . 
L 7 HOH   275 1075 771 HOH   HOH A . 
L 7 HOH   276 1076 412 HOH   HOH A . 
L 7 HOH   277 1077 99  HOH   HOH A . 
L 7 HOH   278 1078 197 HOH   HOH A . 
L 7 HOH   279 1079 180 HOH   HOH A . 
L 7 HOH   280 1080 194 HOH   HOH A . 
L 7 HOH   281 1081 109 HOH   HOH A . 
L 7 HOH   282 1082 455 HOH   HOH A . 
L 7 HOH   283 1083 298 HOH   HOH A . 
L 7 HOH   284 1084 201 HOH   HOH A . 
L 7 HOH   285 1085 699 HOH   HOH A . 
L 7 HOH   286 1086 472 HOH   HOH A . 
L 7 HOH   287 1087 329 HOH   HOH A . 
L 7 HOH   288 1088 351 HOH   HOH A . 
L 7 HOH   289 1089 426 HOH   HOH A . 
L 7 HOH   290 1090 73  HOH   HOH A . 
L 7 HOH   291 1091 352 HOH   HOH A . 
L 7 HOH   292 1092 337 HOH   HOH A . 
L 7 HOH   293 1093 48  HOH   HOH A . 
L 7 HOH   294 1094 196 HOH   HOH A . 
L 7 HOH   295 1095 516 HOH   HOH A . 
L 7 HOH   296 1096 345 HOH   HOH A . 
L 7 HOH   297 1097 746 HOH   HOH A . 
L 7 HOH   298 1098 172 HOH   HOH A . 
L 7 HOH   299 1099 47  HOH   HOH A . 
L 7 HOH   300 1100 319 HOH   HOH A . 
L 7 HOH   301 1101 21  HOH   HOH A . 
L 7 HOH   302 1102 757 HOH   HOH A . 
L 7 HOH   303 1103 693 HOH   HOH A . 
L 7 HOH   304 1104 58  HOH   HOH A . 
L 7 HOH   305 1105 683 HOH   HOH A . 
L 7 HOH   306 1106 140 HOH   HOH A . 
L 7 HOH   307 1107 432 HOH   HOH A . 
L 7 HOH   308 1108 379 HOH   HOH A . 
L 7 HOH   309 1109 285 HOH   HOH A . 
L 7 HOH   310 1110 778 HOH   HOH A . 
L 7 HOH   311 1111 443 HOH   HOH A . 
L 7 HOH   312 1112 64  HOH   HOH A . 
L 7 HOH   313 1113 39  HOH   HOH A . 
L 7 HOH   314 1114 105 HOH   HOH A . 
L 7 HOH   315 1115 500 HOH   HOH A . 
L 7 HOH   316 1116 142 HOH   HOH A . 
L 7 HOH   317 1117 378 HOH   HOH A . 
L 7 HOH   318 1118 635 HOH   HOH A . 
L 7 HOH   319 1119 781 HOH   HOH A . 
L 7 HOH   320 1120 454 HOH   HOH A . 
L 7 HOH   321 1121 267 HOH   HOH A . 
L 7 HOH   322 1122 749 HOH   HOH A . 
L 7 HOH   323 1123 57  HOH   HOH A . 
L 7 HOH   324 1124 213 HOH   HOH A . 
L 7 HOH   325 1125 700 HOH   HOH A . 
L 7 HOH   326 1126 548 HOH   HOH A . 
L 7 HOH   327 1127 556 HOH   HOH A . 
L 7 HOH   328 1128 258 HOH   HOH A . 
L 7 HOH   329 1129 605 HOH   HOH A . 
L 7 HOH   330 1130 733 HOH   HOH A . 
L 7 HOH   331 1131 166 HOH   HOH A . 
L 7 HOH   332 1132 764 HOH   HOH A . 
L 7 HOH   333 1133 306 HOH   HOH A . 
L 7 HOH   334 1134 626 HOH   HOH A . 
L 7 HOH   335 1135 123 HOH   HOH A . 
L 7 HOH   336 1136 637 HOH   HOH A . 
L 7 HOH   337 1137 322 HOH   HOH A . 
L 7 HOH   338 1138 83  HOH   HOH A . 
L 7 HOH   339 1139 103 HOH   HOH A . 
L 7 HOH   340 1140 357 HOH   HOH A . 
L 7 HOH   341 1141 395 HOH   HOH A . 
L 7 HOH   342 1142 302 HOH   HOH A . 
L 7 HOH   343 1143 672 HOH   HOH A . 
L 7 HOH   344 1144 503 HOH   HOH A . 
L 7 HOH   345 1145 203 HOH   HOH A . 
L 7 HOH   346 1146 289 HOH   HOH A . 
L 7 HOH   347 1147 475 HOH   HOH A . 
L 7 HOH   348 1148 654 HOH   HOH A . 
L 7 HOH   349 1149 474 HOH   HOH A . 
L 7 HOH   350 1150 16  HOH   HOH A . 
L 7 HOH   351 1151 495 HOH   HOH A . 
L 7 HOH   352 1152 188 HOH   HOH A . 
L 7 HOH   353 1153 28  HOH   HOH A . 
L 7 HOH   354 1154 539 HOH   HOH A . 
L 7 HOH   355 1155 116 HOH   HOH A . 
L 7 HOH   356 1156 110 HOH   HOH A . 
L 7 HOH   357 1157 305 HOH   HOH A . 
L 7 HOH   358 1158 770 HOH   HOH A . 
L 7 HOH   359 1159 411 HOH   HOH A . 
L 7 HOH   360 1160 63  HOH   HOH A . 
L 7 HOH   361 1161 465 HOH   HOH A . 
L 7 HOH   362 1162 476 HOH   HOH A . 
L 7 HOH   363 1163 43  HOH   HOH A . 
L 7 HOH   364 1164 536 HOH   HOH A . 
L 7 HOH   365 1165 434 HOH   HOH A . 
L 7 HOH   366 1166 268 HOH   HOH A . 
L 7 HOH   367 1167 433 HOH   HOH A . 
L 7 HOH   368 1168 628 HOH   HOH A . 
L 7 HOH   369 1169 279 HOH   HOH A . 
L 7 HOH   370 1170 790 HOH   HOH A . 
L 7 HOH   371 1171 595 HOH   HOH A . 
L 7 HOH   372 1172 246 HOH   HOH A . 
L 7 HOH   373 1173 291 HOH   HOH A . 
L 7 HOH   374 1174 591 HOH   HOH A . 
L 7 HOH   375 1175 179 HOH   HOH A . 
L 7 HOH   376 1176 787 HOH   HOH A . 
L 7 HOH   377 1177 53  HOH   HOH A . 
L 7 HOH   378 1178 207 HOH   HOH A . 
L 7 HOH   379 1179 801 HOH   HOH A . 
L 7 HOH   380 1180 423 HOH   HOH A . 
L 7 HOH   381 1181 604 HOH   HOH A . 
L 7 HOH   382 1182 714 HOH   HOH A . 
L 7 HOH   383 1183 403 HOH   HOH A . 
L 7 HOH   384 1184 431 HOH   HOH A . 
L 7 HOH   385 1185 402 HOH   HOH A . 
L 7 HOH   386 1186 721 HOH   HOH A . 
L 7 HOH   387 1187 779 HOH   HOH A . 
L 7 HOH   388 1188 494 HOH   HOH A . 
L 7 HOH   389 1189 186 HOH   HOH A . 
L 7 HOH   390 1190 364 HOH   HOH A . 
L 7 HOH   391 1191 550 HOH   HOH A . 
L 7 HOH   392 1192 751 HOH   HOH A . 
L 7 HOH   393 1193 517 HOH   HOH A . 
L 7 HOH   394 1194 593 HOH   HOH A . 
L 7 HOH   395 1195 581 HOH   HOH A . 
L 7 HOH   396 1196 601 HOH   HOH A . 
L 7 HOH   397 1197 782 HOH   HOH A . 
L 7 HOH   398 1198 189 HOH   HOH A . 
L 7 HOH   399 1199 686 HOH   HOH A . 
L 7 HOH   400 1200 8   HOH   HOH A . 
L 7 HOH   401 1201 32  HOH   HOH A . 
L 7 HOH   402 1202 187 HOH   HOH A . 
L 7 HOH   403 1203 209 HOH   HOH A . 
L 7 HOH   404 1204 499 HOH   HOH A . 
L 7 HOH   405 1205 97  HOH   HOH A . 
L 7 HOH   406 1206 648 HOH   HOH A . 
L 7 HOH   407 1207 462 HOH   HOH A . 
L 7 HOH   408 1208 644 HOH   HOH A . 
L 7 HOH   409 1209 598 HOH   HOH A . 
L 7 HOH   410 1210 519 HOH   HOH A . 
L 7 HOH   411 1211 421 HOH   HOH A . 
L 7 HOH   412 1212 796 HOH   HOH A . 
L 7 HOH   413 1213 578 HOH   HOH A . 
L 7 HOH   414 1214 458 HOH   HOH A . 
L 7 HOH   415 1215 416 HOH   HOH A . 
L 7 HOH   416 1216 795 HOH   HOH A . 
L 7 HOH   417 1217 625 HOH   HOH A . 
L 7 HOH   418 1218 665 HOH   HOH A . 
L 7 HOH   419 1219 723 HOH   HOH A . 
L 7 HOH   420 1220 724 HOH   HOH A . 
L 7 HOH   421 1221 62  HOH   HOH A . 
L 7 HOH   422 1222 650 HOH   HOH A . 
L 7 HOH   423 1223 294 HOH   HOH A . 
L 7 HOH   424 1224 275 HOH   HOH A . 
L 7 HOH   425 1225 565 HOH   HOH A . 
L 7 HOH   426 1226 506 HOH   HOH A . 
L 7 HOH   427 1227 802 HOH   HOH A . 
L 7 HOH   428 1228 353 HOH   HOH A . 
L 7 HOH   429 1229 784 HOH   HOH A . 
L 7 HOH   430 1230 218 HOH   HOH A . 
L 7 HOH   431 1231 381 HOH   HOH A . 
L 7 HOH   432 1232 656 HOH   HOH A . 
L 7 HOH   433 1233 643 HOH   HOH A . 
L 7 HOH   434 1234 786 HOH   HOH A . 
L 7 HOH   435 1235 722 HOH   HOH A . 
L 7 HOH   436 1236 586 HOH   HOH A . 
L 7 HOH   437 1237 165 HOH   HOH A . 
L 7 HOH   438 1238 668 HOH   HOH A . 
L 7 HOH   439 1239 775 HOH   HOH A . 
L 7 HOH   440 1240 671 HOH   HOH A . 
L 7 HOH   441 1241 325 HOH   HOH A . 
L 7 HOH   442 1242 642 HOH   HOH A . 
L 7 HOH   443 1243 662 HOH   HOH A . 
L 7 HOH   444 1244 327 HOH   HOH A . 
L 7 HOH   445 1245 358 HOH   HOH A . 
L 7 HOH   446 1246 627 HOH   HOH A . 
M 7 HOH   1   801  544 HOH   HOH B . 
M 7 HOH   2   802  589 HOH   HOH B . 
M 7 HOH   3   803  630 HOH   HOH B . 
M 7 HOH   4   804  750 HOH   HOH B . 
M 7 HOH   5   805  473 HOH   HOH B . 
M 7 HOH   6   806  318 HOH   HOH B . 
M 7 HOH   7   807  393 HOH   HOH B . 
M 7 HOH   8   808  468 HOH   HOH B . 
M 7 HOH   9   809  427 HOH   HOH B . 
M 7 HOH   10  810  510 HOH   HOH B . 
M 7 HOH   11  811  577 HOH   HOH B . 
M 7 HOH   12  812  677 HOH   HOH B . 
M 7 HOH   13  813  215 HOH   HOH B . 
M 7 HOH   14  814  618 HOH   HOH B . 
M 7 HOH   15  815  341 HOH   HOH B . 
M 7 HOH   16  816  464 HOH   HOH B . 
M 7 HOH   17  817  300 HOH   HOH B . 
M 7 HOH   18  818  571 HOH   HOH B . 
M 7 HOH   19  819  113 HOH   HOH B . 
M 7 HOH   20  820  96  HOH   HOH B . 
M 7 HOH   21  821  546 HOH   HOH B . 
M 7 HOH   22  822  692 HOH   HOH B . 
M 7 HOH   23  823  269 HOH   HOH B . 
M 7 HOH   24  824  107 HOH   HOH B . 
M 7 HOH   25  825  111 HOH   HOH B . 
M 7 HOH   26  826  1   HOH   HOH B . 
M 7 HOH   27  827  580 HOH   HOH B . 
M 7 HOH   28  828  282 HOH   HOH B . 
M 7 HOH   29  829  388 HOH   HOH B . 
M 7 HOH   30  830  685 HOH   HOH B . 
M 7 HOH   31  831  574 HOH   HOH B . 
M 7 HOH   32  832  296 HOH   HOH B . 
M 7 HOH   33  833  424 HOH   HOH B . 
M 7 HOH   34  834  568 HOH   HOH B . 
M 7 HOH   35  835  250 HOH   HOH B . 
M 7 HOH   36  836  762 HOH   HOH B . 
M 7 HOH   37  837  596 HOH   HOH B . 
M 7 HOH   38  838  450 HOH   HOH B . 
M 7 HOH   39  839  570 HOH   HOH B . 
M 7 HOH   40  840  385 HOH   HOH B . 
M 7 HOH   41  841  533 HOH   HOH B . 
M 7 HOH   42  842  229 HOH   HOH B . 
M 7 HOH   43  843  487 HOH   HOH B . 
M 7 HOH   44  844  86  HOH   HOH B . 
M 7 HOH   45  845  469 HOH   HOH B . 
M 7 HOH   46  846  370 HOH   HOH B . 
M 7 HOH   47  847  451 HOH   HOH B . 
M 7 HOH   48  848  572 HOH   HOH B . 
M 7 HOH   49  849  526 HOH   HOH B . 
M 7 HOH   50  850  35  HOH   HOH B . 
M 7 HOH   51  851  616 HOH   HOH B . 
M 7 HOH   52  852  524 HOH   HOH B . 
M 7 HOH   53  853  719 HOH   HOH B . 
M 7 HOH   54  854  3   HOH   HOH B . 
M 7 HOH   55  855  20  HOH   HOH B . 
M 7 HOH   56  856  222 HOH   HOH B . 
M 7 HOH   57  857  615 HOH   HOH B . 
M 7 HOH   58  858  675 HOH   HOH B . 
M 7 HOH   59  859  636 HOH   HOH B . 
M 7 HOH   60  860  184 HOH   HOH B . 
M 7 HOH   61  861  561 HOH   HOH B . 
M 7 HOH   62  862  202 HOH   HOH B . 
M 7 HOH   63  863  414 HOH   HOH B . 
M 7 HOH   64  864  263 HOH   HOH B . 
M 7 HOH   65  865  46  HOH   HOH B . 
M 7 HOH   66  866  146 HOH   HOH B . 
M 7 HOH   67  867  335 HOH   HOH B . 
M 7 HOH   68  868  368 HOH   HOH B . 
M 7 HOH   69  869  375 HOH   HOH B . 
M 7 HOH   70  870  408 HOH   HOH B . 
M 7 HOH   71  871  459 HOH   HOH B . 
M 7 HOH   72  872  634 HOH   HOH B . 
M 7 HOH   73  873  149 HOH   HOH B . 
M 7 HOH   74  874  235 HOH   HOH B . 
M 7 HOH   75  875  695 HOH   HOH B . 
M 7 HOH   76  876  210 HOH   HOH B . 
M 7 HOH   77  877  283 HOH   HOH B . 
M 7 HOH   78  878  371 HOH   HOH B . 
M 7 HOH   79  879  78  HOH   HOH B . 
M 7 HOH   80  880  281 HOH   HOH B . 
M 7 HOH   81  881  256 HOH   HOH B . 
M 7 HOH   82  882  788 HOH   HOH B . 
M 7 HOH   83  883  328 HOH   HOH B . 
M 7 HOH   84  884  92  HOH   HOH B . 
M 7 HOH   85  885  448 HOH   HOH B . 
M 7 HOH   86  886  346 HOH   HOH B . 
M 7 HOH   87  887  227 HOH   HOH B . 
M 7 HOH   88  888  600 HOH   HOH B . 
M 7 HOH   89  889  407 HOH   HOH B . 
M 7 HOH   90  890  231 HOH   HOH B . 
M 7 HOH   91  891  436 HOH   HOH B . 
M 7 HOH   92  892  712 HOH   HOH B . 
M 7 HOH   93  893  257 HOH   HOH B . 
M 7 HOH   94  894  763 HOH   HOH B . 
M 7 HOH   95  895  587 HOH   HOH B . 
M 7 HOH   96  896  705 HOH   HOH B . 
M 7 HOH   97  897  726 HOH   HOH B . 
M 7 HOH   98  898  354 HOH   HOH B . 
M 7 HOH   99  899  264 HOH   HOH B . 
M 7 HOH   100 900  523 HOH   HOH B . 
M 7 HOH   101 901  340 HOH   HOH B . 
M 7 HOH   102 902  678 HOH   HOH B . 
M 7 HOH   103 903  343 HOH   HOH B . 
M 7 HOH   104 904  710 HOH   HOH B . 
M 7 HOH   105 905  185 HOH   HOH B . 
M 7 HOH   106 906  486 HOH   HOH B . 
M 7 HOH   107 907  430 HOH   HOH B . 
M 7 HOH   108 908  490 HOH   HOH B . 
M 7 HOH   109 909  152 HOH   HOH B . 
M 7 HOH   110 910  753 HOH   HOH B . 
M 7 HOH   111 911  398 HOH   HOH B . 
M 7 HOH   112 912  310 HOH   HOH B . 
M 7 HOH   113 913  360 HOH   HOH B . 
M 7 HOH   114 914  297 HOH   HOH B . 
M 7 HOH   115 915  323 HOH   HOH B . 
M 7 HOH   116 916  521 HOH   HOH B . 
M 7 HOH   117 917  301 HOH   HOH B . 
M 7 HOH   118 918  518 HOH   HOH B . 
M 7 HOH   119 919  553 HOH   HOH B . 
M 7 HOH   120 920  178 HOH   HOH B . 
M 7 HOH   121 921  344 HOH   HOH B . 
M 7 HOH   122 922  93  HOH   HOH B . 
M 7 HOH   123 923  315 HOH   HOH B . 
M 7 HOH   124 924  195 HOH   HOH B . 
M 7 HOH   125 925  290 HOH   HOH B . 
M 7 HOH   126 926  130 HOH   HOH B . 
M 7 HOH   127 927  125 HOH   HOH B . 
M 7 HOH   128 928  399 HOH   HOH B . 
M 7 HOH   129 929  694 HOH   HOH B . 
M 7 HOH   130 930  716 HOH   HOH B . 
M 7 HOH   131 931  741 HOH   HOH B . 
M 7 HOH   132 932  173 HOH   HOH B . 
M 7 HOH   133 933  85  HOH   HOH B . 
M 7 HOH   134 934  193 HOH   HOH B . 
M 7 HOH   135 935  532 HOH   HOH B . 
M 7 HOH   136 936  156 HOH   HOH B . 
M 7 HOH   137 937  236 HOH   HOH B . 
M 7 HOH   138 938  415 HOH   HOH B . 
M 7 HOH   139 939  641 HOH   HOH B . 
M 7 HOH   140 940  555 HOH   HOH B . 
M 7 HOH   141 941  139 HOH   HOH B . 
M 7 HOH   142 942  330 HOH   HOH B . 
M 7 HOH   143 943  151 HOH   HOH B . 
M 7 HOH   144 944  234 HOH   HOH B . 
M 7 HOH   145 945  228 HOH   HOH B . 
M 7 HOH   146 946  527 HOH   HOH B . 
M 7 HOH   147 947  212 HOH   HOH B . 
M 7 HOH   148 948  535 HOH   HOH B . 
M 7 HOH   149 949  154 HOH   HOH B . 
M 7 HOH   150 950  284 HOH   HOH B . 
M 7 HOH   151 951  102 HOH   HOH B . 
M 7 HOH   152 952  52  HOH   HOH B . 
M 7 HOH   153 953  321 HOH   HOH B . 
M 7 HOH   154 954  192 HOH   HOH B . 
M 7 HOH   155 955  237 HOH   HOH B . 
M 7 HOH   156 956  118 HOH   HOH B . 
M 7 HOH   157 957  339 HOH   HOH B . 
M 7 HOH   158 958  446 HOH   HOH B . 
M 7 HOH   159 959  225 HOH   HOH B . 
M 7 HOH   160 960  413 HOH   HOH B . 
M 7 HOH   161 961  280 HOH   HOH B . 
M 7 HOH   162 962  177 HOH   HOH B . 
M 7 HOH   163 963  404 HOH   HOH B . 
M 7 HOH   164 964  612 HOH   HOH B . 
M 7 HOH   165 965  392 HOH   HOH B . 
M 7 HOH   166 966  80  HOH   HOH B . 
M 7 HOH   167 967  498 HOH   HOH B . 
M 7 HOH   168 968  56  HOH   HOH B . 
M 7 HOH   169 969  247 HOH   HOH B . 
M 7 HOH   170 970  309 HOH   HOH B . 
M 7 HOH   171 971  259 HOH   HOH B . 
M 7 HOH   172 972  248 HOH   HOH B . 
M 7 HOH   173 973  420 HOH   HOH B . 
M 7 HOH   174 974  159 HOH   HOH B . 
M 7 HOH   175 975  676 HOH   HOH B . 
M 7 HOH   176 976  312 HOH   HOH B . 
M 7 HOH   177 977  684 HOH   HOH B . 
M 7 HOH   178 978  153 HOH   HOH B . 
M 7 HOH   179 979  170 HOH   HOH B . 
M 7 HOH   180 980  84  HOH   HOH B . 
M 7 HOH   181 981  270 HOH   HOH B . 
M 7 HOH   182 982  789 HOH   HOH B . 
M 7 HOH   183 983  369 HOH   HOH B . 
M 7 HOH   184 984  205 HOH   HOH B . 
M 7 HOH   185 985  136 HOH   HOH B . 
M 7 HOH   186 986  703 HOH   HOH B . 
M 7 HOH   187 987  449 HOH   HOH B . 
M 7 HOH   188 988  162 HOH   HOH B . 
M 7 HOH   189 989  390 HOH   HOH B . 
M 7 HOH   190 990  148 HOH   HOH B . 
M 7 HOH   191 991  50  HOH   HOH B . 
M 7 HOH   192 992  460 HOH   HOH B . 
M 7 HOH   193 993  223 HOH   HOH B . 
M 7 HOH   194 994  531 HOH   HOH B . 
M 7 HOH   195 995  26  HOH   HOH B . 
M 7 HOH   196 996  238 HOH   HOH B . 
M 7 HOH   197 997  466 HOH   HOH B . 
M 7 HOH   198 998  141 HOH   HOH B . 
M 7 HOH   199 999  729 HOH   HOH B . 
M 7 HOH   200 1000 478 HOH   HOH B . 
M 7 HOH   201 1001 783 HOH   HOH B . 
M 7 HOH   202 1002 444 HOH   HOH B . 
M 7 HOH   203 1003 554 HOH   HOH B . 
M 7 HOH   204 1004 365 HOH   HOH B . 
M 7 HOH   205 1005 347 HOH   HOH B . 
M 7 HOH   206 1006 383 HOH   HOH B . 
M 7 HOH   207 1007 583 HOH   HOH B . 
M 7 HOH   208 1008 273 HOH   HOH B . 
M 7 HOH   209 1009 240 HOH   HOH B . 
M 7 HOH   210 1010 445 HOH   HOH B . 
M 7 HOH   211 1011 417 HOH   HOH B . 
M 7 HOH   212 1012 157 HOH   HOH B . 
M 7 HOH   213 1013 106 HOH   HOH B . 
M 7 HOH   214 1014 690 HOH   HOH B . 
M 7 HOH   215 1015 88  HOH   HOH B . 
M 7 HOH   216 1016 382 HOH   HOH B . 
M 7 HOH   217 1017 579 HOH   HOH B . 
M 7 HOH   218 1018 261 HOH   HOH B . 
M 7 HOH   219 1019 734 HOH   HOH B . 
M 7 HOH   220 1020 597 HOH   HOH B . 
M 7 HOH   221 1021 602 HOH   HOH B . 
M 7 HOH   222 1022 299 HOH   HOH B . 
M 7 HOH   223 1023 463 HOH   HOH B . 
M 7 HOH   224 1024 706 HOH   HOH B . 
M 7 HOH   225 1025 507 HOH   HOH B . 
M 7 HOH   226 1026 543 HOH   HOH B . 
M 7 HOH   227 1027 493 HOH   HOH B . 
M 7 HOH   228 1028 727 HOH   HOH B . 
M 7 HOH   229 1029 405 HOH   HOH B . 
M 7 HOH   230 1030 509 HOH   HOH B . 
M 7 HOH   231 1031 181 HOH   HOH B . 
M 7 HOH   232 1032 715 HOH   HOH B . 
M 7 HOH   233 1033 127 HOH   HOH B . 
M 7 HOH   234 1034 740 HOH   HOH B . 
M 7 HOH   235 1035 271 HOH   HOH B . 
M 7 HOH   236 1036 575 HOH   HOH B . 
M 7 HOH   237 1037 738 HOH   HOH B . 
M 7 HOH   238 1038 367 HOH   HOH B . 
M 7 HOH   239 1039 150 HOH   HOH B . 
M 7 HOH   240 1040 534 HOH   HOH B . 
M 7 HOH   241 1041 482 HOH   HOH B . 
M 7 HOH   242 1042 182 HOH   HOH B . 
M 7 HOH   243 1043 742 HOH   HOH B . 
M 7 HOH   244 1044 277 HOH   HOH B . 
M 7 HOH   245 1045 590 HOH   HOH B . 
M 7 HOH   246 1046 681 HOH   HOH B . 
M 7 HOH   247 1047 511 HOH   HOH B . 
M 7 HOH   248 1048 387 HOH   HOH B . 
M 7 HOH   249 1049 698 HOH   HOH B . 
M 7 HOH   250 1050 230 HOH   HOH B . 
M 7 HOH   251 1051 701 HOH   HOH B . 
M 7 HOH   252 1052 623 HOH   HOH B . 
M 7 HOH   253 1053 161 HOH   HOH B . 
M 7 HOH   254 1054 221 HOH   HOH B . 
M 7 HOH   255 1055 732 HOH   HOH B . 
M 7 HOH   256 1056 89  HOH   HOH B . 
M 7 HOH   257 1057 249 HOH   HOH B . 
M 7 HOH   258 1058 708 HOH   HOH B . 
M 7 HOH   259 1059 394 HOH   HOH B . 
M 7 HOH   260 1060 429 HOH   HOH B . 
M 7 HOH   261 1061 304 HOH   HOH B . 
M 7 HOH   262 1062 126 HOH   HOH B . 
M 7 HOH   263 1063 735 HOH   HOH B . 
M 7 HOH   264 1064 525 HOH   HOH B . 
M 7 HOH   265 1065 356 HOH   HOH B . 
M 7 HOH   266 1066 324 HOH   HOH B . 
M 7 HOH   267 1067 515 HOH   HOH B . 
M 7 HOH   268 1068 709 HOH   HOH B . 
M 7 HOH   269 1069 552 HOH   HOH B . 
M 7 HOH   270 1070 406 HOH   HOH B . 
M 7 HOH   271 1071 537 HOH   HOH B . 
M 7 HOH   272 1072 759 HOH   HOH B . 
M 7 HOH   273 1073 287 HOH   HOH B . 
M 7 HOH   274 1074 696 HOH   HOH B . 
M 7 HOH   275 1075 663 HOH   HOH B . 
M 7 HOH   276 1076 632 HOH   HOH B . 
M 7 HOH   277 1077 754 HOH   HOH B . 
M 7 HOH   278 1078 564 HOH   HOH B . 
M 7 HOH   279 1079 422 HOH   HOH B . 
M 7 HOH   280 1080 374 HOH   HOH B . 
M 7 HOH   281 1081 216 HOH   HOH B . 
M 7 HOH   282 1082 274 HOH   HOH B . 
M 7 HOH   283 1083 363 HOH   HOH B . 
M 7 HOH   284 1084 529 HOH   HOH B . 
M 7 HOH   285 1085 689 HOH   HOH B . 
M 7 HOH   286 1086 702 HOH   HOH B . 
M 7 HOH   287 1087 711 HOH   HOH B . 
M 7 HOH   288 1088 492 HOH   HOH B . 
M 7 HOH   289 1089 744 HOH   HOH B . 
M 7 HOH   290 1090 772 HOH   HOH B . 
M 7 HOH   291 1091 461 HOH   HOH B . 
M 7 HOH   292 1092 559 HOH   HOH B . 
M 7 HOH   293 1093 660 HOH   HOH B . 
M 7 HOH   294 1094 410 HOH   HOH B . 
M 7 HOH   295 1095 332 HOH   HOH B . 
M 7 HOH   296 1096 739 HOH   HOH B . 
M 7 HOH   297 1097 720 HOH   HOH B . 
M 7 HOH   298 1098 687 HOH   HOH B . 
M 7 HOH   299 1099 349 HOH   HOH B . 
M 7 HOH   300 1100 530 HOH   HOH B . 
M 7 HOH   301 1101 617 HOH   HOH B . 
M 7 HOH   302 1102 522 HOH   HOH B . 
M 7 HOH   303 1103 386 HOH   HOH B . 
M 7 HOH   304 1104 481 HOH   HOH B . 
M 7 HOH   305 1105 326 HOH   HOH B . 
M 7 HOH   306 1106 447 HOH   HOH B . 
M 7 HOH   307 1107 147 HOH   HOH B . 
M 7 HOH   308 1108 164 HOH   HOH B . 
M 7 HOH   309 1109 440 HOH   HOH B . 
M 7 HOH   310 1110 652 HOH   HOH B . 
M 7 HOH   311 1111 666 HOH   HOH B . 
M 7 HOH   312 1112 313 HOH   HOH B . 
M 7 HOH   313 1113 453 HOH   HOH B . 
M 7 HOH   314 1114 659 HOH   HOH B . 
M 7 HOH   315 1115 175 HOH   HOH B . 
M 7 HOH   316 1116 606 HOH   HOH B . 
M 7 HOH   317 1117 14  HOH   HOH B . 
M 7 HOH   318 1118 558 HOH   HOH B . 
M 7 HOH   319 1119 621 HOH   HOH B . 
M 7 HOH   320 1120 679 HOH   HOH B . 
M 7 HOH   321 1121 640 HOH   HOH B . 
M 7 HOH   322 1122 307 HOH   HOH B . 
M 7 HOH   323 1123 765 HOH   HOH B . 
M 7 HOH   324 1124 713 HOH   HOH B . 
M 7 HOH   325 1125 497 HOH   HOH B . 
M 7 HOH   326 1126 655 HOH   HOH B . 
M 7 HOH   327 1127 608 HOH   HOH B . 
M 7 HOH   328 1128 661 HOH   HOH B . 
M 7 HOH   329 1129 467 HOH   HOH B . 
M 7 HOH   330 1130 785 HOH   HOH B . 
M 7 HOH   331 1131 278 HOH   HOH B . 
M 7 HOH   332 1132 551 HOH   HOH B . 
M 7 HOH   333 1133 538 HOH   HOH B . 
M 7 HOH   334 1134 501 HOH   HOH B . 
M 7 HOH   335 1135 669 HOH   HOH B . 
M 7 HOH   336 1136 576 HOH   HOH B . 
M 7 HOH   337 1137 582 HOH   HOH B . 
M 7 HOH   338 1138 793 HOH   HOH B . 
M 7 HOH   339 1139 542 HOH   HOH B . 
M 7 HOH   340 1140 651 HOH   HOH B . 
M 7 HOH   341 1141 373 HOH   HOH B . 
M 7 HOH   342 1142 638 HOH   HOH B . 
M 7 HOH   343 1143 647 HOH   HOH B . 
M 7 HOH   344 1144 717 HOH   HOH B . 
M 7 HOH   345 1145 653 HOH   HOH B . 
M 7 HOH   346 1146 342 HOH   HOH B . 
M 7 HOH   347 1147 633 HOH   HOH B . 
M 7 HOH   348 1148 792 HOH   HOH B . 
M 7 HOH   349 1149 560 HOH   HOH B . 
M 7 HOH   350 1150 646 HOH   HOH B . 
M 7 HOH   351 1151 528 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? CRANK2  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.93 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J6N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.364 
_cell.length_a_esd                 ? 
_cell.length_b                     57.346 
_cell.length_b_esd                 ? 
_cell.length_c                     109.732 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9J6N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_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                   9J6N 
_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             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.10 
_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              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '75mM potassium thiocyanate (KSCN), 25% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-28 
_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                    'Numerical link type Si(111) double crystal' 
_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   1.000 
_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                        'PHOTON FACTORY BEAMLINE AR-NW12A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   AR-NW12A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          9.55 
_reflns.entry_id                                       9J6N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               47.46 
_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                                     110248 
_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                           98.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.061 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.097 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5375 
_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                               3.4 
_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                               0.409 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.658 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.641 
_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]                            -0.30 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.01 
_refine.aniso_B[2][2]                            0.29 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.01 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.337 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9J6N 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             47.46 
_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                     104798 
_refine.ls_number_reflns_R_free                  5434 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.96 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15508 
_refine.ls_R_factor_R_free                       0.18934 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15332 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.104 
_refine.pdbx_overall_ESU_R_Free                  0.101 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.236 
_refine.overall_SU_ML                            0.072 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        47.46 
_refine_hist.number_atoms_solvent             797 
_refine_hist.number_atoms_total               9866 
_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        8989 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  9342  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  8601  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.697  1.808  12782 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.595  1.757  19722 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.205  5.000  1160  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.608  5.000  81    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.618 10.000 1350  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.085  0.200  1391  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  11464 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  2276  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.439  1.519  4631  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.429  1.519  4630  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.057  2.724  5782  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.057  2.725  5783  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.856  1.661  4711  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.856  1.661  4712  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.820  2.982  6997  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.175  16.01  10486 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.025  15.20  10311 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             369 
_refine_ls_shell.number_reflns_R_work             7687 
_refine_ls_shell.percent_reflns_obs               96.66 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.236 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.283 
# 
_struct.entry_id                     9J6N 
_struct.title                        'beta-D-galactofuranosidase ORF1110 from Streptomyces sp. JHA19, D-iminogalactitol complex' 
_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        9J6N 
_struct_keywords.text            'Glycoside Hydrolase Family 2, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 7 ? 
M N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0K2SRV3_9ACTN 
_struct_ref.pdbx_db_accession          A0A0K2SRV3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APRAWTPKPSPMTTPWTDQVPVDNPLPEYPRPQLTRPDWANLNGIWDFAVTSANAGQPATFPEQIRVPFVAESALSGIQR
KITQNDKLWYKRTFTVPSNWNGRRVQLNFGASDWRTTVWVNGRQAGAVHSGGYDAFSYDVTDLLTAGTNTLVVSVWDPTE
TGTQAVGKQRIRDVAPHPGGGILYTAASGIWQTVWLEPTAAAHVTRLDLVPDPANSRLKVTVRGAGISGHQARVTVSTGG
TTVGTATGPVGTEFTVPVPNPRLWTPEDPFLYDVRADPLSGGTTVDSVGSYTGMRTIALASVGGHQRPVLNGKFVFQTGT
LDQGYWPDGIYTAPTDAALRHDLQKHKDLGFNMVRKHIKVEPQRWFYWADRLGLLVWQDMPNMERTPDAAARTQWEAEYD
RIIDQHRSSPSLVLWVNQNEGWGQYDQARLADKVKAYDPTRLVDNMSGVNCCGAVDGGNGDVVDHHVYVGPGTTVPSATR
AAVLGEFGGLGFKVAGHEWYPGGGFSYEDQPDLAHLNNRFVGLIDAIREVRMPRGLSASVYTEITDVENEVNGLLTYDRQ
VVKVDEARVRAANRALIDASRGTTAPLTLPV
;
_struct_ref.pdbx_align_begin           45 
# 
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 9J6N A 22 ? 612 ? A0A0K2SRV3 45 ? 635 ? 45 635 
2 1 9J6N B 22 ? 612 ? A0A0K2SRV3 45 ? 635 ? 45 635 
# 
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 9J6N MET A 1  ? UNP A0A0K2SRV3 ? ? 'initiating methionine' 24 1  
1 9J6N GLY A 2  ? UNP A0A0K2SRV3 ? ? 'expression tag'        25 2  
1 9J6N SER A 3  ? UNP A0A0K2SRV3 ? ? 'expression tag'        26 3  
1 9J6N SER A 4  ? UNP A0A0K2SRV3 ? ? 'expression tag'        27 4  
1 9J6N HIS A 5  ? UNP A0A0K2SRV3 ? ? 'expression tag'        28 5  
1 9J6N HIS A 6  ? UNP A0A0K2SRV3 ? ? 'expression tag'        29 6  
1 9J6N HIS A 7  ? UNP A0A0K2SRV3 ? ? 'expression tag'        30 7  
1 9J6N HIS A 8  ? UNP A0A0K2SRV3 ? ? 'expression tag'        31 8  
1 9J6N HIS A 9  ? UNP A0A0K2SRV3 ? ? 'expression tag'        32 9  
1 9J6N HIS A 10 ? UNP A0A0K2SRV3 ? ? 'expression tag'        33 10 
1 9J6N SER A 11 ? UNP A0A0K2SRV3 ? ? 'expression tag'        34 11 
1 9J6N ALA A 12 ? UNP A0A0K2SRV3 ? ? 'expression tag'        35 12 
1 9J6N ALA A 13 ? UNP A0A0K2SRV3 ? ? 'expression tag'        36 13 
1 9J6N LEU A 14 ? UNP A0A0K2SRV3 ? ? 'expression tag'        37 14 
1 9J6N GLU A 15 ? UNP A0A0K2SRV3 ? ? 'expression tag'        38 15 
1 9J6N VAL A 16 ? UNP A0A0K2SRV3 ? ? 'expression tag'        39 16 
1 9J6N LEU A 17 ? UNP A0A0K2SRV3 ? ? 'expression tag'        40 17 
1 9J6N PHE A 18 ? UNP A0A0K2SRV3 ? ? 'expression tag'        41 18 
1 9J6N GLN A 19 ? UNP A0A0K2SRV3 ? ? 'expression tag'        42 19 
1 9J6N GLY A 20 ? UNP A0A0K2SRV3 ? ? 'expression tag'        43 20 
1 9J6N PRO A 21 ? UNP A0A0K2SRV3 ? ? 'expression tag'        44 21 
2 9J6N MET B 1  ? UNP A0A0K2SRV3 ? ? 'initiating methionine' 24 22 
2 9J6N GLY B 2  ? UNP A0A0K2SRV3 ? ? 'expression tag'        25 23 
2 9J6N SER B 3  ? UNP A0A0K2SRV3 ? ? 'expression tag'        26 24 
2 9J6N SER B 4  ? UNP A0A0K2SRV3 ? ? 'expression tag'        27 25 
2 9J6N HIS B 5  ? UNP A0A0K2SRV3 ? ? 'expression tag'        28 26 
2 9J6N HIS B 6  ? UNP A0A0K2SRV3 ? ? 'expression tag'        29 27 
2 9J6N HIS B 7  ? UNP A0A0K2SRV3 ? ? 'expression tag'        30 28 
2 9J6N HIS B 8  ? UNP A0A0K2SRV3 ? ? 'expression tag'        31 29 
2 9J6N HIS B 9  ? UNP A0A0K2SRV3 ? ? 'expression tag'        32 30 
2 9J6N HIS B 10 ? UNP A0A0K2SRV3 ? ? 'expression tag'        33 31 
2 9J6N SER B 11 ? UNP A0A0K2SRV3 ? ? 'expression tag'        34 32 
2 9J6N ALA B 12 ? UNP A0A0K2SRV3 ? ? 'expression tag'        35 33 
2 9J6N ALA B 13 ? UNP A0A0K2SRV3 ? ? 'expression tag'        36 34 
2 9J6N LEU B 14 ? UNP A0A0K2SRV3 ? ? 'expression tag'        37 35 
2 9J6N GLU B 15 ? UNP A0A0K2SRV3 ? ? 'expression tag'        38 36 
2 9J6N VAL B 16 ? UNP A0A0K2SRV3 ? ? 'expression tag'        39 37 
2 9J6N LEU B 17 ? UNP A0A0K2SRV3 ? ? 'expression tag'        40 38 
2 9J6N PHE B 18 ? UNP A0A0K2SRV3 ? ? 'expression tag'        41 39 
2 9J6N GLN B 19 ? UNP A0A0K2SRV3 ? ? 'expression tag'        42 40 
2 9J6N GLY B 20 ? UNP A0A0K2SRV3 ? ? 'expression tag'        43 41 
2 9J6N PRO B 21 ? UNP A0A0K2SRV3 ? ? 'expression tag'        44 42 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
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)' 380   ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  19340 ? 
2 'ABSA (A^2)' 0     ? 
2 MORE         0     ? 
2 'SSA (A^2)'  19320 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,L 
2 1 B,H,I,J,K,M   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 TRP A 37  ? VAL A 41  ? TRP A 60  VAL A 64  5 ? 5  
HELX_P HELX_P2  AA2 PRO A 118 ? ASN A 122 ? PRO A 141 ASN A 145 5 ? 5  
HELX_P HELX_P3  AA3 THR A 162 ? LEU A 165 ? THR A 185 LEU A 188 5 ? 4  
HELX_P HELX_P4  AA4 PRO A 179 ? GLY A 183 ? PRO A 202 GLY A 206 5 ? 5  
HELX_P HELX_P5  AA5 PRO A 234 ? ASN A 236 ? PRO A 257 ASN A 259 5 ? 3  
HELX_P HELX_P6  AA6 THR A 356 ? LEU A 370 ? THR A 379 LEU A 393 1 ? 15 
HELX_P HELX_P7  AA7 PRO A 383 ? GLY A 394 ? PRO A 406 GLY A 417 1 ? 12 
HELX_P HELX_P8  AA8 ASP A 409 ? GLN A 426 ? ASP A 432 GLN A 449 1 ? 18 
HELX_P HELX_P9  AA9 ASP A 447 ? ASP A 459 ? ASP A 470 ASP A 482 1 ? 13 
HELX_P HELX_P10 AB1 ASP A 533 ? VAL A 551 ? ASP A 556 VAL A 574 1 ? 19 
HELX_P HELX_P11 AB2 ASP A 586 ? ARG A 602 ? ASP A 609 ARG A 625 1 ? 17 
HELX_P HELX_P12 AB3 TRP B 37  ? VAL B 41  ? TRP B 60  VAL B 64  5 ? 5  
HELX_P HELX_P13 AB4 PRO B 118 ? ASN B 122 ? PRO B 141 ASN B 145 5 ? 5  
HELX_P HELX_P14 AB5 THR B 162 ? LEU B 165 ? THR B 185 LEU B 188 5 ? 4  
HELX_P HELX_P15 AB6 PRO B 179 ? GLY B 183 ? PRO B 202 GLY B 206 5 ? 5  
HELX_P HELX_P16 AB7 PRO B 234 ? ASN B 236 ? PRO B 257 ASN B 259 5 ? 3  
HELX_P HELX_P17 AB8 THR B 356 ? LEU B 370 ? THR B 379 LEU B 393 1 ? 15 
HELX_P HELX_P18 AB9 PRO B 383 ? GLY B 394 ? PRO B 406 GLY B 417 1 ? 12 
HELX_P HELX_P19 AC1 ASP B 409 ? GLN B 426 ? ASP B 432 GLN B 449 1 ? 18 
HELX_P HELX_P20 AC2 ASP B 447 ? ASP B 459 ? ASP B 470 ASP B 482 1 ? 13 
HELX_P HELX_P21 AC3 ASP B 533 ? VAL B 551 ? ASP B 556 VAL B 574 1 ? 19 
HELX_P HELX_P22 AC4 VAL B 551 ? GLY B 556 ? VAL B 574 GLY B 579 1 ? 6  
HELX_P HELX_P23 AC5 ASP B 586 ? GLY B 603 ? ASP B 609 GLY B 626 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 472 SG  ? ? ? 1_555 A CYS 473 SG ? ? A CYS 495 A CYS 496 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
disulf2  disulf ? ? B CYS 472 SG  ? ? ? 1_555 B CYS 473 SG ? ? B CYS 495 B CYS 496 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc1  metalc ? ? A ASP 134 OD2 ? ? ? 1_555 G MG  .   MG ? ? A ASP 157 A MG  705 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc2  metalc ? ? A ASP 178 OD2 ? ? ? 1_555 G MG  .   MG ? ? A ASP 201 A MG  705 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc3  metalc ? ? A GLN 190 OE1 ? ? ? 1_555 G MG  .   MG ? ? A GLN 213 A MG  705 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc4  metalc ? ? A ALA 208 O   ? ? ? 1_555 G MG  .   MG ? ? A ALA 231 A MG  705 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc5  metalc ? ? G MG  .   MG  ? ? ? 1_555 L HOH .   O  ? ? A MG  705 A HOH 873 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
metalc6  metalc ? ? G MG  .   MG  ? ? ? 1_555 L HOH .   O  ? ? A MG  705 A HOH 919 1_555 ? ? ? ? ? ? ? 2.200 ? ? 
metalc7  metalc ? ? B ASP 134 OD2 ? ? ? 1_555 K MG  .   MG ? ? B ASP 157 B MG  704 1_555 ? ? ? ? ? ? ? 1.941 ? ? 
metalc8  metalc ? ? B ASP 178 OD2 ? ? ? 1_555 K MG  .   MG ? ? B ASP 201 B MG  704 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc9  metalc ? ? B GLN 190 OE1 ? ? ? 1_555 K MG  .   MG ? ? B GLN 213 B MG  704 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc10 metalc ? ? B ALA 208 O   ? ? ? 1_555 K MG  .   MG ? ? B ALA 231 B MG  704 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc11 metalc ? ? K MG  .   MG  ? ? ? 1_555 M HOH .   O  ? ? B MG  704 B HOH 836 1_555 ? ? ? ? ? ? ? 2.162 ? ? 
metalc12 metalc ? ? K MG  .   MG  ? ? ? 1_555 M HOH .   O  ? ? B MG  704 B HOH 894 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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  OD2 ? A ASP 134 ? A ASP 157 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 OD2 ? A ASP 178 ? A ASP 201 ? 1_555 92.6  ? 
2  OD2 ? A ASP 134 ? A ASP 157 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 OE1 ? A GLN 190 ? A GLN 213 ? 1_555 95.6  ? 
3  OD2 ? A ASP 178 ? A ASP 201 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 OE1 ? A GLN 190 ? A GLN 213 ? 1_555 170.4 ? 
4  OD2 ? A ASP 134 ? A ASP 157 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? A ALA 208 ? A ALA 231 ? 1_555 98.1  ? 
5  OD2 ? A ASP 178 ? A ASP 201 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? A ALA 208 ? A ALA 231 ? 1_555 95.2  ? 
6  OE1 ? A GLN 190 ? A GLN 213 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? A ALA 208 ? A ALA 231 ? 1_555 88.6  ? 
7  OD2 ? A ASP 134 ? A ASP 157 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 873 ? 1_555 87.3  ? 
8  OD2 ? A ASP 178 ? A ASP 201 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 873 ? 1_555 88.1  ? 
9  OE1 ? A GLN 190 ? A GLN 213 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 873 ? 1_555 87.3  ? 
10 O   ? A ALA 208 ? A ALA 231 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 873 ? 1_555 173.5 ? 
11 OD2 ? A ASP 134 ? A ASP 157 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 919 ? 1_555 171.0 ? 
12 OD2 ? A ASP 178 ? A ASP 201 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 919 ? 1_555 81.5  ? 
13 OE1 ? A GLN 190 ? A GLN 213 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 919 ? 1_555 89.7  ? 
14 O   ? A ALA 208 ? A ALA 231 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 919 ? 1_555 89.3  ? 
15 O   ? L HOH .   ? A HOH 873 ? 1_555 MG ? G MG . ? A MG 705 ? 1_555 O   ? L HOH .   ? A HOH 919 ? 1_555 85.6  ? 
16 OD2 ? B ASP 134 ? B ASP 157 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 OD2 ? B ASP 178 ? B ASP 201 ? 1_555 87.6  ? 
17 OD2 ? B ASP 134 ? B ASP 157 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 OE1 ? B GLN 190 ? B GLN 213 ? 1_555 94.2  ? 
18 OD2 ? B ASP 178 ? B ASP 201 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 OE1 ? B GLN 190 ? B GLN 213 ? 1_555 178.0 ? 
19 OD2 ? B ASP 134 ? B ASP 157 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? B ALA 208 ? B ALA 231 ? 1_555 93.4  ? 
20 OD2 ? B ASP 178 ? B ASP 201 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? B ALA 208 ? B ALA 231 ? 1_555 94.1  ? 
21 OE1 ? B GLN 190 ? B GLN 213 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? B ALA 208 ? B ALA 231 ? 1_555 84.9  ? 
22 OD2 ? B ASP 134 ? B ASP 157 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 836 ? 1_555 90.8  ? 
23 OD2 ? B ASP 178 ? B ASP 201 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 836 ? 1_555 89.4  ? 
24 OE1 ? B GLN 190 ? B GLN 213 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 836 ? 1_555 91.5  ? 
25 O   ? B ALA 208 ? B ALA 231 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 836 ? 1_555 174.6 ? 
26 OD2 ? B ASP 134 ? B ASP 157 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 894 ? 1_555 176.2 ? 
27 OD2 ? B ASP 178 ? B ASP 201 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 894 ? 1_555 88.7  ? 
28 OE1 ? B GLN 190 ? B GLN 213 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 894 ? 1_555 89.6  ? 
29 O   ? B ALA 208 ? B ALA 231 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 894 ? 1_555 87.8  ? 
30 O   ? M HOH .   ? B HOH 836 ? 1_555 MG ? K MG . ? B MG 704 ? 1_555 O   ? M HOH .   ? B HOH 894 ? 1_555 88.2  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 472 ? CYS A 473 ? CYS A 495 ? 1_555 CYS A 496 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 472 ? CYS B 473 ? CYS B 495 ? 1_555 CYS B 496 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  VAL 88  A . ? VAL 111 A PRO 89  A ? PRO 112 A 1 9.60  
2  ASP 134 A . ? ASP 157 A TRP 135 A ? TRP 158 A 1 6.57  
3  TYR 489 A . ? TYR 512 A VAL 490 A ? VAL 513 A 1 -6.01 
4  GLY 491 A . ? GLY 514 A PRO 492 A ? PRO 515 A 1 5.92  
5  THR 563 A . ? THR 586 A GLU 564 A ? GLU 587 A 1 4.51  
6  VAL 88  B . ? VAL 111 B PRO 89  B ? PRO 112 B 1 2.07  
7  ASP 134 B . ? ASP 157 B TRP 135 B ? TRP 158 B 1 4.73  
8  TYR 489 B . ? TYR 512 B VAL 490 B ? VAL 513 B 1 5.32  
9  GLY 491 B . ? GLY 514 B PRO 492 B ? PRO 515 B 1 6.49  
10 THR 563 B . ? THR 586 B GLU 564 B ? GLU 587 B 1 4.02  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 3 ? 
AB1 ? 8 ? 
AB2 ? 2 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 6 ? 
AB6 ? 2 ? 
AB7 ? 2 ? 
AB8 ? 3 ? 
AB9 ? 4 ? 
AC1 ? 3 ? 
AC2 ? 8 ? 
AC3 ? 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 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB1 5 6 ? parallel      
AB1 6 7 ? parallel      
AB1 7 8 ? parallel      
AB2 1 2 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? parallel      
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC2 1 2 ? parallel      
AC2 2 3 ? parallel      
AC2 3 4 ? parallel      
AC2 4 5 ? parallel      
AC2 5 6 ? parallel      
AC2 6 7 ? parallel      
AC2 7 8 ? parallel      
AC3 1 2 ? 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 ALA A 61  ? ASN A 62  ? ALA A 84  ASN A 85  
AA1 2 VAL A 215 ? THR A 220 ? VAL A 238 THR A 243 
AA1 3 ARG A 125 ? PHE A 130 ? ARG A 148 PHE A 153 
AA1 4 PHE A 157 ? ASP A 160 ? PHE A 180 ASP A 183 
AA2 1 GLU A 84  ? VAL A 88  ? GLU A 107 VAL A 111 
AA2 2 GLY A 65  ? SER A 73  ? GLY A 88  SER A 96  
AA2 3 ASP A 107 ? PHE A 115 ? ASP A 130 PHE A 138 
AA2 4 ASN A 170 ? TRP A 177 ? ASN A 193 TRP A 200 
AA2 5 ARG A 136 ? VAL A 141 ? ARG A 159 VAL A 164 
AA2 6 ARG A 144 ? GLN A 145 ? ARG A 167 GLN A 168 
AA3 1 GLU A 84  ? VAL A 88  ? GLU A 107 VAL A 111 
AA3 2 GLY A 65  ? SER A 73  ? GLY A 88  SER A 96  
AA3 3 ASP A 107 ? PHE A 115 ? ASP A 130 PHE A 138 
AA3 4 ASN A 170 ? TRP A 177 ? ASN A 193 TRP A 200 
AA3 5 ARG A 136 ? VAL A 141 ? ARG A 159 VAL A 164 
AA3 6 HIS A 150 ? SER A 151 ? HIS A 173 SER A 174 
AA4 1 SER A 133 ? ASP A 134 ? SER A 156 ASP A 157 
AA4 2 GLY A 210 ? ILE A 211 ? GLY A 233 ILE A 234 
AA5 1 GLN A 190 ? ARG A 191 ? GLN A 213 ARG A 214 
AA5 2 TYR A 205 ? THR A 206 ? TYR A 228 THR A 229 
AA6 1 HIS A 224 ? ASP A 233 ? HIS A 247 ASP A 256 
AA6 2 ARG A 238 ? ALA A 246 ? ARG A 261 ALA A 269 
AA6 3 PHE A 275 ? PRO A 278 ? PHE A 298 PRO A 301 
AA7 1 THR A 262 ? PRO A 270 ? THR A 285 PRO A 293 
AA7 2 GLN A 252 ? THR A 259 ? GLN A 275 THR A 282 
AA7 3 TYR A 293 ? SER A 301 ? TYR A 316 SER A 324 
AA7 4 THR A 304 ? THR A 305 ? THR A 327 THR A 328 
AA8 1 THR A 262 ? PRO A 270 ? THR A 285 PRO A 293 
AA8 2 GLN A 252 ? THR A 259 ? GLN A 275 THR A 282 
AA8 3 TYR A 293 ? SER A 301 ? TYR A 316 SER A 324 
AA8 4 VAL A 309 ? THR A 313 ? VAL A 332 THR A 336 
AA9 1 ILE A 318 ? VAL A 323 ? ILE A 341 VAL A 346 
AA9 2 HIS A 326 ? LEU A 331 ? HIS A 349 LEU A 354 
AA9 3 LYS A 334 ? PHE A 335 ? LYS A 357 PHE A 358 
AB1 1 LEU A 463 ? ASP A 465 ? LEU A 486 ASP A 488 
AB1 2 LEU A 433 ? VAL A 437 ? LEU A 456 VAL A 460 
AB1 3 LEU A 396 ? ASP A 400 ? LEU A 419 ASP A 423 
AB1 4 MET A 374 ? LYS A 377 ? MET A 397 LYS A 400 
AB1 5 GLN A 338 ? ASP A 343 ? GLN A 361 ASP A 366 
AB1 6 LEU A 557 ? THR A 563 ? LEU A 580 THR A 586 
AB1 7 ALA A 502 ? GLY A 509 ? ALA A 525 GLY A 532 
AB1 8 VAL A 483 ? VAL A 488 ? VAL A 506 VAL A 511 
AB2 1 LEU A 511 ? GLY A 512 ? LEU A 534 GLY A 535 
AB2 2 GLU A 529 ? ASP A 530 ? GLU A 552 ASP A 553 
AB3 1 ALA B 61  ? ASN B 62  ? ALA B 84  ASN B 85  
AB3 2 VAL B 215 ? THR B 220 ? VAL B 238 THR B 243 
AB3 3 ARG B 125 ? PHE B 130 ? ARG B 148 PHE B 153 
AB3 4 PHE B 157 ? ASP B 160 ? PHE B 180 ASP B 183 
AB4 1 GLU B 84  ? VAL B 88  ? GLU B 107 VAL B 111 
AB4 2 GLY B 65  ? SER B 73  ? GLY B 88  SER B 96  
AB4 3 ASP B 107 ? PHE B 115 ? ASP B 130 PHE B 138 
AB4 4 ASN B 170 ? TRP B 177 ? ASN B 193 TRP B 200 
AB4 5 ARG B 136 ? VAL B 141 ? ARG B 159 VAL B 164 
AB4 6 ARG B 144 ? GLN B 145 ? ARG B 167 GLN B 168 
AB5 1 GLU B 84  ? VAL B 88  ? GLU B 107 VAL B 111 
AB5 2 GLY B 65  ? SER B 73  ? GLY B 88  SER B 96  
AB5 3 ASP B 107 ? PHE B 115 ? ASP B 130 PHE B 138 
AB5 4 ASN B 170 ? TRP B 177 ? ASN B 193 TRP B 200 
AB5 5 ARG B 136 ? VAL B 141 ? ARG B 159 VAL B 164 
AB5 6 HIS B 150 ? SER B 151 ? HIS B 173 SER B 174 
AB6 1 SER B 133 ? ASP B 134 ? SER B 156 ASP B 157 
AB6 2 GLY B 210 ? ILE B 211 ? GLY B 233 ILE B 234 
AB7 1 GLN B 190 ? ARG B 191 ? GLN B 213 ARG B 214 
AB7 2 TYR B 205 ? THR B 206 ? TYR B 228 THR B 229 
AB8 1 HIS B 224 ? ASP B 233 ? HIS B 247 ASP B 256 
AB8 2 ARG B 238 ? ALA B 246 ? ARG B 261 ALA B 269 
AB8 3 PHE B 275 ? PRO B 278 ? PHE B 298 PRO B 301 
AB9 1 THR B 262 ? PRO B 270 ? THR B 285 PRO B 293 
AB9 2 GLN B 252 ? THR B 259 ? GLN B 275 THR B 282 
AB9 3 TYR B 293 ? LEU B 300 ? TYR B 316 LEU B 323 
AB9 4 VAL B 309 ? THR B 313 ? VAL B 332 THR B 336 
AC1 1 ILE B 318 ? VAL B 323 ? ILE B 341 VAL B 346 
AC1 2 HIS B 326 ? LEU B 331 ? HIS B 349 LEU B 354 
AC1 3 LYS B 334 ? PHE B 335 ? LYS B 357 PHE B 358 
AC2 1 LEU B 463 ? ASP B 465 ? LEU B 486 ASP B 488 
AC2 2 LEU B 433 ? VAL B 437 ? LEU B 456 VAL B 460 
AC2 3 LEU B 396 ? ASP B 400 ? LEU B 419 ASP B 423 
AC2 4 MET B 374 ? LYS B 377 ? MET B 397 LYS B 400 
AC2 5 GLN B 338 ? ASP B 343 ? GLN B 361 ASP B 366 
AC2 6 LEU B 557 ? THR B 563 ? LEU B 580 THR B 586 
AC2 7 ALA B 502 ? GLY B 509 ? ALA B 525 GLY B 532 
AC2 8 VAL B 483 ? VAL B 488 ? VAL B 506 VAL B 511 
AC3 1 LEU B 511 ? GLY B 512 ? LEU B 534 GLY B 535 
AC3 2 GLU B 529 ? ASP B 530 ? GLU B 552 ASP B 553 
# 
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 ALA A 61  ? N ALA A 84  O LEU A 217 ? O LEU A 240 
AA1 2 3 O TRP A 216 ? O TRP A 239 N ASN A 129 ? N ASN A 152 
AA1 3 4 N PHE A 130 ? N PHE A 153 O PHE A 157 ? O PHE A 180 
AA2 1 2 O ILE A 86  ? O ILE A 109 N TRP A 67  ? N TRP A 90  
AA2 2 3 N ALA A 70  ? N ALA A 93  O TRP A 110 ? O TRP A 133 
AA2 3 4 N ARG A 113 ? N ARG A 136 O LEU A 172 ? O LEU A 195 
AA2 4 5 O TRP A 177 ? O TRP A 200 N ARG A 136 ? N ARG A 159 
AA2 5 6 N VAL A 141 ? N VAL A 164 O ARG A 144 ? O ARG A 167 
AA3 1 2 O ILE A 86  ? O ILE A 109 N TRP A 67  ? N TRP A 90  
AA3 2 3 N ALA A 70  ? N ALA A 93  O TRP A 110 ? O TRP A 133 
AA3 3 4 N ARG A 113 ? N ARG A 136 O LEU A 172 ? O LEU A 195 
AA3 4 5 O TRP A 177 ? O TRP A 200 N ARG A 136 ? N ARG A 159 
AA3 5 6 N THR A 137 ? N THR A 160 O HIS A 150 ? O HIS A 173 
AA4 1 2 N ASP A 134 ? N ASP A 157 O GLY A 210 ? O GLY A 233 
AA5 1 2 N ARG A 191 ? N ARG A 214 O TYR A 205 ? O TYR A 228 
AA6 1 2 N VAL A 231 ? N VAL A 254 O LYS A 240 ? O LYS A 263 
AA6 2 3 N VAL A 241 ? N VAL A 264 O PHE A 275 ? O PHE A 298 
AA7 1 2 O GLY A 265 ? O GLY A 288 N VAL A 257 ? N VAL A 280 
AA7 2 3 N GLN A 252 ? N GLN A 275 O LEU A 300 ? O LEU A 323 
AA7 3 4 N SER A 301 ? N SER A 324 O THR A 304 ? O THR A 327 
AA8 1 2 O GLY A 265 ? O GLY A 288 N VAL A 257 ? N VAL A 280 
AA8 2 3 N GLN A 252 ? N GLN A 275 O LEU A 300 ? O LEU A 323 
AA8 3 4 N VAL A 295 ? N VAL A 318 O SER A 311 ? O SER A 334 
AA9 1 2 N ALA A 319 ? N ALA A 342 O VAL A 330 ? O VAL A 353 
AA9 2 3 N LEU A 331 ? N LEU A 354 O LYS A 334 ? O LYS A 357 
AB1 1 2 O LEU A 463 ? O LEU A 486 N VAL A 434 ? N VAL A 457 
AB1 2 3 O LEU A 435 ? O LEU A 458 N GLN A 399 ? N GLN A 422 
AB1 3 4 O TRP A 398 ? O TRP A 421 N LYS A 377 ? N LYS A 400 
AB1 4 5 O ARG A 376 ? O ARG A 399 N THR A 341 ? N THR A 364 
AB1 5 6 N GLY A 340 ? N GLY A 363 O TYR A 562 ? O TYR A 585 
AB1 6 7 O THR A 563 ? O THR A 586 N PHE A 508 ? N PHE A 531 
AB1 7 8 O ALA A 502 ? O ALA A 525 N VAL A 484 ? N VAL A 507 
AB2 1 2 N GLY A 512 ? N GLY A 535 O GLU A 529 ? O GLU A 552 
AB3 1 2 N ALA B 61  ? N ALA B 84  O LEU B 217 ? O LEU B 240 
AB3 2 3 O GLU B 218 ? O GLU B 241 N GLN B 127 ? N GLN B 150 
AB3 3 4 N LEU B 128 ? N LEU B 151 O TYR B 159 ? O TYR B 182 
AB4 1 2 O ILE B 86  ? O ILE B 109 N TRP B 67  ? N TRP B 90  
AB4 2 3 N ASP B 68  ? N ASP B 91  O LYS B 112 ? O LYS B 135 
AB4 3 4 N PHE B 115 ? N PHE B 138 O ASN B 170 ? O ASN B 193 
AB4 4 5 O TRP B 177 ? O TRP B 200 N ARG B 136 ? N ARG B 159 
AB4 5 6 N VAL B 141 ? N VAL B 164 O ARG B 144 ? O ARG B 167 
AB5 1 2 O ILE B 86  ? O ILE B 109 N TRP B 67  ? N TRP B 90  
AB5 2 3 N ASP B 68  ? N ASP B 91  O LYS B 112 ? O LYS B 135 
AB5 3 4 N PHE B 115 ? N PHE B 138 O ASN B 170 ? O ASN B 193 
AB5 4 5 O TRP B 177 ? O TRP B 200 N ARG B 136 ? N ARG B 159 
AB5 5 6 N THR B 137 ? N THR B 160 O HIS B 150 ? O HIS B 173 
AB6 1 2 N ASP B 134 ? N ASP B 157 O GLY B 210 ? O GLY B 233 
AB7 1 2 N ARG B 191 ? N ARG B 214 O TYR B 205 ? O TYR B 228 
AB8 1 2 N VAL B 231 ? N VAL B 254 O LYS B 240 ? O LYS B 263 
AB8 2 3 N VAL B 241 ? N VAL B 264 O PHE B 275 ? O PHE B 298 
AB9 1 2 O GLY B 269 ? O GLY B 292 N ALA B 253 ? N ALA B 276 
AB9 2 3 N ARG B 254 ? N ARG B 277 O ASP B 298 ? O ASP B 321 
AB9 3 4 N VAL B 295 ? N VAL B 318 O SER B 311 ? O SER B 334 
AC1 1 2 N VAL B 323 ? N VAL B 346 O HIS B 326 ? O HIS B 349 
AC1 2 3 N LEU B 331 ? N LEU B 354 O LYS B 334 ? O LYS B 357 
AC2 1 2 O ASP B 465 ? O ASP B 488 N TRP B 436 ? N TRP B 459 
AC2 2 3 O VAL B 434 ? O VAL B 457 N VAL B 397 ? N VAL B 420 
AC2 3 4 O TRP B 398 ? O TRP B 421 N VAL B 375 ? N VAL B 398 
AC2 4 5 O ARG B 376 ? O ARG B 399 N THR B 341 ? N THR B 364 
AC2 5 6 N GLY B 340 ? N GLY B 363 O TYR B 562 ? O TYR B 585 
AC2 6 7 O THR B 563 ? O THR B 586 N PHE B 508 ? N PHE B 531 
AC2 7 8 O VAL B 504 ? O VAL B 527 N VAL B 484 ? N VAL B 507 
AC3 1 2 N GLY B 512 ? N GLY B 535 O GLU B 529 ? O GLU B 552 
# 
_pdbx_entry_details.entry_id                   9J6N 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C A CYS 495 ? ? N A CYS 496 ? ? 1.567 1.336 0.231 0.023 Y 
2 1 C B CYS 495 ? ? N B CYS 496 ? ? 1.534 1.336 0.198 0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 408 ? ? CZ A ARG 408 ? ? NH1 A ARG 408 ? ? 123.82 120.30 3.52  0.50 N 
2 1 NE A ARG 436 ? ? CZ A ARG 436 ? ? NH2 A ARG 436 ? ? 117.00 120.30 -3.30 0.50 N 
3 1 NE A ARG 473 ? ? CZ A ARG 473 ? ? NH1 A ARG 473 ? ? 123.56 120.30 3.26  0.50 N 
4 1 NE A ARG 473 ? ? CZ A ARG 473 ? ? NH2 A ARG 473 ? ? 116.23 120.30 -4.07 0.50 N 
5 1 NE B ARG 473 ? ? CZ B ARG 473 ? ? NH2 B ARG 473 ? ? 115.33 120.30 -4.97 0.50 N 
6 1 CB B GLU 592 ? ? CA B GLU 592 ? ? C   B GLU 592 ? ? 122.96 110.40 12.56 2.00 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 PRO A 112 ? ? -111.43 62.79   
2  1 THR A 203 ? ? 44.39   -136.76 
3  1 ILE A 374 ? ? 66.81   -91.55  
4  1 ILE A 402 ? ? 32.88   48.38   
5  1 CYS A 496 ? ? 80.33   6.85    
6  1 ASN A 503 ? ? -117.36 -155.47 
7  1 THR A 517 ? ? -141.28 33.24   
8  1 GLU A 552 ? ? -165.40 108.49  
9  1 GLU A 592 ? ? 48.23   -120.17 
10 1 VAL A 595 ? ? -102.40 49.26   
11 1 LEU B 70  ? ? 38.44   64.82   
12 1 PRO B 112 ? ? -105.32 66.80   
13 1 THR B 203 ? ? 44.15   -131.60 
14 1 ILE B 374 ? ? 58.52   -87.21  
15 1 ILE B 402 ? ? 34.45   49.45   
16 1 CYS B 496 ? ? 33.67   -120.77 
17 1 ASN B 503 ? ? -120.86 -154.85 
18 1 GLU B 552 ? ? -170.31 104.75  
19 1 VAL B 574 ? ? -123.26 -54.06  
20 1 GLU B 592 ? ? 53.05   -122.95 
21 1 VAL B 595 ? ? -104.13 47.85   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 384 ? ? 0.101 'SIDE CHAIN' 
2 1 ARG A 399 ? ? 0.075 'SIDE CHAIN' 
3 1 ARG A 473 ? ? 0.105 'SIDE CHAIN' 
4 1 ARG B 47  ? ? 0.083 'SIDE CHAIN' 
5 1 ARG B 216 ? ? 0.164 'SIDE CHAIN' 
6 1 ARG B 306 ? ? 0.088 'SIDE CHAIN' 
7 1 ARG B 473 ? ? 0.073 'SIDE CHAIN' 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             CYS 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              495 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -13.11 
# 
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 24  ? A MET 1   
2  1 Y 1 A GLY 25  ? A GLY 2   
3  1 Y 1 A SER 26  ? A SER 3   
4  1 Y 1 A SER 27  ? A SER 4   
5  1 Y 1 A HIS 28  ? A HIS 5   
6  1 Y 1 A HIS 29  ? A HIS 6   
7  1 Y 1 A HIS 30  ? A HIS 7   
8  1 Y 1 A HIS 31  ? A HIS 8   
9  1 Y 1 A HIS 32  ? A HIS 9   
10 1 Y 1 A HIS 33  ? A HIS 10  
11 1 Y 1 A SER 34  ? A SER 11  
12 1 Y 1 A ALA 35  ? A ALA 12  
13 1 Y 1 A ALA 36  ? A ALA 13  
14 1 Y 1 A LEU 37  ? A LEU 14  
15 1 Y 1 A GLU 38  ? A GLU 15  
16 1 Y 1 A VAL 39  ? A VAL 16  
17 1 Y 1 A LEU 40  ? A LEU 17  
18 1 Y 1 A PHE 41  ? A PHE 18  
19 1 Y 1 A GLN 42  ? A GLN 19  
20 1 Y 1 A GLY 43  ? A GLY 20  
21 1 Y 1 A PRO 44  ? A PRO 21  
22 1 Y 1 A GLY 626 ? A GLY 603 
23 1 Y 1 A THR 627 ? A THR 604 
24 1 Y 1 A THR 628 ? A THR 605 
25 1 Y 1 A ALA 629 ? A ALA 606 
26 1 Y 1 A PRO 630 ? A PRO 607 
27 1 Y 1 A LEU 631 ? A LEU 608 
28 1 Y 1 A THR 632 ? A THR 609 
29 1 Y 1 A LEU 633 ? A LEU 610 
30 1 Y 1 A PRO 634 ? A PRO 611 
31 1 Y 1 A VAL 635 ? A VAL 612 
32 1 Y 1 B MET 24  ? B MET 1   
33 1 Y 1 B GLY 25  ? B GLY 2   
34 1 Y 1 B SER 26  ? B SER 3   
35 1 Y 1 B SER 27  ? B SER 4   
36 1 Y 1 B HIS 28  ? B HIS 5   
37 1 Y 1 B HIS 29  ? B HIS 6   
38 1 Y 1 B HIS 30  ? B HIS 7   
39 1 Y 1 B HIS 31  ? B HIS 8   
40 1 Y 1 B HIS 32  ? B HIS 9   
41 1 Y 1 B HIS 33  ? B HIS 10  
42 1 Y 1 B SER 34  ? B SER 11  
43 1 Y 1 B ALA 35  ? B ALA 12  
44 1 Y 1 B ALA 36  ? B ALA 13  
45 1 Y 1 B LEU 37  ? B LEU 14  
46 1 Y 1 B GLU 38  ? B GLU 15  
47 1 Y 1 B VAL 39  ? B VAL 16  
48 1 Y 1 B LEU 40  ? B LEU 17  
49 1 Y 1 B PHE 41  ? B PHE 18  
50 1 Y 1 B GLN 42  ? B GLN 19  
51 1 Y 1 B GLY 43  ? B GLY 20  
52 1 Y 1 B PRO 44  ? B PRO 21  
53 1 Y 1 B ALA 45  ? B ALA 22  
54 1 Y 1 B SER 324 ? B SER 301 
55 1 Y 1 B GLY 325 ? B GLY 302 
56 1 Y 1 B GLY 326 ? B GLY 303 
57 1 Y 1 B THR 327 ? B THR 304 
58 1 Y 1 B THR 328 ? B THR 305 
59 1 Y 1 B THR 627 ? B THR 604 
60 1 Y 1 B THR 628 ? B THR 605 
61 1 Y 1 B ALA 629 ? B ALA 606 
62 1 Y 1 B PRO 630 ? B PRO 607 
63 1 Y 1 B LEU 631 ? B LEU 608 
64 1 Y 1 B THR 632 ? B THR 609 
65 1 Y 1 B LEU 633 ? B LEU 610 
66 1 Y 1 B PRO 634 ? B PRO 611 
67 1 Y 1 B VAL 635 ? B VAL 612 
# 
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 
A1L3Z C4   C  N N 1   
A1L3Z C5   C  N S 2   
A1L3Z C6   C  N S 3   
A1L3Z N1   N  N N 4   
A1L3Z C3   C  N S 5   
A1L3Z O1   O  N N 6   
A1L3Z C1   C  N N 7   
A1L3Z C2   C  N S 8   
A1L3Z O2   O  N N 9   
A1L3Z O3   O  N N 10  
A1L3Z O4   O  N N 11  
A1L3Z H1   H  N N 12  
A1L3Z H2   H  N N 13  
A1L3Z H3   H  N N 14  
A1L3Z H4   H  N N 15  
A1L3Z H5   H  N N 16  
A1L3Z H7   H  N N 17  
A1L3Z H8   H  N N 18  
A1L3Z H9   H  N N 19  
A1L3Z H10  H  N N 20  
A1L3Z H11  H  N N 21  
A1L3Z H12  H  N N 22  
A1L3Z H13  H  N N 23  
A1L3Z H14  H  N N 24  
ALA   N    N  N N 25  
ALA   CA   C  N S 26  
ALA   C    C  N N 27  
ALA   O    O  N N 28  
ALA   CB   C  N N 29  
ALA   OXT  O  N N 30  
ALA   H    H  N N 31  
ALA   H2   H  N N 32  
ALA   HA   H  N N 33  
ALA   HB1  H  N N 34  
ALA   HB2  H  N N 35  
ALA   HB3  H  N N 36  
ALA   HXT  H  N N 37  
ARG   N    N  N N 38  
ARG   CA   C  N S 39  
ARG   C    C  N N 40  
ARG   O    O  N N 41  
ARG   CB   C  N N 42  
ARG   CG   C  N N 43  
ARG   CD   C  N N 44  
ARG   NE   N  N N 45  
ARG   CZ   C  N N 46  
ARG   NH1  N  N N 47  
ARG   NH2  N  N N 48  
ARG   OXT  O  N N 49  
ARG   H    H  N N 50  
ARG   H2   H  N N 51  
ARG   HA   H  N N 52  
ARG   HB2  H  N N 53  
ARG   HB3  H  N N 54  
ARG   HG2  H  N N 55  
ARG   HG3  H  N N 56  
ARG   HD2  H  N N 57  
ARG   HD3  H  N N 58  
ARG   HE   H  N N 59  
ARG   HH11 H  N N 60  
ARG   HH12 H  N N 61  
ARG   HH21 H  N N 62  
ARG   HH22 H  N N 63  
ARG   HXT  H  N N 64  
ASN   N    N  N N 65  
ASN   CA   C  N S 66  
ASN   C    C  N N 67  
ASN   O    O  N N 68  
ASN   CB   C  N N 69  
ASN   CG   C  N N 70  
ASN   OD1  O  N N 71  
ASN   ND2  N  N N 72  
ASN   OXT  O  N N 73  
ASN   H    H  N N 74  
ASN   H2   H  N N 75  
ASN   HA   H  N N 76  
ASN   HB2  H  N N 77  
ASN   HB3  H  N N 78  
ASN   HD21 H  N N 79  
ASN   HD22 H  N N 80  
ASN   HXT  H  N N 81  
ASP   N    N  N N 82  
ASP   CA   C  N S 83  
ASP   C    C  N N 84  
ASP   O    O  N N 85  
ASP   CB   C  N N 86  
ASP   CG   C  N N 87  
ASP   OD1  O  N N 88  
ASP   OD2  O  N N 89  
ASP   OXT  O  N N 90  
ASP   H    H  N N 91  
ASP   H2   H  N N 92  
ASP   HA   H  N N 93  
ASP   HB2  H  N N 94  
ASP   HB3  H  N N 95  
ASP   HD2  H  N N 96  
ASP   HXT  H  N N 97  
CYS   N    N  N N 98  
CYS   CA   C  N R 99  
CYS   C    C  N N 100 
CYS   O    O  N N 101 
CYS   CB   C  N N 102 
CYS   SG   S  N N 103 
CYS   OXT  O  N N 104 
CYS   H    H  N N 105 
CYS   H2   H  N N 106 
CYS   HA   H  N N 107 
CYS   HB2  H  N N 108 
CYS   HB3  H  N N 109 
CYS   HG   H  N N 110 
CYS   HXT  H  N N 111 
GLN   N    N  N N 112 
GLN   CA   C  N S 113 
GLN   C    C  N N 114 
GLN   O    O  N N 115 
GLN   CB   C  N N 116 
GLN   CG   C  N N 117 
GLN   CD   C  N N 118 
GLN   OE1  O  N N 119 
GLN   NE2  N  N N 120 
GLN   OXT  O  N N 121 
GLN   H    H  N N 122 
GLN   H2   H  N N 123 
GLN   HA   H  N N 124 
GLN   HB2  H  N N 125 
GLN   HB3  H  N N 126 
GLN   HG2  H  N N 127 
GLN   HG3  H  N N 128 
GLN   HE21 H  N N 129 
GLN   HE22 H  N N 130 
GLN   HXT  H  N N 131 
GLU   N    N  N N 132 
GLU   CA   C  N S 133 
GLU   C    C  N N 134 
GLU   O    O  N N 135 
GLU   CB   C  N N 136 
GLU   CG   C  N N 137 
GLU   CD   C  N N 138 
GLU   OE1  O  N N 139 
GLU   OE2  O  N N 140 
GLU   OXT  O  N N 141 
GLU   H    H  N N 142 
GLU   H2   H  N N 143 
GLU   HA   H  N N 144 
GLU   HB2  H  N N 145 
GLU   HB3  H  N N 146 
GLU   HG2  H  N N 147 
GLU   HG3  H  N N 148 
GLU   HE2  H  N N 149 
GLU   HXT  H  N N 150 
GLY   N    N  N N 151 
GLY   CA   C  N N 152 
GLY   C    C  N N 153 
GLY   O    O  N N 154 
GLY   OXT  O  N N 155 
GLY   H    H  N N 156 
GLY   H2   H  N N 157 
GLY   HA2  H  N N 158 
GLY   HA3  H  N N 159 
GLY   HXT  H  N N 160 
HIS   N    N  N N 161 
HIS   CA   C  N S 162 
HIS   C    C  N N 163 
HIS   O    O  N N 164 
HIS   CB   C  N N 165 
HIS   CG   C  Y N 166 
HIS   ND1  N  Y N 167 
HIS   CD2  C  Y N 168 
HIS   CE1  C  Y N 169 
HIS   NE2  N  Y N 170 
HIS   OXT  O  N N 171 
HIS   H    H  N N 172 
HIS   H2   H  N N 173 
HIS   HA   H  N N 174 
HIS   HB2  H  N N 175 
HIS   HB3  H  N N 176 
HIS   HD1  H  N N 177 
HIS   HD2  H  N N 178 
HIS   HE1  H  N N 179 
HIS   HE2  H  N N 180 
HIS   HXT  H  N N 181 
HOH   O    O  N N 182 
HOH   H1   H  N N 183 
HOH   H2   H  N N 184 
ILE   N    N  N N 185 
ILE   CA   C  N S 186 
ILE   C    C  N N 187 
ILE   O    O  N N 188 
ILE   CB   C  N S 189 
ILE   CG1  C  N N 190 
ILE   CG2  C  N N 191 
ILE   CD1  C  N N 192 
ILE   OXT  O  N N 193 
ILE   H    H  N N 194 
ILE   H2   H  N N 195 
ILE   HA   H  N N 196 
ILE   HB   H  N N 197 
ILE   HG12 H  N N 198 
ILE   HG13 H  N N 199 
ILE   HG21 H  N N 200 
ILE   HG22 H  N N 201 
ILE   HG23 H  N N 202 
ILE   HD11 H  N N 203 
ILE   HD12 H  N N 204 
ILE   HD13 H  N N 205 
ILE   HXT  H  N N 206 
LEU   N    N  N N 207 
LEU   CA   C  N S 208 
LEU   C    C  N N 209 
LEU   O    O  N N 210 
LEU   CB   C  N N 211 
LEU   CG   C  N N 212 
LEU   CD1  C  N N 213 
LEU   CD2  C  N N 214 
LEU   OXT  O  N N 215 
LEU   H    H  N N 216 
LEU   H2   H  N N 217 
LEU   HA   H  N N 218 
LEU   HB2  H  N N 219 
LEU   HB3  H  N N 220 
LEU   HG   H  N N 221 
LEU   HD11 H  N N 222 
LEU   HD12 H  N N 223 
LEU   HD13 H  N N 224 
LEU   HD21 H  N N 225 
LEU   HD22 H  N N 226 
LEU   HD23 H  N N 227 
LEU   HXT  H  N N 228 
LYS   N    N  N N 229 
LYS   CA   C  N S 230 
LYS   C    C  N N 231 
LYS   O    O  N N 232 
LYS   CB   C  N N 233 
LYS   CG   C  N N 234 
LYS   CD   C  N N 235 
LYS   CE   C  N N 236 
LYS   NZ   N  N N 237 
LYS   OXT  O  N N 238 
LYS   H    H  N N 239 
LYS   H2   H  N N 240 
LYS   HA   H  N N 241 
LYS   HB2  H  N N 242 
LYS   HB3  H  N N 243 
LYS   HG2  H  N N 244 
LYS   HG3  H  N N 245 
LYS   HD2  H  N N 246 
LYS   HD3  H  N N 247 
LYS   HE2  H  N N 248 
LYS   HE3  H  N N 249 
LYS   HZ1  H  N N 250 
LYS   HZ2  H  N N 251 
LYS   HZ3  H  N N 252 
LYS   HXT  H  N N 253 
MET   N    N  N N 254 
MET   CA   C  N S 255 
MET   C    C  N N 256 
MET   O    O  N N 257 
MET   CB   C  N N 258 
MET   CG   C  N N 259 
MET   SD   S  N N 260 
MET   CE   C  N N 261 
MET   OXT  O  N N 262 
MET   H    H  N N 263 
MET   H2   H  N N 264 
MET   HA   H  N N 265 
MET   HB2  H  N N 266 
MET   HB3  H  N N 267 
MET   HG2  H  N N 268 
MET   HG3  H  N N 269 
MET   HE1  H  N N 270 
MET   HE2  H  N N 271 
MET   HE3  H  N N 272 
MET   HXT  H  N N 273 
MG    MG   MG N N 274 
MPD   C1   C  N N 275 
MPD   C2   C  N N 276 
MPD   O2   O  N N 277 
MPD   CM   C  N N 278 
MPD   C3   C  N N 279 
MPD   C4   C  N S 280 
MPD   O4   O  N N 281 
MPD   C5   C  N N 282 
MPD   H11  H  N N 283 
MPD   H12  H  N N 284 
MPD   H13  H  N N 285 
MPD   HO2  H  N N 286 
MPD   HM1  H  N N 287 
MPD   HM2  H  N N 288 
MPD   HM3  H  N N 289 
MPD   H31  H  N N 290 
MPD   H32  H  N N 291 
MPD   H4   H  N N 292 
MPD   HO4  H  N N 293 
MPD   H51  H  N N 294 
MPD   H52  H  N N 295 
MPD   H53  H  N N 296 
P6G   O1   O  N N 297 
P6G   C2   C  N N 298 
P6G   C3   C  N N 299 
P6G   O4   O  N N 300 
P6G   C5   C  N N 301 
P6G   C6   C  N N 302 
P6G   O7   O  N N 303 
P6G   C8   C  N N 304 
P6G   C9   C  N N 305 
P6G   O10  O  N N 306 
P6G   C11  C  N N 307 
P6G   C12  C  N N 308 
P6G   O13  O  N N 309 
P6G   C14  C  N N 310 
P6G   C15  C  N N 311 
P6G   O16  O  N N 312 
P6G   C17  C  N N 313 
P6G   C18  C  N N 314 
P6G   O19  O  N N 315 
P6G   H1   H  N N 316 
P6G   H21  H  N N 317 
P6G   H22  H  N N 318 
P6G   H31  H  N N 319 
P6G   H32  H  N N 320 
P6G   H51  H  N N 321 
P6G   H52  H  N N 322 
P6G   H61  H  N N 323 
P6G   H62  H  N N 324 
P6G   H81  H  N N 325 
P6G   H82  H  N N 326 
P6G   H91  H  N N 327 
P6G   H92  H  N N 328 
P6G   H111 H  N N 329 
P6G   H112 H  N N 330 
P6G   H121 H  N N 331 
P6G   H122 H  N N 332 
P6G   H141 H  N N 333 
P6G   H142 H  N N 334 
P6G   H151 H  N N 335 
P6G   H152 H  N N 336 
P6G   H171 H  N N 337 
P6G   H172 H  N N 338 
P6G   H181 H  N N 339 
P6G   H182 H  N N 340 
P6G   H19  H  N N 341 
PG4   O1   O  N N 342 
PG4   C1   C  N N 343 
PG4   C2   C  N N 344 
PG4   O2   O  N N 345 
PG4   C3   C  N N 346 
PG4   C4   C  N N 347 
PG4   O3   O  N N 348 
PG4   C5   C  N N 349 
PG4   C6   C  N N 350 
PG4   O4   O  N N 351 
PG4   C7   C  N N 352 
PG4   C8   C  N N 353 
PG4   O5   O  N N 354 
PG4   HO1  H  N N 355 
PG4   H11  H  N N 356 
PG4   H12  H  N N 357 
PG4   H21  H  N N 358 
PG4   H22  H  N N 359 
PG4   H31  H  N N 360 
PG4   H32  H  N N 361 
PG4   H41  H  N N 362 
PG4   H42  H  N N 363 
PG4   H51  H  N N 364 
PG4   H52  H  N N 365 
PG4   H61  H  N N 366 
PG4   H62  H  N N 367 
PG4   H71  H  N N 368 
PG4   H72  H  N N 369 
PG4   H81  H  N N 370 
PG4   H82  H  N N 371 
PG4   HO5  H  N N 372 
PHE   N    N  N N 373 
PHE   CA   C  N S 374 
PHE   C    C  N N 375 
PHE   O    O  N N 376 
PHE   CB   C  N N 377 
PHE   CG   C  Y N 378 
PHE   CD1  C  Y N 379 
PHE   CD2  C  Y N 380 
PHE   CE1  C  Y N 381 
PHE   CE2  C  Y N 382 
PHE   CZ   C  Y N 383 
PHE   OXT  O  N N 384 
PHE   H    H  N N 385 
PHE   H2   H  N N 386 
PHE   HA   H  N N 387 
PHE   HB2  H  N N 388 
PHE   HB3  H  N N 389 
PHE   HD1  H  N N 390 
PHE   HD2  H  N N 391 
PHE   HE1  H  N N 392 
PHE   HE2  H  N N 393 
PHE   HZ   H  N N 394 
PHE   HXT  H  N N 395 
PRO   N    N  N N 396 
PRO   CA   C  N S 397 
PRO   C    C  N N 398 
PRO   O    O  N N 399 
PRO   CB   C  N N 400 
PRO   CG   C  N N 401 
PRO   CD   C  N N 402 
PRO   OXT  O  N N 403 
PRO   H    H  N N 404 
PRO   HA   H  N N 405 
PRO   HB2  H  N N 406 
PRO   HB3  H  N N 407 
PRO   HG2  H  N N 408 
PRO   HG3  H  N N 409 
PRO   HD2  H  N N 410 
PRO   HD3  H  N N 411 
PRO   HXT  H  N N 412 
SER   N    N  N N 413 
SER   CA   C  N S 414 
SER   C    C  N N 415 
SER   O    O  N N 416 
SER   CB   C  N N 417 
SER   OG   O  N N 418 
SER   OXT  O  N N 419 
SER   H    H  N N 420 
SER   H2   H  N N 421 
SER   HA   H  N N 422 
SER   HB2  H  N N 423 
SER   HB3  H  N N 424 
SER   HG   H  N N 425 
SER   HXT  H  N N 426 
THR   N    N  N N 427 
THR   CA   C  N S 428 
THR   C    C  N N 429 
THR   O    O  N N 430 
THR   CB   C  N R 431 
THR   OG1  O  N N 432 
THR   CG2  C  N N 433 
THR   OXT  O  N N 434 
THR   H    H  N N 435 
THR   H2   H  N N 436 
THR   HA   H  N N 437 
THR   HB   H  N N 438 
THR   HG1  H  N N 439 
THR   HG21 H  N N 440 
THR   HG22 H  N N 441 
THR   HG23 H  N N 442 
THR   HXT  H  N N 443 
TRP   N    N  N N 444 
TRP   CA   C  N S 445 
TRP   C    C  N N 446 
TRP   O    O  N N 447 
TRP   CB   C  N N 448 
TRP   CG   C  Y N 449 
TRP   CD1  C  Y N 450 
TRP   CD2  C  Y N 451 
TRP   NE1  N  Y N 452 
TRP   CE2  C  Y N 453 
TRP   CE3  C  Y N 454 
TRP   CZ2  C  Y N 455 
TRP   CZ3  C  Y N 456 
TRP   CH2  C  Y N 457 
TRP   OXT  O  N N 458 
TRP   H    H  N N 459 
TRP   H2   H  N N 460 
TRP   HA   H  N N 461 
TRP   HB2  H  N N 462 
TRP   HB3  H  N N 463 
TRP   HD1  H  N N 464 
TRP   HE1  H  N N 465 
TRP   HE3  H  N N 466 
TRP   HZ2  H  N N 467 
TRP   HZ3  H  N N 468 
TRP   HH2  H  N N 469 
TRP   HXT  H  N N 470 
TYR   N    N  N N 471 
TYR   CA   C  N S 472 
TYR   C    C  N N 473 
TYR   O    O  N N 474 
TYR   CB   C  N N 475 
TYR   CG   C  Y N 476 
TYR   CD1  C  Y N 477 
TYR   CD2  C  Y N 478 
TYR   CE1  C  Y N 479 
TYR   CE2  C  Y N 480 
TYR   CZ   C  Y N 481 
TYR   OH   O  N N 482 
TYR   OXT  O  N N 483 
TYR   H    H  N N 484 
TYR   H2   H  N N 485 
TYR   HA   H  N N 486 
TYR   HB2  H  N N 487 
TYR   HB3  H  N N 488 
TYR   HD1  H  N N 489 
TYR   HD2  H  N N 490 
TYR   HE1  H  N N 491 
TYR   HE2  H  N N 492 
TYR   HH   H  N N 493 
TYR   HXT  H  N N 494 
VAL   N    N  N N 495 
VAL   CA   C  N S 496 
VAL   C    C  N N 497 
VAL   O    O  N N 498 
VAL   CB   C  N N 499 
VAL   CG1  C  N N 500 
VAL   CG2  C  N N 501 
VAL   OXT  O  N N 502 
VAL   H    H  N N 503 
VAL   H2   H  N N 504 
VAL   HA   H  N N 505 
VAL   HB   H  N N 506 
VAL   HG11 H  N N 507 
VAL   HG12 H  N N 508 
VAL   HG13 H  N N 509 
VAL   HG21 H  N N 510 
VAL   HG22 H  N N 511 
VAL   HG23 H  N N 512 
VAL   HXT  H  N N 513 
# 
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 
A1L3Z N1  C4   sing N N 1   
A1L3Z N1  C3   sing N N 2   
A1L3Z C4  C5   sing N N 3   
A1L3Z O3  C5   sing N N 4   
A1L3Z O2  C2   sing N N 5   
A1L3Z C5  C6   sing N N 6   
A1L3Z C2  C3   sing N N 7   
A1L3Z C2  C1   sing N N 8   
A1L3Z C3  C6   sing N N 9   
A1L3Z C6  O4   sing N N 10  
A1L3Z C1  O1   sing N N 11  
A1L3Z C4  H1   sing N N 12  
A1L3Z C4  H2   sing N N 13  
A1L3Z C5  H3   sing N N 14  
A1L3Z C6  H4   sing N N 15  
A1L3Z N1  H5   sing N N 16  
A1L3Z C3  H7   sing N N 17  
A1L3Z O1  H8   sing N N 18  
A1L3Z C1  H9   sing N N 19  
A1L3Z C1  H10  sing N N 20  
A1L3Z C2  H11  sing N N 21  
A1L3Z O2  H12  sing N N 22  
A1L3Z O3  H13  sing N N 23  
A1L3Z O4  H14  sing N N 24  
ALA   N   CA   sing N N 25  
ALA   N   H    sing N N 26  
ALA   N   H2   sing N N 27  
ALA   CA  C    sing N N 28  
ALA   CA  CB   sing N N 29  
ALA   CA  HA   sing N N 30  
ALA   C   O    doub N N 31  
ALA   C   OXT  sing N N 32  
ALA   CB  HB1  sing N N 33  
ALA   CB  HB2  sing N N 34  
ALA   CB  HB3  sing N N 35  
ALA   OXT HXT  sing N N 36  
ARG   N   CA   sing N N 37  
ARG   N   H    sing N N 38  
ARG   N   H2   sing N N 39  
ARG   CA  C    sing N N 40  
ARG   CA  CB   sing N N 41  
ARG   CA  HA   sing N N 42  
ARG   C   O    doub N N 43  
ARG   C   OXT  sing N N 44  
ARG   CB  CG   sing N N 45  
ARG   CB  HB2  sing N N 46  
ARG   CB  HB3  sing N N 47  
ARG   CG  CD   sing N N 48  
ARG   CG  HG2  sing N N 49  
ARG   CG  HG3  sing N N 50  
ARG   CD  NE   sing N N 51  
ARG   CD  HD2  sing N N 52  
ARG   CD  HD3  sing N N 53  
ARG   NE  CZ   sing N N 54  
ARG   NE  HE   sing N N 55  
ARG   CZ  NH1  sing N N 56  
ARG   CZ  NH2  doub N N 57  
ARG   NH1 HH11 sing N N 58  
ARG   NH1 HH12 sing N N 59  
ARG   NH2 HH21 sing N N 60  
ARG   NH2 HH22 sing N N 61  
ARG   OXT HXT  sing N N 62  
ASN   N   CA   sing N N 63  
ASN   N   H    sing N N 64  
ASN   N   H2   sing N N 65  
ASN   CA  C    sing N N 66  
ASN   CA  CB   sing N N 67  
ASN   CA  HA   sing N N 68  
ASN   C   O    doub N N 69  
ASN   C   OXT  sing N N 70  
ASN   CB  CG   sing N N 71  
ASN   CB  HB2  sing N N 72  
ASN   CB  HB3  sing N N 73  
ASN   CG  OD1  doub N N 74  
ASN   CG  ND2  sing N N 75  
ASN   ND2 HD21 sing N N 76  
ASN   ND2 HD22 sing N N 77  
ASN   OXT HXT  sing N N 78  
ASP   N   CA   sing N N 79  
ASP   N   H    sing N N 80  
ASP   N   H2   sing N N 81  
ASP   CA  C    sing N N 82  
ASP   CA  CB   sing N N 83  
ASP   CA  HA   sing N N 84  
ASP   C   O    doub N N 85  
ASP   C   OXT  sing N N 86  
ASP   CB  CG   sing N N 87  
ASP   CB  HB2  sing N N 88  
ASP   CB  HB3  sing N N 89  
ASP   CG  OD1  doub N N 90  
ASP   CG  OD2  sing N N 91  
ASP   OD2 HD2  sing N N 92  
ASP   OXT HXT  sing N N 93  
CYS   N   CA   sing N N 94  
CYS   N   H    sing N N 95  
CYS   N   H2   sing N N 96  
CYS   CA  C    sing N N 97  
CYS   CA  CB   sing N N 98  
CYS   CA  HA   sing N N 99  
CYS   C   O    doub N N 100 
CYS   C   OXT  sing N N 101 
CYS   CB  SG   sing N N 102 
CYS   CB  HB2  sing N N 103 
CYS   CB  HB3  sing N N 104 
CYS   SG  HG   sing N N 105 
CYS   OXT HXT  sing N N 106 
GLN   N   CA   sing N N 107 
GLN   N   H    sing N N 108 
GLN   N   H2   sing N N 109 
GLN   CA  C    sing N N 110 
GLN   CA  CB   sing N N 111 
GLN   CA  HA   sing N N 112 
GLN   C   O    doub N N 113 
GLN   C   OXT  sing N N 114 
GLN   CB  CG   sing N N 115 
GLN   CB  HB2  sing N N 116 
GLN   CB  HB3  sing N N 117 
GLN   CG  CD   sing N N 118 
GLN   CG  HG2  sing N N 119 
GLN   CG  HG3  sing N N 120 
GLN   CD  OE1  doub N N 121 
GLN   CD  NE2  sing N N 122 
GLN   NE2 HE21 sing N N 123 
GLN   NE2 HE22 sing N N 124 
GLN   OXT HXT  sing N N 125 
GLU   N   CA   sing N N 126 
GLU   N   H    sing N N 127 
GLU   N   H2   sing N N 128 
GLU   CA  C    sing N N 129 
GLU   CA  CB   sing N N 130 
GLU   CA  HA   sing N N 131 
GLU   C   O    doub N N 132 
GLU   C   OXT  sing N N 133 
GLU   CB  CG   sing N N 134 
GLU   CB  HB2  sing N N 135 
GLU   CB  HB3  sing N N 136 
GLU   CG  CD   sing N N 137 
GLU   CG  HG2  sing N N 138 
GLU   CG  HG3  sing N N 139 
GLU   CD  OE1  doub N N 140 
GLU   CD  OE2  sing N N 141 
GLU   OE2 HE2  sing N N 142 
GLU   OXT HXT  sing N N 143 
GLY   N   CA   sing N N 144 
GLY   N   H    sing N N 145 
GLY   N   H2   sing N N 146 
GLY   CA  C    sing N N 147 
GLY   CA  HA2  sing N N 148 
GLY   CA  HA3  sing N N 149 
GLY   C   O    doub N N 150 
GLY   C   OXT  sing N N 151 
GLY   OXT HXT  sing N N 152 
HIS   N   CA   sing N N 153 
HIS   N   H    sing N N 154 
HIS   N   H2   sing N N 155 
HIS   CA  C    sing N N 156 
HIS   CA  CB   sing N N 157 
HIS   CA  HA   sing N N 158 
HIS   C   O    doub N N 159 
HIS   C   OXT  sing N N 160 
HIS   CB  CG   sing N N 161 
HIS   CB  HB2  sing N N 162 
HIS   CB  HB3  sing N N 163 
HIS   CG  ND1  sing Y N 164 
HIS   CG  CD2  doub Y N 165 
HIS   ND1 CE1  doub Y N 166 
HIS   ND1 HD1  sing N N 167 
HIS   CD2 NE2  sing Y N 168 
HIS   CD2 HD2  sing N N 169 
HIS   CE1 NE2  sing Y N 170 
HIS   CE1 HE1  sing N N 171 
HIS   NE2 HE2  sing N N 172 
HIS   OXT HXT  sing N N 173 
HOH   O   H1   sing N N 174 
HOH   O   H2   sing N N 175 
ILE   N   CA   sing N N 176 
ILE   N   H    sing N N 177 
ILE   N   H2   sing N N 178 
ILE   CA  C    sing N N 179 
ILE   CA  CB   sing N N 180 
ILE   CA  HA   sing N N 181 
ILE   C   O    doub N N 182 
ILE   C   OXT  sing N N 183 
ILE   CB  CG1  sing N N 184 
ILE   CB  CG2  sing N N 185 
ILE   CB  HB   sing N N 186 
ILE   CG1 CD1  sing N N 187 
ILE   CG1 HG12 sing N N 188 
ILE   CG1 HG13 sing N N 189 
ILE   CG2 HG21 sing N N 190 
ILE   CG2 HG22 sing N N 191 
ILE   CG2 HG23 sing N N 192 
ILE   CD1 HD11 sing N N 193 
ILE   CD1 HD12 sing N N 194 
ILE   CD1 HD13 sing N N 195 
ILE   OXT HXT  sing N N 196 
LEU   N   CA   sing N N 197 
LEU   N   H    sing N N 198 
LEU   N   H2   sing N N 199 
LEU   CA  C    sing N N 200 
LEU   CA  CB   sing N N 201 
LEU   CA  HA   sing N N 202 
LEU   C   O    doub N N 203 
LEU   C   OXT  sing N N 204 
LEU   CB  CG   sing N N 205 
LEU   CB  HB2  sing N N 206 
LEU   CB  HB3  sing N N 207 
LEU   CG  CD1  sing N N 208 
LEU   CG  CD2  sing N N 209 
LEU   CG  HG   sing N N 210 
LEU   CD1 HD11 sing N N 211 
LEU   CD1 HD12 sing N N 212 
LEU   CD1 HD13 sing N N 213 
LEU   CD2 HD21 sing N N 214 
LEU   CD2 HD22 sing N N 215 
LEU   CD2 HD23 sing N N 216 
LEU   OXT HXT  sing N N 217 
LYS   N   CA   sing N N 218 
LYS   N   H    sing N N 219 
LYS   N   H2   sing N N 220 
LYS   CA  C    sing N N 221 
LYS   CA  CB   sing N N 222 
LYS   CA  HA   sing N N 223 
LYS   C   O    doub N N 224 
LYS   C   OXT  sing N N 225 
LYS   CB  CG   sing N N 226 
LYS   CB  HB2  sing N N 227 
LYS   CB  HB3  sing N N 228 
LYS   CG  CD   sing N N 229 
LYS   CG  HG2  sing N N 230 
LYS   CG  HG3  sing N N 231 
LYS   CD  CE   sing N N 232 
LYS   CD  HD2  sing N N 233 
LYS   CD  HD3  sing N N 234 
LYS   CE  NZ   sing N N 235 
LYS   CE  HE2  sing N N 236 
LYS   CE  HE3  sing N N 237 
LYS   NZ  HZ1  sing N N 238 
LYS   NZ  HZ2  sing N N 239 
LYS   NZ  HZ3  sing N N 240 
LYS   OXT HXT  sing N N 241 
MET   N   CA   sing N N 242 
MET   N   H    sing N N 243 
MET   N   H2   sing N N 244 
MET   CA  C    sing N N 245 
MET   CA  CB   sing N N 246 
MET   CA  HA   sing N N 247 
MET   C   O    doub N N 248 
MET   C   OXT  sing N N 249 
MET   CB  CG   sing N N 250 
MET   CB  HB2  sing N N 251 
MET   CB  HB3  sing N N 252 
MET   CG  SD   sing N N 253 
MET   CG  HG2  sing N N 254 
MET   CG  HG3  sing N N 255 
MET   SD  CE   sing N N 256 
MET   CE  HE1  sing N N 257 
MET   CE  HE2  sing N N 258 
MET   CE  HE3  sing N N 259 
MET   OXT HXT  sing N N 260 
MPD   C1  C2   sing N N 261 
MPD   C1  H11  sing N N 262 
MPD   C1  H12  sing N N 263 
MPD   C1  H13  sing N N 264 
MPD   C2  O2   sing N N 265 
MPD   C2  CM   sing N N 266 
MPD   C2  C3   sing N N 267 
MPD   O2  HO2  sing N N 268 
MPD   CM  HM1  sing N N 269 
MPD   CM  HM2  sing N N 270 
MPD   CM  HM3  sing N N 271 
MPD   C3  C4   sing N N 272 
MPD   C3  H31  sing N N 273 
MPD   C3  H32  sing N N 274 
MPD   C4  O4   sing N N 275 
MPD   C4  C5   sing N N 276 
MPD   C4  H4   sing N N 277 
MPD   O4  HO4  sing N N 278 
MPD   C5  H51  sing N N 279 
MPD   C5  H52  sing N N 280 
MPD   C5  H53  sing N N 281 
P6G   O1  C2   sing N N 282 
P6G   O1  H1   sing N N 283 
P6G   C2  C3   sing N N 284 
P6G   C2  H21  sing N N 285 
P6G   C2  H22  sing N N 286 
P6G   C3  O4   sing N N 287 
P6G   C3  H31  sing N N 288 
P6G   C3  H32  sing N N 289 
P6G   O4  C5   sing N N 290 
P6G   C5  C6   sing N N 291 
P6G   C5  H51  sing N N 292 
P6G   C5  H52  sing N N 293 
P6G   C6  O7   sing N N 294 
P6G   C6  H61  sing N N 295 
P6G   C6  H62  sing N N 296 
P6G   O7  C8   sing N N 297 
P6G   C8  C9   sing N N 298 
P6G   C8  H81  sing N N 299 
P6G   C8  H82  sing N N 300 
P6G   C9  O10  sing N N 301 
P6G   C9  H91  sing N N 302 
P6G   C9  H92  sing N N 303 
P6G   O10 C11  sing N N 304 
P6G   C11 C12  sing N N 305 
P6G   C11 H111 sing N N 306 
P6G   C11 H112 sing N N 307 
P6G   C12 O13  sing N N 308 
P6G   C12 H121 sing N N 309 
P6G   C12 H122 sing N N 310 
P6G   O13 C14  sing N N 311 
P6G   C14 C15  sing N N 312 
P6G   C14 H141 sing N N 313 
P6G   C14 H142 sing N N 314 
P6G   C15 O16  sing N N 315 
P6G   C15 H151 sing N N 316 
P6G   C15 H152 sing N N 317 
P6G   O16 C17  sing N N 318 
P6G   C17 C18  sing N N 319 
P6G   C17 H171 sing N N 320 
P6G   C17 H172 sing N N 321 
P6G   C18 O19  sing N N 322 
P6G   C18 H181 sing N N 323 
P6G   C18 H182 sing N N 324 
P6G   O19 H19  sing N N 325 
PG4   O1  C1   sing N N 326 
PG4   O1  HO1  sing N N 327 
PG4   C1  C2   sing N N 328 
PG4   C1  H11  sing N N 329 
PG4   C1  H12  sing N N 330 
PG4   C2  O2   sing N N 331 
PG4   C2  H21  sing N N 332 
PG4   C2  H22  sing N N 333 
PG4   O2  C3   sing N N 334 
PG4   C3  C4   sing N N 335 
PG4   C3  H31  sing N N 336 
PG4   C3  H32  sing N N 337 
PG4   C4  O3   sing N N 338 
PG4   C4  H41  sing N N 339 
PG4   C4  H42  sing N N 340 
PG4   O3  C5   sing N N 341 
PG4   C5  C6   sing N N 342 
PG4   C5  H51  sing N N 343 
PG4   C5  H52  sing N N 344 
PG4   C6  O4   sing N N 345 
PG4   C6  H61  sing N N 346 
PG4   C6  H62  sing N N 347 
PG4   O4  C7   sing N N 348 
PG4   C7  C8   sing N N 349 
PG4   C7  H71  sing N N 350 
PG4   C7  H72  sing N N 351 
PG4   C8  O5   sing N N 352 
PG4   C8  H81  sing N N 353 
PG4   C8  H82  sing N N 354 
PG4   O5  HO5  sing N N 355 
PHE   N   CA   sing N N 356 
PHE   N   H    sing N N 357 
PHE   N   H2   sing N N 358 
PHE   CA  C    sing N N 359 
PHE   CA  CB   sing N N 360 
PHE   CA  HA   sing N N 361 
PHE   C   O    doub N N 362 
PHE   C   OXT  sing N N 363 
PHE   CB  CG   sing N N 364 
PHE   CB  HB2  sing N N 365 
PHE   CB  HB3  sing N N 366 
PHE   CG  CD1  doub Y N 367 
PHE   CG  CD2  sing Y N 368 
PHE   CD1 CE1  sing Y N 369 
PHE   CD1 HD1  sing N N 370 
PHE   CD2 CE2  doub Y N 371 
PHE   CD2 HD2  sing N N 372 
PHE   CE1 CZ   doub Y N 373 
PHE   CE1 HE1  sing N N 374 
PHE   CE2 CZ   sing Y N 375 
PHE   CE2 HE2  sing N N 376 
PHE   CZ  HZ   sing N N 377 
PHE   OXT HXT  sing N N 378 
PRO   N   CA   sing N N 379 
PRO   N   CD   sing N N 380 
PRO   N   H    sing N N 381 
PRO   CA  C    sing N N 382 
PRO   CA  CB   sing N N 383 
PRO   CA  HA   sing N N 384 
PRO   C   O    doub N N 385 
PRO   C   OXT  sing N N 386 
PRO   CB  CG   sing N N 387 
PRO   CB  HB2  sing N N 388 
PRO   CB  HB3  sing N N 389 
PRO   CG  CD   sing N N 390 
PRO   CG  HG2  sing N N 391 
PRO   CG  HG3  sing N N 392 
PRO   CD  HD2  sing N N 393 
PRO   CD  HD3  sing N N 394 
PRO   OXT HXT  sing N N 395 
SER   N   CA   sing N N 396 
SER   N   H    sing N N 397 
SER   N   H2   sing N N 398 
SER   CA  C    sing N N 399 
SER   CA  CB   sing N N 400 
SER   CA  HA   sing N N 401 
SER   C   O    doub N N 402 
SER   C   OXT  sing N N 403 
SER   CB  OG   sing N N 404 
SER   CB  HB2  sing N N 405 
SER   CB  HB3  sing N N 406 
SER   OG  HG   sing N N 407 
SER   OXT HXT  sing N N 408 
THR   N   CA   sing N N 409 
THR   N   H    sing N N 410 
THR   N   H2   sing N N 411 
THR   CA  C    sing N N 412 
THR   CA  CB   sing N N 413 
THR   CA  HA   sing N N 414 
THR   C   O    doub N N 415 
THR   C   OXT  sing N N 416 
THR   CB  OG1  sing N N 417 
THR   CB  CG2  sing N N 418 
THR   CB  HB   sing N N 419 
THR   OG1 HG1  sing N N 420 
THR   CG2 HG21 sing N N 421 
THR   CG2 HG22 sing N N 422 
THR   CG2 HG23 sing N N 423 
THR   OXT HXT  sing N N 424 
TRP   N   CA   sing N N 425 
TRP   N   H    sing N N 426 
TRP   N   H2   sing N N 427 
TRP   CA  C    sing N N 428 
TRP   CA  CB   sing N N 429 
TRP   CA  HA   sing N N 430 
TRP   C   O    doub N N 431 
TRP   C   OXT  sing N N 432 
TRP   CB  CG   sing N N 433 
TRP   CB  HB2  sing N N 434 
TRP   CB  HB3  sing N N 435 
TRP   CG  CD1  doub Y N 436 
TRP   CG  CD2  sing Y N 437 
TRP   CD1 NE1  sing Y N 438 
TRP   CD1 HD1  sing N N 439 
TRP   CD2 CE2  doub Y N 440 
TRP   CD2 CE3  sing Y N 441 
TRP   NE1 CE2  sing Y N 442 
TRP   NE1 HE1  sing N N 443 
TRP   CE2 CZ2  sing Y N 444 
TRP   CE3 CZ3  doub Y N 445 
TRP   CE3 HE3  sing N N 446 
TRP   CZ2 CH2  doub Y N 447 
TRP   CZ2 HZ2  sing N N 448 
TRP   CZ3 CH2  sing Y N 449 
TRP   CZ3 HZ3  sing N N 450 
TRP   CH2 HH2  sing N N 451 
TRP   OXT HXT  sing N N 452 
TYR   N   CA   sing N N 453 
TYR   N   H    sing N N 454 
TYR   N   H2   sing N N 455 
TYR   CA  C    sing N N 456 
TYR   CA  CB   sing N N 457 
TYR   CA  HA   sing N N 458 
TYR   C   O    doub N N 459 
TYR   C   OXT  sing N N 460 
TYR   CB  CG   sing N N 461 
TYR   CB  HB2  sing N N 462 
TYR   CB  HB3  sing N N 463 
TYR   CG  CD1  doub Y N 464 
TYR   CG  CD2  sing Y N 465 
TYR   CD1 CE1  sing Y N 466 
TYR   CD1 HD1  sing N N 467 
TYR   CD2 CE2  doub Y N 468 
TYR   CD2 HD2  sing N N 469 
TYR   CE1 CZ   doub Y N 470 
TYR   CE1 HE1  sing N N 471 
TYR   CE2 CZ   sing Y N 472 
TYR   CE2 HE2  sing N N 473 
TYR   CZ  OH   sing N N 474 
TYR   OH  HH   sing N N 475 
TYR   OXT HXT  sing N N 476 
VAL   N   CA   sing N N 477 
VAL   N   H    sing N N 478 
VAL   N   H2   sing N N 479 
VAL   CA  C    sing N N 480 
VAL   CA  CB   sing N N 481 
VAL   CA  HA   sing N N 482 
VAL   C   O    doub N N 483 
VAL   C   OXT  sing N N 484 
VAL   CB  CG1  sing N N 485 
VAL   CB  CG2  sing N N 486 
VAL   CB  HB   sing N N 487 
VAL   CG1 HG11 sing N N 488 
VAL   CG1 HG12 sing N N 489 
VAL   CG1 HG13 sing N N 490 
VAL   CG2 HG21 sing N N 491 
VAL   CG2 HG22 sing N N 492 
VAL   CG2 HG23 sing N N 493 
VAL   OXT HXT  sing N N 494 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9J6N 
_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]   0.012141 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001047 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017438 
_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]   0.009147 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA   A 1 22  ? -20.201 5.707   60.520  1.00 30.38 ? 45   ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 22  ? -20.896 5.263   59.290  1.00 27.46 ? 45   ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 22  ? -20.836 6.381   58.269  1.00 23.39 ? 45   ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 22  ? -21.093 7.520   58.599  1.00 23.98 ? 45   ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 22  ? -22.333 4.899   59.565  1.00 29.47 ? 45   ALA   A CB  1 
ATOM   6    N  N   . PRO   A 1 23  ? -20.689 6.062   56.972  1.00 19.94 ? 46   PRO   A N   1 
ATOM   7    C  CA  . PRO   A 1 23  ? -20.715 7.073   55.916  1.00 18.82 ? 46   PRO   A CA  1 
ATOM   8    C  C   . PRO   A 1 23  ? -22.153 7.521   55.657  1.00 18.74 ? 46   PRO   A C   1 
ATOM   9    O  O   . PRO   A 1 23  ? -23.095 6.844   56.049  1.00 19.89 ? 46   PRO   A O   1 
ATOM   10   C  CB  . PRO   A 1 23  ? -20.111 6.268   54.755  1.00 18.06 ? 46   PRO   A CB  1 
ATOM   11   C  CG  . PRO   A 1 23  ? -20.695 4.888   54.938  1.00 19.22 ? 46   PRO   A CG  1 
ATOM   12   C  CD  . PRO   A 1 23  ? -20.635 4.694   56.446  1.00 21.72 ? 46   PRO   A CD  1 
ATOM   13   N  N   . ARG   A 1 24  ? -22.306 8.685   55.025  1.00 19.45 ? 47   ARG   A N   1 
ATOM   14   C  CA  . ARG   A 1 24  ? -23.578 9.106   54.466  1.00 19.56 ? 47   ARG   A CA  1 
ATOM   15   C  C   . ARG   A 1 24  ? -24.078 8.039   53.496  1.00 18.85 ? 47   ARG   A C   1 
ATOM   16   O  O   . ARG   A 1 24  ? -23.365 7.651   52.575  1.00 19.72 ? 47   ARG   A O   1 
ATOM   17   C  CB  . ARG   A 1 24  ? -23.317 10.437  53.765  1.00 20.53 ? 47   ARG   A CB  1 
ATOM   18   C  CG  . ARG   A 1 24  ? -24.607 11.147  53.392  1.00 20.79 ? 47   ARG   A CG  1 
ATOM   19   C  CD  . ARG   A 1 24  ? -24.254 12.573  53.064  1.00 21.56 ? 47   ARG   A CD  1 
ATOM   20   N  NE  . ARG   A 1 24  ? -25.481 13.376  53.048  1.00 24.17 ? 47   ARG   A NE  1 
ATOM   21   C  CZ  . ARG   A 1 24  ? -26.062 13.871  51.966  1.00 28.94 ? 47   ARG   A CZ  1 
ATOM   22   N  NH1 . ARG   A 1 24  ? -25.560 13.633  50.758  1.00 29.32 ? 47   ARG   A NH1 1 
ATOM   23   N  NH2 . ARG   A 1 24  ? -27.151 14.607  52.102  1.00 27.42 ? 47   ARG   A NH2 1 
ATOM   24   N  N   . ALA   A 1 25  ? -25.288 7.525   53.739  1.00 18.50 ? 48   ALA   A N   1 
ATOM   25   C  CA  . ALA   A 1 25  ? -25.864 6.461   52.925  1.00 18.01 ? 48   ALA   A CA  1 
ATOM   26   C  C   . ALA   A 1 25  ? -25.858 6.902   51.465  1.00 19.23 ? 48   ALA   A C   1 
ATOM   27   O  O   . ALA   A 1 25  ? -26.016 8.086   51.120  1.00 21.96 ? 48   ALA   A O   1 
ATOM   28   C  CB  . ALA   A 1 25  ? -27.277 6.105   53.358  1.00 16.68 ? 48   ALA   A CB  1 
ATOM   29   N  N   . TRP   A 1 26  ? -25.623 5.917   50.613  1.00 16.23 ? 49   TRP   A N   1 
ATOM   30   C  CA  . TRP   A 1 26  ? -25.656 6.168   49.183  1.00 15.13 ? 49   TRP   A CA  1 
ATOM   31   C  C   . TRP   A 1 26  ? -26.971 6.842   48.778  1.00 17.42 ? 49   TRP   A C   1 
ATOM   32   O  O   . TRP   A 1 26  ? -28.037 6.317   49.108  1.00 18.47 ? 49   TRP   A O   1 
ATOM   33   C  CB  . TRP   A 1 26  ? -25.472 4.852   48.439  1.00 14.87 ? 49   TRP   A CB  1 
ATOM   34   C  CG  . TRP   A 1 26  ? -25.277 5.087   46.968  1.00 12.18 ? 49   TRP   A CG  1 
ATOM   35   C  CD1 . TRP   A 1 26  ? -24.154 5.537   46.344  1.00 12.91 ? 49   TRP   A CD1 1 
ATOM   36   C  CD2 . TRP   A 1 26  ? -26.260 4.882   45.942  1.00 11.73 ? 49   TRP   A CD2 1 
ATOM   37   N  NE1 . TRP   A 1 26  ? -24.392 5.672   45.001  1.00 11.85 ? 49   TRP   A NE1 1 
ATOM   38   C  CE2 . TRP   A 1 26  ? -25.660 5.258   44.729  1.00 11.40 ? 49   TRP   A CE2 1 
ATOM   39   C  CE3 . TRP   A 1 26  ? -27.588 4.438   45.932  1.00 13.12 ? 49   TRP   A CE3 1 
ATOM   40   C  CZ2 . TRP   A 1 26  ? -26.337 5.176   43.517  1.00 12.58 ? 49   TRP   A CZ2 1 
ATOM   41   C  CZ3 . TRP   A 1 26  ? -28.247 4.354   44.731  1.00 12.36 ? 49   TRP   A CZ3 1 
ATOM   42   C  CH2 . TRP   A 1 26  ? -27.611 4.680   43.544  1.00 12.51 ? 49   TRP   A CH2 1 
ATOM   43   N  N   . THR   A 1 27  ? -26.847 7.880   47.937  1.00 16.68 ? 50   THR   A N   1 
ATOM   44   C  CA  . THR   A 1 27  ? -27.923 8.743   47.493  1.00 21.97 ? 50   THR   A CA  1 
ATOM   45   C  C   . THR   A 1 27  ? -27.892 8.785   45.976  1.00 19.02 ? 50   THR   A C   1 
ATOM   46   O  O   . THR   A 1 27  ? -26.896 9.228   45.439  1.00 17.17 ? 50   THR   A O   1 
ATOM   47   C  CB  . THR   A 1 27  ? -27.675 10.170  47.987  1.00 25.12 ? 50   THR   A CB  1 
ATOM   48   O  OG1 . THR   A 1 27  ? -26.477 10.576  47.307  1.00 36.70 ? 50   THR   A OG1 1 
ATOM   49   C  CG2 . THR   A 1 27  ? -27.468 10.253  49.488  1.00 29.10 ? 50   THR   A CG2 1 
ATOM   50   N  N   . PRO   A 1 28  ? -28.955 8.398   45.248  1.00 20.27 ? 51   PRO   A N   1 
ATOM   51   C  CA  . PRO   A 1 28  ? -28.963 8.593   43.797  1.00 18.47 ? 51   PRO   A CA  1 
ATOM   52   C  C   . PRO   A 1 28  ? -28.956 10.073  43.438  1.00 18.00 ? 51   PRO   A C   1 
ATOM   53   O  O   . PRO   A 1 28  ? -29.393 10.927  44.206  1.00 15.87 ? 51   PRO   A O   1 
ATOM   54   C  CB  . PRO   A 1 28  ? -30.215 7.871   43.285  1.00 22.53 ? 51   PRO   A CB  1 
ATOM   55   C  CG  . PRO   A 1 28  ? -30.761 7.133   44.470  1.00 24.53 ? 51   PRO   A CG  1 
ATOM   56   C  CD  . PRO   A 1 28  ? -30.146 7.703   45.738  1.00 23.38 ? 51   PRO   A CD  1 
ATOM   57   N  N   . LYS   A 1 29  ? -28.439 10.351  42.236  1.00 16.58 ? 52   LYS   A N   1 
ATOM   58   C  CA  . LYS   A 1 29  ? -28.312 11.701  41.712  1.00 15.93 ? 52   LYS   A CA  1 
ATOM   59   C  C   . LYS   A 1 29  ? -29.135 11.757  40.432  1.00 16.53 ? 52   LYS   A C   1 
ATOM   60   O  O   . LYS   A 1 29  ? -29.099 10.832  39.612  1.00 14.62 ? 52   LYS   A O   1 
ATOM   61   C  CB  . LYS   A 1 29  ? -26.845 12.039  41.430  1.00 15.43 ? 52   LYS   A CB  1 
ATOM   62   C  CG  . LYS   A 1 29  ? -26.012 12.173  42.688  1.00 16.85 ? 52   LYS   A CG  1 
ATOM   63   C  CD  . LYS   A 1 29  ? -26.231 13.521  43.360  1.00 21.15 ? 52   LYS   A CD  1 
ATOM   64   C  CE  . LYS   A 1 29  ? -25.484 13.621  44.648  1.00 24.28 ? 52   LYS   A CE  1 
ATOM   65   N  NZ  . LYS   A 1 29  ? -25.429 15.044  45.026  1.00 31.94 ? 52   LYS   A NZ  1 
ATOM   66   N  N   . PRO   A 1 30  ? -29.980 12.797  40.263  1.00 18.84 ? 53   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 30  ? -30.682 12.981  38.998  1.00 18.48 ? 53   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 30  ? -29.662 13.142  37.874  1.00 15.36 ? 53   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 30  ? -28.721 13.914  37.948  1.00 15.48 ? 53   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 30  ? -31.541 14.225  39.186  1.00 21.20 ? 53   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 30  ? -30.970 14.888  40.414  1.00 24.76 ? 53   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 30  ? -30.372 13.778  41.282  1.00 22.88 ? 53   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 31  ? -29.876 12.371  36.820  1.00 15.35 ? 54   SER   A N   1 
ATOM   74   C  CA  . SER   A 1 31  ? -29.035 12.418  35.654  1.00 15.30 ? 54   SER   A CA  1 
ATOM   75   C  C   . SER   A 1 31  ? -29.401 13.612  34.761  1.00 14.01 ? 54   SER   A C   1 
ATOM   76   O  O   . SER   A 1 31  ? -30.572 13.945  34.613  1.00 13.03 ? 54   SER   A O   1 
ATOM   77   C  CB  . SER   A 1 31  ? -29.123 11.107  34.925  1.00 17.65 ? 54   SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 31  ? -28.331 11.156  33.745  1.00 20.60 ? 54   SER   A OG  1 
ATOM   79   N  N   . PRO   A 1 32  ? -28.409 14.277  34.142  1.00 13.43 ? 55   PRO   A N   1 
ATOM   80   C  CA  . PRO   A 1 32  ? -28.637 15.394  33.220  1.00 14.42 ? 55   PRO   A CA  1 
ATOM   81   C  C   . PRO   A 1 32  ? -29.560 15.098  32.053  1.00 13.45 ? 55   PRO   A C   1 
ATOM   82   O  O   . PRO   A 1 32  ? -30.211 16.006  31.567  1.00 13.49 ? 55   PRO   A O   1 
ATOM   83   C  CB  . PRO   A 1 32  ? -27.251 15.782  32.708  1.00 14.26 ? 55   PRO   A CB  1 
ATOM   84   C  CG  . PRO   A 1 32  ? -26.288 15.172  33.668  1.00 16.51 ? 55   PRO   A CG  1 
ATOM   85   C  CD  . PRO   A 1 32  ? -26.976 14.043  34.377  1.00 15.21 ? 55   PRO   A CD  1 
ATOM   86   N  N   . MET   A 1 33  ? -29.561 13.829  31.618  1.00 12.28 ? 56   MET   A N   1 
ATOM   87   C  CA  . MET   A 1 33  ? -30.531 13.292  30.680  1.00 11.92 ? 56   MET   A CA  1 
ATOM   88   C  C   . MET   A 1 33  ? -30.816 11.870  31.110  1.00 12.78 ? 56   MET   A C   1 
ATOM   89   O  O   . MET   A 1 33  ? -29.962 11.223  31.704  1.00 13.26 ? 56   MET   A O   1 
ATOM   90   C  CB  . MET   A 1 33  ? -29.984 13.204  29.250  1.00 10.89 ? 56   MET   A CB  1 
ATOM   91   C  CG  . MET   A 1 33  ? -29.294 14.463  28.748  1.00 10.66 ? 56   MET   A CG  1 
ATOM   92   S  SD  . MET   A 1 33  ? -28.697 14.334  27.041  1.00 11.41 ? 56   MET   A SD  1 
ATOM   93   C  CE  . MET   A 1 33  ? -30.168 14.517  26.028  1.00 10.94 ? 56   MET   A CE  1 
ATOM   94   N  N   . THR   A 1 34  ? -31.977 11.363  30.725  1.00 12.08 ? 57   THR   A N   1 
ATOM   95   C  CA  . THR   A 1 34  ? -32.376 10.022  31.104  1.00 12.78 ? 57   THR   A CA  1 
ATOM   96   C  C   . THR   A 1 34  ? -32.204 9.125   29.887  1.00 11.38 ? 57   THR   A C   1 
ATOM   97   O  O   . THR   A 1 34  ? -32.857 9.342   28.880  1.00 10.22 ? 57   THR   A O   1 
ATOM   98   C  CB  . THR   A 1 34  ? -33.825 10.031  31.585  1.00 14.31 ? 57   THR   A CB  1 
ATOM   99   O  OG1 . THR   A 1 34  ? -33.899 10.936  32.686  1.00 15.48 ? 57   THR   A OG1 1 
ATOM   100  C  CG2 . THR   A 1 34  ? -34.267 8.696   32.143  1.00 13.62 ? 57   THR   A CG2 1 
ATOM   101  N  N   . THR   A 1 35  ? -31.417 8.053   30.017  1.00 10.02 ? 58   THR   A N   1 
ATOM   102  C  CA  . THR   A 1 35  ? -31.382 7.064   28.969  1.00 9.56  ? 58   THR   A CA  1 
ATOM   103  C  C   . THR   A 1 35  ? -32.426 6.009   29.269  1.00 9.70  ? 58   THR   A C   1 
ATOM   104  O  O   . THR   A 1 35  ? -32.932 5.940   30.380  1.00 10.37 ? 58   THR   A O   1 
ATOM   105  C  CB  . THR   A 1 35  ? -29.991 6.452   28.828  1.00 9.52  ? 58   THR   A CB  1 
ATOM   106  O  OG1 . THR   A 1 35  ? -29.808 5.497   29.873  1.00 8.51  ? 58   THR   A OG1 1 
ATOM   107  C  CG2 . THR   A 1 35  ? -28.903 7.512   28.764  1.00 9.36  ? 58   THR   A CG2 1 
ATOM   108  N  N   . PRO   A 1 36  ? -32.744 5.096   28.328  1.00 9.88  ? 59   PRO   A N   1 
ATOM   109  C  CA  . PRO   A 1 36  ? -33.680 4.015   28.657  1.00 10.51 ? 59   PRO   A CA  1 
ATOM   110  C  C   . PRO   A 1 36  ? -33.244 3.148   29.832  1.00 11.61 ? 59   PRO   A C   1 
ATOM   111  O  O   . PRO   A 1 36  ? -34.064 2.420   30.361  1.00 10.82 ? 59   PRO   A O   1 
ATOM   112  C  CB  . PRO   A 1 36  ? -33.740 3.219   27.363  1.00 10.24 ? 59   PRO   A CB  1 
ATOM   113  C  CG  . PRO   A 1 36  ? -33.554 4.277   26.297  1.00 10.03 ? 59   PRO   A CG  1 
ATOM   114  C  CD  . PRO   A 1 36  ? -32.474 5.165   26.863  1.00 9.56  ? 59   PRO   A CD  1 
ATOM   115  N  N   . TRP   A 1 37  ? -31.952 3.221   30.209  1.00 11.60 ? 60   TRP   A N   1 
ATOM   116  C  CA  . TRP   A 1 37  ? -31.400 2.299   31.194  1.00 11.07 ? 60   TRP   A CA  1 
ATOM   117  C  C   . TRP   A 1 37  ? -31.004 2.987   32.492  1.00 11.71 ? 60   TRP   A C   1 
ATOM   118  O  O   . TRP   A 1 37  ? -30.501 2.303   33.384  1.00 11.70 ? 60   TRP   A O   1 
ATOM   119  C  CB  . TRP   A 1 37  ? -30.201 1.537   30.613  1.00 12.15 ? 60   TRP   A CB  1 
ATOM   120  C  CG  . TRP   A 1 37  ? -30.571 0.872   29.324  1.00 11.26 ? 60   TRP   A CG  1 
ATOM   121  C  CD1 . TRP   A 1 37  ? -31.227 -0.309  29.137  1.00 11.76 ? 60   TRP   A CD1 1 
ATOM   122  C  CD2 . TRP   A 1 37  ? -30.378 1.449   28.025  1.00 10.96 ? 60   TRP   A CD2 1 
ATOM   123  N  NE1 . TRP   A 1 37  ? -31.434 -0.519  27.803  1.00 11.48 ? 60   TRP   A NE1 1 
ATOM   124  C  CE2 . TRP   A 1 37  ? -30.908 0.534   27.093  1.00 11.16 ? 60   TRP   A CE2 1 
ATOM   125  C  CE3 . TRP   A 1 37  ? -29.769 2.611   27.564  1.00 10.69 ? 60   TRP   A CE3 1 
ATOM   126  C  CZ2 . TRP   A 1 37  ? -30.894 0.782   25.719  1.00 10.49 ? 60   TRP   A CZ2 1 
ATOM   127  C  CZ3 . TRP   A 1 37  ? -29.714 2.832   26.201  1.00 10.84 ? 60   TRP   A CZ3 1 
ATOM   128  C  CH2 . TRP   A 1 37  ? -30.284 1.938   25.292  1.00 10.11 ? 60   TRP   A CH2 1 
ATOM   129  N  N   . THR   A 1 38  ? -31.132 4.314   32.586  1.00 11.37 ? 61   THR   A N   1 
ATOM   130  C  CA  . THR   A 1 38  ? -30.708 5.017   33.790  1.00 12.50 ? 61   THR   A CA  1 
ATOM   131  C  C   . THR   A 1 38  ? -31.352 4.414   35.032  1.00 13.04 ? 61   THR   A C   1 
ATOM   132  O  O   . THR   A 1 38  ? -30.654 4.181   36.020  1.00 11.95 ? 61   THR   A O   1 
ATOM   133  C  CB  . THR   A 1 38  ? -31.068 6.500   33.681  1.00 12.01 ? 61   THR   A CB  1 
ATOM   134  O  OG1 . THR   A 1 38  ? -30.434 7.014   32.522  1.00 10.91 ? 61   THR   A OG1 1 
ATOM   135  C  CG2 . THR   A 1 38  ? -30.661 7.310   34.902  1.00 13.29 ? 61   THR   A CG2 1 
ATOM   136  N  N   . ASP   A 1 39  ? -32.674 4.165   34.980  1.00 13.08 ? 62   ASP   A N   1 
ATOM   137  C  CA  . ASP   A 1 39  ? -33.403 3.581   36.096  1.00 16.20 ? 62   ASP   A CA  1 
ATOM   138  C  C   . ASP   A 1 39  ? -33.273 2.058   36.147  1.00 14.95 ? 62   ASP   A C   1 
ATOM   139  O  O   . ASP   A 1 39  ? -33.851 1.436   37.029  1.00 16.05 ? 62   ASP   A O   1 
ATOM   140  C  CB  . ASP   A 1 39  ? -34.881 3.971   36.049  1.00 17.98 ? 62   ASP   A CB  1 
ATOM   141  C  CG  . ASP   A 1 39  ? -35.700 3.221   35.000  1.00 19.26 ? 62   ASP   A CG  1 
ATOM   142  O  OD1 . ASP   A 1 39  ? -35.102 2.596   34.122  1.00 21.16 ? 62   ASP   A OD1 1 
ATOM   143  O  OD2 . ASP   A 1 39  ? -36.944 3.204   35.085  1.00 24.53 ? 62   ASP   A OD2 1 
ATOM   144  N  N   . GLN   A 1 40  ? -32.471 1.449   35.272  1.00 14.09 ? 63   GLN   A N   1 
ATOM   145  C  CA  . GLN   A 1 40  ? -32.297 0.006   35.246  1.00 15.25 ? 63   GLN   A CA  1 
ATOM   146  C  C   . GLN   A 1 40  ? -30.996 -0.438  35.909  1.00 12.84 ? 63   GLN   A C   1 
ATOM   147  O  O   . GLN   A 1 40  ? -30.625 -1.612  35.882  1.00 14.93 ? 63   GLN   A O   1 
ATOM   148  C  CB  . GLN   A 1 40  ? -32.216 -0.493  33.805  1.00 18.21 ? 63   GLN   A CB  1 
ATOM   149  C  CG  . GLN   A 1 40  ? -33.460 -0.153  33.005  1.00 20.55 ? 63   GLN   A CG  1 
ATOM   150  C  CD  . GLN   A 1 40  ? -34.556 -1.151  33.267  1.00 23.98 ? 63   GLN   A CD  1 
ATOM   151  O  OE1 . GLN   A 1 40  ? -34.479 -2.299  32.808  1.00 26.40 ? 63   GLN   A OE1 1 
ATOM   152  N  NE2 . GLN   A 1 40  ? -35.575 -0.713  33.991  1.00 24.31 ? 63   GLN   A NE2 1 
ATOM   153  N  N   . VAL   A 1 41  ? -30.265 0.486   36.500  1.00 11.17 ? 64   VAL   A N   1 
ATOM   154  C  CA  . VAL   A 1 41  ? -28.990 0.108   37.062  1.00 10.19 ? 64   VAL   A CA  1 
ATOM   155  C  C   . VAL   A 1 41  ? -29.200 -0.438  38.471  1.00 11.07 ? 64   VAL   A C   1 
ATOM   156  O  O   . VAL   A 1 41  ? -29.746 0.261   39.312  1.00 11.38 ? 64   VAL   A O   1 
ATOM   157  C  CB  . VAL   A 1 41  ? -28.052 1.320   37.041  1.00 10.35 ? 64   VAL   A CB  1 
ATOM   158  C  CG1 . VAL   A 1 41  ? -26.699 0.927   37.631  1.00 10.38 ? 64   VAL   A CG1 1 
ATOM   159  C  CG2 . VAL   A 1 41  ? -27.915 1.865   35.619  1.00 10.66 ? 64   VAL   A CG2 1 
ATOM   160  N  N   . PRO   A 1 42  ? -28.806 -1.691  38.775  1.00 11.57 ? 65   PRO   A N   1 
ATOM   161  C  CA  . PRO   A 1 42  ? -28.852 -2.199  40.146  1.00 11.46 ? 65   PRO   A CA  1 
ATOM   162  C  C   . PRO   A 1 42  ? -28.070 -1.320  41.103  1.00 12.86 ? 65   PRO   A C   1 
ATOM   163  O  O   . PRO   A 1 42  ? -27.059 -0.723  40.751  1.00 11.71 ? 65   PRO   A O   1 
ATOM   164  C  CB  . PRO   A 1 42  ? -28.189 -3.566  40.005  1.00 12.07 ? 65   PRO   A CB  1 
ATOM   165  C  CG  . PRO   A 1 42  ? -28.515 -3.978  38.598  1.00 12.03 ? 65   PRO   A CG  1 
ATOM   166  C  CD  . PRO   A 1 42  ? -28.339 -2.705  37.821  1.00 12.14 ? 65   PRO   A CD  1 
ATOM   167  N  N   . VAL   A 1 43  ? -28.506 -1.337  42.364  1.00 13.28 ? 66   VAL   A N   1 
ATOM   168  C  CA  . VAL   A 1 43  ? -27.783 -0.645  43.410  1.00 13.51 ? 66   VAL   A CA  1 
ATOM   169  C  C   . VAL   A 1 43  ? -26.562 -1.467  43.799  1.00 13.63 ? 66   VAL   A C   1 
ATOM   170  O  O   . VAL   A 1 43  ? -25.454 -0.964  43.779  1.00 12.60 ? 66   VAL   A O   1 
ATOM   171  C  CB  . VAL   A 1 43  ? -28.707 -0.404  44.612  1.00 14.58 ? 66   VAL   A CB  1 
ATOM   172  C  CG1 . VAL   A 1 43  ? -27.933 0.140   45.807  1.00 14.05 ? 66   VAL   A CG1 1 
ATOM   173  C  CG2 . VAL   A 1 43  ? -29.850 0.518   44.208  1.00 14.77 ? 66   VAL   A CG2 1 
ATOM   174  N  N   . ASP   A 1 44  ? -26.767 -2.725  44.168  1.00 14.30 ? 67   ASP   A N   1 
ATOM   175  C  CA  . ASP   A 1 44  ? -25.717 -3.533  44.760  1.00 17.96 ? 67   ASP   A CA  1 
ATOM   176  C  C   . ASP   A 1 44  ? -24.916 -4.337  43.747  1.00 20.12 ? 67   ASP   A C   1 
ATOM   177  O  O   . ASP   A 1 44  ? -23.794 -4.729  44.058  1.00 22.61 ? 67   ASP   A O   1 
ATOM   178  C  CB  . ASP   A 1 44  ? -26.260 -4.418  45.855  1.00 21.31 ? 67   ASP   A CB  1 
ATOM   179  C  CG  . ASP   A 1 44  ? -26.761 -3.610  47.046  1.00 29.10 ? 67   ASP   A CG  1 
ATOM   180  O  OD1 . ASP   A 1 44  ? -25.958 -2.821  47.602  1.00 34.25 ? 67   ASP   A OD1 1 
ATOM   181  O  OD2 . ASP   A 1 44  ? -27.947 -3.763  47.407  1.00 37.14 ? 67   ASP   A OD2 1 
ATOM   182  N  N   . ASN   A 1 45  ? -25.460 -4.677  42.587  1.00 19.18 ? 68   ASN   A N   1 
ATOM   183  C  CA  . ASN   A 1 45  ? -24.578 -5.417  41.687  1.00 20.41 ? 68   ASN   A CA  1 
ATOM   184  C  C   . ASN   A 1 45  ? -24.739 -4.886  40.274  1.00 14.63 ? 68   ASN   A C   1 
ATOM   185  O  O   . ASN   A 1 45  ? -25.190 -5.601  39.378  1.00 14.67 ? 68   ASN   A O   1 
ATOM   186  C  CB  . ASN   A 1 45  ? -24.755 -6.934  41.708  1.00 24.56 ? 68   ASN   A CB  1 
ATOM   187  C  CG  . ASN   A 1 45  ? -23.535 -7.621  41.100  1.00 33.33 ? 68   ASN   A CG  1 
ATOM   188  O  OD1 . ASN   A 1 45  ? -22.454 -7.013  41.021  1.00 39.84 ? 68   ASN   A OD1 1 
ATOM   189  N  ND2 . ASN   A 1 45  ? -23.656 -8.868  40.647  1.00 34.18 ? 68   ASN   A ND2 1 
ATOM   190  N  N   . PRO   A 1 46  ? -24.397 -3.611  40.019  1.00 11.65 ? 69   PRO   A N   1 
ATOM   191  C  CA  . PRO   A 1 46  ? -24.500 -3.112  38.650  1.00 10.57 ? 69   PRO   A CA  1 
ATOM   192  C  C   . PRO   A 1 46  ? -23.434 -3.796  37.780  1.00 10.19 ? 69   PRO   A C   1 
ATOM   193  O  O   . PRO   A 1 46  ? -22.472 -4.377  38.299  1.00 11.24 ? 69   PRO   A O   1 
ATOM   194  C  CB  . PRO   A 1 46  ? -24.243 -1.641  38.815  1.00 10.33 ? 69   PRO   A CB  1 
ATOM   195  C  CG  . PRO   A 1 46  ? -23.228 -1.581  39.942  1.00 10.86 ? 69   PRO   A CG  1 
ATOM   196  C  CD  . PRO   A 1 46  ? -23.697 -2.655  40.898  1.00 11.28 ? 69   PRO   A CD  1 
ATOM   197  N  N   . LEU   A 1 47  ? -23.630 -3.747  36.464  1.00 9.69  ? 70   LEU   A N   1 
ATOM   198  C  CA  . LEU   A 1 47  ? -22.769 -4.376  35.468  1.00 9.86  ? 70   LEU   A CA  1 
ATOM   199  C  C   . LEU   A 1 47  ? -22.383 -5.783  35.937  1.00 10.19 ? 70   LEU   A C   1 
ATOM   200  O  O   . LEU   A 1 47  ? -21.204 -6.103  36.167  1.00 9.24  ? 70   LEU   A O   1 
ATOM   201  C  CB  . LEU   A 1 47  ? -21.552 -3.501  35.168  1.00 11.85 ? 70   LEU   A CB  1 
ATOM   202  C  CG  . LEU   A 1 47  ? -21.781 -2.146  34.489  1.00 14.40 ? 70   LEU   A CG  1 
ATOM   203  C  CD1 . LEU   A 1 47  ? -20.431 -1.718  33.900  1.00 15.12 ? 70   LEU   A CD1 1 
ATOM   204  C  CD2 . LEU   A 1 47  ? -22.805 -2.218  33.399  1.00 16.75 ? 70   LEU   A CD2 1 
ATOM   205  N  N   . PRO   A 1 48  ? -23.398 -6.670  36.110  1.00 10.55 ? 71   PRO   A N   1 
ATOM   206  C  CA  . PRO   A 1 48  ? -23.200 -7.996  36.694  1.00 11.06 ? 71   PRO   A CA  1 
ATOM   207  C  C   . PRO   A 1 48  ? -22.538 -9.004  35.770  1.00 10.94 ? 71   PRO   A C   1 
ATOM   208  O  O   . PRO   A 1 48  ? -22.037 -10.012 36.251  1.00 12.28 ? 71   PRO   A O   1 
ATOM   209  C  CB  . PRO   A 1 48  ? -24.627 -8.458  37.026  1.00 10.31 ? 71   PRO   A CB  1 
ATOM   210  C  CG  . PRO   A 1 48  ? -25.465 -7.743  36.000  1.00 10.29 ? 71   PRO   A CG  1 
ATOM   211  C  CD  . PRO   A 1 48  ? -24.819 -6.397  35.863  1.00 10.50 ? 71   PRO   A CD  1 
ATOM   212  N  N   . GLU   A 1 49  ? -22.532 -8.723  34.461  1.00 10.41 ? 72   GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 49  ? -22.067 -9.674  33.458  1.00 10.43 ? 72   GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 49  ? -20.566 -9.958  33.582  1.00 9.58  ? 72   GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 49  ? -19.739 -9.112  33.998  1.00 8.61  ? 72   GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 49  ? -22.383 -9.208  32.041  1.00 10.94 ? 72   GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 49  ? -23.870 -9.164  31.696  1.00 12.08 ? 72   GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 49  ? -24.628 -7.964  32.245  1.00 12.42 ? 72   GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 49  ? -24.016 -7.010  32.800  1.00 13.18 ? 72   GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 49  ? -25.859 -8.025  32.153  1.00 14.57 ? 72   GLU   A OE2 1 
ATOM   221  N  N   . TYR   A 1 50  ? -20.211 -11.191 33.195  1.00 8.70  ? 73   TYR   A N   1 
ATOM   222  C  CA  . TYR   A 1 50  ? -18.819 -11.588 33.216  1.00 9.18  ? 73   TYR   A CA  1 
ATOM   223  C  C   . TYR   A 1 50  ? -17.959 -10.604 32.422  1.00 8.83  ? 73   TYR   A C   1 
ATOM   224  O  O   . TYR   A 1 50  ? -18.201 -10.319 31.248  1.00 9.32  ? 73   TYR   A O   1 
ATOM   225  C  CB  . TYR   A 1 50  ? -18.599 -12.987 32.650  1.00 8.81  ? 73   TYR   A CB  1 
ATOM   226  C  CG  . TYR   A 1 50  ? -17.256 -13.606 32.992  1.00 8.27  ? 73   TYR   A CG  1 
ATOM   227  C  CD1 . TYR   A 1 50  ? -17.011 -14.113 34.257  1.00 8.54  ? 73   TYR   A CD1 1 
ATOM   228  C  CD2 . TYR   A 1 50  ? -16.253 -13.722 32.049  1.00 8.24  ? 73   TYR   A CD2 1 
ATOM   229  C  CE1 . TYR   A 1 50  ? -15.822 -14.719 34.566  1.00 8.79  ? 73   TYR   A CE1 1 
ATOM   230  C  CE2 . TYR   A 1 50  ? -15.040 -14.314 32.350  1.00 8.39  ? 73   TYR   A CE2 1 
ATOM   231  C  CZ  . TYR   A 1 50  ? -14.824 -14.822 33.613  1.00 8.64  ? 73   TYR   A CZ  1 
ATOM   232  O  OH  . TYR   A 1 50  ? -13.629 -15.426 33.916  1.00 8.11  ? 73   TYR   A OH  1 
ATOM   233  N  N   . PRO   A 1 51  ? -16.914 -10.039 33.055  1.00 9.21  ? 74   PRO   A N   1 
ATOM   234  C  CA  . PRO   A 1 51  ? -16.185 -8.947  32.416  1.00 9.59  ? 74   PRO   A CA  1 
ATOM   235  C  C   . PRO   A 1 51  ? -15.128 -9.272  31.369  1.00 9.14  ? 74   PRO   A C   1 
ATOM   236  O  O   . PRO   A 1 51  ? -14.560 -8.360  30.790  1.00 10.08 ? 74   PRO   A O   1 
ATOM   237  C  CB  . PRO   A 1 51  ? -15.544 -8.240  33.594  1.00 10.31 ? 74   PRO   A CB  1 
ATOM   238  C  CG  . PRO   A 1 51  ? -15.795 -9.036  34.800  1.00 10.49 ? 74   PRO   A CG  1 
ATOM   239  C  CD  . PRO   A 1 51  ? -16.538 -10.273 34.456  1.00 9.67  ? 74   PRO   A CD  1 
ATOM   240  N  N   . ARG   A 1 52  ? -14.806 -10.555 31.189  1.00 8.87  ? 75   ARG   A N   1 
ATOM   241  C  CA  . ARG   A 1 52  ? -13.708 -10.936 30.317  1.00 9.04  ? 75   ARG   A CA  1 
ATOM   242  C  C   . ARG   A 1 52  ? -14.167 -12.114 29.467  1.00 9.38  ? 75   ARG   A C   1 
ATOM   243  O  O   . ARG   A 1 52  ? -13.674 -13.232 29.636  1.00 8.93  ? 75   ARG   A O   1 
ATOM   244  C  CB  . ARG   A 1 52  ? -12.481 -11.233 31.184  1.00 8.89  ? 75   ARG   A CB  1 
ATOM   245  C  CG  . ARG   A 1 52  ? -11.180 -11.401 30.418  1.00 9.28  ? 75   ARG   A CG  1 
ATOM   246  C  CD  . ARG   A 1 52  ? -10.082 -11.838 31.362  1.00 9.16  ? 75   ARG   A CD  1 
ATOM   247  N  NE  . ARG   A 1 52  ? -10.426 -13.135 31.946  1.00 8.99  ? 75   ARG   A NE  1 
ATOM   248  C  CZ  . ARG   A 1 52  ? -10.047 -13.593 33.137  1.00 9.57  ? 75   ARG   A CZ  1 
ATOM   249  N  NH1 . ARG   A 1 52  ? -9.233  -12.891 33.894  1.00 10.39 ? 75   ARG   A NH1 1 
ATOM   250  N  NH2 . ARG   A 1 52  ? -10.545 -14.726 33.626  1.00 9.61  ? 75   ARG   A NH2 1 
ATOM   251  N  N   . PRO   A 1 53  ? -15.188 -11.922 28.619  1.00 8.95  ? 76   PRO   A N   1 
ATOM   252  C  CA  . PRO   A 1 53  ? -15.825 -13.067 27.945  1.00 9.51  ? 76   PRO   A CA  1 
ATOM   253  C  C   . PRO   A 1 53  ? -14.956 -13.834 26.957  1.00 9.81  ? 76   PRO   A C   1 
ATOM   254  O  O   . PRO   A 1 53  ? -15.364 -14.942 26.571  1.00 10.51 ? 76   PRO   A O   1 
ATOM   255  C  CB  . PRO   A 1 53  ? -17.060 -12.493 27.292  1.00 9.21  ? 76   PRO   A CB  1 
ATOM   256  C  CG  . PRO   A 1 53  ? -16.801 -11.051 27.198  1.00 9.64  ? 76   PRO   A CG  1 
ATOM   257  C  CD  . PRO   A 1 53  ? -15.823 -10.644 28.284  1.00 9.28  ? 76   PRO   A CD  1 
ATOM   258  N  N   . GLN   A 1 54  ? -13.769 -13.315 26.579  1.00 9.30  ? 77   GLN   A N   1 
ATOM   259  C  CA  . GLN   A 1 54  ? -12.903 -14.080 25.703  1.00 9.42  ? 77   GLN   A CA  1 
ATOM   260  C  C   . GLN   A 1 54  ? -11.815 -14.844 26.474  1.00 9.54  ? 77   GLN   A C   1 
ATOM   261  O  O   . GLN   A 1 54  ? -10.923 -15.431 25.854  1.00 8.99  ? 77   GLN   A O   1 
ATOM   262  C  CB  . GLN   A 1 54  ? -12.361 -13.153 24.621  1.00 9.59  ? 77   GLN   A CB  1 
ATOM   263  C  CG  . GLN   A 1 54  ? -11.742 -13.924 23.463  1.00 9.37  ? 77   GLN   A CG  1 
ATOM   264  C  CD  . GLN   A 1 54  ? -11.360 -13.071 22.274  1.00 9.56  ? 77   GLN   A CD  1 
ATOM   265  O  OE1 . GLN   A 1 54  ? -11.069 -11.862 22.366  1.00 10.47 ? 77   GLN   A OE1 1 
ATOM   266  N  NE2 . GLN   A 1 54  ? -11.475 -13.697 21.116  1.00 9.27  ? 77   GLN   A NE2 1 
ATOM   267  N  N   . LEU   A 1 55  ? -11.851 -14.840 27.831  1.00 9.36  ? 78   LEU   A N   1 
ATOM   268  C  CA  . LEU   A 1 55  ? -10.974 -15.708 28.617  1.00 9.94  ? 78   LEU   A CA  1 
ATOM   269  C  C   . LEU   A 1 55  ? -11.709 -16.068 29.912  1.00 9.13  ? 78   LEU   A C   1 
ATOM   270  O  O   . LEU   A 1 55  ? -11.714 -15.301 30.872  1.00 9.31  ? 78   LEU   A O   1 
ATOM   271  C  CB  . LEU   A 1 55  ? -9.660  -14.988 28.878  1.00 11.94 ? 78   LEU   A CB  1 
ATOM   272  C  CG  . LEU   A 1 55  ? -8.522  -15.845 29.433  1.00 14.39 ? 78   LEU   A CG  1 
ATOM   273  C  CD1 . LEU   A 1 55  ? -8.006  -16.782 28.437  1.00 17.07 ? 78   LEU   A CD1 1 
ATOM   274  C  CD2 . LEU   A 1 55  ? -7.390  -14.976 29.926  1.00 18.57 ? 78   LEU   A CD2 1 
ATOM   275  N  N   . THR   A 1 56  ? -12.415 -17.198 29.920  1.00 9.09  ? 79   THR   A N   1 
ATOM   276  C  CA  . THR   A 1 56  ? -13.423 -17.446 30.944  1.00 9.11  ? 79   THR   A CA  1 
ATOM   277  C  C   . THR   A 1 56  ? -13.009 -18.584 31.878  1.00 9.12  ? 79   THR   A C   1 
ATOM   278  O  O   . THR   A 1 56  ? -12.423 -19.575 31.466  1.00 8.67  ? 79   THR   A O   1 
ATOM   279  C  CB  . THR   A 1 56  ? -14.792 -17.797 30.369  1.00 9.76  ? 79   THR   A CB  1 
ATOM   280  O  OG1 . THR   A 1 56  ? -14.689 -19.055 29.687  1.00 10.30 ? 79   THR   A OG1 1 
ATOM   281  C  CG2 . THR   A 1 56  ? -15.295 -16.734 29.414  1.00 9.36  ? 79   THR   A CG2 1 
ATOM   282  N  N   . ARG   A 1 57  ? -13.451 -18.450 33.129  1.00 9.58  ? 80   ARG   A N   1 
ATOM   283  C  CA  . ARG   A 1 57  ? -13.532 -19.562 34.075  1.00 9.53  ? 80   ARG   A CA  1 
ATOM   284  C  C   . ARG   A 1 57  ? -14.870 -19.438 34.779  1.00 10.36 ? 80   ARG   A C   1 
ATOM   285  O  O   . ARG   A 1 57  ? -15.436 -18.349 34.853  1.00 10.59 ? 80   ARG   A O   1 
ATOM   286  C  CB  . ARG   A 1 57  ? -12.438 -19.476 35.156  1.00 9.09  ? 80   ARG   A CB  1 
ATOM   287  C  CG  . ARG   A 1 57  ? -11.005 -19.582 34.667  1.00 8.76  ? 80   ARG   A CG  1 
ATOM   288  C  CD  . ARG   A 1 57  ? -10.031 -19.444 35.772  1.00 8.42  ? 80   ARG   A CD  1 
ATOM   289  N  NE  . ARG   A 1 57  ? -8.648  -19.499 35.315  1.00 8.81  ? 80   ARG   A NE  1 
ATOM   290  C  CZ  . ARG   A 1 57  ? -7.904  -18.501 34.854  1.00 8.77  ? 80   ARG   A CZ  1 
ATOM   291  N  NH1 . ARG   A 1 57  ? -8.334  -17.254 34.901  1.00 9.84  ? 80   ARG   A NH1 1 
ATOM   292  N  NH2 . ARG   A 1 57  ? -6.726  -18.776 34.329  1.00 9.60  ? 80   ARG   A NH2 1 
ATOM   293  N  N   . PRO   A 1 58  ? -15.418 -20.543 35.333  1.00 11.07 ? 81   PRO   A N   1 
ATOM   294  C  CA  . PRO   A 1 58  ? -16.746 -20.494 35.935  1.00 11.54 ? 81   PRO   A CA  1 
ATOM   295  C  C   . PRO   A 1 58  ? -16.843 -19.738 37.253  1.00 11.87 ? 81   PRO   A C   1 
ATOM   296  O  O   . PRO   A 1 58  ? -17.892 -19.180 37.563  1.00 11.36 ? 81   PRO   A O   1 
ATOM   297  C  CB  . PRO   A 1 58  ? -17.160 -21.953 36.054  1.00 11.54 ? 81   PRO   A CB  1 
ATOM   298  C  CG  . PRO   A 1 58  ? -15.859 -22.717 36.013  1.00 12.32 ? 81   PRO   A CG  1 
ATOM   299  C  CD  . PRO   A 1 58  ? -14.876 -21.918 35.177  1.00 11.99 ? 81   PRO   A CD  1 
ATOM   300  N  N   . ASP   A 1 59  ? -15.733 -19.691 37.999  1.00 11.36 ? 82   ASP   A N   1 
ATOM   301  C  CA  . ASP   A 1 59  ? -15.736 -19.136 39.344  1.00 11.24 ? 82   ASP   A CA  1 
ATOM   302  C  C   . ASP   A 1 59  ? -15.247 -17.688 39.298  1.00 10.23 ? 82   ASP   A C   1 
ATOM   303  O  O   . ASP   A 1 59  ? -14.198 -17.424 38.714  1.00 10.22 ? 82   ASP   A O   1 
ATOM   304  C  CB  . ASP   A 1 59  ? -14.820 -19.926 40.254  1.00 11.80 ? 82   ASP   A CB  1 
ATOM   305  C  CG  . ASP   A 1 59  ? -15.261 -21.360 40.487  1.00 13.08 ? 82   ASP   A CG  1 
ATOM   306  O  OD1 . ASP   A 1 59  ? -16.407 -21.543 40.933  1.00 12.89 ? 82   ASP   A OD1 1 
ATOM   307  O  OD2 . ASP   A 1 59  ? -14.465 -22.270 40.188  1.00 16.08 ? 82   ASP   A OD2 1 
ATOM   308  N  N   . TRP   A 1 60  ? -16.034 -16.784 39.898  1.00 10.29 ? 83   TRP   A N   1 
ATOM   309  C  CA  . TRP   A 1 60  ? -15.679 -15.373 40.019  1.00 9.92  ? 83   TRP   A CA  1 
ATOM   310  C  C   . TRP   A 1 60  ? -16.637 -14.712 40.998  1.00 9.66  ? 83   TRP   A C   1 
ATOM   311  O  O   . TRP   A 1 60  ? -17.601 -15.345 41.399  1.00 10.50 ? 83   TRP   A O   1 
ATOM   312  C  CB  . TRP   A 1 60  ? -15.694 -14.672 38.655  1.00 9.86  ? 83   TRP   A CB  1 
ATOM   313  C  CG  . TRP   A 1 60  ? -17.048 -14.364 38.094  1.00 9.90  ? 83   TRP   A CG  1 
ATOM   314  C  CD1 . TRP   A 1 60  ? -17.938 -15.248 37.580  1.00 11.45 ? 83   TRP   A CD1 1 
ATOM   315  C  CD2 . TRP   A 1 60  ? -17.590 -13.060 37.841  1.00 9.74  ? 83   TRP   A CD2 1 
ATOM   316  N  NE1 . TRP   A 1 60  ? -19.025 -14.591 37.079  1.00 11.11 ? 83   TRP   A NE1 1 
ATOM   317  C  CE2 . TRP   A 1 60  ? -18.828 -13.246 37.204  1.00 10.69 ? 83   TRP   A CE2 1 
ATOM   318  C  CE3 . TRP   A 1 60  ? -17.148 -11.769 38.100  1.00 9.68  ? 83   TRP   A CE3 1 
ATOM   319  C  CZ2 . TRP   A 1 60  ? -19.631 -12.183 36.825  1.00 9.74  ? 83   TRP   A CZ2 1 
ATOM   320  C  CZ3 . TRP   A 1 60  ? -17.908 -10.707 37.667  1.00 10.04 ? 83   TRP   A CZ3 1 
ATOM   321  C  CH2 . TRP   A 1 60  ? -19.133 -10.921 37.043  1.00 9.96  ? 83   TRP   A CH2 1 
ATOM   322  N  N   . ALA   A 1 61  ? -16.279 -13.517 41.454  1.00 9.62  ? 84   ALA   A N   1 
ATOM   323  C  CA  . ALA   A 1 61  ? -17.169 -12.715 42.263  1.00 10.13 ? 84   ALA   A CA  1 
ATOM   324  C  C   . ALA   A 1 61  ? -17.052 -11.270 41.825  1.00 9.40  ? 84   ALA   A C   1 
ATOM   325  O  O   . ALA   A 1 61  ? -15.947 -10.773 41.679  1.00 10.45 ? 84   ALA   A O   1 
ATOM   326  C  CB  . ALA   A 1 61  ? -16.813 -12.878 43.703  1.00 9.91  ? 84   ALA   A CB  1 
ATOM   327  N  N   . ASN   A 1 62  ? -18.194 -10.614 41.666  1.00 9.63  ? 85   ASN   A N   1 
ATOM   328  C  CA  . ASN   A 1 62  ? -18.241 -9.233  41.209  1.00 10.29 ? 85   ASN   A CA  1 
ATOM   329  C  C   . ASN   A 1 62  ? -18.210 -8.307  42.426  1.00 10.28 ? 85   ASN   A C   1 
ATOM   330  O  O   . ASN   A 1 62  ? -19.061 -8.468  43.306  1.00 11.65 ? 85   ASN   A O   1 
ATOM   331  C  CB  . ASN   A 1 62  ? -19.555 -9.019  40.468  1.00 10.60 ? 85   ASN   A CB  1 
ATOM   332  C  CG  . ASN   A 1 62  ? -19.540 -7.757  39.635  1.00 12.04 ? 85   ASN   A CG  1 
ATOM   333  O  OD1 . ASN   A 1 62  ? -18.930 -6.744  40.018  1.00 10.35 ? 85   ASN   A OD1 1 
ATOM   334  N  ND2 . ASN   A 1 62  ? -20.086 -7.849  38.428  1.00 12.90 ? 85   ASN   A ND2 1 
ATOM   335  N  N   . LEU   A 1 63  ? -17.272 -7.352  42.490  1.00 10.01 ? 86   LEU   A N   1 
ATOM   336  C  CA  . LEU   A 1 63  ? -17.190 -6.428  43.622  1.00 10.03 ? 86   LEU   A CA  1 
ATOM   337  C  C   . LEU   A 1 63  ? -17.838 -5.080  43.306  1.00 10.29 ? 86   LEU   A C   1 
ATOM   338  O  O   . LEU   A 1 63  ? -17.706 -4.127  44.103  1.00 9.42  ? 86   LEU   A O   1 
ATOM   339  C  CB  . LEU   A 1 63  ? -15.749 -6.224  44.047  1.00 11.18 ? 86   LEU   A CB  1 
ATOM   340  C  CG  . LEU   A 1 63  ? -15.032 -7.474  44.587  1.00 12.39 ? 86   LEU   A CG  1 
ATOM   341  C  CD1 . LEU   A 1 63  ? -13.576 -7.150  44.811  1.00 12.39 ? 86   LEU   A CD1 1 
ATOM   342  C  CD2 . LEU   A 1 63  ? -15.697 -7.993  45.837  1.00 14.31 ? 86   LEU   A CD2 1 
ATOM   343  N  N   . ASN   A 1 64  ? -18.471 -4.947  42.127  1.00 9.40  ? 87   ASN   A N   1 
ATOM   344  C  CA  . ASN   A 1 64  ? -19.263 -3.751  41.869  1.00 9.53  ? 87   ASN   A CA  1 
ATOM   345  C  C   . ASN   A 1 64  ? -20.325 -3.558  42.958  1.00 10.61 ? 87   ASN   A C   1 
ATOM   346  O  O   . ASN   A 1 64  ? -20.744 -4.514  43.625  1.00 10.61 ? 87   ASN   A O   1 
ATOM   347  C  CB  . ASN   A 1 64  ? -19.953 -3.827  40.506  1.00 9.12  ? 87   ASN   A CB  1 
ATOM   348  C  CG  . ASN   A 1 64  ? -18.992 -3.810  39.340  1.00 8.26  ? 87   ASN   A CG  1 
ATOM   349  O  OD1 . ASN   A 1 64  ? -17.803 -3.539  39.525  1.00 8.71  ? 87   ASN   A OD1 1 
ATOM   350  N  ND2 . ASN   A 1 64  ? -19.471 -4.106  38.135  1.00 8.25  ? 87   ASN   A ND2 1 
ATOM   351  N  N   . GLY   A 1 65  ? -20.818 -2.313  43.070  1.00 9.39  ? 88   GLY   A N   1 
ATOM   352  C  CA  . GLY   A 1 65  ? -21.911 -2.011  43.981  1.00 10.13 ? 88   GLY   A CA  1 
ATOM   353  C  C   . GLY   A 1 65  ? -21.548 -0.829  44.863  1.00 9.30  ? 88   GLY   A C   1 
ATOM   354  O  O   . GLY   A 1 65  ? -20.798 0.055   44.426  1.00 8.42  ? 88   GLY   A O   1 
ATOM   355  N  N   . ILE   A 1 66  ? -22.033 -0.831  46.124  1.00 10.30 ? 89   ILE   A N   1 
ATOM   356  C  CA  . ILE   A 1 66  ? -21.914 0.366   46.957  1.00 11.19 ? 89   ILE   A CA  1 
ATOM   357  C  C   . ILE   A 1 66  ? -20.654 0.272   47.810  1.00 11.10 ? 89   ILE   A C   1 
ATOM   358  O  O   . ILE   A 1 66  ? -20.538 -0.564  48.703  1.00 12.37 ? 89   ILE   A O   1 
ATOM   359  C  CB  . ILE   A 1 66  ? -23.198 0.656   47.773  1.00 11.31 ? 89   ILE   A CB  1 
ATOM   360  C  CG1 . ILE   A 1 66  ? -24.424 0.775   46.893  1.00 11.82 ? 89   ILE   A CG1 1 
ATOM   361  C  CG2 . ILE   A 1 66  ? -23.032 1.916   48.629  1.00 11.94 ? 89   ILE   A CG2 1 
ATOM   362  C  CD1 . ILE   A 1 66  ? -24.319 1.745   45.723  1.00 12.45 ? 89   ILE   A CD1 1 
ATOM   363  N  N   . TRP   A 1 67  ? -19.715 1.171   47.552  1.00 10.05 ? 90   TRP   A N   1 
ATOM   364  C  CA  . TRP   A 1 67  ? -18.498 1.265   48.346  1.00 10.41 ? 90   TRP   A CA  1 
ATOM   365  C  C   . TRP   A 1 67  ? -18.556 2.520   49.195  1.00 10.44 ? 90   TRP   A C   1 
ATOM   366  O  O   . TRP   A 1 67  ? -19.150 3.530   48.813  1.00 11.26 ? 90   TRP   A O   1 
ATOM   367  C  CB  . TRP   A 1 67  ? -17.263 1.337   47.454  1.00 10.06 ? 90   TRP   A CB  1 
ATOM   368  C  CG  . TRP   A 1 67  ? -16.979 0.129   46.575  1.00 9.90  ? 90   TRP   A CG  1 
ATOM   369  C  CD1 . TRP   A 1 67  ? -17.850 -0.599  45.803  1.00 9.99  ? 90   TRP   A CD1 1 
ATOM   370  C  CD2 . TRP   A 1 67  ? -15.667 -0.420  46.301  1.00 9.73  ? 90   TRP   A CD2 1 
ATOM   371  N  NE1 . TRP   A 1 67  ? -17.151 -1.531  45.043  1.00 10.43 ? 90   TRP   A NE1 1 
ATOM   372  C  CE2 . TRP   A 1 67  ? -15.821 -1.450  45.346  1.00 9.31  ? 90   TRP   A CE2 1 
ATOM   373  C  CE3 . TRP   A 1 67  ? -14.387 -0.137  46.769  1.00 9.85  ? 90   TRP   A CE3 1 
ATOM   374  C  CZ2 . TRP   A 1 67  ? -14.737 -2.189  44.865  1.00 10.28 ? 90   TRP   A CZ2 1 
ATOM   375  C  CZ3 . TRP   A 1 67  ? -13.307 -0.876  46.315  1.00 10.95 ? 90   TRP   A CZ3 1 
ATOM   376  C  CH2 . TRP   A 1 67  ? -13.482 -1.873  45.334  1.00 10.54 ? 90   TRP   A CH2 1 
ATOM   377  N  N   . ASP   A 1 68  ? -17.802 2.511   50.297  1.00 11.00 ? 91   ASP   A N   1 
ATOM   378  C  CA  . ASP   A 1 68  ? -17.610 3.753   51.018  1.00 10.93 ? 91   ASP   A CA  1 
ATOM   379  C  C   . ASP   A 1 68  ? -16.564 4.571   50.279  1.00 10.74 ? 91   ASP   A C   1 
ATOM   380  O  O   . ASP   A 1 68  ? -15.745 4.044   49.511  1.00 10.42 ? 91   ASP   A O   1 
ATOM   381  C  CB  . ASP   A 1 68  ? -17.222 3.475   52.466  1.00 12.04 ? 91   ASP   A CB  1 
ATOM   382  C  CG  . ASP   A 1 68  ? -18.185 2.617   53.264  1.00 14.90 ? 91   ASP   A CG  1 
ATOM   383  O  OD1 . ASP   A 1 68  ? -19.321 2.490   52.847  1.00 14.30 ? 91   ASP   A OD1 1 
ATOM   384  O  OD2 . ASP   A 1 68  ? -17.725 2.024   54.273  1.00 16.39 ? 91   ASP   A OD2 1 
ATOM   385  N  N   . PHE   A 1 69  ? -16.664 5.894   50.440  1.00 10.65 ? 92   PHE   A N   1 
ATOM   386  C  CA  . PHE   A 1 69  ? -15.952 6.806   49.564  1.00 10.94 ? 92   PHE   A CA  1 
ATOM   387  C  C   . PHE   A 1 69  ? -15.515 8.074   50.290  1.00 12.86 ? 92   PHE   A C   1 
ATOM   388  O  O   . PHE   A 1 69  ? -16.213 8.570   51.176  1.00 13.00 ? 92   PHE   A O   1 
ATOM   389  C  CB  . PHE   A 1 69  ? -16.935 7.143   48.445  1.00 11.30 ? 92   PHE   A CB  1 
ATOM   390  C  CG  . PHE   A 1 69  ? -16.397 8.058   47.354  1.00 10.49 ? 92   PHE   A CG  1 
ATOM   391  C  CD1 . PHE   A 1 69  ? -15.431 7.619   46.460  1.00 11.38 ? 92   PHE   A CD1 1 
ATOM   392  C  CD2 . PHE   A 1 69  ? -16.834 9.368   47.250  1.00 10.88 ? 92   PHE   A CD2 1 
ATOM   393  C  CE1 . PHE   A 1 69  ? -14.994 8.445   45.439  1.00 11.10 ? 92   PHE   A CE1 1 
ATOM   394  C  CE2 . PHE   A 1 69  ? -16.364 10.189  46.242  1.00 11.13 ? 92   PHE   A CE2 1 
ATOM   395  C  CZ  . PHE   A 1 69  ? -15.460 9.721   45.347  1.00 11.89 ? 92   PHE   A CZ  1 
ATOM   396  N  N   . ALA   A 1 70  ? -14.399 8.637   49.815  1.00 12.48 ? 93   ALA   A N   1 
ATOM   397  C  CA  . ALA   A 1 70  ? -13.926 9.937   50.280  1.00 13.15 ? 93   ALA   A CA  1 
ATOM   398  C  C   . ALA   A 1 70  ? -13.180 10.625  49.156  1.00 12.92 ? 93   ALA   A C   1 
ATOM   399  O  O   . ALA   A 1 70  ? -12.561 9.951   48.323  1.00 13.23 ? 93   ALA   A O   1 
ATOM   400  C  CB  . ALA   A 1 70  ? -12.975 9.781   51.441  1.00 13.03 ? 93   ALA   A CB  1 
ATOM   401  N  N   . VAL   A 1 71  ? -13.173 11.961  49.210  1.00 12.84 ? 94   VAL   A N   1 
ATOM   402  C  CA  . VAL   A 1 71  ? -12.278 12.737  48.382  1.00 12.47 ? 94   VAL   A CA  1 
ATOM   403  C  C   . VAL   A 1 71  ? -11.318 13.465  49.306  1.00 13.84 ? 94   VAL   A C   1 
ATOM   404  O  O   . VAL   A 1 71  ? -11.765 14.266  50.130  1.00 13.32 ? 94   VAL   A O   1 
ATOM   405  C  CB  . VAL   A 1 71  ? -13.015 13.721  47.456  1.00 13.41 ? 94   VAL   A CB  1 
ATOM   406  C  CG1 . VAL   A 1 71  ? -12.065 14.510  46.580  1.00 14.02 ? 94   VAL   A CG1 1 
ATOM   407  C  CG2 . VAL   A 1 71  ? -14.048 13.017  46.584  1.00 13.20 ? 94   VAL   A CG2 1 
ATOM   408  N  N   . THR   A 1 72  ? -10.012 13.203  49.130  1.00 11.87 ? 95   THR   A N   1 
ATOM   409  C  CA  . THR   A 1 72  ? -8.995  13.927  49.869  1.00 12.00 ? 95   THR   A CA  1 
ATOM   410  C  C   . THR   A 1 72  ? -8.258  14.823  48.895  1.00 12.35 ? 95   THR   A C   1 
ATOM   411  O  O   . THR   A 1 72  ? -8.524  14.831  47.695  1.00 11.66 ? 95   THR   A O   1 
ATOM   412  C  CB  . THR   A 1 72  ? -8.058  12.941  50.571  1.00 11.68 ? 95   THR   A CB  1 
ATOM   413  O  OG1 . THR   A 1 72  ? -7.330  12.245  49.568  1.00 11.44 ? 95   THR   A OG1 1 
ATOM   414  C  CG2 . THR   A 1 72  ? -8.806  11.998  51.496  1.00 12.53 ? 95   THR   A CG2 1 
ATOM   415  N  N   . SER   A 1 73  ? -7.292  15.570  49.424  1.00 14.92 ? 96   SER   A N   1 
ATOM   416  C  CA  . SER   A 1 73  ? -6.256  16.145  48.593  1.00 14.20 ? 96   SER   A CA  1 
ATOM   417  C  C   . SER   A 1 73  ? -5.425  15.048  47.919  1.00 13.81 ? 96   SER   A C   1 
ATOM   418  O  O   . SER   A 1 73  ? -5.362  13.897  48.390  1.00 13.07 ? 96   SER   A O   1 
ATOM   419  C  CB  . SER   A 1 73  ? -5.390  17.114  49.373  1.00 17.36 ? 96   SER   A CB  1 
ATOM   420  O  OG  . SER   A 1 73  ? -4.524  16.442  50.272  1.00 17.68 ? 96   SER   A OG  1 
ATOM   421  N  N   . ALA   A 1 74  ? -4.731  15.464  46.848  1.00 13.45 ? 97   ALA   A N   1 
ATOM   422  C  CA  . ALA   A 1 74  ? -4.014  14.570  45.940  1.00 13.53 ? 97   ALA   A CA  1 
ATOM   423  C  C   . ALA   A 1 74  ? -2.969  13.756  46.687  1.00 15.29 ? 97   ALA   A C   1 
ATOM   424  O  O   . ALA   A 1 74  ? -2.759  12.592  46.349  1.00 13.88 ? 97   ALA   A O   1 
ATOM   425  C  CB  . ALA   A 1 74  ? -3.347  15.330  44.816  1.00 14.77 ? 97   ALA   A CB  1 
ATOM   426  N  N   . ASN   A 1 75  ? -2.264  14.381  47.648  1.00 14.55 ? 98   ASN   A N   1 
ATOM   427  C  CA  . ASN   A 1 75  ? -1.160  13.691  48.297  1.00 15.64 ? 98   ASN   A CA  1 
ATOM   428  C  C   . ASN   A 1 75  ? -1.535  13.209  49.701  1.00 14.02 ? 98   ASN   A C   1 
ATOM   429  O  O   . ASN   A 1 75  ? -0.671  12.750  50.449  1.00 13.57 ? 98   ASN   A O   1 
ATOM   430  C  CB  . ASN   A 1 75  ? 0.076   14.580  48.374  1.00 20.42 ? 98   ASN   A CB  1 
ATOM   431  C  CG  . ASN   A 1 75  ? 0.664   14.832  47.005  1.00 26.38 ? 98   ASN   A CG  1 
ATOM   432  O  OD1 . ASN   A 1 75  ? 0.907   15.987  46.647  1.00 32.01 ? 98   ASN   A OD1 1 
ATOM   433  N  ND2 . ASN   A 1 75  ? 0.921   13.786  46.237  1.00 29.45 ? 98   ASN   A ND2 1 
ATOM   434  N  N   . ALA   A 1 76  ? -2.831  13.189  50.013  1.00 12.45 ? 99   ALA   A N   1 
ATOM   435  C  CA  . ALA   A 1 76  ? -3.269  12.675  51.310  1.00 12.85 ? 99   ALA   A CA  1 
ATOM   436  C  C   . ALA   A 1 76  ? -3.071  11.174  51.357  1.00 14.74 ? 99   ALA   A C   1 
ATOM   437  O  O   . ALA   A 1 76  ? -3.219  10.500  50.341  1.00 14.61 ? 99   ALA   A O   1 
ATOM   438  C  CB  . ALA   A 1 76  ? -4.713  13.019  51.575  1.00 13.21 ? 99   ALA   A CB  1 
ATOM   439  N  N   . GLY   A 1 77  ? -2.793  10.643  52.559  1.00 13.26 ? 100  GLY   A N   1 
ATOM   440  C  CA  . GLY   A 1 77  ? -2.934  9.213   52.719  1.00 14.31 ? 100  GLY   A CA  1 
ATOM   441  C  C   . GLY   A 1 77  ? -4.380  8.839   53.028  1.00 12.29 ? 100  GLY   A C   1 
ATOM   442  O  O   . GLY   A 1 77  ? -5.309  9.664   52.973  1.00 11.49 ? 100  GLY   A O   1 
ATOM   443  N  N   . GLN   A 1 78  ? -4.551  7.566   53.403  1.00 10.78 ? 101  GLN   A N   1 
ATOM   444  C  CA  . GLN   A 1 78  ? -5.854  7.012   53.600  1.00 10.99 ? 101  GLN   A CA  1 
ATOM   445  C  C   . GLN   A 1 78  ? -6.603  7.807   54.670  1.00 12.58 ? 101  GLN   A C   1 
ATOM   446  O  O   . GLN   A 1 78  ? -6.090  8.022   55.774  1.00 13.52 ? 101  GLN   A O   1 
ATOM   447  C  CB  . GLN   A 1 78  ? -5.714  5.559   54.034  1.00 10.71 ? 101  GLN   A CB  1 
ATOM   448  C  CG  . GLN   A 1 78  ? -7.066  4.881   54.175  1.00 11.21 ? 101  GLN   A CG  1 
ATOM   449  C  CD  . GLN   A 1 78  ? -6.938  3.421   54.512  1.00 11.47 ? 101  GLN   A CD  1 
ATOM   450  O  OE1 . GLN   A 1 78  ? -6.157  2.692   53.894  1.00 13.66 ? 101  GLN   A OE1 1 
ATOM   451  N  NE2 . GLN   A 1 78  ? -7.674  2.984   55.525  1.00 13.48 ? 101  GLN   A NE2 1 
ATOM   452  N  N   . PRO   A 1 79  ? -7.848  8.250   54.424  1.00 12.97 ? 102  PRO   A N   1 
ATOM   453  C  CA  . PRO   A 1 79  ? -8.570  8.989   55.458  1.00 13.90 ? 102  PRO   A CA  1 
ATOM   454  C  C   . PRO   A 1 79  ? -8.995  8.079   56.604  1.00 13.99 ? 102  PRO   A C   1 
ATOM   455  O  O   . PRO   A 1 79  ? -9.239  6.898   56.417  1.00 13.10 ? 102  PRO   A O   1 
ATOM   456  C  CB  . PRO   A 1 79  ? -9.769  9.600   54.724  1.00 14.80 ? 102  PRO   A CB  1 
ATOM   457  C  CG  . PRO   A 1 79  ? -9.932  8.755   53.489  1.00 14.80 ? 102  PRO   A CG  1 
ATOM   458  C  CD  . PRO   A 1 79  ? -8.617  8.054   53.190  1.00 13.78 ? 102  PRO   A CD  1 
ATOM   459  N  N   . ALA   A 1 80  ? -9.068  8.654   57.811  1.00 14.25 ? 103  ALA   A N   1 
ATOM   460  C  CA  . ALA   A 1 80  ? -9.515  7.929   58.989  1.00 13.93 ? 103  ALA   A CA  1 
ATOM   461  C  C   . ALA   A 1 80  ? -10.998 7.588   58.886  1.00 15.00 ? 103  ALA   A C   1 
ATOM   462  O  O   . ALA   A 1 80  ? -11.430 6.558   59.384  1.00 13.79 ? 103  ALA   A O   1 
ATOM   463  C  CB  . ALA   A 1 80  ? -9.243  8.791   60.222  1.00 14.41 ? 103  ALA   A CB  1 
ATOM   464  N  N   . THR   A 1 81  ? -11.770 8.460   58.221  1.00 15.47 ? 104  THR   A N   1 
ATOM   465  C  CA  . THR   A 1 81  ? -13.196 8.270   58.007  1.00 18.64 ? 104  THR   A CA  1 
ATOM   466  C  C   . THR   A 1 81  ? -13.506 8.404   56.522  1.00 17.68 ? 104  THR   A C   1 
ATOM   467  O  O   . THR   A 1 81  ? -13.092 9.384   55.916  1.00 18.68 ? 104  THR   A O   1 
ATOM   468  C  CB  . THR   A 1 81  ? -14.034 9.333   58.725  1.00 21.42 ? 104  THR   A CB  1 
ATOM   469  O  OG1 . THR   A 1 81  ? -13.597 9.379   60.073  1.00 24.52 ? 104  THR   A OG1 1 
ATOM   470  C  CG2 . THR   A 1 81  ? -15.490 8.931   58.762  1.00 24.02 ? 104  THR   A CG2 1 
ATOM   471  N  N   . PHE   A 1 82  ? -14.310 7.473   56.007  1.00 15.49 ? 105  PHE   A N   1 
ATOM   472  C  CA  . PHE   A 1 82  ? -14.900 7.596   54.682  1.00 14.72 ? 105  PHE   A CA  1 
ATOM   473  C  C   . PHE   A 1 82  ? -16.304 8.184   54.865  1.00 15.55 ? 105  PHE   A C   1 
ATOM   474  O  O   . PHE   A 1 82  ? -17.226 7.507   55.295  1.00 17.65 ? 105  PHE   A O   1 
ATOM   475  C  CB  . PHE   A 1 82  ? -14.909 6.223   54.012  1.00 13.50 ? 105  PHE   A CB  1 
ATOM   476  C  CG  . PHE   A 1 82  ? -13.571 5.715   53.535  1.00 14.18 ? 105  PHE   A CG  1 
ATOM   477  C  CD1 . PHE   A 1 82  ? -12.574 5.361   54.446  1.00 14.39 ? 105  PHE   A CD1 1 
ATOM   478  C  CD2 . PHE   A 1 82  ? -13.300 5.565   52.173  1.00 13.37 ? 105  PHE   A CD2 1 
ATOM   479  C  CE1 . PHE   A 1 82  ? -11.356 4.873   54.011  1.00 14.30 ? 105  PHE   A CE1 1 
ATOM   480  C  CE2 . PHE   A 1 82  ? -12.076 5.085   51.757  1.00 13.24 ? 105  PHE   A CE2 1 
ATOM   481  C  CZ  . PHE   A 1 82  ? -11.102 4.755   52.668  1.00 14.48 ? 105  PHE   A CZ  1 
ATOM   482  N  N   . PRO   A 1 83  ? -16.540 9.466   54.564  1.00 15.30 ? 106  PRO   A N   1 
ATOM   483  C  CA  . PRO   A 1 83  ? -17.850 10.070  54.821  1.00 16.83 ? 106  PRO   A CA  1 
ATOM   484  C  C   . PRO   A 1 83  ? -19.012 9.856   53.860  1.00 16.23 ? 106  PRO   A C   1 
ATOM   485  O  O   . PRO   A 1 83  ? -20.149 10.233  54.159  1.00 15.72 ? 106  PRO   A O   1 
ATOM   486  C  CB  . PRO   A 1 83  ? -17.477 11.548  54.872  1.00 17.65 ? 106  PRO   A CB  1 
ATOM   487  C  CG  . PRO   A 1 83  ? -16.335 11.703  53.912  1.00 18.84 ? 106  PRO   A CG  1 
ATOM   488  C  CD  . PRO   A 1 83  ? -15.573 10.394  53.977  1.00 16.28 ? 106  PRO   A CD  1 
ATOM   489  N  N   . GLU   A 1 84  ? -18.752 9.193   52.740  1.00 13.85 ? 107  GLU   A N   1 
ATOM   490  C  CA  . GLU   A 1 84  ? -19.750 9.071   51.700  1.00 12.86 ? 107  GLU   A CA  1 
ATOM   491  C  C   . GLU   A 1 84  ? -19.776 7.642   51.177  1.00 12.04 ? 107  GLU   A C   1 
ATOM   492  O  O   . GLU   A 1 84  ? -19.001 6.790   51.628  1.00 10.83 ? 107  GLU   A O   1 
ATOM   493  C  CB  . GLU   A 1 84  ? -19.374 10.089  50.627  1.00 15.01 ? 107  GLU   A CB  1 
ATOM   494  C  CG  . GLU   A 1 84  ? -19.498 11.539  51.085  1.00 17.12 ? 107  GLU   A CG  1 
ATOM   495  C  CD  . GLU   A 1 84  ? -19.263 12.490  49.913  1.00 19.41 ? 107  GLU   A CD  1 
ATOM   496  O  OE1 . GLU   A 1 84  ? -18.108 12.653  49.475  1.00 19.55 ? 107  GLU   A OE1 1 
ATOM   497  O  OE2 . GLU   A 1 84  ? -20.271 13.038  49.430  1.00 21.94 ? 107  GLU   A OE2 1 
ATOM   498  N  N   . GLN   A 1 85  ? -20.671 7.398   50.206  1.00 10.70 ? 108  GLN   A N   1 
ATOM   499  C  CA  . GLN   A 1 85  ? -20.697 6.143   49.478  1.00 11.09 ? 108  GLN   A CA  1 
ATOM   500  C  C   . GLN   A 1 85  ? -20.811 6.440   47.977  1.00 10.73 ? 108  GLN   A C   1 
ATOM   501  O  O   . GLN   A 1 85  ? -21.434 7.427   47.592  1.00 10.34 ? 108  GLN   A O   1 
ATOM   502  C  CB  . GLN   A 1 85  ? -21.840 5.263   49.961  1.00 11.88 ? 108  GLN   A CB  1 
ATOM   503  C  CG  . GLN   A 1 85  ? -21.731 4.838   51.432  1.00 12.74 ? 108  GLN   A CG  1 
ATOM   504  C  CD  . GLN   A 1 85  ? -22.706 3.735   51.794  1.00 13.11 ? 108  GLN   A CD  1 
ATOM   505  O  OE1 . GLN   A 1 85  ? -23.910 3.796   51.528  1.00 11.25 ? 108  GLN   A OE1 1 
ATOM   506  N  NE2 . GLN   A 1 85  ? -22.191 2.661   52.387  1.00 14.28 ? 108  GLN   A NE2 1 
ATOM   507  N  N   . ILE   A 1 86  ? -20.227 5.550   47.171  1.00 9.41  ? 109  ILE   A N   1 
ATOM   508  C  CA  . ILE   A 1 86  ? -20.275 5.642   45.725  1.00 9.27  ? 109  ILE   A CA  1 
ATOM   509  C  C   . ILE   A 1 86  ? -20.684 4.298   45.134  1.00 9.51  ? 109  ILE   A C   1 
ATOM   510  O  O   . ILE   A 1 86  ? -20.427 3.246   45.712  1.00 9.86  ? 109  ILE   A O   1 
ATOM   511  C  CB  . ILE   A 1 86  ? -18.907 6.122   45.218  1.00 9.04  ? 109  ILE   A CB  1 
ATOM   512  C  CG1 . ILE   A 1 86  ? -18.961 6.618   43.770  1.00 8.78  ? 109  ILE   A CG1 1 
ATOM   513  C  CG2 . ILE   A 1 86  ? -17.840 5.029   45.414  1.00 9.28  ? 109  ILE   A CG2 1 
ATOM   514  C  CD1 . ILE   A 1 86  ? -17.691 7.296   43.288  1.00 9.13  ? 109  ILE   A CD1 1 
ATOM   515  N  N   . ARG   A 1 87  ? -21.281 4.350   43.926  1.00 9.29  ? 110  ARG   A N   1 
ATOM   516  C  CA  . ARG   A 1 87  ? -21.633 3.135   43.210  1.00 9.48  ? 110  ARG   A CA  1 
ATOM   517  C  C   . ARG   A 1 87  ? -20.583 2.833   42.141  1.00 8.79  ? 110  ARG   A C   1 
ATOM   518  O  O   . ARG   A 1 87  ? -20.524 3.471   41.101  1.00 8.54  ? 110  ARG   A O   1 
ATOM   519  C  CB  . ARG   A 1 87  ? -23.037 3.191   42.603  1.00 8.92  ? 110  ARG   A CB  1 
ATOM   520  C  CG  . ARG   A 1 87  ? -23.435 1.911   41.887  1.00 9.15  ? 110  ARG   A CG  1 
ATOM   521  C  CD  . ARG   A 1 87  ? -24.912 1.860   41.714  1.00 9.46  ? 110  ARG   A CD  1 
ATOM   522  N  NE  . ARG   A 1 87  ? -25.400 2.959   40.868  1.00 9.94  ? 110  ARG   A NE  1 
ATOM   523  C  CZ  . ARG   A 1 87  ? -26.656 3.145   40.504  1.00 9.78  ? 110  ARG   A CZ  1 
ATOM   524  N  NH1 . ARG   A 1 87  ? -27.555 2.161   40.653  1.00 9.61  ? 110  ARG   A NH1 1 
ATOM   525  N  NH2 . ARG   A 1 87  ? -27.000 4.303   39.963  1.00 9.34  ? 110  ARG   A NH2 1 
ATOM   526  N  N   . VAL   A 1 88  ? -19.746 1.857   42.444  1.00 8.78  ? 111  VAL   A N   1 
ATOM   527  C  CA  . VAL   A 1 88  ? -18.739 1.317   41.548  1.00 9.01  ? 111  VAL   A CA  1 
ATOM   528  C  C   . VAL   A 1 88  ? -19.461 0.452   40.505  1.00 8.58  ? 111  VAL   A C   1 
ATOM   529  O  O   . VAL   A 1 88  ? -20.266 -0.389  40.870  1.00 7.89  ? 111  VAL   A O   1 
ATOM   530  C  CB  . VAL   A 1 88  ? -17.685 0.494   42.328  1.00 10.00 ? 111  VAL   A CB  1 
ATOM   531  C  CG1 . VAL   A 1 88  ? -16.811 -0.396  41.437  1.00 9.98  ? 111  VAL   A CG1 1 
ATOM   532  C  CG2 . VAL   A 1 88  ? -16.822 1.407   43.181  1.00 10.77 ? 111  VAL   A CG2 1 
ATOM   533  N  N   . PRO   A 1 89  ? -19.149 0.527   39.184  1.00 8.82  ? 112  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 89  ? -17.992 1.260   38.662  1.00 8.66  ? 112  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 89  ? -18.331 2.508   37.852  1.00 8.57  ? 112  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 89  ? -18.036 2.569   36.652  1.00 8.41  ? 112  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 89  ? -17.396 0.152   37.768  1.00 8.83  ? 112  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 89  ? -18.630 -0.480  37.127  1.00 8.42  ? 112  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 89  ? -19.766 -0.296  38.145  1.00 8.47  ? 112  PRO   A CD  1 
ATOM   540  N  N   . PHE   A 1 90  ? -18.969 3.494   38.502  1.00 8.05  ? 113  PHE   A N   1 
ATOM   541  C  CA  . PHE   A 1 90  ? -19.261 4.757   37.838  1.00 8.64  ? 113  PHE   A CA  1 
ATOM   542  C  C   . PHE   A 1 90  ? -18.393 5.881   38.397  1.00 9.26  ? 113  PHE   A C   1 
ATOM   543  O  O   . PHE   A 1 90  ? -18.257 6.021   39.623  1.00 9.99  ? 113  PHE   A O   1 
ATOM   544  C  CB  . PHE   A 1 90  ? -20.740 5.057   38.034  1.00 8.38  ? 113  PHE   A CB  1 
ATOM   545  C  CG  . PHE   A 1 90  ? -21.656 4.042   37.365  1.00 8.58  ? 113  PHE   A CG  1 
ATOM   546  C  CD1 . PHE   A 1 90  ? -21.836 4.042   35.986  1.00 8.42  ? 113  PHE   A CD1 1 
ATOM   547  C  CD2 . PHE   A 1 90  ? -22.295 3.059   38.115  1.00 8.68  ? 113  PHE   A CD2 1 
ATOM   548  C  CE1 . PHE   A 1 90  ? -22.660 3.089   35.378  1.00 9.02  ? 113  PHE   A CE1 1 
ATOM   549  C  CE2 . PHE   A 1 90  ? -23.082 2.094   37.500  1.00 8.84  ? 113  PHE   A CE2 1 
ATOM   550  C  CZ  . PHE   A 1 90  ? -23.262 2.113   36.137  1.00 8.94  ? 113  PHE   A CZ  1 
ATOM   551  N  N   . VAL   A 1 91  ? -17.811 6.675   37.492  1.00 8.56  ? 114  VAL   A N   1 
ATOM   552  C  CA  . VAL   A 1 91  ? -16.857 7.679   37.934  1.00 8.91  ? 114  VAL   A CA  1 
ATOM   553  C  C   . VAL   A 1 91  ? -17.571 8.703   38.796  1.00 8.88  ? 114  VAL   A C   1 
ATOM   554  O  O   . VAL   A 1 91  ? -18.786 8.899   38.712  1.00 7.59  ? 114  VAL   A O   1 
ATOM   555  C  CB  . VAL   A 1 91  ? -16.142 8.374   36.766  1.00 8.29  ? 114  VAL   A CB  1 
ATOM   556  C  CG1 . VAL   A 1 91  ? -15.281 7.371   36.008  1.00 8.51  ? 114  VAL   A CG1 1 
ATOM   557  C  CG2 . VAL   A 1 91  ? -17.101 9.117   35.832  1.00 8.49  ? 114  VAL   A CG2 1 
ATOM   558  N  N   . ALA   A 1 92  ? -16.770 9.438   39.564  1.00 9.42  ? 115  ALA   A N   1 
ATOM   559  C  CA  . ALA   A 1 92  ? -17.312 10.412  40.505  1.00 9.27  ? 115  ALA   A CA  1 
ATOM   560  C  C   . ALA   A 1 92  ? -18.078 11.554  39.821  1.00 9.19  ? 115  ALA   A C   1 
ATOM   561  O  O   . ALA   A 1 92  ? -19.005 12.119  40.398  1.00 8.22  ? 115  ALA   A O   1 
ATOM   562  C  CB  . ALA   A 1 92  ? -16.182 10.955  41.359  1.00 10.10 ? 115  ALA   A CB  1 
ATOM   563  N  N   . GLU   A 1 93  ? -17.767 11.837  38.551  1.00 9.09  ? 116  GLU   A N   1 
ATOM   564  C  CA  . GLU   A 1 93  ? -18.393 12.928  37.820  1.00 8.84  ? 116  GLU   A CA  1 
ATOM   565  C  C   . GLU   A 1 93  ? -19.789 12.559  37.360  1.00 8.91  ? 116  GLU   A C   1 
ATOM   566  O  O   . GLU   A 1 93  ? -20.593 13.440  37.054  1.00 9.69  ? 116  GLU   A O   1 
ATOM   567  C  CB  . GLU   A 1 93  ? -17.603 13.330  36.579  1.00 8.49  ? 116  GLU   A CB  1 
ATOM   568  C  CG  . GLU   A 1 93  ? -16.233 13.928  36.876  1.00 8.09  ? 116  GLU   A CG  1 
ATOM   569  C  CD  . GLU   A 1 93  ? -15.051 12.994  37.035  1.00 8.03  ? 116  GLU   A CD  1 
ATOM   570  O  OE1 . GLU   A 1 93  ? -15.274 11.754  37.226  1.00 7.77  ? 116  GLU   A OE1 1 
ATOM   571  O  OE2 . GLU   A 1 93  ? -13.914 13.514  36.951  1.00 9.10  ? 116  GLU   A OE2 1 
ATOM   572  N  N   . SER   A 1 94  ? -20.104 11.259  37.356  1.00 8.16  ? 117  SER   A N   1 
ATOM   573  C  CA  . SER   A 1 94  ? -21.362 10.775  36.840  1.00 8.63  ? 117  SER   A CA  1 
ATOM   574  C  C   . SER   A 1 94  ? -22.487 10.837  37.873  1.00 8.67  ? 117  SER   A C   1 
ATOM   575  O  O   . SER   A 1 94  ? -22.272 10.635  39.078  1.00 7.65  ? 117  SER   A O   1 
ATOM   576  C  CB  . SER   A 1 94  ? -21.191 9.348   36.340  1.00 8.63  ? 117  SER   A CB  1 
ATOM   577  O  OG  . SER   A 1 94  ? -21.133 8.422   37.410  1.00 8.59  ? 117  SER   A OG  1 
ATOM   578  N  N   . ALA   A 1 95  ? -23.706 10.977  37.341  1.00 9.09  ? 118  ALA   A N   1 
ATOM   579  C  CA  . ALA   A 1 95  ? -24.892 10.856  38.171  1.00 9.58  ? 118  ALA   A CA  1 
ATOM   580  C  C   . ALA   A 1 95  ? -25.038 9.426   38.692  1.00 9.45  ? 118  ALA   A C   1 
ATOM   581  O  O   . ALA   A 1 95  ? -25.388 9.220   39.855  1.00 10.08 ? 118  ALA   A O   1 
ATOM   582  C  CB  . ALA   A 1 95  ? -26.111 11.298  37.433  1.00 10.41 ? 118  ALA   A CB  1 
ATOM   583  N  N   . LEU   A 1 96  ? -24.722 8.409   37.875  1.00 9.66  ? 119  LEU   A N   1 
ATOM   584  C  CA  . LEU   A 1 96  ? -24.943 7.027   38.290  1.00 9.75  ? 119  LEU   A CA  1 
ATOM   585  C  C   . LEU   A 1 96  ? -24.107 6.632   39.502  1.00 10.71 ? 119  LEU   A C   1 
ATOM   586  O  O   . LEU   A 1 96  ? -24.498 5.691   40.201  1.00 11.77 ? 119  LEU   A O   1 
ATOM   587  C  CB  . LEU   A 1 96  ? -24.785 6.048   37.123  1.00 10.42 ? 119  LEU   A CB  1 
ATOM   588  C  CG  . LEU   A 1 96  ? -25.848 6.198   36.035  1.00 10.10 ? 119  LEU   A CG  1 
ATOM   589  C  CD1 . LEU   A 1 96  ? -25.494 5.359   34.822  1.00 10.39 ? 119  LEU   A CD1 1 
ATOM   590  C  CD2 . LEU   A 1 96  ? -27.194 5.777   36.604  1.00 10.88 ? 119  LEU   A CD2 1 
ATOM   591  N  N   . SER   A 1 97  ? -23.000 7.335   39.768  1.00 9.66  ? 120  SER   A N   1 
ATOM   592  C  CA  . SER   A 1 97  ? -22.121 7.033   40.892  1.00 9.98  ? 120  SER   A CA  1 
ATOM   593  C  C   . SER   A 1 97  ? -22.820 7.355   42.217  1.00 10.29 ? 120  SER   A C   1 
ATOM   594  O  O   . SER   A 1 97  ? -22.442 6.847   43.270  1.00 10.11 ? 120  SER   A O   1 
ATOM   595  C  CB  . SER   A 1 97  ? -20.865 7.854   40.787  1.00 9.77  ? 120  SER   A CB  1 
ATOM   596  O  OG  . SER   A 1 97  ? -21.139 9.246   40.965  1.00 8.84  ? 120  SER   A OG  1 
ATOM   597  N  N   . GLY   A 1 98  ? -23.812 8.259   42.160  1.00 9.76  ? 121  GLY   A N   1 
ATOM   598  C  CA  . GLY   A 1 98  ? -24.410 8.797   43.383  1.00 10.19 ? 121  GLY   A CA  1 
ATOM   599  C  C   . GLY   A 1 98  ? -23.601 9.956   43.977  1.00 10.55 ? 121  GLY   A C   1 
ATOM   600  O  O   . GLY   A 1 98  ? -23.954 10.464  45.027  1.00 9.95  ? 121  GLY   A O   1 
ATOM   601  N  N   . ILE   A 1 99  ? -22.523 10.375  43.313  1.00 10.46 ? 122  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 99  ? -21.664 11.443  43.792  1.00 10.79 ? 122  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 99  ? -21.830 12.660  42.888  1.00 10.69 ? 122  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 99  ? -22.265 13.730  43.334  1.00 10.32 ? 122  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 99  ? -20.220 10.933  43.920  1.00 10.97 ? 122  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 99  ? -20.144 9.861   44.997  1.00 11.52 ? 122  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 99  ? -19.232 12.066  44.190  1.00 11.06 ? 122  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 99  ? -20.348 10.394  46.407  1.00 12.57 ? 122  ILE   A CD1 1 
ATOM   609  N  N   . GLN   A 1 100 ? -21.462 12.520  41.622  1.00 11.03 ? 123  GLN   A N   1 
ATOM   610  C  CA  . GLN   A 1 100 ? -21.672 13.573  40.633  1.00 11.61 ? 123  GLN   A CA  1 
ATOM   611  C  C   . GLN   A 1 100 ? -20.967 14.882  40.992  1.00 12.17 ? 123  GLN   A C   1 
ATOM   612  O  O   . GLN   A 1 100 ? -21.611 15.923  41.226  1.00 12.14 ? 123  GLN   A O   1 
ATOM   613  C  CB  . GLN   A 1 100 ? -23.154 13.821  40.394  1.00 13.05 ? 123  GLN   A CB  1 
ATOM   614  C  CG  . GLN   A 1 100 ? -23.364 14.466  39.033  1.00 15.40 ? 123  GLN   A CG  1 
ATOM   615  C  CD  . GLN   A 1 100 ? -24.760 14.948  38.781  1.00 18.03 ? 123  GLN   A CD  1 
ATOM   616  O  OE1 . GLN   A 1 100 ? -25.568 15.118  39.701  1.00 18.71 ? 123  GLN   A OE1 1 
ATOM   617  N  NE2 . GLN   A 1 100 ? -25.035 15.131  37.497  1.00 20.76 ? 123  GLN   A NE2 1 
ATOM   618  N  N   . ARG   A 1 101 ? -19.645 14.807  41.107  1.00 12.42 ? 124  ARG   A N   1 
ATOM   619  C  CA  . ARG   A 1 101 ? -18.836 15.961  41.462  1.00 15.03 ? 124  ARG   A CA  1 
ATOM   620  C  C   . ARG   A 1 101 ? -17.626 16.077  40.550  1.00 13.04 ? 124  ARG   A C   1 
ATOM   621  O  O   . ARG   A 1 101 ? -17.042 15.087  40.151  1.00 10.51 ? 124  ARG   A O   1 
ATOM   622  C  CB  . ARG   A 1 101 ? -18.356 15.894  42.918  1.00 18.37 ? 124  ARG   A CB  1 
ATOM   623  C  CG  . ARG   A 1 101 ? -19.522 16.172  43.850  1.00 22.08 ? 124  ARG   A CG  1 
ATOM   624  C  CD  . ARG   A 1 101 ? -19.171 16.593  45.259  1.00 24.43 ? 124  ARG   A CD  1 
ATOM   625  N  NE  . ARG   A 1 101 ? -18.154 15.713  45.834  1.00 22.29 ? 124  ARG   A NE  1 
ATOM   626  C  CZ  . ARG   A 1 101 ? -18.391 14.839  46.806  1.00 20.40 ? 124  ARG   A CZ  1 
ATOM   627  N  NH1 . ARG   A 1 101 ? -19.626 14.544  47.158  1.00 20.06 ? 124  ARG   A NH1 1 
ATOM   628  N  NH2 . ARG   A 1 101 ? -17.379 14.269  47.428  1.00 18.22 ? 124  ARG   A NH2 1 
ATOM   629  N  N   . LYS   A 1 102 ? -17.237 17.327  40.294  1.00 12.80 ? 125  LYS   A N   1 
ATOM   630  C  CA  . LYS   A 1 102 ? -16.034 17.669  39.582  1.00 12.07 ? 125  LYS   A CA  1 
ATOM   631  C  C   . LYS   A 1 102 ? -14.830 17.275  40.434  1.00 11.62 ? 125  LYS   A C   1 
ATOM   632  O  O   . LYS   A 1 102 ? -14.818 17.590  41.628  1.00 11.11 ? 125  LYS   A O   1 
ATOM   633  C  CB  . LYS   A 1 102 ? -15.981 19.187  39.350  1.00 12.18 ? 125  LYS   A CB  1 
ATOM   634  C  CG  . LYS   A 1 102 ? -14.754 19.627  38.605  1.00 13.21 ? 125  LYS   A CG  1 
ATOM   635  C  CD  . LYS   A 1 102 ? -14.720 21.108  38.250  1.00 14.28 ? 125  LYS   A CD  1 
ATOM   636  C  CE  . LYS   A 1 102 ? -14.651 21.999  39.436  1.00 16.39 ? 125  LYS   A CE  1 
ATOM   637  N  NZ  . LYS   A 1 102 ? -14.916 23.356  38.954  1.00 17.08 ? 125  LYS   A NZ  1 
ATOM   638  N  N   . ILE   A 1 103 ? -13.881 16.583  39.804  1.00 10.99 ? 126  ILE   A N   1 
ATOM   639  C  CA  . ILE   A 1 103 ? -12.658 16.081  40.420  1.00 10.99 ? 126  ILE   A CA  1 
ATOM   640  C  C   . ILE   A 1 103 ? -11.465 16.717  39.710  1.00 11.01 ? 126  ILE   A C   1 
ATOM   641  O  O   . ILE   A 1 103 ? -11.363 16.627  38.487  1.00 11.63 ? 126  ILE   A O   1 
ATOM   642  C  CB  . ILE   A 1 103 ? -12.599 14.543  40.337  1.00 10.86 ? 126  ILE   A CB  1 
ATOM   643  C  CG1 . ILE   A 1 103 ? -13.792 13.823  40.951  1.00 10.52 ? 126  ILE   A CG1 1 
ATOM   644  C  CG2 . ILE   A 1 103 ? -11.269 14.057  40.899  1.00 10.84 ? 126  ILE   A CG2 1 
ATOM   645  C  CD1 . ILE   A 1 103 ? -14.058 14.169  42.394  1.00 12.37 ? 126  ILE   A CD1 1 
ATOM   646  N  N   . THR   A 1 104 ? -10.558 17.372  40.456  1.00 12.05 ? 127  THR   A N   1 
ATOM   647  C  CA  . THR   A 1 104 ? -9.425  18.072  39.882  1.00 11.81 ? 127  THR   A CA  1 
ATOM   648  C  C   . THR   A 1 104 ? -8.162  17.288  40.185  1.00 11.42 ? 127  THR   A C   1 
ATOM   649  O  O   . THR   A 1 104 ? -8.186  16.329  40.959  1.00 12.11 ? 127  THR   A O   1 
ATOM   650  C  CB  . THR   A 1 104 ? -9.315  19.488  40.462  1.00 12.29 ? 127  THR   A CB  1 
ATOM   651  O  OG1 . THR   A 1 104 ? -8.792  19.369  41.792  1.00 12.45 ? 127  THR   A OG1 1 
ATOM   652  C  CG2 . THR   A 1 104 ? -10.647 20.202  40.453  1.00 13.46 ? 127  THR   A CG2 1 
ATOM   653  N  N   . GLN   A 1 105 ? -7.051  17.813  39.679  1.00 11.04 ? 128  GLN   A N   1 
ATOM   654  C  CA  . GLN   A 1 105 ? -5.734  17.236  39.904  1.00 12.07 ? 128  GLN   A CA  1 
ATOM   655  C  C   . GLN   A 1 105 ? -5.282  17.393  41.356  1.00 10.61 ? 128  GLN   A C   1 
ATOM   656  O  O   . GLN   A 1 105 ? -4.308  16.778  41.747  1.00 11.75 ? 128  GLN   A O   1 
ATOM   657  C  CB  . GLN   A 1 105 ? -4.673  17.849  39.003  1.00 13.17 ? 128  GLN   A CB  1 
ATOM   658  C  CG  . GLN   A 1 105 ? -4.323  19.295  39.351  1.00 13.64 ? 128  GLN   A CG  1 
ATOM   659  C  CD  . GLN   A 1 105 ? -5.261  20.331  38.775  1.00 13.80 ? 128  GLN   A CD  1 
ATOM   660  O  OE1 . GLN   A 1 105 ? -6.423  20.089  38.462  1.00 13.81 ? 128  GLN   A OE1 1 
ATOM   661  N  NE2 . GLN   A 1 105 ? -4.765  21.556  38.706  1.00 15.98 ? 128  GLN   A NE2 1 
ATOM   662  N  N   . ASN   A 1 106 ? -5.943  18.252  42.125  1.00 11.04 ? 129  ASN   A N   1 
ATOM   663  C  CA  . ASN   A 1 106 ? -5.573  18.511  43.516  1.00 12.28 ? 129  ASN   A CA  1 
ATOM   664  C  C   . ASN   A 1 106 ? -6.350  17.597  44.466  1.00 12.39 ? 129  ASN   A C   1 
ATOM   665  O  O   . ASN   A 1 106 ? -6.179  17.691  45.692  1.00 12.42 ? 129  ASN   A O   1 
ATOM   666  C  CB  . ASN   A 1 106 ? -5.824  19.963  43.897  1.00 14.08 ? 129  ASN   A CB  1 
ATOM   667  C  CG  . ASN   A 1 106 ? -4.926  20.904  43.134  1.00 16.83 ? 129  ASN   A CG  1 
ATOM   668  O  OD1 . ASN   A 1 106 ? -3.738  20.627  42.975  1.00 22.72 ? 129  ASN   A OD1 1 
ATOM   669  N  ND2 . ASN   A 1 106 ? -5.475  21.967  42.573  1.00 21.30 ? 129  ASN   A ND2 1 
ATOM   670  N  N   . ASP   A 1 107 ? -7.211  16.749  43.890  1.00 11.10 ? 130  ASP   A N   1 
ATOM   671  C  CA  . ASP   A 1 107 ? -8.044  15.799  44.609  1.00 12.20 ? 130  ASP   A CA  1 
ATOM   672  C  C   . ASP   A 1 107 ? -7.490  14.379  44.463  1.00 11.38 ? 130  ASP   A C   1 
ATOM   673  O  O   . ASP   A 1 107 ? -6.667  14.119  43.589  1.00 11.34 ? 130  ASP   A O   1 
ATOM   674  C  CB  . ASP   A 1 107 ? -9.451  15.822  44.039  1.00 11.98 ? 130  ASP   A CB  1 
ATOM   675  C  CG  . ASP   A 1 107 ? -10.147 17.169  44.132  1.00 14.43 ? 130  ASP   A CG  1 
ATOM   676  O  OD1 . ASP   A 1 107 ? -9.863  17.883  45.107  1.00 14.21 ? 130  ASP   A OD1 1 
ATOM   677  O  OD2 . ASP   A 1 107 ? -10.935 17.490  43.213  1.00 13.67 ? 130  ASP   A OD2 1 
ATOM   678  N  N   . LYS   A 1 108 ? -7.954  13.471  45.325  1.00 10.82 ? 131  LYS   A N   1 
ATOM   679  C  CA  . LYS   A 1 108 ? -7.724  12.043  45.146  1.00 10.67 ? 131  LYS   A CA  1 
ATOM   680  C  C   . LYS   A 1 108 ? -8.956  11.306  45.652  1.00 10.23 ? 131  LYS   A C   1 
ATOM   681  O  O   . LYS   A 1 108 ? -9.540  11.681  46.672  1.00 10.34 ? 131  LYS   A O   1 
ATOM   682  C  CB  . LYS   A 1 108 ? -6.454  11.553  45.863  1.00 10.75 ? 131  LYS   A CB  1 
ATOM   683  C  CG  . LYS   A 1 108 ? -6.120  10.076  45.694  1.00 10.96 ? 131  LYS   A CG  1 
ATOM   684  C  CD  . LYS   A 1 108 ? -4.668  9.754   46.041  1.00 12.22 ? 131  LYS   A CD  1 
ATOM   685  C  CE  . LYS   A 1 108 ? -4.352  9.932   47.481  1.00 12.56 ? 131  LYS   A CE  1 
ATOM   686  N  NZ  . LYS   A 1 108 ? -2.909  9.807   47.674  1.00 13.11 ? 131  LYS   A NZ  1 
ATOM   687  N  N   . LEU   A 1 109 ? -9.353  10.258  44.915  1.00 9.10  ? 132  LEU   A N   1 
ATOM   688  C  CA  . LEU   A 1 109 ? -10.502 9.467   45.274  1.00 9.45  ? 132  LEU   A CA  1 
ATOM   689  C  C   . LEU   A 1 109 ? -10.068 8.294   46.148  1.00 9.59  ? 132  LEU   A C   1 
ATOM   690  O  O   . LEU   A 1 109 ? -9.042  7.682   45.849  1.00 9.48  ? 132  LEU   A O   1 
ATOM   691  C  CB  . LEU   A 1 109 ? -11.158 8.988   43.981  1.00 10.11 ? 132  LEU   A CB  1 
ATOM   692  C  CG  . LEU   A 1 109 ? -11.490 10.066  42.940  1.00 11.32 ? 132  LEU   A CG  1 
ATOM   693  C  CD1 . LEU   A 1 109 ? -12.224 9.386   41.792  1.00 12.59 ? 132  LEU   A CD1 1 
ATOM   694  C  CD2 . LEU   A 1 109 ? -12.291 11.246  43.497  1.00 12.55 ? 132  LEU   A CD2 1 
ATOM   695  N  N   . TRP   A 1 110 ? -10.840 8.044   47.223  1.00 9.48  ? 133  TRP   A N   1 
ATOM   696  C  CA  . TRP   A 1 110 ? -10.675 6.896   48.099  1.00 9.50  ? 133  TRP   A CA  1 
ATOM   697  C  C   . TRP   A 1 110 ? -11.935 6.036   48.133  1.00 9.32  ? 133  TRP   A C   1 
ATOM   698  O  O   . TRP   A 1 110 ? -13.045 6.505   48.399  1.00 8.41  ? 133  TRP   A O   1 
ATOM   699  C  CB  . TRP   A 1 110 ? -10.291 7.317   49.524  1.00 8.95  ? 133  TRP   A CB  1 
ATOM   700  C  CG  . TRP   A 1 110 ? -8.900  7.881   49.617  1.00 9.31  ? 133  TRP   A CG  1 
ATOM   701  C  CD1 . TRP   A 1 110 ? -8.515  9.165   49.406  1.00 9.98  ? 133  TRP   A CD1 1 
ATOM   702  C  CD2 . TRP   A 1 110 ? -7.694  7.146   49.859  1.00 9.59  ? 133  TRP   A CD2 1 
ATOM   703  N  NE1 . TRP   A 1 110 ? -7.166  9.295   49.564  1.00 10.27 ? 133  TRP   A NE1 1 
ATOM   704  C  CE2 . TRP   A 1 110 ? -6.627  8.068   49.845  1.00 10.00 ? 133  TRP   A CE2 1 
ATOM   705  C  CE3 . TRP   A 1 110 ? -7.417  5.809   50.136  1.00 10.30 ? 133  TRP   A CE3 1 
ATOM   706  C  CZ2 . TRP   A 1 110 ? -5.300  7.694   50.049  1.00 10.65 ? 133  TRP   A CZ2 1 
ATOM   707  C  CZ3 . TRP   A 1 110 ? -6.101  5.428   50.294  1.00 10.52 ? 133  TRP   A CZ3 1 
ATOM   708  C  CH2 . TRP   A 1 110 ? -5.070  6.365   50.313  1.00 10.83 ? 133  TRP   A CH2 1 
ATOM   709  N  N   . TYR   A 1 111 ? -11.712 4.754   47.857  1.00 8.82  ? 134  TYR   A N   1 
ATOM   710  C  CA  . TYR   A 1 111 ? -12.764 3.756   47.879  1.00 8.64  ? 134  TYR   A CA  1 
ATOM   711  C  C   . TYR   A 1 111 ? -12.430 2.678   48.895  1.00 9.03  ? 134  TYR   A C   1 
ATOM   712  O  O   . TYR   A 1 111 ? -11.274 2.279   49.031  1.00 8.83  ? 134  TYR   A O   1 
ATOM   713  C  CB  . TYR   A 1 111 ? -12.821 3.070   46.521  1.00 9.48  ? 134  TYR   A CB  1 
ATOM   714  C  CG  . TYR   A 1 111 ? -13.184 3.859   45.284  1.00 8.55  ? 134  TYR   A CG  1 
ATOM   715  C  CD1 . TYR   A 1 111 ? -12.201 4.498   44.552  1.00 8.68  ? 134  TYR   A CD1 1 
ATOM   716  C  CD2 . TYR   A 1 111 ? -14.460 3.798   44.748  1.00 9.04  ? 134  TYR   A CD2 1 
ATOM   717  C  CE1 . TYR   A 1 111 ? -12.509 5.194   43.398  1.00 8.75  ? 134  TYR   A CE1 1 
ATOM   718  C  CE2 . TYR   A 1 111 ? -14.782 4.444   43.567  1.00 9.38  ? 134  TYR   A CE2 1 
ATOM   719  C  CZ  . TYR   A 1 111 ? -13.796 5.143   42.881  1.00 9.30  ? 134  TYR   A CZ  1 
ATOM   720  O  OH  . TYR   A 1 111 ? -14.104 5.724   41.665  1.00 9.94  ? 134  TYR   A OH  1 
ATOM   721  N  N   . LYS   A 1 112 ? -13.455 2.203   49.580  1.00 9.87  ? 135  LYS   A N   1 
ATOM   722  C  CA  . LYS   A 1 112 ? -13.305 1.125   50.546  1.00 10.91 ? 135  LYS   A CA  1 
ATOM   723  C  C   . LYS   A 1 112 ? -14.547 0.249   50.536  1.00 9.60  ? 135  LYS   A C   1 
ATOM   724  O  O   . LYS   A 1 112 ? -15.676 0.729   50.590  1.00 9.86  ? 135  LYS   A O   1 
ATOM   725  C  CB  . LYS   A 1 112 ? -13.112 1.631   51.973  1.00 12.36 ? 135  LYS   A CB  1 
ATOM   726  C  CG  . LYS   A 1 112 ? -13.038 0.505   53.001  1.00 14.64 ? 135  LYS   A CG  1 
ATOM   727  C  CD  . LYS   A 1 112 ? -12.738 1.017   54.399  1.00 18.65 ? 135  LYS   A CD  1 
ATOM   728  C  CE  . LYS   A 1 112 ? -13.792 1.969   54.849  1.00 23.27 ? 135  LYS   A CE  1 
ATOM   729  N  NZ  . LYS   A 1 112 ? -13.945 2.068   56.312  1.00 27.54 ? 135  LYS   A NZ  1 
ATOM   730  N  N   . ARG   A 1 113 ? -14.324 -1.072  50.495  1.00 10.41 ? 136  ARG   A N   1 
ATOM   731  C  CA  . ARG   A 1 113 ? -15.406 -2.002  50.764  1.00 10.96 ? 136  ARG   A CA  1 
ATOM   732  C  C   . ARG   A 1 113 ? -14.884 -3.269  51.439  1.00 11.82 ? 136  ARG   A C   1 
ATOM   733  O  O   . ARG   A 1 113 ? -13.695 -3.590  51.374  1.00 10.84 ? 136  ARG   A O   1 
ATOM   734  C  CB  . ARG   A 1 113 ? -16.190 -2.410  49.517  1.00 11.39 ? 136  ARG   A CB  1 
ATOM   735  C  CG  . ARG   A 1 113 ? -15.452 -3.319  48.549  1.00 11.50 ? 136  ARG   A CG  1 
ATOM   736  C  CD  . ARG   A 1 113 ? -16.394 -3.949  47.557  1.00 13.32 ? 136  ARG   A CD  1 
ATOM   737  N  NE  . ARG   A 1 113 ? -17.168 -4.973  48.265  1.00 15.53 ? 136  ARG   A NE  1 
ATOM   738  C  CZ  . ARG   A 1 113 ? -18.298 -5.501  47.821  1.00 19.34 ? 136  ARG   A CZ  1 
ATOM   739  N  NH1 . ARG   A 1 113 ? -18.787 -5.172  46.639  1.00 17.93 ? 136  ARG   A NH1 1 
ATOM   740  N  NH2 . ARG   A 1 113 ? -18.946 -6.366  48.580  1.00 22.09 ? 136  ARG   A NH2 1 
ATOM   741  N  N   . THR   A 1 114 ? -15.805 -3.933  52.137  1.00 13.50 ? 137  THR   A N   1 
ATOM   742  C  CA  . THR   A 1 114 ? -15.527 -5.235  52.711  1.00 13.75 ? 137  THR   A CA  1 
ATOM   743  C  C   . THR   A 1 114 ? -15.942 -6.309  51.703  1.00 15.31 ? 137  THR   A C   1 
ATOM   744  O  O   . THR   A 1 114 ? -16.808 -6.086  50.854  1.00 14.81 ? 137  THR   A O   1 
ATOM   745  C  CB  . THR   A 1 114 ? -16.256 -5.384  54.046  1.00 13.53 ? 137  THR   A CB  1 
ATOM   746  O  OG1 . THR   A 1 114 ? -17.663 -5.220  53.853  1.00 14.47 ? 137  THR   A OG1 1 
ATOM   747  C  CG2 . THR   A 1 114 ? -15.731 -4.421  55.093  1.00 15.19 ? 137  THR   A CG2 1 
ATOM   748  N  N   . PHE   A 1 115 ? -15.334 -7.487  51.821  1.00 14.62 ? 138  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 115 ? -15.708 -8.606  50.971  1.00 16.13 ? 138  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 115 ? -15.272 -9.903  51.649  1.00 17.15 ? 138  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 115 ? -14.381 -9.902  52.483  1.00 16.76 ? 138  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 115 ? -15.089 -8.519  49.569  1.00 16.21 ? 138  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 115 ? -13.583 -8.697  49.521  1.00 15.45 ? 138  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 115 ? -12.733 -7.622  49.727  1.00 14.77 ? 138  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 115 ? -13.024 -9.952  49.305  1.00 15.78 ? 138  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 115 ? -11.363 -7.783  49.703  1.00 15.40 ? 138  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 115 ? -11.646 -10.104 49.252  1.00 13.62 ? 138  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 115 ? -10.819 -9.019  49.443  1.00 15.16 ? 138  PHE   A CZ  1 
ATOM   759  N  N   . THR   A 1 116 ? -15.917 -11.001 51.263  1.00 16.95 ? 139  THR   A N   1 
ATOM   760  C  CA  A THR   A 1 116 ? -15.632 -12.344 51.736  0.50 18.08 ? 139  THR   A CA  1 
ATOM   761  C  CA  B THR   A 1 116 ? -15.514 -12.312 51.734  0.50 17.74 ? 139  THR   A CA  1 
ATOM   762  C  C   . THR   A 1 116 ? -15.181 -13.161 50.517  1.00 18.62 ? 139  THR   A C   1 
ATOM   763  O  O   . THR   A 1 116 ? -15.642 -12.892 49.421  1.00 21.55 ? 139  THR   A O   1 
ATOM   764  C  CB  A THR   A 1 116 ? -16.921 -12.840 52.407  0.50 18.69 ? 139  THR   A CB  1 
ATOM   765  C  CB  B THR   A 1 116 ? -16.635 -12.932 52.557  0.50 17.76 ? 139  THR   A CB  1 
ATOM   766  O  OG1 A THR   A 1 116 ? -16.973 -12.261 53.716  0.50 19.85 ? 139  THR   A OG1 1 
ATOM   767  O  OG1 B THR   A 1 116 ? -16.143 -14.139 53.135  0.50 20.15 ? 139  THR   A OG1 1 
ATOM   768  C  CG2 A THR   A 1 116 ? -17.011 -14.343 52.590  0.50 19.49 ? 139  THR   A CG2 1 
ATOM   769  C  CG2 B THR   A 1 116 ? -17.855 -13.209 51.707  0.50 16.96 ? 139  THR   A CG2 1 
ATOM   770  N  N   . VAL   A 1 117 ? -14.291 -14.136 50.706  1.00 16.17 ? 140  VAL   A N   1 
ATOM   771  C  CA  . VAL   A 1 117 ? -13.857 -15.009 49.624  1.00 16.81 ? 140  VAL   A CA  1 
ATOM   772  C  C   . VAL   A 1 117 ? -14.742 -16.260 49.667  1.00 15.45 ? 140  VAL   A C   1 
ATOM   773  O  O   . VAL   A 1 117 ? -14.806 -16.887 50.728  1.00 15.71 ? 140  VAL   A O   1 
ATOM   774  C  CB  . VAL   A 1 117 ? -12.368 -15.377 49.830  1.00 19.00 ? 140  VAL   A CB  1 
ATOM   775  C  CG1 . VAL   A 1 117 ? -11.865 -16.376 48.805  1.00 19.98 ? 140  VAL   A CG1 1 
ATOM   776  C  CG2 . VAL   A 1 117 ? -11.454 -14.159 49.833  1.00 20.04 ? 140  VAL   A CG2 1 
ATOM   777  N  N   . PRO   A 1 118 ? -15.408 -16.688 48.571  1.00 14.88 ? 141  PRO   A N   1 
ATOM   778  C  CA  . PRO   A 1 118 ? -16.195 -17.931 48.600  1.00 14.36 ? 141  PRO   A CA  1 
ATOM   779  C  C   . PRO   A 1 118 ? -15.358 -19.107 49.128  1.00 15.50 ? 141  PRO   A C   1 
ATOM   780  O  O   . PRO   A 1 118 ? -14.230 -19.379 48.714  1.00 15.47 ? 141  PRO   A O   1 
ATOM   781  C  CB  . PRO   A 1 118 ? -16.646 -18.105 47.140  1.00 14.70 ? 141  PRO   A CB  1 
ATOM   782  C  CG  . PRO   A 1 118 ? -16.684 -16.701 46.610  1.00 14.95 ? 141  PRO   A CG  1 
ATOM   783  C  CD  . PRO   A 1 118 ? -15.471 -16.027 47.256  1.00 14.43 ? 141  PRO   A CD  1 
ATOM   784  N  N   . SER   A 1 119 ? -15.912 -19.855 50.076  1.00 15.63 ? 142  SER   A N   1 
ATOM   785  C  CA  . SER   A 1 119 ? -15.133 -20.879 50.750  1.00 17.42 ? 142  SER   A CA  1 
ATOM   786  C  C   . SER   A 1 119 ? -14.711 -21.995 49.788  1.00 14.77 ? 142  SER   A C   1 
ATOM   787  O  O   . SER   A 1 119 ? -13.722 -22.670 50.042  1.00 15.75 ? 142  SER   A O   1 
ATOM   788  C  CB  . SER   A 1 119 ? -15.900 -21.410 51.940  1.00 18.98 ? 142  SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 119 ? -17.152 -21.870 51.458  1.00 21.81 ? 142  SER   A OG  1 
ATOM   790  N  N   . ASN   A 1 120 ? -15.425 -22.162 48.671  1.00 14.32 ? 143  ASN   A N   1 
ATOM   791  C  CA  . ASN   A 1 120 ? -15.133 -23.187 47.680  1.00 15.07 ? 143  ASN   A CA  1 
ATOM   792  C  C   . ASN   A 1 120 ? -13.881 -22.850 46.879  1.00 14.54 ? 143  ASN   A C   1 
ATOM   793  O  O   . ASN   A 1 120 ? -13.434 -23.678 46.105  1.00 13.58 ? 143  ASN   A O   1 
ATOM   794  C  CB  . ASN   A 1 120 ? -16.323 -23.468 46.761  1.00 15.89 ? 143  ASN   A CB  1 
ATOM   795  C  CG  . ASN   A 1 120 ? -16.884 -22.211 46.128  1.00 18.06 ? 143  ASN   A CG  1 
ATOM   796  O  OD1 . ASN   A 1 120 ? -17.210 -21.250 46.834  1.00 22.56 ? 143  ASN   A OD1 1 
ATOM   797  N  ND2 . ASN   A 1 120 ? -16.969 -22.162 44.807  1.00 19.74 ? 143  ASN   A ND2 1 
ATOM   798  N  N   . TRP   A 1 121 ? -13.279 -21.660 47.112  1.00 12.27 ? 144  TRP   A N   1 
ATOM   799  C  CA  . TRP   A 1 121 ? -12.056 -21.264 46.441  1.00 11.47 ? 144  TRP   A CA  1 
ATOM   800  C  C   . TRP   A 1 121 ? -10.837 -21.685 47.257  1.00 12.41 ? 144  TRP   A C   1 
ATOM   801  O  O   . TRP   A 1 121 ? -9.707  -21.448 46.870  1.00 13.34 ? 144  TRP   A O   1 
ATOM   802  C  CB  . TRP   A 1 121 ? -12.024 -19.752 46.208  1.00 10.57 ? 144  TRP   A CB  1 
ATOM   803  C  CG  . TRP   A 1 121 ? -13.118 -19.253 45.296  1.00 9.74  ? 144  TRP   A CG  1 
ATOM   804  C  CD1 . TRP   A 1 121 ? -14.193 -19.908 44.777  1.00 9.94  ? 144  TRP   A CD1 1 
ATOM   805  C  CD2 . TRP   A 1 121 ? -13.216 -17.899 44.831  1.00 10.12 ? 144  TRP   A CD2 1 
ATOM   806  N  NE1 . TRP   A 1 121 ? -14.960 -19.055 44.012  1.00 10.37 ? 144  TRP   A NE1 1 
ATOM   807  C  CE2 . TRP   A 1 121 ? -14.382 -17.810 44.038  1.00 10.28 ? 144  TRP   A CE2 1 
ATOM   808  C  CE3 . TRP   A 1 121 ? -12.425 -16.772 45.044  1.00 10.42 ? 144  TRP   A CE3 1 
ATOM   809  C  CZ2 . TRP   A 1 121 ? -14.783 -16.600 43.478  1.00 11.01 ? 144  TRP   A CZ2 1 
ATOM   810  C  CZ3 . TRP   A 1 121 ? -12.822 -15.585 44.487  1.00 10.48 ? 144  TRP   A CZ3 1 
ATOM   811  C  CH2 . TRP   A 1 121 ? -13.970 -15.512 43.706  1.00 10.77 ? 144  TRP   A CH2 1 
ATOM   812  N  N   . ASN   A 1 122 ? -11.074 -22.333 48.393  1.00 14.39 ? 145  ASN   A N   1 
ATOM   813  C  CA  . ASN   A 1 122 ? -9.984  -22.780 49.250  1.00 16.27 ? 145  ASN   A CA  1 
ATOM   814  C  C   . ASN   A 1 122 ? -8.969  -23.566 48.418  1.00 13.55 ? 145  ASN   A C   1 
ATOM   815  O  O   . ASN   A 1 122 ? -9.347  -24.470 47.682  1.00 13.99 ? 145  ASN   A O   1 
ATOM   816  C  CB  . ASN   A 1 122 ? -10.553 -23.655 50.365  1.00 17.58 ? 145  ASN   A CB  1 
ATOM   817  C  CG  . ASN   A 1 122 ? -9.531  -24.079 51.394  1.00 21.10 ? 145  ASN   A CG  1 
ATOM   818  O  OD1 . ASN   A 1 122 ? -8.865  -23.239 51.997  1.00 22.99 ? 145  ASN   A OD1 1 
ATOM   819  N  ND2 . ASN   A 1 122 ? -9.420  -25.376 51.628  1.00 22.16 ? 145  ASN   A ND2 1 
ATOM   820  N  N   . GLY   A 1 123 ? -7.683  -23.251 48.575  1.00 13.61 ? 146  GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 123 ? -6.617  -23.990 47.914  1.00 14.50 ? 146  GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 123 ? -6.240  -23.445 46.537  1.00 14.18 ? 146  GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 123 ? -5.354  -23.997 45.899  1.00 14.33 ? 146  GLY   A O   1 
ATOM   824  N  N   . ARG   A 1 124 ? -6.934  -22.384 46.085  1.00 12.69 ? 147  ARG   A N   1 
ATOM   825  C  CA  . ARG   A 1 124 ? -6.557  -21.641 44.899  1.00 11.96 ? 147  ARG   A CA  1 
ATOM   826  C  C   . ARG   A 1 124 ? -5.992  -20.282 45.287  1.00 11.09 ? 147  ARG   A C   1 
ATOM   827  O  O   . ARG   A 1 124 ? -6.189  -19.793 46.400  1.00 9.00  ? 147  ARG   A O   1 
ATOM   828  C  CB  . ARG   A 1 124 ? -7.776  -21.538 43.984  1.00 12.85 ? 147  ARG   A CB  1 
ATOM   829  C  CG  . ARG   A 1 124 ? -7.913  -22.831 43.197  1.00 14.58 ? 147  ARG   A CG  1 
ATOM   830  C  CD  . ARG   A 1 124 ? -9.145  -22.822 42.297  1.00 16.66 ? 147  ARG   A CD  1 
ATOM   831  N  NE  . ARG   A 1 124 ? -10.410 -23.028 43.010  1.00 15.82 ? 147  ARG   A NE  1 
ATOM   832  C  CZ  . ARG   A 1 124 ? -11.638 -22.958 42.475  1.00 15.46 ? 147  ARG   A CZ  1 
ATOM   833  N  NH1 . ARG   A 1 124 ? -11.768 -22.645 41.202  1.00 13.72 ? 147  ARG   A NH1 1 
ATOM   834  N  NH2 . ARG   A 1 124 ? -12.715 -23.255 43.205  1.00 15.13 ? 147  ARG   A NH2 1 
ATOM   835  N  N   . ARG   A 1 125 ? -5.215  -19.732 44.342  1.00 10.82 ? 148  ARG   A N   1 
ATOM   836  C  CA  . ARG   A 1 125 ? -4.777  -18.357 44.394  1.00 10.98 ? 148  ARG   A CA  1 
ATOM   837  C  C   . ARG   A 1 125 ? -5.992  -17.512 44.059  1.00 10.00 ? 148  ARG   A C   1 
ATOM   838  O  O   . ARG   A 1 125 ? -6.959  -17.994 43.455  1.00 9.53  ? 148  ARG   A O   1 
ATOM   839  C  CB  . ARG   A 1 125 ? -3.564  -18.120 43.493  1.00 11.76 ? 148  ARG   A CB  1 
ATOM   840  C  CG  . ARG   A 1 125 ? -2.407  -18.975 44.018  1.00 12.84 ? 148  ARG   A CG  1 
ATOM   841  C  CD  . ARG   A 1 125 ? -1.025  -18.552 43.648  1.00 13.97 ? 148  ARG   A CD  1 
ATOM   842  N  NE  . ARG   A 1 125 ? -0.775  -17.275 44.313  1.00 14.27 ? 148  ARG   A NE  1 
ATOM   843  C  CZ  . ARG   A 1 125 ? -0.147  -17.116 45.471  1.00 14.86 ? 148  ARG   A CZ  1 
ATOM   844  N  NH1 . ARG   A 1 125 ? 0.289   -18.185 46.134  1.00 14.34 ? 148  ARG   A NH1 1 
ATOM   845  N  NH2 . ARG   A 1 125 ? 0.062   -15.900 45.937  1.00 13.01 ? 148  ARG   A NH2 1 
ATOM   846  N  N   . VAL   A 1 126 ? -5.945  -16.255 44.500  1.00 10.06 ? 149  VAL   A N   1 
ATOM   847  C  CA  . VAL   A 1 126 ? -7.056  -15.367 44.269  1.00 9.19  ? 149  VAL   A CA  1 
ATOM   848  C  C   . VAL   A 1 126 ? -6.525  -14.120 43.601  1.00 9.50  ? 149  VAL   A C   1 
ATOM   849  O  O   . VAL   A 1 126 ? -5.639  -13.475 44.152  1.00 9.57  ? 149  VAL   A O   1 
ATOM   850  C  CB  . VAL   A 1 126 ? -7.794  -15.057 45.577  1.00 9.70  ? 149  VAL   A CB  1 
ATOM   851  C  CG1 . VAL   A 1 126 ? -8.878  -14.020 45.370  1.00 10.20 ? 149  VAL   A CG1 1 
ATOM   852  C  CG2 . VAL   A 1 126 ? -8.365  -16.349 46.167  1.00 10.42 ? 149  VAL   A CG2 1 
ATOM   853  N  N   . GLN   A 1 127 ? -7.102  -13.794 42.434  1.00 8.98  ? 150  GLN   A N   1 
ATOM   854  C  CA  . GLN   A 1 127 ? -6.716  -12.621 41.677  1.00 8.93  ? 150  GLN   A CA  1 
ATOM   855  C  C   . GLN   A 1 127 ? -7.795  -11.552 41.834  1.00 9.19  ? 150  GLN   A C   1 
ATOM   856  O  O   . GLN   A 1 127 ? -8.990  -11.839 41.809  1.00 9.34  ? 150  GLN   A O   1 
ATOM   857  C  CB  . GLN   A 1 127 ? -6.565  -12.954 40.197  1.00 9.90  ? 150  GLN   A CB  1 
ATOM   858  C  CG  . GLN   A 1 127 ? -5.871  -14.287 39.936  1.00 10.72 ? 150  GLN   A CG  1 
ATOM   859  C  CD  . GLN   A 1 127 ? -4.473  -14.313 40.499  1.00 11.36 ? 150  GLN   A CD  1 
ATOM   860  O  OE1 . GLN   A 1 127 ? -3.855  -13.263 40.672  1.00 11.64 ? 150  GLN   A OE1 1 
ATOM   861  N  NE2 . GLN   A 1 127 ? -3.938  -15.498 40.736  1.00 12.15 ? 150  GLN   A NE2 1 
ATOM   862  N  N   . LEU   A 1 128 ? -7.336  -10.319 42.054  1.00 8.91  ? 151  LEU   A N   1 
ATOM   863  C  CA  . LEU   A 1 128 ? -8.199  -9.154  42.067  1.00 8.77  ? 151  LEU   A CA  1 
ATOM   864  C  C   . LEU   A 1 128 ? -7.982  -8.407  40.756  1.00 8.86  ? 151  LEU   A C   1 
ATOM   865  O  O   . LEU   A 1 128 ? -6.851  -7.967  40.474  1.00 8.99  ? 151  LEU   A O   1 
ATOM   866  C  CB  . LEU   A 1 128 ? -7.764  -8.312  43.267  1.00 8.65  ? 151  LEU   A CB  1 
ATOM   867  C  CG  . LEU   A 1 128 ? -8.416  -6.928  43.371  1.00 9.68  ? 151  LEU   A CG  1 
ATOM   868  C  CD1 . LEU   A 1 128 ? -9.935  -7.025  43.490  1.00 9.59  ? 151  LEU   A CD1 1 
ATOM   869  C  CD2 . LEU   A 1 128 ? -7.754  -6.172  44.502  1.00 10.33 ? 151  LEU   A CD2 1 
ATOM   870  N  N   . ASN   A 1 129 ? -9.084  -8.208  40.027  1.00 8.29  ? 152  ASN   A N   1 
ATOM   871  C  CA  . ASN   A 1 129 ? -9.034  -7.764  38.645  1.00 8.54  ? 152  ASN   A CA  1 
ATOM   872  C  C   . ASN   A 1 129 ? -9.724  -6.413  38.531  1.00 7.70  ? 152  ASN   A C   1 
ATOM   873  O  O   . ASN   A 1 129 ? -10.845 -6.268  39.009  1.00 8.62  ? 152  ASN   A O   1 
ATOM   874  C  CB  . ASN   A 1 129 ? -9.780  -8.740  37.745  1.00 8.52  ? 152  ASN   A CB  1 
ATOM   875  C  CG  . ASN   A 1 129 ? -9.070  -10.065 37.659  1.00 9.33  ? 152  ASN   A CG  1 
ATOM   876  O  OD1 . ASN   A 1 129 ? -7.833  -10.124 37.730  1.00 9.32  ? 152  ASN   A OD1 1 
ATOM   877  N  ND2 . ASN   A 1 129 ? -9.830  -11.120 37.425  1.00 9.98  ? 152  ASN   A ND2 1 
ATOM   878  N  N   . PHE   A 1 130 ? -9.047  -5.438  37.915  1.00 7.96  ? 153  PHE   A N   1 
ATOM   879  C  CA  . PHE   A 1 130 ? -9.658  -4.152  37.577  1.00 7.80  ? 153  PHE   A CA  1 
ATOM   880  C  C   . PHE   A 1 130 ? -9.723  -4.034  36.057  1.00 7.63  ? 153  PHE   A C   1 
ATOM   881  O  O   . PHE   A 1 130 ? -8.693  -4.145  35.405  1.00 7.65  ? 153  PHE   A O   1 
ATOM   882  C  CB  . PHE   A 1 130 ? -8.808  -2.974  38.068  1.00 8.01  ? 153  PHE   A CB  1 
ATOM   883  C  CG  . PHE   A 1 130 ? -8.755  -2.892  39.583  1.00 8.74  ? 153  PHE   A CG  1 
ATOM   884  C  CD1 . PHE   A 1 130 ? -7.873  -3.682  40.295  1.00 8.57  ? 153  PHE   A CD1 1 
ATOM   885  C  CD2 . PHE   A 1 130 ? -9.585  -2.017  40.276  1.00 8.92  ? 153  PHE   A CD2 1 
ATOM   886  C  CE1 . PHE   A 1 130 ? -7.848  -3.612  41.687  1.00 9.00  ? 153  PHE   A CE1 1 
ATOM   887  C  CE2 . PHE   A 1 130 ? -9.562  -1.950  41.659  1.00 9.66  ? 153  PHE   A CE2 1 
ATOM   888  C  CZ  . PHE   A 1 130 ? -8.680  -2.730  42.362  1.00 9.62  ? 153  PHE   A CZ  1 
ATOM   889  N  N   . GLY   A 1 131 ? -10.903 -3.795  35.485  1.00 7.33  ? 154  GLY   A N   1 
ATOM   890  C  CA  . GLY   A 1 131 ? -10.944 -3.578  34.042  1.00 7.02  ? 154  GLY   A CA  1 
ATOM   891  C  C   . GLY   A 1 131 ? -10.273 -2.252  33.645  1.00 7.08  ? 154  GLY   A C   1 
ATOM   892  O  O   . GLY   A 1 131 ? -9.631  -2.118  32.617  1.00 7.28  ? 154  GLY   A O   1 
ATOM   893  N  N   . ALA   A 1 132 ? -10.550 -1.209  34.427  1.00 7.28  ? 155  ALA   A N   1 
ATOM   894  C  CA  . ALA   A 1 132 ? -9.928  0.101   34.232  1.00 7.38  ? 155  ALA   A CA  1 
ATOM   895  C  C   . ALA   A 1 132 ? -10.210 1.035   35.412  1.00 7.16  ? 155  ALA   A C   1 
ATOM   896  O  O   . ALA   A 1 132 ? -11.276 0.963   36.040  1.00 7.84  ? 155  ALA   A O   1 
ATOM   897  C  CB  . ALA   A 1 132 ? -10.415 0.763   32.963  1.00 7.20  ? 155  ALA   A CB  1 
ATOM   898  N  N   . SER   A 1 133 ? -9.276  1.962   35.634  1.00 7.95  ? 156  SER   A N   1 
ATOM   899  C  CA  . SER   A 1 133 ? -9.374  2.968   36.688  1.00 8.02  ? 156  SER   A CA  1 
ATOM   900  C  C   . SER   A 1 133 ? -8.496  4.126   36.244  1.00 7.63  ? 156  SER   A C   1 
ATOM   901  O  O   . SER   A 1 133 ? -7.329  3.923   35.893  1.00 7.41  ? 156  SER   A O   1 
ATOM   902  C  CB  . SER   A 1 133 ? -8.974  2.403   38.045  1.00 8.35  ? 156  SER   A CB  1 
ATOM   903  O  OG  . SER   A 1 133 ? -8.926  3.391   39.096  1.00 8.55  ? 156  SER   A OG  1 
ATOM   904  N  N   . ASP   A 1 134 ? -9.075  5.329   36.210  1.00 8.10  ? 157  ASP   A N   1 
ATOM   905  C  CA  . ASP   A 1 134 ? -8.397  6.484   35.629  1.00 7.92  ? 157  ASP   A CA  1 
ATOM   906  C  C   . ASP   A 1 134 ? -8.014  7.423   36.785  1.00 7.91  ? 157  ASP   A C   1 
ATOM   907  O  O   . ASP   A 1 134 ? -8.913  7.875   37.489  1.00 7.07  ? 157  ASP   A O   1 
ATOM   908  C  CB  . ASP   A 1 134 ? -9.310  7.163   34.613  1.00 8.09  ? 157  ASP   A CB  1 
ATOM   909  C  CG  . ASP   A 1 134 ? -8.592  8.082   33.622  1.00 9.17  ? 157  ASP   A CG  1 
ATOM   910  O  OD1 . ASP   A 1 134 ? -7.368  7.925   33.492  1.00 8.20  ? 157  ASP   A OD1 1 
ATOM   911  O  OD2 . ASP   A 1 134 ? -9.248  8.969   33.022  1.00 7.89  ? 157  ASP   A OD2 1 
ATOM   912  N  N   . TRP   A 1 135 ? -6.719  7.716   37.021  1.00 7.62  ? 158  TRP   A N   1 
ATOM   913  C  CA  . TRP   A 1 135 ? -5.583  7.337   36.201  1.00 8.18  ? 158  TRP   A CA  1 
ATOM   914  C  C   . TRP   A 1 135 ? -4.550  6.499   36.961  1.00 8.61  ? 158  TRP   A C   1 
ATOM   915  O  O   . TRP   A 1 135 ? -4.010  5.538   36.420  1.00 9.86  ? 158  TRP   A O   1 
ATOM   916  C  CB  . TRP   A 1 135 ? -4.923  8.617   35.678  1.00 8.34  ? 158  TRP   A CB  1 
ATOM   917  C  CG  . TRP   A 1 135 ? -3.774  8.321   34.775  1.00 8.56  ? 158  TRP   A CG  1 
ATOM   918  C  CD1 . TRP   A 1 135 ? -3.838  7.745   33.537  1.00 8.46  ? 158  TRP   A CD1 1 
ATOM   919  C  CD2 . TRP   A 1 135 ? -2.383  8.552   35.063  1.00 9.26  ? 158  TRP   A CD2 1 
ATOM   920  N  NE1 . TRP   A 1 135 ? -2.572  7.607   33.033  1.00 8.68  ? 158  TRP   A NE1 1 
ATOM   921  C  CE2 . TRP   A 1 135 ? -1.663  8.088   33.949  1.00 9.22  ? 158  TRP   A CE2 1 
ATOM   922  C  CE3 . TRP   A 1 135 ? -1.684  9.128   36.139  1.00 10.24 ? 158  TRP   A CE3 1 
ATOM   923  C  CZ2 . TRP   A 1 135 ? -0.273  8.187   33.882  1.00 10.14 ? 158  TRP   A CZ2 1 
ATOM   924  C  CZ3 . TRP   A 1 135 ? -0.309  9.179   36.087  1.00 11.31 ? 158  TRP   A CZ3 1 
ATOM   925  C  CH2 . TRP   A 1 135 ? 0.382   8.723   34.977  1.00 10.84 ? 158  TRP   A CH2 1 
ATOM   926  N  N   . ARG   A 1 136 ? -4.238  6.905   38.201  1.00 8.61  ? 159  ARG   A N   1 
ATOM   927  C  CA  . ARG   A 1 136 ? -3.174  6.287   38.975  1.00 9.21  ? 159  ARG   A CA  1 
ATOM   928  C  C   . ARG   A 1 136 ? -3.808  5.641   40.207  1.00 9.13  ? 159  ARG   A C   1 
ATOM   929  O  O   . ARG   A 1 136 ? -4.364  6.324   41.063  1.00 7.86  ? 159  ARG   A O   1 
ATOM   930  C  CB  . ARG   A 1 136 ? -2.082  7.292   39.343  1.00 11.96 ? 159  ARG   A CB  1 
ATOM   931  C  CG  . ARG   A 1 136 ? -0.976  6.653   40.176  1.00 14.08 ? 159  ARG   A CG  1 
ATOM   932  C  CD  . ARG   A 1 136 ? 0.129   7.628   40.552  1.00 19.36 ? 159  ARG   A CD  1 
ATOM   933  N  NE  . ARG   A 1 136 ? 0.830   7.924   39.302  1.00 27.59 ? 159  ARG   A NE  1 
ATOM   934  C  CZ  . ARG   A 1 136 ? 2.072   7.613   38.963  1.00 35.37 ? 159  ARG   A CZ  1 
ATOM   935  N  NH1 . ARG   A 1 136 ? 2.765   6.732   39.681  1.00 42.88 ? 159  ARG   A NH1 1 
ATOM   936  N  NH2 . ARG   A 1 136 ? 2.602   8.157   37.880  1.00 29.23 ? 159  ARG   A NH2 1 
ATOM   937  N  N   . THR   A 1 137 ? -3.773  4.302   40.233  1.00 8.17  ? 160  THR   A N   1 
ATOM   938  C  CA  . THR   A 1 137 ? -4.526  3.508   41.196  1.00 9.55  ? 160  THR   A CA  1 
ATOM   939  C  C   . THR   A 1 137 ? -3.574  2.783   42.138  1.00 8.87  ? 160  THR   A C   1 
ATOM   940  O  O   . THR   A 1 137 ? -2.671  2.102   41.653  1.00 9.53  ? 160  THR   A O   1 
ATOM   941  C  CB  . THR   A 1 137 ? -5.374  2.497   40.434  1.00 9.58  ? 160  THR   A CB  1 
ATOM   942  O  OG1 . THR   A 1 137 ? -6.208  3.268   39.565  1.00 9.50  ? 160  THR   A OG1 1 
ATOM   943  C  CG2 . THR   A 1 137 ? -6.209  1.708   41.411  1.00 10.30 ? 160  THR   A CG2 1 
ATOM   944  N  N   . THR   A 1 138 ? -3.824  2.878   43.453  1.00 10.09 ? 161  THR   A N   1 
ATOM   945  C  CA  . THR   A 1 138 ? -3.066  2.141   44.460  1.00 9.62  ? 161  THR   A CA  1 
ATOM   946  C  C   . THR   A 1 138 ? -4.042  1.297   45.280  1.00 9.60  ? 161  THR   A C   1 
ATOM   947  O  O   . THR   A 1 138 ? -5.130  1.736   45.614  1.00 8.94  ? 161  THR   A O   1 
ATOM   948  C  CB  . THR   A 1 138 ? -2.304  3.095   45.385  1.00 9.88  ? 161  THR   A CB  1 
ATOM   949  O  OG1 . THR   A 1 138 ? -1.666  4.107   44.603  1.00 9.64  ? 161  THR   A OG1 1 
ATOM   950  C  CG2 . THR   A 1 138 ? -1.303  2.322   46.241  1.00 10.41 ? 161  THR   A CG2 1 
ATOM   951  N  N   . VAL   A 1 139 ? -3.650  0.062   45.600  1.00 9.17  ? 162  VAL   A N   1 
ATOM   952  C  CA  . VAL   A 1 139 ? -4.586  -0.885  46.168  1.00 9.50  ? 162  VAL   A CA  1 
ATOM   953  C  C   . VAL   A 1 139 ? -4.001  -1.507  47.437  1.00 9.72  ? 162  VAL   A C   1 
ATOM   954  O  O   . VAL   A 1 139 ? -2.837  -1.956  47.413  1.00 10.53 ? 162  VAL   A O   1 
ATOM   955  C  CB  . VAL   A 1 139 ? -4.908  -1.967  45.124  1.00 9.73  ? 162  VAL   A CB  1 
ATOM   956  C  CG1 . VAL   A 1 139 ? -5.816  -3.039  45.716  1.00 10.33 ? 162  VAL   A CG1 1 
ATOM   957  C  CG2 . VAL   A 1 139 ? -5.508  -1.380  43.843  1.00 9.69  ? 162  VAL   A CG2 1 
ATOM   958  N  N   . TRP   A 1 140 ? -4.823  -1.497  48.508  1.00 9.61  ? 163  TRP   A N   1 
ATOM   959  C  CA  . TRP   A 1 140 ? -4.514  -2.189  49.752  1.00 10.17 ? 163  TRP   A CA  1 
ATOM   960  C  C   . TRP   A 1 140 ? -5.592  -3.209  50.113  1.00 10.43 ? 163  TRP   A C   1 
ATOM   961  O  O   . TRP   A 1 140 ? -6.804  -2.944  50.097  1.00 11.11 ? 163  TRP   A O   1 
ATOM   962  C  CB  . TRP   A 1 140 ? -4.378  -1.166  50.875  1.00 10.76 ? 163  TRP   A CB  1 
ATOM   963  C  CG  . TRP   A 1 140 ? -3.261  -0.179  50.702  1.00 10.36 ? 163  TRP   A CG  1 
ATOM   964  C  CD1 . TRP   A 1 140 ? -2.029  -0.249  51.278  1.00 11.05 ? 163  TRP   A CD1 1 
ATOM   965  C  CD2 . TRP   A 1 140 ? -3.318  1.082   50.005  1.00 11.26 ? 163  TRP   A CD2 1 
ATOM   966  N  NE1 . TRP   A 1 140 ? -1.290  0.846   50.938  1.00 11.56 ? 163  TRP   A NE1 1 
ATOM   967  C  CE2 . TRP   A 1 140 ? -2.071  1.707   50.212  1.00 11.52 ? 163  TRP   A CE2 1 
ATOM   968  C  CE3 . TRP   A 1 140 ? -4.309  1.759   49.280  1.00 11.30 ? 163  TRP   A CE3 1 
ATOM   969  C  CZ2 . TRP   A 1 140 ? -1.769  2.940   49.668  1.00 11.51 ? 163  TRP   A CZ2 1 
ATOM   970  C  CZ3 . TRP   A 1 140 ? -4.001  2.990   48.733  1.00 10.93 ? 163  TRP   A CZ3 1 
ATOM   971  C  CH2 . TRP   A 1 140 ? -2.763  3.583   48.962  1.00 11.34 ? 163  TRP   A CH2 1 
ATOM   972  N  N   . VAL   A 1 141 ? -5.131  -4.402  50.470  1.00 10.16 ? 164  VAL   A N   1 
ATOM   973  C  CA  . VAL   A 1 141 ? -6.007  -5.445  50.958  1.00 9.93  ? 164  VAL   A CA  1 
ATOM   974  C  C   . VAL   A 1 141 ? -5.643  -5.670  52.418  1.00 9.58  ? 164  VAL   A C   1 
ATOM   975  O  O   . VAL   A 1 141 ? -4.490  -5.975  52.690  1.00 9.16  ? 164  VAL   A O   1 
ATOM   976  C  CB  . VAL   A 1 141 ? -5.875  -6.732  50.127  1.00 10.23 ? 164  VAL   A CB  1 
ATOM   977  C  CG1 . VAL   A 1 141 ? -6.644  -7.879  50.742  1.00 10.08 ? 164  VAL   A CG1 1 
ATOM   978  C  CG2 . VAL   A 1 141 ? -6.333  -6.530  48.671  1.00 10.86 ? 164  VAL   A CG2 1 
ATOM   979  N  N   . ASN   A 1 142 ? -6.613  -5.474  53.311  1.00 10.04 ? 165  ASN   A N   1 
ATOM   980  C  CA  . ASN   A 1 142 ? -6.374  -5.632  54.745  1.00 11.29 ? 165  ASN   A CA  1 
ATOM   981  C  C   . ASN   A 1 142 ? -5.155  -4.828  55.185  1.00 11.91 ? 165  ASN   A C   1 
ATOM   982  O  O   . ASN   A 1 142 ? -4.337  -5.262  56.007  1.00 13.71 ? 165  ASN   A O   1 
ATOM   983  C  CB  . ASN   A 1 142 ? -6.265  -7.094  55.147  1.00 11.39 ? 165  ASN   A CB  1 
ATOM   984  C  CG  . ASN   A 1 142 ? -7.530  -7.846  54.840  1.00 11.24 ? 165  ASN   A CG  1 
ATOM   985  O  OD1 . ASN   A 1 142 ? -8.624  -7.365  55.138  1.00 11.20 ? 165  ASN   A OD1 1 
ATOM   986  N  ND2 . ASN   A 1 142 ? -7.400  -8.999  54.220  1.00 11.74 ? 165  ASN   A ND2 1 
ATOM   987  N  N   . GLY   A 1 143 ? -5.016  -3.638  54.613  1.00 12.26 ? 166  GLY   A N   1 
ATOM   988  C  CA  . GLY   A 1 143 ? -4.010  -2.698  55.062  1.00 13.42 ? 166  GLY   A CA  1 
ATOM   989  C  C   . GLY   A 1 143 ? -2.661  -2.881  54.382  1.00 13.20 ? 166  GLY   A C   1 
ATOM   990  O  O   . GLY   A 1 143 ? -1.741  -2.138  54.716  1.00 12.57 ? 166  GLY   A O   1 
ATOM   991  N  N   . ARG   A 1 144 ? -2.541  -3.850  53.462  1.00 13.30 ? 167  ARG   A N   1 
ATOM   992  C  CA  . ARG   A 1 144 ? -1.267  -4.204  52.851  1.00 14.75 ? 167  ARG   A CA  1 
ATOM   993  C  C   . ARG   A 1 144 ? -1.351  -3.893  51.366  1.00 12.98 ? 167  ARG   A C   1 
ATOM   994  O  O   . ARG   A 1 144 ? -2.283  -4.314  50.688  1.00 10.88 ? 167  ARG   A O   1 
ATOM   995  C  CB  . ARG   A 1 144 ? -0.950  -5.686  53.116  1.00 19.43 ? 167  ARG   A CB  1 
ATOM   996  C  CG  . ARG   A 1 144 ? -0.980  -6.033  54.605  1.00 23.80 ? 167  ARG   A CG  1 
ATOM   997  C  CD  . ARG   A 1 144 ? -0.514  -7.450  54.945  1.00 34.30 ? 167  ARG   A CD  1 
ATOM   998  N  NE  . ARG   A 1 144 ? -0.854  -7.845  56.324  1.00 43.36 ? 167  ARG   A NE  1 
ATOM   999  C  CZ  . ARG   A 1 144 ? -1.880  -8.606  56.755  1.00 53.02 ? 167  ARG   A CZ  1 
ATOM   1000 N  NH1 . ARG   A 1 144 ? -2.682  -9.263  55.922  1.00 56.09 ? 167  ARG   A NH1 1 
ATOM   1001 N  NH2 . ARG   A 1 144 ? -2.091  -8.719  58.058  1.00 58.38 ? 167  ARG   A NH2 1 
ATOM   1002 N  N   . GLN   A 1 145 ? -0.359  -3.168  50.860  1.00 12.05 ? 168  GLN   A N   1 
ATOM   1003 C  CA  . GLN   A 1 145 ? -0.350  -2.813  49.453  1.00 12.49 ? 168  GLN   A CA  1 
ATOM   1004 C  C   . GLN   A 1 145 ? -0.284  -4.076  48.601  1.00 13.39 ? 168  GLN   A C   1 
ATOM   1005 O  O   . GLN   A 1 145 ? 0.539   -4.942  48.849  1.00 13.05 ? 168  GLN   A O   1 
ATOM   1006 C  CB  . GLN   A 1 145 ? 0.840   -1.907  49.197  1.00 13.55 ? 168  GLN   A CB  1 
ATOM   1007 C  CG  . GLN   A 1 145 ? 0.716   -1.226  47.850  1.00 13.55 ? 168  GLN   A CG  1 
ATOM   1008 C  CD  . GLN   A 1 145 ? 1.767   -0.181  47.612  1.00 16.21 ? 168  GLN   A CD  1 
ATOM   1009 O  OE1 . GLN   A 1 145 ? 2.087   0.613   48.513  1.00 19.70 ? 168  GLN   A OE1 1 
ATOM   1010 N  NE2 . GLN   A 1 145 ? 2.272   -0.159  46.381  1.00 15.31 ? 168  GLN   A NE2 1 
ATOM   1011 N  N   . ALA   A 1 146 ? -1.164  -4.186  47.603  1.00 11.67 ? 169  ALA   A N   1 
ATOM   1012 C  CA  . ALA   A 1 146 ? -1.326  -5.425  46.870  1.00 11.55 ? 169  ALA   A CA  1 
ATOM   1013 C  C   . ALA   A 1 146 ? -0.263  -5.591  45.802  1.00 12.00 ? 169  ALA   A C   1 
ATOM   1014 O  O   . ALA   A 1 146 ? -0.054  -6.708  45.348  1.00 11.40 ? 169  ALA   A O   1 
ATOM   1015 C  CB  . ALA   A 1 146 ? -2.701  -5.459  46.265  1.00 12.27 ? 169  ALA   A CB  1 
ATOM   1016 N  N   . GLY   A 1 147 ? 0.401   -4.495  45.373  1.00 11.40 ? 170  GLY   A N   1 
ATOM   1017 C  CA  . GLY   A 1 147 ? 1.413   -4.569  44.347  1.00 11.89 ? 170  GLY   A CA  1 
ATOM   1018 C  C   . GLY   A 1 147 ? 1.719   -3.160  43.861  1.00 12.00 ? 170  GLY   A C   1 
ATOM   1019 O  O   . GLY   A 1 147 ? 1.316   -2.217  44.519  1.00 11.72 ? 170  GLY   A O   1 
ATOM   1020 N  N   . ALA   A 1 148 ? 2.348   -3.053  42.699  1.00 12.25 ? 171  ALA   A N   1 
ATOM   1021 C  CA  . ALA   A 1 148 ? 2.778   -1.775  42.158  1.00 11.94 ? 171  ALA   A CA  1 
ATOM   1022 C  C   . ALA   A 1 148 ? 1.573   -0.881  41.883  1.00 11.05 ? 171  ALA   A C   1 
ATOM   1023 O  O   . ALA   A 1 148 ? 0.502   -1.365  41.493  1.00 12.05 ? 171  ALA   A O   1 
ATOM   1024 C  CB  . ALA   A 1 148 ? 3.597   -2.008  40.911  1.00 12.72 ? 171  ALA   A CB  1 
ATOM   1025 N  N   . VAL   A 1 149 ? 1.771   0.421   42.083  1.00 11.00 ? 172  VAL   A N   1 
ATOM   1026 C  CA  . VAL   A 1 149 ? 0.817   1.416   41.637  1.00 10.23 ? 172  VAL   A CA  1 
ATOM   1027 C  C   . VAL   A 1 149 ? 0.612   1.237   40.127  1.00 10.58 ? 172  VAL   A C   1 
ATOM   1028 O  O   . VAL   A 1 149 ? 1.573   1.044   39.386  1.00 10.20 ? 172  VAL   A O   1 
ATOM   1029 C  CB  . VAL   A 1 149 ? 1.383   2.816   41.958  1.00 11.61 ? 172  VAL   A CB  1 
ATOM   1030 C  CG1 . VAL   A 1 149 ? 0.554   3.912   41.318  1.00 12.31 ? 172  VAL   A CG1 1 
ATOM   1031 C  CG2 . VAL   A 1 149 ? 1.497   3.050   43.462  1.00 12.15 ? 172  VAL   A CG2 1 
ATOM   1032 N  N   . HIS   A 1 150 ? -0.637  1.324   39.665  1.00 9.46  ? 173  HIS   A N   1 
ATOM   1033 C  CA  . HIS   A 1 150 ? -0.941  1.212   38.252  1.00 9.03  ? 173  HIS   A CA  1 
ATOM   1034 C  C   . HIS   A 1 150 ? -1.261  2.589   37.682  1.00 9.69  ? 173  HIS   A C   1 
ATOM   1035 O  O   . HIS   A 1 150 ? -2.142  3.286   38.213  1.00 10.26 ? 173  HIS   A O   1 
ATOM   1036 C  CB  . HIS   A 1 150 ? -2.137  0.276   38.058  1.00 8.30  ? 173  HIS   A CB  1 
ATOM   1037 C  CG  . HIS   A 1 150 ? -2.533  0.232   36.630  1.00 7.89  ? 173  HIS   A CG  1 
ATOM   1038 N  ND1 . HIS   A 1 150 ? -3.471  1.060   36.033  1.00 8.31  ? 173  HIS   A ND1 1 
ATOM   1039 C  CD2 . HIS   A 1 150 ? -2.030  -0.550  35.648  1.00 7.84  ? 173  HIS   A CD2 1 
ATOM   1040 C  CE1 . HIS   A 1 150 ? -3.510  0.767   34.713  1.00 8.27  ? 173  HIS   A CE1 1 
ATOM   1041 N  NE2 . HIS   A 1 150 ? -2.647  -0.206  34.458  1.00 8.15  ? 173  HIS   A NE2 1 
ATOM   1042 N  N   . SER   A 1 151 ? -0.575  2.940   36.593  1.00 9.48  ? 174  SER   A N   1 
ATOM   1043 C  CA  . SER   A 1 151 ? -0.779  4.218   35.940  1.00 9.62  ? 174  SER   A CA  1 
ATOM   1044 C  C   . SER   A 1 151 ? -1.304  3.949   34.535  1.00 9.42  ? 174  SER   A C   1 
ATOM   1045 O  O   . SER   A 1 151 ? -0.662  3.234   33.789  1.00 9.67  ? 174  SER   A O   1 
ATOM   1046 C  CB  . SER   A 1 151 ? 0.470   5.033   35.946  1.00 10.95 ? 174  SER   A CB  1 
ATOM   1047 O  OG  . SER   A 1 151 ? 0.855   5.342   37.278  1.00 11.53 ? 174  SER   A OG  1 
ATOM   1048 N  N   . GLY   A 1 152 ? -2.520  4.436   34.242  1.00 8.98  ? 175  GLY   A N   1 
ATOM   1049 C  CA  . GLY   A 1 152 ? -3.126  4.286   32.911  1.00 8.40  ? 175  GLY   A CA  1 
ATOM   1050 C  C   . GLY   A 1 152 ? -4.609  4.016   33.076  1.00 8.31  ? 175  GLY   A C   1 
ATOM   1051 O  O   . GLY   A 1 152 ? -4.978  3.213   33.922  1.00 8.54  ? 175  GLY   A O   1 
ATOM   1052 N  N   . GLY   A 1 153 ? -5.439  4.758   32.326  1.00 8.54  ? 176  GLY   A N   1 
ATOM   1053 C  CA  . GLY   A 1 153 ? -6.873  4.766   32.543  1.00 8.48  ? 176  GLY   A CA  1 
ATOM   1054 C  C   . GLY   A 1 153 ? -7.647  3.836   31.636  1.00 8.35  ? 176  GLY   A C   1 
ATOM   1055 O  O   . GLY   A 1 153 ? -8.862  3.768   31.782  1.00 7.77  ? 176  GLY   A O   1 
ATOM   1056 N  N   . TYR   A 1 154 ? -6.966  3.116   30.742  1.00 8.70  ? 177  TYR   A N   1 
ATOM   1057 C  CA  . TYR   A 1 154 ? -7.662  2.387   29.693  1.00 8.37  ? 177  TYR   A CA  1 
ATOM   1058 C  C   . TYR   A 1 154 ? -7.289  0.912   29.628  1.00 8.70  ? 177  TYR   A C   1 
ATOM   1059 O  O   . TYR   A 1 154 ? -7.825  0.212   28.762  1.00 8.91  ? 177  TYR   A O   1 
ATOM   1060 C  CB  . TYR   A 1 154 ? -7.415  3.008   28.320  1.00 7.88  ? 177  TYR   A CB  1 
ATOM   1061 C  CG  . TYR   A 1 154 ? -7.897  4.451   28.244  1.00 7.14  ? 177  TYR   A CG  1 
ATOM   1062 C  CD1 . TYR   A 1 154 ? -9.229  4.732   27.993  1.00 6.43  ? 177  TYR   A CD1 1 
ATOM   1063 C  CD2 . TYR   A 1 154 ? -7.013  5.522   28.388  1.00 6.93  ? 177  TYR   A CD2 1 
ATOM   1064 C  CE1 . TYR   A 1 154 ? -9.690  6.034   27.937  1.00 6.66  ? 177  TYR   A CE1 1 
ATOM   1065 C  CE2 . TYR   A 1 154 ? -7.475  6.832   28.335  1.00 6.74  ? 177  TYR   A CE2 1 
ATOM   1066 C  CZ  . TYR   A 1 154 ? -8.807  7.090   28.067  1.00 6.68  ? 177  TYR   A CZ  1 
ATOM   1067 O  OH  . TYR   A 1 154 ? -9.236  8.398   28.007  1.00 7.26  ? 177  TYR   A OH  1 
ATOM   1068 N  N   . ASP   A 1 155 ? -6.318  0.481   30.448  1.00 8.41  ? 178  ASP   A N   1 
ATOM   1069 C  CA  . ASP   A 1 155 ? -5.848  -0.894  30.401  1.00 9.85  ? 178  ASP   A CA  1 
ATOM   1070 C  C   . ASP   A 1 155 ? -6.191  -1.582  31.712  1.00 9.42  ? 178  ASP   A C   1 
ATOM   1071 O  O   . ASP   A 1 155 ? -6.131  -0.954  32.769  1.00 8.93  ? 178  ASP   A O   1 
ATOM   1072 C  CB  . ASP   A 1 155 ? -4.355  -0.999  30.112  1.00 10.28 ? 178  ASP   A CB  1 
ATOM   1073 C  CG  . ASP   A 1 155 ? -3.488  -0.399  31.206  1.00 11.83 ? 178  ASP   A CG  1 
ATOM   1074 O  OD1 . ASP   A 1 155 ? -3.623  0.812   31.442  1.00 12.13 ? 178  ASP   A OD1 1 
ATOM   1075 O  OD2 . ASP   A 1 155 ? -2.756  -1.156  31.886  1.00 11.49 ? 178  ASP   A OD2 1 
ATOM   1076 N  N   . ALA   A 1 156 ? -6.604  -2.861  31.567  1.00 8.50  ? 179  ALA   A N   1 
ATOM   1077 C  CA  . ALA   A 1 156 ? -6.896  -3.714  32.697  1.00 8.76  ? 179  ALA   A CA  1 
ATOM   1078 C  C   . ALA   A 1 156 ? -5.624  -4.120  33.420  1.00 8.87  ? 179  ALA   A C   1 
ATOM   1079 O  O   . ALA   A 1 156 ? -4.555  -4.154  32.821  1.00 8.69  ? 179  ALA   A O   1 
ATOM   1080 C  CB  . ALA   A 1 156 ? -7.602  -4.957  32.233  1.00 8.58  ? 179  ALA   A CB  1 
ATOM   1081 N  N   . PHE   A 1 157 ? -5.782  -4.402  34.727  1.00 8.45  ? 180  PHE   A N   1 
ATOM   1082 C  CA  . PHE   A 1 157 ? -4.655  -4.741  35.585  1.00 8.85  ? 180  PHE   A CA  1 
ATOM   1083 C  C   . PHE   A 1 157 ? -5.171  -5.597  36.731  1.00 9.34  ? 180  PHE   A C   1 
ATOM   1084 O  O   . PHE   A 1 157 ? -6.365  -5.653  36.986  1.00 8.92  ? 180  PHE   A O   1 
ATOM   1085 C  CB  . PHE   A 1 157 ? -3.937  -3.452  36.001  1.00 8.75  ? 180  PHE   A CB  1 
ATOM   1086 C  CG  . PHE   A 1 157 ? -4.735  -2.436  36.805  1.00 9.01  ? 180  PHE   A CG  1 
ATOM   1087 C  CD1 . PHE   A 1 157 ? -5.541  -1.509  36.162  1.00 8.87  ? 180  PHE   A CD1 1 
ATOM   1088 C  CD2 . PHE   A 1 157 ? -4.676  -2.421  38.205  1.00 8.65  ? 180  PHE   A CD2 1 
ATOM   1089 C  CE1 . PHE   A 1 157 ? -6.274  -0.600  36.887  1.00 8.60  ? 180  PHE   A CE1 1 
ATOM   1090 C  CE2 . PHE   A 1 157 ? -5.384  -1.491  38.927  1.00 9.11  ? 180  PHE   A CE2 1 
ATOM   1091 C  CZ  . PHE   A 1 157 ? -6.193  -0.580  38.271  1.00 9.06  ? 180  PHE   A CZ  1 
ATOM   1092 N  N   . SER   A 1 158 ? -4.273  -6.337  37.373  1.00 10.62 ? 181  SER   A N   1 
ATOM   1093 C  CA  . SER   A 1 158 ? -4.716  -7.278  38.373  1.00 12.55 ? 181  SER   A CA  1 
ATOM   1094 C  C   . SER   A 1 158 ? -3.586  -7.509  39.362  1.00 11.48 ? 181  SER   A C   1 
ATOM   1095 O  O   . SER   A 1 158 ? -2.443  -7.192  39.077  1.00 11.29 ? 181  SER   A O   1 
ATOM   1096 C  CB  . SER   A 1 158 ? -5.196  -8.566  37.714  1.00 15.95 ? 181  SER   A CB  1 
ATOM   1097 O  OG  . SER   A 1 158 ? -4.064  -9.367  37.486  1.00 22.93 ? 181  SER   A OG  1 
ATOM   1098 N  N   . TYR   A 1 159 ? -3.961  -7.903  40.570  1.00 10.99 ? 182  TYR   A N   1 
ATOM   1099 C  CA  . TYR   A 1 159 ? -3.029  -8.320  41.604  1.00 10.17 ? 182  TYR   A CA  1 
ATOM   1100 C  C   . TYR   A 1 159 ? -3.364  -9.698  42.155  1.00 10.07 ? 182  TYR   A C   1 
ATOM   1101 O  O   . TYR   A 1 159 ? -4.520  -10.053 42.383  1.00 10.16 ? 182  TYR   A O   1 
ATOM   1102 C  CB  . TYR   A 1 159 ? -3.136  -7.335  42.757  1.00 10.84 ? 182  TYR   A CB  1 
ATOM   1103 C  CG  . TYR   A 1 159 ? -2.868  -5.900  42.350  1.00 10.86 ? 182  TYR   A CG  1 
ATOM   1104 C  CD1 . TYR   A 1 159 ? -1.574  -5.411  42.285  1.00 13.01 ? 182  TYR   A CD1 1 
ATOM   1105 C  CD2 . TYR   A 1 159 ? -3.918  -5.028  42.076  1.00 10.77 ? 182  TYR   A CD2 1 
ATOM   1106 C  CE1 . TYR   A 1 159 ? -1.310  -4.099  41.918  1.00 12.62 ? 182  TYR   A CE1 1 
ATOM   1107 C  CE2 . TYR   A 1 159 ? -3.664  -3.728  41.681  1.00 11.25 ? 182  TYR   A CE2 1 
ATOM   1108 C  CZ  . TYR   A 1 159 ? -2.365  -3.248  41.637  1.00 12.10 ? 182  TYR   A CZ  1 
ATOM   1109 O  OH  . TYR   A 1 159 ? -2.092  -1.950  41.304  1.00 12.35 ? 182  TYR   A OH  1 
ATOM   1110 N  N   . ASP   A 1 160 ? -2.313  -10.444 42.455  1.00 9.79  ? 183  ASP   A N   1 
ATOM   1111 C  CA  . ASP   A 1 160 ? -2.510  -11.698 43.142  1.00 9.87  ? 183  ASP   A CA  1 
ATOM   1112 C  C   . ASP   A 1 160 ? -2.556  -11.377 44.640  1.00 10.00 ? 183  ASP   A C   1 
ATOM   1113 O  O   . ASP   A 1 160 ? -1.529  -11.026 45.212  1.00 10.86 ? 183  ASP   A O   1 
ATOM   1114 C  CB  . ASP   A 1 160 ? -1.409  -12.674 42.759  1.00 9.86  ? 183  ASP   A CB  1 
ATOM   1115 C  CG  . ASP   A 1 160 ? -1.600  -14.029 43.421  1.00 10.98 ? 183  ASP   A CG  1 
ATOM   1116 O  OD1 . ASP   A 1 160 ? -2.039  -14.045 44.592  1.00 11.07 ? 183  ASP   A OD1 1 
ATOM   1117 O  OD2 . ASP   A 1 160 ? -1.302  -15.046 42.765  1.00 11.90 ? 183  ASP   A OD2 1 
ATOM   1118 N  N   . VAL   A 1 161 ? -3.735  -11.492 45.253  1.00 10.25 ? 184  VAL   A N   1 
ATOM   1119 C  CA  . VAL   A 1 161 ? -3.957  -11.038 46.620  1.00 10.53 ? 184  VAL   A CA  1 
ATOM   1120 C  C   . VAL   A 1 161 ? -4.060  -12.184 47.622  1.00 11.09 ? 184  VAL   A C   1 
ATOM   1121 O  O   . VAL   A 1 161 ? -4.379  -11.936 48.790  1.00 11.29 ? 184  VAL   A O   1 
ATOM   1122 C  CB  . VAL   A 1 161 ? -5.194  -10.137 46.721  1.00 10.96 ? 184  VAL   A CB  1 
ATOM   1123 C  CG1 . VAL   A 1 161 ? -5.019  -8.846  45.906  1.00 10.89 ? 184  VAL   A CG1 1 
ATOM   1124 C  CG2 . VAL   A 1 161 ? -6.507  -10.846 46.396  1.00 12.53 ? 184  VAL   A CG2 1 
ATOM   1125 N  N   . THR   A 1 162 ? -3.758  -13.407 47.179  1.00 10.66 ? 185  THR   A N   1 
ATOM   1126 C  CA  . THR   A 1 162 ? -3.906  -14.620 47.973  1.00 11.00 ? 185  THR   A CA  1 
ATOM   1127 C  C   . THR   A 1 162 ? -3.342  -14.431 49.390  1.00 11.04 ? 185  THR   A C   1 
ATOM   1128 O  O   . THR   A 1 162 ? -4.020  -14.738 50.355  1.00 11.55 ? 185  THR   A O   1 
ATOM   1129 C  CB  . THR   A 1 162 ? -3.146  -15.750 47.300  1.00 11.76 ? 185  THR   A CB  1 
ATOM   1130 O  OG1 . THR   A 1 162 ? -3.539  -15.826 45.937  1.00 9.87  ? 185  THR   A OG1 1 
ATOM   1131 C  CG2 . THR   A 1 162 ? -3.442  -17.094 47.954  1.00 12.03 ? 185  THR   A CG2 1 
ATOM   1132 N  N   . ASP   A 1 163 ? -2.117  -13.926 49.482  1.00 12.37 ? 186  ASP   A N   1 
ATOM   1133 C  CA  . ASP   A 1 163 ? -1.372  -13.921 50.736  1.00 14.78 ? 186  ASP   A CA  1 
ATOM   1134 C  C   . ASP   A 1 163 ? -1.879  -12.854 51.703  1.00 14.02 ? 186  ASP   A C   1 
ATOM   1135 O  O   . ASP   A 1 163 ? -1.552  -12.920 52.899  1.00 12.35 ? 186  ASP   A O   1 
ATOM   1136 C  CB  . ASP   A 1 163 ? 0.114   -13.732 50.498  1.00 17.10 ? 186  ASP   A CB  1 
ATOM   1137 C  CG  . ASP   A 1 163 ? 0.745   -14.795 49.617  1.00 20.96 ? 186  ASP   A CG  1 
ATOM   1138 O  OD1 . ASP   A 1 163 ? 0.465   -15.986 49.846  1.00 25.27 ? 186  ASP   A OD1 1 
ATOM   1139 O  OD2 . ASP   A 1 163 ? 1.545   -14.414 48.743  1.00 30.58 ? 186  ASP   A OD2 1 
ATOM   1140 N  N   . LEU   A 1 164 ? -2.718  -11.940 51.197  1.00 12.56 ? 187  LEU   A N   1 
ATOM   1141 C  CA  . LEU   A 1 164 ? -3.196  -10.804 51.979  1.00 13.25 ? 187  LEU   A CA  1 
ATOM   1142 C  C   . LEU   A 1 164 ? -4.575  -11.046 52.577  1.00 11.82 ? 187  LEU   A C   1 
ATOM   1143 O  O   . LEU   A 1 164 ? -5.031  -10.213 53.364  1.00 12.79 ? 187  LEU   A O   1 
ATOM   1144 C  CB  . LEU   A 1 164 ? -3.208  -9.564  51.080  1.00 12.47 ? 187  LEU   A CB  1 
ATOM   1145 C  CG  . LEU   A 1 164 ? -1.869  -9.164  50.458  1.00 13.33 ? 187  LEU   A CG  1 
ATOM   1146 C  CD1 . LEU   A 1 164 ? -2.019  -7.878  49.639  1.00 13.96 ? 187  LEU   A CD1 1 
ATOM   1147 C  CD2 . LEU   A 1 164 ? -0.758  -9.020  51.504  1.00 15.72 ? 187  LEU   A CD2 1 
ATOM   1148 N  N   . LEU   A 1 165 ? -5.254  -12.114 52.154  1.00 10.97 ? 188  LEU   A N   1 
ATOM   1149 C  CA  . LEU   A 1 165 ? -6.625  -12.387 52.521  1.00 12.38 ? 188  LEU   A CA  1 
ATOM   1150 C  C   . LEU   A 1 165 ? -6.732  -13.000 53.915  1.00 13.26 ? 188  LEU   A C   1 
ATOM   1151 O  O   . LEU   A 1 165 ? -5.851  -13.752 54.334  1.00 13.19 ? 188  LEU   A O   1 
ATOM   1152 C  CB  . LEU   A 1 165 ? -7.225  -13.353 51.504  1.00 12.50 ? 188  LEU   A CB  1 
ATOM   1153 C  CG  . LEU   A 1 165 ? -7.273  -12.829 50.064  1.00 12.00 ? 188  LEU   A CG  1 
ATOM   1154 C  CD1 . LEU   A 1 165 ? -7.700  -13.910 49.089  1.00 13.24 ? 188  LEU   A CD1 1 
ATOM   1155 C  CD2 . LEU   A 1 165 ? -8.235  -11.663 49.975  1.00 12.63 ? 188  LEU   A CD2 1 
ATOM   1156 N  N   . THR   A 1 166 ? -7.901  -12.804 54.522  1.00 13.69 ? 189  THR   A N   1 
ATOM   1157 C  CA  . THR   A 1 166 ? -8.289  -13.577 55.697  1.00 17.12 ? 189  THR   A CA  1 
ATOM   1158 C  C   . THR   A 1 166 ? -9.480  -14.452 55.335  1.00 17.62 ? 189  THR   A C   1 
ATOM   1159 O  O   . THR   A 1 166 ? -10.118 -14.252 54.306  1.00 17.20 ? 189  THR   A O   1 
ATOM   1160 C  CB  . THR   A 1 166 ? -8.620  -12.618 56.836  1.00 18.93 ? 189  THR   A CB  1 
ATOM   1161 O  OG1 . THR   A 1 166 ? -8.889  -13.309 58.055  1.00 26.96 ? 189  THR   A OG1 1 
ATOM   1162 C  CG2 . THR   A 1 166 ? -9.909  -11.871 56.577  1.00 18.72 ? 189  THR   A CG2 1 
ATOM   1163 N  N   . ALA   A 1 167 ? -9.782  -15.414 56.210  1.00 16.41 ? 190  ALA   A N   1 
ATOM   1164 C  CA  . ALA   A 1 167 ? -10.963 -16.250 56.070  1.00 18.02 ? 190  ALA   A CA  1 
ATOM   1165 C  C   . ALA   A 1 167 ? -12.206 -15.502 56.536  1.00 21.16 ? 190  ALA   A C   1 
ATOM   1166 O  O   . ALA   A 1 167 ? -13.319 -15.990 56.394  1.00 27.71 ? 190  ALA   A O   1 
ATOM   1167 C  CB  . ALA   A 1 167 ? -10.760 -17.539 56.841  1.00 17.87 ? 190  ALA   A CB  1 
ATOM   1168 N  N   . GLY   A 1 168 ? -12.009 -14.344 57.154  1.00 20.40 ? 191  GLY   A N   1 
ATOM   1169 C  CA  . GLY   A 1 168 ? -13.116 -13.547 57.641  1.00 23.70 ? 191  GLY   A CA  1 
ATOM   1170 C  C   . GLY   A 1 168 ? -13.540 -12.486 56.630  1.00 19.51 ? 191  GLY   A C   1 
ATOM   1171 O  O   . GLY   A 1 168 ? -13.488 -12.674 55.418  1.00 18.98 ? 191  GLY   A O   1 
ATOM   1172 N  N   . THR   A 1 169 ? -13.919 -11.352 57.192  1.00 20.82 ? 192  THR   A N   1 
ATOM   1173 C  CA  . THR   A 1 169 ? -14.230 -10.167 56.430  1.00 17.84 ? 192  THR   A CA  1 
ATOM   1174 C  C   . THR   A 1 169 ? -12.917 -9.518  56.026  1.00 15.68 ? 192  THR   A C   1 
ATOM   1175 O  O   . THR   A 1 169 ? -12.109 -9.206  56.887  1.00 14.65 ? 192  THR   A O   1 
ATOM   1176 C  CB  . THR   A 1 169 ? -15.064 -9.219  57.287  1.00 20.12 ? 192  THR   A CB  1 
ATOM   1177 O  OG1 . THR   A 1 169 ? -16.178 -10.032 57.637  1.00 20.18 ? 192  THR   A OG1 1 
ATOM   1178 C  CG2 . THR   A 1 169 ? -15.492 -7.987  56.502  1.00 19.29 ? 192  THR   A CG2 1 
ATOM   1179 N  N   . ASN   A 1 170 ? -12.732 -9.329  54.714  1.00 12.52 ? 193  ASN   A N   1 
ATOM   1180 C  CA  . ASN   A 1 170 ? -11.591 -8.620  54.175  1.00 11.39 ? 193  ASN   A CA  1 
ATOM   1181 C  C   . ASN   A 1 170 ? -12.001 -7.181  53.864  1.00 10.70 ? 193  ASN   A C   1 
ATOM   1182 O  O   . ASN   A 1 170 ? -13.180 -6.902  53.639  1.00 13.10 ? 193  ASN   A O   1 
ATOM   1183 C  CB  . ASN   A 1 170 ? -11.126 -9.275  52.878  1.00 11.84 ? 193  ASN   A CB  1 
ATOM   1184 C  CG  . ASN   A 1 170 ? -10.595 -10.674 53.087  1.00 11.15 ? 193  ASN   A CG  1 
ATOM   1185 O  OD1 . ASN   A 1 170 ? -9.391  -10.832 53.296  1.00 11.20 ? 193  ASN   A OD1 1 
ATOM   1186 N  ND2 . ASN   A 1 170 ? -11.456 -11.680 53.037  1.00 12.44 ? 193  ASN   A ND2 1 
ATOM   1187 N  N   . THR   A 1 171 ? -11.023 -6.280  53.892  1.00 11.27 ? 194  THR   A N   1 
ATOM   1188 C  CA  . THR   A 1 171 ? -11.219 -4.906  53.480  1.00 11.43 ? 194  THR   A CA  1 
ATOM   1189 C  C   . THR   A 1 171 ? -10.355 -4.644  52.249  1.00 11.04 ? 194  THR   A C   1 
ATOM   1190 O  O   . THR   A 1 171 ? -9.180  -5.015  52.215  1.00 11.53 ? 194  THR   A O   1 
ATOM   1191 C  CB  . THR   A 1 171 ? -10.841 -3.984  54.641  1.00 13.01 ? 194  THR   A CB  1 
ATOM   1192 O  OG1 . THR   A 1 171 ? -11.722 -4.286  55.728  1.00 13.20 ? 194  THR   A OG1 1 
ATOM   1193 C  CG2 . THR   A 1 171 ? -10.920 -2.518  54.252  1.00 14.94 ? 194  THR   A CG2 1 
ATOM   1194 N  N   . LEU   A 1 172 ? -10.959 -3.981  51.259  1.00 10.44 ? 195  LEU   A N   1 
ATOM   1195 C  CA  . LEU   A 1 172 ? -10.300 -3.478  50.061  1.00 10.03 ? 195  LEU   A CA  1 
ATOM   1196 C  C   . LEU   A 1 172 ? -10.382 -1.954  50.046  1.00 9.28  ? 195  LEU   A C   1 
ATOM   1197 O  O   . LEU   A 1 172 ? -11.490 -1.423  50.120  1.00 9.92  ? 195  LEU   A O   1 
ATOM   1198 C  CB  . LEU   A 1 172 ? -11.036 -4.041  48.843  1.00 9.26  ? 195  LEU   A CB  1 
ATOM   1199 C  CG  . LEU   A 1 172 ? -10.549 -3.584  47.454  1.00 10.08 ? 195  LEU   A CG  1 
ATOM   1200 C  CD1 . LEU   A 1 172 ? -9.059  -3.691  47.252  1.00 10.40 ? 195  LEU   A CD1 1 
ATOM   1201 C  CD2 . LEU   A 1 172 ? -11.304 -4.328  46.348  1.00 10.56 ? 195  LEU   A CD2 1 
ATOM   1202 N  N   . VAL   A 1 173 ? -9.217  -1.295  50.014  1.00 9.31  ? 196  VAL   A N   1 
ATOM   1203 C  CA  . VAL   A 1 173 ? -9.109  0.152   49.875  1.00 9.60  ? 196  VAL   A CA  1 
ATOM   1204 C  C   . VAL   A 1 173 ? -8.366  0.483   48.576  1.00 8.76  ? 196  VAL   A C   1 
ATOM   1205 O  O   . VAL   A 1 173 ? -7.309  -0.080  48.303  1.00 8.42  ? 196  VAL   A O   1 
ATOM   1206 C  CB  . VAL   A 1 173 ? -8.400  0.797   51.082  1.00 9.52  ? 196  VAL   A CB  1 
ATOM   1207 C  CG1 . VAL   A 1 173 ? -8.138  2.292   50.825  1.00 9.54  ? 196  VAL   A CG1 1 
ATOM   1208 C  CG2 . VAL   A 1 173 ? -9.194  0.549   52.353  1.00 9.47  ? 196  VAL   A CG2 1 
ATOM   1209 N  N   . VAL   A 1 174 ? -8.913  1.399   47.789  1.00 8.72  ? 197  VAL   A N   1 
ATOM   1210 C  CA  . VAL   A 1 174 ? -8.304  1.825   46.551  1.00 8.43  ? 197  VAL   A CA  1 
ATOM   1211 C  C   . VAL   A 1 174 ? -8.238  3.355   46.518  1.00 8.02  ? 197  VAL   A C   1 
ATOM   1212 O  O   . VAL   A 1 174 ? -9.283  4.015   46.689  1.00 9.11  ? 197  VAL   A O   1 
ATOM   1213 C  CB  . VAL   A 1 174 ? -9.137  1.286   45.372  1.00 8.87  ? 197  VAL   A CB  1 
ATOM   1214 C  CG1 . VAL   A 1 174 ? -8.504  1.677   44.067  1.00 8.58  ? 197  VAL   A CG1 1 
ATOM   1215 C  CG2 . VAL   A 1 174 ? -9.359  -0.250  45.447  1.00 9.27  ? 197  VAL   A CG2 1 
ATOM   1216 N  N   . SER   A 1 175 ? -7.058  3.903   46.229  1.00 8.05  ? 198  SER   A N   1 
ATOM   1217 C  CA  . SER   A 1 175 ? -6.946  5.326   45.942  1.00 8.20  ? 198  SER   A CA  1 
ATOM   1218 C  C   . SER   A 1 175 ? -6.781  5.479   44.433  1.00 7.50  ? 198  SER   A C   1 
ATOM   1219 O  O   . SER   A 1 175 ? -6.114  4.685   43.768  1.00 7.66  ? 198  SER   A O   1 
ATOM   1220 C  CB  . SER   A 1 175 ? -5.820  6.040   46.713  1.00 8.54  ? 198  SER   A CB  1 
ATOM   1221 O  OG  . SER   A 1 175 ? -4.517  5.698   46.240  1.00 8.96  ? 198  SER   A OG  1 
ATOM   1222 N  N   . VAL   A 1 176 ? -7.406  6.539   43.899  1.00 7.98  ? 199  VAL   A N   1 
ATOM   1223 C  CA  . VAL   A 1 176 ? -7.276  6.885   42.488  1.00 8.54  ? 199  VAL   A CA  1 
ATOM   1224 C  C   . VAL   A 1 176 ? -7.089  8.392   42.349  1.00 8.88  ? 199  VAL   A C   1 
ATOM   1225 O  O   . VAL   A 1 176 ? -7.984  9.136   42.728  1.00 8.62  ? 199  VAL   A O   1 
ATOM   1226 C  CB  . VAL   A 1 176 ? -8.463  6.429   41.633  1.00 8.52  ? 199  VAL   A CB  1 
ATOM   1227 C  CG1 . VAL   A 1 176 ? -8.125  6.540   40.135  1.00 8.97  ? 199  VAL   A CG1 1 
ATOM   1228 C  CG2 . VAL   A 1 176 ? -8.878  5.010   41.999  1.00 8.63  ? 199  VAL   A CG2 1 
ATOM   1229 N  N   . TRP   A 1 177 ? -5.939  8.749   41.752  1.00 9.70  ? 200  TRP   A N   1 
ATOM   1230 C  CA  . TRP   A 1 177 ? -5.604  10.112  41.386  1.00 9.88  ? 200  TRP   A CA  1 
ATOM   1231 C  C   . TRP   A 1 177 ? -5.773  10.249  39.878  1.00 10.10 ? 200  TRP   A C   1 
ATOM   1232 O  O   . TRP   A 1 177 ? -5.364  9.366   39.118  1.00 10.64 ? 200  TRP   A O   1 
ATOM   1233 C  CB  . TRP   A 1 177 ? -4.170  10.444  41.800  1.00 10.14 ? 200  TRP   A CB  1 
ATOM   1234 C  CG  . TRP   A 1 177 ? -3.726  11.816  41.396  1.00 10.53 ? 200  TRP   A CG  1 
ATOM   1235 C  CD1 . TRP   A 1 177 ? -4.162  13.000  41.921  1.00 11.05 ? 200  TRP   A CD1 1 
ATOM   1236 C  CD2 . TRP   A 1 177 ? -2.696  12.150  40.442  1.00 10.27 ? 200  TRP   A CD2 1 
ATOM   1237 N  NE1 . TRP   A 1 177 ? -3.534  14.051  41.318  1.00 10.15 ? 200  TRP   A NE1 1 
ATOM   1238 C  CE2 . TRP   A 1 177 ? -2.601  13.564  40.446  1.00 10.39 ? 200  TRP   A CE2 1 
ATOM   1239 C  CE3 . TRP   A 1 177 ? -1.852  11.403  39.607  1.00 10.59 ? 200  TRP   A CE3 1 
ATOM   1240 C  CZ2 . TRP   A 1 177 ? -1.699  14.245  39.635  1.00 11.01 ? 200  TRP   A CZ2 1 
ATOM   1241 C  CZ3 . TRP   A 1 177 ? -0.950  12.083  38.808  1.00 11.51 ? 200  TRP   A CZ3 1 
ATOM   1242 C  CH2 . TRP   A 1 177 ? -0.890  13.488  38.810  1.00 11.75 ? 200  TRP   A CH2 1 
ATOM   1243 N  N   . ASP   A 1 178 ? -6.411  11.349  39.448  1.00 9.14  ? 201  ASP   A N   1 
ATOM   1244 C  CA  . ASP   A 1 178 ? -6.526  11.613  38.026  1.00 8.62  ? 201  ASP   A CA  1 
ATOM   1245 C  C   . ASP   A 1 178 ? -6.366  13.110  37.796  1.00 8.82  ? 201  ASP   A C   1 
ATOM   1246 O  O   . ASP   A 1 178 ? -7.199  13.860  38.260  1.00 9.40  ? 201  ASP   A O   1 
ATOM   1247 C  CB  . ASP   A 1 178 ? -7.883  11.148  37.537  1.00 8.81  ? 201  ASP   A CB  1 
ATOM   1248 C  CG  . ASP   A 1 178 ? -8.040  11.163  36.035  1.00 8.88  ? 201  ASP   A CG  1 
ATOM   1249 O  OD1 . ASP   A 1 178 ? -7.238  11.887  35.366  1.00 8.78  ? 201  ASP   A OD1 1 
ATOM   1250 O  OD2 . ASP   A 1 178 ? -8.950  10.427  35.571  1.00 8.75  ? 201  ASP   A OD2 1 
ATOM   1251 N  N   . PRO   A 1 179 ? -5.303  13.567  37.113  1.00 9.69  ? 202  PRO   A N   1 
ATOM   1252 C  CA  . PRO   A 1 179 ? -5.081  14.980  36.836  1.00 9.93  ? 202  PRO   A CA  1 
ATOM   1253 C  C   . PRO   A 1 179 ? -5.820  15.479  35.596  1.00 9.81  ? 202  PRO   A C   1 
ATOM   1254 O  O   . PRO   A 1 179 ? -5.695  16.646  35.247  1.00 9.28  ? 202  PRO   A O   1 
ATOM   1255 C  CB  . PRO   A 1 179 ? -3.557  15.003  36.641  1.00 9.83  ? 202  PRO   A CB  1 
ATOM   1256 C  CG  . PRO   A 1 179 ? -3.274  13.696  35.904  1.00 9.46  ? 202  PRO   A CG  1 
ATOM   1257 C  CD  . PRO   A 1 179 ? -4.216  12.721  36.596  1.00 10.38 ? 202  PRO   A CD  1 
ATOM   1258 N  N   . THR   A 1 180 ? -6.495  14.562  34.882  1.00 9.06  ? 203  THR   A N   1 
ATOM   1259 C  CA  . THR   A 1 180 ? -7.080  14.838  33.574  1.00 9.19  ? 203  THR   A CA  1 
ATOM   1260 C  C   . THR   A 1 180 ? -6.055  15.619  32.740  1.00 9.59  ? 203  THR   A C   1 
ATOM   1261 O  O   . THR   A 1 180 ? -4.897  15.188  32.632  1.00 9.54  ? 203  THR   A O   1 
ATOM   1262 C  CB  . THR   A 1 180 ? -8.476  15.464  33.716  1.00 8.86  ? 203  THR   A CB  1 
ATOM   1263 O  OG1 . THR   A 1 180 ? -9.211  14.878  34.794  1.00 8.68  ? 203  THR   A OG1 1 
ATOM   1264 C  CG2 . THR   A 1 180 ? -9.305  15.244  32.461  1.00 8.91  ? 203  THR   A CG2 1 
ATOM   1265 N  N   . GLU   A 1 181 ? -6.487  16.666  32.018  1.00 9.49  ? 204  GLU   A N   1 
ATOM   1266 C  CA  . GLU   A 1 181 ? -5.602  17.274  31.032  1.00 9.59  ? 204  GLU   A CA  1 
ATOM   1267 C  C   . GLU   A 1 181 ? -4.437  18.043  31.677  1.00 9.12  ? 204  GLU   A C   1 
ATOM   1268 O  O   . GLU   A 1 181 ? -3.528  18.475  30.958  1.00 9.11  ? 204  GLU   A O   1 
ATOM   1269 C  CB  . GLU   A 1 181 ? -6.419  18.171  30.103  1.00 11.02 ? 204  GLU   A CB  1 
ATOM   1270 C  CG  . GLU   A 1 181 ? -6.782  19.525  30.717  1.00 12.00 ? 204  GLU   A CG  1 
ATOM   1271 C  CD  . GLU   A 1 181 ? -8.024  19.529  31.588  1.00 12.96 ? 204  GLU   A CD  1 
ATOM   1272 O  OE1 . GLU   A 1 181 ? -8.550  18.489  32.030  1.00 10.91 ? 204  GLU   A OE1 1 
ATOM   1273 O  OE2 . GLU   A 1 181 ? -8.583  20.633  31.788  1.00 17.56 ? 204  GLU   A OE2 1 
ATOM   1274 N  N   . THR   A 1 182 ? -4.425  18.241  33.010  1.00 9.65  ? 205  THR   A N   1 
ATOM   1275 C  CA  . THR   A 1 182 ? -3.261  18.872  33.639  1.00 10.16 ? 205  THR   A CA  1 
ATOM   1276 C  C   . THR   A 1 182 ? -2.069  17.924  33.657  1.00 10.83 ? 205  THR   A C   1 
ATOM   1277 O  O   . THR   A 1 182 ? -0.938  18.376  33.790  1.00 10.64 ? 205  THR   A O   1 
ATOM   1278 C  CB  . THR   A 1 182 ? -3.551  19.398  35.047  1.00 10.63 ? 205  THR   A CB  1 
ATOM   1279 O  OG1 . THR   A 1 182 ? -3.703  18.363  36.022  1.00 11.96 ? 205  THR   A OG1 1 
ATOM   1280 C  CG2 . THR   A 1 182 ? -4.738  20.347  35.057  1.00 10.73 ? 205  THR   A CG2 1 
ATOM   1281 N  N   . GLY   A 1 183 ? -2.331  16.605  33.525  1.00 11.35 ? 206  GLY   A N   1 
ATOM   1282 C  CA  . GLY   A 1 183 ? -1.277  15.611  33.385  1.00 11.13 ? 206  GLY   A CA  1 
ATOM   1283 C  C   . GLY   A 1 183 ? -0.800  15.467  31.941  1.00 11.49 ? 206  GLY   A C   1 
ATOM   1284 O  O   . GLY   A 1 183 ? -1.355  16.078  31.018  1.00 12.75 ? 206  GLY   A O   1 
ATOM   1285 N  N   . THR   A 1 184 ? 0.257   14.651  31.762  1.00 11.50 ? 207  THR   A N   1 
ATOM   1286 C  CA  . THR   A 1 184 ? 0.881   14.426  30.462  1.00 10.83 ? 207  THR   A CA  1 
ATOM   1287 C  C   . THR   A 1 184 ? 0.410   13.083  29.888  1.00 10.45 ? 207  THR   A C   1 
ATOM   1288 O  O   . THR   A 1 184 ? 1.023   12.555  28.947  1.00 11.18 ? 207  THR   A O   1 
ATOM   1289 C  CB  . THR   A 1 184 ? 2.407   14.462  30.590  1.00 13.60 ? 207  THR   A CB  1 
ATOM   1290 O  OG1 . THR   A 1 184 ? 2.840   13.524  31.568  1.00 13.11 ? 207  THR   A OG1 1 
ATOM   1291 C  CG2 . THR   A 1 184 ? 2.955   15.832  30.955  1.00 14.86 ? 207  THR   A CG2 1 
ATOM   1292 N  N   . GLN   A 1 185 ? -0.626  12.505  30.486  1.00 9.99  ? 208  GLN   A N   1 
ATOM   1293 C  CA  . GLN   A 1 185 ? -1.061  11.150  30.154  1.00 9.20  ? 208  GLN   A CA  1 
ATOM   1294 C  C   . GLN   A 1 185 ? -2.216  11.113  29.142  1.00 9.20  ? 208  GLN   A C   1 
ATOM   1295 O  O   . GLN   A 1 185 ? -2.880  12.112  28.870  1.00 8.99  ? 208  GLN   A O   1 
ATOM   1296 C  CB  . GLN   A 1 185 ? -1.477  10.441  31.446  1.00 9.06  ? 208  GLN   A CB  1 
ATOM   1297 C  CG  . GLN   A 1 185 ? -2.920  10.633  31.865  1.00 9.36  ? 208  GLN   A CG  1 
ATOM   1298 C  CD  . GLN   A 1 185 ? -3.217  12.008  32.412  1.00 9.76  ? 208  GLN   A CD  1 
ATOM   1299 O  OE1 . GLN   A 1 185 ? -2.309  12.825  32.627  1.00 10.81 ? 208  GLN   A OE1 1 
ATOM   1300 N  NE2 . GLN   A 1 185 ? -4.496  12.239  32.692  1.00 9.81  ? 208  GLN   A NE2 1 
ATOM   1301 N  N   . ALA   A 1 186 ? -2.445  9.920   28.568  1.00 8.62  ? 209  ALA   A N   1 
ATOM   1302 C  CA  . ALA   A 1 186 ? -3.588  9.689   27.686  1.00 9.24  ? 209  ALA   A CA  1 
ATOM   1303 C  C   . ALA   A 1 186 ? -4.902  10.088  28.364  1.00 8.58  ? 209  ALA   A C   1 
ATOM   1304 O  O   . ALA   A 1 186 ? -5.220  9.560   29.429  1.00 8.35  ? 209  ALA   A O   1 
ATOM   1305 C  CB  . ALA   A 1 186 ? -3.638  8.237   27.301  1.00 9.60  ? 209  ALA   A CB  1 
ATOM   1306 N  N   . VAL   A 1 187 ? -5.657  11.030  27.747  1.00 8.79  ? 210  VAL   A N   1 
ATOM   1307 C  CA  . VAL   A 1 187 ? -6.883  11.596  28.304  1.00 9.64  ? 210  VAL   A CA  1 
ATOM   1308 C  C   . VAL   A 1 187 ? -8.057  11.598  27.332  1.00 9.14  ? 210  VAL   A C   1 
ATOM   1309 O  O   . VAL   A 1 187 ? -9.206  11.704  27.744  1.00 8.42  ? 210  VAL   A O   1 
ATOM   1310 C  CB  . VAL   A 1 187 ? -6.688  13.048  28.787  1.00 11.62 ? 210  VAL   A CB  1 
ATOM   1311 C  CG1 . VAL   A 1 187 ? -5.866  13.059  30.057  1.00 15.33 ? 210  VAL   A CG1 1 
ATOM   1312 C  CG2 . VAL   A 1 187 ? -6.115  13.970  27.711  1.00 10.84 ? 210  VAL   A CG2 1 
ATOM   1313 N  N   . GLY   A 1 188 ? -7.766  11.608  26.034  1.00 8.90  ? 211  GLY   A N   1 
ATOM   1314 C  CA  . GLY   A 1 188 ? -8.825  11.655  25.039  1.00 8.80  ? 211  GLY   A CA  1 
ATOM   1315 C  C   . GLY   A 1 188 ? -9.644  12.934  25.187  1.00 8.70  ? 211  GLY   A C   1 
ATOM   1316 O  O   . GLY   A 1 188 ? -9.064  14.022  25.225  1.00 9.44  ? 211  GLY   A O   1 
ATOM   1317 N  N   . LYS   A 1 189 ? -10.970 12.780  25.249  1.00 8.28  ? 212  LYS   A N   1 
ATOM   1318 C  CA  . LYS   A 1 189 ? -11.920 13.898  25.283  1.00 8.06  ? 212  LYS   A CA  1 
ATOM   1319 C  C   . LYS   A 1 189 ? -12.166 14.448  26.701  1.00 8.23  ? 212  LYS   A C   1 
ATOM   1320 O  O   . LYS   A 1 189 ? -12.871 15.456  26.869  1.00 9.13  ? 212  LYS   A O   1 
ATOM   1321 C  CB  . LYS   A 1 189 ? -13.255 13.476  24.643  1.00 8.42  ? 212  LYS   A CB  1 
ATOM   1322 C  CG  . LYS   A 1 189 ? -13.234 13.288  23.139  1.00 7.64  ? 212  LYS   A CG  1 
ATOM   1323 C  CD  . LYS   A 1 189 ? -12.610 14.519  22.449  1.00 7.99  ? 212  LYS   A CD  1 
ATOM   1324 C  CE  . LYS   A 1 189 ? -12.864 14.594  20.958  1.00 8.31  ? 212  LYS   A CE  1 
ATOM   1325 N  NZ  . LYS   A 1 189 ? -14.267 14.920  20.680  1.00 8.60  ? 212  LYS   A NZ  1 
ATOM   1326 N  N   . GLN   A 1 190 ? -11.569 13.848  27.722  1.00 7.69  ? 213  GLN   A N   1 
ATOM   1327 C  CA  . GLN   A 1 190 ? -11.861 14.207  29.091  1.00 7.66  ? 213  GLN   A CA  1 
ATOM   1328 C  C   . GLN   A 1 190 ? -11.244 15.558  29.429  1.00 8.15  ? 213  GLN   A C   1 
ATOM   1329 O  O   . GLN   A 1 190 ? -10.070 15.770  29.156  1.00 8.10  ? 213  GLN   A O   1 
ATOM   1330 C  CB  . GLN   A 1 190 ? -11.217 13.243  30.061  1.00 7.49  ? 213  GLN   A CB  1 
ATOM   1331 C  CG  . GLN   A 1 190 ? -11.717 11.810  29.966  1.00 7.29  ? 213  GLN   A CG  1 
ATOM   1332 C  CD  . GLN   A 1 190 ? -10.930 10.994  30.937  1.00 7.62  ? 213  GLN   A CD  1 
ATOM   1333 O  OE1 . GLN   A 1 190 ? -11.089 11.185  32.133  1.00 7.29  ? 213  GLN   A OE1 1 
ATOM   1334 N  NE2 . GLN   A 1 190 ? -10.027 10.158  30.461  1.00 8.55  ? 213  GLN   A NE2 1 
ATOM   1335 N  N   . ARG   A 1 191 ? -12.040 16.445  30.034  1.00 9.66  ? 214  ARG   A N   1 
ATOM   1336 C  CA  . ARG   A 1 191 ? -11.513 17.702  30.565  1.00 10.23 ? 214  ARG   A CA  1 
ATOM   1337 C  C   . ARG   A 1 191 ? -12.161 18.004  31.908  1.00 9.75  ? 214  ARG   A C   1 
ATOM   1338 O  O   . ARG   A 1 191 ? -13.318 17.691  32.137  1.00 8.85  ? 214  ARG   A O   1 
ATOM   1339 C  CB  . ARG   A 1 191 ? -11.717 18.896  29.637  1.00 11.00 ? 214  ARG   A CB  1 
ATOM   1340 C  CG  . ARG   A 1 191 ? -10.923 18.824  28.341  1.00 11.02 ? 214  ARG   A CG  1 
ATOM   1341 C  CD  . ARG   A 1 191 ? -9.396  18.858  28.478  1.00 11.49 ? 214  ARG   A CD  1 
ATOM   1342 N  NE  . ARG   A 1 191 ? -8.666  18.844  27.212  1.00 11.90 ? 214  ARG   A NE  1 
ATOM   1343 C  CZ  . ARG   A 1 191 ? -8.496  17.794  26.441  1.00 11.30 ? 214  ARG   A CZ  1 
ATOM   1344 N  NH1 . ARG   A 1 191 ? -8.942  16.599  26.784  1.00 11.79 ? 214  ARG   A NH1 1 
ATOM   1345 N  NH2 . ARG   A 1 191 ? -7.817  17.952  25.349  1.00 11.51 ? 214  ARG   A NH2 1 
ATOM   1346 N  N   . ILE   A 1 192 ? -11.428 18.702  32.776  1.00 10.01 ? 215  ILE   A N   1 
ATOM   1347 C  CA  . ILE   A 1 192 ? -11.990 19.072  34.064  1.00 11.05 ? 215  ILE   A CA  1 
ATOM   1348 C  C   . ILE   A 1 192 ? -13.096 20.091  33.796  1.00 11.72 ? 215  ILE   A C   1 
ATOM   1349 O  O   . ILE   A 1 192 ? -12.822 21.207  33.325  1.00 11.46 ? 215  ILE   A O   1 
ATOM   1350 C  CB  . ILE   A 1 192 ? -10.882 19.590  34.993  1.00 11.34 ? 215  ILE   A CB  1 
ATOM   1351 C  CG1 . ILE   A 1 192 ? -9.870  18.457  35.274  1.00 12.24 ? 215  ILE   A CG1 1 
ATOM   1352 C  CG2 . ILE   A 1 192 ? -11.477 20.139  36.277  1.00 11.28 ? 215  ILE   A CG2 1 
ATOM   1353 C  CD1 . ILE   A 1 192 ? -8.587  18.875  35.964  1.00 11.67 ? 215  ILE   A CD1 1 
ATOM   1354 N  N   . ARG   A 1 193 ? -14.321 19.688  34.141  1.00 11.07 ? 216  ARG   A N   1 
ATOM   1355 C  CA  . ARG   A 1 193 ? -15.520 20.440  33.838  1.00 12.33 ? 216  ARG   A CA  1 
ATOM   1356 C  C   . ARG   A 1 193 ? -16.482 20.376  35.006  1.00 12.01 ? 216  ARG   A C   1 
ATOM   1357 O  O   . ARG   A 1 193 ? -16.635 19.326  35.647  1.00 10.49 ? 216  ARG   A O   1 
ATOM   1358 C  CB  . ARG   A 1 193 ? -16.227 19.859  32.616  1.00 12.60 ? 216  ARG   A CB  1 
ATOM   1359 C  CG  . ARG   A 1 193 ? -15.462 20.047  31.319  1.00 12.50 ? 216  ARG   A CG  1 
ATOM   1360 C  CD  . ARG   A 1 193 ? -15.554 21.498  30.853  1.00 13.36 ? 216  ARG   A CD  1 
ATOM   1361 N  NE  . ARG   A 1 193 ? -14.810 21.782  29.622  1.00 12.60 ? 216  ARG   A NE  1 
ATOM   1362 C  CZ  . ARG   A 1 193 ? -15.197 21.411  28.394  1.00 13.10 ? 216  ARG   A CZ  1 
ATOM   1363 N  NH1 . ARG   A 1 193 ? -16.322 20.754  28.224  1.00 13.05 ? 216  ARG   A NH1 1 
ATOM   1364 N  NH2 . ARG   A 1 193 ? -14.452 21.729  27.351  1.00 12.89 ? 216  ARG   A NH2 1 
ATOM   1365 N  N   . ASP   A 1 194 ? -17.131 21.524  35.273  1.00 12.28 ? 217  ASP   A N   1 
ATOM   1366 C  CA  . ASP   A 1 194 ? -18.292 21.482  36.135  1.00 13.71 ? 217  ASP   A CA  1 
ATOM   1367 C  C   . ASP   A 1 194 ? -19.294 20.500  35.548  1.00 14.16 ? 217  ASP   A C   1 
ATOM   1368 O  O   . ASP   A 1 194 ? -19.466 20.404  34.339  1.00 13.65 ? 217  ASP   A O   1 
ATOM   1369 C  CB  . ASP   A 1 194 ? -18.876 22.862  36.399  1.00 15.43 ? 217  ASP   A CB  1 
ATOM   1370 C  CG  . ASP   A 1 194 ? -18.025 23.669  37.365  1.00 17.62 ? 217  ASP   A CG  1 
ATOM   1371 O  OD1 . ASP   A 1 194 ? -17.742 23.158  38.473  1.00 19.35 ? 217  ASP   A OD1 1 
ATOM   1372 O  OD2 . ASP   A 1 194 ? -17.637 24.765  36.981  1.00 21.50 ? 217  ASP   A OD2 1 
ATOM   1373 N  N   . VAL   A 1 195 ? -19.929 19.730  36.423  1.00 12.70 ? 218  VAL   A N   1 
ATOM   1374 C  CA  . VAL   A 1 195 ? -20.685 18.583  35.960  1.00 12.83 ? 218  VAL   A CA  1 
ATOM   1375 C  C   . VAL   A 1 195 ? -22.068 18.968  35.427  1.00 12.62 ? 218  VAL   A C   1 
ATOM   1376 O  O   . VAL   A 1 195 ? -22.601 18.223  34.619  1.00 12.73 ? 218  VAL   A O   1 
ATOM   1377 C  CB  . VAL   A 1 195 ? -20.787 17.478  37.015  1.00 13.62 ? 218  VAL   A CB  1 
ATOM   1378 C  CG1 . VAL   A 1 195 ? -19.412 16.858  37.262  1.00 14.44 ? 218  VAL   A CG1 1 
ATOM   1379 C  CG2 . VAL   A 1 195 ? -21.434 17.922  38.309  1.00 12.74 ? 218  VAL   A CG2 1 
ATOM   1380 N  N   . ALA   A 1 196 ? -22.683 20.058  35.903  1.00 11.44 ? 219  ALA   A N   1 
ATOM   1381 C  CA  . ALA   A 1 196 ? -24.035 20.376  35.449  1.00 12.67 ? 219  ALA   A CA  1 
ATOM   1382 C  C   . ALA   A 1 196 ? -23.952 20.805  33.985  1.00 12.25 ? 219  ALA   A C   1 
ATOM   1383 O  O   . ALA   A 1 196 ? -22.991 21.474  33.621  1.00 11.34 ? 219  ALA   A O   1 
ATOM   1384 C  CB  . ALA   A 1 196 ? -24.660 21.476  36.270  1.00 14.34 ? 219  ALA   A CB  1 
ATOM   1385 N  N   . PRO   A 1 197 ? -24.896 20.404  33.105  1.00 11.65 ? 220  PRO   A N   1 
ATOM   1386 C  CA  . PRO   A 1 197 ? -24.864 20.864  31.715  1.00 12.18 ? 220  PRO   A CA  1 
ATOM   1387 C  C   . PRO   A 1 197 ? -24.690 22.377  31.629  1.00 13.08 ? 220  PRO   A C   1 
ATOM   1388 O  O   . PRO   A 1 197 ? -25.257 23.129  32.411  1.00 12.60 ? 220  PRO   A O   1 
ATOM   1389 C  CB  . PRO   A 1 197 ? -26.212 20.431  31.186  1.00 12.69 ? 220  PRO   A CB  1 
ATOM   1390 C  CG  . PRO   A 1 197 ? -26.494 19.162  31.963  1.00 13.33 ? 220  PRO   A CG  1 
ATOM   1391 C  CD  . PRO   A 1 197 ? -25.979 19.437  33.368  1.00 12.59 ? 220  PRO   A CD  1 
ATOM   1392 N  N   . HIS   A 1 198 ? -23.858 22.786  30.677  1.00 13.23 ? 221  HIS   A N   1 
ATOM   1393 C  CA  . HIS   A 1 198 ? -23.628 24.180  30.385  1.00 14.55 ? 221  HIS   A CA  1 
ATOM   1394 C  C   . HIS   A 1 198 ? -23.240 24.266  28.917  1.00 14.80 ? 221  HIS   A C   1 
ATOM   1395 O  O   . HIS   A 1 198 ? -22.663 23.314  28.400  1.00 17.40 ? 221  HIS   A O   1 
ATOM   1396 C  CB  . HIS   A 1 198 ? -22.590 24.747  31.368  1.00 15.93 ? 221  HIS   A CB  1 
ATOM   1397 C  CG  . HIS   A 1 198 ? -21.283 24.048  31.510  1.00 18.42 ? 221  HIS   A CG  1 
ATOM   1398 N  ND1 . HIS   A 1 198 ? -21.129 22.834  32.142  1.00 20.15 ? 221  HIS   A ND1 1 
ATOM   1399 C  CD2 . HIS   A 1 198 ? -20.030 24.453  31.190  1.00 20.64 ? 221  HIS   A CD2 1 
ATOM   1400 C  CE1 . HIS   A 1 198 ? -19.838 22.509  32.166  1.00 19.36 ? 221  HIS   A CE1 1 
ATOM   1401 N  NE2 . HIS   A 1 198 ? -19.151 23.472  31.597  1.00 19.68 ? 221  HIS   A NE2 1 
ATOM   1402 N  N   . PRO   A 1 199 ? -23.320 25.448  28.279  1.00 15.20 ? 222  PRO   A N   1 
ATOM   1403 C  CA  . PRO   A 1 199 ? -22.771 25.602  26.933  1.00 14.78 ? 222  PRO   A CA  1 
ATOM   1404 C  C   . PRO   A 1 199 ? -21.290 25.943  26.927  1.00 13.53 ? 222  PRO   A C   1 
ATOM   1405 O  O   . PRO   A 1 199 ? -20.740 26.328  27.961  1.00 14.32 ? 222  PRO   A O   1 
ATOM   1406 C  CB  . PRO   A 1 199 ? -23.628 26.737  26.352  1.00 16.86 ? 222  PRO   A CB  1 
ATOM   1407 C  CG  . PRO   A 1 199 ? -24.000 27.594  27.545  1.00 16.64 ? 222  PRO   A CG  1 
ATOM   1408 C  CD  . PRO   A 1 199 ? -23.980 26.664  28.783  1.00 15.68 ? 222  PRO   A CD  1 
ATOM   1409 N  N   . GLY   A 1 200 ? -20.686 25.809  25.738  1.00 15.14 ? 223  GLY   A N   1 
ATOM   1410 C  CA  . GLY   A 1 200 ? -19.420 26.422  25.382  1.00 15.49 ? 223  GLY   A CA  1 
ATOM   1411 C  C   . GLY   A 1 200 ? -18.211 25.521  25.619  1.00 14.44 ? 223  GLY   A C   1 
ATOM   1412 O  O   . GLY   A 1 200 ? -17.083 26.012  25.670  1.00 18.18 ? 223  GLY   A O   1 
ATOM   1413 N  N   . GLY   A 1 201 ? -18.450 24.229  25.810  1.00 11.42 ? 224  GLY   A N   1 
ATOM   1414 C  CA  . GLY   A 1 201 ? -17.373 23.255  25.979  1.00 11.11 ? 224  GLY   A CA  1 
ATOM   1415 C  C   . GLY   A 1 201 ? -16.819 22.662  24.682  1.00 11.32 ? 224  GLY   A C   1 
ATOM   1416 O  O   . GLY   A 1 201 ? -15.777 21.981  24.691  1.00 9.53  ? 224  GLY   A O   1 
ATOM   1417 N  N   . GLY   A 1 202 ? -17.465 22.939  23.542  1.00 10.46 ? 225  GLY   A N   1 
ATOM   1418 C  CA  . GLY   A 1 202 ? -16.947 22.442  22.272  1.00 10.50 ? 225  GLY   A CA  1 
ATOM   1419 C  C   . GLY   A 1 202 ? -16.885 20.907  22.225  1.00 10.03 ? 225  GLY   A C   1 
ATOM   1420 O  O   . GLY   A 1 202 ? -17.781 20.211  22.717  1.00 9.45  ? 225  GLY   A O   1 
ATOM   1421 N  N   . ILE   A 1 203 ? -15.837 20.393  21.571  1.00 9.75  ? 226  ILE   A N   1 
ATOM   1422 C  CA  . ILE   A 1 203 ? -15.722 18.958  21.333  1.00 10.05 ? 226  ILE   A CA  1 
ATOM   1423 C  C   . ILE   A 1 203 ? -15.021 18.240  22.488  1.00 10.10 ? 226  ILE   A C   1 
ATOM   1424 O  O   . ILE   A 1 203 ? -14.612 17.100  22.295  1.00 11.26 ? 226  ILE   A O   1 
ATOM   1425 C  CB  . ILE   A 1 203 ? -15.039 18.654  19.990  1.00 10.13 ? 226  ILE   A CB  1 
ATOM   1426 C  CG1 . ILE   A 1 203 ? -13.555 19.097  19.951  1.00 10.51 ? 226  ILE   A CG1 1 
ATOM   1427 C  CG2 . ILE   A 1 203 ? -15.846 19.267  18.833  1.00 10.50 ? 226  ILE   A CG2 1 
ATOM   1428 C  CD1 . ILE   A 1 203 ? -12.733 18.481  18.828  1.00 10.97 ? 226  ILE   A CD1 1 
ATOM   1429 N  N   . LEU   A 1 204 ? -14.842 18.884  23.643  1.00 9.33  ? 227  LEU   A N   1 
ATOM   1430 C  CA  . LEU   A 1 204 ? -14.278 18.230  24.829  1.00 9.44  ? 227  LEU   A CA  1 
ATOM   1431 C  C   . LEU   A 1 204 ? -15.345 18.141  25.900  1.00 9.57  ? 227  LEU   A C   1 
ATOM   1432 O  O   . LEU   A 1 204 ? -16.211 19.000  25.952  1.00 8.90  ? 227  LEU   A O   1 
ATOM   1433 C  CB  . LEU   A 1 204 ? -13.077 19.069  25.270  1.00 10.14 ? 227  LEU   A CB  1 
ATOM   1434 C  CG  . LEU   A 1 204 ? -11.999 19.259  24.199  1.00 11.32 ? 227  LEU   A CG  1 
ATOM   1435 C  CD1 . LEU   A 1 204 ? -10.894 20.195  24.637  1.00 12.47 ? 227  LEU   A CD1 1 
ATOM   1436 C  CD2 . LEU   A 1 204 ? -11.374 17.928  23.811  1.00 11.63 ? 227  LEU   A CD2 1 
ATOM   1437 N  N   . TYR   A 1 205 ? -15.311 17.092  26.734  1.00 9.65  ? 228  TYR   A N   1 
ATOM   1438 C  CA  . TYR   A 1 205 ? -16.446 16.755  27.564  1.00 9.00  ? 228  TYR   A CA  1 
ATOM   1439 C  C   . TYR   A 1 205 ? -16.024 16.522  29.015  1.00 8.75  ? 228  TYR   A C   1 
ATOM   1440 O  O   . TYR   A 1 205 ? -14.839 16.649  29.356  1.00 9.97  ? 228  TYR   A O   1 
ATOM   1441 C  CB  . TYR   A 1 205 ? -17.113 15.499  26.976  1.00 9.00  ? 228  TYR   A CB  1 
ATOM   1442 C  CG  . TYR   A 1 205 ? -17.256 15.516  25.461  1.00 8.87  ? 228  TYR   A CG  1 
ATOM   1443 C  CD1 . TYR   A 1 205 ? -17.895 16.560  24.796  1.00 8.93  ? 228  TYR   A CD1 1 
ATOM   1444 C  CD2 . TYR   A 1 205 ? -16.693 14.511  24.677  1.00 8.46  ? 228  TYR   A CD2 1 
ATOM   1445 C  CE1 . TYR   A 1 205 ? -18.018 16.560  23.415  1.00 8.83  ? 228  TYR   A CE1 1 
ATOM   1446 C  CE2 . TYR   A 1 205 ? -16.770 14.538  23.296  1.00 8.28  ? 228  TYR   A CE2 1 
ATOM   1447 C  CZ  . TYR   A 1 205 ? -17.467 15.553  22.654  1.00 8.52  ? 228  TYR   A CZ  1 
ATOM   1448 O  OH  . TYR   A 1 205 ? -17.491 15.632  21.285  1.00 7.67  ? 228  TYR   A OH  1 
ATOM   1449 N  N   . THR   A 1 206 ? -17.051 16.203  29.817  1.00 8.39  ? 229  THR   A N   1 
ATOM   1450 C  CA  . THR   A 1 206 ? -16.934 15.860  31.225  1.00 8.30  ? 229  THR   A CA  1 
ATOM   1451 C  C   . THR   A 1 206 ? -15.816 14.835  31.413  1.00 9.07  ? 229  THR   A C   1 
ATOM   1452 O  O   . THR   A 1 206 ? -15.720 13.890  30.661  1.00 9.60  ? 229  THR   A O   1 
ATOM   1453 C  CB  . THR   A 1 206 ? -18.256 15.316  31.755  1.00 8.04  ? 229  THR   A CB  1 
ATOM   1454 O  OG1 . THR   A 1 206 ? -19.277 16.309  31.599  1.00 7.63  ? 229  THR   A OG1 1 
ATOM   1455 C  CG2 . THR   A 1 206 ? -18.119 15.104  33.250  1.00 8.21  ? 229  THR   A CG2 1 
ATOM   1456 N  N   . ALA   A 1 207 ? -14.970 15.073  32.409  1.00 8.90  ? 230  ALA   A N   1 
ATOM   1457 C  CA  . ALA   A 1 207 ? -13.906 14.151  32.765  1.00 8.79  ? 230  ALA   A CA  1 
ATOM   1458 C  C   . ALA   A 1 207 ? -14.465 12.892  33.416  1.00 8.55  ? 230  ALA   A C   1 
ATOM   1459 O  O   . ALA   A 1 207 ? -15.583 12.849  33.915  1.00 8.65  ? 230  ALA   A O   1 
ATOM   1460 C  CB  . ALA   A 1 207 ? -12.906 14.817  33.676  1.00 9.08  ? 230  ALA   A CB  1 
ATOM   1461 N  N   . ALA   A 1 208 ? -13.616 11.856  33.433  1.00 8.20  ? 231  ALA   A N   1 
ATOM   1462 C  CA  . ALA   A 1 208 ? -13.944 10.569  34.026  1.00 8.00  ? 231  ALA   A CA  1 
ATOM   1463 C  C   . ALA   A 1 208 ? -12.829 10.198  34.992  1.00 7.44  ? 231  ALA   A C   1 
ATOM   1464 O  O   . ALA   A 1 208 ? -11.732 9.827   34.552  1.00 7.77  ? 231  ALA   A O   1 
ATOM   1465 C  CB  . ALA   A 1 208 ? -14.061 9.497   32.950  1.00 7.90  ? 231  ALA   A CB  1 
ATOM   1466 N  N   . SER   A 1 209 ? -13.123 10.270  36.303  1.00 7.84  ? 232  SER   A N   1 
ATOM   1467 C  CA  . SER   A 1 209 ? -12.117 9.984   37.318  1.00 8.02  ? 232  SER   A CA  1 
ATOM   1468 C  C   . SER   A 1 209 ? -12.576 8.856   38.208  1.00 8.11  ? 232  SER   A C   1 
ATOM   1469 O  O   . SER   A 1 209 ? -13.700 8.899   38.729  1.00 8.40  ? 232  SER   A O   1 
ATOM   1470 C  CB  . SER   A 1 209 ? -11.858 11.208  38.154  1.00 7.64  ? 232  SER   A CB  1 
ATOM   1471 O  OG  . SER   A 1 209 ? -11.600 12.327  37.330  1.00 8.24  ? 232  SER   A OG  1 
ATOM   1472 N  N   . GLY   A 1 210 ? -11.676 7.861   38.370  1.00 8.40  ? 233  GLY   A N   1 
ATOM   1473 C  CA  . GLY   A 1 210 ? -11.857 6.754   39.283  1.00 8.12  ? 233  GLY   A CA  1 
ATOM   1474 C  C   . GLY   A 1 210 ? -12.103 5.445   38.547  1.00 8.15  ? 233  GLY   A C   1 
ATOM   1475 O  O   . GLY   A 1 210 ? -11.746 5.264   37.382  1.00 6.84  ? 233  GLY   A O   1 
ATOM   1476 N  N   . ILE   A 1 211 ? -12.757 4.537   39.273  1.00 7.99  ? 234  ILE   A N   1 
ATOM   1477 C  CA  . ILE   A 1 211 ? -12.958 3.182   38.836  1.00 8.32  ? 234  ILE   A CA  1 
ATOM   1478 C  C   . ILE   A 1 211 ? -14.163 3.206   37.905  1.00 8.39  ? 234  ILE   A C   1 
ATOM   1479 O  O   . ILE   A 1 211 ? -15.262 3.523   38.330  1.00 9.11  ? 234  ILE   A O   1 
ATOM   1480 C  CB  . ILE   A 1 211 ? -13.189 2.238   40.030  1.00 8.40  ? 234  ILE   A CB  1 
ATOM   1481 C  CG1 . ILE   A 1 211 ? -11.979 2.235   40.942  1.00 8.54  ? 234  ILE   A CG1 1 
ATOM   1482 C  CG2 . ILE   A 1 211 ? -13.566 0.835   39.550  1.00 8.28  ? 234  ILE   A CG2 1 
ATOM   1483 C  CD1 . ILE   A 1 211 ? -12.179 1.482   42.240  1.00 8.97  ? 234  ILE   A CD1 1 
ATOM   1484 N  N   . TRP   A 1 212 ? -13.954 2.826   36.641  1.00 8.02  ? 235  TRP   A N   1 
ATOM   1485 C  CA  . TRP   A 1 212 ? -15.026 2.963   35.672  1.00 7.70  ? 235  TRP   A CA  1 
ATOM   1486 C  C   . TRP   A 1 212 ? -15.343 1.647   34.960  1.00 7.77  ? 235  TRP   A C   1 
ATOM   1487 O  O   . TRP   A 1 212 ? -16.171 1.667   34.082  1.00 7.76  ? 235  TRP   A O   1 
ATOM   1488 C  CB  . TRP   A 1 212 ? -14.732 4.113   34.696  1.00 7.37  ? 235  TRP   A CB  1 
ATOM   1489 C  CG  . TRP   A 1 212 ? -13.560 3.933   33.760  1.00 7.12  ? 235  TRP   A CG  1 
ATOM   1490 C  CD1 . TRP   A 1 212 ? -12.259 4.248   34.001  1.00 6.81  ? 235  TRP   A CD1 1 
ATOM   1491 C  CD2 . TRP   A 1 212 ? -13.616 3.566   32.361  1.00 6.98  ? 235  TRP   A CD2 1 
ATOM   1492 N  NE1 . TRP   A 1 212 ? -11.504 4.046   32.869  1.00 7.42  ? 235  TRP   A NE1 1 
ATOM   1493 C  CE2 . TRP   A 1 212 ? -12.303 3.638   31.848  1.00 7.11  ? 235  TRP   A CE2 1 
ATOM   1494 C  CE3 . TRP   A 1 212 ? -14.653 3.198   31.502  1.00 8.00  ? 235  TRP   A CE3 1 
ATOM   1495 C  CZ2 . TRP   A 1 212 ? -11.987 3.371   30.517  1.00 7.31  ? 235  TRP   A CZ2 1 
ATOM   1496 C  CZ3 . TRP   A 1 212 ? -14.352 2.950   30.176  1.00 7.42  ? 235  TRP   A CZ3 1 
ATOM   1497 C  CH2 . TRP   A 1 212 ? -13.041 3.044   29.697  1.00 7.56  ? 235  TRP   A CH2 1 
ATOM   1498 N  N   . GLN   A 1 213 ? -14.696 0.538   35.337  1.00 8.19  ? 236  GLN   A N   1 
ATOM   1499 C  CA  . GLN   A 1 213 ? -15.031 -0.781  34.810  1.00 8.29  ? 236  GLN   A CA  1 
ATOM   1500 C  C   . GLN   A 1 213 ? -15.066 -1.748  35.989  1.00 8.29  ? 236  GLN   A C   1 
ATOM   1501 O  O   . GLN   A 1 213 ? -14.550 -1.430  37.073  1.00 7.57  ? 236  GLN   A O   1 
ATOM   1502 C  CB  . GLN   A 1 213 ? -13.969 -1.220  33.807  1.00 8.58  ? 236  GLN   A CB  1 
ATOM   1503 C  CG  . GLN   A 1 213 ? -13.966 -0.357  32.555  1.00 8.93  ? 236  GLN   A CG  1 
ATOM   1504 C  CD  . GLN   A 1 213 ? -13.013 -0.878  31.503  1.00 9.33  ? 236  GLN   A CD  1 
ATOM   1505 O  OE1 . GLN   A 1 213 ? -12.592 -2.036  31.598  1.00 8.91  ? 236  GLN   A OE1 1 
ATOM   1506 N  NE2 . GLN   A 1 213 ? -12.674 -0.064  30.498  1.00 9.33  ? 236  GLN   A NE2 1 
ATOM   1507 N  N   . THR   A 1 214 ? -15.731 -2.896  35.771  1.00 7.75  ? 237  THR   A N   1 
ATOM   1508 C  CA  . THR   A 1 214 ? -15.966 -3.883  36.815  1.00 8.56  ? 237  THR   A CA  1 
ATOM   1509 C  C   . THR   A 1 214 ? -14.685 -4.206  37.590  1.00 8.40  ? 237  THR   A C   1 
ATOM   1510 O  O   . THR   A 1 214 ? -13.601 -4.396  37.024  1.00 9.50  ? 237  THR   A O   1 
ATOM   1511 C  CB  . THR   A 1 214 ? -16.607 -5.128  36.204  1.00 8.25  ? 237  THR   A CB  1 
ATOM   1512 O  OG1 . THR   A 1 214 ? -17.880 -4.723  35.703  1.00 7.96  ? 237  THR   A OG1 1 
ATOM   1513 C  CG2 . THR   A 1 214 ? -16.793 -6.228  37.221  1.00 7.82  ? 237  THR   A CG2 1 
ATOM   1514 N  N   . VAL   A 1 215 ? -14.835 -4.302  38.924  1.00 8.58  ? 238  VAL   A N   1 
ATOM   1515 C  CA  . VAL   A 1 215 ? -13.798 -4.837  39.791  1.00 8.55  ? 238  VAL   A CA  1 
ATOM   1516 C  C   . VAL   A 1 215 ? -14.269 -6.199  40.253  1.00 8.24  ? 238  VAL   A C   1 
ATOM   1517 O  O   . VAL   A 1 215 ? -15.444 -6.367  40.601  1.00 7.95  ? 238  VAL   A O   1 
ATOM   1518 C  CB  . VAL   A 1 215 ? -13.564 -3.929  41.014  1.00 9.57  ? 238  VAL   A CB  1 
ATOM   1519 C  CG1 . VAL   A 1 215 ? -12.456 -4.471  41.919  1.00 9.59  ? 238  VAL   A CG1 1 
ATOM   1520 C  CG2 . VAL   A 1 215 ? -13.345 -2.488  40.587  1.00 10.52 ? 238  VAL   A CG2 1 
ATOM   1521 N  N   . TRP   A 1 216 ? -13.362 -7.175  40.218  1.00 7.89  ? 239  TRP   A N   1 
ATOM   1522 C  CA  . TRP   A 1 216 ? -13.819 -8.525  40.507  1.00 7.98  ? 239  TRP   A CA  1 
ATOM   1523 C  C   . TRP   A 1 216 ? -12.676 -9.401  40.995  1.00 8.56  ? 239  TRP   A C   1 
ATOM   1524 O  O   . TRP   A 1 216 ? -11.496 -9.065  40.851  1.00 8.66  ? 239  TRP   A O   1 
ATOM   1525 C  CB  . TRP   A 1 216 ? -14.499 -9.119  39.266  1.00 7.59  ? 239  TRP   A CB  1 
ATOM   1526 C  CG  . TRP   A 1 216 ? -13.717 -9.138  37.989  1.00 7.24  ? 239  TRP   A CG  1 
ATOM   1527 C  CD1 . TRP   A 1 216 ? -13.280 -8.091  37.225  1.00 7.63  ? 239  TRP   A CD1 1 
ATOM   1528 C  CD2 . TRP   A 1 216 ? -13.346 -10.321 37.254  1.00 7.52  ? 239  TRP   A CD2 1 
ATOM   1529 N  NE1 . TRP   A 1 216 ? -12.671 -8.520  36.066  1.00 7.44  ? 239  TRP   A NE1 1 
ATOM   1530 C  CE2 . TRP   A 1 216 ? -12.699 -9.898  36.065  1.00 7.68  ? 239  TRP   A CE2 1 
ATOM   1531 C  CE3 . TRP   A 1 216 ? -13.496 -11.688 37.493  1.00 8.11  ? 239  TRP   A CE3 1 
ATOM   1532 C  CZ2 . TRP   A 1 216 ? -12.201 -10.824 35.145  1.00 7.60  ? 239  TRP   A CZ2 1 
ATOM   1533 C  CZ3 . TRP   A 1 216 ? -13.039 -12.594 36.569  1.00 7.92  ? 239  TRP   A CZ3 1 
ATOM   1534 C  CH2 . TRP   A 1 216 ? -12.436 -12.167 35.393  1.00 8.15  ? 239  TRP   A CH2 1 
ATOM   1535 N  N   . LEU   A 1 217 ? -13.095 -10.554 41.530  1.00 8.72  ? 240  LEU   A N   1 
ATOM   1536 C  CA  . LEU   A 1 217 ? -12.177 -11.548 42.023  1.00 8.56  ? 240  LEU   A CA  1 
ATOM   1537 C  C   . LEU   A 1 217 ? -12.335 -12.838 41.232  1.00 7.89  ? 240  LEU   A C   1 
ATOM   1538 O  O   . LEU   A 1 217 ? -13.427 -13.191 40.776  1.00 7.81  ? 240  LEU   A O   1 
ATOM   1539 C  CB  . LEU   A 1 217 ? -12.489 -11.841 43.494  1.00 9.30  ? 240  LEU   A CB  1 
ATOM   1540 C  CG  . LEU   A 1 217 ? -12.358 -10.685 44.477  1.00 9.84  ? 240  LEU   A CG  1 
ATOM   1541 C  CD1 . LEU   A 1 217 ? -13.042 -11.074 45.760  1.00 10.57 ? 240  LEU   A CD1 1 
ATOM   1542 C  CD2 . LEU   A 1 217 ? -10.905 -10.385 44.720  1.00 10.06 ? 240  LEU   A CD2 1 
ATOM   1543 N  N   . GLU   A 1 218 ? -11.249 -13.586 41.153  1.00 8.44  ? 241  GLU   A N   1 
ATOM   1544 C  CA  . GLU   A 1 218 ? -11.383 -14.953 40.684  1.00 8.61  ? 241  GLU   A CA  1 
ATOM   1545 C  C   . GLU   A 1 218 ? -10.335 -15.849 41.303  1.00 8.87  ? 241  GLU   A C   1 
ATOM   1546 O  O   . GLU   A 1 218 ? -9.201  -15.438 41.536  1.00 8.99  ? 241  GLU   A O   1 
ATOM   1547 C  CB  . GLU   A 1 218 ? -11.289 -15.067 39.166  1.00 8.99  ? 241  GLU   A CB  1 
ATOM   1548 C  CG  . GLU   A 1 218 ? -9.920  -14.750 38.594  1.00 8.61  ? 241  GLU   A CG  1 
ATOM   1549 C  CD  . GLU   A 1 218 ? -9.827  -14.792 37.073  1.00 9.05  ? 241  GLU   A CD  1 
ATOM   1550 O  OE1 . GLU   A 1 218 ? -10.460 -15.649 36.371  1.00 9.72  ? 241  GLU   A OE1 1 
ATOM   1551 O  OE2 . GLU   A 1 218 ? -9.105  -13.903 36.587  1.00 9.09  ? 241  GLU   A OE2 1 
ATOM   1552 N  N   . PRO   A 1 219 ? -10.683 -17.138 41.530  1.00 8.97  ? 242  PRO   A N   1 
ATOM   1553 C  CA  . PRO   A 1 219 ? -9.675  -18.137 41.914  1.00 9.13  ? 242  PRO   A CA  1 
ATOM   1554 C  C   . PRO   A 1 219 ? -8.982  -18.773 40.721  1.00 9.30  ? 242  PRO   A C   1 
ATOM   1555 O  O   . PRO   A 1 219 ? -9.619  -19.012 39.699  1.00 10.23 ? 242  PRO   A O   1 
ATOM   1556 C  CB  . PRO   A 1 219 ? -10.547 -19.151 42.656  1.00 9.10  ? 242  PRO   A CB  1 
ATOM   1557 C  CG  . PRO   A 1 219 ? -11.820 -19.179 41.855  1.00 8.98  ? 242  PRO   A CG  1 
ATOM   1558 C  CD  . PRO   A 1 219 ? -12.017 -17.703 41.425  1.00 9.32  ? 242  PRO   A CD  1 
ATOM   1559 N  N   . THR   A 1 220 ? -7.705  -19.110 40.887  1.00 10.31 ? 243  THR   A N   1 
ATOM   1560 C  CA  . THR   A 1 220 ? -6.890  -19.710 39.837  1.00 10.94 ? 243  THR   A CA  1 
ATOM   1561 C  C   . THR   A 1 220 ? -5.939  -20.690 40.499  1.00 11.78 ? 243  THR   A C   1 
ATOM   1562 O  O   . THR   A 1 220 ? -5.521  -20.483 41.638  1.00 12.29 ? 243  THR   A O   1 
ATOM   1563 C  CB  . THR   A 1 220 ? -6.051  -18.709 39.031  1.00 10.45 ? 243  THR   A CB  1 
ATOM   1564 O  OG1 . THR   A 1 220 ? -5.029  -18.192 39.866  1.00 10.15 ? 243  THR   A OG1 1 
ATOM   1565 C  CG2 . THR   A 1 220 ? -6.867  -17.586 38.419  1.00 10.79 ? 243  THR   A CG2 1 
ATOM   1566 N  N   . ALA   A 1 221 ? -5.552  -21.717 39.754  1.00 11.70 ? 244  ALA   A N   1 
ATOM   1567 C  CA  . ALA   A 1 221 ? -4.388  -22.501 40.133  1.00 12.29 ? 244  ALA   A CA  1 
ATOM   1568 C  C   . ALA   A 1 221 ? -3.193  -21.564 40.238  1.00 11.99 ? 244  ALA   A C   1 
ATOM   1569 O  O   . ALA   A 1 221 ? -3.147  -20.516 39.602  1.00 11.92 ? 244  ALA   A O   1 
ATOM   1570 C  CB  . ALA   A 1 221 ? -4.137  -23.596 39.134  1.00 13.07 ? 244  ALA   A CB  1 
ATOM   1571 N  N   . ALA   A 1 222 ? -2.148  -21.978 40.947  1.00 13.06 ? 245  ALA   A N   1 
ATOM   1572 C  CA  . ALA   A 1 222 ? -0.949  -21.149 40.972  1.00 13.42 ? 245  ALA   A CA  1 
ATOM   1573 C  C   . ALA   A 1 222 ? -0.394  -20.950 39.556  1.00 14.27 ? 245  ALA   A C   1 
ATOM   1574 O  O   . ALA   A 1 222 ? -0.060  -19.820 39.132  1.00 16.32 ? 245  ALA   A O   1 
ATOM   1575 C  CB  . ALA   A 1 222 ? 0.097   -21.740 41.901  1.00 14.18 ? 245  ALA   A CB  1 
ATOM   1576 N  N   . ALA   A 1 223 ? -0.319  -22.041 38.800  1.00 12.83 ? 246  ALA   A N   1 
ATOM   1577 C  CA  . ALA   A 1 223 ? 0.094   -21.974 37.409  1.00 13.54 ? 246  ALA   A CA  1 
ATOM   1578 C  C   . ALA   A 1 223 ? -1.162  -21.820 36.568  1.00 12.30 ? 246  ALA   A C   1 
ATOM   1579 O  O   . ALA   A 1 223 ? -1.998  -22.699 36.548  1.00 13.15 ? 246  ALA   A O   1 
ATOM   1580 C  CB  . ALA   A 1 223 ? 0.905   -23.215 37.035  1.00 15.08 ? 246  ALA   A CB  1 
ATOM   1581 N  N   . HIS   A 1 224 ? -1.348  -20.671 35.904  1.00 10.42 ? 247  HIS   A N   1 
ATOM   1582 C  CA  . HIS   A 1 224 ? -2.630  -20.418 35.259  1.00 9.70  ? 247  HIS   A CA  1 
ATOM   1583 C  C   . HIS   A 1 224 ? -2.441  -19.531 34.034  1.00 9.16  ? 247  HIS   A C   1 
ATOM   1584 O  O   . HIS   A 1 224 ? -1.459  -18.802 33.927  1.00 10.09 ? 247  HIS   A O   1 
ATOM   1585 C  CB  . HIS   A 1 224 ? -3.617  -19.751 36.222  1.00 9.93  ? 247  HIS   A CB  1 
ATOM   1586 C  CG  . HIS   A 1 224 ? -3.187  -18.430 36.729  1.00 9.94  ? 247  HIS   A CG  1 
ATOM   1587 N  ND1 . HIS   A 1 224 ? -2.259  -18.271 37.737  1.00 10.13 ? 247  HIS   A ND1 1 
ATOM   1588 C  CD2 . HIS   A 1 224 ? -3.589  -17.199 36.369  1.00 10.96 ? 247  HIS   A CD2 1 
ATOM   1589 C  CE1 . HIS   A 1 224 ? -2.092  -16.951 37.941  1.00 11.57 ? 247  HIS   A CE1 1 
ATOM   1590 N  NE2 . HIS   A 1 224 ? -2.879  -16.281 37.113  1.00 11.41 ? 247  HIS   A NE2 1 
ATOM   1591 N  N   . VAL   A 1 225 ? -3.412  -19.583 33.144  1.00 9.16  ? 248  VAL   A N   1 
ATOM   1592 C  CA  . VAL   A 1 225 ? -3.417  -18.796 31.922  1.00 9.59  ? 248  VAL   A CA  1 
ATOM   1593 C  C   . VAL   A 1 225 ? -3.815  -17.351 32.223  1.00 10.08 ? 248  VAL   A C   1 
ATOM   1594 O  O   . VAL   A 1 225 ? -4.786  -17.116 32.950  1.00 10.10 ? 248  VAL   A O   1 
ATOM   1595 C  CB  . VAL   A 1 225 ? -4.391  -19.369 30.883  1.00 9.39  ? 248  VAL   A CB  1 
ATOM   1596 C  CG1 . VAL   A 1 225 ? -4.410  -18.539 29.592  1.00 8.95  ? 248  VAL   A CG1 1 
ATOM   1597 C  CG2 . VAL   A 1 225 ? -4.087  -20.801 30.526  1.00 10.25 ? 248  VAL   A CG2 1 
ATOM   1598 N  N   . THR   A 1 226 ? -3.063  -16.400 31.666  1.00 9.87  ? 249  THR   A N   1 
ATOM   1599 C  CA  . THR   A 1 226 ? -3.409  -14.993 31.825  1.00 11.05 ? 249  THR   A CA  1 
ATOM   1600 C  C   . THR   A 1 226 ? -3.780  -14.352 30.497  1.00 10.76 ? 249  THR   A C   1 
ATOM   1601 O  O   . THR   A 1 226 ? -4.378  -13.276 30.496  1.00 11.26 ? 249  THR   A O   1 
ATOM   1602 C  CB  . THR   A 1 226 ? -2.290  -14.178 32.475  1.00 11.22 ? 249  THR   A CB  1 
ATOM   1603 O  OG1 . THR   A 1 226 ? -1.177  -14.279 31.591  1.00 10.90 ? 249  THR   A OG1 1 
ATOM   1604 C  CG2 . THR   A 1 226 ? -2.007  -14.711 33.868  1.00 10.70 ? 249  THR   A CG2 1 
ATOM   1605 N  N   . ARG   A 1 227 ? -3.451  -14.982 29.394  1.00 10.85 ? 250  ARG   A N   1 
ATOM   1606 C  CA  . ARG   A 1 227 ? -3.662  -14.326 28.113  1.00 10.04 ? 250  ARG   A CA  1 
ATOM   1607 C  C   . ARG   A 1 227 ? -3.630  -15.353 26.998  1.00 10.73 ? 250  ARG   A C   1 
ATOM   1608 O  O   . ARG   A 1 227 ? -2.843  -16.289 27.067  1.00 10.25 ? 250  ARG   A O   1 
ATOM   1609 C  CB  . ARG   A 1 227 ? -2.582  -13.256 27.923  1.00 10.82 ? 250  ARG   A CB  1 
ATOM   1610 C  CG  . ARG   A 1 227 ? -2.467  -12.714 26.513  1.00 11.99 ? 250  ARG   A CG  1 
ATOM   1611 C  CD  . ARG   A 1 227 ? -1.408  -11.605 26.553  1.00 11.37 ? 250  ARG   A CD  1 
ATOM   1612 N  NE  . ARG   A 1 227 ? -0.789  -11.440 25.246  1.00 10.85 ? 250  ARG   A NE  1 
ATOM   1613 C  CZ  . ARG   A 1 227 ? 0.382   -10.850 25.010  1.00 10.39 ? 250  ARG   A CZ  1 
ATOM   1614 N  NH1 . ARG   A 1 227 ? 1.036   -10.216 25.986  1.00 10.72 ? 250  ARG   A NH1 1 
ATOM   1615 N  NH2 . ARG   A 1 227 ? 0.903   -10.917 23.799  1.00 9.17  ? 250  ARG   A NH2 1 
ATOM   1616 N  N   . LEU   A 1 228 ? -4.520  -15.160 26.020  1.00 11.00 ? 251  LEU   A N   1 
ATOM   1617 C  CA  . LEU   A 1 228 ? -4.535  -15.971 24.821  1.00 12.42 ? 251  LEU   A CA  1 
ATOM   1618 C  C   . LEU   A 1 228 ? -4.383  -15.052 23.630  1.00 12.68 ? 251  LEU   A C   1 
ATOM   1619 O  O   . LEU   A 1 228 ? -5.131  -14.068 23.533  1.00 15.35 ? 251  LEU   A O   1 
ATOM   1620 C  CB  . LEU   A 1 228 ? -5.834  -16.736 24.641  1.00 13.86 ? 251  LEU   A CB  1 
ATOM   1621 C  CG  . LEU   A 1 228 ? -6.120  -17.888 25.585  1.00 14.72 ? 251  LEU   A CG  1 
ATOM   1622 C  CD1 . LEU   A 1 228 ? -7.531  -18.424 25.257  1.00 15.57 ? 251  LEU   A CD1 1 
ATOM   1623 C  CD2 . LEU   A 1 228 ? -5.070  -18.970 25.441  1.00 16.60 ? 251  LEU   A CD2 1 
ATOM   1624 N  N   . ASP   A 1 229 ? -3.492  -15.439 22.698  1.00 11.06 ? 252  ASP   A N   1 
ATOM   1625 C  CA  . ASP   A 1 229 ? -3.351  -14.717 21.457  1.00 10.15 ? 252  ASP   A CA  1 
ATOM   1626 C  C   . ASP   A 1 229 ? -3.778  -15.666 20.337  1.00 10.35 ? 252  ASP   A C   1 
ATOM   1627 O  O   . ASP   A 1 229 ? -3.041  -16.591 19.963  1.00 10.96 ? 252  ASP   A O   1 
ATOM   1628 C  CB  . ASP   A 1 229 ? -1.922  -14.231 21.282  1.00 10.84 ? 252  ASP   A CB  1 
ATOM   1629 C  CG  . ASP   A 1 229 ? -1.358  -13.332 22.377  1.00 11.18 ? 252  ASP   A CG  1 
ATOM   1630 O  OD1 . ASP   A 1 229 ? -2.175  -12.720 23.124  1.00 10.32 ? 252  ASP   A OD1 1 
ATOM   1631 O  OD2 . ASP   A 1 229 ? -0.094  -13.263 22.496  1.00 11.84 ? 252  ASP   A OD2 1 
ATOM   1632 N  N   . LEU   A 1 230 ? -4.988  -15.438 19.844  1.00 9.32  ? 253  LEU   A N   1 
ATOM   1633 C  CA  . LEU   A 1 230 ? -5.594  -16.325 18.866  1.00 9.29  ? 253  LEU   A CA  1 
ATOM   1634 C  C   . LEU   A 1 230 ? -5.598  -15.566 17.557  1.00 9.24  ? 253  LEU   A C   1 
ATOM   1635 O  O   . LEU   A 1 230 ? -6.336  -14.588 17.444  1.00 9.46  ? 253  LEU   A O   1 
ATOM   1636 C  CB  . LEU   A 1 230 ? -7.006  -16.636 19.322  1.00 9.87  ? 253  LEU   A CB  1 
ATOM   1637 C  CG  . LEU   A 1 230 ? -7.136  -17.315 20.694  1.00 10.25 ? 253  LEU   A CG  1 
ATOM   1638 C  CD1 . LEU   A 1 230 ? -8.585  -17.613 20.999  1.00 9.65  ? 253  LEU   A CD1 1 
ATOM   1639 C  CD2 . LEU   A 1 230 ? -6.326  -18.606 20.810  1.00 10.46 ? 253  LEU   A CD2 1 
ATOM   1640 N  N   . VAL   A 1 231 ? -4.786  -16.027 16.603  1.00 8.69  ? 254  VAL   A N   1 
ATOM   1641 C  CA  . VAL   A 1 231 ? -4.607  -15.325 15.341  1.00 9.65  ? 254  VAL   A CA  1 
ATOM   1642 C  C   . VAL   A 1 231 ? -5.099  -16.184 14.193  1.00 8.97  ? 254  VAL   A C   1 
ATOM   1643 O  O   . VAL   A 1 231 ? -4.431  -17.186 13.868  1.00 9.39  ? 254  VAL   A O   1 
ATOM   1644 C  CB  . VAL   A 1 231 ? -3.134  -14.960 15.143  1.00 10.34 ? 254  VAL   A CB  1 
ATOM   1645 C  CG1 . VAL   A 1 231 ? -2.897  -14.301 13.792  1.00 11.45 ? 254  VAL   A CG1 1 
ATOM   1646 C  CG2 . VAL   A 1 231 ? -2.657  -14.093 16.301  1.00 10.70 ? 254  VAL   A CG2 1 
ATOM   1647 N  N   . PRO   A 1 232 ? -6.295  -15.907 13.609  1.00 9.41  ? 255  PRO   A N   1 
ATOM   1648 C  CA  . PRO   A 1 232 ? -6.809  -16.723 12.493  1.00 9.52  ? 255  PRO   A CA  1 
ATOM   1649 C  C   . PRO   A 1 232 ? -5.881  -16.738 11.290  1.00 10.49 ? 255  PRO   A C   1 
ATOM   1650 O  O   . PRO   A 1 232 ? -5.260  -15.711 10.948  1.00 9.25  ? 255  PRO   A O   1 
ATOM   1651 C  CB  . PRO   A 1 232 ? -8.142  -16.068 12.145  1.00 9.65  ? 255  PRO   A CB  1 
ATOM   1652 C  CG  . PRO   A 1 232 ? -8.527  -15.450 13.449  1.00 9.73  ? 255  PRO   A CG  1 
ATOM   1653 C  CD  . PRO   A 1 232 ? -7.249  -14.845 13.966  1.00 9.31  ? 255  PRO   A CD  1 
ATOM   1654 N  N   . ASP   A 1 233 ? -5.739  -17.938 10.724  1.00 11.12 ? 256  ASP   A N   1 
ATOM   1655 C  CA  . ASP   A 1 233 ? -5.024  -18.137 9.471   1.00 11.78 ? 256  ASP   A CA  1 
ATOM   1656 C  C   . ASP   A 1 233 ? -5.921  -19.008 8.609   1.00 11.88 ? 256  ASP   A C   1 
ATOM   1657 O  O   . ASP   A 1 233 ? -5.537  -20.124 8.243   1.00 12.90 ? 256  ASP   A O   1 
ATOM   1658 C  CB  . ASP   A 1 233 ? -3.684  -18.807 9.714   1.00 11.90 ? 256  ASP   A CB  1 
ATOM   1659 C  CG  . ASP   A 1 233 ? -2.735  -18.844 8.534   1.00 14.21 ? 256  ASP   A CG  1 
ATOM   1660 O  OD1 . ASP   A 1 233 ? -3.045  -18.182 7.510   1.00 14.80 ? 256  ASP   A OD1 1 
ATOM   1661 O  OD2 . ASP   A 1 233 ? -1.719  -19.537 8.686   1.00 15.16 ? 256  ASP   A OD2 1 
ATOM   1662 N  N   . PRO   A 1 234 ? -7.131  -18.534 8.248   1.00 11.95 ? 257  PRO   A N   1 
ATOM   1663 C  CA  . PRO   A 1 234 ? -8.059  -19.334 7.444   1.00 12.71 ? 257  PRO   A CA  1 
ATOM   1664 C  C   . PRO   A 1 234 ? -7.538  -19.808 6.084   1.00 13.47 ? 257  PRO   A C   1 
ATOM   1665 O  O   . PRO   A 1 234 ? -7.968  -20.857 5.618   1.00 14.34 ? 257  PRO   A O   1 
ATOM   1666 C  CB  . PRO   A 1 234 ? -9.271  -18.442 7.257   1.00 12.71 ? 257  PRO   A CB  1 
ATOM   1667 C  CG  . PRO   A 1 234 ? -8.731  -17.044 7.454   1.00 12.35 ? 257  PRO   A CG  1 
ATOM   1668 C  CD  . PRO   A 1 234 ? -7.707  -17.221 8.576   1.00 12.59 ? 257  PRO   A CD  1 
ATOM   1669 N  N   . ALA   A 1 235 ? -6.643  -19.034 5.454   1.00 14.92 ? 258  ALA   A N   1 
ATOM   1670 C  CA  . ALA   A 1 235 ? -6.073  -19.419 4.163   1.00 16.08 ? 258  ALA   A CA  1 
ATOM   1671 C  C   . ALA   A 1 235 ? -5.282  -20.714 4.315   1.00 17.20 ? 258  ALA   A C   1 
ATOM   1672 O  O   . ALA   A 1 235 ? -5.052  -21.425 3.342   1.00 19.41 ? 258  ALA   A O   1 
ATOM   1673 C  CB  . ALA   A 1 235 ? -5.193  -18.314 3.612   1.00 17.18 ? 258  ALA   A CB  1 
ATOM   1674 N  N   . ASN   A 1 236 ? -4.845  -21.006 5.540   1.00 16.79 ? 259  ASN   A N   1 
ATOM   1675 C  CA  . ASN   A 1 236 ? -4.121  -22.219 5.846   1.00 15.01 ? 259  ASN   A CA  1 
ATOM   1676 C  C   . ASN   A 1 236 ? -4.959  -23.140 6.732   1.00 13.44 ? 259  ASN   A C   1 
ATOM   1677 O  O   . ASN   A 1 236 ? -4.432  -24.094 7.303   1.00 13.73 ? 259  ASN   A O   1 
ATOM   1678 C  CB  . ASN   A 1 236 ? -2.781  -21.916 6.498   1.00 16.57 ? 259  ASN   A CB  1 
ATOM   1679 C  CG  . ASN   A 1 236 ? -1.803  -21.328 5.511   1.00 19.08 ? 259  ASN   A CG  1 
ATOM   1680 O  OD1 . ASN   A 1 236 ? -1.659  -21.868 4.413   1.00 18.70 ? 259  ASN   A OD1 1 
ATOM   1681 N  ND2 . ASN   A 1 236 ? -1.095  -20.272 5.880   1.00 21.43 ? 259  ASN   A ND2 1 
ATOM   1682 N  N   . SER   A 1 237 ? -6.266  -22.893 6.798   1.00 13.51 ? 260  SER   A N   1 
ATOM   1683 C  CA  . SER   A 1 237 ? -7.218  -23.728 7.524   1.00 12.48 ? 260  SER   A CA  1 
ATOM   1684 C  C   . SER   A 1 237 ? -6.752  -24.009 8.951   1.00 11.67 ? 260  SER   A C   1 
ATOM   1685 O  O   . SER   A 1 237 ? -6.764  -25.140 9.400   1.00 10.97 ? 260  SER   A O   1 
ATOM   1686 C  CB  . SER   A 1 237 ? -7.491  -25.048 6.816   1.00 14.34 ? 260  SER   A CB  1 
ATOM   1687 O  OG  . SER   A 1 237 ? -7.996  -24.788 5.521   1.00 15.79 ? 260  SER   A OG  1 
ATOM   1688 N  N   . ARG   A 1 238 ? -6.267  -22.988 9.637   1.00 10.83 ? 261  ARG   A N   1 
ATOM   1689 C  CA  . ARG   A 1 238 ? -5.730  -23.194 10.967  1.00 11.48 ? 261  ARG   A CA  1 
ATOM   1690 C  C   . ARG   A 1 238 ? -5.839  -21.915 11.800  1.00 11.11 ? 261  ARG   A C   1 
ATOM   1691 O  O   . ARG   A 1 238 ? -6.051  -20.835 11.264  1.00 11.23 ? 261  ARG   A O   1 
ATOM   1692 C  CB  . ARG   A 1 238 ? -4.300  -23.703 10.851  1.00 13.32 ? 261  ARG   A CB  1 
ATOM   1693 C  CG  . ARG   A 1 238 ? -3.340  -22.634 10.367  1.00 16.32 ? 261  ARG   A CG  1 
ATOM   1694 C  CD  . ARG   A 1 238 ? -2.028  -23.200 9.844   1.00 21.57 ? 261  ARG   A CD  1 
ATOM   1695 N  NE  . ARG   A 1 238 ? -1.068  -22.084 9.769   1.00 25.27 ? 261  ARG   A NE  1 
ATOM   1696 C  CZ  . ARG   A 1 238 ? 0.018   -22.090 9.003   1.00 33.01 ? 261  ARG   A CZ  1 
ATOM   1697 N  NH1 . ARG   A 1 238 ? 0.297   -23.130 8.231   1.00 34.00 ? 261  ARG   A NH1 1 
ATOM   1698 N  NH2 . ARG   A 1 238 ? 0.821   -21.045 9.022   1.00 35.60 ? 261  ARG   A NH2 1 
ATOM   1699 N  N   . LEU   A 1 239 ? -5.752  -22.095 13.120  1.00 11.43 ? 262  LEU   A N   1 
ATOM   1700 C  CA  . LEU   A 1 239 ? -5.725  -21.005 14.088  1.00 11.24 ? 262  LEU   A CA  1 
ATOM   1701 C  C   . LEU   A 1 239 ? -4.332  -21.021 14.703  1.00 10.95 ? 262  LEU   A C   1 
ATOM   1702 O  O   . LEU   A 1 239 ? -3.893  -22.056 15.197  1.00 10.20 ? 262  LEU   A O   1 
ATOM   1703 C  CB  . LEU   A 1 239 ? -6.820  -21.223 15.146  1.00 11.10 ? 262  LEU   A CB  1 
ATOM   1704 C  CG  . LEU   A 1 239 ? -6.921  -20.169 16.259  1.00 11.83 ? 262  LEU   A CG  1 
ATOM   1705 C  CD1 . LEU   A 1 239 ? -7.340  -18.840 15.669  1.00 11.31 ? 262  LEU   A CD1 1 
ATOM   1706 C  CD2 . LEU   A 1 239 ? -7.870  -20.652 17.350  1.00 11.80 ? 262  LEU   A CD2 1 
ATOM   1707 N  N   . LYS   A 1 240 ? -3.679  -19.852 14.695  1.00 11.15 ? 263  LYS   A N   1 
ATOM   1708 C  CA  . LYS   A 1 240 ? -2.394  -19.669 15.337  1.00 12.69 ? 263  LYS   A CA  1 
ATOM   1709 C  C   . LYS   A 1 240 ? -2.651  -19.258 16.778  1.00 12.32 ? 263  LYS   A C   1 
ATOM   1710 O  O   . LYS   A 1 240 ? -3.362  -18.276 17.041  1.00 13.74 ? 263  LYS   A O   1 
ATOM   1711 C  CB  . LYS   A 1 240 ? -1.552  -18.633 14.591  1.00 14.39 ? 263  LYS   A CB  1 
ATOM   1712 C  CG  . LYS   A 1 240 ? -1.106  -19.169 13.231  1.00 18.50 ? 263  LYS   A CG  1 
ATOM   1713 C  CD  . LYS   A 1 240 ? -0.577  -18.168 12.223  1.00 23.25 ? 263  LYS   A CD  1 
ATOM   1714 C  CE  . LYS   A 1 240 ? -0.088  -16.891 12.743  1.00 29.98 ? 263  LYS   A CE  1 
ATOM   1715 N  NZ  . LYS   A 1 240 ? 0.998   -16.465 11.848  1.00 34.24 ? 263  LYS   A NZ  1 
ATOM   1716 N  N   . VAL   A 1 241 ? -2.074  -20.021 17.706  1.00 11.05 ? 264  VAL   A N   1 
ATOM   1717 C  CA  . VAL   A 1 241 ? -2.372  -19.797 19.111  1.00 10.91 ? 264  VAL   A CA  1 
ATOM   1718 C  C   . VAL   A 1 241 ? -1.082  -19.621 19.905  1.00 10.18 ? 264  VAL   A C   1 
ATOM   1719 O  O   . VAL   A 1 241 ? -0.134  -20.415 19.751  1.00 10.10 ? 264  VAL   A O   1 
ATOM   1720 C  CB  . VAL   A 1 241 ? -3.212  -20.953 19.672  1.00 12.22 ? 264  VAL   A CB  1 
ATOM   1721 C  CG1 . VAL   A 1 241 ? -4.495  -21.128 18.890  1.00 13.56 ? 264  VAL   A CG1 1 
ATOM   1722 C  CG2 . VAL   A 1 241 ? -2.441  -22.265 19.725  1.00 13.45 ? 264  VAL   A CG2 1 
ATOM   1723 N  N   . THR   A 1 242 ? -1.093  -18.615 20.782  1.00 9.44  ? 265  THR   A N   1 
ATOM   1724 C  CA  . THR   A 1 242 ? -0.078  -18.509 21.821  1.00 8.83  ? 265  THR   A CA  1 
ATOM   1725 C  C   . THR   A 1 242 ? -0.802  -18.466 23.159  1.00 9.13  ? 265  THR   A C   1 
ATOM   1726 O  O   . THR   A 1 242 ? -1.496  -17.490 23.460  1.00 8.56  ? 265  THR   A O   1 
ATOM   1727 C  CB  . THR   A 1 242 ? 0.836   -17.290 21.628  1.00 9.34  ? 265  THR   A CB  1 
ATOM   1728 O  OG1 . THR   A 1 242 ? 1.359   -17.227 20.296  1.00 9.43  ? 265  THR   A OG1 1 
ATOM   1729 C  CG2 . THR   A 1 242 ? 2.018   -17.335 22.574  1.00 9.67  ? 265  THR   A CG2 1 
ATOM   1730 N  N   . VAL   A 1 243 ? -0.552  -19.485 23.991  1.00 9.63  ? 266  VAL   A N   1 
ATOM   1731 C  CA  . VAL   A 1 243 ? -1.061  -19.546 25.349  1.00 9.02  ? 266  VAL   A CA  1 
ATOM   1732 C  C   . VAL   A 1 243 ? -0.031  -18.902 26.246  1.00 9.09  ? 266  VAL   A C   1 
ATOM   1733 O  O   . VAL   A 1 243 ? 1.130   -19.246 26.147  1.00 10.20 ? 266  VAL   A O   1 
ATOM   1734 C  CB  . VAL   A 1 243 ? -1.315  -21.013 25.760  1.00 9.50  ? 266  VAL   A CB  1 
ATOM   1735 C  CG1 . VAL   A 1 243 ? -1.820  -21.121 27.191  1.00 9.55  ? 266  VAL   A CG1 1 
ATOM   1736 C  CG2 . VAL   A 1 243 ? -2.278  -21.674 24.798  1.00 9.26  ? 266  VAL   A CG2 1 
ATOM   1737 N  N   . ARG   A 1 244 ? -0.449  -17.970 27.109  1.00 8.67  ? 267  ARG   A N   1 
ATOM   1738 C  CA  . ARG   A 1 244 ? 0.470   -17.254 27.979  1.00 8.59  ? 267  ARG   A CA  1 
ATOM   1739 C  C   . ARG   A 1 244 ? -0.064  -17.243 29.404  1.00 9.31  ? 267  ARG   A C   1 
ATOM   1740 O  O   . ARG   A 1 244 ? -1.272  -17.246 29.630  1.00 8.54  ? 267  ARG   A O   1 
ATOM   1741 C  CB  . ARG   A 1 244 ? 0.613   -15.812 27.492  1.00 9.11  ? 267  ARG   A CB  1 
ATOM   1742 C  CG  . ARG   A 1 244 ? 1.143   -15.741 26.066  1.00 8.47  ? 267  ARG   A CG  1 
ATOM   1743 C  CD  . ARG   A 1 244 ? 1.383   -14.273 25.700  1.00 8.88  ? 267  ARG   A CD  1 
ATOM   1744 N  NE  . ARG   A 1 244 ? 1.786   -14.059 24.313  1.00 9.01  ? 267  ARG   A NE  1 
ATOM   1745 C  CZ  . ARG   A 1 244 ? 3.023   -14.175 23.857  1.00 10.09 ? 267  ARG   A CZ  1 
ATOM   1746 N  NH1 . ARG   A 1 244 ? 3.973   -14.539 24.702  1.00 10.30 ? 267  ARG   A NH1 1 
ATOM   1747 N  NH2 . ARG   A 1 244 ? 3.317   -13.871 22.593  1.00 9.91  ? 267  ARG   A NH2 1 
ATOM   1748 N  N   . GLY   A 1 245 ? 0.842   -17.212 30.371  1.00 9.37  ? 268  GLY   A N   1 
ATOM   1749 C  CA  . GLY   A 1 245 ? 0.363   -17.003 31.726  1.00 10.84 ? 268  GLY   A CA  1 
ATOM   1750 C  C   . GLY   A 1 245 ? 1.450   -16.920 32.787  1.00 11.01 ? 268  GLY   A C   1 
ATOM   1751 O  O   . GLY   A 1 245 ? 2.563   -16.434 32.536  1.00 11.58 ? 268  GLY   A O   1 
ATOM   1752 N  N   . ALA   A 1 246 ? 1.069   -17.387 33.985  1.00 10.71 ? 269  ALA   A N   1 
ATOM   1753 C  CA  . ALA   A 1 246 ? 1.864   -17.250 35.190  1.00 11.14 ? 269  ALA   A CA  1 
ATOM   1754 C  C   . ALA   A 1 246 ? 2.316   -18.640 35.615  1.00 12.82 ? 269  ALA   A C   1 
ATOM   1755 O  O   . ALA   A 1 246 ? 1.486   -19.499 35.934  1.00 14.20 ? 269  ALA   A O   1 
ATOM   1756 C  CB  . ALA   A 1 246 ? 1.051   -16.596 36.306  1.00 12.45 ? 269  ALA   A CB  1 
ATOM   1757 N  N   . GLY   A 1 247 ? 3.630   -18.886 35.590  1.00 12.95 ? 270  GLY   A N   1 
ATOM   1758 C  CA  . GLY   A 1 247 ? 4.139   -20.154 36.080  1.00 14.13 ? 270  GLY   A CA  1 
ATOM   1759 C  C   . GLY   A 1 247 ? 3.962   -21.310 35.102  1.00 14.57 ? 270  GLY   A C   1 
ATOM   1760 O  O   . GLY   A 1 247 ? 4.216   -22.439 35.481  1.00 17.28 ? 270  GLY   A O   1 
ATOM   1761 N  N   . ILE   A 1 248 ? 3.493   -21.068 33.866  1.00 13.74 ? 271  ILE   A N   1 
ATOM   1762 C  CA  . ILE   A 1 248 ? 3.146   -22.180 32.991  1.00 14.66 ? 271  ILE   A CA  1 
ATOM   1763 C  C   . ILE   A 1 248 ? 4.161   -22.325 31.856  1.00 13.17 ? 271  ILE   A C   1 
ATOM   1764 O  O   . ILE   A 1 248 ? 3.965   -23.098 30.915  1.00 12.83 ? 271  ILE   A O   1 
ATOM   1765 C  CB  . ILE   A 1 248 ? 1.705   -22.072 32.444  1.00 14.12 ? 271  ILE   A CB  1 
ATOM   1766 C  CG1 . ILE   A 1 248 ? 1.347   -20.680 31.869  1.00 12.97 ? 271  ILE   A CG1 1 
ATOM   1767 C  CG2 . ILE   A 1 248 ? 0.705   -22.479 33.530  1.00 15.72 ? 271  ILE   A CG2 1 
ATOM   1768 C  CD1 . ILE   A 1 248 ? 0.095   -20.710 31.015  1.00 11.37 ? 271  ILE   A CD1 1 
ATOM   1769 N  N   . SER   A 1 249 ? 5.263   -21.573 31.908  1.00 14.53 ? 272  SER   A N   1 
ATOM   1770 C  CA  . SER   A 1 249 ? 6.129   -21.489 30.744  1.00 17.51 ? 272  SER   A CA  1 
ATOM   1771 C  C   . SER   A 1 249 ? 6.845   -22.818 30.520  1.00 19.14 ? 272  SER   A C   1 
ATOM   1772 O  O   . SER   A 1 249 ? 7.319   -23.078 29.412  1.00 23.57 ? 272  SER   A O   1 
ATOM   1773 C  CB  . SER   A 1 249 ? 7.133   -20.335 30.825  1.00 19.67 ? 272  SER   A CB  1 
ATOM   1774 O  OG  . SER   A 1 249 ? 7.932   -20.462 31.986  1.00 20.71 ? 272  SER   A OG  1 
ATOM   1775 N  N   . GLY   A 1 250 ? 6.880   -23.686 31.527  1.00 19.92 ? 273  GLY   A N   1 
ATOM   1776 C  CA  . GLY   A 1 250 ? 7.482   -24.991 31.274  1.00 24.17 ? 273  GLY   A CA  1 
ATOM   1777 C  C   . GLY   A 1 250 ? 6.503   -26.057 30.776  1.00 24.76 ? 273  GLY   A C   1 
ATOM   1778 O  O   . GLY   A 1 250 ? 6.892   -27.209 30.586  1.00 24.00 ? 273  GLY   A O   1 
ATOM   1779 N  N   . HIS   A 1 251 ? 5.235   -25.687 30.591  1.00 22.41 ? 274  HIS   A N   1 
ATOM   1780 C  CA  . HIS   A 1 251 ? 4.184   -26.660 30.349  1.00 20.19 ? 274  HIS   A CA  1 
ATOM   1781 C  C   . HIS   A 1 251 ? 3.860   -26.720 28.859  1.00 18.36 ? 274  HIS   A C   1 
ATOM   1782 O  O   . HIS   A 1 251 ? 4.191   -25.850 28.065  1.00 15.99 ? 274  HIS   A O   1 
ATOM   1783 C  CB  . HIS   A 1 251 ? 2.926   -26.263 31.121  1.00 23.28 ? 274  HIS   A CB  1 
ATOM   1784 C  CG  . HIS   A 1 251 ? 3.016   -26.292 32.609  1.00 26.62 ? 274  HIS   A CG  1 
ATOM   1785 N  ND1 . HIS   A 1 251 ? 4.056   -25.735 33.321  1.00 28.06 ? 274  HIS   A ND1 1 
ATOM   1786 C  CD2 . HIS   A 1 251 ? 2.137   -26.754 33.522  1.00 28.64 ? 274  HIS   A CD2 1 
ATOM   1787 C  CE1 . HIS   A 1 251 ? 3.812   -25.872 34.617  1.00 28.39 ? 274  HIS   A CE1 1 
ATOM   1788 N  NE2 . HIS   A 1 251 ? 2.649   -26.482 34.769  1.00 30.61 ? 274  HIS   A NE2 1 
ATOM   1789 N  N   . GLN   A 1 252 ? 3.156   -27.771 28.472  1.00 17.25 ? 275  GLN   A N   1 
ATOM   1790 C  CA  . GLN   A 1 252 ? 2.465   -27.813 27.210  1.00 17.31 ? 275  GLN   A CA  1 
ATOM   1791 C  C   . GLN   A 1 252 ? 1.062   -27.264 27.443  1.00 16.52 ? 275  GLN   A C   1 
ATOM   1792 O  O   . GLN   A 1 252 ? 0.595   -27.172 28.579  1.00 15.42 ? 275  GLN   A O   1 
ATOM   1793 C  CB  . GLN   A 1 252 ? 2.380   -29.255 26.702  1.00 18.28 ? 275  GLN   A CB  1 
ATOM   1794 C  CG  . GLN   A 1 252 ? 3.733   -29.849 26.335  1.00 21.69 ? 275  GLN   A CG  1 
ATOM   1795 C  CD  . GLN   A 1 252 ? 4.232   -29.417 24.965  1.00 29.63 ? 275  GLN   A CD  1 
ATOM   1796 O  OE1 . GLN   A 1 252 ? 5.046   -28.498 24.832  1.00 34.13 ? 275  GLN   A OE1 1 
ATOM   1797 N  NE2 . GLN   A 1 252 ? 3.753   -30.072 23.914  1.00 35.92 ? 275  GLN   A NE2 1 
ATOM   1798 N  N   . ALA   A 1 253 ? 0.366   -27.007 26.339  1.00 13.97 ? 276  ALA   A N   1 
ATOM   1799 C  CA  . ALA   A 1 253 ? -1.028  -26.616 26.400  1.00 14.61 ? 276  ALA   A CA  1 
ATOM   1800 C  C   . ALA   A 1 253 ? -1.805  -27.315 25.299  1.00 13.85 ? 276  ALA   A C   1 
ATOM   1801 O  O   . ALA   A 1 253 ? -1.357  -27.314 24.149  1.00 15.66 ? 276  ALA   A O   1 
ATOM   1802 C  CB  . ALA   A 1 253 ? -1.190  -25.142 26.268  1.00 15.39 ? 276  ALA   A CB  1 
ATOM   1803 N  N   . ARG   A 1 254 ? -2.976  -27.830 25.665  1.00 13.65 ? 277  ARG   A N   1 
ATOM   1804 C  CA  . ARG   A 1 254 ? -3.924  -28.358 24.710  1.00 14.38 ? 277  ARG   A CA  1 
ATOM   1805 C  C   . ARG   A 1 254 ? -4.922  -27.263 24.337  1.00 13.56 ? 277  ARG   A C   1 
ATOM   1806 O  O   . ARG   A 1 254 ? -5.574  -26.703 25.209  1.00 14.07 ? 277  ARG   A O   1 
ATOM   1807 C  CB  . ARG   A 1 254 ? -4.671  -29.568 25.273  1.00 16.90 ? 277  ARG   A CB  1 
ATOM   1808 C  CG  . ARG   A 1 254 ? -5.466  -30.301 24.205  1.00 21.63 ? 277  ARG   A CG  1 
ATOM   1809 C  CD  . ARG   A 1 254 ? -6.432  -31.367 24.713  1.00 24.49 ? 277  ARG   A CD  1 
ATOM   1810 N  NE  . ARG   A 1 254 ? -6.145  -31.822 26.076  1.00 32.91 ? 277  ARG   A NE  1 
ATOM   1811 C  CZ  . ARG   A 1 254 ? -5.449  -32.902 26.422  1.00 33.32 ? 277  ARG   A CZ  1 
ATOM   1812 N  NH1 . ARG   A 1 254 ? -4.871  -33.690 25.527  1.00 36.83 ? 277  ARG   A NH1 1 
ATOM   1813 N  NH2 . ARG   A 1 254 ? -5.306  -33.172 27.697  1.00 39.28 ? 277  ARG   A NH2 1 
ATOM   1814 N  N   . VAL   A 1 255 ? -5.000  -26.943 23.044  1.00 11.53 ? 278  VAL   A N   1 
ATOM   1815 C  CA  . VAL   A 1 255 ? -6.000  -25.992 22.573  1.00 12.08 ? 278  VAL   A CA  1 
ATOM   1816 C  C   . VAL   A 1 255 ? -6.919  -26.695 21.592  1.00 11.97 ? 278  VAL   A C   1 
ATOM   1817 O  O   . VAL   A 1 255 ? -6.427  -27.347 20.666  1.00 12.74 ? 278  VAL   A O   1 
ATOM   1818 C  CB  . VAL   A 1 255 ? -5.366  -24.749 21.923  1.00 11.13 ? 278  VAL   A CB  1 
ATOM   1819 C  CG1 . VAL   A 1 255 ? -6.426  -23.739 21.464  1.00 12.04 ? 278  VAL   A CG1 1 
ATOM   1820 C  CG2 . VAL   A 1 255 ? -4.365  -24.126 22.879  1.00 12.34 ? 278  VAL   A CG2 1 
ATOM   1821 N  N   . THR   A 1 256 ? -8.226  -26.506 21.806  1.00 11.86 ? 279  THR   A N   1 
ATOM   1822 C  CA  . THR   A 1 256 ? -9.266  -27.177 21.036  1.00 11.54 ? 279  THR   A CA  1 
ATOM   1823 C  C   . THR   A 1 256 ? -10.227 -26.120 20.501  1.00 11.17 ? 279  THR   A C   1 
ATOM   1824 O  O   . THR   A 1 256 ? -10.674 -25.230 21.223  1.00 10.25 ? 279  THR   A O   1 
ATOM   1825 C  CB  . THR   A 1 256 ? -10.012 -28.186 21.905  1.00 12.44 ? 279  THR   A CB  1 
ATOM   1826 O  OG1 . THR   A 1 256 ? -9.002  -29.068 22.378  1.00 12.55 ? 279  THR   A OG1 1 
ATOM   1827 C  CG2 . THR   A 1 256 ? -11.107 -28.922 21.155  1.00 13.35 ? 279  THR   A CG2 1 
ATOM   1828 N  N   . VAL   A 1 257 ? -10.514 -26.222 19.209  1.00 10.45 ? 280  VAL   A N   1 
ATOM   1829 C  CA  . VAL   A 1 257 ? -11.511 -25.401 18.537  1.00 10.87 ? 280  VAL   A CA  1 
ATOM   1830 C  C   . VAL   A 1 257 ? -12.731 -26.279 18.288  1.00 11.47 ? 280  VAL   A C   1 
ATOM   1831 O  O   . VAL   A 1 257 ? -12.571 -27.438 17.885  1.00 11.99 ? 280  VAL   A O   1 
ATOM   1832 C  CB  . VAL   A 1 257 ? -10.966 -24.856 17.210  1.00 10.49 ? 280  VAL   A CB  1 
ATOM   1833 C  CG1 . VAL   A 1 257 ? -11.974 -23.967 16.507  1.00 11.53 ? 280  VAL   A CG1 1 
ATOM   1834 C  CG2 . VAL   A 1 257 ? -9.670  -24.077 17.390  1.00 10.74 ? 280  VAL   A CG2 1 
ATOM   1835 N  N   . SER   A 1 258 ? -13.918 -25.723 18.546  1.00 10.87 ? 281  SER   A N   1 
ATOM   1836 C  CA  . SER   A 1 258 ? -15.162 -26.453 18.445  1.00 11.23 ? 281  SER   A CA  1 
ATOM   1837 C  C   . SER   A 1 258 ? -16.294 -25.505 18.072  1.00 12.02 ? 281  SER   A C   1 
ATOM   1838 O  O   . SER   A 1 258 ? -16.167 -24.288 18.117  1.00 11.63 ? 281  SER   A O   1 
ATOM   1839 C  CB  . SER   A 1 258 ? -15.458 -27.185 19.745  1.00 11.34 ? 281  SER   A CB  1 
ATOM   1840 O  OG  . SER   A 1 258 ? -15.643 -26.280 20.831  1.00 11.35 ? 281  SER   A OG  1 
ATOM   1841 N  N   . THR   A 1 259 ? -17.428 -26.112 17.740  1.00 13.26 ? 282  THR   A N   1 
ATOM   1842 C  CA  . THR   A 1 259 ? -18.667 -25.408 17.480  1.00 12.24 ? 282  THR   A CA  1 
ATOM   1843 C  C   . THR   A 1 259 ? -19.770 -26.336 17.980  1.00 14.16 ? 282  THR   A C   1 
ATOM   1844 O  O   . THR   A 1 259 ? -19.808 -27.486 17.582  1.00 14.39 ? 282  THR   A O   1 
ATOM   1845 C  CB  . THR   A 1 259 ? -18.828 -24.995 16.022  1.00 13.73 ? 282  THR   A CB  1 
ATOM   1846 O  OG1 . THR   A 1 259 ? -20.092 -24.348 15.887  1.00 13.78 ? 282  THR   A OG1 1 
ATOM   1847 C  CG2 . THR   A 1 259 ? -18.800 -26.122 15.011  1.00 14.07 ? 282  THR   A CG2 1 
ATOM   1848 N  N   . GLY   A 1 260 ? -20.580 -25.838 18.908  1.00 15.44 ? 283  GLY   A N   1 
ATOM   1849 C  CA  . GLY   A 1 260 ? -21.557 -26.674 19.585  1.00 17.51 ? 283  GLY   A CA  1 
ATOM   1850 C  C   . GLY   A 1 260 ? -20.851 -27.875 20.190  1.00 16.56 ? 283  GLY   A C   1 
ATOM   1851 O  O   . GLY   A 1 260 ? -19.814 -27.699 20.816  1.00 15.81 ? 283  GLY   A O   1 
ATOM   1852 N  N   . GLY   A 1 261 ? -21.361 -29.094 19.936  1.00 16.83 ? 284  GLY   A N   1 
ATOM   1853 C  CA  . GLY   A 1 261 ? -20.734 -30.282 20.501  1.00 14.89 ? 284  GLY   A CA  1 
ATOM   1854 C  C   . GLY   A 1 261 ? -19.636 -30.877 19.603  1.00 15.56 ? 284  GLY   A C   1 
ATOM   1855 O  O   . GLY   A 1 261 ? -19.071 -31.913 19.933  1.00 15.45 ? 284  GLY   A O   1 
ATOM   1856 N  N   . THR   A 1 262 ? -19.339 -30.226 18.465  1.00 15.18 ? 285  THR   A N   1 
ATOM   1857 C  CA  . THR   A 1 262 ? -18.432 -30.724 17.446  1.00 15.71 ? 285  THR   A CA  1 
ATOM   1858 C  C   . THR   A 1 262 ? -17.028 -30.184 17.679  1.00 15.08 ? 285  THR   A C   1 
ATOM   1859 O  O   . THR   A 1 262 ? -16.799 -28.987 17.530  1.00 14.16 ? 285  THR   A O   1 
ATOM   1860 C  CB  . THR   A 1 262 ? -18.896 -30.264 16.056  1.00 18.28 ? 285  THR   A CB  1 
ATOM   1861 O  OG1 . THR   A 1 262 ? -20.163 -30.849 15.816  1.00 23.11 ? 285  THR   A OG1 1 
ATOM   1862 C  CG2 . THR   A 1 262 ? -17.940 -30.697 14.964  1.00 19.25 ? 285  THR   A CG2 1 
ATOM   1863 N  N   . THR   A 1 263 ? -16.073 -31.078 17.939  1.00 13.71 ? 286  THR   A N   1 
ATOM   1864 C  CA  . THR   A 1 263 ? -14.678 -30.733 17.888  1.00 14.57 ? 286  THR   A CA  1 
ATOM   1865 C  C   . THR   A 1 263 ? -14.275 -30.464 16.444  1.00 15.30 ? 286  THR   A C   1 
ATOM   1866 O  O   . THR   A 1 263 ? -14.507 -31.308 15.588  1.00 15.67 ? 286  THR   A O   1 
ATOM   1867 C  CB  . THR   A 1 263 ? -13.853 -31.888 18.439  1.00 16.22 ? 286  THR   A CB  1 
ATOM   1868 O  OG1 . THR   A 1 263 ? -14.399 -32.188 19.724  1.00 17.66 ? 286  THR   A OG1 1 
ATOM   1869 C  CG2 . THR   A 1 263 ? -12.378 -31.539 18.468  1.00 15.75 ? 286  THR   A CG2 1 
ATOM   1870 N  N   . VAL   A 1 264 ? -13.625 -29.323 16.189  1.00 13.17 ? 287  VAL   A N   1 
ATOM   1871 C  CA  . VAL   A 1 264 ? -13.194 -28.957 14.847  1.00 13.75 ? 287  VAL   A CA  1 
ATOM   1872 C  C   . VAL   A 1 264 ? -11.710 -29.259 14.661  1.00 13.60 ? 287  VAL   A C   1 
ATOM   1873 O  O   . VAL   A 1 264 ? -11.277 -29.670 13.581  1.00 14.00 ? 287  VAL   A O   1 
ATOM   1874 C  CB  . VAL   A 1 264 ? -13.521 -27.460 14.655  1.00 16.04 ? 287  VAL   A CB  1 
ATOM   1875 C  CG1 . VAL   A 1 264 ? -12.853 -26.881 13.423  1.00 17.46 ? 287  VAL   A CG1 1 
ATOM   1876 C  CG2 . VAL   A 1 264 ? -15.027 -27.238 14.626  1.00 16.04 ? 287  VAL   A CG2 1 
ATOM   1877 N  N   . GLY   A 1 265 ? -10.926 -28.963 15.703  1.00 13.58 ? 288  GLY   A N   1 
ATOM   1878 C  CA  . GLY   A 1 265 ? -9.533  -29.339 15.750  1.00 12.90 ? 288  GLY   A CA  1 
ATOM   1879 C  C   . GLY   A 1 265 ? -8.961  -29.144 17.148  1.00 13.26 ? 288  GLY   A C   1 
ATOM   1880 O  O   . GLY   A 1 265 ? -9.513  -28.424 17.997  1.00 12.49 ? 288  GLY   A O   1 
ATOM   1881 N  N   . THR   A 1 266 ? -7.846  -29.838 17.360  1.00 13.12 ? 289  THR   A N   1 
ATOM   1882 C  CA  . THR   A 1 266 ? -7.123  -29.783 18.614  1.00 14.05 ? 289  THR   A CA  1 
ATOM   1883 C  C   . THR   A 1 266 ? -5.636  -29.989 18.332  1.00 15.40 ? 289  THR   A C   1 
ATOM   1884 O  O   . THR   A 1 266 ? -5.247  -30.613 17.327  1.00 15.80 ? 289  THR   A O   1 
ATOM   1885 C  CB  . THR   A 1 266 ? -7.731  -30.836 19.551  1.00 14.92 ? 289  THR   A CB  1 
ATOM   1886 O  OG1 . THR   A 1 266 ? -7.156  -30.613 20.837  1.00 14.46 ? 289  THR   A OG1 1 
ATOM   1887 C  CG2 . THR   A 1 266 ? -7.401  -32.248 19.105  1.00 15.63 ? 289  THR   A CG2 1 
ATOM   1888 N  N   . ALA   A 1 267 ? -4.801  -29.389 19.183  1.00 14.00 ? 290  ALA   A N   1 
ATOM   1889 C  CA  . ALA   A 1 267 ? -3.367  -29.577 19.125  1.00 14.22 ? 290  ALA   A CA  1 
ATOM   1890 C  C   . ALA   A 1 267 ? -2.807  -29.309 20.510  1.00 14.17 ? 290  ALA   A C   1 
ATOM   1891 O  O   . ALA   A 1 267 ? -3.388  -28.547 21.291  1.00 13.08 ? 290  ALA   A O   1 
ATOM   1892 C  CB  . ALA   A 1 267 ? -2.749  -28.690 18.075  1.00 14.38 ? 290  ALA   A CB  1 
ATOM   1893 N  N   . THR   A 1 268 ? -1.692  -29.987 20.811  1.00 14.61 ? 291  THR   A N   1 
ATOM   1894 C  CA  . THR   A 1 268 ? -0.948  -29.712 22.019  1.00 15.19 ? 291  THR   A CA  1 
ATOM   1895 C  C   . THR   A 1 268 ? 0.361   -29.056 21.599  1.00 16.36 ? 291  THR   A C   1 
ATOM   1896 O  O   . THR   A 1 268 ? 1.051   -29.514 20.692  1.00 17.85 ? 291  THR   A O   1 
ATOM   1897 C  CB  . THR   A 1 268 ? -0.773  -30.986 22.849  1.00 16.79 ? 291  THR   A CB  1 
ATOM   1898 O  OG1 . THR   A 1 268 ? -2.057  -31.455 23.266  1.00 17.64 ? 291  THR   A OG1 1 
ATOM   1899 C  CG2 . THR   A 1 268 ? 0.024   -30.743 24.112  1.00 19.39 ? 291  THR   A CG2 1 
ATOM   1900 N  N   . GLY   A 1 269 ? 0.706   -27.935 22.236  1.00 14.72 ? 292  GLY   A N   1 
ATOM   1901 C  CA  . GLY   A 1 269 ? 1.933   -27.260 21.875  1.00 13.56 ? 292  GLY   A CA  1 
ATOM   1902 C  C   . GLY   A 1 269 ? 2.542   -26.584 23.088  1.00 13.73 ? 292  GLY   A C   1 
ATOM   1903 O  O   . GLY   A 1 269 ? 2.009   -26.691 24.187  1.00 15.35 ? 292  GLY   A O   1 
ATOM   1904 N  N   . PRO   A 1 270 ? 3.674   -25.886 22.915  1.00 14.84 ? 293  PRO   A N   1 
ATOM   1905 C  CA  . PRO   A 1 270 ? 4.408   -25.295 24.027  1.00 14.59 ? 293  PRO   A CA  1 
ATOM   1906 C  C   . PRO   A 1 270 ? 3.679   -24.034 24.459  1.00 15.30 ? 293  PRO   A C   1 
ATOM   1907 O  O   . PRO   A 1 270 ? 3.204   -23.293 23.609  1.00 18.05 ? 293  PRO   A O   1 
ATOM   1908 C  CB  . PRO   A 1 270 ? 5.763   -24.972 23.400  1.00 15.94 ? 293  PRO   A CB  1 
ATOM   1909 C  CG  . PRO   A 1 270 ? 5.437   -24.742 21.938  1.00 16.56 ? 293  PRO   A CG  1 
ATOM   1910 C  CD  . PRO   A 1 270 ? 4.284   -25.639 21.604  1.00 16.79 ? 293  PRO   A CD  1 
ATOM   1911 N  N   . VAL   A 1 271 ? 3.634   -23.761 25.761  1.00 14.20 ? 294  VAL   A N   1 
ATOM   1912 C  CA  . VAL   A 1 271 ? 3.172   -22.467 26.238  1.00 12.98 ? 294  VAL   A CA  1 
ATOM   1913 C  C   . VAL   A 1 271 ? 4.164   -21.381 25.838  1.00 12.71 ? 294  VAL   A C   1 
ATOM   1914 O  O   . VAL   A 1 271 ? 5.362   -21.585 25.941  1.00 12.78 ? 294  VAL   A O   1 
ATOM   1915 C  CB  . VAL   A 1 271 ? 3.022   -22.544 27.767  1.00 11.43 ? 294  VAL   A CB  1 
ATOM   1916 C  CG1 . VAL   A 1 271 ? 2.879   -21.185 28.444  1.00 12.91 ? 294  VAL   A CG1 1 
ATOM   1917 C  CG2 . VAL   A 1 271 ? 1.838   -23.435 28.113  1.00 11.13 ? 294  VAL   A CG2 1 
ATOM   1918 N  N   . GLY   A 1 272 ? 3.654   -20.216 25.439  1.00 11.69 ? 295  GLY   A N   1 
ATOM   1919 C  CA  . GLY   A 1 272 ? 4.495   -19.044 25.232  1.00 11.56 ? 295  GLY   A CA  1 
ATOM   1920 C  C   . GLY   A 1 272 ? 5.093   -18.953 23.831  1.00 11.92 ? 295  GLY   A C   1 
ATOM   1921 O  O   . GLY   A 1 272 ? 5.719   -17.955 23.507  1.00 11.52 ? 295  GLY   A O   1 
ATOM   1922 N  N   . THR   A 1 273 ? 4.879   -19.964 23.002  1.00 11.95 ? 296  THR   A N   1 
ATOM   1923 C  CA  . THR   A 1 273 ? 5.343   -19.959 21.621  1.00 12.74 ? 296  THR   A CA  1 
ATOM   1924 C  C   . THR   A 1 273 ? 4.169   -20.314 20.718  1.00 12.37 ? 296  THR   A C   1 
ATOM   1925 O  O   . THR   A 1 273 ? 3.404   -21.225 21.030  1.00 10.83 ? 296  THR   A O   1 
ATOM   1926 C  CB  . THR   A 1 273 ? 6.457   -21.001 21.493  1.00 15.40 ? 296  THR   A CB  1 
ATOM   1927 O  OG1 . THR   A 1 273 ? 7.560   -20.530 22.272  1.00 17.53 ? 296  THR   A OG1 1 
ATOM   1928 C  CG2 . THR   A 1 273 ? 6.955   -21.209 20.073  1.00 15.14 ? 296  THR   A CG2 1 
ATOM   1929 N  N   . GLU   A 1 274 ? 4.047   -19.613 19.595  1.00 11.61 ? 297  GLU   A N   1 
ATOM   1930 C  CA  . GLU   A 1 274 ? 2.908   -19.810 18.697  1.00 11.74 ? 297  GLU   A CA  1 
ATOM   1931 C  C   . GLU   A 1 274 ? 2.904   -21.229 18.128  1.00 11.78 ? 297  GLU   A C   1 
ATOM   1932 O  O   . GLU   A 1 274 ? 3.941   -21.738 17.706  1.00 12.49 ? 297  GLU   A O   1 
ATOM   1933 C  CB  . GLU   A 1 274 ? 2.965   -18.762 17.585  1.00 12.89 ? 297  GLU   A CB  1 
ATOM   1934 C  CG  . GLU   A 1 274 ? 1.680   -18.646 16.780  1.00 13.07 ? 297  GLU   A CG  1 
ATOM   1935 C  CD  . GLU   A 1 274 ? 1.655   -17.428 15.888  1.00 15.86 ? 297  GLU   A CD  1 
ATOM   1936 O  OE1 . GLU   A 1 274 ? 2.421   -17.444 14.913  1.00 17.41 ? 297  GLU   A OE1 1 
ATOM   1937 O  OE2 . GLU   A 1 274 ? 0.859   -16.501 16.147  1.00 18.17 ? 297  GLU   A OE2 1 
ATOM   1938 N  N   . PHE   A 1 275 ? 1.725   -21.851 18.063  1.00 10.49 ? 298  PHE   A N   1 
ATOM   1939 C  CA  . PHE   A 1 275 ? 1.587   -23.146 17.396  1.00 10.44 ? 298  PHE   A CA  1 
ATOM   1940 C  C   . PHE   A 1 275 ? 0.238   -23.146 16.721  1.00 11.65 ? 298  PHE   A C   1 
ATOM   1941 O  O   . PHE   A 1 275 ? -0.511  -22.191 16.900  1.00 12.20 ? 298  PHE   A O   1 
ATOM   1942 C  CB  . PHE   A 1 275 ? 1.803   -24.327 18.342  1.00 11.11 ? 298  PHE   A CB  1 
ATOM   1943 C  CG  . PHE   A 1 275 ? 0.801   -24.542 19.466  1.00 10.73 ? 298  PHE   A CG  1 
ATOM   1944 C  CD1 . PHE   A 1 275 ? 0.946   -23.865 20.678  1.00 10.58 ? 298  PHE   A CD1 1 
ATOM   1945 C  CD2 . PHE   A 1 275 ? -0.266  -25.427 19.314  1.00 10.05 ? 298  PHE   A CD2 1 
ATOM   1946 C  CE1 . PHE   A 1 275 ? 0.077   -24.119 21.737  1.00 11.37 ? 298  PHE   A CE1 1 
ATOM   1947 C  CE2 . PHE   A 1 275 ? -1.130  -25.686 20.386  1.00 10.03 ? 298  PHE   A CE2 1 
ATOM   1948 C  CZ  . PHE   A 1 275 ? -0.991  -25.004 21.586  1.00 10.77 ? 298  PHE   A CZ  1 
ATOM   1949 N  N   . THR   A 1 276 ? -0.068  -24.137 15.876  1.00 12.35 ? 299  THR   A N   1 
ATOM   1950 C  CA  . THR   A 1 276 ? -1.292  -24.012 15.116  1.00 13.62 ? 299  THR   A CA  1 
ATOM   1951 C  C   . THR   A 1 276 ? -2.242  -25.144 15.498  1.00 11.96 ? 299  THR   A C   1 
ATOM   1952 O  O   . THR   A 1 276 ? -1.821  -26.216 15.904  1.00 10.86 ? 299  THR   A O   1 
ATOM   1953 C  CB  . THR   A 1 276 ? -1.047  -23.961 13.603  1.00 16.27 ? 299  THR   A CB  1 
ATOM   1954 O  OG1 . THR   A 1 276 ? -0.431  -25.179 13.222  1.00 17.05 ? 299  THR   A OG1 1 
ATOM   1955 C  CG2 . THR   A 1 276 ? -0.168  -22.803 13.173  1.00 16.53 ? 299  THR   A CG2 1 
ATOM   1956 N  N   . VAL   A 1 277 ? -3.538  -24.833 15.433  1.00 11.60 ? 300  VAL   A N   1 
ATOM   1957 C  CA  . VAL   A 1 277 ? -4.606  -25.787 15.677  1.00 11.51 ? 300  VAL   A CA  1 
ATOM   1958 C  C   . VAL   A 1 277 ? -5.391  -25.873 14.384  1.00 12.39 ? 300  VAL   A C   1 
ATOM   1959 O  O   . VAL   A 1 277 ? -5.761  -24.835 13.838  1.00 12.64 ? 300  VAL   A O   1 
ATOM   1960 C  CB  . VAL   A 1 277 ? -5.526  -25.370 16.833  1.00 11.79 ? 300  VAL   A CB  1 
ATOM   1961 C  CG1 . VAL   A 1 277 ? -6.677  -26.377 17.000  1.00 11.79 ? 300  VAL   A CG1 1 
ATOM   1962 C  CG2 . VAL   A 1 277 ? -4.732  -25.169 18.120  1.00 12.67 ? 300  VAL   A CG2 1 
ATOM   1963 N  N   . PRO   A 1 278 ? -5.643  -27.067 13.805  1.00 12.32 ? 301  PRO   A N   1 
ATOM   1964 C  CA  . PRO   A 1 278 ? -6.438  -27.134 12.577  1.00 12.67 ? 301  PRO   A CA  1 
ATOM   1965 C  C   . PRO   A 1 278 ? -7.844  -26.575 12.724  1.00 13.02 ? 301  PRO   A C   1 
ATOM   1966 O  O   . PRO   A 1 278 ? -8.508  -26.785 13.729  1.00 11.17 ? 301  PRO   A O   1 
ATOM   1967 C  CB  . PRO   A 1 278 ? -6.521  -28.628 12.251  1.00 13.28 ? 301  PRO   A CB  1 
ATOM   1968 C  CG  . PRO   A 1 278 ? -5.379  -29.245 13.002  1.00 13.53 ? 301  PRO   A CG  1 
ATOM   1969 C  CD  . PRO   A 1 278 ? -5.240  -28.399 14.289  1.00 12.77 ? 301  PRO   A CD  1 
ATOM   1970 N  N   . VAL   A 1 279 ? -8.301  -25.889 11.681  1.00 12.79 ? 302  VAL   A N   1 
ATOM   1971 C  CA  . VAL   A 1 279 ? -9.681  -25.440 11.563  1.00 12.36 ? 302  VAL   A CA  1 
ATOM   1972 C  C   . VAL   A 1 279 ? -10.083 -25.784 10.132  1.00 13.40 ? 302  VAL   A C   1 
ATOM   1973 O  O   . VAL   A 1 279 ? -10.083 -24.952 9.213   1.00 13.21 ? 302  VAL   A O   1 
ATOM   1974 C  CB  . VAL   A 1 279 ? -9.894  -23.943 11.872  1.00 12.38 ? 302  VAL   A CB  1 
ATOM   1975 C  CG1 . VAL   A 1 279 ? -11.370 -23.540 11.745  1.00 13.05 ? 302  VAL   A CG1 1 
ATOM   1976 C  CG2 . VAL   A 1 279 ? -9.340  -23.547 13.247  1.00 11.87 ? 302  VAL   A CG2 1 
ATOM   1977 N  N   . PRO   A 1 280 ? -10.380 -27.066 9.867   1.00 15.09 ? 303  PRO   A N   1 
ATOM   1978 C  CA  . PRO   A 1 280 ? -10.687 -27.472 8.491   1.00 14.90 ? 303  PRO   A CA  1 
ATOM   1979 C  C   . PRO   A 1 280 ? -11.964 -26.808 7.995   1.00 14.51 ? 303  PRO   A C   1 
ATOM   1980 O  O   . PRO   A 1 280 ? -12.909 -26.636 8.767   1.00 14.38 ? 303  PRO   A O   1 
ATOM   1981 C  CB  . PRO   A 1 280 ? -10.813 -29.005 8.575   1.00 15.50 ? 303  PRO   A CB  1 
ATOM   1982 C  CG  . PRO   A 1 280 ? -10.325 -29.399 9.956   1.00 17.86 ? 303  PRO   A CG  1 
ATOM   1983 C  CD  . PRO   A 1 280 ? -10.391 -28.177 10.838  1.00 16.72 ? 303  PRO   A CD  1 
ATOM   1984 N  N   . ASN   A 1 281 ? -12.006 -26.505 6.695   1.00 15.53 ? 304  ASN   A N   1 
ATOM   1985 C  CA  . ASN   A 1 281 ? -13.213 -25.984 6.062   1.00 17.88 ? 304  ASN   A CA  1 
ATOM   1986 C  C   . ASN   A 1 281 ? -13.729 -24.795 6.866   1.00 16.33 ? 304  ASN   A C   1 
ATOM   1987 O  O   . ASN   A 1 281 ? -14.863 -24.775 7.283   1.00 14.92 ? 304  ASN   A O   1 
ATOM   1988 C  CB  . ASN   A 1 281 ? -14.302 -27.044 5.929   1.00 22.81 ? 304  ASN   A CB  1 
ATOM   1989 C  CG  . ASN   A 1 281 ? -13.859 -28.172 5.015   1.00 30.49 ? 304  ASN   A CG  1 
ATOM   1990 O  OD1 . ASN   A 1 281 ? -13.532 -27.946 3.843   1.00 34.30 ? 304  ASN   A OD1 1 
ATOM   1991 N  ND2 . ASN   A 1 281 ? -13.782 -29.381 5.543   1.00 37.06 ? 304  ASN   A ND2 1 
ATOM   1992 N  N   . PRO   A 1 282 ? -12.908 -23.777 7.168   1.00 13.84 ? 305  PRO   A N   1 
ATOM   1993 C  CA  . PRO   A 1 282 ? -13.350 -22.743 8.099   1.00 14.05 ? 305  PRO   A CA  1 
ATOM   1994 C  C   . PRO   A 1 282 ? -14.542 -21.931 7.621   1.00 14.18 ? 305  PRO   A C   1 
ATOM   1995 O  O   . PRO   A 1 282 ? -14.595 -21.470 6.476   1.00 16.33 ? 305  PRO   A O   1 
ATOM   1996 C  CB  . PRO   A 1 282 ? -12.132 -21.856 8.220   1.00 13.43 ? 305  PRO   A CB  1 
ATOM   1997 C  CG  . PRO   A 1 282 ? -11.373 -22.098 6.935   1.00 13.96 ? 305  PRO   A CG  1 
ATOM   1998 C  CD  . PRO   A 1 282 ? -11.544 -23.583 6.675   1.00 14.14 ? 305  PRO   A CD  1 
ATOM   1999 N  N   . ARG   A 1 283 ? -15.476 -21.715 8.539   1.00 12.94 ? 306  ARG   A N   1 
ATOM   2000 C  CA  . ARG   A 1 283 ? -16.520 -20.714 8.352   1.00 12.33 ? 306  ARG   A CA  1 
ATOM   2001 C  C   . ARG   A 1 283 ? -15.968 -19.359 8.796   1.00 12.06 ? 306  ARG   A C   1 
ATOM   2002 O  O   . ARG   A 1 283 ? -15.514 -19.203 9.932   1.00 11.67 ? 306  ARG   A O   1 
ATOM   2003 C  CB  . ARG   A 1 283 ? -17.766 -21.181 9.103   1.00 12.53 ? 306  ARG   A CB  1 
ATOM   2004 C  CG  . ARG   A 1 283 ? -18.912 -20.198 8.923   1.00 13.14 ? 306  ARG   A CG  1 
ATOM   2005 C  CD  . ARG   A 1 283 ? -20.233 -20.794 9.354   1.00 13.69 ? 306  ARG   A CD  1 
ATOM   2006 N  NE  . ARG   A 1 283 ? -21.230 -19.736 9.537   1.00 14.58 ? 306  ARG   A NE  1 
ATOM   2007 C  CZ  . ARG   A 1 283 ? -22.458 -19.960 9.964   1.00 17.52 ? 306  ARG   A CZ  1 
ATOM   2008 N  NH1 . ARG   A 1 283 ? -22.824 -21.163 10.358  1.00 17.89 ? 306  ARG   A NH1 1 
ATOM   2009 N  NH2 . ARG   A 1 283 ? -23.303 -18.968 10.083  1.00 16.78 ? 306  ARG   A NH2 1 
ATOM   2010 N  N   . LEU   A 1 284 ? -15.968 -18.418 7.858   1.00 11.87 ? 307  LEU   A N   1 
ATOM   2011 C  CA  . LEU   A 1 284 ? -15.261 -17.152 8.030   1.00 12.37 ? 307  LEU   A CA  1 
ATOM   2012 C  C   . LEU   A 1 284 ? -16.128 -16.197 8.845   1.00 11.68 ? 307  LEU   A C   1 
ATOM   2013 O  O   . LEU   A 1 284 ? -17.353 -16.185 8.737   1.00 13.34 ? 307  LEU   A O   1 
ATOM   2014 C  CB  . LEU   A 1 284 ? -14.888 -16.527 6.689   1.00 12.02 ? 307  LEU   A CB  1 
ATOM   2015 C  CG  . LEU   A 1 284 ? -14.028 -17.397 5.757   1.00 12.94 ? 307  LEU   A CG  1 
ATOM   2016 C  CD1 . LEU   A 1 284 ? -13.729 -16.656 4.466   1.00 14.81 ? 307  LEU   A CD1 1 
ATOM   2017 C  CD2 . LEU   A 1 284 ? -12.762 -17.824 6.430   1.00 14.30 ? 307  LEU   A CD2 1 
ATOM   2018 N  N   . TRP   A 1 285 ? -15.451 -15.376 9.638   1.00 10.13 ? 308  TRP   A N   1 
ATOM   2019 C  CA  . TRP   A 1 285 ? -16.084 -14.238 10.277  1.00 10.24 ? 308  TRP   A CA  1 
ATOM   2020 C  C   . TRP   A 1 285 ? -16.113 -13.058 9.310   1.00 9.73  ? 308  TRP   A C   1 
ATOM   2021 O  O   . TRP   A 1 285 ? -15.080 -12.676 8.782   1.00 9.08  ? 308  TRP   A O   1 
ATOM   2022 C  CB  . TRP   A 1 285 ? -15.314 -13.875 11.559  1.00 10.20 ? 308  TRP   A CB  1 
ATOM   2023 C  CG  . TRP   A 1 285 ? -15.937 -12.781 12.379  1.00 10.08 ? 308  TRP   A CG  1 
ATOM   2024 C  CD1 . TRP   A 1 285 ? -16.627 -12.968 13.539  1.00 10.38 ? 308  TRP   A CD1 1 
ATOM   2025 C  CD2 . TRP   A 1 285 ? -15.836 -11.341 12.205  1.00 9.76  ? 308  TRP   A CD2 1 
ATOM   2026 N  NE1 . TRP   A 1 285 ? -17.000 -11.767 14.073  1.00 10.52 ? 308  TRP   A NE1 1 
ATOM   2027 C  CE2 . TRP   A 1 285 ? -16.535 -10.754 13.285  1.00 9.67  ? 308  TRP   A CE2 1 
ATOM   2028 C  CE3 . TRP   A 1 285 ? -15.285 -10.498 11.237  1.00 9.07  ? 308  TRP   A CE3 1 
ATOM   2029 C  CZ2 . TRP   A 1 285 ? -16.649 -9.377  13.447  1.00 9.21  ? 308  TRP   A CZ2 1 
ATOM   2030 C  CZ3 . TRP   A 1 285 ? -15.419 -9.131  11.386  1.00 8.85  ? 308  TRP   A CZ3 1 
ATOM   2031 C  CH2 . TRP   A 1 285 ? -16.079 -8.587  12.484  1.00 8.84  ? 308  TRP   A CH2 1 
ATOM   2032 N  N   . THR   A 1 286 ? -17.317 -12.478 9.127   1.00 9.43  ? 309  THR   A N   1 
ATOM   2033 C  CA  . THR   A 1 286 ? -17.533 -11.234 8.412   1.00 10.17 ? 309  THR   A CA  1 
ATOM   2034 C  C   . THR   A 1 286 ? -18.599 -10.465 9.168   1.00 10.70 ? 309  THR   A C   1 
ATOM   2035 O  O   . THR   A 1 286 ? -19.347 -11.005 9.988   1.00 10.11 ? 309  THR   A O   1 
ATOM   2036 C  CB  . THR   A 1 286 ? -17.970 -11.404 6.953   1.00 10.93 ? 309  THR   A CB  1 
ATOM   2037 O  OG1 . THR   A 1 286 ? -19.231 -12.077 6.974   1.00 10.14 ? 309  THR   A OG1 1 
ATOM   2038 C  CG2 . THR   A 1 286 ? -16.950 -12.185 6.152   1.00 11.33 ? 309  THR   A CG2 1 
ATOM   2039 N  N   . PRO   A 1 287 ? -18.720 -9.153  8.893   1.00 10.73 ? 310  PRO   A N   1 
ATOM   2040 C  CA  . PRO   A 1 287 ? -19.853 -8.443  9.447   1.00 11.19 ? 310  PRO   A CA  1 
ATOM   2041 C  C   . PRO   A 1 287 ? -21.215 -9.061  9.140   1.00 11.83 ? 310  PRO   A C   1 
ATOM   2042 O  O   . PRO   A 1 287 ? -22.113 -8.982  9.990   1.00 11.03 ? 310  PRO   A O   1 
ATOM   2043 C  CB  . PRO   A 1 287 ? -19.648 -7.036  8.879   1.00 11.00 ? 310  PRO   A CB  1 
ATOM   2044 C  CG  . PRO   A 1 287 ? -18.181 -6.940  8.648   1.00 11.28 ? 310  PRO   A CG  1 
ATOM   2045 C  CD  . PRO   A 1 287 ? -17.783 -8.313  8.125   1.00 11.23 ? 310  PRO   A CD  1 
ATOM   2046 N  N   . GLU   A 1 288 ? -21.378 -9.644  7.943   1.00 12.14 ? 311  GLU   A N   1 
ATOM   2047 C  CA  . GLU   A 1 288 ? -22.640 -10.237 7.532   1.00 14.35 ? 311  GLU   A CA  1 
ATOM   2048 C  C   . GLU   A 1 288 ? -22.861 -11.580 8.199   1.00 14.47 ? 311  GLU   A C   1 
ATOM   2049 O  O   . GLU   A 1 288 ? -24.012 -11.971 8.428   1.00 15.44 ? 311  GLU   A O   1 
ATOM   2050 C  CB  . GLU   A 1 288 ? -22.721 -10.478 6.029   1.00 16.42 ? 311  GLU   A CB  1 
ATOM   2051 C  CG  . GLU   A 1 288 ? -22.631 -9.176  5.245   1.00 20.79 ? 311  GLU   A CG  1 
ATOM   2052 C  CD  . GLU   A 1 288 ? -21.235 -8.615  4.970   1.00 23.96 ? 311  GLU   A CD  1 
ATOM   2053 O  OE1 . GLU   A 1 288 ? -20.145 -9.183  5.243   1.00 25.15 ? 311  GLU   A OE1 1 
ATOM   2054 O  OE2 . GLU   A 1 288 ? -21.264 -7.500  4.412   1.00 34.26 ? 311  GLU   A OE2 1 
ATOM   2055 N  N   . ASP   A 1 289 ? -21.770 -12.322 8.443   1.00 13.39 ? 312  ASP   A N   1 
ATOM   2056 C  CA  . ASP   A 1 289 ? -21.847 -13.612 9.130   1.00 12.62 ? 312  ASP   A CA  1 
ATOM   2057 C  C   . ASP   A 1 289 ? -20.755 -13.692 10.200  1.00 11.11 ? 312  ASP   A C   1 
ATOM   2058 O  O   . ASP   A 1 289 ? -19.679 -14.255 9.980   1.00 11.73 ? 312  ASP   A O   1 
ATOM   2059 C  CB  . ASP   A 1 289 ? -21.697 -14.779 8.162   1.00 13.85 ? 312  ASP   A CB  1 
ATOM   2060 C  CG  . ASP   A 1 289 ? -21.800 -16.164 8.801   1.00 15.08 ? 312  ASP   A CG  1 
ATOM   2061 O  OD1 . ASP   A 1 289 ? -22.383 -16.246 9.884   1.00 16.61 ? 312  ASP   A OD1 1 
ATOM   2062 O  OD2 . ASP   A 1 289 ? -21.282 -17.137 8.222   1.00 14.30 ? 312  ASP   A OD2 1 
ATOM   2063 N  N   . PRO   A 1 290 ? -20.963 -13.070 11.381  1.00 9.69  ? 313  PRO   A N   1 
ATOM   2064 C  CA  . PRO   A 1 290 ? -19.915 -13.021 12.402  1.00 10.09 ? 313  PRO   A CA  1 
ATOM   2065 C  C   . PRO   A 1 290 ? -19.731 -14.308 13.183  1.00 10.20 ? 313  PRO   A C   1 
ATOM   2066 O  O   . PRO   A 1 290 ? -19.871 -14.359 14.416  1.00 9.65  ? 313  PRO   A O   1 
ATOM   2067 C  CB  . PRO   A 1 290 ? -20.394 -11.854 13.258  1.00 10.19 ? 313  PRO   A CB  1 
ATOM   2068 C  CG  . PRO   A 1 290 ? -21.889 -11.900 13.154  1.00 9.44  ? 313  PRO   A CG  1 
ATOM   2069 C  CD  . PRO   A 1 290 ? -22.127 -12.214 11.689  1.00 9.56  ? 313  PRO   A CD  1 
ATOM   2070 N  N   . PHE   A 1 291 ? -19.429 -15.360 12.428  1.00 10.25 ? 314  PHE   A N   1 
ATOM   2071 C  CA  . PHE   A 1 291 ? -19.375 -16.694 13.003  1.00 10.57 ? 314  PHE   A CA  1 
ATOM   2072 C  C   . PHE   A 1 291 ? -18.221 -16.771 13.996  1.00 9.47  ? 314  PHE   A C   1 
ATOM   2073 O  O   . PHE   A 1 291 ? -17.101 -16.365 13.679  1.00 8.61  ? 314  PHE   A O   1 
ATOM   2074 C  CB  . PHE   A 1 291 ? -19.239 -17.735 11.901  1.00 10.92 ? 314  PHE   A CB  1 
ATOM   2075 C  CG  . PHE   A 1 291 ? -19.344 -19.130 12.487  1.00 11.33 ? 314  PHE   A CG  1 
ATOM   2076 C  CD1 . PHE   A 1 291 ? -20.591 -19.629 12.883  1.00 12.94 ? 314  PHE   A CD1 1 
ATOM   2077 C  CD2 . PHE   A 1 291 ? -18.210 -19.903 12.696  1.00 10.90 ? 314  PHE   A CD2 1 
ATOM   2078 C  CE1 . PHE   A 1 291 ? -20.699 -20.885 13.461  1.00 13.45 ? 314  PHE   A CE1 1 
ATOM   2079 C  CE2 . PHE   A 1 291 ? -18.315 -21.159 13.261  1.00 12.30 ? 314  PHE   A CE2 1 
ATOM   2080 C  CZ  . PHE   A 1 291 ? -19.568 -21.652 13.647  1.00 13.38 ? 314  PHE   A CZ  1 
ATOM   2081 N  N   . LEU   A 1 292 ? -18.512 -17.358 15.154  1.00 9.46  ? 315  LEU   A N   1 
ATOM   2082 C  CA  . LEU   A 1 292 ? -17.529 -17.568 16.202  1.00 9.11  ? 315  LEU   A CA  1 
ATOM   2083 C  C   . LEU   A 1 292 ? -17.457 -19.048 16.583  1.00 9.43  ? 315  LEU   A C   1 
ATOM   2084 O  O   . LEU   A 1 292 ? -18.478 -19.681 16.832  1.00 11.63 ? 315  LEU   A O   1 
ATOM   2085 C  CB  . LEU   A 1 292 ? -17.828 -16.732 17.443  1.00 9.17  ? 315  LEU   A CB  1 
ATOM   2086 C  CG  . LEU   A 1 292 ? -17.928 -15.212 17.244  1.00 9.08  ? 315  LEU   A CG  1 
ATOM   2087 C  CD1 . LEU   A 1 292 ? -18.446 -14.566 18.533  1.00 8.34  ? 315  LEU   A CD1 1 
ATOM   2088 C  CD2 . LEU   A 1 292 ? -16.612 -14.599 16.803  1.00 8.95  ? 315  LEU   A CD2 1 
ATOM   2089 N  N   . TYR   A 1 293 ? -16.238 -19.542 16.677  1.00 8.96  ? 316  TYR   A N   1 
ATOM   2090 C  CA  . TYR   A 1 293 ? -15.933 -20.875 17.147  1.00 8.67  ? 316  TYR   A CA  1 
ATOM   2091 C  C   . TYR   A 1 293 ? -15.575 -20.767 18.622  1.00 8.91  ? 316  TYR   A C   1 
ATOM   2092 O  O   . TYR   A 1 293 ? -14.901 -19.820 19.028  1.00 8.81  ? 316  TYR   A O   1 
ATOM   2093 C  CB  . TYR   A 1 293 ? -14.741 -21.493 16.429  1.00 8.69  ? 316  TYR   A CB  1 
ATOM   2094 C  CG  . TYR   A 1 293 ? -14.907 -21.892 14.957  1.00 9.52  ? 316  TYR   A CG  1 
ATOM   2095 C  CD1 . TYR   A 1 293 ? -14.739 -20.970 13.920  1.00 9.76  ? 316  TYR   A CD1 1 
ATOM   2096 C  CD2 . TYR   A 1 293 ? -15.201 -23.205 14.601  1.00 10.64 ? 316  TYR   A CD2 1 
ATOM   2097 C  CE1 . TYR   A 1 293 ? -14.814 -21.351 12.588  1.00 10.42 ? 316  TYR   A CE1 1 
ATOM   2098 C  CE2 . TYR   A 1 293 ? -15.291 -23.603 13.278  1.00 10.10 ? 316  TYR   A CE2 1 
ATOM   2099 C  CZ  . TYR   A 1 293 ? -15.094 -22.673 12.264  1.00 11.39 ? 316  TYR   A CZ  1 
ATOM   2100 O  OH  . TYR   A 1 293 ? -15.156 -23.094 10.968  1.00 10.74 ? 316  TYR   A OH  1 
ATOM   2101 N  N   . ASP   A 1 294 ? -15.962 -21.778 19.402  1.00 9.87  ? 317  ASP   A N   1 
ATOM   2102 C  CA  . ASP   A 1 294 ? -15.451 -21.921 20.751  1.00 10.63 ? 317  ASP   A CA  1 
ATOM   2103 C  C   . ASP   A 1 294 ? -13.991 -22.360 20.726  1.00 10.39 ? 317  ASP   A C   1 
ATOM   2104 O  O   . ASP   A 1 294 ? -13.563 -23.172 19.883  1.00 10.51 ? 317  ASP   A O   1 
ATOM   2105 C  CB  . ASP   A 1 294 ? -16.302 -22.890 21.543  1.00 11.87 ? 317  ASP   A CB  1 
ATOM   2106 C  CG  . ASP   A 1 294 ? -17.728 -22.443 21.754  1.00 15.11 ? 317  ASP   A CG  1 
ATOM   2107 O  OD1 . ASP   A 1 294 ? -17.939 -21.361 22.328  1.00 19.31 ? 317  ASP   A OD1 1 
ATOM   2108 O  OD2 . ASP   A 1 294 ? -18.619 -23.138 21.311  1.00 16.53 ? 317  ASP   A OD2 1 
ATOM   2109 N  N   . VAL   A 1 295 ? -13.246 -21.915 21.744  1.00 9.94  ? 318  VAL   A N   1 
ATOM   2110 C  CA  . VAL   A 1 295 ? -11.834 -22.236 21.908  1.00 10.98 ? 318  VAL   A CA  1 
ATOM   2111 C  C   . VAL   A 1 295 ? -11.632 -22.554 23.390  1.00 12.99 ? 318  VAL   A C   1 
ATOM   2112 O  O   . VAL   A 1 295 ? -12.216 -21.896 24.256  1.00 13.68 ? 318  VAL   A O   1 
ATOM   2113 C  CB  . VAL   A 1 295 ? -10.848 -21.142 21.426  1.00 12.07 ? 318  VAL   A CB  1 
ATOM   2114 C  CG1 . VAL   A 1 295 ? -9.385  -21.477 21.702  1.00 14.03 ? 318  VAL   A CG1 1 
ATOM   2115 C  CG2 . VAL   A 1 295 ? -10.998 -20.797 19.946  1.00 11.04 ? 318  VAL   A CG2 1 
ATOM   2116 N  N   . ARG   A 1 296 ? -10.918 -23.653 23.680  1.00 12.12 ? 319  ARG   A N   1 
ATOM   2117 C  CA  . ARG   A 1 296 ? -10.585 -23.966 25.067  1.00 13.44 ? 319  ARG   A CA  1 
ATOM   2118 C  C   . ARG   A 1 296 ? -9.076  -24.157 25.126  1.00 13.06 ? 319  ARG   A C   1 
ATOM   2119 O  O   . ARG   A 1 296 ? -8.510  -24.720 24.206  1.00 11.82 ? 319  ARG   A O   1 
ATOM   2120 C  CB  . ARG   A 1 296 ? -11.347 -25.198 25.575  1.00 15.53 ? 319  ARG   A CB  1 
ATOM   2121 C  CG  . ARG   A 1 296 ? -10.930 -25.641 26.966  1.00 19.55 ? 319  ARG   A CG  1 
ATOM   2122 C  CD  . ARG   A 1 296 ? -12.075 -26.175 27.829  1.00 21.78 ? 319  ARG   A CD  1 
ATOM   2123 N  NE  . ARG   A 1 296 ? -13.164 -25.203 27.942  1.00 22.62 ? 319  ARG   A NE  1 
ATOM   2124 C  CZ  . ARG   A 1 296 ? -13.440 -24.378 28.964  1.00 20.42 ? 319  ARG   A CZ  1 
ATOM   2125 N  NH1 . ARG   A 1 296 ? -12.678 -24.304 30.036  1.00 19.41 ? 319  ARG   A NH1 1 
ATOM   2126 N  NH2 . ARG   A 1 296 ? -14.495 -23.600 28.867  1.00 21.57 ? 319  ARG   A NH2 1 
ATOM   2127 N  N   . ALA   A 1 297 ? -8.428  -23.654 26.186  1.00 12.04 ? 320  ALA   A N   1 
ATOM   2128 C  CA  . ALA   A 1 297 ? -6.991  -23.802 26.360  1.00 10.82 ? 320  ALA   A CA  1 
ATOM   2129 C  C   . ALA   A 1 297 ? -6.685  -24.371 27.735  1.00 11.55 ? 320  ALA   A C   1 
ATOM   2130 O  O   . ALA   A 1 297 ? -7.120  -23.813 28.756  1.00 10.67 ? 320  ALA   A O   1 
ATOM   2131 C  CB  . ALA   A 1 297 ? -6.319  -22.475 26.173  1.00 10.54 ? 320  ALA   A CB  1 
ATOM   2132 N  N   . ASP   A 1 298 ? -5.916  -25.476 27.755  1.00 11.47 ? 321  ASP   A N   1 
ATOM   2133 C  CA  . ASP   A 1 298 ? -5.612  -26.190 28.987  1.00 13.47 ? 321  ASP   A CA  1 
ATOM   2134 C  C   . ASP   A 1 298 ? -4.101  -26.374 29.113  1.00 13.63 ? 321  ASP   A C   1 
ATOM   2135 O  O   . ASP   A 1 298 ? -3.509  -27.222 28.450  1.00 13.70 ? 321  ASP   A O   1 
ATOM   2136 C  CB  . ASP   A 1 298 ? -6.303  -27.549 29.000  1.00 15.70 ? 321  ASP   A CB  1 
ATOM   2137 C  CG  . ASP   A 1 298 ? -7.824  -27.542 28.938  1.00 18.38 ? 321  ASP   A CG  1 
ATOM   2138 O  OD1 . ASP   A 1 298 ? -8.416  -26.490 29.084  1.00 16.76 ? 321  ASP   A OD1 1 
ATOM   2139 O  OD2 . ASP   A 1 298 ? -8.423  -28.608 28.764  1.00 24.25 ? 321  ASP   A OD2 1 
ATOM   2140 N  N   . PRO   A 1 299 ? -3.408  -25.604 29.964  1.00 13.20 ? 322  PRO   A N   1 
ATOM   2141 C  CA  . PRO   A 1 299 ? -2.028  -25.936 30.317  1.00 13.23 ? 322  PRO   A CA  1 
ATOM   2142 C  C   . PRO   A 1 299 ? -2.033  -27.301 30.991  1.00 13.09 ? 322  PRO   A C   1 
ATOM   2143 O  O   . PRO   A 1 299 ? -2.916  -27.584 31.806  1.00 12.44 ? 322  PRO   A O   1 
ATOM   2144 C  CB  . PRO   A 1 299 ? -1.543  -24.838 31.248  1.00 14.52 ? 322  PRO   A CB  1 
ATOM   2145 C  CG  . PRO   A 1 299 ? -2.557  -23.753 31.072  1.00 15.21 ? 322  PRO   A CG  1 
ATOM   2146 C  CD  . PRO   A 1 299 ? -3.875  -24.370 30.589  1.00 13.07 ? 322  PRO   A CD  1 
ATOM   2147 N  N   . LEU   A 1 300 ? -1.023  -28.116 30.624  1.00 13.75 ? 323  LEU   A N   1 
ATOM   2148 C  CA  . LEU   A 1 300 ? -0.934  -29.522 30.991  1.00 15.15 ? 323  LEU   A CA  1 
ATOM   2149 C  C   . LEU   A 1 300 ? 0.413   -29.759 31.654  1.00 15.78 ? 323  LEU   A C   1 
ATOM   2150 O  O   . LEU   A 1 300 ? 1.421   -29.203 31.227  1.00 15.44 ? 323  LEU   A O   1 
ATOM   2151 C  CB  . LEU   A 1 300 ? -0.968  -30.434 29.765  1.00 16.03 ? 323  LEU   A CB  1 
ATOM   2152 C  CG  . LEU   A 1 300 ? -2.228  -30.438 28.911  1.00 18.56 ? 323  LEU   A CG  1 
ATOM   2153 C  CD1 . LEU   A 1 300 ? -2.007  -31.283 27.694  1.00 19.55 ? 323  LEU   A CD1 1 
ATOM   2154 C  CD2 . LEU   A 1 300 ? -3.483  -30.884 29.655  1.00 20.72 ? 323  LEU   A CD2 1 
ATOM   2155 N  N   . SER   A 1 301 ? 0.389   -30.642 32.645  1.00 16.55 ? 324  SER   A N   1 
ATOM   2156 C  CA  . SER   A 1 301 ? 1.556   -31.356 33.106  1.00 18.53 ? 324  SER   A CA  1 
ATOM   2157 C  C   . SER   A 1 301 ? 1.343   -32.833 32.782  1.00 17.51 ? 324  SER   A C   1 
ATOM   2158 O  O   . SER   A 1 301 ? 0.494   -33.468 33.401  1.00 15.48 ? 324  SER   A O   1 
ATOM   2159 C  CB  . SER   A 1 301 ? 1.710   -31.121 34.579  1.00 20.34 ? 324  SER   A CB  1 
ATOM   2160 O  OG  . SER   A 1 301 ? 2.875   -31.778 35.037  1.00 24.78 ? 324  SER   A OG  1 
ATOM   2161 N  N   . GLY   A 1 302 ? 2.055   -33.356 31.775  1.00 16.06 ? 325  GLY   A N   1 
ATOM   2162 C  CA  . GLY   A 1 302 ? 1.786   -34.694 31.270  1.00 16.71 ? 325  GLY   A CA  1 
ATOM   2163 C  C   . GLY   A 1 302 ? 0.401   -34.768 30.625  1.00 17.54 ? 325  GLY   A C   1 
ATOM   2164 O  O   . GLY   A 1 302 ? 0.162   -34.184 29.584  1.00 18.43 ? 325  GLY   A O   1 
ATOM   2165 N  N   . GLY   A 1 303 ? -0.524  -35.468 31.295  1.00 16.66 ? 326  GLY   A N   1 
ATOM   2166 C  CA  . GLY   A 1 303 ? -1.924  -35.525 30.913  1.00 16.91 ? 326  GLY   A CA  1 
ATOM   2167 C  C   . GLY   A 1 303 ? -2.803  -34.835 31.943  1.00 15.85 ? 326  GLY   A C   1 
ATOM   2168 O  O   . GLY   A 1 303 ? -4.033  -34.929 31.853  1.00 16.41 ? 326  GLY   A O   1 
ATOM   2169 N  N   . THR   A 1 304 ? -2.173  -34.146 32.907  1.00 15.17 ? 327  THR   A N   1 
ATOM   2170 C  CA  . THR   A 1 304 ? -2.923  -33.508 33.987  1.00 15.28 ? 327  THR   A CA  1 
ATOM   2171 C  C   . THR   A 1 304 ? -3.194  -32.047 33.626  1.00 14.53 ? 327  THR   A C   1 
ATOM   2172 O  O   . THR   A 1 304 ? -2.254  -31.293 33.351  1.00 13.28 ? 327  THR   A O   1 
ATOM   2173 C  CB  . THR   A 1 304 ? -2.176  -33.595 35.310  1.00 15.60 ? 327  THR   A CB  1 
ATOM   2174 O  OG1 . THR   A 1 304 ? -1.905  -34.971 35.553  1.00 17.04 ? 327  THR   A OG1 1 
ATOM   2175 C  CG2 . THR   A 1 304 ? -3.036  -33.034 36.431  1.00 16.41 ? 327  THR   A CG2 1 
ATOM   2176 N  N   . THR   A 1 305 ? -4.472  -31.657 33.642  1.00 15.63 ? 328  THR   A N   1 
ATOM   2177 C  CA  . THR   A 1 305 ? -4.862  -30.286 33.345  1.00 17.17 ? 328  THR   A CA  1 
ATOM   2178 C  C   . THR   A 1 305 ? -4.594  -29.472 34.598  1.00 15.51 ? 328  THR   A C   1 
ATOM   2179 O  O   . THR   A 1 305 ? -5.071  -29.844 35.658  1.00 17.33 ? 328  THR   A O   1 
ATOM   2180 C  CB  . THR   A 1 305 ? -6.351  -30.211 32.990  1.00 21.52 ? 328  THR   A CB  1 
ATOM   2181 O  OG1 . THR   A 1 305 ? -6.567  -30.914 31.760  1.00 26.98 ? 328  THR   A OG1 1 
ATOM   2182 C  CG2 . THR   A 1 305 ? -6.785  -28.767 32.821  1.00 22.58 ? 328  THR   A CG2 1 
ATOM   2183 N  N   . VAL   A 1 306 ? -3.891  -28.355 34.459  1.00 14.77 ? 329  VAL   A N   1 
ATOM   2184 C  CA  . VAL   A 1 306 ? -3.483  -27.531 35.585  1.00 16.64 ? 329  VAL   A CA  1 
ATOM   2185 C  C   . VAL   A 1 306 ? -4.440  -26.347 35.735  1.00 14.89 ? 329  VAL   A C   1 
ATOM   2186 O  O   . VAL   A 1 306 ? -4.653  -25.849 36.840  1.00 13.91 ? 329  VAL   A O   1 
ATOM   2187 C  CB  . VAL   A 1 306 ? -2.011  -27.188 35.255  1.00 20.00 ? 329  VAL   A CB  1 
ATOM   2188 C  CG1 . VAL   A 1 306 ? -1.546  -25.784 35.604  1.00 22.27 ? 329  VAL   A CG1 1 
ATOM   2189 C  CG2 . VAL   A 1 306 ? -1.078  -28.256 35.818  1.00 22.49 ? 329  VAL   A CG2 1 
ATOM   2190 N  N   . ASP   A 1 307 ? -5.016  -25.933 34.599  1.00 13.32 ? 330  ASP   A N   1 
ATOM   2191 C  CA  . ASP   A 1 307 ? -5.967  -24.836 34.501  1.00 12.03 ? 330  ASP   A CA  1 
ATOM   2192 C  C   . ASP   A 1 307 ? -6.685  -25.037 33.172  1.00 10.99 ? 330  ASP   A C   1 
ATOM   2193 O  O   . ASP   A 1 307 ? -6.222  -25.816 32.342  1.00 11.27 ? 330  ASP   A O   1 
ATOM   2194 C  CB  . ASP   A 1 307 ? -5.227  -23.503 34.521  1.00 11.25 ? 330  ASP   A CB  1 
ATOM   2195 C  CG  . ASP   A 1 307 ? -6.048  -22.224 34.447  1.00 10.75 ? 330  ASP   A CG  1 
ATOM   2196 O  OD1 . ASP   A 1 307 ? -7.116  -22.183 35.097  1.00 10.45 ? 330  ASP   A OD1 1 
ATOM   2197 O  OD2 . ASP   A 1 307 ? -5.588  -21.245 33.780  1.00 10.85 ? 330  ASP   A OD2 1 
ATOM   2198 N  N   . SER   A 1 308 ? -7.827  -24.364 33.001  1.00 11.49 ? 331  SER   A N   1 
ATOM   2199 C  CA  . SER   A 1 308 ? -8.629  -24.437 31.804  1.00 11.76 ? 331  SER   A CA  1 
ATOM   2200 C  C   . SER   A 1 308 ? -9.401  -23.136 31.633  1.00 11.47 ? 331  SER   A C   1 
ATOM   2201 O  O   . SER   A 1 308 ? -10.106 -22.696 32.536  1.00 11.70 ? 331  SER   A O   1 
ATOM   2202 C  CB  . SER   A 1 308 ? -9.569  -25.615 31.879  1.00 11.89 ? 331  SER   A CB  1 
ATOM   2203 O  OG  . SER   A 1 308 ? -10.275 -25.767 30.647  1.00 13.57 ? 331  SER   A OG  1 
ATOM   2204 N  N   . VAL   A 1 309 ? -9.299  -22.538 30.449  1.00 10.27 ? 332  VAL   A N   1 
ATOM   2205 C  CA  . VAL   A 1 309 ? -10.031 -21.317 30.162  1.00 9.80  ? 332  VAL   A CA  1 
ATOM   2206 C  C   . VAL   A 1 309 ? -10.810 -21.497 28.870  1.00 9.62  ? 332  VAL   A C   1 
ATOM   2207 O  O   . VAL   A 1 309 ? -10.348 -22.160 27.945  1.00 10.68 ? 332  VAL   A O   1 
ATOM   2208 C  CB  . VAL   A 1 309 ? -9.066  -20.117 30.083  1.00 8.92  ? 332  VAL   A CB  1 
ATOM   2209 C  CG1 . VAL   A 1 309 ? -8.379  -19.840 31.417  1.00 8.88  ? 332  VAL   A CG1 1 
ATOM   2210 C  CG2 . VAL   A 1 309 ? -8.027  -20.262 28.983  1.00 9.40  ? 332  VAL   A CG2 1 
ATOM   2211 N  N   . GLY   A 1 310 ? -11.987 -20.859 28.828  1.00 8.65  ? 333  GLY   A N   1 
ATOM   2212 C  CA  . GLY   A 1 310 ? -12.799 -20.802 27.633  1.00 8.83  ? 333  GLY   A CA  1 
ATOM   2213 C  C   . GLY   A 1 310 ? -12.520 -19.529 26.850  1.00 8.90  ? 333  GLY   A C   1 
ATOM   2214 O  O   . GLY   A 1 310 ? -12.181 -18.484 27.429  1.00 9.87  ? 333  GLY   A O   1 
ATOM   2215 N  N   . SER   A 1 311 ? -12.680 -19.625 25.534  1.00 8.46  ? 334  SER   A N   1 
ATOM   2216 C  CA  . SER   A 1 311 ? -12.501 -18.474 24.675  1.00 8.51  ? 334  SER   A CA  1 
ATOM   2217 C  C   . SER   A 1 311 ? -13.302 -18.670 23.397  1.00 8.25  ? 334  SER   A C   1 
ATOM   2218 O  O   . SER   A 1 311 ? -14.123 -19.590 23.337  1.00 8.35  ? 334  SER   A O   1 
ATOM   2219 C  CB  . SER   A 1 311 ? -11.009 -18.267 24.460  1.00 9.39  ? 334  SER   A CB  1 
ATOM   2220 O  OG  . SER   A 1 311 ? -10.699 -17.050 23.796  1.00 9.45  ? 334  SER   A OG  1 
ATOM   2221 N  N   . TYR   A 1 312 ? -12.950 -17.905 22.369  1.00 7.82  ? 335  TYR   A N   1 
ATOM   2222 C  CA  . TYR   A 1 312 ? -13.569 -17.983 21.056  1.00 7.84  ? 335  TYR   A CA  1 
ATOM   2223 C  C   . TYR   A 1 312 ? -12.698 -17.235 20.058  1.00 8.57  ? 335  TYR   A C   1 
ATOM   2224 O  O   . TYR   A 1 312 ? -11.830 -16.453 20.434  1.00 7.90  ? 335  TYR   A O   1 
ATOM   2225 C  CB  . TYR   A 1 312 ? -15.001 -17.420 21.062  1.00 8.03  ? 335  TYR   A CB  1 
ATOM   2226 C  CG  . TYR   A 1 312 ? -15.070 -15.937 21.405  1.00 7.60  ? 335  TYR   A CG  1 
ATOM   2227 C  CD1 . TYR   A 1 312 ? -14.871 -14.957 20.428  1.00 7.74  ? 335  TYR   A CD1 1 
ATOM   2228 C  CD2 . TYR   A 1 312 ? -15.394 -15.492 22.683  1.00 8.19  ? 335  TYR   A CD2 1 
ATOM   2229 C  CE1 . TYR   A 1 312 ? -14.946 -13.598 20.707  1.00 7.60  ? 335  TYR   A CE1 1 
ATOM   2230 C  CE2 . TYR   A 1 312 ? -15.447 -14.137 22.980  1.00 7.28  ? 335  TYR   A CE2 1 
ATOM   2231 C  CZ  . TYR   A 1 312 ? -15.195 -13.185 22.010  1.00 7.54  ? 335  TYR   A CZ  1 
ATOM   2232 O  OH  . TYR   A 1 312 ? -15.288 -11.851 22.312  1.00 7.57  ? 335  TYR   A OH  1 
ATOM   2233 N  N   . THR   A 1 313 ? -12.959 -17.508 18.764  1.00 8.08  ? 336  THR   A N   1 
ATOM   2234 C  CA  . THR   A 1 313 ? -12.296 -16.832 17.685  1.00 8.35  ? 336  THR   A CA  1 
ATOM   2235 C  C   . THR   A 1 313 ? -13.287 -16.658 16.549  1.00 8.36  ? 336  THR   A C   1 
ATOM   2236 O  O   . THR   A 1 313 ? -14.205 -17.470 16.301  1.00 9.45  ? 336  THR   A O   1 
ATOM   2237 C  CB  . THR   A 1 313 ? -11.074 -17.647 17.253  1.00 8.25  ? 336  THR   A CB  1 
ATOM   2238 O  OG1 . THR   A 1 313 ? -10.361 -16.865 16.299  1.00 7.98  ? 336  THR   A OG1 1 
ATOM   2239 C  CG2 . THR   A 1 313 ? -11.441 -19.004 16.663  1.00 8.51  ? 336  THR   A CG2 1 
ATOM   2240 N  N   . GLY   A 1 314 ? -13.064 -15.576 15.816  1.00 8.07  ? 337  GLY   A N   1 
ATOM   2241 C  CA  . GLY   A 1 314 ? -13.686 -15.402 14.509  1.00 8.47  ? 337  GLY   A CA  1 
ATOM   2242 C  C   . GLY   A 1 314 ? -12.600 -15.524 13.439  1.00 8.91  ? 337  GLY   A C   1 
ATOM   2243 O  O   . GLY   A 1 314 ? -11.625 -14.778 13.487  1.00 8.49  ? 337  GLY   A O   1 
ATOM   2244 N  N   . MET   A 1 315 ? -12.816 -16.405 12.458  1.00 9.31  ? 338  MET   A N   1 
ATOM   2245 C  CA  . MET   A 1 315 ? -11.796 -16.738 11.484  1.00 9.18  ? 338  MET   A CA  1 
ATOM   2246 C  C   . MET   A 1 315 ? -11.781 -15.686 10.389  1.00 8.62  ? 338  MET   A C   1 
ATOM   2247 O  O   . MET   A 1 315 ? -12.590 -15.728 9.481   1.00 9.20  ? 338  MET   A O   1 
ATOM   2248 C  CB  . MET   A 1 315 ? -12.002 -18.157 10.940  1.00 10.98 ? 338  MET   A CB  1 
ATOM   2249 C  CG  . MET   A 1 315 ? -11.759 -19.241 11.999  1.00 12.06 ? 338  MET   A CG  1 
ATOM   2250 S  SD  . MET   A 1 315 ? -10.029 -19.448 12.488  1.00 12.34 ? 338  MET   A SD  1 
ATOM   2251 C  CE  . MET   A 1 315 ? -9.306  -20.153 11.005  1.00 12.20 ? 338  MET   A CE  1 
ATOM   2252 N  N   . ARG   A 1 316 ? -10.893 -14.703 10.515  1.00 8.76  ? 339  ARG   A N   1 
ATOM   2253 C  CA  . ARG   A 1 316 ? -10.863 -13.619 9.538   1.00 8.66  ? 339  ARG   A CA  1 
ATOM   2254 C  C   . ARG   A 1 316 ? -9.440  -13.076 9.452   1.00 8.72  ? 339  ARG   A C   1 
ATOM   2255 O  O   . ARG   A 1 316 ? -8.705  -13.190 10.435  1.00 8.30  ? 339  ARG   A O   1 
ATOM   2256 C  CB  . ARG   A 1 316 ? -11.885 -12.554 9.963   1.00 8.31  ? 339  ARG   A CB  1 
ATOM   2257 C  CG  . ARG   A 1 316 ? -11.528 -11.763 11.221  1.00 8.77  ? 339  ARG   A CG  1 
ATOM   2258 C  CD  . ARG   A 1 316 ? -10.616 -10.559 10.973  1.00 8.88  ? 339  ARG   A CD  1 
ATOM   2259 N  NE  . ARG   A 1 316 ? -10.182 -10.000 12.260  1.00 9.36  ? 339  ARG   A NE  1 
ATOM   2260 C  CZ  . ARG   A 1 316 ? -8.992  -10.173 12.825  1.00 10.08 ? 339  ARG   A CZ  1 
ATOM   2261 N  NH1 . ARG   A 1 316 ? -8.094  -11.014 12.327  1.00 9.10  ? 339  ARG   A NH1 1 
ATOM   2262 N  NH2 . ARG   A 1 316 ? -8.722  -9.501  13.919  1.00 12.01 ? 339  ARG   A NH2 1 
ATOM   2263 N  N   . THR   A 1 317 ? -9.124  -12.446 8.300   1.00 8.74  ? 340  THR   A N   1 
ATOM   2264 C  CA  . THR   A 1 317 ? -7.884  -11.729 8.104   1.00 9.24  ? 340  THR   A CA  1 
ATOM   2265 C  C   . THR   A 1 317 ? -8.194  -10.332 7.580   1.00 9.48  ? 340  THR   A C   1 
ATOM   2266 O  O   . THR   A 1 317 ? -9.187  -10.093 6.880   1.00 9.26  ? 340  THR   A O   1 
ATOM   2267 C  CB  . THR   A 1 317 ? -6.946  -12.481 7.156   1.00 9.75  ? 340  THR   A CB  1 
ATOM   2268 O  OG1 . THR   A 1 317 ? -7.576  -12.547 5.883   1.00 10.14 ? 340  THR   A OG1 1 
ATOM   2269 C  CG2 . THR   A 1 317 ? -6.601  -13.850 7.703   1.00 10.36 ? 340  THR   A CG2 1 
ATOM   2270 N  N   . ILE   A 1 318 ? -7.277  -9.420  7.892   1.00 9.98  ? 341  ILE   A N   1 
ATOM   2271 C  CA  . ILE   A 1 318 ? -7.282  -8.095  7.297   1.00 10.20 ? 341  ILE   A CA  1 
ATOM   2272 C  C   . ILE   A 1 318 ? -5.853  -7.803  6.846   1.00 10.50 ? 341  ILE   A C   1 
ATOM   2273 O  O   . ILE   A 1 318 ? -4.895  -8.098  7.556   1.00 9.62  ? 341  ILE   A O   1 
ATOM   2274 C  CB  . ILE   A 1 318 ? -7.807  -7.045  8.303   1.00 11.14 ? 341  ILE   A CB  1 
ATOM   2275 C  CG1 . ILE   A 1 318 ? -8.087  -5.721  7.653   1.00 11.02 ? 341  ILE   A CG1 1 
ATOM   2276 C  CG2 . ILE   A 1 318 ? -6.849  -6.866  9.481   1.00 11.88 ? 341  ILE   A CG2 1 
ATOM   2277 C  CD1 . ILE   A 1 318 ? -9.274  -5.733  6.728   1.00 11.32 ? 341  ILE   A CD1 1 
ATOM   2278 N  N   . ALA   A 1 319 ? -5.725  -7.240  5.651   1.00 10.23 ? 342  ALA   A N   1 
ATOM   2279 C  CA  . ALA   A 1 319 ? -4.442  -6.885  5.084   1.00 11.04 ? 342  ALA   A CA  1 
ATOM   2280 C  C   . ALA   A 1 319 ? -4.684  -5.854  3.996   1.00 11.66 ? 342  ALA   A C   1 
ATOM   2281 O  O   . ALA   A 1 319 ? -5.822  -5.556  3.696   1.00 11.00 ? 342  ALA   A O   1 
ATOM   2282 C  CB  . ALA   A 1 319 ? -3.774  -8.100  4.487   1.00 11.74 ? 342  ALA   A CB  1 
ATOM   2283 N  N   . LEU   A 1 320 ? -3.601  -5.359  3.395   1.00 12.37 ? 343  LEU   A N   1 
ATOM   2284 C  CA  . LEU   A 1 320 ? -3.713  -4.573  2.172   1.00 13.41 ? 343  LEU   A CA  1 
ATOM   2285 C  C   . LEU   A 1 320 ? -3.465  -5.480  0.974   1.00 14.93 ? 343  LEU   A C   1 
ATOM   2286 O  O   . LEU   A 1 320 ? -2.618  -6.368  1.030   1.00 17.39 ? 343  LEU   A O   1 
ATOM   2287 C  CB  . LEU   A 1 320 ? -2.655  -3.477  2.123   1.00 13.70 ? 343  LEU   A CB  1 
ATOM   2288 C  CG  . LEU   A 1 320 ? -2.788  -2.295  3.071   1.00 14.65 ? 343  LEU   A CG  1 
ATOM   2289 C  CD1 . LEU   A 1 320 ? -1.661  -1.321  2.687   1.00 15.55 ? 343  LEU   A CD1 1 
ATOM   2290 C  CD2 . LEU   A 1 320 ? -4.168  -1.691  2.944   1.00 14.89 ? 343  LEU   A CD2 1 
ATOM   2291 N  N   . ALA   A 1 321 ? -4.085  -5.127  -0.145  1.00 14.25 ? 344  ALA   A N   1 
ATOM   2292 C  CA  . ALA   A 1 321 ? -3.791  -5.750  -1.411  1.00 15.64 ? 344  ALA   A CA  1 
ATOM   2293 C  C   . ALA   A 1 321 ? -4.160  -4.774  -2.522  1.00 16.01 ? 344  ALA   A C   1 
ATOM   2294 O  O   . ALA   A 1 321 ? -5.037  -3.906  -2.380  1.00 12.97 ? 344  ALA   A O   1 
ATOM   2295 C  CB  . ALA   A 1 321 ? -4.556  -7.050  -1.568  1.00 16.45 ? 344  ALA   A CB  1 
ATOM   2296 N  N   . SER   A 1 322 ? -3.524  -5.008  -3.665  1.00 16.81 ? 345  SER   A N   1 
ATOM   2297 C  CA  . SER   A 1 322 ? -3.819  -4.241  -4.849  1.00 18.29 ? 345  SER   A CA  1 
ATOM   2298 C  C   . SER   A 1 322 ? -4.985  -4.898  -5.593  1.00 21.16 ? 345  SER   A C   1 
ATOM   2299 O  O   . SER   A 1 322 ? -4.899  -6.045  -6.055  1.00 22.95 ? 345  SER   A O   1 
ATOM   2300 C  CB  . SER   A 1 322 ? -2.556  -4.098  -5.689  1.00 20.96 ? 345  SER   A CB  1 
ATOM   2301 O  OG  . SER   A 1 322 ? -2.864  -3.404  -6.886  1.00 22.88 ? 345  SER   A OG  1 
ATOM   2302 N  N   . VAL   A 1 323 ? -6.107  -4.172  -5.648  1.00 23.40 ? 346  VAL   A N   1 
ATOM   2303 C  CA  . VAL   A 1 323 ? -7.346  -4.648  -6.234  1.00 24.69 ? 346  VAL   A CA  1 
ATOM   2304 C  C   . VAL   A 1 323 ? -7.829  -3.645  -7.279  1.00 25.39 ? 346  VAL   A C   1 
ATOM   2305 O  O   . VAL   A 1 323 ? -8.071  -2.472  -6.980  1.00 21.52 ? 346  VAL   A O   1 
ATOM   2306 C  CB  . VAL   A 1 323 ? -8.407  -4.806  -5.126  1.00 27.73 ? 346  VAL   A CB  1 
ATOM   2307 C  CG1 . VAL   A 1 323 ? -9.742  -5.231  -5.710  1.00 29.56 ? 346  VAL   A CG1 1 
ATOM   2308 C  CG2 . VAL   A 1 323 ? -7.963  -5.762  -4.022  1.00 27.70 ? 346  VAL   A CG2 1 
ATOM   2309 N  N   . GLY   A 1 324 ? -7.960  -4.112  -8.524  1.00 26.38 ? 347  GLY   A N   1 
ATOM   2310 C  CA  . GLY   A 1 324 ? -8.478  -3.255  -9.572  1.00 26.65 ? 347  GLY   A CA  1 
ATOM   2311 C  C   . GLY   A 1 324 ? -7.645  -1.985  -9.713  1.00 24.56 ? 347  GLY   A C   1 
ATOM   2312 O  O   . GLY   A 1 324 ? -8.175  -0.933  -10.051 1.00 32.75 ? 347  GLY   A O   1 
ATOM   2313 N  N   . GLY   A 1 325 ? -6.339  -2.071  -9.451  1.00 23.23 ? 348  GLY   A N   1 
ATOM   2314 C  CA  . GLY   A 1 325 ? -5.463  -0.927  -9.645  1.00 21.27 ? 348  GLY   A CA  1 
ATOM   2315 C  C   . GLY   A 1 325 ? -5.289  -0.044  -8.405  1.00 20.23 ? 348  GLY   A C   1 
ATOM   2316 O  O   . GLY   A 1 325 ? -4.522  0.907   -8.442  1.00 19.37 ? 348  GLY   A O   1 
ATOM   2317 N  N   . HIS   A 1 326 ? -5.893  -0.400  -7.263  1.00 16.24 ? 349  HIS   A N   1 
ATOM   2318 C  CA  . HIS   A 1 326 ? -5.786  0.439   -6.082  1.00 15.55 ? 349  HIS   A CA  1 
ATOM   2319 C  C   . HIS   A 1 326 ? -5.426  -0.391  -4.856  1.00 14.00 ? 349  HIS   A C   1 
ATOM   2320 O  O   . HIS   A 1 326 ? -5.936  -1.496  -4.698  1.00 14.00 ? 349  HIS   A O   1 
ATOM   2321 C  CB  . HIS   A 1 326 ? -7.144  1.035   -5.715  1.00 16.03 ? 349  HIS   A CB  1 
ATOM   2322 C  CG  . HIS   A 1 326 ? -7.737  1.978   -6.680  1.00 17.94 ? 349  HIS   A CG  1 
ATOM   2323 N  ND1 . HIS   A 1 326 ? -7.140  3.154   -7.056  1.00 19.47 ? 349  HIS   A ND1 1 
ATOM   2324 C  CD2 . HIS   A 1 326 ? -8.932  1.954   -7.264  1.00 19.12 ? 349  HIS   A CD2 1 
ATOM   2325 C  CE1 . HIS   A 1 326 ? -7.938  3.786   -7.908  1.00 19.43 ? 349  HIS   A CE1 1 
ATOM   2326 N  NE2 . HIS   A 1 326 ? -9.032  3.080   -8.034  1.00 19.96 ? 349  HIS   A NE2 1 
ATOM   2327 N  N   . GLN   A 1 327 ? -4.607  0.159   -3.970  1.00 14.71 ? 350  GLN   A N   1 
ATOM   2328 C  CA  . GLN   A 1 327 ? -4.384  -0.478  -2.672  1.00 14.68 ? 350  GLN   A CA  1 
ATOM   2329 C  C   . GLN   A 1 327 ? -5.705  -0.447  -1.922  1.00 13.44 ? 350  GLN   A C   1 
ATOM   2330 O  O   . GLN   A 1 327 ? -6.299  0.606   -1.788  1.00 12.27 ? 350  GLN   A O   1 
ATOM   2331 C  CB  . GLN   A 1 327 ? -3.354  0.197   -1.762  1.00 17.99 ? 350  GLN   A CB  1 
ATOM   2332 C  CG  . GLN   A 1 327 ? -1.935  0.052   -2.276  1.00 20.85 ? 350  GLN   A CG  1 
ATOM   2333 C  CD  . GLN   A 1 327 ? -1.481  -1.382  -2.245  1.00 24.01 ? 350  GLN   A CD  1 
ATOM   2334 O  OE1 . GLN   A 1 327 ? -1.733  -2.101  -1.286  1.00 23.85 ? 350  GLN   A OE1 1 
ATOM   2335 N  NE2 . GLN   A 1 327 ? -0.890  -1.845  -3.332  1.00 31.92 ? 350  GLN   A NE2 1 
ATOM   2336 N  N   . ARG   A 1 328 ? -6.133  -1.593  -1.387  1.00 12.57 ? 351  ARG   A N   1 
ATOM   2337 C  CA  . ARG   A 1 328 ? -7.398  -1.660  -0.686  1.00 12.65 ? 351  ARG   A CA  1 
ATOM   2338 C  C   . ARG   A 1 328 ? -7.227  -2.532  0.547   1.00 12.39 ? 351  ARG   A C   1 
ATOM   2339 O  O   . ARG   A 1 328 ? -6.412  -3.439  0.536   1.00 11.47 ? 351  ARG   A O   1 
ATOM   2340 C  CB  . ARG   A 1 328 ? -8.460  -2.403  -1.481  1.00 13.52 ? 351  ARG   A CB  1 
ATOM   2341 C  CG  . ARG   A 1 328 ? -8.825  -1.871  -2.861  1.00 14.48 ? 351  ARG   A CG  1 
ATOM   2342 C  CD  . ARG   A 1 328 ? -9.771  -0.743  -2.715  1.00 13.25 ? 351  ARG   A CD  1 
ATOM   2343 N  NE  . ARG   A 1 328 ? -10.418 -0.389  -3.982  1.00 12.82 ? 351  ARG   A NE  1 
ATOM   2344 C  CZ  . ARG   A 1 328 ? -11.244 0.654   -4.004  1.00 13.83 ? 351  ARG   A CZ  1 
ATOM   2345 N  NH1 . ARG   A 1 328 ? -11.466 1.369   -2.908  1.00 12.50 ? 351  ARG   A NH1 1 
ATOM   2346 N  NH2 . ARG   A 1 328 ? -11.887 0.969   -5.107  1.00 13.79 ? 351  ARG   A NH2 1 
ATOM   2347 N  N   . PRO   A 1 329 ? -7.948  -2.248  1.653   1.00 11.03 ? 352  PRO   A N   1 
ATOM   2348 C  CA  . PRO   A 1 329 ? -7.981  -3.176  2.776   1.00 11.01 ? 352  PRO   A CA  1 
ATOM   2349 C  C   . PRO   A 1 329 ? -8.874  -4.353  2.395   1.00 11.03 ? 352  PRO   A C   1 
ATOM   2350 O  O   . PRO   A 1 329 ? -10.044 -4.169  2.042   1.00 11.69 ? 352  PRO   A O   1 
ATOM   2351 C  CB  . PRO   A 1 329 ? -8.583  -2.362  3.883   1.00 10.84 ? 352  PRO   A CB  1 
ATOM   2352 C  CG  . PRO   A 1 329 ? -9.518  -1.399  3.145   1.00 10.93 ? 352  PRO   A CG  1 
ATOM   2353 C  CD  . PRO   A 1 329 ? -8.805  -1.074  1.817   1.00 10.91 ? 352  PRO   A CD  1 
ATOM   2354 N  N   . VAL   A 1 330 ? -8.325  -5.556  2.519   1.00 10.21 ? 353  VAL   A N   1 
ATOM   2355 C  CA  . VAL   A 1 330 ? -9.057  -6.747  2.145   1.00 10.78 ? 353  VAL   A CA  1 
ATOM   2356 C  C   . VAL   A 1 330 ? -9.343  -7.564  3.397   1.00 10.21 ? 353  VAL   A C   1 
ATOM   2357 O  O   . VAL   A 1 330 ? -8.456  -7.816  4.205   1.00 11.36 ? 353  VAL   A O   1 
ATOM   2358 C  CB  . VAL   A 1 330 ? -8.325  -7.567  1.063   1.00 11.55 ? 353  VAL   A CB  1 
ATOM   2359 C  CG1 . VAL   A 1 330 ? -8.293  -6.814  -0.252  1.00 11.82 ? 353  VAL   A CG1 1 
ATOM   2360 C  CG2 . VAL   A 1 330 ? -6.913  -7.963  1.481   1.00 12.30 ? 353  VAL   A CG2 1 
ATOM   2361 N  N   . LEU   A 1 331 ? -10.607 -7.942  3.523   1.00 10.09 ? 354  LEU   A N   1 
ATOM   2362 C  CA  . LEU   A 1 331 ? -11.102 -8.786  4.588   1.00 10.25 ? 354  LEU   A CA  1 
ATOM   2363 C  C   . LEU   A 1 331 ? -11.213 -10.192 4.005   1.00 9.24  ? 354  LEU   A C   1 
ATOM   2364 O  O   . LEU   A 1 331 ? -11.911 -10.409 3.008   1.00 9.95  ? 354  LEU   A O   1 
ATOM   2365 C  CB  . LEU   A 1 331 ? -12.449 -8.261  5.078   1.00 11.12 ? 354  LEU   A CB  1 
ATOM   2366 C  CG  . LEU   A 1 331 ? -13.113 -9.085  6.176   1.00 12.61 ? 354  LEU   A CG  1 
ATOM   2367 C  CD1 . LEU   A 1 331 ? -12.282 -8.993  7.401   1.00 13.58 ? 354  LEU   A CD1 1 
ATOM   2368 C  CD2 . LEU   A 1 331 ? -14.563 -8.660  6.424   1.00 13.32 ? 354  LEU   A CD2 1 
ATOM   2369 N  N   . ASN   A 1 332 ? -10.516 -11.154 4.608   1.00 9.64  ? 355  ASN   A N   1 
ATOM   2370 C  CA  . ASN   A 1 332 ? -10.566 -12.514 4.100   1.00 10.37 ? 355  ASN   A CA  1 
ATOM   2371 C  C   . ASN   A 1 332 ? -10.254 -12.503 2.602   1.00 10.92 ? 355  ASN   A C   1 
ATOM   2372 O  O   . ASN   A 1 332 ? -10.864 -13.250 1.855   1.00 12.00 ? 355  ASN   A O   1 
ATOM   2373 C  CB  . ASN   A 1 332 ? -11.907 -13.193 4.362   1.00 10.64 ? 355  ASN   A CB  1 
ATOM   2374 C  CG  . ASN   A 1 332 ? -12.308 -13.086 5.822   1.00 10.78 ? 355  ASN   A CG  1 
ATOM   2375 O  OD1 . ASN   A 1 332 ? -11.424 -13.040 6.678   1.00 9.88  ? 355  ASN   A OD1 1 
ATOM   2376 N  ND2 . ASN   A 1 332 ? -13.599 -13.017 6.102   1.00 10.48 ? 355  ASN   A ND2 1 
ATOM   2377 N  N   . GLY   A 1 333 ? -9.290  -11.694 2.199   1.00 11.49 ? 356  GLY   A N   1 
ATOM   2378 C  CA  . GLY   A 1 333 ? -8.761  -11.678 0.851   1.00 12.43 ? 356  GLY   A CA  1 
ATOM   2379 C  C   . GLY   A 1 333 ? -9.588  -10.882 -0.151  1.00 14.50 ? 356  GLY   A C   1 
ATOM   2380 O  O   . GLY   A 1 333 ? -9.236  -10.881 -1.329  1.00 15.05 ? 356  GLY   A O   1 
ATOM   2381 N  N   . LYS   A 1 334 ? -10.702 -10.279 0.273   1.00 13.46 ? 357  LYS   A N   1 
ATOM   2382 C  CA  . LYS   A 1 334 ? -11.569 -9.560  -0.630  1.00 15.78 ? 357  LYS   A CA  1 
ATOM   2383 C  C   . LYS   A 1 334 ? -11.809 -8.154  -0.102  1.00 15.18 ? 357  LYS   A C   1 
ATOM   2384 O  O   . LYS   A 1 334 ? -12.010 -7.940  1.101   1.00 11.97 ? 357  LYS   A O   1 
ATOM   2385 C  CB  . LYS   A 1 334 ? -12.897 -10.312 -0.718  1.00 21.29 ? 357  LYS   A CB  1 
ATOM   2386 C  CG  . LYS   A 1 334 ? -12.751 -11.664 -1.427  1.00 27.44 ? 357  LYS   A CG  1 
ATOM   2387 C  CD  . LYS   A 1 334 ? -14.084 -12.367 -1.623  1.00 37.74 ? 357  LYS   A CD  1 
ATOM   2388 C  CE  . LYS   A 1 334 ? -14.100 -13.188 -2.872  1.00 43.38 ? 357  LYS   A CE  1 
ATOM   2389 N  NZ  . LYS   A 1 334 ? -15.418 -13.818 -3.008  1.00 47.87 ? 357  LYS   A NZ  1 
ATOM   2390 N  N   . PHE   A 1 335 ? -11.799 -7.178  -1.017  1.00 12.55 ? 358  PHE   A N   1 
ATOM   2391 C  CA  . PHE   A 1 335 ? -12.149 -5.825  -0.627  1.00 12.35 ? 358  PHE   A CA  1 
ATOM   2392 C  C   . PHE   A 1 335 ? -13.632 -5.750  -0.276  1.00 13.12 ? 358  PHE   A C   1 
ATOM   2393 O  O   . PHE   A 1 335 ? -14.502 -6.198  -1.051  1.00 14.49 ? 358  PHE   A O   1 
ATOM   2394 C  CB  . PHE   A 1 335 ? -11.808 -4.850  -1.754  1.00 12.75 ? 358  PHE   A CB  1 
ATOM   2395 C  CG  . PHE   A 1 335 ? -12.378 -3.473  -1.497  1.00 12.69 ? 358  PHE   A CG  1 
ATOM   2396 C  CD1 . PHE   A 1 335 ? -12.132 -2.814  -0.300  1.00 11.98 ? 358  PHE   A CD1 1 
ATOM   2397 C  CD2 . PHE   A 1 335 ? -13.133 -2.834  -2.471  1.00 13.23 ? 358  PHE   A CD2 1 
ATOM   2398 C  CE1 . PHE   A 1 335 ? -12.636 -1.551  -0.086  1.00 12.99 ? 358  PHE   A CE1 1 
ATOM   2399 C  CE2 . PHE   A 1 335 ? -13.648 -1.573  -2.247  1.00 13.19 ? 358  PHE   A CE2 1 
ATOM   2400 C  CZ  . PHE   A 1 335 ? -13.410 -0.938  -1.046  1.00 13.02 ? 358  PHE   A CZ  1 
ATOM   2401 N  N   . VAL   A 1 336 ? -13.925 -5.114  0.874   1.00 12.28 ? 359  VAL   A N   1 
ATOM   2402 C  CA  . VAL   A 1 336 ? -15.241 -4.577  1.161   1.00 12.86 ? 359  VAL   A CA  1 
ATOM   2403 C  C   . VAL   A 1 336 ? -15.029 -3.169  1.701   1.00 11.47 ? 359  VAL   A C   1 
ATOM   2404 O  O   . VAL   A 1 336 ? -14.156 -2.929  2.535   1.00 10.73 ? 359  VAL   A O   1 
ATOM   2405 C  CB  . VAL   A 1 336 ? -16.047 -5.445  2.154   1.00 14.56 ? 359  VAL   A CB  1 
ATOM   2406 C  CG1 . VAL   A 1 336 ? -15.297 -5.633  3.483   1.00 14.74 ? 359  VAL   A CG1 1 
ATOM   2407 C  CG2 . VAL   A 1 336 ? -17.471 -4.929  2.392   1.00 14.19 ? 359  VAL   A CG2 1 
ATOM   2408 N  N   . PHE   A 1 337 ? -15.898 -2.258  1.299   1.00 10.80 ? 360  PHE   A N   1 
ATOM   2409 C  CA  . PHE   A 1 337 ? -15.850 -0.915  1.845   1.00 9.33  ? 360  PHE   A CA  1 
ATOM   2410 C  C   . PHE   A 1 337 ? -16.296 -0.940  3.309   1.00 8.99  ? 360  PHE   A C   1 
ATOM   2411 O  O   . PHE   A 1 337 ? -17.271 -1.589  3.651   1.00 8.36  ? 360  PHE   A O   1 
ATOM   2412 C  CB  . PHE   A 1 337 ? -16.745 -0.013  0.999   1.00 10.59 ? 360  PHE   A CB  1 
ATOM   2413 C  CG  . PHE   A 1 337 ? -16.563 1.445   1.363   1.00 9.55  ? 360  PHE   A CG  1 
ATOM   2414 C  CD1 . PHE   A 1 337 ? -17.241 2.002   2.439   1.00 10.06 ? 360  PHE   A CD1 1 
ATOM   2415 C  CD2 . PHE   A 1 337 ? -15.678 2.238   0.641   1.00 9.82  ? 360  PHE   A CD2 1 
ATOM   2416 C  CE1 . PHE   A 1 337 ? -17.053 3.343   2.777   1.00 9.88  ? 360  PHE   A CE1 1 
ATOM   2417 C  CE2 . PHE   A 1 337 ? -15.508 3.569   0.959   1.00 10.21 ? 360  PHE   A CE2 1 
ATOM   2418 C  CZ  . PHE   A 1 337 ? -16.186 4.114   2.059   1.00 9.64  ? 360  PHE   A CZ  1 
ATOM   2419 N  N   . GLN   A 1 338 ? -15.551 -0.220  4.149   1.00 8.33  ? 361  GLN   A N   1 
ATOM   2420 C  CA  . GLN   A 1 338 ? -15.835 -0.124  5.569   1.00 8.41  ? 361  GLN   A CA  1 
ATOM   2421 C  C   . GLN   A 1 338 ? -16.559 1.192   5.810   1.00 8.67  ? 361  GLN   A C   1 
ATOM   2422 O  O   . GLN   A 1 338 ? -15.933 2.250   5.815   1.00 8.68  ? 361  GLN   A O   1 
ATOM   2423 C  CB  . GLN   A 1 338 ? -14.567 -0.286  6.383   1.00 8.19  ? 361  GLN   A CB  1 
ATOM   2424 C  CG  . GLN   A 1 338 ? -13.772 -1.533  6.032   1.00 9.04  ? 361  GLN   A CG  1 
ATOM   2425 C  CD  . GLN   A 1 338 ? -12.581 -1.708  6.945   1.00 11.33 ? 361  GLN   A CD  1 
ATOM   2426 O  OE1 . GLN   A 1 338 ? -12.471 -1.119  8.036   1.00 11.50 ? 361  GLN   A OE1 1 
ATOM   2427 N  NE2 . GLN   A 1 338 ? -11.667 -2.562  6.509   1.00 12.09 ? 361  GLN   A NE2 1 
ATOM   2428 N  N   . THR   A 1 339 ? -17.894 1.112   5.922   1.00 9.32  ? 362  THR   A N   1 
ATOM   2429 C  CA  . THR   A 1 339 ? -18.699 2.299   6.202   1.00 8.39  ? 362  THR   A CA  1 
ATOM   2430 C  C   . THR   A 1 339 ? -19.088 2.259   7.681   1.00 8.77  ? 362  THR   A C   1 
ATOM   2431 O  O   . THR   A 1 339 ? -19.806 1.342   8.156   1.00 9.05  ? 362  THR   A O   1 
ATOM   2432 C  CB  . THR   A 1 339 ? -19.927 2.411   5.289   1.00 8.87  ? 362  THR   A CB  1 
ATOM   2433 O  OG1 . THR   A 1 339 ? -20.717 3.493   5.804   1.00 9.11  ? 362  THR   A OG1 1 
ATOM   2434 C  CG2 . THR   A 1 339 ? -20.759 1.148   5.234   1.00 9.18  ? 362  THR   A CG2 1 
ATOM   2435 N  N   . GLY   A 1 340 ? -18.481 3.199   8.411   1.00 9.10  ? 363  GLY   A N   1 
ATOM   2436 C  CA  . GLY   A 1 340 ? -18.591 3.258   9.863   1.00 8.30  ? 363  GLY   A CA  1 
ATOM   2437 C  C   . GLY   A 1 340 ? -19.055 4.606   10.409  1.00 8.78  ? 363  GLY   A C   1 
ATOM   2438 O  O   . GLY   A 1 340 ? -19.267 5.580   9.669   1.00 8.36  ? 363  GLY   A O   1 
ATOM   2439 N  N   . THR   A 1 341 ? -19.171 4.659   11.742  1.00 8.59  ? 364  THR   A N   1 
ATOM   2440 C  CA  . THR   A 1 341 ? -19.384 5.915   12.449  1.00 9.29  ? 364  THR   A CA  1 
ATOM   2441 C  C   . THR   A 1 341 ? -18.214 6.126   13.404  1.00 9.46  ? 364  THR   A C   1 
ATOM   2442 O  O   . THR   A 1 341 ? -17.515 5.194   13.799  1.00 10.48 ? 364  THR   A O   1 
ATOM   2443 C  CB  . THR   A 1 341 ? -20.686 5.981   13.263  1.00 10.16 ? 364  THR   A CB  1 
ATOM   2444 O  OG1 . THR   A 1 341 ? -20.457 5.447   14.576  1.00 10.63 ? 364  THR   A OG1 1 
ATOM   2445 C  CG2 . THR   A 1 341 ? -21.871 5.309   12.588  1.00 9.84  ? 364  THR   A CG2 1 
ATOM   2446 N  N   . LEU   A 1 342 ? -18.036 7.380   13.779  1.00 8.87  ? 365  LEU   A N   1 
ATOM   2447 C  CA  . LEU   A 1 342 ? -17.272 7.774   14.940  1.00 8.37  ? 365  LEU   A CA  1 
ATOM   2448 C  C   . LEU   A 1 342 ? -18.128 7.554   16.176  1.00 8.58  ? 365  LEU   A C   1 
ATOM   2449 O  O   . LEU   A 1 342 ? -19.224 8.088   16.310  1.00 8.68  ? 365  LEU   A O   1 
ATOM   2450 C  CB  . LEU   A 1 342 ? -16.847 9.232   14.815  1.00 8.41  ? 365  LEU   A CB  1 
ATOM   2451 C  CG  . LEU   A 1 342 ? -15.744 9.735   15.761  1.00 9.21  ? 365  LEU   A CG  1 
ATOM   2452 C  CD1 . LEU   A 1 342 ? -14.402 9.180   15.299  1.00 9.56  ? 365  LEU   A CD1 1 
ATOM   2453 C  CD2 . LEU   A 1 342 ? -15.685 11.257  15.835  1.00 9.55  ? 365  LEU   A CD2 1 
ATOM   2454 N  N   . ASP   A 1 343 ? -17.571 6.803   17.136  1.00 8.06  ? 366  ASP   A N   1 
ATOM   2455 C  CA  . ASP   A 1 343 ? -18.272 6.485   18.357  1.00 8.24  ? 366  ASP   A CA  1 
ATOM   2456 C  C   . ASP   A 1 343 ? -17.366 6.877   19.530  1.00 7.96  ? 366  ASP   A C   1 
ATOM   2457 O  O   . ASP   A 1 343 ? -16.290 6.296   19.706  1.00 7.58  ? 366  ASP   A O   1 
ATOM   2458 C  CB  . ASP   A 1 343 ? -18.701 5.029   18.280  1.00 8.22  ? 366  ASP   A CB  1 
ATOM   2459 C  CG  . ASP   A 1 343 ? -19.411 4.531   19.517  1.00 8.54  ? 366  ASP   A CG  1 
ATOM   2460 O  OD1 . ASP   A 1 343 ? -19.182 5.119   20.599  1.00 8.15  ? 366  ASP   A OD1 1 
ATOM   2461 O  OD2 . ASP   A 1 343 ? -20.177 3.604   19.356  1.00 9.20  ? 366  ASP   A OD2 1 
ATOM   2462 N  N   . GLN   A 1 344 ? -17.805 7.853   20.338  1.00 7.21  ? 367  GLN   A N   1 
ATOM   2463 C  CA  . GLN   A 1 344 ? -16.991 8.408   21.396  1.00 7.18  ? 367  GLN   A CA  1 
ATOM   2464 C  C   . GLN   A 1 344 ? -17.198 7.720   22.740  1.00 7.27  ? 367  GLN   A C   1 
ATOM   2465 O  O   . GLN   A 1 344 ? -16.451 7.993   23.665  1.00 6.68  ? 367  GLN   A O   1 
ATOM   2466 C  CB  . GLN   A 1 344 ? -17.172 9.919   21.504  1.00 7.53  ? 367  GLN   A CB  1 
ATOM   2467 C  CG  . GLN   A 1 344 ? -16.935 10.623  20.172  1.00 7.42  ? 367  GLN   A CG  1 
ATOM   2468 C  CD  . GLN   A 1 344 ? -16.674 12.092  20.396  1.00 7.67  ? 367  GLN   A CD  1 
ATOM   2469 O  OE1 . GLN   A 1 344 ? -15.618 12.512  20.905  1.00 8.16  ? 367  GLN   A OE1 1 
ATOM   2470 N  NE2 . GLN   A 1 344 ? -17.705 12.879  20.162  1.00 7.58  ? 367  GLN   A NE2 1 
ATOM   2471 N  N   . GLY   A 1 345 ? -18.213 6.854   22.878  1.00 6.99  ? 368  GLY   A N   1 
ATOM   2472 C  CA  . GLY   A 1 345 ? -18.366 6.090   24.108  1.00 7.46  ? 368  GLY   A CA  1 
ATOM   2473 C  C   . GLY   A 1 345 ? -18.778 6.908   25.322  1.00 7.94  ? 368  GLY   A C   1 
ATOM   2474 O  O   . GLY   A 1 345 ? -18.399 6.525   26.439  1.00 8.56  ? 368  GLY   A O   1 
ATOM   2475 N  N   . TYR   A 1 346 ? -19.537 8.003   25.107  1.00 7.79  ? 369  TYR   A N   1 
ATOM   2476 C  CA  . TYR   A 1 346 ? -19.928 8.902   26.191  1.00 8.46  ? 369  TYR   A CA  1 
ATOM   2477 C  C   . TYR   A 1 346 ? -21.393 8.683   26.513  1.00 8.41  ? 369  TYR   A C   1 
ATOM   2478 O  O   . TYR   A 1 346 ? -22.187 8.409   25.620  1.00 8.56  ? 369  TYR   A O   1 
ATOM   2479 C  CB  . TYR   A 1 346 ? -19.688 10.380  25.906  1.00 7.97  ? 369  TYR   A CB  1 
ATOM   2480 C  CG  . TYR   A 1 346 ? -18.444 10.971  26.551  1.00 7.22  ? 369  TYR   A CG  1 
ATOM   2481 C  CD1 . TYR   A 1 346 ? -17.196 10.765  26.010  1.00 6.57  ? 369  TYR   A CD1 1 
ATOM   2482 C  CD2 . TYR   A 1 346 ? -18.512 11.675  27.741  1.00 7.24  ? 369  TYR   A CD2 1 
ATOM   2483 C  CE1 . TYR   A 1 346 ? -16.046 11.242  26.629  1.00 6.58  ? 369  TYR   A CE1 1 
ATOM   2484 C  CE2 . TYR   A 1 346 ? -17.380 12.229  28.325  1.00 7.43  ? 369  TYR   A CE2 1 
ATOM   2485 C  CZ  . TYR   A 1 346 ? -16.135 12.011  27.786  1.00 6.71  ? 369  TYR   A CZ  1 
ATOM   2486 O  OH  . TYR   A 1 346 ? -15.009 12.548  28.357  1.00 6.52  ? 369  TYR   A OH  1 
ATOM   2487 N  N   . TRP   A 1 347 ? -21.723 8.812   27.801  1.00 9.20  ? 370  TRP   A N   1 
ATOM   2488 C  CA  . TRP   A 1 347 ? -23.065 8.610   28.311  1.00 8.91  ? 370  TRP   A CA  1 
ATOM   2489 C  C   . TRP   A 1 347 ? -23.413 9.795   29.211  1.00 8.72  ? 370  TRP   A C   1 
ATOM   2490 O  O   . TRP   A 1 347 ? -22.607 10.184  30.077  1.00 9.11  ? 370  TRP   A O   1 
ATOM   2491 C  CB  . TRP   A 1 347 ? -23.123 7.305   29.125  1.00 9.01  ? 370  TRP   A CB  1 
ATOM   2492 C  CG  . TRP   A 1 347 ? -22.975 6.114   28.239  1.00 9.00  ? 370  TRP   A CG  1 
ATOM   2493 C  CD1 . TRP   A 1 347 ? -21.814 5.548   27.808  1.00 8.73  ? 370  TRP   A CD1 1 
ATOM   2494 C  CD2 . TRP   A 1 347 ? -24.059 5.400   27.619  1.00 9.04  ? 370  TRP   A CD2 1 
ATOM   2495 N  NE1 . TRP   A 1 347 ? -22.104 4.524   26.959  1.00 9.32  ? 370  TRP   A NE1 1 
ATOM   2496 C  CE2 . TRP   A 1 347 ? -23.463 4.403   26.832  1.00 8.82  ? 370  TRP   A CE2 1 
ATOM   2497 C  CE3 . TRP   A 1 347 ? -25.450 5.515   27.655  1.00 8.87  ? 370  TRP   A CE3 1 
ATOM   2498 C  CZ2 . TRP   A 1 347 ? -24.214 3.506   26.089  1.00 9.22  ? 370  TRP   A CZ2 1 
ATOM   2499 C  CZ3 . TRP   A 1 347 ? -26.184 4.609   26.930  1.00 9.37  ? 370  TRP   A CZ3 1 
ATOM   2500 C  CH2 . TRP   A 1 347 ? -25.557 3.651   26.118  1.00 9.37  ? 370  TRP   A CH2 1 
ATOM   2501 N  N   . PRO   A 1 348 ? -24.623 10.375  29.089  1.00 8.19  ? 371  PRO   A N   1 
ATOM   2502 C  CA  . PRO   A 1 348 ? -24.994 11.493  29.950  1.00 8.14  ? 371  PRO   A CA  1 
ATOM   2503 C  C   . PRO   A 1 348 ? -25.161 11.148  31.431  1.00 8.38  ? 371  PRO   A C   1 
ATOM   2504 O  O   . PRO   A 1 348 ? -24.897 11.995  32.271  1.00 9.81  ? 371  PRO   A O   1 
ATOM   2505 C  CB  . PRO   A 1 348 ? -26.314 11.943  29.334  1.00 8.00  ? 371  PRO   A CB  1 
ATOM   2506 C  CG  . PRO   A 1 348 ? -26.880 10.713  28.643  1.00 8.85  ? 371  PRO   A CG  1 
ATOM   2507 C  CD  . PRO   A 1 348 ? -25.694 9.940   28.177  1.00 8.48  ? 371  PRO   A CD  1 
ATOM   2508 N  N   . ASP   A 1 349 ? -25.567 9.878   31.704  1.00 8.66  ? 372  ASP   A N   1 
ATOM   2509 C  CA  . ASP   A 1 349 ? -25.788 9.333   33.033  1.00 8.62  ? 372  ASP   A CA  1 
ATOM   2510 C  C   . ASP   A 1 349 ? -24.510 8.728   33.631  1.00 8.61  ? 372  ASP   A C   1 
ATOM   2511 O  O   . ASP   A 1 349 ? -24.239 8.888   34.826  1.00 7.49  ? 372  ASP   A O   1 
ATOM   2512 C  CB  . ASP   A 1 349 ? -26.962 8.357   33.015  1.00 8.49  ? 372  ASP   A CB  1 
ATOM   2513 C  CG  . ASP   A 1 349 ? -26.990 7.312   31.909  1.00 9.14  ? 372  ASP   A CG  1 
ATOM   2514 O  OD1 . ASP   A 1 349 ? -26.005 7.281   31.117  1.00 9.14  ? 372  ASP   A OD1 1 
ATOM   2515 O  OD2 . ASP   A 1 349 ? -27.975 6.511   31.905  1.00 9.45  ? 372  ASP   A OD2 1 
ATOM   2516 N  N   . GLY   A 1 350 ? -23.750 8.002   32.810  1.00 8.15  ? 373  GLY   A N   1 
ATOM   2517 C  CA  . GLY   A 1 350 ? -22.611 7.239   33.286  1.00 8.59  ? 373  GLY   A CA  1 
ATOM   2518 C  C   . GLY   A 1 350 ? -21.256 7.847   32.924  1.00 8.75  ? 373  GLY   A C   1 
ATOM   2519 O  O   . GLY   A 1 350 ? -20.228 7.365   33.440  1.00 9.04  ? 373  GLY   A O   1 
ATOM   2520 N  N   . ILE   A 1 351 ? -21.241 8.863   32.043  1.00 8.50  ? 374  ILE   A N   1 
ATOM   2521 C  CA  . ILE   A 1 351 ? -20.026 9.536   31.574  1.00 8.54  ? 374  ILE   A CA  1 
ATOM   2522 C  C   . ILE   A 1 351 ? -19.213 8.526   30.738  1.00 9.14  ? 374  ILE   A C   1 
ATOM   2523 O  O   . ILE   A 1 351 ? -19.487 8.385   29.548  1.00 9.48  ? 374  ILE   A O   1 
ATOM   2524 C  CB  . ILE   A 1 351 ? -19.240 10.245  32.698  1.00 8.66  ? 374  ILE   A CB  1 
ATOM   2525 C  CG1 . ILE   A 1 351 ? -20.074 11.239  33.455  1.00 9.15  ? 374  ILE   A CG1 1 
ATOM   2526 C  CG2 . ILE   A 1 351 ? -18.013 10.950  32.120  1.00 9.43  ? 374  ILE   A CG2 1 
ATOM   2527 C  CD1 . ILE   A 1 351 ? -20.836 12.218  32.587  1.00 9.12  ? 374  ILE   A CD1 1 
ATOM   2528 N  N   . TYR   A 1 352 ? -18.283 7.776   31.347  1.00 8.63  ? 375  TYR   A N   1 
ATOM   2529 C  CA  . TYR   A 1 352 ? -17.458 6.799   30.620  1.00 8.36  ? 375  TYR   A CA  1 
ATOM   2530 C  C   . TYR   A 1 352 ? -18.024 5.379   30.638  1.00 8.39  ? 375  TYR   A C   1 
ATOM   2531 O  O   . TYR   A 1 352 ? -17.518 4.517   29.916  1.00 8.85  ? 375  TYR   A O   1 
ATOM   2532 C  CB  . TYR   A 1 352 ? -16.031 6.782   31.188  1.00 8.59  ? 375  TYR   A CB  1 
ATOM   2533 C  CG  . TYR   A 1 352 ? -14.933 7.389   30.325  1.00 8.34  ? 375  TYR   A CG  1 
ATOM   2534 C  CD1 . TYR   A 1 352 ? -15.194 8.365   29.350  1.00 8.93  ? 375  TYR   A CD1 1 
ATOM   2535 C  CD2 . TYR   A 1 352 ? -13.622 6.921   30.404  1.00 8.27  ? 375  TYR   A CD2 1 
ATOM   2536 C  CE1 . TYR   A 1 352 ? -14.183 8.880   28.553  1.00 8.40  ? 375  TYR   A CE1 1 
ATOM   2537 C  CE2 . TYR   A 1 352 ? -12.598 7.440   29.609  1.00 8.20  ? 375  TYR   A CE2 1 
ATOM   2538 C  CZ  . TYR   A 1 352 ? -12.876 8.417   28.673  1.00 8.34  ? 375  TYR   A CZ  1 
ATOM   2539 O  OH  . TYR   A 1 352 ? -11.875 8.901   27.882  1.00 8.43  ? 375  TYR   A OH  1 
ATOM   2540 N  N   . THR   A 1 353 ? -19.018 5.134   31.483  1.00 7.96  ? 376  THR   A N   1 
ATOM   2541 C  CA  . THR   A 1 353 ? -19.541 3.787   31.764  1.00 8.38  ? 376  THR   A CA  1 
ATOM   2542 C  C   . THR   A 1 353 ? -21.014 3.684   31.357  1.00 7.75  ? 376  THR   A C   1 
ATOM   2543 O  O   . THR   A 1 353 ? -21.901 4.379   31.852  1.00 6.68  ? 376  THR   A O   1 
ATOM   2544 C  CB  . THR   A 1 353 ? -19.345 3.495   33.258  1.00 8.68  ? 376  THR   A CB  1 
ATOM   2545 O  OG1 . THR   A 1 353 ? -17.957 3.679   33.545  1.00 8.71  ? 376  THR   A OG1 1 
ATOM   2546 C  CG2 . THR   A 1 353 ? -19.767 2.075   33.584  1.00 9.46  ? 376  THR   A CG2 1 
ATOM   2547 N  N   . ALA   A 1 354 ? -21.292 2.791   30.408  1.00 7.80  ? 377  ALA   A N   1 
ATOM   2548 C  CA  . ALA   A 1 354 ? -22.669 2.549   30.009  1.00 8.26  ? 377  ALA   A CA  1 
ATOM   2549 C  C   . ALA   A 1 354 ? -23.441 1.942   31.180  1.00 9.57  ? 377  ALA   A C   1 
ATOM   2550 O  O   . ALA   A 1 354 ? -22.915 1.131   31.954  1.00 9.04  ? 377  ALA   A O   1 
ATOM   2551 C  CB  . ALA   A 1 354 ? -22.728 1.645   28.795  1.00 7.97  ? 377  ALA   A CB  1 
ATOM   2552 N  N   . PRO   A 1 355 ? -24.686 2.388   31.385  1.00 9.48  ? 378  PRO   A N   1 
ATOM   2553 C  CA  . PRO   A 1 355 ? -25.401 2.063   32.626  1.00 9.69  ? 378  PRO   A CA  1 
ATOM   2554 C  C   . PRO   A 1 355 ? -25.628 0.556   32.811  1.00 9.80  ? 378  PRO   A C   1 
ATOM   2555 O  O   . PRO   A 1 355 ? -25.633 0.076   33.950  1.00 8.93  ? 378  PRO   A O   1 
ATOM   2556 C  CB  . PRO   A 1 355 ? -26.699 2.842   32.511  1.00 10.53 ? 378  PRO   A CB  1 
ATOM   2557 C  CG  . PRO   A 1 355 ? -26.787 3.238   31.053  1.00 9.75  ? 378  PRO   A CG  1 
ATOM   2558 C  CD  . PRO   A 1 355 ? -25.364 3.428   30.584  1.00 10.09 ? 378  PRO   A CD  1 
ATOM   2559 N  N   . THR   A 1 356 ? -25.854 -0.166  31.702  1.00 9.08  ? 379  THR   A N   1 
ATOM   2560 C  CA  . THR   A 1 356 ? -26.097 -1.607  31.713  1.00 8.84  ? 379  THR   A CA  1 
ATOM   2561 C  C   . THR   A 1 356 ? -25.439 -2.227  30.483  1.00 9.26  ? 379  THR   A C   1 
ATOM   2562 O  O   . THR   A 1 356 ? -25.123 -1.531  29.517  1.00 8.13  ? 379  THR   A O   1 
ATOM   2563 C  CB  . THR   A 1 356 ? -27.586 -1.981  31.702  1.00 9.39  ? 379  THR   A CB  1 
ATOM   2564 O  OG1 . THR   A 1 356 ? -28.159 -1.660  30.424  1.00 9.02  ? 379  THR   A OG1 1 
ATOM   2565 C  CG2 . THR   A 1 356 ? -28.369 -1.312  32.802  1.00 9.13  ? 379  THR   A CG2 1 
ATOM   2566 N  N   . ASP   A 1 357 ? -25.319 -3.562  30.488  1.00 9.21  ? 380  ASP   A N   1 
ATOM   2567 C  CA  . ASP   A 1 357 ? -24.820 -4.243  29.305  1.00 9.87  ? 380  ASP   A CA  1 
ATOM   2568 C  C   . ASP   A 1 357 ? -25.701 -3.999  28.073  1.00 9.25  ? 380  ASP   A C   1 
ATOM   2569 O  O   . ASP   A 1 357 ? -25.179 -3.860  26.956  1.00 9.20  ? 380  ASP   A O   1 
ATOM   2570 C  CB  . ASP   A 1 357 ? -24.609 -5.708  29.633  1.00 9.63  ? 380  ASP   A CB  1 
ATOM   2571 C  CG  . ASP   A 1 357 ? -23.661 -6.416  28.678  1.00 10.16 ? 380  ASP   A CG  1 
ATOM   2572 O  OD1 . ASP   A 1 357 ? -22.496 -5.936  28.510  1.00 10.17 ? 380  ASP   A OD1 1 
ATOM   2573 O  OD2 . ASP   A 1 357 ? -24.072 -7.466  28.178  1.00 10.35 ? 380  ASP   A OD2 1 
ATOM   2574 N  N   . ALA   A 1 358 ? -27.023 -3.882  28.271  1.00 9.43  ? 381  ALA   A N   1 
ATOM   2575 C  CA  . ALA   A 1 358 ? -27.947 -3.612  27.179  1.00 9.30  ? 381  ALA   A CA  1 
ATOM   2576 C  C   . ALA   A 1 358 ? -27.660 -2.236  26.563  1.00 9.32  ? 381  ALA   A C   1 
ATOM   2577 O  O   . ALA   A 1 358 ? -27.715 -2.057  25.335  1.00 9.13  ? 381  ALA   A O   1 
ATOM   2578 C  CB  . ALA   A 1 358 ? -29.377 -3.720  27.634  1.00 8.84  ? 381  ALA   A CB  1 
ATOM   2579 N  N   . ALA   A 1 359 ? -27.325 -1.283  27.424  1.00 8.42  ? 382  ALA   A N   1 
ATOM   2580 C  CA  . ALA   A 1 359 ? -26.943 0.053   26.997  1.00 8.24  ? 382  ALA   A CA  1 
ATOM   2581 C  C   . ALA   A 1 359 ? -25.640 0.028   26.201  1.00 8.77  ? 382  ALA   A C   1 
ATOM   2582 O  O   . ALA   A 1 359 ? -25.538 0.655   25.140  1.00 8.24  ? 382  ALA   A O   1 
ATOM   2583 C  CB  . ALA   A 1 359 ? -26.823 0.947   28.213  1.00 8.02  ? 382  ALA   A CB  1 
ATOM   2584 N  N   . LEU   A 1 360 ? -24.645 -0.702  26.713  1.00 8.84  ? 383  LEU   A N   1 
ATOM   2585 C  CA  . LEU   A 1 360 ? -23.331 -0.785  26.086  1.00 8.99  ? 383  LEU   A CA  1 
ATOM   2586 C  C   . LEU   A 1 360 ? -23.473 -1.297  24.650  1.00 9.29  ? 383  LEU   A C   1 
ATOM   2587 O  O   . LEU   A 1 360 ? -22.939 -0.721  23.696  1.00 9.21  ? 383  LEU   A O   1 
ATOM   2588 C  CB  . LEU   A 1 360 ? -22.434 -1.700  26.915  1.00 9.46  ? 383  LEU   A CB  1 
ATOM   2589 C  CG  . LEU   A 1 360 ? -21.032 -1.964  26.360  1.00 9.11  ? 383  LEU   A CG  1 
ATOM   2590 C  CD1 . LEU   A 1 360 ? -20.202 -0.687  26.372  1.00 9.14  ? 383  LEU   A CD1 1 
ATOM   2591 C  CD2 . LEU   A 1 360 ? -20.367 -3.092  27.126  1.00 9.60  ? 383  LEU   A CD2 1 
ATOM   2592 N  N   . ARG   A 1 361 ? -24.231 -2.369  24.475  1.00 9.78  ? 384  ARG   A N   1 
ATOM   2593 C  CA  . ARG   A 1 361 ? -24.319 -2.984  23.165  1.00 10.65 ? 384  ARG   A CA  1 
ATOM   2594 C  C   . ARG   A 1 361 ? -25.310 -2.261  22.264  1.00 9.44  ? 384  ARG   A C   1 
ATOM   2595 O  O   . ARG   A 1 361 ? -25.202 -2.359  21.057  1.00 9.64  ? 384  ARG   A O   1 
ATOM   2596 C  CB  . ARG   A 1 361 ? -24.636 -4.472  23.318  1.00 12.68 ? 384  ARG   A CB  1 
ATOM   2597 C  CG  . ARG   A 1 361 ? -26.069 -4.808  23.623  1.00 15.03 ? 384  ARG   A CG  1 
ATOM   2598 C  CD  . ARG   A 1 361 ? -26.243 -6.295  23.156  1.00 16.82 ? 384  ARG   A CD  1 
ATOM   2599 N  NE  . ARG   A 1 361 ? -27.540 -6.657  23.705  1.00 18.23 ? 384  ARG   A NE  1 
ATOM   2600 C  CZ  . ARG   A 1 361 ? -27.767 -6.834  24.998  1.00 19.88 ? 384  ARG   A CZ  1 
ATOM   2601 N  NH1 . ARG   A 1 361 ? -26.809 -7.131  25.816  1.00 19.09 ? 384  ARG   A NH1 1 
ATOM   2602 N  NH2 . ARG   A 1 361 ? -28.983 -6.776  25.474  1.00 20.74 ? 384  ARG   A NH2 1 
ATOM   2603 N  N   . HIS   A 1 362 ? -26.258 -1.489  22.850  1.00 9.82  ? 385  HIS   A N   1 
ATOM   2604 C  CA  . HIS   A 1 362 ? -27.244 -0.758  22.079  1.00 9.44  ? 385  HIS   A CA  1 
ATOM   2605 C  C   . HIS   A 1 362 ? -26.591 0.065   20.965  1.00 9.14  ? 385  HIS   A C   1 
ATOM   2606 O  O   . HIS   A 1 362 ? -27.027 0.035   19.832  1.00 9.03  ? 385  HIS   A O   1 
ATOM   2607 C  CB  . HIS   A 1 362 ? -28.095 0.149   22.980  1.00 9.76  ? 385  HIS   A CB  1 
ATOM   2608 C  CG  . HIS   A 1 362 ? -28.994 1.062   22.243  1.00 10.20 ? 385  HIS   A CG  1 
ATOM   2609 N  ND1 . HIS   A 1 362 ? -30.268 0.691   21.882  1.00 11.28 ? 385  HIS   A ND1 1 
ATOM   2610 C  CD2 . HIS   A 1 362 ? -28.809 2.334   21.785  1.00 10.14 ? 385  HIS   A CD2 1 
ATOM   2611 C  CE1 . HIS   A 1 362 ? -30.854 1.711   21.251  1.00 11.31 ? 385  HIS   A CE1 1 
ATOM   2612 N  NE2 . HIS   A 1 362 ? -29.991 2.723   21.179  1.00 9.46  ? 385  HIS   A NE2 1 
ATOM   2613 N  N   . ASP   A 1 363 ? -25.557 0.830   21.278  1.00 8.73  ? 386  ASP   A N   1 
ATOM   2614 C  CA  . ASP   A 1 363 ? -24.935 1.686   20.285  1.00 8.39  ? 386  ASP   A CA  1 
ATOM   2615 C  C   . ASP   A 1 363 ? -24.412 0.882   19.100  1.00 8.05  ? 386  ASP   A C   1 
ATOM   2616 O  O   . ASP   A 1 363 ? -24.485 1.359   17.953  1.00 7.96  ? 386  ASP   A O   1 
ATOM   2617 C  CB  . ASP   A 1 363 ? -23.813 2.490   20.915  1.00 8.43  ? 386  ASP   A CB  1 
ATOM   2618 C  CG  . ASP   A 1 363 ? -24.211 3.462   22.015  1.00 9.19  ? 386  ASP   A CG  1 
ATOM   2619 O  OD1 . ASP   A 1 363 ? -25.418 3.869   22.056  1.00 9.80  ? 386  ASP   A OD1 1 
ATOM   2620 O  OD2 . ASP   A 1 363 ? -23.290 3.758   22.868  1.00 9.37  ? 386  ASP   A OD2 1 
ATOM   2621 N  N   . LEU   A 1 364 ? -23.882 -0.323  19.375  1.00 7.91  ? 387  LEU   A N   1 
ATOM   2622 C  CA  . LEU   A 1 364 ? -23.409 -1.193  18.312  1.00 8.08  ? 387  LEU   A CA  1 
ATOM   2623 C  C   . LEU   A 1 364 ? -24.565 -1.822  17.522  1.00 8.57  ? 387  LEU   A C   1 
ATOM   2624 O  O   . LEU   A 1 364 ? -24.502 -1.927  16.293  1.00 8.36  ? 387  LEU   A O   1 
ATOM   2625 C  CB  . LEU   A 1 364 ? -22.480 -2.251  18.902  1.00 8.49  ? 387  LEU   A CB  1 
ATOM   2626 C  CG  . LEU   A 1 364 ? -21.224 -1.706  19.583  1.00 9.39  ? 387  LEU   A CG  1 
ATOM   2627 C  CD1 . LEU   A 1 364 ? -20.379 -2.872  20.010  1.00 9.53  ? 387  LEU   A CD1 1 
ATOM   2628 C  CD2 . LEU   A 1 364 ? -20.457 -0.742  18.692  1.00 9.65  ? 387  LEU   A CD2 1 
ATOM   2629 N  N   . GLN   A 1 365 ? -25.622 -2.261  18.221  1.00 8.92  ? 388  GLN   A N   1 
ATOM   2630 C  CA  . GLN   A 1 365 ? -26.823 -2.741  17.550  1.00 9.63  ? 388  GLN   A CA  1 
ATOM   2631 C  C   . GLN   A 1 365 ? -27.321 -1.675  16.574  1.00 9.80  ? 388  GLN   A C   1 
ATOM   2632 O  O   . GLN   A 1 365 ? -27.767 -1.995  15.481  1.00 9.50  ? 388  GLN   A O   1 
ATOM   2633 C  CB  . GLN   A 1 365 ? -27.895 -3.140  18.559  1.00 10.70 ? 388  GLN   A CB  1 
ATOM   2634 C  CG  . GLN   A 1 365 ? -27.521 -4.409  19.316  1.00 10.90 ? 388  GLN   A CG  1 
ATOM   2635 C  CD  . GLN   A 1 365 ? -28.488 -4.800  20.420  1.00 13.19 ? 388  GLN   A CD  1 
ATOM   2636 O  OE1 . GLN   A 1 365 ? -28.480 -5.950  20.874  1.00 14.51 ? 388  GLN   A OE1 1 
ATOM   2637 N  NE2 . GLN   A 1 365 ? -29.260 -3.845  20.922  1.00 14.86 ? 388  GLN   A NE2 1 
ATOM   2638 N  N   . LYS   A 1 366 ? -27.264 -0.387  16.971  1.00 9.12  ? 389  LYS   A N   1 
ATOM   2639 C  CA  . LYS   A 1 366 ? -27.784 0.663   16.110  1.00 9.89  ? 389  LYS   A CA  1 
ATOM   2640 C  C   . LYS   A 1 366 ? -26.910 0.799   14.856  1.00 9.04  ? 389  LYS   A C   1 
ATOM   2641 O  O   . LYS   A 1 366 ? -27.421 1.101   13.771  1.00 8.29  ? 389  LYS   A O   1 
ATOM   2642 C  CB  . LYS   A 1 366 ? -27.931 1.976   16.886  1.00 10.19 ? 389  LYS   A CB  1 
ATOM   2643 C  CG  . LYS   A 1 366 ? -29.001 1.929   17.969  1.00 11.15 ? 389  LYS   A CG  1 
ATOM   2644 C  CD  . LYS   A 1 366 ? -30.346 1.354   17.586  1.00 12.27 ? 389  LYS   A CD  1 
ATOM   2645 C  CE  . LYS   A 1 366 ? -30.997 2.056   16.424  1.00 12.59 ? 389  LYS   A CE  1 
ATOM   2646 N  NZ  . LYS   A 1 366 ? -32.166 1.271   16.027  1.00 12.84 ? 389  LYS   A NZ  1 
ATOM   2647 N  N   . HIS   A 1 367 ? -25.593 0.595   14.977  1.00 8.49  ? 390  HIS   A N   1 
ATOM   2648 C  CA  . HIS   A 1 367 ? -24.738 0.562   13.799  1.00 8.53  ? 390  HIS   A CA  1 
ATOM   2649 C  C   . HIS   A 1 367 ? -25.267 -0.469  12.791  1.00 8.69  ? 390  HIS   A C   1 
ATOM   2650 O  O   . HIS   A 1 367 ? -25.407 -0.190  11.599  1.00 8.89  ? 390  HIS   A O   1 
ATOM   2651 C  CB  . HIS   A 1 367 ? -23.299 0.168   14.149  1.00 8.53  ? 390  HIS   A CB  1 
ATOM   2652 C  CG  . HIS   A 1 367 ? -22.424 1.246   14.692  1.00 8.35  ? 390  HIS   A CG  1 
ATOM   2653 N  ND1 . HIS   A 1 367 ? -22.584 1.749   15.967  1.00 8.13  ? 390  HIS   A ND1 1 
ATOM   2654 C  CD2 . HIS   A 1 367 ? -21.399 1.915   14.131  1.00 8.46  ? 390  HIS   A CD2 1 
ATOM   2655 C  CE1 . HIS   A 1 367 ? -21.626 2.677   16.158  1.00 9.17  ? 390  HIS   A CE1 1 
ATOM   2656 N  NE2 . HIS   A 1 367 ? -20.876 2.770   15.076  1.00 8.57  ? 390  HIS   A NE2 1 
ATOM   2657 N  N   . LYS   A 1 368 ? -25.559 -1.678  13.270  1.00 9.62  ? 391  LYS   A N   1 
ATOM   2658 C  CA  . LYS   A 1 368 ? -26.098 -2.762  12.447  1.00 9.85  ? 391  LYS   A CA  1 
ATOM   2659 C  C   . LYS   A 1 368 ? -27.446 -2.417  11.829  1.00 10.44 ? 391  LYS   A C   1 
ATOM   2660 O  O   . LYS   A 1 368 ? -27.640 -2.631  10.621  1.00 10.56 ? 391  LYS   A O   1 
ATOM   2661 C  CB  . LYS   A 1 368 ? -26.234 -4.069  13.233  1.00 11.00 ? 391  LYS   A CB  1 
ATOM   2662 C  CG  . LYS   A 1 368 ? -24.893 -4.594  13.745  1.00 11.82 ? 391  LYS   A CG  1 
ATOM   2663 C  CD  . LYS   A 1 368 ? -23.920 -5.043  12.649  1.00 13.20 ? 391  LYS   A CD  1 
ATOM   2664 C  CE  . LYS   A 1 368 ? -24.386 -6.280  11.878  1.00 14.92 ? 391  LYS   A CE  1 
ATOM   2665 N  NZ  . LYS   A 1 368 ? -23.299 -6.749  11.019  1.00 14.80 ? 391  LYS   A NZ  1 
ATOM   2666 N  N   . ASP   A 1 369 ? -28.359 -1.897  12.657  1.00 10.23 ? 392  ASP   A N   1 
ATOM   2667 C  CA  . ASP   A 1 369 ? -29.666 -1.463  12.197  1.00 10.69 ? 392  ASP   A CA  1 
ATOM   2668 C  C   . ASP   A 1 369 ? -29.549 -0.451  11.049  1.00 10.77 ? 392  ASP   A C   1 
ATOM   2669 O  O   . ASP   A 1 369 ? -30.396 -0.461  10.154  1.00 11.34 ? 392  ASP   A O   1 
ATOM   2670 C  CB  . ASP   A 1 369 ? -30.441 -0.818  13.319  1.00 11.12 ? 392  ASP   A CB  1 
ATOM   2671 C  CG  . ASP   A 1 369 ? -30.841 -1.747  14.452  1.00 10.75 ? 392  ASP   A CG  1 
ATOM   2672 O  OD1 . ASP   A 1 369 ? -30.762 -3.009  14.253  1.00 12.31 ? 392  ASP   A OD1 1 
ATOM   2673 O  OD2 . ASP   A 1 369 ? -31.206 -1.190  15.539  1.00 11.60 ? 392  ASP   A OD2 1 
ATOM   2674 N  N   . LEU   A 1 370 ? -28.544 0.439   11.118  1.00 10.19 ? 393  LEU   A N   1 
ATOM   2675 C  CA  . LEU   A 1 370 ? -28.362 1.491   10.122  1.00 10.24 ? 393  LEU   A CA  1 
ATOM   2676 C  C   . LEU   A 1 370 ? -27.446 1.064   8.976   1.00 9.96  ? 393  LEU   A C   1 
ATOM   2677 O  O   . LEU   A 1 370 ? -27.081 1.903   8.137   1.00 10.46 ? 393  LEU   A O   1 
ATOM   2678 C  CB  . LEU   A 1 370 ? -27.837 2.698   10.876  1.00 10.42 ? 393  LEU   A CB  1 
ATOM   2679 C  CG  . LEU   A 1 370 ? -28.821 3.316   11.868  1.00 11.02 ? 393  LEU   A CG  1 
ATOM   2680 C  CD1 . LEU   A 1 370 ? -28.148 4.380   12.664  1.00 11.56 ? 393  LEU   A CD1 1 
ATOM   2681 C  CD2 . LEU   A 1 370 ? -30.051 3.902   11.190  1.00 12.12 ? 393  LEU   A CD2 1 
ATOM   2682 N  N   . GLY   A 1 371 ? -27.064 -0.222  8.919   1.00 8.86  ? 394  GLY   A N   1 
ATOM   2683 C  CA  . GLY   A 1 371 ? -26.313 -0.763  7.791   1.00 8.86  ? 394  GLY   A CA  1 
ATOM   2684 C  C   . GLY   A 1 371 ? -24.816 -0.485  7.819   1.00 8.89  ? 394  GLY   A C   1 
ATOM   2685 O  O   . GLY   A 1 371 ? -24.124 -0.875  6.887   1.00 10.39 ? 394  GLY   A O   1 
ATOM   2686 N  N   . PHE   A 1 372 ? -24.281 0.138   8.900   1.00 8.38  ? 395  PHE   A N   1 
ATOM   2687 C  CA  . PHE   A 1 372 ? -22.849 0.289   9.031   1.00 8.88  ? 395  PHE   A CA  1 
ATOM   2688 C  C   . PHE   A 1 372 ? -22.227 -1.088  9.261   1.00 8.88  ? 395  PHE   A C   1 
ATOM   2689 O  O   . PHE   A 1 372 ? -22.825 -1.960  9.879   1.00 10.25 ? 395  PHE   A O   1 
ATOM   2690 C  CB  . PHE   A 1 372 ? -22.463 1.221   10.182  1.00 8.65  ? 395  PHE   A CB  1 
ATOM   2691 C  CG  . PHE   A 1 372 ? -22.934 2.634   9.922   1.00 8.97  ? 395  PHE   A CG  1 
ATOM   2692 C  CD1 . PHE   A 1 372 ? -22.214 3.486   9.084   1.00 9.21  ? 395  PHE   A CD1 1 
ATOM   2693 C  CD2 . PHE   A 1 372 ? -24.104 3.116   10.511  1.00 8.80  ? 395  PHE   A CD2 1 
ATOM   2694 C  CE1 . PHE   A 1 372 ? -22.617 4.802   8.905   1.00 9.63  ? 395  PHE   A CE1 1 
ATOM   2695 C  CE2 . PHE   A 1 372 ? -24.515 4.424   10.298  1.00 8.73  ? 395  PHE   A CE2 1 
ATOM   2696 C  CZ  . PHE   A 1 372 ? -23.781 5.257   9.483   1.00 9.89  ? 395  PHE   A CZ  1 
ATOM   2697 N  N   . ASN   A 1 373 ? -20.994 -1.253  8.803   1.00 8.97  ? 396  ASN   A N   1 
ATOM   2698 C  CA  . ASN   A 1 373 ? -20.230 -2.471  9.027   1.00 8.54  ? 396  ASN   A CA  1 
ATOM   2699 C  C   . ASN   A 1 373 ? -18.937 -2.207  9.785   1.00 8.10  ? 396  ASN   A C   1 
ATOM   2700 O  O   . ASN   A 1 373 ? -18.129 -3.135  9.951   1.00 8.02  ? 396  ASN   A O   1 
ATOM   2701 C  CB  . ASN   A 1 373 ? -19.991 -3.239  7.725   1.00 8.86  ? 396  ASN   A CB  1 
ATOM   2702 C  CG  . ASN   A 1 373 ? -19.107 -2.533  6.739   1.00 9.21  ? 396  ASN   A CG  1 
ATOM   2703 O  OD1 . ASN   A 1 373 ? -18.734 -1.367  6.949   1.00 9.63  ? 396  ASN   A OD1 1 
ATOM   2704 N  ND2 . ASN   A 1 373 ? -18.741 -3.245  5.674   1.00 9.27  ? 396  ASN   A ND2 1 
ATOM   2705 N  N   . MET   A 1 374 ? -18.766 -0.983  10.306  1.00 7.71  ? 397  MET   A N   1 
ATOM   2706 C  CA  . MET   A 1 374 ? -17.539 -0.606  10.985  1.00 8.67  ? 397  MET   A CA  1 
ATOM   2707 C  C   . MET   A 1 374 ? -17.830 0.439   12.048  1.00 8.12  ? 397  MET   A C   1 
ATOM   2708 O  O   . MET   A 1 374 ? -18.793 1.208   11.944  1.00 8.88  ? 397  MET   A O   1 
ATOM   2709 C  CB  . MET   A 1 374 ? -16.521 -0.091  9.958   1.00 9.34  ? 397  MET   A CB  1 
ATOM   2710 C  CG  . MET   A 1 374 ? -15.149 0.283   10.525  1.00 9.19  ? 397  MET   A CG  1 
ATOM   2711 S  SD  . MET   A 1 374 ? -14.977 2.058   10.777  1.00 9.38  ? 397  MET   A SD  1 
ATOM   2712 C  CE  . MET   A 1 374 ? -14.790 2.584   9.067   1.00 9.21  ? 397  MET   A CE  1 
ATOM   2713 N  N   . VAL   A 1 375 ? -16.958 0.490   13.071  1.00 7.74  ? 398  VAL   A N   1 
ATOM   2714 C  CA  . VAL   A 1 375 ? -17.024 1.548   14.057  1.00 8.42  ? 398  VAL   A CA  1 
ATOM   2715 C  C   . VAL   A 1 375 ? -15.610 2.002   14.363  1.00 7.89  ? 398  VAL   A C   1 
ATOM   2716 O  O   . VAL   A 1 375 ? -14.728 1.174   14.534  1.00 6.99  ? 398  VAL   A O   1 
ATOM   2717 C  CB  . VAL   A 1 375 ? -17.784 1.161   15.339  1.00 9.17  ? 398  VAL   A CB  1 
ATOM   2718 C  CG1 . VAL   A 1 375 ? -17.241 -0.107  15.990  1.00 9.60  ? 398  VAL   A CG1 1 
ATOM   2719 C  CG2 . VAL   A 1 375 ? -17.849 2.326   16.335  1.00 9.00  ? 398  VAL   A CG2 1 
ATOM   2720 N  N   . ARG   A 1 376 ? -15.407 3.327   14.419  1.00 7.95  ? 399  ARG   A N   1 
ATOM   2721 C  CA  . ARG   A 1 376 ? -14.152 3.870   14.939  1.00 7.90  ? 399  ARG   A CA  1 
ATOM   2722 C  C   . ARG   A 1 376 ? -14.371 4.345   16.373  1.00 7.64  ? 399  ARG   A C   1 
ATOM   2723 O  O   . ARG   A 1 376 ? -15.118 5.303   16.598  1.00 8.14  ? 399  ARG   A O   1 
ATOM   2724 C  CB  . ARG   A 1 376 ? -13.574 5.003   14.087  1.00 7.73  ? 399  ARG   A CB  1 
ATOM   2725 C  CG  . ARG   A 1 376 ? -12.334 5.643   14.691  1.00 7.88  ? 399  ARG   A CG  1 
ATOM   2726 C  CD  . ARG   A 1 376 ? -11.866 6.828   13.847  1.00 8.17  ? 399  ARG   A CD  1 
ATOM   2727 N  NE  . ARG   A 1 376 ? -10.743 7.507   14.485  1.00 7.78  ? 399  ARG   A NE  1 
ATOM   2728 C  CZ  . ARG   A 1 376 ? -10.520 8.821   14.493  1.00 9.15  ? 399  ARG   A CZ  1 
ATOM   2729 N  NH1 . ARG   A 1 376 ? -11.135 9.603   13.582  1.00 8.92  ? 399  ARG   A NH1 1 
ATOM   2730 N  NH2 . ARG   A 1 376 ? -9.627  9.328   15.358  1.00 8.82  ? 399  ARG   A NH2 1 
ATOM   2731 N  N   . LYS   A 1 377 ? -13.777 3.640   17.348  1.00 7.59  ? 400  LYS   A N   1 
ATOM   2732 C  CA  . LYS   A 1 377 ? -13.930 4.019   18.743  1.00 7.88  ? 400  LYS   A CA  1 
ATOM   2733 C  C   . LYS   A 1 377 ? -12.930 5.147   19.008  1.00 7.34  ? 400  LYS   A C   1 
ATOM   2734 O  O   . LYS   A 1 377 ? -11.729 4.952   18.930  1.00 8.08  ? 400  LYS   A O   1 
ATOM   2735 C  CB  . LYS   A 1 377 ? -13.664 2.899   19.759  1.00 8.27  ? 400  LYS   A CB  1 
ATOM   2736 C  CG  . LYS   A 1 377 ? -13.888 3.291   21.216  1.00 8.09  ? 400  LYS   A CG  1 
ATOM   2737 C  CD  . LYS   A 1 377 ? -15.279 3.802   21.548  1.00 8.08  ? 400  LYS   A CD  1 
ATOM   2738 C  CE  . LYS   A 1 377 ? -16.378 2.796   21.320  1.00 8.42  ? 400  LYS   A CE  1 
ATOM   2739 N  NZ  . LYS   A 1 377 ? -17.612 3.214   21.980  1.00 8.41  ? 400  LYS   A NZ  1 
ATOM   2740 N  N   . HIS   A 1 378 ? -13.438 6.321   19.349  1.00 7.41  ? 401  HIS   A N   1 
ATOM   2741 C  CA  . HIS   A 1 378 ? -12.685 7.574   19.316  1.00 7.34  ? 401  HIS   A CA  1 
ATOM   2742 C  C   . HIS   A 1 378 ? -12.000 7.913   20.648  1.00 7.66  ? 401  HIS   A C   1 
ATOM   2743 O  O   . HIS   A 1 378 ? -12.657 8.216   21.660  1.00 8.47  ? 401  HIS   A O   1 
ATOM   2744 C  CB  . HIS   A 1 378 ? -13.616 8.712   18.887  1.00 7.52  ? 401  HIS   A CB  1 
ATOM   2745 C  CG  . HIS   A 1 378 ? -12.931 9.989   18.578  1.00 7.47  ? 401  HIS   A CG  1 
ATOM   2746 N  ND1 . HIS   A 1 378 ? -11.743 10.023  17.886  1.00 8.08  ? 401  HIS   A ND1 1 
ATOM   2747 C  CD2 . HIS   A 1 378 ? -13.249 11.286  18.859  1.00 8.08  ? 401  HIS   A CD2 1 
ATOM   2748 C  CE1 . HIS   A 1 378 ? -11.356 11.300  17.753  1.00 8.04  ? 401  HIS   A CE1 1 
ATOM   2749 N  NE2 . HIS   A 1 378 ? -12.232 12.083  18.370  1.00 8.06  ? 401  HIS   A NE2 1 
ATOM   2750 N  N   . ILE   A 1 379 ? -10.661 7.934   20.589  1.00 7.66  ? 402  ILE   A N   1 
ATOM   2751 C  CA  . ILE   A 1 379 ? -9.762  8.242   21.685  1.00 7.80  ? 402  ILE   A CA  1 
ATOM   2752 C  C   . ILE   A 1 379 ? -10.321 7.780   23.030  1.00 7.66  ? 402  ILE   A C   1 
ATOM   2753 O  O   . ILE   A 1 379 ? -10.288 8.505   24.033  1.00 7.01  ? 402  ILE   A O   1 
ATOM   2754 C  CB  . ILE   A 1 379 ? -9.297  9.721   21.655  1.00 7.85  ? 402  ILE   A CB  1 
ATOM   2755 C  CG1 . ILE   A 1 379 ? -10.445 10.717  21.647  1.00 8.35  ? 402  ILE   A CG1 1 
ATOM   2756 C  CG2 . ILE   A 1 379 ? -8.332  9.934   20.498  1.00 8.25  ? 402  ILE   A CG2 1 
ATOM   2757 C  CD1 . ILE   A 1 379 ? -10.050 12.172  21.404  1.00 8.37  ? 402  ILE   A CD1 1 
ATOM   2758 N  N   . LYS   A 1 380 ? -10.778 6.517   23.040  1.00 6.89  ? 403  LYS   A N   1 
ATOM   2759 C  CA  . LYS   A 1 380 ? -11.262 5.865   24.250  1.00 7.43  ? 403  LYS   A CA  1 
ATOM   2760 C  C   . LYS   A 1 380 ? -11.133 4.359   24.032  1.00 7.32  ? 403  LYS   A C   1 
ATOM   2761 O  O   . LYS   A 1 380 ? -11.424 3.906   22.943  1.00 7.27  ? 403  LYS   A O   1 
ATOM   2762 C  CB  . LYS   A 1 380 ? -12.737 6.186   24.511  1.00 7.57  ? 403  LYS   A CB  1 
ATOM   2763 C  CG  . LYS   A 1 380 ? -13.280 5.711   25.845  1.00 8.05  ? 403  LYS   A CG  1 
ATOM   2764 C  CD  . LYS   A 1 380 ? -14.809 5.664   25.936  1.00 7.74  ? 403  LYS   A CD  1 
ATOM   2765 C  CE  . LYS   A 1 380 ? -15.223 5.152   27.283  1.00 7.67  ? 403  LYS   A CE  1 
ATOM   2766 N  NZ  . LYS   A 1 380 ? -16.622 4.760   27.379  1.00 7.50  ? 403  LYS   A NZ  1 
ATOM   2767 N  N   . VAL   A 1 381 ? -10.690 3.592   25.031  1.00 7.53  ? 404  VAL   A N   1 
ATOM   2768 C  CA  . VAL   A 1 381 ? -10.729 2.138   24.936  1.00 7.44  ? 404  VAL   A CA  1 
ATOM   2769 C  C   . VAL   A 1 381 ? -11.839 1.653   25.863  1.00 7.83  ? 404  VAL   A C   1 
ATOM   2770 O  O   . VAL   A 1 381 ? -11.798 1.896   27.067  1.00 8.63  ? 404  VAL   A O   1 
ATOM   2771 C  CB  . VAL   A 1 381 ? -9.379  1.469   25.238  1.00 7.76  ? 404  VAL   A CB  1 
ATOM   2772 C  CG1 . VAL   A 1 381 ? -9.413  -0.049  24.959  1.00 7.80  ? 404  VAL   A CG1 1 
ATOM   2773 C  CG2 . VAL   A 1 381 ? -8.237  2.118   24.476  1.00 8.72  ? 404  VAL   A CG2 1 
ATOM   2774 N  N   . GLU   A 1 382 ? -12.828 0.964   25.302  1.00 7.45  ? 405  GLU   A N   1 
ATOM   2775 C  CA  . GLU   A 1 382 ? -13.948 0.478   26.084  1.00 7.86  ? 405  GLU   A CA  1 
ATOM   2776 C  C   . GLU   A 1 382 ? -13.538 -0.787  26.829  1.00 8.76  ? 405  GLU   A C   1 
ATOM   2777 O  O   . GLU   A 1 382 ? -12.512 -1.377  26.529  1.00 8.57  ? 405  GLU   A O   1 
ATOM   2778 C  CB  . GLU   A 1 382 ? -15.099 0.109   25.157  1.00 8.26  ? 405  GLU   A CB  1 
ATOM   2779 C  CG  . GLU   A 1 382 ? -15.736 1.270   24.395  1.00 8.21  ? 405  GLU   A CG  1 
ATOM   2780 C  CD  . GLU   A 1 382 ? -16.557 2.207   25.259  1.00 9.20  ? 405  GLU   A CD  1 
ATOM   2781 O  OE1 . GLU   A 1 382 ? -16.505 2.086   26.508  1.00 9.96  ? 405  GLU   A OE1 1 
ATOM   2782 O  OE2 . GLU   A 1 382 ? -17.289 3.055   24.699  1.00 8.98  ? 405  GLU   A OE2 1 
ATOM   2783 N  N   . PRO   A 1 383 ? -14.371 -1.245  27.791  1.00 7.69  ? 406  PRO   A N   1 
ATOM   2784 C  CA  . PRO   A 1 383 ? -14.161 -2.526  28.437  1.00 7.80  ? 406  PRO   A CA  1 
ATOM   2785 C  C   . PRO   A 1 383 ? -14.223 -3.703  27.470  1.00 7.23  ? 406  PRO   A C   1 
ATOM   2786 O  O   . PRO   A 1 383 ? -14.775 -3.630  26.365  1.00 8.17  ? 406  PRO   A O   1 
ATOM   2787 C  CB  . PRO   A 1 383 ? -15.314 -2.597  29.429  1.00 7.53  ? 406  PRO   A CB  1 
ATOM   2788 C  CG  . PRO   A 1 383 ? -16.362 -1.665  28.862  1.00 7.53  ? 406  PRO   A CG  1 
ATOM   2789 C  CD  . PRO   A 1 383 ? -15.545 -0.521  28.329  1.00 7.55  ? 406  PRO   A CD  1 
ATOM   2790 N  N   . GLN   A 1 384 ? -13.694 -4.837  27.949  1.00 6.70  ? 407  GLN   A N   1 
ATOM   2791 C  CA  . GLN   A 1 384 ? -13.622 -6.037  27.133  1.00 7.57  ? 407  GLN   A CA  1 
ATOM   2792 C  C   . GLN   A 1 384 ? -15.001 -6.442  26.613  1.00 7.13  ? 407  GLN   A C   1 
ATOM   2793 O  O   . GLN   A 1 384 ? -15.100 -6.920  25.472  1.00 7.29  ? 407  GLN   A O   1 
ATOM   2794 C  CB  . GLN   A 1 384 ? -12.971 -7.199  27.868  1.00 8.55  ? 407  GLN   A CB  1 
ATOM   2795 C  CG  . GLN   A 1 384 ? -11.450 -7.117  27.961  1.00 9.60  ? 407  GLN   A CG  1 
ATOM   2796 C  CD  . GLN   A 1 384 ? -10.735 -7.306  26.639  1.00 11.01 ? 407  GLN   A CD  1 
ATOM   2797 O  OE1 . GLN   A 1 384 ? -11.349 -7.568  25.598  1.00 16.46 ? 407  GLN   A OE1 1 
ATOM   2798 N  NE2 . GLN   A 1 384 ? -9.490  -6.900  26.593  1.00 10.79 ? 407  GLN   A NE2 1 
ATOM   2799 N  N   . ARG   A 1 385 ? -16.068 -6.236  27.393  1.00 6.96  ? 408  ARG   A N   1 
ATOM   2800 C  CA  . ARG   A 1 385 ? -17.398 -6.625  26.934  1.00 7.07  ? 408  ARG   A CA  1 
ATOM   2801 C  C   . ARG   A 1 385 ? -17.820 -5.895  25.647  1.00 7.14  ? 408  ARG   A C   1 
ATOM   2802 O  O   . ARG   A 1 385 ? -18.571 -6.419  24.854  1.00 7.65  ? 408  ARG   A O   1 
ATOM   2803 C  CB  . ARG   A 1 385 ? -18.505 -6.510  27.983  1.00 7.05  ? 408  ARG   A CB  1 
ATOM   2804 C  CG  . ARG   A 1 385 ? -18.386 -7.589  29.062  1.00 7.39  ? 408  ARG   A CG  1 
ATOM   2805 C  CD  . ARG   A 1 385 ? -19.586 -7.598  29.940  1.00 7.78  ? 408  ARG   A CD  1 
ATOM   2806 N  NE  . ARG   A 1 385 ? -20.752 -8.085  29.197  1.00 7.79  ? 408  ARG   A NE  1 
ATOM   2807 C  CZ  . ARG   A 1 385 ? -21.068 -9.362  28.952  1.00 8.36  ? 408  ARG   A CZ  1 
ATOM   2808 N  NH1 . ARG   A 1 385 ? -20.320 -10.392 29.324  1.00 8.47  ? 408  ARG   A NH1 1 
ATOM   2809 N  NH2 . ARG   A 1 385 ? -22.154 -9.623  28.254  1.00 8.39  ? 408  ARG   A NH2 1 
ATOM   2810 N  N   . TRP   A 1 386 ? -17.340 -4.682  25.449  1.00 6.68  ? 409  TRP   A N   1 
ATOM   2811 C  CA  . TRP   A 1 386 ? -17.599 -3.947  24.225  1.00 6.89  ? 409  TRP   A CA  1 
ATOM   2812 C  C   . TRP   A 1 386 ? -17.017 -4.662  23.018  1.00 6.69  ? 409  TRP   A C   1 
ATOM   2813 O  O   . TRP   A 1 386 ? -17.694 -4.780  21.996  1.00 7.27  ? 409  TRP   A O   1 
ATOM   2814 C  CB  . TRP   A 1 386 ? -17.027 -2.540  24.360  1.00 7.13  ? 409  TRP   A CB  1 
ATOM   2815 C  CG  . TRP   A 1 386 ? -17.392 -1.663  23.186  1.00 7.06  ? 409  TRP   A CG  1 
ATOM   2816 C  CD1 . TRP   A 1 386 ? -18.524 -0.917  22.986  1.00 7.48  ? 409  TRP   A CD1 1 
ATOM   2817 C  CD2 . TRP   A 1 386 ? -16.562 -1.478  22.032  1.00 6.75  ? 409  TRP   A CD2 1 
ATOM   2818 N  NE1 . TRP   A 1 386 ? -18.459 -0.319  21.767  1.00 7.52  ? 409  TRP   A NE1 1 
ATOM   2819 C  CE2 . TRP   A 1 386 ? -17.274 -0.647  21.154  1.00 7.23  ? 409  TRP   A CE2 1 
ATOM   2820 C  CE3 . TRP   A 1 386 ? -15.308 -1.978  21.626  1.00 7.72  ? 409  TRP   A CE3 1 
ATOM   2821 C  CZ2 . TRP   A 1 386 ? -16.757 -0.252  19.916  1.00 7.18  ? 409  TRP   A CZ2 1 
ATOM   2822 C  CZ3 . TRP   A 1 386 ? -14.835 -1.653  20.374  1.00 7.62  ? 409  TRP   A CZ3 1 
ATOM   2823 C  CH2 . TRP   A 1 386 ? -15.548 -0.781  19.537  1.00 7.43  ? 409  TRP   A CH2 1 
ATOM   2824 N  N   . PHE   A 1 387 ? -15.755 -5.103  23.128  1.00 6.58  ? 410  PHE   A N   1 
ATOM   2825 C  CA  . PHE   A 1 387 ? -15.115 -5.844  22.039  1.00 6.63  ? 410  PHE   A CA  1 
ATOM   2826 C  C   . PHE   A 1 387 ? -15.884 -7.137  21.762  1.00 6.92  ? 410  PHE   A C   1 
ATOM   2827 O  O   . PHE   A 1 387 ? -16.061 -7.495  20.610  1.00 7.60  ? 410  PHE   A O   1 
ATOM   2828 C  CB  . PHE   A 1 387 ? -13.657 -6.195  22.339  1.00 6.34  ? 410  PHE   A CB  1 
ATOM   2829 C  CG  . PHE   A 1 387 ? -12.773 -4.960  22.297  1.00 6.53  ? 410  PHE   A CG  1 
ATOM   2830 C  CD1 . PHE   A 1 387 ? -12.668 -4.129  23.406  1.00 6.51  ? 410  PHE   A CD1 1 
ATOM   2831 C  CD2 . PHE   A 1 387 ? -12.176 -4.565  21.114  1.00 6.23  ? 410  PHE   A CD2 1 
ATOM   2832 C  CE1 . PHE   A 1 387 ? -11.929 -2.947  23.330  1.00 7.05  ? 410  PHE   A CE1 1 
ATOM   2833 C  CE2 . PHE   A 1 387 ? -11.386 -3.416  21.071  1.00 7.37  ? 410  PHE   A CE2 1 
ATOM   2834 C  CZ  . PHE   A 1 387 ? -11.296 -2.608  22.174  1.00 7.12  ? 410  PHE   A CZ  1 
ATOM   2835 N  N   . TYR   A 1 388 ? -16.321 -7.808  22.830  1.00 7.47  ? 411  TYR   A N   1 
ATOM   2836 C  CA  . TYR   A 1 388 ? -17.150 -8.990  22.699  1.00 7.14  ? 411  TYR   A CA  1 
ATOM   2837 C  C   . TYR   A 1 388 ? -18.416 -8.693  21.921  1.00 6.61  ? 411  TYR   A C   1 
ATOM   2838 O  O   . TYR   A 1 388 ? -18.784 -9.460  21.032  1.00 6.65  ? 411  TYR   A O   1 
ATOM   2839 C  CB  . TYR   A 1 388 ? -17.485 -9.443  24.108  1.00 7.55  ? 411  TYR   A CB  1 
ATOM   2840 C  CG  . TYR   A 1 388 ? -18.589 -10.471 24.258  1.00 8.17  ? 411  TYR   A CG  1 
ATOM   2841 C  CD1 . TYR   A 1 388 ? -18.333 -11.834 24.073  1.00 9.06  ? 411  TYR   A CD1 1 
ATOM   2842 C  CD2 . TYR   A 1 388 ? -19.849 -10.090 24.702  1.00 9.46  ? 411  TYR   A CD2 1 
ATOM   2843 C  CE1 . TYR   A 1 388 ? -19.340 -12.770 24.252  1.00 9.58  ? 411  TYR   A CE1 1 
ATOM   2844 C  CE2 . TYR   A 1 388 ? -20.840 -11.033 24.944  1.00 10.43 ? 411  TYR   A CE2 1 
ATOM   2845 C  CZ  . TYR   A 1 388 ? -20.581 -12.367 24.721  1.00 11.03 ? 411  TYR   A CZ  1 
ATOM   2846 O  OH  . TYR   A 1 388 ? -21.616 -13.249 24.955  1.00 12.04 ? 411  TYR   A OH  1 
ATOM   2847 N  N   . TRP   A 1 389 ? -19.044 -7.547  22.188  1.00 6.40  ? 412  TRP   A N   1 
ATOM   2848 C  CA  . TRP   A 1 389 ? -20.248 -7.229  21.438  1.00 6.98  ? 412  TRP   A CA  1 
ATOM   2849 C  C   . TRP   A 1 389 ? -19.979 -6.961  19.963  1.00 6.94  ? 412  TRP   A C   1 
ATOM   2850 O  O   . TRP   A 1 389 ? -20.773 -7.387  19.105  1.00 8.04  ? 412  TRP   A O   1 
ATOM   2851 C  CB  . TRP   A 1 389 ? -21.060 -6.101  22.100  1.00 7.43  ? 412  TRP   A CB  1 
ATOM   2852 C  CG  . TRP   A 1 389 ? -21.771 -6.589  23.333  1.00 7.61  ? 412  TRP   A CG  1 
ATOM   2853 C  CD1 . TRP   A 1 389 ? -21.652 -6.106  24.605  1.00 8.19  ? 412  TRP   A CD1 1 
ATOM   2854 C  CD2 . TRP   A 1 389 ? -22.667 -7.715  23.415  1.00 8.29  ? 412  TRP   A CD2 1 
ATOM   2855 N  NE1 . TRP   A 1 389 ? -22.420 -6.835  25.467  1.00 8.55  ? 412  TRP   A NE1 1 
ATOM   2856 C  CE2 . TRP   A 1 389 ? -23.042 -7.840  24.768  1.00 8.10  ? 412  TRP   A CE2 1 
ATOM   2857 C  CE3 . TRP   A 1 389 ? -23.168 -8.626  22.476  1.00 8.75  ? 412  TRP   A CE3 1 
ATOM   2858 C  CZ2 . TRP   A 1 389 ? -23.900 -8.844  25.203  1.00 8.50  ? 412  TRP   A CZ2 1 
ATOM   2859 C  CZ3 . TRP   A 1 389 ? -23.984 -9.642  22.914  1.00 9.13  ? 412  TRP   A CZ3 1 
ATOM   2860 C  CH2 . TRP   A 1 389 ? -24.336 -9.751  24.266  1.00 9.14  ? 412  TRP   A CH2 1 
ATOM   2861 N  N   . ALA   A 1 390 ? -18.904 -6.240  19.641  1.00 6.57  ? 413  ALA   A N   1 
ATOM   2862 C  CA  . ALA   A 1 390 ? -18.563 -6.043  18.221  1.00 7.02  ? 413  ALA   A CA  1 
ATOM   2863 C  C   . ALA   A 1 390 ? -18.229 -7.371  17.518  1.00 7.20  ? 413  ALA   A C   1 
ATOM   2864 O  O   . ALA   A 1 390 ? -18.615 -7.618  16.366  1.00 7.19  ? 413  ALA   A O   1 
ATOM   2865 C  CB  . ALA   A 1 390 ? -17.404 -5.105  18.060  1.00 7.33  ? 413  ALA   A CB  1 
ATOM   2866 N  N   . ASP   A 1 391 ? -17.538 -8.249  18.262  1.00 7.31  ? 414  ASP   A N   1 
ATOM   2867 C  CA  . ASP   A 1 391 ? -17.204 -9.589  17.811  1.00 7.63  ? 414  ASP   A CA  1 
ATOM   2868 C  C   . ASP   A 1 391 ? -18.464 -10.366 17.455  1.00 7.93  ? 414  ASP   A C   1 
ATOM   2869 O  O   . ASP   A 1 391 ? -18.507 -11.014 16.405  1.00 8.63  ? 414  ASP   A O   1 
ATOM   2870 C  CB  . ASP   A 1 391 ? -16.417 -10.369 18.863  1.00 7.83  ? 414  ASP   A CB  1 
ATOM   2871 C  CG  . ASP   A 1 391 ? -15.012 -9.881  19.219  1.00 7.66  ? 414  ASP   A CG  1 
ATOM   2872 O  OD1 . ASP   A 1 391 ? -14.452 -9.032  18.457  1.00 8.56  ? 414  ASP   A OD1 1 
ATOM   2873 O  OD2 . ASP   A 1 391 ? -14.513 -10.336 20.302  1.00 7.79  ? 414  ASP   A OD2 1 
ATOM   2874 N  N   . ARG   A 1 392 ? -19.469 -10.314 18.342  1.00 8.66  ? 415  ARG   A N   1 
ATOM   2875 C  CA  . ARG   A 1 392 ? -20.702 -11.053 18.131  1.00 9.37  ? 415  ARG   A CA  1 
ATOM   2876 C  C   . ARG   A 1 392 ? -21.616 -10.403 17.086  1.00 9.94  ? 415  ARG   A C   1 
ATOM   2877 O  O   . ARG   A 1 392 ? -22.296 -11.108 16.334  1.00 9.24  ? 415  ARG   A O   1 
ATOM   2878 C  CB  . ARG   A 1 392 ? -21.476 -11.258 19.435  1.00 9.90  ? 415  ARG   A CB  1 
ATOM   2879 C  CG  . ARG   A 1 392 ? -20.754 -12.158 20.425  1.00 9.72  ? 415  ARG   A CG  1 
ATOM   2880 C  CD  . ARG   A 1 392 ? -21.670 -12.491 21.576  1.00 9.97  ? 415  ARG   A CD  1 
ATOM   2881 N  NE  . ARG   A 1 392 ? -22.807 -13.256 21.067  1.00 10.66 ? 415  ARG   A NE  1 
ATOM   2882 C  CZ  . ARG   A 1 392 ? -23.914 -13.579 21.726  1.00 11.25 ? 415  ARG   A CZ  1 
ATOM   2883 N  NH1 . ARG   A 1 392 ? -24.036 -13.259 22.984  1.00 11.34 ? 415  ARG   A NH1 1 
ATOM   2884 N  NH2 . ARG   A 1 392 ? -24.903 -14.185 21.103  1.00 11.26 ? 415  ARG   A NH2 1 
ATOM   2885 N  N   . LEU   A 1 393 ? -21.703 -9.070  17.077  1.00 9.26  ? 416  LEU   A N   1 
ATOM   2886 C  CA  . LEU   A 1 393 ? -22.658 -8.382  16.220  1.00 10.22 ? 416  LEU   A CA  1 
ATOM   2887 C  C   . LEU   A 1 393 ? -22.150 -8.275  14.786  1.00 10.68 ? 416  LEU   A C   1 
ATOM   2888 O  O   . LEU   A 1 393 ? -22.956 -8.071  13.869  1.00 10.99 ? 416  LEU   A O   1 
ATOM   2889 C  CB  . LEU   A 1 393 ? -22.986 -7.012  16.790  1.00 11.06 ? 416  LEU   A CB  1 
ATOM   2890 C  CG  . LEU   A 1 393 ? -23.801 -7.018  18.085  1.00 12.63 ? 416  LEU   A CG  1 
ATOM   2891 C  CD1 . LEU   A 1 393 ? -23.721 -5.676  18.794  1.00 13.06 ? 416  LEU   A CD1 1 
ATOM   2892 C  CD2 . LEU   A 1 393 ? -25.250 -7.408  17.837  1.00 13.43 ? 416  LEU   A CD2 1 
ATOM   2893 N  N   . GLY   A 1 394 ? -20.833 -8.367  14.593  1.00 9.93  ? 417  GLY   A N   1 
ATOM   2894 C  CA  . GLY   A 1 394 ? -20.272 -8.224  13.265  1.00 10.22 ? 417  GLY   A CA  1 
ATOM   2895 C  C   . GLY   A 1 394 ? -20.103 -6.765  12.878  1.00 10.25 ? 417  GLY   A C   1 
ATOM   2896 O  O   . GLY   A 1 394 ? -20.706 -6.273  11.913  1.00 11.31 ? 417  GLY   A O   1 
ATOM   2897 N  N   . LEU   A 1 395 ? -19.182 -6.127  13.569  1.00 9.38  ? 418  LEU   A N   1 
ATOM   2898 C  CA  . LEU   A 1 395 ? -18.722 -4.807  13.166  1.00 9.94  ? 418  LEU   A CA  1 
ATOM   2899 C  C   . LEU   A 1 395 ? -17.208 -4.866  13.107  1.00 9.55  ? 418  LEU   A C   1 
ATOM   2900 O  O   . LEU   A 1 395 ? -16.611 -5.295  14.068  1.00 9.90  ? 418  LEU   A O   1 
ATOM   2901 C  CB  . LEU   A 1 395 ? -19.154 -3.729  14.162  1.00 10.62 ? 418  LEU   A CB  1 
ATOM   2902 C  CG  . LEU   A 1 395 ? -20.635 -3.359  14.175  1.00 10.58 ? 418  LEU   A CG  1 
ATOM   2903 C  CD1 . LEU   A 1 395 ? -20.868 -2.498  15.401  1.00 11.16 ? 418  LEU   A CD1 1 
ATOM   2904 C  CD2 . LEU   A 1 395 ? -21.094 -2.640  12.918  1.00 9.99  ? 418  LEU   A CD2 1 
ATOM   2905 N  N   . LEU   A 1 396 ? -16.607 -4.318  12.053  1.00 9.43  ? 419  LEU   A N   1 
ATOM   2906 C  CA  . LEU   A 1 396 ? -15.178 -4.034  12.045  1.00 9.34  ? 419  LEU   A CA  1 
ATOM   2907 C  C   . LEU   A 1 396 ? -14.892 -2.898  13.006  1.00 8.83  ? 419  LEU   A C   1 
ATOM   2908 O  O   . LEU   A 1 396 ? -15.672 -1.932  13.042  1.00 9.39  ? 419  LEU   A O   1 
ATOM   2909 C  CB  . LEU   A 1 396 ? -14.787 -3.679  10.620  1.00 10.69 ? 419  LEU   A CB  1 
ATOM   2910 C  CG  . LEU   A 1 396 ? -15.066 -4.788  9.597   1.00 11.16 ? 419  LEU   A CG  1 
ATOM   2911 C  CD1 . LEU   A 1 396 ? -15.070 -4.264  8.189   1.00 11.89 ? 419  LEU   A CD1 1 
ATOM   2912 C  CD2 . LEU   A 1 396 ? -14.034 -5.919  9.719   1.00 11.96 ? 419  LEU   A CD2 1 
ATOM   2913 N  N   . VAL   A 1 397 ? -13.797 -3.024  13.763  1.00 7.94  ? 420  VAL   A N   1 
ATOM   2914 C  CA  . VAL   A 1 397 ? -13.445 -2.050  14.772  1.00 7.96  ? 420  VAL   A CA  1 
ATOM   2915 C  C   . VAL   A 1 397 ? -12.117 -1.406  14.393  1.00 7.20  ? 420  VAL   A C   1 
ATOM   2916 O  O   . VAL   A 1 397 ? -11.132 -2.105  14.150  1.00 7.02  ? 420  VAL   A O   1 
ATOM   2917 C  CB  . VAL   A 1 397 ? -13.427 -2.650  16.186  1.00 7.71  ? 420  VAL   A CB  1 
ATOM   2918 C  CG1 . VAL   A 1 397 ? -12.819 -1.675  17.188  1.00 7.85  ? 420  VAL   A CG1 1 
ATOM   2919 C  CG2 . VAL   A 1 397 ? -14.849 -3.030  16.588  1.00 8.27  ? 420  VAL   A CG2 1 
ATOM   2920 N  N   . TRP   A 1 398 ? -12.119 -0.074  14.400  1.00 7.32  ? 421  TRP   A N   1 
ATOM   2921 C  CA  . TRP   A 1 398 ? -10.910 0.717   14.439  1.00 7.70  ? 421  TRP   A CA  1 
ATOM   2922 C  C   . TRP   A 1 398 ? -10.779 1.269   15.857  1.00 7.79  ? 421  TRP   A C   1 
ATOM   2923 O  O   . TRP   A 1 398 ? -11.728 1.848   16.408  1.00 7.92  ? 421  TRP   A O   1 
ATOM   2924 C  CB  . TRP   A 1 398 ? -10.979 1.891   13.456  1.00 7.90  ? 421  TRP   A CB  1 
ATOM   2925 C  CG  . TRP   A 1 398 ? -11.099 1.535   12.006  1.00 8.64  ? 421  TRP   A CG  1 
ATOM   2926 C  CD1 . TRP   A 1 398 ? -11.413 0.358   11.405  1.00 8.60  ? 421  TRP   A CD1 1 
ATOM   2927 C  CD2 . TRP   A 1 398 ? -10.938 2.500   10.953  1.00 8.98  ? 421  TRP   A CD2 1 
ATOM   2928 N  NE1 . TRP   A 1 398 ? -11.418 0.523   10.037  1.00 9.43  ? 421  TRP   A NE1 1 
ATOM   2929 C  CE2 . TRP   A 1 398 ? -11.132 1.824   9.735   1.00 9.28  ? 421  TRP   A CE2 1 
ATOM   2930 C  CE3 . TRP   A 1 398 ? -10.627 3.862   10.948  1.00 9.52  ? 421  TRP   A CE3 1 
ATOM   2931 C  CZ2 . TRP   A 1 398 ? -11.051 2.479   8.504   1.00 10.30 ? 421  TRP   A CZ2 1 
ATOM   2932 C  CZ3 . TRP   A 1 398 ? -10.564 4.501   9.728   1.00 8.99  ? 421  TRP   A CZ3 1 
ATOM   2933 C  CH2 . TRP   A 1 398 ? -10.775 3.825   8.540   1.00 9.10  ? 421  TRP   A CH2 1 
ATOM   2934 N  N   . GLN   A 1 399 ? -9.603  1.043   16.437  1.00 7.61  ? 422  GLN   A N   1 
ATOM   2935 C  CA  . GLN   A 1 399 ? -9.332  1.451   17.811  1.00 7.03  ? 422  GLN   A CA  1 
ATOM   2936 C  C   . GLN   A 1 399 ? -8.323  2.586   17.861  1.00 7.07  ? 422  GLN   A C   1 
ATOM   2937 O  O   . GLN   A 1 399 ? -7.152  2.386   17.539  1.00 7.22  ? 422  GLN   A O   1 
ATOM   2938 C  CB  . GLN   A 1 399 ? -8.805  0.292   18.661  1.00 7.21  ? 422  GLN   A CB  1 
ATOM   2939 C  CG  . GLN   A 1 399 ? -8.573  0.686   20.124  1.00 7.93  ? 422  GLN   A CG  1 
ATOM   2940 C  CD  . GLN   A 1 399 ? -9.840  1.130   20.831  1.00 8.19  ? 422  GLN   A CD  1 
ATOM   2941 O  OE1 . GLN   A 1 399 ? -10.792 0.357   20.946  1.00 9.20  ? 422  GLN   A OE1 1 
ATOM   2942 N  NE2 . GLN   A 1 399 ? -9.904  2.395   21.235  1.00 8.23  ? 422  GLN   A NE2 1 
ATOM   2943 N  N   . ASP   A 1 400 ? -8.772  3.791   18.249  1.00 7.05  ? 423  ASP   A N   1 
ATOM   2944 C  CA  . ASP   A 1 400 ? -7.819  4.850   18.566  1.00 7.26  ? 423  ASP   A CA  1 
ATOM   2945 C  C   . ASP   A 1 400 ? -7.091  4.620   19.898  1.00 7.39  ? 423  ASP   A C   1 
ATOM   2946 O  O   . ASP   A 1 400 ? -7.700  4.236   20.898  1.00 8.51  ? 423  ASP   A O   1 
ATOM   2947 C  CB  . ASP   A 1 400 ? -8.529  6.173   18.777  1.00 8.02  ? 423  ASP   A CB  1 
ATOM   2948 C  CG  . ASP   A 1 400 ? -9.228  6.808   17.579  1.00 8.39  ? 423  ASP   A CG  1 
ATOM   2949 O  OD1 . ASP   A 1 400 ? -9.218  6.239   16.495  1.00 8.19  ? 423  ASP   A OD1 1 
ATOM   2950 O  OD2 . ASP   A 1 400 ? -9.794  7.905   17.787  1.00 8.87  ? 423  ASP   A OD2 1 
ATOM   2951 N  N   . MET   A 1 401 ? -5.790  4.909   19.920  1.00 7.47  ? 424  MET   A N   1 
ATOM   2952 C  CA  . MET   A 1 401 ? -5.076  5.074   21.173  1.00 7.33  ? 424  MET   A CA  1 
ATOM   2953 C  C   . MET   A 1 401 ? -5.441  6.465   21.694  1.00 7.31  ? 424  MET   A C   1 
ATOM   2954 O  O   . MET   A 1 401 ? -5.279  7.431   20.978  1.00 7.55  ? 424  MET   A O   1 
ATOM   2955 C  CB  . MET   A 1 401 ? -3.559  4.969   21.028  1.00 7.62  ? 424  MET   A CB  1 
ATOM   2956 C  CG  . MET   A 1 401 ? -2.788  5.330   22.281  1.00 7.83  ? 424  MET   A CG  1 
ATOM   2957 S  SD  . MET   A 1 401 ? -3.153  4.136   23.577  1.00 8.57  ? 424  MET   A SD  1 
ATOM   2958 C  CE  . MET   A 1 401 ? -2.532  5.080   24.973  1.00 8.21  ? 424  MET   A CE  1 
ATOM   2959 N  N   . PRO   A 1 402 ? -5.981  6.601   22.917  1.00 7.13  ? 425  PRO   A N   1 
ATOM   2960 C  CA  . PRO   A 1 402 ? -6.314  7.929   23.457  1.00 7.37  ? 425  PRO   A CA  1 
ATOM   2961 C  C   . PRO   A 1 402 ? -5.096  8.835   23.487  1.00 7.43  ? 425  PRO   A C   1 
ATOM   2962 O  O   . PRO   A 1 402 ? -4.017  8.424   23.876  1.00 7.05  ? 425  PRO   A O   1 
ATOM   2963 C  CB  . PRO   A 1 402 ? -6.889  7.668   24.821  1.00 7.27  ? 425  PRO   A CB  1 
ATOM   2964 C  CG  . PRO   A 1 402 ? -7.447  6.253   24.700  1.00 7.44  ? 425  PRO   A CG  1 
ATOM   2965 C  CD  . PRO   A 1 402 ? -6.465  5.509   23.785  1.00 7.38  ? 425  PRO   A CD  1 
ATOM   2966 N  N   . ASN   A 1 403 ? -5.298  10.079  23.056  1.00 7.52  ? 426  ASN   A N   1 
ATOM   2967 C  CA  . ASN   A 1 403 ? -4.209  11.031  22.949  1.00 8.24  ? 426  ASN   A CA  1 
ATOM   2968 C  C   . ASN   A 1 403 ? -3.894  11.676  24.292  1.00 8.94  ? 426  ASN   A C   1 
ATOM   2969 O  O   . ASN   A 1 403 ? -4.760  11.817  25.177  1.00 8.41  ? 426  ASN   A O   1 
ATOM   2970 C  CB  . ASN   A 1 403 ? -4.601  12.140  21.980  1.00 8.41  ? 426  ASN   A CB  1 
ATOM   2971 C  CG  . ASN   A 1 403 ? -5.822  12.897  22.470  1.00 8.45  ? 426  ASN   A CG  1 
ATOM   2972 O  OD1 . ASN   A 1 403 ? -6.926  12.385  22.444  1.00 8.53  ? 426  ASN   A OD1 1 
ATOM   2973 N  ND2 . ASN   A 1 403 ? -5.666  14.111  22.962  1.00 8.51  ? 426  ASN   A ND2 1 
ATOM   2974 N  N   . MET   A 1 404 ? -2.664  12.211  24.339  1.00 9.42  ? 427  MET   A N   1 
ATOM   2975 C  CA  . MET   A 1 404 ? -2.263  13.190  25.337  1.00 9.90  ? 427  MET   A CA  1 
ATOM   2976 C  C   . MET   A 1 404 ? -2.673  14.595  24.889  1.00 10.26 ? 427  MET   A C   1 
ATOM   2977 O  O   . MET   A 1 404 ? -2.893  14.851  23.714  1.00 9.18  ? 427  MET   A O   1 
ATOM   2978 C  CB  . MET   A 1 404 ? -0.757  13.131  25.517  1.00 10.34 ? 427  MET   A CB  1 
ATOM   2979 C  CG  . MET   A 1 404 ? -0.316  11.782  26.021  1.00 10.22 ? 427  MET   A CG  1 
ATOM   2980 S  SD  . MET   A 1 404 ? 1.470   11.542  25.990  1.00 11.46 ? 427  MET   A SD  1 
ATOM   2981 C  CE  . MET   A 1 404 ? 1.620   11.205  24.234  1.00 11.29 ? 427  MET   A CE  1 
ATOM   2982 N  N   . GLU   A 1 405 ? -2.730  15.507  25.858  1.00 10.66 ? 428  GLU   A N   1 
ATOM   2983 C  CA  . GLU   A 1 405 ? -3.260  16.830  25.615  1.00 12.52 ? 428  GLU   A CA  1 
ATOM   2984 C  C   . GLU   A 1 405 ? -2.223  17.743  24.992  1.00 12.45 ? 428  GLU   A C   1 
ATOM   2985 O  O   . GLU   A 1 405 ? -2.611  18.727  24.372  1.00 13.91 ? 428  GLU   A O   1 
ATOM   2986 C  CB  . GLU   A 1 405 ? -3.665  17.409  26.960  1.00 15.84 ? 428  GLU   A CB  1 
ATOM   2987 C  CG  . GLU   A 1 405 ? -4.366  18.751  26.860  1.00 21.56 ? 428  GLU   A CG  1 
ATOM   2988 C  CD  . GLU   A 1 405 ? -3.568  19.997  27.143  1.00 23.43 ? 428  GLU   A CD  1 
ATOM   2989 O  OE1 . GLU   A 1 405 ? -4.275  20.981  26.913  1.00 32.56 ? 428  GLU   A OE1 1 
ATOM   2990 O  OE2 . GLU   A 1 405 ? -2.369  20.042  27.530  1.00 22.98 ? 428  GLU   A OE2 1 
ATOM   2991 N  N   . ARG   A 1 406 ? -0.935  17.425  25.145  1.00 11.58 ? 429  ARG   A N   1 
ATOM   2992 C  CA  . ARG   A 1 406 ? 0.133   18.229  24.570  1.00 11.79 ? 429  ARG   A CA  1 
ATOM   2993 C  C   . ARG   A 1 406 ? 1.357   17.343  24.298  1.00 12.64 ? 429  ARG   A C   1 
ATOM   2994 O  O   . ARG   A 1 406 ? 1.422   16.215  24.772  1.00 12.37 ? 429  ARG   A O   1 
ATOM   2995 C  CB  . ARG   A 1 406 ? 0.511   19.324  25.566  1.00 12.60 ? 429  ARG   A CB  1 
ATOM   2996 C  CG  . ARG   A 1 406 ? 0.946   18.853  26.944  1.00 12.37 ? 429  ARG   A CG  1 
ATOM   2997 C  CD  . ARG   A 1 406 ? 0.955   19.995  27.931  1.00 13.36 ? 429  ARG   A CD  1 
ATOM   2998 N  NE  . ARG   A 1 406 ? 1.253   19.569  29.294  1.00 13.97 ? 429  ARG   A NE  1 
ATOM   2999 C  CZ  . ARG   A 1 406 ? 0.354   18.982  30.108  1.00 14.28 ? 429  ARG   A CZ  1 
ATOM   3000 N  NH1 . ARG   A 1 406 ? -0.903  18.787  29.733  1.00 15.43 ? 429  ARG   A NH1 1 
ATOM   3001 N  NH2 . ARG   A 1 406 ? 0.724   18.614  31.297  1.00 15.48 ? 429  ARG   A NH2 1 
ATOM   3002 N  N   . THR   A 1 407 ? 2.346   17.913  23.606  1.00 13.84 ? 430  THR   A N   1 
ATOM   3003 C  CA  . THR   A 1 407 ? 3.578   17.226  23.252  1.00 14.76 ? 430  THR   A CA  1 
ATOM   3004 C  C   . THR   A 1 407 ? 4.180   16.575  24.483  1.00 14.57 ? 430  THR   A C   1 
ATOM   3005 O  O   . THR   A 1 407 ? 4.501   17.234  25.462  1.00 16.22 ? 430  THR   A O   1 
ATOM   3006 C  CB  . THR   A 1 407 ? 4.596   18.210  22.668  1.00 18.01 ? 430  THR   A CB  1 
ATOM   3007 O  OG1 . THR   A 1 407 ? 4.021   18.987  21.627  1.00 17.65 ? 430  THR   A OG1 1 
ATOM   3008 C  CG2 . THR   A 1 407 ? 5.790   17.471  22.095  1.00 18.47 ? 430  THR   A CG2 1 
ATOM   3009 N  N   . PRO   A 1 408 ? 4.423   15.253  24.461  1.00 13.84 ? 431  PRO   A N   1 
ATOM   3010 C  CA  . PRO   A 1 408 ? 5.051   14.584  25.597  1.00 13.99 ? 431  PRO   A CA  1 
ATOM   3011 C  C   . PRO   A 1 408 ? 6.554   14.801  25.800  1.00 13.89 ? 431  PRO   A C   1 
ATOM   3012 O  O   . PRO   A 1 408 ? 7.286   14.818  24.809  1.00 13.94 ? 431  PRO   A O   1 
ATOM   3013 C  CB  . PRO   A 1 408 ? 4.757   13.119  25.270  1.00 14.25 ? 431  PRO   A CB  1 
ATOM   3014 C  CG  . PRO   A 1 408 ? 4.708   13.050  23.767  1.00 13.69 ? 431  PRO   A CG  1 
ATOM   3015 C  CD  . PRO   A 1 408 ? 4.050   14.345  23.356  1.00 13.69 ? 431  PRO   A CD  1 
ATOM   3016 N  N   . ASP   A 1 409 ? 6.957   14.882  27.072  1.00 13.46 ? 432  ASP   A N   1 
ATOM   3017 C  CA  . ASP   A 1 409 ? 8.364   14.801  27.451  1.00 15.11 ? 432  ASP   A CA  1 
ATOM   3018 C  C   . ASP   A 1 409 ? 8.736   13.318  27.536  1.00 14.60 ? 432  ASP   A C   1 
ATOM   3019 O  O   . ASP   A 1 409 ? 7.929   12.451  27.263  1.00 12.31 ? 432  ASP   A O   1 
ATOM   3020 C  CB  . ASP   A 1 409 ? 8.644   15.634  28.688  1.00 16.38 ? 432  ASP   A CB  1 
ATOM   3021 C  CG  . ASP   A 1 409 ? 8.038   15.145  29.997  1.00 17.04 ? 432  ASP   A CG  1 
ATOM   3022 O  OD1 . ASP   A 1 409 ? 7.327   14.090  29.990  1.00 16.95 ? 432  ASP   A OD1 1 
ATOM   3023 O  OD2 . ASP   A 1 409 ? 8.312   15.796  31.040  1.00 18.28 ? 432  ASP   A OD2 1 
ATOM   3024 N  N   . ALA   A 1 410 ? 9.992   13.026  27.881  1.00 15.04 ? 433  ALA   A N   1 
ATOM   3025 C  CA  . ALA   A 1 410 ? 10.526  11.669  27.801  1.00 13.66 ? 433  ALA   A CA  1 
ATOM   3026 C  C   . ALA   A 1 410 ? 9.744   10.679  28.687  1.00 12.66 ? 433  ALA   A C   1 
ATOM   3027 O  O   . ALA   A 1 410 ? 9.349   9.602   28.221  1.00 12.76 ? 433  ALA   A O   1 
ATOM   3028 C  CB  . ALA   A 1 410 ? 11.983  11.721  28.200  1.00 13.49 ? 433  ALA   A CB  1 
ATOM   3029 N  N   . ALA   A 1 411 ? 9.450   11.056  29.935  1.00 12.03 ? 434  ALA   A N   1 
ATOM   3030 C  CA  . ALA   A 1 411 ? 8.673   10.196  30.831  1.00 12.69 ? 434  ALA   A CA  1 
ATOM   3031 C  C   . ALA   A 1 411 ? 7.244   9.986   30.309  1.00 13.65 ? 434  ALA   A C   1 
ATOM   3032 O  O   . ALA   A 1 411 ? 6.672   8.894   30.450  1.00 13.61 ? 434  ALA   A O   1 
ATOM   3033 C  CB  . ALA   A 1 411 ? 8.692   10.756  32.230  1.00 13.98 ? 434  ALA   A CB  1 
ATOM   3034 N  N   . ALA   A 1 412 ? 6.660   11.037  29.721  1.00 12.73 ? 435  ALA   A N   1 
ATOM   3035 C  CA  . ALA   A 1 412 ? 5.295   10.967  29.210  1.00 13.16 ? 435  ALA   A CA  1 
ATOM   3036 C  C   . ALA   A 1 412 ? 5.257   10.024  28.009  1.00 12.06 ? 435  ALA   A C   1 
ATOM   3037 O  O   . ALA   A 1 412 ? 4.296   9.295   27.818  1.00 11.27 ? 435  ALA   A O   1 
ATOM   3038 C  CB  . ALA   A 1 412 ? 4.791   12.327  28.830  1.00 12.96 ? 435  ALA   A CB  1 
ATOM   3039 N  N   . ARG   A 1 413 ? 6.307   10.038  27.199  1.00 12.27 ? 436  ARG   A N   1 
ATOM   3040 C  CA  . ARG   A 1 413 ? 6.365   9.155   26.048  1.00 12.23 ? 436  ARG   A CA  1 
ATOM   3041 C  C   . ARG   A 1 413 ? 6.490   7.712   26.536  1.00 12.32 ? 436  ARG   A C   1 
ATOM   3042 O  O   . ARG   A 1 413 ? 5.828   6.840   25.986  1.00 11.92 ? 436  ARG   A O   1 
ATOM   3043 C  CB  . ARG   A 1 413 ? 7.521   9.494   25.121  1.00 12.52 ? 436  ARG   A CB  1 
ATOM   3044 C  CG  . ARG   A 1 413 ? 7.351   10.804  24.365  1.00 13.71 ? 436  ARG   A CG  1 
ATOM   3045 C  CD  . ARG   A 1 413 ? 8.687   11.323  23.884  1.00 13.82 ? 436  ARG   A CD  1 
ATOM   3046 N  NE  . ARG   A 1 413 ? 8.523   12.686  23.383  1.00 14.49 ? 436  ARG   A NE  1 
ATOM   3047 C  CZ  . ARG   A 1 413 ? 9.077   13.214  22.310  1.00 15.00 ? 436  ARG   A CZ  1 
ATOM   3048 N  NH1 . ARG   A 1 413 ? 9.761   12.497  21.428  1.00 15.07 ? 436  ARG   A NH1 1 
ATOM   3049 N  NH2 . ARG   A 1 413 ? 8.874   14.496  22.103  1.00 15.53 ? 436  ARG   A NH2 1 
ATOM   3050 N  N   . THR   A 1 414 ? 7.401   7.450   27.489  1.00 12.31 ? 437  THR   A N   1 
ATOM   3051 C  CA  . THR   A 1 414 ? 7.587   6.094   28.003  1.00 12.56 ? 437  THR   A CA  1 
ATOM   3052 C  C   . THR   A 1 414 ? 6.246   5.568   28.519  1.00 12.14 ? 437  THR   A C   1 
ATOM   3053 O  O   . THR   A 1 414 ? 5.840   4.427   28.265  1.00 11.32 ? 437  THR   A O   1 
ATOM   3054 C  CB  . THR   A 1 414 ? 8.631   6.083   29.134  1.00 14.81 ? 437  THR   A CB  1 
ATOM   3055 O  OG1 . THR   A 1 414 ? 9.835   6.554   28.540  1.00 15.83 ? 437  THR   A OG1 1 
ATOM   3056 C  CG2 . THR   A 1 414 ? 8.841   4.713   29.737  1.00 15.99 ? 437  THR   A CG2 1 
ATOM   3057 N  N   . GLN   A 1 415 ? 5.565   6.399   29.315  1.00 10.97 ? 438  GLN   A N   1 
ATOM   3058 C  CA  . GLN   A 1 415 ? 4.301   5.997   29.909  1.00 10.54 ? 438  GLN   A CA  1 
ATOM   3059 C  C   . GLN   A 1 415 ? 3.210   5.770   28.869  1.00 9.86  ? 438  GLN   A C   1 
ATOM   3060 O  O   . GLN   A 1 415 ? 2.444   4.815   28.995  1.00 9.70  ? 438  GLN   A O   1 
ATOM   3061 C  CB  . GLN   A 1 415 ? 3.859   7.083   30.885  1.00 11.51 ? 438  GLN   A CB  1 
ATOM   3062 C  CG  . GLN   A 1 415 ? 2.459   6.918   31.465  1.00 11.54 ? 438  GLN   A CG  1 
ATOM   3063 C  CD  . GLN   A 1 415 ? 2.277   5.668   32.298  1.00 12.18 ? 438  GLN   A CD  1 
ATOM   3064 O  OE1 . GLN   A 1 415 ? 3.192   5.189   32.971  1.00 12.59 ? 438  GLN   A OE1 1 
ATOM   3065 N  NE2 . GLN   A 1 415 ? 1.080   5.118   32.283  1.00 11.99 ? 438  GLN   A NE2 1 
ATOM   3066 N  N   . TRP   A 1 416 ? 3.073   6.679   27.892  1.00 10.50 ? 439  TRP   A N   1 
ATOM   3067 C  CA  . TRP   A 1 416 ? 2.045   6.534   26.881  1.00 9.76  ? 439  TRP   A CA  1 
ATOM   3068 C  C   . TRP   A 1 416 ? 2.264   5.267   26.047  1.00 10.82 ? 439  TRP   A C   1 
ATOM   3069 O  O   . TRP   A 1 416 ? 1.313   4.517   25.783  1.00 9.59  ? 439  TRP   A O   1 
ATOM   3070 C  CB  . TRP   A 1 416 ? 1.998   7.787   26.021  1.00 9.60  ? 439  TRP   A CB  1 
ATOM   3071 C  CG  . TRP   A 1 416 ? 0.916   7.836   24.980  1.00 9.46  ? 439  TRP   A CG  1 
ATOM   3072 C  CD1 . TRP   A 1 416 ? -0.384  8.191   25.178  1.00 8.85  ? 439  TRP   A CD1 1 
ATOM   3073 C  CD2 . TRP   A 1 416 ? 1.052   7.538   23.579  1.00 8.92  ? 439  TRP   A CD2 1 
ATOM   3074 N  NE1 . TRP   A 1 416 ? -1.061  8.151   23.996  1.00 9.91  ? 439  TRP   A NE1 1 
ATOM   3075 C  CE2 . TRP   A 1 416 ? -0.217  7.777   22.994  1.00 9.15  ? 439  TRP   A CE2 1 
ATOM   3076 C  CE3 . TRP   A 1 416 ? 2.107   7.097   22.770  1.00 8.59  ? 439  TRP   A CE3 1 
ATOM   3077 C  CZ2 . TRP   A 1 416 ? -0.466  7.578   21.637  1.00 8.85  ? 439  TRP   A CZ2 1 
ATOM   3078 C  CZ3 . TRP   A 1 416 ? 1.857   6.910   21.427  1.00 9.20  ? 439  TRP   A CZ3 1 
ATOM   3079 C  CH2 . TRP   A 1 416 ? 0.580   7.136   20.869  1.00 9.53  ? 439  TRP   A CH2 1 
ATOM   3080 N  N   . GLU   A 1 417 ? 3.532   5.020   25.663  1.00 10.39 ? 440  GLU   A N   1 
ATOM   3081 C  CA  . GLU   A 1 417 ? 3.889   3.829   24.899  1.00 10.34 ? 440  GLU   A CA  1 
ATOM   3082 C  C   . GLU   A 1 417 ? 3.634   2.532   25.675  1.00 10.43 ? 440  GLU   A C   1 
ATOM   3083 O  O   . GLU   A 1 417 ? 3.165   1.556   25.071  1.00 10.02 ? 440  GLU   A O   1 
ATOM   3084 C  CB  . GLU   A 1 417 ? 5.335   3.926   24.432  1.00 10.33 ? 440  GLU   A CB  1 
ATOM   3085 C  CG  . GLU   A 1 417 ? 5.474   4.919   23.278  1.00 11.62 ? 440  GLU   A CG  1 
ATOM   3086 C  CD  . GLU   A 1 417 ? 6.796   4.985   22.577  1.00 11.52 ? 440  GLU   A CD  1 
ATOM   3087 O  OE1 . GLU   A 1 417 ? 7.416   3.918   22.335  1.00 13.30 ? 440  GLU   A OE1 1 
ATOM   3088 O  OE2 . GLU   A 1 417 ? 7.222   6.108   22.276  1.00 11.95 ? 440  GLU   A OE2 1 
ATOM   3089 N  N   . ALA   A 1 418 ? 3.940   2.543   26.984  1.00 9.98  ? 441  ALA   A N   1 
ATOM   3090 C  CA  . ALA   A 1 418 ? 3.658   1.436   27.878  1.00 10.11 ? 441  ALA   A CA  1 
ATOM   3091 C  C   . ALA   A 1 418 ? 2.156   1.149   27.914  1.00 9.18  ? 441  ALA   A C   1 
ATOM   3092 O  O   . ALA   A 1 418 ? 1.758   -0.007  27.888  1.00 8.24  ? 441  ALA   A O   1 
ATOM   3093 C  CB  . ALA   A 1 418 ? 4.232   1.744   29.253  1.00 10.46 ? 441  ALA   A CB  1 
ATOM   3094 N  N   . GLU   A 1 419 ? 1.325   2.199   28.080  1.00 8.27  ? 442  GLU   A N   1 
ATOM   3095 C  CA  . GLU   A 1 419 ? -0.121  2.030   28.030  1.00 8.05  ? 442  GLU   A CA  1 
ATOM   3096 C  C   . GLU   A 1 419 ? -0.545  1.399   26.700  1.00 7.67  ? 442  GLU   A C   1 
ATOM   3097 O  O   . GLU   A 1 419 ? -1.359  0.467   26.671  1.00 7.99  ? 442  GLU   A O   1 
ATOM   3098 C  CB  . GLU   A 1 419 ? -0.864  3.351   28.279  1.00 7.79  ? 442  GLU   A CB  1 
ATOM   3099 C  CG  . GLU   A 1 419 ? -0.699  3.933   29.678  1.00 7.95  ? 442  GLU   A CG  1 
ATOM   3100 C  CD  . GLU   A 1 419 ? -1.521  5.169   29.964  1.00 8.89  ? 442  GLU   A CD  1 
ATOM   3101 O  OE1 . GLU   A 1 419 ? -2.682  5.193   29.450  1.00 9.82  ? 442  GLU   A OE1 1 
ATOM   3102 O  OE2 . GLU   A 1 419 ? -1.017  6.053   30.710  1.00 8.68  ? 442  GLU   A OE2 1 
ATOM   3103 N  N   . TYR   A 1 420 ? -0.069  1.961   25.597  1.00 7.85  ? 443  TYR   A N   1 
ATOM   3104 C  CA  . TYR   A 1 420 ? -0.462  1.477   24.293  1.00 8.33  ? 443  TYR   A CA  1 
ATOM   3105 C  C   . TYR   A 1 420 ? -0.079  0.001   24.117  1.00 8.71  ? 443  TYR   A C   1 
ATOM   3106 O  O   . TYR   A 1 420 ? -0.903  -0.780  23.625  1.00 8.69  ? 443  TYR   A O   1 
ATOM   3107 C  CB  . TYR   A 1 420 ? 0.135   2.352   23.200  1.00 8.39  ? 443  TYR   A CB  1 
ATOM   3108 C  CG  . TYR   A 1 420 ? -0.521  2.315   21.830  1.00 8.41  ? 443  TYR   A CG  1 
ATOM   3109 C  CD1 . TYR   A 1 420 ? -1.591  1.462   21.502  1.00 7.89  ? 443  TYR   A CD1 1 
ATOM   3110 C  CD2 . TYR   A 1 420 ? -0.030  3.156   20.841  1.00 7.86  ? 443  TYR   A CD2 1 
ATOM   3111 C  CE1 . TYR   A 1 420 ? -2.171  1.470   20.253  1.00 7.55  ? 443  TYR   A CE1 1 
ATOM   3112 C  CE2 . TYR   A 1 420 ? -0.597  3.159   19.583  1.00 7.66  ? 443  TYR   A CE2 1 
ATOM   3113 C  CZ  . TYR   A 1 420 ? -1.653  2.309   19.284  1.00 7.69  ? 443  TYR   A CZ  1 
ATOM   3114 O  OH  . TYR   A 1 420 ? -2.177  2.315   18.016  1.00 8.52  ? 443  TYR   A OH  1 
ATOM   3115 N  N   . ASP   A 1 421 ? 1.140   -0.379  24.521  1.00 8.57  ? 444  ASP   A N   1 
ATOM   3116 C  CA  . ASP   A 1 421 ? 1.591   -1.763  24.426  1.00 10.35 ? 444  ASP   A CA  1 
ATOM   3117 C  C   . ASP   A 1 421 ? 0.587   -2.663  25.141  1.00 9.42  ? 444  ASP   A C   1 
ATOM   3118 O  O   . ASP   A 1 421 ? 0.204   -3.738  24.648  1.00 8.55  ? 444  ASP   A O   1 
ATOM   3119 C  CB  . ASP   A 1 421 ? 2.976   -1.956  25.032  1.00 11.82 ? 444  ASP   A CB  1 
ATOM   3120 C  CG  . ASP   A 1 421 ? 4.147   -1.388  24.242  1.00 15.42 ? 444  ASP   A CG  1 
ATOM   3121 O  OD1 . ASP   A 1 421 ? 3.956   -1.042  23.055  1.00 17.43 ? 444  ASP   A OD1 1 
ATOM   3122 O  OD2 . ASP   A 1 421 ? 5.230   -1.308  24.859  1.00 19.02 ? 444  ASP   A OD2 1 
ATOM   3123 N  N   . ARG   A 1 422 ? 0.178   -2.231  26.342  1.00 9.60  ? 445  ARG   A N   1 
ATOM   3124 C  CA  . ARG   A 1 422 ? -0.724  -3.042  27.159  1.00 10.15 ? 445  ARG   A CA  1 
ATOM   3125 C  C   . ARG   A 1 422 ? -2.097  -3.162  26.478  1.00 9.58  ? 445  ARG   A C   1 
ATOM   3126 O  O   . ARG   A 1 422 ? -2.714  -4.220  26.463  1.00 9.46  ? 445  ARG   A O   1 
ATOM   3127 C  CB  . ARG   A 1 422 ? -0.865  -2.584  28.618  1.00 11.95 ? 445  ARG   A CB  1 
ATOM   3128 C  CG  . ARG   A 1 422 ? 0.408   -2.702  29.447  1.00 13.91 ? 445  ARG   A CG  1 
ATOM   3129 C  CD  . ARG   A 1 422 ? 0.208   -2.271  30.900  1.00 16.42 ? 445  ARG   A CD  1 
ATOM   3130 N  NE  . ARG   A 1 422 ? -0.853  -2.927  31.681  1.00 21.62 ? 445  ARG   A NE  1 
ATOM   3131 C  CZ  . ARG   A 1 422 ? -0.798  -4.090  32.310  1.00 24.08 ? 445  ARG   A CZ  1 
ATOM   3132 N  NH1 . ARG   A 1 422 ? 0.286   -4.844  32.186  1.00 25.80 ? 445  ARG   A NH1 1 
ATOM   3133 N  NH2 . ARG   A 1 422 ? -1.803  -4.508  33.057  1.00 23.64 ? 445  ARG   A NH2 1 
ATOM   3134 N  N   . ILE   A 1 423 ? -2.574  -2.057  25.887  1.00 8.84  ? 446  ILE   A N   1 
ATOM   3135 C  CA  . ILE   A 1 423 ? -3.849  -2.059  25.185  1.00 7.92  ? 446  ILE   A CA  1 
ATOM   3136 C  C   . ILE   A 1 423 ? -3.771  -2.987  23.981  1.00 7.73  ? 446  ILE   A C   1 
ATOM   3137 O  O   . ILE   A 1 423 ? -4.700  -3.748  23.749  1.00 7.47  ? 446  ILE   A O   1 
ATOM   3138 C  CB  . ILE   A 1 423 ? -4.169  -0.605  24.802  1.00 7.43  ? 446  ILE   A CB  1 
ATOM   3139 C  CG1 . ILE   A 1 423 ? -4.529  0.173   26.036  1.00 7.26  ? 446  ILE   A CG1 1 
ATOM   3140 C  CG2 . ILE   A 1 423 ? -5.251  -0.512  23.750  1.00 7.33  ? 446  ILE   A CG2 1 
ATOM   3141 C  CD1 . ILE   A 1 423 ? -4.393  1.668   25.882  1.00 7.23  ? 446  ILE   A CD1 1 
ATOM   3142 N  N   . ILE   A 1 424 ? -2.657  -2.976  23.258  1.00 7.13  ? 447  ILE   A N   1 
ATOM   3143 C  CA  . ILE   A 1 424 ? -2.506  -3.886  22.122  1.00 7.78  ? 447  ILE   A CA  1 
ATOM   3144 C  C   . ILE   A 1 424 ? -2.528  -5.328  22.621  1.00 7.63  ? 447  ILE   A C   1 
ATOM   3145 O  O   . ILE   A 1 424 ? -3.196  -6.188  22.033  1.00 8.05  ? 447  ILE   A O   1 
ATOM   3146 C  CB  . ILE   A 1 424 ? -1.260  -3.546  21.298  1.00 8.44  ? 447  ILE   A CB  1 
ATOM   3147 C  CG1 . ILE   A 1 424 ? -1.392  -2.143  20.663  1.00 8.99  ? 447  ILE   A CG1 1 
ATOM   3148 C  CG2 . ILE   A 1 424 ? -0.963  -4.625  20.259  1.00 8.49  ? 447  ILE   A CG2 1 
ATOM   3149 C  CD1 . ILE   A 1 424 ? -0.076  -1.554  20.197  1.00 9.15  ? 447  ILE   A CD1 1 
ATOM   3150 N  N   . ASP   A 1 425 ? -1.748  -5.605  23.673  1.00 8.57  ? 448  ASP   A N   1 
ATOM   3151 C  CA  . ASP   A 1 425 ? -1.603  -6.972  24.173  1.00 9.39  ? 448  ASP   A CA  1 
ATOM   3152 C  C   . ASP   A 1 425 ? -2.920  -7.523  24.716  1.00 9.45  ? 448  ASP   A C   1 
ATOM   3153 O  O   . ASP   A 1 425 ? -3.142  -8.741  24.680  1.00 11.20 ? 448  ASP   A O   1 
ATOM   3154 C  CB  . ASP   A 1 425 ? -0.487  -7.092  25.186  1.00 9.86  ? 448  ASP   A CB  1 
ATOM   3155 C  CG  . ASP   A 1 425 ? 0.909   -7.034  24.600  1.00 10.93 ? 448  ASP   A CG  1 
ATOM   3156 O  OD1 . ASP   A 1 425 ? 1.092   -7.574  23.500  1.00 10.87 ? 448  ASP   A OD1 1 
ATOM   3157 O  OD2 . ASP   A 1 425 ? 1.798   -6.472  25.270  1.00 11.30 ? 448  ASP   A OD2 1 
ATOM   3158 N  N   . GLN   A 1 426 ? -3.800  -6.627  25.179  1.00 8.02  ? 449  GLN   A N   1 
ATOM   3159 C  CA  . GLN   A 1 426 ? -5.068  -7.050  25.744  1.00 8.48  ? 449  GLN   A CA  1 
ATOM   3160 C  C   . GLN   A 1 426 ? -6.162  -7.351  24.710  1.00 8.35  ? 449  GLN   A C   1 
ATOM   3161 O  O   . GLN   A 1 426 ? -7.230  -7.828  25.107  1.00 9.16  ? 449  GLN   A O   1 
ATOM   3162 C  CB  . GLN   A 1 426 ? -5.553  -6.022  26.765  1.00 8.79  ? 449  GLN   A CB  1 
ATOM   3163 C  CG  . GLN   A 1 426 ? -4.685  -6.046  28.014  1.00 9.10  ? 449  GLN   A CG  1 
ATOM   3164 C  CD  . GLN   A 1 426 ? -5.012  -4.994  29.054  1.00 9.71  ? 449  GLN   A CD  1 
ATOM   3165 O  OE1 . GLN   A 1 426 ? -6.047  -4.323  29.021  1.00 10.30 ? 449  GLN   A OE1 1 
ATOM   3166 N  NE2 . GLN   A 1 426 ? -4.166  -4.961  30.074  1.00 10.42 ? 449  GLN   A NE2 1 
ATOM   3167 N  N   . HIS   A 1 427 ? -5.926  -7.094  23.413  1.00 8.17  ? 450  HIS   A N   1 
ATOM   3168 C  CA  . HIS   A 1 427 ? -6.952  -7.225  22.387  1.00 8.45  ? 450  HIS   A CA  1 
ATOM   3169 C  C   . HIS   A 1 427 ? -6.518  -8.077  21.196  1.00 8.05  ? 450  HIS   A C   1 
ATOM   3170 O  O   . HIS   A 1 427 ? -7.142  -8.032  20.139  1.00 8.38  ? 450  HIS   A O   1 
ATOM   3171 C  CB  . HIS   A 1 427 ? -7.397  -5.842  21.904  1.00 8.42  ? 450  HIS   A CB  1 
ATOM   3172 C  CG  . HIS   A 1 427 ? -8.028  -5.102  23.032  1.00 8.70  ? 450  HIS   A CG  1 
ATOM   3173 N  ND1 . HIS   A 1 427 ? -7.318  -4.254  23.866  1.00 9.58  ? 450  HIS   A ND1 1 
ATOM   3174 C  CD2 . HIS   A 1 427 ? -9.272  -5.157  23.514  1.00 9.20  ? 450  HIS   A CD2 1 
ATOM   3175 C  CE1 . HIS   A 1 427 ? -8.133  -3.804  24.808  1.00 10.08 ? 450  HIS   A CE1 1 
ATOM   3176 N  NE2 . HIS   A 1 427 ? -9.343  -4.333  24.630  1.00 8.94  ? 450  HIS   A NE2 1 
ATOM   3177 N  N   . ARG   A 1 428 ? -5.474  -8.886  21.340  1.00 8.44  ? 451  ARG   A N   1 
ATOM   3178 C  CA  . ARG   A 1 428 ? -4.936  -9.601  20.177  1.00 8.04  ? 451  ARG   A CA  1 
ATOM   3179 C  C   . ARG   A 1 428 ? -5.950  -10.562 19.553  1.00 7.94  ? 451  ARG   A C   1 
ATOM   3180 O  O   . ARG   A 1 428 ? -5.874  -10.792 18.344  1.00 8.04  ? 451  ARG   A O   1 
ATOM   3181 C  CB  . ARG   A 1 428 ? -3.654  -10.386 20.462  1.00 8.18  ? 451  ARG   A CB  1 
ATOM   3182 C  CG  . ARG   A 1 428 ? -2.518  -9.420  20.747  1.00 8.18  ? 451  ARG   A CG  1 
ATOM   3183 C  CD  . ARG   A 1 428 ? -1.254  -10.120 21.189  1.00 8.57  ? 451  ARG   A CD  1 
ATOM   3184 N  NE  . ARG   A 1 428 ? -0.156  -9.162  21.337  1.00 7.95  ? 451  ARG   A NE  1 
ATOM   3185 C  CZ  . ARG   A 1 428 ? 0.502   -8.594  20.342  1.00 8.34  ? 451  ARG   A CZ  1 
ATOM   3186 N  NH1 . ARG   A 1 428 ? 0.298   -8.933  19.086  1.00 8.93  ? 451  ARG   A NH1 1 
ATOM   3187 N  NH2 . ARG   A 1 428 ? 1.407   -7.684  20.600  1.00 8.82  ? 451  ARG   A NH2 1 
ATOM   3188 N  N   . SER   A 1 429 ? -6.860  -11.140 20.342  1.00 7.42  ? 452  SER   A N   1 
ATOM   3189 C  CA  . SER   A 1 429 ? -7.753  -12.189 19.842  1.00 7.50  ? 452  SER   A CA  1 
ATOM   3190 C  C   . SER   A 1 429 ? -9.101  -11.700 19.272  1.00 7.68  ? 452  SER   A C   1 
ATOM   3191 O  O   . SER   A 1 429 ? -9.930  -12.510 18.846  1.00 8.03  ? 452  SER   A O   1 
ATOM   3192 C  CB  . SER   A 1 429 ? -7.979  -13.228 20.926  1.00 7.31  ? 452  SER   A CB  1 
ATOM   3193 O  OG  . SER   A 1 429 ? -6.735  -13.757 21.369  1.00 7.42  ? 452  SER   A OG  1 
ATOM   3194 N  N   . SER   A 1 430 ? -9.398  -10.412 19.378  1.00 7.76  ? 453  SER   A N   1 
ATOM   3195 C  CA  . SER   A 1 430 ? -10.704 -9.887  18.958  1.00 7.87  ? 453  SER   A CA  1 
ATOM   3196 C  C   . SER   A 1 430 ? -10.860 -9.967  17.442  1.00 7.22  ? 453  SER   A C   1 
ATOM   3197 O  O   . SER   A 1 430 ? -10.089 -9.363  16.717  1.00 6.52  ? 453  SER   A O   1 
ATOM   3198 C  CB  . SER   A 1 430 ? -10.888 -8.453  19.404  1.00 8.09  ? 453  SER   A CB  1 
ATOM   3199 O  OG  . SER   A 1 430 ? -11.973 -7.822  18.734  1.00 7.91  ? 453  SER   A OG  1 
ATOM   3200 N  N   . PRO   A 1 431 ? -11.852 -10.685 16.876  1.00 7.00  ? 454  PRO   A N   1 
ATOM   3201 C  CA  . PRO   A 1 431 ? -12.013 -10.654 15.426  1.00 7.04  ? 454  PRO   A CA  1 
ATOM   3202 C  C   . PRO   A 1 431 ? -12.468 -9.285  14.931  1.00 6.94  ? 454  PRO   A C   1 
ATOM   3203 O  O   . PRO   A 1 431 ? -12.148 -8.885  13.799  1.00 7.31  ? 454  PRO   A O   1 
ATOM   3204 C  CB  . PRO   A 1 431 ? -13.064 -11.727 15.177  1.00 7.01  ? 454  PRO   A CB  1 
ATOM   3205 C  CG  . PRO   A 1 431 ? -13.798 -11.896 16.494  1.00 7.03  ? 454  PRO   A CG  1 
ATOM   3206 C  CD  . PRO   A 1 431 ? -12.699 -11.713 17.518  1.00 7.17  ? 454  PRO   A CD  1 
ATOM   3207 N  N   . SER   A 1 432 ? -13.295 -8.603  15.716  1.00 7.32  ? 455  SER   A N   1 
ATOM   3208 C  CA  . SER   A 1 432 ? -13.828 -7.321  15.257  1.00 7.47  ? 455  SER   A CA  1 
ATOM   3209 C  C   . SER   A 1 432 ? -12.673 -6.340  15.024  1.00 7.44  ? 455  SER   A C   1 
ATOM   3210 O  O   . SER   A 1 432 ? -12.680 -5.556  14.070  1.00 7.58  ? 455  SER   A O   1 
ATOM   3211 C  CB  . SER   A 1 432 ? -14.886 -6.715  16.203  1.00 7.45  ? 455  SER   A CB  1 
ATOM   3212 O  OG  . SER   A 1 432 ? -14.404 -6.499  17.528  1.00 7.44  ? 455  SER   A OG  1 
ATOM   3213 N  N   . LEU   A 1 433 ? -11.721 -6.289  15.948  1.00 7.40  ? 456  LEU   A N   1 
ATOM   3214 C  CA  . LEU   A 1 433 ? -10.638 -5.306  15.867  1.00 7.66  ? 456  LEU   A CA  1 
ATOM   3215 C  C   . LEU   A 1 433 ? -9.770  -5.612  14.642  1.00 7.96  ? 456  LEU   A C   1 
ATOM   3216 O  O   . LEU   A 1 433 ? -9.161  -6.686  14.558  1.00 8.14  ? 456  LEU   A O   1 
ATOM   3217 C  CB  . LEU   A 1 433 ? -9.844  -5.290  17.172  1.00 7.96  ? 456  LEU   A CB  1 
ATOM   3218 C  CG  . LEU   A 1 433 ? -8.568  -4.440  17.207  1.00 8.49  ? 456  LEU   A CG  1 
ATOM   3219 C  CD1 . LEU   A 1 433 ? -8.887  -3.010  16.963  1.00 8.83  ? 456  LEU   A CD1 1 
ATOM   3220 C  CD2 . LEU   A 1 433 ? -7.867  -4.644  18.533  1.00 8.85  ? 456  LEU   A CD2 1 
ATOM   3221 N  N   . VAL   A 1 434 ? -9.673  -4.654  13.718  1.00 8.41  ? 457  VAL   A N   1 
ATOM   3222 C  CA  . VAL   A 1 434 ? -8.886  -4.831  12.497  1.00 8.37  ? 457  VAL   A CA  1 
ATOM   3223 C  C   . VAL   A 1 434 ? -7.893  -3.685  12.226  1.00 8.11  ? 457  VAL   A C   1 
ATOM   3224 O  O   . VAL   A 1 434 ? -7.052  -3.819  11.322  1.00 8.76  ? 457  VAL   A O   1 
ATOM   3225 C  CB  . VAL   A 1 434 ? -9.816  -5.006  11.284  1.00 8.88  ? 457  VAL   A CB  1 
ATOM   3226 C  CG1 . VAL   A 1 434 ? -10.579 -6.320  11.362  1.00 9.07  ? 457  VAL   A CG1 1 
ATOM   3227 C  CG2 . VAL   A 1 434 ? -10.731 -3.798  11.098  1.00 9.47  ? 457  VAL   A CG2 1 
ATOM   3228 N  N   . LEU   A 1 435 ? -7.983  -2.577  12.981  1.00 7.78  ? 458  LEU   A N   1 
ATOM   3229 C  CA  . LEU   A 1 435 ? -7.168  -1.400  12.686  1.00 7.87  ? 458  LEU   A CA  1 
ATOM   3230 C  C   . LEU   A 1 435 ? -6.884  -0.602  13.947  1.00 7.89  ? 458  LEU   A C   1 
ATOM   3231 O  O   . LEU   A 1 435 ? -7.801  -0.370  14.739  1.00 7.88  ? 458  LEU   A O   1 
ATOM   3232 C  CB  . LEU   A 1 435 ? -7.867  -0.538  11.620  1.00 8.49  ? 458  LEU   A CB  1 
ATOM   3233 C  CG  . LEU   A 1 435 ? -7.100  0.676   11.098  1.00 8.57  ? 458  LEU   A CG  1 
ATOM   3234 C  CD1 . LEU   A 1 435 ? -7.508  0.975   9.633   1.00 8.73  ? 458  LEU   A CD1 1 
ATOM   3235 C  CD2 . LEU   A 1 435 ? -7.329  1.893   11.925  1.00 8.56  ? 458  LEU   A CD2 1 
ATOM   3236 N  N   . TRP   A 1 436 ? -5.603  -0.203  14.089  1.00 7.81  ? 459  TRP   A N   1 
ATOM   3237 C  CA  . TRP   A 1 436 ? -5.150  0.721   15.125  1.00 8.11  ? 459  TRP   A CA  1 
ATOM   3238 C  C   . TRP   A 1 436 ? -4.959  2.136   14.568  1.00 8.53  ? 459  TRP   A C   1 
ATOM   3239 O  O   . TRP   A 1 436 ? -4.330  2.284   13.511  1.00 7.92  ? 459  TRP   A O   1 
ATOM   3240 C  CB  . TRP   A 1 436 ? -3.819  0.246   15.741  1.00 8.17  ? 459  TRP   A CB  1 
ATOM   3241 C  CG  . TRP   A 1 436 ? -3.914  -1.067  16.437  1.00 8.46  ? 459  TRP   A CG  1 
ATOM   3242 C  CD1 . TRP   A 1 436 ? -3.468  -2.289  16.012  1.00 10.39 ? 459  TRP   A CD1 1 
ATOM   3243 C  CD2 . TRP   A 1 436 ? -4.452  -1.268  17.756  1.00 9.14  ? 459  TRP   A CD2 1 
ATOM   3244 N  NE1 . TRP   A 1 436 ? -3.734  -3.247  16.949  1.00 9.96  ? 459  TRP   A NE1 1 
ATOM   3245 C  CE2 . TRP   A 1 436 ? -4.344  -2.649  18.030  1.00 10.12 ? 459  TRP   A CE2 1 
ATOM   3246 C  CE3 . TRP   A 1 436 ? -5.030  -0.423  18.705  1.00 9.12  ? 459  TRP   A CE3 1 
ATOM   3247 C  CZ2 . TRP   A 1 436 ? -4.758  -3.177  19.245  1.00 9.90  ? 459  TRP   A CZ2 1 
ATOM   3248 C  CZ3 . TRP   A 1 436 ? -5.447  -0.952  19.902  1.00 9.92  ? 459  TRP   A CZ3 1 
ATOM   3249 C  CH2 . TRP   A 1 436 ? -5.317  -2.310  20.159  1.00 9.53  ? 459  TRP   A CH2 1 
ATOM   3250 N  N   . VAL   A 1 437 ? -5.515  3.143   15.268  1.00 8.37  ? 460  VAL   A N   1 
ATOM   3251 C  CA  . VAL   A 1 437 ? -5.306  4.546   14.959  1.00 8.49  ? 460  VAL   A CA  1 
ATOM   3252 C  C   . VAL   A 1 437 ? -4.376  5.126   16.015  1.00 8.60  ? 460  VAL   A C   1 
ATOM   3253 O  O   . VAL   A 1 437 ? -4.793  5.376   17.140  1.00 8.33  ? 460  VAL   A O   1 
ATOM   3254 C  CB  . VAL   A 1 437 ? -6.606  5.360   14.880  1.00 9.15  ? 460  VAL   A CB  1 
ATOM   3255 C  CG1 . VAL   A 1 437 ? -6.337  6.773   14.435  1.00 9.18  ? 460  VAL   A CG1 1 
ATOM   3256 C  CG2 . VAL   A 1 437 ? -7.606  4.731   13.943  1.00 9.28  ? 460  VAL   A CG2 1 
ATOM   3257 N  N   . ASN   A 1 438 ? -3.103  5.326   15.653  1.00 8.87  ? 461  ASN   A N   1 
ATOM   3258 C  CA  . ASN   A 1 438 ? -2.110  5.714   16.648  1.00 9.69  ? 461  ASN   A CA  1 
ATOM   3259 C  C   . ASN   A 1 438 ? -2.345  7.103   17.235  1.00 9.25  ? 461  ASN   A C   1 
ATOM   3260 O  O   . ASN   A 1 438 ? -2.174  7.294   18.439  1.00 10.52 ? 461  ASN   A O   1 
ATOM   3261 C  CB  . ASN   A 1 438 ? -0.707  5.727   16.068  1.00 9.43  ? 461  ASN   A CB  1 
ATOM   3262 C  CG  . ASN   A 1 438 ? -0.150  4.357   15.793  1.00 9.96  ? 461  ASN   A CG  1 
ATOM   3263 O  OD1 . ASN   A 1 438 ? -0.786  3.339   16.084  1.00 10.54 ? 461  ASN   A OD1 1 
ATOM   3264 N  ND2 . ASN   A 1 438 ? 1.058   4.343   15.252  1.00 10.30 ? 461  ASN   A ND2 1 
ATOM   3265 N  N   . GLN   A 1 439 ? -2.671  8.082   16.377  1.00 9.35  ? 462  GLN   A N   1 
ATOM   3266 C  CA  . GLN   A 1 439 ? -2.732  9.477   16.755  1.00 9.86  ? 462  GLN   A CA  1 
ATOM   3267 C  C   . GLN   A 1 439 ? -3.843  10.140  15.955  1.00 8.59  ? 462  GLN   A C   1 
ATOM   3268 O  O   . GLN   A 1 439 ? -4.193  9.670   14.883  1.00 8.71  ? 462  GLN   A O   1 
ATOM   3269 C  CB  . GLN   A 1 439 ? -1.368  10.138  16.536  1.00 10.37 ? 462  GLN   A CB  1 
ATOM   3270 C  CG  . GLN   A 1 439 ? -0.228  9.385   17.219  1.00 11.53 ? 462  GLN   A CG  1 
ATOM   3271 C  CD  . GLN   A 1 439 ? 1.107   10.092  17.193  1.00 12.57 ? 462  GLN   A CD  1 
ATOM   3272 O  OE1 . GLN   A 1 439 ? 1.290   11.111  17.860  1.00 14.54 ? 462  GLN   A OE1 1 
ATOM   3273 N  NE2 . GLN   A 1 439 ? 2.066   9.502   16.514  1.00 11.81 ? 462  GLN   A NE2 1 
ATOM   3274 N  N   . ASN   A 1 440 ? -4.329  11.261  16.464  1.00 9.29  ? 463  ASN   A N   1 
ATOM   3275 C  CA  . ASN   A 1 440 ? -5.503  11.926  15.928  1.00 9.21  ? 463  ASN   A CA  1 
ATOM   3276 C  C   . ASN   A 1 440 ? -5.240  13.424  15.797  1.00 9.66  ? 463  ASN   A C   1 
ATOM   3277 O  O   . ASN   A 1 440 ? -5.007  14.072  16.813  1.00 8.99  ? 463  ASN   A O   1 
ATOM   3278 C  CB  . ASN   A 1 440 ? -6.737  11.743  16.814  1.00 8.70  ? 463  ASN   A CB  1 
ATOM   3279 C  CG  . ASN   A 1 440 ? -7.972  12.363  16.174  1.00 8.79  ? 463  ASN   A CG  1 
ATOM   3280 O  OD1 . ASN   A 1 440 ? -8.416  11.918  15.113  1.00 9.42  ? 463  ASN   A OD1 1 
ATOM   3281 N  ND2 . ASN   A 1 440 ? -8.457  13.471  16.726  1.00 8.46  ? 463  ASN   A ND2 1 
ATOM   3282 N  N   . GLU   A 1 441 ? -5.327  13.924  14.553  1.00 9.22  ? 464  GLU   A N   1 
ATOM   3283 C  CA  . GLU   A 1 441 ? -5.246  15.344  14.219  1.00 10.52 ? 464  GLU   A CA  1 
ATOM   3284 C  C   . GLU   A 1 441 ? -4.068  16.023  14.907  1.00 10.71 ? 464  GLU   A C   1 
ATOM   3285 O  O   . GLU   A 1 441 ? -4.155  17.193  15.286  1.00 11.04 ? 464  GLU   A O   1 
ATOM   3286 C  CB  . GLU   A 1 441 ? -6.565  16.041  14.587  1.00 10.84 ? 464  GLU   A CB  1 
ATOM   3287 C  CG  . GLU   A 1 441 ? -7.749  15.615  13.730  1.00 10.55 ? 464  GLU   A CG  1 
ATOM   3288 C  CD  . GLU   A 1 441 ? -8.947  16.606  13.667  1.00 10.23 ? 464  GLU   A CD  1 
ATOM   3289 O  OE1 . GLU   A 1 441 ? -9.008  17.616  14.416  1.00 10.56 ? 464  GLU   A OE1 1 
ATOM   3290 O  OE2 . GLU   A 1 441 ? -9.823  16.348  12.798  1.00 10.12 ? 464  GLU   A OE2 1 
ATOM   3291 N  N   . GLY   A 1 442 ? -2.941  15.303  15.039  1.00 10.78 ? 465  GLY   A N   1 
ATOM   3292 C  CA  . GLY   A 1 442 ? -1.733  15.895  15.598  1.00 10.27 ? 465  GLY   A CA  1 
ATOM   3293 C  C   . GLY   A 1 442 ? -1.721  16.072  17.119  1.00 10.28 ? 465  GLY   A C   1 
ATOM   3294 O  O   . GLY   A 1 442 ? -0.778  16.651  17.643  1.00 10.13 ? 465  GLY   A O   1 
ATOM   3295 N  N   . TRP   A 1 443 ? -2.714  15.542  17.844  1.00 10.80 ? 466  TRP   A N   1 
ATOM   3296 C  CA  . TRP   A 1 443 ? -2.900  15.870  19.253  1.00 10.46 ? 466  TRP   A CA  1 
ATOM   3297 C  C   . TRP   A 1 443 ? -1.836  15.167  20.069  1.00 10.93 ? 466  TRP   A C   1 
ATOM   3298 O  O   . TRP   A 1 443 ? -1.780  13.938  20.098  1.00 11.70 ? 466  TRP   A O   1 
ATOM   3299 C  CB  . TRP   A 1 443 ? -4.300  15.496  19.769  1.00 10.61 ? 466  TRP   A CB  1 
ATOM   3300 C  CG  . TRP   A 1 443 ? -5.415  16.272  19.125  1.00 10.28 ? 466  TRP   A CG  1 
ATOM   3301 C  CD1 . TRP   A 1 443 ? -5.292  17.339  18.276  1.00 10.58 ? 466  TRP   A CD1 1 
ATOM   3302 C  CD2 . TRP   A 1 443 ? -6.828  16.013  19.245  1.00 10.46 ? 466  TRP   A CD2 1 
ATOM   3303 N  NE1 . TRP   A 1 443 ? -6.523  17.770  17.862  1.00 10.97 ? 466  TRP   A NE1 1 
ATOM   3304 C  CE2 . TRP   A 1 443 ? -7.490  16.967  18.432  1.00 10.31 ? 466  TRP   A CE2 1 
ATOM   3305 C  CE3 . TRP   A 1 443 ? -7.591  15.057  19.949  1.00 10.31 ? 466  TRP   A CE3 1 
ATOM   3306 C  CZ2 . TRP   A 1 443 ? -8.879  17.012  18.315  1.00 10.63 ? 466  TRP   A CZ2 1 
ATOM   3307 C  CZ3 . TRP   A 1 443 ? -8.967  15.123  19.855  1.00 10.42 ? 466  TRP   A CZ3 1 
ATOM   3308 C  CH2 . TRP   A 1 443 ? -9.597  16.070  19.021  1.00 10.51 ? 466  TRP   A CH2 1 
ATOM   3309 N  N   . GLY   A 1 444 ? -0.957  15.956  20.674  1.00 10.64 ? 467  GLY   A N   1 
ATOM   3310 C  CA  . GLY   A 1 444 ? 0.139   15.401  21.441  1.00 10.68 ? 467  GLY   A CA  1 
ATOM   3311 C  C   . GLY   A 1 444 ? 1.121   14.653  20.556  1.00 11.29 ? 467  GLY   A C   1 
ATOM   3312 O  O   . GLY   A 1 444 ? 1.821   13.769  21.037  1.00 13.12 ? 467  GLY   A O   1 
ATOM   3313 N  N   . GLN   A 1 445 ? 1.188   15.003  19.259  1.00 11.44 ? 468  GLN   A N   1 
ATOM   3314 C  CA  . GLN   A 1 445 ? 1.846   14.127  18.299  1.00 11.22 ? 468  GLN   A CA  1 
ATOM   3315 C  C   . GLN   A 1 445 ? 3.366   14.081  18.478  1.00 11.24 ? 468  GLN   A C   1 
ATOM   3316 O  O   . GLN   A 1 445 ? 3.986   15.088  18.810  1.00 10.91 ? 468  GLN   A O   1 
ATOM   3317 C  CB  . GLN   A 1 445 ? 1.503   14.504  16.868  1.00 11.54 ? 468  GLN   A CB  1 
ATOM   3318 C  CG  . GLN   A 1 445 ? 2.111   15.836  16.446  1.00 11.20 ? 468  GLN   A CG  1 
ATOM   3319 C  CD  . GLN   A 1 445 ? 1.592   16.307  15.115  1.00 11.53 ? 468  GLN   A CD  1 
ATOM   3320 O  OE1 . GLN   A 1 445 ? 1.404   15.509  14.200  1.00 14.15 ? 468  GLN   A OE1 1 
ATOM   3321 N  NE2 . GLN   A 1 445 ? 1.449   17.621  14.959  1.00 11.88 ? 468  GLN   A NE2 1 
ATOM   3322 N  N   . TYR   A 1 446 ? 3.947   12.909  18.170  1.00 10.35 ? 469  TYR   A N   1 
ATOM   3323 C  CA  . TYR   A 1 446 ? 5.392   12.760  18.043  1.00 10.28 ? 469  TYR   A CA  1 
ATOM   3324 C  C   . TYR   A 1 446 ? 5.668   11.447  17.317  1.00 10.28 ? 469  TYR   A C   1 
ATOM   3325 O  O   . TYR   A 1 446 ? 4.763   10.610  17.210  1.00 11.10 ? 469  TYR   A O   1 
ATOM   3326 C  CB  . TYR   A 1 446 ? 6.044   12.784  19.427  1.00 10.63 ? 469  TYR   A CB  1 
ATOM   3327 C  CG  . TYR   A 1 446 ? 5.872   11.498  20.249  1.00 10.76 ? 469  TYR   A CG  1 
ATOM   3328 C  CD1 . TYR   A 1 446 ? 4.655   11.195  20.824  1.00 10.64 ? 469  TYR   A CD1 1 
ATOM   3329 C  CD2 . TYR   A 1 446 ? 6.917   10.601  20.460  1.00 10.75 ? 469  TYR   A CD2 1 
ATOM   3330 C  CE1 . TYR   A 1 446 ? 4.463   10.046  21.575  1.00 10.23 ? 469  TYR   A CE1 1 
ATOM   3331 C  CE2 . TYR   A 1 446 ? 6.755   9.455   21.227  1.00 10.65 ? 469  TYR   A CE2 1 
ATOM   3332 C  CZ  . TYR   A 1 446 ? 5.508   9.164   21.772  1.00 10.80 ? 469  TYR   A CZ  1 
ATOM   3333 O  OH  . TYR   A 1 446 ? 5.269   8.086   22.557  1.00 10.39 ? 469  TYR   A OH  1 
ATOM   3334 N  N   . ASP   A 1 447 ? 6.913   11.272  16.842  1.00 10.68 ? 470  ASP   A N   1 
ATOM   3335 C  CA  . ASP   A 1 447 ? 7.380   10.003  16.297  1.00 11.24 ? 470  ASP   A CA  1 
ATOM   3336 C  C   . ASP   A 1 447 ? 6.333   9.286   15.423  1.00 11.22 ? 470  ASP   A C   1 
ATOM   3337 O  O   . ASP   A 1 447 ? 6.112   8.079   15.582  1.00 11.52 ? 470  ASP   A O   1 
ATOM   3338 C  CB  . ASP   A 1 447 ? 7.850   9.087   17.420  1.00 11.24 ? 470  ASP   A CB  1 
ATOM   3339 C  CG  . ASP   A 1 447 ? 9.175   9.446   18.100  1.00 12.10 ? 470  ASP   A CG  1 
ATOM   3340 O  OD1 . ASP   A 1 447 ? 9.743   10.516  17.808  1.00 13.18 ? 470  ASP   A OD1 1 
ATOM   3341 O  OD2 . ASP   A 1 447 ? 9.636   8.651   18.945  1.00 11.84 ? 470  ASP   A OD2 1 
ATOM   3342 N  N   . GLN   A 1 448 ? 5.761   9.989   14.437  1.00 10.90 ? 471  GLN   A N   1 
ATOM   3343 C  CA  . GLN   A 1 448 ? 4.623   9.484   13.682  1.00 12.12 ? 471  GLN   A CA  1 
ATOM   3344 C  C   . GLN   A 1 448 ? 4.991   8.215   12.920  1.00 12.78 ? 471  GLN   A C   1 
ATOM   3345 O  O   . GLN   A 1 448 ? 4.267   7.208   12.949  1.00 14.11 ? 471  GLN   A O   1 
ATOM   3346 C  CB  . GLN   A 1 448 ? 4.092   10.559  12.748  1.00 12.22 ? 471  GLN   A CB  1 
ATOM   3347 C  CG  . GLN   A 1 448 ? 3.501   11.774  13.464  1.00 13.49 ? 471  GLN   A CG  1 
ATOM   3348 C  CD  . GLN   A 1 448 ? 4.517   12.823  13.886  1.00 15.74 ? 471  GLN   A CD  1 
ATOM   3349 O  OE1 . GLN   A 1 448 ? 5.740   12.631  13.836  1.00 15.48 ? 471  GLN   A OE1 1 
ATOM   3350 N  NE2 . GLN   A 1 448 ? 4.028   13.952  14.381  1.00 17.10 ? 471  GLN   A NE2 1 
ATOM   3351 N  N   . ALA   A 1 449 ? 6.130   8.270   12.217  1.00 12.62 ? 472  ALA   A N   1 
ATOM   3352 C  CA  . ALA   A 1 449 ? 6.569   7.148   11.394  1.00 12.52 ? 472  ALA   A CA  1 
ATOM   3353 C  C   . ALA   A 1 449 ? 7.058   5.992   12.261  1.00 12.59 ? 472  ALA   A C   1 
ATOM   3354 O  O   . ALA   A 1 449 ? 6.708   4.826   12.023  1.00 12.58 ? 472  ALA   A O   1 
ATOM   3355 C  CB  . ALA   A 1 449 ? 7.648   7.591   10.403  1.00 12.03 ? 472  ALA   A CB  1 
ATOM   3356 N  N   . ARG   A 1 450 ? 7.875   6.302   13.273  1.00 11.41 ? 473  ARG   A N   1 
ATOM   3357 C  CA  . ARG   A 1 450 ? 8.398   5.268   14.152  1.00 12.25 ? 473  ARG   A CA  1 
ATOM   3358 C  C   . ARG   A 1 450 ? 7.232   4.511   14.817  1.00 11.53 ? 473  ARG   A C   1 
ATOM   3359 O  O   . ARG   A 1 450 ? 7.308   3.300   14.903  1.00 10.76 ? 473  ARG   A O   1 
ATOM   3360 C  CB  . ARG   A 1 450 ? 9.327   5.866   15.203  1.00 13.52 ? 473  ARG   A CB  1 
ATOM   3361 C  CG  . ARG   A 1 450 ? 9.604   4.993   16.406  1.00 15.06 ? 473  ARG   A CG  1 
ATOM   3362 C  CD  . ARG   A 1 450 ? 10.516  5.704   17.373  1.00 14.19 ? 473  ARG   A CD  1 
ATOM   3363 N  NE  . ARG   A 1 450 ? 10.447  4.923   18.591  1.00 14.36 ? 473  ARG   A NE  1 
ATOM   3364 C  CZ  . ARG   A 1 450 ? 9.504   5.008   19.544  1.00 15.20 ? 473  ARG   A CZ  1 
ATOM   3365 N  NH1 . ARG   A 1 450 ? 8.841   6.121   19.821  1.00 13.41 ? 473  ARG   A NH1 1 
ATOM   3366 N  NH2 . ARG   A 1 450 ? 9.373   3.959   20.328  1.00 15.76 ? 473  ARG   A NH2 1 
ATOM   3367 N  N   . LEU   A 1 451 ? 6.208   5.212   15.339  1.00 10.47 ? 474  LEU   A N   1 
ATOM   3368 C  CA  . LEU   A 1 451 ? 5.119   4.537   16.050  1.00 10.75 ? 474  LEU   A CA  1 
ATOM   3369 C  C   . LEU   A 1 451 ? 4.276   3.657   15.114  1.00 10.72 ? 474  LEU   A C   1 
ATOM   3370 O  O   . LEU   A 1 451 ? 3.769   2.581   15.498  1.00 11.78 ? 474  LEU   A O   1 
ATOM   3371 C  CB  . LEU   A 1 451 ? 4.289   5.563   16.828  1.00 10.48 ? 474  LEU   A CB  1 
ATOM   3372 C  CG  . LEU   A 1 451 ? 5.013   6.184   18.018  1.00 10.16 ? 474  LEU   A CG  1 
ATOM   3373 C  CD1 . LEU   A 1 451 ? 4.230   7.393   18.466  1.00 10.11 ? 474  LEU   A CD1 1 
ATOM   3374 C  CD2 . LEU   A 1 451 ? 5.144   5.205   19.153  1.00 10.91 ? 474  LEU   A CD2 1 
ATOM   3375 N  N   . ALA   A 1 452 ? 4.088   4.103   13.871  1.00 10.20 ? 475  ALA   A N   1 
ATOM   3376 C  CA  . ALA   A 1 452 ? 3.426   3.261   12.888  1.00 11.07 ? 475  ALA   A CA  1 
ATOM   3377 C  C   . ALA   A 1 452 ? 4.182   1.936   12.725  1.00 10.38 ? 475  ALA   A C   1 
ATOM   3378 O  O   . ALA   A 1 452 ? 3.578   0.879   12.724  1.00 9.86  ? 475  ALA   A O   1 
ATOM   3379 C  CB  . ALA   A 1 452 ? 3.304   3.993   11.592  1.00 11.28 ? 475  ALA   A CB  1 
ATOM   3380 N  N   . ASP   A 1 453 ? 5.499   1.987   12.538  1.00 11.31 ? 476  ASP   A N   1 
ATOM   3381 C  CA  . ASP   A 1 453 ? 6.274   0.765   12.356  1.00 11.59 ? 476  ASP   A CA  1 
ATOM   3382 C  C   . ASP   A 1 453 ? 6.260   -0.076  13.624  1.00 10.69 ? 476  ASP   A C   1 
ATOM   3383 O  O   . ASP   A 1 453 ? 6.191   -1.294  13.535  1.00 9.64  ? 476  ASP   A O   1 
ATOM   3384 C  CB  . ASP   A 1 453 ? 7.681   1.052   11.855  1.00 12.72 ? 476  ASP   A CB  1 
ATOM   3385 C  CG  . ASP   A 1 453 ? 7.715   1.481   10.392  1.00 16.24 ? 476  ASP   A CG  1 
ATOM   3386 O  OD1 . ASP   A 1 453 ? 6.774   1.095   9.661   1.00 16.87 ? 476  ASP   A OD1 1 
ATOM   3387 O  OD2 . ASP   A 1 453 ? 8.691   2.160   10.000  1.00 21.62 ? 476  ASP   A OD2 1 
ATOM   3388 N  N   . LYS   A 1 454 ? 6.341   0.590   14.786  1.00 10.05 ? 477  LYS   A N   1 
ATOM   3389 C  CA  . LYS   A 1 454 ? 6.364   -0.116  16.059  1.00 10.07 ? 477  LYS   A CA  1 
ATOM   3390 C  C   . LYS   A 1 454 ? 5.077   -0.910  16.252  1.00 9.76  ? 477  LYS   A C   1 
ATOM   3391 O  O   . LYS   A 1 454 ? 5.100   -2.087  16.608  1.00 9.14  ? 477  LYS   A O   1 
ATOM   3392 C  CB  . LYS   A 1 454 ? 6.573   0.907   17.178  1.00 10.50 ? 477  LYS   A CB  1 
ATOM   3393 C  CG  . LYS   A 1 454 ? 6.686   0.251   18.523  1.00 11.67 ? 477  LYS   A CG  1 
ATOM   3394 C  CD  . LYS   A 1 454 ? 6.392   1.173   19.689  1.00 14.45 ? 477  LYS   A CD  1 
ATOM   3395 C  CE  . LYS   A 1 454 ? 6.687   0.511   20.993  1.00 17.33 ? 477  LYS   A CE  1 
ATOM   3396 N  NZ  . LYS   A 1 454 ? 6.289   1.358   22.127  1.00 18.01 ? 477  LYS   A NZ  1 
ATOM   3397 N  N   . VAL   A 1 455 ? 3.924   -0.252  16.054  1.00 8.65  ? 478  VAL   A N   1 
ATOM   3398 C  CA  . VAL   A 1 455 ? 2.643   -0.896  16.249  1.00 9.40  ? 478  VAL   A CA  1 
ATOM   3399 C  C   . VAL   A 1 455 ? 2.439   -2.012  15.234  1.00 9.28  ? 478  VAL   A C   1 
ATOM   3400 O  O   . VAL   A 1 455 ? 1.980   -3.094  15.610  1.00 9.20  ? 478  VAL   A O   1 
ATOM   3401 C  CB  . VAL   A 1 455 ? 1.493   0.123   16.221  1.00 9.29  ? 478  VAL   A CB  1 
ATOM   3402 C  CG1 . VAL   A 1 455 ? 0.128   -0.521  16.260  1.00 9.11  ? 478  VAL   A CG1 1 
ATOM   3403 C  CG2 . VAL   A 1 455 ? 1.610   1.094   17.392  1.00 10.33 ? 478  VAL   A CG2 1 
ATOM   3404 N  N   . LYS   A 1 456 ? 2.783   -1.771  13.982  1.00 10.21 ? 479  LYS   A N   1 
ATOM   3405 C  CA  . LYS   A 1 456 ? 2.604   -2.801  12.974  1.00 10.75 ? 479  LYS   A CA  1 
ATOM   3406 C  C   . LYS   A 1 456 ? 3.430   -4.053  13.303  1.00 11.27 ? 479  LYS   A C   1 
ATOM   3407 O  O   . LYS   A 1 456 ? 2.976   -5.194  13.126  1.00 11.23 ? 479  LYS   A O   1 
ATOM   3408 C  CB  . LYS   A 1 456 ? 3.019   -2.236  11.613  1.00 10.54 ? 479  LYS   A CB  1 
ATOM   3409 C  CG  . LYS   A 1 456 ? 2.679   -3.181  10.474  1.00 11.97 ? 479  LYS   A CG  1 
ATOM   3410 C  CD  . LYS   A 1 456 ? 1.194   -3.338  10.151  1.00 11.74 ? 479  LYS   A CD  1 
ATOM   3411 C  CE  . LYS   A 1 456 ? 0.901   -4.262  8.998   1.00 12.45 ? 479  LYS   A CE  1 
ATOM   3412 N  NZ  . LYS   A 1 456 ? -0.533  -4.238  8.696   1.00 11.90 ? 479  LYS   A NZ  1 
ATOM   3413 N  N   . ALA   A 1 457 ? 4.671   -3.836  13.730  1.00 10.89 ? 480  ALA   A N   1 
ATOM   3414 C  CA  . ALA   A 1 457 ? 5.557   -4.944  14.062  1.00 10.20 ? 480  ALA   A CA  1 
ATOM   3415 C  C   . ALA   A 1 457 ? 5.041   -5.663  15.297  1.00 9.77  ? 480  ALA   A C   1 
ATOM   3416 O  O   . ALA   A 1 457 ? 5.270   -6.855  15.437  1.00 10.88 ? 480  ALA   A O   1 
ATOM   3417 C  CB  . ALA   A 1 457 ? 6.940   -4.457  14.337  1.00 10.05 ? 480  ALA   A CB  1 
ATOM   3418 N  N   . TYR   A 1 458 ? 4.365   -4.930  16.180  1.00 9.67  ? 481  TYR   A N   1 
ATOM   3419 C  CA  . TYR   A 1 458 ? 3.883   -5.533  17.409  1.00 10.10 ? 481  TYR   A CA  1 
ATOM   3420 C  C   . TYR   A 1 458 ? 2.590   -6.316  17.143  1.00 9.90  ? 481  TYR   A C   1 
ATOM   3421 O  O   . TYR   A 1 458 ? 2.254   -7.210  17.913  1.00 11.04 ? 481  TYR   A O   1 
ATOM   3422 C  CB  . TYR   A 1 458 ? 3.690   -4.452  18.474  1.00 10.92 ? 481  TYR   A CB  1 
ATOM   3423 C  CG  . TYR   A 1 458 ? 3.706   -4.935  19.921  1.00 11.12 ? 481  TYR   A CG  1 
ATOM   3424 C  CD1 . TYR   A 1 458 ? 4.755   -5.740  20.364  1.00 11.79 ? 481  TYR   A CD1 1 
ATOM   3425 C  CD2 . TYR   A 1 458 ? 2.744   -4.537  20.854  1.00 11.47 ? 481  TYR   A CD2 1 
ATOM   3426 C  CE1 . TYR   A 1 458 ? 4.810   -6.189  21.672  1.00 13.41 ? 481  TYR   A CE1 1 
ATOM   3427 C  CE2 . TYR   A 1 458 ? 2.792   -4.995  22.161  1.00 11.69 ? 481  TYR   A CE2 1 
ATOM   3428 C  CZ  . TYR   A 1 458 ? 3.834   -5.809  22.579  1.00 12.78 ? 481  TYR   A CZ  1 
ATOM   3429 O  OH  . TYR   A 1 458 ? 3.939   -6.253  23.878  1.00 14.38 ? 481  TYR   A OH  1 
ATOM   3430 N  N   . ASP   A 1 459 ? 1.805   -5.904  16.146  1.00 9.49  ? 482  ASP   A N   1 
ATOM   3431 C  CA  . ASP   A 1 459 ? 0.536   -6.556  15.839  1.00 8.99  ? 482  ASP   A CA  1 
ATOM   3432 C  C   . ASP   A 1 459 ? 0.348   -6.586  14.314  1.00 9.69  ? 482  ASP   A C   1 
ATOM   3433 O  O   . ASP   A 1 459 ? -0.543  -5.901  13.778  1.00 8.69  ? 482  ASP   A O   1 
ATOM   3434 C  CB  . ASP   A 1 459 ? -0.639  -5.815  16.463  1.00 8.59  ? 482  ASP   A CB  1 
ATOM   3435 C  CG  . ASP   A 1 459 ? -1.946  -6.588  16.545  1.00 9.62  ? 482  ASP   A CG  1 
ATOM   3436 O  OD1 . ASP   A 1 459 ? -1.930  -7.804  16.253  1.00 9.67  ? 482  ASP   A OD1 1 
ATOM   3437 O  OD2 . ASP   A 1 459 ? -2.945  -5.967  16.927  1.00 9.11  ? 482  ASP   A OD2 1 
ATOM   3438 N  N   . PRO   A 1 460 ? 1.151   -7.369  13.557  1.00 10.05 ? 483  PRO   A N   1 
ATOM   3439 C  CA  . PRO   A 1 460 ? 1.150   -7.228  12.092  1.00 10.28 ? 483  PRO   A CA  1 
ATOM   3440 C  C   . PRO   A 1 460 ? -0.128  -7.699  11.400  1.00 10.49 ? 483  PRO   A C   1 
ATOM   3441 O  O   . PRO   A 1 460 ? -0.341  -7.355  10.231  1.00 11.72 ? 483  PRO   A O   1 
ATOM   3442 C  CB  . PRO   A 1 460 ? 2.414   -8.005  11.661  1.00 11.14 ? 483  PRO   A CB  1 
ATOM   3443 C  CG  . PRO   A 1 460 ? 2.562   -9.037  12.777  1.00 10.90 ? 483  PRO   A CG  1 
ATOM   3444 C  CD  . PRO   A 1 460 ? 2.170   -8.303  14.054  1.00 10.85 ? 483  PRO   A CD  1 
ATOM   3445 N  N   . THR   A 1 461 ? -0.991  -8.471  12.106  1.00 9.99  ? 484  THR   A N   1 
ATOM   3446 C  CA  . THR   A 1 461 ? -2.227  -9.010  11.543  1.00 8.97  ? 484  THR   A CA  1 
ATOM   3447 C  C   . THR   A 1 461 ? -3.381  -8.001  11.620  1.00 9.11  ? 484  THR   A C   1 
ATOM   3448 O  O   . THR   A 1 461 ? -4.500  -8.301  11.180  1.00 8.90  ? 484  THR   A O   1 
ATOM   3449 C  CB  . THR   A 1 461 ? -2.635  -10.331 12.192  1.00 10.14 ? 484  THR   A CB  1 
ATOM   3450 O  OG1 . THR   A 1 461 ? -3.067  -10.135 13.540  1.00 9.56  ? 484  THR   A OG1 1 
ATOM   3451 C  CG2 . THR   A 1 461 ? -1.534  -11.376 12.059  1.00 11.09 ? 484  THR   A CG2 1 
ATOM   3452 N  N   . ARG   A 1 462 ? -3.092  -6.804  12.128  1.00 7.99  ? 485  ARG   A N   1 
ATOM   3453 C  CA  . ARG   A 1 462 ? -4.011  -5.679  12.078  1.00 8.13  ? 485  ARG   A CA  1 
ATOM   3454 C  C   . ARG   A 1 462 ? -3.420  -4.594  11.172  1.00 7.76  ? 485  ARG   A C   1 
ATOM   3455 O  O   . ARG   A 1 462 ? -2.206  -4.510  10.970  1.00 8.34  ? 485  ARG   A O   1 
ATOM   3456 C  CB  . ARG   A 1 462 ? -4.258  -5.081  13.475  1.00 8.34  ? 485  ARG   A CB  1 
ATOM   3457 C  CG  . ARG   A 1 462 ? -5.332  -5.732  14.354  1.00 8.88  ? 485  ARG   A CG  1 
ATOM   3458 C  CD  . ARG   A 1 462 ? -5.243  -7.206  14.511  1.00 9.29  ? 485  ARG   A CD  1 
ATOM   3459 N  NE  . ARG   A 1 462 ? -6.428  -7.592  15.285  1.00 9.31  ? 485  ARG   A NE  1 
ATOM   3460 C  CZ  . ARG   A 1 462 ? -6.452  -7.736  16.593  1.00 8.77  ? 485  ARG   A CZ  1 
ATOM   3461 N  NH1 . ARG   A 1 462 ? -5.388  -7.360  17.278  1.00 8.59  ? 485  ARG   A NH1 1 
ATOM   3462 N  NH2 . ARG   A 1 462 ? -7.563  -8.121  17.187  1.00 8.42  ? 485  ARG   A NH2 1 
ATOM   3463 N  N   . LEU   A 1 463 ? -4.297  -3.719  10.673  1.00 8.13  ? 486  LEU   A N   1 
ATOM   3464 C  CA  . LEU   A 1 463 ? -3.891  -2.522  9.937   1.00 8.24  ? 486  LEU   A CA  1 
ATOM   3465 C  C   . LEU   A 1 463 ? -3.471  -1.470  10.944  1.00 8.20  ? 486  LEU   A C   1 
ATOM   3466 O  O   . LEU   A 1 463 ? -3.961  -1.489  12.081  1.00 8.90  ? 486  LEU   A O   1 
ATOM   3467 C  CB  . LEU   A 1 463 ? -4.976  -1.982  9.014   1.00 8.33  ? 486  LEU   A CB  1 
ATOM   3468 C  CG  . LEU   A 1 463 ? -5.488  -2.979  7.950   1.00 9.95  ? 486  LEU   A CG  1 
ATOM   3469 C  CD1 . LEU   A 1 463 ? -6.625  -2.327  7.138   1.00 10.60 ? 486  LEU   A CD1 1 
ATOM   3470 C  CD2 . LEU   A 1 463 ? -4.402  -3.506  7.040   1.00 10.70 ? 486  LEU   A CD2 1 
ATOM   3471 N  N   . VAL   A 1 464 ? -2.587  -0.558  10.495  1.00 7.92  ? 487  VAL   A N   1 
ATOM   3472 C  CA  . VAL   A 1 464 ? -2.132  0.565   11.295  1.00 9.16  ? 487  VAL   A CA  1 
ATOM   3473 C  C   . VAL   A 1 464 ? -2.293  1.861   10.522  1.00 8.62  ? 487  VAL   A C   1 
ATOM   3474 O  O   . VAL   A 1 464 ? -1.872  1.963   9.368   1.00 9.49  ? 487  VAL   A O   1 
ATOM   3475 C  CB  . VAL   A 1 464 ? -0.679  0.420   11.773  1.00 10.94 ? 487  VAL   A CB  1 
ATOM   3476 C  CG1 . VAL   A 1 464 ? -0.241  1.572   12.669  1.00 11.99 ? 487  VAL   A CG1 1 
ATOM   3477 C  CG2 . VAL   A 1 464 ? -0.587  -0.873  12.562  1.00 12.57 ? 487  VAL   A CG2 1 
ATOM   3478 N  N   . ASP   A 1 465 ? -2.813  2.852   11.241  1.00 8.93  ? 488  ASP   A N   1 
ATOM   3479 C  CA  . ASP   A 1 465 ? -3.034  4.210   10.756  1.00 8.73  ? 488  ASP   A CA  1 
ATOM   3480 C  C   . ASP   A 1 465 ? -2.125  5.107   11.592  1.00 8.84  ? 488  ASP   A C   1 
ATOM   3481 O  O   . ASP   A 1 465 ? -2.304  5.235   12.816  1.00 8.52  ? 488  ASP   A O   1 
ATOM   3482 C  CB  . ASP   A 1 465 ? -4.507  4.534   10.923  1.00 8.76  ? 488  ASP   A CB  1 
ATOM   3483 C  CG  . ASP   A 1 465 ? -5.036  5.907   10.519  1.00 8.91  ? 488  ASP   A CG  1 
ATOM   3484 O  OD1 . ASP   A 1 465 ? -4.220  6.806   10.222  1.00 9.85  ? 488  ASP   A OD1 1 
ATOM   3485 O  OD2 . ASP   A 1 465 ? -6.300  6.067   10.463  1.00 9.44  ? 488  ASP   A OD2 1 
ATOM   3486 N  N   . ASN   A 1 466 ? -1.129  5.701   10.958  1.00 9.62  ? 489  ASN   A N   1 
ATOM   3487 C  CA  . ASN   A 1 466 ? -0.117  6.468   11.671  1.00 10.03 ? 489  ASN   A CA  1 
ATOM   3488 C  C   . ASN   A 1 466 ? -0.679  7.748   12.287  1.00 9.53  ? 489  ASN   A C   1 
ATOM   3489 O  O   . ASN   A 1 466 ? -0.220  8.210   13.338  1.00 10.31 ? 489  ASN   A O   1 
ATOM   3490 C  CB  . ASN   A 1 466 ? 1.102   6.780   10.804  1.00 10.02 ? 489  ASN   A CB  1 
ATOM   3491 C  CG  . ASN   A 1 466 ? 1.005   8.049   9.997   1.00 10.67 ? 489  ASN   A CG  1 
ATOM   3492 O  OD1 . ASN   A 1 466 ? 1.561   9.049   10.432  1.00 9.97  ? 489  ASN   A OD1 1 
ATOM   3493 N  ND2 . ASN   A 1 466 ? 0.376   8.022   8.825   1.00 10.92 ? 489  ASN   A ND2 1 
ATOM   3494 N  N   . MET   A 1 467 ? -1.609  8.358   11.564  1.00 9.05  ? 490  MET   A N   1 
ATOM   3495 C  CA  . MET   A 1 467 ? -2.149  9.638   11.948  1.00 9.88  ? 490  MET   A CA  1 
ATOM   3496 C  C   . MET   A 1 467 ? -3.499  9.839   11.268  1.00 9.49  ? 490  MET   A C   1 
ATOM   3497 O  O   . MET   A 1 467 ? -3.586  9.797   10.042  1.00 10.14 ? 490  MET   A O   1 
ATOM   3498 C  CB  . MET   A 1 467 ? -1.187  10.745  11.497  1.00 9.81  ? 490  MET   A CB  1 
ATOM   3499 C  CG  . MET   A 1 467 ? -1.690  12.135  11.892  1.00 10.28 ? 490  MET   A CG  1 
ATOM   3500 S  SD  . MET   A 1 467 ? -1.781  12.395  13.675  1.00 11.31 ? 490  MET   A SD  1 
ATOM   3501 C  CE  . MET   A 1 467 ? -0.033  12.354  14.109  1.00 12.29 ? 490  MET   A CE  1 
ATOM   3502 N  N   . SER   A 1 468 ? -4.533  10.153  12.054  1.00 9.26  ? 491  SER   A N   1 
ATOM   3503 C  CA  . SER   A 1 468 ? -5.868  10.338  11.514  1.00 8.82  ? 491  SER   A CA  1 
ATOM   3504 C  C   . SER   A 1 468 ? -6.060  11.833  11.241  1.00 9.13  ? 491  SER   A C   1 
ATOM   3505 O  O   . SER   A 1 468 ? -5.930  12.618  12.172  1.00 8.95  ? 491  SER   A O   1 
ATOM   3506 C  CB  . SER   A 1 468 ? -6.910  9.787   12.484  1.00 9.18  ? 491  SER   A CB  1 
ATOM   3507 O  OG  . SER   A 1 468 ? -8.194  9.615   11.900  1.00 8.29  ? 491  SER   A OG  1 
ATOM   3508 N  N   . GLY   A 1 469 ? -6.290  12.189  9.964   1.00 9.21  ? 492  GLY   A N   1 
ATOM   3509 C  CA  . GLY   A 1 469 ? -6.505  13.567  9.522   1.00 10.54 ? 492  GLY   A CA  1 
ATOM   3510 C  C   . GLY   A 1 469 ? -5.224  14.276  9.048   1.00 10.85 ? 492  GLY   A C   1 
ATOM   3511 O  O   . GLY   A 1 469 ? -4.941  15.385  9.462   1.00 11.55 ? 492  GLY   A O   1 
ATOM   3512 N  N   . VAL   A 1 470 ? -4.428  13.620  8.196   1.00 12.10 ? 493  VAL   A N   1 
ATOM   3513 C  CA  . VAL   A 1 470 ? -3.140  14.151  7.745   1.00 12.30 ? 493  VAL   A CA  1 
ATOM   3514 C  C   . VAL   A 1 470 ? -3.359  15.334  6.791   1.00 14.72 ? 493  VAL   A C   1 
ATOM   3515 O  O   . VAL   A 1 470 ? -2.408  16.060  6.470   1.00 13.39 ? 493  VAL   A O   1 
ATOM   3516 C  CB  . VAL   A 1 470 ? -2.280  13.050  7.095   1.00 12.56 ? 493  VAL   A CB  1 
ATOM   3517 C  CG1 . VAL   A 1 470 ? -1.795  12.013  8.108   1.00 12.49 ? 493  VAL   A CG1 1 
ATOM   3518 C  CG2 . VAL   A 1 470 ? -2.977  12.395  5.920   1.00 11.97 ? 493  VAL   A CG2 1 
ATOM   3519 N  N   . ASN   A 1 471 ? -4.615  15.541  6.364   1.00 14.03 ? 494  ASN   A N   1 
ATOM   3520 C  CA  . ASN   A 1 471 ? -4.948  16.643  5.466   1.00 14.94 ? 494  ASN   A CA  1 
ATOM   3521 C  C   . ASN   A 1 471 ? -5.191  17.931  6.246   1.00 16.13 ? 494  ASN   A C   1 
ATOM   3522 O  O   . ASN   A 1 471 ? -5.488  18.980  5.644   1.00 17.81 ? 494  ASN   A O   1 
ATOM   3523 C  CB  . ASN   A 1 471 ? -6.139  16.337  4.576   1.00 13.79 ? 494  ASN   A CB  1 
ATOM   3524 C  CG  . ASN   A 1 471 ? -7.379  16.136  5.419   1.00 13.74 ? 494  ASN   A CG  1 
ATOM   3525 O  OD1 . ASN   A 1 471 ? -7.318  15.375  6.390   1.00 11.02 ? 494  ASN   A OD1 1 
ATOM   3526 N  ND2 . ASN   A 1 471 ? -8.488  16.782  5.068   1.00 13.92 ? 494  ASN   A ND2 1 
ATOM   3527 N  N   . CYS   A 1 472 ? -5.154  17.866  7.579   1.00 17.49 ? 495  CYS   A N   1 
ATOM   3528 C  CA  . CYS   A 1 472 ? -5.646  19.008  8.329   1.00 19.05 ? 495  CYS   A CA  1 
ATOM   3529 C  C   . CYS   A 1 472 ? -4.880  19.166  9.636   1.00 16.17 ? 495  CYS   A C   1 
ATOM   3530 O  O   . CYS   A 1 472 ? -3.965  18.396  9.917   1.00 16.93 ? 495  CYS   A O   1 
ATOM   3531 C  CB  . CYS   A 1 472 ? -7.130  18.876  8.655   1.00 20.65 ? 495  CYS   A CB  1 
ATOM   3532 S  SG  . CYS   A 1 472 ? -7.393  17.837  10.118  1.00 21.50 ? 495  CYS   A SG  1 
ATOM   3533 N  N   . CYS   A 1 473 ? -5.102  20.535  10.365  1.00 17.02 ? 496  CYS   A N   1 
ATOM   3534 C  CA  . CYS   A 1 473 ? -4.997  20.530  11.839  1.00 19.39 ? 496  CYS   A CA  1 
ATOM   3535 C  C   . CYS   A 1 473 ? -3.537  20.568  12.277  1.00 18.04 ? 496  CYS   A C   1 
ATOM   3536 O  O   . CYS   A 1 473 ? -3.260  20.430  13.465  1.00 19.37 ? 496  CYS   A O   1 
ATOM   3537 C  CB  . CYS   A 1 473 ? -5.742  19.319  12.411  1.00 22.26 ? 496  CYS   A CB  1 
ATOM   3538 S  SG  . CYS   A 1 473 ? -7.413  19.100  11.736  1.00 25.50 ? 496  CYS   A SG  1 
ATOM   3539 N  N   . GLY   A 1 474 ? -2.590  20.741  11.332  1.00 16.84 ? 497  GLY   A N   1 
ATOM   3540 C  CA  . GLY   A 1 474 ? -1.181  20.666  11.683  1.00 16.68 ? 497  GLY   A CA  1 
ATOM   3541 C  C   . GLY   A 1 474 ? -0.732  19.231  11.975  1.00 16.16 ? 497  GLY   A C   1 
ATOM   3542 O  O   . GLY   A 1 474 ? 0.338   19.018  12.549  1.00 16.20 ? 497  GLY   A O   1 
ATOM   3543 N  N   . ALA   A 1 475 ? -1.531  18.250  11.547  1.00 13.93 ? 498  ALA   A N   1 
ATOM   3544 C  CA  . ALA   A 1 475 ? -1.189  16.859  11.788  1.00 14.44 ? 498  ALA   A CA  1 
ATOM   3545 C  C   . ALA   A 1 475 ? -0.049  16.486  10.844  1.00 15.23 ? 498  ALA   A C   1 
ATOM   3546 O  O   . ALA   A 1 475 ? -0.193  16.717  9.647   1.00 17.46 ? 498  ALA   A O   1 
ATOM   3547 C  CB  . ALA   A 1 475 ? -2.403  15.990  11.525  1.00 14.22 ? 498  ALA   A CB  1 
ATOM   3548 N  N   . VAL   A 1 476 ? 1.025   15.885  11.371  1.00 14.92 ? 499  VAL   A N   1 
ATOM   3549 C  CA  . VAL   A 1 476 ? 2.117   15.405  10.541  1.00 15.08 ? 499  VAL   A CA  1 
ATOM   3550 C  C   . VAL   A 1 476 ? 1.897   13.937  10.167  1.00 15.24 ? 499  VAL   A C   1 
ATOM   3551 O  O   . VAL   A 1 476 ? 1.683   13.092  11.033  1.00 13.49 ? 499  VAL   A O   1 
ATOM   3552 C  CB  . VAL   A 1 476 ? 3.450   15.615  11.276  1.00 17.21 ? 499  VAL   A CB  1 
ATOM   3553 C  CG1 . VAL   A 1 476 ? 4.608   14.877  10.613  1.00 17.40 ? 499  VAL   A CG1 1 
ATOM   3554 C  CG2 . VAL   A 1 476 ? 3.758   17.101  11.462  1.00 19.21 ? 499  VAL   A CG2 1 
ATOM   3555 N  N   . ASP   A 1 477 ? 1.988   13.669  8.858   1.00 14.94 ? 500  ASP   A N   1 
ATOM   3556 C  CA  . ASP   A 1 477 ? 1.940   12.328  8.312   1.00 13.88 ? 500  ASP   A CA  1 
ATOM   3557 C  C   . ASP   A 1 477 ? 3.334   11.707  8.407   1.00 14.10 ? 500  ASP   A C   1 
ATOM   3558 O  O   . ASP   A 1 477 ? 4.251   12.183  7.746   1.00 13.84 ? 500  ASP   A O   1 
ATOM   3559 C  CB  . ASP   A 1 477 ? 1.518   12.368  6.851   1.00 14.30 ? 500  ASP   A CB  1 
ATOM   3560 C  CG  . ASP   A 1 477 ? 1.136   11.035  6.234   1.00 14.26 ? 500  ASP   A CG  1 
ATOM   3561 O  OD1 . ASP   A 1 477 ? 1.288   9.981   6.914   1.00 11.60 ? 500  ASP   A OD1 1 
ATOM   3562 O  OD2 . ASP   A 1 477 ? 0.673   11.054  5.065   1.00 14.75 ? 500  ASP   A OD2 1 
ATOM   3563 N  N   . GLY   A 1 478 ? 3.453   10.546  9.067   1.00 12.70 ? 501  GLY   A N   1 
ATOM   3564 C  CA  . GLY   A 1 478 ? 4.700   9.794   9.075   1.00 12.07 ? 501  GLY   A CA  1 
ATOM   3565 C  C   . GLY   A 1 478 ? 5.057   9.259   7.682   1.00 13.10 ? 501  GLY   A C   1 
ATOM   3566 O  O   . GLY   A 1 478 ? 6.220   8.948   7.409   1.00 15.68 ? 501  GLY   A O   1 
ATOM   3567 N  N   . GLY   A 1 479 ? 4.036   9.069   6.838   1.00 11.14 ? 502  GLY   A N   1 
ATOM   3568 C  CA  . GLY   A 1 479 ? 4.172   8.635   5.460   1.00 11.49 ? 502  GLY   A CA  1 
ATOM   3569 C  C   . GLY   A 1 479 ? 4.033   7.118   5.312   1.00 12.01 ? 502  GLY   A C   1 
ATOM   3570 O  O   . GLY   A 1 479 ? 3.985   6.603   4.202   1.00 14.08 ? 502  GLY   A O   1 
ATOM   3571 N  N   . ASN   A 1 480 ? 3.981   6.410   6.439   1.00 11.29 ? 503  ASN   A N   1 
ATOM   3572 C  CA  . ASN   A 1 480 ? 3.951   4.960   6.455   1.00 11.67 ? 503  ASN   A CA  1 
ATOM   3573 C  C   . ASN   A 1 480 ? 2.639   4.493   7.080   1.00 12.69 ? 503  ASN   A C   1 
ATOM   3574 O  O   . ASN   A 1 480 ? 1.623   5.196   7.012   1.00 12.09 ? 503  ASN   A O   1 
ATOM   3575 C  CB  . ASN   A 1 480 ? 5.218   4.405   7.100   1.00 12.41 ? 503  ASN   A CB  1 
ATOM   3576 C  CG  . ASN   A 1 480 ? 5.353   4.843   8.534   1.00 12.59 ? 503  ASN   A CG  1 
ATOM   3577 O  OD1 . ASN   A 1 480 ? 4.635   5.745   8.996   1.00 12.24 ? 503  ASN   A OD1 1 
ATOM   3578 N  ND2 . ASN   A 1 480 ? 6.257   4.206   9.250   1.00 14.09 ? 503  ASN   A ND2 1 
ATOM   3579 N  N   . GLY   A 1 481 ? 2.660   3.274   7.625   1.00 12.46 ? 504  GLY   A N   1 
ATOM   3580 C  CA  . GLY   A 1 481 ? 1.414   2.626   7.994   1.00 11.98 ? 504  GLY   A CA  1 
ATOM   3581 C  C   . GLY   A 1 481 ? 0.628   2.207   6.765   1.00 11.23 ? 504  GLY   A C   1 
ATOM   3582 O  O   . GLY   A 1 481 ? 1.142   2.245   5.645   1.00 12.41 ? 504  GLY   A O   1 
ATOM   3583 N  N   . ASP   A 1 482 ? -0.607  1.753   6.977   1.00 10.54 ? 505  ASP   A N   1 
ATOM   3584 C  CA  . ASP   A 1 482 ? -1.352  1.100   5.914   1.00 10.63 ? 505  ASP   A CA  1 
ATOM   3585 C  C   . ASP   A 1 482 ? -2.360  2.014   5.235   1.00 9.54  ? 505  ASP   A C   1 
ATOM   3586 O  O   . ASP   A 1 482 ? -2.861  1.641   4.174   1.00 9.95  ? 505  ASP   A O   1 
ATOM   3587 C  CB  . ASP   A 1 482 ? -2.085  -0.124  6.435   1.00 11.19 ? 505  ASP   A CB  1 
ATOM   3588 C  CG  . ASP   A 1 482 ? -1.120  -1.144  7.014   1.00 13.66 ? 505  ASP   A CG  1 
ATOM   3589 O  OD1 . ASP   A 1 482 ? -0.135  -1.465  6.287   1.00 14.66 ? 505  ASP   A OD1 1 
ATOM   3590 O  OD2 . ASP   A 1 482 ? -1.353  -1.591  8.159   1.00 10.74 ? 505  ASP   A OD2 1 
ATOM   3591 N  N   . VAL   A 1 483 ? -2.676  3.163   5.845   1.00 8.95  ? 506  VAL   A N   1 
ATOM   3592 C  CA  . VAL   A 1 483 ? -3.718  4.029   5.303   1.00 9.21  ? 506  VAL   A CA  1 
ATOM   3593 C  C   . VAL   A 1 483 ? -3.309  5.508   5.300   1.00 9.22  ? 506  VAL   A C   1 
ATOM   3594 O  O   . VAL   A 1 483 ? -2.608  6.004   6.198   1.00 10.36 ? 506  VAL   A O   1 
ATOM   3595 C  CB  . VAL   A 1 483 ? -5.057  3.865   6.059   1.00 9.54  ? 506  VAL   A CB  1 
ATOM   3596 C  CG1 . VAL   A 1 483 ? -5.615  2.479   5.878   1.00 10.08 ? 506  VAL   A CG1 1 
ATOM   3597 C  CG2 . VAL   A 1 483 ? -4.963  4.153   7.551   1.00 10.11 ? 506  VAL   A CG2 1 
ATOM   3598 N  N   . VAL   A 1 484 ? -3.855  6.213   4.294   1.00 9.05  ? 507  VAL   A N   1 
ATOM   3599 C  CA  . VAL   A 1 484 ? -3.803  7.662   4.266   1.00 9.68  ? 507  VAL   A CA  1 
ATOM   3600 C  C   . VAL   A 1 484 ? -5.197  8.121   4.682   1.00 8.65  ? 507  VAL   A C   1 
ATOM   3601 O  O   . VAL   A 1 484 ? -6.160  7.766   4.024   1.00 9.70  ? 507  VAL   A O   1 
ATOM   3602 C  CB  . VAL   A 1 484 ? -3.340  8.259   2.923   1.00 10.14 ? 507  VAL   A CB  1 
ATOM   3603 C  CG1 . VAL   A 1 484 ? -4.155  7.807   1.731   1.00 12.15 ? 507  VAL   A CG1 1 
ATOM   3604 C  CG2 . VAL   A 1 484 ? -3.334  9.771   3.000   1.00 10.67 ? 507  VAL   A CG2 1 
ATOM   3605 N  N   . ASP   A 1 485 ? -5.277  8.827   5.814   1.00 8.61  ? 508  ASP   A N   1 
ATOM   3606 C  CA  . ASP   A 1 485 ? -6.523  9.049   6.526   1.00 9.25  ? 508  ASP   A CA  1 
ATOM   3607 C  C   . ASP   A 1 485 ? -6.776  10.556  6.591   1.00 9.17  ? 508  ASP   A C   1 
ATOM   3608 O  O   . ASP   A 1 485 ? -6.007  11.284  7.198   1.00 9.31  ? 508  ASP   A O   1 
ATOM   3609 C  CB  . ASP   A 1 485 ? -6.425  8.415   7.913   1.00 9.85  ? 508  ASP   A CB  1 
ATOM   3610 C  CG  . ASP   A 1 485 ? -7.557  8.722   8.879   1.00 11.14 ? 508  ASP   A CG  1 
ATOM   3611 O  OD1 . ASP   A 1 485 ? -8.347  9.629   8.573   1.00 9.85  ? 508  ASP   A OD1 1 
ATOM   3612 O  OD2 . ASP   A 1 485 ? -7.625  8.039   9.948   1.00 12.01 ? 508  ASP   A OD2 1 
ATOM   3613 N  N   . HIS   A 1 486 ? -7.800  11.017  5.857   1.00 9.26  ? 509  HIS   A N   1 
ATOM   3614 C  CA  . HIS   A 1 486 ? -8.219  12.408  5.864   1.00 10.10 ? 509  HIS   A CA  1 
ATOM   3615 C  C   . HIS   A 1 486 ? -9.486  12.555  6.690   1.00 9.23  ? 509  HIS   A C   1 
ATOM   3616 O  O   . HIS   A 1 486 ? -10.285 11.615  6.786   1.00 9.09  ? 509  HIS   A O   1 
ATOM   3617 C  CB  . HIS   A 1 486 ? -8.558  12.895  4.448   1.00 10.97 ? 509  HIS   A CB  1 
ATOM   3618 C  CG  . HIS   A 1 486 ? -7.361  12.980  3.594   1.00 11.40 ? 509  HIS   A CG  1 
ATOM   3619 N  ND1 . HIS   A 1 486 ? -7.453  13.448  2.305   1.00 12.69 ? 509  HIS   A ND1 1 
ATOM   3620 C  CD2 . HIS   A 1 486 ? -6.051  12.800  3.843   1.00 11.70 ? 509  HIS   A CD2 1 
ATOM   3621 C  CE1 . HIS   A 1 486 ? -6.233  13.507  1.778   1.00 12.42 ? 509  HIS   A CE1 1 
ATOM   3622 N  NE2 . HIS   A 1 486 ? -5.357  13.073  2.671   1.00 11.32 ? 509  HIS   A NE2 1 
ATOM   3623 N  N   . HIS   A 1 487 ? -9.607  13.741  7.307   1.00 9.35  ? 510  HIS   A N   1 
ATOM   3624 C  CA  . HIS   A 1 487 ? -10.819 14.215  7.944   1.00 9.04  ? 510  HIS   A CA  1 
ATOM   3625 C  C   . HIS   A 1 487 ? -11.342 15.367  7.102   1.00 9.50  ? 510  HIS   A C   1 
ATOM   3626 O  O   . HIS   A 1 487 ? -10.626 16.355  6.910   1.00 10.60 ? 510  HIS   A O   1 
ATOM   3627 C  CB  . HIS   A 1 487 ? -10.502 14.739  9.337   1.00 9.58  ? 510  HIS   A CB  1 
ATOM   3628 C  CG  . HIS   A 1 487 ? -10.006 13.687  10.268  1.00 9.82  ? 510  HIS   A CG  1 
ATOM   3629 N  ND1 . HIS   A 1 487 ? -9.746  14.037  11.569  1.00 10.00 ? 510  HIS   A ND1 1 
ATOM   3630 C  CD2 . HIS   A 1 487 ? -9.703  12.390  10.130  1.00 9.67  ? 510  HIS   A CD2 1 
ATOM   3631 C  CE1 . HIS   A 1 487 ? -9.343  12.941  12.226  1.00 10.55 ? 510  HIS   A CE1 1 
ATOM   3632 N  NE2 . HIS   A 1 487 ? -9.340  11.924  11.385  1.00 9.46  ? 510  HIS   A NE2 1 
ATOM   3633 N  N   . VAL   A 1 488 ? -12.536 15.173  6.554   1.00 10.28 ? 511  VAL   A N   1 
ATOM   3634 C  CA  . VAL   A 1 488 ? -13.114 16.130  5.617   1.00 10.84 ? 511  VAL   A CA  1 
ATOM   3635 C  C   . VAL   A 1 488 ? -14.557 16.391  6.010   1.00 10.34 ? 511  VAL   A C   1 
ATOM   3636 O  O   . VAL   A 1 488 ? -15.393 15.505  5.921   1.00 9.36  ? 511  VAL   A O   1 
ATOM   3637 C  CB  . VAL   A 1 488 ? -13.061 15.717  4.133   1.00 11.16 ? 511  VAL   A CB  1 
ATOM   3638 C  CG1 . VAL   A 1 488 ? -13.552 16.881  3.276   1.00 11.85 ? 511  VAL   A CG1 1 
ATOM   3639 C  CG2 . VAL   A 1 488 ? -11.670 15.278  3.677   1.00 12.26 ? 511  VAL   A CG2 1 
ATOM   3640 N  N   . TYR   A 1 489 ? -14.837 17.638  6.381   1.00 10.33 ? 512  TYR   A N   1 
ATOM   3641 C  CA  . TYR   A 1 489 ? -16.159 18.079  6.744   1.00 10.38 ? 512  TYR   A CA  1 
ATOM   3642 C  C   . TYR   A 1 489 ? -16.637 19.192  5.826   1.00 11.28 ? 512  TYR   A C   1 
ATOM   3643 O  O   . TYR   A 1 489 ? -15.895 20.160  5.615   1.00 11.66 ? 512  TYR   A O   1 
ATOM   3644 C  CB  . TYR   A 1 489 ? -16.052 18.624  8.162   1.00 10.69 ? 512  TYR   A CB  1 
ATOM   3645 C  CG  . TYR   A 1 489 ? -15.874 17.550  9.222   1.00 9.90  ? 512  TYR   A CG  1 
ATOM   3646 C  CD1 . TYR   A 1 489 ? -16.966 16.817  9.653   1.00 9.26  ? 512  TYR   A CD1 1 
ATOM   3647 C  CD2 . TYR   A 1 489 ? -14.647 17.306  9.823   1.00 10.08 ? 512  TYR   A CD2 1 
ATOM   3648 C  CE1 . TYR   A 1 489 ? -16.840 15.866  10.650  1.00 10.21 ? 512  TYR   A CE1 1 
ATOM   3649 C  CE2 . TYR   A 1 489 ? -14.511 16.357  10.829  1.00 9.30  ? 512  TYR   A CE2 1 
ATOM   3650 C  CZ  . TYR   A 1 489 ? -15.607 15.626  11.227  1.00 9.68  ? 512  TYR   A CZ  1 
ATOM   3651 O  OH  . TYR   A 1 489 ? -15.573 14.718  12.232  1.00 9.79  ? 512  TYR   A OH  1 
ATOM   3652 N  N   . VAL   A 1 490 ? -17.895 19.098  5.384   1.00 10.67 ? 513  VAL   A N   1 
ATOM   3653 C  CA  . VAL   A 1 490 ? -18.780 17.960  5.615   1.00 11.06 ? 513  VAL   A CA  1 
ATOM   3654 C  C   . VAL   A 1 490 ? -18.309 16.726  4.836   1.00 11.61 ? 513  VAL   A C   1 
ATOM   3655 O  O   . VAL   A 1 490 ? -18.625 15.605  5.225   1.00 10.22 ? 513  VAL   A O   1 
ATOM   3656 C  CB  . VAL   A 1 490 ? -20.240 18.358  5.290   1.00 12.40 ? 513  VAL   A CB  1 
ATOM   3657 C  CG1 . VAL   A 1 490 ? -21.175 17.162  5.151   1.00 12.37 ? 513  VAL   A CG1 1 
ATOM   3658 C  CG2 . VAL   A 1 490 ? -20.761 19.339  6.316   1.00 10.85 ? 513  VAL   A CG2 1 
ATOM   3659 N  N   . GLY   A 1 491 ? -17.628 16.921  3.692   1.00 11.82 ? 514  GLY   A N   1 
ATOM   3660 C  CA  . GLY   A 1 491 ? -17.121 15.792  2.932   1.00 12.82 ? 514  GLY   A CA  1 
ATOM   3661 C  C   . GLY   A 1 491 ? -17.981 15.415  1.735   1.00 14.32 ? 514  GLY   A C   1 
ATOM   3662 O  O   . GLY   A 1 491 ? -18.942 16.113  1.383   1.00 15.25 ? 514  GLY   A O   1 
ATOM   3663 N  N   . PRO   A 1 492 ? -17.648 14.301  1.037   1.00 14.40 ? 515  PRO   A N   1 
ATOM   3664 C  CA  . PRO   A 1 492 ? -16.582 13.383  1.457   1.00 15.58 ? 515  PRO   A CA  1 
ATOM   3665 C  C   . PRO   A 1 492 ? -15.134 13.656  1.057   1.00 17.06 ? 515  PRO   A C   1 
ATOM   3666 O  O   . PRO   A 1 492 ? -14.245 12.893  1.429   1.00 18.44 ? 515  PRO   A O   1 
ATOM   3667 C  CB  . PRO   A 1 492 ? -17.124 12.115  0.810   1.00 15.66 ? 515  PRO   A CB  1 
ATOM   3668 C  CG  . PRO   A 1 492 ? -17.644 12.539  -0.535  1.00 15.44 ? 515  PRO   A CG  1 
ATOM   3669 C  CD  . PRO   A 1 492 ? -18.351 13.822  -0.165  1.00 15.83 ? 515  PRO   A CD  1 
ATOM   3670 N  N   . GLY   A 1 493 ? -14.889 14.709  0.267   1.00 15.21 ? 516  GLY   A N   1 
ATOM   3671 C  CA  . GLY   A 1 493 ? -13.532 15.062  -0.116  1.00 15.74 ? 516  GLY   A CA  1 
ATOM   3672 C  C   . GLY   A 1 493 ? -13.039 14.201  -1.278  1.00 15.05 ? 516  GLY   A C   1 
ATOM   3673 O  O   . GLY   A 1 493 ? -13.819 13.545  -1.937  1.00 16.72 ? 516  GLY   A O   1 
ATOM   3674 N  N   . THR   A 1 494 ? -11.726 14.170  -1.480  1.00 16.40 ? 517  THR   A N   1 
ATOM   3675 C  CA  . THR   A 1 494 ? -11.144 13.634  -2.700  1.00 17.39 ? 517  THR   A CA  1 
ATOM   3676 C  C   . THR   A 1 494 ? -9.869  12.851  -2.396  1.00 17.03 ? 517  THR   A C   1 
ATOM   3677 O  O   . THR   A 1 494 ? -8.958  12.781  -3.222  1.00 15.38 ? 517  THR   A O   1 
ATOM   3678 C  CB  . THR   A 1 494 ? -10.918 14.793  -3.673  1.00 19.47 ? 517  THR   A CB  1 
ATOM   3679 O  OG1 . THR   A 1 494 ? -10.049 15.728  -3.049  1.00 19.92 ? 517  THR   A OG1 1 
ATOM   3680 C  CG2 . THR   A 1 494 ? -12.240 15.430  -4.076  1.00 21.64 ? 517  THR   A CG2 1 
ATOM   3681 N  N   . THR   A 1 495 ? -9.845  12.200  -1.228  1.00 14.31 ? 518  THR   A N   1 
ATOM   3682 C  CA  . THR   A 1 495 ? -8.750  11.313  -0.848  1.00 13.43 ? 518  THR   A CA  1 
ATOM   3683 C  C   . THR   A 1 495 ? -8.597  10.166  -1.853  1.00 13.41 ? 518  THR   A C   1 
ATOM   3684 O  O   . THR   A 1 495 ? -9.564  9.498   -2.208  1.00 14.28 ? 518  THR   A O   1 
ATOM   3685 C  CB  . THR   A 1 495 ? -9.003  10.723  0.550   1.00 13.21 ? 518  THR   A CB  1 
ATOM   3686 O  OG1 . THR   A 1 495 ? -9.548  11.693  1.438   1.00 14.23 ? 518  THR   A OG1 1 
ATOM   3687 C  CG2 . THR   A 1 495 ? -7.724  10.194  1.169   1.00 13.64 ? 518  THR   A CG2 1 
ATOM   3688 N  N   . VAL   A 1 496 ? -7.338  9.890   -2.219  1.00 14.17 ? 519  VAL   A N   1 
ATOM   3689 C  CA  . VAL   A 1 496 ? -6.994  8.832   -3.151  1.00 13.52 ? 519  VAL   A CA  1 
ATOM   3690 C  C   . VAL   A 1 496 ? -5.857  8.034   -2.530  1.00 13.21 ? 519  VAL   A C   1 
ATOM   3691 O  O   . VAL   A 1 496 ? -5.033  8.554   -1.766  1.00 13.11 ? 519  VAL   A O   1 
ATOM   3692 C  CB  . VAL   A 1 496 ? -6.600  9.374   -4.550  1.00 16.12 ? 519  VAL   A CB  1 
ATOM   3693 C  CG1 . VAL   A 1 496 ? -7.793  9.981   -5.293  1.00 16.30 ? 519  VAL   A CG1 1 
ATOM   3694 C  CG2 . VAL   A 1 496 ? -5.458  10.381  -4.451  1.00 17.01 ? 519  VAL   A CG2 1 
ATOM   3695 N  N   . PRO   A 1 497 ? -5.808  6.725   -2.819  1.00 12.82 ? 520  PRO   A N   1 
ATOM   3696 C  CA  . PRO   A 1 497 ? -4.752  5.879   -2.281  1.00 12.49 ? 520  PRO   A CA  1 
ATOM   3697 C  C   . PRO   A 1 497 ? -3.418  6.182   -2.946  1.00 14.86 ? 520  PRO   A C   1 
ATOM   3698 O  O   . PRO   A 1 497 ? -3.384  6.865   -3.971  1.00 13.25 ? 520  PRO   A O   1 
ATOM   3699 C  CB  . PRO   A 1 497 ? -5.277  4.503   -2.542  1.00 12.52 ? 520  PRO   A CB  1 
ATOM   3700 C  CG  . PRO   A 1 497 ? -6.194  4.630   -3.761  1.00 11.81 ? 520  PRO   A CG  1 
ATOM   3701 C  CD  . PRO   A 1 497 ? -6.802  5.996   -3.615  1.00 12.54 ? 520  PRO   A CD  1 
ATOM   3702 N  N   . SER   A 1 498 ? -2.343  5.739   -2.284  1.00 13.44 ? 521  SER   A N   1 
ATOM   3703 C  CA  . SER   A 1 498 ? -1.001  5.779   -2.828  1.00 14.28 ? 521  SER   A CA  1 
ATOM   3704 C  C   . SER   A 1 498 ? -0.627  4.386   -3.333  1.00 16.45 ? 521  SER   A C   1 
ATOM   3705 O  O   . SER   A 1 498 ? -1.400  3.429   -3.194  1.00 16.15 ? 521  SER   A O   1 
ATOM   3706 C  CB  . SER   A 1 498 ? -0.019  6.275   -1.799  1.00 15.42 ? 521  SER   A CB  1 
ATOM   3707 O  OG  . SER   A 1 498 ? 0.211   5.309   -0.783  1.00 14.14 ? 521  SER   A OG  1 
ATOM   3708 N  N   . ALA   A 1 499 ? 0.589   4.256   -3.861  1.00 16.52 ? 522  ALA   A N   1 
ATOM   3709 C  CA  . ALA   A 1 499 ? 1.070   2.942   -4.247  1.00 19.58 ? 522  ALA   A CA  1 
ATOM   3710 C  C   . ALA   A 1 499 ? 1.203   2.034   -3.017  1.00 18.64 ? 522  ALA   A C   1 
ATOM   3711 O  O   . ALA   A 1 499 ? 1.209   0.827   -3.158  1.00 17.97 ? 522  ALA   A O   1 
ATOM   3712 C  CB  . ALA   A 1 499 ? 2.368   3.076   -5.005  1.00 20.29 ? 522  ALA   A CB  1 
ATOM   3713 N  N   . THR   A 1 500 ? 1.339   2.597   -1.811  1.00 19.35 ? 523  THR   A N   1 
ATOM   3714 C  CA  . THR   A 1 500 ? 1.629   1.775   -0.642  1.00 18.31 ? 523  THR   A CA  1 
ATOM   3715 C  C   . THR   A 1 500 ? 0.488   1.768   0.373   1.00 16.61 ? 523  THR   A C   1 
ATOM   3716 O  O   . THR   A 1 500 ? 0.516   0.949   1.290   1.00 17.09 ? 523  THR   A O   1 
ATOM   3717 C  CB  . THR   A 1 500 ? 2.918   2.259   0.021   1.00 20.30 ? 523  THR   A CB  1 
ATOM   3718 O  OG1 . THR   A 1 500 ? 2.853   3.675   0.116   1.00 19.44 ? 523  THR   A OG1 1 
ATOM   3719 C  CG2 . THR   A 1 500 ? 4.149   1.835   -0.766  1.00 20.85 ? 523  THR   A CG2 1 
ATOM   3720 N  N   . ARG   A 1 501 ? -0.473  2.696   0.265   1.00 13.62 ? 524  ARG   A N   1 
ATOM   3721 C  CA  . ARG   A 1 501 ? -1.450  2.906   1.338   1.00 13.02 ? 524  ARG   A CA  1 
ATOM   3722 C  C   . ARG   A 1 501 ? -2.855  3.085   0.768   1.00 13.24 ? 524  ARG   A C   1 
ATOM   3723 O  O   . ARG   A 1 501 ? -3.035  3.829   -0.185  1.00 13.87 ? 524  ARG   A O   1 
ATOM   3724 C  CB  . ARG   A 1 501 ? -1.135  4.102   2.230   1.00 12.89 ? 524  ARG   A CB  1 
ATOM   3725 C  CG  . ARG   A 1 501 ? 0.264   4.049   2.824   1.00 12.69 ? 524  ARG   A CG  1 
ATOM   3726 C  CD  . ARG   A 1 501 ? 0.559   5.130   3.880   1.00 14.03 ? 524  ARG   A CD  1 
ATOM   3727 N  NE  . ARG   A 1 501 ? 0.446   6.508   3.387   1.00 13.75 ? 524  ARG   A NE  1 
ATOM   3728 C  CZ  . ARG   A 1 501 ? 0.551   7.600   4.131   1.00 14.54 ? 524  ARG   A CZ  1 
ATOM   3729 N  NH1 . ARG   A 1 501 ? 0.776   7.498   5.427   1.00 14.48 ? 524  ARG   A NH1 1 
ATOM   3730 N  NH2 . ARG   A 1 501 ? 0.488   8.819   3.577   1.00 15.95 ? 524  ARG   A NH2 1 
ATOM   3731 N  N   . ALA   A 1 502 ? -3.830  2.429   1.409   1.00 10.68 ? 525  ALA   A N   1 
ATOM   3732 C  CA  . ALA   A 1 502 ? -5.239  2.589   1.080   1.00 10.30 ? 525  ALA   A CA  1 
ATOM   3733 C  C   . ALA   A 1 502 ? -5.706  3.936   1.602   1.00 10.87 ? 525  ALA   A C   1 
ATOM   3734 O  O   . ALA   A 1 502 ? -5.122  4.456   2.566   1.00 10.97 ? 525  ALA   A O   1 
ATOM   3735 C  CB  . ALA   A 1 502 ? -6.068  1.500   1.695   1.00 10.38 ? 525  ALA   A CB  1 
ATOM   3736 N  N   . ALA   A 1 503 ? -6.747  4.459   0.960   1.00 10.63 ? 526  ALA   A N   1 
ATOM   3737 C  CA  . ALA   A 1 503 ? -7.296  5.760   1.286   1.00 10.75 ? 526  ALA   A CA  1 
ATOM   3738 C  C   . ALA   A 1 503 ? -8.521  5.549   2.164   1.00 9.21  ? 526  ALA   A C   1 
ATOM   3739 O  O   . ALA   A 1 503 ? -9.361  4.710   1.855   1.00 9.27  ? 526  ALA   A O   1 
ATOM   3740 C  CB  . ALA   A 1 503 ? -7.674  6.503   0.006   1.00 10.88 ? 526  ALA   A CB  1 
ATOM   3741 N  N   . VAL   A 1 504 ? -8.592  6.311   3.245   1.00 9.31  ? 527  VAL   A N   1 
ATOM   3742 C  CA  . VAL   A 1 504 ? -9.730  6.242   4.142   1.00 9.61  ? 527  VAL   A CA  1 
ATOM   3743 C  C   . VAL   A 1 504 ? -10.111 7.669   4.538   1.00 9.57  ? 527  VAL   A C   1 
ATOM   3744 O  O   . VAL   A 1 504 ? -9.269  8.565   4.645   1.00 9.24  ? 527  VAL   A O   1 
ATOM   3745 C  CB  . VAL   A 1 504 ? -9.529  5.377   5.411   1.00 10.28 ? 527  VAL   A CB  1 
ATOM   3746 C  CG1 . VAL   A 1 504 ? -9.115  3.951   5.067   1.00 10.47 ? 527  VAL   A CG1 1 
ATOM   3747 C  CG2 . VAL   A 1 504 ? -8.547  5.989   6.402   1.00 10.77 ? 527  VAL   A CG2 1 
ATOM   3748 N  N   . LEU   A 1 505 ? -11.403 7.828   4.816   1.00 9.13  ? 528  LEU   A N   1 
ATOM   3749 C  CA  . LEU   A 1 505 ? -11.967 9.067   5.343   1.00 10.00 ? 528  LEU   A CA  1 
ATOM   3750 C  C   . LEU   A 1 505 ? -12.250 8.809   6.825   1.00 8.97  ? 528  LEU   A C   1 
ATOM   3751 O  O   . LEU   A 1 505 ? -13.297 8.250   7.178   1.00 10.10 ? 528  LEU   A O   1 
ATOM   3752 C  CB  . LEU   A 1 505 ? -13.198 9.350   4.466   1.00 10.92 ? 528  LEU   A CB  1 
ATOM   3753 C  CG  . LEU   A 1 505 ? -14.005 10.616  4.750   1.00 11.81 ? 528  LEU   A CG  1 
ATOM   3754 C  CD1 . LEU   A 1 505 ? -13.179 11.868  4.557   1.00 11.41 ? 528  LEU   A CD1 1 
ATOM   3755 C  CD2 . LEU   A 1 505 ? -15.215 10.690  3.844   1.00 11.97 ? 528  LEU   A CD2 1 
ATOM   3756 N  N   . GLY   A 1 506 ? -11.263 9.126   7.662   1.00 8.41  ? 529  GLY   A N   1 
ATOM   3757 C  CA  . GLY   A 1 506 ? -11.273 8.801   9.087   1.00 8.29  ? 529  GLY   A CA  1 
ATOM   3758 C  C   . GLY   A 1 506 ? -12.251 9.659   9.876   1.00 8.61  ? 529  GLY   A C   1 
ATOM   3759 O  O   . GLY   A 1 506 ? -12.543 9.333   11.023  1.00 9.65  ? 529  GLY   A O   1 
ATOM   3760 N  N   . GLU   A 1 507 ? -12.783 10.716  9.249   1.00 8.33  ? 530  GLU   A N   1 
ATOM   3761 C  CA  . GLU   A 1 507 ? -13.922 11.447  9.792   1.00 8.26  ? 530  GLU   A CA  1 
ATOM   3762 C  C   . GLU   A 1 507 ? -14.534 12.259  8.645   1.00 8.66  ? 530  GLU   A C   1 
ATOM   3763 O  O   . GLU   A 1 507 ? -13.800 12.765  7.784   1.00 9.07  ? 530  GLU   A O   1 
ATOM   3764 C  CB  . GLU   A 1 507 ? -13.557 12.485  10.855  1.00 8.66  ? 530  GLU   A CB  1 
ATOM   3765 C  CG  . GLU   A 1 507 ? -13.198 11.968  12.245  1.00 9.34  ? 530  GLU   A CG  1 
ATOM   3766 C  CD  . GLU   A 1 507 ? -12.675 12.985  13.261  1.00 9.77  ? 530  GLU   A CD  1 
ATOM   3767 O  OE1 . GLU   A 1 507 ? -13.190 14.148  13.281  1.00 9.85  ? 530  GLU   A OE1 1 
ATOM   3768 O  OE2 . GLU   A 1 507 ? -11.784 12.592  14.060  1.00 10.11 ? 530  GLU   A OE2 1 
ATOM   3769 N  N   . PHE   A 1 508 ? -15.857 12.381  8.654   1.00 8.82  ? 531  PHE   A N   1 
ATOM   3770 C  CA  . PHE   A 1 508 ? -16.596 13.241  7.740   1.00 8.94  ? 531  PHE   A CA  1 
ATOM   3771 C  C   . PHE   A 1 508 ? -17.999 13.423  8.313   1.00 9.40  ? 531  PHE   A C   1 
ATOM   3772 O  O   . PHE   A 1 508 ? -18.380 12.792  9.303   1.00 9.01  ? 531  PHE   A O   1 
ATOM   3773 C  CB  . PHE   A 1 508 ? -16.670 12.681  6.306   1.00 9.51  ? 531  PHE   A CB  1 
ATOM   3774 C  CG  . PHE   A 1 508 ? -17.659 11.548  6.114   1.00 10.18 ? 531  PHE   A CG  1 
ATOM   3775 C  CD1 . PHE   A 1 508 ? -17.395 10.282  6.639   1.00 10.35 ? 531  PHE   A CD1 1 
ATOM   3776 C  CD2 . PHE   A 1 508 ? -18.870 11.748  5.453   1.00 10.72 ? 531  PHE   A CD2 1 
ATOM   3777 C  CE1 . PHE   A 1 508 ? -18.315 9.258   6.524   1.00 10.21 ? 531  PHE   A CE1 1 
ATOM   3778 C  CE2 . PHE   A 1 508 ? -19.795 10.724  5.348   1.00 11.57 ? 531  PHE   A CE2 1 
ATOM   3779 C  CZ  . PHE   A 1 508 ? -19.507 9.467   5.856   1.00 11.05 ? 531  PHE   A CZ  1 
ATOM   3780 N  N   . GLY   A 1 509 ? -18.796 14.293  7.673   1.00 8.92  ? 532  GLY   A N   1 
ATOM   3781 C  CA  . GLY   A 1 509 ? -20.208 14.390  8.006   1.00 9.07  ? 532  GLY   A CA  1 
ATOM   3782 C  C   . GLY   A 1 509 ? -20.486 15.452  9.063   1.00 9.03  ? 532  GLY   A C   1 
ATOM   3783 O  O   . GLY   A 1 509 ? -20.323 16.645  8.807   1.00 9.83  ? 532  GLY   A O   1 
ATOM   3784 N  N   . GLY   A 1 510 ? -20.850 15.028  10.290  1.00 8.66  ? 533  GLY   A N   1 
ATOM   3785 C  CA  . GLY   A 1 510 ? -20.962 15.969  11.385  1.00 8.59  ? 533  GLY   A CA  1 
ATOM   3786 C  C   . GLY   A 1 510 ? -22.222 16.847  11.315  1.00 8.14  ? 533  GLY   A C   1 
ATOM   3787 O  O   . GLY   A 1 510 ? -22.209 17.957  11.855  1.00 8.94  ? 533  GLY   A O   1 
ATOM   3788 N  N   . LEU   A 1 511 ? -23.296 16.312  10.712  1.00 8.64  ? 534  LEU   A N   1 
ATOM   3789 C  CA  . LEU   A 1 511 ? -24.536 17.042  10.477  1.00 8.95  ? 534  LEU   A CA  1 
ATOM   3790 C  C   . LEU   A 1 511 ? -25.286 17.183  11.798  1.00 9.62  ? 534  LEU   A C   1 
ATOM   3791 O  O   . LEU   A 1 511 ? -25.576 16.186  12.457  1.00 9.00  ? 534  LEU   A O   1 
ATOM   3792 C  CB  . LEU   A 1 511 ? -25.389 16.372  9.397   1.00 9.28  ? 534  LEU   A CB  1 
ATOM   3793 C  CG  . LEU   A 1 511 ? -24.677 16.063  8.068   1.00 10.25 ? 534  LEU   A CG  1 
ATOM   3794 C  CD1 . LEU   A 1 511 ? -25.647 15.245  7.197   1.00 10.76 ? 534  LEU   A CD1 1 
ATOM   3795 C  CD2 . LEU   A 1 511 ? -24.156 17.261  7.249   1.00 10.89 ? 534  LEU   A CD2 1 
ATOM   3796 N  N   . GLY   A 1 512 ? -25.638 18.428  12.140  1.00 10.29 ? 535  GLY   A N   1 
ATOM   3797 C  CA  . GLY   A 1 512 ? -26.257 18.717  13.425  1.00 10.61 ? 535  GLY   A CA  1 
ATOM   3798 C  C   . GLY   A 1 512 ? -27.773 18.855  13.365  1.00 9.92  ? 535  GLY   A C   1 
ATOM   3799 O  O   . GLY   A 1 512 ? -28.348 19.345  12.390  1.00 9.94  ? 535  GLY   A O   1 
ATOM   3800 N  N   . PHE   A 1 513 ? -28.418 18.438  14.460  1.00 9.65  ? 536  PHE   A N   1 
ATOM   3801 C  CA  . PHE   A 1 513 ? -29.831 18.722  14.645  1.00 11.21 ? 536  PHE   A CA  1 
ATOM   3802 C  C   . PHE   A 1 513 ? -30.166 18.631  16.124  1.00 10.77 ? 536  PHE   A C   1 
ATOM   3803 O  O   . PHE   A 1 513 ? -29.943 17.596  16.743  1.00 10.87 ? 536  PHE   A O   1 
ATOM   3804 C  CB  . PHE   A 1 513 ? -30.719 17.780  13.813  1.00 12.59 ? 536  PHE   A CB  1 
ATOM   3805 C  CG  . PHE   A 1 513 ? -32.188 18.143  13.974  1.00 13.49 ? 536  PHE   A CG  1 
ATOM   3806 C  CD1 . PHE   A 1 513 ? -32.701 19.290  13.365  1.00 15.65 ? 536  PHE   A CD1 1 
ATOM   3807 C  CD2 . PHE   A 1 513 ? -33.016 17.403  14.799  1.00 14.97 ? 536  PHE   A CD2 1 
ATOM   3808 C  CE1 . PHE   A 1 513 ? -34.034 19.660  13.564  1.00 16.42 ? 536  PHE   A CE1 1 
ATOM   3809 C  CE2 . PHE   A 1 513 ? -34.342 17.758  14.987  1.00 15.94 ? 536  PHE   A CE2 1 
ATOM   3810 C  CZ  . PHE   A 1 513 ? -34.854 18.892  14.369  1.00 16.96 ? 536  PHE   A CZ  1 
ATOM   3811 N  N   . LYS   A 1 514 ? -30.670 19.743  16.677  1.00 11.30 ? 537  LYS   A N   1 
ATOM   3812 C  CA  . LYS   A 1 514 ? -31.123 19.781  18.061  1.00 11.89 ? 537  LYS   A CA  1 
ATOM   3813 C  C   . LYS   A 1 514 ? -32.540 19.220  18.174  1.00 12.43 ? 537  LYS   A C   1 
ATOM   3814 O  O   . LYS   A 1 514 ? -33.504 19.760  17.620  1.00 12.30 ? 537  LYS   A O   1 
ATOM   3815 C  CB  . LYS   A 1 514 ? -31.094 21.211  18.610  1.00 12.87 ? 537  LYS   A CB  1 
ATOM   3816 C  CG  . LYS   A 1 514 ? -29.739 21.849  18.555  1.00 14.51 ? 537  LYS   A CG  1 
ATOM   3817 C  CD  . LYS   A 1 514 ? -29.656 23.259  19.147  1.00 16.12 ? 537  LYS   A CD  1 
ATOM   3818 C  CE  . LYS   A 1 514 ? -30.545 24.284  18.567  1.00 19.27 ? 537  LYS   A CE  1 
ATOM   3819 N  NZ  . LYS   A 1 514 ? -30.092 24.509  17.213  1.00 21.93 ? 537  LYS   A NZ  1 
ATOM   3820 N  N   . VAL   A 1 515 ? -32.655 18.092  18.865  1.00 11.28 ? 538  VAL   A N   1 
ATOM   3821 C  CA  . VAL   A 1 515 ? -33.939 17.478  19.121  1.00 11.92 ? 538  VAL   A CA  1 
ATOM   3822 C  C   . VAL   A 1 515 ? -34.502 17.998  20.439  1.00 12.71 ? 538  VAL   A C   1 
ATOM   3823 O  O   . VAL   A 1 515 ? -34.020 17.598  21.490  1.00 12.22 ? 538  VAL   A O   1 
ATOM   3824 C  CB  . VAL   A 1 515 ? -33.781 15.954  19.188  1.00 10.74 ? 538  VAL   A CB  1 
ATOM   3825 C  CG1 . VAL   A 1 515 ? -35.103 15.251  19.499  1.00 10.95 ? 538  VAL   A CG1 1 
ATOM   3826 C  CG2 . VAL   A 1 515 ? -33.162 15.422  17.897  1.00 10.61 ? 538  VAL   A CG2 1 
ATOM   3827 N  N   . ALA   A 1 516 ? -35.620 18.744  20.359  1.00 13.40 ? 539  ALA   A N   1 
ATOM   3828 C  CA  . ALA   A 1 516 ? -36.266 19.278  21.538  1.00 12.71 ? 539  ALA   A CA  1 
ATOM   3829 C  C   . ALA   A 1 516 ? -36.636 18.158  22.492  1.00 11.96 ? 539  ALA   A C   1 
ATOM   3830 O  O   . ALA   A 1 516 ? -37.209 17.149  22.066  1.00 13.91 ? 539  ALA   A O   1 
ATOM   3831 C  CB  . ALA   A 1 516 ? -37.524 20.040  21.174  1.00 13.23 ? 539  ALA   A CB  1 
ATOM   3832 N  N   . GLY   A 1 517 ? -36.364 18.403  23.788  1.00 11.56 ? 540  GLY   A N   1 
ATOM   3833 C  CA  . GLY   A 1 517 ? -36.572 17.431  24.840  1.00 11.77 ? 540  GLY   A CA  1 
ATOM   3834 C  C   . GLY   A 1 517 ? -35.379 16.489  25.030  1.00 12.06 ? 540  GLY   A C   1 
ATOM   3835 O  O   . GLY   A 1 517 ? -35.407 15.669  25.947  1.00 11.34 ? 540  GLY   A O   1 
ATOM   3836 N  N   . HIS   A 1 518 ? -34.405 16.531  24.112  1.00 10.23 ? 541  HIS   A N   1 
ATOM   3837 C  CA  . HIS   A 1 518 ? -33.327 15.549  24.087  1.00 10.92 ? 541  HIS   A CA  1 
ATOM   3838 C  C   . HIS   A 1 518 ? -32.006 16.267  23.817  1.00 11.26 ? 541  HIS   A C   1 
ATOM   3839 O  O   . HIS   A 1 518 ? -31.168 15.830  22.998  1.00 11.67 ? 541  HIS   A O   1 
ATOM   3840 C  CB  . HIS   A 1 518 ? -33.623 14.449  23.060  1.00 10.82 ? 541  HIS   A CB  1 
ATOM   3841 C  CG  . HIS   A 1 518 ? -34.862 13.661  23.381  1.00 11.46 ? 541  HIS   A CG  1 
ATOM   3842 N  ND1 . HIS   A 1 518 ? -34.986 12.660  24.327  1.00 13.16 ? 541  HIS   A ND1 1 
ATOM   3843 C  CD2 . HIS   A 1 518 ? -36.099 13.866  22.896  1.00 12.31 ? 541  HIS   A CD2 1 
ATOM   3844 C  CE1 . HIS   A 1 518 ? -36.247 12.247  24.344  1.00 13.03 ? 541  HIS   A CE1 1 
ATOM   3845 N  NE2 . HIS   A 1 518 ? -36.938 12.942  23.461  1.00 12.22 ? 541  HIS   A NE2 1 
ATOM   3846 N  N   . GLU   A 1 519 ? -31.883 17.436  24.449  1.00 10.88 ? 542  GLU   A N   1 
ATOM   3847 C  CA  . GLU   A 1 519 ? -30.676 18.228  24.384  1.00 11.29 ? 542  GLU   A CA  1 
ATOM   3848 C  C   . GLU   A 1 519 ? -30.024 18.210  25.766  1.00 11.92 ? 542  GLU   A C   1 
ATOM   3849 O  O   . GLU   A 1 519 ? -30.688 18.489  26.774  1.00 11.63 ? 542  GLU   A O   1 
ATOM   3850 C  CB  . GLU   A 1 519 ? -30.961 19.680  24.024  1.00 11.80 ? 542  GLU   A CB  1 
ATOM   3851 C  CG  . GLU   A 1 519 ? -31.584 19.866  22.647  1.00 11.71 ? 542  GLU   A CG  1 
ATOM   3852 C  CD  . GLU   A 1 519 ? -31.995 21.330  22.500  1.00 12.72 ? 542  GLU   A CD  1 
ATOM   3853 O  OE1 . GLU   A 1 519 ? -31.138 22.126  22.113  1.00 12.05 ? 542  GLU   A OE1 1 
ATOM   3854 O  OE2 . GLU   A 1 519 ? -33.163 21.633  22.861  1.00 15.27 ? 542  GLU   A OE2 1 
ATOM   3855 N  N   . TRP   A 1 520 ? -28.728 17.887  25.798  1.00 11.09 ? 543  TRP   A N   1 
ATOM   3856 C  CA  . TRP   A 1 520 ? -27.954 17.897  27.026  1.00 10.96 ? 543  TRP   A CA  1 
ATOM   3857 C  C   . TRP   A 1 520 ? -27.992 19.278  27.675  1.00 11.48 ? 543  TRP   A C   1 
ATOM   3858 O  O   . TRP   A 1 520 ? -28.204 19.379  28.877  1.00 11.19 ? 543  TRP   A O   1 
ATOM   3859 C  CB  . TRP   A 1 520 ? -26.516 17.484  26.722  1.00 10.90 ? 543  TRP   A CB  1 
ATOM   3860 C  CG  . TRP   A 1 520 ? -25.650 17.296  27.944  1.00 12.23 ? 543  TRP   A CG  1 
ATOM   3861 C  CD1 . TRP   A 1 520 ? -25.648 16.252  28.829  1.00 11.55 ? 543  TRP   A CD1 1 
ATOM   3862 C  CD2 . TRP   A 1 520 ? -24.564 18.149  28.330  1.00 12.04 ? 543  TRP   A CD2 1 
ATOM   3863 N  NE1 . TRP   A 1 520 ? -24.652 16.401  29.750  1.00 11.91 ? 543  TRP   A NE1 1 
ATOM   3864 C  CE2 . TRP   A 1 520 ? -23.968 17.562  29.468  1.00 12.33 ? 543  TRP   A CE2 1 
ATOM   3865 C  CE3 . TRP   A 1 520 ? -24.070 19.363  27.854  1.00 12.40 ? 543  TRP   A CE3 1 
ATOM   3866 C  CZ2 . TRP   A 1 520 ? -22.887 18.145  30.113  1.00 13.03 ? 543  TRP   A CZ2 1 
ATOM   3867 C  CZ3 . TRP   A 1 520 ? -22.970 19.915  28.472  1.00 13.73 ? 543  TRP   A CZ3 1 
ATOM   3868 C  CH2 . TRP   A 1 520 ? -22.369 19.296  29.574  1.00 13.10 ? 543  TRP   A CH2 1 
ATOM   3869 N  N   . TYR   A 1 521 ? -27.897 20.334  26.852  1.00 11.44 ? 544  TYR   A N   1 
ATOM   3870 C  CA  . TYR   A 1 521 ? -28.085 21.698  27.327  1.00 12.07 ? 544  TYR   A CA  1 
ATOM   3871 C  C   . TYR   A 1 521 ? -28.929 22.418  26.273  1.00 12.91 ? 544  TYR   A C   1 
ATOM   3872 O  O   . TYR   A 1 521 ? -28.492 22.649  25.156  1.00 12.01 ? 544  TYR   A O   1 
ATOM   3873 C  CB  . TYR   A 1 521 ? -26.745 22.398  27.600  1.00 11.66 ? 544  TYR   A CB  1 
ATOM   3874 C  CG  . TYR   A 1 521 ? -26.994 23.799  28.141  1.00 13.50 ? 544  TYR   A CG  1 
ATOM   3875 C  CD1 . TYR   A 1 521 ? -27.211 24.007  29.499  1.00 13.90 ? 544  TYR   A CD1 1 
ATOM   3876 C  CD2 . TYR   A 1 521 ? -27.110 24.897  27.285  1.00 14.35 ? 544  TYR   A CD2 1 
ATOM   3877 C  CE1 . TYR   A 1 521 ? -27.493 25.271  29.997  1.00 14.26 ? 544  TYR   A CE1 1 
ATOM   3878 C  CE2 . TYR   A 1 521 ? -27.392 26.172  27.778  1.00 14.04 ? 544  TYR   A CE2 1 
ATOM   3879 C  CZ  . TYR   A 1 521 ? -27.590 26.352  29.134  1.00 14.79 ? 544  TYR   A CZ  1 
ATOM   3880 O  OH  . TYR   A 1 521 ? -27.894 27.587  29.668  1.00 14.63 ? 544  TYR   A OH  1 
ATOM   3881 N  N   . PRO   A 1 522 ? -30.205 22.727  26.568  1.00 13.79 ? 545  PRO   A N   1 
ATOM   3882 C  CA  . PRO   A 1 522 ? -31.100 23.283  25.546  1.00 15.19 ? 545  PRO   A CA  1 
ATOM   3883 C  C   . PRO   A 1 522 ? -30.502 24.514  24.890  1.00 14.05 ? 545  PRO   A C   1 
ATOM   3884 O  O   . PRO   A 1 522 ? -30.103 25.446  25.587  1.00 14.64 ? 545  PRO   A O   1 
ATOM   3885 C  CB  . PRO   A 1 522 ? -32.343 23.604  26.355  1.00 16.05 ? 545  PRO   A CB  1 
ATOM   3886 C  CG  . PRO   A 1 522 ? -32.376 22.494  27.372  1.00 17.47 ? 545  PRO   A CG  1 
ATOM   3887 C  CD  . PRO   A 1 522 ? -30.902 22.418  27.824  1.00 16.30 ? 545  PRO   A CD  1 
ATOM   3888 N  N   . GLY   A 1 523 ? -30.388 24.474  23.549  1.00 12.99 ? 546  GLY   A N   1 
ATOM   3889 C  CA  . GLY   A 1 523 ? -29.882 25.600  22.781  1.00 12.47 ? 546  GLY   A CA  1 
ATOM   3890 C  C   . GLY   A 1 523 ? -28.372 25.612  22.666  1.00 11.61 ? 546  GLY   A C   1 
ATOM   3891 O  O   . GLY   A 1 523 ? -27.826 26.511  22.025  1.00 11.91 ? 546  GLY   A O   1 
ATOM   3892 N  N   . GLY   A 1 524 ? -27.704 24.648  23.332  1.00 10.09 ? 547  GLY   A N   1 
ATOM   3893 C  CA  . GLY   A 1 524 ? -26.258 24.622  23.416  1.00 10.72 ? 547  GLY   A CA  1 
ATOM   3894 C  C   . GLY   A 1 524 ? -25.610 24.003  22.187  1.00 10.55 ? 547  GLY   A C   1 
ATOM   3895 O  O   . GLY   A 1 524 ? -24.410 24.165  21.957  1.00 11.95 ? 547  GLY   A O   1 
ATOM   3896 N  N   . GLY   A 1 525 ? -26.410 23.365  21.348  1.00 10.95 ? 548  GLY   A N   1 
ATOM   3897 C  CA  . GLY   A 1 525 ? -25.862 22.467  20.340  1.00 11.73 ? 548  GLY   A CA  1 
ATOM   3898 C  C   . GLY   A 1 525 ? -25.124 23.142  19.190  1.00 11.96 ? 548  GLY   A C   1 
ATOM   3899 O  O   . GLY   A 1 525 ? -25.525 24.201  18.712  1.00 12.48 ? 548  GLY   A O   1 
ATOM   3900 N  N   . PHE   A 1 526 ? -24.049 22.493  18.729  1.00 11.62 ? 549  PHE   A N   1 
ATOM   3901 C  CA  . PHE   A 1 526 ? -23.290 22.918  17.570  1.00 11.01 ? 549  PHE   A CA  1 
ATOM   3902 C  C   . PHE   A 1 526 ? -22.962 21.690  16.722  1.00 10.84 ? 549  PHE   A C   1 
ATOM   3903 O  O   . PHE   A 1 526 ? -23.064 20.535  17.163  1.00 9.75  ? 549  PHE   A O   1 
ATOM   3904 C  CB  . PHE   A 1 526 ? -22.031 23.673  18.020  1.00 11.16 ? 549  PHE   A CB  1 
ATOM   3905 C  CG  . PHE   A 1 526 ? -21.030 22.732  18.673  1.00 11.12 ? 549  PHE   A CG  1 
ATOM   3906 C  CD1 . PHE   A 1 526 ? -20.189 21.948  17.887  1.00 11.50 ? 549  PHE   A CD1 1 
ATOM   3907 C  CD2 . PHE   A 1 526 ? -20.971 22.579  20.064  1.00 11.34 ? 549  PHE   A CD2 1 
ATOM   3908 C  CE1 . PHE   A 1 526 ? -19.285 21.070  18.452  1.00 12.47 ? 549  PHE   A CE1 1 
ATOM   3909 C  CE2 . PHE   A 1 526 ? -20.063 21.683  20.617  1.00 11.14 ? 549  PHE   A CE2 1 
ATOM   3910 C  CZ  . PHE   A 1 526 ? -19.224 20.956  19.814  1.00 11.55 ? 549  PHE   A CZ  1 
ATOM   3911 N  N   . SER   A 1 527 ? -22.597 21.939  15.467  1.00 10.83 ? 550  SER   A N   1 
ATOM   3912 C  CA  . SER   A 1 527 ? -22.206 20.883  14.552  1.00 10.27 ? 550  SER   A CA  1 
ATOM   3913 C  C   . SER   A 1 527 ? -21.386 21.437  13.403  1.00 9.92  ? 550  SER   A C   1 
ATOM   3914 O  O   . SER   A 1 527 ? -21.051 22.614  13.364  1.00 10.49 ? 550  SER   A O   1 
ATOM   3915 C  CB  . SER   A 1 527 ? -23.432 20.178  14.021  1.00 11.06 ? 550  SER   A CB  1 
ATOM   3916 O  OG  . SER   A 1 527 ? -24.074 20.977  13.019  1.00 10.19 ? 550  SER   A OG  1 
ATOM   3917 N  N   . TYR   A 1 528 ? -21.045 20.584  12.452  1.00 10.45 ? 551  TYR   A N   1 
ATOM   3918 C  CA  . TYR   A 1 528 ? -20.330 21.065  11.292  1.00 10.56 ? 551  TYR   A CA  1 
ATOM   3919 C  C   . TYR   A 1 528 ? -21.277 21.624  10.231  1.00 11.09 ? 551  TYR   A C   1 
ATOM   3920 O  O   . TYR   A 1 528 ? -20.805 22.253  9.286   1.00 11.44 ? 551  TYR   A O   1 
ATOM   3921 C  CB  . TYR   A 1 528 ? -19.494 19.959  10.669  1.00 10.77 ? 551  TYR   A CB  1 
ATOM   3922 C  CG  . TYR   A 1 528 ? -18.259 19.587  11.467  1.00 10.68 ? 551  TYR   A CG  1 
ATOM   3923 C  CD1 . TYR   A 1 528 ? -18.310 18.659  12.497  1.00 11.79 ? 551  TYR   A CD1 1 
ATOM   3924 C  CD2 . TYR   A 1 528 ? -17.051 20.196  11.224  1.00 11.53 ? 551  TYR   A CD2 1 
ATOM   3925 C  CE1 . TYR   A 1 528 ? -17.168 18.295  13.188  1.00 12.99 ? 551  TYR   A CE1 1 
ATOM   3926 C  CE2 . TYR   A 1 528 ? -15.901 19.864  11.922  1.00 12.55 ? 551  TYR   A CE2 1 
ATOM   3927 C  CZ  . TYR   A 1 528 ? -15.964 18.912  12.919  1.00 12.76 ? 551  TYR   A CZ  1 
ATOM   3928 O  OH  . TYR   A 1 528 ? -14.810 18.583  13.562  1.00 13.56 ? 551  TYR   A OH  1 
ATOM   3929 N  N   . GLU   A 1 529 ? -22.567 21.342  10.324  1.00 11.44 ? 552  GLU   A N   1 
ATOM   3930 C  CA  . GLU   A 1 529 ? -23.564 21.926  9.440   1.00 11.74 ? 552  GLU   A CA  1 
ATOM   3931 C  C   . GLU   A 1 529 ? -24.935 21.673  10.057  1.00 13.37 ? 552  GLU   A C   1 
ATOM   3932 O  O   . GLU   A 1 529 ? -25.428 20.554  10.095  1.00 11.95 ? 552  GLU   A O   1 
ATOM   3933 C  CB  . GLU   A 1 529 ? -23.502 21.364  8.019   1.00 11.64 ? 552  GLU   A CB  1 
ATOM   3934 C  CG  . GLU   A 1 529 ? -24.518 21.999  7.070   1.00 12.07 ? 552  GLU   A CG  1 
ATOM   3935 C  CD  . GLU   A 1 529 ? -24.568 21.385  5.683   1.00 12.85 ? 552  GLU   A CD  1 
ATOM   3936 O  OE1 . GLU   A 1 529 ? -23.576 21.550  4.947   1.00 14.09 ? 552  GLU   A OE1 1 
ATOM   3937 O  OE2 . GLU   A 1 529 ? -25.583 20.779  5.351   1.00 12.38 ? 552  GLU   A OE2 1 
ATOM   3938 N  N   . ASP   A 1 530 ? -25.557 22.733  10.570  1.00 14.85 ? 553  ASP   A N   1 
ATOM   3939 C  CA  . ASP   A 1 530 ? -26.846 22.587  11.235  1.00 16.93 ? 553  ASP   A CA  1 
ATOM   3940 C  C   . ASP   A 1 530 ? -27.941 22.357  10.210  1.00 16.93 ? 553  ASP   A C   1 
ATOM   3941 O  O   . ASP   A 1 530 ? -27.980 23.043  9.177   1.00 15.84 ? 553  ASP   A O   1 
ATOM   3942 C  CB  . ASP   A 1 530 ? -27.093 23.777  12.152  1.00 19.86 ? 553  ASP   A CB  1 
ATOM   3943 C  CG  . ASP   A 1 530 ? -26.100 23.864  13.303  1.00 25.04 ? 553  ASP   A CG  1 
ATOM   3944 O  OD1 . ASP   A 1 530 ? -25.762 22.791  13.895  1.00 26.85 ? 553  ASP   A OD1 1 
ATOM   3945 O  OD2 . ASP   A 1 530 ? -25.734 25.007  13.653  1.00 31.73 ? 553  ASP   A OD2 1 
ATOM   3946 N  N   . GLN   A 1 531 ? -28.808 21.372  10.500  1.00 15.71 ? 554  GLN   A N   1 
ATOM   3947 C  CA  . GLN   A 1 531 ? -29.913 21.043  9.614   1.00 15.59 ? 554  GLN   A CA  1 
ATOM   3948 C  C   . GLN   A 1 531 ? -31.185 21.657  10.168  1.00 15.88 ? 554  GLN   A C   1 
ATOM   3949 O  O   . GLN   A 1 531 ? -31.419 21.607  11.367  1.00 16.64 ? 554  GLN   A O   1 
ATOM   3950 C  CB  . GLN   A 1 531 ? -30.128 19.535  9.557   1.00 15.46 ? 554  GLN   A CB  1 
ATOM   3951 C  CG  . GLN   A 1 531 ? -28.888 18.764  9.127   1.00 14.70 ? 554  GLN   A CG  1 
ATOM   3952 C  CD  . GLN   A 1 531 ? -28.377 19.203  7.771   1.00 14.70 ? 554  GLN   A CD  1 
ATOM   3953 O  OE1 . GLN   A 1 531 ? -29.140 19.242  6.795   1.00 15.08 ? 554  GLN   A OE1 1 
ATOM   3954 N  NE2 . GLN   A 1 531 ? -27.128 19.629  7.718   1.00 14.01 ? 554  GLN   A NE2 1 
ATOM   3955 N  N   . PRO   A 1 532 ? -32.045 22.312  9.361   1.00 16.90 ? 555  PRO   A N   1 
ATOM   3956 C  CA  . PRO   A 1 532 ? -33.240 22.921  9.949   1.00 17.74 ? 555  PRO   A CA  1 
ATOM   3957 C  C   . PRO   A 1 532 ? -34.343 21.958  10.371  1.00 15.36 ? 555  PRO   A C   1 
ATOM   3958 O  O   . PRO   A 1 532 ? -35.158 22.323  11.212  1.00 16.43 ? 555  PRO   A O   1 
ATOM   3959 C  CB  . PRO   A 1 532 ? -33.694 23.872  8.842   1.00 18.35 ? 555  PRO   A CB  1 
ATOM   3960 C  CG  . PRO   A 1 532 ? -33.278 23.136  7.611   1.00 18.72 ? 555  PRO   A CG  1 
ATOM   3961 C  CD  . PRO   A 1 532 ? -31.875 22.582  7.923   1.00 18.14 ? 555  PRO   A CD  1 
ATOM   3962 N  N   . ASP   A 1 533 ? -34.333 20.721  9.843   1.00 13.80 ? 556  ASP   A N   1 
ATOM   3963 C  CA  . ASP   A 1 533 ? -35.302 19.704  10.215  1.00 13.85 ? 556  ASP   A CA  1 
ATOM   3964 C  C   . ASP   A 1 533 ? -34.772 18.329  9.821   1.00 13.97 ? 556  ASP   A C   1 
ATOM   3965 O  O   . ASP   A 1 533 ? -33.697 18.219  9.218   1.00 13.37 ? 556  ASP   A O   1 
ATOM   3966 C  CB  . ASP   A 1 533 ? -36.672 19.956  9.606   1.00 16.45 ? 556  ASP   A CB  1 
ATOM   3967 C  CG  . ASP   A 1 533 ? -36.634 20.040  8.093   1.00 18.10 ? 556  ASP   A CG  1 
ATOM   3968 O  OD1 . ASP   A 1 533 ? -35.921 19.215  7.467   1.00 18.83 ? 556  ASP   A OD1 1 
ATOM   3969 O  OD2 . ASP   A 1 533 ? -37.295 20.926  7.561   1.00 22.37 ? 556  ASP   A OD2 1 
ATOM   3970 N  N   . LEU   A 1 534 ? -35.546 17.299  10.187  1.00 14.79 ? 557  LEU   A N   1 
ATOM   3971 C  CA  . LEU   A 1 534 ? -35.114 15.926  10.050  1.00 14.78 ? 557  LEU   A CA  1 
ATOM   3972 C  C   . LEU   A 1 534 ? -35.131 15.505  8.580   1.00 14.91 ? 557  LEU   A C   1 
ATOM   3973 O  O   . LEU   A 1 534 ? -34.334 14.660  8.144   1.00 13.58 ? 557  LEU   A O   1 
ATOM   3974 C  CB  . LEU   A 1 534 ? -35.967 15.031  10.932  1.00 15.79 ? 557  LEU   A CB  1 
ATOM   3975 C  CG  . LEU   A 1 534 ? -35.726 15.155  12.437  1.00 16.50 ? 557  LEU   A CG  1 
ATOM   3976 C  CD1 . LEU   A 1 534 ? -36.634 14.190  13.182  1.00 17.92 ? 557  LEU   A CD1 1 
ATOM   3977 C  CD2 . LEU   A 1 534 ? -34.314 14.859  12.793  1.00 17.33 ? 557  LEU   A CD2 1 
ATOM   3978 N  N   . ALA   A 1 535 ? -36.021 16.103  7.800   1.00 15.07 ? 558  ALA   A N   1 
ATOM   3979 C  CA  . ALA   A 1 535 ? -36.056 15.794  6.381   1.00 15.46 ? 558  ALA   A CA  1 
ATOM   3980 C  C   . ALA   A 1 535 ? -34.734 16.214  5.749   1.00 14.54 ? 558  ALA   A C   1 
ATOM   3981 O  O   . ALA   A 1 535 ? -34.192 15.461  4.950   1.00 16.71 ? 558  ALA   A O   1 
ATOM   3982 C  CB  . ALA   A 1 535 ? -37.238 16.464  5.707   1.00 15.87 ? 558  ALA   A CB  1 
ATOM   3983 N  N   . HIS   A 1 536 ? -34.244 17.404  6.110   1.00 12.72 ? 559  HIS   A N   1 
ATOM   3984 C  CA  . HIS   A 1 536 ? -32.969 17.900  5.602   1.00 13.10 ? 559  HIS   A CA  1 
ATOM   3985 C  C   . HIS   A 1 536 ? -31.843 16.943  6.024   1.00 12.83 ? 559  HIS   A C   1 
ATOM   3986 O  O   . HIS   A 1 536 ? -31.005 16.559  5.219   1.00 12.18 ? 559  HIS   A O   1 
ATOM   3987 C  CB  . HIS   A 1 536 ? -32.640 19.314  6.095   1.00 13.53 ? 559  HIS   A CB  1 
ATOM   3988 C  CG  . HIS   A 1 536 ? -33.310 20.467  5.423   1.00 15.15 ? 559  HIS   A CG  1 
ATOM   3989 N  ND1 . HIS   A 1 536 ? -34.670 20.670  5.486   1.00 16.84 ? 559  HIS   A ND1 1 
ATOM   3990 C  CD2 . HIS   A 1 536 ? -32.791 21.484  4.714   1.00 16.42 ? 559  HIS   A CD2 1 
ATOM   3991 C  CE1 . HIS   A 1 536 ? -34.957 21.796  4.856   1.00 16.58 ? 559  HIS   A CE1 1 
ATOM   3992 N  NE2 . HIS   A 1 536 ? -33.838 22.302  4.398   1.00 16.56 ? 559  HIS   A NE2 1 
ATOM   3993 N  N   . LEU   A 1 537 ? -31.798 16.572  7.310   1.00 12.61 ? 560  LEU   A N   1 
ATOM   3994 C  CA  . LEU   A 1 537 ? -30.732 15.704  7.811   1.00 11.26 ? 560  LEU   A CA  1 
ATOM   3995 C  C   . LEU   A 1 537 ? -30.686 14.403  7.010   1.00 11.73 ? 560  LEU   A C   1 
ATOM   3996 O  O   . LEU   A 1 537 ? -29.619 13.898  6.644   1.00 12.14 ? 560  LEU   A O   1 
ATOM   3997 C  CB  . LEU   A 1 537 ? -31.023 15.401  9.281   1.00 11.72 ? 560  LEU   A CB  1 
ATOM   3998 C  CG  . LEU   A 1 537 ? -30.107 14.394  9.987   1.00 10.94 ? 560  LEU   A CG  1 
ATOM   3999 C  CD1 . LEU   A 1 537 ? -28.728 14.964  10.038  1.00 11.50 ? 560  LEU   A CD1 1 
ATOM   4000 C  CD2 . LEU   A 1 537 ? -30.564 14.024  11.399  1.00 12.67 ? 560  LEU   A CD2 1 
ATOM   4001 N  N   . ASN   A 1 538 ? -31.864 13.815  6.790   1.00 11.72 ? 561  ASN   A N   1 
ATOM   4002 C  CA  . ASN   A 1 538 ? -31.937 12.535  6.112   1.00 12.27 ? 561  ASN   A CA  1 
ATOM   4003 C  C   . ASN   A 1 538 ? -31.454 12.637  4.672   1.00 12.08 ? 561  ASN   A C   1 
ATOM   4004 O  O   . ASN   A 1 538 ? -30.631 11.836  4.230   1.00 11.72 ? 561  ASN   A O   1 
ATOM   4005 C  CB  . ASN   A 1 538 ? -33.338 11.949  6.211   1.00 13.40 ? 561  ASN   A CB  1 
ATOM   4006 C  CG  . ASN   A 1 538 ? -33.559 11.310  7.566   1.00 16.12 ? 561  ASN   A CG  1 
ATOM   4007 O  OD1 . ASN   A 1 538 ? -33.091 10.209  7.812   1.00 15.07 ? 561  ASN   A OD1 1 
ATOM   4008 N  ND2 . ASN   A 1 538 ? -34.234 11.985  8.477   1.00 20.57 ? 561  ASN   A ND2 1 
ATOM   4009 N  N   . ASN   A 1 539 ? -31.947 13.625  3.927   1.00 12.73 ? 562  ASN   A N   1 
ATOM   4010 C  CA  . ASN   A 1 539 ? -31.494 13.807  2.556   1.00 12.25 ? 562  ASN   A CA  1 
ATOM   4011 C  C   . ASN   A 1 539 ? -29.985 14.040  2.477   1.00 11.34 ? 562  ASN   A C   1 
ATOM   4012 O  O   . ASN   A 1 539 ? -29.313 13.550  1.564   1.00 11.75 ? 562  ASN   A O   1 
ATOM   4013 C  CB  . ASN   A 1 539 ? -32.260 14.934  1.865   1.00 12.09 ? 562  ASN   A CB  1 
ATOM   4014 C  CG  . ASN   A 1 539 ? -33.679 14.535  1.564   1.00 13.07 ? 562  ASN   A CG  1 
ATOM   4015 O  OD1 . ASN   A 1 539 ? -33.985 13.359  1.335   1.00 13.93 ? 562  ASN   A OD1 1 
ATOM   4016 N  ND2 . ASN   A 1 539 ? -34.578 15.511  1.514   1.00 14.91 ? 562  ASN   A ND2 1 
ATOM   4017 N  N   . ARG   A 1 540 ? -29.464 14.881  3.367   1.00 11.44 ? 563  ARG   A N   1 
ATOM   4018 C  CA  . ARG   A 1 540 ? -28.077 15.292  3.322   1.00 10.24 ? 563  ARG   A CA  1 
ATOM   4019 C  C   . ARG   A 1 540 ? -27.195 14.093  3.678   1.00 11.06 ? 563  ARG   A C   1 
ATOM   4020 O  O   . ARG   A 1 540 ? -26.221 13.832  2.988   1.00 11.95 ? 563  ARG   A O   1 
ATOM   4021 C  CB  . ARG   A 1 540 ? -27.903 16.438  4.317   1.00 10.27 ? 563  ARG   A CB  1 
ATOM   4022 C  CG  . ARG   A 1 540 ? -26.549 17.114  4.312   1.00 10.55 ? 563  ARG   A CG  1 
ATOM   4023 C  CD  . ARG   A 1 540 ? -26.292 17.867  3.017   1.00 10.67 ? 563  ARG   A CD  1 
ATOM   4024 N  NE  . ARG   A 1 540 ? -25.148 18.760  3.206   1.00 11.47 ? 563  ARG   A NE  1 
ATOM   4025 C  CZ  . ARG   A 1 540 ? -23.909 18.574  2.758   1.00 12.23 ? 563  ARG   A CZ  1 
ATOM   4026 N  NH1 . ARG   A 1 540 ? -23.634 17.534  2.000   1.00 12.50 ? 563  ARG   A NH1 1 
ATOM   4027 N  NH2 . ARG   A 1 540 ? -22.952 19.443  3.043   1.00 12.94 ? 563  ARG   A NH2 1 
ATOM   4028 N  N   . PHE   A 1 541 ? -27.597 13.334  4.703   1.00 10.55 ? 564  PHE   A N   1 
ATOM   4029 C  CA  . PHE   A 1 541 ? -26.853 12.147  5.101   1.00 11.34 ? 564  PHE   A CA  1 
ATOM   4030 C  C   . PHE   A 1 541 ? -26.799 11.149  3.946   1.00 11.47 ? 564  PHE   A C   1 
ATOM   4031 O  O   . PHE   A 1 541 ? -25.719 10.675  3.582   1.00 11.77 ? 564  PHE   A O   1 
ATOM   4032 C  CB  . PHE   A 1 541 ? -27.450 11.526  6.367   1.00 11.75 ? 564  PHE   A CB  1 
ATOM   4033 C  CG  . PHE   A 1 541 ? -26.713 10.241  6.679   1.00 11.61 ? 564  PHE   A CG  1 
ATOM   4034 C  CD1 . PHE   A 1 541 ? -27.079 9.040   6.073   1.00 10.91 ? 564  PHE   A CD1 1 
ATOM   4035 C  CD2 . PHE   A 1 541 ? -25.612 10.263  7.537   1.00 11.80 ? 564  PHE   A CD2 1 
ATOM   4036 C  CE1 . PHE   A 1 541 ? -26.352 7.890   6.300   1.00 11.85 ? 564  PHE   A CE1 1 
ATOM   4037 C  CE2 . PHE   A 1 541 ? -24.886 9.100   7.761   1.00 11.63 ? 564  PHE   A CE2 1 
ATOM   4038 C  CZ  . PHE   A 1 541 ? -25.260 7.916   7.152   1.00 11.30 ? 564  PHE   A CZ  1 
ATOM   4039 N  N   . VAL   A 1 542 ? -27.951 10.838  3.326   1.00 10.95 ? 565  VAL   A N   1 
ATOM   4040 C  CA  . VAL   A 1 542 ? -27.967 9.789   2.321   1.00 11.13 ? 565  VAL   A CA  1 
ATOM   4041 C  C   . VAL   A 1 542 ? -27.168 10.266  1.101   1.00 10.98 ? 565  VAL   A C   1 
ATOM   4042 O  O   . VAL   A 1 542 ? -26.466 9.466   0.471   1.00 11.71 ? 565  VAL   A O   1 
ATOM   4043 C  CB  . VAL   A 1 542 ? -29.418 9.379   2.008   1.00 11.62 ? 565  VAL   A CB  1 
ATOM   4044 C  CG1 . VAL   A 1 542 ? -29.553 8.529   0.751   1.00 12.84 ? 565  VAL   A CG1 1 
ATOM   4045 C  CG2 . VAL   A 1 542 ? -30.042 8.600   3.157   1.00 11.70 ? 565  VAL   A CG2 1 
ATOM   4046 N  N   . GLY   A 1 543 ? -27.189 11.580  0.827   1.00 10.69 ? 566  GLY   A N   1 
ATOM   4047 C  CA  . GLY   A 1 543 ? -26.390 12.149  -0.262  1.00 10.48 ? 566  GLY   A CA  1 
ATOM   4048 C  C   . GLY   A 1 543 ? -24.878 11.949  -0.078  1.00 10.60 ? 566  GLY   A C   1 
ATOM   4049 O  O   . GLY   A 1 543 ? -24.155 11.817  -1.050  1.00 11.04 ? 566  GLY   A O   1 
ATOM   4050 N  N   . LEU   A 1 544 ? -24.392 11.984  1.177   1.00 10.22 ? 567  LEU   A N   1 
ATOM   4051 C  CA  . LEU   A 1 544 ? -22.988 11.733  1.464   1.00 9.77  ? 567  LEU   A CA  1 
ATOM   4052 C  C   . LEU   A 1 544 ? -22.600 10.287  1.138   1.00 10.12 ? 567  LEU   A C   1 
ATOM   4053 O  O   . LEU   A 1 544 ? -21.585 10.046  0.477   1.00 10.07 ? 567  LEU   A O   1 
ATOM   4054 C  CB  . LEU   A 1 544 ? -22.735 12.086  2.924   1.00 10.40 ? 567  LEU   A CB  1 
ATOM   4055 C  CG  . LEU   A 1 544 ? -22.641 13.579  3.250   1.00 10.86 ? 567  LEU   A CG  1 
ATOM   4056 C  CD1 . LEU   A 1 544 ? -22.685 13.776  4.742   1.00 10.61 ? 567  LEU   A CD1 1 
ATOM   4057 C  CD2 . LEU   A 1 544 ? -21.416 14.233  2.697   1.00 12.28 ? 567  LEU   A CD2 1 
ATOM   4058 N  N   . ILE   A 1 545 ? -23.407 9.332   1.604   1.00 9.27  ? 568  ILE   A N   1 
ATOM   4059 C  CA  . ILE   A 1 545 ? -23.198 7.906   1.338   1.00 10.90 ? 568  ILE   A CA  1 
ATOM   4060 C  C   . ILE   A 1 545 ? -23.306 7.589   -0.169  1.00 11.06 ? 568  ILE   A C   1 
ATOM   4061 O  O   . ILE   A 1 545 ? -22.470 6.903   -0.745  1.00 10.35 ? 568  ILE   A O   1 
ATOM   4062 C  CB  . ILE   A 1 545 ? -24.170 7.044   2.164   1.00 10.92 ? 568  ILE   A CB  1 
ATOM   4063 C  CG1 . ILE   A 1 545 ? -24.075 7.322   3.673   1.00 11.73 ? 568  ILE   A CG1 1 
ATOM   4064 C  CG2 . ILE   A 1 545 ? -23.939 5.558   1.887   1.00 11.84 ? 568  ILE   A CG2 1 
ATOM   4065 C  CD1 . ILE   A 1 545 ? -22.673 7.241   4.248   1.00 12.71 ? 568  ILE   A CD1 1 
ATOM   4066 N  N   . ASP   A 1 546 ? -24.274 8.189   -0.862  1.00 11.86 ? 569  ASP   A N   1 
ATOM   4067 C  CA  . ASP   A 1 546 ? -24.370 8.000   -2.307  1.00 11.88 ? 569  ASP   A CA  1 
ATOM   4068 C  C   . ASP   A 1 546 ? -23.147 8.556   -3.049  1.00 12.11 ? 569  ASP   A C   1 
ATOM   4069 O  O   . ASP   A 1 546 ? -22.721 7.968   -4.057  1.00 12.01 ? 569  ASP   A O   1 
ATOM   4070 C  CB  . ASP   A 1 546 ? -25.714 8.540   -2.801  1.00 12.38 ? 569  ASP   A CB  1 
ATOM   4071 C  CG  . ASP   A 1 546 ? -26.937 7.701   -2.418  1.00 13.42 ? 569  ASP   A CG  1 
ATOM   4072 O  OD1 . ASP   A 1 546 ? -26.804 6.471   -2.356  1.00 13.96 ? 569  ASP   A OD1 1 
ATOM   4073 O  OD2 . ASP   A 1 546 ? -28.055 8.266   -2.264  1.00 13.08 ? 569  ASP   A OD2 1 
ATOM   4074 N  N   . ALA   A 1 547 ? -22.588 9.694   -2.589  1.00 11.11 ? 570  ALA   A N   1 
ATOM   4075 C  CA  . ALA   A 1 547 ? -21.362 10.270  -3.131  1.00 11.67 ? 570  ALA   A CA  1 
ATOM   4076 C  C   . ALA   A 1 547 ? -20.203 9.289   -3.002  1.00 11.12 ? 570  ALA   A C   1 
ATOM   4077 O  O   . ALA   A 1 547 ? -19.410 9.099   -3.929  1.00 11.28 ? 570  ALA   A O   1 
ATOM   4078 C  CB  . ALA   A 1 547 ? -21.050 11.594  -2.469  1.00 11.99 ? 570  ALA   A CB  1 
ATOM   4079 N  N   . ILE   A 1 548 ? -20.067 8.709   -1.814  1.00 11.26 ? 571  ILE   A N   1 
ATOM   4080 C  CA  . ILE   A 1 548 ? -19.018 7.734   -1.567  1.00 10.77 ? 571  ILE   A CA  1 
ATOM   4081 C  C   . ILE   A 1 548 ? -19.214 6.548   -2.498  1.00 11.39 ? 571  ILE   A C   1 
ATOM   4082 O  O   . ILE   A 1 548 ? -18.242 6.096   -3.098  1.00 11.65 ? 571  ILE   A O   1 
ATOM   4083 C  CB  . ILE   A 1 548 ? -18.996 7.390   -0.067  1.00 11.19 ? 571  ILE   A CB  1 
ATOM   4084 C  CG1 . ILE   A 1 548 ? -18.542 8.600   0.719   1.00 11.51 ? 571  ILE   A CG1 1 
ATOM   4085 C  CG2 . ILE   A 1 548 ? -18.127 6.170   0.235   1.00 12.13 ? 571  ILE   A CG2 1 
ATOM   4086 C  CD1 . ILE   A 1 548 ? -18.710 8.462   2.218   1.00 11.54 ? 571  ILE   A CD1 1 
ATOM   4087 N  N   . ARG   A 1 549 ? -20.440 6.033   -2.600  1.00 11.54 ? 572  ARG   A N   1 
ATOM   4088 C  CA  . ARG   A 1 549 ? -20.706 4.870   -3.422  1.00 11.94 ? 572  ARG   A CA  1 
ATOM   4089 C  C   . ARG   A 1 549 ? -20.393 5.137   -4.896  1.00 13.09 ? 572  ARG   A C   1 
ATOM   4090 O  O   . ARG   A 1 549 ? -19.734 4.311   -5.528  1.00 15.03 ? 572  ARG   A O   1 
ATOM   4091 C  CB  . ARG   A 1 549 ? -22.125 4.329   -3.247  1.00 12.12 ? 572  ARG   A CB  1 
ATOM   4092 C  CG  . ARG   A 1 549 ? -22.471 3.192   -4.202  1.00 12.52 ? 572  ARG   A CG  1 
ATOM   4093 C  CD  . ARG   A 1 549 ? -23.839 2.629   -3.966  1.00 12.85 ? 572  ARG   A CD  1 
ATOM   4094 N  NE  . ARG   A 1 549 ? -24.885 3.643   -3.958  1.00 13.97 ? 572  ARG   A NE  1 
ATOM   4095 C  CZ  . ARG   A 1 549 ? -25.405 4.220   -5.036  1.00 17.22 ? 572  ARG   A CZ  1 
ATOM   4096 N  NH1 . ARG   A 1 549 ? -25.100 3.765   -6.245  1.00 17.54 ? 572  ARG   A NH1 1 
ATOM   4097 N  NH2 . ARG   A 1 549 ? -26.239 5.231   -4.900  1.00 18.59 ? 572  ARG   A NH2 1 
ATOM   4098 N  N   . GLU   A 1 550 ? -20.929 6.223   -5.442  1.00 12.25 ? 573  GLU   A N   1 
ATOM   4099 C  CA  . GLU   A 1 550 ? -20.888 6.441   -6.881  1.00 13.35 ? 573  GLU   A CA  1 
ATOM   4100 C  C   . GLU   A 1 550 ? -19.581 7.067   -7.356  1.00 14.24 ? 573  GLU   A C   1 
ATOM   4101 O  O   . GLU   A 1 550 ? -19.174 6.794   -8.492  1.00 16.15 ? 573  GLU   A O   1 
ATOM   4102 C  CB  . GLU   A 1 550 ? -22.085 7.318   -7.261  1.00 14.66 ? 573  GLU   A CB  1 
ATOM   4103 C  CG  . GLU   A 1 550 ? -23.406 6.573   -7.113  1.00 17.27 ? 573  GLU   A CG  1 
ATOM   4104 C  CD  . GLU   A 1 550 ? -24.608 7.052   -7.940  1.00 19.34 ? 573  GLU   A CD  1 
ATOM   4105 O  OE1 . GLU   A 1 550 ? -24.426 7.954   -8.788  1.00 24.22 ? 573  GLU   A OE1 1 
ATOM   4106 O  OE2 . GLU   A 1 550 ? -25.701 6.474   -7.763  1.00 24.07 ? 573  GLU   A OE2 1 
ATOM   4107 N  N   . VAL   A 1 551 ? -18.918 7.895   -6.538  1.00 15.17 ? 574  VAL   A N   1 
ATOM   4108 C  CA  . VAL   A 1 551 ? -17.713 8.561   -7.007  1.00 16.31 ? 574  VAL   A CA  1 
ATOM   4109 C  C   . VAL   A 1 551 ? -16.455 8.188   -6.227  1.00 16.60 ? 574  VAL   A C   1 
ATOM   4110 O  O   . VAL   A 1 551 ? -15.434 7.866   -6.843  1.00 16.30 ? 574  VAL   A O   1 
ATOM   4111 C  CB  . VAL   A 1 551 ? -17.943 10.076  -7.039  1.00 18.47 ? 574  VAL   A CB  1 
ATOM   4112 C  CG1 . VAL   A 1 551 ? -16.674 10.812  -7.461  1.00 19.03 ? 574  VAL   A CG1 1 
ATOM   4113 C  CG2 . VAL   A 1 551 ? -19.102 10.404  -7.992  1.00 19.47 ? 574  VAL   A CG2 1 
ATOM   4114 N  N   . ARG   A 1 552 ? -16.454 8.333   -4.886  1.00 12.86 ? 575  ARG   A N   1 
ATOM   4115 C  CA  . ARG   A 1 552 ? -15.191 8.240   -4.177  1.00 13.47 ? 575  ARG   A CA  1 
ATOM   4116 C  C   . ARG   A 1 552 ? -14.707 6.790   -4.088  1.00 12.64 ? 575  ARG   A C   1 
ATOM   4117 O  O   . ARG   A 1 552 ? -13.521 6.538   -4.280  1.00 12.27 ? 575  ARG   A O   1 
ATOM   4118 C  CB  . ARG   A 1 552 ? -15.262 8.868   -2.778  1.00 15.15 ? 575  ARG   A CB  1 
ATOM   4119 C  CG  . ARG   A 1 552 ? -15.706 10.324  -2.771  1.00 16.82 ? 575  ARG   A CG  1 
ATOM   4120 C  CD  . ARG   A 1 552 ? -14.954 11.169  -3.780  1.00 17.76 ? 575  ARG   A CD  1 
ATOM   4121 N  NE  . ARG   A 1 552 ? -13.500 10.958  -3.818  1.00 19.66 ? 575  ARG   A NE  1 
ATOM   4122 C  CZ  . ARG   A 1 552 ? -12.769 11.224  -4.879  1.00 25.06 ? 575  ARG   A CZ  1 
ATOM   4123 N  NH1 . ARG   A 1 552 ? -11.520 10.800  -4.967  1.00 24.28 ? 575  ARG   A NH1 1 
ATOM   4124 N  NH2 . ARG   A 1 552 ? -13.329 11.896  -5.876  1.00 30.66 ? 575  ARG   A NH2 1 
ATOM   4125 N  N   . MET   A 1 553 ? -15.591 5.826   -3.819  1.00 12.46 ? 576  MET   A N   1 
ATOM   4126 C  CA  A MET   A 1 553 ? -15.136 4.456   -3.652  0.50 13.97 ? 576  MET   A CA  1 
ATOM   4127 C  CA  B MET   A 1 553 ? -15.161 4.442   -3.650  0.50 11.62 ? 576  MET   A CA  1 
ATOM   4128 C  C   . MET   A 1 553 ? -14.556 3.911   -4.958  1.00 14.14 ? 576  MET   A C   1 
ATOM   4129 O  O   . MET   A 1 553 ? -13.470 3.324   -4.970  1.00 13.50 ? 576  MET   A O   1 
ATOM   4130 C  CB  A MET   A 1 553 ? -16.239 3.520   -3.166  0.50 16.85 ? 576  MET   A CB  1 
ATOM   4131 C  CB  B MET   A 1 553 ? -16.304 3.572   -3.108  0.50 10.80 ? 576  MET   A CB  1 
ATOM   4132 C  CG  A MET   A 1 553 ? -15.776 2.075   -3.159  0.50 18.78 ? 576  MET   A CG  1 
ATOM   4133 C  CG  B MET   A 1 553 ? -15.944 2.093   -2.891  0.50 9.53  ? 576  MET   A CG  1 
ATOM   4134 S  SD  A MET   A 1 553 ? -17.103 0.965   -2.680  0.50 24.18 ? 576  MET   A SD  1 
ATOM   4135 S  SD  B MET   A 1 553 ? -16.252 1.116   -4.377  0.50 7.95  ? 576  MET   A SD  1 
ATOM   4136 C  CE  A MET   A 1 553 ? -18.383 1.256   -3.910  0.50 22.64 ? 576  MET   A CE  1 
ATOM   4137 C  CE  B MET   A 1 553 ? -18.049 1.188   -4.392  0.50 8.32  ? 576  MET   A CE  1 
ATOM   4138 N  N   . PRO   A 1 554 ? -15.197 4.093   -6.118  1.00 15.77 ? 577  PRO   A N   1 
ATOM   4139 C  CA  . PRO   A 1 554 ? -14.577 3.633   -7.362  1.00 16.03 ? 577  PRO   A CA  1 
ATOM   4140 C  C   . PRO   A 1 554 ? -13.232 4.300   -7.681  1.00 16.72 ? 577  PRO   A C   1 
ATOM   4141 O  O   . PRO   A 1 554 ? -12.385 3.689   -8.335  1.00 16.69 ? 577  PRO   A O   1 
ATOM   4142 C  CB  . PRO   A 1 554 ? -15.666 3.942   -8.378  1.00 16.11 ? 577  PRO   A CB  1 
ATOM   4143 C  CG  . PRO   A 1 554 ? -16.941 3.887   -7.572  1.00 16.38 ? 577  PRO   A CG  1 
ATOM   4144 C  CD  . PRO   A 1 554 ? -16.552 4.646   -6.326  1.00 15.60 ? 577  PRO   A CD  1 
ATOM   4145 N  N   . ARG   A 1 555 ? -12.997 5.510   -7.156  1.00 15.31 ? 578  ARG   A N   1 
ATOM   4146 C  CA  . ARG   A 1 555 ? -11.747 6.217   -7.340  1.00 16.55 ? 578  ARG   A CA  1 
ATOM   4147 C  C   . ARG   A 1 555 ? -10.717 5.889   -6.259  1.00 14.76 ? 578  ARG   A C   1 
ATOM   4148 O  O   . ARG   A 1 555 ? -9.647  6.477   -6.249  1.00 17.25 ? 578  ARG   A O   1 
ATOM   4149 C  CB  . ARG   A 1 555 ? -11.977 7.730   -7.365  1.00 19.18 ? 578  ARG   A CB  1 
ATOM   4150 C  CG  . ARG   A 1 555 ? -12.538 8.106   -8.725  1.00 24.72 ? 578  ARG   A CG  1 
ATOM   4151 C  CD  . ARG   A 1 555 ? -12.831 9.582   -8.931  1.00 28.46 ? 578  ARG   A CD  1 
ATOM   4152 N  NE  . ARG   A 1 555 ? -13.499 9.753   -10.230 1.00 34.75 ? 578  ARG   A NE  1 
ATOM   4153 C  CZ  . ARG   A 1 555 ? -14.674 9.197   -10.553 1.00 39.53 ? 578  ARG   A CZ  1 
ATOM   4154 N  NH1 . ARG   A 1 555 ? -15.395 8.577   -9.637  1.00 44.07 ? 578  ARG   A NH1 1 
ATOM   4155 N  NH2 . ARG   A 1 555 ? -15.165 9.276   -11.777 1.00 39.41 ? 578  ARG   A NH2 1 
ATOM   4156 N  N   . GLY   A 1 556 ? -11.007 4.956   -5.342  1.00 12.19 ? 579  GLY   A N   1 
ATOM   4157 C  CA  . GLY   A 1 556 ? -9.982  4.477   -4.435  1.00 11.17 ? 579  GLY   A CA  1 
ATOM   4158 C  C   . GLY   A 1 556 ? -10.288 4.660   -2.955  1.00 10.92 ? 579  GLY   A C   1 
ATOM   4159 O  O   . GLY   A 1 556 ? -9.512  4.203   -2.115  1.00 10.85 ? 579  GLY   A O   1 
ATOM   4160 N  N   . LEU   A 1 557 ? -11.402 5.317   -2.605  1.00 10.55 ? 580  LEU   A N   1 
ATOM   4161 C  CA  . LEU   A 1 557 ? -11.735 5.380   -1.184  1.00 10.23 ? 580  LEU   A CA  1 
ATOM   4162 C  C   . LEU   A 1 557 ? -12.219 4.013   -0.696  1.00 10.35 ? 580  LEU   A C   1 
ATOM   4163 O  O   . LEU   A 1 557 ? -13.089 3.391   -1.309  1.00 11.04 ? 580  LEU   A O   1 
ATOM   4164 C  CB  . LEU   A 1 557 ? -12.800 6.436   -0.956  1.00 10.74 ? 580  LEU   A CB  1 
ATOM   4165 C  CG  . LEU   A 1 557 ? -13.026 6.764   0.512   1.00 10.32 ? 580  LEU   A CG  1 
ATOM   4166 C  CD1 . LEU   A 1 557 ? -11.786 7.441   1.082   1.00 9.78  ? 580  LEU   A CD1 1 
ATOM   4167 C  CD2 . LEU   A 1 557 ? -14.254 7.656   0.646   1.00 10.90 ? 580  LEU   A CD2 1 
ATOM   4168 N  N   . SER   A 1 558 ? -11.700 3.580   0.468   1.00 9.32  ? 581  SER   A N   1 
ATOM   4169 C  CA  . SER   A 1 558 ? -11.981 2.248   0.949   1.00 9.21  ? 581  SER   A CA  1 
ATOM   4170 C  C   . SER   A 1 558 ? -12.709 2.203   2.284   1.00 8.78  ? 581  SER   A C   1 
ATOM   4171 O  O   . SER   A 1 558 ? -13.163 1.122   2.666   1.00 9.01  ? 581  SER   A O   1 
ATOM   4172 C  CB  . SER   A 1 558 ? -10.697 1.447   1.104   1.00 9.21  ? 581  SER   A CB  1 
ATOM   4173 O  OG  . SER   A 1 558 ? -10.170 1.100   -0.168  1.00 10.75 ? 581  SER   A OG  1 
ATOM   4174 N  N   . ALA   A 1 559 ? -12.761 3.329   2.988   1.00 8.83  ? 582  ALA   A N   1 
ATOM   4175 C  CA  . ALA   A 1 559 ? -13.499 3.379   4.237   1.00 8.80  ? 582  ALA   A CA  1 
ATOM   4176 C  C   . ALA   A 1 559 ? -13.911 4.814   4.555   1.00 8.51  ? 582  ALA   A C   1 
ATOM   4177 O  O   . ALA   A 1 559 ? -13.246 5.762   4.163   1.00 9.49  ? 582  ALA   A O   1 
ATOM   4178 C  CB  . ALA   A 1 559 ? -12.648 2.834   5.357   1.00 8.55  ? 582  ALA   A CB  1 
ATOM   4179 N  N   . SER   A 1 560 ? -14.953 4.962   5.371   1.00 8.71  ? 583  SER   A N   1 
ATOM   4180 C  CA  . SER   A 1 560 ? -15.406 6.269   5.822   1.00 8.78  ? 583  SER   A CA  1 
ATOM   4181 C  C   . SER   A 1 560 ? -15.953 6.145   7.237   1.00 8.60  ? 583  SER   A C   1 
ATOM   4182 O  O   . SER   A 1 560 ? -16.543 5.129   7.579   1.00 8.70  ? 583  SER   A O   1 
ATOM   4183 C  CB  . SER   A 1 560 ? -16.441 6.837   4.881   1.00 9.08  ? 583  SER   A CB  1 
ATOM   4184 O  OG  . SER   A 1 560 ? -17.553 5.968   4.755   1.00 9.33  ? 583  SER   A OG  1 
ATOM   4185 N  N   . VAL   A 1 561 ? -15.740 7.194   8.028   1.00 8.50  ? 584  VAL   A N   1 
ATOM   4186 C  CA  . VAL   A 1 561 ? -16.154 7.228   9.414   1.00 8.00  ? 584  VAL   A CA  1 
ATOM   4187 C  C   . VAL   A 1 561 ? -17.057 8.449   9.602   1.00 7.94  ? 584  VAL   A C   1 
ATOM   4188 O  O   . VAL   A 1 561 ? -16.571 9.586   9.642   1.00 7.52  ? 584  VAL   A O   1 
ATOM   4189 C  CB  . VAL   A 1 561 ? -14.924 7.304   10.329  1.00 8.33  ? 584  VAL   A CB  1 
ATOM   4190 C  CG1 . VAL   A 1 561 ? -15.323 7.535   11.773  1.00 8.34  ? 584  VAL   A CG1 1 
ATOM   4191 C  CG2 . VAL   A 1 561 ? -13.999 6.102   10.158  1.00 8.64  ? 584  VAL   A CG2 1 
ATOM   4192 N  N   . TYR   A 1 562 ? -18.349 8.203   9.746   1.00 8.07  ? 585  TYR   A N   1 
ATOM   4193 C  CA  . TYR   A 1 562 ? -19.337 9.277   9.860   1.00 8.34  ? 585  TYR   A CA  1 
ATOM   4194 C  C   . TYR   A 1 562 ? -19.418 9.764   11.316  1.00 8.68  ? 585  TYR   A C   1 
ATOM   4195 O  O   . TYR   A 1 562 ? -19.747 9.001   12.227  1.00 8.46  ? 585  TYR   A O   1 
ATOM   4196 C  CB  . TYR   A 1 562 ? -20.703 8.822   9.371   1.00 8.72  ? 585  TYR   A CB  1 
ATOM   4197 C  CG  . TYR   A 1 562 ? -21.702 9.958   9.505   1.00 9.02  ? 585  TYR   A CG  1 
ATOM   4198 C  CD1 . TYR   A 1 562 ? -21.828 10.905  8.494   1.00 9.26  ? 585  TYR   A CD1 1 
ATOM   4199 C  CD2 . TYR   A 1 562 ? -22.462 10.115  10.664  1.00 8.61  ? 585  TYR   A CD2 1 
ATOM   4200 C  CE1 . TYR   A 1 562 ? -22.729 11.946  8.601   1.00 8.84  ? 585  TYR   A CE1 1 
ATOM   4201 C  CE2 . TYR   A 1 562 ? -23.352 11.172  10.788  1.00 8.83  ? 585  TYR   A CE2 1 
ATOM   4202 C  CZ  . TYR   A 1 562 ? -23.427 12.116  9.781   1.00 8.77  ? 585  TYR   A CZ  1 
ATOM   4203 O  OH  . TYR   A 1 562 ? -24.276 13.159  9.926   1.00 10.36 ? 585  TYR   A OH  1 
ATOM   4204 N  N   . THR   A 1 563 ? -19.213 11.074  11.505  1.00 8.17  ? 586  THR   A N   1 
ATOM   4205 C  CA  . THR   A 1 563 ? -19.325 11.719  12.809  1.00 8.20  ? 586  THR   A CA  1 
ATOM   4206 C  C   . THR   A 1 563 ? -20.786 12.102  13.014  1.00 9.38  ? 586  THR   A C   1 
ATOM   4207 O  O   . THR   A 1 563 ? -21.264 12.981  12.297  1.00 9.99  ? 586  THR   A O   1 
ATOM   4208 C  CB  . THR   A 1 563 ? -18.412 12.939  12.840  1.00 8.18  ? 586  THR   A CB  1 
ATOM   4209 O  OG1 . THR   A 1 563 ? -17.085 12.485  12.633  1.00 8.85  ? 586  THR   A OG1 1 
ATOM   4210 C  CG2 . THR   A 1 563 ? -18.472 13.718  14.142  1.00 7.86  ? 586  THR   A CG2 1 
ATOM   4211 N  N   . GLU   A 1 564 ? -21.534 11.432  13.913  1.00 8.06  ? 587  GLU   A N   1 
ATOM   4212 C  CA  . GLU   A 1 564 ? -21.081 10.390  14.825  1.00 7.75  ? 587  GLU   A CA  1 
ATOM   4213 C  C   . GLU   A 1 564 ? -22.325 9.593   15.250  1.00 7.64  ? 587  GLU   A C   1 
ATOM   4214 O  O   . GLU   A 1 564 ? -23.466 9.942   14.908  1.00 8.09  ? 587  GLU   A O   1 
ATOM   4215 C  CB  . GLU   A 1 564 ? -20.344 10.988  16.035  1.00 8.11  ? 587  GLU   A CB  1 
ATOM   4216 C  CG  . GLU   A 1 564 ? -21.203 11.963  16.831  1.00 8.52  ? 587  GLU   A CG  1 
ATOM   4217 C  CD  . GLU   A 1 564 ? -20.496 12.574  18.023  1.00 9.21  ? 587  GLU   A CD  1 
ATOM   4218 O  OE1 . GLU   A 1 564 ? -20.484 13.858  18.182  1.00 9.60  ? 587  GLU   A OE1 1 
ATOM   4219 O  OE2 . GLU   A 1 564 ? -19.938 11.770  18.797  1.00 9.06  ? 587  GLU   A OE2 1 
ATOM   4220 N  N   . ILE   A 1 565 ? -22.121 8.508   16.021  1.00 7.32  ? 588  ILE   A N   1 
ATOM   4221 C  CA  . ILE   A 1 565 ? -23.247 7.665   16.359  1.00 8.01  ? 588  ILE   A CA  1 
ATOM   4222 C  C   . ILE   A 1 565 ? -24.219 8.426   17.264  1.00 8.35  ? 588  ILE   A C   1 
ATOM   4223 O  O   . ILE   A 1 565 ? -25.428 8.356   17.030  1.00 8.11  ? 588  ILE   A O   1 
ATOM   4224 C  CB  . ILE   A 1 565 ? -22.820 6.285   16.901  1.00 7.91  ? 588  ILE   A CB  1 
ATOM   4225 C  CG1 . ILE   A 1 565 ? -24.019 5.328   17.028  1.00 8.80  ? 588  ILE   A CG1 1 
ATOM   4226 C  CG2 . ILE   A 1 565 ? -22.082 6.387   18.245  1.00 7.45  ? 588  ILE   A CG2 1 
ATOM   4227 C  CD1 . ILE   A 1 565 ? -24.706 4.965   15.746  1.00 9.22  ? 588  ILE   A CD1 1 
ATOM   4228 N  N   . THR   A 1 566 ? -23.752 9.096   18.333  1.00 8.42  ? 589  THR   A N   1 
ATOM   4229 C  CA  . THR   A 1 566 ? -24.687 9.819   19.208  1.00 8.42  ? 589  THR   A CA  1 
ATOM   4230 C  C   . THR   A 1 566 ? -24.259 11.262  19.357  1.00 8.31  ? 589  THR   A C   1 
ATOM   4231 O  O   . THR   A 1 566 ? -23.084 11.557  19.284  1.00 8.94  ? 589  THR   A O   1 
ATOM   4232 C  CB  . THR   A 1 566 ? -24.817 9.224   20.630  1.00 8.49  ? 589  THR   A CB  1 
ATOM   4233 O  OG1 . THR   A 1 566 ? -23.653 9.496   21.406  1.00 10.42 ? 589  THR   A OG1 1 
ATOM   4234 C  CG2 . THR   A 1 566 ? -25.077 7.728   20.631  1.00 8.76  ? 589  THR   A CG2 1 
ATOM   4235 N  N   . ASP   A 1 567 ? -25.216 12.152  19.655  1.00 8.92  ? 590  ASP   A N   1 
ATOM   4236 C  CA  . ASP   A 1 567 ? -24.830 13.435  20.213  1.00 8.53  ? 590  ASP   A CA  1 
ATOM   4237 C  C   . ASP   A 1 567 ? -23.949 13.189  21.426  1.00 9.03  ? 590  ASP   A C   1 
ATOM   4238 O  O   . ASP   A 1 567 ? -24.149 12.196  22.102  1.00 9.18  ? 590  ASP   A O   1 
ATOM   4239 C  CB  . ASP   A 1 567 ? -26.033 14.245  20.635  1.00 8.82  ? 590  ASP   A CB  1 
ATOM   4240 C  CG  . ASP   A 1 567 ? -27.007 14.620  19.524  1.00 8.68  ? 590  ASP   A CG  1 
ATOM   4241 O  OD1 . ASP   A 1 567 ? -26.599 14.596  18.307  1.00 8.87  ? 590  ASP   A OD1 1 
ATOM   4242 O  OD2 . ASP   A 1 567 ? -28.160 14.972  19.876  1.00 10.09 ? 590  ASP   A OD2 1 
ATOM   4243 N  N   . VAL   A 1 568 ? -23.010 14.092  21.690  1.00 8.61  ? 591  VAL   A N   1 
ATOM   4244 C  CA  . VAL   A 1 568 ? -22.252 14.074  22.935  1.00 9.08  ? 591  VAL   A CA  1 
ATOM   4245 C  C   . VAL   A 1 568 ? -22.219 15.495  23.478  1.00 9.05  ? 591  VAL   A C   1 
ATOM   4246 O  O   . VAL   A 1 568 ? -21.722 16.390  22.811  1.00 9.36  ? 591  VAL   A O   1 
ATOM   4247 C  CB  . VAL   A 1 568 ? -20.806 13.558  22.785  1.00 9.62  ? 591  VAL   A CB  1 
ATOM   4248 C  CG1 . VAL   A 1 568 ? -20.049 13.613  24.128  1.00 9.45  ? 591  VAL   A CG1 1 
ATOM   4249 C  CG2 . VAL   A 1 568 ? -20.811 12.142  22.239  1.00 10.25 ? 591  VAL   A CG2 1 
ATOM   4250 N  N   . GLU   A 1 569 ? -22.773 15.671  24.674  1.00 9.41  ? 592  GLU   A N   1 
ATOM   4251 C  CA  . GLU   A 1 569 ? -22.919 16.980  25.303  1.00 9.60  ? 592  GLU   A CA  1 
ATOM   4252 C  C   . GLU   A 1 569 ? -23.516 17.932  24.278  1.00 9.62  ? 592  GLU   A C   1 
ATOM   4253 O  O   . GLU   A 1 569 ? -24.590 17.628  23.808  1.00 10.11 ? 592  GLU   A O   1 
ATOM   4254 C  CB  . GLU   A 1 569 ? -21.610 17.390  25.968  1.00 9.69  ? 592  GLU   A CB  1 
ATOM   4255 C  CG  . GLU   A 1 569 ? -21.314 16.469  27.159  1.00 10.30 ? 592  GLU   A CG  1 
ATOM   4256 C  CD  . GLU   A 1 569 ? -20.194 16.874  28.116  1.00 9.71  ? 592  GLU   A CD  1 
ATOM   4257 O  OE1 . GLU   A 1 569 ? -19.592 17.937  27.913  1.00 10.64 ? 592  GLU   A OE1 1 
ATOM   4258 O  OE2 . GLU   A 1 569 ? -19.936 16.118  29.079  1.00 10.43 ? 592  GLU   A OE2 1 
ATOM   4259 N  N   . ASN   A 1 570 ? -22.845 19.027  23.916  1.00 10.17 ? 593  ASN   A N   1 
ATOM   4260 C  CA  . ASN   A 1 570 ? -23.453 19.976  22.999  1.00 10.67 ? 593  ASN   A CA  1 
ATOM   4261 C  C   . ASN   A 1 570 ? -23.066 19.723  21.541  1.00 10.52 ? 593  ASN   A C   1 
ATOM   4262 O  O   . ASN   A 1 570 ? -23.466 20.485  20.675  1.00 10.82 ? 593  ASN   A O   1 
ATOM   4263 C  CB  . ASN   A 1 570 ? -23.165 21.412  23.414  1.00 10.68 ? 593  ASN   A CB  1 
ATOM   4264 C  CG  . ASN   A 1 570 ? -24.001 21.778  24.606  1.00 11.81 ? 593  ASN   A CG  1 
ATOM   4265 O  OD1 . ASN   A 1 570 ? -25.222 21.523  24.638  1.00 11.53 ? 593  ASN   A OD1 1 
ATOM   4266 N  ND2 . ASN   A 1 570 ? -23.329 22.306  25.614  1.00 13.17 ? 593  ASN   A ND2 1 
ATOM   4267 N  N   . GLU   A 1 571 ? -22.316 18.652  21.236  1.00 9.97  ? 594  GLU   A N   1 
ATOM   4268 C  CA  . GLU   A 1 571 ? -22.058 18.314  19.843  1.00 9.29  ? 594  GLU   A CA  1 
ATOM   4269 C  C   . GLU   A 1 571 ? -23.203 17.438  19.337  1.00 8.51  ? 594  GLU   A C   1 
ATOM   4270 O  O   . GLU   A 1 571 ? -23.294 16.238  19.627  1.00 8.40  ? 594  GLU   A O   1 
ATOM   4271 C  CB  . GLU   A 1 571 ? -20.668 17.683  19.730  1.00 9.18  ? 594  GLU   A CB  1 
ATOM   4272 C  CG  . GLU   A 1 571 ? -20.299 17.332  18.291  1.00 9.49  ? 594  GLU   A CG  1 
ATOM   4273 C  CD  . GLU   A 1 571 ? -18.902 16.841  18.005  1.00 11.71 ? 594  GLU   A CD  1 
ATOM   4274 O  OE1 . GLU   A 1 571 ? -18.108 16.693  18.991  1.00 10.05 ? 594  GLU   A OE1 1 
ATOM   4275 O  OE2 . GLU   A 1 571 ? -18.635 16.705  16.780  1.00 12.17 ? 594  GLU   A OE2 1 
ATOM   4276 N  N   . VAL   A 1 572 ? -24.123 18.076  18.591  1.00 8.53  ? 595  VAL   A N   1 
ATOM   4277 C  CA  . VAL   A 1 572 ? -25.426 17.490  18.302  1.00 8.40  ? 595  VAL   A CA  1 
ATOM   4278 C  C   . VAL   A 1 572 ? -25.437 16.940  16.886  1.00 8.22  ? 595  VAL   A C   1 
ATOM   4279 O  O   . VAL   A 1 572 ? -26.413 17.096  16.145  1.00 8.86  ? 595  VAL   A O   1 
ATOM   4280 C  CB  . VAL   A 1 572 ? -26.581 18.491  18.584  1.00 9.24  ? 595  VAL   A CB  1 
ATOM   4281 C  CG1 . VAL   A 1 572 ? -26.694 18.768  20.074  1.00 9.95  ? 595  VAL   A CG1 1 
ATOM   4282 C  CG2 . VAL   A 1 572 ? -26.495 19.801  17.801  1.00 9.69  ? 595  VAL   A CG2 1 
ATOM   4283 N  N   . ASN   A 1 573 ? -24.400 16.153  16.553  1.00 8.50  ? 596  ASN   A N   1 
ATOM   4284 C  CA  . ASN   A 1 573 ? -24.310 15.542  15.233  1.00 8.38  ? 596  ASN   A CA  1 
ATOM   4285 C  C   . ASN   A 1 573 ? -24.378 14.016  15.282  1.00 8.09  ? 596  ASN   A C   1 
ATOM   4286 O  O   . ASN   A 1 573 ? -23.882 13.329  14.376  1.00 7.64  ? 596  ASN   A O   1 
ATOM   4287 C  CB  . ASN   A 1 573 ? -23.042 16.000  14.511  1.00 8.35  ? 596  ASN   A CB  1 
ATOM   4288 C  CG  . ASN   A 1 573 ? -21.782 15.828  15.343  1.00 7.95  ? 596  ASN   A CG  1 
ATOM   4289 O  OD1 . ASN   A 1 573 ? -21.768 15.102  16.336  1.00 7.99  ? 596  ASN   A OD1 1 
ATOM   4290 N  ND2 . ASN   A 1 573 ? -20.724 16.552  15.026  1.00 8.87  ? 596  ASN   A ND2 1 
ATOM   4291 N  N   . GLY   A 1 574 ? -24.988 13.467  16.328  1.00 8.09  ? 597  GLY   A N   1 
ATOM   4292 C  CA  . GLY   A 1 574 ? -25.334 12.061  16.355  1.00 8.01  ? 597  GLY   A CA  1 
ATOM   4293 C  C   . GLY   A 1 574 ? -26.450 11.705  15.373  1.00 8.88  ? 597  GLY   A C   1 
ATOM   4294 O  O   . GLY   A 1 574 ? -27.383 12.503  15.160  1.00 9.73  ? 597  GLY   A O   1 
ATOM   4295 N  N   . LEU   A 1 575 ? -26.449 10.434  14.948  1.00 8.80  ? 598  LEU   A N   1 
ATOM   4296 C  CA  . LEU   A 1 575 ? -27.614 9.797   14.369  1.00 10.02 ? 598  LEU   A CA  1 
ATOM   4297 C  C   . LEU   A 1 575 ? -28.655 9.500   15.448  1.00 9.73  ? 598  LEU   A C   1 
ATOM   4298 O  O   . LEU   A 1 575 ? -29.845 9.361   15.122  1.00 9.24  ? 598  LEU   A O   1 
ATOM   4299 C  CB  . LEU   A 1 575 ? -27.162 8.539   13.639  1.00 10.04 ? 598  LEU   A CB  1 
ATOM   4300 C  CG  . LEU   A 1 575 ? -26.096 8.772   12.557  1.00 10.63 ? 598  LEU   A CG  1 
ATOM   4301 C  CD1 . LEU   A 1 575 ? -25.701 7.436   11.964  1.00 10.80 ? 598  LEU   A CD1 1 
ATOM   4302 C  CD2 . LEU   A 1 575 ? -26.582 9.744   11.456  1.00 10.62 ? 598  LEU   A CD2 1 
ATOM   4303 N  N   . LEU   A 1 576 ? -28.158 9.376   16.692  1.00 9.70  ? 599  LEU   A N   1 
ATOM   4304 C  CA  . LEU   A 1 576 ? -28.964 9.174   17.896  1.00 10.03 ? 599  LEU   A CA  1 
ATOM   4305 C  C   . LEU   A 1 576 ? -28.764 10.372  18.827  1.00 8.75  ? 599  LEU   A C   1 
ATOM   4306 O  O   . LEU   A 1 576 ? -27.712 11.010  18.836  1.00 8.45  ? 599  LEU   A O   1 
ATOM   4307 C  CB  . LEU   A 1 576 ? -28.628 7.894   18.668  1.00 9.95  ? 599  LEU   A CB  1 
ATOM   4308 C  CG  . LEU   A 1 576 ? -28.219 6.651   17.877  1.00 11.55 ? 599  LEU   A CG  1 
ATOM   4309 C  CD1 . LEU   A 1 576 ? -27.764 5.559   18.876  1.00 11.88 ? 599  LEU   A CD1 1 
ATOM   4310 C  CD2 . LEU   A 1 576 ? -29.319 6.184   16.916  1.00 11.40 ? 599  LEU   A CD2 1 
ATOM   4311 N  N   . THR   A 1 577 ? -29.810 10.728  19.598  1.00 8.52  ? 600  THR   A N   1 
ATOM   4312 C  CA  . THR   A 1 577 ? -29.611 11.679  20.675  1.00 8.45  ? 600  THR   A CA  1 
ATOM   4313 C  C   . THR   A 1 577 ? -28.673 11.094  21.740  1.00 8.17  ? 600  THR   A C   1 
ATOM   4314 O  O   . THR   A 1 577 ? -28.483 9.877   21.836  1.00 7.90  ? 600  THR   A O   1 
ATOM   4315 C  CB  . THR   A 1 577 ? -30.950 12.144  21.238  1.00 8.91  ? 600  THR   A CB  1 
ATOM   4316 O  OG1 . THR   A 1 577 ? -31.699 11.027  21.701  1.00 9.23  ? 600  THR   A OG1 1 
ATOM   4317 C  CG2 . THR   A 1 577 ? -31.754 12.885  20.190  1.00 9.91  ? 600  THR   A CG2 1 
ATOM   4318 N  N   . TYR   A 1 578 ? -28.107 11.983  22.570  1.00 8.05  ? 601  TYR   A N   1 
ATOM   4319 C  CA  . TYR   A 1 578 ? -27.154 11.625  23.623  1.00 7.81  ? 601  TYR   A CA  1 
ATOM   4320 C  C   . TYR   A 1 578 ? -27.758 10.673  24.653  1.00 8.16  ? 601  TYR   A C   1 
ATOM   4321 O  O   . TYR   A 1 578 ? -27.065 9.810   25.201  1.00 8.48  ? 601  TYR   A O   1 
ATOM   4322 C  CB  . TYR   A 1 578 ? -26.562 12.889  24.248  1.00 7.73  ? 601  TYR   A CB  1 
ATOM   4323 C  CG  . TYR   A 1 578 ? -25.347 12.727  25.172  1.00 7.71  ? 601  TYR   A CG  1 
ATOM   4324 C  CD1 . TYR   A 1 578 ? -24.439 11.688  25.001  1.00 8.56  ? 601  TYR   A CD1 1 
ATOM   4325 C  CD2 . TYR   A 1 578 ? -25.124 13.604  26.249  1.00 7.57  ? 601  TYR   A CD2 1 
ATOM   4326 C  CE1 . TYR   A 1 578 ? -23.341 11.532  25.829  1.00 8.01  ? 601  TYR   A CE1 1 
ATOM   4327 C  CE2 . TYR   A 1 578 ? -23.987 13.487  27.036  1.00 8.01  ? 601  TYR   A CE2 1 
ATOM   4328 C  CZ  . TYR   A 1 578 ? -23.124 12.422  26.856  1.00 8.32  ? 601  TYR   A CZ  1 
ATOM   4329 O  OH  . TYR   A 1 578 ? -21.994 12.315  27.620  1.00 8.51  ? 601  TYR   A OH  1 
ATOM   4330 N  N   . ASP   A 1 579 ? -29.063 10.786  24.902  1.00 8.43  ? 602  ASP   A N   1 
ATOM   4331 C  CA  . ASP   A 1 579 ? -29.772 9.901   25.822  1.00 9.07  ? 602  ASP   A CA  1 
ATOM   4332 C  C   . ASP   A 1 579 ? -30.232 8.580   25.179  1.00 9.01  ? 602  ASP   A C   1 
ATOM   4333 O  O   . ASP   A 1 579 ? -30.867 7.786   25.820  1.00 8.87  ? 602  ASP   A O   1 
ATOM   4334 C  CB  . ASP   A 1 579 ? -30.955 10.620  26.443  1.00 9.16  ? 602  ASP   A CB  1 
ATOM   4335 C  CG  . ASP   A 1 579 ? -31.988 11.131  25.465  1.00 10.49 ? 602  ASP   A CG  1 
ATOM   4336 O  OD1 . ASP   A 1 579 ? -31.918 10.747  24.272  1.00 11.11 ? 602  ASP   A OD1 1 
ATOM   4337 O  OD2 . ASP   A 1 579 ? -32.837 11.922  25.923  1.00 11.37 ? 602  ASP   A OD2 1 
ATOM   4338 N  N   . ARG   A 1 580 ? -29.896 8.325   23.919  1.00 8.76  ? 603  ARG   A N   1 
ATOM   4339 C  CA  . ARG   A 1 580 ? -30.274 7.123   23.188  1.00 9.28  ? 603  ARG   A CA  1 
ATOM   4340 C  C   . ARG   A 1 580 ? -31.792 6.996   22.982  1.00 9.85  ? 603  ARG   A C   1 
ATOM   4341 O  O   . ARG   A 1 580 ? -32.254 5.949   22.548  1.00 10.46 ? 603  ARG   A O   1 
ATOM   4342 C  CB  . ARG   A 1 580 ? -29.660 5.848   23.782  1.00 9.26  ? 603  ARG   A CB  1 
ATOM   4343 C  CG  . ARG   A 1 580 ? -28.192 5.637   23.427  1.00 9.09  ? 603  ARG   A CG  1 
ATOM   4344 C  CD  . ARG   A 1 580 ? -27.234 6.635   24.000  1.00 9.40  ? 603  ARG   A CD  1 
ATOM   4345 N  NE  . ARG   A 1 580 ? -25.842 6.223   23.763  1.00 9.44  ? 603  ARG   A NE  1 
ATOM   4346 C  CZ  . ARG   A 1 580 ? -24.749 6.840   24.214  1.00 9.86  ? 603  ARG   A CZ  1 
ATOM   4347 N  NH1 . ARG   A 1 580 ? -23.553 6.256   24.091  1.00 9.35  ? 603  ARG   A NH1 1 
ATOM   4348 N  NH2 . ARG   A 1 580 ? -24.876 8.005   24.827  1.00 9.96  ? 603  ARG   A NH2 1 
ATOM   4349 N  N   . GLN   A 1 581 ? -32.575 8.038   23.280  1.00 10.31 ? 604  GLN   A N   1 
ATOM   4350 C  CA  . GLN   A 1 581 ? -34.022 7.908   23.234  1.00 11.38 ? 604  GLN   A CA  1 
ATOM   4351 C  C   . GLN   A 1 581 ? -34.575 8.075   21.829  1.00 11.35 ? 604  GLN   A C   1 
ATOM   4352 O  O   . GLN   A 1 581 ? -35.658 7.545   21.553  1.00 11.25 ? 604  GLN   A O   1 
ATOM   4353 C  CB  . GLN   A 1 581 ? -34.687 8.972   24.107  1.00 13.00 ? 604  GLN   A CB  1 
ATOM   4354 C  CG  . GLN   A 1 581 ? -34.384 8.800   25.585  1.00 15.69 ? 604  GLN   A CG  1 
ATOM   4355 C  CD  . GLN   A 1 581 ? -35.182 7.673   26.182  1.00 22.77 ? 604  GLN   A CD  1 
ATOM   4356 O  OE1 . GLN   A 1 581 ? -36.054 7.096   25.514  1.00 24.78 ? 604  GLN   A OE1 1 
ATOM   4357 N  NE2 . GLN   A 1 581 ? -34.926 7.368   27.453  1.00 27.64 ? 604  GLN   A NE2 1 
ATOM   4358 N  N   . VAL   A 1 582 ? -33.884 8.829   20.975  1.00 10.96 ? 605  VAL   A N   1 
ATOM   4359 C  CA  . VAL   A 1 582 ? -34.411 9.187   19.662  1.00 12.58 ? 605  VAL   A CA  1 
ATOM   4360 C  C   . VAL   A 1 582 ? -33.383 8.793   18.608  1.00 12.24 ? 605  VAL   A C   1 
ATOM   4361 O  O   . VAL   A 1 582 ? -32.200 9.147   18.706  1.00 11.20 ? 605  VAL   A O   1 
ATOM   4362 C  CB  . VAL   A 1 582 ? -34.764 10.688  19.563  1.00 13.01 ? 605  VAL   A CB  1 
ATOM   4363 C  CG1 . VAL   A 1 582 ? -35.194 11.117  18.155  1.00 14.06 ? 605  VAL   A CG1 1 
ATOM   4364 C  CG2 . VAL   A 1 582 ? -35.861 11.084  20.555  1.00 13.57 ? 605  VAL   A CG2 1 
ATOM   4365 N  N   . VAL   A 1 583 ? -33.872 8.070   17.586  1.00 12.29 ? 606  VAL   A N   1 
ATOM   4366 C  CA  . VAL   A 1 583 ? -33.128 7.814   16.363  1.00 12.13 ? 606  VAL   A CA  1 
ATOM   4367 C  C   . VAL   A 1 583 ? -33.525 8.908   15.382  1.00 11.78 ? 606  VAL   A C   1 
ATOM   4368 O  O   . VAL   A 1 583 ? -34.701 9.010   15.061  1.00 11.44 ? 606  VAL   A O   1 
ATOM   4369 C  CB  . VAL   A 1 583 ? -33.456 6.418   15.822  1.00 12.42 ? 606  VAL   A CB  1 
ATOM   4370 C  CG1 . VAL   A 1 583 ? -32.707 6.135   14.539  1.00 12.89 ? 606  VAL   A CG1 1 
ATOM   4371 C  CG2 . VAL   A 1 583 ? -33.175 5.345   16.875  1.00 13.43 ? 606  VAL   A CG2 1 
ATOM   4372 N  N   . LYS   A 1 584 ? -32.616 9.830   15.061  1.00 11.19 ? 607  LYS   A N   1 
ATOM   4373 C  CA  . LYS   A 1 584 ? -32.956 11.024  14.291  1.00 11.79 ? 607  LYS   A CA  1 
ATOM   4374 C  C   . LYS   A 1 584 ? -33.203 10.747  12.811  1.00 14.45 ? 607  LYS   A C   1 
ATOM   4375 O  O   . LYS   A 1 584 ? -33.833 11.564  12.135  1.00 17.10 ? 607  LYS   A O   1 
ATOM   4376 C  CB  . LYS   A 1 584 ? -31.785 12.018  14.283  1.00 11.26 ? 607  LYS   A CB  1 
ATOM   4377 C  CG  . LYS   A 1 584 ? -31.345 12.478  15.659  1.00 10.56 ? 607  LYS   A CG  1 
ATOM   4378 C  CD  . LYS   A 1 584 ? -30.457 13.714  15.582  1.00 10.20 ? 607  LYS   A CD  1 
ATOM   4379 C  CE  . LYS   A 1 584 ? -29.700 14.014  16.836  1.00 10.28 ? 607  LYS   A CE  1 
ATOM   4380 N  NZ  . LYS   A 1 584 ? -28.724 15.079  16.565  1.00 9.98  ? 607  LYS   A NZ  1 
ATOM   4381 N  N   . VAL   A 1 585 ? -32.722 9.600   12.317  1.00 13.34 ? 608  VAL   A N   1 
ATOM   4382 C  CA  . VAL   A 1 585 ? -32.711 9.325   10.886  1.00 12.90 ? 608  VAL   A CA  1 
ATOM   4383 C  C   . VAL   A 1 585 ? -33.682 8.201   10.568  1.00 13.43 ? 608  VAL   A C   1 
ATOM   4384 O  O   . VAL   A 1 585 ? -34.013 7.366   11.414  1.00 14.17 ? 608  VAL   A O   1 
ATOM   4385 C  CB  . VAL   A 1 585 ? -31.313 8.991   10.352  1.00 12.44 ? 608  VAL   A CB  1 
ATOM   4386 C  CG1 . VAL   A 1 585 ? -30.429 10.221  10.378  1.00 12.26 ? 608  VAL   A CG1 1 
ATOM   4387 C  CG2 . VAL   A 1 585 ? -30.700 7.833   11.115  1.00 12.86 ? 608  VAL   A CG2 1 
ATOM   4388 N  N   . ASP   A 1 586 ? -34.139 8.204   9.311   1.00 13.48 ? 609  ASP   A N   1 
ATOM   4389 C  CA  . ASP   A 1 586 ? -34.997 7.140   8.832   1.00 13.98 ? 609  ASP   A CA  1 
ATOM   4390 C  C   . ASP   A 1 586 ? -34.140 5.882   8.662   1.00 13.56 ? 609  ASP   A C   1 
ATOM   4391 O  O   . ASP   A 1 586 ? -33.259 5.842   7.789   1.00 12.04 ? 609  ASP   A O   1 
ATOM   4392 C  CB  . ASP   A 1 586 ? -35.596 7.562   7.509   1.00 16.29 ? 609  ASP   A CB  1 
ATOM   4393 C  CG  . ASP   A 1 586 ? -36.537 6.560   6.866   1.00 19.19 ? 609  ASP   A CG  1 
ATOM   4394 O  OD1 . ASP   A 1 586 ? -36.211 5.363   6.815   1.00 20.36 ? 609  ASP   A OD1 1 
ATOM   4395 O  OD2 . ASP   A 1 586 ? -37.594 7.017   6.432   1.00 23.21 ? 609  ASP   A OD2 1 
ATOM   4396 N  N   . GLU   A 1 587 ? -34.412 4.838   9.437   1.00 12.86 ? 610  GLU   A N   1 
ATOM   4397 C  CA  A GLU   A 1 587 ? -33.466 3.735   9.560   0.50 13.75 ? 610  GLU   A CA  1 
ATOM   4398 C  CA  B GLU   A 1 587 ? -33.465 3.738   9.561   0.50 13.06 ? 610  GLU   A CA  1 
ATOM   4399 C  C   . GLU   A 1 587 ? -33.403 2.935   8.264   1.00 13.44 ? 610  GLU   A C   1 
ATOM   4400 O  O   . GLU   A 1 587 ? -32.316 2.554   7.831   1.00 13.40 ? 610  GLU   A O   1 
ATOM   4401 C  CB  A GLU   A 1 587 ? -33.793 2.799   10.721  0.50 15.29 ? 610  GLU   A CB  1 
ATOM   4402 C  CB  B GLU   A 1 587 ? -33.830 2.849   10.745  0.50 13.51 ? 610  GLU   A CB  1 
ATOM   4403 C  CG  A GLU   A 1 587 ? -33.449 3.396   12.077  0.50 16.57 ? 610  GLU   A CG  1 
ATOM   4404 C  CG  B GLU   A 1 587 ? -34.053 3.644   12.022  0.50 13.77 ? 610  GLU   A CG  1 
ATOM   4405 C  CD  A GLU   A 1 587 ? -33.455 2.362   13.187  0.50 18.29 ? 610  GLU   A CD  1 
ATOM   4406 C  CD  B GLU   A 1 587 ? -34.264 2.749   13.232  0.50 14.03 ? 610  GLU   A CD  1 
ATOM   4407 O  OE1 A GLU   A 1 587 ? -33.534 1.147   12.856  0.50 20.06 ? 610  GLU   A OE1 1 
ATOM   4408 O  OE1 B GLU   A 1 587 ? -33.293 2.010   13.507  0.50 14.11 ? 610  GLU   A OE1 1 
ATOM   4409 O  OE2 A GLU   A 1 587 ? -33.411 2.788   14.374  0.50 20.38 ? 610  GLU   A OE2 1 
ATOM   4410 O  OE2 B GLU   A 1 587 ? -35.318 2.825   13.897  0.50 13.95 ? 610  GLU   A OE2 1 
ATOM   4411 N  N   . ALA   A 1 588 ? -34.571 2.687   7.655   1.00 13.26 ? 611  ALA   A N   1 
ATOM   4412 C  CA  . ALA   A 1 588 ? -34.614 1.962   6.385   1.00 12.83 ? 611  ALA   A CA  1 
ATOM   4413 C  C   . ALA   A 1 588 ? -33.836 2.672   5.283   1.00 12.04 ? 611  ALA   A C   1 
ATOM   4414 O  O   . ALA   A 1 588 ? -33.182 2.024   4.464   1.00 12.92 ? 611  ALA   A O   1 
ATOM   4415 C  CB  . ALA   A 1 588 ? -36.056 1.742   5.942   1.00 13.02 ? 611  ALA   A CB  1 
ATOM   4416 N  N   . ARG   A 1 589 ? -33.945 3.989   5.203   1.00 11.92 ? 612  ARG   A N   1 
ATOM   4417 C  CA  . ARG   A 1 589 ? -33.229 4.748   4.185   1.00 11.94 ? 612  ARG   A CA  1 
ATOM   4418 C  C   . ARG   A 1 589 ? -31.716 4.721   4.425   1.00 11.65 ? 612  ARG   A C   1 
ATOM   4419 O  O   . ARG   A 1 589 ? -30.924 4.602   3.498   1.00 11.85 ? 612  ARG   A O   1 
ATOM   4420 C  CB  . ARG   A 1 589 ? -33.737 6.185   4.136   1.00 12.28 ? 612  ARG   A CB  1 
ATOM   4421 C  CG  . ARG   A 1 589 ? -35.168 6.264   3.628   1.00 14.85 ? 612  ARG   A CG  1 
ATOM   4422 C  CD  . ARG   A 1 589 ? -35.771 7.660   3.621   1.00 16.05 ? 612  ARG   A CD  1 
ATOM   4423 N  NE  . ARG   A 1 589 ? -34.863 8.692   3.117   1.00 15.86 ? 612  ARG   A NE  1 
ATOM   4424 C  CZ  . ARG   A 1 589 ? -35.024 10.003  3.341   1.00 16.65 ? 612  ARG   A CZ  1 
ATOM   4425 N  NH1 . ARG   A 1 589 ? -35.971 10.452  4.188   1.00 17.01 ? 612  ARG   A NH1 1 
ATOM   4426 N  NH2 . ARG   A 1 589 ? -34.171 10.837  2.766   1.00 16.94 ? 612  ARG   A NH2 1 
ATOM   4427 N  N   . VAL   A 1 590 ? -31.279 4.899   5.679   1.00 11.36 ? 613  VAL   A N   1 
ATOM   4428 C  CA  . VAL   A 1 590 ? -29.854 4.921   5.962   1.00 11.11 ? 613  VAL   A CA  1 
ATOM   4429 C  C   . VAL   A 1 590 ? -29.268 3.525   5.719   1.00 10.79 ? 613  VAL   A C   1 
ATOM   4430 O  O   . VAL   A 1 590 ? -28.213 3.412   5.102   1.00 10.94 ? 613  VAL   A O   1 
ATOM   4431 C  CB  . VAL   A 1 590 ? -29.596 5.435   7.389   1.00 10.78 ? 613  VAL   A CB  1 
ATOM   4432 C  CG1 . VAL   A 1 590 ? -28.173 5.167   7.845   1.00 10.77 ? 613  VAL   A CG1 1 
ATOM   4433 C  CG2 . VAL   A 1 590 ? -29.972 6.906   7.546   1.00 11.89 ? 613  VAL   A CG2 1 
ATOM   4434 N  N   . ARG   A 1 591 ? -29.952 2.461   6.169   1.00 11.74 ? 614  ARG   A N   1 
ATOM   4435 C  CA  . ARG   A 1 591 ? -29.521 1.093   5.983   1.00 12.77 ? 614  ARG   A CA  1 
ATOM   4436 C  C   . ARG   A 1 591 ? -29.401 0.794   4.490   1.00 11.80 ? 614  ARG   A C   1 
ATOM   4437 O  O   . ARG   A 1 591 ? -28.442 0.192   4.052   1.00 11.20 ? 614  ARG   A O   1 
ATOM   4438 C  CB  . ARG   A 1 591 ? -30.504 0.140   6.666   1.00 16.77 ? 614  ARG   A CB  1 
ATOM   4439 C  CG  . ARG   A 1 591 ? -30.165 -1.331  6.481   1.00 19.36 ? 614  ARG   A CG  1 
ATOM   4440 C  CD  . ARG   A 1 591 ? -31.227 -2.182  7.119   1.00 26.64 ? 614  ARG   A CD  1 
ATOM   4441 N  NE  . ARG   A 1 591 ? -30.666 -3.537  7.211   1.00 34.35 ? 614  ARG   A NE  1 
ATOM   4442 C  CZ  . ARG   A 1 591 ? -30.537 -4.260  8.328   1.00 49.52 ? 614  ARG   A CZ  1 
ATOM   4443 N  NH1 . ARG   A 1 591 ? -30.871 -3.773  9.514   1.00 54.81 ? 614  ARG   A NH1 1 
ATOM   4444 N  NH2 . ARG   A 1 591 ? -30.093 -5.505  8.249   1.00 55.85 ? 614  ARG   A NH2 1 
ATOM   4445 N  N   . ALA   A 1 592 ? -30.389 1.216   3.704   1.00 11.88 ? 615  ALA   A N   1 
ATOM   4446 C  CA  . ALA   A 1 592 ? -30.366 0.964   2.264   1.00 10.83 ? 615  ALA   A CA  1 
ATOM   4447 C  C   . ALA   A 1 592 ? -29.163 1.641   1.598   1.00 10.32 ? 615  ALA   A C   1 
ATOM   4448 O  O   . ALA   A 1 592 ? -28.501 1.060   0.721   1.00 11.84 ? 615  ALA   A O   1 
ATOM   4449 C  CB  . ALA   A 1 592 ? -31.679 1.413   1.675   1.00 10.62 ? 615  ALA   A CB  1 
ATOM   4450 N  N   . ALA   A 1 593 ? -28.859 2.875   2.000   1.00 10.18 ? 616  ALA   A N   1 
ATOM   4451 C  CA  . ALA   A 1 593 ? -27.724 3.575   1.422   1.00 10.35 ? 616  ALA   A CA  1 
ATOM   4452 C  C   . ALA   A 1 593 ? -26.418 2.862   1.774   1.00 9.91  ? 616  ALA   A C   1 
ATOM   4453 O  O   . ALA   A 1 593 ? -25.565 2.662   0.900   1.00 8.90  ? 616  ALA   A O   1 
ATOM   4454 C  CB  . ALA   A 1 593 ? -27.717 5.015   1.870   1.00 10.65 ? 616  ALA   A CB  1 
ATOM   4455 N  N   . ASN   A 1 594 ? -26.264 2.502   3.063   1.00 8.85  ? 617  ASN   A N   1 
ATOM   4456 C  CA  . ASN   A 1 594 ? -25.059 1.806   3.508   1.00 9.26  ? 617  ASN   A CA  1 
ATOM   4457 C  C   . ASN   A 1 594 ? -24.924 0.444   2.835   1.00 10.62 ? 617  ASN   A C   1 
ATOM   4458 O  O   . ASN   A 1 594 ? -23.826 0.101   2.409   1.00 10.89 ? 617  ASN   A O   1 
ATOM   4459 C  CB  . ASN   A 1 594 ? -24.994 1.658   5.013   1.00 9.10  ? 617  ASN   A CB  1 
ATOM   4460 C  CG  . ASN   A 1 594 ? -24.393 2.875   5.673   1.00 8.83  ? 617  ASN   A CG  1 
ATOM   4461 O  OD1 . ASN   A 1 594 ? -23.412 3.427   5.181   1.00 9.06  ? 617  ASN   A OD1 1 
ATOM   4462 N  ND2 . ASN   A 1 594 ? -24.906 3.272   6.829   1.00 9.34  ? 617  ASN   A ND2 1 
ATOM   4463 N  N   . ARG   A 1 595 ? -26.025 -0.303  2.726   1.00 11.87 ? 618  ARG   A N   1 
ATOM   4464 C  CA  . ARG   A 1 595 ? -25.951 -1.627  2.138   1.00 14.65 ? 618  ARG   A CA  1 
ATOM   4465 C  C   . ARG   A 1 595 ? -25.618 -1.520  0.649   1.00 13.14 ? 618  ARG   A C   1 
ATOM   4466 O  O   . ARG   A 1 595 ? -24.864 -2.338  0.141   1.00 12.00 ? 618  ARG   A O   1 
ATOM   4467 C  CB  . ARG   A 1 595 ? -27.220 -2.435  2.380   1.00 20.38 ? 618  ARG   A CB  1 
ATOM   4468 C  CG  . ARG   A 1 595 ? -27.241 -3.091  3.755   1.00 27.77 ? 618  ARG   A CG  1 
ATOM   4469 C  CD  . ARG   A 1 595 ? -28.501 -3.944  3.932   1.00 36.78 ? 618  ARG   A CD  1 
ATOM   4470 N  NE  . ARG   A 1 595 ? -28.178 -5.302  4.383   1.00 48.28 ? 618  ARG   A NE  1 
ATOM   4471 C  CZ  . ARG   A 1 595 ? -27.435 -6.168  3.683   1.00 61.94 ? 618  ARG   A CZ  1 
ATOM   4472 N  NH1 . ARG   A 1 595 ? -27.062 -5.886  2.434   1.00 67.41 ? 618  ARG   A NH1 1 
ATOM   4473 N  NH2 . ARG   A 1 595 ? -27.077 -7.322  4.234   1.00 62.82 ? 618  ARG   A NH2 1 
ATOM   4474 N  N   . ALA   A 1 596 ? -26.165 -0.512  -0.034  1.00 12.28 ? 619  ALA   A N   1 
ATOM   4475 C  CA  . ALA   A 1 596 ? -25.860 -0.287  -1.437  1.00 12.19 ? 619  ALA   A CA  1 
ATOM   4476 C  C   . ALA   A 1 596 ? -24.368 -0.039  -1.643  1.00 12.25 ? 619  ALA   A C   1 
ATOM   4477 O  O   . ALA   A 1 596 ? -23.774 -0.571  -2.590  1.00 11.41 ? 619  ALA   A O   1 
ATOM   4478 C  CB  . ALA   A 1 596 ? -26.692 0.859   -1.988  1.00 12.21 ? 619  ALA   A CB  1 
ATOM   4479 N  N   . LEU   A 1 597 ? -23.773 0.798   -0.773  1.00 11.32 ? 620  LEU   A N   1 
ATOM   4480 C  CA  . LEU   A 1 597 ? -22.344 1.074   -0.796  1.00 11.10 ? 620  LEU   A CA  1 
ATOM   4481 C  C   . LEU   A 1 597 ? -21.511 -0.197  -0.590  1.00 11.55 ? 620  LEU   A C   1 
ATOM   4482 O  O   . LEU   A 1 597 ? -20.544 -0.465  -1.312  1.00 11.89 ? 620  LEU   A O   1 
ATOM   4483 C  CB  . LEU   A 1 597 ? -22.074 2.115   0.291   1.00 11.24 ? 620  LEU   A CB  1 
ATOM   4484 C  CG  . LEU   A 1 597 ? -20.606 2.370   0.648   1.00 11.07 ? 620  LEU   A CG  1 
ATOM   4485 C  CD1 . LEU   A 1 597 ? -19.678 2.726   -0.504  1.00 11.39 ? 620  LEU   A CD1 1 
ATOM   4486 C  CD2 . LEU   A 1 597 ? -20.589 3.488   1.649   1.00 10.91 ? 620  LEU   A CD2 1 
ATOM   4487 N  N   . ILE   A 1 598 ? -21.831 -0.967  0.448   1.00 11.38 ? 621  ILE   A N   1 
ATOM   4488 C  CA  . ILE   A 1 598 ? -21.131 -2.217  0.709   1.00 12.08 ? 621  ILE   A CA  1 
ATOM   4489 C  C   . ILE   A 1 598 ? -21.259 -3.185  -0.483  1.00 13.30 ? 621  ILE   A C   1 
ATOM   4490 O  O   . ILE   A 1 598 ? -20.255 -3.715  -0.973  1.00 14.18 ? 621  ILE   A O   1 
ATOM   4491 C  CB  . ILE   A 1 598 ? -21.659 -2.830  2.017   1.00 11.85 ? 621  ILE   A CB  1 
ATOM   4492 C  CG1 . ILE   A 1 598 ? -21.298 -1.942  3.221   1.00 10.89 ? 621  ILE   A CG1 1 
ATOM   4493 C  CG2 . ILE   A 1 598 ? -21.128 -4.247  2.180   1.00 12.18 ? 621  ILE   A CG2 1 
ATOM   4494 C  CD1 . ILE   A 1 598 ? -22.014 -2.288  4.514   1.00 10.99 ? 621  ILE   A CD1 1 
ATOM   4495 N  N   . ASP   A 1 599 ? -22.493 -3.398  -0.960  1.00 14.12 ? 622  ASP   A N   1 
ATOM   4496 C  CA  . ASP   A 1 599 ? -22.774 -4.308  -2.062  1.00 16.42 ? 622  ASP   A CA  1 
ATOM   4497 C  C   . ASP   A 1 599 ? -21.982 -3.889  -3.305  1.00 15.64 ? 622  ASP   A C   1 
ATOM   4498 O  O   . ASP   A 1 599 ? -21.349 -4.726  -3.960  1.00 14.50 ? 622  ASP   A O   1 
ATOM   4499 C  CB  . ASP   A 1 599 ? -24.275 -4.433  -2.284  1.00 19.08 ? 622  ASP   A CB  1 
ATOM   4500 C  CG  . ASP   A 1 599 ? -25.055 -5.220  -1.236  1.00 22.67 ? 622  ASP   A CG  1 
ATOM   4501 O  OD1 . ASP   A 1 599 ? -24.419 -5.890  -0.391  1.00 29.83 ? 622  ASP   A OD1 1 
ATOM   4502 O  OD2 . ASP   A 1 599 ? -26.311 -5.162  -1.263  1.00 23.53 ? 622  ASP   A OD2 1 
ATOM   4503 N  N   . ALA   A 1 600 ? -22.015 -2.596  -3.629  1.00 15.30 ? 623  ALA   A N   1 
ATOM   4504 C  CA  . ALA   A 1 600 ? -21.273 -2.075  -4.767  1.00 15.92 ? 623  ALA   A CA  1 
ATOM   4505 C  C   . ALA   A 1 600 ? -19.775 -2.337  -4.612  1.00 17.01 ? 623  ALA   A C   1 
ATOM   4506 O  O   . ALA   A 1 600 ? -19.077 -2.514  -5.596  1.00 18.16 ? 623  ALA   A O   1 
ATOM   4507 C  CB  . ALA   A 1 600 ? -21.518 -0.620  -4.956  1.00 15.74 ? 623  ALA   A CB  1 
ATOM   4508 N  N   . SER   A 1 601 ? -19.247 -2.287  -3.390  1.00 13.60 ? 624  SER   A N   1 
ATOM   4509 C  CA  . SER   A 1 601 ? -17.811 -2.446  -3.239  1.00 15.14 ? 624  SER   A CA  1 
ATOM   4510 C  C   . SER   A 1 601 ? -17.414 -3.900  -3.497  1.00 17.23 ? 624  SER   A C   1 
ATOM   4511 O  O   . SER   A 1 601 ? -16.257 -4.169  -3.818  1.00 17.65 ? 624  SER   A O   1 
ATOM   4512 C  CB  . SER   A 1 601 ? -17.352 -1.999  -1.859  1.00 14.14 ? 624  SER   A CB  1 
ATOM   4513 O  OG  . SER   A 1 601 ? -17.762 -2.932  -0.875  1.00 13.21 ? 624  SER   A OG  1 
ATOM   4514 N  N   . ARG   A 1 602 ? -18.367 -4.800  -3.267  1.00 21.22 ? 625  ARG   A N   1 
ATOM   4515 C  CA  . ARG   A 1 602 ? -18.183 -6.236  -3.412  1.00 28.54 ? 625  ARG   A CA  1 
ATOM   4516 C  C   . ARG   A 1 602 ? -18.504 -6.632  -4.869  1.00 33.71 ? 625  ARG   A C   1 
ATOM   4517 O  O   . ARG   A 1 602 ? -18.225 -7.808  -5.187  1.00 34.33 ? 625  ARG   A O   1 
ATOM   4518 C  CB  . ARG   A 1 602 ? -19.067 -7.001  -2.409  1.00 28.06 ? 625  ARG   A CB  1 
ATOM   4519 C  CG  . ARG   A 1 602 ? -18.666 -6.985  -0.932  1.00 30.75 ? 625  ARG   A CG  1 
ATOM   4520 C  CD  . ARG   A 1 602 ? -19.321 -8.120  -0.099  1.00 30.89 ? 625  ARG   A CD  1 
ATOM   4521 N  NE  . ARG   A 1 602 ? -19.144 -8.125  1.367   1.00 30.85 ? 625  ARG   A NE  1 
ATOM   4522 C  CZ  . ARG   A 1 602 ? -18.120 -8.578  2.122   1.00 35.93 ? 625  ARG   A CZ  1 
ATOM   4523 N  NH1 . ARG   A 1 602 ? -17.065 -9.149  1.569   1.00 38.94 ? 625  ARG   A NH1 1 
ATOM   4524 N  NH2 . ARG   A 1 602 ? -18.158 -8.503  3.459   1.00 38.87 ? 625  ARG   A NH2 1 
ATOM   4525 N  N   . PRO   B 1 23  ? -52.599 -8.098  64.397  1.00 66.05 ? 46   PRO   B N   1 
ATOM   4526 C  CA  . PRO   B 1 23  ? -51.762 -6.946  64.078  1.00 64.67 ? 46   PRO   B CA  1 
ATOM   4527 C  C   . PRO   B 1 23  ? -52.519 -5.629  63.859  1.00 62.35 ? 46   PRO   B C   1 
ATOM   4528 O  O   . PRO   B 1 23  ? -52.635 -5.119  62.745  1.00 68.44 ? 46   PRO   B O   1 
ATOM   4529 C  CB  . PRO   B 1 23  ? -51.024 -7.459  62.818  1.00 66.07 ? 46   PRO   B CB  1 
ATOM   4530 C  CG  . PRO   B 1 23  ? -50.914 -8.971  63.008  1.00 64.66 ? 46   PRO   B CG  1 
ATOM   4531 C  CD  . PRO   B 1 23  ? -51.866 -9.334  64.134  1.00 65.81 ? 46   PRO   B CD  1 
ATOM   4532 N  N   . ARG   B 1 24  ? -53.010 -5.067  64.964  1.00 60.12 ? 47   ARG   B N   1 
ATOM   4533 C  CA  . ARG   B 1 24  ? -53.631 -3.751  65.014  1.00 60.97 ? 47   ARG   B CA  1 
ATOM   4534 C  C   . ARG   B 1 24  ? -52.892 -2.704  64.171  1.00 61.45 ? 47   ARG   B C   1 
ATOM   4535 O  O   . ARG   B 1 24  ? -53.534 -1.847  63.567  1.00 68.94 ? 47   ARG   B O   1 
ATOM   4536 C  CB  . ARG   B 1 24  ? -53.620 -3.329  66.487  1.00 65.75 ? 47   ARG   B CB  1 
ATOM   4537 C  CG  . ARG   B 1 24  ? -54.581 -2.200  66.807  1.00 69.71 ? 47   ARG   B CG  1 
ATOM   4538 C  CD  . ARG   B 1 24  ? -56.050 -2.585  66.657  1.00 64.83 ? 47   ARG   B CD  1 
ATOM   4539 N  NE  . ARG   B 1 24  ? -56.738 -1.310  66.451  1.00 67.03 ? 47   ARG   B NE  1 
ATOM   4540 C  CZ  . ARG   B 1 24  ? -56.489 -0.512  65.414  1.00 65.98 ? 47   ARG   B CZ  1 
ATOM   4541 N  NH1 . ARG   B 1 24  ? -55.869 -0.995  64.347  1.00 67.33 ? 47   ARG   B NH1 1 
ATOM   4542 N  NH2 . ARG   B 1 24  ? -56.889 0.753   65.425  1.00 59.20 ? 47   ARG   B NH2 1 
ATOM   4543 N  N   . ALA   B 1 25  ? -51.550 -2.740  64.170  1.00 52.20 ? 48   ALA   B N   1 
ATOM   4544 C  CA  . ALA   B 1 25  ? -50.728 -1.822  63.384  1.00 48.30 ? 48   ALA   B CA  1 
ATOM   4545 C  C   . ALA   B 1 25  ? -50.170 -2.516  62.130  1.00 42.44 ? 48   ALA   B C   1 
ATOM   4546 O  O   . ALA   B 1 25  ? -49.868 -3.708  62.144  1.00 37.86 ? 48   ALA   B O   1 
ATOM   4547 C  CB  . ALA   B 1 25  ? -49.619 -1.283  64.262  1.00 44.58 ? 48   ALA   B CB  1 
ATOM   4548 N  N   . TRP   B 1 26  ? -49.981 -1.756  61.045  1.00 41.73 ? 49   TRP   B N   1 
ATOM   4549 C  CA  . TRP   B 1 26  ? -49.552 -2.318  59.762  1.00 39.77 ? 49   TRP   B CA  1 
ATOM   4550 C  C   . TRP   B 1 26  ? -48.263 -3.123  59.904  1.00 38.04 ? 49   TRP   B C   1 
ATOM   4551 O  O   . TRP   B 1 26  ? -47.261 -2.604  60.374  1.00 48.29 ? 49   TRP   B O   1 
ATOM   4552 C  CB  . TRP   B 1 26  ? -49.384 -1.199  58.723  1.00 37.42 ? 49   TRP   B CB  1 
ATOM   4553 C  CG  . TRP   B 1 26  ? -49.195 -1.701  57.315  1.00 38.55 ? 49   TRP   B CG  1 
ATOM   4554 C  CD1 . TRP   B 1 26  ? -50.158 -2.171  56.463  1.00 40.50 ? 49   TRP   B CD1 1 
ATOM   4555 C  CD2 . TRP   B 1 26  ? -47.949 -1.770  56.588  1.00 40.08 ? 49   TRP   B CD2 1 
ATOM   4556 N  NE1 . TRP   B 1 26  ? -49.602 -2.542  55.266  1.00 39.08 ? 49   TRP   B NE1 1 
ATOM   4557 C  CE2 . TRP   B 1 26  ? -48.248 -2.304  55.310  1.00 41.04 ? 49   TRP   B CE2 1 
ATOM   4558 C  CE3 . TRP   B 1 26  ? -46.623 -1.430  56.889  1.00 36.22 ? 49   TRP   B CE3 1 
ATOM   4559 C  CZ2 . TRP   B 1 26  ? -47.261 -2.505  54.343  1.00 41.09 ? 49   TRP   B CZ2 1 
ATOM   4560 C  CZ3 . TRP   B 1 26  ? -45.653 -1.636  55.931  1.00 40.26 ? 49   TRP   B CZ3 1 
ATOM   4561 C  CH2 . TRP   B 1 26  ? -45.969 -2.166  54.678  1.00 40.57 ? 49   TRP   B CH2 1 
ATOM   4562 N  N   . THR   B 1 27  ? -48.290 -4.381  59.465  1.00 39.56 ? 50   THR   B N   1 
ATOM   4563 C  CA  . THR   B 1 27  ? -47.139 -5.268  59.508  1.00 44.14 ? 50   THR   B CA  1 
ATOM   4564 C  C   . THR   B 1 27  ? -46.815 -5.714  58.084  1.00 47.73 ? 50   THR   B C   1 
ATOM   4565 O  O   . THR   B 1 27  ? -47.664 -6.298  57.407  1.00 48.03 ? 50   THR   B O   1 
ATOM   4566 C  CB  . THR   B 1 27  ? -47.468 -6.456  60.412  1.00 45.66 ? 50   THR   B CB  1 
ATOM   4567 O  OG1 . THR   B 1 27  ? -47.678 -5.781  61.644  1.00 48.57 ? 50   THR   B OG1 1 
ATOM   4568 C  CG2 . THR   B 1 27  ? -46.360 -7.490  60.536  1.00 46.37 ? 50   THR   B CG2 1 
ATOM   4569 N  N   . PRO   B 1 28  ? -45.586 -5.470  57.575  1.00 45.70 ? 51   PRO   B N   1 
ATOM   4570 C  CA  . PRO   B 1 28  ? -45.237 -5.897  56.225  1.00 41.94 ? 51   PRO   B CA  1 
ATOM   4571 C  C   . PRO   B 1 28  ? -45.008 -7.400  56.291  1.00 40.45 ? 51   PRO   B C   1 
ATOM   4572 O  O   . PRO   B 1 28  ? -44.694 -7.946  57.347  1.00 39.44 ? 51   PRO   B O   1 
ATOM   4573 C  CB  . PRO   B 1 28  ? -43.983 -5.087  55.838  1.00 46.41 ? 51   PRO   B CB  1 
ATOM   4574 C  CG  . PRO   B 1 28  ? -43.604 -4.296  57.086  1.00 48.30 ? 51   PRO   B CG  1 
ATOM   4575 C  CD  . PRO   B 1 28  ? -44.488 -4.750  58.238  1.00 48.55 ? 51   PRO   B CD  1 
ATOM   4576 N  N   . LYS   B 1 29  ? -45.219 -8.067  55.161  1.00 38.60 ? 52   LYS   B N   1 
ATOM   4577 C  CA  . LYS   B 1 29  ? -45.151 -9.511  55.098  1.00 35.71 ? 52   LYS   B CA  1 
ATOM   4578 C  C   . LYS   B 1 29  ? -43.968 -9.885  54.231  1.00 36.95 ? 52   LYS   B C   1 
ATOM   4579 O  O   . LYS   B 1 29  ? -43.659 -9.156  53.301  1.00 34.35 ? 52   LYS   B O   1 
ATOM   4580 C  CB  . LYS   B 1 29  ? -46.418 -10.045 54.425  1.00 34.68 ? 52   LYS   B CB  1 
ATOM   4581 C  CG  . LYS   B 1 29  ? -47.685 -9.734  55.167  1.00 37.78 ? 52   LYS   B CG  1 
ATOM   4582 C  CD  . LYS   B 1 29  ? -47.871 -10.652 56.369  1.00 41.38 ? 52   LYS   B CD  1 
ATOM   4583 C  CE  . LYS   B 1 29  ? -48.846 -10.051 57.318  1.00 44.08 ? 52   LYS   B CE  1 
ATOM   4584 N  NZ  . LYS   B 1 29  ? -48.997 -10.971 58.436  1.00 49.87 ? 52   LYS   B NZ  1 
ATOM   4585 N  N   . PRO   B 1 30  ? -43.301 -11.032 54.476  1.00 43.14 ? 53   PRO   B N   1 
ATOM   4586 C  CA  . PRO   B 1 30  ? -42.193 -11.452 53.628  1.00 44.12 ? 53   PRO   B CA  1 
ATOM   4587 C  C   . PRO   B 1 30  ? -42.710 -11.889 52.256  1.00 43.96 ? 53   PRO   B C   1 
ATOM   4588 O  O   . PRO   B 1 30  ? -43.520 -12.810 52.140  1.00 39.96 ? 53   PRO   B O   1 
ATOM   4589 C  CB  . PRO   B 1 30  ? -41.535 -12.590 54.414  1.00 43.13 ? 53   PRO   B CB  1 
ATOM   4590 C  CG  . PRO   B 1 30  ? -42.645 -13.135 55.295  1.00 47.42 ? 53   PRO   B CG  1 
ATOM   4591 C  CD  . PRO   B 1 30  ? -43.584 -11.976 55.566  1.00 45.10 ? 53   PRO   B CD  1 
ATOM   4592 N  N   . SER   B 1 31  ? -42.222 -11.217 51.209  1.00 39.61 ? 54   SER   B N   1 
ATOM   4593 C  CA  . SER   B 1 31  ? -42.649 -11.518 49.857  1.00 32.83 ? 54   SER   B CA  1 
ATOM   4594 C  C   . SER   B 1 31  ? -42.183 -12.917 49.484  1.00 29.22 ? 54   SER   B C   1 
ATOM   4595 O  O   . SER   B 1 31  ? -41.092 -13.328 49.841  1.00 28.84 ? 54   SER   B O   1 
ATOM   4596 C  CB  . SER   B 1 31  ? -42.152 -10.468 48.890  1.00 33.82 ? 54   SER   B CB  1 
ATOM   4597 O  OG  . SER   B 1 31  ? -42.844 -10.578 47.657  1.00 37.44 ? 54   SER   B OG  1 
ATOM   4598 N  N   . PRO   B 1 32  ? -42.985 -13.713 48.756  1.00 27.00 ? 55   PRO   B N   1 
ATOM   4599 C  CA  . PRO   B 1 32  ? -42.545 -15.031 48.301  1.00 25.96 ? 55   PRO   B CA  1 
ATOM   4600 C  C   . PRO   B 1 32  ? -41.265 -14.978 47.461  1.00 25.32 ? 55   PRO   B C   1 
ATOM   4601 O  O   . PRO   B 1 32  ? -40.547 -15.976 47.332  1.00 27.38 ? 55   PRO   B O   1 
ATOM   4602 C  CB  . PRO   B 1 32  ? -43.713 -15.562 47.463  1.00 26.97 ? 55   PRO   B CB  1 
ATOM   4603 C  CG  . PRO   B 1 32  ? -44.887 -14.719 47.856  1.00 26.67 ? 55   PRO   B CG  1 
ATOM   4604 C  CD  . PRO   B 1 32  ? -44.364 -13.386 48.357  1.00 26.22 ? 55   PRO   B CD  1 
ATOM   4605 N  N   . MET   B 1 33  ? -41.055 -13.828 46.810  1.00 26.51 ? 56   MET   B N   1 
ATOM   4606 C  CA  . MET   B 1 33  ? -39.868 -13.570 46.018  1.00 24.38 ? 56   MET   B CA  1 
ATOM   4607 C  C   . MET   B 1 33  ? -39.563 -12.084 46.141  1.00 23.15 ? 56   MET   B C   1 
ATOM   4608 O  O   . MET   B 1 33  ? -40.455 -11.277 46.387  1.00 25.70 ? 56   MET   B O   1 
ATOM   4609 C  CB  . MET   B 1 33  ? -40.068 -13.929 44.539  1.00 25.68 ? 56   MET   B CB  1 
ATOM   4610 C  CG  . MET   B 1 33  ? -40.561 -15.333 44.264  1.00 26.12 ? 56   MET   B CG  1 
ATOM   4611 S  SD  . MET   B 1 33  ? -40.680 -15.625 42.487  1.00 25.33 ? 56   MET   B SD  1 
ATOM   4612 C  CE  . MET   B 1 33  ? -39.053 -16.290 42.107  1.00 26.34 ? 56   MET   B CE  1 
ATOM   4613 N  N   . THR   B 1 34  ? -38.294 -11.706 45.976  1.00 23.97 ? 57   THR   B N   1 
ATOM   4614 C  CA  . THR   B 1 34  ? -37.948 -10.296 46.012  1.00 24.66 ? 57   THR   B CA  1 
ATOM   4615 C  C   . THR   B 1 34  ? -37.646 -9.796  44.598  1.00 21.86 ? 57   THR   B C   1 
ATOM   4616 O  O   . THR   B 1 34  ? -36.731 -10.304 43.957  1.00 20.73 ? 57   THR   B O   1 
ATOM   4617 C  CB  . THR   B 1 34  ? -36.763 -10.074 46.953  1.00 28.28 ? 57   THR   B CB  1 
ATOM   4618 O  OG1 . THR   B 1 34  ? -37.209 -10.435 48.255  1.00 30.24 ? 57   THR   B OG1 1 
ATOM   4619 C  CG2 . THR   B 1 34  ? -36.369 -8.614  47.071  1.00 28.04 ? 57   THR   B CG2 1 
ATOM   4620 N  N   . THR   B 1 35  ? -38.406 -8.786  44.155  1.00 23.58 ? 58   THR   B N   1 
ATOM   4621 C  CA  . THR   B 1 35  ? -38.122 -8.069  42.923  1.00 21.26 ? 58   THR   B CA  1 
ATOM   4622 C  C   . THR   B 1 35  ? -37.211 -6.893  43.268  1.00 23.41 ? 58   THR   B C   1 
ATOM   4623 O  O   . THR   B 1 35  ? -37.069 -6.513  44.442  1.00 21.31 ? 58   THR   B O   1 
ATOM   4624 C  CB  . THR   B 1 35  ? -39.396 -7.596  42.225  1.00 19.71 ? 58   THR   B CB  1 
ATOM   4625 O  OG1 . THR   B 1 35  ? -39.811 -6.405  42.882  1.00 17.45 ? 58   THR   B OG1 1 
ATOM   4626 C  CG2 . THR   B 1 35  ? -40.440 -8.696  42.084  1.00 19.59 ? 58   THR   B CG2 1 
ATOM   4627 N  N   . PRO   B 1 36  ? -36.536 -6.291  42.261  1.00 21.79 ? 59   PRO   B N   1 
ATOM   4628 C  CA  . PRO   B 1 36  ? -35.670 -5.146  42.529  1.00 20.71 ? 59   PRO   B CA  1 
ATOM   4629 C  C   . PRO   B 1 36  ? -36.364 -4.012  43.281  1.00 19.20 ? 59   PRO   B C   1 
ATOM   4630 O  O   . PRO   B 1 36  ? -35.682 -3.179  43.836  1.00 19.62 ? 59   PRO   B O   1 
ATOM   4631 C  CB  . PRO   B 1 36  ? -35.220 -4.740  41.119  1.00 20.97 ? 59   PRO   B CB  1 
ATOM   4632 C  CG  . PRO   B 1 36  ? -35.263 -6.031  40.334  1.00 21.87 ? 59   PRO   B CG  1 
ATOM   4633 C  CD  . PRO   B 1 36  ? -36.483 -6.741  40.856  1.00 20.52 ? 59   PRO   B CD  1 
ATOM   4634 N  N   . TRP   B 1 37  ? -37.712 -3.977  43.296  1.00 20.52 ? 60   TRP   B N   1 
ATOM   4635 C  CA  . TRP   B 1 37  ? -38.467 -2.842  43.800  1.00 17.88 ? 60   TRP   B CA  1 
ATOM   4636 C  C   . TRP   B 1 37  ? -39.313 -3.170  45.041  1.00 17.82 ? 60   TRP   B C   1 
ATOM   4637 O  O   . TRP   B 1 37  ? -39.953 -2.255  45.560  1.00 17.69 ? 60   TRP   B O   1 
ATOM   4638 C  CB  . TRP   B 1 37  ? -39.364 -2.273  42.693  1.00 21.98 ? 60   TRP   B CB  1 
ATOM   4639 C  CG  . TRP   B 1 37  ? -38.641 -2.082  41.388  1.00 21.21 ? 60   TRP   B CG  1 
ATOM   4640 C  CD1 . TRP   B 1 37  ? -37.900 -1.011  40.981  1.00 21.45 ? 60   TRP   B CD1 1 
ATOM   4641 C  CD2 . TRP   B 1 37  ? -38.584 -3.045  40.316  1.00 22.90 ? 60   TRP   B CD2 1 
ATOM   4642 N  NE1 . TRP   B 1 37  ? -37.423 -1.220  39.705  1.00 22.50 ? 60   TRP   B NE1 1 
ATOM   4643 C  CE2 . TRP   B 1 37  ? -37.805 -2.468  39.282  1.00 21.75 ? 60   TRP   B CE2 1 
ATOM   4644 C  CE3 . TRP   B 1 37  ? -39.134 -4.322  40.130  1.00 21.48 ? 60   TRP   B CE3 1 
ATOM   4645 C  CZ2 . TRP   B 1 37  ? -37.556 -3.135  38.087  1.00 20.06 ? 60   TRP   B CZ2 1 
ATOM   4646 C  CZ3 . TRP   B 1 37  ? -38.868 -4.985  38.951  1.00 22.59 ? 60   TRP   B CZ3 1 
ATOM   4647 C  CH2 . TRP   B 1 37  ? -38.090 -4.396  37.947  1.00 22.70 ? 60   TRP   B CH2 1 
ATOM   4648 N  N   . THR   B 1 38  ? -39.331 -4.431  45.483  1.00 19.87 ? 61   THR   B N   1 
ATOM   4649 C  CA  . THR   B 1 38  ? -40.169 -4.834  46.601  1.00 23.29 ? 61   THR   B CA  1 
ATOM   4650 C  C   . THR   B 1 38  ? -39.855 -3.945  47.800  1.00 26.65 ? 61   THR   B C   1 
ATOM   4651 O  O   . THR   B 1 38  ? -40.767 -3.455  48.454  1.00 27.08 ? 61   THR   B O   1 
ATOM   4652 C  CB  . THR   B 1 38  ? -39.943 -6.298  46.957  1.00 23.70 ? 61   THR   B CB  1 
ATOM   4653 O  OG1 . THR   B 1 38  ? -40.119 -7.074  45.781  1.00 24.16 ? 61   THR   B OG1 1 
ATOM   4654 C  CG2 . THR   B 1 38  ? -40.849 -6.748  48.094  1.00 24.35 ? 61   THR   B CG2 1 
ATOM   4655 N  N   . ASP   B 1 39  ? -38.554 -3.703  48.025  1.00 27.24 ? 62   ASP   B N   1 
ATOM   4656 C  CA  . ASP   B 1 39  ? -38.092 -2.988  49.201  1.00 29.53 ? 62   ASP   B CA  1 
ATOM   4657 C  C   . ASP   B 1 39  ? -38.077 -1.485  48.936  1.00 28.37 ? 62   ASP   B C   1 
ATOM   4658 O  O   . ASP   B 1 39  ? -37.586 -0.741  49.773  1.00 31.00 ? 62   ASP   B O   1 
ATOM   4659 C  CB  . ASP   B 1 39  ? -36.764 -3.562  49.684  1.00 32.60 ? 62   ASP   B CB  1 
ATOM   4660 C  CG  . ASP   B 1 39  ? -35.569 -3.395  48.746  1.00 41.30 ? 62   ASP   B CG  1 
ATOM   4661 O  OD1 . ASP   B 1 39  ? -35.682 -2.611  47.762  1.00 42.30 ? 62   ASP   B OD1 1 
ATOM   4662 O  OD2 . ASP   B 1 39  ? -34.535 -4.073  48.984  1.00 47.14 ? 62   ASP   B OD2 1 
ATOM   4663 N  N   . GLN   B 1 40  ? -38.575 -1.036  47.774  1.00 25.78 ? 63   GLN   B N   1 
ATOM   4664 C  CA  . GLN   B 1 40  ? -38.608 0.372   47.427  1.00 27.02 ? 63   GLN   B CA  1 
ATOM   4665 C  C   . GLN   B 1 40  ? -40.033 0.908   47.464  1.00 26.06 ? 63   GLN   B C   1 
ATOM   4666 O  O   . GLN   B 1 40  ? -40.286 2.016   47.015  1.00 27.11 ? 63   GLN   B O   1 
ATOM   4667 C  CB  . GLN   B 1 40  ? -38.011 0.573   46.037  1.00 31.38 ? 63   GLN   B CB  1 
ATOM   4668 C  CG  . GLN   B 1 40  ? -36.572 0.080   45.960  1.00 38.45 ? 63   GLN   B CG  1 
ATOM   4669 C  CD  . GLN   B 1 40  ? -35.911 0.328   44.623  1.00 43.06 ? 63   GLN   B CD  1 
ATOM   4670 O  OE1 . GLN   B 1 40  ? -36.457 0.991   43.738  1.00 49.02 ? 63   GLN   B OE1 1 
ATOM   4671 N  NE2 . GLN   B 1 40  ? -34.717 -0.217  44.463  1.00 46.47 ? 63   GLN   B NE2 1 
ATOM   4672 N  N   . VAL   B 1 41  ? -40.970 0.139   48.017  1.00 22.85 ? 64   VAL   B N   1 
ATOM   4673 C  CA  . VAL   B 1 41  ? -42.348 0.596   48.066  1.00 22.84 ? 64   VAL   B CA  1 
ATOM   4674 C  C   . VAL   B 1 41  ? -42.547 1.462   49.307  1.00 23.02 ? 64   VAL   B C   1 
ATOM   4675 O  O   . VAL   B 1 41  ? -42.389 0.982   50.428  1.00 23.25 ? 64   VAL   B O   1 
ATOM   4676 C  CB  . VAL   B 1 41  ? -43.289 -0.621  48.055  1.00 24.33 ? 64   VAL   B CB  1 
ATOM   4677 C  CG1 . VAL   B 1 41  ? -44.749 -0.189  48.013  1.00 26.25 ? 64   VAL   B CG1 1 
ATOM   4678 C  CG2 . VAL   B 1 41  ? -42.982 -1.564  46.893  1.00 27.02 ? 64   VAL   B CG2 1 
ATOM   4679 N  N   . PRO   B 1 42  ? -42.911 2.743   49.151  1.00 22.50 ? 65   PRO   B N   1 
ATOM   4680 C  CA  . PRO   B 1 42  ? -43.187 3.614   50.298  1.00 24.91 ? 65   PRO   B CA  1 
ATOM   4681 C  C   . PRO   B 1 42  ? -44.341 3.040   51.118  1.00 32.25 ? 65   PRO   B C   1 
ATOM   4682 O  O   . PRO   B 1 42  ? -45.201 2.333   50.577  1.00 27.56 ? 65   PRO   B O   1 
ATOM   4683 C  CB  . PRO   B 1 42  ? -43.553 4.970   49.704  1.00 24.09 ? 65   PRO   B CB  1 
ATOM   4684 C  CG  . PRO   B 1 42  ? -43.188 4.888   48.232  1.00 23.29 ? 65   PRO   B CG  1 
ATOM   4685 C  CD  . PRO   B 1 42  ? -43.037 3.429   47.862  1.00 22.23 ? 65   PRO   B CD  1 
ATOM   4686 N  N   . VAL   B 1 43  ? -44.339 3.323   52.430  1.00 32.61 ? 66   VAL   B N   1 
ATOM   4687 C  CA  . VAL   B 1 43  ? -45.391 2.834   53.310  1.00 34.72 ? 66   VAL   B CA  1 
ATOM   4688 C  C   . VAL   B 1 43  ? -46.617 3.743   53.172  1.00 35.52 ? 66   VAL   B C   1 
ATOM   4689 O  O   . VAL   B 1 43  ? -47.724 3.242   52.936  1.00 34.56 ? 66   VAL   B O   1 
ATOM   4690 C  CB  . VAL   B 1 43  ? -44.879 2.697   54.760  1.00 35.46 ? 66   VAL   B CB  1 
ATOM   4691 C  CG1 . VAL   B 1 43  ? -45.961 2.245   55.736  1.00 34.92 ? 66   VAL   B CG1 1 
ATOM   4692 C  CG2 . VAL   B 1 43  ? -43.704 1.732   54.844  1.00 33.83 ? 66   VAL   B CG2 1 
ATOM   4693 N  N   . ASP   B 1 44  ? -46.401 5.071   53.242  1.00 33.21 ? 67   ASP   B N   1 
ATOM   4694 C  CA  . ASP   B 1 44  ? -47.477 6.052   53.295  1.00 37.99 ? 67   ASP   B CA  1 
ATOM   4695 C  C   . ASP   B 1 44  ? -47.858 6.595   51.921  1.00 36.69 ? 67   ASP   B C   1 
ATOM   4696 O  O   . ASP   B 1 44  ? -48.938 7.170   51.761  1.00 33.85 ? 67   ASP   B O   1 
ATOM   4697 C  CB  . ASP   B 1 44  ? -47.112 7.254   54.156  1.00 42.33 ? 67   ASP   B CB  1 
ATOM   4698 C  CG  . ASP   B 1 44  ? -46.943 6.956   55.640  1.00 49.95 ? 67   ASP   B CG  1 
ATOM   4699 O  OD1 . ASP   B 1 44  ? -46.324 5.919   55.967  1.00 52.01 ? 67   ASP   B OD1 1 
ATOM   4700 O  OD2 . ASP   B 1 44  ? -47.431 7.767   56.457  1.00 58.81 ? 67   ASP   B OD2 1 
ATOM   4701 N  N   . ASN   B 1 45  ? -46.954 6.491   50.940  1.00 34.44 ? 68   ASN   B N   1 
ATOM   4702 C  CA  . ASN   B 1 45  ? -47.221 7.152   49.675  1.00 36.09 ? 68   ASN   B CA  1 
ATOM   4703 C  C   . ASN   B 1 45  ? -46.801 6.255   48.513  1.00 30.59 ? 68   ASN   B C   1 
ATOM   4704 O  O   . ASN   B 1 45  ? -46.089 6.720   47.628  1.00 26.91 ? 68   ASN   B O   1 
ATOM   4705 C  CB  . ASN   B 1 45  ? -46.578 8.536   49.647  1.00 39.43 ? 68   ASN   B CB  1 
ATOM   4706 C  CG  . ASN   B 1 45  ? -47.192 9.464   50.669  1.00 45.86 ? 68   ASN   B CG  1 
ATOM   4707 O  OD1 . ASN   B 1 45  ? -46.600 9.708   51.726  1.00 51.32 ? 68   ASN   B OD1 1 
ATOM   4708 N  ND2 . ASN   B 1 45  ? -48.385 9.972   50.390  1.00 45.52 ? 68   ASN   B ND2 1 
ATOM   4709 N  N   . PRO   B 1 46  ? -47.253 4.977   48.458  1.00 29.15 ? 69   PRO   B N   1 
ATOM   4710 C  CA  . PRO   B 1 46  ? -46.989 4.129   47.293  1.00 28.56 ? 69   PRO   B CA  1 
ATOM   4711 C  C   . PRO   B 1 46  ? -47.700 4.661   46.050  1.00 25.21 ? 69   PRO   B C   1 
ATOM   4712 O  O   . PRO   B 1 46  ? -48.690 5.397   46.136  1.00 25.43 ? 69   PRO   B O   1 
ATOM   4713 C  CB  . PRO   B 1 46  ? -47.493 2.736   47.690  1.00 29.59 ? 69   PRO   B CB  1 
ATOM   4714 C  CG  . PRO   B 1 46  ? -48.606 3.034   48.673  1.00 29.90 ? 69   PRO   B CG  1 
ATOM   4715 C  CD  . PRO   B 1 46  ? -48.134 4.300   49.431  1.00 30.02 ? 69   PRO   B CD  1 
ATOM   4716 N  N   . LEU   B 1 47  ? -47.155 4.244   44.902  1.00 25.13 ? 70   LEU   B N   1 
ATOM   4717 C  CA  . LEU   B 1 47  ? -47.623 4.607   43.575  1.00 25.65 ? 70   LEU   B CA  1 
ATOM   4718 C  C   . LEU   B 1 47  ? -48.062 6.064   43.547  1.00 23.50 ? 70   LEU   B C   1 
ATOM   4719 O  O   . LEU   B 1 47  ? -49.240 6.367   43.365  1.00 22.96 ? 70   LEU   B O   1 
ATOM   4720 C  CB  . LEU   B 1 47  ? -48.711 3.626   43.139  1.00 28.14 ? 70   LEU   B CB  1 
ATOM   4721 C  CG  . LEU   B 1 47  ? -48.234 2.222   42.753  1.00 32.24 ? 70   LEU   B CG  1 
ATOM   4722 C  CD1 . LEU   B 1 47  ? -47.719 1.370   43.888  1.00 36.72 ? 70   LEU   B CD1 1 
ATOM   4723 C  CD2 . LEU   B 1 47  ? -49.387 1.499   42.072  1.00 33.92 ? 70   LEU   B CD2 1 
ATOM   4724 N  N   . PRO   B 1 48  ? -47.115 7.017   43.756  1.00 25.47 ? 71   PRO   B N   1 
ATOM   4725 C  CA  . PRO   B 1 48  ? -47.435 8.450   43.824  1.00 23.93 ? 71   PRO   B CA  1 
ATOM   4726 C  C   . PRO   B 1 48  ? -47.754 9.175   42.527  1.00 22.77 ? 71   PRO   B C   1 
ATOM   4727 O  O   . PRO   B 1 48  ? -48.292 10.272  42.533  1.00 19.55 ? 71   PRO   B O   1 
ATOM   4728 C  CB  . PRO   B 1 48  ? -46.159 9.036   44.472  1.00 25.57 ? 71   PRO   B CB  1 
ATOM   4729 C  CG  . PRO   B 1 48  ? -45.060 8.101   44.044  1.00 25.17 ? 71   PRO   B CG  1 
ATOM   4730 C  CD  . PRO   B 1 48  ? -45.700 6.731   44.080  1.00 26.79 ? 71   PRO   B CD  1 
ATOM   4731 N  N   . GLU   B 1 49  ? -47.400 8.557   41.396  1.00 23.61 ? 72   GLU   B N   1 
ATOM   4732 C  CA  . GLU   B 1 49  ? -47.481 9.235   40.115  1.00 20.39 ? 72   GLU   B CA  1 
ATOM   4733 C  C   . GLU   B 1 49  ? -48.926 9.468   39.687  1.00 20.77 ? 72   GLU   B C   1 
ATOM   4734 O  O   . GLU   B 1 49  ? -49.829 8.739   40.088  1.00 21.79 ? 72   GLU   B O   1 
ATOM   4735 C  CB  . GLU   B 1 49  ? -46.762 8.401   39.051  1.00 22.21 ? 72   GLU   B CB  1 
ATOM   4736 C  CG  . GLU   B 1 49  ? -45.262 8.261   39.304  1.00 21.65 ? 72   GLU   B CG  1 
ATOM   4737 C  CD  . GLU   B 1 49  ? -44.805 7.220   40.299  1.00 23.91 ? 72   GLU   B CD  1 
ATOM   4738 O  OE1 . GLU   B 1 49  ? -45.604 6.383   40.781  1.00 27.09 ? 72   GLU   B OE1 1 
ATOM   4739 O  OE2 . GLU   B 1 49  ? -43.593 7.262   40.591  1.00 25.86 ? 72   GLU   B OE2 1 
ATOM   4740 N  N   . TYR   B 1 50  ? -49.108 10.506  38.874  1.00 20.33 ? 73   TYR   B N   1 
ATOM   4741 C  CA  . TYR   B 1 50  ? -50.405 10.888  38.343  1.00 20.40 ? 73   TYR   B CA  1 
ATOM   4742 C  C   . TYR   B 1 50  ? -51.001 9.679   37.628  1.00 22.67 ? 73   TYR   B C   1 
ATOM   4743 O  O   . TYR   B 1 50  ? -50.417 9.172   36.667  1.00 20.99 ? 73   TYR   B O   1 
ATOM   4744 C  CB  . TYR   B 1 50  ? -50.368 12.053  37.357  1.00 19.70 ? 73   TYR   B CB  1 
ATOM   4745 C  CG  . TYR   B 1 50  ? -51.716 12.709  37.081  1.00 21.49 ? 73   TYR   B CG  1 
ATOM   4746 C  CD1 . TYR   B 1 50  ? -52.326 13.514  38.033  1.00 21.23 ? 73   TYR   B CD1 1 
ATOM   4747 C  CD2 . TYR   B 1 50  ? -52.349 12.589  35.850  1.00 19.54 ? 73   TYR   B CD2 1 
ATOM   4748 C  CE1 . TYR   B 1 50  ? -53.548 14.126  37.810  1.00 21.02 ? 73   TYR   B CE1 1 
ATOM   4749 C  CE2 . TYR   B 1 50  ? -53.551 13.221  35.593  1.00 20.14 ? 73   TYR   B CE2 1 
ATOM   4750 C  CZ  . TYR   B 1 50  ? -54.155 13.998  36.575  1.00 21.32 ? 73   TYR   B CZ  1 
ATOM   4751 O  OH  . TYR   B 1 50  ? -55.341 14.609  36.307  1.00 21.64 ? 73   TYR   B OH  1 
ATOM   4752 N  N   . PRO   B 1 51  ? -52.211 9.224   38.026  1.00 23.09 ? 74   PRO   B N   1 
ATOM   4753 C  CA  . PRO   B 1 51  ? -52.747 7.965   37.501  1.00 22.14 ? 74   PRO   B CA  1 
ATOM   4754 C  C   . PRO   B 1 51  ? -53.412 7.987   36.124  1.00 20.97 ? 74   PRO   B C   1 
ATOM   4755 O  O   . PRO   B 1 51  ? -53.803 6.933   35.640  1.00 22.31 ? 74   PRO   B O   1 
ATOM   4756 C  CB  . PRO   B 1 51  ? -53.739 7.508   38.601  1.00 23.95 ? 74   PRO   B CB  1 
ATOM   4757 C  CG  . PRO   B 1 51  ? -53.914 8.675   39.549  1.00 26.19 ? 74   PRO   B CG  1 
ATOM   4758 C  CD  . PRO   B 1 51  ? -53.083 9.849   39.041  1.00 25.07 ? 74   PRO   B CD  1 
ATOM   4759 N  N   . ARG   B 1 52  ? -53.579 9.171   35.516  1.00 17.92 ? 75   ARG   B N   1 
ATOM   4760 C  CA  . ARG   B 1 52  ? -54.357 9.341   34.297  1.00 19.13 ? 75   ARG   B CA  1 
ATOM   4761 C  C   . ARG   B 1 52  ? -53.598 10.254  33.333  1.00 18.72 ? 75   ARG   B C   1 
ATOM   4762 O  O   . ARG   B 1 52  ? -54.071 11.315  32.913  1.00 16.47 ? 75   ARG   B O   1 
ATOM   4763 C  CB  . ARG   B 1 52  ? -55.743 9.913   34.614  1.00 18.52 ? 75   ARG   B CB  1 
ATOM   4764 C  CG  . ARG   B 1 52  ? -56.751 9.759   33.487  1.00 20.84 ? 75   ARG   B CG  1 
ATOM   4765 C  CD  . ARG   B 1 52  ? -58.105 10.345  33.853  1.00 22.27 ? 75   ARG   B CD  1 
ATOM   4766 N  NE  . ARG   B 1 52  ? -57.943 11.789  34.054  1.00 22.58 ? 75   ARG   B NE  1 
ATOM   4767 C  CZ  . ARG   B 1 52  ? -58.577 12.526  34.951  1.00 25.85 ? 75   ARG   B CZ  1 
ATOM   4768 N  NH1 . ARG   B 1 52  ? -59.633 12.052  35.580  1.00 23.88 ? 75   ARG   B NH1 1 
ATOM   4769 N  NH2 . ARG   B 1 52  ? -58.194 13.771  35.158  1.00 25.99 ? 75   ARG   B NH2 1 
ATOM   4770 N  N   . PRO   B 1 53  ? -52.381 9.848   32.904  1.00 18.28 ? 76   PRO   B N   1 
ATOM   4771 C  CA  . PRO   B 1 53  ? -51.511 10.757  32.144  1.00 18.30 ? 76   PRO   B CA  1 
ATOM   4772 C  C   . PRO   B 1 53  ? -51.981 11.223  30.779  1.00 18.05 ? 76   PRO   B C   1 
ATOM   4773 O  O   . PRO   B 1 53  ? -51.375 12.151  30.255  1.00 17.32 ? 76   PRO   B O   1 
ATOM   4774 C  CB  . PRO   B 1 53  ? -50.186 9.983   31.990  1.00 19.29 ? 76   PRO   B CB  1 
ATOM   4775 C  CG  . PRO   B 1 53  ? -50.511 8.563   32.328  1.00 20.43 ? 76   PRO   B CG  1 
ATOM   4776 C  CD  . PRO   B 1 53  ? -51.794 8.523   33.130  1.00 18.50 ? 76   PRO   B CD  1 
ATOM   4777 N  N   . GLN   B 1 54  ? -53.033 10.598  30.196  1.00 16.35 ? 77   GLN   B N   1 
ATOM   4778 C  CA  . GLN   B 1 54  ? -53.576 11.071  28.932  1.00 16.37 ? 77   GLN   B CA  1 
ATOM   4779 C  C   . GLN   B 1 54  ? -54.798 11.987  29.118  1.00 16.85 ? 77   GLN   B C   1 
ATOM   4780 O  O   . GLN   B 1 54  ? -55.405 12.399  28.138  1.00 17.69 ? 77   GLN   B O   1 
ATOM   4781 C  CB  . GLN   B 1 54  ? -53.910 9.912   27.989  1.00 15.82 ? 77   GLN   B CB  1 
ATOM   4782 C  CG  . GLN   B 1 54  ? -53.927 10.331  26.531  1.00 15.53 ? 77   GLN   B CG  1 
ATOM   4783 C  CD  . GLN   B 1 54  ? -53.927 9.169   25.563  1.00 14.82 ? 77   GLN   B CD  1 
ATOM   4784 O  OE1 . GLN   B 1 54  ? -54.325 8.033   25.886  1.00 16.44 ? 77   GLN   B OE1 1 
ATOM   4785 N  NE2 . GLN   B 1 54  ? -53.538 9.485   24.338  1.00 15.49 ? 77   GLN   B NE2 1 
ATOM   4786 N  N   . LEU   B 1 55  ? -55.117 12.364  30.361  1.00 18.62 ? 78   LEU   B N   1 
ATOM   4787 C  CA  . LEU   B 1 55  ? -56.157 13.361  30.607  1.00 19.04 ? 78   LEU   B CA  1 
ATOM   4788 C  C   . LEU   B 1 55  ? -55.838 14.072  31.916  1.00 18.90 ? 78   LEU   B C   1 
ATOM   4789 O  O   . LEU   B 1 55  ? -56.189 13.587  32.992  1.00 20.40 ? 78   LEU   B O   1 
ATOM   4790 C  CB  . LEU   B 1 55  ? -57.556 12.740  30.634  1.00 19.69 ? 78   LEU   B CB  1 
ATOM   4791 C  CG  . LEU   B 1 55  ? -58.740 13.704  30.512  1.00 21.74 ? 78   LEU   B CG  1 
ATOM   4792 C  CD1 . LEU   B 1 55  ? -58.889 14.155  29.108  1.00 22.99 ? 78   LEU   B CD1 1 
ATOM   4793 C  CD2 . LEU   B 1 55  ? -60.017 13.033  30.951  1.00 25.57 ? 78   LEU   B CD2 1 
ATOM   4794 N  N   . THR   B 1 56  ? -55.150 15.218  31.808  1.00 19.30 ? 79   THR   B N   1 
ATOM   4795 C  CA  . THR   B 1 56  ? -54.524 15.813  32.975  1.00 19.07 ? 79   THR   B CA  1 
ATOM   4796 C  C   . THR   B 1 56  ? -55.185 17.124  33.383  1.00 18.24 ? 79   THR   B C   1 
ATOM   4797 O  O   . THR   B 1 56  ? -55.572 17.944  32.544  1.00 19.83 ? 79   THR   B O   1 
ATOM   4798 C  CB  . THR   B 1 56  ? -53.044 16.055  32.695  1.00 18.54 ? 79   THR   B CB  1 
ATOM   4799 O  OG1 . THR   B 1 56  ? -53.128 17.044  31.681  1.00 20.38 ? 79   THR   B OG1 1 
ATOM   4800 C  CG2 . THR   B 1 56  ? -52.346 14.754  32.326  1.00 21.27 ? 79   THR   B CG2 1 
ATOM   4801 N  N   . ARG   B 1 57  ? -55.206 17.288  34.704  1.00 19.06 ? 80   ARG   B N   1 
ATOM   4802 C  CA  . ARG   B 1 57  ? -55.384 18.574  35.363  1.00 21.16 ? 80   ARG   B CA  1 
ATOM   4803 C  C   . ARG   B 1 57  ? -54.312 18.720  36.439  1.00 21.14 ? 80   ARG   B C   1 
ATOM   4804 O  O   . ARG   B 1 57  ? -53.822 17.735  36.985  1.00 20.94 ? 80   ARG   B O   1 
ATOM   4805 C  CB  . ARG   B 1 57  ? -56.746 18.677  36.050  1.00 20.56 ? 80   ARG   B CB  1 
ATOM   4806 C  CG  . ARG   B 1 57  ? -57.921 18.713  35.083  1.00 22.05 ? 80   ARG   B CG  1 
ATOM   4807 C  CD  . ARG   B 1 57  ? -59.252 18.685  35.846  1.00 21.15 ? 80   ARG   B CD  1 
ATOM   4808 N  NE  . ARG   B 1 57  ? -60.339 18.523  34.872  1.00 21.54 ? 80   ARG   B NE  1 
ATOM   4809 C  CZ  . ARG   B 1 57  ? -60.934 17.381  34.549  1.00 19.61 ? 80   ARG   B CZ  1 
ATOM   4810 N  NH1 . ARG   B 1 57  ? -60.587 16.263  35.158  1.00 21.26 ? 80   ARG   B NH1 1 
ATOM   4811 N  NH2 . ARG   B 1 57  ? -61.871 17.389  33.610  1.00 22.13 ? 80   ARG   B NH2 1 
ATOM   4812 N  N   . PRO   B 1 58  ? -53.905 19.974  36.746  1.00 25.50 ? 81   PRO   B N   1 
ATOM   4813 C  CA  . PRO   B 1 58  ? -52.895 20.231  37.773  1.00 24.87 ? 81   PRO   B CA  1 
ATOM   4814 C  C   . PRO   B 1 58  ? -53.238 19.839  39.202  1.00 24.13 ? 81   PRO   B C   1 
ATOM   4815 O  O   . PRO   B 1 58  ? -52.355 19.411  39.949  1.00 23.05 ? 81   PRO   B O   1 
ATOM   4816 C  CB  . PRO   B 1 58  ? -52.622 21.738  37.652  1.00 27.35 ? 81   PRO   B CB  1 
ATOM   4817 C  CG  . PRO   B 1 58  ? -53.757 22.302  36.847  1.00 26.30 ? 81   PRO   B CG  1 
ATOM   4818 C  CD  . PRO   B 1 58  ? -54.276 21.172  35.976  1.00 25.35 ? 81   PRO   B CD  1 
ATOM   4819 N  N   . ASP   B 1 59  ? -54.517 19.944  39.574  1.00 23.52 ? 82   ASP   B N   1 
ATOM   4820 C  CA  . ASP   B 1 59  ? -54.929 19.674  40.944  1.00 26.20 ? 82   ASP   B CA  1 
ATOM   4821 C  C   . ASP   B 1 59  ? -55.372 18.229  41.135  1.00 25.69 ? 82   ASP   B C   1 
ATOM   4822 O  O   . ASP   B 1 59  ? -56.275 17.772  40.443  1.00 28.06 ? 82   ASP   B O   1 
ATOM   4823 C  CB  . ASP   B 1 59  ? -56.073 20.593  41.337  1.00 30.35 ? 82   ASP   B CB  1 
ATOM   4824 C  CG  . ASP   B 1 59  ? -55.716 22.069  41.239  1.00 32.07 ? 82   ASP   B CG  1 
ATOM   4825 O  OD1 . ASP   B 1 59  ? -54.856 22.474  42.050  1.00 34.98 ? 82   ASP   B OD1 1 
ATOM   4826 O  OD2 . ASP   B 1 59  ? -56.235 22.762  40.311  1.00 29.42 ? 82   ASP   B OD2 1 
ATOM   4827 N  N   . TRP   B 1 60  ? -54.827 17.580  42.164  1.00 22.28 ? 83   TRP   B N   1 
ATOM   4828 C  CA  . TRP   B 1 60  ? -55.300 16.282  42.591  1.00 25.35 ? 83   TRP   B CA  1 
ATOM   4829 C  C   . TRP   B 1 60  ? -54.701 15.903  43.948  1.00 24.92 ? 83   TRP   B C   1 
ATOM   4830 O  O   . TRP   B 1 60  ? -53.806 16.567  44.454  1.00 27.69 ? 83   TRP   B O   1 
ATOM   4831 C  CB  . TRP   B 1 60  ? -54.923 15.288  41.485  1.00 25.61 ? 83   TRP   B CB  1 
ATOM   4832 C  CG  . TRP   B 1 60  ? -53.464 14.942  41.424  1.00 24.64 ? 83   TRP   B CG  1 
ATOM   4833 C  CD1 . TRP   B 1 60  ? -52.425 15.726  41.015  1.00 25.68 ? 83   TRP   B CD1 1 
ATOM   4834 C  CD2 . TRP   B 1 60  ? -52.907 13.648  41.724  1.00 23.99 ? 83   TRP   B CD2 1 
ATOM   4835 N  NE1 . TRP   B 1 60  ? -51.259 15.017  41.092  1.00 26.32 ? 83   TRP   B NE1 1 
ATOM   4836 C  CE2 . TRP   B 1 60  ? -51.519 13.741  41.517  1.00 23.56 ? 83   TRP   B CE2 1 
ATOM   4837 C  CE3 . TRP   B 1 60  ? -53.443 12.437  42.161  1.00 22.97 ? 83   TRP   B CE3 1 
ATOM   4838 C  CZ2 . TRP   B 1 60  ? -50.673 12.657  41.717  1.00 21.66 ? 83   TRP   B CZ2 1 
ATOM   4839 C  CZ3 . TRP   B 1 60  ? -52.605 11.364  42.354  1.00 22.41 ? 83   TRP   B CZ3 1 
ATOM   4840 C  CH2 . TRP   B 1 60  ? -51.244 11.466  42.092  1.00 22.72 ? 83   TRP   B CH2 1 
ATOM   4841 N  N   . ALA   B 1 61  ? -55.154 14.804  44.545  1.00 24.90 ? 84   ALA   B N   1 
ATOM   4842 C  CA  . ALA   B 1 61  ? -54.498 14.241  45.715  1.00 26.18 ? 84   ALA   B CA  1 
ATOM   4843 C  C   . ALA   B 1 61  ? -54.608 12.730  45.691  1.00 27.13 ? 84   ALA   B C   1 
ATOM   4844 O  O   . ALA   B 1 61  ? -55.662 12.212  45.343  1.00 30.52 ? 84   ALA   B O   1 
ATOM   4845 C  CB  . ALA   B 1 61  ? -55.126 14.756  46.996  1.00 26.71 ? 84   ALA   B CB  1 
ATOM   4846 N  N   . ASN   B 1 62  ? -53.563 12.066  46.195  1.00 25.84 ? 85   ASN   B N   1 
ATOM   4847 C  CA  . ASN   B 1 62  ? -53.406 10.628  46.133  1.00 29.40 ? 85   ASN   B CA  1 
ATOM   4848 C  C   . ASN   B 1 62  ? -53.783 10.061  47.492  1.00 29.83 ? 85   ASN   B C   1 
ATOM   4849 O  O   . ASN   B 1 62  ? -53.168 10.436  48.483  1.00 31.22 ? 85   ASN   B O   1 
ATOM   4850 C  CB  . ASN   B 1 62  ? -51.951 10.277  45.825  1.00 27.70 ? 85   ASN   B CB  1 
ATOM   4851 C  CG  . ASN   B 1 62  ? -51.734 8.848   45.399  1.00 30.21 ? 85   ASN   B CG  1 
ATOM   4852 O  OD1 . ASN   B 1 62  ? -52.164 7.904   46.076  1.00 27.03 ? 85   ASN   B OD1 1 
ATOM   4853 N  ND2 . ASN   B 1 62  ? -51.009 8.673   44.293  1.00 30.49 ? 85   ASN   B ND2 1 
ATOM   4854 N  N   . LEU   B 1 63  ? -54.741 9.126   47.537  1.00 26.58 ? 86   LEU   B N   1 
ATOM   4855 C  CA  . LEU   B 1 63  ? -55.188 8.551   48.794  1.00 22.65 ? 86   LEU   B CA  1 
ATOM   4856 C  C   . LEU   B 1 63  ? -54.554 7.207   49.058  1.00 23.18 ? 86   LEU   B C   1 
ATOM   4857 O  O   . LEU   B 1 63  ? -54.957 6.514   49.992  1.00 23.02 ? 86   LEU   B O   1 
ATOM   4858 C  CB  . LEU   B 1 63  ? -56.701 8.418   48.756  1.00 25.39 ? 86   LEU   B CB  1 
ATOM   4859 C  CG  . LEU   B 1 63  ? -57.450 9.738   48.684  1.00 27.40 ? 86   LEU   B CG  1 
ATOM   4860 C  CD1 . LEU   B 1 63  ? -58.922 9.448   48.636  1.00 27.99 ? 86   LEU   B CD1 1 
ATOM   4861 C  CD2 . LEU   B 1 63  ? -57.078 10.604  49.898  1.00 28.65 ? 86   LEU   B CD2 1 
ATOM   4862 N  N   . ASN   B 1 64  ? -53.559 6.828   48.245  1.00 22.75 ? 87   ASN   B N   1 
ATOM   4863 C  CA  . ASN   B 1 64  ? -52.823 5.614   48.532  1.00 23.86 ? 87   ASN   B CA  1 
ATOM   4864 C  C   . ASN   B 1 64  ? -52.182 5.732   49.914  1.00 25.17 ? 87   ASN   B C   1 
ATOM   4865 O  O   . ASN   B 1 64  ? -51.943 6.829   50.394  1.00 28.18 ? 87   ASN   B O   1 
ATOM   4866 C  CB  . ASN   B 1 64  ? -51.764 5.314   47.471  1.00 25.20 ? 87   ASN   B CB  1 
ATOM   4867 C  CG  . ASN   B 1 64  ? -52.348 4.956   46.117  1.00 26.94 ? 87   ASN   B CG  1 
ATOM   4868 O  OD1 . ASN   B 1 64  ? -53.565 4.774   45.988  1.00 21.25 ? 87   ASN   B OD1 1 
ATOM   4869 N  ND2 . ASN   B 1 64  ? -51.491 4.852   45.101  1.00 21.99 ? 87   ASN   B ND2 1 
ATOM   4870 N  N   . GLY   B 1 65  ? -51.951 4.588   50.554  1.00 28.27 ? 88   GLY   B N   1 
ATOM   4871 C  CA  . GLY   B 1 65  ? -51.185 4.532   51.785  1.00 31.25 ? 88   GLY   B CA  1 
ATOM   4872 C  C   . GLY   B 1 65  ? -51.775 3.515   52.756  1.00 31.57 ? 88   GLY   B C   1 
ATOM   4873 O  O   . GLY   B 1 65  ? -52.265 2.462   52.346  1.00 24.80 ? 88   GLY   B O   1 
ATOM   4874 N  N   . ILE   B 1 66  ? -51.689 3.811   54.056  1.00 28.63 ? 89   ILE   B N   1 
ATOM   4875 C  CA  . ILE   B 1 66  ? -52.143 2.840   55.032  1.00 29.16 ? 89   ILE   B CA  1 
ATOM   4876 C  C   . ILE   B 1 66  ? -53.586 3.180   55.389  1.00 31.91 ? 89   ILE   B C   1 
ATOM   4877 O  O   . ILE   B 1 66  ? -53.889 4.332   55.690  1.00 31.08 ? 89   ILE   B O   1 
ATOM   4878 C  CB  . ILE   B 1 66  ? -51.177 2.766   56.226  1.00 30.88 ? 89   ILE   B CB  1 
ATOM   4879 C  CG1 . ILE   B 1 66  ? -49.752 2.467   55.736  1.00 30.63 ? 89   ILE   B CG1 1 
ATOM   4880 C  CG2 . ILE   B 1 66  ? -51.642 1.742   57.260  1.00 30.10 ? 89   ILE   B CG2 1 
ATOM   4881 C  CD1 . ILE   B 1 66  ? -49.569 1.105   55.090  1.00 31.83 ? 89   ILE   B CD1 1 
ATOM   4882 N  N   . TRP   B 1 67  ? -54.479 2.182   55.224  1.00 31.74 ? 90   TRP   B N   1 
ATOM   4883 C  CA  . TRP   B 1 67  ? -55.881 2.290   55.604  1.00 27.63 ? 90   TRP   B CA  1 
ATOM   4884 C  C   . TRP   B 1 67  ? -56.155 1.264   56.693  1.00 24.45 ? 90   TRP   B C   1 
ATOM   4885 O  O   . TRP   B 1 67  ? -55.502 0.210   56.756  1.00 30.75 ? 90   TRP   B O   1 
ATOM   4886 C  CB  . TRP   B 1 67  ? -56.849 2.017   54.436  1.00 27.57 ? 90   TRP   B CB  1 
ATOM   4887 C  CG  . TRP   B 1 67  ? -56.747 2.928   53.241  1.00 26.95 ? 90   TRP   B CG  1 
ATOM   4888 C  CD1 . TRP   B 1 67  ? -55.610 3.397   52.638  1.00 28.65 ? 90   TRP   B CD1 1 
ATOM   4889 C  CD2 . TRP   B 1 67  ? -57.851 3.422   52.456  1.00 28.88 ? 90   TRP   B CD2 1 
ATOM   4890 N  NE1 . TRP   B 1 67  ? -55.928 4.181   51.564  1.00 26.14 ? 90   TRP   B NE1 1 
ATOM   4891 C  CE2 . TRP   B 1 67  ? -57.295 4.213   51.420  1.00 31.15 ? 90   TRP   B CE2 1 
ATOM   4892 C  CE3 . TRP   B 1 67  ? -59.244 3.298   52.530  1.00 28.35 ? 90   TRP   B CE3 1 
ATOM   4893 C  CZ2 . TRP   B 1 67  ? -58.088 4.853   50.470  1.00 30.90 ? 90   TRP   B CZ2 1 
ATOM   4894 C  CZ3 . TRP   B 1 67  ? -60.023 3.933   51.586  1.00 31.37 ? 90   TRP   B CZ3 1 
ATOM   4895 C  CH2 . TRP   B 1 67  ? -59.455 4.684   50.559  1.00 32.06 ? 90   TRP   B CH2 1 
ATOM   4896 N  N   . ASP   B 1 68  ? -57.159 1.565   57.520  1.00 29.43 ? 91   ASP   B N   1 
ATOM   4897 C  CA  . ASP   B 1 68  ? -57.726 0.563   58.416  1.00 30.56 ? 91   ASP   B CA  1 
ATOM   4898 C  C   . ASP   B 1 68  ? -58.422 -0.498  57.574  1.00 30.89 ? 91   ASP   B C   1 
ATOM   4899 O  O   . ASP   B 1 68  ? -58.914 -0.186  56.497  1.00 27.99 ? 91   ASP   B O   1 
ATOM   4900 C  CB  . ASP   B 1 68  ? -58.722 1.197   59.370  1.00 33.26 ? 91   ASP   B CB  1 
ATOM   4901 C  CG  . ASP   B 1 68  ? -58.092 2.293   60.219  1.00 34.46 ? 91   ASP   B CG  1 
ATOM   4902 O  OD1 . ASP   B 1 68  ? -56.939 2.069   60.642  1.00 30.58 ? 91   ASP   B OD1 1 
ATOM   4903 O  OD2 . ASP   B 1 68  ? -58.733 3.358   60.382  1.00 37.43 ? 91   ASP   B OD2 1 
ATOM   4904 N  N   . PHE   B 1 69  ? -58.468 -1.728  58.090  1.00 28.19 ? 92   PHE   B N   1 
ATOM   4905 C  CA  . PHE   B 1 69  ? -58.949 -2.855  57.318  1.00 28.71 ? 92   PHE   B CA  1 
ATOM   4906 C  C   . PHE   B 1 69  ? -59.620 -3.911  58.190  1.00 31.38 ? 92   PHE   B C   1 
ATOM   4907 O  O   . PHE   B 1 69  ? -59.151 -4.227  59.291  1.00 28.97 ? 92   PHE   B O   1 
ATOM   4908 C  CB  . PHE   B 1 69  ? -57.732 -3.497  56.662  1.00 27.99 ? 92   PHE   B CB  1 
ATOM   4909 C  CG  . PHE   B 1 69  ? -58.050 -4.609  55.680  1.00 23.36 ? 92   PHE   B CG  1 
ATOM   4910 C  CD1 . PHE   B 1 69  ? -58.662 -4.316  54.473  1.00 26.34 ? 92   PHE   B CD1 1 
ATOM   4911 C  CD2 . PHE   B 1 69  ? -57.696 -5.916  55.949  1.00 26.13 ? 92   PHE   B CD2 1 
ATOM   4912 C  CE1 . PHE   B 1 69  ? -58.929 -5.318  53.571  1.00 24.56 ? 92   PHE   B CE1 1 
ATOM   4913 C  CE2 . PHE   B 1 69  ? -57.941 -6.918  55.031  1.00 27.47 ? 92   PHE   B CE2 1 
ATOM   4914 C  CZ  . PHE   B 1 69  ? -58.568 -6.611  53.850  1.00 26.23 ? 92   PHE   B CZ  1 
ATOM   4915 N  N   . ALA   B 1 70  ? -60.681 -4.509  57.627  1.00 28.65 ? 93   ALA   B N   1 
ATOM   4916 C  CA  . ALA   B 1 70  ? -61.345 -5.651  58.231  1.00 30.48 ? 93   ALA   B CA  1 
ATOM   4917 C  C   . ALA   B 1 70  ? -61.845 -6.592  57.136  1.00 30.40 ? 93   ALA   B C   1 
ATOM   4918 O  O   . ALA   B 1 70  ? -62.232 -6.120  56.069  1.00 29.06 ? 93   ALA   B O   1 
ATOM   4919 C  CB  . ALA   B 1 70  ? -62.499 -5.190  59.083  1.00 31.73 ? 93   ALA   B CB  1 
ATOM   4920 N  N   . VAL   B 1 71  ? -61.807 -7.900  57.433  1.00 27.96 ? 94   VAL   B N   1 
ATOM   4921 C  CA  . VAL   B 1 71  ? -62.444 -8.931  56.624  1.00 30.04 ? 94   VAL   B CA  1 
ATOM   4922 C  C   . VAL   B 1 71  ? -63.662 -9.467  57.384  1.00 31.06 ? 94   VAL   B C   1 
ATOM   4923 O  O   . VAL   B 1 71  ? -63.507 -10.094 58.436  1.00 28.58 ? 94   VAL   B O   1 
ATOM   4924 C  CB  . VAL   B 1 71  ? -61.494 -10.107 56.312  1.00 33.57 ? 94   VAL   B CB  1 
ATOM   4925 C  CG1 . VAL   B 1 71  ? -62.182 -11.172 55.467  1.00 35.09 ? 94   VAL   B CG1 1 
ATOM   4926 C  CG2 . VAL   B 1 71  ? -60.188 -9.678  55.651  1.00 33.79 ? 94   VAL   B CG2 1 
ATOM   4927 N  N   . THR   B 1 72  ? -64.863 -9.287  56.819  1.00 27.49 ? 95   THR   B N   1 
ATOM   4928 C  CA  . THR   B 1 72  ? -66.066 -9.886  57.387  1.00 27.59 ? 95   THR   B CA  1 
ATOM   4929 C  C   . THR   B 1 72  ? -66.600 -11.007 56.490  1.00 29.49 ? 95   THR   B C   1 
ATOM   4930 O  O   . THR   B 1 72  ? -66.054 -11.296 55.413  1.00 26.49 ? 95   THR   B O   1 
ATOM   4931 C  CB  . THR   B 1 72  ? -67.146 -8.820  57.530  1.00 26.32 ? 95   THR   B CB  1 
ATOM   4932 O  OG1 . THR   B 1 72  ? -67.576 -8.609  56.197  1.00 25.50 ? 95   THR   B OG1 1 
ATOM   4933 C  CG2 . THR   B 1 72  ? -66.680 -7.521  58.156  1.00 28.27 ? 95   THR   B CG2 1 
ATOM   4934 N  N   . SER   B 1 73  ? -67.720 -11.603 56.939  1.00 27.01 ? 96   SER   B N   1 
ATOM   4935 C  CA  . SER   B 1 73  ? -68.622 -12.353 56.073  1.00 26.20 ? 96   SER   B CA  1 
ATOM   4936 C  C   . SER   B 1 73  ? -69.054 -11.490 54.885  1.00 25.71 ? 96   SER   B C   1 
ATOM   4937 O  O   . SER   B 1 73  ? -69.102 -10.264 54.966  1.00 24.18 ? 96   SER   B O   1 
ATOM   4938 C  CB  . SER   B 1 73  ? -69.849 -12.843 56.844  1.00 27.43 ? 96   SER   B CB  1 
ATOM   4939 O  OG  . SER   B 1 73  ? -70.776 -11.776 57.006  1.00 28.41 ? 96   SER   B OG  1 
ATOM   4940 N  N   . ALA   B 1 74  ? -69.419 -12.163 53.787  1.00 28.17 ? 97   ALA   B N   1 
ATOM   4941 C  CA  . ALA   B 1 74  ? -69.782 -11.505 52.541  1.00 28.44 ? 97   ALA   B CA  1 
ATOM   4942 C  C   . ALA   B 1 74  ? -70.979 -10.561 52.681  1.00 28.07 ? 97   ALA   B C   1 
ATOM   4943 O  O   . ALA   B 1 74  ? -70.993 -9.494  52.064  1.00 23.32 ? 97   ALA   B O   1 
ATOM   4944 C  CB  . ALA   B 1 74  ? -70.045 -12.565 51.494  1.00 31.57 ? 97   ALA   B CB  1 
ATOM   4945 N  N   . ASN   B 1 75  ? -72.008 -10.966 53.451  1.00 30.00 ? 98   ASN   B N   1 
ATOM   4946 C  CA  . ASN   B 1 75  ? -73.234 -10.186 53.569  1.00 32.62 ? 98   ASN   B CA  1 
ATOM   4947 C  C   . ASN   B 1 75  ? -73.245 -9.280  54.797  1.00 32.38 ? 98   ASN   B C   1 
ATOM   4948 O  O   . ASN   B 1 75  ? -74.222 -8.575  54.984  1.00 32.95 ? 98   ASN   B O   1 
ATOM   4949 C  CB  . ASN   B 1 75  ? -74.477 -11.067 53.680  1.00 35.92 ? 98   ASN   B CB  1 
ATOM   4950 C  CG  . ASN   B 1 75  ? -74.653 -11.895 52.435  1.00 39.17 ? 98   ASN   B CG  1 
ATOM   4951 O  OD1 . ASN   B 1 75  ? -74.878 -11.334 51.363  1.00 42.64 ? 98   ASN   B OD1 1 
ATOM   4952 N  ND2 . ASN   B 1 75  ? -74.516 -13.206 52.546  1.00 46.68 ? 98   ASN   B ND2 1 
ATOM   4953 N  N   . ALA   B 1 76  ? -72.180 -9.299  55.609  1.00 30.56 ? 99   ALA   B N   1 
ATOM   4954 C  CA  . ALA   B 1 76  ? -72.115 -8.474  56.809  1.00 31.49 ? 99   ALA   B CA  1 
ATOM   4955 C  C   . ALA   B 1 76  ? -72.155 -6.992  56.443  1.00 30.09 ? 99   ALA   B C   1 
ATOM   4956 O  O   . ALA   B 1 76  ? -71.777 -6.586  55.344  1.00 31.85 ? 99   ALA   B O   1 
ATOM   4957 C  CB  . ALA   B 1 76  ? -70.868 -8.798  57.607  1.00 30.93 ? 99   ALA   B CB  1 
ATOM   4958 N  N   . GLY   B 1 77  ? -72.615 -6.176  57.391  1.00 28.82 ? 100  GLY   B N   1 
ATOM   4959 C  CA  . GLY   B 1 77  ? -72.537 -4.735  57.255  1.00 27.36 ? 100  GLY   B CA  1 
ATOM   4960 C  C   . GLY   B 1 77  ? -71.180 -4.251  57.760  1.00 25.77 ? 100  GLY   B C   1 
ATOM   4961 O  O   . GLY   B 1 77  ? -70.329 -5.044  58.188  1.00 29.15 ? 100  GLY   B O   1 
ATOM   4962 N  N   . GLN   B 1 78  ? -70.988 -2.939  57.720  1.00 24.82 ? 101  GLN   B N   1 
ATOM   4963 C  CA  . GLN   B 1 78  ? -69.753 -2.334  58.199  1.00 29.30 ? 101  GLN   B CA  1 
ATOM   4964 C  C   . GLN   B 1 78  ? -69.451 -2.740  59.641  1.00 34.40 ? 101  GLN   B C   1 
ATOM   4965 O  O   . GLN   B 1 78  ? -70.238 -2.456  60.538  1.00 36.89 ? 101  GLN   B O   1 
ATOM   4966 C  CB  . GLN   B 1 78  ? -69.902 -0.818  58.112  1.00 28.17 ? 101  GLN   B CB  1 
ATOM   4967 C  CG  . GLN   B 1 78  ? -68.608 -0.073  58.397  1.00 29.68 ? 101  GLN   B CG  1 
ATOM   4968 C  CD  . GLN   B 1 78  ? -68.780 1.420   58.276  1.00 28.27 ? 101  GLN   B CD  1 
ATOM   4969 O  OE1 . GLN   B 1 78  ? -69.310 1.955   57.298  1.00 30.58 ? 101  GLN   B OE1 1 
ATOM   4970 N  NE2 . GLN   B 1 78  ? -68.353 2.120   59.308  1.00 35.72 ? 101  GLN   B NE2 1 
ATOM   4971 N  N   . PRO   B 1 79  ? -68.289 -3.372  59.931  1.00 38.87 ? 102  PRO   B N   1 
ATOM   4972 C  CA  . PRO   B 1 79  ? -67.921 -3.690  61.312  1.00 39.62 ? 102  PRO   B CA  1 
ATOM   4973 C  C   . PRO   B 1 79  ? -67.690 -2.433  62.152  1.00 44.69 ? 102  PRO   B C   1 
ATOM   4974 O  O   . PRO   B 1 79  ? -67.413 -1.363  61.607  1.00 46.24 ? 102  PRO   B O   1 
ATOM   4975 C  CB  . PRO   B 1 79  ? -66.676 -4.575  61.201  1.00 37.92 ? 102  PRO   B CB  1 
ATOM   4976 C  CG  . PRO   B 1 79  ? -66.125 -4.297  59.825  1.00 41.18 ? 102  PRO   B CG  1 
ATOM   4977 C  CD  . PRO   B 1 79  ? -67.282 -3.819  58.957  1.00 39.55 ? 102  PRO   B CD  1 
ATOM   4978 N  N   . ALA   B 1 80  ? -67.859 -2.574  63.479  1.00 43.72 ? 103  ALA   B N   1 
ATOM   4979 C  CA  . ALA   B 1 80  ? -67.720 -1.454  64.402  1.00 45.20 ? 103  ALA   B CA  1 
ATOM   4980 C  C   . ALA   B 1 80  ? -66.252 -1.046  64.516  1.00 44.10 ? 103  ALA   B C   1 
ATOM   4981 O  O   . ALA   B 1 80  ? -65.936 0.139   64.464  1.00 49.23 ? 103  ALA   B O   1 
ATOM   4982 C  CB  . ALA   B 1 80  ? -68.297 -1.814  65.757  1.00 45.17 ? 103  ALA   B CB  1 
ATOM   4983 N  N   . THR   B 1 81  ? -65.367 -2.043  64.651  1.00 42.64 ? 104  THR   B N   1 
ATOM   4984 C  CA  . THR   B 1 81  ? -63.934 -1.806  64.744  1.00 44.45 ? 104  THR   B CA  1 
ATOM   4985 C  C   . THR   B 1 81  ? -63.190 -2.547  63.625  1.00 42.39 ? 104  THR   B C   1 
ATOM   4986 O  O   . THR   B 1 81  ? -63.525 -3.674  63.255  1.00 40.22 ? 104  THR   B O   1 
ATOM   4987 C  CB  . THR   B 1 81  ? -63.420 -2.211  66.129  1.00 48.78 ? 104  THR   B CB  1 
ATOM   4988 O  OG1 . THR   B 1 81  ? -63.341 -3.635  66.184  1.00 45.94 ? 104  THR   B OG1 1 
ATOM   4989 C  CG2 . THR   B 1 81  ? -64.288 -1.671  67.255  1.00 52.12 ? 104  THR   B CG2 1 
ATOM   4990 N  N   . PHE   B 1 82  ? -62.145 -1.897  63.109  1.00 36.49 ? 105  PHE   B N   1 
ATOM   4991 C  CA  . PHE   B 1 82  ? -61.276 -2.475  62.101  1.00 35.78 ? 105  PHE   B CA  1 
ATOM   4992 C  C   . PHE   B 1 82  ? -60.063 -3.076  62.799  1.00 32.21 ? 105  PHE   B C   1 
ATOM   4993 O  O   . PHE   B 1 82  ? -59.200 -2.353  63.255  1.00 32.10 ? 105  PHE   B O   1 
ATOM   4994 C  CB  . PHE   B 1 82  ? -60.984 -1.316  61.140  1.00 39.24 ? 105  PHE   B CB  1 
ATOM   4995 C  CG  . PHE   B 1 82  ? -62.138 -0.966  60.209  1.00 39.02 ? 105  PHE   B CG  1 
ATOM   4996 C  CD1 . PHE   B 1 82  ? -63.325 -0.423  60.696  1.00 43.52 ? 105  PHE   B CD1 1 
ATOM   4997 C  CD2 . PHE   B 1 82  ? -62.039 -1.188  58.836  1.00 37.55 ? 105  PHE   B CD2 1 
ATOM   4998 C  CE1 . PHE   B 1 82  ? -64.382 -0.124  59.841  1.00 38.55 ? 105  PHE   B CE1 1 
ATOM   4999 C  CE2 . PHE   B 1 82  ? -63.089 -0.875  57.986  1.00 36.63 ? 105  PHE   B CE2 1 
ATOM   5000 C  CZ  . PHE   B 1 82  ? -64.258 -0.346  58.484  1.00 39.80 ? 105  PHE   B CZ  1 
ATOM   5001 N  N   . PRO   B 1 83  ? -59.949 -4.406  62.954  1.00 34.69 ? 106  PRO   B N   1 
ATOM   5002 C  CA  . PRO   B 1 83  ? -58.795 -4.974  63.656  1.00 36.09 ? 106  PRO   B CA  1 
ATOM   5003 C  C   . PRO   B 1 83  ? -57.427 -4.955  62.971  1.00 35.64 ? 106  PRO   B C   1 
ATOM   5004 O  O   . PRO   B 1 83  ? -56.463 -5.466  63.536  1.00 33.16 ? 106  PRO   B O   1 
ATOM   5005 C  CB  . PRO   B 1 83  ? -59.253 -6.428  63.916  1.00 39.66 ? 106  PRO   B CB  1 
ATOM   5006 C  CG  . PRO   B 1 83  ? -60.263 -6.734  62.815  1.00 36.13 ? 106  PRO   B CG  1 
ATOM   5007 C  CD  . PRO   B 1 83  ? -60.926 -5.412  62.503  1.00 35.71 ? 106  PRO   B CD  1 
ATOM   5008 N  N   . GLU   B 1 84  ? -57.335 -4.430  61.740  1.00 36.63 ? 107  GLU   B N   1 
ATOM   5009 C  CA  . GLU   B 1 84  ? -56.118 -4.586  60.952  1.00 34.17 ? 107  GLU   B CA  1 
ATOM   5010 C  C   . GLU   B 1 84  ? -55.843 -3.328  60.148  1.00 29.00 ? 107  GLU   B C   1 
ATOM   5011 O  O   . GLU   B 1 84  ? -56.647 -2.399  60.145  1.00 26.73 ? 107  GLU   B O   1 
ATOM   5012 C  CB  . GLU   B 1 84  ? -56.226 -5.729  59.944  1.00 38.86 ? 107  GLU   B CB  1 
ATOM   5013 C  CG  . GLU   B 1 84  ? -56.572 -7.063  60.583  1.00 39.45 ? 107  GLU   B CG  1 
ATOM   5014 C  CD  . GLU   B 1 84  ? -56.574 -8.184  59.580  1.00 41.69 ? 107  GLU   B CD  1 
ATOM   5015 O  OE1 . GLU   B 1 84  ? -57.660 -8.632  59.161  1.00 44.68 ? 107  GLU   B OE1 1 
ATOM   5016 O  OE2 . GLU   B 1 84  ? -55.466 -8.605  59.223  1.00 42.45 ? 107  GLU   B OE2 1 
ATOM   5017 N  N   . GLN   B 1 85  ? -54.692 -3.325  59.450  1.00 27.35 ? 108  GLN   B N   1 
ATOM   5018 C  CA  . GLN   B 1 85  ? -54.354 -2.222  58.560  1.00 26.12 ? 108  GLN   B CA  1 
ATOM   5019 C  C   . GLN   B 1 85  ? -53.821 -2.768  57.232  1.00 22.20 ? 108  GLN   B C   1 
ATOM   5020 O  O   . GLN   B 1 85  ? -53.168 -3.813  57.203  1.00 22.77 ? 108  GLN   B O   1 
ATOM   5021 C  CB  . GLN   B 1 85  ? -53.299 -1.312  59.192  1.00 26.42 ? 108  GLN   B CB  1 
ATOM   5022 C  CG  . GLN   B 1 85  ? -53.795 -0.480  60.371  1.00 28.55 ? 108  GLN   B CG  1 
ATOM   5023 C  CD  . GLN   B 1 85  ? -52.697 0.337   61.023  1.00 31.49 ? 108  GLN   B CD  1 
ATOM   5024 O  OE1 . GLN   B 1 85  ? -51.500 0.092   60.828  1.00 31.76 ? 108  GLN   B OE1 1 
ATOM   5025 N  NE2 . GLN   B 1 85  ? -53.100 1.299   61.839  1.00 38.32 ? 108  GLN   B NE2 1 
ATOM   5026 N  N   . ILE   B 1 86  ? -54.061 -2.028  56.144  1.00 23.86 ? 109  ILE   B N   1 
ATOM   5027 C  CA  . ILE   B 1 86  ? -53.673 -2.512  54.816  1.00 24.84 ? 109  ILE   B CA  1 
ATOM   5028 C  C   . ILE   B 1 86  ? -53.078 -1.377  53.999  1.00 22.17 ? 109  ILE   B C   1 
ATOM   5029 O  O   . ILE   B 1 86  ? -53.504 -0.238  54.125  1.00 24.97 ? 109  ILE   B O   1 
ATOM   5030 C  CB  . ILE   B 1 86  ? -54.867 -3.135  54.064  1.00 22.45 ? 109  ILE   B CB  1 
ATOM   5031 C  CG1 . ILE   B 1 86  ? -54.406 -3.853  52.790  1.00 25.52 ? 109  ILE   B CG1 1 
ATOM   5032 C  CG2 . ILE   B 1 86  ? -55.915 -2.077  53.749  1.00 21.81 ? 109  ILE   B CG2 1 
ATOM   5033 C  CD1 . ILE   B 1 86  ? -55.454 -4.773  52.187  1.00 25.73 ? 109  ILE   B CD1 1 
ATOM   5034 N  N   . ARG   B 1 87  ? -52.164 -1.731  53.079  1.00 24.62 ? 110  ARG   B N   1 
ATOM   5035 C  CA  . ARG   B 1 87  ? -51.520 -0.740  52.233  1.00 23.56 ? 110  ARG   B CA  1 
ATOM   5036 C  C   . ARG   B 1 87  ? -52.174 -0.732  50.854  1.00 24.06 ? 110  ARG   B C   1 
ATOM   5037 O  O   . ARG   B 1 87  ? -52.040 -1.670  50.083  1.00 24.60 ? 110  ARG   B O   1 
ATOM   5038 C  CB  . ARG   B 1 87  ? -50.002 -0.935  52.129  1.00 24.46 ? 110  ARG   B CB  1 
ATOM   5039 C  CG  . ARG   B 1 87  ? -49.407 0.207   51.326  1.00 26.30 ? 110  ARG   B CG  1 
ATOM   5040 C  CD  . ARG   B 1 87  ? -47.888 0.262   51.334  1.00 25.09 ? 110  ARG   B CD  1 
ATOM   5041 N  NE  . ARG   B 1 87  ? -47.238 -1.017  51.065  1.00 25.71 ? 110  ARG   B NE  1 
ATOM   5042 C  CZ  . ARG   B 1 87  ? -45.951 -1.247  51.193  1.00 24.45 ? 110  ARG   B CZ  1 
ATOM   5043 N  NH1 . ARG   B 1 87  ? -45.096 -0.238  51.322  1.00 28.47 ? 110  ARG   B NH1 1 
ATOM   5044 N  NH2 . ARG   B 1 87  ? -45.523 -2.476  51.175  1.00 25.77 ? 110  ARG   B NH2 1 
ATOM   5045 N  N   . VAL   B 1 88  ? -52.868 0.363   50.581  1.00 25.52 ? 111  VAL   B N   1 
ATOM   5046 C  CA  . VAL   B 1 88  ? -53.551 0.598   49.329  1.00 27.67 ? 111  VAL   B CA  1 
ATOM   5047 C  C   . VAL   B 1 88  ? -52.540 1.222   48.375  1.00 27.10 ? 111  VAL   B C   1 
ATOM   5048 O  O   . VAL   B 1 88  ? -51.747 2.064   48.804  1.00 24.44 ? 111  VAL   B O   1 
ATOM   5049 C  CB  . VAL   B 1 88  ? -54.732 1.531   49.645  1.00 25.92 ? 111  VAL   B CB  1 
ATOM   5050 C  CG1 . VAL   B 1 88  ? -55.345 2.176   48.412  1.00 24.37 ? 111  VAL   B CG1 1 
ATOM   5051 C  CG2 . VAL   B 1 88  ? -55.785 0.810   50.491  1.00 27.66 ? 111  VAL   B CG2 1 
ATOM   5052 N  N   . PRO   B 1 89  ? -52.498 0.847   47.072  1.00 26.11 ? 112  PRO   B N   1 
ATOM   5053 C  CA  . PRO   B 1 89  ? -53.415 -0.126  46.462  1.00 22.50 ? 112  PRO   B CA  1 
ATOM   5054 C  C   . PRO   B 1 89  ? -52.937 -1.542  46.130  1.00 22.65 ? 112  PRO   B C   1 
ATOM   5055 O  O   . PRO   B 1 89  ? -52.877 -1.936  44.960  1.00 21.20 ? 112  PRO   B O   1 
ATOM   5056 C  CB  . PRO   B 1 89  ? -53.717 0.707   45.190  1.00 21.98 ? 112  PRO   B CB  1 
ATOM   5057 C  CG  . PRO   B 1 89  ? -52.394 1.389   44.807  1.00 24.96 ? 112  PRO   B CG  1 
ATOM   5058 C  CD  . PRO   B 1 89  ? -51.579 1.453   46.093  1.00 24.19 ? 112  PRO   B CD  1 
ATOM   5059 N  N   . PHE   B 1 90  ? -52.629 -2.327  47.174  1.00 21.31 ? 113  PHE   B N   1 
ATOM   5060 C  CA  . PHE   B 1 90  ? -52.193 -3.700  47.036  1.00 22.04 ? 113  PHE   B CA  1 
ATOM   5061 C  C   . PHE   B 1 90  ? -53.275 -4.636  47.564  1.00 25.34 ? 113  PHE   B C   1 
ATOM   5062 O  O   . PHE   B 1 90  ? -53.833 -4.417  48.643  1.00 24.30 ? 113  PHE   B O   1 
ATOM   5063 C  CB  . PHE   B 1 90  ? -50.883 -3.913  47.791  1.00 23.82 ? 113  PHE   B CB  1 
ATOM   5064 C  CG  . PHE   B 1 90  ? -49.755 -3.104  47.173  1.00 22.67 ? 113  PHE   B CG  1 
ATOM   5065 C  CD1 . PHE   B 1 90  ? -49.153 -3.529  45.995  1.00 23.60 ? 113  PHE   B CD1 1 
ATOM   5066 C  CD2 . PHE   B 1 90  ? -49.358 -1.890  47.722  1.00 24.69 ? 113  PHE   B CD2 1 
ATOM   5067 C  CE1 . PHE   B 1 90  ? -48.166 -2.764  45.392  1.00 22.68 ? 113  PHE   B CE1 1 
ATOM   5068 C  CE2 . PHE   B 1 90  ? -48.366 -1.129  47.114  1.00 23.51 ? 113  PHE   B CE2 1 
ATOM   5069 C  CZ  . PHE   B 1 90  ? -47.768 -1.578  45.949  1.00 24.02 ? 113  PHE   B CZ  1 
ATOM   5070 N  N   . VAL   B 1 91  ? -53.545 -5.712  46.817  1.00 23.11 ? 114  VAL   B N   1 
ATOM   5071 C  CA  . VAL   B 1 91  ? -54.670 -6.570  47.155  1.00 22.13 ? 114  VAL   B CA  1 
ATOM   5072 C  C   . VAL   B 1 91  ? -54.345 -7.389  48.405  1.00 22.67 ? 114  VAL   B C   1 
ATOM   5073 O  O   . VAL   B 1 91  ? -53.198 -7.694  48.705  1.00 21.53 ? 114  VAL   B O   1 
ATOM   5074 C  CB  . VAL   B 1 91  ? -55.103 -7.497  46.001  1.00 20.27 ? 114  VAL   B CB  1 
ATOM   5075 C  CG1 . VAL   B 1 91  ? -55.667 -6.701  44.833  1.00 20.73 ? 114  VAL   B CG1 1 
ATOM   5076 C  CG2 . VAL   B 1 91  ? -54.005 -8.451  45.552  1.00 21.63 ? 114  VAL   B CG2 1 
ATOM   5077 N  N   . ALA   B 1 92  ? -55.399 -7.866  49.077  1.00 24.12 ? 115  ALA   B N   1 
ATOM   5078 C  CA  . ALA   B 1 92  ? -55.245 -8.572  50.347  1.00 22.64 ? 115  ALA   B CA  1 
ATOM   5079 C  C   . ALA   B 1 92  ? -54.424 -9.847  50.228  1.00 24.05 ? 115  ALA   B C   1 
ATOM   5080 O  O   . ALA   B 1 92  ? -53.835 -10.293 51.224  1.00 24.46 ? 115  ALA   B O   1 
ATOM   5081 C  CB  . ALA   B 1 92  ? -56.604 -8.913  50.932  1.00 24.05 ? 115  ALA   B CB  1 
ATOM   5082 N  N   . GLU   B 1 93  ? -54.398 -10.463 49.039  1.00 18.78 ? 116  GLU   B N   1 
ATOM   5083 C  CA  . GLU   B 1 93  ? -53.618 -11.667 48.833  1.00 19.92 ? 116  GLU   B CA  1 
ATOM   5084 C  C   . GLU   B 1 93  ? -52.113 -11.352 48.782  1.00 15.81 ? 116  GLU   B C   1 
ATOM   5085 O  O   . GLU   B 1 93  ? -51.308 -12.267 48.855  1.00 19.01 ? 116  GLU   B O   1 
ATOM   5086 C  CB  . GLU   B 1 93  ? -54.023 -12.381 47.532  1.00 19.92 ? 116  GLU   B CB  1 
ATOM   5087 C  CG  . GLU   B 1 93  ? -55.456 -12.906 47.505  1.00 20.89 ? 116  GLU   B CG  1 
ATOM   5088 C  CD  . GLU   B 1 93  ? -56.525 -11.925 47.108  1.00 19.94 ? 116  GLU   B CD  1 
ATOM   5089 O  OE1 . GLU   B 1 93  ? -56.397 -10.676 46.991  1.00 20.19 ? 116  GLU   B OE1 1 
ATOM   5090 O  OE2 . GLU   B 1 93  ? -57.608 -12.514 46.903  1.00 23.53 ? 116  GLU   B OE2 1 
ATOM   5091 N  N   . SER   B 1 94  ? -51.760 -10.088 48.564  1.00 19.47 ? 117  SER   B N   1 
ATOM   5092 C  CA  . SER   B 1 94  ? -50.366 -9.727  48.320  1.00 21.46 ? 117  SER   B CA  1 
ATOM   5093 C  C   . SER   B 1 94  ? -49.598 -9.506  49.622  1.00 23.57 ? 117  SER   B C   1 
ATOM   5094 O  O   . SER   B 1 94  ? -50.160 -9.000  50.589  1.00 26.10 ? 117  SER   B O   1 
ATOM   5095 C  CB  . SER   B 1 94  ? -50.224 -8.505  47.461  1.00 19.75 ? 117  SER   B CB  1 
ATOM   5096 O  OG  . SER   B 1 94  ? -50.619 -7.303  48.097  1.00 21.95 ? 117  SER   B OG  1 
ATOM   5097 N  N   . ALA   B 1 95  ? -48.292 -9.795  49.557  1.00 25.60 ? 118  ALA   B N   1 
ATOM   5098 C  CA  . ALA   B 1 95  ? -47.350 -9.495  50.630  1.00 25.09 ? 118  ALA   B CA  1 
ATOM   5099 C  C   . ALA   B 1 95  ? -47.222 -7.983  50.769  1.00 22.47 ? 118  ALA   B C   1 
ATOM   5100 O  O   . ALA   B 1 95  ? -47.211 -7.448  51.875  1.00 23.02 ? 118  ALA   B O   1 
ATOM   5101 C  CB  . ALA   B 1 95  ? -46.022 -10.171 50.347  1.00 27.18 ? 118  ALA   B CB  1 
ATOM   5102 N  N   . LEU   B 1 96  ? -47.291 -7.256  49.651  1.00 21.80 ? 119  LEU   B N   1 
ATOM   5103 C  CA  . LEU   B 1 96  ? -47.121 -5.814  49.702  1.00 20.55 ? 119  LEU   B CA  1 
ATOM   5104 C  C   . LEU   B 1 96  ? -48.272 -5.128  50.439  1.00 20.37 ? 119  LEU   B C   1 
ATOM   5105 O  O   . LEU   B 1 96  ? -48.098 -4.005  50.920  1.00 20.61 ? 119  LEU   B O   1 
ATOM   5106 C  CB  . LEU   B 1 96  ? -46.876 -5.201  48.322  1.00 21.93 ? 119  LEU   B CB  1 
ATOM   5107 C  CG  . LEU   B 1 96  ? -45.471 -5.379  47.730  1.00 23.89 ? 119  LEU   B CG  1 
ATOM   5108 C  CD1 . LEU   B 1 96  ? -45.441 -4.994  46.266  1.00 23.87 ? 119  LEU   B CD1 1 
ATOM   5109 C  CD2 . LEU   B 1 96  ? -44.442 -4.564  48.509  1.00 23.23 ? 119  LEU   B CD2 1 
ATOM   5110 N  N   . SER   B 1 97  ? -49.464 -5.758  50.506  1.00 20.00 ? 120  SER   B N   1 
ATOM   5111 C  CA  . SER   B 1 97  ? -50.582 -5.198  51.253  1.00 20.44 ? 120  SER   B CA  1 
ATOM   5112 C  C   . SER   B 1 97  ? -50.238 -5.077  52.741  1.00 20.92 ? 120  SER   B C   1 
ATOM   5113 O  O   . SER   B 1 97  ? -50.753 -4.178  53.386  1.00 25.57 ? 120  SER   B O   1 
ATOM   5114 C  CB  . SER   B 1 97  ? -51.839 -6.056  51.161  1.00 18.64 ? 120  SER   B CB  1 
ATOM   5115 O  OG  . SER   B 1 97  ? -51.542 -7.402  51.520  1.00 20.20 ? 120  SER   B OG  1 
ATOM   5116 N  N   . GLY   B 1 98  ? -49.533 -6.081  53.254  1.00 25.11 ? 121  GLY   B N   1 
ATOM   5117 C  CA  . GLY   B 1 98  ? -49.344 -6.264  54.688  1.00 29.55 ? 121  GLY   B CA  1 
ATOM   5118 C  C   . GLY   B 1 98  ? -50.312 -7.287  55.286  1.00 33.78 ? 121  GLY   B C   1 
ATOM   5119 O  O   . GLY   B 1 98  ? -50.260 -7.546  56.492  1.00 29.12 ? 121  GLY   B O   1 
ATOM   5120 N  N   . ILE   B 1 99  ? -51.183 -7.884  54.446  1.00 31.62 ? 122  ILE   B N   1 
ATOM   5121 C  CA  . ILE   B 1 99  ? -52.193 -8.817  54.920  1.00 27.21 ? 122  ILE   B CA  1 
ATOM   5122 C  C   . ILE   B 1 99  ? -51.819 -10.202 54.434  1.00 28.80 ? 122  ILE   B C   1 
ATOM   5123 O  O   . ILE   B 1 99  ? -51.591 -11.105 55.232  1.00 26.10 ? 122  ILE   B O   1 
ATOM   5124 C  CB  . ILE   B 1 99  ? -53.597 -8.373  54.462  1.00 32.32 ? 122  ILE   B CB  1 
ATOM   5125 C  CG1 . ILE   B 1 99  ? -53.943 -6.961  54.942  1.00 33.08 ? 122  ILE   B CG1 1 
ATOM   5126 C  CG2 . ILE   B 1 99  ? -54.664 -9.384  54.871  1.00 32.51 ? 122  ILE   B CG2 1 
ATOM   5127 C  CD1 . ILE   B 1 99  ? -53.982 -6.814  56.459  1.00 36.37 ? 122  ILE   B CD1 1 
ATOM   5128 N  N   . GLN   B 1 100 ? -51.746 -10.365 53.105  1.00 27.00 ? 123  GLN   B N   1 
ATOM   5129 C  CA  . GLN   B 1 100 ? -51.347 -11.623 52.521  1.00 29.49 ? 123  GLN   B CA  1 
ATOM   5130 C  C   . GLN   B 1 100 ? -52.202 -12.766 53.073  1.00 30.91 ? 123  GLN   B C   1 
ATOM   5131 O  O   . GLN   B 1 100 ? -51.717 -13.677 53.761  1.00 28.64 ? 123  GLN   B O   1 
ATOM   5132 C  CB  . GLN   B 1 100 ? -49.855 -11.881 52.700  1.00 32.63 ? 123  GLN   B CB  1 
ATOM   5133 C  CG  . GLN   B 1 100 ? -49.355 -12.943 51.732  1.00 33.91 ? 123  GLN   B CG  1 
ATOM   5134 C  CD  . GLN   B 1 100 ? -47.976 -13.464 52.053  1.00 39.39 ? 123  GLN   B CD  1 
ATOM   5135 O  OE1 . GLN   B 1 100 ? -47.459 -13.317 53.171  1.00 36.92 ? 123  GLN   B OE1 1 
ATOM   5136 N  NE2 . GLN   B 1 100 ? -47.387 -14.104 51.055  1.00 40.71 ? 123  GLN   B NE2 1 
ATOM   5137 N  N   . ARG   B 1 101 ? -53.477 -12.746 52.678  1.00 27.21 ? 124  ARG   B N   1 
ATOM   5138 C  CA  . ARG   B 1 101 ? -54.434 -13.760 53.081  1.00 29.26 ? 124  ARG   B CA  1 
ATOM   5139 C  C   . ARG   B 1 101 ? -55.396 -14.087 51.937  1.00 24.18 ? 124  ARG   B C   1 
ATOM   5140 O  O   . ARG   B 1 101 ? -55.843 -13.170 51.270  1.00 23.48 ? 124  ARG   B O   1 
ATOM   5141 C  CB  . ARG   B 1 101 ? -55.219 -13.114 54.216  1.00 28.64 ? 124  ARG   B CB  1 
ATOM   5142 C  CG  . ARG   B 1 101 ? -56.154 -14.090 54.912  1.00 34.10 ? 124  ARG   B CG  1 
ATOM   5143 C  CD  . ARG   B 1 101 ? -56.956 -13.351 55.997  1.00 35.57 ? 124  ARG   B CD  1 
ATOM   5144 N  NE  . ARG   B 1 101 ? -56.070 -12.700 56.970  1.00 28.71 ? 124  ARG   B NE  1 
ATOM   5145 C  CZ  . ARG   B 1 101 ? -56.233 -11.515 57.517  1.00 28.21 ? 124  ARG   B CZ  1 
ATOM   5146 N  NH1 . ARG   B 1 101 ? -57.370 -10.848 57.447  1.00 28.02 ? 124  ARG   B NH1 1 
ATOM   5147 N  NH2 . ARG   B 1 101 ? -55.215 -11.007 58.186  1.00 30.72 ? 124  ARG   B NH2 1 
ATOM   5148 N  N   . LYS   B 1 102 ? -55.722 -15.377 51.784  1.00 24.68 ? 125  LYS   B N   1 
ATOM   5149 C  CA  . LYS   B 1 102 ? -56.726 -15.854 50.847  1.00 24.39 ? 125  LYS   B CA  1 
ATOM   5150 C  C   . LYS   B 1 102 ? -58.082 -15.250 51.199  1.00 27.99 ? 125  LYS   B C   1 
ATOM   5151 O  O   . LYS   B 1 102 ? -58.478 -15.241 52.372  1.00 26.19 ? 125  LYS   B O   1 
ATOM   5152 C  CB  . LYS   B 1 102 ? -56.768 -17.384 50.888  1.00 24.53 ? 125  LYS   B CB  1 
ATOM   5153 C  CG  . LYS   B 1 102 ? -57.955 -18.029 50.211  1.00 24.10 ? 125  LYS   B CG  1 
ATOM   5154 C  CD  . LYS   B 1 102 ? -57.955 -19.543 50.313  1.00 24.10 ? 125  LYS   B CD  1 
ATOM   5155 C  CE  . LYS   B 1 102 ? -58.342 -20.043 51.688  1.00 23.83 ? 125  LYS   B CE  1 
ATOM   5156 N  NZ  . LYS   B 1 102 ? -58.253 -21.504 51.711  1.00 24.73 ? 125  LYS   B NZ  1 
ATOM   5157 N  N   . ILE   B 1 103 ? -58.768 -14.748 50.159  1.00 25.59 ? 126  ILE   B N   1 
ATOM   5158 C  CA  . ILE   B 1 103 ? -60.070 -14.109 50.247  1.00 23.69 ? 126  ILE   B CA  1 
ATOM   5159 C  C   . ILE   B 1 103 ? -61.035 -14.941 49.414  1.00 26.77 ? 126  ILE   B C   1 
ATOM   5160 O  O   . ILE   B 1 103 ? -60.726 -15.285 48.262  1.00 21.48 ? 126  ILE   B O   1 
ATOM   5161 C  CB  . ILE   B 1 103 ? -60.032 -12.664 49.722  1.00 23.74 ? 126  ILE   B CB  1 
ATOM   5162 C  CG1 . ILE   B 1 103 ? -58.989 -11.833 50.437  1.00 24.29 ? 126  ILE   B CG1 1 
ATOM   5163 C  CG2 . ILE   B 1 103 ? -61.401 -11.978 49.767  1.00 21.48 ? 126  ILE   B CG2 1 
ATOM   5164 C  CD1 . ILE   B 1 103 ? -59.167 -11.769 51.954  1.00 24.95 ? 126  ILE   B CD1 1 
ATOM   5165 N  N   . THR   B 1 104 ? -62.212 -15.220 50.003  1.00 25.28 ? 127  THR   B N   1 
ATOM   5166 C  CA  . THR   B 1 104 ? -63.173 -16.098 49.364  1.00 23.97 ? 127  THR   B CA  1 
ATOM   5167 C  C   . THR   B 1 104 ? -64.379 -15.260 48.983  1.00 20.19 ? 127  THR   B C   1 
ATOM   5168 O  O   . THR   B 1 104 ? -64.481 -14.084 49.334  1.00 21.98 ? 127  THR   B O   1 
ATOM   5169 C  CB  . THR   B 1 104 ? -63.549 -17.297 50.247  1.00 23.56 ? 127  THR   B CB  1 
ATOM   5170 O  OG1 . THR   B 1 104 ? -64.389 -16.791 51.290  1.00 23.57 ? 127  THR   B OG1 1 
ATOM   5171 C  CG2 . THR   B 1 104 ? -62.335 -18.094 50.706  1.00 22.72 ? 127  THR   B CG2 1 
ATOM   5172 N  N   . GLN   B 1 105 ? -65.314 -15.908 48.270  1.00 22.88 ? 128  GLN   B N   1 
ATOM   5173 C  CA  . GLN   B 1 105 ? -66.602 -15.304 47.958  1.00 22.89 ? 128  GLN   B CA  1 
ATOM   5174 C  C   . GLN   B 1 105 ? -67.467 -15.186 49.214  1.00 23.05 ? 128  GLN   B C   1 
ATOM   5175 O  O   . GLN   B 1 105 ? -68.478 -14.494 49.195  1.00 24.61 ? 128  GLN   B O   1 
ATOM   5176 C  CB  . GLN   B 1 105 ? -67.373 -16.110 46.903  1.00 21.91 ? 128  GLN   B CB  1 
ATOM   5177 C  CG  . GLN   B 1 105 ? -68.001 -17.428 47.366  1.00 21.57 ? 128  GLN   B CG  1 
ATOM   5178 C  CD  . GLN   B 1 105 ? -67.049 -18.577 47.594  1.00 22.14 ? 128  GLN   B CD  1 
ATOM   5179 O  OE1 . GLN   B 1 105 ? -65.819 -18.443 47.555  1.00 23.54 ? 128  GLN   B OE1 1 
ATOM   5180 N  NE2 . GLN   B 1 105 ? -67.611 -19.762 47.784  1.00 23.43 ? 128  GLN   B NE2 1 
ATOM   5181 N  N   . ASN   B 1 106 ? -67.076 -15.877 50.292  1.00 22.86 ? 129  ASN   B N   1 
ATOM   5182 C  CA  . ASN   B 1 106 ? -67.803 -15.769 51.550  1.00 23.93 ? 129  ASN   B CA  1 
ATOM   5183 C  C   . ASN   B 1 106 ? -67.225 -14.677 52.436  1.00 26.64 ? 129  ASN   B C   1 
ATOM   5184 O  O   . ASN   B 1 106 ? -67.691 -14.502 53.561  1.00 28.52 ? 129  ASN   B O   1 
ATOM   5185 C  CB  . ASN   B 1 106 ? -67.812 -17.092 52.290  1.00 23.42 ? 129  ASN   B CB  1 
ATOM   5186 C  CG  . ASN   B 1 106 ? -68.812 -17.994 51.636  1.00 22.78 ? 129  ASN   B CG  1 
ATOM   5187 O  OD1 . ASN   B 1 106 ? -69.945 -17.562 51.450  1.00 28.78 ? 129  ASN   B OD1 1 
ATOM   5188 N  ND2 . ASN   B 1 106 ? -68.444 -19.215 51.292  1.00 24.87 ? 129  ASN   B ND2 1 
ATOM   5189 N  N   . ASP   B 1 107 ? -66.233 -13.947 51.911  1.00 22.61 ? 130  ASP   B N   1 
ATOM   5190 C  CA  . ASP   B 1 107 ? -65.614 -12.862 52.635  1.00 25.01 ? 130  ASP   B CA  1 
ATOM   5191 C  C   . ASP   B 1 107 ? -65.987 -11.541 51.987  1.00 24.31 ? 130  ASP   B C   1 
ATOM   5192 O  O   . ASP   B 1 107 ? -66.419 -11.469 50.835  1.00 25.32 ? 130  ASP   B O   1 
ATOM   5193 C  CB  . ASP   B 1 107 ? -64.103 -13.045 52.720  1.00 24.67 ? 130  ASP   B CB  1 
ATOM   5194 C  CG  . ASP   B 1 107 ? -63.655 -14.375 53.298  1.00 26.93 ? 130  ASP   B CG  1 
ATOM   5195 O  OD1 . ASP   B 1 107 ? -64.107 -14.719 54.407  1.00 27.78 ? 130  ASP   B OD1 1 
ATOM   5196 O  OD2 . ASP   B 1 107 ? -62.857 -15.064 52.652  1.00 29.52 ? 130  ASP   B OD2 1 
ATOM   5197 N  N   . LYS   B 1 108 ? -65.795 -10.471 52.745  1.00 23.69 ? 131  LYS   B N   1 
ATOM   5198 C  CA  . LYS   B 1 108 ? -65.870 -9.138  52.185  1.00 22.34 ? 131  LYS   B CA  1 
ATOM   5199 C  C   . LYS   B 1 108 ? -64.798 -8.276  52.833  1.00 24.86 ? 131  LYS   B C   1 
ATOM   5200 O  O   . LYS   B 1 108 ? -64.519 -8.421  54.035  1.00 23.50 ? 131  LYS   B O   1 
ATOM   5201 C  CB  . LYS   B 1 108 ? -67.247 -8.519  52.389  1.00 24.29 ? 131  LYS   B CB  1 
ATOM   5202 C  CG  . LYS   B 1 108 ? -67.375 -7.130  51.803  1.00 23.09 ? 131  LYS   B CG  1 
ATOM   5203 C  CD  . LYS   B 1 108 ? -68.808 -6.771  51.479  1.00 25.99 ? 131  LYS   B CD  1 
ATOM   5204 C  CE  . LYS   B 1 108 ? -69.585 -6.741  52.745  1.00 27.58 ? 131  LYS   B CE  1 
ATOM   5205 N  NZ  . LYS   B 1 108 ? -70.937 -6.273  52.505  1.00 26.43 ? 131  LYS   B NZ  1 
ATOM   5206 N  N   . LEU   B 1 109 ? -64.244 -7.386  52.000  1.00 25.80 ? 132  LEU   B N   1 
ATOM   5207 C  CA  . LEU   B 1 109 ? -63.180 -6.459  52.358  1.00 27.55 ? 132  LEU   B CA  1 
ATOM   5208 C  C   . LEU   B 1 109 ? -63.730 -5.096  52.746  1.00 26.26 ? 132  LEU   B C   1 
ATOM   5209 O  O   . LEU   B 1 109 ? -64.513 -4.480  52.026  1.00 21.40 ? 132  LEU   B O   1 
ATOM   5210 C  CB  . LEU   B 1 109 ? -62.239 -6.300  51.164  1.00 29.34 ? 132  LEU   B CB  1 
ATOM   5211 C  CG  . LEU   B 1 109 ? -61.034 -7.240  51.116  1.00 31.02 ? 132  LEU   B CG  1 
ATOM   5212 C  CD1 . LEU   B 1 109 ? -61.329 -8.668  51.496  1.00 29.18 ? 132  LEU   B CD1 1 
ATOM   5213 C  CD2 . LEU   B 1 109 ? -60.372 -7.194  49.740  1.00 29.55 ? 132  LEU   B CD2 1 
ATOM   5214 N  N   . TRP   B 1 110 ? -63.202 -4.581  53.864  1.00 25.11 ? 133  TRP   B N   1 
ATOM   5215 C  CA  . TRP   B 1 110 ? -63.565 -3.279  54.380  1.00 25.00 ? 133  TRP   B CA  1 
ATOM   5216 C  C   . TRP   B 1 110 ? -62.325 -2.401  54.517  1.00 25.54 ? 133  TRP   B C   1 
ATOM   5217 O  O   . TRP   B 1 110 ? -61.348 -2.793  55.136  1.00 29.91 ? 133  TRP   B O   1 
ATOM   5218 C  CB  . TRP   B 1 110 ? -64.231 -3.450  55.751  1.00 25.57 ? 133  TRP   B CB  1 
ATOM   5219 C  CG  . TRP   B 1 110 ? -65.591 -4.082  55.628  1.00 24.68 ? 133  TRP   B CG  1 
ATOM   5220 C  CD1 . TRP   B 1 110 ? -65.912 -5.403  55.730  1.00 24.57 ? 133  TRP   B CD1 1 
ATOM   5221 C  CD2 . TRP   B 1 110 ? -66.806 -3.381  55.307  1.00 21.89 ? 133  TRP   B CD2 1 
ATOM   5222 N  NE1 . TRP   B 1 110 ? -67.258 -5.576  55.539  1.00 23.72 ? 133  TRP   B NE1 1 
ATOM   5223 C  CE2 . TRP   B 1 110 ? -67.827 -4.349  55.260  1.00 22.79 ? 133  TRP   B CE2 1 
ATOM   5224 C  CE3 . TRP   B 1 110 ? -67.129 -2.042  55.069  1.00 21.43 ? 133  TRP   B CE3 1 
ATOM   5225 C  CZ2 . TRP   B 1 110 ? -69.145 -4.000  54.984  1.00 24.52 ? 133  TRP   B CZ2 1 
ATOM   5226 C  CZ3 . TRP   B 1 110 ? -68.431 -1.704  54.784  1.00 23.74 ? 133  TRP   B CZ3 1 
ATOM   5227 C  CH2 . TRP   B 1 110 ? -69.428 -2.674  54.745  1.00 24.26 ? 133  TRP   B CH2 1 
ATOM   5228 N  N   . TYR   B 1 111 ? -62.410 -1.215  53.944  1.00 23.56 ? 134  TYR   B N   1 
ATOM   5229 C  CA  . TYR   B 1 111 ? -61.311 -0.274  53.955  1.00 26.86 ? 134  TYR   B CA  1 
ATOM   5230 C  C   . TYR   B 1 111 ? -61.824 1.018   54.568  1.00 25.34 ? 134  TYR   B C   1 
ATOM   5231 O  O   . TYR   B 1 111 ? -62.909 1.450   54.224  1.00 26.25 ? 134  TYR   B O   1 
ATOM   5232 C  CB  . TYR   B 1 111 ? -60.828 0.090   52.545  1.00 27.61 ? 134  TYR   B CB  1 
ATOM   5233 C  CG  . TYR   B 1 111 ? -60.198 -1.000  51.689  1.00 27.39 ? 134  TYR   B CG  1 
ATOM   5234 C  CD1 . TYR   B 1 111 ? -60.975 -1.944  51.016  1.00 24.41 ? 134  TYR   B CD1 1 
ATOM   5235 C  CD2 . TYR   B 1 111 ? -58.816 -1.034  51.494  1.00 28.38 ? 134  TYR   B CD2 1 
ATOM   5236 C  CE1 . TYR   B 1 111 ? -60.392 -2.906  50.203  1.00 25.25 ? 134  TYR   B CE1 1 
ATOM   5237 C  CE2 . TYR   B 1 111 ? -58.223 -1.993  50.693  1.00 28.85 ? 134  TYR   B CE2 1 
ATOM   5238 C  CZ  . TYR   B 1 111 ? -59.014 -2.910  50.010  1.00 25.13 ? 134  TYR   B CZ  1 
ATOM   5239 O  OH  . TYR   B 1 111 ? -58.382 -3.847  49.233  1.00 23.86 ? 134  TYR   B OH  1 
ATOM   5240 N  N   . LYS   B 1 112 ? -61.009 1.652   55.434  1.00 27.57 ? 135  LYS   B N   1 
ATOM   5241 C  CA  . LYS   B 1 112 ? -61.342 2.967   55.954  1.00 29.32 ? 135  LYS   B CA  1 
ATOM   5242 C  C   . LYS   B 1 112 ? -60.078 3.804   56.185  1.00 26.36 ? 135  LYS   B C   1 
ATOM   5243 O  O   . LYS   B 1 112 ? -59.076 3.321   56.720  1.00 30.67 ? 135  LYS   B O   1 
ATOM   5244 C  CB  . LYS   B 1 112 ? -62.079 2.815   57.290  1.00 30.85 ? 135  LYS   B CB  1 
ATOM   5245 C  CG  . LYS   B 1 112 ? -62.762 4.056   57.865  1.00 36.00 ? 135  LYS   B CG  1 
ATOM   5246 C  CD  . LYS   B 1 112 ? -63.376 3.800   59.244  1.00 36.92 ? 135  LYS   B CD  1 
ATOM   5247 C  CE  . LYS   B 1 112 ? -62.395 3.135   60.171  1.00 40.17 ? 135  LYS   B CE  1 
ATOM   5248 N  NZ  . LYS   B 1 112 ? -62.898 2.997   61.537  1.00 44.35 ? 135  LYS   B NZ  1 
ATOM   5249 N  N   . ARG   B 1 113 ? -60.194 5.071   55.816  1.00 23.26 ? 136  ARG   B N   1 
ATOM   5250 C  CA  . ARG   B 1 113 ? -59.169 6.052   56.113  1.00 28.27 ? 136  ARG   B CA  1 
ATOM   5251 C  C   . ARG   B 1 113 ? -59.854 7.412   56.132  1.00 28.27 ? 136  ARG   B C   1 
ATOM   5252 O  O   . ARG   B 1 113 ? -60.992 7.538   55.691  1.00 32.50 ? 136  ARG   B O   1 
ATOM   5253 C  CB  . ARG   B 1 113 ? -58.056 6.054   55.056  1.00 27.36 ? 136  ARG   B CB  1 
ATOM   5254 C  CG  . ARG   B 1 113 ? -58.502 6.807   53.809  1.00 28.76 ? 136  ARG   B CG  1 
ATOM   5255 C  CD  . ARG   B 1 113 ? -57.314 7.221   52.976  1.00 35.05 ? 136  ARG   B CD  1 
ATOM   5256 N  NE  . ARG   B 1 113 ? -56.651 8.433   53.477  1.00 38.45 ? 136  ARG   B NE  1 
ATOM   5257 C  CZ  . ARG   B 1 113 ? -55.383 8.765   53.235  1.00 42.07 ? 136  ARG   B CZ  1 
ATOM   5258 N  NH1 . ARG   B 1 113 ? -54.613 8.030   52.437  1.00 40.62 ? 136  ARG   B NH1 1 
ATOM   5259 N  NH2 . ARG   B 1 113 ? -54.881 9.842   53.820  1.00 43.88 ? 136  ARG   B NH2 1 
ATOM   5260 N  N   . THR   B 1 114 ? -59.156 8.418   56.666  1.00 31.00 ? 137  THR   B N   1 
ATOM   5261 C  CA  . THR   B 1 114 ? -59.695 9.762   56.716  1.00 32.79 ? 137  THR   B CA  1 
ATOM   5262 C  C   . THR   B 1 114 ? -58.919 10.610  55.720  1.00 32.46 ? 137  THR   B C   1 
ATOM   5263 O  O   . THR   B 1 114 ? -57.816 10.239  55.309  1.00 30.87 ? 137  THR   B O   1 
ATOM   5264 C  CB  . THR   B 1 114 ? -59.605 10.333  58.137  1.00 36.47 ? 137  THR   B CB  1 
ATOM   5265 O  OG1 . THR   B 1 114 ? -58.222 10.506  58.425  1.00 37.43 ? 137  THR   B OG1 1 
ATOM   5266 C  CG2 . THR   B 1 114 ? -60.193 9.409   59.190  1.00 36.21 ? 137  THR   B CG2 1 
ATOM   5267 N  N   . PHE   B 1 115 ? -59.502 11.747  55.350  1.00 32.23 ? 138  PHE   B N   1 
ATOM   5268 C  CA  . PHE   B 1 115 ? -58.803 12.697  54.505  1.00 32.80 ? 138  PHE   B CA  1 
ATOM   5269 C  C   . PHE   B 1 115 ? -59.442 14.069  54.658  1.00 33.59 ? 138  PHE   B C   1 
ATOM   5270 O  O   . PHE   B 1 115 ? -60.574 14.183  55.111  1.00 33.62 ? 138  PHE   B O   1 
ATOM   5271 C  CB  . PHE   B 1 115 ? -58.888 12.237  53.047  1.00 35.01 ? 138  PHE   B CB  1 
ATOM   5272 C  CG  . PHE   B 1 115 ? -60.301 12.340  52.490  1.00 34.33 ? 138  PHE   B CG  1 
ATOM   5273 C  CD1 . PHE   B 1 115 ? -61.235 11.321  52.702  1.00 34.52 ? 138  PHE   B CD1 1 
ATOM   5274 C  CD2 . PHE   B 1 115 ? -60.704 13.484  51.813  1.00 30.37 ? 138  PHE   B CD2 1 
ATOM   5275 C  CE1 . PHE   B 1 115 ? -62.521 11.428  52.200  1.00 34.36 ? 138  PHE   B CE1 1 
ATOM   5276 C  CE2 . PHE   B 1 115 ? -61.993 13.587  51.321  1.00 33.22 ? 138  PHE   B CE2 1 
ATOM   5277 C  CZ  . PHE   B 1 115 ? -62.902 12.567  51.519  1.00 33.69 ? 138  PHE   B CZ  1 
ATOM   5278 N  N   . THR   B 1 116 ? -58.708 15.099  54.230  1.00 36.66 ? 139  THR   B N   1 
ATOM   5279 C  CA  . THR   B 1 116 ? -59.210 16.466  54.170  1.00 37.55 ? 139  THR   B CA  1 
ATOM   5280 C  C   . THR   B 1 116 ? -59.010 16.960  52.745  1.00 35.40 ? 139  THR   B C   1 
ATOM   5281 O  O   . THR   B 1 116 ? -58.140 16.440  52.058  1.00 36.60 ? 139  THR   B O   1 
ATOM   5282 C  CB  . THR   B 1 116 ? -58.442 17.328  55.175  1.00 40.85 ? 139  THR   B CB  1 
ATOM   5283 O  OG1 . THR   B 1 116 ? -57.251 17.675  54.486  1.00 43.02 ? 139  THR   B OG1 1 
ATOM   5284 C  CG2 . THR   B 1 116 ? -58.058 16.577  56.439  1.00 39.93 ? 139  THR   B CG2 1 
ATOM   5285 N  N   . VAL   B 1 117 ? -59.795 17.954  52.316  1.00 37.47 ? 140  VAL   B N   1 
ATOM   5286 C  CA  . VAL   B 1 117 ? -59.731 18.433  50.945  1.00 42.90 ? 140  VAL   B CA  1 
ATOM   5287 C  C   . VAL   B 1 117 ? -59.035 19.792  50.919  1.00 42.72 ? 140  VAL   B C   1 
ATOM   5288 O  O   . VAL   B 1 117 ? -59.321 20.639  51.756  1.00 42.40 ? 140  VAL   B O   1 
ATOM   5289 C  CB  . VAL   B 1 117 ? -61.116 18.481  50.271  1.00 44.81 ? 140  VAL   B CB  1 
ATOM   5290 C  CG1 . VAL   B 1 117 ? -61.876 17.183  50.522  1.00 50.12 ? 140  VAL   B CG1 1 
ATOM   5291 C  CG2 . VAL   B 1 117 ? -61.967 19.670  50.687  1.00 42.90 ? 140  VAL   B CG2 1 
ATOM   5292 N  N   . PRO   B 1 118 ? -58.094 20.029  49.970  1.00 40.79 ? 141  PRO   B N   1 
ATOM   5293 C  CA  . PRO   B 1 118 ? -57.485 21.349  49.771  1.00 42.24 ? 141  PRO   B CA  1 
ATOM   5294 C  C   . PRO   B 1 118 ? -58.420 22.558  49.696  1.00 40.17 ? 141  PRO   B C   1 
ATOM   5295 O  O   . PRO   B 1 118 ? -59.307 22.632  48.846  1.00 39.39 ? 141  PRO   B O   1 
ATOM   5296 C  CB  . PRO   B 1 118 ? -56.713 21.172  48.436  1.00 41.80 ? 141  PRO   B CB  1 
ATOM   5297 C  CG  . PRO   B 1 118 ? -56.326 19.712  48.433  1.00 42.92 ? 141  PRO   B CG  1 
ATOM   5298 C  CD  . PRO   B 1 118 ? -57.533 19.015  49.063  1.00 43.51 ? 141  PRO   B CD  1 
ATOM   5299 N  N   . SER   B 1 119 ? -58.117 23.565  50.523  1.00 39.50 ? 142  SER   B N   1 
ATOM   5300 C  CA  . SER   B 1 119 ? -58.882 24.800  50.593  1.00 37.67 ? 142  SER   B CA  1 
ATOM   5301 C  C   . SER   B 1 119 ? -59.029 25.479  49.223  1.00 34.54 ? 142  SER   B C   1 
ATOM   5302 O  O   . SER   B 1 119 ? -60.065 26.079  48.922  1.00 32.60 ? 142  SER   B O   1 
ATOM   5303 C  CB  . SER   B 1 119 ? -58.259 25.726  51.631  1.00 39.92 ? 142  SER   B CB  1 
ATOM   5304 O  OG  . SER   B 1 119 ? -58.259 27.065  51.162  1.00 48.55 ? 142  SER   B OG  1 
ATOM   5305 N  N   . ASN   B 1 120 ? -58.012 25.366  48.359  1.00 34.26 ? 143  ASN   B N   1 
ATOM   5306 C  CA  . ASN   B 1 120 ? -58.064 25.989  47.042  1.00 32.59 ? 143  ASN   B CA  1 
ATOM   5307 C  C   . ASN   B 1 120 ? -59.043 25.260  46.106  1.00 32.51 ? 143  ASN   B C   1 
ATOM   5308 O  O   . ASN   B 1 120 ? -59.272 25.730  44.996  1.00 32.56 ? 143  ASN   B O   1 
ATOM   5309 C  CB  . ASN   B 1 120 ? -56.667 26.137  46.430  1.00 34.69 ? 143  ASN   B CB  1 
ATOM   5310 C  CG  . ASN   B 1 120 ? -55.905 24.829  46.316  1.00 39.00 ? 143  ASN   B CG  1 
ATOM   5311 O  OD1 . ASN   B 1 120 ? -55.608 24.187  47.334  1.00 41.76 ? 143  ASN   B OD1 1 
ATOM   5312 N  ND2 . ASN   B 1 120 ? -55.539 24.429  45.101  1.00 38.10 ? 143  ASN   B ND2 1 
ATOM   5313 N  N   . TRP   B 1 121 ? -59.660 24.143  46.529  1.00 33.76 ? 144  TRP   B N   1 
ATOM   5314 C  CA  . TRP   B 1 121 ? -60.645 23.463  45.681  1.00 33.84 ? 144  TRP   B CA  1 
ATOM   5315 C  C   . TRP   B 1 121 ? -62.060 23.992  45.916  1.00 37.18 ? 144  TRP   B C   1 
ATOM   5316 O  O   . TRP   B 1 121 ? -62.968 23.704  45.129  1.00 33.12 ? 144  TRP   B O   1 
ATOM   5317 C  CB  . TRP   B 1 121 ? -60.626 21.944  45.902  1.00 33.92 ? 144  TRP   B CB  1 
ATOM   5318 C  CG  . TRP   B 1 121 ? -59.333 21.258  45.539  1.00 34.07 ? 144  TRP   B CG  1 
ATOM   5319 C  CD1 . TRP   B 1 121 ? -58.155 21.826  45.143  1.00 32.41 ? 144  TRP   B CD1 1 
ATOM   5320 C  CD2 . TRP   B 1 121 ? -59.102 19.833  45.581  1.00 33.45 ? 144  TRP   B CD2 1 
ATOM   5321 N  NE1 . TRP   B 1 121 ? -57.204 20.860  44.960  1.00 32.85 ? 144  TRP   B NE1 1 
ATOM   5322 C  CE2 . TRP   B 1 121 ? -57.755 19.628  45.210  1.00 33.13 ? 144  TRP   B CE2 1 
ATOM   5323 C  CE3 . TRP   B 1 121 ? -59.896 18.724  45.893  1.00 31.56 ? 144  TRP   B CE3 1 
ATOM   5324 C  CZ2 . TRP   B 1 121 ? -57.195 18.352  45.148  1.00 30.84 ? 144  TRP   B CZ2 1 
ATOM   5325 C  CZ3 . TRP   B 1 121 ? -59.345 17.464  45.816  1.00 30.26 ? 144  TRP   B CZ3 1 
ATOM   5326 C  CH2 . TRP   B 1 121 ? -58.005 17.284  45.463  1.00 33.15 ? 144  TRP   B CH2 1 
ATOM   5327 N  N   . ASN   B 1 122 ? -62.252 24.775  46.994  1.00 36.06 ? 145  ASN   B N   1 
ATOM   5328 C  CA  . ASN   B 1 122 ? -63.549 25.368  47.288  1.00 35.88 ? 145  ASN   B CA  1 
ATOM   5329 C  C   . ASN   B 1 122 ? -64.080 26.036  46.021  1.00 31.46 ? 145  ASN   B C   1 
ATOM   5330 O  O   . ASN   B 1 122 ? -63.345 26.761  45.362  1.00 27.92 ? 145  ASN   B O   1 
ATOM   5331 C  CB  . ASN   B 1 122 ? -63.456 26.363  48.446  1.00 42.59 ? 145  ASN   B CB  1 
ATOM   5332 C  CG  . ASN   B 1 122 ? -64.815 26.711  49.019  1.00 47.92 ? 145  ASN   B CG  1 
ATOM   5333 O  OD1 . ASN   B 1 122 ? -65.460 25.861  49.646  1.00 52.93 ? 145  ASN   B OD1 1 
ATOM   5334 N  ND2 . ASN   B 1 122 ? -65.268 27.942  48.830  1.00 49.83 ? 145  ASN   B ND2 1 
ATOM   5335 N  N   . GLY   B 1 123 ? -65.339 25.763  45.653  1.00 30.79 ? 146  GLY   B N   1 
ATOM   5336 C  CA  . GLY   B 1 123 ? -65.924 26.388  44.478  1.00 32.91 ? 146  GLY   B CA  1 
ATOM   5337 C  C   . GLY   B 1 123 ? -65.966 25.431  43.288  1.00 33.13 ? 146  GLY   B C   1 
ATOM   5338 O  O   . GLY   B 1 123 ? -66.497 25.772  42.247  1.00 33.17 ? 146  GLY   B O   1 
ATOM   5339 N  N   . ARG   B 1 124 ? -65.393 24.237  43.433  1.00 36.78 ? 147  ARG   B N   1 
ATOM   5340 C  CA  . ARG   B 1 124 ? -65.416 23.264  42.351  1.00 32.84 ? 147  ARG   B CA  1 
ATOM   5341 C  C   . ARG   B 1 124 ? -66.047 21.972  42.857  1.00 31.85 ? 147  ARG   B C   1 
ATOM   5342 O  O   . ARG   B 1 124 ? -66.070 21.723  44.067  1.00 26.87 ? 147  ARG   B O   1 
ATOM   5343 C  CB  . ARG   B 1 124 ? -63.992 22.999  41.848  1.00 32.92 ? 147  ARG   B CB  1 
ATOM   5344 C  CG  . ARG   B 1 124 ? -63.467 23.984  40.818  1.00 31.59 ? 147  ARG   B CG  1 
ATOM   5345 C  CD  . ARG   B 1 124 ? -61.987 23.720  40.488  1.00 32.69 ? 147  ARG   B CD  1 
ATOM   5346 N  NE  . ARG   B 1 124 ? -61.028 24.021  41.566  1.00 32.18 ? 147  ARG   B NE  1 
ATOM   5347 C  CZ  . ARG   B 1 124 ? -59.694 23.904  41.466  1.00 33.32 ? 147  ARG   B CZ  1 
ATOM   5348 N  NH1 . ARG   B 1 124 ? -59.136 23.332  40.400  1.00 31.07 ? 147  ARG   B NH1 1 
ATOM   5349 N  NH2 . ARG   B 1 124 ? -58.909 24.337  42.445  1.00 32.09 ? 147  ARG   B NH2 1 
ATOM   5350 N  N   . ARG   B 1 125 ? -66.509 21.125  41.916  1.00 28.76 ? 148  ARG   B N   1 
ATOM   5351 C  CA  . ARG   B 1 125 ? -66.952 19.792  42.299  1.00 31.81 ? 148  ARG   B CA  1 
ATOM   5352 C  C   . ARG   B 1 125 ? -65.716 18.994  42.698  1.00 29.95 ? 148  ARG   B C   1 
ATOM   5353 O  O   . ARG   B 1 125 ? -64.615 19.290  42.250  1.00 30.31 ? 148  ARG   B O   1 
ATOM   5354 C  CB  . ARG   B 1 125 ? -67.737 19.063  41.205  1.00 31.78 ? 148  ARG   B CB  1 
ATOM   5355 C  CG  . ARG   B 1 125 ? -68.743 19.857  40.382  1.00 33.50 ? 148  ARG   B CG  1 
ATOM   5356 C  CD  . ARG   B 1 125 ? -69.997 20.174  41.143  1.00 35.71 ? 148  ARG   B CD  1 
ATOM   5357 N  NE  . ARG   B 1 125 ? -70.600 18.960  41.715  1.00 35.07 ? 148  ARG   B NE  1 
ATOM   5358 C  CZ  . ARG   B 1 125 ? -71.432 19.001  42.743  1.00 37.25 ? 148  ARG   B CZ  1 
ATOM   5359 N  NH1 . ARG   B 1 125 ? -71.795 20.175  43.221  1.00 39.28 ? 148  ARG   B NH1 1 
ATOM   5360 N  NH2 . ARG   B 1 125 ? -71.886 17.897  43.311  1.00 33.21 ? 148  ARG   B NH2 1 
ATOM   5361 N  N   . VAL   B 1 126 ? -65.895 17.986  43.549  1.00 29.04 ? 149  VAL   B N   1 
ATOM   5362 C  CA  . VAL   B 1 126 ? -64.802 17.105  43.910  1.00 28.68 ? 149  VAL   B CA  1 
ATOM   5363 C  C   . VAL   B 1 126 ? -65.141 15.671  43.490  1.00 30.37 ? 149  VAL   B C   1 
ATOM   5364 O  O   . VAL   B 1 126 ? -66.145 15.103  43.930  1.00 26.29 ? 149  VAL   B O   1 
ATOM   5365 C  CB  . VAL   B 1 126 ? -64.445 17.171  45.405  1.00 29.03 ? 149  VAL   B CB  1 
ATOM   5366 C  CG1 . VAL   B 1 126 ? -63.381 16.145  45.791  1.00 28.88 ? 149  VAL   B CG1 1 
ATOM   5367 C  CG2 . VAL   B 1 126 ? -63.994 18.563  45.823  1.00 29.58 ? 149  VAL   B CG2 1 
ATOM   5368 N  N   . GLN   B 1 127 ? -64.227 15.076  42.709  1.00 27.28 ? 150  GLN   B N   1 
ATOM   5369 C  CA  . GLN   B 1 127 ? -64.365 13.719  42.203  1.00 24.23 ? 150  GLN   B CA  1 
ATOM   5370 C  C   . GLN   B 1 127 ? -63.504 12.749  43.004  1.00 23.95 ? 150  GLN   B C   1 
ATOM   5371 O  O   . GLN   B 1 127 ? -62.323 12.997  43.250  1.00 24.35 ? 150  GLN   B O   1 
ATOM   5372 C  CB  . GLN   B 1 127 ? -63.936 13.710  40.729  1.00 22.99 ? 150  GLN   B CB  1 
ATOM   5373 C  CG  . GLN   B 1 127 ? -64.522 14.809  39.847  1.00 23.46 ? 150  GLN   B CG  1 
ATOM   5374 C  CD  . GLN   B 1 127 ? -66.038 14.835  39.759  1.00 24.68 ? 150  GLN   B CD  1 
ATOM   5375 O  OE1 . GLN   B 1 127 ? -66.730 13.951  40.256  1.00 23.90 ? 150  GLN   B OE1 1 
ATOM   5376 N  NE2 . GLN   B 1 127 ? -66.584 15.851  39.107  1.00 26.45 ? 150  GLN   B NE2 1 
ATOM   5377 N  N   . LEU   B 1 128 ? -64.073 11.597  43.376  1.00 22.39 ? 151  LEU   B N   1 
ATOM   5378 C  CA  . LEU   B 1 128 ? -63.308 10.498  43.934  1.00 22.46 ? 151  LEU   B CA  1 
ATOM   5379 C  C   . LEU   B 1 128 ? -63.129 9.424   42.851  1.00 25.27 ? 151  LEU   B C   1 
ATOM   5380 O  O   . LEU   B 1 128 ? -64.117 8.821   42.381  1.00 22.82 ? 151  LEU   B O   1 
ATOM   5381 C  CB  . LEU   B 1 128 ? -64.034 9.947   45.152  1.00 22.54 ? 151  LEU   B CB  1 
ATOM   5382 C  CG  . LEU   B 1 128 ? -63.485 8.655   45.753  1.00 23.87 ? 151  LEU   B CG  1 
ATOM   5383 C  CD1 . LEU   B 1 128 ? -62.080 8.831   46.271  1.00 22.22 ? 151  LEU   B CD1 1 
ATOM   5384 C  CD2 . LEU   B 1 128 ? -64.409 8.202   46.852  1.00 25.71 ? 151  LEU   B CD2 1 
ATOM   5385 N  N   . ASN   B 1 129 ? -61.854 9.234   42.470  1.00 23.12 ? 152  ASN   B N   1 
ATOM   5386 C  CA  . ASN   B 1 129 ? -61.399 8.354   41.401  1.00 21.97 ? 152  ASN   B CA  1 
ATOM   5387 C  C   . ASN   B 1 129 ? -60.848 7.026   41.908  1.00 20.50 ? 152  ASN   B C   1 
ATOM   5388 O  O   . ASN   B 1 129 ? -60.000 6.959   42.789  1.00 20.52 ? 152  ASN   B O   1 
ATOM   5389 C  CB  . ASN   B 1 129 ? -60.364 9.088   40.559  1.00 22.24 ? 152  ASN   B CB  1 
ATOM   5390 C  CG  . ASN   B 1 129 ? -61.023 10.228  39.847  1.00 23.23 ? 152  ASN   B CG  1 
ATOM   5391 O  OD1 . ASN   B 1 129 ? -62.228 10.154  39.598  1.00 26.00 ? 152  ASN   B OD1 1 
ATOM   5392 N  ND2 . ASN   B 1 129 ? -60.291 11.280  39.519  1.00 23.81 ? 152  ASN   B ND2 1 
ATOM   5393 N  N   . PHE   B 1 130 ? -61.325 5.940   41.267  1.00 18.86 ? 153  PHE   B N   1 
ATOM   5394 C  CA  . PHE   B 1 130 ? -60.806 4.602   41.469  1.00 18.23 ? 153  PHE   B CA  1 
ATOM   5395 C  C   . PHE   B 1 130 ? -60.299 4.085   40.127  1.00 16.45 ? 153  PHE   B C   1 
ATOM   5396 O  O   . PHE   B 1 130 ? -61.061 4.086   39.181  1.00 19.77 ? 153  PHE   B O   1 
ATOM   5397 C  CB  . PHE   B 1 130 ? -61.930 3.690   41.958  1.00 18.95 ? 153  PHE   B CB  1 
ATOM   5398 C  CG  . PHE   B 1 130 ? -62.318 3.885   43.415  1.00 18.80 ? 153  PHE   B CG  1 
ATOM   5399 C  CD1 . PHE   B 1 130 ? -63.254 4.836   43.763  1.00 21.16 ? 153  PHE   B CD1 1 
ATOM   5400 C  CD2 . PHE   B 1 130 ? -61.742 3.106   44.413  1.00 20.04 ? 153  PHE   B CD2 1 
ATOM   5401 C  CE1 . PHE   B 1 130 ? -63.608 5.014   45.096  1.00 19.82 ? 153  PHE   B CE1 1 
ATOM   5402 C  CE2 . PHE   B 1 130 ? -62.106 3.275   45.745  1.00 23.09 ? 153  PHE   B CE2 1 
ATOM   5403 C  CZ  . PHE   B 1 130 ? -63.043 4.225   46.076  1.00 21.30 ? 153  PHE   B CZ  1 
ATOM   5404 N  N   . GLY   B 1 131 ? -59.009 3.766   40.030  1.00 18.20 ? 154  GLY   B N   1 
ATOM   5405 C  CA  . GLY   B 1 131 ? -58.457 3.165   38.824  1.00 17.75 ? 154  GLY   B CA  1 
ATOM   5406 C  C   . GLY   B 1 131 ? -59.057 1.783   38.582  1.00 18.70 ? 154  GLY   B C   1 
ATOM   5407 O  O   . GLY   B 1 131 ? -59.428 1.468   37.459  1.00 18.49 ? 154  GLY   B O   1 
ATOM   5408 N  N   . ALA   B 1 132 ? -59.132 0.985   39.648  1.00 19.06 ? 155  ALA   B N   1 
ATOM   5409 C  CA  . ALA   B 1 132 ? -59.696 -0.357  39.630  1.00 19.93 ? 155  ALA   B CA  1 
ATOM   5410 C  C   . ALA   B 1 132 ? -59.897 -0.910  41.050  1.00 20.51 ? 155  ALA   B C   1 
ATOM   5411 O  O   . ALA   B 1 132 ? -59.099 -0.722  41.975  1.00 17.99 ? 155  ALA   B O   1 
ATOM   5412 C  CB  . ALA   B 1 132 ? -58.856 -1.323  38.802  1.00 18.49 ? 155  ALA   B CB  1 
ATOM   5413 N  N   . SER   B 1 133 ? -60.986 -1.674  41.203  1.00 18.33 ? 156  SER   B N   1 
ATOM   5414 C  CA  . SER   B 1 133 ? -61.238 -2.407  42.429  1.00 16.72 ? 156  SER   B CA  1 
ATOM   5415 C  C   . SER   B 1 133 ? -62.029 -3.651  42.059  1.00 14.98 ? 156  SER   B C   1 
ATOM   5416 O  O   . SER   B 1 133 ? -63.051 -3.511  41.372  1.00 16.79 ? 156  SER   B O   1 
ATOM   5417 C  CB  . SER   B 1 133 ? -61.989 -1.589  43.448  1.00 17.42 ? 156  SER   B CB  1 
ATOM   5418 O  OG  . SER   B 1 133 ? -62.168 -2.353  44.631  1.00 18.71 ? 156  SER   B OG  1 
ATOM   5419 N  N   . ASP   B 1 134 ? -61.528 -4.816  42.498  1.00 16.75 ? 157  ASP   B N   1 
ATOM   5420 C  CA  . ASP   B 1 134 ? -62.073 -6.121  42.118  1.00 16.08 ? 157  ASP   B CA  1 
ATOM   5421 C  C   . ASP   B 1 134 ? -62.812 -6.753  43.307  1.00 17.56 ? 157  ASP   B C   1 
ATOM   5422 O  O   . ASP   B 1 134 ? -62.161 -7.053  44.309  1.00 16.72 ? 157  ASP   B O   1 
ATOM   5423 C  CB  . ASP   B 1 134 ? -60.967 -7.069  41.682  1.00 16.60 ? 157  ASP   B CB  1 
ATOM   5424 C  CG  . ASP   B 1 134 ? -61.353 -8.222  40.766  1.00 16.89 ? 157  ASP   B CG  1 
ATOM   5425 O  OD1 . ASP   B 1 134 ? -62.456 -8.155  40.188  1.00 15.79 ? 157  ASP   B OD1 1 
ATOM   5426 O  OD2 . ASP   B 1 134 ? -60.612 -9.242  40.754  1.00 18.49 ? 157  ASP   B OD2 1 
ATOM   5427 N  N   . TRP   B 1 135 ? -64.125 -7.059  43.187  1.00 16.35 ? 158  TRP   B N   1 
ATOM   5428 C  CA  . TRP   B 1 135 ? -64.952 -6.946  41.988  1.00 15.83 ? 158  TRP   B CA  1 
ATOM   5429 C  C   . TRP   B 1 135 ? -66.105 -5.944  42.155  1.00 14.62 ? 158  TRP   B C   1 
ATOM   5430 O  O   . TRP   B 1 135 ? -66.346 -5.112  41.272  1.00 13.85 ? 158  TRP   B O   1 
ATOM   5431 C  CB  . TRP   B 1 135 ? -65.522 -8.324  41.624  1.00 15.87 ? 158  TRP   B CB  1 
ATOM   5432 C  CG  . TRP   B 1 135 ? -66.387 -8.228  40.402  1.00 16.76 ? 158  TRP   B CG  1 
ATOM   5433 C  CD1 . TRP   B 1 135 ? -65.938 -7.915  39.151  1.00 17.41 ? 158  TRP   B CD1 1 
ATOM   5434 C  CD2 . TRP   B 1 135 ? -67.818 -8.417  40.295  1.00 16.99 ? 158  TRP   B CD2 1 
ATOM   5435 N  NE1 . TRP   B 1 135 ? -66.987 -7.870  38.272  1.00 17.03 ? 158  TRP   B NE1 1 
ATOM   5436 C  CE2 . TRP   B 1 135 ? -68.149 -8.198  38.937  1.00 16.35 ? 158  TRP   B CE2 1 
ATOM   5437 C  CE3 . TRP   B 1 135 ? -68.832 -8.752  41.200  1.00 16.94 ? 158  TRP   B CE3 1 
ATOM   5438 C  CZ2 . TRP   B 1 135 ? -69.464 -8.285  38.470  1.00 17.68 ? 158  TRP   B CZ2 1 
ATOM   5439 C  CZ3 . TRP   B 1 135 ? -70.130 -8.833  40.738  1.00 17.77 ? 158  TRP   B CZ3 1 
ATOM   5440 C  CH2 . TRP   B 1 135 ? -70.438 -8.622  39.393  1.00 17.49 ? 158  TRP   B CH2 1 
ATOM   5441 N  N   . ARG   B 1 136 ? -66.817 -5.998  43.310  1.00 16.49 ? 159  ARG   B N   1 
ATOM   5442 C  CA  . ARG   B 1 136 ? -67.998 -5.179  43.559  1.00 17.53 ? 159  ARG   B CA  1 
ATOM   5443 C  C   . ARG   B 1 136 ? -67.734 -4.222  44.727  1.00 17.57 ? 159  ARG   B C   1 
ATOM   5444 O  O   . ARG   B 1 136 ? -67.457 -4.687  45.840  1.00 19.96 ? 159  ARG   B O   1 
ATOM   5445 C  CB  . ARG   B 1 136 ? -69.205 -6.082  43.848  1.00 20.43 ? 159  ARG   B CB  1 
ATOM   5446 C  CG  . ARG   B 1 136 ? -70.487 -5.307  44.141  1.00 21.59 ? 159  ARG   B CG  1 
ATOM   5447 C  CD  . ARG   B 1 136 ? -71.679 -6.235  44.377  1.00 25.95 ? 159  ARG   B CD  1 
ATOM   5448 N  NE  . ARG   B 1 136 ? -71.998 -6.888  43.101  1.00 32.95 ? 159  ARG   B NE  1 
ATOM   5449 C  CZ  . ARG   B 1 136 ? -72.975 -6.574  42.263  1.00 35.41 ? 159  ARG   B CZ  1 
ATOM   5450 N  NH1 . ARG   B 1 136 ? -73.640 -5.441  42.422  1.00 46.96 ? 159  ARG   B NH1 1 
ATOM   5451 N  NH2 . ARG   B 1 136 ? -73.263 -7.353  41.224  1.00 31.02 ? 159  ARG   B NH2 1 
ATOM   5452 N  N   . THR   B 1 137 ? -67.739 -2.928  44.394  1.00 18.06 ? 160  THR   B N   1 
ATOM   5453 C  CA  . THR   B 1 137 ? -67.261 -1.866  45.261  1.00 18.99 ? 160  THR   B CA  1 
ATOM   5454 C  C   . THR   B 1 137 ? -68.419 -0.931  45.629  1.00 19.30 ? 160  THR   B C   1 
ATOM   5455 O  O   . THR   B 1 137 ? -69.136 -0.397  44.778  1.00 19.58 ? 160  THR   B O   1 
ATOM   5456 C  CB  . THR   B 1 137 ? -66.126 -1.093  44.588  1.00 20.00 ? 160  THR   B CB  1 
ATOM   5457 O  OG1 . THR   B 1 137 ? -65.136 -2.045  44.242  1.00 17.78 ? 160  THR   B OG1 1 
ATOM   5458 C  CG2 . THR   B 1 137 ? -65.487 -0.124  45.568  1.00 21.60 ? 160  THR   B CG2 1 
ATOM   5459 N  N   . THR   B 1 138 ? -68.566 -0.726  46.944  1.00 22.64 ? 161  THR   B N   1 
ATOM   5460 C  CA  . THR   B 1 138 ? -69.515 0.233   47.484  1.00 21.94 ? 161  THR   B CA  1 
ATOM   5461 C  C   . THR   B 1 138 ? -68.714 1.223   48.328  1.00 20.28 ? 161  THR   B C   1 
ATOM   5462 O  O   . THR   B 1 138 ? -67.817 0.814   49.067  1.00 20.41 ? 161  THR   B O   1 
ATOM   5463 C  CB  . THR   B 1 138 ? -70.576 -0.489  48.320  1.00 23.32 ? 161  THR   B CB  1 
ATOM   5464 O  OG1 . THR   B 1 138 ? -70.966 -1.700  47.671  1.00 24.05 ? 161  THR   B OG1 1 
ATOM   5465 C  CG2 . THR   B 1 138 ? -71.804 0.368   48.548  1.00 23.67 ? 161  THR   B CG2 1 
ATOM   5466 N  N   . VAL   B 1 139 ? -69.037 2.502   48.182  1.00 20.54 ? 162  VAL   B N   1 
ATOM   5467 C  CA  . VAL   B 1 139 ? -68.259 3.568   48.785  1.00 25.64 ? 162  VAL   B CA  1 
ATOM   5468 C  C   . VAL   B 1 139 ? -69.160 4.413   49.686  1.00 27.10 ? 162  VAL   B C   1 
ATOM   5469 O  O   . VAL   B 1 139 ? -70.240 4.829   49.276  1.00 25.78 ? 162  VAL   B O   1 
ATOM   5470 C  CB  . VAL   B 1 139 ? -67.621 4.454   47.697  1.00 29.53 ? 162  VAL   B CB  1 
ATOM   5471 C  CG1 . VAL   B 1 139 ? -66.740 5.542   48.302  1.00 28.77 ? 162  VAL   B CG1 1 
ATOM   5472 C  CG2 . VAL   B 1 139 ? -66.827 3.602   46.708  1.00 28.45 ? 162  VAL   B CG2 1 
ATOM   5473 N  N   . TRP   B 1 140 ? -68.653 4.702   50.893  1.00 31.06 ? 163  TRP   B N   1 
ATOM   5474 C  CA  . TRP   B 1 140 ? -69.311 5.630   51.800  1.00 33.08 ? 163  TRP   B CA  1 
ATOM   5475 C  C   . TRP   B 1 140 ? -68.320 6.734   52.179  1.00 30.03 ? 163  TRP   B C   1 
ATOM   5476 O  O   . TRP   B 1 140 ? -67.206 6.450   52.632  1.00 31.63 ? 163  TRP   B O   1 
ATOM   5477 C  CB  . TRP   B 1 140 ? -69.862 4.903   53.039  1.00 32.46 ? 163  TRP   B CB  1 
ATOM   5478 C  CG  . TRP   B 1 140 ? -70.946 3.887   52.767  1.00 30.95 ? 163  TRP   B CG  1 
ATOM   5479 C  CD1 . TRP   B 1 140 ? -72.296 4.093   52.770  1.00 29.85 ? 163  TRP   B CD1 1 
ATOM   5480 C  CD2 . TRP   B 1 140 ? -70.767 2.481   52.501  1.00 30.41 ? 163  TRP   B CD2 1 
ATOM   5481 N  NE1 . TRP   B 1 140 ? -72.963 2.930   52.494  1.00 27.88 ? 163  TRP   B NE1 1 
ATOM   5482 C  CE2 . TRP   B 1 140 ? -72.058 1.921   52.347  1.00 29.73 ? 163  TRP   B CE2 1 
ATOM   5483 C  CE3 . TRP   B 1 140 ? -69.654 1.646   52.385  1.00 31.04 ? 163  TRP   B CE3 1 
ATOM   5484 C  CZ2 . TRP   B 1 140 ? -72.255 0.573   52.084  1.00 29.33 ? 163  TRP   B CZ2 1 
ATOM   5485 C  CZ3 . TRP   B 1 140 ? -69.854 0.305   52.140  1.00 32.48 ? 163  TRP   B CZ3 1 
ATOM   5486 C  CH2 . TRP   B 1 140 ? -71.139 -0.227  52.021  1.00 32.11 ? 163  TRP   B CH2 1 
ATOM   5487 N  N   . VAL   B 1 141 ? -68.737 7.974   51.888  1.00 28.53 ? 164  VAL   B N   1 
ATOM   5488 C  CA  . VAL   B 1 141 ? -68.119 9.178   52.404  1.00 29.28 ? 164  VAL   B CA  1 
ATOM   5489 C  C   . VAL   B 1 141 ? -68.946 9.684   53.589  1.00 34.08 ? 164  VAL   B C   1 
ATOM   5490 O  O   . VAL   B 1 141 ? -70.084 10.122  53.403  1.00 35.02 ? 164  VAL   B O   1 
ATOM   5491 C  CB  . VAL   B 1 141 ? -68.039 10.212  51.271  1.00 29.15 ? 164  VAL   B CB  1 
ATOM   5492 C  CG1 . VAL   B 1 141 ? -67.483 11.559  51.726  1.00 31.45 ? 164  VAL   B CG1 1 
ATOM   5493 C  CG2 . VAL   B 1 141 ? -67.210 9.660   50.113  1.00 29.04 ? 164  VAL   B CG2 1 
ATOM   5494 N  N   . ASN   B 1 142 ? -68.350 9.630   54.785  1.00 34.43 ? 165  ASN   B N   1 
ATOM   5495 C  CA  . ASN   B 1 142 ? -68.974 10.165  55.988  1.00 38.68 ? 165  ASN   B CA  1 
ATOM   5496 C  C   . ASN   B 1 142 ? -70.303 9.433   56.200  1.00 39.11 ? 165  ASN   B C   1 
ATOM   5497 O  O   . ASN   B 1 142 ? -71.350 10.066  56.292  1.00 38.16 ? 165  ASN   B O   1 
ATOM   5498 C  CB  . ASN   B 1 142 ? -69.137 11.687  55.927  1.00 33.44 ? 165  ASN   B CB  1 
ATOM   5499 C  CG  . ASN   B 1 142 ? -67.811 12.428  55.872  1.00 28.60 ? 165  ASN   B CG  1 
ATOM   5500 O  OD1 . ASN   B 1 142 ? -66.818 11.992  56.460  1.00 32.71 ? 165  ASN   B OD1 1 
ATOM   5501 N  ND2 . ASN   B 1 142 ? -67.752 13.527  55.139  1.00 25.22 ? 165  ASN   B ND2 1 
ATOM   5502 N  N   . GLY   B 1 143 ? -70.238 8.095   56.168  1.00 37.87 ? 166  GLY   B N   1 
ATOM   5503 C  CA  . GLY   B 1 143 ? -71.362 7.231   56.494  1.00 35.83 ? 166  GLY   B CA  1 
ATOM   5504 C  C   . GLY   B 1 143 ? -72.450 7.208   55.422  1.00 36.21 ? 166  GLY   B C   1 
ATOM   5505 O  O   . GLY   B 1 143 ? -73.398 6.435   55.557  1.00 33.68 ? 166  GLY   B O   1 
ATOM   5506 N  N   . ARG   B 1 144 ? -72.293 8.007   54.350  1.00 39.35 ? 167  ARG   B N   1 
ATOM   5507 C  CA  . ARG   B 1 144 ? -73.286 8.118   53.286  1.00 37.33 ? 167  ARG   B CA  1 
ATOM   5508 C  C   . ARG   B 1 144 ? -72.769 7.529   51.968  1.00 38.34 ? 167  ARG   B C   1 
ATOM   5509 O  O   . ARG   B 1 144 ? -71.626 7.767   51.586  1.00 37.15 ? 167  ARG   B O   1 
ATOM   5510 C  CB  . ARG   B 1 144 ? -73.561 9.602   53.050  1.00 39.08 ? 167  ARG   B CB  1 
ATOM   5511 C  CG  . ARG   B 1 144 ? -75.060 9.846   53.041  1.00 46.75 ? 167  ARG   B CG  1 
ATOM   5512 C  CD  . ARG   B 1 144 ? -75.404 11.236  53.523  1.00 47.73 ? 167  ARG   B CD  1 
ATOM   5513 N  NE  . ARG   B 1 144 ? -76.698 11.240  54.223  1.00 50.73 ? 167  ARG   B NE  1 
ATOM   5514 C  CZ  . ARG   B 1 144 ? -76.887 11.396  55.539  1.00 50.35 ? 167  ARG   B CZ  1 
ATOM   5515 N  NH1 . ARG   B 1 144 ? -75.862 11.371  56.390  1.00 55.14 ? 167  ARG   B NH1 1 
ATOM   5516 N  NH2 . ARG   B 1 144 ? -78.118 11.533  56.011  1.00 46.26 ? 167  ARG   B NH2 1 
ATOM   5517 N  N   . GLN   B 1 145 ? -73.633 6.807   51.240  1.00 36.45 ? 168  GLN   B N   1 
ATOM   5518 C  CA  . GLN   B 1 145 ? -73.226 6.092   50.034  1.00 32.59 ? 168  GLN   B CA  1 
ATOM   5519 C  C   . GLN   B 1 145 ? -73.002 7.069   48.877  1.00 29.65 ? 168  GLN   B C   1 
ATOM   5520 O  O   . GLN   B 1 145 ? -73.859 7.880   48.535  1.00 29.09 ? 168  GLN   B O   1 
ATOM   5521 C  CB  . GLN   B 1 145 ? -74.232 4.991   49.694  1.00 32.91 ? 168  GLN   B CB  1 
ATOM   5522 C  CG  . GLN   B 1 145 ? -73.972 4.320   48.350  1.00 34.42 ? 168  GLN   B CG  1 
ATOM   5523 C  CD  . GLN   B 1 145 ? -74.909 3.166   48.057  1.00 36.61 ? 168  GLN   B CD  1 
ATOM   5524 O  OE1 . GLN   B 1 145 ? -75.448 2.515   48.961  1.00 39.63 ? 168  GLN   B OE1 1 
ATOM   5525 N  NE2 . GLN   B 1 145 ? -75.056 2.867   46.776  1.00 33.06 ? 168  GLN   B NE2 1 
ATOM   5526 N  N   . ALA   B 1 146 ? -71.843 6.960   48.219  1.00 29.51 ? 169  ALA   B N   1 
ATOM   5527 C  CA  . ALA   B 1 146 ? -71.447 7.979   47.256  1.00 28.64 ? 169  ALA   B CA  1 
ATOM   5528 C  C   . ALA   B 1 146 ? -72.177 7.836   45.924  1.00 27.27 ? 169  ALA   B C   1 
ATOM   5529 O  O   . ALA   B 1 146 ? -72.235 8.790   45.173  1.00 29.14 ? 169  ALA   B O   1 
ATOM   5530 C  CB  . ALA   B 1 146 ? -69.944 7.945   47.051  1.00 31.81 ? 169  ALA   B CB  1 
ATOM   5531 N  N   . GLY   B 1 147 ? -72.721 6.657   45.610  1.00 27.97 ? 170  GLY   B N   1 
ATOM   5532 C  CA  . GLY   B 1 147 ? -73.415 6.467   44.343  1.00 25.29 ? 170  GLY   B CA  1 
ATOM   5533 C  C   . GLY   B 1 147 ? -73.643 4.987   44.081  1.00 22.67 ? 170  GLY   B C   1 
ATOM   5534 O  O   . GLY   B 1 147 ? -73.417 4.166   44.965  1.00 27.02 ? 170  GLY   B O   1 
ATOM   5535 N  N   . ALA   B 1 148 ? -74.063 4.669   42.855  1.00 26.80 ? 171  ALA   B N   1 
ATOM   5536 C  CA  . ALA   B 1 148 ? -74.304 3.294   42.439  1.00 26.04 ? 171  ALA   B CA  1 
ATOM   5537 C  C   . ALA   B 1 148 ? -73.099 2.423   42.781  1.00 25.43 ? 171  ALA   B C   1 
ATOM   5538 O  O   . ALA   B 1 148 ? -71.956 2.855   42.590  1.00 26.31 ? 171  ALA   B O   1 
ATOM   5539 C  CB  . ALA   B 1 148 ? -74.608 3.271   40.951  1.00 26.07 ? 171  ALA   B CB  1 
ATOM   5540 N  N   . VAL   B 1 149 ? -73.366 1.221   43.309  1.00 23.95 ? 172  VAL   B N   1 
ATOM   5541 C  CA  . VAL   B 1 149 ? -72.376 0.167   43.451  1.00 24.81 ? 172  VAL   B CA  1 
ATOM   5542 C  C   . VAL   B 1 149 ? -71.708 -0.084  42.093  1.00 23.62 ? 172  VAL   B C   1 
ATOM   5543 O  O   . VAL   B 1 149 ? -72.384 -0.078  41.062  1.00 22.13 ? 172  VAL   B O   1 
ATOM   5544 C  CB  . VAL   B 1 149 ? -73.017 -1.105  44.043  1.00 24.31 ? 172  VAL   B CB  1 
ATOM   5545 C  CG1 . VAL   B 1 149 ? -72.104 -2.311  43.960  1.00 23.43 ? 172  VAL   B CG1 1 
ATOM   5546 C  CG2 . VAL   B 1 149 ? -73.411 -0.927  45.510  1.00 24.63 ? 172  VAL   B CG2 1 
ATOM   5547 N  N   . HIS   B 1 150 ? -70.367 -0.241  42.110  1.00 20.78 ? 173  HIS   B N   1 
ATOM   5548 C  CA  . HIS   B 1 150 ? -69.596 -0.459  40.883  1.00 18.93 ? 173  HIS   B CA  1 
ATOM   5549 C  C   . HIS   B 1 150 ? -69.230 -1.933  40.794  1.00 16.76 ? 173  HIS   B C   1 
ATOM   5550 O  O   . HIS   B 1 150 ? -68.600 -2.470  41.691  1.00 15.46 ? 173  HIS   B O   1 
ATOM   5551 C  CB  . HIS   B 1 150 ? -68.263 0.305   40.861  1.00 17.69 ? 173  HIS   B CB  1 
ATOM   5552 C  CG  . HIS   B 1 150 ? -67.470 0.017   39.618  1.00 16.84 ? 173  HIS   B CG  1 
ATOM   5553 N  ND1 . HIS   B 1 150 ? -66.561 -1.005  39.522  1.00 18.00 ? 173  HIS   B ND1 1 
ATOM   5554 C  CD2 . HIS   B 1 150 ? -67.558 0.555   38.408  1.00 16.68 ? 173  HIS   B CD2 1 
ATOM   5555 C  CE1 . HIS   B 1 150 ? -66.108 -1.053  38.263  1.00 17.43 ? 173  HIS   B CE1 1 
ATOM   5556 N  NE2 . HIS   B 1 150 ? -66.673 -0.094  37.575  1.00 16.42 ? 173  HIS   B NE2 1 
ATOM   5557 N  N   . SER   B 1 151 ? -69.608 -2.555  39.672  1.00 16.62 ? 174  SER   B N   1 
ATOM   5558 C  CA  . SER   B 1 151 ? -69.285 -3.942  39.419  1.00 15.50 ? 174  SER   B CA  1 
ATOM   5559 C  C   . SER   B 1 151 ? -68.342 -4.023  38.227  1.00 14.01 ? 174  SER   B C   1 
ATOM   5560 O  O   . SER   B 1 151 ? -68.687 -3.532  37.164  1.00 11.68 ? 174  SER   B O   1 
ATOM   5561 C  CB  . SER   B 1 151 ? -70.529 -4.740  39.172  1.00 17.35 ? 174  SER   B CB  1 
ATOM   5562 O  OG  . SER   B 1 151 ? -71.240 -4.843  40.399  1.00 20.06 ? 174  SER   B OG  1 
ATOM   5563 N  N   . GLY   B 1 152 ? -67.171 -4.627  38.455  1.00 15.08 ? 175  GLY   B N   1 
ATOM   5564 C  CA  . GLY   B 1 152 ? -66.150 -4.805  37.423  1.00 14.77 ? 175  GLY   B CA  1 
ATOM   5565 C  C   . GLY   B 1 152 ? -64.758 -4.522  37.997  1.00 14.99 ? 175  GLY   B C   1 
ATOM   5566 O  O   . GLY   B 1 152 ? -64.540 -3.467  38.602  1.00 14.31 ? 175  GLY   B O   1 
ATOM   5567 N  N   . GLY   B 1 153 ? -63.821 -5.472  37.845  1.00 14.84 ? 176  GLY   B N   1 
ATOM   5568 C  CA  . GLY   B 1 153 ? -62.506 -5.321  38.469  1.00 14.13 ? 176  GLY   B CA  1 
ATOM   5569 C  C   . GLY   B 1 153 ? -61.412 -4.659  37.624  1.00 14.71 ? 176  GLY   B C   1 
ATOM   5570 O  O   . GLY   B 1 153 ? -60.273 -4.610  38.080  1.00 16.32 ? 176  GLY   B O   1 
ATOM   5571 N  N   . TYR   B 1 154 ? -61.710 -4.190  36.403  1.00 14.39 ? 177  TYR   B N   1 
ATOM   5572 C  CA  . TYR   B 1 154 ? -60.700 -3.780  35.439  1.00 14.47 ? 177  TYR   B CA  1 
ATOM   5573 C  C   . TYR   B 1 154 ? -60.949 -2.397  34.849  1.00 13.74 ? 177  TYR   B C   1 
ATOM   5574 O  O   . TYR   B 1 154 ? -60.125 -1.920  34.070  1.00 15.32 ? 177  TYR   B O   1 
ATOM   5575 C  CB  . TYR   B 1 154 ? -60.585 -4.774  34.270  1.00 14.06 ? 177  TYR   B CB  1 
ATOM   5576 C  CG  . TYR   B 1 154 ? -60.170 -6.178  34.680  1.00 13.23 ? 177  TYR   B CG  1 
ATOM   5577 C  CD1 . TYR   B 1 154 ? -58.840 -6.500  34.953  1.00 11.87 ? 177  TYR   B CD1 1 
ATOM   5578 C  CD2 . TYR   B 1 154 ? -61.107 -7.179  34.869  1.00 12.90 ? 177  TYR   B CD2 1 
ATOM   5579 C  CE1 . TYR   B 1 154 ? -58.472 -7.773  35.356  1.00 11.95 ? 177  TYR   B CE1 1 
ATOM   5580 C  CE2 . TYR   B 1 154 ? -60.745 -8.449  35.277  1.00 13.17 ? 177  TYR   B CE2 1 
ATOM   5581 C  CZ  . TYR   B 1 154 ? -59.423 -8.751  35.551  1.00 11.72 ? 177  TYR   B CZ  1 
ATOM   5582 O  OH  . TYR   B 1 154 ? -59.096 -10.032 35.888  1.00 12.01 ? 177  TYR   B OH  1 
ATOM   5583 N  N   . ASP   B 1 155 ? -62.086 -1.765  35.157  1.00 14.05 ? 178  ASP   B N   1 
ATOM   5584 C  CA  . ASP   B 1 155 ? -62.429 -0.476  34.598  1.00 14.26 ? 178  ASP   B CA  1 
ATOM   5585 C  C   . ASP   B 1 155 ? -62.407 0.575   35.717  1.00 15.52 ? 178  ASP   B C   1 
ATOM   5586 O  O   . ASP   B 1 155 ? -62.843 0.288   36.817  1.00 15.83 ? 178  ASP   B O   1 
ATOM   5587 C  CB  . ASP   B 1 155 ? -63.804 -0.467  33.945  1.00 15.46 ? 178  ASP   B CB  1 
ATOM   5588 C  CG  . ASP   B 1 155 ? -64.966 -0.827  34.864  1.00 16.24 ? 178  ASP   B CG  1 
ATOM   5589 O  OD1 . ASP   B 1 155 ? -64.983 -1.952  35.409  1.00 16.53 ? 178  ASP   B OD1 1 
ATOM   5590 O  OD2 . ASP   B 1 155 ? -65.841 0.037   34.993  1.00 17.97 ? 178  ASP   B OD2 1 
ATOM   5591 N  N   . ALA   B 1 156 ? -61.897 1.758   35.389  1.00 15.57 ? 179  ALA   B N   1 
ATOM   5592 C  CA  . ALA   B 1 156 ? -61.896 2.890   36.304  1.00 16.25 ? 179  ALA   B CA  1 
ATOM   5593 C  C   . ALA   B 1 156 ? -63.320 3.390   36.496  1.00 16.29 ? 179  ALA   B C   1 
ATOM   5594 O  O   . ALA   B 1 156 ? -64.149 3.273   35.596  1.00 16.07 ? 179  ALA   B O   1 
ATOM   5595 C  CB  . ALA   B 1 156 ? -61.009 3.997   35.769  1.00 15.96 ? 179  ALA   B CB  1 
ATOM   5596 N  N   . PHE   B 1 157 ? -63.563 3.975   37.673  1.00 16.74 ? 180  PHE   B N   1 
ATOM   5597 C  CA  . PHE   B 1 157 ? -64.852 4.589   37.948  1.00 17.96 ? 180  PHE   B CA  1 
ATOM   5598 C  C   . PHE   B 1 157 ? -64.649 5.745   38.924  1.00 18.95 ? 180  PHE   B C   1 
ATOM   5599 O  O   . PHE   B 1 157 ? -63.624 5.841   39.573  1.00 19.43 ? 180  PHE   B O   1 
ATOM   5600 C  CB  . PHE   B 1 157 ? -65.807 3.527   38.509  1.00 15.83 ? 180  PHE   B CB  1 
ATOM   5601 C  CG  . PHE   B 1 157 ? -65.307 2.746   39.715  1.00 16.78 ? 180  PHE   B CG  1 
ATOM   5602 C  CD1 . PHE   B 1 157 ? -64.463 1.663   39.572  1.00 15.78 ? 180  PHE   B CD1 1 
ATOM   5603 C  CD2 . PHE   B 1 157 ? -65.720 3.064   41.004  1.00 16.81 ? 180  PHE   B CD2 1 
ATOM   5604 C  CE1 . PHE   B 1 157 ? -64.023 0.933   40.666  1.00 16.51 ? 180  PHE   B CE1 1 
ATOM   5605 C  CE2 . PHE   B 1 157 ? -65.279 2.338   42.091  1.00 15.85 ? 180  PHE   B CE2 1 
ATOM   5606 C  CZ  . PHE   B 1 157 ? -64.441 1.271   41.934  1.00 16.86 ? 180  PHE   B CZ  1 
ATOM   5607 N  N   . SER   B 1 158 ? -65.693 6.550   39.063  1.00 20.40 ? 181  SER   B N   1 
ATOM   5608 C  CA  . SER   B 1 158 ? -65.614 7.833   39.742  1.00 23.59 ? 181  SER   B CA  1 
ATOM   5609 C  C   . SER   B 1 158 ? -66.939 8.121   40.445  1.00 24.55 ? 181  SER   B C   1 
ATOM   5610 O  O   . SER   B 1 158 ? -68.011 7.795   39.928  1.00 24.29 ? 181  SER   B O   1 
ATOM   5611 C  CB  . SER   B 1 158 ? -65.348 8.907   38.751  1.00 23.97 ? 181  SER   B CB  1 
ATOM   5612 O  OG  . SER   B 1 158 ? -64.717 9.996   39.393  1.00 32.79 ? 181  SER   B OG  1 
ATOM   5613 N  N   . TYR   B 1 159 ? -66.864 8.810   41.577  1.00 24.02 ? 182  TYR   B N   1 
ATOM   5614 C  CA  . TYR   B 1 159 ? -68.052 9.411   42.156  1.00 24.35 ? 182  TYR   B CA  1 
ATOM   5615 C  C   . TYR   B 1 159 ? -67.806 10.878  42.469  1.00 25.93 ? 182  TYR   B C   1 
ATOM   5616 O  O   . TYR   B 1 159 ? -66.766 11.181  43.071  1.00 24.38 ? 182  TYR   B O   1 
ATOM   5617 C  CB  . TYR   B 1 159 ? -68.332 8.676   43.452  1.00 23.82 ? 182  TYR   B CB  1 
ATOM   5618 C  CG  . TYR   B 1 159 ? -68.567 7.180   43.348  1.00 23.46 ? 182  TYR   B CG  1 
ATOM   5619 C  CD1 . TYR   B 1 159 ? -69.815 6.699   42.984  1.00 25.34 ? 182  TYR   B CD1 1 
ATOM   5620 C  CD2 . TYR   B 1 159 ? -67.584 6.263   43.683  1.00 25.74 ? 182  TYR   B CD2 1 
ATOM   5621 C  CE1 . TYR   B 1 159 ? -70.069 5.337   42.941  1.00 24.99 ? 182  TYR   B CE1 1 
ATOM   5622 C  CE2 . TYR   B 1 159 ? -67.824 4.899   43.648  1.00 24.81 ? 182  TYR   B CE2 1 
ATOM   5623 C  CZ  . TYR   B 1 159 ? -69.074 4.438   43.264  1.00 25.51 ? 182  TYR   B CZ  1 
ATOM   5624 O  OH  . TYR   B 1 159 ? -69.365 3.110   43.271  1.00 22.92 ? 182  TYR   B OH  1 
ATOM   5625 N  N   . ASP   B 1 160 ? -68.769 11.738  42.063  1.00 25.98 ? 183  ASP   B N   1 
ATOM   5626 C  CA  . ASP   B 1 160 ? -68.791 13.141  42.449  1.00 26.88 ? 183  ASP   B CA  1 
ATOM   5627 C  C   . ASP   B 1 160 ? -69.325 13.237  43.867  1.00 28.77 ? 183  ASP   B C   1 
ATOM   5628 O  O   . ASP   B 1 160 ? -70.526 13.104  44.067  1.00 28.28 ? 183  ASP   B O   1 
ATOM   5629 C  CB  . ASP   B 1 160 ? -69.657 14.009  41.558  1.00 26.91 ? 183  ASP   B CB  1 
ATOM   5630 C  CG  . ASP   B 1 160 ? -69.773 15.463  42.001  1.00 26.01 ? 183  ASP   B CG  1 
ATOM   5631 O  OD1 . ASP   B 1 160 ? -69.507 15.756  43.197  1.00 27.02 ? 183  ASP   B OD1 1 
ATOM   5632 O  OD2 . ASP   B 1 160 ? -70.045 16.290  41.135  1.00 28.42 ? 183  ASP   B OD2 1 
ATOM   5633 N  N   . VAL   B 1 161 ? -68.420 13.496  44.812  1.00 29.80 ? 184  VAL   B N   1 
ATOM   5634 C  CA  . VAL   B 1 161 ? -68.683 13.345  46.231  1.00 30.06 ? 184  VAL   B CA  1 
ATOM   5635 C  C   . VAL   B 1 161 ? -68.801 14.727  46.882  1.00 30.91 ? 184  VAL   B C   1 
ATOM   5636 O  O   . VAL   B 1 161 ? -68.750 14.815  48.101  1.00 27.66 ? 184  VAL   B O   1 
ATOM   5637 C  CB  . VAL   B 1 161 ? -67.601 12.515  46.947  1.00 31.25 ? 184  VAL   B CB  1 
ATOM   5638 C  CG1 . VAL   B 1 161 ? -67.495 11.101  46.384  1.00 31.29 ? 184  VAL   B CG1 1 
ATOM   5639 C  CG2 . VAL   B 1 161 ? -66.232 13.193  46.937  1.00 32.11 ? 184  VAL   B CG2 1 
ATOM   5640 N  N   . THR   B 1 162 ? -68.978 15.782  46.082  1.00 31.81 ? 185  THR   B N   1 
ATOM   5641 C  CA  . THR   B 1 162 ? -68.935 17.141  46.598  1.00 35.49 ? 185  THR   B CA  1 
ATOM   5642 C  C   . THR   B 1 162 ? -69.846 17.265  47.827  1.00 38.00 ? 185  THR   B C   1 
ATOM   5643 O  O   . THR   B 1 162 ? -69.413 17.677  48.902  1.00 36.88 ? 185  THR   B O   1 
ATOM   5644 C  CB  . THR   B 1 162 ? -69.354 18.124  45.509  1.00 34.40 ? 185  THR   B CB  1 
ATOM   5645 O  OG1 . THR   B 1 162 ? -68.646 17.812  44.311  1.00 32.72 ? 185  THR   B OG1 1 
ATOM   5646 C  CG2 . THR   B 1 162 ? -69.061 19.554  45.920  1.00 34.44 ? 185  THR   B CG2 1 
ATOM   5647 N  N   . ASP   B 1 163 ? -71.096 16.823  47.664  1.00 38.62 ? 186  ASP   B N   1 
ATOM   5648 C  CA  . ASP   B 1 163 ? -72.182 17.120  48.586  1.00 37.68 ? 186  ASP   B CA  1 
ATOM   5649 C  C   . ASP   B 1 163 ? -72.184 16.240  49.824  1.00 39.74 ? 186  ASP   B C   1 
ATOM   5650 O  O   . ASP   B 1 163 ? -73.121 16.337  50.614  1.00 45.43 ? 186  ASP   B O   1 
ATOM   5651 C  CB  . ASP   B 1 163 ? -73.510 16.943  47.882  1.00 36.97 ? 186  ASP   B CB  1 
ATOM   5652 C  CG  . ASP   B 1 163 ? -73.644 17.917  46.738  1.00 34.17 ? 186  ASP   B CG  1 
ATOM   5653 O  OD1 . ASP   B 1 163 ? -72.922 18.907  46.791  1.00 42.63 ? 186  ASP   B OD1 1 
ATOM   5654 O  OD2 . ASP   B 1 163 ? -74.381 17.636  45.795  1.00 36.18 ? 186  ASP   B OD2 1 
ATOM   5655 N  N   . LEU   B 1 164 ? -71.170 15.384  49.973  1.00 35.64 ? 187  LEU   B N   1 
ATOM   5656 C  CA  . LEU   B 1 164 ? -71.015 14.541  51.147  1.00 36.39 ? 187  LEU   B CA  1 
ATOM   5657 C  C   . LEU   B 1 164 ? -69.890 15.077  52.025  1.00 35.52 ? 187  LEU   B C   1 
ATOM   5658 O  O   . LEU   B 1 164 ? -69.629 14.533  53.103  1.00 36.60 ? 187  LEU   B O   1 
ATOM   5659 C  CB  . LEU   B 1 164 ? -70.718 13.105  50.703  1.00 38.80 ? 187  LEU   B CB  1 
ATOM   5660 C  CG  . LEU   B 1 164 ? -71.898 12.316  50.130  1.00 43.84 ? 187  LEU   B CG  1 
ATOM   5661 C  CD1 . LEU   B 1 164 ? -72.626 13.082  49.025  1.00 44.24 ? 187  LEU   B CD1 1 
ATOM   5662 C  CD2 . LEU   B 1 164 ? -71.405 10.970  49.623  1.00 44.67 ? 187  LEU   B CD2 1 
ATOM   5663 N  N   . LEU   B 1 165 ? -69.187 16.105  51.522  1.00 36.35 ? 188  LEU   B N   1 
ATOM   5664 C  CA  . LEU   B 1 165 ? -67.942 16.549  52.133  1.00 38.61 ? 188  LEU   B CA  1 
ATOM   5665 C  C   . LEU   B 1 165 ? -68.270 17.541  53.246  1.00 41.65 ? 188  LEU   B C   1 
ATOM   5666 O  O   . LEU   B 1 165 ? -69.183 18.340  53.090  1.00 41.79 ? 188  LEU   B O   1 
ATOM   5667 C  CB  . LEU   B 1 165 ? -67.024 17.199  51.092  1.00 39.61 ? 188  LEU   B CB  1 
ATOM   5668 C  CG  . LEU   B 1 165 ? -66.434 16.285  50.010  1.00 35.90 ? 188  LEU   B CG  1 
ATOM   5669 C  CD1 . LEU   B 1 165 ? -65.571 17.123  49.085  1.00 38.69 ? 188  LEU   B CD1 1 
ATOM   5670 C  CD2 . LEU   B 1 165 ? -65.640 15.122  50.589  1.00 34.37 ? 188  LEU   B CD2 1 
ATOM   5671 N  N   . THR   B 1 166 ? -67.498 17.472  54.339  1.00 43.99 ? 189  THR   B N   1 
ATOM   5672 C  CA  . THR   B 1 166 ? -67.426 18.514  55.355  1.00 43.07 ? 189  THR   B CA  1 
ATOM   5673 C  C   . THR   B 1 166 ? -66.113 19.269  55.191  1.00 45.36 ? 189  THR   B C   1 
ATOM   5674 O  O   . THR   B 1 166 ? -65.232 18.814  54.464  1.00 46.57 ? 189  THR   B O   1 
ATOM   5675 C  CB  . THR   B 1 166 ? -67.415 17.891  56.745  1.00 39.24 ? 189  THR   B CB  1 
ATOM   5676 O  OG1 . THR   B 1 166 ? -66.065 17.443  56.842  1.00 46.41 ? 189  THR   B OG1 1 
ATOM   5677 C  CG2 . THR   B 1 166 ? -68.375 16.731  56.929  1.00 41.18 ? 189  THR   B CG2 1 
ATOM   5678 N  N   . ALA   B 1 167 ? -65.927 20.311  56.012  1.00 48.61 ? 190  ALA   B N   1 
ATOM   5679 C  CA  . ALA   B 1 167 ? -64.715 21.111  55.978  1.00 45.96 ? 190  ALA   B CA  1 
ATOM   5680 C  C   . ALA   B 1 167 ? -63.599 20.525  56.846  1.00 46.43 ? 190  ALA   B C   1 
ATOM   5681 O  O   . ALA   B 1 167 ? -62.497 21.061  56.811  1.00 54.86 ? 190  ALA   B O   1 
ATOM   5682 C  CB  . ALA   B 1 167 ? -65.025 22.529  56.397  1.00 46.95 ? 190  ALA   B CB  1 
ATOM   5683 N  N   . GLY   B 1 168 ? -63.842 19.443  57.603  1.00 42.12 ? 191  GLY   B N   1 
ATOM   5684 C  CA  . GLY   B 1 168 ? -62.845 18.926  58.531  1.00 40.68 ? 191  GLY   B CA  1 
ATOM   5685 C  C   . GLY   B 1 168 ? -62.155 17.665  58.014  1.00 40.93 ? 191  GLY   B C   1 
ATOM   5686 O  O   . GLY   B 1 168 ? -61.918 17.521  56.819  1.00 42.20 ? 191  GLY   B O   1 
ATOM   5687 N  N   . THR   B 1 169 ? -61.815 16.740  58.916  1.00 41.26 ? 192  THR   B N   1 
ATOM   5688 C  CA  . THR   B 1 169 ? -61.415 15.412  58.474  1.00 46.63 ? 192  THR   B CA  1 
ATOM   5689 C  C   . THR   B 1 169 ? -62.655 14.746  57.864  1.00 43.91 ? 192  THR   B C   1 
ATOM   5690 O  O   . THR   B 1 169 ? -63.765 14.973  58.337  1.00 46.72 ? 192  THR   B O   1 
ATOM   5691 C  CB  . THR   B 1 169 ? -60.807 14.595  59.618  1.00 49.52 ? 192  THR   B CB  1 
ATOM   5692 O  OG1 . THR   B 1 169 ? -61.832 14.495  60.597  1.00 57.84 ? 192  THR   B OG1 1 
ATOM   5693 C  CG2 . THR   B 1 169 ? -59.581 15.236  60.246  1.00 48.25 ? 192  THR   B CG2 1 
ATOM   5694 N  N   . ASN   B 1 170 ? -62.484 13.997  56.766  1.00 39.75 ? 193  ASN   B N   1 
ATOM   5695 C  CA  . ASN   B 1 170 ? -63.575 13.231  56.178  1.00 33.22 ? 193  ASN   B CA  1 
ATOM   5696 C  C   . ASN   B 1 170 ? -63.273 11.749  56.340  1.00 32.21 ? 193  ASN   B C   1 
ATOM   5697 O  O   . ASN   B 1 170 ? -62.130 11.376  56.591  1.00 32.76 ? 193  ASN   B O   1 
ATOM   5698 C  CB  . ASN   B 1 170 ? -63.851 13.584  54.725  1.00 33.68 ? 193  ASN   B CB  1 
ATOM   5699 C  CG  . ASN   B 1 170 ? -64.389 14.982  54.574  1.00 32.10 ? 193  ASN   B CG  1 
ATOM   5700 O  OD1 . ASN   B 1 170 ? -65.589 15.189  54.373  1.00 35.38 ? 193  ASN   B OD1 1 
ATOM   5701 N  ND2 . ASN   B 1 170 ? -63.512 15.961  54.681  1.00 38.06 ? 193  ASN   B ND2 1 
ATOM   5702 N  N   . THR   B 1 171 ? -64.325 10.919  56.237  1.00 29.28 ? 194  THR   B N   1 
ATOM   5703 C  CA  . THR   B 1 171 ? -64.187 9.489   56.462  1.00 33.77 ? 194  THR   B CA  1 
ATOM   5704 C  C   . THR   B 1 171 ? -64.541 8.792   55.152  1.00 29.48 ? 194  THR   B C   1 
ATOM   5705 O  O   . THR   B 1 171 ? -65.503 9.173   54.491  1.00 29.05 ? 194  THR   B O   1 
ATOM   5706 C  CB  . THR   B 1 171 ? -65.048 9.016   57.635  1.00 36.47 ? 194  THR   B CB  1 
ATOM   5707 O  OG1 . THR   B 1 171 ? -64.432 9.549   58.803  1.00 39.52 ? 194  THR   B OG1 1 
ATOM   5708 C  CG2 . THR   B 1 171 ? -65.043 7.506   57.820  1.00 38.49 ? 194  THR   B CG2 1 
ATOM   5709 N  N   . LEU   B 1 172 ? -63.723 7.794   54.789  1.00 32.71 ? 195  LEU   B N   1 
ATOM   5710 C  CA  . LEU   B 1 172 ? -63.933 7.035   53.563  1.00 28.16 ? 195  LEU   B CA  1 
ATOM   5711 C  C   . LEU   B 1 172 ? -63.968 5.564   53.933  1.00 24.21 ? 195  LEU   B C   1 
ATOM   5712 O  O   . LEU   B 1 172 ? -63.024 5.041   54.526  1.00 23.60 ? 195  LEU   B O   1 
ATOM   5713 C  CB  . LEU   B 1 172 ? -62.837 7.348   52.547  1.00 35.08 ? 195  LEU   B CB  1 
ATOM   5714 C  CG  . LEU   B 1 172 ? -62.973 6.719   51.152  1.00 36.20 ? 195  LEU   B CG  1 
ATOM   5715 C  CD1 . LEU   B 1 172 ? -64.332 6.923   50.494  1.00 35.56 ? 195  LEU   B CD1 1 
ATOM   5716 C  CD2 . LEU   B 1 172 ? -61.889 7.296   50.257  1.00 34.80 ? 195  LEU   B CD2 1 
ATOM   5717 N  N   . VAL   B 1 173 ? -65.100 4.921   53.612  1.00 24.03 ? 196  VAL   B N   1 
ATOM   5718 C  CA  . VAL   B 1 173 ? -65.250 3.495   53.849  1.00 25.51 ? 196  VAL   B CA  1 
ATOM   5719 C  C   . VAL   B 1 173 ? -65.484 2.876   52.483  1.00 22.10 ? 196  VAL   B C   1 
ATOM   5720 O  O   . VAL   B 1 173 ? -66.213 3.459   51.694  1.00 23.14 ? 196  VAL   B O   1 
ATOM   5721 C  CB  . VAL   B 1 173 ? -66.383 3.153   54.840  1.00 26.09 ? 196  VAL   B CB  1 
ATOM   5722 C  CG1 . VAL   B 1 173 ? -66.641 1.655   54.913  1.00 25.50 ? 196  VAL   B CG1 1 
ATOM   5723 C  CG2 . VAL   B 1 173 ? -66.048 3.690   56.234  1.00 28.19 ? 196  VAL   B CG2 1 
ATOM   5724 N  N   . VAL   B 1 174 ? -64.799 1.764   52.221  1.00 25.16 ? 197  VAL   B N   1 
ATOM   5725 C  CA  . VAL   B 1 174 ? -65.018 1.064   50.970  1.00 22.75 ? 197  VAL   B CA  1 
ATOM   5726 C  C   . VAL   B 1 174 ? -65.151 -0.401  51.328  1.00 19.39 ? 197  VAL   B C   1 
ATOM   5727 O  O   . VAL   B 1 174 ? -64.328 -0.941  52.064  1.00 24.93 ? 197  VAL   B O   1 
ATOM   5728 C  CB  . VAL   B 1 174 ? -63.889 1.348   49.955  1.00 24.16 ? 197  VAL   B CB  1 
ATOM   5729 C  CG1 . VAL   B 1 174 ? -64.126 0.621   48.626  1.00 22.51 ? 197  VAL   B CG1 1 
ATOM   5730 C  CG2 . VAL   B 1 174 ? -63.727 2.847   49.695  1.00 22.17 ? 197  VAL   B CG2 1 
ATOM   5731 N  N   . SER   B 1 175 ? -66.274 -0.989  50.911  1.00 19.71 ? 198  SER   B N   1 
ATOM   5732 C  CA  . SER   B 1 175 ? -66.414 -2.432  50.911  1.00 20.76 ? 198  SER   B CA  1 
ATOM   5733 C  C   . SER   B 1 175 ? -66.172 -2.941  49.494  1.00 17.90 ? 198  SER   B C   1 
ATOM   5734 O  O   . SER   B 1 175 ? -66.628 -2.326  48.517  1.00 20.04 ? 198  SER   B O   1 
ATOM   5735 C  CB  . SER   B 1 175 ? -67.775 -2.897  51.395  1.00 21.96 ? 198  SER   B CB  1 
ATOM   5736 O  OG  . SER   B 1 175 ? -68.791 -2.535  50.480  1.00 22.30 ? 198  SER   B OG  1 
ATOM   5737 N  N   . VAL   B 1 176 ? -65.491 -4.078  49.438  1.00 22.82 ? 199  VAL   B N   1 
ATOM   5738 C  CA  . VAL   B 1 176 ? -65.235 -4.763  48.185  1.00 18.72 ? 199  VAL   B CA  1 
ATOM   5739 C  C   . VAL   B 1 176 ? -65.486 -6.236  48.374  1.00 21.01 ? 199  VAL   B C   1 
ATOM   5740 O  O   . VAL   B 1 176 ? -64.842 -6.896  49.201  1.00 23.07 ? 199  VAL   B O   1 
ATOM   5741 C  CB  . VAL   B 1 176 ? -63.802 -4.507  47.684  1.00 19.50 ? 199  VAL   B CB  1 
ATOM   5742 C  CG1 . VAL   B 1 176 ? -63.635 -5.085  46.284  1.00 18.73 ? 199  VAL   B CG1 1 
ATOM   5743 C  CG2 . VAL   B 1 176 ? -63.471 -3.027  47.690  1.00 20.18 ? 199  VAL   B CG2 1 
ATOM   5744 N  N   . TRP   B 1 177 ? -66.425 -6.737  47.553  1.00 19.11 ? 200  TRP   B N   1 
ATOM   5745 C  CA  . TRP   B 1 177 ? -66.717 -8.152  47.473  1.00 18.38 ? 200  TRP   B CA  1 
ATOM   5746 C  C   . TRP   B 1 177 ? -66.124 -8.666  46.162  1.00 15.90 ? 200  TRP   B C   1 
ATOM   5747 O  O   . TRP   B 1 177 ? -66.288 -7.988  45.162  1.00 17.26 ? 200  TRP   B O   1 
ATOM   5748 C  CB  . TRP   B 1 177 ? -68.244 -8.365  47.514  1.00 17.87 ? 200  TRP   B CB  1 
ATOM   5749 C  CG  . TRP   B 1 177 ? -68.658 -9.807  47.411  1.00 18.75 ? 200  TRP   B CG  1 
ATOM   5750 C  CD1 . TRP   B 1 177 ? -68.390 -10.819 48.276  1.00 17.90 ? 200  TRP   B CD1 1 
ATOM   5751 C  CD2 . TRP   B 1 177 ? -69.381 -10.401 46.318  1.00 18.82 ? 200  TRP   B CD2 1 
ATOM   5752 N  NE1 . TRP   B 1 177 ? -68.919 -11.997 47.828  1.00 21.04 ? 200  TRP   B NE1 1 
ATOM   5753 C  CE2 . TRP   B 1 177 ? -69.524 -11.773 46.617  1.00 20.29 ? 200  TRP   B CE2 1 
ATOM   5754 C  CE3 . TRP   B 1 177 ? -69.908 -9.896  45.123  1.00 20.19 ? 200  TRP   B CE3 1 
ATOM   5755 C  CZ2 . TRP   B 1 177 ? -70.179 -12.655 45.760  1.00 21.01 ? 200  TRP   B CZ2 1 
ATOM   5756 C  CZ3 . TRP   B 1 177 ? -70.549 -10.771 44.280  1.00 19.83 ? 200  TRP   B CZ3 1 
ATOM   5757 C  CH2 . TRP   B 1 177 ? -70.673 -12.123 44.589  1.00 19.59 ? 200  TRP   B CH2 1 
ATOM   5758 N  N   . ASP   B 1 178 ? -65.446 -9.807  46.243  1.00 16.88 ? 201  ASP   B N   1 
ATOM   5759 C  CA  . ASP   B 1 178 ? -64.859 -10.494 45.106  1.00 17.43 ? 201  ASP   B CA  1 
ATOM   5760 C  C   . ASP   B 1 178 ? -65.091 -11.995 45.244  1.00 17.94 ? 201  ASP   B C   1 
ATOM   5761 O  O   . ASP   B 1 178 ? -64.449 -12.688 46.057  1.00 19.44 ? 201  ASP   B O   1 
ATOM   5762 C  CB  . ASP   B 1 178 ? -63.385 -10.150 44.966  1.00 17.07 ? 201  ASP   B CB  1 
ATOM   5763 C  CG  . ASP   B 1 178 ? -62.808 -10.518 43.604  1.00 18.03 ? 201  ASP   B CG  1 
ATOM   5764 O  OD1 . ASP   B 1 178 ? -63.376 -11.469 42.987  1.00 15.95 ? 201  ASP   B OD1 1 
ATOM   5765 O  OD2 . ASP   B 1 178 ? -61.824 -9.842  43.167  1.00 17.73 ? 201  ASP   B OD2 1 
ATOM   5766 N  N   . PRO   B 1 179 ? -65.964 -12.588 44.389  1.00 16.94 ? 202  PRO   B N   1 
ATOM   5767 C  CA  . PRO   B 1 179 ? -66.156 -14.040 44.376  1.00 16.44 ? 202  PRO   B CA  1 
ATOM   5768 C  C   . PRO   B 1 179 ? -65.141 -14.837 43.568  1.00 16.02 ? 202  PRO   B C   1 
ATOM   5769 O  O   . PRO   B 1 179 ? -65.173 -16.072 43.530  1.00 16.19 ? 202  PRO   B O   1 
ATOM   5770 C  CB  . PRO   B 1 179 ? -67.556 -14.125 43.746  1.00 16.85 ? 202  PRO   B CB  1 
ATOM   5771 C  CG  . PRO   B 1 179 ? -67.530 -13.050 42.692  1.00 16.58 ? 202  PRO   B CG  1 
ATOM   5772 C  CD  . PRO   B 1 179 ? -66.765 -11.903 43.364  1.00 17.11 ? 202  PRO   B CD  1 
ATOM   5773 N  N   . THR   B 1 180 ? -64.214 -14.118 42.916  1.00 17.22 ? 203  THR   B N   1 
ATOM   5774 C  CA  . THR   B 1 180 ? -63.274 -14.719 41.979  1.00 16.24 ? 203  THR   B CA  1 
ATOM   5775 C  C   . THR   B 1 180 ? -64.030 -15.701 41.078  1.00 14.53 ? 203  THR   B C   1 
ATOM   5776 O  O   . THR   B 1 180 ? -65.057 -15.303 40.540  1.00 16.53 ? 203  THR   B O   1 
ATOM   5777 C  CB  . THR   B 1 180 ? -62.056 -15.293 42.717  1.00 16.98 ? 203  THR   B CB  1 
ATOM   5778 O  OG1 . THR   B 1 180 ? -61.698 -14.371 43.751  1.00 18.23 ? 203  THR   B OG1 1 
ATOM   5779 C  CG2 . THR   B 1 180 ? -60.878 -15.488 41.780  1.00 16.31 ? 203  THR   B CG2 1 
ATOM   5780 N  N   . GLU   B 1 181 ? -63.542 -16.937 40.886  1.00 14.50 ? 204  GLU   B N   1 
ATOM   5781 C  CA  . GLU   B 1 181 ? -64.057 -17.843 39.862  1.00 15.73 ? 204  GLU   B CA  1 
ATOM   5782 C  C   . GLU   B 1 181 ? -65.386 -18.485 40.276  1.00 16.77 ? 204  GLU   B C   1 
ATOM   5783 O  O   . GLU   B 1 181 ? -66.031 -19.147 39.459  1.00 14.49 ? 204  GLU   B O   1 
ATOM   5784 C  CB  . GLU   B 1 181 ? -63.019 -18.887 39.454  1.00 17.62 ? 204  GLU   B CB  1 
ATOM   5785 C  CG  . GLU   B 1 181 ? -62.864 -20.086 40.387  1.00 18.49 ? 204  GLU   B CG  1 
ATOM   5786 C  CD  . GLU   B 1 181 ? -62.022 -19.874 41.643  1.00 18.88 ? 204  GLU   B CD  1 
ATOM   5787 O  OE1 . GLU   B 1 181 ? -61.639 -18.733 41.978  1.00 17.18 ? 204  GLU   B OE1 1 
ATOM   5788 O  OE2 . GLU   B 1 181 ? -61.728 -20.897 42.268  1.00 22.15 ? 204  GLU   B OE2 1 
ATOM   5789 N  N   . THR   B 1 182 ? -65.835 -18.263 41.530  1.00 18.38 ? 205  THR   B N   1 
ATOM   5790 C  CA  . THR   B 1 182 ? -67.158 -18.746 41.924  1.00 17.37 ? 205  THR   B CA  1 
ATOM   5791 C  C   . THR   B 1 182 ? -68.250 -17.849 41.343  1.00 17.99 ? 205  THR   B C   1 
ATOM   5792 O  O   . THR   B 1 182 ? -69.393 -18.288 41.243  1.00 17.22 ? 205  THR   B O   1 
ATOM   5793 C  CB  . THR   B 1 182 ? -67.314 -18.924 43.447  1.00 17.74 ? 205  THR   B CB  1 
ATOM   5794 O  OG1 . THR   B 1 182 ? -67.463 -17.662 44.083  1.00 16.13 ? 205  THR   B OG1 1 
ATOM   5795 C  CG2 . THR   B 1 182 ? -66.184 -19.745 44.053  1.00 18.88 ? 205  THR   B CG2 1 
ATOM   5796 N  N   . GLY   B 1 183 ? -67.906 -16.618 40.934  1.00 17.53 ? 206  GLY   B N   1 
ATOM   5797 C  CA  . GLY   B 1 183 ? -68.834 -15.711 40.278  1.00 17.62 ? 206  GLY   B CA  1 
ATOM   5798 C  C   . GLY   B 1 183 ? -68.796 -15.915 38.759  1.00 15.46 ? 206  GLY   B C   1 
ATOM   5799 O  O   . GLY   B 1 183 ? -68.059 -16.768 38.262  1.00 15.16 ? 206  GLY   B O   1 
ATOM   5800 N  N   . THR   B 1 184 ? -69.655 -15.177 38.057  1.00 14.77 ? 207  THR   B N   1 
ATOM   5801 C  CA  . THR   B 1 184 ? -69.834 -15.305 36.610  1.00 14.98 ? 207  THR   B CA  1 
ATOM   5802 C  C   . THR   B 1 184 ? -69.183 -14.119 35.886  1.00 14.67 ? 207  THR   B C   1 
ATOM   5803 O  O   . THR   B 1 184 ? -69.458 -13.892 34.706  1.00 13.35 ? 207  THR   B O   1 
ATOM   5804 C  CB  . THR   B 1 184 ? -71.334 -15.364 36.280  1.00 15.82 ? 207  THR   B CB  1 
ATOM   5805 O  OG1 . THR   B 1 184 ? -71.956 -14.177 36.769  1.00 14.49 ? 207  THR   B OG1 1 
ATOM   5806 C  CG2 . THR   B 1 184 ? -72.014 -16.575 36.873  1.00 17.58 ? 207  THR   B CG2 1 
ATOM   5807 N  N   . GLN   B 1 185 ? -68.305 -13.398 36.594  1.00 14.44 ? 208  GLN   B N   1 
ATOM   5808 C  CA  . GLN   B 1 185 ? -67.707 -12.165 36.115  1.00 13.71 ? 208  GLN   B CA  1 
ATOM   5809 C  C   . GLN   B 1 185 ? -66.302 -12.406 35.539  1.00 12.10 ? 208  GLN   B C   1 
ATOM   5810 O  O   . GLN   B 1 185 ? -65.716 -13.447 35.743  1.00 12.04 ? 208  GLN   B O   1 
ATOM   5811 C  CB  . GLN   B 1 185 ? -67.657 -11.109 37.223  1.00 15.95 ? 208  GLN   B CB  1 
ATOM   5812 C  CG  . GLN   B 1 185 ? -66.488 -11.213 38.194  1.00 16.60 ? 208  GLN   B CG  1 
ATOM   5813 C  CD  . GLN   B 1 185 ? -66.439 -12.457 39.046  1.00 18.96 ? 208  GLN   B CD  1 
ATOM   5814 O  OE1 . GLN   B 1 185 ? -67.410 -13.218 39.170  1.00 16.49 ? 208  GLN   B OE1 1 
ATOM   5815 N  NE2 . GLN   B 1 185 ? -65.290 -12.653 39.687  1.00 19.95 ? 208  GLN   B NE2 1 
ATOM   5816 N  N   . ALA   B 1 186 ? -65.797 -11.406 34.814  1.00 11.74 ? 209  ALA   B N   1 
ATOM   5817 C  CA  . ALA   B 1 186 ? -64.452 -11.391 34.266  1.00 11.72 ? 209  ALA   B CA  1 
ATOM   5818 C  C   . ALA   B 1 186 ? -63.442 -11.564 35.404  1.00 11.90 ? 209  ALA   B C   1 
ATOM   5819 O  O   . ALA   B 1 186 ? -63.404 -10.748 36.320  1.00 12.01 ? 209  ALA   B O   1 
ATOM   5820 C  CB  . ALA   B 1 186 ? -64.214 -10.104 33.500  1.00 11.86 ? 209  ALA   B CB  1 
ATOM   5821 N  N   . VAL   B 1 187 ? -62.665 -12.644 35.344  1.00 11.33 ? 210  VAL   B N   1 
ATOM   5822 C  CA  . VAL   B 1 187 ? -61.674 -12.989 36.368  1.00 12.41 ? 210  VAL   B CA  1 
ATOM   5823 C  C   . VAL   B 1 187 ? -60.296 -13.238 35.768  1.00 12.17 ? 210  VAL   B C   1 
ATOM   5824 O  O   . VAL   B 1 187 ? -59.320 -13.243 36.515  1.00 11.58 ? 210  VAL   B O   1 
ATOM   5825 C  CB  . VAL   B 1 187 ? -62.026 -14.269 37.145  1.00 14.79 ? 210  VAL   B CB  1 
ATOM   5826 C  CG1 . VAL   B 1 187 ? -63.103 -14.065 38.181  1.00 17.16 ? 210  VAL   B CG1 1 
ATOM   5827 C  CG2 . VAL   B 1 187 ? -62.372 -15.412 36.210  1.00 13.32 ? 210  VAL   B CG2 1 
ATOM   5828 N  N   . GLY   B 1 188 ? -60.193 -13.585 34.478  1.00 11.26 ? 211  GLY   B N   1 
ATOM   5829 C  CA  . GLY   B 1 188 ? -58.855 -13.852 33.943  1.00 12.38 ? 211  GLY   B CA  1 
ATOM   5830 C  C   . GLY   B 1 188 ? -58.192 -15.041 34.647  1.00 12.60 ? 211  GLY   B C   1 
ATOM   5831 O  O   . GLY   B 1 188 ? -58.780 -16.126 34.771  1.00 13.25 ? 211  GLY   B O   1 
ATOM   5832 N  N   . LYS   B 1 189 ? -56.938 -14.850 35.085  1.00 12.81 ? 212  LYS   B N   1 
ATOM   5833 C  CA  . LYS   B 1 189 ? -56.170 -15.954 35.633  1.00 12.63 ? 212  LYS   B CA  1 
ATOM   5834 C  C   . LYS   B 1 189 ? -56.391 -16.119 37.141  1.00 14.26 ? 212  LYS   B C   1 
ATOM   5835 O  O   . LYS   B 1 189 ? -55.832 -17.035 37.748  1.00 16.70 ? 212  LYS   B O   1 
ATOM   5836 C  CB  . LYS   B 1 189 ? -54.679 -15.696 35.418  1.00 12.33 ? 212  LYS   B CB  1 
ATOM   5837 C  CG  . LYS   B 1 189 ? -54.281 -15.852 33.962  1.00 11.96 ? 212  LYS   B CG  1 
ATOM   5838 C  CD  . LYS   B 1 189 ? -54.642 -17.249 33.498  1.00 12.20 ? 212  LYS   B CD  1 
ATOM   5839 C  CE  . LYS   B 1 189 ? -54.004 -17.753 32.218  1.00 12.40 ? 212  LYS   B CE  1 
ATOM   5840 N  NZ  . LYS   B 1 189 ? -52.581 -18.093 32.426  1.00 12.72 ? 212  LYS   B NZ  1 
ATOM   5841 N  N   . GLN   B 1 190 ? -57.167 -15.236 37.739  1.00 13.77 ? 213  GLN   B N   1 
ATOM   5842 C  CA  . GLN   B 1 190 ? -57.361 -15.291 39.183  1.00 14.69 ? 213  GLN   B CA  1 
ATOM   5843 C  C   . GLN   B 1 190 ? -58.142 -16.532 39.613  1.00 16.12 ? 213  GLN   B C   1 
ATOM   5844 O  O   . GLN   B 1 190 ? -59.223 -16.799 39.067  1.00 14.32 ? 213  GLN   B O   1 
ATOM   5845 C  CB  . GLN   B 1 190 ? -58.200 -14.128 39.675  1.00 14.61 ? 213  GLN   B CB  1 
ATOM   5846 C  CG  . GLN   B 1 190 ? -57.682 -12.745 39.289  1.00 14.77 ? 213  GLN   B CG  1 
ATOM   5847 C  CD  . GLN   B 1 190 ? -58.608 -11.660 39.803  1.00 16.15 ? 213  GLN   B CD  1 
ATOM   5848 O  OE1 . GLN   B 1 190 ? -58.772 -11.462 41.022  1.00 16.65 ? 213  GLN   B OE1 1 
ATOM   5849 N  NE2 . GLN   B 1 190 ? -59.281 -10.978 38.887  1.00 16.44 ? 213  GLN   B NE2 1 
ATOM   5850 N  N   . ARG   B 1 191 ? -57.629 -17.218 40.645  1.00 15.84 ? 214  ARG   B N   1 
ATOM   5851 C  CA  . ARG   B 1 191 ? -58.376 -18.273 41.333  1.00 15.73 ? 214  ARG   B CA  1 
ATOM   5852 C  C   . ARG   B 1 191 ? -58.173 -18.199 42.845  1.00 18.34 ? 214  ARG   B C   1 
ATOM   5853 O  O   . ARG   B 1 191 ? -57.124 -17.763 43.330  1.00 16.43 ? 214  ARG   B O   1 
ATOM   5854 C  CB  . ARG   B 1 191 ? -57.964 -19.664 40.864  1.00 16.25 ? 214  ARG   B CB  1 
ATOM   5855 C  CG  . ARG   B 1 191 ? -58.261 -19.932 39.395  1.00 17.15 ? 214  ARG   B CG  1 
ATOM   5856 C  CD  . ARG   B 1 191 ? -59.746 -19.988 39.069  1.00 17.36 ? 214  ARG   B CD  1 
ATOM   5857 N  NE  . ARG   B 1 191 ? -60.041 -20.290 37.667  1.00 16.87 ? 214  ARG   B NE  1 
ATOM   5858 C  CZ  . ARG   B 1 191 ? -59.933 -19.444 36.654  1.00 16.50 ? 214  ARG   B CZ  1 
ATOM   5859 N  NH1 . ARG   B 1 191 ? -59.535 -18.191 36.827  1.00 16.38 ? 214  ARG   B NH1 1 
ATOM   5860 N  NH2 . ARG   B 1 191 ? -60.207 -19.875 35.453  1.00 17.18 ? 214  ARG   B NH2 1 
ATOM   5861 N  N   . ILE   B 1 192 ? -59.186 -18.650 43.603  1.00 17.67 ? 215  ILE   B N   1 
ATOM   5862 C  CA  . ILE   B 1 192 ? -59.054 -18.640 45.058  1.00 20.06 ? 215  ILE   B CA  1 
ATOM   5863 C  C   . ILE   B 1 192 ? -58.002 -19.676 45.449  1.00 18.70 ? 215  ILE   B C   1 
ATOM   5864 O  O   . ILE   B 1 192 ? -58.165 -20.857 45.203  1.00 18.10 ? 215  ILE   B O   1 
ATOM   5865 C  CB  . ILE   B 1 192 ? -60.411 -18.895 45.745  1.00 19.66 ? 215  ILE   B CB  1 
ATOM   5866 C  CG1 . ILE   B 1 192 ? -61.396 -17.797 45.419  1.00 20.28 ? 215  ILE   B CG1 1 
ATOM   5867 C  CG2 . ILE   B 1 192 ? -60.217 -19.056 47.262  1.00 21.89 ? 215  ILE   B CG2 1 
ATOM   5868 C  CD1 . ILE   B 1 192 ? -62.847 -18.113 45.748  1.00 19.86 ? 215  ILE   B CD1 1 
ATOM   5869 N  N   . ARG   B 1 193 ? -56.900 -19.203 46.029  1.00 21.59 ? 216  ARG   B N   1 
ATOM   5870 C  CA  . ARG   B 1 193 ? -55.776 -20.065 46.349  1.00 24.41 ? 216  ARG   B CA  1 
ATOM   5871 C  C   . ARG   B 1 193 ? -55.192 -19.719 47.716  1.00 21.75 ? 216  ARG   B C   1 
ATOM   5872 O  O   . ARG   B 1 193 ? -55.167 -18.564 48.081  1.00 23.18 ? 216  ARG   B O   1 
ATOM   5873 C  CB  . ARG   B 1 193 ? -54.655 -19.805 45.338  1.00 26.49 ? 216  ARG   B CB  1 
ATOM   5874 C  CG  . ARG   B 1 193 ? -54.431 -20.932 44.358  1.00 26.81 ? 216  ARG   B CG  1 
ATOM   5875 C  CD  . ARG   B 1 193 ? -55.514 -21.116 43.393  1.00 25.27 ? 216  ARG   B CD  1 
ATOM   5876 N  NE  . ARG   B 1 193 ? -55.332 -22.275 42.522  1.00 23.60 ? 216  ARG   B NE  1 
ATOM   5877 C  CZ  . ARG   B 1 193 ? -54.548 -22.256 41.452  1.00 23.77 ? 216  ARG   B CZ  1 
ATOM   5878 N  NH1 . ARG   B 1 193 ? -53.397 -21.596 41.480  1.00 24.70 ? 216  ARG   B NH1 1 
ATOM   5879 N  NH2 . ARG   B 1 193 ? -54.883 -22.980 40.398  1.00 23.58 ? 216  ARG   B NH2 1 
ATOM   5880 N  N   . ASP   B 1 194 ? -54.588 -20.714 48.374  1.00 25.40 ? 217  ASP   B N   1 
ATOM   5881 C  CA  . ASP   B 1 194 ? -53.677 -20.438 49.483  1.00 26.01 ? 217  ASP   B CA  1 
ATOM   5882 C  C   . ASP   B 1 194 ? -52.523 -19.578 48.948  1.00 25.18 ? 217  ASP   B C   1 
ATOM   5883 O  O   . ASP   B 1 194 ? -51.972 -19.883 47.897  1.00 27.98 ? 217  ASP   B O   1 
ATOM   5884 C  CB  . ASP   B 1 194 ? -53.402 -21.732 50.234  1.00 25.45 ? 217  ASP   B CB  1 
ATOM   5885 C  CG  . ASP   B 1 194 ? -54.631 -22.204 51.014  1.00 27.75 ? 217  ASP   B CG  1 
ATOM   5886 O  OD1 . ASP   B 1 194 ? -55.209 -21.377 51.729  1.00 27.60 ? 217  ASP   B OD1 1 
ATOM   5887 O  OD2 . ASP   B 1 194 ? -55.048 -23.355 50.854  1.00 31.96 ? 217  ASP   B OD2 1 
ATOM   5888 N  N   . VAL   B 1 195 ? -52.235 -18.469 49.637  1.00 27.07 ? 218  VAL   B N   1 
ATOM   5889 C  CA  . VAL   B 1 195 ? -51.316 -17.446 49.152  1.00 27.58 ? 218  VAL   B CA  1 
ATOM   5890 C  C   . VAL   B 1 195 ? -49.855 -17.894 49.283  1.00 30.28 ? 218  VAL   B C   1 
ATOM   5891 O  O   . VAL   B 1 195 ? -49.030 -17.482 48.466  1.00 28.58 ? 218  VAL   B O   1 
ATOM   5892 C  CB  . VAL   B 1 195 ? -51.546 -16.060 49.785  1.00 26.93 ? 218  VAL   B CB  1 
ATOM   5893 C  CG1 . VAL   B 1 195 ? -52.940 -15.537 49.489  1.00 28.78 ? 218  VAL   B CG1 1 
ATOM   5894 C  CG2 . VAL   B 1 195 ? -51.293 -16.007 51.289  1.00 31.29 ? 218  VAL   B CG2 1 
ATOM   5895 N  N   . ALA   B 1 196 ? -49.522 -18.781 50.234  1.00 28.10 ? 219  ALA   B N   1 
ATOM   5896 C  CA  . ALA   B 1 196 ? -48.146 -19.254 50.312  1.00 30.06 ? 219  ALA   B CA  1 
ATOM   5897 C  C   . ALA   B 1 196 ? -47.827 -20.045 49.048  1.00 30.05 ? 219  ALA   B C   1 
ATOM   5898 O  O   . ALA   B 1 196 ? -48.653 -20.811 48.550  1.00 31.40 ? 219  ALA   B O   1 
ATOM   5899 C  CB  . ALA   B 1 196 ? -47.879 -20.084 51.565  1.00 27.61 ? 219  ALA   B CB  1 
ATOM   5900 N  N   . PRO   B 1 197 ? -46.620 -19.873 48.471  1.00 30.07 ? 220  PRO   B N   1 
ATOM   5901 C  CA  . PRO   B 1 197 ? -46.192 -20.720 47.367  1.00 29.67 ? 220  PRO   B CA  1 
ATOM   5902 C  C   . PRO   B 1 197 ? -46.423 -22.208 47.571  1.00 33.11 ? 220  PRO   B C   1 
ATOM   5903 O  O   . PRO   B 1 197 ? -46.135 -22.742 48.631  1.00 33.40 ? 220  PRO   B O   1 
ATOM   5904 C  CB  . PRO   B 1 197 ? -44.701 -20.382 47.271  1.00 28.26 ? 220  PRO   B CB  1 
ATOM   5905 C  CG  . PRO   B 1 197 ? -44.645 -18.939 47.641  1.00 30.48 ? 220  PRO   B CG  1 
ATOM   5906 C  CD  . PRO   B 1 197 ? -45.660 -18.792 48.770  1.00 31.23 ? 220  PRO   B CD  1 
ATOM   5907 N  N   . HIS   B 1 198 ? -46.861 -22.880 46.513  1.00 32.90 ? 221  HIS   B N   1 
ATOM   5908 C  CA  . HIS   B 1 198 ? -47.202 -24.291 46.565  1.00 35.69 ? 221  HIS   B CA  1 
ATOM   5909 C  C   . HIS   B 1 198 ? -47.383 -24.771 45.136  1.00 41.21 ? 221  HIS   B C   1 
ATOM   5910 O  O   . HIS   B 1 198 ? -47.829 -24.000 44.295  1.00 48.20 ? 221  HIS   B O   1 
ATOM   5911 C  CB  . HIS   B 1 198 ? -48.489 -24.540 47.369  1.00 37.90 ? 221  HIS   B CB  1 
ATOM   5912 C  CG  . HIS   B 1 198 ? -49.758 -23.968 46.807  1.00 41.35 ? 221  HIS   B CG  1 
ATOM   5913 N  ND1 . HIS   B 1 198 ? -50.139 -22.647 46.948  1.00 41.62 ? 221  HIS   B ND1 1 
ATOM   5914 C  CD2 . HIS   B 1 198 ? -50.756 -24.566 46.141  1.00 42.71 ? 221  HIS   B CD2 1 
ATOM   5915 C  CE1 . HIS   B 1 198 ? -51.320 -22.467 46.365  1.00 43.75 ? 221  HIS   B CE1 1 
ATOM   5916 N  NE2 . HIS   B 1 198 ? -51.713 -23.619 45.875  1.00 46.17 ? 221  HIS   B NE2 1 
ATOM   5917 N  N   . PRO   B 1 199 ? -47.053 -26.038 44.809  1.00 43.48 ? 222  PRO   B N   1 
ATOM   5918 C  CA  . PRO   B 1 199 ? -47.215 -26.528 43.440  1.00 43.02 ? 222  PRO   B CA  1 
ATOM   5919 C  C   . PRO   B 1 199 ? -48.650 -26.887 43.067  1.00 41.91 ? 222  PRO   B C   1 
ATOM   5920 O  O   . PRO   B 1 199 ? -49.550 -26.823 43.903  1.00 51.80 ? 222  PRO   B O   1 
ATOM   5921 C  CB  . PRO   B 1 199 ? -46.264 -27.734 43.382  1.00 43.89 ? 222  PRO   B CB  1 
ATOM   5922 C  CG  . PRO   B 1 199 ? -46.143 -28.221 44.825  1.00 43.78 ? 222  PRO   B CG  1 
ATOM   5923 C  CD  . PRO   B 1 199 ? -46.477 -27.037 45.723  1.00 44.91 ? 222  PRO   B CD  1 
ATOM   5924 N  N   . GLY   B 1 200 ? -48.854 -27.202 41.785  1.00 37.25 ? 223  GLY   B N   1 
ATOM   5925 C  CA  . GLY   B 1 200 ? -50.054 -27.877 41.305  1.00 35.16 ? 223  GLY   B CA  1 
ATOM   5926 C  C   . GLY   B 1 200 ? -51.158 -26.905 40.874  1.00 33.07 ? 223  GLY   B C   1 
ATOM   5927 O  O   . GLY   B 1 200 ? -52.275 -27.342 40.603  1.00 31.72 ? 223  GLY   B O   1 
ATOM   5928 N  N   . GLY   B 1 201 ? -50.826 -25.610 40.770  1.00 26.89 ? 224  GLY   B N   1 
ATOM   5929 C  CA  . GLY   B 1 201 ? -51.787 -24.574 40.405  1.00 25.44 ? 224  GLY   B CA  1 
ATOM   5930 C  C   . GLY   B 1 201 ? -51.964 -24.417 38.889  1.00 22.85 ? 224  GLY   B C   1 
ATOM   5931 O  O   . GLY   B 1 201 ? -52.935 -23.797 38.462  1.00 22.93 ? 224  GLY   B O   1 
ATOM   5932 N  N   . GLY   B 1 202 ? -51.019 -24.947 38.099  1.00 21.23 ? 225  GLY   B N   1 
ATOM   5933 C  CA  . GLY   B 1 202 ? -51.085 -24.958 36.639  1.00 20.48 ? 225  GLY   B CA  1 
ATOM   5934 C  C   . GLY   B 1 202 ? -50.973 -23.537 36.081  1.00 18.73 ? 225  GLY   B C   1 
ATOM   5935 O  O   . GLY   B 1 202 ? -50.246 -22.701 36.623  1.00 20.27 ? 225  GLY   B O   1 
ATOM   5936 N  N   . ILE   B 1 203 ? -51.772 -23.235 35.049  1.00 16.82 ? 226  ILE   B N   1 
ATOM   5937 C  CA  . ILE   B 1 203 ? -51.731 -21.914 34.434  1.00 15.93 ? 226  ILE   B CA  1 
ATOM   5938 C  C   . ILE   B 1 203 ? -52.693 -20.923 35.094  1.00 16.51 ? 226  ILE   B C   1 
ATOM   5939 O  O   . ILE   B 1 203 ? -52.964 -19.873 34.507  1.00 16.59 ? 226  ILE   B O   1 
ATOM   5940 C  CB  . ILE   B 1 203 ? -51.978 -22.010 32.920  1.00 14.26 ? 226  ILE   B CB  1 
ATOM   5941 C  CG1 . ILE   B 1 203 ? -53.441 -22.409 32.603  1.00 13.72 ? 226  ILE   B CG1 1 
ATOM   5942 C  CG2 . ILE   B 1 203 ? -50.977 -22.950 32.230  1.00 14.26 ? 226  ILE   B CG2 1 
ATOM   5943 C  CD1 . ILE   B 1 203 ? -53.738 -22.429 31.128  1.00 13.86 ? 226  ILE   B CD1 1 
ATOM   5944 N  N   . LEU   B 1 204 ? -53.170 -21.203 36.322  1.00 14.61 ? 227  LEU   B N   1 
ATOM   5945 C  CA  . LEU   B 1 204 ? -54.010 -20.288 37.063  1.00 15.78 ? 227  LEU   B CA  1 
ATOM   5946 C  C   . LEU   B 1 204 ? -53.302 -19.943 38.367  1.00 16.22 ? 227  LEU   B C   1 
ATOM   5947 O  O   . LEU   B 1 204 ? -52.575 -20.759 38.916  1.00 17.60 ? 227  LEU   B O   1 
ATOM   5948 C  CB  . LEU   B 1 204 ? -55.421 -20.836 37.315  1.00 15.63 ? 227  LEU   B CB  1 
ATOM   5949 C  CG  . LEU   B 1 204 ? -56.135 -21.383 36.077  1.00 17.85 ? 227  LEU   B CG  1 
ATOM   5950 C  CD1 . LEU   B 1 204 ? -57.309 -22.286 36.420  1.00 19.18 ? 227  LEU   B CD1 1 
ATOM   5951 C  CD2 . LEU   B 1 204 ? -56.605 -20.205 35.206  1.00 18.95 ? 227  LEU   B CD2 1 
ATOM   5952 N  N   . TYR   B 1 205 ? -53.546 -18.735 38.841  1.00 15.59 ? 228  TYR   B N   1 
ATOM   5953 C  CA  . TYR   B 1 205 ? -52.674 -18.118 39.815  1.00 16.88 ? 228  TYR   B CA  1 
ATOM   5954 C  C   . TYR   B 1 205 ? -53.488 -17.546 40.958  1.00 18.40 ? 228  TYR   B C   1 
ATOM   5955 O  O   . TYR   B 1 205 ? -54.720 -17.547 40.917  1.00 17.07 ? 228  TYR   B O   1 
ATOM   5956 C  CB  . TYR   B 1 205 ? -51.859 -16.999 39.138  1.00 15.73 ? 228  TYR   B CB  1 
ATOM   5957 C  CG  . TYR   B 1 205 ? -51.231 -17.443 37.830  1.00 15.12 ? 228  TYR   B CG  1 
ATOM   5958 C  CD1 . TYR   B 1 205 ? -50.457 -18.596 37.713  1.00 14.28 ? 228  TYR   B CD1 1 
ATOM   5959 C  CD2 . TYR   B 1 205 ? -51.478 -16.702 36.670  1.00 15.95 ? 228  TYR   B CD2 1 
ATOM   5960 C  CE1 . TYR   B 1 205 ? -49.917 -18.989 36.490  1.00 14.18 ? 228  TYR   B CE1 1 
ATOM   5961 C  CE2 . TYR   B 1 205 ? -50.946 -17.078 35.453  1.00 14.27 ? 228  TYR   B CE2 1 
ATOM   5962 C  CZ  . TYR   B 1 205 ? -50.173 -18.220 35.356  1.00 13.72 ? 228  TYR   B CZ  1 
ATOM   5963 O  OH  . TYR   B 1 205 ? -49.708 -18.548 34.113  1.00 14.07 ? 228  TYR   B OH  1 
ATOM   5964 N  N   . THR   B 1 206 ? -52.745 -16.992 41.936  1.00 18.63 ? 229  THR   B N   1 
ATOM   5965 C  CA  . THR   B 1 206 ? -53.291 -16.311 43.096  1.00 18.69 ? 229  THR   B CA  1 
ATOM   5966 C  C   . THR   B 1 206 ? -54.336 -15.288 42.662  1.00 18.88 ? 229  THR   B C   1 
ATOM   5967 O  O   . THR   B 1 206 ? -54.115 -14.505 41.733  1.00 16.67 ? 229  THR   B O   1 
ATOM   5968 C  CB  . THR   B 1 206 ? -52.170 -15.617 43.883  1.00 18.86 ? 229  THR   B CB  1 
ATOM   5969 O  OG1 . THR   B 1 206 ? -51.185 -16.581 44.242  1.00 19.23 ? 229  THR   B OG1 1 
ATOM   5970 C  CG2 . THR   B 1 206 ? -52.676 -14.886 45.114  1.00 20.53 ? 229  THR   B CG2 1 
ATOM   5971 N  N   . ALA   B 1 207 ? -55.419 -15.195 43.450  1.00 17.33 ? 230  ALA   B N   1 
ATOM   5972 C  CA  . ALA   B 1 207 ? -56.470 -14.247 43.146  1.00 17.73 ? 230  ALA   B CA  1 
ATOM   5973 C  C   . ALA   B 1 207 ? -56.028 -12.859 43.573  1.00 17.39 ? 230  ALA   B C   1 
ATOM   5974 O  O   . ALA   B 1 207 ? -55.062 -12.720 44.334  1.00 18.24 ? 230  ALA   B O   1 
ATOM   5975 C  CB  . ALA   B 1 207 ? -57.786 -14.649 43.785  1.00 17.84 ? 230  ALA   B CB  1 
ATOM   5976 N  N   . ALA   B 1 208 ? -56.759 -11.860 43.058  1.00 15.61 ? 231  ALA   B N   1 
ATOM   5977 C  CA  . ALA   B 1 208 ? -56.588 -10.467 43.388  1.00 15.73 ? 231  ALA   B CA  1 
ATOM   5978 C  C   . ALA   B 1 208 ? -57.919 -9.886  43.847  1.00 16.71 ? 231  ALA   B C   1 
ATOM   5979 O  O   . ALA   B 1 208 ? -58.790 -9.558  43.055  1.00 15.71 ? 231  ALA   B O   1 
ATOM   5980 C  CB  . ALA   B 1 208 ? -56.016 -9.689  42.196  1.00 16.24 ? 231  ALA   B CB  1 
ATOM   5981 N  N   . SER   B 1 209 ? -58.018 -9.564  45.136  1.00 17.64 ? 232  SER   B N   1 
ATOM   5982 C  CA  . SER   B 1 209 ? -59.270 -9.082  45.696  1.00 19.25 ? 232  SER   B CA  1 
ATOM   5983 C  C   . SER   B 1 209 ? -59.046 -7.736  46.368  1.00 20.55 ? 232  SER   B C   1 
ATOM   5984 O  O   . SER   B 1 209 ? -58.158 -7.631  47.230  1.00 19.95 ? 232  SER   B O   1 
ATOM   5985 C  CB  . SER   B 1 209 ? -59.841 -10.080 46.666  1.00 16.30 ? 232  SER   B CB  1 
ATOM   5986 O  OG  . SER   B 1 209 ? -59.915 -11.376 46.111  1.00 17.85 ? 232  SER   B OG  1 
ATOM   5987 N  N   . GLY   B 1 210 ? -59.817 -6.739  45.906  1.00 20.30 ? 233  GLY   B N   1 
ATOM   5988 C  CA  . GLY   B 1 210 ? -59.890 -5.430  46.526  1.00 20.70 ? 233  GLY   B CA  1 
ATOM   5989 C  C   . GLY   B 1 210 ? -59.356 -4.309  45.643  1.00 20.70 ? 233  GLY   B C   1 
ATOM   5990 O  O   . GLY   B 1 210 ? -59.350 -4.369  44.407  1.00 19.65 ? 233  GLY   B O   1 
ATOM   5991 N  N   . ILE   B 1 211 ? -58.912 -3.247  46.302  1.00 19.24 ? 234  ILE   B N   1 
ATOM   5992 C  CA  . ILE   B 1 211 ? -58.432 -2.059  45.615  1.00 19.45 ? 234  ILE   B CA  1 
ATOM   5993 C  C   . ILE   B 1 211 ? -57.002 -2.331  45.135  1.00 19.36 ? 234  ILE   B C   1 
ATOM   5994 O  O   . ILE   B 1 211 ? -56.102 -2.550  45.957  1.00 20.87 ? 234  ILE   B O   1 
ATOM   5995 C  CB  . ILE   B 1 211 ? -58.513 -0.843  46.563  1.00 21.82 ? 234  ILE   B CB  1 
ATOM   5996 C  CG1 . ILE   B 1 211 ? -59.947 -0.623  47.078  1.00 24.69 ? 234  ILE   B CG1 1 
ATOM   5997 C  CG2 . ILE   B 1 211 ? -57.977 0.430   45.920  1.00 21.88 ? 234  ILE   B CG2 1 
ATOM   5998 C  CD1 . ILE   B 1 211 ? -60.111 0.542   48.041  1.00 25.14 ? 234  ILE   B CD1 1 
ATOM   5999 N  N   . TRP   B 1 212 ? -56.780 -2.309  43.804  1.00 19.57 ? 235  TRP   B N   1 
ATOM   6000 C  CA  . TRP   B 1 212 ? -55.465 -2.668  43.282  1.00 19.00 ? 235  TRP   B CA  1 
ATOM   6001 C  C   . TRP   B 1 212 ? -54.841 -1.608  42.373  1.00 18.88 ? 235  TRP   B C   1 
ATOM   6002 O  O   . TRP   B 1 212 ? -53.766 -1.847  41.818  1.00 18.96 ? 235  TRP   B O   1 
ATOM   6003 C  CB  . TRP   B 1 212 ? -55.527 -4.027  42.579  1.00 18.96 ? 235  TRP   B CB  1 
ATOM   6004 C  CG  . TRP   B 1 212 ? -56.371 -4.133  41.335  1.00 18.53 ? 235  TRP   B CG  1 
ATOM   6005 C  CD1 . TRP   B 1 212 ? -57.723 -4.376  41.260  1.00 19.56 ? 235  TRP   B CD1 1 
ATOM   6006 C  CD2 . TRP   B 1 212 ? -55.884 -4.164  39.969  1.00 17.82 ? 235  TRP   B CD2 1 
ATOM   6007 N  NE1 . TRP   B 1 212 ? -58.111 -4.495  39.943  1.00 17.37 ? 235  TRP   B NE1 1 
ATOM   6008 C  CE2 . TRP   B 1 212 ? -57.004 -4.395  39.135  1.00 17.75 ? 235  TRP   B CE2 1 
ATOM   6009 C  CE3 . TRP   B 1 212 ? -54.620 -4.016  39.374  1.00 19.80 ? 235  TRP   B CE3 1 
ATOM   6010 C  CZ2 . TRP   B 1 212 ? -56.889 -4.484  37.747  1.00 17.23 ? 235  TRP   B CZ2 1 
ATOM   6011 C  CZ3 . TRP   B 1 212 ? -54.517 -4.073  37.998  1.00 16.90 ? 235  TRP   B CZ3 1 
ATOM   6012 C  CH2 . TRP   B 1 212 ? -55.635 -4.345  37.200  1.00 16.72 ? 235  TRP   B CH2 1 
ATOM   6013 N  N   . GLN   B 1 213 ? -55.520 -0.474  42.214  1.00 17.07 ? 236  GLN   B N   1 
ATOM   6014 C  CA  . GLN   B 1 213 ? -54.988 0.690   41.547  1.00 18.12 ? 236  GLN   B CA  1 
ATOM   6015 C  C   . GLN   B 1 213 ? -55.238 1.925   42.418  1.00 21.74 ? 236  GLN   B C   1 
ATOM   6016 O  O   . GLN   B 1 213 ? -56.062 1.903   43.346  1.00 18.03 ? 236  GLN   B O   1 
ATOM   6017 C  CB  . GLN   B 1 213 ? -55.612 0.900   40.171  1.00 17.02 ? 236  GLN   B CB  1 
ATOM   6018 C  CG  . GLN   B 1 213 ? -55.387 -0.280  39.231  1.00 15.96 ? 236  GLN   B CG  1 
ATOM   6019 C  CD  . GLN   B 1 213 ? -55.896 -0.003  37.835  1.00 15.66 ? 236  GLN   B CD  1 
ATOM   6020 O  OE1 . GLN   B 1 213 ? -56.225 1.122   37.469  1.00 16.10 ? 236  GLN   B OE1 1 
ATOM   6021 N  NE2 . GLN   B 1 213 ? -55.973 -1.053  37.037  1.00 16.88 ? 236  GLN   B NE2 1 
ATOM   6022 N  N   . THR   B 1 214 ? -54.532 3.010   42.065  1.00 22.00 ? 237  THR   B N   1 
ATOM   6023 C  CA  . THR   B 1 214 ? -54.549 4.247   42.829  1.00 23.33 ? 237  THR   B CA  1 
ATOM   6024 C  C   . THR   B 1 214 ? -55.975 4.759   43.046  1.00 26.53 ? 237  THR   B C   1 
ATOM   6025 O  O   . THR   B 1 214 ? -56.761 4.872   42.106  1.00 24.29 ? 237  THR   B O   1 
ATOM   6026 C  CB  . THR   B 1 214 ? -53.693 5.296   42.115  1.00 22.55 ? 237  THR   B CB  1 
ATOM   6027 O  OG1 . THR   B 1 214 ? -52.356 4.787   42.137  1.00 20.93 ? 237  THR   B OG1 1 
ATOM   6028 C  CG2 . THR   B 1 214 ? -53.711 6.643   42.815  1.00 21.56 ? 237  THR   B CG2 1 
ATOM   6029 N  N   . VAL   B 1 215 ? -56.251 5.137   44.309  1.00 24.84 ? 238  VAL   B N   1 
ATOM   6030 C  CA  . VAL   B 1 215 ? -57.421 5.912   44.690  1.00 24.35 ? 238  VAL   B CA  1 
ATOM   6031 C  C   . VAL   B 1 215 ? -56.996 7.369   44.858  1.00 23.28 ? 238  VAL   B C   1 
ATOM   6032 O  O   . VAL   B 1 215 ? -55.963 7.646   45.484  1.00 23.53 ? 238  VAL   B O   1 
ATOM   6033 C  CB  . VAL   B 1 215 ? -58.012 5.365   46.003  1.00 25.90 ? 238  VAL   B CB  1 
ATOM   6034 C  CG1 . VAL   B 1 215 ? -59.300 6.081   46.398  1.00 28.77 ? 238  VAL   B CG1 1 
ATOM   6035 C  CG2 . VAL   B 1 215 ? -58.232 3.862   45.942  1.00 26.65 ? 238  VAL   B CG2 1 
ATOM   6036 N  N   . TRP   B 1 216 ? -57.776 8.288   44.301  1.00 20.76 ? 239  TRP   B N   1 
ATOM   6037 C  CA  . TRP   B 1 216 ? -57.389 9.679   44.327  1.00 22.35 ? 239  TRP   B CA  1 
ATOM   6038 C  C   . TRP   B 1 216 ? -58.588 10.604  44.196  1.00 23.68 ? 239  TRP   B C   1 
ATOM   6039 O  O   . TRP   B 1 216 ? -59.693 10.156  43.899  1.00 24.79 ? 239  TRP   B O   1 
ATOM   6040 C  CB  . TRP   B 1 216 ? -56.346 9.935   43.238  1.00 20.90 ? 239  TRP   B CB  1 
ATOM   6041 C  CG  . TRP   B 1 216 ? -56.729 9.595   41.825  1.00 19.05 ? 239  TRP   B CG  1 
ATOM   6042 C  CD1 . TRP   B 1 216 ? -56.908 8.352   41.300  1.00 19.32 ? 239  TRP   B CD1 1 
ATOM   6043 C  CD2 . TRP   B 1 216 ? -56.825 10.519  40.722  1.00 18.74 ? 239  TRP   B CD2 1 
ATOM   6044 N  NE1 . TRP   B 1 216 ? -57.163 8.445   39.952  1.00 18.47 ? 239  TRP   B NE1 1 
ATOM   6045 C  CE2 . TRP   B 1 216 ? -57.116 9.757   39.569  1.00 17.46 ? 239  TRP   B CE2 1 
ATOM   6046 C  CE3 . TRP   B 1 216 ? -56.710 11.901  40.593  1.00 17.38 ? 239  TRP   B CE3 1 
ATOM   6047 C  CZ2 . TRP   B 1 216 ? -57.270 10.340  38.320  1.00 17.95 ? 239  TRP   B CZ2 1 
ATOM   6048 C  CZ3 . TRP   B 1 216 ? -56.844 12.480  39.351  1.00 17.50 ? 239  TRP   B CZ3 1 
ATOM   6049 C  CH2 . TRP   B 1 216 ? -57.125 11.706  38.222  1.00 17.91 ? 239  TRP   B CH2 1 
ATOM   6050 N  N   . LEU   B 1 217 ? -58.340 11.894  44.468  1.00 22.50 ? 240  LEU   B N   1 
ATOM   6051 C  CA  . LEU   B 1 217 ? -59.335 12.945  44.389  1.00 22.63 ? 240  LEU   B CA  1 
ATOM   6052 C  C   . LEU   B 1 217 ? -58.904 13.954  43.349  1.00 21.06 ? 240  LEU   B C   1 
ATOM   6053 O  O   . LEU   B 1 217 ? -57.698 14.149  43.182  1.00 24.93 ? 240  LEU   B O   1 
ATOM   6054 C  CB  . LEU   B 1 217 ? -59.420 13.686  45.724  1.00 24.94 ? 240  LEU   B CB  1 
ATOM   6055 C  CG  . LEU   B 1 217 ? -59.982 12.906  46.911  1.00 27.81 ? 240  LEU   B CG  1 
ATOM   6056 C  CD1 . LEU   B 1 217 ? -59.613 13.649  48.207  1.00 29.59 ? 240  LEU   B CD1 1 
ATOM   6057 C  CD2 . LEU   B 1 217 ? -61.500 12.787  46.740  1.00 26.77 ? 240  LEU   B CD2 1 
ATOM   6058 N  N   . GLU   B 1 218 ? -59.876 14.619  42.708  1.00 20.59 ? 241  GLU   B N   1 
ATOM   6059 C  CA  . GLU   B 1 218 ? -59.572 15.756  41.870  1.00 21.79 ? 241  GLU   B CA  1 
ATOM   6060 C  C   . GLU   B 1 218 ? -60.754 16.721  41.808  1.00 25.97 ? 241  GLU   B C   1 
ATOM   6061 O  O   . GLU   B 1 218 ? -61.931 16.311  41.786  1.00 26.50 ? 241  GLU   B O   1 
ATOM   6062 C  CB  . GLU   B 1 218 ? -59.124 15.373  40.458  1.00 24.03 ? 241  GLU   B CB  1 
ATOM   6063 C  CG  . GLU   B 1 218 ? -60.297 15.203  39.508  1.00 25.67 ? 241  GLU   B CG  1 
ATOM   6064 C  CD  . GLU   B 1 218 ? -59.956 14.695  38.121  1.00 26.78 ? 241  GLU   B CD  1 
ATOM   6065 O  OE1 . GLU   B 1 218 ? -59.209 15.356  37.355  1.00 24.16 ? 241  GLU   B OE1 1 
ATOM   6066 O  OE2 . GLU   B 1 218 ? -60.511 13.620  37.828  1.00 22.58 ? 241  GLU   B OE2 1 
ATOM   6067 N  N   . PRO   B 1 219 ? -60.486 18.050  41.769  1.00 28.19 ? 242  PRO   B N   1 
ATOM   6068 C  CA  . PRO   B 1 219 ? -61.533 19.040  41.557  1.00 26.08 ? 242  PRO   B CA  1 
ATOM   6069 C  C   . PRO   B 1 219 ? -61.758 19.344  40.081  1.00 24.31 ? 242  PRO   B C   1 
ATOM   6070 O  O   . PRO   B 1 219 ? -60.819 19.321  39.289  1.00 29.00 ? 242  PRO   B O   1 
ATOM   6071 C  CB  . PRO   B 1 219 ? -60.931 20.234  42.320  1.00 29.56 ? 242  PRO   B CB  1 
ATOM   6072 C  CG  . PRO   B 1 219 ? -59.470 20.183  41.932  1.00 29.53 ? 242  PRO   B CG  1 
ATOM   6073 C  CD  . PRO   B 1 219 ? -59.168 18.687  41.973  1.00 29.51 ? 242  PRO   B CD  1 
ATOM   6074 N  N   . THR   B 1 220 ? -63.019 19.593  39.728  1.00 21.37 ? 243  THR   B N   1 
ATOM   6075 C  CA  . THR   B 1 220 ? -63.413 20.024  38.395  1.00 22.90 ? 243  THR   B CA  1 
ATOM   6076 C  C   . THR   B 1 220 ? -64.465 21.114  38.520  1.00 23.98 ? 243  THR   B C   1 
ATOM   6077 O  O   . THR   B 1 220 ? -65.191 21.166  39.506  1.00 28.39 ? 243  THR   B O   1 
ATOM   6078 C  CB  . THR   B 1 220 ? -63.988 18.871  37.556  1.00 24.81 ? 243  THR   B CB  1 
ATOM   6079 O  OG1 . THR   B 1 220 ? -65.238 18.461  38.118  1.00 23.75 ? 243  THR   B OG1 1 
ATOM   6080 C  CG2 . THR   B 1 220 ? -63.054 17.667  37.499  1.00 24.53 ? 243  THR   B CG2 1 
ATOM   6081 N  N   . ALA   B 1 221 ? -64.551 21.942  37.483  1.00 24.42 ? 244  ALA   B N   1 
ATOM   6082 C  CA  . ALA   B 1 221 ? -65.768 22.677  37.204  1.00 28.43 ? 244  ALA   B CA  1 
ATOM   6083 C  C   . ALA   B 1 221 ? -66.937 21.685  37.093  1.00 30.87 ? 244  ALA   B C   1 
ATOM   6084 O  O   . ALA   B 1 221 ? -66.752 20.512  36.751  1.00 27.19 ? 244  ALA   B O   1 
ATOM   6085 C  CB  . ALA   B 1 221 ? -65.586 23.495  35.949  1.00 27.50 ? 244  ALA   B CB  1 
ATOM   6086 N  N   . ALA   B 1 222 ? -68.139 22.142  37.456  1.00 28.06 ? 245  ALA   B N   1 
ATOM   6087 C  CA  . ALA   B 1 222 ? -69.335 21.334  37.296  1.00 29.55 ? 245  ALA   B CA  1 
ATOM   6088 C  C   . ALA   B 1 222 ? -69.428 20.847  35.850  1.00 28.16 ? 245  ALA   B C   1 
ATOM   6089 O  O   . ALA   B 1 222 ? -69.595 19.649  35.609  1.00 29.80 ? 245  ALA   B O   1 
ATOM   6090 C  CB  . ALA   B 1 222 ? -70.568 22.141  37.713  1.00 29.79 ? 245  ALA   B CB  1 
ATOM   6091 N  N   . ALA   B 1 223 ? -69.325 21.785  34.905  1.00 25.43 ? 246  ALA   B N   1 
ATOM   6092 C  CA  . ALA   B 1 223 ? -69.261 21.474  33.493  1.00 26.86 ? 246  ALA   B CA  1 
ATOM   6093 C  C   . ALA   B 1 223 ? -67.818 21.109  33.171  1.00 28.67 ? 246  ALA   B C   1 
ATOM   6094 O  O   . ALA   B 1 223 ? -66.964 21.990  33.190  1.00 28.37 ? 246  ALA   B O   1 
ATOM   6095 C  CB  . ALA   B 1 223 ? -69.729 22.645  32.671  1.00 25.12 ? 246  ALA   B CB  1 
ATOM   6096 N  N   . HIS   B 1 224 ? -67.537 19.813  32.969  1.00 26.58 ? 247  HIS   B N   1 
ATOM   6097 C  CA  . HIS   B 1 224 ? -66.157 19.375  32.765  1.00 26.33 ? 247  HIS   B CA  1 
ATOM   6098 C  C   . HIS   B 1 224 ? -66.029 18.274  31.709  1.00 24.47 ? 247  HIS   B C   1 
ATOM   6099 O  O   . HIS   B 1 224 ? -67.007 17.649  31.312  1.00 21.93 ? 247  HIS   B O   1 
ATOM   6100 C  CB  . HIS   B 1 224 ? -65.515 18.984  34.099  1.00 26.49 ? 247  HIS   B CB  1 
ATOM   6101 C  CG  . HIS   B 1 224 ? -66.148 17.819  34.777  1.00 26.42 ? 247  HIS   B CG  1 
ATOM   6102 N  ND1 . HIS   B 1 224 ? -67.374 17.845  35.417  1.00 23.63 ? 247  HIS   B ND1 1 
ATOM   6103 C  CD2 . HIS   B 1 224 ? -65.672 16.569  34.907  1.00 27.68 ? 247  HIS   B CD2 1 
ATOM   6104 C  CE1 . HIS   B 1 224 ? -67.610 16.644  35.923  1.00 27.44 ? 247  HIS   B CE1 1 
ATOM   6105 N  NE2 . HIS   B 1 224 ? -66.586 15.846  35.627  1.00 27.14 ? 247  HIS   B NE2 1 
ATOM   6106 N  N   . VAL   B 1 225 ? -64.796 18.119  31.196  1.00 22.18 ? 248  VAL   B N   1 
ATOM   6107 C  CA  . VAL   B 1 225 ? -64.435 17.048  30.273  1.00 19.23 ? 248  VAL   B CA  1 
ATOM   6108 C  C   . VAL   B 1 225 ? -64.249 15.757  31.057  1.00 19.73 ? 248  VAL   B C   1 
ATOM   6109 O  O   . VAL   B 1 225 ? -63.560 15.726  32.083  1.00 22.00 ? 248  VAL   B O   1 
ATOM   6110 C  CB  . VAL   B 1 225 ? -63.156 17.405  29.492  1.00 18.65 ? 248  VAL   B CB  1 
ATOM   6111 C  CG1 . VAL   B 1 225 ? -62.671 16.261  28.608  1.00 17.52 ? 248  VAL   B CG1 1 
ATOM   6112 C  CG2 . VAL   B 1 225 ? -63.322 18.675  28.673  1.00 17.19 ? 248  VAL   B CG2 1 
ATOM   6113 N  N   . THR   B 1 226 ? -64.884 14.679  30.559  1.00 17.00 ? 249  THR   B N   1 
ATOM   6114 C  CA  . THR   B 1 226 ? -64.710 13.369  31.156  1.00 17.50 ? 249  THR   B CA  1 
ATOM   6115 C  C   . THR   B 1 226 ? -64.004 12.431  30.189  1.00 16.61 ? 249  THR   B C   1 
ATOM   6116 O  O   . THR   B 1 226 ? -63.507 11.420  30.642  1.00 18.70 ? 249  THR   B O   1 
ATOM   6117 C  CB  . THR   B 1 226 ? -66.041 12.775  31.602  1.00 18.00 ? 249  THR   B CB  1 
ATOM   6118 O  OG1 . THR   B 1 226 ? -66.808 12.705  30.397  1.00 18.79 ? 249  THR   B OG1 1 
ATOM   6119 C  CG2 . THR   B 1 226 ? -66.693 13.621  32.677  1.00 19.42 ? 249  THR   B CG2 1 
ATOM   6120 N  N   . ARG   B 1 227 ? -63.934 12.773  28.909  1.00 17.57 ? 250  ARG   B N   1 
ATOM   6121 C  CA  . ARG   B 1 227 ? -63.351 11.874  27.935  1.00 18.87 ? 250  ARG   B CA  1 
ATOM   6122 C  C   . ARG   B 1 227 ? -62.897 12.665  26.708  1.00 19.55 ? 250  ARG   B C   1 
ATOM   6123 O  O   . ARG   B 1 227 ? -63.554 13.608  26.275  1.00 17.49 ? 250  ARG   B O   1 
ATOM   6124 C  CB  . ARG   B 1 227 ? -64.438 10.858  27.559  1.00 18.73 ? 250  ARG   B CB  1 
ATOM   6125 C  CG  . ARG   B 1 227 ? -63.884 9.514   27.174  1.00 19.80 ? 250  ARG   B CG  1 
ATOM   6126 C  CD  . ARG   B 1 227 ? -65.015 8.533   26.951  1.00 19.47 ? 250  ARG   B CD  1 
ATOM   6127 N  NE  . ARG   B 1 227 ? -65.189 8.265   25.525  1.00 17.06 ? 250  ARG   B NE  1 
ATOM   6128 C  CZ  . ARG   B 1 227 ? -66.201 7.583   25.052  1.00 16.13 ? 250  ARG   B CZ  1 
ATOM   6129 N  NH1 . ARG   B 1 227 ? -67.097 7.042   25.891  1.00 18.80 ? 250  ARG   B NH1 1 
ATOM   6130 N  NH2 . ARG   B 1 227 ? -66.293 7.422   23.774  1.00 17.17 ? 250  ARG   B NH2 1 
ATOM   6131 N  N   . LEU   B 1 228 ? -61.726 12.288  26.182  1.00 20.67 ? 251  LEU   B N   1 
ATOM   6132 C  CA  . LEU   B 1 228 ? -61.208 12.825  24.937  1.00 23.32 ? 251  LEU   B CA  1 
ATOM   6133 C  C   . LEU   B 1 228 ? -60.924 11.629  24.054  1.00 22.25 ? 251  LEU   B C   1 
ATOM   6134 O  O   . LEU   B 1 228 ? -60.069 10.820  24.413  1.00 25.22 ? 251  LEU   B O   1 
ATOM   6135 C  CB  . LEU   B 1 228 ? -59.899 13.591  25.134  1.00 26.07 ? 251  LEU   B CB  1 
ATOM   6136 C  CG  . LEU   B 1 228 ? -59.919 15.117  25.165  1.00 27.87 ? 251  LEU   B CG  1 
ATOM   6137 C  CD1 . LEU   B 1 228 ? -58.452 15.508  25.345  1.00 26.49 ? 251  LEU   B CD1 1 
ATOM   6138 C  CD2 . LEU   B 1 228 ? -60.476 15.785  23.914  1.00 27.01 ? 251  LEU   B CD2 1 
ATOM   6139 N  N   . ASP   B 1 229 ? -61.627 11.552  22.930  1.00 19.52 ? 252  ASP   B N   1 
ATOM   6140 C  CA  . ASP   B 1 229 ? -61.395 10.524  21.944  1.00 17.88 ? 252  ASP   B CA  1 
ATOM   6141 C  C   . ASP   B 1 229 ? -60.562 11.114  20.814  1.00 18.72 ? 252  ASP   B C   1 
ATOM   6142 O  O   . ASP   B 1 229 ? -61.080 11.852  19.974  1.00 21.05 ? 252  ASP   B O   1 
ATOM   6143 C  CB  . ASP   B 1 229 ? -62.693 9.925   21.435  1.00 17.25 ? 252  ASP   B CB  1 
ATOM   6144 C  CG  . ASP   B 1 229 ? -63.615 9.384   22.524  1.00 17.63 ? 252  ASP   B CG  1 
ATOM   6145 O  OD1 . ASP   B 1 229 ? -63.128 9.069   23.630  1.00 16.14 ? 252  ASP   B OD1 1 
ATOM   6146 O  OD2 . ASP   B 1 229 ? -64.827 9.266   22.237  1.00 17.67 ? 252  ASP   B OD2 1 
ATOM   6147 N  N   . LEU   B 1 230 ? -59.262 10.765  20.807  1.00 16.27 ? 253  LEU   B N   1 
ATOM   6148 C  CA  . LEU   B 1 230 ? -58.321 11.315  19.848  1.00 14.44 ? 253  LEU   B CA  1 
ATOM   6149 C  C   . LEU   B 1 230 ? -57.954 10.220  18.869  1.00 14.40 ? 253  LEU   B C   1 
ATOM   6150 O  O   . LEU   B 1 230 ? -57.304 9.262   19.278  1.00 13.97 ? 253  LEU   B O   1 
ATOM   6151 C  CB  . LEU   B 1 230 ? -57.055 11.845  20.527  1.00 14.10 ? 253  LEU   B CB  1 
ATOM   6152 C  CG  . LEU   B 1 230 ? -57.238 12.788  21.711  1.00 14.90 ? 253  LEU   B CG  1 
ATOM   6153 C  CD1 . LEU   B 1 230 ? -55.918 13.225  22.330  1.00 15.23 ? 253  LEU   B CD1 1 
ATOM   6154 C  CD2 . LEU   B 1 230 ? -57.990 13.989  21.222  1.00 15.40 ? 253  LEU   B CD2 1 
ATOM   6155 N  N   . VAL   B 1 231 ? -58.332 10.406  17.599  1.00 13.90 ? 254  VAL   B N   1 
ATOM   6156 C  CA  . VAL   B 1 231 ? -58.205 9.399   16.561  1.00 14.77 ? 254  VAL   B CA  1 
ATOM   6157 C  C   . VAL   B 1 231 ? -57.345 9.984   15.450  1.00 15.98 ? 254  VAL   B C   1 
ATOM   6158 O  O   . VAL   B 1 231 ? -57.781 10.837  14.660  1.00 16.50 ? 254  VAL   B O   1 
ATOM   6159 C  CB  . VAL   B 1 231 ? -59.556 8.890   16.019  1.00 13.63 ? 254  VAL   B CB  1 
ATOM   6160 C  CG1 . VAL   B 1 231 ? -59.409 7.887   14.904  1.00 13.40 ? 254  VAL   B CG1 1 
ATOM   6161 C  CG2 . VAL   B 1 231 ? -60.399 8.303   17.130  1.00 13.79 ? 254  VAL   B CG2 1 
ATOM   6162 N  N   . PRO   B 1 232 ? -56.073 9.546   15.344  1.00 15.74 ? 255  PRO   B N   1 
ATOM   6163 C  CA  . PRO   B 1 232 ? -55.213 10.099  14.312  1.00 15.08 ? 255  PRO   B CA  1 
ATOM   6164 C  C   . PRO   B 1 232 ? -55.698 9.808   12.902  1.00 16.04 ? 255  PRO   B C   1 
ATOM   6165 O  O   . PRO   B 1 232 ? -56.185 8.716   12.622  1.00 13.95 ? 255  PRO   B O   1 
ATOM   6166 C  CB  . PRO   B 1 232 ? -53.851 9.450   14.590  1.00 15.04 ? 255  PRO   B CB  1 
ATOM   6167 C  CG  . PRO   B 1 232 ? -53.900 9.118   16.061  1.00 15.24 ? 255  PRO   B CG  1 
ATOM   6168 C  CD  . PRO   B 1 232 ? -55.354 8.690   16.309  1.00 15.42 ? 255  PRO   B CD  1 
ATOM   6169 N  N   . ASP   B 1 233 ? -55.532 10.796  12.007  1.00 16.56 ? 256  ASP   B N   1 
ATOM   6170 C  CA  . ASP   B 1 233 ? -55.803 10.606  10.594  1.00 17.71 ? 256  ASP   B CA  1 
ATOM   6171 C  C   . ASP   B 1 233 ? -54.641 11.214  9.813   1.00 19.15 ? 256  ASP   B C   1 
ATOM   6172 O  O   . ASP   B 1 233 ? -54.844 12.171  9.062   1.00 20.75 ? 256  ASP   B O   1 
ATOM   6173 C  CB  . ASP   B 1 233 ? -57.128 11.246  10.179  1.00 18.43 ? 256  ASP   B CB  1 
ATOM   6174 C  CG  . ASP   B 1 233 ? -57.628 10.958  8.768   1.00 19.65 ? 256  ASP   B CG  1 
ATOM   6175 O  OD1 . ASP   B 1 233 ? -57.079 10.065  8.097   1.00 20.77 ? 256  ASP   B OD1 1 
ATOM   6176 O  OD2 . ASP   B 1 233 ? -58.587 11.641  8.345   1.00 23.47 ? 256  ASP   B OD2 1 
ATOM   6177 N  N   . PRO   B 1 234 ? -53.400 10.710  9.999   1.00 17.97 ? 257  PRO   B N   1 
ATOM   6178 C  CA  . PRO   B 1 234 ? -52.229 11.283  9.336   1.00 18.35 ? 257  PRO   B CA  1 
ATOM   6179 C  C   . PRO   B 1 234 ? -52.311 11.304  7.814   1.00 20.87 ? 257  PRO   B C   1 
ATOM   6180 O  O   . PRO   B 1 234 ? -51.794 12.240  7.188   1.00 21.31 ? 257  PRO   B O   1 
ATOM   6181 C  CB  . PRO   B 1 234 ? -51.053 10.453  9.892   1.00 18.04 ? 257  PRO   B CB  1 
ATOM   6182 C  CG  . PRO   B 1 234 ? -51.711 9.152   10.323  1.00 19.36 ? 257  PRO   B CG  1 
ATOM   6183 C  CD  . PRO   B 1 234 ? -53.045 9.602   10.900  1.00 18.84 ? 257  PRO   B CD  1 
ATOM   6184 N  N   . ALA   B 1 235 ? -52.999 10.341  7.196   1.00 18.98 ? 258  ALA   B N   1 
ATOM   6185 C  CA  . ALA   B 1 235 ? -53.090 10.364  5.743   1.00 20.90 ? 258  ALA   B CA  1 
ATOM   6186 C  C   . ALA   B 1 235 ? -53.717 11.686  5.303   1.00 23.02 ? 258  ALA   B C   1 
ATOM   6187 O  O   . ALA   B 1 235 ? -53.420 12.163  4.206   1.00 26.93 ? 258  ALA   B O   1 
ATOM   6188 C  CB  . ALA   B 1 235 ? -53.872 9.202   5.187   1.00 22.25 ? 258  ALA   B CB  1 
ATOM   6189 N  N   . ASN   B 1 236 ? -54.564 12.274  6.156   1.00 24.03 ? 259  ASN   B N   1 
ATOM   6190 C  CA  . ASN   B 1 236 ? -55.244 13.517  5.818   1.00 26.23 ? 259  ASN   B CA  1 
ATOM   6191 C  C   . ASN   B 1 236 ? -54.698 14.649  6.682   1.00 25.07 ? 259  ASN   B C   1 
ATOM   6192 O  O   . ASN   B 1 236 ? -55.330 15.690  6.796   1.00 24.04 ? 259  ASN   B O   1 
ATOM   6193 C  CB  . ASN   B 1 236 ? -56.763 13.425  5.957   1.00 26.48 ? 259  ASN   B CB  1 
ATOM   6194 C  CG  . ASN   B 1 236 ? -57.391 12.537  4.907   1.00 31.94 ? 259  ASN   B CG  1 
ATOM   6195 O  OD1 . ASN   B 1 236 ? -57.154 12.725  3.706   1.00 30.02 ? 259  ASN   B OD1 1 
ATOM   6196 N  ND2 . ASN   B 1 236 ? -58.179 11.555  5.337   1.00 31.11 ? 259  ASN   B ND2 1 
ATOM   6197 N  N   . SER   B 1 237 ? -53.529 14.435  7.281   1.00 23.98 ? 260  SER   B N   1 
ATOM   6198 C  CA  . SER   B 1 237 ? -52.817 15.480  7.993   1.00 23.20 ? 260  SER   B CA  1 
ATOM   6199 C  C   . SER   B 1 237 ? -53.712 16.096  9.069   1.00 22.61 ? 260  SER   B C   1 
ATOM   6200 O  O   . SER   B 1 237 ? -53.778 17.319  9.224   1.00 19.88 ? 260  SER   B O   1 
ATOM   6201 C  CB  . SER   B 1 237 ? -52.296 16.528  7.008   1.00 24.63 ? 260  SER   B CB  1 
ATOM   6202 O  OG  . SER   B 1 237 ? -51.400 15.948  6.068   1.00 24.27 ? 260  SER   B OG  1 
ATOM   6203 N  N   . ARG   B 1 238 ? -54.440 15.259  9.826   1.00 20.39 ? 261  ARG   B N   1 
ATOM   6204 C  CA  . ARG   B 1 238 ? -55.291 15.815  10.872  1.00 20.14 ? 261  ARG   B CA  1 
ATOM   6205 C  C   . ARG   B 1 238 ? -55.503 14.819  12.002  1.00 18.35 ? 261  ARG   B C   1 
ATOM   6206 O  O   . ARG   B 1 238 ? -55.269 13.637  11.833  1.00 16.86 ? 261  ARG   B O   1 
ATOM   6207 C  CB  . ARG   B 1 238 ? -56.649 16.252  10.311  1.00 21.90 ? 261  ARG   B CB  1 
ATOM   6208 C  CG  . ARG   B 1 238 ? -57.382 15.065  9.704   1.00 25.46 ? 261  ARG   B CG  1 
ATOM   6209 C  CD  . ARG   B 1 238 ? -58.595 15.468  8.888   1.00 27.14 ? 261  ARG   B CD  1 
ATOM   6210 N  NE  . ARG   B 1 238 ? -59.341 14.270  8.496   1.00 27.07 ? 261  ARG   B NE  1 
ATOM   6211 C  CZ  . ARG   B 1 238 ? -60.375 14.267  7.690   1.00 30.09 ? 261  ARG   B CZ  1 
ATOM   6212 N  NH1 . ARG   B 1 238 ? -60.870 15.403  7.282   1.00 30.46 ? 261  ARG   B NH1 1 
ATOM   6213 N  NH2 . ARG   B 1 238 ? -60.956 13.138  7.331   1.00 30.26 ? 261  ARG   B NH2 1 
ATOM   6214 N  N   . LEU   B 1 239 ? -55.940 15.348  13.145  1.00 19.14 ? 262  LEU   B N   1 
ATOM   6215 C  CA  . LEU   B 1 239 ? -56.403 14.576  14.275  1.00 18.42 ? 262  LEU   B CA  1 
ATOM   6216 C  C   . LEU   B 1 239 ? -57.927 14.657  14.393  1.00 18.00 ? 262  LEU   B C   1 
ATOM   6217 O  O   . LEU   B 1 239 ? -58.505 15.748  14.358  1.00 17.30 ? 262  LEU   B O   1 
ATOM   6218 C  CB  . LEU   B 1 239 ? -55.760 15.167  15.514  1.00 17.68 ? 262  LEU   B CB  1 
ATOM   6219 C  CG  . LEU   B 1 239 ? -56.039 14.394  16.810  1.00 18.02 ? 262  LEU   B CG  1 
ATOM   6220 C  CD1 . LEU   B 1 239 ? -55.578 12.926  16.763  1.00 17.74 ? 262  LEU   B CD1 1 
ATOM   6221 C  CD2 . LEU   B 1 239 ? -55.425 15.074  18.008  1.00 17.72 ? 262  LEU   B CD2 1 
ATOM   6222 N  N   . LYS   B 1 240 ? -58.582 13.498  14.467  1.00 16.62 ? 263  LYS   B N   1 
ATOM   6223 C  CA  . LYS   B 1 240 ? -60.015 13.466  14.735  1.00 17.18 ? 263  LYS   B CA  1 
ATOM   6224 C  C   . LYS   B 1 240 ? -60.247 13.491  16.235  1.00 18.61 ? 263  LYS   B C   1 
ATOM   6225 O  O   . LYS   B 1 240 ? -59.714 12.651  16.938  1.00 21.82 ? 263  LYS   B O   1 
ATOM   6226 C  CB  . LYS   B 1 240 ? -60.710 12.267  14.095  1.00 18.45 ? 263  LYS   B CB  1 
ATOM   6227 C  CG  . LYS   B 1 240 ? -60.630 12.197  12.593  1.00 20.27 ? 263  LYS   B CG  1 
ATOM   6228 C  CD  . LYS   B 1 240 ? -61.153 10.868  12.054  1.00 25.54 ? 263  LYS   B CD  1 
ATOM   6229 C  CE  . LYS   B 1 240 ? -61.595 10.994  10.645  1.00 30.60 ? 263  LYS   B CE  1 
ATOM   6230 N  NZ  . LYS   B 1 240 ? -61.802 9.675   10.035  1.00 35.25 ? 263  LYS   B NZ  1 
ATOM   6231 N  N   . VAL   B 1 241 ? -61.099 14.418  16.697  1.00 16.91 ? 264  VAL   B N   1 
ATOM   6232 C  CA  . VAL   B 1 241 ? -61.272 14.657  18.107  1.00 18.34 ? 264  VAL   B CA  1 
ATOM   6233 C  C   . VAL   B 1 241 ? -62.765 14.590  18.442  1.00 17.33 ? 264  VAL   B C   1 
ATOM   6234 O  O   . VAL   B 1 241 ? -63.580 15.162  17.729  1.00 15.89 ? 264  VAL   B O   1 
ATOM   6235 C  CB  . VAL   B 1 241 ? -60.671 16.001  18.534  1.00 22.97 ? 264  VAL   B CB  1 
ATOM   6236 C  CG1 . VAL   B 1 241 ? -60.846 16.179  20.025  1.00 24.89 ? 264  VAL   B CG1 1 
ATOM   6237 C  CG2 . VAL   B 1 241 ? -59.195 16.112  18.159  1.00 26.26 ? 264  VAL   B CG2 1 
ATOM   6238 N  N   . THR   B 1 242 ? -63.095 13.845  19.501  1.00 16.75 ? 265  THR   B N   1 
ATOM   6239 C  CA  . THR   B 1 242 ? -64.384 14.002  20.157  1.00 15.91 ? 265  THR   B CA  1 
ATOM   6240 C  C   . THR   B 1 242 ? -64.159 14.343  21.622  1.00 15.17 ? 265  THR   B C   1 
ATOM   6241 O  O   . THR   B 1 242 ? -63.615 13.545  22.394  1.00 14.70 ? 265  THR   B O   1 
ATOM   6242 C  CB  . THR   B 1 242 ? -65.276 12.765  19.997  1.00 15.41 ? 265  THR   B CB  1 
ATOM   6243 O  OG1 . THR   B 1 242 ? -65.257 12.280  18.658  1.00 15.87 ? 265  THR   B OG1 1 
ATOM   6244 C  CG2 . THR   B 1 242 ? -66.715 13.113  20.332  1.00 16.08 ? 265  THR   B CG2 1 
ATOM   6245 N  N   . VAL   B 1 243 ? -64.640 15.535  22.009  1.00 14.94 ? 266  VAL   B N   1 
ATOM   6246 C  CA  . VAL   B 1 243 ? -64.589 16.002  23.376  1.00 16.10 ? 266  VAL   B CA  1 
ATOM   6247 C  C   . VAL   B 1 243 ? -65.917 15.619  24.024  1.00 16.95 ? 266  VAL   B C   1 
ATOM   6248 O  O   . VAL   B 1 243 ? -66.952 15.894  23.433  1.00 19.09 ? 266  VAL   B O   1 
ATOM   6249 C  CB  . VAL   B 1 243 ? -64.428 17.538  23.361  1.00 18.67 ? 266  VAL   B CB  1 
ATOM   6250 C  CG1 . VAL   B 1 243 ? -64.427 18.093  24.770  1.00 19.85 ? 266  VAL   B CG1 1 
ATOM   6251 C  CG2 . VAL   B 1 243 ? -63.215 18.001  22.551  1.00 19.36 ? 266  VAL   B CG2 1 
ATOM   6252 N  N   . ARG   B 1 244 ? -65.877 15.009  25.198  1.00 17.91 ? 267  ARG   B N   1 
ATOM   6253 C  CA  . ARG   B 1 244 ? -67.073 14.530  25.865  1.00 18.19 ? 267  ARG   B CA  1 
ATOM   6254 C  C   . ARG   B 1 244 ? -67.000 14.913  27.339  1.00 18.53 ? 267  ARG   B C   1 
ATOM   6255 O  O   . ARG   B 1 244 ? -65.937 15.005  27.945  1.00 18.56 ? 267  ARG   B O   1 
ATOM   6256 C  CB  . ARG   B 1 244 ? -67.272 13.008  25.715  1.00 16.84 ? 267  ARG   B CB  1 
ATOM   6257 C  CG  . ARG   B 1 244 ? -67.257 12.523  24.273  1.00 15.51 ? 267  ARG   B CG  1 
ATOM   6258 C  CD  . ARG   B 1 244 ? -67.439 11.016  24.181  1.00 15.11 ? 267  ARG   B CD  1 
ATOM   6259 N  NE  . ARG   B 1 244 ? -67.423 10.452  22.834  1.00 14.23 ? 267  ARG   B NE  1 
ATOM   6260 C  CZ  . ARG   B 1 244 ? -68.468 10.360  22.019  1.00 16.67 ? 267  ARG   B CZ  1 
ATOM   6261 N  NH1 . ARG   B 1 244 ? -69.659 10.843  22.374  1.00 15.62 ? 267  ARG   B NH1 1 
ATOM   6262 N  NH2 . ARG   B 1 244 ? -68.306 9.790   20.831  1.00 18.13 ? 267  ARG   B NH2 1 
ATOM   6263 N  N   . GLY   B 1 245 ? -68.151 15.142  27.963  1.00 18.39 ? 268  GLY   B N   1 
ATOM   6264 C  CA  . GLY   B 1 245 ? -68.103 15.328  29.399  1.00 19.45 ? 268  GLY   B CA  1 
ATOM   6265 C  C   . GLY   B 1 245 ? -69.477 15.508  30.027  1.00 20.66 ? 268  GLY   B C   1 
ATOM   6266 O  O   . GLY   B 1 245 ? -70.475 15.022  29.493  1.00 20.93 ? 268  GLY   B O   1 
ATOM   6267 N  N   . ALA   B 1 246 ? -69.480 16.201  31.174  1.00 20.02 ? 269  ALA   B N   1 
ATOM   6268 C  CA  . ALA   B 1 246 ? -70.665 16.402  31.989  1.00 20.42 ? 269  ALA   B CA  1 
ATOM   6269 C  C   . ALA   B 1 246 ? -71.101 17.859  31.883  1.00 22.11 ? 269  ALA   B C   1 
ATOM   6270 O  O   . ALA   B 1 246 ? -70.311 18.743  32.179  1.00 22.01 ? 269  ALA   B O   1 
ATOM   6271 C  CB  . ALA   B 1 246 ? -70.349 16.020  33.405  1.00 19.62 ? 269  ALA   B CB  1 
ATOM   6272 N  N   . GLY   B 1 247 ? -72.325 18.118  31.410  1.00 22.81 ? 270  GLY   B N   1 
ATOM   6273 C  CA  . GLY   B 1 247 ? -72.840 19.482  31.349  1.00 22.97 ? 270  GLY   B CA  1 
ATOM   6274 C  C   . GLY   B 1 247 ? -72.331 20.312  30.168  1.00 24.28 ? 270  GLY   B C   1 
ATOM   6275 O  O   . GLY   B 1 247 ? -72.587 21.517  30.109  1.00 26.23 ? 270  GLY   B O   1 
ATOM   6276 N  N   . ILE   B 1 248 ? -71.658 19.702  29.187  1.00 23.09 ? 271  ILE   B N   1 
ATOM   6277 C  CA  . ILE   B 1 248 ? -71.001 20.472  28.142  1.00 23.52 ? 271  ILE   B CA  1 
ATOM   6278 C  C   . ILE   B 1 248 ? -71.525 20.132  26.746  1.00 23.63 ? 271  ILE   B C   1 
ATOM   6279 O  O   . ILE   B 1 248 ? -70.993 20.604  25.748  1.00 20.52 ? 271  ILE   B O   1 
ATOM   6280 C  CB  . ILE   B 1 248 ? -69.465 20.331  28.239  1.00 25.72 ? 271  ILE   B CB  1 
ATOM   6281 C  CG1 . ILE   B 1 248 ? -68.992 18.872  28.267  1.00 26.42 ? 271  ILE   B CG1 1 
ATOM   6282 C  CG2 . ILE   B 1 248 ? -68.931 21.093  29.453  1.00 23.69 ? 271  ILE   B CG2 1 
ATOM   6283 C  CD1 . ILE   B 1 248 ? -67.492 18.727  28.055  1.00 28.52 ? 271  ILE   B CD1 1 
ATOM   6284 N  N   . SER   B 1 249 ? -72.609 19.358  26.650  1.00 26.12 ? 272  SER   B N   1 
ATOM   6285 C  CA  . SER   B 1 249 ? -73.139 19.010  25.341  1.00 25.61 ? 272  SER   B CA  1 
ATOM   6286 C  C   . SER   B 1 249 ? -73.626 20.242  24.571  1.00 29.10 ? 272  SER   B C   1 
ATOM   6287 O  O   . SER   B 1 249 ? -73.625 20.263  23.343  1.00 32.64 ? 272  SER   B O   1 
ATOM   6288 C  CB  . SER   B 1 249 ? -74.241 17.991  25.449  1.00 25.87 ? 272  SER   B CB  1 
ATOM   6289 O  OG  . SER   B 1 249 ? -75.398 18.581  26.019  1.00 28.06 ? 272  SER   B OG  1 
ATOM   6290 N  N   . GLY   B 1 250 ? -74.022 21.300  25.258  1.00 30.43 ? 273  GLY   B N   1 
ATOM   6291 C  CA  . GLY   B 1 250 ? -74.420 22.482  24.505  1.00 39.38 ? 273  GLY   B CA  1 
ATOM   6292 C  C   . GLY   B 1 250 ? -73.255 23.166  23.772  1.00 40.63 ? 273  GLY   B C   1 
ATOM   6293 O  O   . GLY   B 1 250 ? -73.471 23.890  22.798  1.00 45.08 ? 273  GLY   B O   1 
ATOM   6294 N  N   . HIS   B 1 251 ? -72.017 22.910  24.210  1.00 37.33 ? 274  HIS   B N   1 
ATOM   6295 C  CA  . HIS   B 1 251 ? -70.933 23.861  24.013  1.00 32.97 ? 274  HIS   B CA  1 
ATOM   6296 C  C   . HIS   B 1 251 ? -70.086 23.506  22.797  1.00 31.78 ? 274  HIS   B C   1 
ATOM   6297 O  O   . HIS   B 1 251 ? -70.173 22.399  22.276  1.00 28.32 ? 274  HIS   B O   1 
ATOM   6298 C  CB  . HIS   B 1 251 ? -70.019 23.886  25.237  1.00 34.85 ? 274  HIS   B CB  1 
ATOM   6299 C  CG  . HIS   B 1 251 ? -70.736 24.065  26.525  1.00 41.98 ? 274  HIS   B CG  1 
ATOM   6300 N  ND1 . HIS   B 1 251 ? -72.087 23.830  26.688  1.00 49.22 ? 274  HIS   B ND1 1 
ATOM   6301 C  CD2 . HIS   B 1 251 ? -70.274 24.454  27.727  1.00 47.37 ? 274  HIS   B CD2 1 
ATOM   6302 C  CE1 . HIS   B 1 251 ? -72.418 24.075  27.951  1.00 49.96 ? 274  HIS   B CE1 1 
ATOM   6303 N  NE2 . HIS   B 1 251 ? -71.326 24.436  28.607  1.00 44.74 ? 274  HIS   B NE2 1 
ATOM   6304 N  N   . GLN   B 1 252 ? -69.268 24.484  22.375  1.00 27.64 ? 275  GLN   B N   1 
ATOM   6305 C  CA  . GLN   B 1 252 ? -68.174 24.289  21.443  1.00 28.41 ? 275  GLN   B CA  1 
ATOM   6306 C  C   . GLN   B 1 252 ? -66.918 24.013  22.266  1.00 26.37 ? 275  GLN   B C   1 
ATOM   6307 O  O   . GLN   B 1 252 ? -66.863 24.333  23.459  1.00 28.36 ? 275  GLN   B O   1 
ATOM   6308 C  CB  . GLN   B 1 252 ? -67.973 25.518  20.557  1.00 31.13 ? 275  GLN   B CB  1 
ATOM   6309 C  CG  . GLN   B 1 252 ? -69.079 25.763  19.535  1.00 33.78 ? 275  GLN   B CG  1 
ATOM   6310 C  CD  . GLN   B 1 252 ? -68.907 24.992  18.243  1.00 37.74 ? 275  GLN   B CD  1 
ATOM   6311 O  OE1 . GLN   B 1 252 ? -69.827 24.321  17.774  1.00 43.04 ? 275  GLN   B OE1 1 
ATOM   6312 N  NE2 . GLN   B 1 252 ? -67.745 25.100  17.617  1.00 39.75 ? 275  GLN   B NE2 1 
ATOM   6313 N  N   . ALA   B 1 253 ? -65.916 23.395  21.627  1.00 24.94 ? 276  ALA   B N   1 
ATOM   6314 C  CA  . ALA   B 1 253 ? -64.646 23.158  22.290  1.00 26.25 ? 276  ALA   B CA  1 
ATOM   6315 C  C   . ALA   B 1 253 ? -63.488 23.581  21.381  1.00 21.50 ? 276  ALA   B C   1 
ATOM   6316 O  O   . ALA   B 1 253 ? -63.594 23.505  20.155  1.00 22.23 ? 276  ALA   B O   1 
ATOM   6317 C  CB  . ALA   B 1 253 ? -64.547 21.700  22.726  1.00 25.83 ? 276  ALA   B CB  1 
ATOM   6318 N  N   . ARG   B 1 254 ? -62.418 24.093  21.997  1.00 21.36 ? 277  ARG   B N   1 
ATOM   6319 C  CA  . ARG   B 1 254 ? -61.176 24.345  21.273  1.00 22.10 ? 277  ARG   B CA  1 
ATOM   6320 C  C   . ARG   B 1 254 ? -60.208 23.195  21.552  1.00 20.98 ? 277  ARG   B C   1 
ATOM   6321 O  O   . ARG   B 1 254 ? -59.958 22.841  22.711  1.00 20.95 ? 277  ARG   B O   1 
ATOM   6322 C  CB  . ARG   B 1 254 ? -60.451 25.661  21.589  1.00 23.70 ? 277  ARG   B CB  1 
ATOM   6323 C  CG  . ARG   B 1 254 ? -59.206 25.749  20.704  1.00 27.95 ? 277  ARG   B CG  1 
ATOM   6324 C  CD  . ARG   B 1 254 ? -58.548 27.114  20.604  1.00 29.43 ? 277  ARG   B CD  1 
ATOM   6325 N  NE  . ARG   B 1 254 ? -59.421 28.107  19.967  1.00 30.64 ? 277  ARG   B NE  1 
ATOM   6326 C  CZ  . ARG   B 1 254 ? -59.388 28.496  18.705  1.00 30.80 ? 277  ARG   B CZ  1 
ATOM   6327 N  NH1 . ARG   B 1 254 ? -58.565 27.908  17.842  1.00 30.06 ? 277  ARG   B NH1 1 
ATOM   6328 N  NH2 . ARG   B 1 254 ? -60.217 29.455  18.316  1.00 26.98 ? 277  ARG   B NH2 1 
ATOM   6329 N  N   . VAL   B 1 255 ? -59.645 22.633  20.481  1.00 21.77 ? 278  VAL   B N   1 
ATOM   6330 C  CA  . VAL   B 1 255 ? -58.631 21.600  20.639  1.00 21.68 ? 278  VAL   B CA  1 
ATOM   6331 C  C   . VAL   B 1 255 ? -57.380 22.006  19.866  1.00 19.92 ? 278  VAL   B C   1 
ATOM   6332 O  O   . VAL   B 1 255 ? -57.476 22.321  18.688  1.00 20.98 ? 278  VAL   B O   1 
ATOM   6333 C  CB  . VAL   B 1 255 ? -59.150 20.218  20.207  1.00 23.93 ? 278  VAL   B CB  1 
ATOM   6334 C  CG1 . VAL   B 1 255 ? -58.052 19.158  20.297  1.00 25.20 ? 278  VAL   B CG1 1 
ATOM   6335 C  CG2 . VAL   B 1 255 ? -60.355 19.810  21.061  1.00 25.78 ? 278  VAL   B CG2 1 
ATOM   6336 N  N   . THR   B 1 256 ? -56.235 21.958  20.572  1.00 20.27 ? 279  THR   B N   1 
ATOM   6337 C  CA  . THR   B 1 256 ? -54.943 22.394  20.070  1.00 22.17 ? 279  THR   B CA  1 
ATOM   6338 C  C   . THR   B 1 256 ? -53.896 21.283  20.222  1.00 20.05 ? 279  THR   B C   1 
ATOM   6339 O  O   . THR   B 1 256 ? -53.626 20.757  21.299  1.00 18.24 ? 279  THR   B O   1 
ATOM   6340 C  CB  . THR   B 1 256 ? -54.515 23.660  20.813  1.00 23.70 ? 279  THR   B CB  1 
ATOM   6341 O  OG1 . THR   B 1 256 ? -55.589 24.585  20.627  1.00 24.96 ? 279  THR   B OG1 1 
ATOM   6342 C  CG2 . THR   B 1 256 ? -53.220 24.224  20.251  1.00 23.39 ? 279  THR   B CG2 1 
ATOM   6343 N  N   . VAL   B 1 257 ? -53.275 20.973  19.094  1.00 19.58 ? 280  VAL   B N   1 
ATOM   6344 C  CA  . VAL   B 1 257 ? -52.132 20.090  19.044  1.00 18.56 ? 280  VAL   B CA  1 
ATOM   6345 C  C   . VAL   B 1 257 ? -50.852 20.909  18.925  1.00 20.02 ? 280  VAL   B C   1 
ATOM   6346 O  O   . VAL   B 1 257 ? -50.750 21.746  18.033  1.00 18.74 ? 280  VAL   B O   1 
ATOM   6347 C  CB  . VAL   B 1 257 ? -52.243 19.193  17.813  1.00 17.57 ? 280  VAL   B CB  1 
ATOM   6348 C  CG1 . VAL   B 1 257 ? -51.053 18.249  17.746  1.00 17.88 ? 280  VAL   B CG1 1 
ATOM   6349 C  CG2 . VAL   B 1 257 ? -53.576 18.439  17.773  1.00 18.17 ? 280  VAL   B CG2 1 
ATOM   6350 N  N   . SER   B 1 258 ? -49.861 20.553  19.737  1.00 21.42 ? 281  SER   B N   1 
ATOM   6351 C  CA  . SER   B 1 258 ? -48.587 21.256  19.754  1.00 21.84 ? 281  SER   B CA  1 
ATOM   6352 C  C   . SER   B 1 258 ? -47.449 20.261  19.989  1.00 22.50 ? 281  SER   B C   1 
ATOM   6353 O  O   . SER   B 1 258 ? -47.671 19.089  20.333  1.00 19.57 ? 281  SER   B O   1 
ATOM   6354 C  CB  . SER   B 1 258 ? -48.605 22.331  20.811  1.00 21.21 ? 281  SER   B CB  1 
ATOM   6355 O  OG  . SER   B 1 258 ? -48.769 21.777  22.119  1.00 20.61 ? 281  SER   B OG  1 
ATOM   6356 N  N   . THR   B 1 259 ? -46.217 20.745  19.754  1.00 21.61 ? 282  THR   B N   1 
ATOM   6357 C  CA  . THR   B 1 259 ? -45.014 20.057  20.193  1.00 21.57 ? 282  THR   B CA  1 
ATOM   6358 C  C   . THR   B 1 259 ? -43.974 21.084  20.620  1.00 23.01 ? 282  THR   B C   1 
ATOM   6359 O  O   . THR   B 1 259 ? -43.741 22.045  19.881  1.00 27.16 ? 282  THR   B O   1 
ATOM   6360 C  CB  . THR   B 1 259 ? -44.484 19.170  19.066  1.00 21.88 ? 282  THR   B CB  1 
ATOM   6361 O  OG1 . THR   B 1 259 ? -43.313 18.602  19.635  1.00 19.84 ? 282  THR   B OG1 1 
ATOM   6362 C  CG2 . THR   B 1 259 ? -44.145 19.905  17.786  1.00 24.39 ? 282  THR   B CG2 1 
ATOM   6363 N  N   . GLY   B 1 260 ? -43.364 20.845  21.787  1.00 23.24 ? 283  GLY   B N   1 
ATOM   6364 C  CA  . GLY   B 1 260 ? -42.474 21.799  22.438  1.00 28.30 ? 283  GLY   B CA  1 
ATOM   6365 C  C   . GLY   B 1 260 ? -43.004 23.239  22.445  1.00 30.62 ? 283  GLY   B C   1 
ATOM   6366 O  O   . GLY   B 1 260 ? -42.235 24.187  22.284  1.00 31.64 ? 283  GLY   B O   1 
ATOM   6367 N  N   . GLY   B 1 261 ? -44.312 23.418  22.658  1.00 26.19 ? 284  GLY   B N   1 
ATOM   6368 C  CA  . GLY   B 1 261 ? -44.878 24.743  22.835  1.00 27.25 ? 284  GLY   B CA  1 
ATOM   6369 C  C   . GLY   B 1 261 ? -45.181 25.443  21.515  1.00 25.16 ? 284  GLY   B C   1 
ATOM   6370 O  O   . GLY   B 1 261 ? -45.692 26.566  21.551  1.00 30.12 ? 284  GLY   B O   1 
ATOM   6371 N  N   . THR   B 1 262 ? -44.875 24.794  20.376  1.00 24.58 ? 285  THR   B N   1 
ATOM   6372 C  CA  . THR   B 1 262 ? -45.271 25.263  19.052  1.00 25.60 ? 285  THR   B CA  1 
ATOM   6373 C  C   . THR   B 1 262 ? -46.601 24.623  18.648  1.00 28.87 ? 285  THR   B C   1 
ATOM   6374 O  O   . THR   B 1 262 ? -46.693 23.399  18.509  1.00 25.90 ? 285  THR   B O   1 
ATOM   6375 C  CB  . THR   B 1 262 ? -44.244 24.960  17.961  1.00 27.58 ? 285  THR   B CB  1 
ATOM   6376 O  OG1 . THR   B 1 262 ? -42.978 25.509  18.307  1.00 27.15 ? 285  THR   B OG1 1 
ATOM   6377 C  CG2 . THR   B 1 262 ? -44.641 25.573  16.632  1.00 26.94 ? 285  THR   B CG2 1 
ATOM   6378 N  N   . THR   B 1 263 ? -47.605 25.479  18.421  1.00 27.53 ? 286  THR   B N   1 
ATOM   6379 C  CA  . THR   B 1 263 ? -48.905 25.050  17.932  1.00 27.30 ? 286  THR   B CA  1 
ATOM   6380 C  C   . THR   B 1 263 ? -48.761 24.564  16.498  1.00 27.35 ? 286  THR   B C   1 
ATOM   6381 O  O   . THR   B 1 263 ? -48.282 25.265  15.615  1.00 27.62 ? 286  THR   B O   1 
ATOM   6382 C  CB  . THR   B 1 263 ? -49.921 26.192  18.012  1.00 27.15 ? 286  THR   B CB  1 
ATOM   6383 O  OG1 . THR   B 1 263 ? -50.021 26.401  19.411  1.00 25.78 ? 286  THR   B OG1 1 
ATOM   6384 C  CG2 . THR   B 1 263 ? -51.265 25.847  17.394  1.00 30.23 ? 286  THR   B CG2 1 
ATOM   6385 N  N   . VAL   B 1 264 ? -49.256 23.353  16.262  1.00 24.03 ? 287  VAL   B N   1 
ATOM   6386 C  CA  . VAL   B 1 264 ? -49.199 22.729  14.964  1.00 23.44 ? 287  VAL   B CA  1 
ATOM   6387 C  C   . VAL   B 1 264 ? -50.535 22.895  14.259  1.00 22.24 ? 287  VAL   B C   1 
ATOM   6388 O  O   . VAL   B 1 264 ? -50.600 23.105  13.051  1.00 21.98 ? 287  VAL   B O   1 
ATOM   6389 C  CB  . VAL   B 1 264 ? -48.831 21.271  15.331  1.00 30.80 ? 287  VAL   B CB  1 
ATOM   6390 C  CG1 . VAL   B 1 264 ? -49.110 20.289  14.207  1.00 32.51 ? 287  VAL   B CG1 1 
ATOM   6391 C  CG2 . VAL   B 1 264 ? -47.391 21.183  15.835  1.00 31.88 ? 287  VAL   B CG2 1 
ATOM   6392 N  N   . GLY   B 1 265 ? -51.614 22.748  15.031  1.00 22.77 ? 288  GLY   B N   1 
ATOM   6393 C  CA  . GLY   B 1 265 ? -52.962 22.923  14.532  1.00 21.80 ? 288  GLY   B CA  1 
ATOM   6394 C  C   . GLY   B 1 265 ? -53.915 23.242  15.679  1.00 20.29 ? 288  GLY   B C   1 
ATOM   6395 O  O   . GLY   B 1 265 ? -53.677 22.871  16.837  1.00 19.40 ? 288  GLY   B O   1 
ATOM   6396 N  N   . THR   B 1 266 ? -54.979 23.969  15.341  1.00 21.91 ? 289  THR   B N   1 
ATOM   6397 C  CA  . THR   B 1 266 ? -56.042 24.254  16.292  1.00 23.47 ? 289  THR   B CA  1 
ATOM   6398 C  C   . THR   B 1 266 ? -57.389 24.258  15.564  1.00 24.28 ? 289  THR   B C   1 
ATOM   6399 O  O   . THR   B 1 266 ? -57.446 24.571  14.371  1.00 25.90 ? 289  THR   B O   1 
ATOM   6400 C  CB  . THR   B 1 266 ? -55.765 25.591  16.973  1.00 26.20 ? 289  THR   B CB  1 
ATOM   6401 O  OG1 . THR   B 1 266 ? -56.704 25.573  18.042  1.00 26.76 ? 289  THR   B OG1 1 
ATOM   6402 C  CG2 . THR   B 1 266 ? -55.884 26.772  16.017  1.00 25.52 ? 289  THR   B CG2 1 
ATOM   6403 N  N   . ALA   B 1 267 ? -58.465 23.897  16.288  1.00 23.20 ? 290  ALA   B N   1 
ATOM   6404 C  CA  . ALA   B 1 267 ? -59.814 24.015  15.759  1.00 22.58 ? 290  ALA   B CA  1 
ATOM   6405 C  C   . ALA   B 1 267 ? -60.806 24.030  16.906  1.00 23.04 ? 290  ALA   B C   1 
ATOM   6406 O  O   . ALA   B 1 267 ? -60.478 23.657  18.039  1.00 25.16 ? 290  ALA   B O   1 
ATOM   6407 C  CB  . ALA   B 1 267 ? -60.116 22.913  14.770  1.00 22.19 ? 290  ALA   B CB  1 
ATOM   6408 N  N   . THR   B 1 268 ? -61.971 24.618  16.611  1.00 26.61 ? 291  THR   B N   1 
ATOM   6409 C  CA  . THR   B 1 268 ? -63.115 24.573  17.504  1.00 26.07 ? 291  THR   B CA  1 
ATOM   6410 C  C   . THR   B 1 268 ? -64.198 23.786  16.794  1.00 25.46 ? 291  THR   B C   1 
ATOM   6411 O  O   . THR   B 1 268 ? -64.282 23.726  15.561  1.00 24.53 ? 291  THR   B O   1 
ATOM   6412 C  CB  . THR   B 1 268 ? -63.613 25.958  17.916  1.00 31.33 ? 291  THR   B CB  1 
ATOM   6413 O  OG1 . THR   B 1 268 ? -64.025 26.523  16.671  1.00 34.23 ? 291  THR   B OG1 1 
ATOM   6414 C  CG2 . THR   B 1 268 ? -62.560 26.771  18.658  1.00 31.32 ? 291  THR   B CG2 1 
ATOM   6415 N  N   . GLY   B 1 269 ? -64.985 23.118  17.624  1.00 24.44 ? 292  GLY   B N   1 
ATOM   6416 C  CA  . GLY   B 1 269 ? -66.039 22.280  17.108  1.00 23.87 ? 292  GLY   B CA  1 
ATOM   6417 C  C   . GLY   B 1 269 ? -66.970 21.916  18.241  1.00 20.22 ? 292  GLY   B C   1 
ATOM   6418 O  O   . GLY   B 1 269 ? -66.751 22.290  19.395  1.00 20.70 ? 292  GLY   B O   1 
ATOM   6419 N  N   . PRO   B 1 270 ? -68.066 21.230  17.892  1.00 22.84 ? 293  PRO   B N   1 
ATOM   6420 C  CA  . PRO   B 1 270 ? -69.102 20.870  18.852  1.00 23.96 ? 293  PRO   B CA  1 
ATOM   6421 C  C   . PRO   B 1 270 ? -68.626 19.763  19.786  1.00 23.39 ? 293  PRO   B C   1 
ATOM   6422 O  O   . PRO   B 1 270 ? -68.058 18.786  19.311  1.00 23.35 ? 293  PRO   B O   1 
ATOM   6423 C  CB  . PRO   B 1 270 ? -70.257 20.413  17.938  1.00 26.41 ? 293  PRO   B CB  1 
ATOM   6424 C  CG  . PRO   B 1 270 ? -69.622 20.005  16.642  1.00 27.19 ? 293  PRO   B CG  1 
ATOM   6425 C  CD  . PRO   B 1 270 ? -68.370 20.837  16.503  1.00 27.25 ? 293  PRO   B CD  1 
ATOM   6426 N  N   . VAL   B 1 271 ? -68.912 19.920  21.078  1.00 21.95 ? 294  VAL   B N   1 
ATOM   6427 C  CA  . VAL   B 1 271 ? -68.740 18.862  22.060  1.00 24.02 ? 294  VAL   B CA  1 
ATOM   6428 C  C   . VAL   B 1 271 ? -69.671 17.703  21.680  1.00 22.78 ? 294  VAL   B C   1 
ATOM   6429 O  O   . VAL   B 1 271 ? -70.798 17.922  21.250  1.00 24.62 ? 294  VAL   B O   1 
ATOM   6430 C  CB  . VAL   B 1 271 ? -69.016 19.363  23.490  1.00 23.52 ? 294  VAL   B CB  1 
ATOM   6431 C  CG1 . VAL   B 1 271 ? -69.189 18.237  24.492  1.00 26.02 ? 294  VAL   B CG1 1 
ATOM   6432 C  CG2 . VAL   B 1 271 ? -67.935 20.317  23.983  1.00 23.88 ? 294  VAL   B CG2 1 
ATOM   6433 N  N   . GLY   B 1 272 ? -69.165 16.467  21.795  1.00 21.96 ? 295  GLY   B N   1 
ATOM   6434 C  CA  . GLY   B 1 272 ? -69.953 15.269  21.578  1.00 19.44 ? 295  GLY   B CA  1 
ATOM   6435 C  C   . GLY   B 1 272 ? -70.016 14.859  20.109  1.00 19.74 ? 295  GLY   B C   1 
ATOM   6436 O  O   . GLY   B 1 272 ? -70.603 13.825  19.782  1.00 18.53 ? 295  GLY   B O   1 
ATOM   6437 N  N   . THR   B 1 273 ? -69.416 15.657  19.218  1.00 19.07 ? 296  THR   B N   1 
ATOM   6438 C  CA  . THR   B 1 273 ? -69.402 15.309  17.802  1.00 20.77 ? 296  THR   B CA  1 
ATOM   6439 C  C   . THR   B 1 273 ? -67.952 15.326  17.316  1.00 21.60 ? 296  THR   B C   1 
ATOM   6440 O  O   . THR   B 1 273 ? -67.247 16.278  17.590  1.00 20.00 ? 296  THR   B O   1 
ATOM   6441 C  CB  . THR   B 1 273 ? -70.251 16.309  17.014  1.00 22.95 ? 296  THR   B CB  1 
ATOM   6442 O  OG1 . THR   B 1 273 ? -71.596 16.071  17.422  1.00 28.54 ? 296  THR   B OG1 1 
ATOM   6443 C  CG2 . THR   B 1 273 ? -70.100 16.144  15.510  1.00 25.36 ? 296  THR   B CG2 1 
ATOM   6444 N  N   . GLU   B 1 274 ? -67.547 14.317  16.545  1.00 21.95 ? 297  GLU   B N   1 
ATOM   6445 C  CA  . GLU   B 1 274 ? -66.194 14.269  16.019  1.00 21.00 ? 297  GLU   B CA  1 
ATOM   6446 C  C   . GLU   B 1 274 ? -65.956 15.467  15.095  1.00 22.84 ? 297  GLU   B C   1 
ATOM   6447 O  O   . GLU   B 1 274 ? -66.747 15.721  14.181  1.00 23.43 ? 297  GLU   B O   1 
ATOM   6448 C  CB  . GLU   B 1 274 ? -65.959 12.965  15.261  1.00 21.90 ? 297  GLU   B CB  1 
ATOM   6449 C  CG  . GLU   B 1 274 ? -64.512 12.745  14.825  1.00 21.11 ? 297  GLU   B CG  1 
ATOM   6450 C  CD  . GLU   B 1 274 ? -64.249 11.313  14.417  1.00 21.77 ? 297  GLU   B CD  1 
ATOM   6451 O  OE1 . GLU   B 1 274 ? -64.652 11.035  13.277  1.00 23.82 ? 297  GLU   B OE1 1 
ATOM   6452 O  OE2 . GLU   B 1 274 ? -63.689 10.490  15.188  1.00 20.68 ? 297  GLU   B OE2 1 
ATOM   6453 N  N   . PHE   B 1 275 ? -64.836 16.166  15.310  1.00 21.27 ? 298  PHE   B N   1 
ATOM   6454 C  CA  . PHE   B 1 275 ? -64.348 17.163  14.364  1.00 19.79 ? 298  PHE   B CA  1 
ATOM   6455 C  C   . PHE   B 1 275 ? -62.844 16.973  14.183  1.00 21.23 ? 298  PHE   B C   1 
ATOM   6456 O  O   . PHE   B 1 275 ? -62.246 16.090  14.806  1.00 20.73 ? 298  PHE   B O   1 
ATOM   6457 C  CB  . PHE   B 1 275 ? -64.741 18.587  14.792  1.00 20.35 ? 298  PHE   B CB  1 
ATOM   6458 C  CG  . PHE   B 1 275 ? -64.167 19.102  16.101  1.00 18.45 ? 298  PHE   B CG  1 
ATOM   6459 C  CD1 . PHE   B 1 275 ? -64.781 18.807  17.312  1.00 19.01 ? 298  PHE   B CD1 1 
ATOM   6460 C  CD2 . PHE   B 1 275 ? -63.037 19.923  16.115  1.00 18.22 ? 298  PHE   B CD2 1 
ATOM   6461 C  CE1 . PHE   B 1 275 ? -64.292 19.299  18.512  1.00 17.35 ? 298  PHE   B CE1 1 
ATOM   6462 C  CE2 . PHE   B 1 275 ? -62.532 20.388  17.313  1.00 18.63 ? 298  PHE   B CE2 1 
ATOM   6463 C  CZ  . PHE   B 1 275 ? -63.162 20.095  18.502  1.00 19.28 ? 298  PHE   B CZ  1 
ATOM   6464 N  N   . THR   B 1 276 ? -62.249 17.756  13.270  1.00 21.37 ? 299  THR   B N   1 
ATOM   6465 C  CA  . THR   B 1 276 ? -60.840 17.558  12.935  1.00 21.36 ? 299  THR   B CA  1 
ATOM   6466 C  C   . THR   B 1 276 ? -60.016 18.785  13.306  1.00 21.72 ? 299  THR   B C   1 
ATOM   6467 O  O   . THR   B 1 276 ? -60.503 19.918  13.299  1.00 21.06 ? 299  THR   B O   1 
ATOM   6468 C  CB  . THR   B 1 276 ? -60.621 17.207  11.469  1.00 23.44 ? 299  THR   B CB  1 
ATOM   6469 O  OG1 . THR   B 1 276 ? -61.029 18.345  10.727  1.00 24.19 ? 299  THR   B OG1 1 
ATOM   6470 C  CG2 . THR   B 1 276 ? -61.391 15.971  11.041  1.00 24.11 ? 299  THR   B CG2 1 
ATOM   6471 N  N   . VAL   B 1 277 ? -58.771 18.503  13.698  1.00 20.92 ? 300  VAL   B N   1 
ATOM   6472 C  CA  . VAL   B 1 277 ? -57.768 19.511  14.004  1.00 20.89 ? 300  VAL   B CA  1 
ATOM   6473 C  C   . VAL   B 1 277 ? -56.608 19.268  13.047  1.00 20.26 ? 300  VAL   B C   1 
ATOM   6474 O  O   . VAL   B 1 277 ? -56.166 18.119  12.939  1.00 20.02 ? 300  VAL   B O   1 
ATOM   6475 C  CB  . VAL   B 1 277 ? -57.276 19.431  15.460  1.00 20.88 ? 300  VAL   B CB  1 
ATOM   6476 C  CG1 . VAL   B 1 277 ? -56.194 20.453  15.772  1.00 21.54 ? 300  VAL   B CG1 1 
ATOM   6477 C  CG2 . VAL   B 1 277 ? -58.380 19.537  16.489  1.00 21.18 ? 300  VAL   B CG2 1 
ATOM   6478 N  N   . PRO   B 1 278 ? -56.067 20.302  12.350  1.00 21.93 ? 301  PRO   B N   1 
ATOM   6479 C  CA  . PRO   B 1 278 ? -54.902 20.122  11.481  1.00 21.55 ? 301  PRO   B CA  1 
ATOM   6480 C  C   . PRO   B 1 278 ? -53.672 19.612  12.224  1.00 21.16 ? 301  PRO   B C   1 
ATOM   6481 O  O   . PRO   B 1 278 ? -53.387 20.047  13.328  1.00 19.84 ? 301  PRO   B O   1 
ATOM   6482 C  CB  . PRO   B 1 278 ? -54.619 21.517  10.888  1.00 23.01 ? 301  PRO   B CB  1 
ATOM   6483 C  CG  . PRO   B 1 278 ? -55.926 22.258  11.046  1.00 23.02 ? 301  PRO   B CG  1 
ATOM   6484 C  CD  . PRO   B 1 278 ? -56.558 21.692  12.319  1.00 23.06 ? 301  PRO   B CD  1 
ATOM   6485 N  N   . VAL   B 1 279 ? -52.930 18.712  11.574  1.00 20.19 ? 302  VAL   B N   1 
ATOM   6486 C  CA  . VAL   B 1 279 ? -51.632 18.295  12.070  1.00 20.59 ? 302  VAL   B CA  1 
ATOM   6487 C  C   . VAL   B 1 279 ? -50.735 18.216  10.846  1.00 22.56 ? 302  VAL   B C   1 
ATOM   6488 O  O   . VAL   B 1 279 ? -50.542 17.146  10.291  1.00 23.86 ? 302  VAL   B O   1 
ATOM   6489 C  CB  . VAL   B 1 279 ? -51.628 16.971  12.867  1.00 22.43 ? 302  VAL   B CB  1 
ATOM   6490 C  CG1 . VAL   B 1 279 ? -50.237 16.690  13.473  1.00 21.66 ? 302  VAL   B CG1 1 
ATOM   6491 C  CG2 . VAL   B 1 279 ? -52.700 16.945  13.959  1.00 22.23 ? 302  VAL   B CG2 1 
ATOM   6492 N  N   . PRO   B 1 280 ? -50.288 19.369  10.287  1.00 26.08 ? 303  PRO   B N   1 
ATOM   6493 C  CA  . PRO   B 1 280 ? -49.586 19.374  8.998   1.00 26.28 ? 303  PRO   B CA  1 
ATOM   6494 C  C   . PRO   B 1 280 ? -48.250 18.651  9.132   1.00 23.64 ? 303  PRO   B C   1 
ATOM   6495 O  O   . PRO   B 1 280 ? -47.620 18.752  10.169  1.00 19.09 ? 303  PRO   B O   1 
ATOM   6496 C  CB  . PRO   B 1 280 ? -49.404 20.866  8.643   1.00 26.82 ? 303  PRO   B CB  1 
ATOM   6497 C  CG  . PRO   B 1 280 ? -49.583 21.594  9.961   1.00 27.84 ? 303  PRO   B CG  1 
ATOM   6498 C  CD  . PRO   B 1 280 ? -50.501 20.717  10.826  1.00 28.48 ? 303  PRO   B CD  1 
ATOM   6499 N  N   . ASN   B 1 281 ? -47.873 17.896  8.097   1.00 23.68 ? 304  ASN   B N   1 
ATOM   6500 C  CA  . ASN   B 1 281 ? -46.567 17.255  8.063   1.00 26.56 ? 304  ASN   B CA  1 
ATOM   6501 C  C   . ASN   B 1 281 ? -46.333 16.440  9.340   1.00 24.41 ? 304  ASN   B C   1 
ATOM   6502 O  O   . ASN   B 1 281 ? -45.364 16.629  10.089  1.00 23.18 ? 304  ASN   B O   1 
ATOM   6503 C  CB  . ASN   B 1 281 ? -45.493 18.297  7.779   1.00 31.29 ? 304  ASN   B CB  1 
ATOM   6504 C  CG  . ASN   B 1 281 ? -44.191 17.637  7.413   1.00 39.94 ? 304  ASN   B CG  1 
ATOM   6505 O  OD1 . ASN   B 1 281 ? -44.206 16.556  6.812   1.00 44.87 ? 304  ASN   B OD1 1 
ATOM   6506 N  ND2 . ASN   B 1 281 ? -43.071 18.238  7.799   1.00 42.66 ? 304  ASN   B ND2 1 
ATOM   6507 N  N   . PRO   B 1 282 ? -47.230 15.471  9.634   1.00 21.71 ? 305  PRO   B N   1 
ATOM   6508 C  CA  . PRO   B 1 282 ? -47.202 14.793  10.923  1.00 21.98 ? 305  PRO   B CA  1 
ATOM   6509 C  C   . PRO   B 1 282 ? -45.969 13.902  10.989  1.00 19.96 ? 305  PRO   B C   1 
ATOM   6510 O  O   . PRO   B 1 282 ? -45.637 13.256  9.986   1.00 20.07 ? 305  PRO   B O   1 
ATOM   6511 C  CB  . PRO   B 1 282 ? -48.496 13.987  10.985  1.00 22.57 ? 305  PRO   B CB  1 
ATOM   6512 C  CG  . PRO   B 1 282 ? -48.960 13.881  9.563   1.00 21.84 ? 305  PRO   B CG  1 
ATOM   6513 C  CD  . PRO   B 1 282 ? -48.295 14.980  8.752   1.00 22.33 ? 305  PRO   B CD  1 
ATOM   6514 N  N   . ARG   B 1 283 ? -45.323 13.937  12.153  1.00 18.34 ? 306  ARG   B N   1 
ATOM   6515 C  CA  . ARG   B 1 283 ? -44.314 12.968  12.539  1.00 18.65 ? 306  ARG   B CA  1 
ATOM   6516 C  C   . ARG   B 1 283 ? -45.067 11.765  13.116  1.00 18.69 ? 306  ARG   B C   1 
ATOM   6517 O  O   . ARG   B 1 283 ? -45.742 11.908  14.128  1.00 20.08 ? 306  ARG   B O   1 
ATOM   6518 C  CB  . ARG   B 1 283 ? -43.384 13.590  13.583  1.00 20.00 ? 306  ARG   B CB  1 
ATOM   6519 C  CG  . ARG   B 1 283 ? -42.283 12.622  14.004  1.00 20.20 ? 306  ARG   B CG  1 
ATOM   6520 C  CD  . ARG   B 1 283 ? -41.144 13.283  14.695  1.00 21.10 ? 306  ARG   B CD  1 
ATOM   6521 N  NE  . ARG   B 1 283 ? -40.164 12.345  15.257  1.00 19.36 ? 306  ARG   B NE  1 
ATOM   6522 C  CZ  . ARG   B 1 283 ? -39.310 12.721  16.217  1.00 20.16 ? 306  ARG   B CZ  1 
ATOM   6523 N  NH1 . ARG   B 1 283 ? -39.121 14.015  16.455  1.00 20.86 ? 306  ARG   B NH1 1 
ATOM   6524 N  NH2 . ARG   B 1 283 ? -38.662 11.840  16.962  1.00 20.41 ? 306  ARG   B NH2 1 
ATOM   6525 N  N   . LEU   B 1 284 ? -44.932 10.599  12.475  1.00 16.55 ? 307  LEU   B N   1 
ATOM   6526 C  CA  . LEU   B 1 284 ? -45.767 9.448   12.787  1.00 17.63 ? 307  LEU   B CA  1 
ATOM   6527 C  C   . LEU   B 1 284 ? -45.258 8.768   14.040  1.00 16.75 ? 307  LEU   B C   1 
ATOM   6528 O  O   . LEU   B 1 284 ? -44.051 8.768   14.304  1.00 17.84 ? 307  LEU   B O   1 
ATOM   6529 C  CB  . LEU   B 1 284 ? -45.742 8.495   11.600  1.00 18.29 ? 307  LEU   B CB  1 
ATOM   6530 C  CG  . LEU   B 1 284 ? -46.318 9.040   10.303  1.00 19.84 ? 307  LEU   B CG  1 
ATOM   6531 C  CD1 . LEU   B 1 284 ? -46.316 7.983   9.214   1.00 22.07 ? 307  LEU   B CD1 1 
ATOM   6532 C  CD2 . LEU   B 1 284 ? -47.711 9.620   10.535  1.00 20.35 ? 307  LEU   B CD2 1 
ATOM   6533 N  N   . TRP   B 1 285 ? -46.180 8.154   14.787  1.00 14.03 ? 308  TRP   B N   1 
ATOM   6534 C  CA  . TRP   B 1 285 ? -45.809 7.302   15.904  1.00 13.25 ? 308  TRP   B CA  1 
ATOM   6535 C  C   . TRP   B 1 285 ? -45.545 5.889   15.375  1.00 12.97 ? 308  TRP   B C   1 
ATOM   6536 O  O   . TRP   B 1 285 ? -46.319 5.371   14.580  1.00 12.18 ? 308  TRP   B O   1 
ATOM   6537 C  CB  . TRP   B 1 285 ? -46.931 7.321   16.945  1.00 12.21 ? 308  TRP   B CB  1 
ATOM   6538 C  CG  . TRP   B 1 285 ? -46.674 6.542   18.202  1.00 11.06 ? 308  TRP   B CG  1 
ATOM   6539 C  CD1 . TRP   B 1 285 ? -46.337 7.060   19.409  1.00 12.03 ? 308  TRP   B CD1 1 
ATOM   6540 C  CD2 . TRP   B 1 285 ? -46.786 5.113   18.385  1.00 12.09 ? 308  TRP   B CD2 1 
ATOM   6541 N  NE1 . TRP   B 1 285 ? -46.238 6.058   20.334  1.00 13.34 ? 308  TRP   B NE1 1 
ATOM   6542 C  CE2 . TRP   B 1 285 ? -46.498 4.852   19.737  1.00 11.29 ? 308  TRP   B CE2 1 
ATOM   6543 C  CE3 . TRP   B 1 285 ? -47.079 4.035   17.542  1.00 11.62 ? 308  TRP   B CE3 1 
ATOM   6544 C  CZ2 . TRP   B 1 285 ? -46.499 3.570   20.277  1.00 11.68 ? 308  TRP   B CZ2 1 
ATOM   6545 C  CZ3 . TRP   B 1 285 ? -47.101 2.766   18.077  1.00 12.17 ? 308  TRP   B CZ3 1 
ATOM   6546 C  CH2 . TRP   B 1 285 ? -46.794 2.537   19.418  1.00 11.79 ? 308  TRP   B CH2 1 
ATOM   6547 N  N   . THR   B 1 286 ? -44.415 5.308   15.787  1.00 13.20 ? 309  THR   B N   1 
ATOM   6548 C  CA  . THR   B 1 286 ? -44.113 3.899   15.547  1.00 13.04 ? 309  THR   B CA  1 
ATOM   6549 C  C   . THR   B 1 286 ? -43.394 3.373   16.784  1.00 12.20 ? 309  THR   B C   1 
ATOM   6550 O  O   . THR   B 1 286 ? -42.892 4.151   17.595  1.00 12.33 ? 309  THR   B O   1 
ATOM   6551 C  CB  . THR   B 1 286 ? -43.176 3.707   14.351  1.00 14.04 ? 309  THR   B CB  1 
ATOM   6552 O  OG1 . THR   B 1 286 ? -41.892 4.246   14.708  1.00 14.82 ? 309  THR   B OG1 1 
ATOM   6553 C  CG2 . THR   B 1 286 ? -43.694 4.314   13.068  1.00 14.13 ? 309  THR   B CG2 1 
ATOM   6554 N  N   . PRO   B 1 287 ? -43.262 2.040   16.950  1.00 11.91 ? 310  PRO   B N   1 
ATOM   6555 C  CA  . PRO   B 1 287 ? -42.445 1.515   18.040  1.00 11.25 ? 310  PRO   B CA  1 
ATOM   6556 C  C   . PRO   B 1 287 ? -41.014 2.069   18.040  1.00 13.97 ? 310  PRO   B C   1 
ATOM   6557 O  O   . PRO   B 1 287 ? -40.466 2.270   19.125  1.00 13.09 ? 310  PRO   B O   1 
ATOM   6558 C  CB  . PRO   B 1 287 ? -42.559 0.012   17.841  1.00 11.80 ? 310  PRO   B CB  1 
ATOM   6559 C  CG  . PRO   B 1 287 ? -43.944 -0.138  17.186  1.00 10.51 ? 310  PRO   B CG  1 
ATOM   6560 C  CD  . PRO   B 1 287 ? -43.980 0.999   16.190  1.00 11.18 ? 310  PRO   B CD  1 
ATOM   6561 N  N   . GLU   B 1 288 ? -40.463 2.387   16.860  1.00 14.11 ? 311  GLU   B N   1 
ATOM   6562 C  CA  . GLU   B 1 288 ? -39.081 2.832   16.730  1.00 15.87 ? 311  GLU   B CA  1 
ATOM   6563 C  C   . GLU   B 1 288 ? -38.947 4.346   16.937  1.00 16.58 ? 311  GLU   B C   1 
ATOM   6564 O  O   . GLU   B 1 288 ? -37.891 4.825   17.357  1.00 15.22 ? 311  GLU   B O   1 
ATOM   6565 C  CB  . GLU   B 1 288 ? -38.529 2.472   15.354  1.00 17.31 ? 311  GLU   B CB  1 
ATOM   6566 C  CG  . GLU   B 1 288 ? -38.550 0.968   15.050  1.00 18.97 ? 311  GLU   B CG  1 
ATOM   6567 C  CD  . GLU   B 1 288 ? -39.932 0.323   14.812  1.00 22.36 ? 311  GLU   B CD  1 
ATOM   6568 O  OE1 . GLU   B 1 288 ? -40.822 0.867   14.079  1.00 20.69 ? 311  GLU   B OE1 1 
ATOM   6569 O  OE2 . GLU   B 1 288 ? -40.093 -0.822  15.370  1.00 24.60 ? 311  GLU   B OE2 1 
ATOM   6570 N  N   . ASP   B 1 289 ? -40.022 5.088   16.644  1.00 14.53 ? 312  ASP   B N   1 
ATOM   6571 C  CA  . ASP   B 1 289 ? -40.063 6.513   16.905  1.00 15.64 ? 312  ASP   B CA  1 
ATOM   6572 C  C   . ASP   B 1 289 ? -41.414 6.843   17.520  1.00 15.31 ? 312  ASP   B C   1 
ATOM   6573 O  O   . ASP   B 1 289 ? -42.317 7.285   16.809  1.00 15.62 ? 312  ASP   B O   1 
ATOM   6574 C  CB  . ASP   B 1 289 ? -39.862 7.321   15.639  1.00 15.77 ? 312  ASP   B CB  1 
ATOM   6575 C  CG  . ASP   B 1 289 ? -39.760 8.821   15.868  1.00 18.81 ? 312  ASP   B CG  1 
ATOM   6576 O  OD1 . ASP   B 1 289 ? -39.340 9.203   16.977  1.00 21.80 ? 312  ASP   B OD1 1 
ATOM   6577 O  OD2 . ASP   B 1 289 ? -40.041 9.573   14.925  1.00 16.87 ? 312  ASP   B OD2 1 
ATOM   6578 N  N   . PRO   B 1 290 ? -41.597 6.566   18.825  1.00 16.05 ? 313  PRO   B N   1 
ATOM   6579 C  CA  . PRO   B 1 290 ? -42.900 6.770   19.475  1.00 16.10 ? 313  PRO   B CA  1 
ATOM   6580 C  C   . PRO   B 1 290 ? -43.201 8.237   19.747  1.00 14.50 ? 313  PRO   B C   1 
ATOM   6581 O  O   . PRO   B 1 290 ? -43.376 8.604   20.899  1.00 17.47 ? 313  PRO   B O   1 
ATOM   6582 C  CB  . PRO   B 1 290 ? -42.753 5.957   20.754  1.00 15.85 ? 313  PRO   B CB  1 
ATOM   6583 C  CG  . PRO   B 1 290 ? -41.264 6.022   21.066  1.00 16.35 ? 313  PRO   B CG  1 
ATOM   6584 C  CD  . PRO   B 1 290 ? -40.632 5.877   19.703  1.00 16.18 ? 313  PRO   B CD  1 
ATOM   6585 N  N   . PHE   B 1 291 ? -43.225 9.037   18.690  1.00 15.93 ? 314  PHE   B N   1 
ATOM   6586 C  CA  . PHE   B 1 291 ? -43.312 10.488  18.818  1.00 16.73 ? 314  PHE   B CA  1 
ATOM   6587 C  C   . PHE   B 1 291 ? -44.714 10.857  19.301  1.00 17.02 ? 314  PHE   B C   1 
ATOM   6588 O  O   . PHE   B 1 291 ? -45.686 10.337  18.773  1.00 14.88 ? 314  PHE   B O   1 
ATOM   6589 C  CB  . PHE   B 1 291 ? -43.067 11.206  17.497  1.00 17.28 ? 314  PHE   B CB  1 
ATOM   6590 C  CG  . PHE   B 1 291 ? -43.038 12.713  17.725  1.00 19.01 ? 314  PHE   B CG  1 
ATOM   6591 C  CD1 . PHE   B 1 291 ? -41.903 13.323  18.267  1.00 19.62 ? 314  PHE   B CD1 1 
ATOM   6592 C  CD2 . PHE   B 1 291 ? -44.150 13.511  17.421  1.00 20.16 ? 314  PHE   B CD2 1 
ATOM   6593 C  CE1 . PHE   B 1 291 ? -41.888 14.692  18.509  1.00 20.08 ? 314  PHE   B CE1 1 
ATOM   6594 C  CE2 . PHE   B 1 291 ? -44.125 14.891  17.649  1.00 20.63 ? 314  PHE   B CE2 1 
ATOM   6595 C  CZ  . PHE   B 1 291 ? -42.990 15.478  18.190  1.00 20.15 ? 314  PHE   B CZ  1 
ATOM   6596 N  N   . LEU   B 1 292 ? -44.795 11.729  20.306  1.00 17.76 ? 315  LEU   B N   1 
ATOM   6597 C  CA  . LEU   B 1 292 ? -46.073 12.188  20.830  1.00 17.13 ? 315  LEU   B CA  1 
ATOM   6598 C  C   . LEU   B 1 292 ? -46.182 13.705  20.710  1.00 18.82 ? 315  LEU   B C   1 
ATOM   6599 O  O   . LEU   B 1 292 ? -45.239 14.417  21.031  1.00 16.59 ? 315  LEU   B O   1 
ATOM   6600 C  CB  . LEU   B 1 292 ? -46.169 11.760  22.291  1.00 16.65 ? 315  LEU   B CB  1 
ATOM   6601 C  CG  . LEU   B 1 292 ? -46.057 10.257  22.556  1.00 15.81 ? 315  LEU   B CG  1 
ATOM   6602 C  CD1 . LEU   B 1 292 ? -46.056 10.017  24.019  1.00 15.41 ? 315  LEU   B CD1 1 
ATOM   6603 C  CD2 . LEU   B 1 292 ? -47.174 9.472   21.908  1.00 17.47 ? 315  LEU   B CD2 1 
ATOM   6604 N  N   . TYR   B 1 293 ? -47.369 14.160  20.294  1.00 17.61 ? 316  TYR   B N   1 
ATOM   6605 C  CA  . TYR   B 1 293 ? -47.767 15.551  20.306  1.00 18.04 ? 316  TYR   B CA  1 
ATOM   6606 C  C   . TYR   B 1 293 ? -48.570 15.834  21.572  1.00 20.77 ? 316  TYR   B C   1 
ATOM   6607 O  O   . TYR   B 1 293 ? -49.304 14.979  22.100  1.00 20.37 ? 316  TYR   B O   1 
ATOM   6608 C  CB  . TYR   B 1 293 ? -48.637 15.896  19.100  1.00 17.47 ? 316  TYR   B CB  1 
ATOM   6609 C  CG  . TYR   B 1 293 ? -47.976 15.929  17.727  1.00 19.19 ? 316  TYR   B CG  1 
ATOM   6610 C  CD1 . TYR   B 1 293 ? -47.839 14.773  16.968  1.00 17.02 ? 316  TYR   B CD1 1 
ATOM   6611 C  CD2 . TYR   B 1 293 ? -47.480 17.113  17.196  1.00 19.07 ? 316  TYR   B CD2 1 
ATOM   6612 C  CE1 . TYR   B 1 293 ? -47.256 14.797  15.711  1.00 19.12 ? 316  TYR   B CE1 1 
ATOM   6613 C  CE2 . TYR   B 1 293 ? -46.909 17.159  15.939  1.00 19.86 ? 316  TYR   B CE2 1 
ATOM   6614 C  CZ  . TYR   B 1 293 ? -46.774 15.995  15.200  1.00 19.03 ? 316  TYR   B CZ  1 
ATOM   6615 O  OH  . TYR   B 1 293 ? -46.229 16.055  13.948  1.00 21.68 ? 316  TYR   B OH  1 
ATOM   6616 N  N   . ASP   B 1 294 ? -48.435 17.071  22.060  1.00 21.05 ? 317  ASP   B N   1 
ATOM   6617 C  CA  . ASP   B 1 294 ? -49.291 17.530  23.137  1.00 20.49 ? 317  ASP   B CA  1 
ATOM   6618 C  C   . ASP   B 1 294 ? -50.646 17.878  22.558  1.00 19.70 ? 317  ASP   B C   1 
ATOM   6619 O  O   . ASP   B 1 294 ? -50.752 18.284  21.391  1.00 19.31 ? 317  ASP   B O   1 
ATOM   6620 C  CB  . ASP   B 1 294 ? -48.727 18.756  23.828  1.00 21.78 ? 317  ASP   B CB  1 
ATOM   6621 C  CG  . ASP   B 1 294 ? -47.424 18.453  24.534  1.00 23.53 ? 317  ASP   B CG  1 
ATOM   6622 O  OD1 . ASP   B 1 294 ? -47.446 17.605  25.453  1.00 22.30 ? 317  ASP   B OD1 1 
ATOM   6623 O  OD2 . ASP   B 1 294 ? -46.404 19.016  24.099  1.00 25.28 ? 317  ASP   B OD2 1 
ATOM   6624 N  N   . VAL   B 1 295 ? -51.668 17.701  23.396  1.00 21.55 ? 318  VAL   B N   1 
ATOM   6625 C  CA  . VAL   B 1 295 ? -53.018 18.050  23.011  1.00 20.97 ? 318  VAL   B CA  1 
ATOM   6626 C  C   . VAL   B 1 295 ? -53.645 18.757  24.195  1.00 21.88 ? 318  VAL   B C   1 
ATOM   6627 O  O   . VAL   B 1 295 ? -53.435 18.357  25.332  1.00 25.39 ? 318  VAL   B O   1 
ATOM   6628 C  CB  . VAL   B 1 295 ? -53.845 16.811  22.600  1.00 20.97 ? 318  VAL   B CB  1 
ATOM   6629 C  CG1 . VAL   B 1 295 ? -55.249 17.219  22.170  1.00 21.07 ? 318  VAL   B CG1 1 
ATOM   6630 C  CG2 . VAL   B 1 295 ? -53.192 16.043  21.454  1.00 21.13 ? 318  VAL   B CG2 1 
ATOM   6631 N  N   . ARG   B 1 296 ? -54.457 19.770  23.916  1.00 23.58 ? 319  ARG   B N   1 
ATOM   6632 C  CA  . ARG   B 1 296 ? -55.218 20.389  24.985  1.00 25.29 ? 319  ARG   B CA  1 
ATOM   6633 C  C   . ARG   B 1 296 ? -56.642 20.640  24.499  1.00 21.88 ? 319  ARG   B C   1 
ATOM   6634 O  O   . ARG   B 1 296 ? -56.857 21.032  23.350  1.00 23.55 ? 319  ARG   B O   1 
ATOM   6635 C  CB  . ARG   B 1 296 ? -54.474 21.649  25.442  1.00 29.98 ? 319  ARG   B CB  1 
ATOM   6636 C  CG  . ARG   B 1 296 ? -55.277 22.476  26.433  1.00 32.98 ? 319  ARG   B CG  1 
ATOM   6637 C  CD  . ARG   B 1 296 ? -54.364 23.345  27.276  1.00 33.35 ? 319  ARG   B CD  1 
ATOM   6638 N  NE  . ARG   B 1 296 ? -53.468 22.533  28.110  1.00 29.25 ? 319  ARG   B NE  1 
ATOM   6639 C  CZ  . ARG   B 1 296 ? -53.738 22.019  29.298  1.00 29.06 ? 319  ARG   B CZ  1 
ATOM   6640 N  NH1 . ARG   B 1 296 ? -54.926 22.171  29.851  1.00 31.25 ? 319  ARG   B NH1 1 
ATOM   6641 N  NH2 . ARG   B 1 296 ? -52.803 21.347  29.954  1.00 30.55 ? 319  ARG   B NH2 1 
ATOM   6642 N  N   . ALA   B 1 297 ? -57.595 20.429  25.414  1.00 22.64 ? 320  ALA   B N   1 
ATOM   6643 C  CA  . ALA   B 1 297 ? -59.012 20.575  25.111  1.00 21.99 ? 320  ALA   B CA  1 
ATOM   6644 C  C   . ALA   B 1 297 ? -59.695 21.488  26.133  1.00 21.67 ? 320  ALA   B C   1 
ATOM   6645 O  O   . ALA   B 1 297 ? -59.491 21.345  27.343  1.00 23.08 ? 320  ALA   B O   1 
ATOM   6646 C  CB  . ALA   B 1 297 ? -59.672 19.227  25.064  1.00 21.15 ? 320  ALA   B CB  1 
ATOM   6647 N  N   . ASP   B 1 298 ? -60.461 22.446  25.587  1.00 24.56 ? 321  ASP   B N   1 
ATOM   6648 C  CA  . ASP   B 1 298 ? -61.065 23.539  26.340  1.00 25.72 ? 321  ASP   B CA  1 
ATOM   6649 C  C   . ASP   B 1 298 ? -62.493 23.720  25.844  1.00 24.25 ? 321  ASP   B C   1 
ATOM   6650 O  O   . ASP   B 1 298 ? -62.713 24.231  24.744  1.00 26.68 ? 321  ASP   B O   1 
ATOM   6651 C  CB  . ASP   B 1 298 ? -60.271 24.829  26.197  1.00 28.67 ? 321  ASP   B CB  1 
ATOM   6652 C  CG  . ASP   B 1 298 ? -58.842 24.756  26.728  1.00 32.41 ? 321  ASP   B CG  1 
ATOM   6653 O  OD1 . ASP   B 1 298 ? -58.655 24.695  27.964  1.00 33.59 ? 321  ASP   B OD1 1 
ATOM   6654 O  OD2 . ASP   B 1 298 ? -57.934 24.714  25.901  1.00 36.60 ? 321  ASP   B OD2 1 
ATOM   6655 N  N   . PRO   B 1 299 ? -63.494 23.246  26.617  1.00 24.85 ? 322  PRO   B N   1 
ATOM   6656 C  CA  . PRO   B 1 299 ? -64.895 23.550  26.331  1.00 26.44 ? 322  PRO   B CA  1 
ATOM   6657 C  C   . PRO   B 1 299 ? -65.047 25.050  26.583  1.00 26.89 ? 322  PRO   B C   1 
ATOM   6658 O  O   . PRO   B 1 299 ? -64.468 25.561  27.550  1.00 24.39 ? 322  PRO   B O   1 
ATOM   6659 C  CB  . PRO   B 1 299 ? -65.697 22.689  27.317  1.00 26.36 ? 322  PRO   B CB  1 
ATOM   6660 C  CG  . PRO   B 1 299 ? -64.722 22.298  28.411  1.00 27.38 ? 322  PRO   B CG  1 
ATOM   6661 C  CD  . PRO   B 1 299 ? -63.312 22.529  27.885  1.00 25.26 ? 322  PRO   B CD  1 
ATOM   6662 N  N   . LEU   B 1 300 ? -65.846 25.714  25.745  1.00 29.94 ? 323  LEU   B N   1 
ATOM   6663 C  CA  . LEU   B 1 300 ? -65.941 27.172  25.754  1.00 30.15 ? 323  LEU   B CA  1 
ATOM   6664 C  C   . LEU   B 1 300 ? -67.278 27.644  26.362  1.00 30.80 ? 323  LEU   B C   1 
ATOM   6665 O  O   . LEU   B 1 300 ? -68.296 27.266  25.751  1.00 32.73 ? 323  LEU   B O   1 
ATOM   6666 C  CB  . LEU   B 1 300 ? -65.767 27.609  24.305  1.00 31.06 ? 323  LEU   B CB  1 
ATOM   6667 C  CG  . LEU   B 1 300 ? -64.416 27.239  23.671  1.00 30.74 ? 323  LEU   B CG  1 
ATOM   6668 C  CD1 . LEU   B 1 300 ? -64.321 27.638  22.221  1.00 29.62 ? 323  LEU   B CD1 1 
ATOM   6669 C  CD2 . LEU   B 1 300 ? -63.245 27.827  24.446  1.00 30.76 ? 323  LEU   B CD2 1 
ATOM   6670 N  N   . VAL   B 1 306 ? -63.852 27.533  31.611  1.00 54.87 ? 329  VAL   B N   1 
ATOM   6671 C  CA  . VAL   B 1 306 ? -64.726 26.533  32.302  1.00 55.49 ? 329  VAL   B CA  1 
ATOM   6672 C  C   . VAL   B 1 306 ? -63.824 25.432  32.858  1.00 50.04 ? 329  VAL   B C   1 
ATOM   6673 O  O   . VAL   B 1 306 ? -63.607 25.356  34.064  1.00 66.21 ? 329  VAL   B O   1 
ATOM   6674 C  CB  . VAL   B 1 306 ? -65.875 26.019  31.390  1.00 57.54 ? 329  VAL   B CB  1 
ATOM   6675 C  CG1 . VAL   B 1 306 ? -65.558 26.151  29.903  1.00 58.11 ? 329  VAL   B CG1 1 
ATOM   6676 C  CG2 . VAL   B 1 306 ? -66.351 24.597  31.710  1.00 53.14 ? 329  VAL   B CG2 1 
ATOM   6677 N  N   . ASP   B 1 307 ? -63.258 24.627  31.957  1.00 45.01 ? 330  ASP   B N   1 
ATOM   6678 C  CA  . ASP   B 1 307 ? -62.414 23.488  32.288  1.00 36.48 ? 330  ASP   B CA  1 
ATOM   6679 C  C   . ASP   B 1 307 ? -61.329 23.434  31.220  1.00 33.02 ? 330  ASP   B C   1 
ATOM   6680 O  O   . ASP   B 1 307 ? -61.488 24.005  30.142  1.00 28.68 ? 330  ASP   B O   1 
ATOM   6681 C  CB  . ASP   B 1 307 ? -63.211 22.186  32.341  1.00 32.99 ? 330  ASP   B CB  1 
ATOM   6682 C  CG  . ASP   B 1 307 ? -62.454 20.921  32.733  1.00 32.19 ? 330  ASP   B CG  1 
ATOM   6683 O  OD1 . ASP   B 1 307 ? -61.584 21.011  33.625  1.00 24.91 ? 330  ASP   B OD1 1 
ATOM   6684 O  OD2 . ASP   B 1 307 ? -62.786 19.827  32.188  1.00 24.29 ? 330  ASP   B OD2 1 
ATOM   6685 N  N   . SER   B 1 308 ? -60.223 22.764  31.530  1.00 27.23 ? 331  SER   B N   1 
ATOM   6686 C  CA  . SER   B 1 308 ? -59.144 22.626  30.565  1.00 25.36 ? 331  SER   B CA  1 
ATOM   6687 C  C   . SER   B 1 308 ? -58.412 21.346  30.894  1.00 21.22 ? 331  SER   B C   1 
ATOM   6688 O  O   . SER   B 1 308 ? -58.119 21.096  32.068  1.00 23.45 ? 331  SER   B O   1 
ATOM   6689 C  CB  . SER   B 1 308 ? -58.187 23.793  30.599  1.00 25.57 ? 331  SER   B CB  1 
ATOM   6690 O  OG  . SER   B 1 308 ? -57.275 23.726  29.509  1.00 27.03 ? 331  SER   B OG  1 
ATOM   6691 N  N   . VAL   B 1 309 ? -58.152 20.522  29.868  1.00 21.77 ? 332  VAL   B N   1 
ATOM   6692 C  CA  . VAL   B 1 309 ? -57.431 19.274  30.110  1.00 20.33 ? 332  VAL   B CA  1 
ATOM   6693 C  C   . VAL   B 1 309 ? -56.233 19.137  29.164  1.00 17.86 ? 332  VAL   B C   1 
ATOM   6694 O  O   . VAL   B 1 309 ? -56.290 19.481  27.985  1.00 19.28 ? 332  VAL   B O   1 
ATOM   6695 C  CB  . VAL   B 1 309 ? -58.344 18.028  29.989  1.00 20.21 ? 332  VAL   B CB  1 
ATOM   6696 C  CG1 . VAL   B 1 309 ? -59.405 18.004  31.080  1.00 22.95 ? 332  VAL   B CG1 1 
ATOM   6697 C  CG2 . VAL   B 1 309 ? -58.978 17.917  28.608  1.00 20.87 ? 332  VAL   B CG2 1 
ATOM   6698 N  N   . GLY   B 1 310 ? -55.182 18.503  29.698  1.00 18.87 ? 333  GLY   B N   1 
ATOM   6699 C  CA  . GLY   B 1 310 ? -54.011 18.147  28.914  1.00 20.59 ? 333  GLY   B CA  1 
ATOM   6700 C  C   . GLY   B 1 310 ? -54.086 16.679  28.468  1.00 21.84 ? 333  GLY   B C   1 
ATOM   6701 O  O   . GLY   B 1 310 ? -54.634 15.829  29.174  1.00 20.90 ? 333  GLY   B O   1 
ATOM   6702 N  N   . SER   B 1 311 ? -53.568 16.413  27.268  1.00 20.91 ? 334  SER   B N   1 
ATOM   6703 C  CA  . SER   B 1 311 ? -53.548 15.062  26.730  1.00 20.19 ? 334  SER   B CA  1 
ATOM   6704 C  C   . SER   B 1 311 ? -52.381 14.973  25.754  1.00 20.09 ? 334  SER   B C   1 
ATOM   6705 O  O   . SER   B 1 311 ? -51.493 15.835  25.726  1.00 18.27 ? 334  SER   B O   1 
ATOM   6706 C  CB  . SER   B 1 311 ? -54.879 14.705  26.054  1.00 21.28 ? 334  SER   B CB  1 
ATOM   6707 O  OG  . SER   B 1 311 ? -55.049 13.303  25.822  1.00 19.08 ? 334  SER   B OG  1 
ATOM   6708 N  N   . TYR   B 1 312 ? -52.356 13.891  24.974  1.00 18.01 ? 335  TYR   B N   1 
ATOM   6709 C  CA  . TYR   B 1 312 ? -51.320 13.732  23.975  1.00 17.14 ? 335  TYR   B CA  1 
ATOM   6710 C  C   . TYR   B 1 312 ? -51.829 12.746  22.931  1.00 18.18 ? 335  TYR   B C   1 
ATOM   6711 O  O   . TYR   B 1 312 ? -52.782 12.016  23.190  1.00 17.84 ? 335  TYR   B O   1 
ATOM   6712 C  CB  . TYR   B 1 312 ? -50.029 13.234  24.622  1.00 16.58 ? 335  TYR   B CB  1 
ATOM   6713 C  CG  . TYR   B 1 312 ? -50.101 11.872  25.298  1.00 14.67 ? 335  TYR   B CG  1 
ATOM   6714 C  CD1 . TYR   B 1 312 ? -50.020 10.683  24.557  1.00 14.62 ? 335  TYR   B CD1 1 
ATOM   6715 C  CD2 . TYR   B 1 312 ? -50.294 11.771  26.669  1.00 13.98 ? 335  TYR   B CD2 1 
ATOM   6716 C  CE1 . TYR   B 1 312 ? -50.057 9.452   25.193  1.00 13.01 ? 335  TYR   B CE1 1 
ATOM   6717 C  CE2 . TYR   B 1 312 ? -50.353 10.544  27.313  1.00 14.12 ? 335  TYR   B CE2 1 
ATOM   6718 C  CZ  . TYR   B 1 312 ? -50.258 9.373   26.557  1.00 14.23 ? 335  TYR   B CZ  1 
ATOM   6719 O  OH  . TYR   B 1 312 ? -50.311 8.163   27.188  1.00 15.52 ? 335  TYR   B OH  1 
ATOM   6720 N  N   . THR   B 1 313 ? -51.215 12.743  21.758  1.00 16.64 ? 336  THR   B N   1 
ATOM   6721 C  CA  . THR   B 1 313 ? -51.556 11.729  20.777  1.00 17.42 ? 336  THR   B CA  1 
ATOM   6722 C  C   . THR   B 1 313 ? -50.272 11.223  20.135  1.00 17.22 ? 336  THR   B C   1 
ATOM   6723 O  O   . THR   B 1 313 ? -49.306 11.969  20.014  1.00 17.32 ? 336  THR   B O   1 
ATOM   6724 C  CB  . THR   B 1 313 ? -52.518 12.293  19.745  1.00 16.85 ? 336  THR   B CB  1 
ATOM   6725 O  OG1 . THR   B 1 313 ? -52.900 11.252  18.846  1.00 15.81 ? 336  THR   B OG1 1 
ATOM   6726 C  CG2 . THR   B 1 313 ? -51.898 13.432  18.942  1.00 17.75 ? 336  THR   B CG2 1 
ATOM   6727 N  N   . GLY   B 1 314 ? -50.279 9.939   19.749  1.00 13.85 ? 337  GLY   B N   1 
ATOM   6728 C  CA  . GLY   B 1 314 ? -49.308 9.419   18.803  1.00 12.24 ? 337  GLY   B CA  1 
ATOM   6729 C  C   . GLY   B 1 314 ? -49.953 9.271   17.431  1.00 13.39 ? 337  GLY   B C   1 
ATOM   6730 O  O   . GLY   B 1 314 ? -50.941 8.532   17.289  1.00 13.74 ? 337  GLY   B O   1 
ATOM   6731 N  N   . MET   B 1 315 ? -49.423 9.961   16.424  1.00 13.02 ? 338  MET   B N   1 
ATOM   6732 C  CA  . MET   B 1 315 ? -50.046 9.946   15.115  1.00 13.65 ? 338  MET   B CA  1 
ATOM   6733 C  C   . MET   B 1 315 ? -49.727 8.643   14.389  1.00 12.69 ? 338  MET   B C   1 
ATOM   6734 O  O   . MET   B 1 315 ? -48.706 8.504   13.733  1.00 13.14 ? 338  MET   B O   1 
ATOM   6735 C  CB  . MET   B 1 315 ? -49.662 11.158  14.253  1.00 15.69 ? 338  MET   B CB  1 
ATOM   6736 C  CG  . MET   B 1 315 ? -50.120 12.484  14.857  1.00 16.03 ? 338  MET   B CG  1 
ATOM   6737 S  SD  . MET   B 1 315 ? -51.889 12.797  14.717  1.00 18.23 ? 338  MET   B SD  1 
ATOM   6738 C  CE  . MET   B 1 315 ? -52.100 12.903  12.946  1.00 18.27 ? 338  MET   B CE  1 
ATOM   6739 N  N   . ARG   B 1 316 ? -50.666 7.699   14.477  1.00 13.79 ? 339  ARG   B N   1 
ATOM   6740 C  CA  . ARG   B 1 316 ? -50.505 6.407   13.830  1.00 13.53 ? 339  ARG   B CA  1 
ATOM   6741 C  C   . ARG   B 1 316 ? -51.884 5.877   13.437  1.00 12.87 ? 339  ARG   B C   1 
ATOM   6742 O  O   . ARG   B 1 316 ? -52.866 6.257   14.051  1.00 13.31 ? 339  ARG   B O   1 
ATOM   6743 C  CB  . ARG   B 1 316 ? -49.803 5.478   14.816  1.00 12.75 ? 339  ARG   B CB  1 
ATOM   6744 C  CG  . ARG   B 1 316 ? -50.639 5.151   16.039  1.00 12.36 ? 339  ARG   B CG  1 
ATOM   6745 C  CD  . ARG   B 1 316 ? -51.436 3.857   15.899  1.00 13.06 ? 339  ARG   B CD  1 
ATOM   6746 N  NE  . ARG   B 1 316 ? -52.295 3.629   17.066  1.00 13.66 ? 339  ARG   B NE  1 
ATOM   6747 C  CZ  . ARG   B 1 316 ? -53.594 3.899   17.132  1.00 14.14 ? 339  ARG   B CZ  1 
ATOM   6748 N  NH1 . ARG   B 1 316 ? -54.246 4.522   16.150  1.00 13.23 ? 339  ARG   B NH1 1 
ATOM   6749 N  NH2 . ARG   B 1 316 ? -54.257 3.572   18.218  1.00 17.37 ? 339  ARG   B NH2 1 
ATOM   6750 N  N   . THR   B 1 317 ? -51.914 4.989   12.447  1.00 12.51 ? 340  THR   B N   1 
ATOM   6751 C  CA  . THR   B 1 317 ? -53.102 4.222   12.120  1.00 12.11 ? 340  THR   B CA  1 
ATOM   6752 C  C   . THR   B 1 317 ? -52.760 2.741   12.144  1.00 11.60 ? 340  THR   B C   1 
ATOM   6753 O  O   . THR   B 1 317 ? -51.635 2.375   11.863  1.00 11.72 ? 340  THR   B O   1 
ATOM   6754 C  CB  . THR   B 1 317 ? -53.637 4.579   10.728  1.00 13.52 ? 340  THR   B CB  1 
ATOM   6755 O  OG1 . THR   B 1 317 ? -52.618 4.332   9.763   1.00 13.90 ? 340  THR   B OG1 1 
ATOM   6756 C  CG2 . THR   B 1 317 ? -54.082 6.022   10.597  1.00 14.85 ? 340  THR   B CG2 1 
ATOM   6757 N  N   . ILE   B 1 318 ? -53.794 1.910   12.348  1.00 11.18 ? 341  ILE   B N   1 
ATOM   6758 C  CA  . ILE   B 1 318 ? -53.710 0.469   12.235  1.00 10.73 ? 341  ILE   B CA  1 
ATOM   6759 C  C   . ILE   B 1 318 ? -54.972 0.021   11.506  1.00 10.74 ? 341  ILE   B C   1 
ATOM   6760 O  O   . ILE   B 1 318 ? -56.058 0.487   11.826  1.00 11.57 ? 341  ILE   B O   1 
ATOM   6761 C  CB  . ILE   B 1 318 ? -53.565 -0.229  13.600  1.00 11.16 ? 341  ILE   B CB  1 
ATOM   6762 C  CG1 . ILE   B 1 318 ? -53.220 -1.710  13.385  1.00 11.63 ? 341  ILE   B CG1 1 
ATOM   6763 C  CG2 . ILE   B 1 318 ? -54.790 -0.001  14.501  1.00 11.43 ? 341  ILE   B CG2 1 
ATOM   6764 C  CD1 . ILE   B 1 318 ? -51.781 -1.970  12.960  1.00 11.50 ? 341  ILE   B CD1 1 
ATOM   6765 N  N   . ALA   B 1 319 ? -54.798 -0.816  10.497  1.00 10.63 ? 342  ALA   B N   1 
ATOM   6766 C  CA  . ALA   B 1 319 ? -55.901 -1.301  9.681   1.00 11.47 ? 342  ALA   B CA  1 
ATOM   6767 C  C   . ALA   B 1 319 ? -55.478 -2.605  9.039   1.00 12.44 ? 342  ALA   B C   1 
ATOM   6768 O  O   . ALA   B 1 319 ? -54.302 -2.961  9.055   1.00 12.96 ? 342  ALA   B O   1 
ATOM   6769 C  CB  . ALA   B 1 319 ? -56.294 -0.307  8.608   1.00 11.52 ? 342  ALA   B CB  1 
ATOM   6770 N  N   . LEU   B 1 320 ? -56.465 -3.302  8.490   1.00 12.75 ? 343  LEU   B N   1 
ATOM   6771 C  CA  . LEU   B 1 320 ? -56.221 -4.481  7.672   1.00 15.69 ? 343  LEU   B CA  1 
ATOM   6772 C  C   . LEU   B 1 320 ? -56.198 -4.012  6.228   1.00 18.08 ? 343  LEU   B C   1 
ATOM   6773 O  O   . LEU   B 1 320 ? -57.104 -3.291  5.846   1.00 21.41 ? 343  LEU   B O   1 
ATOM   6774 C  CB  . LEU   B 1 320 ? -57.397 -5.414  7.982   1.00 17.26 ? 343  LEU   B CB  1 
ATOM   6775 C  CG  . LEU   B 1 320 ? -57.169 -6.895  7.731   1.00 20.13 ? 343  LEU   B CG  1 
ATOM   6776 C  CD1 . LEU   B 1 320 ? -56.014 -7.370  8.566   1.00 19.33 ? 343  LEU   B CD1 1 
ATOM   6777 C  CD2 . LEU   B 1 320 ? -58.464 -7.626  8.027   1.00 19.58 ? 343  LEU   B CD2 1 
ATOM   6778 N  N   . ALA   B 1 321 ? -55.129 -4.294  5.482   1.00 18.20 ? 344  ALA   B N   1 
ATOM   6779 C  CA  . ALA   B 1 321 ? -55.096 -3.973  4.062   1.00 18.34 ? 344  ALA   B CA  1 
ATOM   6780 C  C   . ALA   B 1 321 ? -54.438 -5.117  3.322   1.00 19.54 ? 344  ALA   B C   1 
ATOM   6781 O  O   . ALA   B 1 321 ? -53.758 -5.954  3.922   1.00 17.12 ? 344  ALA   B O   1 
ATOM   6782 C  CB  . ALA   B 1 321 ? -54.354 -2.679  3.811   1.00 18.92 ? 344  ALA   B CB  1 
ATOM   6783 N  N   . SER   B 1 322 ? -54.628 -5.119  2.003   1.00 19.19 ? 345  SER   B N   1 
ATOM   6784 C  CA  . SER   B 1 322 ? -53.998 -6.117  1.163   1.00 18.62 ? 345  SER   B CA  1 
ATOM   6785 C  C   . SER   B 1 322 ? -52.592 -5.632  0.782   1.00 18.70 ? 345  SER   B C   1 
ATOM   6786 O  O   . SER   B 1 322 ? -52.429 -4.565  0.183   1.00 19.86 ? 345  SER   B O   1 
ATOM   6787 C  CB  . SER   B 1 322 ? -54.889 -6.379  -0.046  1.00 20.76 ? 345  SER   B CB  1 
ATOM   6788 O  OG  . SER   B 1 322 ? -54.366 -7.466  -0.795  1.00 20.88 ? 345  SER   B OG  1 
ATOM   6789 N  N   . VAL   B 1 323 ? -51.560 -6.414  1.126   1.00 15.99 ? 346  VAL   B N   1 
ATOM   6790 C  CA  . VAL   B 1 323 ? -50.189 -6.042  0.839   1.00 16.46 ? 346  VAL   B CA  1 
ATOM   6791 C  C   . VAL   B 1 323 ? -49.516 -7.241  0.194   1.00 15.97 ? 346  VAL   B C   1 
ATOM   6792 O  O   . VAL   B 1 323 ? -49.517 -8.316  0.788   1.00 14.77 ? 346  VAL   B O   1 
ATOM   6793 C  CB  . VAL   B 1 323 ? -49.436 -5.638  2.124   1.00 16.20 ? 346  VAL   B CB  1 
ATOM   6794 C  CG1 . VAL   B 1 323 ? -47.945 -5.456  1.883   1.00 17.22 ? 346  VAL   B CG1 1 
ATOM   6795 C  CG2 . VAL   B 1 323 ? -50.073 -4.418  2.762   1.00 16.77 ? 346  VAL   B CG2 1 
ATOM   6796 N  N   . GLY   B 1 324 ? -49.027 -7.105  -1.042  1.00 15.13 ? 347  GLY   B N   1 
ATOM   6797 C  CA  . GLY   B 1 324 ? -48.382 -8.254  -1.671  1.00 15.11 ? 347  GLY   B CA  1 
ATOM   6798 C  C   . GLY   B 1 324 ? -49.341 -9.433  -1.923  1.00 14.08 ? 347  GLY   B C   1 
ATOM   6799 O  O   . GLY   B 1 324 ? -48.913 -10.590 -2.098  1.00 14.05 ? 347  GLY   B O   1 
ATOM   6800 N  N   . GLY   B 1 325 ? -50.648 -9.137  -1.930  1.00 14.52 ? 348  GLY   B N   1 
ATOM   6801 C  CA  . GLY   B 1 325 ? -51.656 -10.178 -2.126  1.00 14.21 ? 348  GLY   B CA  1 
ATOM   6802 C  C   . GLY   B 1 325 ? -52.138 -10.834 -0.829  1.00 15.43 ? 348  GLY   B C   1 
ATOM   6803 O  O   . GLY   B 1 325 ? -52.988 -11.724 -0.874  1.00 14.56 ? 348  GLY   B O   1 
ATOM   6804 N  N   . HIS   B 1 326 ? -51.569 -10.428 0.320   1.00 13.23 ? 349  HIS   B N   1 
ATOM   6805 C  CA  . HIS   B 1 326 ? -51.937 -10.988 1.613   1.00 13.21 ? 349  HIS   B CA  1 
ATOM   6806 C  C   . HIS   B 1 326 ? -52.653 -9.916  2.420   1.00 11.92 ? 349  HIS   B C   1 
ATOM   6807 O  O   . HIS   B 1 326 ? -52.247 -8.775  2.384   1.00 12.86 ? 349  HIS   B O   1 
ATOM   6808 C  CB  . HIS   B 1 326 ? -50.705 -11.386 2.416   1.00 12.30 ? 349  HIS   B CB  1 
ATOM   6809 C  CG  . HIS   B 1 326 ? -50.107 -12.725 2.079   1.00 11.61 ? 349  HIS   B CG  1 
ATOM   6810 N  ND1 . HIS   B 1 326 ? -48.763 -13.007 1.951   1.00 11.96 ? 349  HIS   B ND1 1 
ATOM   6811 C  CD2 . HIS   B 1 326 ? -50.740 -13.870 1.838   1.00 10.70 ? 349  HIS   B CD2 1 
ATOM   6812 C  CE1 . HIS   B 1 326 ? -48.618 -14.294 1.698   1.00 11.41 ? 349  HIS   B CE1 1 
ATOM   6813 N  NE2 . HIS   B 1 326 ? -49.808 -14.821 1.597   1.00 11.46 ? 349  HIS   B NE2 1 
ATOM   6814 N  N   . GLN   B 1 327 ? -53.728 -10.273 3.122   1.00 11.53 ? 350  GLN   B N   1 
ATOM   6815 C  CA  . GLN   B 1 327 ? -54.255 -9.436  4.173   1.00 13.08 ? 350  GLN   B CA  1 
ATOM   6816 C  C   . GLN   B 1 327 ? -53.193 -9.333  5.258   1.00 12.19 ? 350  GLN   B C   1 
ATOM   6817 O  O   . GLN   B 1 327 ? -52.733 -10.351 5.762   1.00 12.89 ? 350  GLN   B O   1 
ATOM   6818 C  CB  . GLN   B 1 327 ? -55.523 -10.041 4.779   1.00 14.71 ? 350  GLN   B CB  1 
ATOM   6819 C  CG  . GLN   B 1 327 ? -56.704 -9.987  3.821   1.00 17.28 ? 350  GLN   B CG  1 
ATOM   6820 C  CD  . GLN   B 1 327 ? -57.173 -8.571  3.629   1.00 20.16 ? 350  GLN   B CD  1 
ATOM   6821 O  OE1 . GLN   B 1 327 ? -56.842 -7.921  2.650   1.00 24.24 ? 350  GLN   B OE1 1 
ATOM   6822 N  NE2 . GLN   B 1 327 ? -57.896 -8.065  4.606   1.00 24.86 ? 350  GLN   B NE2 1 
ATOM   6823 N  N   . ARG   B 1 328 ? -52.851 -8.089  5.590   1.00 11.57 ? 351  ARG   B N   1 
ATOM   6824 C  CA  . ARG   B 1 328 ? -51.808 -7.757  6.537   1.00 11.69 ? 351  ARG   B CA  1 
ATOM   6825 C  C   . ARG   B 1 328 ? -52.299 -6.670  7.474   1.00 11.02 ? 351  ARG   B C   1 
ATOM   6826 O  O   . ARG   B 1 328 ? -53.012 -5.758  7.074   1.00 12.20 ? 351  ARG   B O   1 
ATOM   6827 C  CB  . ARG   B 1 328 ? -50.523 -7.195  5.919   1.00 12.80 ? 351  ARG   B CB  1 
ATOM   6828 C  CG  . ARG   B 1 328 ? -49.670 -8.097  5.039   1.00 14.38 ? 351  ARG   B CG  1 
ATOM   6829 C  CD  . ARG   B 1 328 ? -49.134 -9.327  5.697   1.00 12.93 ? 351  ARG   B CD  1 
ATOM   6830 N  NE  . ARG   B 1 328 ? -48.096 -9.952  4.847   1.00 11.68 ? 351  ARG   B NE  1 
ATOM   6831 C  CZ  . ARG   B 1 328 ? -47.399 -10.995 5.269   1.00 11.19 ? 351  ARG   B CZ  1 
ATOM   6832 N  NH1 . ARG   B 1 328 ? -47.596 -11.468 6.481   1.00 9.72  ? 351  ARG   B NH1 1 
ATOM   6833 N  NH2 . ARG   B 1 328 ? -46.439 -11.525 4.541   1.00 11.54 ? 351  ARG   B NH2 1 
ATOM   6834 N  N   . PRO   B 1 329 ? -51.862 -6.666  8.752   1.00 9.89  ? 352  PRO   B N   1 
ATOM   6835 C  CA  . PRO   B 1 329 ? -52.049 -5.497  9.593   1.00 9.83  ? 352  PRO   B CA  1 
ATOM   6836 C  C   . PRO   B 1 329 ? -51.033 -4.440  9.183   1.00 10.91 ? 352  PRO   B C   1 
ATOM   6837 O  O   . PRO   B 1 329 ? -49.841 -4.713  9.193   1.00 10.70 ? 352  PRO   B O   1 
ATOM   6838 C  CB  . PRO   B 1 329 ? -51.811 -6.054  10.983  1.00 9.60  ? 352  PRO   B CB  1 
ATOM   6839 C  CG  . PRO   B 1 329 ? -50.790 -7.174  10.790  1.00 9.27  ? 352  PRO   B CG  1 
ATOM   6840 C  CD  . PRO   B 1 329 ? -51.099 -7.736  9.407   1.00 9.87  ? 352  PRO   B CD  1 
ATOM   6841 N  N   . VAL   B 1 330 ? -51.528 -3.263  8.762   1.00 11.07 ? 353  VAL   B N   1 
ATOM   6842 C  CA  . VAL   B 1 330 ? -50.672 -2.186  8.295   1.00 11.32 ? 353  VAL   B CA  1 
ATOM   6843 C  C   . VAL   B 1 330 ? -50.688 -1.073  9.342   1.00 11.33 ? 353  VAL   B C   1 
ATOM   6844 O  O   . VAL   B 1 330 ? -51.743 -0.614  9.784   1.00 11.12 ? 353  VAL   B O   1 
ATOM   6845 C  CB  . VAL   B 1 330 ? -51.021 -1.694  6.873   1.00 12.35 ? 353  VAL   B CB  1 
ATOM   6846 C  CG1 . VAL   B 1 330 ? -50.725 -2.780  5.843   1.00 12.31 ? 353  VAL   B CG1 1 
ATOM   6847 C  CG2 . VAL   B 1 330 ? -52.459 -1.175  6.743   1.00 12.18 ? 353  VAL   B CG2 1 
ATOM   6848 N  N   . LEU   B 1 331 ? -49.476 -0.667  9.748   1.00 10.54 ? 354  LEU   B N   1 
ATOM   6849 C  CA  . LEU   B 1 331 ? -49.249 0.439   10.655  1.00 11.15 ? 354  LEU   B CA  1 
ATOM   6850 C  C   . LEU   B 1 331 ? -48.825 1.597   9.760   1.00 11.49 ? 354  LEU   B C   1 
ATOM   6851 O  O   . LEU   B 1 331 ? -47.867 1.458   9.007   1.00 11.55 ? 354  LEU   B O   1 
ATOM   6852 C  CB  . LEU   B 1 331 ? -48.127 0.063   11.629  1.00 12.38 ? 354  LEU   B CB  1 
ATOM   6853 C  CG  . LEU   B 1 331 ? -47.625 1.160   12.571  1.00 12.40 ? 354  LEU   B CG  1 
ATOM   6854 C  CD1 . LEU   B 1 331 ? -48.677 1.537   13.597  1.00 13.51 ? 354  LEU   B CD1 1 
ATOM   6855 C  CD2 . LEU   B 1 331 ? -46.336 0.684   13.268  1.00 13.36 ? 354  LEU   B CD2 1 
ATOM   6856 N  N   . ASN   B 1 332 ? -49.568 2.694   9.799   1.00 12.53 ? 355  ASN   B N   1 
ATOM   6857 C  CA  . ASN   B 1 332 ? -49.265 3.874   9.013   1.00 13.52 ? 355  ASN   B CA  1 
ATOM   6858 C  C   . ASN   B 1 332 ? -49.176 3.512   7.534   1.00 13.98 ? 355  ASN   B C   1 
ATOM   6859 O  O   . ASN   B 1 332 ? -48.299 3.998   6.817   1.00 13.25 ? 355  ASN   B O   1 
ATOM   6860 C  CB  . ASN   B 1 332 ? -47.988 4.522   9.534   1.00 13.93 ? 355  ASN   B CB  1 
ATOM   6861 C  CG  . ASN   B 1 332 ? -48.100 4.851   11.004  1.00 14.31 ? 355  ASN   B CG  1 
ATOM   6862 O  OD1 . ASN   B 1 332 ? -49.209 5.043   11.518  1.00 16.89 ? 355  ASN   B OD1 1 
ATOM   6863 N  ND2 . ASN   B 1 332 ? -46.983 4.888   11.723  1.00 14.75 ? 355  ASN   B ND2 1 
ATOM   6864 N  N   . GLY   B 1 333 ? -50.036 2.593   7.114   1.00 13.75 ? 356  GLY   B N   1 
ATOM   6865 C  CA  . GLY   B 1 333 ? -50.144 2.197   5.724   1.00 15.07 ? 356  GLY   B CA  1 
ATOM   6866 C  C   . GLY   B 1 333 ? -49.122 1.166   5.257   1.00 14.37 ? 356  GLY   B C   1 
ATOM   6867 O  O   . GLY   B 1 333 ? -49.188 0.777   4.101   1.00 17.30 ? 356  GLY   B O   1 
ATOM   6868 N  N   . LYS   B 1 334 ? -48.248 0.650   6.136   1.00 13.37 ? 357  LYS   B N   1 
ATOM   6869 C  CA  . LYS   B 1 334 ? -47.229 -0.312  5.733   1.00 15.21 ? 357  LYS   B CA  1 
ATOM   6870 C  C   . LYS   B 1 334 ? -47.246 -1.530  6.653   1.00 14.33 ? 357  LYS   B C   1 
ATOM   6871 O  O   . LYS   B 1 334 ? -47.431 -1.402  7.861   1.00 12.23 ? 357  LYS   B O   1 
ATOM   6872 C  CB  . LYS   B 1 334 ? -45.844 0.332   5.850   1.00 19.12 ? 357  LYS   B CB  1 
ATOM   6873 C  CG  . LYS   B 1 334 ? -45.647 1.585   4.975   1.00 24.37 ? 357  LYS   B CG  1 
ATOM   6874 C  CD  . LYS   B 1 334 ? -45.699 1.231   3.499   1.00 29.03 ? 357  LYS   B CD  1 
ATOM   6875 C  CE  . LYS   B 1 334 ? -45.323 2.324   2.545   1.00 36.68 ? 357  LYS   B CE  1 
ATOM   6876 N  NZ  . LYS   B 1 334 ? -44.922 1.666   1.294   1.00 41.69 ? 357  LYS   B NZ  1 
ATOM   6877 N  N   . PHE   B 1 335 ? -47.032 -2.718  6.084   1.00 12.88 ? 358  PHE   B N   1 
ATOM   6878 C  CA  . PHE   B 1 335 ? -47.005 -3.922  6.898   1.00 11.90 ? 358  PHE   B CA  1 
ATOM   6879 C  C   . PHE   B 1 335 ? -45.696 -3.948  7.693   1.00 12.44 ? 358  PHE   B C   1 
ATOM   6880 O  O   . PHE   B 1 335 ? -44.623 -3.716  7.147   1.00 12.65 ? 358  PHE   B O   1 
ATOM   6881 C  CB  . PHE   B 1 335 ? -47.118 -5.162  6.022   1.00 11.63 ? 358  PHE   B CB  1 
ATOM   6882 C  CG  . PHE   B 1 335 ? -46.763 -6.434  6.766   1.00 10.80 ? 358  PHE   B CG  1 
ATOM   6883 C  CD1 . PHE   B 1 335 ? -47.374 -6.754  7.967   1.00 11.30 ? 358  PHE   B CD1 1 
ATOM   6884 C  CD2 . PHE   B 1 335 ? -45.838 -7.330  6.245   1.00 11.13 ? 358  PHE   B CD2 1 
ATOM   6885 C  CE1 . PHE   B 1 335 ? -47.072 -7.933  8.643   1.00 11.59 ? 358  PHE   B CE1 1 
ATOM   6886 C  CE2 . PHE   B 1 335 ? -45.548 -8.505  6.906   1.00 11.98 ? 358  PHE   B CE2 1 
ATOM   6887 C  CZ  . PHE   B 1 335 ? -46.152 -8.787  8.131   1.00 12.32 ? 358  PHE   B CZ  1 
ATOM   6888 N  N   . VAL   B 1 336 ? -45.803 -4.239  8.986   1.00 11.42 ? 359  VAL   B N   1 
ATOM   6889 C  CA  . VAL   B 1 336 ? -44.661 -4.638  9.789   1.00 10.91 ? 359  VAL   B CA  1 
ATOM   6890 C  C   . VAL   B 1 336 ? -45.099 -5.830  10.612  1.00 10.41 ? 359  VAL   B C   1 
ATOM   6891 O  O   . VAL   B 1 336 ? -46.198 -5.827  11.147  1.00 10.25 ? 359  VAL   B O   1 
ATOM   6892 C  CB  . VAL   B 1 336 ? -44.043 -3.527  10.662  1.00 12.30 ? 359  VAL   B CB  1 
ATOM   6893 C  CG1 . VAL   B 1 336 ? -45.005 -3.004  11.712  1.00 13.96 ? 359  VAL   B CG1 1 
ATOM   6894 C  CG2 . VAL   B 1 336 ? -42.758 -3.965  11.336  1.00 11.50 ? 359  VAL   B CG2 1 
ATOM   6895 N  N   . PHE   B 1 337 ? -44.252 -6.857  10.666  1.00 9.26  ? 360  PHE   B N   1 
ATOM   6896 C  CA  . PHE   B 1 337 ? -44.562 -8.024  11.468  1.00 9.11  ? 360  PHE   B CA  1 
ATOM   6897 C  C   . PHE   B 1 337 ? -44.577 -7.601  12.938  1.00 9.53  ? 360  PHE   B C   1 
ATOM   6898 O  O   . PHE   B 1 337 ? -43.690 -6.863  13.370  1.00 9.46  ? 360  PHE   B O   1 
ATOM   6899 C  CB  . PHE   B 1 337 ? -43.544 -9.138  11.233  1.00 8.85  ? 360  PHE   B CB  1 
ATOM   6900 C  CG  . PHE   B 1 337 ? -43.940 -10.442 11.899  1.00 8.53  ? 360  PHE   B CG  1 
ATOM   6901 C  CD1 . PHE   B 1 337 ? -43.694 -10.642 13.251  1.00 8.32  ? 360  PHE   B CD1 1 
ATOM   6902 C  CD2 . PHE   B 1 337 ? -44.587 -11.447 11.184  1.00 8.34  ? 360  PHE   B CD2 1 
ATOM   6903 C  CE1 . PHE   B 1 337 ? -44.019 -11.834 13.858  1.00 8.56  ? 360  PHE   B CE1 1 
ATOM   6904 C  CE2 . PHE   B 1 337 ? -44.962 -12.618 11.807  1.00 8.46  ? 360  PHE   B CE2 1 
ATOM   6905 C  CZ  . PHE   B 1 337 ? -44.691 -12.808 13.148  1.00 8.57  ? 360  PHE   B CZ  1 
ATOM   6906 N  N   . GLN   B 1 338 ? -45.561 -8.096  13.688  1.00 9.94  ? 361  GLN   B N   1 
ATOM   6907 C  CA  . GLN   B 1 338 ? -45.660 -7.762  15.104  1.00 9.63  ? 361  GLN   B CA  1 
ATOM   6908 C  C   . GLN   B 1 338 ? -45.161 -8.964  15.878  1.00 9.10  ? 361  GLN   B C   1 
ATOM   6909 O  O   . GLN   B 1 338 ? -45.862 -9.979  15.964  1.00 8.96  ? 361  GLN   B O   1 
ATOM   6910 C  CB  . GLN   B 1 338 ? -47.084 -7.384  15.480  1.00 9.61  ? 361  GLN   B CB  1 
ATOM   6911 C  CG  . GLN   B 1 338 ? -47.694 -6.367  14.517  1.00 10.74 ? 361  GLN   B CG  1 
ATOM   6912 C  CD  . GLN   B 1 338 ? -49.003 -5.787  15.014  1.00 11.49 ? 361  GLN   B CD  1 
ATOM   6913 O  OE1 . GLN   B 1 338 ? -49.445 -6.105  16.123  1.00 12.53 ? 361  GLN   B OE1 1 
ATOM   6914 N  NE2 . GLN   B 1 338 ? -49.648 -4.958  14.196  1.00 11.55 ? 361  GLN   B NE2 1 
ATOM   6915 N  N   . THR   B 1 339 ? -43.935 -8.842  16.388  1.00 9.29  ? 362  THR   B N   1 
ATOM   6916 C  CA  . THR   B 1 339 ? -43.342 -9.897  17.192  1.00 8.38  ? 362  THR   B CA  1 
ATOM   6917 C  C   . THR   B 1 339 ? -43.435 -9.440  18.649  1.00 8.49  ? 362  THR   B C   1 
ATOM   6918 O  O   . THR   B 1 339 ? -42.820 -8.449  19.055  1.00 9.56  ? 362  THR   B O   1 
ATOM   6919 C  CB  . THR   B 1 339 ? -41.923 -10.271 16.752  1.00 8.55  ? 362  THR   B CB  1 
ATOM   6920 O  OG1 . THR   B 1 339 ? -41.437 -11.187 17.735  1.00 7.56  ? 362  THR   B OG1 1 
ATOM   6921 C  CG2 . THR   B 1 339 ? -40.931 -9.128  16.710  1.00 8.88  ? 362  THR   B CG2 1 
ATOM   6922 N  N   . GLY   B 1 340 ? -44.212 -10.172 19.437  1.00 8.77  ? 363  GLY   B N   1 
ATOM   6923 C  CA  . GLY   B 1 340 ? -44.505 -9.786  20.803  1.00 9.23  ? 363  GLY   B CA  1 
ATOM   6924 C  C   . GLY   B 1 340 ? -44.339 -10.933 21.785  1.00 9.71  ? 363  GLY   B C   1 
ATOM   6925 O  O   . GLY   B 1 340 ? -44.015 -12.082 21.407  1.00 9.00  ? 363  GLY   B O   1 
ATOM   6926 N  N   . THR   B 1 341 ? -44.577 -10.591 23.071  1.00 10.38 ? 364  THR   B N   1 
ATOM   6927 C  CA  . THR   B 1 341 ? -44.725 -11.617 24.089  1.00 10.03 ? 364  THR   B CA  1 
ATOM   6928 C  C   . THR   B 1 341 ? -46.138 -11.647 24.649  1.00 9.78  ? 364  THR   B C   1 
ATOM   6929 O  O   . THR   B 1 341 ? -46.902 -10.682 24.565  1.00 10.59 ? 364  THR   B O   1 
ATOM   6930 C  CB  . THR   B 1 341 ? -43.742 -11.488 25.264  1.00 9.76  ? 364  THR   B CB  1 
ATOM   6931 O  OG1 . THR   B 1 341 ? -44.292 -10.553 26.172  1.00 10.50 ? 364  THR   B OG1 1 
ATOM   6932 C  CG2 . THR   B 1 341 ? -42.336 -11.113 24.845  1.00 9.92  ? 364  THR   B CG2 1 
ATOM   6933 N  N   . LEU   B 1 342 ? -46.464 -12.792 25.252  1.00 9.33  ? 365  LEU   B N   1 
ATOM   6934 C  CA  . LEU   B 1 342 ? -47.558 -12.867 26.210  1.00 9.07  ? 365  LEU   B CA  1 
ATOM   6935 C  C   . LEU   B 1 342 ? -47.064 -12.300 27.542  1.00 9.38  ? 365  LEU   B C   1 
ATOM   6936 O  O   . LEU   B 1 342 ? -46.050 -12.745 28.069  1.00 10.54 ? 365  LEU   B O   1 
ATOM   6937 C  CB  . LEU   B 1 342 ? -48.030 -14.310 26.388  1.00 9.41  ? 365  LEU   B CB  1 
ATOM   6938 C  CG  . LEU   B 1 342 ? -49.419 -14.499 27.012  1.00 9.97  ? 365  LEU   B CG  1 
ATOM   6939 C  CD1 . LEU   B 1 342 ? -50.536 -14.148 26.021  1.00 9.87  ? 365  LEU   B CD1 1 
ATOM   6940 C  CD2 . LEU   B 1 342 ? -49.570 -15.929 27.509  1.00 10.33 ? 365  LEU   B CD2 1 
ATOM   6941 N  N   . ASP   B 1 343 ? -47.821 -11.355 28.092  1.00 9.83  ? 366  ASP   B N   1 
ATOM   6942 C  CA  . ASP   B 1 343 ? -47.480 -10.683 29.325  1.00 10.43 ? 366  ASP   B CA  1 
ATOM   6943 C  C   . ASP   B 1 343 ? -48.717 -10.667 30.220  1.00 10.49 ? 366  ASP   B C   1 
ATOM   6944 O  O   . ASP   B 1 343 ? -49.726 -10.047 29.899  1.00 11.00 ? 366  ASP   B O   1 
ATOM   6945 C  CB  . ASP   B 1 343 ? -47.024 -9.269  29.014  1.00 10.71 ? 366  ASP   B CB  1 
ATOM   6946 C  CG  . ASP   B 1 343 ? -46.580 -8.413  30.185  1.00 11.65 ? 366  ASP   B CG  1 
ATOM   6947 O  OD1 . ASP   B 1 343 ? -47.159 -8.596  31.310  1.00 12.19 ? 366  ASP   B OD1 1 
ATOM   6948 O  OD2 . ASP   B 1 343 ? -45.719 -7.477  29.935  1.00 12.55 ? 366  ASP   B OD2 1 
ATOM   6949 N  N   . GLN   B 1 344 ? -48.630 -11.417 31.321  1.00 11.46 ? 367  GLN   B N   1 
ATOM   6950 C  CA  . GLN   B 1 344 ? -49.773 -11.659 32.168  1.00 12.12 ? 367  GLN   B CA  1 
ATOM   6951 C  C   . GLN   B 1 344 ? -49.899 -10.645 33.295  1.00 12.12 ? 367  GLN   B C   1 
ATOM   6952 O  O   . GLN   B 1 344 ? -50.914 -10.616 33.987  1.00 12.28 ? 367  GLN   B O   1 
ATOM   6953 C  CB  . GLN   B 1 344 ? -49.610 -13.081 32.702  1.00 12.64 ? 367  GLN   B CB  1 
ATOM   6954 C  CG  . GLN   B 1 344 ? -49.643 -14.143 31.620  1.00 11.99 ? 367  GLN   B CG  1 
ATOM   6955 C  CD  . GLN   B 1 344 ? -50.030 -15.481 32.179  1.00 12.87 ? 367  GLN   B CD  1 
ATOM   6956 O  OE1 . GLN   B 1 344 ? -51.211 -15.738 32.399  1.00 11.63 ? 367  GLN   B OE1 1 
ATOM   6957 N  NE2 . GLN   B 1 344 ? -49.052 -16.358 32.371  1.00 12.34 ? 367  GLN   B NE2 1 
ATOM   6958 N  N   . GLY   B 1 345 ? -48.901 -9.768  33.477  1.00 11.94 ? 368  GLY   B N   1 
ATOM   6959 C  CA  . GLY   B 1 345 ? -49.044 -8.675  34.427  1.00 11.82 ? 368  GLY   B CA  1 
ATOM   6960 C  C   . GLY   B 1 345 ? -49.118 -9.131  35.890  1.00 12.98 ? 368  GLY   B C   1 
ATOM   6961 O  O   . GLY   B 1 345 ? -49.810 -8.473  36.674  1.00 14.98 ? 368  GLY   B O   1 
ATOM   6962 N  N   . TYR   B 1 346 ? -48.478 -10.265 36.215  1.00 13.49 ? 369  TYR   B N   1 
ATOM   6963 C  CA  . TYR   B 1 346 ? -48.445 -10.764 37.586  1.00 14.73 ? 369  TYR   B CA  1 
ATOM   6964 C  C   . TYR   B 1 346 ? -47.110 -10.417 38.246  1.00 15.84 ? 369  TYR   B C   1 
ATOM   6965 O  O   . TYR   B 1 346 ? -46.050 -10.404 37.597  1.00 14.77 ? 369  TYR   B O   1 
ATOM   6966 C  CB  . TYR   B 1 346 ? -48.680 -12.265 37.578  1.00 14.91 ? 369  TYR   B CB  1 
ATOM   6967 C  CG  . TYR   B 1 346 ? -50.107 -12.657 37.937  1.00 15.01 ? 369  TYR   B CG  1 
ATOM   6968 C  CD1 . TYR   B 1 346 ? -51.147 -12.609 37.010  1.00 16.08 ? 369  TYR   B CD1 1 
ATOM   6969 C  CD2 . TYR   B 1 346 ? -50.402 -13.101 39.230  1.00 16.39 ? 369  TYR   B CD2 1 
ATOM   6970 C  CE1 . TYR   B 1 346 ? -52.438 -12.997 37.362  1.00 16.16 ? 369  TYR   B CE1 1 
ATOM   6971 C  CE2 . TYR   B 1 346 ? -51.687 -13.493 39.594  1.00 16.73 ? 369  TYR   B CE2 1 
ATOM   6972 C  CZ  . TYR   B 1 346 ? -52.711 -13.422 38.658  1.00 16.95 ? 369  TYR   B CZ  1 
ATOM   6973 O  OH  . TYR   B 1 346 ? -53.952 -13.843 39.033  1.00 16.83 ? 369  TYR   B OH  1 
ATOM   6974 N  N   . TRP   B 1 347 ? -47.178 -10.299 39.580  1.00 16.44 ? 370  TRP   B N   1 
ATOM   6975 C  CA  . TRP   B 1 347 ? -46.030 -9.934  40.392  1.00 17.99 ? 370  TRP   B CA  1 
ATOM   6976 C  C   . TRP   B 1 347 ? -45.993 -10.787 41.656  1.00 18.78 ? 370  TRP   B C   1 
ATOM   6977 O  O   . TRP   B 1 347 ? -47.045 -11.006 42.252  1.00 18.08 ? 370  TRP   B O   1 
ATOM   6978 C  CB  . TRP   B 1 347 ? -46.178 -8.457  40.741  1.00 17.30 ? 370  TRP   B CB  1 
ATOM   6979 C  CG  . TRP   B 1 347 ? -46.010 -7.534  39.565  1.00 17.34 ? 370  TRP   B CG  1 
ATOM   6980 C  CD1 . TRP   B 1 347 ? -46.934 -7.062  38.672  1.00 16.62 ? 370  TRP   B CD1 1 
ATOM   6981 C  CD2 . TRP   B 1 347 ? -44.751 -6.977  39.159  1.00 18.61 ? 370  TRP   B CD2 1 
ATOM   6982 N  NE1 . TRP   B 1 347 ? -46.342 -6.246  37.756  1.00 16.10 ? 370  TRP   B NE1 1 
ATOM   6983 C  CE2 . TRP   B 1 347 ? -45.005 -6.174  38.023  1.00 16.79 ? 370  TRP   B CE2 1 
ATOM   6984 C  CE3 . TRP   B 1 347 ? -43.449 -7.081  39.662  1.00 18.11 ? 370  TRP   B CE3 1 
ATOM   6985 C  CZ2 . TRP   B 1 347 ? -43.988 -5.477  37.376  1.00 17.12 ? 370  TRP   B CZ2 1 
ATOM   6986 C  CZ3 . TRP   B 1 347 ? -42.447 -6.392  39.017  1.00 18.12 ? 370  TRP   B CZ3 1 
ATOM   6987 C  CH2 . TRP   B 1 347 ? -42.712 -5.625  37.879  1.00 17.80 ? 370  TRP   B CH2 1 
ATOM   6988 N  N   . PRO   B 1 348 ? -44.835 -11.354 42.086  1.00 20.48 ? 371  PRO   B N   1 
ATOM   6989 C  CA  . PRO   B 1 348 ? -44.826 -12.242 43.251  1.00 20.51 ? 371  PRO   B CA  1 
ATOM   6990 C  C   . PRO   B 1 348 ? -45.124 -11.470 44.531  1.00 21.83 ? 371  PRO   B C   1 
ATOM   6991 O  O   . PRO   B 1 348 ? -45.656 -12.054 45.479  1.00 22.46 ? 371  PRO   B O   1 
ATOM   6992 C  CB  . PRO   B 1 348 ? -43.421 -12.881 43.221  1.00 21.01 ? 371  PRO   B CB  1 
ATOM   6993 C  CG  . PRO   B 1 348 ? -42.584 -11.835 42.585  1.00 21.08 ? 371  PRO   B CG  1 
ATOM   6994 C  CD  . PRO   B 1 348 ? -43.485 -11.191 41.520  1.00 22.47 ? 371  PRO   B CD  1 
ATOM   6995 N  N   . ASP   B 1 349 ? -44.841 -10.156 44.509  1.00 21.31 ? 372  ASP   B N   1 
ATOM   6996 C  CA  . ASP   B 1 349 ? -44.905 -9.303  45.678  1.00 22.87 ? 372  ASP   B CA  1 
ATOM   6997 C  C   . ASP   B 1 349 ? -46.241 -8.566  45.700  1.00 23.46 ? 372  ASP   B C   1 
ATOM   6998 O  O   . ASP   B 1 349 ? -46.829 -8.419  46.768  1.00 25.84 ? 372  ASP   B O   1 
ATOM   6999 C  CB  . ASP   B 1 349 ? -43.674 -8.400  45.759  1.00 24.02 ? 372  ASP   B CB  1 
ATOM   7000 C  CG  . ASP   B 1 349 ? -43.306 -7.618  44.499  1.00 25.78 ? 372  ASP   B CG  1 
ATOM   7001 O  OD1 . ASP   B 1 349 ? -43.992 -7.832  43.478  1.00 22.40 ? 372  ASP   B OD1 1 
ATOM   7002 O  OD2 . ASP   B 1 349 ? -42.352 -6.780  44.553  1.00 21.79 ? 372  ASP   B OD2 1 
ATOM   7003 N  N   . GLY   B 1 350 ? -46.727 -8.101  44.529  1.00 20.07 ? 373  GLY   B N   1 
ATOM   7004 C  CA  . GLY   B 1 350 ? -47.909 -7.250  44.456  1.00 18.25 ? 373  GLY   B CA  1 
ATOM   7005 C  C   . GLY   B 1 350 ? -49.128 -7.949  43.833  1.00 17.47 ? 373  GLY   B C   1 
ATOM   7006 O  O   . GLY   B 1 350 ? -50.208 -7.356  43.777  1.00 20.08 ? 373  GLY   B O   1 
ATOM   7007 N  N   . ILE   B 1 351 ? -48.931 -9.184  43.375  1.00 19.15 ? 374  ILE   B N   1 
ATOM   7008 C  CA  . ILE   B 1 351 ? -49.927 -9.977  42.661  1.00 19.36 ? 374  ILE   B CA  1 
ATOM   7009 C  C   . ILE   B 1 351 ? -50.362 -9.218  41.403  1.00 17.64 ? 374  ILE   B C   1 
ATOM   7010 O  O   . ILE   B 1 351 ? -49.785 -9.438  40.341  1.00 18.22 ? 374  ILE   B O   1 
ATOM   7011 C  CB  . ILE   B 1 351 ? -51.102 -10.402 43.568  1.00 19.59 ? 374  ILE   B CB  1 
ATOM   7012 C  CG1 . ILE   B 1 351 ? -50.608 -11.019 44.881  1.00 19.48 ? 374  ILE   B CG1 1 
ATOM   7013 C  CG2 . ILE   B 1 351 ? -52.015 -11.384 42.825  1.00 18.41 ? 374  ILE   B CG2 1 
ATOM   7014 C  CD1 . ILE   B 1 351 ? -49.835 -12.311 44.690  1.00 19.36 ? 374  ILE   B CD1 1 
ATOM   7015 N  N   . TYR   B 1 352 ? -51.363 -8.337  41.510  1.00 18.05 ? 375  TYR   B N   1 
ATOM   7016 C  CA  . TYR   B 1 352 ? -51.912 -7.626  40.364  1.00 16.50 ? 375  TYR   B CA  1 
ATOM   7017 C  C   . TYR   B 1 352 ? -51.319 -6.231  40.209  1.00 16.64 ? 375  TYR   B C   1 
ATOM   7018 O  O   . TYR   B 1 352 ? -51.541 -5.589  39.183  1.00 15.65 ? 375  TYR   B O   1 
ATOM   7019 C  CB  . TYR   B 1 352 ? -53.431 -7.446  40.448  1.00 16.06 ? 375  TYR   B CB  1 
ATOM   7020 C  CG  . TYR   B 1 352 ? -54.271 -8.294  39.490  1.00 15.57 ? 375  TYR   B CG  1 
ATOM   7021 C  CD1 . TYR   B 1 352 ? -53.808 -9.498  38.976  1.00 15.15 ? 375  TYR   B CD1 1 
ATOM   7022 C  CD2 . TYR   B 1 352 ? -55.487 -7.803  39.018  1.00 15.56 ? 375  TYR   B CD2 1 
ATOM   7023 C  CE1 . TYR   B 1 352 ? -54.577 -10.252 38.098  1.00 15.19 ? 375  TYR   B CE1 1 
ATOM   7024 C  CE2 . TYR   B 1 352 ? -56.271 -8.546  38.143  1.00 16.24 ? 375  TYR   B CE2 1 
ATOM   7025 C  CZ  . TYR   B 1 352 ? -55.794 -9.753  37.659  1.00 15.43 ? 375  TYR   B CZ  1 
ATOM   7026 O  OH  . TYR   B 1 352 ? -56.536 -10.457 36.742  1.00 15.53 ? 375  TYR   B OH  1 
ATOM   7027 N  N   . THR   B 1 353 ? -50.568 -5.752  41.216  1.00 17.44 ? 376  THR   B N   1 
ATOM   7028 C  CA  . THR   B 1 353 ? -50.116 -4.376  41.231  1.00 17.06 ? 376  THR   B CA  1 
ATOM   7029 C  C   . THR   B 1 353 ? -48.585 -4.383  41.244  1.00 19.15 ? 376  THR   B C   1 
ATOM   7030 O  O   . THR   B 1 353 ? -47.962 -5.055  42.076  1.00 18.93 ? 376  THR   B O   1 
ATOM   7031 C  CB  . THR   B 1 353 ? -50.673 -3.647  42.455  1.00 18.70 ? 376  THR   B CB  1 
ATOM   7032 O  OG1 . THR   B 1 353 ? -52.102 -3.710  42.445  1.00 19.79 ? 376  THR   B OG1 1 
ATOM   7033 C  CG2 . THR   B 1 353 ? -50.263 -2.193  42.490  1.00 17.74 ? 376  THR   B CG2 1 
ATOM   7034 N  N   . ALA   B 1 354 ? -48.003 -3.674  40.274  1.00 16.75 ? 377  ALA   B N   1 
ATOM   7035 C  CA  . ALA   B 1 354 ? -46.555 -3.520  40.216  1.00 18.54 ? 377  ALA   B CA  1 
ATOM   7036 C  C   . ALA   B 1 354 ? -46.092 -2.697  41.424  1.00 17.99 ? 377  ALA   B C   1 
ATOM   7037 O  O   . ALA   B 1 354 ? -46.715 -1.689  41.744  1.00 17.99 ? 377  ALA   B O   1 
ATOM   7038 C  CB  . ALA   B 1 354 ? -46.150 -2.864  38.926  1.00 17.85 ? 377  ALA   B CB  1 
ATOM   7039 N  N   . PRO   B 1 355 ? -45.008 -3.099  42.127  1.00 19.22 ? 378  PRO   B N   1 
ATOM   7040 C  CA  . PRO   B 1 355 ? -44.574 -2.377  43.335  1.00 19.84 ? 378  PRO   B CA  1 
ATOM   7041 C  C   . PRO   B 1 355 ? -44.387 -0.861  43.202  1.00 20.82 ? 378  PRO   B C   1 
ATOM   7042 O  O   . PRO   B 1 355 ? -44.803 -0.095  44.075  1.00 21.16 ? 378  PRO   B O   1 
ATOM   7043 C  CB  . PRO   B 1 355 ? -43.286 -3.126  43.755  1.00 19.52 ? 378  PRO   B CB  1 
ATOM   7044 C  CG  . PRO   B 1 355 ? -42.947 -4.066  42.622  1.00 19.22 ? 378  PRO   B CG  1 
ATOM   7045 C  CD  . PRO   B 1 355 ? -44.281 -4.362  41.943  1.00 18.94 ? 378  PRO   B CD  1 
ATOM   7046 N  N   . THR   B 1 356 ? -43.761 -0.429  42.103  1.00 17.66 ? 379  THR   B N   1 
ATOM   7047 C  CA  . THR   B 1 356 ? -43.476 0.962   41.828  1.00 19.28 ? 379  THR   B CA  1 
ATOM   7048 C  C   . THR   B 1 356 ? -43.701 1.194   40.342  1.00 18.95 ? 379  THR   B C   1 
ATOM   7049 O  O   . THR   B 1 356 ? -43.803 0.226   39.597  1.00 20.84 ? 379  THR   B O   1 
ATOM   7050 C  CB  . THR   B 1 356 ? -42.021 1.301   42.201  1.00 21.11 ? 379  THR   B CB  1 
ATOM   7051 O  OG1 . THR   B 1 356 ? -41.166 0.543   41.340  1.00 20.18 ? 379  THR   B OG1 1 
ATOM   7052 C  CG2 . THR   B 1 356 ? -41.688 1.009   43.653  1.00 19.79 ? 379  THR   B CG2 1 
ATOM   7053 N  N   . ASP   B 1 357 ? -43.734 2.468   39.940  1.00 18.78 ? 380  ASP   B N   1 
ATOM   7054 C  CA  . ASP   B 1 357 ? -43.891 2.834   38.543  1.00 19.40 ? 380  ASP   B CA  1 
ATOM   7055 C  C   . ASP   B 1 357 ? -42.704 2.317   37.717  1.00 20.87 ? 380  ASP   B C   1 
ATOM   7056 O  O   . ASP   B 1 357 ? -42.869 1.906   36.559  1.00 20.25 ? 380  ASP   B O   1 
ATOM   7057 C  CB  . ASP   B 1 357 ? -44.033 4.329   38.407  1.00 18.99 ? 380  ASP   B CB  1 
ATOM   7058 C  CG  . ASP   B 1 357 ? -44.610 4.788   37.080  1.00 20.20 ? 380  ASP   B CG  1 
ATOM   7059 O  OD1 . ASP   B 1 357 ? -45.715 4.304   36.727  1.00 17.74 ? 380  ASP   B OD1 1 
ATOM   7060 O  OD2 . ASP   B 1 357 ? -43.978 5.639   36.439  1.00 19.29 ? 380  ASP   B OD2 1 
ATOM   7061 N  N   . ALA   B 1 358 ? -41.504 2.309   38.322  1.00 19.86 ? 381  ALA   B N   1 
ATOM   7062 C  CA  . ALA   B 1 358 ? -40.340 1.738   37.656  1.00 17.86 ? 381  ALA   B CA  1 
ATOM   7063 C  C   . ALA   B 1 358 ? -40.533 0.242   37.361  1.00 17.46 ? 381  ALA   B C   1 
ATOM   7064 O  O   . ALA   B 1 358 ? -40.116 -0.272  36.297  1.00 13.99 ? 381  ALA   B O   1 
ATOM   7065 C  CB  . ALA   B 1 358 ? -39.101 1.983   38.505  1.00 17.08 ? 381  ALA   B CB  1 
ATOM   7066 N  N   . ALA   B 1 359 ? -41.115 -0.476  38.329  1.00 16.43 ? 382  ALA   B N   1 
ATOM   7067 C  CA  . ALA   B 1 359 ? -41.381 -1.896  38.178  1.00 16.87 ? 382  ALA   B CA  1 
ATOM   7068 C  C   . ALA   B 1 359 ? -42.362 -2.094  37.019  1.00 17.14 ? 382  ALA   B C   1 
ATOM   7069 O  O   . ALA   B 1 359 ? -42.159 -2.988  36.207  1.00 15.16 ? 382  ALA   B O   1 
ATOM   7070 C  CB  . ALA   B 1 359 ? -41.910 -2.469  39.460  1.00 16.33 ? 382  ALA   B CB  1 
ATOM   7071 N  N   . LEU   B 1 360 ? -43.431 -1.279  37.006  1.00 17.38 ? 383  LEU   B N   1 
ATOM   7072 C  CA  . LEU   B 1 360 ? -44.432 -1.318  35.945  1.00 18.68 ? 383  LEU   B CA  1 
ATOM   7073 C  C   . LEU   B 1 360 ? -43.766 -1.115  34.587  1.00 17.70 ? 383  LEU   B C   1 
ATOM   7074 O  O   . LEU   B 1 360 ? -43.980 -1.929  33.687  1.00 20.39 ? 383  LEU   B O   1 
ATOM   7075 C  CB  . LEU   B 1 360 ? -45.498 -0.261  36.211  1.00 18.23 ? 383  LEU   B CB  1 
ATOM   7076 C  CG  . LEU   B 1 360 ? -46.686 -0.225  35.257  1.00 17.52 ? 383  LEU   B CG  1 
ATOM   7077 C  CD1 . LEU   B 1 360 ? -47.559 -1.452  35.411  1.00 16.86 ? 383  LEU   B CD1 1 
ATOM   7078 C  CD2 . LEU   B 1 360 ? -47.478 1.045   35.470  1.00 18.08 ? 383  LEU   B CD2 1 
ATOM   7079 N  N   . ARG   B 1 361 ? -42.935 -0.063  34.453  1.00 17.59 ? 384  ARG   B N   1 
ATOM   7080 C  CA  . ARG   B 1 361 ? -42.266 0.290   33.192  1.00 19.40 ? 384  ARG   B CA  1 
ATOM   7081 C  C   . ARG   B 1 361 ? -41.285 -0.820  32.766  1.00 16.15 ? 384  ARG   B C   1 
ATOM   7082 O  O   . ARG   B 1 361 ? -41.041 -1.076  31.582  1.00 12.72 ? 384  ARG   B O   1 
ATOM   7083 C  CB  . ARG   B 1 361 ? -41.537 1.630   33.439  1.00 24.41 ? 384  ARG   B CB  1 
ATOM   7084 C  CG  . ARG   B 1 361 ? -40.778 2.248   32.269  1.00 34.99 ? 384  ARG   B CG  1 
ATOM   7085 C  CD  . ARG   B 1 361 ? -39.614 3.198   32.642  1.00 42.73 ? 384  ARG   B CD  1 
ATOM   7086 N  NE  . ARG   B 1 361 ? -38.761 3.421   31.458  1.00 49.83 ? 384  ARG   B NE  1 
ATOM   7087 C  CZ  . ARG   B 1 361 ? -37.585 2.838   31.124  1.00 45.68 ? 384  ARG   B CZ  1 
ATOM   7088 N  NH1 . ARG   B 1 361 ? -36.887 2.171   32.027  1.00 41.14 ? 384  ARG   B NH1 1 
ATOM   7089 N  NH2 . ARG   B 1 361 ? -37.082 2.964   29.886  1.00 39.13 ? 384  ARG   B NH2 1 
ATOM   7090 N  N   . HIS   B 1 362 ? -40.680 -1.477  33.750  1.00 13.68 ? 385  HIS   B N   1 
ATOM   7091 C  CA  . HIS   B 1 362 ? -39.550 -2.360  33.522  1.00 14.39 ? 385  HIS   B CA  1 
ATOM   7092 C  C   . HIS   B 1 362 ? -39.894 -3.436  32.491  1.00 14.65 ? 385  HIS   B C   1 
ATOM   7093 O  O   . HIS   B 1 362 ? -39.085 -3.752  31.619  1.00 15.63 ? 385  HIS   B O   1 
ATOM   7094 C  CB  . HIS   B 1 362 ? -39.138 -3.024  34.843  1.00 14.09 ? 385  HIS   B CB  1 
ATOM   7095 C  CG  . HIS   B 1 362 ? -38.185 -4.131  34.676  1.00 15.01 ? 385  HIS   B CG  1 
ATOM   7096 N  ND1 . HIS   B 1 362 ? -38.611 -5.443  34.540  1.00 15.61 ? 385  HIS   B ND1 1 
ATOM   7097 C  CD2 . HIS   B 1 362 ? -36.850 -4.132  34.532  1.00 14.28 ? 385  HIS   B CD2 1 
ATOM   7098 C  CE1 . HIS   B 1 362 ? -37.537 -6.206  34.399  1.00 16.34 ? 385  HIS   B CE1 1 
ATOM   7099 N  NE2 . HIS   B 1 362 ? -36.472 -5.434  34.398  1.00 14.75 ? 385  HIS   B NE2 1 
ATOM   7100 N  N   . ASP   B 1 363 ? -41.061 -4.093  32.644  1.00 13.60 ? 386  ASP   B N   1 
ATOM   7101 C  CA  . ASP   B 1 363 ? -41.353 -5.241  31.798  1.00 13.75 ? 386  ASP   B CA  1 
ATOM   7102 C  C   . ASP   B 1 363 ? -41.447 -4.787  30.341  1.00 12.30 ? 386  ASP   B C   1 
ATOM   7103 O  O   . ASP   B 1 363 ? -41.088 -5.557  29.458  1.00 13.86 ? 386  ASP   B O   1 
ATOM   7104 C  CB  . ASP   B 1 363 ? -42.616 -5.963  32.236  1.00 13.79 ? 386  ASP   B CB  1 
ATOM   7105 C  CG  . ASP   B 1 363 ? -42.630 -6.521  33.660  1.00 15.58 ? 386  ASP   B CG  1 
ATOM   7106 O  OD1 . ASP   B 1 363 ? -41.532 -6.824  34.226  1.00 16.12 ? 386  ASP   B OD1 1 
ATOM   7107 O  OD2 . ASP   B 1 363 ? -43.752 -6.668  34.194  1.00 15.46 ? 386  ASP   B OD2 1 
ATOM   7108 N  N   . LEU   B 1 364 ? -41.868 -3.542  30.115  1.00 11.78 ? 387  LEU   B N   1 
ATOM   7109 C  CA  . LEU   B 1 364 ? -41.960 -2.992  28.760  1.00 12.68 ? 387  LEU   B CA  1 
ATOM   7110 C  C   . LEU   B 1 364 ? -40.567 -2.632  28.237  1.00 13.55 ? 387  LEU   B C   1 
ATOM   7111 O  O   . LEU   B 1 364 ? -40.237 -2.846  27.067  1.00 12.74 ? 387  LEU   B O   1 
ATOM   7112 C  CB  . LEU   B 1 364 ? -42.902 -1.789  28.775  1.00 12.20 ? 387  LEU   B CB  1 
ATOM   7113 C  CG  . LEU   B 1 364 ? -44.347 -2.078  29.184  1.00 12.99 ? 387  LEU   B CG  1 
ATOM   7114 C  CD1 . LEU   B 1 364 ? -45.193 -0.808  29.111  1.00 12.76 ? 387  LEU   B CD1 1 
ATOM   7115 C  CD2 . LEU   B 1 364 ? -44.959 -3.235  28.362  1.00 14.12 ? 387  LEU   B CD2 1 
ATOM   7116 N  N   . GLN   B 1 365 ? -39.743 -2.042  29.110  1.00 13.15 ? 388  GLN   B N   1 
ATOM   7117 C  CA  . GLN   B 1 365 ? -38.357 -1.790  28.741  1.00 13.26 ? 388  GLN   B CA  1 
ATOM   7118 C  C   . GLN   B 1 365 ? -37.677 -3.103  28.344  1.00 11.84 ? 388  GLN   B C   1 
ATOM   7119 O  O   . GLN   B 1 365 ? -36.942 -3.128  27.364  1.00 12.00 ? 388  GLN   B O   1 
ATOM   7120 C  CB  . GLN   B 1 365 ? -37.551 -1.047  29.810  1.00 14.64 ? 388  GLN   B CB  1 
ATOM   7121 C  CG  . GLN   B 1 365 ? -36.110 -0.728  29.396  1.00 15.96 ? 388  GLN   B CG  1 
ATOM   7122 C  CD  . GLN   B 1 365 ? -36.009 0.111   28.132  1.00 18.35 ? 388  GLN   B CD  1 
ATOM   7123 O  OE1 . GLN   B 1 365 ? -36.746 1.089   27.926  1.00 14.61 ? 388  GLN   B OE1 1 
ATOM   7124 N  NE2 . GLN   B 1 365 ? -35.118 -0.295  27.236  1.00 20.19 ? 388  GLN   B NE2 1 
ATOM   7125 N  N   . LYS   B 1 366 ? -37.976 -4.216  29.026  1.00 11.97 ? 389  LYS   B N   1 
ATOM   7126 C  CA  . LYS   B 1 366 ? -37.354 -5.478  28.673  1.00 11.42 ? 389  LYS   B CA  1 
ATOM   7127 C  C   . LYS   B 1 366 ? -37.832 -5.952  27.300  1.00 11.18 ? 389  LYS   B C   1 
ATOM   7128 O  O   . LYS   B 1 366 ? -37.030 -6.539  26.593  1.00 10.54 ? 389  LYS   B O   1 
ATOM   7129 C  CB  . LYS   B 1 366 ? -37.533 -6.552  29.746  1.00 11.99 ? 389  LYS   B CB  1 
ATOM   7130 C  CG  . LYS   B 1 366 ? -36.864 -6.191  31.041  1.00 12.81 ? 389  LYS   B CG  1 
ATOM   7131 C  CD  . LYS   B 1 366 ? -35.409 -5.763  30.948  1.00 13.63 ? 389  LYS   B CD  1 
ATOM   7132 C  CE  . LYS   B 1 366 ? -34.626 -6.776  30.166  1.00 14.17 ? 389  LYS   B CE  1 
ATOM   7133 N  NZ  . LYS   B 1 366 ? -33.212 -6.444  30.102  1.00 14.80 ? 389  LYS   B NZ  1 
ATOM   7134 N  N   . HIS   B 1 367 ? -39.093 -5.661  26.916  1.00 10.84 ? 390  HIS   B N   1 
ATOM   7135 C  CA  . HIS   B 1 367 ? -39.539 -5.946  25.556  1.00 10.67 ? 390  HIS   B CA  1 
ATOM   7136 C  C   . HIS   B 1 367 ? -38.634 -5.256  24.540  1.00 10.83 ? 390  HIS   B C   1 
ATOM   7137 O  O   . HIS   B 1 367 ? -38.183 -5.856  23.584  1.00 10.44 ? 390  HIS   B O   1 
ATOM   7138 C  CB  . HIS   B 1 367 ? -40.979 -5.493  25.296  1.00 11.02 ? 390  HIS   B CB  1 
ATOM   7139 C  CG  . HIS   B 1 367 ? -42.029 -6.430  25.803  1.00 10.15 ? 390  HIS   B CG  1 
ATOM   7140 N  ND1 . HIS   B 1 367 ? -42.348 -6.508  27.149  1.00 10.41 ? 390  HIS   B ND1 1 
ATOM   7141 C  CD2 . HIS   B 1 367 ? -42.831 -7.326  25.158  1.00 10.35 ? 390  HIS   B CD2 1 
ATOM   7142 C  CE1 . HIS   B 1 367 ? -43.318 -7.411  27.288  1.00 11.07 ? 390  HIS   B CE1 1 
ATOM   7143 N  NE2 . HIS   B 1 367 ? -43.642 -7.904  26.093  1.00 10.32 ? 390  HIS   B NE2 1 
ATOM   7144 N  N   . LYS   B 1 368 ? -38.330 -3.984  24.788  1.00 11.28 ? 391  LYS   B N   1 
ATOM   7145 C  CA  . LYS   B 1 368 ? -37.485 -3.198  23.890  1.00 11.67 ? 391  LYS   B CA  1 
ATOM   7146 C  C   . LYS   B 1 368 ? -36.087 -3.801  23.766  1.00 11.41 ? 391  LYS   B C   1 
ATOM   7147 O  O   . LYS   B 1 368 ? -35.604 -4.006  22.658  1.00 12.32 ? 391  LYS   B O   1 
ATOM   7148 C  CB  . LYS   B 1 368 ? -37.441 -1.739  24.339  1.00 12.31 ? 391  LYS   B CB  1 
ATOM   7149 C  CG  . LYS   B 1 368 ? -38.799 -1.020  24.352  1.00 13.55 ? 391  LYS   B CG  1 
ATOM   7150 C  CD  . LYS   B 1 368 ? -39.511 -0.831  23.022  1.00 14.53 ? 391  LYS   B CD  1 
ATOM   7151 C  CE  . LYS   B 1 368 ? -38.735 0.127   22.117  1.00 15.66 ? 391  LYS   B CE  1 
ATOM   7152 N  NZ  . LYS   B 1 368 ? -39.344 0.170   20.793  1.00 16.16 ? 391  LYS   B NZ  1 
ATOM   7153 N  N   . ASP   B 1 369 ? -35.460 -4.131  24.893  1.00 12.13 ? 392  ASP   B N   1 
ATOM   7154 C  CA  . ASP   B 1 369 ? -34.110 -4.684  24.916  1.00 11.73 ? 392  ASP   B CA  1 
ATOM   7155 C  C   . ASP   B 1 369 ? -34.062 -6.024  24.175  1.00 10.22 ? 392  ASP   B C   1 
ATOM   7156 O  O   . ASP   B 1 369 ? -33.032 -6.400  23.622  1.00 9.34  ? 392  ASP   B O   1 
ATOM   7157 C  CB  . ASP   B 1 369 ? -33.636 -4.936  26.344  1.00 12.30 ? 392  ASP   B CB  1 
ATOM   7158 C  CG  . ASP   B 1 369 ? -33.443 -3.698  27.216  1.00 13.84 ? 392  ASP   B CG  1 
ATOM   7159 O  OD1 . ASP   B 1 369 ? -33.348 -2.626  26.654  1.00 14.80 ? 392  ASP   B OD1 1 
ATOM   7160 O  OD2 . ASP   B 1 369 ? -33.408 -3.838  28.461  1.00 16.80 ? 392  ASP   B OD2 1 
ATOM   7161 N  N   . LEU   B 1 370 ? -35.166 -6.783  24.250  1.00 9.19  ? 393  LEU   B N   1 
ATOM   7162 C  CA  . LEU   B 1 370 ? -35.276 -8.091  23.625  1.00 9.70  ? 393  LEU   B CA  1 
ATOM   7163 C  C   . LEU   B 1 370 ? -35.752 -7.985  22.175  1.00 9.72  ? 393  LEU   B C   1 
ATOM   7164 O  O   . LEU   B 1 370 ? -35.875 -8.996  21.499  1.00 10.14 ? 393  LEU   B O   1 
ATOM   7165 C  CB  . LEU   B 1 370 ? -36.218 -8.962  24.449  1.00 10.13 ? 393  LEU   B CB  1 
ATOM   7166 C  CG  . LEU   B 1 370 ? -35.662 -9.468  25.776  1.00 10.65 ? 393  LEU   B CG  1 
ATOM   7167 C  CD1 . LEU   B 1 370 ? -36.752 -9.874  26.747  1.00 11.07 ? 393  LEU   B CD1 1 
ATOM   7168 C  CD2 . LEU   B 1 370 ? -34.665 -10.621 25.566  1.00 10.74 ? 393  LEU   B CD2 1 
ATOM   7169 N  N   . GLY   B 1 371 ? -36.008 -6.763  21.691  1.00 9.47  ? 394  GLY   B N   1 
ATOM   7170 C  CA  . GLY   B 1 371 ? -36.306 -6.547  20.273  1.00 9.05  ? 394  GLY   B CA  1 
ATOM   7171 C  C   . GLY   B 1 371 ? -37.773 -6.748  19.873  1.00 9.29  ? 394  GLY   B C   1 
ATOM   7172 O  O   . GLY   B 1 371 ? -38.081 -6.618  18.690  1.00 9.62  ? 394  GLY   B O   1 
ATOM   7173 N  N   . PHE   B 1 372 ? -38.659 -7.088  20.817  1.00 8.30  ? 395  PHE   B N   1 
ATOM   7174 C  CA  . PHE   B 1 372 ? -40.091 -7.190  20.548  1.00 9.04  ? 395  PHE   B CA  1 
ATOM   7175 C  C   . PHE   B 1 372 ? -40.640 -5.807  20.225  1.00 9.26  ? 395  PHE   B C   1 
ATOM   7176 O  O   . PHE   B 1 372 ? -40.228 -4.825  20.856  1.00 9.74  ? 395  PHE   B O   1 
ATOM   7177 C  CB  . PHE   B 1 372 ? -40.814 -7.794  21.753  1.00 9.04  ? 395  PHE   B CB  1 
ATOM   7178 C  CG  . PHE   B 1 372 ? -40.414 -9.233  22.033  1.00 9.93  ? 395  PHE   B CG  1 
ATOM   7179 C  CD1 . PHE   B 1 372 ? -40.938 -10.283 21.295  1.00 10.11 ? 395  PHE   B CD1 1 
ATOM   7180 C  CD2 . PHE   B 1 372 ? -39.550 -9.529  23.067  1.00 9.46  ? 395  PHE   B CD2 1 
ATOM   7181 C  CE1 . PHE   B 1 372 ? -40.579 -11.597 21.562  1.00 10.55 ? 395  PHE   B CE1 1 
ATOM   7182 C  CE2 . PHE   B 1 372 ? -39.155 -10.834 23.307  1.00 10.06 ? 395  PHE   B CE2 1 
ATOM   7183 C  CZ  . PHE   B 1 372 ? -39.690 -11.877 22.575  1.00 10.03 ? 395  PHE   B CZ  1 
ATOM   7184 N  N   . ASN   B 1 373 ? -41.575 -5.751  19.269  1.00 8.50  ? 396  ASN   B N   1 
ATOM   7185 C  CA  . ASN   B 1 373 ? -42.254 -4.499  18.965  1.00 8.42  ? 396  ASN   B CA  1 
ATOM   7186 C  C   . ASN   B 1 373 ? -43.716 -4.523  19.418  1.00 8.26  ? 396  ASN   B C   1 
ATOM   7187 O  O   . ASN   B 1 373 ? -44.460 -3.579  19.149  1.00 8.08  ? 396  ASN   B O   1 
ATOM   7188 C  CB  . ASN   B 1 373 ? -42.111 -4.118  17.494  1.00 8.61  ? 396  ASN   B CB  1 
ATOM   7189 C  CG  . ASN   B 1 373 ? -42.766 -5.087  16.557  1.00 8.89  ? 396  ASN   B CG  1 
ATOM   7190 O  OD1 . ASN   B 1 373 ? -43.149 -6.188  16.963  1.00 9.30  ? 396  ASN   B OD1 1 
ATOM   7191 N  ND2 . ASN   B 1 373 ? -42.790 -4.727  15.287  1.00 9.02  ? 396  ASN   B ND2 1 
ATOM   7192 N  N   . MET   B 1 374 ? -44.132 -5.579  20.127  1.00 8.65  ? 397  MET   B N   1 
ATOM   7193 C  CA  . MET   B 1 374 ? -45.534 -5.754  20.502  1.00 8.86  ? 397  MET   B CA  1 
ATOM   7194 C  C   . MET   B 1 374 ? -45.619 -6.482  21.847  1.00 8.97  ? 397  MET   B C   1 
ATOM   7195 O  O   . MET   B 1 374 ? -44.706 -7.224  22.230  1.00 8.14  ? 397  MET   B O   1 
ATOM   7196 C  CB  . MET   B 1 374 ? -46.264 -6.490  19.371  1.00 9.40  ? 397  MET   B CB  1 
ATOM   7197 C  CG  . MET   B 1 374 ? -47.735 -6.781  19.611  1.00 9.42  ? 397  MET   B CG  1 
ATOM   7198 S  SD  . MET   B 1 374 ? -48.134 -8.410  20.261  1.00 9.81  ? 397  MET   B SD  1 
ATOM   7199 C  CE  . MET   B 1 374 ? -47.926 -9.407  18.789  1.00 9.98  ? 397  MET   B CE  1 
ATOM   7200 N  N   . VAL   B 1 375 ? -46.741 -6.286  22.550  1.00 8.76  ? 398  VAL   B N   1 
ATOM   7201 C  CA  . VAL   B 1 375 ? -47.040 -7.058  23.744  1.00 8.38  ? 398  VAL   B CA  1 
ATOM   7202 C  C   . VAL   B 1 375 ? -48.513 -7.437  23.705  1.00 8.23  ? 398  VAL   B C   1 
ATOM   7203 O  O   . VAL   B 1 375 ? -49.328 -6.574  23.415  1.00 7.73  ? 398  VAL   B O   1 
ATOM   7204 C  CB  . VAL   B 1 375 ? -46.692 -6.313  25.043  1.00 9.01  ? 398  VAL   B CB  1 
ATOM   7205 C  CG1 . VAL   B 1 375 ? -47.376 -4.946  25.080  1.00 9.02  ? 398  VAL   B CG1 1 
ATOM   7206 C  CG2 . VAL   B 1 375 ? -46.983 -7.177  26.268  1.00 9.19  ? 398  VAL   B CG2 1 
ATOM   7207 N  N   . ARG   B 1 376 ? -48.865 -8.698  24.016  1.00 8.73  ? 399  ARG   B N   1 
ATOM   7208 C  CA  . ARG   B 1 376 ? -50.262 -9.024  24.298  1.00 8.39  ? 399  ARG   B CA  1 
ATOM   7209 C  C   . ARG   B 1 376 ? -50.465 -9.132  25.808  1.00 9.58  ? 399  ARG   B C   1 
ATOM   7210 O  O   . ARG   B 1 376 ? -49.906 -10.020 26.480  1.00 10.95 ? 399  ARG   B O   1 
ATOM   7211 C  CB  . ARG   B 1 376 ? -50.651 -10.334 23.618  1.00 8.76  ? 399  ARG   B CB  1 
ATOM   7212 C  CG  . ARG   B 1 376 ? -52.050 -10.836 23.956  1.00 8.21  ? 399  ARG   B CG  1 
ATOM   7213 C  CD  . ARG   B 1 376 ? -52.333 -12.177 23.276  1.00 8.61  ? 399  ARG   B CD  1 
ATOM   7214 N  NE  . ARG   B 1 376 ? -53.604 -12.716 23.760  1.00 8.60  ? 399  ARG   B NE  1 
ATOM   7215 C  CZ  . ARG   B 1 376 ? -53.899 -13.972 24.038  1.00 9.59  ? 399  ARG   B CZ  1 
ATOM   7216 N  NH1 . ARG   B 1 376 ? -53.136 -14.955 23.605  1.00 10.01 ? 399  ARG   B NH1 1 
ATOM   7217 N  NH2 . ARG   B 1 376 ? -55.024 -14.244 24.685  1.00 9.89  ? 399  ARG   B NH2 1 
ATOM   7218 N  N   . LYS   B 1 377 ? -51.251 -8.198  26.319  1.00 9.18  ? 400  LYS   B N   1 
ATOM   7219 C  CA  . LYS   B 1 377 ? -51.555 -8.210  27.733  1.00 9.65  ? 400  LYS   B CA  1 
ATOM   7220 C  C   . LYS   B 1 377 ? -52.662 -9.227  27.962  1.00 9.04  ? 400  LYS   B C   1 
ATOM   7221 O  O   . LYS   B 1 377 ? -53.779 -9.057  27.447  1.00 9.15  ? 400  LYS   B O   1 
ATOM   7222 C  CB  . LYS   B 1 377 ? -51.974 -6.809  28.209  1.00 10.16 ? 400  LYS   B CB  1 
ATOM   7223 C  CG  . LYS   B 1 377 ? -52.240 -6.777  29.749  1.00 10.35 ? 400  LYS   B CG  1 
ATOM   7224 C  CD  . LYS   B 1 377 ? -51.095 -7.207  30.663  1.00 10.82 ? 400  LYS   B CD  1 
ATOM   7225 C  CE  . LYS   B 1 377 ? -49.868 -6.375  30.420  1.00 11.35 ? 400  LYS   B CE  1 
ATOM   7226 N  NZ  . LYS   B 1 377 ? -48.892 -6.443  31.533  1.00 11.28 ? 400  LYS   B NZ  1 
ATOM   7227 N  N   . HIS   B 1 378 ? -52.366 -10.253 28.742  1.00 9.13  ? 401  HIS   B N   1 
ATOM   7228 C  CA  . HIS   B 1 378 ? -53.165 -11.457 28.747  1.00 9.92  ? 401  HIS   B CA  1 
ATOM   7229 C  C   . HIS   B 1 378 ? -54.239 -11.431 29.846  1.00 10.88 ? 401  HIS   B C   1 
ATOM   7230 O  O   . HIS   B 1 378 ? -53.944 -11.424 31.052  1.00 11.62 ? 401  HIS   B O   1 
ATOM   7231 C  CB  . HIS   B 1 378 ? -52.239 -12.654 28.893  1.00 9.81  ? 401  HIS   B CB  1 
ATOM   7232 C  CG  . HIS   B 1 378 ? -52.934 -13.956 28.791  1.00 10.95 ? 401  HIS   B CG  1 
ATOM   7233 N  ND1 . HIS   B 1 378 ? -53.819 -14.184 27.760  1.00 11.08 ? 401  HIS   B ND1 1 
ATOM   7234 C  CD2 . HIS   B 1 378 ? -52.797 -15.110 29.467  1.00 10.87 ? 401  HIS   B CD2 1 
ATOM   7235 C  CE1 . HIS   B 1 378 ? -54.272 -15.436 27.874  1.00 11.87 ? 401  HIS   B CE1 1 
ATOM   7236 N  NE2 . HIS   B 1 378 ? -53.655 -16.033 28.927  1.00 11.81 ? 401  HIS   B NE2 1 
ATOM   7237 N  N   . ILE   B 1 379 ? -55.509 -11.438 29.401  1.00 11.23 ? 402  ILE   B N   1 
ATOM   7238 C  CA  . ILE   B 1 379 ? -56.705 -11.477 30.239  1.00 10.94 ? 402  ILE   B CA  1 
ATOM   7239 C  C   . ILE   B 1 379 ? -56.521 -10.703 31.555  1.00 10.68 ? 402  ILE   B C   1 
ATOM   7240 O  O   . ILE   B 1 379 ? -56.971 -11.103 32.638  1.00 11.04 ? 402  ILE   B O   1 
ATOM   7241 C  CB  . ILE   B 1 379 ? -57.220 -12.922 30.384  1.00 10.96 ? 402  ILE   B CB  1 
ATOM   7242 C  CG1 . ILE   B 1 379 ? -56.194 -13.865 30.981  1.00 10.53 ? 402  ILE   B CG1 1 
ATOM   7243 C  CG2 . ILE   B 1 379 ? -57.784 -13.405 29.045  1.00 11.08 ? 402  ILE   B CG2 1 
ATOM   7244 C  CD1 . ILE   B 1 379 ? -56.605 -15.329 31.019  1.00 11.29 ? 402  ILE   B CD1 1 
ATOM   7245 N  N   . LYS   B 1 380 ? -56.027 -9.472  31.393  1.00 11.47 ? 403  LYS   B N   1 
ATOM   7246 C  CA  . LYS   B 1 380 ? -55.855 -8.493  32.450  1.00 12.32 ? 403  LYS   B CA  1 
ATOM   7247 C  C   . LYS   B 1 380 ? -55.796 -7.117  31.802  1.00 11.70 ? 403  LYS   B C   1 
ATOM   7248 O  O   . LYS   B 1 380 ? -55.183 -6.967  30.765  1.00 11.89 ? 403  LYS   B O   1 
ATOM   7249 C  CB  . LYS   B 1 380 ? -54.568 -8.745  33.239  1.00 11.50 ? 403  LYS   B CB  1 
ATOM   7250 C  CG  . LYS   B 1 380 ? -54.407 -7.835  34.474  1.00 12.37 ? 403  LYS   B CG  1 
ATOM   7251 C  CD  . LYS   B 1 380 ? -52.971 -7.739  34.992  1.00 12.70 ? 403  LYS   B CD  1 
ATOM   7252 C  CE  . LYS   B 1 380 ? -52.967 -6.884  36.195  1.00 13.65 ? 403  LYS   B CE  1 
ATOM   7253 N  NZ  . LYS   B 1 380 ? -51.596 -6.621  36.677  1.00 14.37 ? 403  LYS   B NZ  1 
ATOM   7254 N  N   . VAL   B 1 381 ? -56.471 -6.117  32.368  1.00 11.17 ? 404  VAL   B N   1 
ATOM   7255 C  CA  . VAL   B 1 381 ? -56.307 -4.743  31.918  1.00 11.03 ? 404  VAL   B CA  1 
ATOM   7256 C  C   . VAL   B 1 381 ? -55.526 -3.951  32.977  1.00 12.90 ? 404  VAL   B C   1 
ATOM   7257 O  O   . VAL   B 1 381 ? -55.893 -3.888  34.161  1.00 14.06 ? 404  VAL   B O   1 
ATOM   7258 C  CB  . VAL   B 1 381 ? -57.632 -4.034  31.598  1.00 10.43 ? 404  VAL   B CB  1 
ATOM   7259 C  CG1 . VAL   B 1 381 ? -57.382 -2.684  30.956  1.00 10.51 ? 404  VAL   B CG1 1 
ATOM   7260 C  CG2 . VAL   B 1 381 ? -58.587 -4.853  30.716  1.00 11.20 ? 404  VAL   B CG2 1 
ATOM   7261 N  N   . GLU   B 1 382 ? -54.379 -3.431  32.543  1.00 14.13 ? 405  GLU   B N   1 
ATOM   7262 C  CA  . GLU   B 1 382 ? -53.449 -2.738  33.424  1.00 14.32 ? 405  GLU   B CA  1 
ATOM   7263 C  C   . GLU   B 1 382 ? -53.969 -1.333  33.701  1.00 13.71 ? 405  GLU   B C   1 
ATOM   7264 O  O   . GLU   B 1 382 ? -54.835 -0.810  32.989  1.00 14.33 ? 405  GLU   B O   1 
ATOM   7265 C  CB  . GLU   B 1 382 ? -52.057 -2.616  32.808  1.00 13.48 ? 405  GLU   B CB  1 
ATOM   7266 C  CG  . GLU   B 1 382 ? -51.306 -3.933  32.646  1.00 13.05 ? 405  GLU   B CG  1 
ATOM   7267 C  CD  . GLU   B 1 382 ? -50.874 -4.609  33.926  1.00 12.60 ? 405  GLU   B CD  1 
ATOM   7268 O  OE1 . GLU   B 1 382 ? -51.337 -4.130  35.000  1.00 12.65 ? 405  GLU   B OE1 1 
ATOM   7269 O  OE2 . GLU   B 1 382 ? -50.086 -5.587  33.879  1.00 11.77 ? 405  GLU   B OE2 1 
ATOM   7270 N  N   . PRO   B 1 383 ? -53.460 -0.669  34.763  1.00 14.18 ? 406  PRO   B N   1 
ATOM   7271 C  CA  . PRO   B 1 383 ? -53.712 0.757   34.962  1.00 14.54 ? 406  PRO   B CA  1 
ATOM   7272 C  C   . PRO   B 1 383 ? -53.266 1.641   33.802  1.00 14.16 ? 406  PRO   B C   1 
ATOM   7273 O  O   . PRO   B 1 383 ? -52.362 1.286   33.036  1.00 15.67 ? 406  PRO   B O   1 
ATOM   7274 C  CB  . PRO   B 1 383 ? -52.893 1.067   36.239  1.00 14.23 ? 406  PRO   B CB  1 
ATOM   7275 C  CG  . PRO   B 1 383 ? -51.844 -0.001  36.271  1.00 14.69 ? 406  PRO   B CG  1 
ATOM   7276 C  CD  . PRO   B 1 383 ? -52.627 -1.241  35.831  1.00 14.62 ? 406  PRO   B CD  1 
ATOM   7277 N  N   . GLN   B 1 384 ? -53.875 2.825   33.716  1.00 14.18 ? 407  GLN   B N   1 
ATOM   7278 C  CA  . GLN   B 1 384 ? -53.637 3.732   32.605  1.00 14.18 ? 407  GLN   B CA  1 
ATOM   7279 C  C   . GLN   B 1 384 ? -52.135 4.036   32.424  1.00 13.61 ? 407  GLN   B C   1 
ATOM   7280 O  O   . GLN   B 1 384 ? -51.660 4.239   31.315  1.00 14.80 ? 407  GLN   B O   1 
ATOM   7281 C  CB  . GLN   B 1 384 ? -54.432 5.009   32.826  1.00 15.24 ? 407  GLN   B CB  1 
ATOM   7282 C  CG  . GLN   B 1 384 ? -55.927 4.851   32.547  1.00 15.99 ? 407  GLN   B CG  1 
ATOM   7283 C  CD  . GLN   B 1 384 ? -56.218 4.752   31.066  1.00 17.29 ? 407  GLN   B CD  1 
ATOM   7284 O  OE1 . GLN   B 1 384 ? -55.343 4.995   30.228  1.00 19.84 ? 407  GLN   B OE1 1 
ATOM   7285 N  NE2 . GLN   B 1 384 ? -57.442 4.389   30.703  1.00 16.96 ? 407  GLN   B NE2 1 
ATOM   7286 N  N   . ARG   B 1 385 ? -51.397 4.145   33.511  1.00 14.34 ? 408  ARG   B N   1 
ATOM   7287 C  CA  . ARG   B 1 385 ? -49.968 4.457   33.442  1.00 14.30 ? 408  ARG   B CA  1 
ATOM   7288 C  C   . ARG   B 1 385 ? -49.206 3.396   32.653  1.00 15.01 ? 408  ARG   B C   1 
ATOM   7289 O  O   . ARG   B 1 385 ? -48.190 3.700   32.015  1.00 14.51 ? 408  ARG   B O   1 
ATOM   7290 C  CB  . ARG   B 1 385 ? -49.376 4.597   34.848  1.00 15.48 ? 408  ARG   B CB  1 
ATOM   7291 C  CG  . ARG   B 1 385 ? -49.623 5.985   35.420  1.00 16.40 ? 408  ARG   B CG  1 
ATOM   7292 C  CD  . ARG   B 1 385 ? -48.835 6.261   36.720  1.00 16.07 ? 408  ARG   B CD  1 
ATOM   7293 N  NE  . ARG   B 1 385 ? -47.446 6.620   36.388  1.00 17.26 ? 408  ARG   B NE  1 
ATOM   7294 C  CZ  . ARG   B 1 385 ? -47.028 7.720   35.749  1.00 15.87 ? 408  ARG   B CZ  1 
ATOM   7295 N  NH1 . ARG   B 1 385 ? -47.828 8.751   35.518  1.00 19.42 ? 408  ARG   B NH1 1 
ATOM   7296 N  NH2 . ARG   B 1 385 ? -45.756 7.821   35.379  1.00 18.72 ? 408  ARG   B NH2 1 
ATOM   7297 N  N   . TRP   B 1 386 ? -49.696 2.151   32.663  1.00 14.19 ? 409  TRP   B N   1 
ATOM   7298 C  CA  . TRP   B 1 386 ? -49.071 1.136   31.832  1.00 12.71 ? 409  TRP   B CA  1 
ATOM   7299 C  C   . TRP   B 1 386 ? -49.230 1.486   30.349  1.00 13.45 ? 409  TRP   B C   1 
ATOM   7300 O  O   . TRP   B 1 386 ? -48.277 1.346   29.595  1.00 14.21 ? 409  TRP   B O   1 
ATOM   7301 C  CB  . TRP   B 1 386 ? -49.660 -0.234  32.155  1.00 11.39 ? 409  TRP   B CB  1 
ATOM   7302 C  CG  . TRP   B 1 386 ? -49.055 -1.354  31.350  1.00 11.26 ? 409  TRP   B CG  1 
ATOM   7303 C  CD1 . TRP   B 1 386 ? -47.975 -2.114  31.678  1.00 11.32 ? 409  TRP   B CD1 1 
ATOM   7304 C  CD2 . TRP   B 1 386 ? -49.506 -1.841  30.066  1.00 11.08 ? 409  TRP   B CD2 1 
ATOM   7305 N  NE1 . TRP   B 1 386 ? -47.739 -3.052  30.724  1.00 11.37 ? 409  TRP   B NE1 1 
ATOM   7306 C  CE2 . TRP   B 1 386 ? -48.648 -2.905  29.722  1.00 11.44 ? 409  TRP   B CE2 1 
ATOM   7307 C  CE3 . TRP   B 1 386 ? -50.545 -1.502  29.196  1.00 11.00 ? 409  TRP   B CE3 1 
ATOM   7308 C  CZ2 . TRP   B 1 386 ? -48.798 -3.625  28.545  1.00 12.02 ? 409  TRP   B CZ2 1 
ATOM   7309 C  CZ3 . TRP   B 1 386 ? -50.714 -2.246  28.049  1.00 11.57 ? 409  TRP   B CZ3 1 
ATOM   7310 C  CH2 . TRP   B 1 386 ? -49.857 -3.294  27.735  1.00 11.26 ? 409  TRP   B CH2 1 
ATOM   7311 N  N   . PHE   B 1 387 ? -50.439 1.900   29.922  1.00 13.19 ? 410  PHE   B N   1 
ATOM   7312 C  CA  . PHE   B 1 387 ? -50.674 2.317   28.548  1.00 11.94 ? 410  PHE   B CA  1 
ATOM   7313 C  C   . PHE   B 1 387 ? -49.784 3.512   28.214  1.00 13.10 ? 410  PHE   B C   1 
ATOM   7314 O  O   . PHE   B 1 387 ? -49.235 3.621   27.121  1.00 11.35 ? 410  PHE   B O   1 
ATOM   7315 C  CB  . PHE   B 1 387 ? -52.153 2.654   28.321  1.00 12.27 ? 410  PHE   B CB  1 
ATOM   7316 C  CG  . PHE   B 1 387 ? -53.027 1.407   28.275  1.00 12.28 ? 410  PHE   B CG  1 
ATOM   7317 C  CD1 . PHE   B 1 387 ? -53.530 0.803   29.422  1.00 13.12 ? 410  PHE   B CD1 1 
ATOM   7318 C  CD2 . PHE   B 1 387 ? -53.252 0.792   27.052  1.00 12.58 ? 410  PHE   B CD2 1 
ATOM   7319 C  CE1 . PHE   B 1 387 ? -54.278 -0.368  29.340  1.00 12.79 ? 410  PHE   B CE1 1 
ATOM   7320 C  CE2 . PHE   B 1 387 ? -54.034 -0.346  26.966  1.00 12.69 ? 410  PHE   B CE2 1 
ATOM   7321 C  CZ  . PHE   B 1 387 ? -54.539 -0.924  28.094  1.00 13.05 ? 410  PHE   B CZ  1 
ATOM   7322 N  N   . TYR   B 1 388 ? -49.634 4.431   29.174  1.00 13.80 ? 411  TYR   B N   1 
ATOM   7323 C  CA  . TYR   B 1 388 ? -48.768 5.578   28.950  1.00 15.41 ? 411  TYR   B CA  1 
ATOM   7324 C  C   . TYR   B 1 388 ? -47.336 5.128   28.648  1.00 15.50 ? 411  TYR   B C   1 
ATOM   7325 O  O   . TYR   B 1 388 ? -46.718 5.653   27.723  1.00 14.34 ? 411  TYR   B O   1 
ATOM   7326 C  CB  . TYR   B 1 388 ? -48.829 6.388   30.235  1.00 16.68 ? 411  TYR   B CB  1 
ATOM   7327 C  CG  . TYR   B 1 388 ? -47.808 7.493   30.407  1.00 18.21 ? 411  TYR   B CG  1 
ATOM   7328 C  CD1 . TYR   B 1 388 ? -47.977 8.703   29.762  1.00 22.80 ? 411  TYR   B CD1 1 
ATOM   7329 C  CD2 . TYR   B 1 388 ? -46.715 7.332   31.250  1.00 22.50 ? 411  TYR   B CD2 1 
ATOM   7330 C  CE1 . TYR   B 1 388 ? -47.093 9.751   29.969  1.00 25.30 ? 411  TYR   B CE1 1 
ATOM   7331 C  CE2 . TYR   B 1 388 ? -45.817 8.372   31.460  1.00 23.63 ? 411  TYR   B CE2 1 
ATOM   7332 C  CZ  . TYR   B 1 388 ? -46.033 9.588   30.840  1.00 25.81 ? 411  TYR   B CZ  1 
ATOM   7333 O  OH  . TYR   B 1 388 ? -45.169 10.638  30.992  1.00 30.22 ? 411  TYR   B OH  1 
ATOM   7334 N  N   . TRP   B 1 389 ? -46.845 4.131   29.399  1.00 14.38 ? 412  TRP   B N   1 
ATOM   7335 C  CA  . TRP   B 1 389 ? -45.486 3.650   29.221  1.00 14.59 ? 412  TRP   B CA  1 
ATOM   7336 C  C   . TRP   B 1 389 ? -45.323 2.934   27.883  1.00 14.56 ? 412  TRP   B C   1 
ATOM   7337 O  O   . TRP   B 1 389 ? -44.318 3.098   27.216  1.00 12.81 ? 412  TRP   B O   1 
ATOM   7338 C  CB  . TRP   B 1 389 ? -45.020 2.793   30.402  1.00 15.49 ? 412  TRP   B CB  1 
ATOM   7339 C  CG  . TRP   B 1 389 ? -44.637 3.629   31.597  1.00 17.62 ? 412  TRP   B CG  1 
ATOM   7340 C  CD1 . TRP   B 1 389 ? -45.135 3.536   32.860  1.00 21.16 ? 412  TRP   B CD1 1 
ATOM   7341 C  CD2 . TRP   B 1 389 ? -43.682 4.713   31.623  1.00 18.37 ? 412  TRP   B CD2 1 
ATOM   7342 N  NE1 . TRP   B 1 389 ? -44.551 4.474   33.678  1.00 21.07 ? 412  TRP   B NE1 1 
ATOM   7343 C  CE2 . TRP   B 1 389 ? -43.657 5.205   32.947  1.00 21.84 ? 412  TRP   B CE2 1 
ATOM   7344 C  CE3 . TRP   B 1 389 ? -42.843 5.295   30.666  1.00 20.67 ? 412  TRP   B CE3 1 
ATOM   7345 C  CZ2 . TRP   B 1 389 ? -42.836 6.267   33.330  1.00 21.45 ? 412  TRP   B CZ2 1 
ATOM   7346 C  CZ3 . TRP   B 1 389 ? -42.010 6.329   31.050  1.00 22.45 ? 412  TRP   B CZ3 1 
ATOM   7347 C  CH2 . TRP   B 1 389 ? -42.040 6.829   32.355  1.00 21.50 ? 412  TRP   B CH2 1 
ATOM   7348 N  N   . ALA   B 1 390 ? -46.353 2.218   27.423  1.00 12.97 ? 413  ALA   B N   1 
ATOM   7349 C  CA  . ALA   B 1 390 ? -46.270 1.630   26.094  1.00 12.22 ? 413  ALA   B CA  1 
ATOM   7350 C  C   . ALA   B 1 390 ? -46.312 2.703   25.012  1.00 11.98 ? 413  ALA   B C   1 
ATOM   7351 O  O   . ALA   B 1 390 ? -45.596 2.625   24.012  1.00 12.24 ? 413  ALA   B O   1 
ATOM   7352 C  CB  . ALA   B 1 390 ? -47.405 0.625   25.896  1.00 11.77 ? 413  ALA   B CB  1 
ATOM   7353 N  N   . ASP   B 1 391 ? -47.173 3.715   25.216  1.00 11.84 ? 414  ASP   B N   1 
ATOM   7354 C  CA  . ASP   B 1 391 ? -47.215 4.871   24.340  1.00 11.94 ? 414  ASP   B CA  1 
ATOM   7355 C  C   . ASP   B 1 391 ? -45.835 5.541   24.222  1.00 11.85 ? 414  ASP   B C   1 
ATOM   7356 O  O   . ASP   B 1 391 ? -45.431 5.984   23.139  1.00 11.52 ? 414  ASP   B O   1 
ATOM   7357 C  CB  . ASP   B 1 391 ? -48.252 5.852   24.853  1.00 11.82 ? 414  ASP   B CB  1 
ATOM   7358 C  CG  . ASP   B 1 391 ? -49.720 5.428   24.831  1.00 13.30 ? 414  ASP   B CG  1 
ATOM   7359 O  OD1 . ASP   B 1 391 ? -50.067 4.421   24.180  1.00 12.63 ? 414  ASP   B OD1 1 
ATOM   7360 O  OD2 . ASP   B 1 391 ? -50.505 6.116   25.514  1.00 13.53 ? 414  ASP   B OD2 1 
ATOM   7361 N  N   . ARG   B 1 392 ? -45.156 5.705   25.353  1.00 13.40 ? 415  ARG   B N   1 
ATOM   7362 C  CA  . ARG   B 1 392 ? -43.899 6.454   25.397  1.00 15.62 ? 415  ARG   B CA  1 
ATOM   7363 C  C   . ARG   B 1 392 ? -42.729 5.621   24.896  1.00 16.82 ? 415  ARG   B C   1 
ATOM   7364 O  O   . ARG   B 1 392 ? -41.874 6.135   24.145  1.00 15.22 ? 415  ARG   B O   1 
ATOM   7365 C  CB  . ARG   B 1 392 ? -43.600 6.918   26.824  1.00 18.38 ? 415  ARG   B CB  1 
ATOM   7366 C  CG  . ARG   B 1 392 ? -44.531 8.064   27.159  1.00 21.81 ? 415  ARG   B CG  1 
ATOM   7367 C  CD  . ARG   B 1 392 ? -43.994 8.850   28.356  1.00 26.70 ? 415  ARG   B CD  1 
ATOM   7368 N  NE  . ARG   B 1 392 ? -42.641 9.370   28.130  1.00 29.60 ? 415  ARG   B NE  1 
ATOM   7369 C  CZ  . ARG   B 1 392 ? -41.874 9.857   29.102  1.00 39.16 ? 415  ARG   B CZ  1 
ATOM   7370 N  NH1 . ARG   B 1 392 ? -42.298 9.861   30.364  1.00 39.25 ? 415  ARG   B NH1 1 
ATOM   7371 N  NH2 . ARG   B 1 392 ? -40.676 10.333  28.812  1.00 43.02 ? 415  ARG   B NH2 1 
ATOM   7372 N  N   . LEU   B 1 393 ? -42.698 4.349   25.321  1.00 15.17 ? 416  LEU   B N   1 
ATOM   7373 C  CA  . LEU   B 1 393 ? -41.559 3.492   25.005  1.00 15.17 ? 416  LEU   B CA  1 
ATOM   7374 C  C   . LEU   B 1 393 ? -41.632 2.981   23.571  1.00 16.15 ? 416  LEU   B C   1 
ATOM   7375 O  O   . LEU   B 1 393 ? -40.602 2.600   22.991  1.00 14.80 ? 416  LEU   B O   1 
ATOM   7376 C  CB  . LEU   B 1 393 ? -41.437 2.304   25.945  1.00 16.98 ? 416  LEU   B CB  1 
ATOM   7377 C  CG  . LEU   B 1 393 ? -40.956 2.595   27.365  1.00 20.10 ? 416  LEU   B CG  1 
ATOM   7378 C  CD1 . LEU   B 1 393 ? -40.798 1.225   27.951  1.00 21.96 ? 416  LEU   B CD1 1 
ATOM   7379 C  CD2 . LEU   B 1 393 ? -39.667 3.368   27.428  1.00 22.49 ? 416  LEU   B CD2 1 
ATOM   7380 N  N   . GLY   B 1 394 ? -42.855 2.843   23.031  1.00 14.15 ? 417  GLY   B N   1 
ATOM   7381 C  CA  . GLY   B 1 394 ? -43.032 2.412   21.658  1.00 13.08 ? 417  GLY   B CA  1 
ATOM   7382 C  C   . GLY   B 1 394 ? -43.196 0.894   21.570  1.00 13.97 ? 417  GLY   B C   1 
ATOM   7383 O  O   . GLY   B 1 394 ? -42.292 0.165   21.146  1.00 14.77 ? 417  GLY   B O   1 
ATOM   7384 N  N   . LEU   B 1 395 ? -44.373 0.411   21.953  1.00 11.77 ? 418  LEU   B N   1 
ATOM   7385 C  CA  . LEU   B 1 395 ? -44.728 -0.988  21.756  1.00 12.27 ? 418  LEU   B CA  1 
ATOM   7386 C  C   . LEU   B 1 395 ? -46.164 -1.026  21.270  1.00 12.43 ? 418  LEU   B C   1 
ATOM   7387 O  O   . LEU   B 1 395 ? -46.991 -0.316  21.811  1.00 12.19 ? 418  LEU   B O   1 
ATOM   7388 C  CB  . LEU   B 1 395 ? -44.628 -1.763  23.055  1.00 13.42 ? 418  LEU   B CB  1 
ATOM   7389 C  CG  . LEU   B 1 395 ? -43.227 -2.161  23.499  1.00 15.23 ? 418  LEU   B CG  1 
ATOM   7390 C  CD1 . LEU   B 1 395 ? -43.353 -2.641  24.944  1.00 15.82 ? 418  LEU   B CD1 1 
ATOM   7391 C  CD2 . LEU   B 1 395 ? -42.609 -3.237  22.627  1.00 13.62 ? 418  LEU   B CD2 1 
ATOM   7392 N  N   . LEU   B 1 396 ? -46.437 -1.833  20.242  1.00 11.15 ? 419  LEU   B N   1 
ATOM   7393 C  CA  . LEU   B 1 396 ? -47.810 -2.162  19.890  1.00 10.74 ? 419  LEU   B CA  1 
ATOM   7394 C  C   . LEU   B 1 396 ? -48.426 -2.999  20.994  1.00 10.59 ? 419  LEU   B C   1 
ATOM   7395 O  O   . LEU   B 1 396 ? -47.823 -3.960  21.472  1.00 11.41 ? 419  LEU   B O   1 
ATOM   7396 C  CB  . LEU   B 1 396 ? -47.834 -2.914  18.562  1.00 10.49 ? 419  LEU   B CB  1 
ATOM   7397 C  CG  . LEU   B 1 396 ? -47.128 -2.171  17.424  1.00 10.05 ? 419  LEU   B CG  1 
ATOM   7398 C  CD1 . LEU   B 1 396 ? -46.874 -2.995  16.182  1.00 10.84 ? 419  LEU   B CD1 1 
ATOM   7399 C  CD2 . LEU   B 1 396 ? -47.852 -0.859  17.084  1.00 11.32 ? 419  LEU   B CD2 1 
ATOM   7400 N  N   . VAL   B 1 397 ? -49.685 -2.685  21.332  1.00 9.08  ? 420  VAL   B N   1 
ATOM   7401 C  CA  . VAL   B 1 397 ? -50.367 -3.412  22.382  1.00 9.41  ? 420  VAL   B CA  1 
ATOM   7402 C  C   . VAL   B 1 397 ? -51.601 -4.122  21.834  1.00 9.48  ? 420  VAL   B C   1 
ATOM   7403 O  O   . VAL   B 1 397 ? -52.433 -3.532  21.138  1.00 8.69  ? 420  VAL   B O   1 
ATOM   7404 C  CB  . VAL   B 1 397 ? -50.784 -2.484  23.532  1.00 9.80  ? 420  VAL   B CB  1 
ATOM   7405 C  CG1 . VAL   B 1 397 ? -51.764 -3.195  24.454  1.00 10.49 ? 420  VAL   B CG1 1 
ATOM   7406 C  CG2 . VAL   B 1 397 ? -49.564 -1.936  24.254  1.00 9.36  ? 420  VAL   B CG2 1 
ATOM   7407 N  N   . TRP   B 1 398 ? -51.700 -5.411  22.178  1.00 9.20  ? 421  TRP   B N   1 
ATOM   7408 C  CA  . TRP   B 1 398 ? -52.962 -6.131  22.036  1.00 9.37  ? 421  TRP   B CA  1 
ATOM   7409 C  C   . TRP   B 1 398 ? -53.570 -6.271  23.425  1.00 8.86  ? 421  TRP   B C   1 
ATOM   7410 O  O   . TRP   B 1 398 ? -52.894 -6.749  24.325  1.00 9.31  ? 421  TRP   B O   1 
ATOM   7411 C  CB  . TRP   B 1 398 ? -52.744 -7.552  21.502  1.00 9.38  ? 421  TRP   B CB  1 
ATOM   7412 C  CG  . TRP   B 1 398 ? -52.151 -7.630  20.124  1.00 9.08  ? 421  TRP   B CG  1 
ATOM   7413 C  CD1 . TRP   B 1 398 ? -51.570 -6.650  19.365  1.00 9.92  ? 421  TRP   B CD1 1 
ATOM   7414 C  CD2 . TRP   B 1 398 ? -52.074 -8.830  19.353  1.00 10.22 ? 421  TRP   B CD2 1 
ATOM   7415 N  NE1 . TRP   B 1 398 ? -51.162 -7.146  18.161  1.00 9.56  ? 421  TRP   B NE1 1 
ATOM   7416 C  CE2 . TRP   B 1 398 ? -51.459 -8.486  18.126  1.00 10.51 ? 421  TRP   B CE2 1 
ATOM   7417 C  CE3 . TRP   B 1 398 ? -52.461 -10.145 19.586  1.00 9.82  ? 421  TRP   B CE3 1 
ATOM   7418 C  CZ2 . TRP   B 1 398 ? -51.234 -9.428  17.124  1.00 10.87 ? 421  TRP   B CZ2 1 
ATOM   7419 C  CZ3 . TRP   B 1 398 ? -52.269 -11.062 18.576  1.00 10.62 ? 421  TRP   B CZ3 1 
ATOM   7420 C  CH2 . TRP   B 1 398 ? -51.622 -10.722 17.390  1.00 10.81 ? 421  TRP   B CH2 1 
ATOM   7421 N  N   . GLN   B 1 399 ? -54.844 -5.927  23.580  1.00 8.76  ? 422  GLN   B N   1 
ATOM   7422 C  CA  . GLN   B 1 399 ? -55.475 -5.977  24.887  1.00 8.90  ? 422  GLN   B CA  1 
ATOM   7423 C  C   . GLN   B 1 399 ? -56.561 -7.037  24.882  1.00 9.23  ? 422  GLN   B C   1 
ATOM   7424 O  O   . GLN   B 1 399 ? -57.491 -6.944  24.089  1.00 8.67  ? 422  GLN   B O   1 
ATOM   7425 C  CB  . GLN   B 1 399 ? -56.124 -4.632  25.188  1.00 9.52  ? 422  GLN   B CB  1 
ATOM   7426 C  CG  . GLN   B 1 399 ? -56.841 -4.593  26.524  1.00 10.11 ? 422  GLN   B CG  1 
ATOM   7427 C  CD  . GLN   B 1 399 ? -55.872 -4.851  27.662  1.00 10.81 ? 422  GLN   B CD  1 
ATOM   7428 O  OE1 . GLN   B 1 399 ? -54.939 -4.072  27.930  1.00 11.20 ? 422  GLN   B OE1 1 
ATOM   7429 N  NE2 . GLN   B 1 399 ? -56.068 -5.963  28.334  1.00 10.33 ? 422  GLN   B NE2 1 
ATOM   7430 N  N   . ASP   B 1 400 ? -56.405 -8.061  25.709  1.00 9.13  ? 423  ASP   B N   1 
ATOM   7431 C  CA  . ASP   B 1 400 ? -57.422 -9.081  25.926  1.00 9.18  ? 423  ASP   B CA  1 
ATOM   7432 C  C   . ASP   B 1 400 ? -58.521 -8.519  26.831  1.00 10.12 ? 423  ASP   B C   1 
ATOM   7433 O  O   . ASP   B 1 400 ? -58.238 -7.902  27.869  1.00 11.01 ? 423  ASP   B O   1 
ATOM   7434 C  CB  . ASP   B 1 400 ? -56.838 -10.287 26.648  1.00 10.02 ? 423  ASP   B CB  1 
ATOM   7435 C  CG  . ASP   B 1 400 ? -55.864 -11.207 25.935  1.00 9.61  ? 423  ASP   B CG  1 
ATOM   7436 O  OD1 . ASP   B 1 400 ? -55.587 -10.989 24.726  1.00 9.38  ? 423  ASP   B OD1 1 
ATOM   7437 O  OD2 . ASP   B 1 400 ? -55.465 -12.223 26.597  1.00 10.13 ? 423  ASP   B OD2 1 
ATOM   7438 N  N   . MET   B 1 401 ? -59.792 -8.796  26.515  1.00 9.78  ? 424  MET   B N   1 
ATOM   7439 C  CA  . MET   B 1 401 ? -60.825 -8.627  27.522  1.00 9.78  ? 424  MET   B CA  1 
ATOM   7440 C  C   . MET   B 1 401 ? -60.704 -9.794  28.505  1.00 9.76  ? 424  MET   B C   1 
ATOM   7441 O  O   . MET   B 1 401 ? -60.711 -10.940 28.086  1.00 9.47  ? 424  MET   B O   1 
ATOM   7442 C  CB  . MET   B 1 401 ? -62.208 -8.626  26.875  1.00 10.24 ? 424  MET   B CB  1 
ATOM   7443 C  CG  . MET   B 1 401 ? -63.354 -8.555  27.869  1.00 10.10 ? 424  MET   B CG  1 
ATOM   7444 S  SD  . MET   B 1 401 ? -63.314 -7.071  28.910  1.00 11.02 ? 424  MET   B SD  1 
ATOM   7445 C  CE  . MET   B 1 401 ? -64.245 -7.697  30.312  1.00 11.52 ? 424  MET   B CE  1 
ATOM   7446 N  N   . PRO   B 1 402 ? -60.557 -9.585  29.830  1.00 9.48  ? 425  PRO   B N   1 
ATOM   7447 C  CA  . PRO   B 1 402 ? -60.471 -10.720 30.761  1.00 10.06 ? 425  PRO   B CA  1 
ATOM   7448 C  C   . PRO   B 1 402 ? -61.705 -11.618 30.693  1.00 9.25  ? 425  PRO   B C   1 
ATOM   7449 O  O   . PRO   B 1 402 ? -62.827 -11.138 30.551  1.00 10.23 ? 425  PRO   B O   1 
ATOM   7450 C  CB  . PRO   B 1 402 ? -60.289 -10.046 32.166  1.00 9.60  ? 425  PRO   B CB  1 
ATOM   7451 C  CG  . PRO   B 1 402 ? -59.708 -8.701  31.817  1.00 9.66  ? 425  PRO   B CG  1 
ATOM   7452 C  CD  . PRO   B 1 402 ? -60.340 -8.296  30.503  1.00 9.85  ? 425  PRO   B CD  1 
ATOM   7453 N  N   . ASN   B 1 403 ? -61.462 -12.925 30.617  1.00 9.91  ? 426  ASN   B N   1 
ATOM   7454 C  CA  . ASN   B 1 403 ? -62.521 -13.917 30.510  1.00 10.52 ? 426  ASN   B CA  1 
ATOM   7455 C  C   . ASN   B 1 403 ? -63.254 -14.208 31.817  1.00 10.92 ? 426  ASN   B C   1 
ATOM   7456 O  O   . ASN   B 1 403 ? -62.722 -14.040 32.923  1.00 11.68 ? 426  ASN   B O   1 
ATOM   7457 C  CB  . ASN   B 1 403 ? -61.961 -15.239 30.010  1.00 10.14 ? 426  ASN   B CB  1 
ATOM   7458 C  CG  . ASN   B 1 403 ? -60.963 -15.819 30.989  1.00 10.73 ? 426  ASN   B CG  1 
ATOM   7459 O  OD1 . ASN   B 1 403 ? -59.853 -15.300 31.181  1.00 10.32 ? 426  ASN   B OD1 1 
ATOM   7460 N  ND2 . ASN   B 1 403 ? -61.371 -16.881 31.661  1.00 10.89 ? 426  ASN   B ND2 1 
ATOM   7461 N  N   . MET   B 1 404 ? -64.478 -14.722 31.619  1.00 10.75 ? 427  MET   B N   1 
ATOM   7462 C  CA  . MET   B 1 404 ? -65.226 -15.459 32.627  1.00 10.89 ? 427  MET   B CA  1 
ATOM   7463 C  C   . MET   B 1 404 ? -64.752 -16.908 32.671  1.00 11.08 ? 427  MET   B C   1 
ATOM   7464 O  O   . MET   B 1 404 ? -64.226 -17.457 31.704  1.00 11.29 ? 427  MET   B O   1 
ATOM   7465 C  CB  . MET   B 1 404 ? -66.727 -15.320 32.339  1.00 10.40 ? 427  MET   B CB  1 
ATOM   7466 C  CG  . MET   B 1 404 ? -67.233 -13.887 32.336  1.00 10.12 ? 427  MET   B CG  1 
ATOM   7467 S  SD  . MET   B 1 404 ? -68.883 -13.662 31.618  1.00 11.11 ? 427  MET   B SD  1 
ATOM   7468 C  CE  . MET   B 1 404 ? -68.570 -13.908 29.863  1.00 11.33 ? 427  MET   B CE  1 
ATOM   7469 N  N   . GLU   B 1 405 ? -64.959 -17.520 33.826  1.00 11.82 ? 428  GLU   B N   1 
ATOM   7470 C  CA  . GLU   B 1 405 ? -64.549 -18.889 34.076  1.00 15.08 ? 428  GLU   B CA  1 
ATOM   7471 C  C   . GLU   B 1 405 ? -65.447 -19.900 33.372  1.00 14.71 ? 428  GLU   B C   1 
ATOM   7472 O  O   . GLU   B 1 405 ? -64.996 -21.004 33.126  1.00 15.26 ? 428  GLU   B O   1 
ATOM   7473 C  CB  . GLU   B 1 405 ? -64.586 -19.125 35.586  1.00 18.23 ? 428  GLU   B CB  1 
ATOM   7474 C  CG  . GLU   B 1 405 ? -64.017 -20.473 36.026  1.00 21.64 ? 428  GLU   B CG  1 
ATOM   7475 C  CD  . GLU   B 1 405 ? -65.064 -21.549 36.189  1.00 24.39 ? 428  GLU   B CD  1 
ATOM   7476 O  OE1 . GLU   B 1 405 ? -64.669 -22.694 35.948  1.00 30.84 ? 428  GLU   B OE1 1 
ATOM   7477 O  OE2 . GLU   B 1 405 ? -66.242 -21.265 36.457  1.00 25.15 ? 428  GLU   B OE2 1 
ATOM   7478 N  N   . ARG   B 1 406 ? -66.719 -19.584 33.110  1.00 13.74 ? 429  ARG   B N   1 
ATOM   7479 C  CA  . ARG   B 1 406 ? -67.579 -20.563 32.464  1.00 13.57 ? 429  ARG   B CA  1 
ATOM   7480 C  C   . ARG   B 1 406 ? -68.611 -19.845 31.605  1.00 12.81 ? 429  ARG   B C   1 
ATOM   7481 O  O   . ARG   B 1 406 ? -68.774 -18.633 31.710  1.00 12.95 ? 429  ARG   B O   1 
ATOM   7482 C  CB  . ARG   B 1 406 ? -68.228 -21.446 33.538  1.00 14.42 ? 429  ARG   B CB  1 
ATOM   7483 C  CG  . ARG   B 1 406 ? -69.100 -20.709 34.535  1.00 16.03 ? 429  ARG   B CG  1 
ATOM   7484 C  CD  . ARG   B 1 406 ? -69.439 -21.457 35.831  1.00 16.99 ? 429  ARG   B CD  1 
ATOM   7485 N  NE  . ARG   B 1 406 ? -70.237 -20.602 36.726  1.00 18.70 ? 429  ARG   B NE  1 
ATOM   7486 C  CZ  . ARG   B 1 406 ? -69.704 -19.935 37.761  1.00 21.71 ? 429  ARG   B CZ  1 
ATOM   7487 N  NH1 . ARG   B 1 406 ? -68.394 -19.921 37.930  1.00 24.06 ? 429  ARG   B NH1 1 
ATOM   7488 N  NH2 . ARG   B 1 406 ? -70.450 -19.209 38.557  1.00 24.26 ? 429  ARG   B NH2 1 
ATOM   7489 N  N   . THR   B 1 407 ? -69.377 -20.614 30.836  1.00 12.50 ? 430  THR   B N   1 
ATOM   7490 C  CA  . THR   B 1 407 ? -70.379 -20.027 29.963  1.00 11.96 ? 430  THR   B CA  1 
ATOM   7491 C  C   . THR   B 1 407 ? -71.273 -19.081 30.754  1.00 12.08 ? 430  THR   B C   1 
ATOM   7492 O  O   . THR   B 1 407 ? -71.911 -19.472 31.744  1.00 12.00 ? 430  THR   B O   1 
ATOM   7493 C  CB  . THR   B 1 407 ? -71.256 -21.082 29.304  1.00 13.27 ? 430  THR   B CB  1 
ATOM   7494 O  OG1 . THR   B 1 407 ? -70.440 -22.096 28.746  1.00 13.54 ? 430  THR   B OG1 1 
ATOM   7495 C  CG2 . THR   B 1 407 ? -72.133 -20.451 28.237  1.00 14.40 ? 430  THR   B CG2 1 
ATOM   7496 N  N   . PRO   B 1 408 ? -71.396 -17.815 30.312  1.00 11.87 ? 431  PRO   B N   1 
ATOM   7497 C  CA  . PRO   B 1 408 ? -72.260 -16.862 30.994  1.00 11.56 ? 431  PRO   B CA  1 
ATOM   7498 C  C   . PRO   B 1 408 ? -73.750 -17.055 30.762  1.00 11.07 ? 431  PRO   B C   1 
ATOM   7499 O  O   . PRO   B 1 408 ? -74.191 -17.344 29.664  1.00 10.62 ? 431  PRO   B O   1 
ATOM   7500 C  CB  . PRO   B 1 408 ? -71.800 -15.541 30.400  1.00 12.34 ? 431  PRO   B CB  1 
ATOM   7501 C  CG  . PRO   B 1 408 ? -71.388 -15.873 29.009  1.00 11.78 ? 431  PRO   B CG  1 
ATOM   7502 C  CD  . PRO   B 1 408 ? -70.751 -17.248 29.110  1.00 12.05 ? 431  PRO   B CD  1 
ATOM   7503 N  N   . ASP   B 1 409 ? -74.524 -16.781 31.809  1.00 11.24 ? 432  ASP   B N   1 
ATOM   7504 C  CA  . ASP   B 1 409 ? -75.966 -16.641 31.679  1.00 10.83 ? 432  ASP   B CA  1 
ATOM   7505 C  C   . ASP   B 1 409 ? -76.299 -15.204 31.279  1.00 10.46 ? 432  ASP   B C   1 
ATOM   7506 O  O   . ASP   B 1 409 ? -75.391 -14.412 31.016  1.00 10.63 ? 432  ASP   B O   1 
ATOM   7507 C  CB  . ASP   B 1 409 ? -76.613 -17.150 32.933  1.00 10.75 ? 432  ASP   B CB  1 
ATOM   7508 C  CG  . ASP   B 1 409 ? -76.413 -16.282 34.165  1.00 12.51 ? 432  ASP   B CG  1 
ATOM   7509 O  OD1 . ASP   B 1 409 ? -75.770 -15.192 34.086  1.00 12.43 ? 432  ASP   B OD1 1 
ATOM   7510 O  OD2 . ASP   B 1 409 ? -76.972 -16.688 35.184  1.00 11.08 ? 432  ASP   B OD2 1 
ATOM   7511 N  N   . ALA   B 1 410 ? -77.599 -14.857 31.236  1.00 11.83 ? 433  ALA   B N   1 
ATOM   7512 C  CA  . ALA   B 1 410 ? -78.011 -13.608 30.596  1.00 12.15 ? 433  ALA   B CA  1 
ATOM   7513 C  C   . ALA   B 1 410 ? -77.410 -12.411 31.331  1.00 11.91 ? 433  ALA   B C   1 
ATOM   7514 O  O   . ALA   B 1 410 ? -76.884 -11.478 30.699  1.00 11.86 ? 433  ALA   B O   1 
ATOM   7515 C  CB  . ALA   B 1 410 ? -79.537 -13.517 30.525  1.00 12.99 ? 433  ALA   B CB  1 
ATOM   7516 N  N   . ALA   B 1 411 ? -77.537 -12.411 32.668  1.00 12.35 ? 434  ALA   B N   1 
ATOM   7517 C  CA  . ALA   B 1 411 ? -77.057 -11.294 33.475  1.00 13.26 ? 434  ALA   B CA  1 
ATOM   7518 C  C   . ALA   B 1 411 ? -75.530 -11.175 33.378  1.00 13.10 ? 434  ALA   B C   1 
ATOM   7519 O  O   . ALA   B 1 411 ? -74.990 -10.057 33.378  1.00 10.74 ? 434  ALA   B O   1 
ATOM   7520 C  CB  . ALA   B 1 411 ? -77.516 -11.451 34.904  1.00 14.96 ? 434  ALA   B CB  1 
ATOM   7521 N  N   . ALA   B 1 412 ? -74.857 -12.325 33.314  1.00 12.73 ? 435  ALA   B N   1 
ATOM   7522 C  CA  . ALA   B 1 412 ? -73.405 -12.355 33.210  1.00 12.25 ? 435  ALA   B CA  1 
ATOM   7523 C  C   . ALA   B 1 412 ? -72.929 -11.753 31.895  1.00 12.33 ? 435  ALA   B C   1 
ATOM   7524 O  O   . ALA   B 1 412 ? -71.956 -10.998 31.862  1.00 11.13 ? 435  ALA   B O   1 
ATOM   7525 C  CB  . ALA   B 1 412 ? -72.879 -13.748 33.426  1.00 11.86 ? 435  ALA   B CB  1 
ATOM   7526 N  N   . ARG   B 1 413 ? -73.668 -12.028 30.825  1.00 12.54 ? 436  ARG   B N   1 
ATOM   7527 C  CA  . ARG   B 1 413 ? -73.370 -11.455 29.526  1.00 13.17 ? 436  ARG   B CA  1 
ATOM   7528 C  C   . ARG   B 1 413 ? -73.563 -9.939  29.527  1.00 13.65 ? 436  ARG   B C   1 
ATOM   7529 O  O   . ARG   B 1 413 ? -72.733 -9.213  28.980  1.00 12.72 ? 436  ARG   B O   1 
ATOM   7530 C  CB  . ARG   B 1 413 ? -74.291 -12.038 28.451  1.00 12.31 ? 436  ARG   B CB  1 
ATOM   7531 C  CG  . ARG   B 1 413 ? -73.999 -13.516 28.279  1.00 12.42 ? 436  ARG   B CG  1 
ATOM   7532 C  CD  . ARG   B 1 413 ? -74.883 -14.197 27.201  1.00 12.07 ? 436  ARG   B CD  1 
ATOM   7533 N  NE  . ARG   B 1 413 ? -74.760 -15.650 27.369  1.00 11.96 ? 436  ARG   B NE  1 
ATOM   7534 C  CZ  . ARG   B 1 413 ? -74.935 -16.562 26.423  1.00 12.64 ? 436  ARG   B CZ  1 
ATOM   7535 N  NH1 . ARG   B 1 413 ? -75.256 -16.161 25.209  1.00 11.06 ? 436  ARG   B NH1 1 
ATOM   7536 N  NH2 . ARG   B 1 413 ? -74.794 -17.858 26.692  1.00 12.30 ? 436  ARG   B NH2 1 
ATOM   7537 N  N   . THR   B 1 414 ? -74.689 -9.455  30.073  1.00 14.26 ? 437  THR   B N   1 
ATOM   7538 C  CA  . THR   B 1 414 ? -74.907 -8.023  30.190  1.00 14.58 ? 437  THR   B CA  1 
ATOM   7539 C  C   . THR   B 1 414 ? -73.765 -7.348  30.947  1.00 13.77 ? 437  THR   B C   1 
ATOM   7540 O  O   . THR   B 1 414 ? -73.264 -6.306  30.513  1.00 14.87 ? 437  THR   B O   1 
ATOM   7541 C  CB  . THR   B 1 414 ? -76.236 -7.773  30.899  1.00 16.40 ? 437  THR   B CB  1 
ATOM   7542 O  OG1 . THR   B 1 414 ? -77.185 -8.304  29.977  1.00 17.62 ? 437  THR   B OG1 1 
ATOM   7543 C  CG2 . THR   B 1 414 ? -76.473 -6.299  31.120  1.00 18.14 ? 437  THR   B CG2 1 
ATOM   7544 N  N   . GLN   B 1 415 ? -73.379 -7.953  32.073  1.00 13.06 ? 438  GLN   B N   1 
ATOM   7545 C  CA  . GLN   B 1 415 ? -72.359 -7.385  32.930  1.00 12.28 ? 438  GLN   B CA  1 
ATOM   7546 C  C   . GLN   B 1 415 ? -71.014 -7.380  32.204  1.00 12.14 ? 438  GLN   B C   1 
ATOM   7547 O  O   . GLN   B 1 415 ? -70.295 -6.368  32.234  1.00 11.36 ? 438  GLN   B O   1 
ATOM   7548 C  CB  . GLN   B 1 415 ? -72.278 -8.172  34.237  1.00 12.29 ? 438  GLN   B CB  1 
ATOM   7549 C  CG  . GLN   B 1 415 ? -71.137 -7.767  35.162  1.00 12.37 ? 438  GLN   B CG  1 
ATOM   7550 C  CD  . GLN   B 1 415 ? -71.193 -6.328  35.617  1.00 12.96 ? 438  GLN   B CD  1 
ATOM   7551 O  OE1 . GLN   B 1 415 ? -72.266 -5.739  35.778  1.00 14.54 ? 438  GLN   B OE1 1 
ATOM   7552 N  NE2 . GLN   B 1 415 ? -70.022 -5.720  35.780  1.00 12.78 ? 438  GLN   B NE2 1 
ATOM   7553 N  N   . TRP   B 1 416 ? -70.640 -8.534  31.626  1.00 10.95 ? 439  TRP   B N   1 
ATOM   7554 C  CA  . TRP   B 1 416 ? -69.363 -8.647  30.933  1.00 10.38 ? 439  TRP   B CA  1 
ATOM   7555 C  C   . TRP   B 1 416 ? -69.260 -7.637  29.788  1.00 10.66 ? 439  TRP   B C   1 
ATOM   7556 O  O   . TRP   B 1 416 ? -68.220 -7.000  29.565  1.00 9.78  ? 439  TRP   B O   1 
ATOM   7557 C  CB  . TRP   B 1 416 ? -69.167 -10.086 30.449  1.00 10.05 ? 439  TRP   B CB  1 
ATOM   7558 C  CG  . TRP   B 1 416 ? -67.822 -10.367 29.853  1.00 10.56 ? 439  TRP   B CG  1 
ATOM   7559 C  CD1 . TRP   B 1 416 ? -66.687 -10.698 30.524  1.00 10.41 ? 439  TRP   B CD1 1 
ATOM   7560 C  CD2 . TRP   B 1 416 ? -67.490 -10.419 28.445  1.00 10.55 ? 439  TRP   B CD2 1 
ATOM   7561 N  NE1 . TRP   B 1 416 ? -65.670 -10.934 29.637  1.00 10.45 ? 439  TRP   B NE1 1 
ATOM   7562 C  CE2 . TRP   B 1 416 ? -66.126 -10.772 28.360  1.00 10.90 ? 439  TRP   B CE2 1 
ATOM   7563 C  CE3 . TRP   B 1 416 ? -68.187 -10.176 27.256  1.00 10.25 ? 439  TRP   B CE3 1 
ATOM   7564 C  CZ2 . TRP   B 1 416 ? -65.467 -10.900 27.143  1.00 10.57 ? 439  TRP   B CZ2 1 
ATOM   7565 C  CZ3 . TRP   B 1 416 ? -67.530 -10.330 26.044  1.00 10.37 ? 439  TRP   B CZ3 1 
ATOM   7566 C  CH2 . TRP   B 1 416 ? -66.193 -10.725 25.991  1.00 10.28 ? 439  TRP   B CH2 1 
ATOM   7567 N  N   . GLU   B 1 417 ? -70.326 -7.523  29.001  1.00 10.76 ? 440  GLU   B N   1 
ATOM   7568 C  CA  . GLU   B 1 417 ? -70.325 -6.581  27.888  1.00 11.25 ? 440  GLU   B CA  1 
ATOM   7569 C  C   . GLU   B 1 417 ? -70.280 -5.126  28.349  1.00 10.59 ? 440  GLU   B C   1 
ATOM   7570 O  O   . GLU   B 1 417 ? -69.633 -4.316  27.687  1.00 10.38 ? 440  GLU   B O   1 
ATOM   7571 C  CB  . GLU   B 1 417 ? -71.522 -6.858  26.994  1.00 12.66 ? 440  GLU   B CB  1 
ATOM   7572 C  CG  . GLU   B 1 417 ? -71.301 -8.104  26.150  1.00 13.88 ? 440  GLU   B CG  1 
ATOM   7573 C  CD  . GLU   B 1 417 ? -72.394 -8.409  25.148  1.00 15.06 ? 440  GLU   B CD  1 
ATOM   7574 O  OE1 . GLU   B 1 417 ? -72.819 -9.615  25.156  1.00 12.59 ? 440  GLU   B OE1 1 
ATOM   7575 O  OE2 . GLU   B 1 417 ? -72.791 -7.513  24.352  1.00 15.12 ? 440  GLU   B OE2 1 
ATOM   7576 N  N   . ALA   B 1 418 ? -70.890 -4.809  29.494  1.00 11.15 ? 441  ALA   B N   1 
ATOM   7577 C  CA  . ALA   B 1 418 ? -70.851 -3.457  30.043  1.00 12.10 ? 441  ALA   B CA  1 
ATOM   7578 C  C   . ALA   B 1 418 ? -69.427 -3.119  30.491  1.00 11.36 ? 441  ALA   B C   1 
ATOM   7579 O  O   . ALA   B 1 418 ? -68.954 -1.995  30.295  1.00 13.51 ? 441  ALA   B O   1 
ATOM   7580 C  CB  . ALA   B 1 418 ? -71.830 -3.362  31.199  1.00 13.52 ? 441  ALA   B CB  1 
ATOM   7581 N  N   . GLU   B 1 419 ? -68.758 -4.102  31.108  1.00 11.25 ? 442  GLU   B N   1 
ATOM   7582 C  CA  . GLU   B 1 419 ? -67.369 -3.946  31.504  1.00 11.82 ? 442  GLU   B CA  1 
ATOM   7583 C  C   . GLU   B 1 419 ? -66.511 -3.703  30.265  1.00 12.31 ? 442  GLU   B C   1 
ATOM   7584 O  O   . GLU   B 1 419 ? -65.787 -2.719  30.216  1.00 11.94 ? 442  GLU   B O   1 
ATOM   7585 C  CB  . GLU   B 1 419 ? -66.787 -5.093  32.326  1.00 12.06 ? 442  GLU   B CB  1 
ATOM   7586 C  CG  . GLU   B 1 419 ? -67.445 -5.274  33.700  1.00 12.51 ? 442  GLU   B CG  1 
ATOM   7587 C  CD  . GLU   B 1 419 ? -66.894 -6.427  34.514  1.00 13.08 ? 442  GLU   B CD  1 
ATOM   7588 O  OE1 . GLU   B 1 419 ? -65.659 -6.539  34.389  1.00 12.67 ? 442  GLU   B OE1 1 
ATOM   7589 O  OE2 . GLU   B 1 419 ? -67.580 -7.158  35.294  1.00 13.94 ? 442  GLU   B OE2 1 
ATOM   7590 N  N   . TYR   B 1 420 ? -66.627 -4.564  29.241  1.00 12.43 ? 443  TYR   B N   1 
ATOM   7591 C  CA  . TYR   B 1 420 ? -65.848 -4.397  28.028  1.00 12.24 ? 443  TYR   B CA  1 
ATOM   7592 C  C   . TYR   B 1 420 ? -66.107 -3.045  27.351  1.00 12.33 ? 443  TYR   B C   1 
ATOM   7593 O  O   . TYR   B 1 420 ? -65.193 -2.373  26.853  1.00 12.41 ? 443  TYR   B O   1 
ATOM   7594 C  CB  . TYR   B 1 420 ? -66.170 -5.572  27.099  1.00 11.32 ? 443  TYR   B CB  1 
ATOM   7595 C  CG  . TYR   B 1 420 ? -65.129 -5.900  26.034  1.00 11.00 ? 443  TYR   B CG  1 
ATOM   7596 C  CD1 . TYR   B 1 420 ? -63.950 -5.167  25.896  1.00 9.90  ? 443  TYR   B CD1 1 
ATOM   7597 C  CD2 . TYR   B 1 420 ? -65.373 -6.917  25.115  1.00 10.54 ? 443  TYR   B CD2 1 
ATOM   7598 C  CE1 . TYR   B 1 420 ? -63.041 -5.465  24.895  1.00 9.81  ? 443  TYR   B CE1 1 
ATOM   7599 C  CE2 . TYR   B 1 420 ? -64.470 -7.231  24.112  1.00 9.87  ? 443  TYR   B CE2 1 
ATOM   7600 C  CZ  . TYR   B 1 420 ? -63.303 -6.485  23.997  1.00 9.59  ? 443  TYR   B CZ  1 
ATOM   7601 O  OH  . TYR   B 1 420 ? -62.394 -6.788  23.024  1.00 9.27  ? 443  TYR   B OH  1 
ATOM   7602 N  N   . ASP   B 1 421 ? -67.365 -2.629  27.256  1.00 11.92 ? 444  ASP   B N   1 
ATOM   7603 C  CA  . ASP   B 1 421 ? -67.664 -1.311  26.712  1.00 12.74 ? 444  ASP   B CA  1 
ATOM   7604 C  C   . ASP   B 1 421 ? -66.878 -0.221  27.430  1.00 12.63 ? 444  ASP   B C   1 
ATOM   7605 O  O   . ASP   B 1 421 ? -66.320 0.641   26.764  1.00 13.40 ? 444  ASP   B O   1 
ATOM   7606 C  CB  . ASP   B 1 421 ? -69.143 -0.967  26.826  1.00 14.32 ? 444  ASP   B CB  1 
ATOM   7607 C  CG  . ASP   B 1 421 ? -70.049 -1.680  25.840  1.00 16.93 ? 444  ASP   B CG  1 
ATOM   7608 O  OD1 . ASP   B 1 421 ? -69.511 -2.314  24.906  1.00 17.99 ? 444  ASP   B OD1 1 
ATOM   7609 O  OD2 . ASP   B 1 421 ? -71.275 -1.577  26.017  1.00 19.71 ? 444  ASP   B OD2 1 
ATOM   7610 N  N   . ARG   B 1 422 ? -66.818 -0.275  28.766  1.00 12.52 ? 445  ARG   B N   1 
ATOM   7611 C  CA  . ARG   B 1 422 ? -66.135 0.764   29.526  1.00 13.86 ? 445  ARG   B CA  1 
ATOM   7612 C  C   . ARG   B 1 422 ? -64.624 0.727   29.269  1.00 13.60 ? 445  ARG   B C   1 
ATOM   7613 O  O   . ARG   B 1 422 ? -63.961 1.762   29.133  1.00 14.22 ? 445  ARG   B O   1 
ATOM   7614 C  CB  . ARG   B 1 422 ? -66.405 0.659   31.031  1.00 15.01 ? 445  ARG   B CB  1 
ATOM   7615 C  CG  . ARG   B 1 422 ? -67.833 1.040   31.403  1.00 18.12 ? 445  ARG   B CG  1 
ATOM   7616 C  CD  . ARG   B 1 422 ? -68.124 0.804   32.870  1.00 21.30 ? 445  ARG   B CD  1 
ATOM   7617 N  NE  . ARG   B 1 422 ? -67.348 1.694   33.745  1.00 24.98 ? 445  ARG   B NE  1 
ATOM   7618 C  CZ  . ARG   B 1 422 ? -67.621 2.944   34.110  1.00 26.75 ? 445  ARG   B CZ  1 
ATOM   7619 N  NH1 . ARG   B 1 422 ? -68.607 3.628   33.551  1.00 24.94 ? 445  ARG   B NH1 1 
ATOM   7620 N  NH2 . ARG   B 1 422 ? -66.878 3.511   35.053  1.00 28.19 ? 445  ARG   B NH2 1 
ATOM   7621 N  N   . ILE   B 1 423 ? -64.071 -0.490  29.218  1.00 13.45 ? 446  ILE   B N   1 
ATOM   7622 C  CA  . ILE   B 1 423 ? -62.654 -0.674  28.924  1.00 11.65 ? 446  ILE   B CA  1 
ATOM   7623 C  C   . ILE   B 1 423 ? -62.322 -0.085  27.559  1.00 11.62 ? 446  ILE   B C   1 
ATOM   7624 O  O   . ILE   B 1 423 ? -61.364 0.692   27.434  1.00 11.96 ? 446  ILE   B O   1 
ATOM   7625 C  CB  . ILE   B 1 423 ? -62.324 -2.167  29.060  1.00 11.58 ? 446  ILE   B CB  1 
ATOM   7626 C  CG1 . ILE   B 1 423 ? -62.461 -2.607  30.537  1.00 11.31 ? 446  ILE   B CG1 1 
ATOM   7627 C  CG2 . ILE   B 1 423 ? -60.936 -2.450  28.499  1.00 12.07 ? 446  ILE   B CG2 1 
ATOM   7628 C  CD1 . ILE   B 1 423 ? -62.639 -4.098  30.747  1.00 11.19 ? 446  ILE   B CD1 1 
ATOM   7629 N  N   . ILE   B 1 424 ? -63.121 -0.407  26.535  1.00 11.24 ? 447  ILE   B N   1 
ATOM   7630 C  CA  . ILE   B 1 424 ? -62.924 0.213   25.221  1.00 11.19 ? 447  ILE   B CA  1 
ATOM   7631 C  C   . ILE   B 1 424 ? -62.974 1.745   25.315  1.00 12.60 ? 447  ILE   B C   1 
ATOM   7632 O  O   . ILE   B 1 424 ? -62.094 2.463   24.776  1.00 12.47 ? 447  ILE   B O   1 
ATOM   7633 C  CB  . ILE   B 1 424 ? -63.903 -0.352  24.193  1.00 10.71 ? 447  ILE   B CB  1 
ATOM   7634 C  CG1 . ILE   B 1 424 ? -63.680 -1.869  24.050  1.00 10.41 ? 447  ILE   B CG1 1 
ATOM   7635 C  CG2 . ILE   B 1 424 ? -63.763 0.370   22.843  1.00 10.35 ? 447  ILE   B CG2 1 
ATOM   7636 C  CD1 . ILE   B 1 424 ? -64.828 -2.632  23.388  1.00 10.33 ? 447  ILE   B CD1 1 
ATOM   7637 N  N   . ASP   B 1 425 ? -64.021 2.260   25.966  1.00 12.12 ? 448  ASP   B N   1 
ATOM   7638 C  CA  . ASP   B 1 425 ? -64.205 3.708   26.007  1.00 14.28 ? 448  ASP   B CA  1 
ATOM   7639 C  C   . ASP   B 1 425 ? -63.028 4.403   26.684  1.00 13.92 ? 448  ASP   B C   1 
ATOM   7640 O  O   . ASP   B 1 425 ? -62.676 5.508   26.270  1.00 18.32 ? 448  ASP   B O   1 
ATOM   7641 C  CB  . ASP   B 1 425 ? -65.552 4.102   26.584  1.00 13.96 ? 448  ASP   B CB  1 
ATOM   7642 C  CG  . ASP   B 1 425 ? -66.714 3.873   25.629  1.00 14.47 ? 448  ASP   B CG  1 
ATOM   7643 O  OD1 . ASP   B 1 425 ? -66.533 4.127   24.425  1.00 13.14 ? 448  ASP   B OD1 1 
ATOM   7644 O  OD2 . ASP   B 1 425 ? -67.811 3.481   26.097  1.00 14.58 ? 448  ASP   B OD2 1 
ATOM   7645 N  N   . GLN   B 1 426 ? -62.435 3.750   27.677  1.00 13.44 ? 449  GLN   B N   1 
ATOM   7646 C  CA  . GLN   B 1 426 ? -61.389 4.309   28.520  1.00 13.99 ? 449  GLN   B CA  1 
ATOM   7647 C  C   . GLN   B 1 426 ? -60.021 4.314   27.835  1.00 14.73 ? 449  GLN   B C   1 
ATOM   7648 O  O   . GLN   B 1 426 ? -59.089 4.880   28.398  1.00 15.20 ? 449  GLN   B O   1 
ATOM   7649 C  CB  . GLN   B 1 426 ? -61.338 3.585   29.865  1.00 14.45 ? 449  GLN   B CB  1 
ATOM   7650 C  CG  . GLN   B 1 426 ? -62.551 3.899   30.746  1.00 14.78 ? 449  GLN   B CG  1 
ATOM   7651 C  CD  . GLN   B 1 426 ? -62.607 3.152   32.052  1.00 16.28 ? 449  GLN   B CD  1 
ATOM   7652 O  OE1 . GLN   B 1 426 ? -61.637 2.521   32.495  1.00 16.58 ? 449  GLN   B OE1 1 
ATOM   7653 N  NE2 . GLN   B 1 426 ? -63.784 3.206   32.687  1.00 16.54 ? 449  GLN   B NE2 1 
ATOM   7654 N  N   . HIS   B 1 427 ? -59.879 3.701   26.647  1.00 12.84 ? 450  HIS   B N   1 
ATOM   7655 C  CA  . HIS   B 1 427 ? -58.582 3.562   26.004  1.00 12.76 ? 450  HIS   B CA  1 
ATOM   7656 C  C   . HIS   B 1 427 ? -58.590 3.987   24.541  1.00 12.82 ? 450  HIS   B C   1 
ATOM   7657 O  O   . HIS   B 1 427 ? -57.668 3.663   23.808  1.00 13.80 ? 450  HIS   B O   1 
ATOM   7658 C  CB  . HIS   B 1 427 ? -58.063 2.121   26.078  1.00 12.62 ? 450  HIS   B CB  1 
ATOM   7659 C  CG  . HIS   B 1 427 ? -57.857 1.679   27.485  1.00 12.89 ? 450  HIS   B CG  1 
ATOM   7660 N  ND1 . HIS   B 1 427 ? -58.824 1.053   28.235  1.00 13.19 ? 450  HIS   B ND1 1 
ATOM   7661 C  CD2 . HIS   B 1 427 ? -56.789 1.806   28.283  1.00 12.91 ? 450  HIS   B CD2 1 
ATOM   7662 C  CE1 . HIS   B 1 427 ? -58.342 0.825   29.466  1.00 12.15 ? 450  HIS   B CE1 1 
ATOM   7663 N  NE2 . HIS   B 1 427 ? -57.088 1.267   29.505  1.00 12.70 ? 450  HIS   B NE2 1 
ATOM   7664 N  N   . ARG   B 1 428 ? -59.562 4.802   24.099  1.00 13.40 ? 451  ARG   B N   1 
ATOM   7665 C  CA  . ARG   B 1 428 ? -59.668 5.137   22.690  1.00 11.62 ? 451  ARG   B CA  1 
ATOM   7666 C  C   . ARG   B 1 428 ? -58.471 5.931   22.143  1.00 11.79 ? 451  ARG   B C   1 
ATOM   7667 O  O   . ARG   B 1 428 ? -58.225 5.871   20.935  1.00 13.43 ? 451  ARG   B O   1 
ATOM   7668 C  CB  . ARG   B 1 428 ? -60.920 5.963   22.423  1.00 11.79 ? 451  ARG   B CB  1 
ATOM   7669 C  CG  . ARG   B 1 428 ? -62.175 5.116   22.595  1.00 12.47 ? 451  ARG   B CG  1 
ATOM   7670 C  CD  . ARG   B 1 428 ? -63.443 5.925   22.351  1.00 12.62 ? 451  ARG   B CD  1 
ATOM   7671 N  NE  . ARG   B 1 428 ? -64.606 5.029   22.451  1.00 12.90 ? 451  ARG   B NE  1 
ATOM   7672 C  CZ  . ARG   B 1 428 ? -64.997 4.216   21.473  1.00 12.89 ? 451  ARG   B CZ  1 
ATOM   7673 N  NH1 . ARG   B 1 428 ? -64.394 4.242   20.293  1.00 13.47 ? 451  ARG   B NH1 1 
ATOM   7674 N  NH2 . ARG   B 1 428 ? -65.966 3.328   21.664  1.00 13.52 ? 451  ARG   B NH2 1 
ATOM   7675 N  N   . SER   B 1 429 ? -57.766 6.684   22.998  1.00 13.21 ? 452  SER   B N   1 
ATOM   7676 C  CA  . SER   B 1 429 ? -56.749 7.617   22.524  1.00 13.31 ? 452  SER   B CA  1 
ATOM   7677 C  C   . SER   B 1 429 ? -55.334 7.040   22.596  1.00 13.45 ? 452  SER   B C   1 
ATOM   7678 O  O   . SER   B 1 429 ? -54.384 7.738   22.253  1.00 13.93 ? 452  SER   B O   1 
ATOM   7679 C  CB  . SER   B 1 429 ? -56.812 8.929   23.316  1.00 14.35 ? 452  SER   B CB  1 
ATOM   7680 O  OG  . SER   B 1 429 ? -58.110 9.503   23.187  1.00 12.88 ? 452  SER   B OG  1 
ATOM   7681 N  N   . SER   B 1 430 ? -55.165 5.810   23.070  1.00 13.00 ? 453  SER   B N   1 
ATOM   7682 C  CA  . SER   B 1 430 ? -53.819 5.259   23.249  1.00 12.33 ? 453  SER   B CA  1 
ATOM   7683 C  C   . SER   B 1 430 ? -53.208 4.917   21.898  1.00 11.96 ? 453  SER   B C   1 
ATOM   7684 O  O   . SER   B 1 430 ? -53.772 4.131   21.146  1.00 12.10 ? 453  SER   B O   1 
ATOM   7685 C  CB  . SER   B 1 430 ? -53.825 4.042   24.171  1.00 12.93 ? 453  SER   B CB  1 
ATOM   7686 O  OG  . SER   B 1 430 ? -52.598 3.341   24.077  1.00 13.41 ? 453  SER   B OG  1 
ATOM   7687 N  N   . PRO   B 1 431 ? -52.035 5.482   21.514  1.00 11.28 ? 454  PRO   B N   1 
ATOM   7688 C  CA  . PRO   B 1 431 ? -51.390 5.080   20.279  1.00 11.41 ? 454  PRO   B CA  1 
ATOM   7689 C  C   . PRO   B 1 431 ? -50.878 3.637   20.326  1.00 10.48 ? 454  PRO   B C   1 
ATOM   7690 O  O   . PRO   B 1 431 ? -50.895 2.959   19.297  1.00 10.11 ? 454  PRO   B O   1 
ATOM   7691 C  CB  . PRO   B 1 431 ? -50.272 6.143   20.103  1.00 11.43 ? 454  PRO   B CB  1 
ATOM   7692 C  CG  . PRO   B 1 431 ? -49.971 6.555   21.536  1.00 11.28 ? 454  PRO   B CG  1 
ATOM   7693 C  CD  . PRO   B 1 431 ? -51.352 6.623   22.170  1.00 11.80 ? 454  PRO   B CD  1 
ATOM   7694 N  N   . SER   B 1 432 ? -50.395 3.171   21.483  1.00 9.62  ? 455  SER   B N   1 
ATOM   7695 C  CA  . SER   B 1 432 ? -49.823 1.831   21.550  1.00 9.99  ? 455  SER   B CA  1 
ATOM   7696 C  C   . SER   B 1 432 ? -50.894 0.771   21.294  1.00 9.48  ? 455  SER   B C   1 
ATOM   7697 O  O   . SER   B 1 432 ? -50.659 -0.230  20.612  1.00 10.10 ? 455  SER   B O   1 
ATOM   7698 C  CB  . SER   B 1 432 ? -49.118 1.600   22.881  1.00 10.63 ? 455  SER   B CB  1 
ATOM   7699 O  OG  . SER   B 1 432 ? -49.996 1.710   23.997  1.00 11.28 ? 455  SER   B OG  1 
ATOM   7700 N  N   . LEU   B 1 433 ? -52.082 0.992   21.863  1.00 10.25 ? 456  LEU   B N   1 
ATOM   7701 C  CA  . LEU   B 1 433 ? -53.180 0.041   21.754  1.00 10.15 ? 456  LEU   B CA  1 
ATOM   7702 C  C   . LEU   B 1 433 ? -53.626 -0.026  20.298  1.00 9.69  ? 456  LEU   B C   1 
ATOM   7703 O  O   . LEU   B 1 433 ? -54.101 0.966   19.745  1.00 10.27 ? 456  LEU   B O   1 
ATOM   7704 C  CB  . LEU   B 1 433 ? -54.324 0.397   22.689  1.00 10.71 ? 456  LEU   B CB  1 
ATOM   7705 C  CG  . LEU   B 1 433 ? -55.586 -0.459  22.526  1.00 11.23 ? 456  LEU   B CG  1 
ATOM   7706 C  CD1 . LEU   B 1 433 ? -55.231 -1.876  22.767  1.00 11.41 ? 456  LEU   B CD1 1 
ATOM   7707 C  CD2 . LEU   B 1 433 ? -56.622 0.018   23.543  1.00 11.24 ? 456  LEU   B CD2 1 
ATOM   7708 N  N   . VAL   B 1 434 ? -53.516 -1.218  19.697  1.00 9.28  ? 457  VAL   B N   1 
ATOM   7709 C  CA  . VAL   B 1 434 ? -53.832 -1.380  18.280  1.00 9.22  ? 457  VAL   B CA  1 
ATOM   7710 C  C   . VAL   B 1 434 ? -54.807 -2.535  18.021  1.00 9.00  ? 457  VAL   B C   1 
ATOM   7711 O  O   . VAL   B 1 434 ? -55.337 -2.627  16.918  1.00 9.77  ? 457  VAL   B O   1 
ATOM   7712 C  CB  . VAL   B 1 434 ? -52.618 -1.521  17.341  1.00 9.03  ? 457  VAL   B CB  1 
ATOM   7713 C  CG1 . VAL   B 1 434 ? -51.774 -0.246  17.278  1.00 9.17  ? 457  VAL   B CG1 1 
ATOM   7714 C  CG2 . VAL   B 1 434 ? -51.747 -2.733  17.682  1.00 9.06  ? 457  VAL   B CG2 1 
ATOM   7715 N  N   . LEU   B 1 435 ? -55.052 -3.420  18.984  1.00 8.80  ? 458  LEU   B N   1 
ATOM   7716 C  CA  . LEU   B 1 435 ? -55.864 -4.612  18.729  1.00 8.61  ? 458  LEU   B CA  1 
ATOM   7717 C  C   . LEU   B 1 435 ? -56.549 -5.071  20.013  1.00 9.86  ? 458  LEU   B C   1 
ATOM   7718 O  O   . LEU   B 1 435 ? -55.918 -5.046  21.062  1.00 8.54  ? 458  LEU   B O   1 
ATOM   7719 C  CB  . LEU   B 1 435 ? -54.978 -5.697  18.116  1.00 8.83  ? 458  LEU   B CB  1 
ATOM   7720 C  CG  . LEU   B 1 435 ? -55.638 -7.032  17.748  1.00 9.18  ? 458  LEU   B CG  1 
ATOM   7721 C  CD1 . LEU   B 1 435 ? -54.916 -7.741  16.617  1.00 9.27  ? 458  LEU   B CD1 1 
ATOM   7722 C  CD2 . LEU   B 1 435 ? -55.724 -7.961  18.902  1.00 9.36  ? 458  LEU   B CD2 1 
ATOM   7723 N  N   . TRP   B 1 436 ? -57.851 -5.441  19.888  1.00 9.16  ? 459  TRP   B N   1 
ATOM   7724 C  CA  . TRP   B 1 436 ? -58.669 -6.037  20.935  1.00 9.22  ? 459  TRP   B CA  1 
ATOM   7725 C  C   . TRP   B 1 436 ? -58.799 -7.536  20.700  1.00 9.05  ? 459  TRP   B C   1 
ATOM   7726 O  O   . TRP   B 1 436 ? -59.172 -7.940  19.591  1.00 8.17  ? 459  TRP   B O   1 
ATOM   7727 C  CB  . TRP   B 1 436 ? -60.091 -5.454  20.907  1.00 9.41  ? 459  TRP   B CB  1 
ATOM   7728 C  CG  . TRP   B 1 436 ? -60.132 -3.996  21.226  1.00 9.83  ? 459  TRP   B CG  1 
ATOM   7729 C  CD1 . TRP   B 1 436 ? -60.320 -2.989  20.337  1.00 10.63 ? 459  TRP   B CD1 1 
ATOM   7730 C  CD2 . TRP   B 1 436 ? -59.977 -3.400  22.523  1.00 10.09 ? 459  TRP   B CD2 1 
ATOM   7731 N  NE1 . TRP   B 1 436 ? -60.332 -1.791  20.993  1.00 11.49 ? 459  TRP   B NE1 1 
ATOM   7732 C  CE2 . TRP   B 1 436 ? -60.086 -2.010  22.324  1.00 10.54 ? 459  TRP   B CE2 1 
ATOM   7733 C  CE3 . TRP   B 1 436 ? -59.763 -3.911  23.812  1.00 10.49 ? 459  TRP   B CE3 1 
ATOM   7734 C  CZ2 . TRP   B 1 436 ? -59.997 -1.110  23.375  1.00 10.88 ? 459  TRP   B CZ2 1 
ATOM   7735 C  CZ3 . TRP   B 1 436 ? -59.646 -3.012  24.851  1.00 11.15 ? 459  TRP   B CZ3 1 
ATOM   7736 C  CH2 . TRP   B 1 436 ? -59.765 -1.634  24.619  1.00 10.68 ? 459  TRP   B CH2 1 
ATOM   7737 N  N   . VAL   B 1 437 ? -58.526 -8.307  21.758  1.00 9.38  ? 460  VAL   B N   1 
ATOM   7738 C  CA  . VAL   B 1 437 ? -58.744 -9.742  21.800  1.00 9.44  ? 460  VAL   B CA  1 
ATOM   7739 C  C   . VAL   B 1 437 ? -59.983 -10.029 22.641  1.00 9.39  ? 460  VAL   B C   1 
ATOM   7740 O  O   . VAL   B 1 437 ? -59.949 -9.961  23.891  1.00 10.03 ? 460  VAL   B O   1 
ATOM   7741 C  CB  . VAL   B 1 437 ? -57.535 -10.519 22.335  1.00 9.81  ? 460  VAL   B CB  1 
ATOM   7742 C  CG1 . VAL   B 1 437 ? -57.792 -12.009 22.253  1.00 10.73 ? 460  VAL   B CG1 1 
ATOM   7743 C  CG2 . VAL   B 1 437 ? -56.263 -10.163 21.587  1.00 10.03 ? 460  VAL   B CG2 1 
ATOM   7744 N  N   . ASN   B 1 438 ? -61.083 -10.345 21.943  1.00 9.12  ? 461  ASN   B N   1 
ATOM   7745 C  CA  . ASN   B 1 438 ? -62.359 -10.473 22.622  1.00 8.92  ? 461  ASN   B CA  1 
ATOM   7746 C  C   . ASN   B 1 438 ? -62.368 -11.640 23.600  1.00 9.18  ? 461  ASN   B C   1 
ATOM   7747 O  O   . ASN   B 1 438 ? -62.875 -11.518 24.706  1.00 9.11  ? 461  ASN   B O   1 
ATOM   7748 C  CB  . ASN   B 1 438 ? -63.520 -10.629 21.652  1.00 8.43  ? 461  ASN   B CB  1 
ATOM   7749 C  CG  . ASN   B 1 438 ? -63.877 -9.414  20.847  1.00 8.79  ? 461  ASN   B CG  1 
ATOM   7750 O  OD1 . ASN   B 1 438 ? -63.278 -8.348  20.997  1.00 8.81  ? 461  ASN   B OD1 1 
ATOM   7751 N  ND2 . ASN   B 1 438 ? -64.884 -9.567  19.990  1.00 8.57  ? 461  ASN   B ND2 1 
ATOM   7752 N  N   . GLN   B 1 439 ? -61.849 -12.792 23.165  1.00 9.30  ? 462  GLN   B N   1 
ATOM   7753 C  CA  . GLN   B 1 439 ? -62.031 -14.041 23.866  1.00 9.72  ? 462  GLN   B CA  1 
ATOM   7754 C  C   . GLN   B 1 439 ? -60.800 -14.916 23.621  1.00 9.57  ? 462  GLN   B C   1 
ATOM   7755 O  O   . GLN   B 1 439 ? -60.111 -14.744 22.617  1.00 8.56  ? 462  GLN   B O   1 
ATOM   7756 C  CB  . GLN   B 1 439 ? -63.325 -14.710 23.417  1.00 10.25 ? 462  GLN   B CB  1 
ATOM   7757 C  CG  . GLN   B 1 439 ? -64.574 -13.853 23.606  1.00 11.03 ? 462  GLN   B CG  1 
ATOM   7758 C  CD  . GLN   B 1 439 ? -65.866 -14.580 23.307  1.00 12.44 ? 462  GLN   B CD  1 
ATOM   7759 O  OE1 . GLN   B 1 439 ? -66.352 -15.376 24.115  1.00 16.29 ? 462  GLN   B OE1 1 
ATOM   7760 N  NE2 . GLN   B 1 439 ? -66.480 -14.272 22.169  1.00 11.49 ? 462  GLN   B NE2 1 
ATOM   7761 N  N   . ASN   B 1 440 ? -60.588 -15.857 24.540  1.00 9.57  ? 463  ASN   B N   1 
ATOM   7762 C  CA  . ASN   B 1 440 ? -59.367 -16.651 24.621  1.00 9.33  ? 463  ASN   B CA  1 
ATOM   7763 C  C   . ASN   B 1 440 ? -59.688 -18.137 24.811  1.00 10.11 ? 463  ASN   B C   1 
ATOM   7764 O  O   . ASN   B 1 440 ? -60.246 -18.526 25.853  1.00 9.58  ? 463  ASN   B O   1 
ATOM   7765 C  CB  . ASN   B 1 440 ? -58.473 -16.216 25.773  1.00 10.39 ? 463  ASN   B CB  1 
ATOM   7766 C  CG  . ASN   B 1 440 ? -57.171 -16.973 25.784  1.00 11.32 ? 463  ASN   B CG  1 
ATOM   7767 O  OD1 . ASN   B 1 440 ? -56.387 -16.886 24.830  1.00 11.50 ? 463  ASN   B OD1 1 
ATOM   7768 N  ND2 . ASN   B 1 440 ? -56.985 -17.845 26.768  1.00 10.46 ? 463  ASN   B ND2 1 
ATOM   7769 N  N   . GLU   B 1 441 ? -59.302 -18.949 23.814  1.00 9.34  ? 464  GLU   B N   1 
ATOM   7770 C  CA  . GLU   B 1 441 ? -59.343 -20.405 23.907  1.00 10.59 ? 464  GLU   B CA  1 
ATOM   7771 C  C   . GLU   B 1 441 ? -60.718 -20.947 24.312  1.00 10.75 ? 464  GLU   B C   1 
ATOM   7772 O  O   . GLU   B 1 441 ? -60.846 -22.002 24.946  1.00 11.31 ? 464  GLU   B O   1 
ATOM   7773 C  CB  . GLU   B 1 441 ? -58.239 -20.872 24.851  1.00 12.17 ? 464  GLU   B CB  1 
ATOM   7774 C  CG  . GLU   B 1 441 ? -56.860 -20.745 24.214  1.00 12.72 ? 464  GLU   B CG  1 
ATOM   7775 C  CD  . GLU   B 1 441 ? -55.777 -21.652 24.776  1.00 14.38 ? 464  GLU   B CD  1 
ATOM   7776 O  OE1 . GLU   B 1 441 ? -56.063 -22.367 25.762  1.00 14.10 ? 464  GLU   B OE1 1 
ATOM   7777 O  OE2 . GLU   B 1 441 ? -54.665 -21.644 24.170  1.00 14.35 ? 464  GLU   B OE2 1 
ATOM   7778 N  N   . GLY   B 1 442 ? -61.773 -20.224 23.942  1.00 10.17 ? 465  GLY   B N   1 
ATOM   7779 C  CA  . GLY   B 1 442 ? -63.123 -20.672 24.222  1.00 10.87 ? 465  GLY   B CA  1 
ATOM   7780 C  C   . GLY   B 1 442 ? -63.574 -20.407 25.656  1.00 10.57 ? 465  GLY   B C   1 
ATOM   7781 O  O   . GLY   B 1 442 ? -64.651 -20.862 26.011  1.00 10.97 ? 465  GLY   B O   1 
ATOM   7782 N  N   . TRP   B 1 443 ? -62.794 -19.682 26.479  1.00 10.48 ? 466  TRP   B N   1 
ATOM   7783 C  CA  . TRP   B 1 443 ? -63.058 -19.601 27.916  1.00 10.68 ? 466  TRP   B CA  1 
ATOM   7784 C  C   . TRP   B 1 443 ? -64.245 -18.678 28.154  1.00 10.89 ? 466  TRP   B C   1 
ATOM   7785 O  O   . TRP   B 1 443 ? -64.219 -17.527 27.763  1.00 11.19 ? 466  TRP   B O   1 
ATOM   7786 C  CB  . TRP   B 1 443 ? -61.858 -19.088 28.715  1.00 11.68 ? 466  TRP   B CB  1 
ATOM   7787 C  CG  . TRP   B 1 443 ? -60.651 -19.986 28.666  1.00 11.65 ? 466  TRP   B CG  1 
ATOM   7788 C  CD1 . TRP   B 1 443 ? -60.581 -21.235 28.137  1.00 12.41 ? 466  TRP   B CD1 1 
ATOM   7789 C  CD2 . TRP   B 1 443 ? -59.342 -19.688 29.177  1.00 12.07 ? 466  TRP   B CD2 1 
ATOM   7790 N  NE1 . TRP   B 1 443 ? -59.324 -21.754 28.303  1.00 13.08 ? 466  TRP   B NE1 1 
ATOM   7791 C  CE2 . TRP   B 1 443 ? -58.544 -20.831 28.935  1.00 11.65 ? 466  TRP   B CE2 1 
ATOM   7792 C  CE3 . TRP   B 1 443 ? -58.759 -18.569 29.792  1.00 12.61 ? 466  TRP   B CE3 1 
ATOM   7793 C  CZ2 . TRP   B 1 443 ? -57.192 -20.882 29.264  1.00 11.94 ? 466  TRP   B CZ2 1 
ATOM   7794 C  CZ3 . TRP   B 1 443 ? -57.422 -18.635 30.140  1.00 12.29 ? 466  TRP   B CZ3 1 
ATOM   7795 C  CH2 . TRP   B 1 443 ? -56.649 -19.767 29.859  1.00 12.21 ? 466  TRP   B CH2 1 
ATOM   7796 N  N   . GLY   B 1 444 ? -65.318 -19.228 28.726  1.00 10.39 ? 467  GLY   B N   1 
ATOM   7797 C  CA  . GLY   B 1 444 ? -66.517 -18.444 28.946  1.00 10.70 ? 467  GLY   B CA  1 
ATOM   7798 C  C   . GLY   B 1 444 ? -67.169 -18.003 27.642  1.00 11.38 ? 467  GLY   B C   1 
ATOM   7799 O  O   . GLY   B 1 444 ? -67.846 -16.964 27.607  1.00 11.99 ? 467  GLY   B O   1 
ATOM   7800 N  N   . GLN   B 1 445 ? -66.981 -18.765 26.560  1.00 11.03 ? 468  GLN   B N   1 
ATOM   7801 C  CA  . GLN   B 1 445 ? -67.205 -18.173 25.254  1.00 11.26 ? 468  GLN   B CA  1 
ATOM   7802 C  C   . GLN   B 1 445 ? -68.694 -18.110 24.880  1.00 11.18 ? 468  GLN   B C   1 
ATOM   7803 O  O   . GLN   B 1 445 ? -69.519 -18.931 25.306  1.00 11.58 ? 468  GLN   B O   1 
ATOM   7804 C  CB  . GLN   B 1 445 ? -66.440 -18.920 24.167  1.00 11.56 ? 468  GLN   B CB  1 
ATOM   7805 C  CG  . GLN   B 1 445 ? -67.018 -20.296 23.877  1.00 11.84 ? 468  GLN   B CG  1 
ATOM   7806 C  CD  . GLN   B 1 445 ? -66.269 -21.065 22.824  1.00 12.36 ? 468  GLN   B CD  1 
ATOM   7807 O  OE1 . GLN   B 1 445 ? -65.661 -20.501 21.920  1.00 10.83 ? 468  GLN   B OE1 1 
ATOM   7808 N  NE2 . GLN   B 1 445 ? -66.209 -22.384 23.002  1.00 13.73 ? 468  GLN   B NE2 1 
ATOM   7809 N  N   . TYR   B 1 446 ? -69.020 -17.092 24.089  1.00 10.16 ? 469  TYR   B N   1 
ATOM   7810 C  CA  . TYR   B 1 446 ? -70.327 -16.961 23.468  1.00 10.14 ? 469  TYR   B CA  1 
ATOM   7811 C  C   . TYR   B 1 446 ? -70.258 -15.898 22.383  1.00 9.92  ? 469  TYR   B C   1 
ATOM   7812 O  O   . TYR   B 1 446 ? -69.298 -15.144 22.331  1.00 10.73 ? 469  TYR   B O   1 
ATOM   7813 C  CB  . TYR   B 1 446 ? -71.377 -16.630 24.535  1.00 9.89  ? 469  TYR   B CB  1 
ATOM   7814 C  CG  . TYR   B 1 446 ? -71.350 -15.198 25.035  1.00 9.80  ? 469  TYR   B CG  1 
ATOM   7815 C  CD1 . TYR   B 1 446 ? -70.329 -14.752 25.854  1.00 10.59 ? 469  TYR   B CD1 1 
ATOM   7816 C  CD2 . TYR   B 1 446 ? -72.319 -14.281 24.639  1.00 10.51 ? 469  TYR   B CD2 1 
ATOM   7817 C  CE1 . TYR   B 1 446 ? -70.271 -13.436 26.275  1.00 10.59 ? 469  TYR   B CE1 1 
ATOM   7818 C  CE2 . TYR   B 1 446 ? -72.299 -12.975 25.095  1.00 10.82 ? 469  TYR   B CE2 1 
ATOM   7819 C  CZ  . TYR   B 1 446 ? -71.258 -12.544 25.898  1.00 11.03 ? 469  TYR   B CZ  1 
ATOM   7820 O  OH  . TYR   B 1 446 ? -71.214 -11.248 26.326  1.00 11.25 ? 469  TYR   B OH  1 
ATOM   7821 N  N   . ASP   B 1 447 ? -71.287 -15.898 21.525  1.00 9.86  ? 470  ASP   B N   1 
ATOM   7822 C  CA  . ASP   B 1 447 ? -71.543 -14.877 20.513  1.00 10.35 ? 470  ASP   B CA  1 
ATOM   7823 C  C   . ASP   B 1 447 ? -70.261 -14.418 19.828  1.00 9.91  ? 470  ASP   B C   1 
ATOM   7824 O  O   . ASP   B 1 447 ? -69.991 -13.242 19.785  1.00 9.48  ? 470  ASP   B O   1 
ATOM   7825 C  CB  . ASP   B 1 447 ? -72.321 -13.720 21.132  1.00 11.64 ? 470  ASP   B CB  1 
ATOM   7826 C  CG  . ASP   B 1 447 ? -73.783 -14.003 21.452  1.00 12.54 ? 470  ASP   B CG  1 
ATOM   7827 O  OD1 . ASP   B 1 447 ? -74.198 -15.177 21.327  1.00 11.04 ? 470  ASP   B OD1 1 
ATOM   7828 O  OD2 . ASP   B 1 447 ? -74.482 -13.031 21.849  1.00 11.80 ? 470  ASP   B OD2 1 
ATOM   7829 N  N   . GLN   B 1 448 ? -69.474 -15.333 19.242  1.00 10.53 ? 471  GLN   B N   1 
ATOM   7830 C  CA  . GLN   B 1 448 ? -68.136 -14.981 18.781  1.00 10.66 ? 471  GLN   B CA  1 
ATOM   7831 C  C   . GLN   B 1 448 ? -68.193 -13.960 17.657  1.00 11.16 ? 471  GLN   B C   1 
ATOM   7832 O  O   . GLN   B 1 448 ? -67.510 -12.935 17.702  1.00 9.73  ? 471  GLN   B O   1 
ATOM   7833 C  CB  . GLN   B 1 448 ? -67.370 -16.241 18.365  1.00 10.29 ? 471  GLN   B CB  1 
ATOM   7834 C  CG  . GLN   B 1 448 ? -67.152 -17.222 19.519  1.00 10.71 ? 471  GLN   B CG  1 
ATOM   7835 C  CD  . GLN   B 1 448 ? -68.312 -18.126 19.880  1.00 11.80 ? 471  GLN   B CD  1 
ATOM   7836 O  OE1 . GLN   B 1 448 ? -69.408 -18.061 19.318  1.00 13.24 ? 471  GLN   B OE1 1 
ATOM   7837 N  NE2 . GLN   B 1 448 ? -68.075 -19.033 20.817  1.00 12.35 ? 471  GLN   B NE2 1 
ATOM   7838 N  N   . ALA   B 1 449 ? -69.013 -14.265 16.644  1.00 10.06 ? 472  ALA   B N   1 
ATOM   7839 C  CA  . ALA   B 1 449 ? -69.155 -13.368 15.519  1.00 10.30 ? 472  ALA   B CA  1 
ATOM   7840 C  C   . ALA   B 1 449 ? -69.822 -12.046 15.904  1.00 10.08 ? 472  ALA   B C   1 
ATOM   7841 O  O   . ALA   B 1 449 ? -69.335 -10.983 15.508  1.00 9.48  ? 472  ALA   B O   1 
ATOM   7842 C  CB  . ALA   B 1 449 ? -69.910 -14.088 14.430  1.00 10.75 ? 472  ALA   B CB  1 
ATOM   7843 N  N   . ARG   B 1 450 ? -70.933 -12.078 16.645  1.00 11.38 ? 473  ARG   B N   1 
ATOM   7844 C  CA  . ARG   B 1 450 ? -71.610 -10.849 17.026  1.00 11.57 ? 473  ARG   B CA  1 
ATOM   7845 C  C   . ARG   B 1 450 ? -70.621 -9.924  17.743  1.00 11.31 ? 473  ARG   B C   1 
ATOM   7846 O  O   . ARG   B 1 450 ? -70.610 -8.706  17.526  1.00 10.77 ? 473  ARG   B O   1 
ATOM   7847 C  CB  . ARG   B 1 450 ? -72.821 -11.059 17.949  1.00 12.67 ? 473  ARG   B CB  1 
ATOM   7848 C  CG  . ARG   B 1 450 ? -73.339 -9.750  18.538  1.00 14.13 ? 473  ARG   B CG  1 
ATOM   7849 C  CD  . ARG   B 1 450 ? -74.638 -9.759  19.301  1.00 15.33 ? 473  ARG   B CD  1 
ATOM   7850 N  NE  . ARG   B 1 450 ? -74.429 -10.319 20.618  1.00 18.27 ? 473  ARG   B NE  1 
ATOM   7851 C  CZ  . ARG   B 1 450 ? -73.953 -9.706  21.685  1.00 16.32 ? 473  ARG   B CZ  1 
ATOM   7852 N  NH1 . ARG   B 1 450 ? -73.952 -8.383  21.821  1.00 16.92 ? 473  ARG   B NH1 1 
ATOM   7853 N  NH2 . ARG   B 1 450 ? -73.578 -10.485 22.651  1.00 17.96 ? 473  ARG   B NH2 1 
ATOM   7854 N  N   . LEU   B 1 451 ? -69.822 -10.477 18.665  1.00 10.30 ? 474  LEU   B N   1 
ATOM   7855 C  CA  . LEU   B 1 451 ? -68.992 -9.639  19.503  1.00 10.54 ? 474  LEU   B CA  1 
ATOM   7856 C  C   . LEU   B 1 451 ? -67.822 -9.042  18.708  1.00 10.71 ? 474  LEU   B C   1 
ATOM   7857 O  O   . LEU   B 1 451 ? -67.385 -7.946  19.038  1.00 11.11 ? 474  LEU   B O   1 
ATOM   7858 C  CB  . LEU   B 1 451 ? -68.514 -10.388 20.743  1.00 10.94 ? 474  LEU   B CB  1 
ATOM   7859 C  CG  . LEU   B 1 451 ? -69.553 -10.552 21.859  1.00 11.72 ? 474  LEU   B CG  1 
ATOM   7860 C  CD1 . LEU   B 1 451 ? -69.115 -11.581 22.834  1.00 12.18 ? 474  LEU   B CD1 1 
ATOM   7861 C  CD2 . LEU   B 1 451 ? -69.773 -9.248  22.569  1.00 11.97 ? 474  LEU   B CD2 1 
ATOM   7862 N  N   . ALA   B 1 452 ? -67.312 -9.752  17.706  1.00 10.87 ? 475  ALA   B N   1 
ATOM   7863 C  CA  . ALA   B 1 452 ? -66.289 -9.213  16.811  1.00 10.58 ? 475  ALA   B CA  1 
ATOM   7864 C  C   . ALA   B 1 452 ? -66.864 -8.010  16.067  1.00 11.65 ? 475  ALA   B C   1 
ATOM   7865 O  O   . ALA   B 1 452 ? -66.233 -6.954  16.018  1.00 10.26 ? 475  ALA   B O   1 
ATOM   7866 C  CB  . ALA   B 1 452 ? -65.777 -10.258 15.865  1.00 10.78 ? 475  ALA   B CB  1 
ATOM   7867 N  N   . ASP   B 1 453 ? -68.069 -8.166  15.484  1.00 11.77 ? 476  ASP   B N   1 
ATOM   7868 C  CA  . ASP   B 1 453 ? -68.656 -7.039  14.788  1.00 12.96 ? 476  ASP   B CA  1 
ATOM   7869 C  C   . ASP   B 1 453 ? -68.954 -5.873  15.724  1.00 12.55 ? 476  ASP   B C   1 
ATOM   7870 O  O   . ASP   B 1 453 ? -68.745 -4.715  15.350  1.00 13.01 ? 476  ASP   B O   1 
ATOM   7871 C  CB  . ASP   B 1 453 ? -69.874 -7.479  14.003  1.00 13.86 ? 476  ASP   B CB  1 
ATOM   7872 C  CG  . ASP   B 1 453 ? -69.545 -8.275  12.755  1.00 17.06 ? 476  ASP   B CG  1 
ATOM   7873 O  OD1 . ASP   B 1 453 ? -68.435 -8.126  12.226  1.00 17.72 ? 476  ASP   B OD1 1 
ATOM   7874 O  OD2 . ASP   B 1 453 ? -70.385 -9.092  12.404  1.00 19.54 ? 476  ASP   B OD2 1 
ATOM   7875 N  N   . LYS   B 1 454 ? -69.471 -6.182  16.936  1.00 11.03 ? 477  LYS   B N   1 
ATOM   7876 C  CA  . LYS   B 1 454 ? -69.824 -5.167  17.914  1.00 10.77 ? 477  LYS   B CA  1 
ATOM   7877 C  C   . LYS   B 1 454 ? -68.587 -4.360  18.311  1.00 10.65 ? 477  LYS   B C   1 
ATOM   7878 O  O   . LYS   B 1 454 ? -68.613 -3.137  18.369  1.00 12.11 ? 477  LYS   B O   1 
ATOM   7879 C  CB  . LYS   B 1 454 ? -70.423 -5.803  19.171  1.00 10.92 ? 477  LYS   B CB  1 
ATOM   7880 C  CG  . LYS   B 1 454 ? -70.838 -4.780  20.247  1.00 11.13 ? 477  LYS   B CG  1 
ATOM   7881 C  CD  . LYS   B 1 454 ? -71.064 -5.431  21.608  1.00 13.48 ? 477  LYS   B CD  1 
ATOM   7882 C  CE  . LYS   B 1 454 ? -71.680 -4.515  22.612  1.00 17.00 ? 477  LYS   B CE  1 
ATOM   7883 N  NZ  . LYS   B 1 454 ? -71.371 -5.060  23.947  1.00 17.58 ? 477  LYS   B NZ  1 
ATOM   7884 N  N   . VAL   B 1 455 ? -67.465 -5.030  18.574  1.00 9.50  ? 478  VAL   B N   1 
ATOM   7885 C  CA  . VAL   B 1 455 ? -66.301 -4.284  19.028  1.00 9.61  ? 478  VAL   B CA  1 
ATOM   7886 C  C   . VAL   B 1 455 ? -65.706 -3.479  17.879  1.00 9.58  ? 478  VAL   B C   1 
ATOM   7887 O  O   . VAL   B 1 455 ? -65.287 -2.334  18.109  1.00 10.72 ? 478  VAL   B O   1 
ATOM   7888 C  CB  . VAL   B 1 455 ? -65.319 -5.301  19.635  1.00 9.18  ? 478  VAL   B CB  1 
ATOM   7889 C  CG1 . VAL   B 1 455 ? -63.966 -4.672  19.891  1.00 9.32  ? 478  VAL   B CG1 1 
ATOM   7890 C  CG2 . VAL   B 1 455 ? -65.886 -5.848  20.929  1.00 9.61  ? 478  VAL   B CG2 1 
ATOM   7891 N  N   . LYS   B 1 456 ? -65.728 -4.041  16.663  1.00 9.84  ? 479  LYS   B N   1 
ATOM   7892 C  CA  . LYS   B 1 456 ? -65.179 -3.359  15.503  1.00 11.13 ? 479  LYS   B CA  1 
ATOM   7893 C  C   . LYS   B 1 456 ? -65.992 -2.090  15.256  1.00 12.28 ? 479  LYS   B C   1 
ATOM   7894 O  O   . LYS   B 1 456 ? -65.451 -1.022  14.943  1.00 12.53 ? 479  LYS   B O   1 
ATOM   7895 C  CB  . LYS   B 1 456 ? -65.114 -4.213  14.235  1.00 11.43 ? 479  LYS   B CB  1 
ATOM   7896 C  CG  . LYS   B 1 456 ? -64.400 -3.515  13.113  1.00 12.73 ? 479  LYS   B CG  1 
ATOM   7897 C  CD  . LYS   B 1 456 ? -62.876 -3.619  13.242  1.00 13.52 ? 479  LYS   B CD  1 
ATOM   7898 C  CE  . LYS   B 1 456 ? -62.163 -2.920  12.135  1.00 15.12 ? 479  LYS   B CE  1 
ATOM   7899 N  NZ  . LYS   B 1 456 ? -60.697 -3.036  12.270  1.00 16.28 ? 479  LYS   B NZ  1 
ATOM   7900 N  N   . ALA   B 1 457 ? -67.314 -2.213  15.381  1.00 13.03 ? 480  ALA   B N   1 
ATOM   7901 C  CA  . ALA   B 1 457 ? -68.175 -1.062  15.130  1.00 13.29 ? 480  ALA   B CA  1 
ATOM   7902 C  C   . ALA   B 1 457 ? -67.998 -0.038  16.242  1.00 13.40 ? 480  ALA   B C   1 
ATOM   7903 O  O   . ALA   B 1 457 ? -68.206 1.154   16.013  1.00 15.41 ? 480  ALA   B O   1 
ATOM   7904 C  CB  . ALA   B 1 457 ? -69.599 -1.497  14.990  1.00 12.96 ? 480  ALA   B CB  1 
ATOM   7905 N  N   . TYR   B 1 458 ? -67.647 -0.497  17.449  1.00 11.66 ? 481  TYR   B N   1 
ATOM   7906 C  CA  . TYR   B 1 458 ? -67.493 0.389   18.586  1.00 11.65 ? 481  TYR   B CA  1 
ATOM   7907 C  C   . TYR   B 1 458 ? -66.146 1.124   18.536  1.00 11.79 ? 481  TYR   B C   1 
ATOM   7908 O  O   . TYR   B 1 458 ? -65.996 2.166   19.159  1.00 14.58 ? 481  TYR   B O   1 
ATOM   7909 C  CB  . TYR   B 1 458 ? -67.592 -0.368  19.915  1.00 13.32 ? 481  TYR   B CB  1 
ATOM   7910 C  CG  . TYR   B 1 458 ? -68.095 0.433   21.106  1.00 13.39 ? 481  TYR   B CG  1 
ATOM   7911 C  CD1 . TYR   B 1 458 ? -69.190 1.285   20.974  1.00 13.86 ? 481  TYR   B CD1 1 
ATOM   7912 C  CD2 . TYR   B 1 458 ? -67.434 0.428   22.325  1.00 13.31 ? 481  TYR   B CD2 1 
ATOM   7913 C  CE1 . TYR   B 1 458 ? -69.641 2.035   22.038  1.00 14.90 ? 481  TYR   B CE1 1 
ATOM   7914 C  CE2 . TYR   B 1 458 ? -67.867 1.186   23.402  1.00 13.87 ? 481  TYR   B CE2 1 
ATOM   7915 C  CZ  . TYR   B 1 458 ? -68.992 1.991   23.257  1.00 15.22 ? 481  TYR   B CZ  1 
ATOM   7916 O  OH  . TYR   B 1 458 ? -69.443 2.759   24.304  1.00 16.23 ? 481  TYR   B OH  1 
ATOM   7917 N  N   . ASP   B 1 459 ? -65.117 0.486   17.958  1.00 12.36 ? 482  ASP   B N   1 
ATOM   7918 C  CA  . ASP   B 1 459 ? -63.775 1.073   17.878  1.00 12.55 ? 482  ASP   B CA  1 
ATOM   7919 C  C   . ASP   B 1 459 ? -63.152 0.688   16.548  1.00 13.04 ? 482  ASP   B C   1 
ATOM   7920 O  O   . ASP   B 1 459 ? -62.250 -0.137  16.507  1.00 12.04 ? 482  ASP   B O   1 
ATOM   7921 C  CB  . ASP   B 1 459 ? -62.945 0.651   19.075  1.00 12.04 ? 482  ASP   B CB  1 
ATOM   7922 C  CG  . ASP   B 1 459 ? -61.585 1.344   19.192  1.00 12.45 ? 482  ASP   B CG  1 
ATOM   7923 O  OD1 . ASP   B 1 459 ? -61.408 2.377   18.511  1.00 11.99 ? 482  ASP   B OD1 1 
ATOM   7924 O  OD2 . ASP   B 1 459 ? -60.755 0.878   19.997  1.00 12.44 ? 482  ASP   B OD2 1 
ATOM   7925 N  N   . PRO   B 1 460 ? -63.632 1.221   15.393  1.00 14.44 ? 483  PRO   B N   1 
ATOM   7926 C  CA  . PRO   B 1 460 ? -63.179 0.739   14.090  1.00 13.23 ? 483  PRO   B CA  1 
ATOM   7927 C  C   . PRO   B 1 460 ? -61.732 1.080   13.735  1.00 13.48 ? 483  PRO   B C   1 
ATOM   7928 O  O   . PRO   B 1 460 ? -61.211 0.495   12.768  1.00 13.27 ? 483  PRO   B O   1 
ATOM   7929 C  CB  . PRO   B 1 460 ? -64.124 1.361   13.102  1.00 13.68 ? 483  PRO   B CB  1 
ATOM   7930 C  CG  . PRO   B 1 460 ? -64.602 2.582   13.798  1.00 14.57 ? 483  PRO   B CG  1 
ATOM   7931 C  CD  . PRO   B 1 460 ? -64.678 2.246   15.279  1.00 14.91 ? 483  PRO   B CD  1 
ATOM   7932 N  N   . THR   B 1 461 ? -61.109 1.992   14.507  1.00 13.27 ? 484  THR   B N   1 
ATOM   7933 C  CA  . THR   B 1 461 ? -59.730 2.346   14.173  1.00 13.05 ? 484  THR   B CA  1 
ATOM   7934 C  C   . THR   B 1 461 ? -58.737 1.406   14.850  1.00 12.80 ? 484  THR   B C   1 
ATOM   7935 O  O   . THR   B 1 461 ? -57.539 1.629   14.731  1.00 12.47 ? 484  THR   B O   1 
ATOM   7936 C  CB  . THR   B 1 461 ? -59.404 3.813   14.430  1.00 15.10 ? 484  THR   B CB  1 
ATOM   7937 O  OG1 . THR   B 1 461 ? -59.466 3.977   15.845  1.00 15.04 ? 484  THR   B OG1 1 
ATOM   7938 C  CG2 . THR   B 1 461 ? -60.328 4.711   13.624  1.00 16.38 ? 484  THR   B CG2 1 
ATOM   7939 N  N   . ARG   B 1 462 ? -59.231 0.350   15.526  1.00 11.31 ? 485  ARG   B N   1 
ATOM   7940 C  CA  . ARG   B 1 462 ? -58.377 -0.709  16.037  1.00 11.30 ? 485  ARG   B CA  1 
ATOM   7941 C  C   . ARG   B 1 462 ? -58.694 -2.018  15.325  1.00 11.23 ? 485  ARG   B C   1 
ATOM   7942 O  O   . ARG   B 1 462 ? -59.764 -2.155  14.727  1.00 13.74 ? 485  ARG   B O   1 
ATOM   7943 C  CB  . ARG   B 1 462 ? -58.559 -0.975  17.538  1.00 12.70 ? 485  ARG   B CB  1 
ATOM   7944 C  CG  . ARG   B 1 462 ? -57.743 -0.160  18.527  1.00 14.04 ? 485  ARG   B CG  1 
ATOM   7945 C  CD  . ARG   B 1 462 ? -57.561 1.270   18.121  1.00 15.95 ? 485  ARG   B CD  1 
ATOM   7946 N  NE  . ARG   B 1 462 ? -56.808 1.901   19.220  1.00 15.89 ? 485  ARG   B NE  1 
ATOM   7947 C  CZ  . ARG   B 1 462 ? -57.231 2.396   20.350  1.00 16.04 ? 485  ARG   B CZ  1 
ATOM   7948 N  NH1 . ARG   B 1 462 ? -58.503 2.282   20.691  1.00 16.18 ? 485  ARG   B NH1 1 
ATOM   7949 N  NH2 . ARG   B 1 462 ? -56.366 3.060   21.132  1.00 14.79 ? 485  ARG   B NH2 1 
ATOM   7950 N  N   . LEU   B 1 463 ? -57.790 -2.987  15.460  1.00 10.48 ? 486  LEU   B N   1 
ATOM   7951 C  CA  . LEU   B 1 463 ? -58.033 -4.346  14.970  1.00 10.40 ? 486  LEU   B CA  1 
ATOM   7952 C  C   . LEU   B 1 463 ? -58.838 -5.113  16.017  1.00 10.46 ? 486  LEU   B C   1 
ATOM   7953 O  O   . LEU   B 1 463 ? -58.766 -4.835  17.206  1.00 9.81  ? 486  LEU   B O   1 
ATOM   7954 C  CB  . LEU   B 1 463 ? -56.743 -5.091  14.621  1.00 10.71 ? 486  LEU   B CB  1 
ATOM   7955 C  CG  . LEU   B 1 463 ? -55.860 -4.399  13.575  1.00 12.09 ? 486  LEU   B CG  1 
ATOM   7956 C  CD1 . LEU   B 1 463 ? -54.577 -5.170  13.402  1.00 12.52 ? 486  LEU   B CD1 1 
ATOM   7957 C  CD2 . LEU   B 1 463 ? -56.569 -4.314  12.249  1.00 12.63 ? 486  LEU   B CD2 1 
ATOM   7958 N  N   . VAL   B 1 464 ? -59.591 -6.114  15.559  1.00 9.95  ? 487  VAL   B N   1 
ATOM   7959 C  CA  . VAL   B 1 464 ? -60.335 -6.948  16.488  1.00 11.63 ? 487  VAL   B CA  1 
ATOM   7960 C  C   . VAL   B 1 464 ? -60.064 -8.413  16.157  1.00 10.25 ? 487  VAL   B C   1 
ATOM   7961 O  O   . VAL   B 1 464 ? -60.113 -8.837  14.998  1.00 10.72 ? 487  VAL   B O   1 
ATOM   7962 C  CB  . VAL   B 1 464 ? -61.853 -6.686  16.452  1.00 12.97 ? 487  VAL   B CB  1 
ATOM   7963 C  CG1 . VAL   B 1 464 ? -62.628 -7.565  17.423  1.00 13.87 ? 487  VAL   B CG1 1 
ATOM   7964 C  CG2 . VAL   B 1 464 ? -62.158 -5.220  16.721  1.00 14.20 ? 487  VAL   B CG2 1 
ATOM   7965 N  N   . ASP   B 1 465 ? -59.882 -9.167  17.228  1.00 9.72  ? 488  ASP   B N   1 
ATOM   7966 C  CA  . ASP   B 1 465 ? -59.666 -10.603 17.178  1.00 9.24  ? 488  ASP   B CA  1 
ATOM   7967 C  C   . ASP   B 1 465 ? -60.840 -11.279 17.887  1.00 9.66  ? 488  ASP   B C   1 
ATOM   7968 O  O   . ASP   B 1 465 ? -60.984 -11.166 19.116  1.00 9.35  ? 488  ASP   B O   1 
ATOM   7969 C  CB  . ASP   B 1 465 ? -58.320 -10.878 17.826  1.00 9.93  ? 488  ASP   B CB  1 
ATOM   7970 C  CG  . ASP   B 1 465 ? -57.817 -12.308 17.930  1.00 9.72  ? 488  ASP   B CG  1 
ATOM   7971 O  OD1 . ASP   B 1 465 ? -58.613 -13.235 17.632  1.00 8.85  ? 488  ASP   B OD1 1 
ATOM   7972 O  OD2 . ASP   B 1 465 ? -56.591 -12.446 18.293  1.00 9.64  ? 488  ASP   B OD2 1 
ATOM   7973 N  N   . ASN   B 1 466 ? -61.635 -12.049 17.128  1.00 9.62  ? 489  ASN   B N   1 
ATOM   7974 C  CA  . ASN   B 1 466 ? -62.859 -12.592 17.693  1.00 10.52 ? 489  ASN   B CA  1 
ATOM   7975 C  C   . ASN   B 1 466 ? -62.569 -13.653 18.749  1.00 10.41 ? 489  ASN   B C   1 
ATOM   7976 O  O   . ASN   B 1 466 ? -63.352 -13.809 19.675  1.00 10.85 ? 489  ASN   B O   1 
ATOM   7977 C  CB  . ASN   B 1 466 ? -63.793 -13.137 16.618  1.00 9.92  ? 489  ASN   B CB  1 
ATOM   7978 C  CG  . ASN   B 1 466 ? -63.532 -14.588 16.259  1.00 11.05 ? 489  ASN   B CG  1 
ATOM   7979 O  OD1 . ASN   B 1 466 ? -64.303 -15.459 16.683  1.00 10.61 ? 489  ASN   B OD1 1 
ATOM   7980 N  ND2 . ASN   B 1 466 ? -62.523 -14.867 15.437  1.00 10.86 ? 489  ASN   B ND2 1 
ATOM   7981 N  N   . MET   B 1 467 ? -61.490 -14.424 18.561  1.00 9.95  ? 490  MET   B N   1 
ATOM   7982 C  CA  . MET   B 1 467 ? -61.199 -15.556 19.417  1.00 9.47  ? 490  MET   B CA  1 
ATOM   7983 C  C   . MET   B 1 467 ? -59.732 -15.939 19.246  1.00 9.77  ? 490  MET   B C   1 
ATOM   7984 O  O   . MET   B 1 467 ? -59.323 -16.244 18.142  1.00 9.55  ? 490  MET   B O   1 
ATOM   7985 C  CB  . MET   B 1 467 ? -62.097 -16.734 19.030  1.00 9.43  ? 490  MET   B CB  1 
ATOM   7986 C  CG  . MET   B 1 467 ? -61.895 -17.983 19.846  1.00 9.77  ? 490  MET   B CG  1 
ATOM   7987 S  SD  . MET   B 1 467 ? -62.214 -17.735 21.598  1.00 10.24 ? 490  MET   B SD  1 
ATOM   7988 C  CE  . MET   B 1 467 ? -64.015 -17.571 21.496  1.00 10.35 ? 490  MET   B CE  1 
ATOM   7989 N  N   . SER   B 1 468 ? -58.962 -15.898 20.337  1.00 9.91  ? 491  SER   B N   1 
ATOM   7990 C  CA  . SER   B 1 468 ? -57.553 -16.235 20.276  1.00 10.07 ? 491  SER   B CA  1 
ATOM   7991 C  C   . SER   B 1 468 ? -57.431 -17.741 20.475  1.00 10.12 ? 491  SER   B C   1 
ATOM   7992 O  O   . SER   B 1 468 ? -57.923 -18.273 21.479  1.00 10.34 ? 491  SER   B O   1 
ATOM   7993 C  CB  . SER   B 1 468 ? -56.777 -15.465 21.331  1.00 9.49  ? 491  SER   B CB  1 
ATOM   7994 O  OG  . SER   B 1 468 ? -55.395 -15.374 21.016  1.00 9.31  ? 491  SER   B OG  1 
ATOM   7995 N  N   . GLY   B 1 469 ? -56.830 -18.447 19.516  1.00 10.48 ? 492  GLY   B N   1 
ATOM   7996 C  CA  . GLY   B 1 469 ? -56.643 -19.886 19.665  1.00 10.22 ? 492  GLY   B CA  1 
ATOM   7997 C  C   . GLY   B 1 469 ? -57.793 -20.714 19.066  1.00 11.87 ? 492  GLY   B C   1 
ATOM   7998 O  O   . GLY   B 1 469 ? -58.202 -21.717 19.681  1.00 13.48 ? 492  GLY   B O   1 
ATOM   7999 N  N   . VAL   B 1 470 ? -58.261 -20.336 17.865  1.00 12.05 ? 493  VAL   B N   1 
ATOM   8000 C  CA  . VAL   B 1 470 ? -59.390 -20.987 17.212  1.00 12.51 ? 493  VAL   B CA  1 
ATOM   8001 C  C   . VAL   B 1 470 ? -59.059 -22.411 16.765  1.00 14.37 ? 493  VAL   B C   1 
ATOM   8002 O  O   . VAL   B 1 470 ? -59.971 -23.153 16.395  1.00 14.43 ? 493  VAL   B O   1 
ATOM   8003 C  CB  . VAL   B 1 470 ? -59.947 -20.189 16.019  1.00 11.94 ? 493  VAL   B CB  1 
ATOM   8004 C  CG1 . VAL   B 1 470 ? -60.566 -18.893 16.516  1.00 12.09 ? 493  VAL   B CG1 1 
ATOM   8005 C  CG2 . VAL   B 1 470 ? -58.930 -19.982 14.903  1.00 11.96 ? 493  VAL   B CG2 1 
ATOM   8006 N  N   . ASN   B 1 471 ? -57.792 -22.821 16.857  1.00 16.13 ? 494  ASN   B N   1 
ATOM   8007 C  CA  . ASN   B 1 471 ? -57.359 -24.178 16.534  1.00 16.15 ? 494  ASN   B CA  1 
ATOM   8008 C  C   . ASN   B 1 471 ? -57.328 -25.076 17.782  1.00 17.39 ? 494  ASN   B C   1 
ATOM   8009 O  O   . ASN   B 1 471 ? -57.049 -26.266 17.659  1.00 20.61 ? 494  ASN   B O   1 
ATOM   8010 C  CB  . ASN   B 1 471 ? -55.981 -24.074 15.873  1.00 15.68 ? 494  ASN   B CB  1 
ATOM   8011 C  CG  . ASN   B 1 471 ? -54.947 -23.519 16.832  1.00 14.59 ? 494  ASN   B CG  1 
ATOM   8012 O  OD1 . ASN   B 1 471 ? -55.150 -22.461 17.453  1.00 13.15 ? 494  ASN   B OD1 1 
ATOM   8013 N  ND2 . ASN   B 1 471 ? -53.851 -24.238 17.014  1.00 14.00 ? 494  ASN   B ND2 1 
ATOM   8014 N  N   . CYS   B 1 472 ? -57.584 -24.507 18.969  1.00 18.84 ? 495  CYS   B N   1 
ATOM   8015 C  CA  . CYS   B 1 472 ? -57.327 -25.092 20.286  1.00 21.90 ? 495  CYS   B CA  1 
ATOM   8016 C  C   . CYS   B 1 472 ? -58.658 -25.700 20.748  1.00 20.54 ? 495  CYS   B C   1 
ATOM   8017 O  O   . CYS   B 1 472 ? -59.698 -24.996 20.623  1.00 18.37 ? 495  CYS   B O   1 
ATOM   8018 C  CB  . CYS   B 1 472 ? -56.790 -24.081 21.335  1.00 23.52 ? 495  CYS   B CB  1 
ATOM   8019 S  SG  . CYS   B 1 472 ? -56.842 -24.573 23.096  1.00 32.87 ? 495  CYS   B SG  1 
ATOM   8020 N  N   . CYS   B 1 473 ? -58.466 -26.783 21.817  1.00 25.54 ? 496  CYS   B N   1 
ATOM   8021 C  CA  . CYS   B 1 473 ? -59.495 -27.152 22.828  1.00 28.61 ? 496  CYS   B CA  1 
ATOM   8022 C  C   . CYS   B 1 473 ? -60.891 -27.006 22.222  1.00 25.54 ? 496  CYS   B C   1 
ATOM   8023 O  O   . CYS   B 1 473 ? -61.209 -27.661 21.222  1.00 26.01 ? 496  CYS   B O   1 
ATOM   8024 C  CB  . CYS   B 1 473 ? -59.246 -26.339 24.087  1.00 35.39 ? 496  CYS   B CB  1 
ATOM   8025 S  SG  . CYS   B 1 473 ? -58.790 -24.619 23.739  1.00 40.00 ? 496  CYS   B SG  1 
ATOM   8026 N  N   . GLY   B 1 474 ? -61.735 -26.159 22.820  1.00 20.16 ? 497  GLY   B N   1 
ATOM   8027 C  CA  . GLY   B 1 474 ? -63.110 -26.099 22.356  1.00 19.56 ? 497  GLY   B CA  1 
ATOM   8028 C  C   . GLY   B 1 474 ? -63.480 -24.724 21.803  1.00 17.67 ? 497  GLY   B C   1 
ATOM   8029 O  O   . GLY   B 1 474 ? -64.649 -24.359 21.804  1.00 15.20 ? 497  GLY   B O   1 
ATOM   8030 N  N   . ALA   B 1 475 ? -62.478 -23.988 21.304  1.00 15.23 ? 498  ALA   B N   1 
ATOM   8031 C  CA  . ALA   B 1 475 ? -62.695 -22.621 20.878  1.00 14.74 ? 498  ALA   B CA  1 
ATOM   8032 C  C   . ALA   B 1 475 ? -63.510 -22.640 19.596  1.00 15.13 ? 498  ALA   B C   1 
ATOM   8033 O  O   . ALA   B 1 475 ? -63.261 -23.465 18.724  1.00 16.43 ? 498  ALA   B O   1 
ATOM   8034 C  CB  . ALA   B 1 475 ? -61.378 -21.912 20.695  1.00 14.14 ? 498  ALA   B CB  1 
ATOM   8035 N  N   . VAL   B 1 476 ? -64.455 -21.702 19.491  1.00 13.32 ? 499  VAL   B N   1 
ATOM   8036 C  CA  . VAL   B 1 476 ? -65.280 -21.543 18.324  1.00 14.74 ? 499  VAL   B CA  1 
ATOM   8037 C  C   . VAL   B 1 476 ? -64.869 -20.259 17.633  1.00 14.46 ? 499  VAL   B C   1 
ATOM   8038 O  O   . VAL   B 1 476 ? -64.795 -19.209 18.268  1.00 14.97 ? 499  VAL   B O   1 
ATOM   8039 C  CB  . VAL   B 1 476 ? -66.766 -21.507 18.686  1.00 17.06 ? 499  VAL   B CB  1 
ATOM   8040 C  CG1 . VAL   B 1 476 ? -67.599 -21.111 17.475  1.00 17.09 ? 499  VAL   B CG1 1 
ATOM   8041 C  CG2 . VAL   B 1 476 ? -67.184 -22.850 19.266  1.00 17.14 ? 499  VAL   B CG2 1 
ATOM   8042 N  N   . ASP   B 1 477 ? -64.582 -20.379 16.341  1.00 12.33 ? 500  ASP   B N   1 
ATOM   8043 C  CA  . ASP   B 1 477 ? -64.240 -19.228 15.524  1.00 11.73 ? 500  ASP   B CA  1 
ATOM   8044 C  C   . ASP   B 1 477 ? -65.546 -18.633 15.012  1.00 11.49 ? 500  ASP   B C   1 
ATOM   8045 O  O   . ASP   B 1 477 ? -66.355 -19.308 14.352  1.00 11.90 ? 500  ASP   B O   1 
ATOM   8046 C  CB  . ASP   B 1 477 ? -63.361 -19.680 14.373  1.00 12.33 ? 500  ASP   B CB  1 
ATOM   8047 C  CG  . ASP   B 1 477 ? -62.796 -18.589 13.477  1.00 12.27 ? 500  ASP   B CG  1 
ATOM   8048 O  OD1 . ASP   B 1 477 ? -63.005 -17.402 13.773  1.00 10.19 ? 500  ASP   B OD1 1 
ATOM   8049 O  OD2 . ASP   B 1 477 ? -62.179 -18.939 12.456  1.00 15.65 ? 500  ASP   B OD2 1 
ATOM   8050 N  N   . GLY   B 1 478 ? -65.766 -17.361 15.304  1.00 11.04 ? 501  GLY   B N   1 
ATOM   8051 C  CA  . GLY   B 1 478 ? -66.862 -16.610 14.725  1.00 11.54 ? 501  GLY   B CA  1 
ATOM   8052 C  C   . GLY   B 1 478 ? -66.736 -16.486 13.208  1.00 13.14 ? 501  GLY   B C   1 
ATOM   8053 O  O   . GLY   B 1 478 ? -67.737 -16.237 12.544  1.00 13.36 ? 501  GLY   B O   1 
ATOM   8054 N  N   . GLY   B 1 479 ? -65.491 -16.547 12.706  1.00 12.98 ? 502  GLY   B N   1 
ATOM   8055 C  CA  . GLY   B 1 479 ? -65.194 -16.501 11.280  1.00 12.86 ? 502  GLY   B CA  1 
ATOM   8056 C  C   . GLY   B 1 479 ? -64.939 -15.091 10.749  1.00 12.91 ? 502  GLY   B C   1 
ATOM   8057 O  O   . GLY   B 1 479 ? -64.551 -14.910 9.590   1.00 13.94 ? 502  GLY   B O   1 
ATOM   8058 N  N   . ASN   B 1 480 ? -65.155 -14.082 11.602  1.00 11.42 ? 503  ASN   B N   1 
ATOM   8059 C  CA  . ASN   B 1 480 ? -65.045 -12.686 11.226  1.00 11.25 ? 503  ASN   B CA  1 
ATOM   8060 C  C   . ASN   B 1 480 ? -63.987 -12.027 12.107  1.00 10.82 ? 503  ASN   B C   1 
ATOM   8061 O  O   . ASN   B 1 480 ? -63.069 -12.704 12.586  1.00 11.58 ? 503  ASN   B O   1 
ATOM   8062 C  CB  . ASN   B 1 480 ? -66.423 -12.049 11.312  1.00 12.07 ? 503  ASN   B CB  1 
ATOM   8063 C  CG  . ASN   B 1 480 ? -66.979 -12.018 12.721  1.00 11.92 ? 503  ASN   B CG  1 
ATOM   8064 O  OD1 . ASN   B 1 480 ? -66.543 -12.758 13.612  1.00 11.25 ? 503  ASN   B OD1 1 
ATOM   8065 N  ND2 . ASN   B 1 480 ? -67.983 -11.185 12.926  1.00 13.08 ? 503  ASN   B ND2 1 
ATOM   8066 N  N   . GLY   B 1 481 ? -64.098 -10.711 12.284  1.00 11.68 ? 504  GLY   B N   1 
ATOM   8067 C  CA  . GLY   B 1 481 ? -62.999 -9.927  12.821  1.00 11.52 ? 504  GLY   B CA  1 
ATOM   8068 C  C   . GLY   B 1 481 ? -61.868 -9.852  11.806  1.00 11.02 ? 504  GLY   B C   1 
ATOM   8069 O  O   . GLY   B 1 481 ? -62.039 -10.210 10.631  1.00 10.75 ? 504  GLY   B O   1 
ATOM   8070 N  N   . ASP   B 1 482 ? -60.720 -9.359  12.278  1.00 10.38 ? 505  ASP   B N   1 
ATOM   8071 C  CA  . ASP   B 1 482 ? -59.631 -8.974  11.404  1.00 10.40 ? 505  ASP   B CA  1 
ATOM   8072 C  C   . ASP   B 1 482 ? -58.578 -10.066 11.321  1.00 9.78  ? 505  ASP   B C   1 
ATOM   8073 O  O   . ASP   B 1 482 ? -57.746 -10.006 10.425  1.00 11.31 ? 505  ASP   B O   1 
ATOM   8074 C  CB  . ASP   B 1 482 ? -58.999 -7.675  11.879  1.00 11.02 ? 505  ASP   B CB  1 
ATOM   8075 C  CG  . ASP   B 1 482 ? -59.940 -6.484  11.793  1.00 13.11 ? 505  ASP   B CG  1 
ATOM   8076 O  OD1 . ASP   B 1 482 ? -60.591 -6.365  10.734  1.00 14.82 ? 505  ASP   B OD1 1 
ATOM   8077 O  OD2 . ASP   B 1 482 ? -60.054 -5.702  12.775  1.00 13.43 ? 505  ASP   B OD2 1 
ATOM   8078 N  N   . VAL   B 1 483 ? -58.543 -10.978 12.293  1.00 8.95  ? 506  VAL   B N   1 
ATOM   8079 C  CA  . VAL   B 1 483 ? -57.447 -11.940 12.339  1.00 9.05  ? 506  VAL   B CA  1 
ATOM   8080 C  C   . VAL   B 1 483 ? -57.933 -13.354 12.647  1.00 10.11 ? 506  VAL   B C   1 
ATOM   8081 O  O   . VAL   B 1 483 ? -58.894 -13.559 13.391  1.00 11.13 ? 506  VAL   B O   1 
ATOM   8082 C  CB  . VAL   B 1 483 ? -56.324 -11.546 13.325  1.00 9.81  ? 506  VAL   B CB  1 
ATOM   8083 C  CG1 . VAL   B 1 483 ? -55.689 -10.220 12.930  1.00 10.31 ? 506  VAL   B CG1 1 
ATOM   8084 C  CG2 . VAL   B 1 483 ? -56.856 -11.541 14.753  1.00 10.16 ? 506  VAL   B CG2 1 
ATOM   8085 N  N   . VAL   B 1 484 ? -57.262 -14.316 12.007  1.00 10.19 ? 507  VAL   B N   1 
ATOM   8086 C  CA  . VAL   B 1 484 ? -57.383 -15.722 12.328  1.00 11.33 ? 507  VAL   B CA  1 
ATOM   8087 C  C   . VAL   B 1 484 ? -56.183 -16.030 13.220  1.00 10.79 ? 507  VAL   B C   1 
ATOM   8088 O  O   . VAL   B 1 484 ? -55.029 -15.781 12.856  1.00 12.30 ? 507  VAL   B O   1 
ATOM   8089 C  CB  . VAL   B 1 484 ? -57.488 -16.647 11.095  1.00 12.72 ? 507  VAL   B CB  1 
ATOM   8090 C  CG1 . VAL   B 1 484 ? -56.372 -16.466 10.074  1.00 14.67 ? 507  VAL   B CG1 1 
ATOM   8091 C  CG2 . VAL   B 1 484 ? -57.553 -18.105 11.549  1.00 12.99 ? 507  VAL   B CG2 1 
ATOM   8092 N  N   . ASP   B 1 485 ? -56.480 -16.457 14.439  1.00 10.51 ? 508  ASP   B N   1 
ATOM   8093 C  CA  . ASP   B 1 485 ? -55.494 -16.490 15.519  1.00 10.59 ? 508  ASP   B CA  1 
ATOM   8094 C  C   . ASP   B 1 485 ? -55.385 -17.911 16.067  1.00 10.03 ? 508  ASP   B C   1 
ATOM   8095 O  O   . ASP   B 1 485 ? -56.334 -18.433 16.649  1.00 9.26  ? 508  ASP   B O   1 
ATOM   8096 C  CB  . ASP   B 1 485 ? -55.884 -15.482 16.596  1.00 10.26 ? 508  ASP   B CB  1 
ATOM   8097 C  CG  . ASP   B 1 485 ? -55.108 -15.497 17.900  1.00 11.23 ? 508  ASP   B CG  1 
ATOM   8098 O  OD1 . ASP   B 1 485 ? -54.417 -16.488 18.138  1.00 10.21 ? 508  ASP   B OD1 1 
ATOM   8099 O  OD2 . ASP   B 1 485 ? -55.275 -14.533 18.722  1.00 11.99 ? 508  ASP   B OD2 1 
ATOM   8100 N  N   . HIS   B 1 486 ? -54.205 -18.511 15.879  1.00 10.37 ? 509  HIS   B N   1 
ATOM   8101 C  CA  . HIS   B 1 486 ? -53.935 -19.832 16.403  1.00 11.14 ? 509  HIS   B CA  1 
ATOM   8102 C  C   . HIS   B 1 486 ? -53.006 -19.746 17.606  1.00 10.93 ? 509  HIS   B C   1 
ATOM   8103 O  O   . HIS   B 1 486 ? -52.209 -18.822 17.719  1.00 10.40 ? 509  HIS   B O   1 
ATOM   8104 C  CB  . HIS   B 1 486 ? -53.286 -20.745 15.372  1.00 11.97 ? 509  HIS   B CB  1 
ATOM   8105 C  CG  . HIS   B 1 486 ? -54.163 -21.051 14.216  1.00 12.45 ? 509  HIS   B CG  1 
ATOM   8106 N  ND1 . HIS   B 1 486 ? -53.727 -21.847 13.177  1.00 13.51 ? 509  HIS   B ND1 1 
ATOM   8107 C  CD2 . HIS   B 1 486 ? -55.450 -20.787 13.983  1.00 13.26 ? 509  HIS   B CD2 1 
ATOM   8108 C  CE1 . HIS   B 1 486 ? -54.702 -21.938 12.287  1.00 13.56 ? 509  HIS   B CE1 1 
ATOM   8109 N  NE2 . HIS   B 1 486 ? -55.774 -21.319 12.751  1.00 13.62 ? 509  HIS   B NE2 1 
ATOM   8110 N  N   . HIS   B 1 487 ? -53.141 -20.728 18.488  1.00 11.18 ? 510  HIS   B N   1 
ATOM   8111 C  CA  . HIS   B 1 487 ? -52.186 -20.978 19.552  1.00 10.29 ? 510  HIS   B CA  1 
ATOM   8112 C  C   . HIS   B 1 487 ? -51.520 -22.303 19.200  1.00 11.01 ? 510  HIS   B C   1 
ATOM   8113 O  O   . HIS   B 1 487 ? -52.193 -23.329 19.134  1.00 10.50 ? 510  HIS   B O   1 
ATOM   8114 C  CB  . HIS   B 1 487 ? -52.869 -21.082 20.923  1.00 10.03 ? 510  HIS   B CB  1 
ATOM   8115 C  CG  . HIS   B 1 487 ? -53.522 -19.827 21.384  1.00 9.54  ? 510  HIS   B CG  1 
ATOM   8116 N  ND1 . HIS   B 1 487 ? -54.231 -19.733 22.552  1.00 9.03  ? 510  HIS   B ND1 1 
ATOM   8117 C  CD2 . HIS   B 1 487 ? -53.565 -18.623 20.834  1.00 9.78  ? 510  HIS   B CD2 1 
ATOM   8118 C  CE1 . HIS   B 1 487 ? -54.621 -18.495 22.697  1.00 9.81  ? 510  HIS   B CE1 1 
ATOM   8119 N  NE2 . HIS   B 1 487 ? -54.275 -17.800 21.639  1.00 8.41  ? 510  HIS   B NE2 1 
ATOM   8120 N  N   . VAL   B 1 488 ? -50.203 -22.281 19.013  1.00 10.66 ? 511  VAL   B N   1 
ATOM   8121 C  CA  . VAL   B 1 488 ? -49.485 -23.497 18.665  1.00 11.64 ? 511  VAL   B CA  1 
ATOM   8122 C  C   . VAL   B 1 488 ? -48.263 -23.649 19.550  1.00 11.10 ? 511  VAL   B C   1 
ATOM   8123 O  O   . VAL   B 1 488 ? -47.344 -22.835 19.527  1.00 10.60 ? 511  VAL   B O   1 
ATOM   8124 C  CB  . VAL   B 1 488 ? -49.069 -23.521 17.196  1.00 11.98 ? 511  VAL   B CB  1 
ATOM   8125 C  CG1 . VAL   B 1 488 ? -48.470 -24.901 16.863  1.00 12.19 ? 511  VAL   B CG1 1 
ATOM   8126 C  CG2 . VAL   B 1 488 ? -50.218 -23.160 16.275  1.00 12.53 ? 511  VAL   B CG2 1 
ATOM   8127 N  N   . TYR   B 1 489 ? -48.201 -24.747 20.290  1.00 11.76 ? 512  TYR   B N   1 
ATOM   8128 C  CA  . TYR   B 1 489 ? -47.067 -24.954 21.178  1.00 12.61 ? 512  TYR   B CA  1 
ATOM   8129 C  C   . TYR   B 1 489 ? -46.383 -26.255 20.770  1.00 15.07 ? 512  TYR   B C   1 
ATOM   8130 O  O   . TYR   B 1 489 ? -47.061 -27.276 20.608  1.00 17.09 ? 512  TYR   B O   1 
ATOM   8131 C  CB  . TYR   B 1 489 ? -47.508 -25.045 22.628  1.00 13.13 ? 512  TYR   B CB  1 
ATOM   8132 C  CG  . TYR   B 1 489 ? -47.919 -23.742 23.278  1.00 12.04 ? 512  TYR   B CG  1 
ATOM   8133 C  CD1 . TYR   B 1 489 ? -46.955 -22.871 23.780  1.00 12.23 ? 512  TYR   B CD1 1 
ATOM   8134 C  CD2 . TYR   B 1 489 ? -49.247 -23.364 23.362  1.00 11.49 ? 512  TYR   B CD2 1 
ATOM   8135 C  CE1 . TYR   B 1 489 ? -47.309 -21.662 24.377  1.00 12.49 ? 512  TYR   B CE1 1 
ATOM   8136 C  CE2 . TYR   B 1 489 ? -49.612 -22.167 23.951  1.00 11.33 ? 512  TYR   B CE2 1 
ATOM   8137 C  CZ  . TYR   B 1 489 ? -48.644 -21.322 24.483  1.00 11.55 ? 512  TYR   B CZ  1 
ATOM   8138 O  OH  . TYR   B 1 489 ? -48.951 -20.141 25.094  1.00 10.54 ? 512  TYR   B OH  1 
ATOM   8139 N  N   . VAL   B 1 490 ? -45.063 -26.221 20.553  1.00 14.48 ? 513  VAL   B N   1 
ATOM   8140 C  CA  . VAL   B 1 490 ? -44.196 -25.063 20.780  1.00 13.76 ? 513  VAL   B CA  1 
ATOM   8141 C  C   . VAL   B 1 490 ? -44.280 -24.108 19.585  1.00 12.70 ? 513  VAL   B C   1 
ATOM   8142 O  O   . VAL   B 1 490 ? -43.990 -22.917 19.696  1.00 14.19 ? 513  VAL   B O   1 
ATOM   8143 C  CB  . VAL   B 1 490 ? -42.769 -25.621 21.021  1.00 15.01 ? 513  VAL   B CB  1 
ATOM   8144 C  CG1 . VAL   B 1 490 ? -41.700 -24.563 20.955  1.00 17.10 ? 513  VAL   B CG1 1 
ATOM   8145 C  CG2 . VAL   B 1 490 ? -42.644 -26.329 22.349  1.00 15.60 ? 513  VAL   B CG2 1 
ATOM   8146 N  N   . GLY   B 1 491 ? -44.668 -24.622 18.423  1.00 12.45 ? 514  GLY   B N   1 
ATOM   8147 C  CA  . GLY   B 1 491 ? -44.867 -23.790 17.259  1.00 13.27 ? 514  GLY   B CA  1 
ATOM   8148 C  C   . GLY   B 1 491 ? -43.755 -23.944 16.224  1.00 14.98 ? 514  GLY   B C   1 
ATOM   8149 O  O   . GLY   B 1 491 ? -42.882 -24.798 16.368  1.00 14.63 ? 514  GLY   B O   1 
ATOM   8150 N  N   . PRO   B 1 492 ? -43.732 -23.126 15.140  1.00 15.86 ? 515  PRO   B N   1 
ATOM   8151 C  CA  . PRO   B 1 492 ? -44.648 -21.999 14.972  1.00 15.64 ? 515  PRO   B CA  1 
ATOM   8152 C  C   . PRO   B 1 492 ? -46.011 -22.287 14.342  1.00 15.68 ? 515  PRO   B C   1 
ATOM   8153 O  O   . PRO   B 1 492 ? -46.820 -21.391 14.202  1.00 15.68 ? 515  PRO   B O   1 
ATOM   8154 C  CB  . PRO   B 1 492 ? -43.819 -21.050 14.061  1.00 16.82 ? 515  PRO   B CB  1 
ATOM   8155 C  CG  . PRO   B 1 492 ? -42.993 -21.956 13.234  1.00 17.35 ? 515  PRO   B CG  1 
ATOM   8156 C  CD  . PRO   B 1 492 ? -42.707 -23.186 14.088  1.00 17.33 ? 515  PRO   B CD  1 
ATOM   8157 N  N   . GLY   B 1 493 ? -46.277 -23.524 13.948  1.00 16.43 ? 516  GLY   B N   1 
ATOM   8158 C  CA  . GLY   B 1 493 ? -47.576 -23.851 13.362  1.00 17.53 ? 516  GLY   B CA  1 
ATOM   8159 C  C   . GLY   B 1 493 ? -47.665 -23.483 11.881  1.00 16.05 ? 516  GLY   B C   1 
ATOM   8160 O  O   . GLY   B 1 493 ? -46.660 -23.141 11.266  1.00 14.82 ? 516  GLY   B O   1 
ATOM   8161 N  N   . THR   B 1 494 ? -48.900 -23.518 11.343  1.00 14.78 ? 517  THR   B N   1 
ATOM   8162 C  CA  . THR   B 1 494 ? -49.151 -23.389 9.923   1.00 16.39 ? 517  THR   B CA  1 
ATOM   8163 C  C   . THR   B 1 494 ? -50.349 -22.487 9.658   1.00 15.15 ? 517  THR   B C   1 
ATOM   8164 O  O   . THR   B 1 494 ? -51.046 -22.678 8.656   1.00 17.16 ? 517  THR   B O   1 
ATOM   8165 C  CB  . THR   B 1 494 ? -49.362 -24.759 9.266   1.00 19.10 ? 517  THR   B CB  1 
ATOM   8166 O  OG1 . THR   B 1 494 ? -50.395 -25.389 10.016  1.00 24.06 ? 517  THR   B OG1 1 
ATOM   8167 C  CG2 . THR   B 1 494 ? -48.118 -25.620 9.322   1.00 21.61 ? 517  THR   B CG2 1 
ATOM   8168 N  N   . THR   B 1 495 ? -50.514 -21.448 10.475  1.00 13.40 ? 518  THR   B N   1 
ATOM   8169 C  CA  . THR   B 1 495 ? -51.602 -20.503 10.299  1.00 12.75 ? 518  THR   B CA  1 
ATOM   8170 C  C   . THR   B 1 495 ? -51.396 -19.747 8.988   1.00 12.84 ? 518  THR   B C   1 
ATOM   8171 O  O   . THR   B 1 495 ? -50.297 -19.228 8.737   1.00 13.06 ? 518  THR   B O   1 
ATOM   8172 C  CB  . THR   B 1 495 ? -51.619 -19.528 11.478  1.00 11.92 ? 518  THR   B CB  1 
ATOM   8173 O  OG1 . THR   B 1 495 ? -51.387 -20.248 12.682  1.00 11.27 ? 518  THR   B OG1 1 
ATOM   8174 C  CG2 . THR   B 1 495 ? -52.916 -18.741 11.581  1.00 11.92 ? 518  THR   B CG2 1 
ATOM   8175 N  N   . VAL   B 1 496 ? -52.458 -19.622 8.187   1.00 12.21 ? 519  VAL   B N   1 
ATOM   8176 C  CA  . VAL   B 1 496 ? -52.382 -18.902 6.929   1.00 12.51 ? 519  VAL   B CA  1 
ATOM   8177 C  C   . VAL   B 1 496 ? -53.476 -17.863 6.886   1.00 11.40 ? 519  VAL   B C   1 
ATOM   8178 O  O   . VAL   B 1 496 ? -54.558 -18.031 7.464   1.00 12.24 ? 519  VAL   B O   1 
ATOM   8179 C  CB  . VAL   B 1 496 ? -52.474 -19.840 5.714   1.00 13.98 ? 519  VAL   B CB  1 
ATOM   8180 C  CG1 . VAL   B 1 496 ? -51.299 -20.799 5.684   1.00 15.81 ? 519  VAL   B CG1 1 
ATOM   8181 C  CG2 . VAL   B 1 496 ? -53.817 -20.571 5.703   1.00 13.39 ? 519  VAL   B CG2 1 
ATOM   8182 N  N   . PRO   B 1 497 ? -53.235 -16.743 6.192   1.00 11.90 ? 520  PRO   B N   1 
ATOM   8183 C  CA  . PRO   B 1 497 ? -54.242 -15.705 6.115   1.00 12.47 ? 520  PRO   B CA  1 
ATOM   8184 C  C   . PRO   B 1 497 ? -55.291 -16.077 5.082   1.00 12.46 ? 520  PRO   B C   1 
ATOM   8185 O  O   . PRO   B 1 497 ? -55.110 -17.020 4.313   1.00 12.91 ? 520  PRO   B O   1 
ATOM   8186 C  CB  . PRO   B 1 497 ? -53.420 -14.500 5.723   1.00 11.89 ? 520  PRO   B CB  1 
ATOM   8187 C  CG  . PRO   B 1 497 ? -52.364 -15.076 4.815   1.00 12.35 ? 520  PRO   B CG  1 
ATOM   8188 C  CD  . PRO   B 1 497 ? -51.994 -16.366 5.501   1.00 11.99 ? 520  PRO   B CD  1 
ATOM   8189 N  N   . SER   B 1 498 ? -56.377 -15.324 5.114   1.00 12.22 ? 521  SER   B N   1 
ATOM   8190 C  CA  . SER   B 1 498 ? -57.439 -15.496 4.148   1.00 13.09 ? 521  SER   B CA  1 
ATOM   8191 C  C   . SER   B 1 498 ? -57.731 -14.184 3.427   1.00 12.22 ? 521  SER   B C   1 
ATOM   8192 O  O   . SER   B 1 498 ? -57.156 -13.145 3.678   1.00 12.78 ? 521  SER   B O   1 
ATOM   8193 C  CB  . SER   B 1 498 ? -58.648 -16.062 4.844   1.00 13.65 ? 521  SER   B CB  1 
ATOM   8194 O  OG  . SER   B 1 498 ? -59.319 -15.013 5.534   1.00 14.63 ? 521  SER   B OG  1 
ATOM   8195 N  N   . ALA   B 1 499 ? -58.653 -14.225 2.470   1.00 12.92 ? 522  ALA   B N   1 
ATOM   8196 C  CA  . ALA   B 1 499 ? -59.127 -13.054 1.766   1.00 12.41 ? 522  ALA   B CA  1 
ATOM   8197 C  C   . ALA   B 1 499 ? -59.698 -11.982 2.693   1.00 12.97 ? 522  ALA   B C   1 
ATOM   8198 O  O   . ALA   B 1 499 ? -59.683 -10.819 2.318   1.00 14.20 ? 522  ALA   B O   1 
ATOM   8199 C  CB  . ALA   B 1 499 ? -60.193 -13.490 0.760   1.00 13.25 ? 522  ALA   B CB  1 
ATOM   8200 N  N   . THR   B 1 500 ? -60.176 -12.374 3.885   1.00 14.78 ? 523  THR   B N   1 
ATOM   8201 C  CA  . THR   B 1 500 ? -60.826 -11.436 4.793   1.00 15.50 ? 523  THR   B CA  1 
ATOM   8202 C  C   . THR   B 1 500 ? -60.020 -11.165 6.048   1.00 14.78 ? 523  THR   B C   1 
ATOM   8203 O  O   . THR   B 1 500 ? -60.334 -10.168 6.708   1.00 13.33 ? 523  THR   B O   1 
ATOM   8204 C  CB  . THR   B 1 500 ? -62.219 -11.946 5.166   1.00 16.68 ? 523  THR   B CB  1 
ATOM   8205 O  OG1 . THR   B 1 500 ? -62.175 -13.247 5.747   1.00 18.29 ? 523  THR   B OG1 1 
ATOM   8206 C  CG2 . THR   B 1 500 ? -63.083 -12.022 3.923   1.00 18.11 ? 523  THR   B CG2 1 
ATOM   8207 N  N   . ARG   B 1 501 ? -59.077 -12.054 6.401   1.00 12.70 ? 524  ARG   B N   1 
ATOM   8208 C  CA  . ARG   B 1 501 ? -58.394 -11.921 7.688   1.00 12.22 ? 524  ARG   B CA  1 
ATOM   8209 C  C   . ARG   B 1 501 ? -56.894 -12.125 7.533   1.00 11.92 ? 524  ARG   B C   1 
ATOM   8210 O  O   . ARG   B 1 501 ? -56.410 -13.042 6.859   1.00 11.93 ? 524  ARG   B O   1 
ATOM   8211 C  CB  . ARG   B 1 501 ? -58.966 -12.946 8.671   1.00 11.96 ? 524  ARG   B CB  1 
ATOM   8212 C  CG  . ARG   B 1 501 ? -60.465 -12.745 8.859   1.00 11.79 ? 524  ARG   B CG  1 
ATOM   8213 C  CD  . ARG   B 1 501 ? -61.023 -13.493 10.030  1.00 11.89 ? 524  ARG   B CD  1 
ATOM   8214 N  NE  . ARG   B 1 501 ? -60.874 -14.947 9.936   1.00 12.04 ? 524  ARG   B NE  1 
ATOM   8215 C  CZ  . ARG   B 1 501 ? -61.288 -15.803 10.875  1.00 13.33 ? 524  ARG   B CZ  1 
ATOM   8216 N  NH1 . ARG   B 1 501 ? -61.905 -15.408 11.987  1.00 12.25 ? 524  ARG   B NH1 1 
ATOM   8217 N  NH2 . ARG   B 1 501 ? -61.031 -17.077 10.704  1.00 12.42 ? 524  ARG   B NH2 1 
ATOM   8218 N  N   . ALA   B 1 502 ? -56.144 -11.332 8.294   1.00 11.70 ? 525  ALA   B N   1 
ATOM   8219 C  CA  . ALA   B 1 502 ? -54.739 -11.604 8.519   1.00 10.74 ? 525  ALA   B CA  1 
ATOM   8220 C  C   . ALA   B 1 502 ? -54.574 -12.798 9.457   1.00 11.44 ? 525  ALA   B C   1 
ATOM   8221 O  O   . ALA   B 1 502 ? -55.461 -13.121 10.256  1.00 10.80 ? 525  ALA   B O   1 
ATOM   8222 C  CB  . ALA   B 1 502 ? -54.106 -10.369 9.089   1.00 11.19 ? 525  ALA   B CB  1 
ATOM   8223 N  N   . ALA   B 1 503 ? -53.398 -13.417 9.375   1.00 10.31 ? 526  ALA   B N   1 
ATOM   8224 C  CA  . ALA   B 1 503 ? -53.040 -14.583 10.179  1.00 10.21 ? 526  ALA   B CA  1 
ATOM   8225 C  C   . ALA   B 1 503 ? -52.138 -14.155 11.320  1.00 10.32 ? 526  ALA   B C   1 
ATOM   8226 O  O   . ALA   B 1 503 ? -51.132 -13.488 11.062  1.00 9.85  ? 526  ALA   B O   1 
ATOM   8227 C  CB  . ALA   B 1 503 ? -52.289 -15.540 9.321   1.00 10.94 ? 526  ALA   B CB  1 
ATOM   8228 N  N   . VAL   B 1 504 ? -52.451 -14.600 12.546  1.00 9.52  ? 527  VAL   B N   1 
ATOM   8229 C  CA  . VAL   B 1 504 ? -51.593 -14.324 13.679  1.00 9.82  ? 527  VAL   B CA  1 
ATOM   8230 C  C   . VAL   B 1 504 ? -51.422 -15.586 14.503  1.00 9.79  ? 527  VAL   B C   1 
ATOM   8231 O  O   . VAL   B 1 504 ? -52.310 -16.440 14.545  1.00 9.95  ? 527  VAL   B O   1 
ATOM   8232 C  CB  . VAL   B 1 504 ? -52.130 -13.183 14.568  1.00 10.14 ? 527  VAL   B CB  1 
ATOM   8233 C  CG1 . VAL   B 1 504 ? -52.263 -11.912 13.737  1.00 10.42 ? 527  VAL   B CG1 1 
ATOM   8234 C  CG2 . VAL   B 1 504 ? -53.402 -13.597 15.310  1.00 10.85 ? 527  VAL   B CG2 1 
ATOM   8235 N  N   . LEU   B 1 505 ? -50.263 -15.687 15.146  1.00 9.84  ? 528  LEU   B N   1 
ATOM   8236 C  CA  . LEU   B 1 505 ? -49.963 -16.737 16.087  1.00 10.02 ? 528  LEU   B CA  1 
ATOM   8237 C  C   . LEU   B 1 505 ? -50.108 -16.142 17.484  1.00 10.63 ? 528  LEU   B C   1 
ATOM   8238 O  O   . LEU   B 1 505 ? -49.169 -15.541 18.011  1.00 10.51 ? 528  LEU   B O   1 
ATOM   8239 C  CB  . LEU   B 1 505 ? -48.546 -17.233 15.759  1.00 10.50 ? 528  LEU   B CB  1 
ATOM   8240 C  CG  . LEU   B 1 505 ? -47.991 -18.371 16.614  1.00 10.96 ? 528  LEU   B CG  1 
ATOM   8241 C  CD1 . LEU   B 1 505 ? -48.816 -19.667 16.501  1.00 11.24 ? 528  LEU   B CD1 1 
ATOM   8242 C  CD2 . LEU   B 1 505 ? -46.532 -18.671 16.214  1.00 10.83 ? 528  LEU   B CD2 1 
ATOM   8243 N  N   . GLY   B 1 506 ? -51.310 -16.250 18.073  1.00 10.10 ? 529  GLY   B N   1 
ATOM   8244 C  CA  . GLY   B 1 506 ? -51.621 -15.461 19.251  1.00 10.00 ? 529  GLY   B CA  1 
ATOM   8245 C  C   . GLY   B 1 506 ? -50.965 -16.017 20.524  1.00 9.71  ? 529  GLY   B C   1 
ATOM   8246 O  O   . GLY   B 1 506 ? -51.074 -15.378 21.568  1.00 9.19  ? 529  GLY   B O   1 
ATOM   8247 N  N   . GLU   B 1 507 ? -50.381 -17.226 20.442  1.00 9.69  ? 530  GLU   B N   1 
ATOM   8248 C  CA  . GLU   B 1 507 ? -49.554 -17.813 21.488  1.00 10.33 ? 530  GLU   B CA  1 
ATOM   8249 C  C   . GLU   B 1 507 ? -48.681 -18.895 20.860  1.00 10.81 ? 530  GLU   B C   1 
ATOM   8250 O  O   . GLU   B 1 507 ? -49.142 -19.632 19.991  1.00 9.87  ? 530  GLU   B O   1 
ATOM   8251 C  CB  . GLU   B 1 507 ? -50.311 -18.513 22.615  1.00 11.12 ? 530  GLU   B CB  1 
ATOM   8252 C  CG  . GLU   B 1 507 ? -50.902 -17.555 23.639  1.00 12.29 ? 530  GLU   B CG  1 
ATOM   8253 C  CD  . GLU   B 1 507 ? -51.800 -18.241 24.662  1.00 12.33 ? 530  GLU   B CD  1 
ATOM   8254 O  OE1 . GLU   B 1 507 ? -51.404 -19.335 25.080  1.00 12.54 ? 530  GLU   B OE1 1 
ATOM   8255 O  OE2 . GLU   B 1 507 ? -52.872 -17.737 25.016  1.00 11.07 ? 530  GLU   B OE2 1 
ATOM   8256 N  N   . PHE   B 1 508 ? -47.407 -18.953 21.269  1.00 11.21 ? 531  PHE   B N   1 
ATOM   8257 C  CA  . PHE   B 1 508 ? -46.537 -20.060 20.904  1.00 11.85 ? 531  PHE   B CA  1 
ATOM   8258 C  C   . PHE   B 1 508 ? -45.392 -20.080 21.896  1.00 12.34 ? 531  PHE   B C   1 
ATOM   8259 O  O   . PHE   B 1 508 ? -45.261 -19.158 22.700  1.00 11.72 ? 531  PHE   B O   1 
ATOM   8260 C  CB  . PHE   B 1 508 ? -46.013 -19.987 19.462  1.00 12.52 ? 531  PHE   B CB  1 
ATOM   8261 C  CG  . PHE   B 1 508 ? -44.930 -18.937 19.225  1.00 11.92 ? 531  PHE   B CG  1 
ATOM   8262 C  CD1 . PHE   B 1 508 ? -45.223 -17.584 19.297  1.00 12.24 ? 531  PHE   B CD1 1 
ATOM   8263 C  CD2 . PHE   B 1 508 ? -43.604 -19.291 19.012  1.00 12.41 ? 531  PHE   B CD2 1 
ATOM   8264 C  CE1 . PHE   B 1 508 ? -44.235 -16.622 19.170  1.00 12.50 ? 531  PHE   B CE1 1 
ATOM   8265 C  CE2 . PHE   B 1 508 ? -42.623 -18.320 18.822  1.00 12.19 ? 531  PHE   B CE2 1 
ATOM   8266 C  CZ  . PHE   B 1 508 ? -42.933 -16.993 18.907  1.00 12.14 ? 531  PHE   B CZ  1 
ATOM   8267 N  N   . GLY   B 1 509 ? -44.515 -21.080 21.775  1.00 12.38 ? 532  GLY   B N   1 
ATOM   8268 C  CA  . GLY   B 1 509 ? -43.256 -21.101 22.516  1.00 12.15 ? 532  GLY   B CA  1 
ATOM   8269 C  C   . GLY   B 1 509 ? -43.380 -21.853 23.845  1.00 13.02 ? 532  GLY   B C   1 
ATOM   8270 O  O   . GLY   B 1 509 ? -43.465 -23.077 23.860  1.00 13.65 ? 532  GLY   B O   1 
ATOM   8271 N  N   . GLY   B 1 510 ? -43.440 -21.108 24.951  1.00 12.46 ? 533  GLY   B N   1 
ATOM   8272 C  CA  . GLY   B 1 510 ? -43.717 -21.686 26.260  1.00 13.40 ? 533  GLY   B CA  1 
ATOM   8273 C  C   . GLY   B 1 510 ? -42.575 -22.543 26.809  1.00 13.63 ? 533  GLY   B C   1 
ATOM   8274 O  O   . GLY   B 1 510 ? -42.814 -23.517 27.536  1.00 14.65 ? 533  GLY   B O   1 
ATOM   8275 N  N   . LEU   B 1 511 ? -41.328 -22.189 26.439  1.00 13.86 ? 534  LEU   B N   1 
ATOM   8276 C  CA  . LEU   B 1 511 ? -40.124 -22.958 26.765  1.00 13.78 ? 534  LEU   B CA  1 
ATOM   8277 C  C   . LEU   B 1 511 ? -39.716 -22.777 28.237  1.00 14.04 ? 534  LEU   B C   1 
ATOM   8278 O  O   . LEU   B 1 511 ? -39.468 -21.669 28.688  1.00 14.77 ? 534  LEU   B O   1 
ATOM   8279 C  CB  . LEU   B 1 511 ? -39.023 -22.501 25.797  1.00 12.81 ? 534  LEU   B CB  1 
ATOM   8280 C  CG  . LEU   B 1 511 ? -39.279 -22.647 24.295  1.00 13.41 ? 534  LEU   B CG  1 
ATOM   8281 C  CD1 . LEU   B 1 511 ? -38.044 -22.154 23.534  1.00 13.21 ? 534  LEU   B CD1 1 
ATOM   8282 C  CD2 . LEU   B 1 511 ? -39.676 -24.032 23.848  1.00 12.85 ? 534  LEU   B CD2 1 
ATOM   8283 N  N   . GLY   B 1 512 ? -39.640 -23.887 29.005  1.00 15.10 ? 535  GLY   B N   1 
ATOM   8284 C  CA  . GLY   B 1 512 ? -39.425 -23.887 30.437  1.00 15.23 ? 535  GLY   B CA  1 
ATOM   8285 C  C   . GLY   B 1 512 ? -37.953 -23.927 30.866  1.00 15.01 ? 535  GLY   B C   1 
ATOM   8286 O  O   . GLY   B 1 512 ? -37.142 -24.621 30.259  1.00 16.73 ? 535  GLY   B O   1 
ATOM   8287 N  N   . PHE   B 1 513 ? -37.641 -23.206 31.929  1.00 17.11 ? 536  PHE   B N   1 
ATOM   8288 C  CA  . PHE   B 1 513 ? -36.363 -23.415 32.598  1.00 17.93 ? 536  PHE   B CA  1 
ATOM   8289 C  C   . PHE   B 1 513 ? -36.437 -22.882 34.024  1.00 17.52 ? 536  PHE   B C   1 
ATOM   8290 O  O   . PHE   B 1 513 ? -36.801 -21.736 34.268  1.00 18.75 ? 536  PHE   B O   1 
ATOM   8291 C  CB  . PHE   B 1 513 ? -35.213 -22.793 31.792  1.00 18.47 ? 536  PHE   B CB  1 
ATOM   8292 C  CG  . PHE   B 1 513 ? -33.832 -23.096 32.369  1.00 18.78 ? 536  PHE   B CG  1 
ATOM   8293 C  CD1 . PHE   B 1 513 ? -33.198 -24.287 32.056  1.00 19.04 ? 536  PHE   B CD1 1 
ATOM   8294 C  CD2 . PHE   B 1 513 ? -33.214 -22.230 33.259  1.00 19.30 ? 536  PHE   B CD2 1 
ATOM   8295 C  CE1 . PHE   B 1 513 ? -31.964 -24.596 32.588  1.00 20.17 ? 536  PHE   B CE1 1 
ATOM   8296 C  CE2 . PHE   B 1 513 ? -31.968 -22.548 33.771  1.00 21.28 ? 536  PHE   B CE2 1 
ATOM   8297 C  CZ  . PHE   B 1 513 ? -31.348 -23.722 33.430  1.00 19.54 ? 536  PHE   B CZ  1 
ATOM   8298 N  N   . LYS   B 1 514 ? -36.092 -23.766 34.978  1.00 19.03 ? 537  LYS   B N   1 
ATOM   8299 C  CA  . LYS   B 1 514 ? -36.067 -23.419 36.377  1.00 20.94 ? 537  LYS   B CA  1 
ATOM   8300 C  C   . LYS   B 1 514 ? -34.706 -22.829 36.742  1.00 20.90 ? 537  LYS   B C   1 
ATOM   8301 O  O   . LYS   B 1 514 ? -33.692 -23.508 36.685  1.00 25.23 ? 537  LYS   B O   1 
ATOM   8302 C  CB  . LYS   B 1 514 ? -36.341 -24.692 37.182  1.00 23.61 ? 537  LYS   B CB  1 
ATOM   8303 C  CG  . LYS   B 1 514 ? -37.700 -25.298 36.893  1.00 26.30 ? 537  LYS   B CG  1 
ATOM   8304 C  CD  . LYS   B 1 514 ? -37.869 -26.733 37.406  1.00 30.17 ? 537  LYS   B CD  1 
ATOM   8305 C  CE  . LYS   B 1 514 ? -37.536 -27.796 36.401  1.00 32.21 ? 537  LYS   B CE  1 
ATOM   8306 N  NZ  . LYS   B 1 514 ? -38.499 -27.794 35.293  1.00 38.27 ? 537  LYS   B NZ  1 
ATOM   8307 N  N   . VAL   B 1 515 ? -34.712 -21.580 37.159  1.00 22.29 ? 538  VAL   B N   1 
ATOM   8308 C  CA  . VAL   B 1 515 ? -33.513 -20.898 37.595  1.00 22.58 ? 538  VAL   B CA  1 
ATOM   8309 C  C   . VAL   B 1 515 ? -33.385 -21.059 39.107  1.00 23.37 ? 538  VAL   B C   1 
ATOM   8310 O  O   . VAL   B 1 515 ? -34.116 -20.458 39.869  1.00 22.41 ? 538  VAL   B O   1 
ATOM   8311 C  CB  . VAL   B 1 515 ? -33.567 -19.419 37.194  1.00 22.85 ? 538  VAL   B CB  1 
ATOM   8312 C  CG1 . VAL   B 1 515 ? -32.324 -18.664 37.631  1.00 22.75 ? 538  VAL   B CG1 1 
ATOM   8313 C  CG2 . VAL   B 1 515 ? -33.782 -19.260 35.697  1.00 21.96 ? 538  VAL   B CG2 1 
ATOM   8314 N  N   . ALA   B 1 516 ? -32.401 -21.852 39.538  1.00 25.16 ? 539  ALA   B N   1 
ATOM   8315 C  CA  . ALA   B 1 516 ? -32.175 -22.001 40.959  1.00 23.80 ? 539  ALA   B CA  1 
ATOM   8316 C  C   . ALA   B 1 516 ? -32.011 -20.640 41.613  1.00 22.32 ? 539  ALA   B C   1 
ATOM   8317 O  O   . ALA   B 1 516 ? -31.280 -19.775 41.134  1.00 23.94 ? 539  ALA   B O   1 
ATOM   8318 C  CB  . ALA   B 1 516 ? -30.956 -22.879 41.145  1.00 27.57 ? 539  ALA   B CB  1 
ATOM   8319 N  N   . GLY   B 1 517 ? -32.689 -20.432 42.738  1.00 20.54 ? 540  GLY   B N   1 
ATOM   8320 C  CA  . GLY   B 1 517 ? -32.624 -19.170 43.443  1.00 21.20 ? 540  GLY   B CA  1 
ATOM   8321 C  C   . GLY   B 1 517 ? -33.801 -18.263 43.117  1.00 21.00 ? 540  GLY   B C   1 
ATOM   8322 O  O   . GLY   B 1 517 ? -34.066 -17.343 43.875  1.00 24.69 ? 540  GLY   B O   1 
ATOM   8323 N  N   . HIS   B 1 518 ? -34.487 -18.534 41.994  1.00 23.06 ? 541  HIS   B N   1 
ATOM   8324 C  CA  . HIS   B 1 518 ? -35.446 -17.603 41.420  1.00 24.33 ? 541  HIS   B CA  1 
ATOM   8325 C  C   . HIS   B 1 518 ? -36.659 -18.396 40.942  1.00 24.59 ? 541  HIS   B C   1 
ATOM   8326 O  O   . HIS   B 1 518 ? -37.136 -18.204 39.826  1.00 24.41 ? 541  HIS   B O   1 
ATOM   8327 C  CB  . HIS   B 1 518 ? -34.780 -16.789 40.306  1.00 23.35 ? 541  HIS   B CB  1 
ATOM   8328 C  CG  . HIS   B 1 518 ? -33.646 -15.967 40.800  1.00 22.60 ? 541  HIS   B CG  1 
ATOM   8329 N  ND1 . HIS   B 1 518 ? -33.765 -14.704 41.350  1.00 24.59 ? 541  HIS   B ND1 1 
ATOM   8330 C  CD2 . HIS   B 1 518 ? -32.358 -16.301 40.893  1.00 22.36 ? 541  HIS   B CD2 1 
ATOM   8331 C  CE1 . HIS   B 1 518 ? -32.551 -14.285 41.719  1.00 24.41 ? 541  HIS   B CE1 1 
ATOM   8332 N  NE2 . HIS   B 1 518 ? -31.694 -15.240 41.440  1.00 20.81 ? 541  HIS   B NE2 1 
ATOM   8333 N  N   . GLU   B 1 519 ? -37.078 -19.335 41.793  1.00 22.99 ? 542  GLU   B N   1 
ATOM   8334 C  CA  . GLU   B 1 519 ? -38.249 -20.170 41.603  1.00 24.42 ? 542  GLU   B CA  1 
ATOM   8335 C  C   . GLU   B 1 519 ? -39.285 -19.786 42.656  1.00 25.13 ? 542  GLU   B C   1 
ATOM   8336 O  O   . GLU   B 1 519 ? -38.977 -19.705 43.846  1.00 25.28 ? 542  GLU   B O   1 
ATOM   8337 C  CB  . GLU   B 1 519 ? -37.959 -21.651 41.815  1.00 26.23 ? 542  GLU   B CB  1 
ATOM   8338 C  CG  . GLU   B 1 519 ? -37.126 -22.331 40.737  1.00 28.22 ? 542  GLU   B CG  1 
ATOM   8339 C  CD  . GLU   B 1 519 ? -36.768 -23.780 41.053  1.00 30.82 ? 542  GLU   B CD  1 
ATOM   8340 O  OE1 . GLU   B 1 519 ? -35.874 -23.968 41.917  1.00 32.36 ? 542  GLU   B OE1 1 
ATOM   8341 O  OE2 . GLU   B 1 519 ? -37.360 -24.728 40.476  1.00 26.93 ? 542  GLU   B OE2 1 
ATOM   8342 N  N   . TRP   B 1 520 ? -40.520 -19.505 42.218  1.00 24.41 ? 543  TRP   B N   1 
ATOM   8343 C  CA  . TRP   B 1 520 ? -41.601 -19.191 43.144  1.00 20.43 ? 543  TRP   B CA  1 
ATOM   8344 C  C   . TRP   B 1 520 ? -41.828 -20.334 44.133  1.00 22.20 ? 543  TRP   B C   1 
ATOM   8345 O  O   . TRP   B 1 520 ? -42.130 -20.110 45.307  1.00 25.25 ? 543  TRP   B O   1 
ATOM   8346 C  CB  . TRP   B 1 520 ? -42.890 -18.937 42.355  1.00 20.49 ? 543  TRP   B CB  1 
ATOM   8347 C  CG  . TRP   B 1 520 ? -44.041 -18.384 43.151  1.00 18.14 ? 543  TRP   B CG  1 
ATOM   8348 C  CD1 . TRP   B 1 520 ? -44.186 -17.129 43.657  1.00 17.40 ? 543  TRP   B CD1 1 
ATOM   8349 C  CD2 . TRP   B 1 520 ? -45.278 -19.075 43.419  1.00 17.30 ? 543  TRP   B CD2 1 
ATOM   8350 N  NE1 . TRP   B 1 520 ? -45.417 -17.001 44.233  1.00 20.47 ? 543  TRP   B NE1 1 
ATOM   8351 C  CE2 . TRP   B 1 520 ? -46.108 -18.176 44.099  1.00 17.13 ? 543  TRP   B CE2 1 
ATOM   8352 C  CE3 . TRP   B 1 520 ? -45.746 -20.364 43.143  1.00 17.13 ? 543  TRP   B CE3 1 
ATOM   8353 C  CZ2 . TRP   B 1 520 ? -47.391 -18.512 44.523  1.00 19.99 ? 543  TRP   B CZ2 1 
ATOM   8354 C  CZ3 . TRP   B 1 520 ? -47.029 -20.689 43.535  1.00 19.72 ? 543  TRP   B CZ3 1 
ATOM   8355 C  CH2 . TRP   B 1 520 ? -47.830 -19.783 44.221  1.00 19.58 ? 543  TRP   B CH2 1 
ATOM   8356 N  N   . TYR   B 1 521 ? -41.747 -21.551 43.627  1.00 25.36 ? 544  TYR   B N   1 
ATOM   8357 C  CA  . TYR   B 1 521 ? -41.757 -22.731 44.469  1.00 28.62 ? 544  TYR   B CA  1 
ATOM   8358 C  C   . TYR   B 1 521 ? -40.705 -23.694 43.933  1.00 29.00 ? 544  TYR   B C   1 
ATOM   8359 O  O   . TYR   B 1 521 ? -40.900 -24.339 42.897  1.00 29.55 ? 544  TYR   B O   1 
ATOM   8360 C  CB  . TYR   B 1 521 ? -43.171 -23.324 44.530  1.00 35.76 ? 544  TYR   B CB  1 
ATOM   8361 C  CG  . TYR   B 1 521 ? -43.256 -24.379 45.623  1.00 39.96 ? 544  TYR   B CG  1 
ATOM   8362 C  CD1 . TYR   B 1 521 ? -43.563 -24.035 46.934  1.00 41.52 ? 544  TYR   B CD1 1 
ATOM   8363 C  CD2 . TYR   B 1 521 ? -42.918 -25.699 45.354  1.00 45.44 ? 544  TYR   B CD2 1 
ATOM   8364 C  CE1 . TYR   B 1 521 ? -43.587 -24.987 47.938  1.00 43.91 ? 544  TYR   B CE1 1 
ATOM   8365 C  CE2 . TYR   B 1 521 ? -42.940 -26.659 46.348  1.00 48.12 ? 544  TYR   B CE2 1 
ATOM   8366 C  CZ  . TYR   B 1 521 ? -43.273 -26.303 47.642  1.00 47.84 ? 544  TYR   B CZ  1 
ATOM   8367 O  OH  . TYR   B 1 521 ? -43.275 -27.265 48.615  1.00 57.02 ? 544  TYR   B OH  1 
ATOM   8368 N  N   . PRO   B 1 522 ? -39.539 -23.824 44.611  1.00 26.27 ? 545  PRO   B N   1 
ATOM   8369 C  CA  . PRO   B 1 522 ? -38.471 -24.687 44.105  1.00 28.31 ? 545  PRO   B CA  1 
ATOM   8370 C  C   . PRO   B 1 522 ? -38.976 -26.077 43.763  1.00 28.47 ? 545  PRO   B C   1 
ATOM   8371 O  O   . PRO   B 1 522 ? -39.706 -26.699 44.541  1.00 34.05 ? 545  PRO   B O   1 
ATOM   8372 C  CB  . PRO   B 1 522 ? -37.413 -24.677 45.226  1.00 29.74 ? 545  PRO   B CB  1 
ATOM   8373 C  CG  . PRO   B 1 522 ? -37.640 -23.334 45.899  1.00 28.23 ? 545  PRO   B CG  1 
ATOM   8374 C  CD  . PRO   B 1 522 ? -39.138 -23.066 45.804  1.00 27.79 ? 545  PRO   B CD  1 
ATOM   8375 N  N   . GLY   B 1 523 ? -38.624 -26.504 42.549  1.00 26.88 ? 546  GLY   B N   1 
ATOM   8376 C  CA  . GLY   B 1 523 ? -39.125 -27.728 41.955  1.00 27.23 ? 546  GLY   B CA  1 
ATOM   8377 C  C   . GLY   B 1 523 ? -40.604 -27.664 41.556  1.00 27.64 ? 546  GLY   B C   1 
ATOM   8378 O  O   . GLY   B 1 523 ? -41.128 -28.656 41.058  1.00 29.82 ? 546  GLY   B O   1 
ATOM   8379 N  N   . GLY   B 1 524 ? -41.276 -26.517 41.718  1.00 26.68 ? 547  GLY   B N   1 
ATOM   8380 C  CA  . GLY   B 1 524 ? -42.677 -26.445 41.329  1.00 30.37 ? 547  GLY   B CA  1 
ATOM   8381 C  C   . GLY   B 1 524 ? -42.896 -26.357 39.808  1.00 28.44 ? 547  GLY   B C   1 
ATOM   8382 O  O   . GLY   B 1 524 ? -43.979 -26.680 39.316  1.00 27.93 ? 547  GLY   B O   1 
ATOM   8383 N  N   . GLY   B 1 525 ? -41.884 -25.914 39.053  1.00 25.25 ? 548  GLY   B N   1 
ATOM   8384 C  CA  . GLY   B 1 525 ? -42.114 -25.356 37.723  1.00 23.57 ? 548  GLY   B CA  1 
ATOM   8385 C  C   . GLY   B 1 525 ? -42.535 -26.379 36.670  1.00 22.81 ? 548  GLY   B C   1 
ATOM   8386 O  O   . GLY   B 1 525 ? -42.120 -27.537 36.705  1.00 24.64 ? 548  GLY   B O   1 
ATOM   8387 N  N   . PHE   B 1 526 ? -43.327 -25.912 35.684  1.00 20.13 ? 549  PHE   B N   1 
ATOM   8388 C  CA  . PHE   B 1 526 ? -43.711 -26.672 34.506  1.00 17.71 ? 549  PHE   B CA  1 
ATOM   8389 C  C   . PHE   B 1 526 ? -43.708 -25.740 33.286  1.00 18.04 ? 549  PHE   B C   1 
ATOM   8390 O  O   . PHE   B 1 526 ? -43.658 -24.525 33.438  1.00 19.14 ? 549  PHE   B O   1 
ATOM   8391 C  CB  . PHE   B 1 526 ? -45.114 -27.263 34.669  1.00 20.29 ? 549  PHE   B CB  1 
ATOM   8392 C  CG  . PHE   B 1 526 ? -46.228 -26.224 34.610  1.00 20.07 ? 549  PHE   B CG  1 
ATOM   8393 C  CD1 . PHE   B 1 526 ? -46.792 -25.860 33.392  1.00 20.74 ? 549  PHE   B CD1 1 
ATOM   8394 C  CD2 . PHE   B 1 526 ? -46.687 -25.599 35.759  1.00 22.17 ? 549  PHE   B CD2 1 
ATOM   8395 C  CE1 . PHE   B 1 526 ? -47.767 -24.883 33.325  1.00 19.94 ? 549  PHE   B CE1 1 
ATOM   8396 C  CE2 . PHE   B 1 526 ? -47.680 -24.632 35.688  1.00 22.85 ? 549  PHE   B CE2 1 
ATOM   8397 C  CZ  . PHE   B 1 526 ? -48.221 -24.286 34.461  1.00 20.99 ? 549  PHE   B CZ  1 
ATOM   8398 N  N   . SER   B 1 527 ? -43.766 -26.316 32.094  1.00 16.54 ? 550  SER   B N   1 
ATOM   8399 C  CA  . SER   B 1 527 ? -43.798 -25.543 30.862  1.00 17.44 ? 550  SER   B CA  1 
ATOM   8400 C  C   . SER   B 1 527 ? -44.354 -26.421 29.756  1.00 17.22 ? 550  SER   B C   1 
ATOM   8401 O  O   . SER   B 1 527 ? -44.639 -27.603 29.973  1.00 20.92 ? 550  SER   B O   1 
ATOM   8402 C  CB  . SER   B 1 527 ? -42.402 -25.036 30.497  1.00 16.78 ? 550  SER   B CB  1 
ATOM   8403 O  OG  . SER   B 1 527 ? -41.667 -26.108 29.909  1.00 17.35 ? 550  SER   B OG  1 
ATOM   8404 N  N   . TYR   B 1 528 ? -44.462 -25.881 28.546  1.00 15.81 ? 551  TYR   B N   1 
ATOM   8405 C  CA  . TYR   B 1 528 ? -44.813 -26.685 27.395  1.00 16.19 ? 551  TYR   B CA  1 
ATOM   8406 C  C   . TYR   B 1 528 ? -43.650 -27.514 26.849  1.00 19.20 ? 551  TYR   B C   1 
ATOM   8407 O  O   . TYR   B 1 528 ? -43.867 -28.354 25.979  1.00 23.34 ? 551  TYR   B O   1 
ATOM   8408 C  CB  . TYR   B 1 528 ? -45.307 -25.813 26.246  1.00 16.31 ? 551  TYR   B CB  1 
ATOM   8409 C  CG  . TYR   B 1 528 ? -46.694 -25.241 26.484  1.00 16.12 ? 551  TYR   B CG  1 
ATOM   8410 C  CD1 . TYR   B 1 528 ? -47.839 -25.936 26.095  1.00 17.91 ? 551  TYR   B CD1 1 
ATOM   8411 C  CD2 . TYR   B 1 528 ? -46.853 -23.980 27.046  1.00 15.73 ? 551  TYR   B CD2 1 
ATOM   8412 C  CE1 . TYR   B 1 528 ? -49.105 -25.396 26.298  1.00 18.48 ? 551  TYR   B CE1 1 
ATOM   8413 C  CE2 . TYR   B 1 528 ? -48.112 -23.444 27.274  1.00 16.06 ? 551  TYR   B CE2 1 
ATOM   8414 C  CZ  . TYR   B 1 528 ? -49.244 -24.149 26.882  1.00 17.13 ? 551  TYR   B CZ  1 
ATOM   8415 O  OH  . TYR   B 1 528 ? -50.509 -23.633 27.045  1.00 16.60 ? 551  TYR   B OH  1 
ATOM   8416 N  N   . GLU   B 1 529 ? -42.414 -27.218 27.269  1.00 20.47 ? 552  GLU   B N   1 
ATOM   8417 C  CA  . GLU   B 1 529 ? -41.260 -28.012 26.869  1.00 18.55 ? 552  GLU   B CA  1 
ATOM   8418 C  C   . GLU   B 1 529 ? -40.078 -27.548 27.712  1.00 19.12 ? 552  GLU   B C   1 
ATOM   8419 O  O   . GLU   B 1 529 ? -39.551 -26.449 27.504  1.00 14.78 ? 552  GLU   B O   1 
ATOM   8420 C  CB  . GLU   B 1 529 ? -40.975 -27.889 25.377  1.00 18.01 ? 552  GLU   B CB  1 
ATOM   8421 C  CG  . GLU   B 1 529 ? -39.773 -28.676 24.864  1.00 18.25 ? 552  GLU   B CG  1 
ATOM   8422 C  CD  . GLU   B 1 529 ? -39.356 -28.376 23.429  1.00 19.04 ? 552  GLU   B CD  1 
ATOM   8423 O  OE1 . GLU   B 1 529 ? -39.999 -28.883 22.486  1.00 21.59 ? 552  GLU   B OE1 1 
ATOM   8424 O  OE2 . GLU   B 1 529 ? -38.324 -27.669 23.214  1.00 18.98 ? 552  GLU   B OE2 1 
ATOM   8425 N  N   . ASP   B 1 530 ? -39.727 -28.383 28.698  1.00 18.13 ? 553  ASP   B N   1 
ATOM   8426 C  CA  . ASP   B 1 530 ? -38.665 -28.075 29.630  1.00 20.17 ? 553  ASP   B CA  1 
ATOM   8427 C  C   . ASP   B 1 530 ? -37.344 -28.168 28.881  1.00 18.43 ? 553  ASP   B C   1 
ATOM   8428 O  O   . ASP   B 1 530 ? -37.086 -29.135 28.156  1.00 20.42 ? 553  ASP   B O   1 
ATOM   8429 C  CB  . ASP   B 1 530 ? -38.708 -28.992 30.847  1.00 21.31 ? 553  ASP   B CB  1 
ATOM   8430 C  CG  . ASP   B 1 530 ? -39.967 -28.840 31.682  1.00 26.39 ? 553  ASP   B CG  1 
ATOM   8431 O  OD1 . ASP   B 1 530 ? -40.683 -27.833 31.503  1.00 28.74 ? 553  ASP   B OD1 1 
ATOM   8432 O  OD2 . ASP   B 1 530 ? -40.235 -29.724 32.501  1.00 30.72 ? 553  ASP   B OD2 1 
ATOM   8433 N  N   . GLN   B 1 531 ? -36.557 -27.103 28.992  1.00 16.70 ? 554  GLN   B N   1 
ATOM   8434 C  CA  . GLN   B 1 531 ? -35.282 -27.066 28.309  1.00 15.50 ? 554  GLN   B CA  1 
ATOM   8435 C  C   . GLN   B 1 531 ? -34.220 -27.608 29.259  1.00 13.92 ? 554  GLN   B C   1 
ATOM   8436 O  O   . GLN   B 1 531 ? -34.198 -27.253 30.437  1.00 13.96 ? 554  GLN   B O   1 
ATOM   8437 C  CB  . GLN   B 1 531 ? -34.855 -25.648 27.950  1.00 16.54 ? 554  GLN   B CB  1 
ATOM   8438 C  CG  . GLN   B 1 531 ? -35.890 -24.875 27.133  1.00 16.02 ? 554  GLN   B CG  1 
ATOM   8439 C  CD  . GLN   B 1 531 ? -36.126 -25.498 25.781  1.00 15.76 ? 554  GLN   B CD  1 
ATOM   8440 O  OE1 . GLN   B 1 531 ? -35.318 -25.397 24.846  1.00 18.27 ? 554  GLN   B OE1 1 
ATOM   8441 N  NE2 . GLN   B 1 531 ? -37.255 -26.184 25.652  1.00 15.43 ? 554  GLN   B NE2 1 
ATOM   8442 N  N   . PRO   B 1 532 ? -33.245 -28.392 28.762  1.00 14.47 ? 555  PRO   B N   1 
ATOM   8443 C  CA  . PRO   B 1 532 ? -32.205 -28.960 29.647  1.00 14.76 ? 555  PRO   B CA  1 
ATOM   8444 C  C   . PRO   B 1 532 ? -31.174 -27.970 30.175  1.00 14.92 ? 555  PRO   B C   1 
ATOM   8445 O  O   . PRO   B 1 532 ? -30.554 -28.205 31.212  1.00 15.34 ? 555  PRO   B O   1 
ATOM   8446 C  CB  . PRO   B 1 532 ? -31.563 -30.028 28.779  1.00 14.77 ? 555  PRO   B CB  1 
ATOM   8447 C  CG  . PRO   B 1 532 ? -31.807 -29.606 27.354  1.00 15.38 ? 555  PRO   B CG  1 
ATOM   8448 C  CD  . PRO   B 1 532 ? -33.122 -28.824 27.368  1.00 15.27 ? 555  PRO   B CD  1 
ATOM   8449 N  N   . ASP   B 1 533 ? -30.988 -26.868 29.436  1.00 14.81 ? 556  ASP   B N   1 
ATOM   8450 C  CA  . ASP   B 1 533 ? -29.968 -25.879 29.725  1.00 14.30 ? 556  ASP   B CA  1 
ATOM   8451 C  C   . ASP   B 1 533 ? -30.282 -24.613 28.913  1.00 14.55 ? 556  ASP   B C   1 
ATOM   8452 O  O   . ASP   B 1 533 ? -31.132 -24.628 28.013  1.00 13.85 ? 556  ASP   B O   1 
ATOM   8453 C  CB  . ASP   B 1 533 ? -28.579 -26.445 29.442  1.00 14.53 ? 556  ASP   B CB  1 
ATOM   8454 C  CG  . ASP   B 1 533 ? -28.385 -26.903 28.002  1.00 17.12 ? 556  ASP   B CG  1 
ATOM   8455 O  OD1 . ASP   B 1 533 ? -28.397 -26.011 27.117  1.00 17.33 ? 556  ASP   B OD1 1 
ATOM   8456 O  OD2 . ASP   B 1 533 ? -28.288 -28.152 27.764  1.00 15.39 ? 556  ASP   B OD2 1 
ATOM   8457 N  N   . LEU   B 1 534 ? -29.614 -23.516 29.287  1.00 15.05 ? 557  LEU   B N   1 
ATOM   8458 C  CA  . LEU   B 1 534 ? -29.866 -22.224 28.682  1.00 15.81 ? 557  LEU   B CA  1 
ATOM   8459 C  C   . LEU   B 1 534 ? -29.413 -22.177 27.228  1.00 16.00 ? 557  LEU   B C   1 
ATOM   8460 O  O   . LEU   B 1 534 ? -29.998 -21.442 26.460  1.00 14.20 ? 557  LEU   B O   1 
ATOM   8461 C  CB  . LEU   B 1 534 ? -29.194 -21.125 29.487  1.00 17.03 ? 557  LEU   B CB  1 
ATOM   8462 C  CG  . LEU   B 1 534 ? -29.732 -20.936 30.904  1.00 17.40 ? 557  LEU   B CG  1 
ATOM   8463 C  CD1 . LEU   B 1 534 ? -28.918 -19.819 31.553  1.00 20.09 ? 557  LEU   B CD1 1 
ATOM   8464 C  CD2 . LEU   B 1 534 ? -31.224 -20.653 30.886  1.00 18.06 ? 557  LEU   B CD2 1 
ATOM   8465 N  N   . ALA   B 1 535 ? -28.389 -22.943 26.832  1.00 15.77 ? 558  ALA   B N   1 
ATOM   8466 C  CA  . ALA   B 1 535 ? -27.937 -22.924 25.444  1.00 15.91 ? 558  ALA   B CA  1 
ATOM   8467 C  C   . ALA   B 1 535 ? -29.010 -23.514 24.546  1.00 15.56 ? 558  ALA   B C   1 
ATOM   8468 O  O   . ALA   B 1 535 ? -29.275 -23.006 23.451  1.00 16.06 ? 558  ALA   B O   1 
ATOM   8469 C  CB  . ALA   B 1 535 ? -26.625 -23.677 25.290  1.00 16.79 ? 558  ALA   B CB  1 
ATOM   8470 N  N   . HIS   B 1 536 ? -29.662 -24.568 25.046  1.00 15.02 ? 559  HIS   B N   1 
ATOM   8471 C  CA  . HIS   B 1 536 ? -30.753 -25.193 24.316  1.00 14.48 ? 559  HIS   B CA  1 
ATOM   8472 C  C   . HIS   B 1 536 ? -31.934 -24.221 24.234  1.00 13.15 ? 559  HIS   B C   1 
ATOM   8473 O  O   . HIS   B 1 536 ? -32.532 -24.053 23.144  1.00 12.88 ? 559  HIS   B O   1 
ATOM   8474 C  CB  . HIS   B 1 536 ? -31.143 -26.500 25.017  1.00 16.08 ? 559  HIS   B CB  1 
ATOM   8475 C  CG  . HIS   B 1 536 ? -32.112 -27.327 24.265  1.00 19.90 ? 559  HIS   B CG  1 
ATOM   8476 N  ND1 . HIS   B 1 536 ? -33.450 -27.020 24.106  1.00 19.84 ? 559  HIS   B ND1 1 
ATOM   8477 C  CD2 . HIS   B 1 536 ? -31.904 -28.499 23.633  1.00 23.84 ? 559  HIS   B CD2 1 
ATOM   8478 C  CE1 . HIS   B 1 536 ? -34.013 -27.965 23.368  1.00 23.36 ? 559  HIS   B CE1 1 
ATOM   8479 N  NE2 . HIS   B 1 536 ? -33.100 -28.878 23.080  1.00 24.90 ? 559  HIS   B NE2 1 
ATOM   8480 N  N   . LEU   B 1 537 ? -32.231 -23.559 25.370  1.00 12.79 ? 560  LEU   B N   1 
ATOM   8481 C  CA  . LEU   B 1 537 ? -33.303 -22.565 25.417  1.00 12.89 ? 560  LEU   B CA  1 
ATOM   8482 C  C   . LEU   B 1 537 ? -33.077 -21.504 24.335  1.00 13.39 ? 560  LEU   B C   1 
ATOM   8483 O  O   . LEU   B 1 537 ? -33.990 -21.191 23.555  1.00 12.12 ? 560  LEU   B O   1 
ATOM   8484 C  CB  . LEU   B 1 537 ? -33.427 -21.930 26.801  1.00 13.14 ? 560  LEU   B CB  1 
ATOM   8485 C  CG  . LEU   B 1 537 ? -34.346 -20.702 26.919  1.00 14.53 ? 560  LEU   B CG  1 
ATOM   8486 C  CD1 . LEU   B 1 537 ? -35.787 -21.044 26.649  1.00 15.68 ? 560  LEU   B CD1 1 
ATOM   8487 C  CD2 . LEU   B 1 537 ? -34.166 -20.082 28.296  1.00 16.11 ? 560  LEU   B CD2 1 
ATOM   8488 N  N   . ASN   B 1 538 ? -31.856 -20.942 24.278  1.00 12.16 ? 561  ASN   B N   1 
ATOM   8489 C  CA  . ASN   B 1 538 ? -31.556 -19.932 23.279  1.00 13.56 ? 561  ASN   B CA  1 
ATOM   8490 C  C   . ASN   B 1 538 ? -31.706 -20.461 21.849  1.00 12.99 ? 561  ASN   B C   1 
ATOM   8491 O  O   . ASN   B 1 538 ? -32.320 -19.810 20.991  1.00 12.37 ? 561  ASN   B O   1 
ATOM   8492 C  CB  . ASN   B 1 538 ? -30.173 -19.323 23.517  1.00 12.95 ? 561  ASN   B CB  1 
ATOM   8493 C  CG  . ASN   B 1 538 ? -30.136 -18.495 24.776  1.00 13.81 ? 561  ASN   B CG  1 
ATOM   8494 O  OD1 . ASN   B 1 538 ? -31.024 -17.662 24.980  1.00 12.63 ? 561  ASN   B OD1 1 
ATOM   8495 N  ND2 . ASN   B 1 538 ? -29.130 -18.671 25.624  1.00 15.76 ? 561  ASN   B ND2 1 
ATOM   8496 N  N   . ASN   B 1 539 ? -31.148 -21.639 21.559  1.00 12.10 ? 562  ASN   B N   1 
ATOM   8497 C  CA  . ASN   B 1 539 ? -31.202 -22.170 20.207  1.00 12.80 ? 562  ASN   B CA  1 
ATOM   8498 C  C   . ASN   B 1 539 ? -32.651 -22.448 19.797  1.00 11.91 ? 562  ASN   B C   1 
ATOM   8499 O  O   . ASN   B 1 539 ? -33.034 -22.159 18.671  1.00 11.34 ? 562  ASN   B O   1 
ATOM   8500 C  CB  . ASN   B 1 539 ? -30.376 -23.444 20.036  1.00 14.39 ? 562  ASN   B CB  1 
ATOM   8501 C  CG  . ASN   B 1 539 ? -28.887 -23.153 20.006  1.00 15.55 ? 562  ASN   B CG  1 
ATOM   8502 O  OD1 . ASN   B 1 539 ? -28.468 -22.032 19.676  1.00 16.12 ? 562  ASN   B OD1 1 
ATOM   8503 N  ND2 . ASN   B 1 539 ? -28.071 -24.156 20.286  1.00 17.16 ? 562  ASN   B ND2 1 
ATOM   8504 N  N   . ARG   B 1 540 ? -33.445 -22.960 20.741  1.00 13.48 ? 563  ARG   B N   1 
ATOM   8505 C  CA  . ARG   B 1 540 ? -34.828 -23.323 20.497  1.00 14.47 ? 563  ARG   B CA  1 
ATOM   8506 C  C   . ARG   B 1 540 ? -35.625 -22.066 20.151  1.00 14.58 ? 563  ARG   B C   1 
ATOM   8507 O  O   . ARG   B 1 540 ? -36.287 -22.032 19.113  1.00 16.18 ? 563  ARG   B O   1 
ATOM   8508 C  CB  . ARG   B 1 540 ? -35.384 -24.048 21.726  1.00 15.98 ? 563  ARG   B CB  1 
ATOM   8509 C  CG  . ARG   B 1 540 ? -36.699 -24.788 21.517  1.00 16.45 ? 563  ARG   B CG  1 
ATOM   8510 C  CD  . ARG   B 1 540 ? -36.554 -26.062 20.736  1.00 17.47 ? 563  ARG   B CD  1 
ATOM   8511 N  NE  . ARG   B 1 540 ? -37.834 -26.781 20.747  1.00 17.98 ? 563  ARG   B NE  1 
ATOM   8512 C  CZ  . ARG   B 1 540 ? -38.771 -26.809 19.776  1.00 19.10 ? 563  ARG   B CZ  1 
ATOM   8513 N  NH1 . ARG   B 1 540 ? -38.649 -26.148 18.636  1.00 18.27 ? 563  ARG   B NH1 1 
ATOM   8514 N  NH2 . ARG   B 1 540 ? -39.868 -27.513 19.976  1.00 19.74 ? 563  ARG   B NH2 1 
ATOM   8515 N  N   . PHE   B 1 541 ? -35.466 -21.029 20.977  1.00 12.45 ? 564  PHE   B N   1 
ATOM   8516 C  CA  . PHE   B 1 541 ? -36.174 -19.772 20.787  1.00 13.66 ? 564  PHE   B CA  1 
ATOM   8517 C  C   . PHE   B 1 541 ? -35.822 -19.156 19.434  1.00 13.11 ? 564  PHE   B C   1 
ATOM   8518 O  O   . PHE   B 1 541 ? -36.695 -18.754 18.656  1.00 11.24 ? 564  PHE   B O   1 
ATOM   8519 C  CB  . PHE   B 1 541 ? -35.791 -18.828 21.930  1.00 15.33 ? 564  PHE   B CB  1 
ATOM   8520 C  CG  . PHE   B 1 541 ? -36.427 -17.463 21.734  1.00 15.42 ? 564  PHE   B CG  1 
ATOM   8521 C  CD1 . PHE   B 1 541 ? -35.829 -16.509 20.910  1.00 15.94 ? 564  PHE   B CD1 1 
ATOM   8522 C  CD2 . PHE   B 1 541 ? -37.691 -17.187 22.247  1.00 16.44 ? 564  PHE   B CD2 1 
ATOM   8523 C  CE1 . PHE   B 1 541 ? -36.456 -15.297 20.646  1.00 14.92 ? 564  PHE   B CE1 1 
ATOM   8524 C  CE2 . PHE   B 1 541 ? -38.310 -15.958 22.000  1.00 15.14 ? 564  PHE   B CE2 1 
ATOM   8525 C  CZ  . PHE   B 1 541 ? -37.686 -15.015 21.208  1.00 15.18 ? 564  PHE   B CZ  1 
ATOM   8526 N  N   . VAL   B 1 542 ? -34.512 -19.037 19.169  1.00 12.22 ? 565  VAL   B N   1 
ATOM   8527 C  CA  . VAL   B 1 542 ? -34.044 -18.408 17.937  1.00 12.29 ? 565  VAL   B CA  1 
ATOM   8528 C  C   . VAL   B 1 542 ? -34.504 -19.208 16.715  1.00 12.26 ? 565  VAL   B C   1 
ATOM   8529 O  O   . VAL   B 1 542 ? -34.859 -18.637 15.670  1.00 12.52 ? 565  VAL   B O   1 
ATOM   8530 C  CB  . VAL   B 1 542 ? -32.514 -18.183 17.933  1.00 12.26 ? 565  VAL   B CB  1 
ATOM   8531 C  CG1 . VAL   B 1 542 ? -31.990 -17.684 16.584  1.00 13.65 ? 565  VAL   B CG1 1 
ATOM   8532 C  CG2 . VAL   B 1 542 ? -32.129 -17.209 19.031  1.00 12.29 ? 565  VAL   B CG2 1 
ATOM   8533 N  N   . GLY   B 1 543 ? -34.476 -20.540 16.819  1.00 12.33 ? 566  GLY   B N   1 
ATOM   8534 C  CA  . GLY   B 1 543 ? -34.964 -21.379 15.741  1.00 12.26 ? 566  GLY   B CA  1 
ATOM   8535 C  C   . GLY   B 1 543 ? -36.435 -21.089 15.389  1.00 13.15 ? 566  GLY   B C   1 
ATOM   8536 O  O   . GLY   B 1 543 ? -36.807 -21.074 14.207  1.00 12.95 ? 566  GLY   B O   1 
ATOM   8537 N  N   . LEU   B 1 544 ? -37.254 -20.802 16.414  1.00 13.13 ? 567  LEU   B N   1 
ATOM   8538 C  CA  . LEU   B 1 544 ? -38.674 -20.515 16.188  1.00 12.38 ? 567  LEU   B CA  1 
ATOM   8539 C  C   . LEU   B 1 544 ? -38.787 -19.176 15.471  1.00 12.31 ? 567  LEU   B C   1 
ATOM   8540 O  O   . LEU   B 1 544 ? -39.501 -19.079 14.512  1.00 12.15 ? 567  LEU   B O   1 
ATOM   8541 C  CB  . LEU   B 1 544 ? -39.482 -20.475 17.485  1.00 12.72 ? 567  LEU   B CB  1 
ATOM   8542 C  CG  . LEU   B 1 544 ? -39.641 -21.785 18.259  1.00 13.53 ? 567  LEU   B CG  1 
ATOM   8543 C  CD1 . LEU   B 1 544 ? -40.107 -21.549 19.679  1.00 13.88 ? 567  LEU   B CD1 1 
ATOM   8544 C  CD2 . LEU   B 1 544 ? -40.633 -22.650 17.563  1.00 14.12 ? 567  LEU   B CD2 1 
ATOM   8545 N  N   . ILE   B 1 545 ? -38.051 -18.143 15.914  1.00 11.61 ? 568  ILE   B N   1 
ATOM   8546 C  CA  . ILE   B 1 545 ? -38.193 -16.838 15.287  1.00 12.26 ? 568  ILE   B CA  1 
ATOM   8547 C  C   . ILE   B 1 545 ? -37.678 -16.887 13.851  1.00 12.47 ? 568  ILE   B C   1 
ATOM   8548 O  O   . ILE   B 1 545 ? -38.280 -16.344 12.905  1.00 11.66 ? 568  ILE   B O   1 
ATOM   8549 C  CB  . ILE   B 1 545 ? -37.503 -15.732 16.117  1.00 13.13 ? 568  ILE   B CB  1 
ATOM   8550 C  CG1 . ILE   B 1 545 ? -38.057 -15.662 17.557  1.00 14.28 ? 568  ILE   B CG1 1 
ATOM   8551 C  CG2 . ILE   B 1 545 ? -37.583 -14.384 15.400  1.00 12.33 ? 568  ILE   B CG2 1 
ATOM   8552 C  CD1 . ILE   B 1 545 ? -39.558 -15.416 17.659  1.00 15.89 ? 568  ILE   B CD1 1 
ATOM   8553 N  N   . ASP   B 1 546 ? -36.534 -17.555 13.666  1.00 12.67 ? 569  ASP   B N   1 
ATOM   8554 C  CA  . ASP   B 1 546 ? -35.996 -17.701 12.321  1.00 13.41 ? 569  ASP   B CA  1 
ATOM   8555 C  C   . ASP   B 1 546 ? -36.990 -18.429 11.418  1.00 13.29 ? 569  ASP   B C   1 
ATOM   8556 O  O   . ASP   B 1 546 ? -37.112 -18.106 10.255  1.00 14.84 ? 569  ASP   B O   1 
ATOM   8557 C  CB  . ASP   B 1 546 ? -34.656 -18.400 12.373  1.00 13.85 ? 569  ASP   B CB  1 
ATOM   8558 C  CG  . ASP   B 1 546 ? -33.508 -17.577 12.949  1.00 16.09 ? 569  ASP   B CG  1 
ATOM   8559 O  OD1 . ASP   B 1 546 ? -33.676 -16.351 13.121  1.00 17.38 ? 569  ASP   B OD1 1 
ATOM   8560 O  OD2 . ASP   B 1 546 ? -32.453 -18.193 13.260  1.00 16.33 ? 569  ASP   B OD2 1 
ATOM   8561 N  N   . ALA   B 1 547 ? -37.698 -19.433 11.928  1.00 12.63 ? 570  ALA   B N   1 
ATOM   8562 C  CA  . ALA   B 1 547 ? -38.664 -20.155 11.108  1.00 13.84 ? 570  ALA   B CA  1 
ATOM   8563 C  C   . ALA   B 1 547 ? -39.859 -19.269 10.747  1.00 12.30 ? 570  ALA   B C   1 
ATOM   8564 O  O   . ALA   B 1 547 ? -40.333 -19.305 9.617   1.00 13.39 ? 570  ALA   B O   1 
ATOM   8565 C  CB  . ALA   B 1 547 ? -39.134 -21.384 11.826  1.00 13.48 ? 570  ALA   B CB  1 
ATOM   8566 N  N   . ILE   B 1 548 ? -40.293 -18.418 11.681  1.00 12.07 ? 571  ILE   B N   1 
ATOM   8567 C  CA  . ILE   B 1 548 ? -41.301 -17.420 11.355  1.00 11.66 ? 571  ILE   B CA  1 
ATOM   8568 C  C   . ILE   B 1 548 ? -40.755 -16.480 10.270  1.00 12.84 ? 571  ILE   B C   1 
ATOM   8569 O  O   . ILE   B 1 548 ? -41.435 -16.177 9.291   1.00 12.56 ? 571  ILE   B O   1 
ATOM   8570 C  CB  . ILE   B 1 548 ? -41.740 -16.679 12.635  1.00 11.77 ? 571  ILE   B CB  1 
ATOM   8571 C  CG1 . ILE   B 1 548 ? -42.441 -17.626 13.620  1.00 12.39 ? 571  ILE   B CG1 1 
ATOM   8572 C  CG2 . ILE   B 1 548 ? -42.616 -15.478 12.317  1.00 11.51 ? 571  ILE   B CG2 1 
ATOM   8573 C  CD1 . ILE   B 1 548 ? -42.589 -17.070 15.021  1.00 12.48 ? 571  ILE   B CD1 1 
ATOM   8574 N  N   . ARG   B 1 549 ? -39.528 -15.971 10.434  1.00 11.87 ? 572  ARG   B N   1 
ATOM   8575 C  CA  . ARG   B 1 549 ? -38.992 -15.039 9.452   1.00 12.11 ? 572  ARG   B CA  1 
ATOM   8576 C  C   . ARG   B 1 549 ? -38.870 -15.685 8.073   1.00 12.07 ? 572  ARG   B C   1 
ATOM   8577 O  O   . ARG   B 1 549 ? -39.206 -15.083 7.046   1.00 12.81 ? 572  ARG   B O   1 
ATOM   8578 C  CB  . ARG   B 1 549 ? -37.612 -14.554 9.880   1.00 12.16 ? 572  ARG   B CB  1 
ATOM   8579 C  CG  . ARG   B 1 549 ? -36.921 -13.727 8.805   1.00 12.86 ? 572  ARG   B CG  1 
ATOM   8580 C  CD  . ARG   B 1 549 ? -35.696 -12.985 9.317   1.00 12.31 ? 572  ARG   B CD  1 
ATOM   8581 N  NE  . ARG   B 1 549 ? -34.719 -13.895 9.917   1.00 13.65 ? 572  ARG   B NE  1 
ATOM   8582 C  CZ  . ARG   B 1 549 ? -33.994 -14.819 9.274   1.00 14.60 ? 572  ARG   B CZ  1 
ATOM   8583 N  NH1 . ARG   B 1 549 ? -33.946 -14.864 7.955   1.00 14.90 ? 572  ARG   B NH1 1 
ATOM   8584 N  NH2 . ARG   B 1 549 ? -33.315 -15.708 9.961   1.00 13.92 ? 572  ARG   B NH2 1 
ATOM   8585 N  N   . GLU   B 1 550 ? -38.352 -16.912 8.040   1.00 13.60 ? 573  GLU   B N   1 
ATOM   8586 C  CA  . GLU   B 1 550 ? -37.965 -17.510 6.753   1.00 15.53 ? 573  GLU   B CA  1 
ATOM   8587 C  C   . GLU   B 1 550 ? -39.133 -18.198 6.058   1.00 15.49 ? 573  GLU   B C   1 
ATOM   8588 O  O   . GLU   B 1 550 ? -39.156 -18.230 4.834   1.00 14.61 ? 573  GLU   B O   1 
ATOM   8589 C  CB  . GLU   B 1 550 ? -36.822 -18.503 6.909   1.00 18.20 ? 573  GLU   B CB  1 
ATOM   8590 C  CG  . GLU   B 1 550 ? -35.549 -17.719 7.198   1.00 23.37 ? 573  GLU   B CG  1 
ATOM   8591 C  CD  . GLU   B 1 550 ? -34.279 -18.503 7.434   1.00 35.02 ? 573  GLU   B CD  1 
ATOM   8592 O  OE1 . GLU   B 1 550 ? -34.313 -19.569 8.089   1.00 39.37 ? 573  GLU   B OE1 1 
ATOM   8593 O  OE2 . GLU   B 1 550 ? -33.240 -17.951 6.997   1.00 41.93 ? 573  GLU   B OE2 1 
ATOM   8594 N  N   . VAL   B 1 551 ? -40.099 -18.713 6.804   1.00 13.12 ? 574  VAL   B N   1 
ATOM   8595 C  CA  . VAL   B 1 551 ? -41.133 -19.537 6.188   1.00 14.00 ? 574  VAL   B CA  1 
ATOM   8596 C  C   . VAL   B 1 551 ? -42.544 -18.994 6.450   1.00 13.43 ? 574  VAL   B C   1 
ATOM   8597 O  O   . VAL   B 1 551 ? -43.327 -18.723 5.512   1.00 13.61 ? 574  VAL   B O   1 
ATOM   8598 C  CB  . VAL   B 1 551 ? -40.965 -20.967 6.712   1.00 15.15 ? 574  VAL   B CB  1 
ATOM   8599 C  CG1 . VAL   B 1 551 ? -42.057 -21.872 6.179   1.00 16.18 ? 574  VAL   B CG1 1 
ATOM   8600 C  CG2 . VAL   B 1 551 ? -39.591 -21.545 6.377   1.00 15.90 ? 574  VAL   B CG2 1 
ATOM   8601 N  N   . ARG   B 1 552 ? -42.888 -18.780 7.737   1.00 13.37 ? 575  ARG   B N   1 
ATOM   8602 C  CA  . ARG   B 1 552 ? -44.281 -18.457 8.073   1.00 12.32 ? 575  ARG   B CA  1 
ATOM   8603 C  C   . ARG   B 1 552 ? -44.661 -17.037 7.636   1.00 11.90 ? 575  ARG   B C   1 
ATOM   8604 O  O   . ARG   B 1 552 ? -45.754 -16.810 7.110   1.00 12.27 ? 575  ARG   B O   1 
ATOM   8605 C  CB  . ARG   B 1 552 ? -44.651 -18.697 9.547   1.00 13.25 ? 575  ARG   B CB  1 
ATOM   8606 C  CG  . ARG   B 1 552 ? -44.406 -20.093 10.110  1.00 14.54 ? 575  ARG   B CG  1 
ATOM   8607 C  CD  . ARG   B 1 552 ? -44.851 -21.236 9.211   1.00 15.33 ? 575  ARG   B CD  1 
ATOM   8608 N  NE  . ARG   B 1 552 ? -46.176 -20.963 8.644   1.00 16.65 ? 575  ARG   B NE  1 
ATOM   8609 C  CZ  . ARG   B 1 552 ? -46.746 -21.634 7.643   1.00 18.20 ? 575  ARG   B CZ  1 
ATOM   8610 N  NH1 . ARG   B 1 552 ? -48.000 -21.377 7.298   1.00 17.06 ? 575  ARG   B NH1 1 
ATOM   8611 N  NH2 . ARG   B 1 552 ? -46.065 -22.607 7.047   1.00 19.42 ? 575  ARG   B NH2 1 
ATOM   8612 N  N   . MET   B 1 553 ? -43.806 -16.043 7.903   1.00 10.86 ? 576  MET   B N   1 
ATOM   8613 C  CA  . MET   B 1 553 ? -44.135 -14.660 7.587   1.00 11.97 ? 576  MET   B CA  1 
ATOM   8614 C  C   . MET   B 1 553 ? -44.291 -14.515 6.069   1.00 12.82 ? 576  MET   B C   1 
ATOM   8615 O  O   . MET   B 1 553 ? -45.290 -13.942 5.618   1.00 12.44 ? 576  MET   B O   1 
ATOM   8616 C  CB  . MET   B 1 553 ? -43.118 -13.698 8.246   1.00 12.49 ? 576  MET   B CB  1 
ATOM   8617 C  CG  . MET   B 1 553 ? -43.296 -12.223 7.902   1.00 13.93 ? 576  MET   B CG  1 
ATOM   8618 S  SD  . MET   B 1 553 ? -42.589 -11.784 6.299   1.00 15.79 ? 576  MET   B SD  1 
ATOM   8619 C  CE  . MET   B 1 553 ? -40.820 -11.760 6.656   1.00 16.13 ? 576  MET   B CE  1 
ATOM   8620 N  N   . PRO   B 1 554 ? -43.366 -15.008 5.208   1.00 12.93 ? 577  PRO   B N   1 
ATOM   8621 C  CA  . PRO   B 1 554 ? -43.601 -14.927 3.761   1.00 13.51 ? 577  PRO   B CA  1 
ATOM   8622 C  C   . PRO   B 1 554 ? -44.889 -15.638 3.301   1.00 13.68 ? 577  PRO   B C   1 
ATOM   8623 O  O   . PRO   B 1 554 ? -45.502 -15.191 2.345   1.00 14.01 ? 577  PRO   B O   1 
ATOM   8624 C  CB  . PRO   B 1 554 ? -42.339 -15.553 3.184   1.00 13.97 ? 577  PRO   B CB  1 
ATOM   8625 C  CG  . PRO   B 1 554 ? -41.280 -15.270 4.227   1.00 14.55 ? 577  PRO   B CG  1 
ATOM   8626 C  CD  . PRO   B 1 554 ? -42.031 -15.557 5.537   1.00 14.21 ? 577  PRO   B CD  1 
ATOM   8627 N  N   . ARG   B 1 555 ? -45.304 -16.710 3.997   1.00 13.24 ? 578  ARG   B N   1 
ATOM   8628 C  CA  . ARG   B 1 555 ? -46.524 -17.459 3.691   1.00 12.84 ? 578  ARG   B CA  1 
ATOM   8629 C  C   . ARG   B 1 555 ? -47.770 -16.690 4.165   1.00 12.73 ? 578  ARG   B C   1 
ATOM   8630 O  O   . ARG   B 1 555 ? -48.887 -17.095 3.845   1.00 12.93 ? 578  ARG   B O   1 
ATOM   8631 C  CB  . ARG   B 1 555 ? -46.396 -18.881 4.259   1.00 13.57 ? 578  ARG   B CB  1 
ATOM   8632 C  CG  . ARG   B 1 555 ? -47.633 -19.771 4.160   1.00 15.22 ? 578  ARG   B CG  1 
ATOM   8633 C  CD  . ARG   B 1 555 ? -48.012 -19.966 2.703   1.00 15.89 ? 578  ARG   B CD  1 
ATOM   8634 N  NE  . ARG   B 1 555 ? -49.251 -20.748 2.542   1.00 16.77 ? 578  ARG   B NE  1 
ATOM   8635 C  CZ  . ARG   B 1 555 ? -50.487 -20.253 2.523   1.00 15.83 ? 578  ARG   B CZ  1 
ATOM   8636 N  NH1 . ARG   B 1 555 ? -50.714 -18.950 2.730   1.00 14.64 ? 578  ARG   B NH1 1 
ATOM   8637 N  NH2 . ARG   B 1 555 ? -51.490 -21.097 2.315   1.00 16.28 ? 578  ARG   B NH2 1 
ATOM   8638 N  N   . GLY   B 1 556 ? -47.581 -15.612 4.952   1.00 12.09 ? 579  GLY   B N   1 
ATOM   8639 C  CA  . GLY   B 1 556 ? -48.666 -14.715 5.338   1.00 11.44 ? 579  GLY   B CA  1 
ATOM   8640 C  C   . GLY   B 1 556 ? -48.913 -14.565 6.844   1.00 11.13 ? 579  GLY   B C   1 
ATOM   8641 O  O   . GLY   B 1 556 ? -49.891 -13.932 7.234   1.00 11.27 ? 579  GLY   B O   1 
ATOM   8642 N  N   . LEU   B 1 557 ? -48.058 -15.116 7.711   1.00 10.27 ? 580  LEU   B N   1 
ATOM   8643 C  CA  . LEU   B 1 557 ? -48.155 -14.827 9.138   1.00 10.45 ? 580  LEU   B CA  1 
ATOM   8644 C  C   . LEU   B 1 557 ? -47.718 -13.377 9.374   1.00 10.62 ? 580  LEU   B C   1 
ATOM   8645 O  O   . LEU   B 1 557 ? -46.697 -12.935 8.851   1.00 11.32 ? 580  LEU   B O   1 
ATOM   8646 C  CB  . LEU   B 1 557 ? -47.331 -15.803 9.980   1.00 9.83  ? 580  LEU   B CB  1 
ATOM   8647 C  CG  . LEU   B 1 557 ? -47.553 -15.759 11.501  1.00 10.21 ? 580  LEU   B CG  1 
ATOM   8648 C  CD1 . LEU   B 1 557 ? -48.944 -16.248 11.833  1.00 10.22 ? 580  LEU   B CD1 1 
ATOM   8649 C  CD2 . LEU   B 1 557 ? -46.525 -16.589 12.235  1.00 11.25 ? 580  LEU   B CD2 1 
ATOM   8650 N  N   . SER   B 1 558 ? -48.473 -12.657 10.196  1.00 10.11 ? 581  SER   B N   1 
ATOM   8651 C  CA  . SER   B 1 558 ? -48.289 -11.220 10.384  1.00 9.61  ? 581  SER   B CA  1 
ATOM   8652 C  C   . SER   B 1 558 ? -47.961 -10.813 11.821  1.00 10.08 ? 581  SER   B C   1 
ATOM   8653 O  O   . SER   B 1 558 ? -47.526 -9.674  12.023  1.00 9.93  ? 581  SER   B O   1 
ATOM   8654 C  CB  . SER   B 1 558 ? -49.522 -10.468 9.950   1.00 9.80  ? 581  SER   B CB  1 
ATOM   8655 O  OG  . SER   B 1 558 ? -49.674 -10.507 8.538   1.00 10.07 ? 581  SER   B OG  1 
ATOM   8656 N  N   . ALA   B 1 559 ? -48.128 -11.728 12.780  1.00 10.45 ? 582  ALA   B N   1 
ATOM   8657 C  CA  . ALA   B 1 559 ? -47.777 -11.463 14.165  1.00 10.11 ? 582  ALA   B CA  1 
ATOM   8658 C  C   . ALA   B 1 559 ? -47.604 -12.774 14.919  1.00 9.61  ? 582  ALA   B C   1 
ATOM   8659 O  O   . ALA   B 1 559 ? -48.184 -13.812 14.547  1.00 9.00  ? 582  ALA   B O   1 
ATOM   8660 C  CB  . ALA   B 1 559 ? -48.828 -10.619 14.803  1.00 10.90 ? 582  ALA   B CB  1 
ATOM   8661 N  N   . SER   B 1 560 ? -46.816 -12.689 16.004  1.00 8.28  ? 583  SER   B N   1 
ATOM   8662 C  CA  . SER   B 1 560 ? -46.595 -13.814 16.892  1.00 8.56  ? 583  SER   B CA  1 
ATOM   8663 C  C   . SER   B 1 560 ? -46.481 -13.322 18.327  1.00 8.49  ? 583  SER   B C   1 
ATOM   8664 O  O   . SER   B 1 560 ? -45.967 -12.246 18.589  1.00 8.59  ? 583  SER   B O   1 
ATOM   8665 C  CB  . SER   B 1 560 ? -45.372 -14.616 16.513  1.00 9.06  ? 583  SER   B CB  1 
ATOM   8666 O  OG  . SER   B 1 560 ? -44.194 -13.820 16.553  1.00 9.85  ? 583  SER   B OG  1 
ATOM   8667 N  N   . VAL   B 1 561 ? -46.954 -14.149 19.245  1.00 8.84  ? 584  VAL   B N   1 
ATOM   8668 C  CA  . VAL   B 1 561 ? -46.966 -13.824 20.646  1.00 8.77  ? 584  VAL   B CA  1 
ATOM   8669 C  C   . VAL   B 1 561 ? -46.259 -14.938 21.421  1.00 9.45  ? 584  VAL   B C   1 
ATOM   8670 O  O   . VAL   B 1 561 ? -46.807 -16.035 21.563  1.00 9.42  ? 584  VAL   B O   1 
ATOM   8671 C  CB  . VAL   B 1 561 ? -48.433 -13.705 21.090  1.00 8.96  ? 584  VAL   B CB  1 
ATOM   8672 C  CG1 . VAL   B 1 561 ? -48.505 -13.538 22.593  1.00 8.51  ? 584  VAL   B CG1 1 
ATOM   8673 C  CG2 . VAL   B 1 561 ? -49.154 -12.539 20.426  1.00 8.94  ? 584  VAL   B CG2 1 
ATOM   8674 N  N   . TYR   B 1 562 ? -45.014 -14.666 21.846  1.00 9.86  ? 585  TYR   B N   1 
ATOM   8675 C  CA  . TYR   B 1 562 ? -44.204 -15.624 22.559  1.00 9.85  ? 585  TYR   B CA  1 
ATOM   8676 C  C   . TYR   B 1 562 ? -44.616 -15.714 24.037  1.00 9.91  ? 585  TYR   B C   1 
ATOM   8677 O  O   . TYR   B 1 562 ? -44.508 -14.747 24.776  1.00 10.94 ? 585  TYR   B O   1 
ATOM   8678 C  CB  . TYR   B 1 562 ? -42.712 -15.260 22.430  1.00 9.90  ? 585  TYR   B CB  1 
ATOM   8679 C  CG  . TYR   B 1 562 ? -41.880 -16.327 23.110  1.00 10.16 ? 585  TYR   B CG  1 
ATOM   8680 C  CD1 . TYR   B 1 562 ? -41.576 -17.514 22.430  1.00 10.80 ? 585  TYR   B CD1 1 
ATOM   8681 C  CD2 . TYR   B 1 562 ? -41.507 -16.201 24.440  1.00 10.53 ? 585  TYR   B CD2 1 
ATOM   8682 C  CE1 . TYR   B 1 562 ? -40.916 -18.537 23.091  1.00 11.96 ? 585  TYR   B CE1 1 
ATOM   8683 C  CE2 . TYR   B 1 562 ? -40.840 -17.221 25.102  1.00 11.54 ? 585  TYR   B CE2 1 
ATOM   8684 C  CZ  . TYR   B 1 562 ? -40.556 -18.394 24.419  1.00 11.65 ? 585  TYR   B CZ  1 
ATOM   8685 O  OH  . TYR   B 1 562 ? -39.888 -19.421 25.010  1.00 13.90 ? 585  TYR   B OH  1 
ATOM   8686 N  N   . THR   B 1 563 ? -44.970 -16.911 24.503  1.00 9.68  ? 586  THR   B N   1 
ATOM   8687 C  CA  . THR   B 1 563 ? -45.222 -17.142 25.915  1.00 11.02 ? 586  THR   B CA  1 
ATOM   8688 C  C   . THR   B 1 563 ? -43.925 -17.492 26.647  1.00 10.30 ? 586  THR   B C   1 
ATOM   8689 O  O   . THR   B 1 563 ? -43.391 -18.575 26.424  1.00 10.85 ? 586  THR   B O   1 
ATOM   8690 C  CB  . THR   B 1 563 ? -46.219 -18.302 26.032  1.00 11.57 ? 586  THR   B CB  1 
ATOM   8691 O  OG1 . THR   B 1 563 ? -47.387 -17.941 25.289  1.00 11.84 ? 586  THR   B OG1 1 
ATOM   8692 C  CG2 . THR   B 1 563 ? -46.621 -18.583 27.464  1.00 11.98 ? 586  THR   B CG2 1 
ATOM   8693 N  N   . GLU   B 1 564 ? -43.437 -16.619 27.536  1.00 11.06 ? 587  GLU   B N   1 
ATOM   8694 C  CA  . GLU   B 1 564 ? -44.053 -15.369 27.963  1.00 10.83 ? 587  GLU   B CA  1 
ATOM   8695 C  C   . GLU   B 1 564 ? -42.932 -14.477 28.497  1.00 10.21 ? 587  GLU   B C   1 
ATOM   8696 O  O   . GLU   B 1 564 ? -41.791 -14.932 28.566  1.00 10.49 ? 587  GLU   B O   1 
ATOM   8697 C  CB  . GLU   B 1 564 ? -45.137 -15.606 29.011  1.00 11.92 ? 587  GLU   B CB  1 
ATOM   8698 C  CG  . GLU   B 1 564 ? -44.650 -16.378 30.251  1.00 11.40 ? 587  GLU   B CG  1 
ATOM   8699 C  CD  . GLU   B 1 564 ? -45.748 -16.579 31.275  1.00 11.90 ? 587  GLU   B CD  1 
ATOM   8700 O  OE1 . GLU   B 1 564 ? -46.371 -15.583 31.662  1.00 10.34 ? 587  GLU   B OE1 1 
ATOM   8701 O  OE2 . GLU   B 1 564 ? -45.966 -17.749 31.666  1.00 12.25 ? 587  GLU   B OE2 1 
ATOM   8702 N  N   . ILE   B 1 565 ? -43.227 -13.224 28.851  1.00 9.98  ? 588  ILE   B N   1 
ATOM   8703 C  CA  . ILE   B 1 565 ? -42.168 -12.325 29.273  1.00 10.54 ? 588  ILE   B CA  1 
ATOM   8704 C  C   . ILE   B 1 565 ? -41.561 -12.771 30.618  1.00 11.68 ? 588  ILE   B C   1 
ATOM   8705 O  O   . ILE   B 1 565 ? -40.342 -12.767 30.736  1.00 11.41 ? 588  ILE   B O   1 
ATOM   8706 C  CB  . ILE   B 1 565 ? -42.641 -10.864 29.286  1.00 10.73 ? 588  ILE   B CB  1 
ATOM   8707 C  CG1 . ILE   B 1 565 ? -41.491 -9.899  29.570  1.00 11.11 ? 588  ILE   B CG1 1 
ATOM   8708 C  CG2 . ILE   B 1 565 ? -43.801 -10.636 30.267  1.00 10.78 ? 588  ILE   B CG2 1 
ATOM   8709 C  CD1 . ILE   B 1 565 ? -40.438 -9.841  28.494  1.00 11.97 ? 588  ILE   B CD1 1 
ATOM   8710 N  N   . THR   B 1 566 ? -42.379 -13.099 31.636  1.00 12.98 ? 589  THR   B N   1 
ATOM   8711 C  CA  . THR   B 1 566 ? -41.839 -13.585 32.907  1.00 14.03 ? 589  THR   B CA  1 
ATOM   8712 C  C   . THR   B 1 566 ? -42.471 -14.920 33.266  1.00 15.05 ? 589  THR   B C   1 
ATOM   8713 O  O   . THR   B 1 566 ? -43.610 -15.204 32.901  1.00 15.69 ? 589  THR   B O   1 
ATOM   8714 C  CB  . THR   B 1 566 ? -42.077 -12.597 34.057  1.00 16.12 ? 589  THR   B CB  1 
ATOM   8715 O  OG1 . THR   B 1 566 ? -43.422 -12.720 34.518  1.00 15.50 ? 589  THR   B OG1 1 
ATOM   8716 C  CG2 . THR   B 1 566 ? -41.801 -11.156 33.678  1.00 15.08 ? 589  THR   B CG2 1 
ATOM   8717 N  N   . ASP   B 1 567 ? -41.741 -15.727 34.035  1.00 13.63 ? 590  ASP   B N   1 
ATOM   8718 C  CA  . ASP   B 1 567 ? -42.354 -16.789 34.800  1.00 14.01 ? 590  ASP   B CA  1 
ATOM   8719 C  C   . ASP   B 1 567 ? -43.549 -16.214 35.550  1.00 12.19 ? 590  ASP   B C   1 
ATOM   8720 O  O   . ASP   B 1 567 ? -43.528 -15.064 36.001  1.00 13.96 ? 590  ASP   B O   1 
ATOM   8721 C  CB  . ASP   B 1 567 ? -41.329 -17.385 35.752  1.00 15.08 ? 590  ASP   B CB  1 
ATOM   8722 C  CG  . ASP   B 1 567 ? -40.165 -18.135 35.119  1.00 15.87 ? 590  ASP   B CG  1 
ATOM   8723 O  OD1 . ASP   B 1 567 ? -40.222 -18.481 33.898  1.00 12.81 ? 590  ASP   B OD1 1 
ATOM   8724 O  OD2 . ASP   B 1 567 ? -39.194 -18.395 35.877  1.00 19.34 ? 590  ASP   B OD2 1 
ATOM   8725 N  N   . VAL   B 1 568 ? -44.571 -17.053 35.770  1.00 12.70 ? 591  VAL   B N   1 
ATOM   8726 C  CA  . VAL   B 1 568 ? -45.634 -16.665 36.673  1.00 13.31 ? 591  VAL   B CA  1 
ATOM   8727 C  C   . VAL   B 1 568 ? -45.978 -17.886 37.542  1.00 14.33 ? 591  VAL   B C   1 
ATOM   8728 O  O   . VAL   B 1 568 ? -46.313 -18.951 37.038  1.00 14.43 ? 591  VAL   B O   1 
ATOM   8729 C  CB  . VAL   B 1 568 ? -46.891 -16.088 35.993  1.00 13.22 ? 591  VAL   B CB  1 
ATOM   8730 C  CG1 . VAL   B 1 568 ? -47.938 -15.737 37.039  1.00 12.90 ? 591  VAL   B CG1 1 
ATOM   8731 C  CG2 . VAL   B 1 568 ? -46.608 -14.881 35.107  1.00 12.38 ? 591  VAL   B CG2 1 
ATOM   8732 N  N   . GLU   B 1 569 ? -45.814 -17.741 38.854  1.00 16.98 ? 592  GLU   B N   1 
ATOM   8733 C  CA  . GLU   B 1 569 ? -45.980 -18.880 39.760  1.00 16.54 ? 592  GLU   B CA  1 
ATOM   8734 C  C   . GLU   B 1 569 ? -45.109 -20.054 39.306  1.00 15.98 ? 592  GLU   B C   1 
ATOM   8735 O  O   . GLU   B 1 569 ? -43.893 -19.855 39.197  1.00 17.91 ? 592  GLU   B O   1 
ATOM   8736 C  CB  . GLU   B 1 569 ? -47.470 -19.026 40.092  1.00 16.85 ? 592  GLU   B CB  1 
ATOM   8737 C  CG  . GLU   B 1 569 ? -47.989 -17.843 40.901  1.00 16.85 ? 592  GLU   B CG  1 
ATOM   8738 C  CD  . GLU   B 1 569 ? -49.371 -17.898 41.552  1.00 17.11 ? 592  GLU   B CD  1 
ATOM   8739 O  OE1 . GLU   B 1 569 ? -49.818 -16.849 42.074  1.00 16.61 ? 592  GLU   B OE1 1 
ATOM   8740 O  OE2 . GLU   B 1 569 ? -49.981 -18.970 41.467  1.00 16.12 ? 592  GLU   B OE2 1 
ATOM   8741 N  N   . ASN   B 1 570 ? -45.687 -21.241 39.046  1.00 15.78 ? 593  ASN   B N   1 
ATOM   8742 C  CA  . ASN   B 1 570 ? -44.958 -22.424 38.626  1.00 17.19 ? 593  ASN   B CA  1 
ATOM   8743 C  C   . ASN   B 1 570 ? -44.929 -22.591 37.115  1.00 15.55 ? 593  ASN   B C   1 
ATOM   8744 O  O   . ASN   B 1 570 ? -44.452 -23.611 36.610  1.00 16.67 ? 593  ASN   B O   1 
ATOM   8745 C  CB  . ASN   B 1 570 ? -45.477 -23.691 39.300  1.00 18.39 ? 593  ASN   B CB  1 
ATOM   8746 C  CG  . ASN   B 1 570 ? -45.112 -23.705 40.765  1.00 21.59 ? 593  ASN   B CG  1 
ATOM   8747 O  OD1 . ASN   B 1 570 ? -43.966 -23.391 41.117  1.00 20.15 ? 593  ASN   B OD1 1 
ATOM   8748 N  ND2 . ASN   B 1 570 ? -46.087 -23.945 41.632  1.00 22.33 ? 593  ASN   B ND2 1 
ATOM   8749 N  N   . GLU   B 1 571 ? -45.393 -21.570 36.372  1.00 14.77 ? 594  GLU   B N   1 
ATOM   8750 C  CA  . GLU   B 1 571 ? -45.243 -21.610 34.935  1.00 14.79 ? 594  GLU   B CA  1 
ATOM   8751 C  C   . GLU   B 1 571 ? -43.918 -20.905 34.606  1.00 13.94 ? 594  GLU   B C   1 
ATOM   8752 O  O   . GLU   B 1 571 ? -43.851 -19.678 34.616  1.00 14.39 ? 594  GLU   B O   1 
ATOM   8753 C  CB  . GLU   B 1 571 ? -46.417 -20.944 34.220  1.00 14.35 ? 594  GLU   B CB  1 
ATOM   8754 C  CG  . GLU   B 1 571 ? -46.365 -21.176 32.714  1.00 13.75 ? 594  GLU   B CG  1 
ATOM   8755 C  CD  . GLU   B 1 571 ? -47.634 -20.826 31.920  1.00 15.11 ? 594  GLU   B CD  1 
ATOM   8756 O  OE1 . GLU   B 1 571 ? -48.649 -20.373 32.523  1.00 15.96 ? 594  GLU   B OE1 1 
ATOM   8757 O  OE2 . GLU   B 1 571 ? -47.588 -20.999 30.678  1.00 15.67 ? 594  GLU   B OE2 1 
ATOM   8758 N  N   . VAL   B 1 572 ? -42.888 -21.701 34.330  1.00 15.41 ? 595  VAL   B N   1 
ATOM   8759 C  CA  . VAL   B 1 572 ? -41.514 -21.224 34.286  1.00 15.75 ? 595  VAL   B CA  1 
ATOM   8760 C  C   . VAL   B 1 572 ? -41.041 -21.086 32.835  1.00 15.98 ? 595  VAL   B C   1 
ATOM   8761 O  O   . VAL   B 1 572 ? -39.947 -21.509 32.455  1.00 16.39 ? 595  VAL   B O   1 
ATOM   8762 C  CB  . VAL   B 1 572 ? -40.592 -22.132 35.131  1.00 17.32 ? 595  VAL   B CB  1 
ATOM   8763 C  CG1 . VAL   B 1 572 ? -40.906 -21.961 36.612  1.00 18.08 ? 595  VAL   B CG1 1 
ATOM   8764 C  CG2 . VAL   B 1 572 ? -40.593 -23.579 34.685  1.00 16.31 ? 595  VAL   B CG2 1 
ATOM   8765 N  N   . ASN   B 1 573 ? -41.884 -20.443 32.013  1.00 12.79 ? 596  ASN   B N   1 
ATOM   8766 C  CA  . ASN   B 1 573 ? -41.523 -20.186 30.635  1.00 12.92 ? 596  ASN   B CA  1 
ATOM   8767 C  C   . ASN   B 1 573 ? -41.367 -18.699 30.321  1.00 13.12 ? 596  ASN   B C   1 
ATOM   8768 O  O   . ASN   B 1 573 ? -41.442 -18.328 29.140  1.00 13.83 ? 596  ASN   B O   1 
ATOM   8769 C  CB  . ASN   B 1 573 ? -42.536 -20.835 29.706  1.00 12.78 ? 596  ASN   B CB  1 
ATOM   8770 C  CG  . ASN   B 1 573 ? -43.969 -20.466 30.039  1.00 12.41 ? 596  ASN   B CG  1 
ATOM   8771 O  OD1 . ASN   B 1 573 ? -44.220 -19.473 30.715  1.00 12.26 ? 596  ASN   B OD1 1 
ATOM   8772 N  ND2 . ASN   B 1 573 ? -44.925 -21.277 29.608  1.00 13.25 ? 596  ASN   B ND2 1 
ATOM   8773 N  N   . GLY   B 1 574 ? -41.089 -17.871 31.336  1.00 12.35 ? 597  GLY   B N   1 
ATOM   8774 C  CA  . GLY   B 1 574 ? -40.605 -16.517 31.118  1.00 12.98 ? 597  GLY   B CA  1 
ATOM   8775 C  C   . GLY   B 1 574 ? -39.232 -16.483 30.430  1.00 13.76 ? 597  GLY   B C   1 
ATOM   8776 O  O   . GLY   B 1 574 ? -38.391 -17.392 30.629  1.00 14.32 ? 597  GLY   B O   1 
ATOM   8777 N  N   . LEU   B 1 575 ? -39.050 -15.451 29.584  1.00 13.30 ? 598  LEU   B N   1 
ATOM   8778 C  CA  . LEU   B 1 575 ? -37.725 -14.942 29.245  1.00 12.37 ? 598  LEU   B CA  1 
ATOM   8779 C  C   . LEU   B 1 575 ? -37.000 -14.446 30.502  1.00 14.11 ? 598  LEU   B C   1 
ATOM   8780 O  O   . LEU   B 1 575 ? -35.763 -14.492 30.562  1.00 15.06 ? 598  LEU   B O   1 
ATOM   8781 C  CB  . LEU   B 1 575 ? -37.829 -13.879 28.147  1.00 11.32 ? 598  LEU   B CB  1 
ATOM   8782 C  CG  . LEU   B 1 575 ? -38.555 -14.363 26.886  1.00 11.62 ? 598  LEU   B CG  1 
ATOM   8783 C  CD1 . LEU   B 1 575 ? -38.817 -13.136 26.011  1.00 12.19 ? 598  LEU   B CD1 1 
ATOM   8784 C  CD2 . LEU   B 1 575 ? -37.853 -15.479 26.093  1.00 10.36 ? 598  LEU   B CD2 1 
ATOM   8785 N  N   . LEU   B 1 576 ? -37.773 -13.970 31.474  1.00 13.87 ? 599  LEU   B N   1 
ATOM   8786 C  CA  . LEU   B 1 576 ? -37.297 -13.484 32.767  1.00 15.28 ? 599  LEU   B CA  1 
ATOM   8787 C  C   . LEU   B 1 576 ? -37.925 -14.351 33.855  1.00 14.53 ? 599  LEU   B C   1 
ATOM   8788 O  O   . LEU   B 1 576 ? -38.988 -14.935 33.659  1.00 12.88 ? 599  LEU   B O   1 
ATOM   8789 C  CB  . LEU   B 1 576 ? -37.705 -12.034 33.000  1.00 16.60 ? 599  LEU   B CB  1 
ATOM   8790 C  CG  . LEU   B 1 576 ? -36.832 -10.959 32.353  1.00 19.12 ? 599  LEU   B CG  1 
ATOM   8791 C  CD1 . LEU   B 1 576 ? -37.017 -10.922 30.868  1.00 18.32 ? 599  LEU   B CD1 1 
ATOM   8792 C  CD2 . LEU   B 1 576 ? -37.120 -9.602  32.970  1.00 19.68 ? 599  LEU   B CD2 1 
ATOM   8793 N  N   . THR   B 1 577 ? -37.248 -14.415 35.007  1.00 15.96 ? 600  THR   B N   1 
ATOM   8794 C  CA  . THR   B 1 577 ? -37.818 -15.034 36.193  1.00 14.63 ? 600  THR   B CA  1 
ATOM   8795 C  C   . THR   B 1 577 ? -38.935 -14.139 36.730  1.00 14.28 ? 600  THR   B C   1 
ATOM   8796 O  O   . THR   B 1 577 ? -39.067 -12.958 36.388  1.00 14.28 ? 600  THR   B O   1 
ATOM   8797 C  CB  . THR   B 1 577 ? -36.689 -15.321 37.197  1.00 13.70 ? 600  THR   B CB  1 
ATOM   8798 O  OG1 . THR   B 1 577 ? -35.964 -14.123 37.497  1.00 13.36 ? 600  THR   B OG1 1 
ATOM   8799 C  CG2 . THR   B 1 577 ? -35.765 -16.365 36.633  1.00 13.80 ? 600  THR   B CG2 1 
ATOM   8800 N  N   . TYR   B 1 578 ? -39.764 -14.702 37.610  1.00 17.07 ? 601  TYR   B N   1 
ATOM   8801 C  CA  . TYR   B 1 578 ? -40.969 -14.032 38.079  1.00 16.06 ? 601  TYR   B CA  1 
ATOM   8802 C  C   . TYR   B 1 578 ? -40.637 -12.824 38.952  1.00 16.26 ? 601  TYR   B C   1 
ATOM   8803 O  O   . TYR   B 1 578 ? -41.450 -11.906 39.078  1.00 15.61 ? 601  TYR   B O   1 
ATOM   8804 C  CB  . TYR   B 1 578 ? -41.803 -15.085 38.826  1.00 18.07 ? 601  TYR   B CB  1 
ATOM   8805 C  CG  . TYR   B 1 578 ? -43.203 -14.675 39.269  1.00 16.78 ? 601  TYR   B CG  1 
ATOM   8806 C  CD1 . TYR   B 1 578 ? -43.944 -13.747 38.561  1.00 17.60 ? 601  TYR   B CD1 1 
ATOM   8807 C  CD2 . TYR   B 1 578 ? -43.783 -15.232 40.410  1.00 19.59 ? 601  TYR   B CD2 1 
ATOM   8808 C  CE1 . TYR   B 1 578 ? -45.215 -13.359 38.951  1.00 17.47 ? 601  TYR   B CE1 1 
ATOM   8809 C  CE2 . TYR   B 1 578 ? -45.072 -14.880 40.800  1.00 17.68 ? 601  TYR   B CE2 1 
ATOM   8810 C  CZ  . TYR   B 1 578 ? -45.799 -13.963 40.048  1.00 18.44 ? 601  TYR   B CZ  1 
ATOM   8811 O  OH  . TYR   B 1 578 ? -47.045 -13.552 40.415  1.00 14.96 ? 601  TYR   B OH  1 
ATOM   8812 N  N   . ASP   B 1 579 ? -39.449 -12.838 39.590  1.00 16.82 ? 602  ASP   B N   1 
ATOM   8813 C  CA  . ASP   B 1 579 ? -39.001 -11.725 40.421  1.00 17.25 ? 602  ASP   B CA  1 
ATOM   8814 C  C   . ASP   B 1 579 ? -38.273 -10.653 39.602  1.00 16.14 ? 602  ASP   B C   1 
ATOM   8815 O  O   . ASP   B 1 579 ? -37.840 -9.630  40.136  1.00 15.76 ? 602  ASP   B O   1 
ATOM   8816 C  CB  . ASP   B 1 579 ? -38.084 -12.186 41.543  1.00 18.25 ? 602  ASP   B CB  1 
ATOM   8817 C  CG  . ASP   B 1 579 ? -36.871 -13.005 41.112  1.00 21.21 ? 602  ASP   B CG  1 
ATOM   8818 O  OD1 . ASP   B 1 579 ? -36.642 -13.192 39.888  1.00 17.10 ? 602  ASP   B OD1 1 
ATOM   8819 O  OD2 . ASP   B 1 579 ? -36.186 -13.532 42.014  1.00 22.81 ? 602  ASP   B OD2 1 
ATOM   8820 N  N   . ARG   B 1 580 ? -38.194 -10.859 38.280  1.00 15.24 ? 603  ARG   B N   1 
ATOM   8821 C  CA  . ARG   B 1 580 ? -37.560 -9.914  37.368  1.00 14.15 ? 603  ARG   B CA  1 
ATOM   8822 C  C   . ARG   B 1 580 ? -36.053 -9.782  37.620  1.00 16.39 ? 603  ARG   B C   1 
ATOM   8823 O  O   . ARG   B 1 580 ? -35.424 -8.872  37.063  1.00 15.81 ? 603  ARG   B O   1 
ATOM   8824 C  CB  . ARG   B 1 580 ? -38.197 -8.533  37.341  1.00 14.40 ? 603  ARG   B CB  1 
ATOM   8825 C  CG  . ARG   B 1 580 ? -39.469 -8.394  36.512  1.00 14.39 ? 603  ARG   B CG  1 
ATOM   8826 C  CD  . ARG   B 1 580 ? -40.671 -9.126  37.091  1.00 14.96 ? 603  ARG   B CD  1 
ATOM   8827 N  NE  . ARG   B 1 580 ? -41.928 -8.733  36.448  1.00 15.54 ? 603  ARG   B NE  1 
ATOM   8828 C  CZ  . ARG   B 1 580 ? -43.151 -9.218  36.752  1.00 14.53 ? 603  ARG   B CZ  1 
ATOM   8829 N  NH1 . ARG   B 1 580 ? -43.280 -10.181 37.646  1.00 13.82 ? 603  ARG   B NH1 1 
ATOM   8830 N  NH2 . ARG   B 1 580 ? -44.214 -8.729  36.150  1.00 13.87 ? 603  ARG   B NH2 1 
ATOM   8831 N  N   . GLN   B 1 581 ? -35.483 -10.746 38.362  1.00 17.46 ? 604  GLN   B N   1 
ATOM   8832 C  CA  . GLN   B 1 581 ? -34.084 -10.707 38.782  1.00 18.42 ? 604  GLN   B CA  1 
ATOM   8833 C  C   . GLN   B 1 581 ? -33.149 -11.213 37.684  1.00 20.11 ? 604  GLN   B C   1 
ATOM   8834 O  O   . GLN   B 1 581 ? -32.003 -10.754 37.604  1.00 19.40 ? 604  GLN   B O   1 
ATOM   8835 C  CB  . GLN   B 1 581 ? -33.883 -11.513 40.070  1.00 19.80 ? 604  GLN   B CB  1 
ATOM   8836 C  CG  . GLN   B 1 581 ? -34.458 -10.837 41.317  1.00 19.95 ? 604  GLN   B CG  1 
ATOM   8837 C  CD  . GLN   B 1 581 ? -33.798 -9.529  41.707  1.00 22.24 ? 604  GLN   B CD  1 
ATOM   8838 O  OE1 . GLN   B 1 581 ? -32.846 -9.049  41.085  1.00 22.67 ? 604  GLN   B OE1 1 
ATOM   8839 N  NE2 . GLN   B 1 581 ? -34.303 -8.916  42.765  1.00 23.00 ? 604  GLN   B NE2 1 
ATOM   8840 N  N   . VAL   B 1 582 ? -33.610 -12.183 36.879  1.00 17.09 ? 605  VAL   B N   1 
ATOM   8841 C  CA  . VAL   B 1 582 ? -32.747 -12.865 35.932  1.00 16.51 ? 605  VAL   B CA  1 
ATOM   8842 C  C   . VAL   B 1 582 ? -33.399 -12.886 34.560  1.00 15.80 ? 605  VAL   B C   1 
ATOM   8843 O  O   . VAL   B 1 582 ? -34.542 -13.326 34.442  1.00 16.23 ? 605  VAL   B O   1 
ATOM   8844 C  CB  . VAL   B 1 582 ? -32.475 -14.306 36.375  1.00 15.77 ? 605  VAL   B CB  1 
ATOM   8845 C  CG1 . VAL   B 1 582 ? -31.733 -15.063 35.313  1.00 16.62 ? 605  VAL   B CG1 1 
ATOM   8846 C  CG2 . VAL   B 1 582 ? -31.694 -14.350 37.682  1.00 16.82 ? 605  VAL   B CG2 1 
ATOM   8847 N  N   . VAL   B 1 583 ? -32.670 -12.391 33.557  1.00 13.92 ? 606  VAL   B N   1 
ATOM   8848 C  CA  . VAL   B 1 583 ? -32.990 -12.626 32.161  1.00 14.30 ? 606  VAL   B CA  1 
ATOM   8849 C  C   . VAL   B 1 583 ? -32.341 -13.942 31.783  1.00 14.71 ? 606  VAL   B C   1 
ATOM   8850 O  O   . VAL   B 1 583 ? -31.120 -14.024 31.805  1.00 15.77 ? 606  VAL   B O   1 
ATOM   8851 C  CB  . VAL   B 1 583 ? -32.473 -11.484 31.260  1.00 12.67 ? 606  VAL   B CB  1 
ATOM   8852 C  CG1 . VAL   B 1 583 ? -32.758 -11.759 29.797  1.00 13.46 ? 606  VAL   B CG1 1 
ATOM   8853 C  CG2 . VAL   B 1 583 ? -33.032 -10.127 31.651  1.00 13.06 ? 606  VAL   B CG2 1 
ATOM   8854 N  N   . LYS   B 1 584 ? -33.143 -14.974 31.488  1.00 13.24 ? 607  LYS   B N   1 
ATOM   8855 C  CA  . LYS   B 1 584 ? -32.616 -16.307 31.276  1.00 13.61 ? 607  LYS   B CA  1 
ATOM   8856 C  C   . LYS   B 1 584 ? -31.904 -16.395 29.939  1.00 13.97 ? 607  LYS   B C   1 
ATOM   8857 O  O   . LYS   B 1 584 ? -30.985 -17.193 29.786  1.00 16.22 ? 607  LYS   B O   1 
ATOM   8858 C  CB  . LYS   B 1 584 ? -33.746 -17.337 31.215  1.00 13.55 ? 607  LYS   B CB  1 
ATOM   8859 C  CG  . LYS   B 1 584 ? -34.649 -17.345 32.445  1.00 13.44 ? 607  LYS   B CG  1 
ATOM   8860 C  CD  . LYS   B 1 584 ? -35.685 -18.469 32.309  1.00 13.98 ? 607  LYS   B CD  1 
ATOM   8861 C  CE  . LYS   B 1 584 ? -36.848 -18.371 33.275  1.00 12.82 ? 607  LYS   B CE  1 
ATOM   8862 N  NZ  . LYS   B 1 584 ? -37.822 -19.448 33.036  1.00 13.05 ? 607  LYS   B NZ  1 
ATOM   8863 N  N   . VAL   B 1 585 ? -32.345 -15.593 28.966  1.00 12.26 ? 608  VAL   B N   1 
ATOM   8864 C  CA  . VAL   B 1 585 ? -31.991 -15.813 27.577  1.00 11.93 ? 608  VAL   B CA  1 
ATOM   8865 C  C   . VAL   B 1 585 ? -30.814 -14.926 27.213  1.00 11.44 ? 608  VAL   B C   1 
ATOM   8866 O  O   . VAL   B 1 585 ? -30.487 -13.974 27.907  1.00 11.50 ? 608  VAL   B O   1 
ATOM   8867 C  CB  . VAL   B 1 585 ? -33.134 -15.576 26.560  1.00 12.22 ? 608  VAL   B CB  1 
ATOM   8868 C  CG1 . VAL   B 1 585 ? -34.193 -16.657 26.642  1.00 12.54 ? 608  VAL   B CG1 1 
ATOM   8869 C  CG2 . VAL   B 1 585 ? -33.793 -14.215 26.698  1.00 12.21 ? 608  VAL   B CG2 1 
ATOM   8870 N  N   . ASP   B 1 586 ? -30.191 -15.264 26.091  1.00 11.12 ? 609  ASP   B N   1 
ATOM   8871 C  CA  . ASP   B 1 586 ? -29.156 -14.450 25.479  1.00 10.74 ? 609  ASP   B CA  1 
ATOM   8872 C  C   . ASP   B 1 586 ? -29.855 -13.259 24.815  1.00 10.74 ? 609  ASP   B C   1 
ATOM   8873 O  O   . ASP   B 1 586 ? -30.266 -13.348 23.659  1.00 10.76 ? 609  ASP   B O   1 
ATOM   8874 C  CB  . ASP   B 1 586 ? -28.357 -15.335 24.543  1.00 12.00 ? 609  ASP   B CB  1 
ATOM   8875 C  CG  . ASP   B 1 586 ? -27.208 -14.694 23.783  1.00 12.46 ? 609  ASP   B CG  1 
ATOM   8876 O  OD1 . ASP   B 1 586 ? -26.977 -13.471 23.997  1.00 14.94 ? 609  ASP   B OD1 1 
ATOM   8877 O  OD2 . ASP   B 1 586 ? -26.560 -15.426 22.998  1.00 12.81 ? 609  ASP   B OD2 1 
ATOM   8878 N  N   . GLU   B 1 587 ? -30.024 -12.185 25.584  1.00 10.66 ? 610  GLU   B N   1 
ATOM   8879 C  CA  . GLU   B 1 587 ? -30.836 -11.029 25.220  1.00 11.48 ? 610  GLU   B CA  1 
ATOM   8880 C  C   . GLU   B 1 587 ? -30.442 -10.485 23.848  1.00 11.19 ? 610  GLU   B C   1 
ATOM   8881 O  O   . GLU   B 1 587 ? -31.282 -10.169 23.000  1.00 9.41  ? 610  GLU   B O   1 
ATOM   8882 C  CB  . GLU   B 1 587 ? -30.722 -10.049 26.389  1.00 12.31 ? 610  GLU   B CB  1 
ATOM   8883 C  CG  . GLU   B 1 587 ? -31.513 -8.768  26.185  1.00 14.38 ? 610  GLU   B CG  1 
ATOM   8884 C  CD  . GLU   B 1 587 ? -31.453 -7.972  27.477  1.00 14.79 ? 610  GLU   B CD  1 
ATOM   8885 O  OE1 . GLU   B 1 587 ? -30.628 -7.075  27.505  1.00 16.55 ? 610  GLU   B OE1 1 
ATOM   8886 O  OE2 . GLU   B 1 587 ? -32.172 -8.253  28.463  1.00 17.56 ? 610  GLU   B OE2 1 
ATOM   8887 N  N   . ALA   B 1 588 ? -29.130 -10.371 23.600  1.00 10.53 ? 611  ALA   B N   1 
ATOM   8888 C  CA  . ALA   B 1 588 ? -28.681 -9.840  22.324  1.00 11.22 ? 611  ALA   B CA  1 
ATOM   8889 C  C   . ALA   B 1 588 ? -29.127 -10.707 21.139  1.00 10.72 ? 611  ALA   B C   1 
ATOM   8890 O  O   . ALA   B 1 588 ? -29.437 -10.181 20.083  1.00 12.69 ? 611  ALA   B O   1 
ATOM   8891 C  CB  . ALA   B 1 588 ? -27.175 -9.656  22.341  1.00 11.12 ? 611  ALA   B CB  1 
ATOM   8892 N  N   . ARG   B 1 589 ? -29.110 -12.032 21.290  1.00 11.45 ? 612  ARG   B N   1 
ATOM   8893 C  CA  . ARG   B 1 589 ? -29.417 -12.932 20.204  1.00 11.49 ? 612  ARG   B CA  1 
ATOM   8894 C  C   . ARG   B 1 589 ? -30.920 -12.906 19.927  1.00 11.12 ? 612  ARG   B C   1 
ATOM   8895 O  O   . ARG   B 1 589 ? -31.338 -12.968 18.776  1.00 11.36 ? 612  ARG   B O   1 
ATOM   8896 C  CB  . ARG   B 1 589 ? -29.010 -14.330 20.655  1.00 13.46 ? 612  ARG   B CB  1 
ATOM   8897 C  CG  . ARG   B 1 589 ? -28.850 -15.257 19.484  1.00 14.12 ? 612  ARG   B CG  1 
ATOM   8898 C  CD  . ARG   B 1 589 ? -28.178 -16.490 20.034  1.00 15.29 ? 612  ARG   B CD  1 
ATOM   8899 N  NE  . ARG   B 1 589 ? -28.319 -17.462 18.960  1.00 15.34 ? 612  ARG   B NE  1 
ATOM   8900 C  CZ  . ARG   B 1 589 ? -28.534 -18.752 19.154  1.00 14.02 ? 612  ARG   B CZ  1 
ATOM   8901 N  NH1 . ARG   B 1 589 ? -28.373 -19.274 20.340  1.00 13.70 ? 612  ARG   B NH1 1 
ATOM   8902 N  NH2 . ARG   B 1 589 ? -28.819 -19.504 18.122  1.00 15.71 ? 612  ARG   B NH2 1 
ATOM   8903 N  N   . VAL   B 1 590 ? -31.700 -12.851 21.008  1.00 10.05 ? 613  VAL   B N   1 
ATOM   8904 C  CA  . VAL   B 1 590 ? -33.147 -12.698 20.925  1.00 9.91  ? 613  VAL   B CA  1 
ATOM   8905 C  C   . VAL   B 1 590 ? -33.471 -11.401 20.184  1.00 9.79  ? 613  VAL   B C   1 
ATOM   8906 O  O   . VAL   B 1 590 ? -34.292 -11.388 19.261  1.00 9.34  ? 613  VAL   B O   1 
ATOM   8907 C  CB  . VAL   B 1 590 ? -33.823 -12.776 22.309  1.00 9.83  ? 613  VAL   B CB  1 
ATOM   8908 C  CG1 . VAL   B 1 590 ? -35.290 -12.410 22.252  1.00 10.75 ? 613  VAL   B CG1 1 
ATOM   8909 C  CG2 . VAL   B 1 590 ? -33.652 -14.151 22.983  1.00 10.84 ? 613  VAL   B CG2 1 
ATOM   8910 N  N   . ARG   B 1 591 ? -32.793 -10.320 20.563  1.00 10.40 ? 614  ARG   B N   1 
ATOM   8911 C  CA  . ARG   B 1 591 ? -33.033 -9.023  19.952  1.00 9.59  ? 614  ARG   B CA  1 
ATOM   8912 C  C   . ARG   B 1 591 ? -32.737 -9.092  18.451  1.00 10.24 ? 614  ARG   B C   1 
ATOM   8913 O  O   . ARG   B 1 591 ? -33.501 -8.579  17.629  1.00 9.74  ? 614  ARG   B O   1 
ATOM   8914 C  CB  . ARG   B 1 591 ? -32.216 -7.954  20.691  1.00 10.23 ? 614  ARG   B CB  1 
ATOM   8915 C  CG  . ARG   B 1 591 ? -32.539 -6.526  20.286  1.00 10.76 ? 614  ARG   B CG  1 
ATOM   8916 C  CD  . ARG   B 1 591 ? -31.843 -6.120  19.026  1.00 11.94 ? 614  ARG   B CD  1 
ATOM   8917 N  NE  . ARG   B 1 591 ? -32.107 -4.689  18.861  1.00 12.72 ? 614  ARG   B NE  1 
ATOM   8918 C  CZ  . ARG   B 1 591 ? -31.746 -3.993  17.803  1.00 11.51 ? 614  ARG   B CZ  1 
ATOM   8919 N  NH1 . ARG   B 1 591 ? -32.221 -2.773  17.679  1.00 11.33 ? 614  ARG   B NH1 1 
ATOM   8920 N  NH2 . ARG   B 1 591 ? -31.032 -4.549  16.830  1.00 11.60 ? 614  ARG   B NH2 1 
ATOM   8921 N  N   . ALA   B 1 592 ? -31.598 -9.686  18.082  1.00 10.54 ? 615  ALA   B N   1 
ATOM   8922 C  CA  . ALA   B 1 592 ? -31.227 -9.848  16.690  1.00 10.79 ? 615  ALA   B CA  1 
ATOM   8923 C  C   . ALA   B 1 592 ? -32.242 -10.692 15.923  1.00 10.39 ? 615  ALA   B C   1 
ATOM   8924 O  O   . ALA   B 1 592 ? -32.518 -10.366 14.791  1.00 10.28 ? 615  ALA   B O   1 
ATOM   8925 C  CB  . ALA   B 1 592 ? -29.855 -10.478 16.570  1.00 11.43 ? 615  ALA   B CB  1 
ATOM   8926 N  N   . ALA   B 1 593 ? -32.755 -11.787 16.495  1.00 10.97 ? 616  ALA   B N   1 
ATOM   8927 C  CA  . ALA   B 1 593 ? -33.723 -12.601 15.773  1.00 10.63 ? 616  ALA   B CA  1 
ATOM   8928 C  C   . ALA   B 1 593 ? -34.998 -11.821 15.493  1.00 10.25 ? 616  ALA   B C   1 
ATOM   8929 O  O   . ALA   B 1 593 ? -35.492 -11.816 14.357  1.00 11.48 ? 616  ALA   B O   1 
ATOM   8930 C  CB  . ALA   B 1 593 ? -34.019 -13.865 16.511  1.00 11.66 ? 616  ALA   B CB  1 
ATOM   8931 N  N   . ASN   B 1 594 ? -35.492 -11.124 16.512  1.00 10.06 ? 617  ASN   B N   1 
ATOM   8932 C  CA  . ASN   B 1 594 ? -36.659 -10.258 16.391  1.00 9.82  ? 617  ASN   B CA  1 
ATOM   8933 C  C   . ASN   B 1 594 ? -36.464 -9.135  15.381  1.00 10.11 ? 617  ASN   B C   1 
ATOM   8934 O  O   . ASN   B 1 594 ? -37.366 -8.852  14.580  1.00 11.11 ? 617  ASN   B O   1 
ATOM   8935 C  CB  . ASN   B 1 594 ? -37.072 -9.678  17.737  1.00 10.09 ? 617  ASN   B CB  1 
ATOM   8936 C  CG  . ASN   B 1 594 ? -37.888 -10.656 18.556  1.00 10.27 ? 617  ASN   B CG  1 
ATOM   8937 O  OD1 . ASN   B 1 594 ? -38.700 -11.400 18.008  1.00 10.36 ? 617  ASN   B OD1 1 
ATOM   8938 N  ND2 . ASN   B 1 594 ? -37.760 -10.611 19.871  1.00 10.43 ? 617  ASN   B ND2 1 
ATOM   8939 N  N   . ARG   B 1 595 ? -35.326 -8.445  15.438  1.00 10.60 ? 618  ARG   B N   1 
ATOM   8940 C  CA  A ARG   B 1 595 ? -35.062 -7.343  14.534  0.50 11.84 ? 618  ARG   B CA  1 
ATOM   8941 C  CA  B ARG   B 1 595 ? -35.078 -7.342  14.534  0.50 11.08 ? 618  ARG   B CA  1 
ATOM   8942 C  C   . ARG   B 1 595 ? -34.969 -7.857  13.099  1.00 11.27 ? 618  ARG   B C   1 
ATOM   8943 O  O   . ARG   B 1 595 ? -35.441 -7.183  12.189  1.00 11.97 ? 618  ARG   B O   1 
ATOM   8944 C  CB  A ARG   B 1 595 ? -33.777 -6.594  14.914  0.50 12.95 ? 618  ARG   B CB  1 
ATOM   8945 C  CB  B ARG   B 1 595 ? -33.834 -6.550  14.958  0.50 11.04 ? 618  ARG   B CB  1 
ATOM   8946 C  CG  A ARG   B 1 595 ? -33.605 -5.220  14.287  0.50 14.78 ? 618  ARG   B CG  1 
ATOM   8947 C  CG  B ARG   B 1 595 ? -33.528 -5.325  14.115  0.50 11.56 ? 618  ARG   B CG  1 
ATOM   8948 C  CD  A ARG   B 1 595 ? -34.719 -4.304  14.750  0.50 17.17 ? 618  ARG   B CD  1 
ATOM   8949 C  CD  B ARG   B 1 595 ? -34.528 -4.208  14.343  0.50 12.24 ? 618  ARG   B CD  1 
ATOM   8950 N  NE  A ARG   B 1 595 ? -34.439 -2.865  14.736  0.50 18.87 ? 618  ARG   B NE  1 
ATOM   8951 N  NE  B ARG   B 1 595 ? -34.369 -3.132  13.367  0.50 12.69 ? 618  ARG   B NE  1 
ATOM   8952 C  CZ  A ARG   B 1 595 ? -33.976 -2.143  13.737  0.50 21.16 ? 618  ARG   B CZ  1 
ATOM   8953 C  CZ  B ARG   B 1 595 ? -34.370 -1.827  13.664  0.50 13.13 ? 618  ARG   B CZ  1 
ATOM   8954 N  NH1 A ARG   B 1 595 ? -33.430 -2.725  12.667  0.50 21.97 ? 618  ARG   B NH1 1 
ATOM   8955 N  NH1 B ARG   B 1 595 ? -34.700 -1.423  14.878  0.50 12.25 ? 618  ARG   B NH1 1 
ATOM   8956 N  NH2 A ARG   B 1 595 ? -34.023 -0.819  13.856  0.50 21.43 ? 618  ARG   B NH2 1 
ATOM   8957 N  NH2 B ARG   B 1 595 ? -34.059 -0.932  12.723  0.50 13.72 ? 618  ARG   B NH2 1 
ATOM   8958 N  N   . ALA   B 1 596 ? -34.346 -9.037  12.899  1.00 11.26 ? 619  ALA   B N   1 
ATOM   8959 C  CA  . ALA   B 1 596 ? -34.238 -9.606  11.558  1.00 11.36 ? 619  ALA   B CA  1 
ATOM   8960 C  C   . ALA   B 1 596 ? -35.634 -9.869  10.996  1.00 10.93 ? 619  ALA   B C   1 
ATOM   8961 O  O   . ALA   B 1 596 ? -35.899 -9.584  9.845   1.00 11.10 ? 619  ALA   B O   1 
ATOM   8962 C  CB  . ALA   B 1 596 ? -33.404 -10.873 11.547  1.00 11.56 ? 619  ALA   B CB  1 
ATOM   8963 N  N   . LEU   B 1 597 ? -36.518 -10.415 11.833  1.00 11.24 ? 620  LEU   B N   1 
ATOM   8964 C  CA  . LEU   B 1 597 ? -37.898 -10.708 11.458  1.00 10.83 ? 620  LEU   B CA  1 
ATOM   8965 C  C   . LEU   B 1 597 ? -38.616 -9.415  11.062  1.00 11.50 ? 620  LEU   B C   1 
ATOM   8966 O  O   . LEU   B 1 597 ? -39.254 -9.316  10.009  1.00 11.35 ? 620  LEU   B O   1 
ATOM   8967 C  CB  . LEU   B 1 597 ? -38.511 -11.408 12.670  1.00 11.35 ? 620  LEU   B CB  1 
ATOM   8968 C  CG  . LEU   B 1 597 ? -40.031 -11.628 12.637  1.00 11.81 ? 620  LEU   B CG  1 
ATOM   8969 C  CD1 . LEU   B 1 597 ? -40.528 -12.253 11.364  1.00 12.13 ? 620  LEU   B CD1 1 
ATOM   8970 C  CD2 . LEU   B 1 597 ? -40.509 -12.462 13.822  1.00 11.87 ? 620  LEU   B CD2 1 
ATOM   8971 N  N   . ILE   B 1 598 ? -38.495 -8.398  11.908  1.00 10.92 ? 621  ILE   B N   1 
ATOM   8972 C  CA  . ILE   B 1 598 ? -39.156 -7.126  11.672  1.00 11.45 ? 621  ILE   B CA  1 
ATOM   8973 C  C   . ILE   B 1 598 ? -38.630 -6.507  10.375  1.00 13.18 ? 621  ILE   B C   1 
ATOM   8974 O  O   . ILE   B 1 598 ? -39.424 -6.074  9.536   1.00 12.46 ? 621  ILE   B O   1 
ATOM   8975 C  CB  . ILE   B 1 598 ? -38.950 -6.164  12.853  1.00 11.96 ? 621  ILE   B CB  1 
ATOM   8976 C  CG1 . ILE   B 1 598 ? -39.747 -6.632  14.084  1.00 11.69 ? 621  ILE   B CG1 1 
ATOM   8977 C  CG2 . ILE   B 1 598 ? -39.295 -4.739  12.417  1.00 12.82 ? 621  ILE   B CG2 1 
ATOM   8978 C  CD1 . ILE   B 1 598 ? -39.312 -6.057  15.420  1.00 11.51 ? 621  ILE   B CD1 1 
ATOM   8979 N  N   . ASP   B 1 599 ? -37.299 -6.396  10.272  1.00 13.72 ? 622  ASP   B N   1 
ATOM   8980 C  CA  . ASP   B 1 599 ? -36.638 -5.871  9.087   1.00 17.06 ? 622  ASP   B CA  1 
ATOM   8981 C  C   . ASP   B 1 599 ? -37.070 -6.624  7.831   1.00 14.50 ? 622  ASP   B C   1 
ATOM   8982 O  O   . ASP   B 1 599 ? -37.406 -5.994  6.828   1.00 14.37 ? 622  ASP   B O   1 
ATOM   8983 C  CB  . ASP   B 1 599 ? -35.120 -6.002  9.171   1.00 19.96 ? 622  ASP   B CB  1 
ATOM   8984 C  CG  . ASP   B 1 599 ? -34.378 -5.022  10.068  1.00 22.53 ? 622  ASP   B CG  1 
ATOM   8985 O  OD1 . ASP   B 1 599 ? -35.006 -4.039  10.496  1.00 16.89 ? 622  ASP   B OD1 1 
ATOM   8986 O  OD2 . ASP   B 1 599 ? -33.165 -5.293  10.340  1.00 29.60 ? 622  ASP   B OD2 1 
ATOM   8987 N  N   . ALA   B 1 600 ? -37.093 -7.954  7.887   1.00 13.32 ? 623  ALA   B N   1 
ATOM   8988 C  CA  . ALA   B 1 600 ? -37.468 -8.730  6.715   1.00 13.59 ? 623  ALA   B CA  1 
ATOM   8989 C  C   . ALA   B 1 600 ? -38.899 -8.413  6.302   1.00 13.61 ? 623  ALA   B C   1 
ATOM   8990 O  O   . ALA   B 1 600 ? -39.184 -8.397  5.107   1.00 14.20 ? 623  ALA   B O   1 
ATOM   8991 C  CB  . ALA   B 1 600 ? -37.256 -10.211 6.921   1.00 14.79 ? 623  ALA   B CB  1 
ATOM   8992 N  N   . SER   B 1 601 ? -39.794 -8.180  7.272   1.00 12.06 ? 624  SER   B N   1 
ATOM   8993 C  CA  . SER   B 1 601 ? -41.215 -8.047  6.992   1.00 13.56 ? 624  SER   B CA  1 
ATOM   8994 C  C   . SER   B 1 601 ? -41.487 -6.742  6.238   1.00 15.08 ? 624  SER   B C   1 
ATOM   8995 O  O   . SER   B 1 601 ? -42.513 -6.609  5.540   1.00 14.50 ? 624  SER   B O   1 
ATOM   8996 C  CB  . SER   B 1 601 ? -42.022 -8.134  8.286   1.00 13.31 ? 624  SER   B CB  1 
ATOM   8997 O  OG  . SER   B 1 601 ? -41.879 -6.929  9.032   1.00 12.67 ? 624  SER   B OG  1 
ATOM   8998 N  N   . ARG   B 1 602 ? -40.561 -5.774  6.366   1.00 16.96 ? 625  ARG   B N   1 
ATOM   8999 C  CA  . ARG   B 1 602 ? -40.755 -4.479  5.733   1.00 21.50 ? 625  ARG   B CA  1 
ATOM   9000 C  C   . ARG   B 1 602 ? -40.400 -4.537  4.240   1.00 27.87 ? 625  ARG   B C   1 
ATOM   9001 O  O   . ARG   B 1 602 ? -40.822 -3.664  3.498   1.00 31.27 ? 625  ARG   B O   1 
ATOM   9002 C  CB  . ARG   B 1 602 ? -40.003 -3.331  6.407   1.00 21.27 ? 625  ARG   B CB  1 
ATOM   9003 C  CG  . ARG   B 1 602 ? -40.363 -3.168  7.875   1.00 23.28 ? 625  ARG   B CG  1 
ATOM   9004 C  CD  . ARG   B 1 602 ? -39.611 -1.939  8.320   1.00 25.30 ? 625  ARG   B CD  1 
ATOM   9005 N  NE  . ARG   B 1 602 ? -39.429 -1.893  9.771   1.00 26.28 ? 625  ARG   B NE  1 
ATOM   9006 C  CZ  . ARG   B 1 602 ? -40.335 -1.427  10.620  1.00 26.37 ? 625  ARG   B CZ  1 
ATOM   9007 N  NH1 . ARG   B 1 602 ? -41.520 -1.034  10.175  1.00 26.43 ? 625  ARG   B NH1 1 
ATOM   9008 N  NH2 . ARG   B 1 602 ? -40.039 -1.347  11.913  1.00 25.48 ? 625  ARG   B NH2 1 
ATOM   9009 N  N   . GLY   B 1 603 ? -39.670 -5.557  3.783   1.00 28.56 ? 626  GLY   B N   1 
ATOM   9010 C  CA  . GLY   B 1 603 ? -39.457 -5.728  2.356   1.00 32.49 ? 626  GLY   B CA  1 
ATOM   9011 C  C   . GLY   B 1 603 ? -40.776 -5.986  1.637   1.00 42.17 ? 626  GLY   B C   1 
ATOM   9012 O  O   . GLY   B 1 603 ? -41.371 -7.087  1.845   1.00 48.19 ? 626  GLY   B O   1 
HETATM 9013 O  O1  . P6G   C 2 .   ? -11.352 7.770   64.051  1.00 41.79 ? 701  P6G   A O1  1 
HETATM 9014 C  C2  . P6G   C 2 .   ? -10.040 7.462   63.639  1.00 37.93 ? 701  P6G   A C2  1 
HETATM 9015 C  C3  . P6G   C 2 .   ? -9.790  6.000   63.444  1.00 43.14 ? 701  P6G   A C3  1 
HETATM 9016 O  O4  . P6G   C 2 .   ? -8.564  5.817   62.731  1.00 45.01 ? 701  P6G   A O4  1 
HETATM 9017 C  C5  . P6G   C 2 .   ? -7.400  6.252   63.426  1.00 36.34 ? 701  P6G   A C5  1 
HETATM 9018 C  C6  . P6G   C 2 .   ? -6.592  7.168   62.568  1.00 33.15 ? 701  P6G   A C6  1 
HETATM 9019 O  O7  . P6G   C 2 .   ? -6.506  6.676   61.238  1.00 31.57 ? 701  P6G   A O7  1 
HETATM 9020 C  C8  . P6G   C 2 .   ? -5.619  7.442   60.432  1.00 31.81 ? 701  P6G   A C8  1 
HETATM 9021 C  C9  . P6G   C 2 .   ? -5.744  7.015   59.014  1.00 35.40 ? 701  P6G   A C9  1 
HETATM 9022 O  O10 . P6G   C 2 .   ? -5.544  5.609   58.933  1.00 39.02 ? 701  P6G   A O10 1 
HETATM 9023 C  C11 . P6G   C 2 .   ? -4.411  5.259   58.152  1.00 43.17 ? 701  P6G   A C11 1 
HETATM 9024 C  C12 . P6G   C 2 .   ? -4.668  3.957   57.510  1.00 42.81 ? 701  P6G   A C12 1 
HETATM 9025 O  O13 . P6G   C 2 .   ? -4.295  2.891   58.382  1.00 43.34 ? 701  P6G   A O13 1 
HETATM 9026 C  C14 . P6G   C 2 .   ? -3.726  1.769   57.706  1.00 41.66 ? 701  P6G   A C14 1 
HETATM 9027 C  C15 . P6G   C 2 .   ? -3.195  2.204   56.382  1.00 38.89 ? 701  P6G   A C15 1 
HETATM 9028 O  O16 . P6G   C 2 .   ? -2.349  1.220   55.821  1.00 39.57 ? 701  P6G   A O16 1 
HETATM 9029 C  C17 . P6G   C 2 .   ? -1.641  1.704   54.688  1.00 36.99 ? 701  P6G   A C17 1 
HETATM 9030 C  C18 . P6G   C 2 .   ? -0.175  1.529   54.891  1.00 37.49 ? 701  P6G   A C18 1 
HETATM 9031 O  O19 . P6G   C 2 .   ? 0.599   2.517   54.219  1.00 39.84 ? 701  P6G   A O19 1 
HETATM 9032 C  C1  . MPD   D 3 .   ? 11.286  7.787   24.708  1.00 20.84 ? 702  MPD   A C1  1 
HETATM 9033 C  C2  . MPD   D 3 .   ? 10.541  6.826   23.782  1.00 23.35 ? 702  MPD   A C2  1 
HETATM 9034 O  O2  . MPD   D 3 .   ? 9.522   7.540   23.035  1.00 20.69 ? 702  MPD   A O2  1 
HETATM 9035 C  CM  . MPD   D 3 .   ? 9.854   5.743   24.591  1.00 21.19 ? 702  MPD   A CM  1 
HETATM 9036 C  C3  . MPD   D 3 .   ? 11.396  6.195   22.675  1.00 28.57 ? 702  MPD   A C3  1 
HETATM 9037 C  C4  . MPD   D 3 .   ? 12.893  6.345   22.542  1.00 30.07 ? 702  MPD   A C4  1 
HETATM 9038 O  O4  . MPD   D 3 .   ? 13.652  5.834   23.640  1.00 26.10 ? 702  MPD   A O4  1 
HETATM 9039 C  C5  . MPD   D 3 .   ? 13.289  5.588   21.302  1.00 30.03 ? 702  MPD   A C5  1 
HETATM 9040 C  C1  . MPD   E 3 .   ? -5.243  -10.447 27.721  1.00 21.72 ? 703  MPD   A C1  1 
HETATM 9041 C  C2  . MPD   E 3 .   ? -6.665  -10.542 28.235  1.00 22.38 ? 703  MPD   A C2  1 
HETATM 9042 O  O2  . MPD   E 3 .   ? -7.235  -9.328  27.689  1.00 19.04 ? 703  MPD   A O2  1 
HETATM 9043 C  CM  . MPD   E 3 .   ? -6.678  -10.553 29.758  1.00 21.57 ? 703  MPD   A CM  1 
HETATM 9044 C  C3  . MPD   E 3 .   ? -7.380  -11.805 27.741  1.00 21.99 ? 703  MPD   A C3  1 
HETATM 9045 C  C4  . MPD   E 3 .   ? -7.309  -12.143 26.275  1.00 20.63 ? 703  MPD   A C4  1 
HETATM 9046 O  O4  . MPD   E 3 .   ? -6.083  -12.790 25.986  1.00 16.58 ? 703  MPD   A O4  1 
HETATM 9047 C  C5  . MPD   E 3 .   ? -8.420  -13.032 25.801  1.00 18.57 ? 703  MPD   A C5  1 
HETATM 9048 C  C4  . A1L3Z F 4 .   ? -12.149 16.576  15.017  1.00 10.11 ? 704  A1L3Z A C4  1 
HETATM 9049 C  C5  . A1L3Z F 4 .   ? -11.648 15.546  16.028  1.00 9.55  ? 704  A1L3Z A C5  1 
HETATM 9050 C  C6  . A1L3Z F 4 .   ? -12.920 14.856  16.550  1.00 9.48  ? 704  A1L3Z A C6  1 
HETATM 9051 N  N1  . A1L3Z F 4 .   ? -13.588 16.232  14.796  1.00 9.65  1 704  A1L3Z A N1  1 
HETATM 9052 C  C3  . A1L3Z F 4 .   ? -14.090 15.756  16.151  1.00 9.51  ? 704  A1L3Z A C3  1 
HETATM 9053 O  O1  . A1L3Z F 4 .   ? -15.860 15.574  18.489  1.00 8.95  ? 704  A1L3Z A O1  1 
HETATM 9054 C  C1  . A1L3Z F 4 .   ? -15.947 14.646  17.419  1.00 9.58  ? 704  A1L3Z A C1  1 
HETATM 9055 C  C2  . A1L3Z F 4 .   ? -15.467 15.153  16.068  1.00 9.50  ? 704  A1L3Z A C2  1 
HETATM 9056 O  O2  . A1L3Z F 4 .   ? -16.400 16.143  15.581  1.00 10.03 ? 704  A1L3Z A O2  1 
HETATM 9057 O  O3  . A1L3Z F 4 .   ? -10.772 14.585  15.446  1.00 9.18  ? 704  A1L3Z A O3  1 
HETATM 9058 O  O4  . A1L3Z F 4 .   ? -12.890 14.703  17.962  1.00 9.15  ? 704  A1L3Z A O4  1 
HETATM 9059 MG MG  . MG    G 5 .   ? -10.036 10.637  33.817  1.00 8.89  ? 705  MG    A MG  1 
HETATM 9060 O  O1  . PG4   H 6 .   ? -28.713 -6.839  36.219  1.00 39.28 ? 701  PG4   B O1  1 
HETATM 9061 C  C1  . PG4   H 6 .   ? -29.614 -7.753  36.821  1.00 39.84 ? 701  PG4   B C1  1 
HETATM 9062 C  C2  . PG4   H 6 .   ? -31.022 -7.350  36.564  1.00 40.71 ? 701  PG4   B C2  1 
HETATM 9063 O  O2  . PG4   H 6 .   ? -31.626 -6.840  37.745  1.00 38.72 ? 701  PG4   B O2  1 
HETATM 9064 C  C3  . PG4   H 6 .   ? -33.035 -6.665  37.603  1.00 36.58 ? 701  PG4   B C3  1 
HETATM 9065 C  C4  . PG4   H 6 .   ? -33.343 -5.362  36.947  1.00 33.39 ? 701  PG4   B C4  1 
HETATM 9066 O  O3  . PG4   H 6 .   ? -32.805 -4.298  37.716  1.00 36.08 ? 701  PG4   B O3  1 
HETATM 9067 C  C5  . PG4   H 6 .   ? -33.677 -3.182  37.851  1.00 32.09 ? 701  PG4   B C5  1 
HETATM 9068 C  C6  . PG4   H 6 .   ? -32.959 -2.045  38.488  1.00 33.11 ? 701  PG4   B C6  1 
HETATM 9069 O  O4  . PG4   H 6 .   ? -33.320 -1.861  39.853  1.00 35.19 ? 701  PG4   B O4  1 
HETATM 9070 C  C7  . PG4   H 6 .   ? -32.982 -0.553  40.302  1.00 41.24 ? 701  PG4   B C7  1 
HETATM 9071 C  C8  . PG4   H 6 .   ? -33.792 -0.168  41.481  1.00 42.12 ? 701  PG4   B C8  1 
HETATM 9072 O  O5  . PG4   H 6 .   ? -33.965 1.239   41.572  1.00 48.43 ? 701  PG4   B O5  1 
HETATM 9073 C  C1  . MPD   I 3 .   ? -75.929 -8.835  26.080  1.00 22.14 ? 702  MPD   B C1  1 
HETATM 9074 C  C2  . MPD   I 3 .   ? -76.430 -10.095 25.399  1.00 26.24 ? 702  MPD   B C2  1 
HETATM 9075 O  O2  . MPD   I 3 .   ? -75.321 -11.010 25.441  1.00 22.17 ? 702  MPD   B O2  1 
HETATM 9076 C  CM  . MPD   I 3 .   ? -77.564 -10.733 26.189  1.00 28.49 ? 702  MPD   B CM  1 
HETATM 9077 C  C3  . MPD   I 3 .   ? -76.755 -9.804  23.930  1.00 28.21 ? 702  MPD   B C3  1 
HETATM 9078 C  C4  . MPD   I 3 .   ? -78.097 -10.115 23.336  1.00 29.09 ? 702  MPD   B C4  1 
HETATM 9079 O  O4  . MPD   I 3 .   ? -79.090 -9.323  23.928  1.00 22.08 ? 702  MPD   B O4  1 
HETATM 9080 C  C5  . MPD   I 3 .   ? -78.102 -9.882  21.840  1.00 30.66 ? 702  MPD   B C5  1 
HETATM 9081 C  C4  . A1L3Z J 4 .   ? -53.128 -21.268 27.043  1.00 12.91 ? 703  A1L3Z B C4  1 
HETATM 9082 C  C5  . A1L3Z J 4 .   ? -53.797 -19.986 27.534  1.00 12.45 ? 703  A1L3Z B C5  1 
HETATM 9083 C  C6  . A1L3Z J 4 .   ? -52.691 -19.191 28.240  1.00 11.35 ? 703  A1L3Z B C6  1 
HETATM 9084 N  N1  . A1L3Z J 4 .   ? -51.653 -21.013 27.194  1.00 12.56 1 703  A1L3Z B N1  1 
HETATM 9085 C  C3  . A1L3Z J 4 .   ? -51.583 -20.241 28.466  1.00 11.90 ? 703  A1L3Z B C3  1 
HETATM 9086 O  O1  . A1L3Z J 4 .   ? -50.550 -19.415 31.102  1.00 12.85 ? 703  A1L3Z B O1  1 
HETATM 9087 C  C1  . A1L3Z J 4 .   ? -50.108 -18.770 29.894  1.00 12.38 ? 703  A1L3Z B C1  1 
HETATM 9088 C  C2  . A1L3Z J 4 .   ? -50.196 -19.652 28.668  1.00 11.81 ? 703  A1L3Z B C2  1 
HETATM 9089 O  O2  . A1L3Z J 4 .   ? -49.252 -20.726 28.739  1.00 11.37 ? 703  A1L3Z B O2  1 
HETATM 9090 O  O3  . A1L3Z J 4 .   ? -54.380 -19.237 26.483  1.00 11.68 ? 703  A1L3Z B O3  1 
HETATM 9091 O  O4  . A1L3Z J 4 .   ? -53.195 -18.641 29.458  1.00 11.57 ? 703  A1L3Z B O4  1 
HETATM 9092 MG MG  . MG    K 5 .   ? -60.297 -10.648 42.054  1.00 14.19 ? 704  MG    B MG  1 
HETATM 9093 O  O   . HOH   L 7 .   ? -0.856  -17.242 51.193  1.00 27.25 ? 801  HOH   A O   1 
HETATM 9094 O  O   . HOH   L 7 .   ? -5.098  -34.939 29.129  1.00 26.18 ? 802  HOH   A O   1 
HETATM 9095 O  O   . HOH   L 7 .   ? -19.868 -5.904  5.342   1.00 18.78 ? 803  HOH   A O   1 
HETATM 9096 O  O   . HOH   L 7 .   ? -21.655 22.926  4.912   1.00 27.43 ? 804  HOH   A O   1 
HETATM 9097 O  O   . HOH   L 7 .   ? -31.024 2.225   39.731  1.00 33.78 ? 805  HOH   A O   1 
HETATM 9098 O  O   . HOH   L 7 .   ? -20.549 -23.117 19.876  1.00 17.86 ? 806  HOH   A O   1 
HETATM 9099 O  O   . HOH   L 7 .   ? -21.611 -7.077  43.295  1.00 19.76 ? 807  HOH   A O   1 
HETATM 9100 O  O   . HOH   L 7 .   ? -38.193 9.221   5.591   1.00 23.35 ? 808  HOH   A O   1 
HETATM 9101 O  O   . HOH   L 7 .   ? -7.329  4.341   60.021  1.00 35.91 ? 809  HOH   A O   1 
HETATM 9102 O  O   . HOH   L 7 .   ? -27.328 26.142  19.653  1.00 34.17 ? 810  HOH   A O   1 
HETATM 9103 O  O   . HOH   L 7 .   ? -22.541 -7.463  -0.147  1.00 41.67 ? 811  HOH   A O   1 
HETATM 9104 O  O   . HOH   L 7 .   ? -20.014 -19.997 22.283  1.00 26.86 ? 812  HOH   A O   1 
HETATM 9105 O  O   . HOH   L 7 .   ? -10.181 -1.230  -6.548  1.00 25.61 ? 813  HOH   A O   1 
HETATM 9106 O  O   . HOH   L 7 .   ? -3.245  -11.608 38.894  1.00 12.66 ? 814  HOH   A O   1 
HETATM 9107 O  O   . HOH   L 7 .   ? -0.405  -15.539 40.478  1.00 21.07 ? 815  HOH   A O   1 
HETATM 9108 O  O   . HOH   L 7 .   ? 2.526   3.575   37.897  1.00 22.91 ? 816  HOH   A O   1 
HETATM 9109 O  O   . HOH   L 7 .   ? -25.457 13.592  12.098  1.00 9.22  ? 817  HOH   A O   1 
HETATM 9110 O  O   . HOH   L 7 .   ? 6.878   0.551   24.495  1.00 24.14 ? 818  HOH   A O   1 
HETATM 9111 O  O   . HOH   L 7 .   ? -38.103 20.725  5.192   1.00 32.60 ? 819  HOH   A O   1 
HETATM 9112 O  O   . HOH   L 7 .   ? -13.709 16.028  36.927  1.00 9.08  ? 820  HOH   A O   1 
HETATM 9113 O  O   . HOH   L 7 .   ? -24.587 -6.071  2.895   1.00 46.94 ? 821  HOH   A O   1 
HETATM 9114 O  O   . HOH   L 7 .   ? -6.348  -34.245 32.595  1.00 36.14 ? 822  HOH   A O   1 
HETATM 9115 O  O   . HOH   L 7 .   ? -35.457 1.282   15.893  1.00 23.14 ? 823  HOH   A O   1 
HETATM 9116 O  O   . HOH   L 7 .   ? -10.636 19.550  14.454  1.00 20.93 ? 824  HOH   A O   1 
HETATM 9117 O  O   . HOH   L 7 .   ? -13.122 -14.269 53.485  1.00 22.08 ? 825  HOH   A O   1 
HETATM 9118 O  O   . HOH   L 7 .   ? -4.276  -10.851 23.843  1.00 13.61 ? 826  HOH   A O   1 
HETATM 9119 O  O   . HOH   L 7 .   ? -15.742 16.489  45.694  1.00 41.73 ? 827  HOH   A O   1 
HETATM 9120 O  O   . HOH   L 7 .   ? -3.271  2.520   -4.649  1.00 22.73 ? 828  HOH   A O   1 
HETATM 9121 O  O   . HOH   L 7 .   ? -15.063 -25.603 10.579  1.00 15.85 ? 829  HOH   A O   1 
HETATM 9122 O  O   . HOH   L 7 .   ? -1.531  -17.196 5.715   1.00 38.32 ? 830  HOH   A O   1 
HETATM 9123 O  O   . HOH   L 7 .   ? -7.974  2.559   -0.922  1.00 10.65 ? 831  HOH   A O   1 
HETATM 9124 O  O   . HOH   L 7 .   ? 6.619   -20.304 34.169  1.00 22.55 ? 832  HOH   A O   1 
HETATM 9125 O  O   . HOH   L 7 .   ? -18.953 -16.906 6.881   1.00 16.76 ? 833  HOH   A O   1 
HETATM 9126 O  O   . HOH   L 7 .   ? -14.566 -6.659  -3.563  1.00 28.34 ? 834  HOH   A O   1 
HETATM 9127 O  O   . HOH   L 7 .   ? 9.033   14.551  33.155  1.00 30.31 ? 835  HOH   A O   1 
HETATM 9128 O  O   . HOH   L 7 .   ? -0.506  -16.464 18.316  1.00 12.23 ? 836  HOH   A O   1 
HETATM 9129 O  O   . HOH   L 7 .   ? -36.096 0.315   37.565  1.00 29.21 ? 837  HOH   A O   1 
HETATM 9130 O  O   . HOH   L 7 .   ? -19.713 -21.868 17.361  1.00 17.87 ? 838  HOH   A O   1 
HETATM 9131 O  O   . HOH   L 7 .   ? 1.454   6.956   0.754   1.00 22.03 ? 839  HOH   A O   1 
HETATM 9132 O  O   . HOH   L 7 .   ? 5.251   -2.495  21.371  1.00 27.05 ? 840  HOH   A O   1 
HETATM 9133 O  O   . HOH   L 7 .   ? -9.438  4.474   57.260  1.00 17.16 ? 841  HOH   A O   1 
HETATM 9134 O  O   . HOH   L 7 .   ? -0.815  -9.682  14.889  1.00 12.40 ? 842  HOH   A O   1 
HETATM 9135 O  O   . HOH   L 7 .   ? -24.193 7.067   -11.195 1.00 16.00 ? 843  HOH   A O   1 
HETATM 9136 O  O   . HOH   L 7 .   ? -10.536 -8.079  23.207  1.00 9.60  ? 844  HOH   A O   1 
HETATM 9137 O  O   . HOH   L 7 .   ? -4.110  -6.490  19.642  1.00 11.47 ? 845  HOH   A O   1 
HETATM 9138 O  O   . HOH   L 7 .   ? -12.236 11.385  0.835   1.00 16.69 ? 846  HOH   A O   1 
HETATM 9139 O  O   . HOH   L 7 .   ? -21.604 13.983  29.554  1.00 8.29  ? 847  HOH   A O   1 
HETATM 9140 O  O   . HOH   L 7 .   ? -29.046 10.646  -2.449  1.00 14.16 ? 848  HOH   A O   1 
HETATM 9141 O  O   . HOH   L 7 .   ? -8.379  7.607   -8.200  1.00 29.27 ? 849  HOH   A O   1 
HETATM 9142 O  O   . HOH   L 7 .   ? -36.681 9.550   26.046  1.00 24.61 ? 850  HOH   A O   1 
HETATM 9143 O  O   . HOH   L 7 .   ? -0.715  -8.787  46.742  1.00 25.95 ? 851  HOH   A O   1 
HETATM 9144 O  O   . HOH   L 7 .   ? -6.008  -25.046 3.882   1.00 28.30 ? 852  HOH   A O   1 
HETATM 9145 O  O   . HOH   L 7 .   ? -10.899 22.040  31.804  1.00 18.94 ? 853  HOH   A O   1 
HETATM 9146 O  O   . HOH   L 7 .   ? -0.227  20.865  33.930  1.00 16.25 ? 854  HOH   A O   1 
HETATM 9147 O  O   . HOH   L 7 .   ? -12.011 3.275   57.552  1.00 33.33 ? 855  HOH   A O   1 
HETATM 9148 O  O   . HOH   L 7 .   ? -21.732 -5.811  32.439  1.00 18.60 ? 856  HOH   A O   1 
HETATM 9149 O  O   . HOH   L 7 .   ? -21.722 1.820   23.625  1.00 8.86  ? 857  HOH   A O   1 
HETATM 9150 O  O   . HOH   L 7 .   ? 3.682   4.300   2.506   1.00 36.18 ? 858  HOH   A O   1 
HETATM 9151 O  O   . HOH   L 7 .   ? 2.081   -17.338 48.305  1.00 20.61 ? 859  HOH   A O   1 
HETATM 9152 O  O   . HOH   L 7 .   ? -7.369  -22.503 54.013  1.00 33.66 ? 860  HOH   A O   1 
HETATM 9153 O  O   . HOH   L 7 .   ? 5.583   13.745  31.911  1.00 20.06 ? 861  HOH   A O   1 
HETATM 9154 O  O   . HOH   L 7 .   ? -17.367 -19.941 42.772  1.00 16.08 ? 862  HOH   A O   1 
HETATM 9155 O  O   . HOH   L 7 .   ? -24.576 26.362  20.537  1.00 42.85 ? 863  HOH   A O   1 
HETATM 9156 O  O   . HOH   L 7 .   ? -16.216 4.595   40.599  1.00 9.07  ? 864  HOH   A O   1 
HETATM 9157 O  O   . HOH   L 7 .   ? -8.132  15.652  23.394  1.00 14.67 ? 865  HOH   A O   1 
HETATM 9158 O  O   . HOH   L 7 .   ? 1.010   -17.736 40.320  1.00 23.19 ? 866  HOH   A O   1 
HETATM 9159 O  O   . HOH   L 7 .   ? -23.277 -4.455  9.188   1.00 21.67 ? 867  HOH   A O   1 
HETATM 9160 O  O   . HOH   L 7 .   ? -23.356 -3.011  47.285  1.00 17.27 ? 868  HOH   A O   1 
HETATM 9161 O  O   . HOH   L 7 .   ? -9.727  -26.694 4.993   1.00 21.40 ? 869  HOH   A O   1 
HETATM 9162 O  O   . HOH   L 7 .   ? -12.879 0.293   22.544  1.00 8.04  ? 870  HOH   A O   1 
HETATM 9163 O  O   . HOH   L 7 .   ? -28.768 14.894  22.464  1.00 7.15  ? 871  HOH   A O   1 
HETATM 9164 O  O   . HOH   L 7 .   ? -20.755 18.020  1.495   1.00 14.68 ? 872  HOH   A O   1 
HETATM 9165 O  O   . HOH   L 7 .   ? -8.368  11.698  32.994  1.00 9.34  ? 873  HOH   A O   1 
HETATM 9166 O  O   . HOH   L 7 .   ? -7.522  19.398  15.665  1.00 15.20 ? 874  HOH   A O   1 
HETATM 9167 O  O   . HOH   L 7 .   ? -15.903 -20.915 24.759  1.00 31.00 ? 875  HOH   A O   1 
HETATM 9168 O  O   . HOH   L 7 .   ? -4.355  6.871   30.607  1.00 9.26  ? 876  HOH   A O   1 
HETATM 9169 O  O   . HOH   L 7 .   ? -34.912 11.604  -0.407  1.00 22.06 ? 877  HOH   A O   1 
HETATM 9170 O  O   . HOH   L 7 .   ? -18.179 -25.735 21.515  1.00 16.37 ? 878  HOH   A O   1 
HETATM 9171 O  O   . HOH   L 7 .   ? -8.871  15.784  37.255  1.00 8.23  ? 879  HOH   A O   1 
HETATM 9172 O  O   . HOH   L 7 .   ? -27.297 20.067  23.882  1.00 11.54 ? 880  HOH   A O   1 
HETATM 9173 O  O   . HOH   L 7 .   ? -34.644 20.528  24.754  1.00 15.24 ? 881  HOH   A O   1 
HETATM 9174 O  O   . HOH   L 7 .   ? -22.440 14.480  35.471  1.00 10.83 ? 882  HOH   A O   1 
HETATM 9175 O  O   . HOH   L 7 .   ? 10.360  9.643   21.290  1.00 12.94 ? 883  HOH   A O   1 
HETATM 9176 O  O   . HOH   L 7 .   ? 12.067  11.187  18.888  1.00 15.34 ? 884  HOH   A O   1 
HETATM 9177 O  O   . HOH   L 7 .   ? -12.207 9.893   25.448  1.00 8.78  ? 885  HOH   A O   1 
HETATM 9178 O  O   . HOH   L 7 .   ? -20.129 1.885   21.374  1.00 7.59  ? 886  HOH   A O   1 
HETATM 9179 O  O   . HOH   L 7 .   ? -5.031  3.152   36.978  1.00 8.96  ? 887  HOH   A O   1 
HETATM 9180 O  O   . HOH   L 7 .   ? -34.064 23.837  21.678  1.00 38.45 ? 888  HOH   A O   1 
HETATM 9181 O  O   . HOH   L 7 .   ? -0.348  -11.839 30.934  1.00 34.21 ? 889  HOH   A O   1 
HETATM 9182 O  O   . HOH   L 7 .   ? -38.609 16.348  19.949  1.00 27.15 ? 890  HOH   A O   1 
HETATM 9183 O  O   . HOH   L 7 .   ? -13.111 -16.214 36.405  1.00 9.45  ? 891  HOH   A O   1 
HETATM 9184 O  O   . HOH   L 7 .   ? -14.518 -34.826 20.062  1.00 19.72 ? 892  HOH   A O   1 
HETATM 9185 O  O   . HOH   L 7 .   ? -5.909  19.489  3.065   1.00 33.54 ? 893  HOH   A O   1 
HETATM 9186 O  O   . HOH   L 7 .   ? -18.827 19.929  26.314  1.00 13.82 ? 894  HOH   A O   1 
HETATM 9187 O  O   . HOH   L 7 .   ? 1.461   -21.317 23.182  1.00 9.96  ? 895  HOH   A O   1 
HETATM 9188 O  O   . HOH   L 7 .   ? -2.414  -26.835 12.548  1.00 25.36 ? 896  HOH   A O   1 
HETATM 9189 O  O   . HOH   L 7 .   ? -10.736 18.594  8.362   1.00 28.70 ? 897  HOH   A O   1 
HETATM 9190 O  O   . HOH   L 7 .   ? -0.113  13.206  3.687   1.00 19.70 ? 898  HOH   A O   1 
HETATM 9191 O  O   . HOH   L 7 .   ? -16.619 5.834   57.291  1.00 42.60 ? 899  HOH   A O   1 
HETATM 9192 O  O   . HOH   L 7 .   ? -1.447  -35.672 38.095  1.00 26.37 ? 900  HOH   A O   1 
HETATM 9193 O  O   . HOH   L 7 .   ? -19.398 -6.457  34.001  1.00 10.62 ? 901  HOH   A O   1 
HETATM 9194 O  O   . HOH   L 7 .   ? -0.829  5.299   8.089   1.00 10.13 ? 902  HOH   A O   1 
HETATM 9195 O  O   . HOH   L 7 .   ? -5.061  -16.716 6.519   1.00 14.55 ? 903  HOH   A O   1 
HETATM 9196 O  O   . HOH   L 7 .   ? -37.311 3.484   8.385   1.00 27.41 ? 904  HOH   A O   1 
HETATM 9197 O  O   . HOH   L 7 .   ? -10.472 -24.596 45.247  1.00 17.04 ? 905  HOH   A O   1 
HETATM 9198 O  O   . HOH   L 7 .   ? 7.999   -20.074 24.883  1.00 18.43 ? 906  HOH   A O   1 
HETATM 9199 O  O   . HOH   L 7 .   ? -11.248 17.883  11.115  1.00 14.40 ? 907  HOH   A O   1 
HETATM 9200 O  O   . HOH   L 7 .   ? -18.173 6.099   34.696  1.00 9.32  ? 908  HOH   A O   1 
HETATM 9201 O  O   . HOH   L 7 .   ? -28.519 21.602  21.802  1.00 11.78 ? 909  HOH   A O   1 
HETATM 9202 O  O   . HOH   L 7 .   ? -26.242 -4.285  9.027   1.00 20.28 ? 910  HOH   A O   1 
HETATM 9203 O  O   . HOH   L 7 .   ? -20.124 19.983  24.018  1.00 14.00 ? 911  HOH   A O   1 
HETATM 9204 O  O   . HOH   L 7 .   ? -17.252 -33.617 18.922  1.00 14.07 ? 912  HOH   A O   1 
HETATM 9205 O  O   . HOH   L 7 .   ? -19.758 19.086  32.010  1.00 11.82 ? 913  HOH   A O   1 
HETATM 9206 O  O   . HOH   L 7 .   ? -37.689 0.414   35.219  1.00 27.14 ? 914  HOH   A O   1 
HETATM 9207 O  O   . HOH   L 7 .   ? -6.861  -11.864 16.080  1.00 14.04 ? 915  HOH   A O   1 
HETATM 9208 O  O   . HOH   L 7 .   ? -32.776 -1.722  10.189  1.00 32.80 ? 916  HOH   A O   1 
HETATM 9209 O  O   . HOH   L 7 .   ? -29.709 -3.142  23.884  1.00 24.37 ? 917  HOH   A O   1 
HETATM 9210 O  O   . HOH   L 7 .   ? -4.228  3.005   29.746  1.00 8.73  ? 918  HOH   A O   1 
HETATM 9211 O  O   . HOH   L 7 .   ? -10.572 12.550  34.761  1.00 8.78  ? 919  HOH   A O   1 
HETATM 9212 O  O   . HOH   L 7 .   ? -25.230 -1.352  -4.728  1.00 31.21 ? 920  HOH   A O   1 
HETATM 9213 O  O   . HOH   L 7 .   ? -9.995  -3.096  30.123  1.00 13.72 ? 921  HOH   A O   1 
HETATM 9214 O  O   . HOH   L 7 .   ? -33.342 -0.669  4.279   1.00 28.25 ? 922  HOH   A O   1 
HETATM 9215 O  O   . HOH   L 7 .   ? 3.031   17.514  19.582  1.00 21.47 ? 923  HOH   A O   1 
HETATM 9216 O  O   . HOH   L 7 .   ? -7.546  -22.531 37.748  1.00 14.21 ? 924  HOH   A O   1 
HETATM 9217 O  O   . HOH   L 7 .   ? -15.098 -17.906 12.273  1.00 8.55  ? 925  HOH   A O   1 
HETATM 9218 O  O   . HOH   L 7 .   ? -21.239 5.470   22.326  1.00 9.66  ? 926  HOH   A O   1 
HETATM 9219 O  O   . HOH   L 7 .   ? -15.301 17.099  34.873  1.00 8.84  ? 927  HOH   A O   1 
HETATM 9220 O  O   . HOH   L 7 .   ? -11.757 -1.381  37.316  1.00 9.44  ? 928  HOH   A O   1 
HETATM 9221 O  O   . HOH   L 7 .   ? -9.458  -10.376 23.966  1.00 23.40 ? 929  HOH   A O   1 
HETATM 9222 O  O   . HOH   L 7 .   ? 3.468   1.483   22.187  1.00 23.33 ? 930  HOH   A O   1 
HETATM 9223 O  O   . HOH   L 7 .   ? -6.416  -14.233 36.406  1.00 21.82 ? 931  HOH   A O   1 
HETATM 9224 O  O   . HOH   L 7 .   ? -10.973 -3.607  26.707  1.00 8.08  ? 932  HOH   A O   1 
HETATM 9225 O  O   . HOH   L 7 .   ? -4.682  -4.134  -8.837  1.00 26.47 ? 933  HOH   A O   1 
HETATM 9226 O  O   . HOH   L 7 .   ? -20.397 2.395   -7.336  1.00 22.17 ? 934  HOH   A O   1 
HETATM 9227 O  O   . HOH   L 7 .   ? -2.495  7.003   47.503  1.00 13.24 ? 935  HOH   A O   1 
HETATM 9228 O  O   . HOH   L 7 .   ? -21.805 -13.798 16.243  1.00 10.97 ? 936  HOH   A O   1 
HETATM 9229 O  O   . HOH   L 7 .   ? 6.454   16.158  18.413  1.00 29.51 ? 937  HOH   A O   1 
HETATM 9230 O  O   . HOH   L 7 .   ? -6.295  -12.874 32.383  1.00 22.08 ? 938  HOH   A O   1 
HETATM 9231 O  O   . HOH   L 7 .   ? 1.193   -6.114  27.898  1.00 22.60 ? 939  HOH   A O   1 
HETATM 9232 O  O   . HOH   L 7 .   ? -30.529 -4.713  12.142  1.00 30.05 ? 940  HOH   A O   1 
HETATM 9233 O  O   . HOH   L 7 .   ? -21.032 -13.020 29.286  1.00 17.56 ? 941  HOH   A O   1 
HETATM 9234 O  O   . HOH   L 7 .   ? -33.166 23.962  2.346   1.00 23.61 ? 942  HOH   A O   1 
HETATM 9235 O  O   . HOH   L 7 .   ? -28.429 20.554  4.515   1.00 21.82 ? 943  HOH   A O   1 
HETATM 9236 O  O   . HOH   L 7 .   ? -12.727 -9.618  22.233  1.00 7.55  ? 944  HOH   A O   1 
HETATM 9237 O  O   . HOH   L 7 .   ? -12.829 -22.792 32.417  1.00 17.76 ? 945  HOH   A O   1 
HETATM 9238 O  O   . HOH   L 7 .   ? -25.173 15.296  0.938   1.00 11.08 ? 946  HOH   A O   1 
HETATM 9239 O  O   . HOH   L 7 .   ? -36.112 7.350   13.417  1.00 20.17 ? 947  HOH   A O   1 
HETATM 9240 O  O   . HOH   L 7 .   ? -14.085 15.697  50.307  1.00 29.29 ? 948  HOH   A O   1 
HETATM 9241 O  O   . HOH   L 7 .   ? -37.017 4.930   13.514  1.00 28.90 ? 949  HOH   A O   1 
HETATM 9242 O  O   . HOH   L 7 .   ? -22.253 -10.494 38.958  1.00 21.04 ? 950  HOH   A O   1 
HETATM 9243 O  O   . HOH   L 7 .   ? -12.366 0.970   -8.062  1.00 26.23 ? 951  HOH   A O   1 
HETATM 9244 O  O   . HOH   L 7 .   ? -29.803 9.087   37.629  1.00 20.41 ? 952  HOH   A O   1 
HETATM 9245 O  O   . HOH   L 7 .   ? -6.994  1.339   33.982  1.00 6.79  ? 953  HOH   A O   1 
HETATM 9246 O  O   . HOH   L 7 .   ? 4.564   1.303   8.064   1.00 24.73 ? 954  HOH   A O   1 
HETATM 9247 O  O   . HOH   L 7 .   ? -20.600 22.459  25.749  1.00 19.06 ? 955  HOH   A O   1 
HETATM 9248 O  O   . HOH   L 7 .   ? -10.081 -21.612 38.973  1.00 15.16 ? 956  HOH   A O   1 
HETATM 9249 O  O   . HOH   L 7 .   ? -6.166  -0.039  54.106  1.00 13.83 ? 957  HOH   A O   1 
HETATM 9250 O  O   . HOH   L 7 .   ? -12.107 -4.028  3.984   1.00 12.60 ? 958  HOH   A O   1 
HETATM 9251 O  O   . HOH   L 7 .   ? -12.500 19.685  12.582  1.00 16.83 ? 959  HOH   A O   1 
HETATM 9252 O  O   . HOH   L 7 .   ? -6.807  -27.801 8.740   1.00 27.73 ? 960  HOH   A O   1 
HETATM 9253 O  O   . HOH   L 7 .   ? -2.522  9.398   -1.056  1.00 18.81 ? 961  HOH   A O   1 
HETATM 9254 O  O   . HOH   L 7 .   ? -23.873 12.143  34.864  1.00 13.29 ? 962  HOH   A O   1 
HETATM 9255 O  O   . HOH   L 7 .   ? 1.942   9.782   29.141  1.00 10.07 ? 963  HOH   A O   1 
HETATM 9256 O  O   . HOH   L 7 .   ? -25.260 4.426   -1.354  1.00 14.17 ? 964  HOH   A O   1 
HETATM 9257 O  O   . HOH   L 7 .   ? -14.187 9.551   23.626  1.00 7.90  ? 965  HOH   A O   1 
HETATM 9258 O  O   . HOH   L 7 .   ? -12.315 22.925  29.810  1.00 29.63 ? 966  HOH   A O   1 
HETATM 9259 O  O   . HOH   L 7 .   ? -12.188 9.960   -1.522  1.00 13.55 ? 967  HOH   A O   1 
HETATM 9260 O  O   . HOH   L 7 .   ? -20.539 -15.742 25.396  1.00 27.91 ? 968  HOH   A O   1 
HETATM 9261 O  O   . HOH   L 7 .   ? -13.058 -21.561 37.932  1.00 14.64 ? 969  HOH   A O   1 
HETATM 9262 O  O   . HOH   L 7 .   ? 4.241   16.563  28.119  1.00 21.03 ? 970  HOH   A O   1 
HETATM 9263 O  O   . HOH   L 7 .   ? -1.192  11.997  22.021  1.00 8.26  ? 971  HOH   A O   1 
HETATM 9264 O  O   . HOH   L 7 .   ? -30.516 -3.767  34.166  1.00 22.39 ? 972  HOH   A O   1 
HETATM 9265 O  O   . HOH   L 7 .   ? -8.752  -4.811  28.807  1.00 15.98 ? 973  HOH   A O   1 
HETATM 9266 O  O   . HOH   L 7 .   ? -22.847 12.165  49.883  1.00 23.15 ? 974  HOH   A O   1 
HETATM 9267 O  O   . HOH   L 7 .   ? 1.976   7.088   14.573  1.00 11.27 ? 975  HOH   A O   1 
HETATM 9268 O  O   . HOH   L 7 .   ? -3.378  6.110   43.762  1.00 11.29 ? 976  HOH   A O   1 
HETATM 9269 O  O   . HOH   L 7 .   ? -14.861 -21.448 31.048  1.00 16.31 ? 977  HOH   A O   1 
HETATM 9270 O  O   . HOH   L 7 .   ? -31.516 5.427   0.931   1.00 19.32 ? 978  HOH   A O   1 
HETATM 9271 O  O   . HOH   L 7 .   ? -4.451  3.762   -6.885  1.00 26.62 ? 979  HOH   A O   1 
HETATM 9272 O  O   . HOH   L 7 .   ? -27.258 16.983  23.499  1.00 9.88  ? 980  HOH   A O   1 
HETATM 9273 O  O   . HOH   L 7 .   ? -2.293  14.799  28.612  1.00 10.64 ? 981  HOH   A O   1 
HETATM 9274 O  O   . HOH   L 7 .   ? -27.365 -7.278  39.074  1.00 36.87 ? 982  HOH   A O   1 
HETATM 9275 O  O   . HOH   L 7 .   ? -18.644 19.802  29.719  1.00 12.97 ? 983  HOH   A O   1 
HETATM 9276 O  O   . HOH   L 7 .   ? -10.444 -0.654  28.587  1.00 11.30 ? 984  HOH   A O   1 
HETATM 9277 O  O   . HOH   L 7 .   ? -5.576  -11.250 13.864  1.00 13.99 ? 985  HOH   A O   1 
HETATM 9278 O  O   . HOH   L 7 .   ? -36.264 19.600  17.602  1.00 19.42 ? 986  HOH   A O   1 
HETATM 9279 O  O   . HOH   L 7 .   ? -13.517 -5.473  34.479  1.00 9.68  ? 987  HOH   A O   1 
HETATM 9280 O  O   . HOH   L 7 .   ? -0.877  -6.047  6.633   1.00 19.99 ? 988  HOH   A O   1 
HETATM 9281 O  O   . HOH   L 7 .   ? -26.050 -5.007  32.730  1.00 18.69 ? 989  HOH   A O   1 
HETATM 9282 O  O   . HOH   L 7 .   ? -0.296  8.048   28.933  1.00 7.45  ? 990  HOH   A O   1 
HETATM 9283 O  O   . HOH   L 7 .   ? -7.387  -10.463 4.071   1.00 12.39 ? 991  HOH   A O   1 
HETATM 9284 O  O   . HOH   L 7 .   ? 7.229   -3.419  17.773  1.00 14.26 ? 992  HOH   A O   1 
HETATM 9285 O  O   . HOH   L 7 .   ? -11.087 -6.409  57.388  1.00 39.97 ? 993  HOH   A O   1 
HETATM 9286 O  O   . HOH   L 7 .   ? -22.280 25.357  23.267  1.00 11.10 ? 994  HOH   A O   1 
HETATM 9287 O  O   . HOH   L 7 .   ? -0.660  1.046   32.089  1.00 16.49 ? 995  HOH   A O   1 
HETATM 9288 O  O   . HOH   L 7 .   ? -0.360  5.945   46.221  1.00 23.38 ? 996  HOH   A O   1 
HETATM 9289 O  O   . HOH   L 7 .   ? -16.040 14.677  -3.158  1.00 21.57 ? 997  HOH   A O   1 
HETATM 9290 O  O   . HOH   L 7 .   ? -24.602 -3.593  6.588   1.00 25.74 ? 998  HOH   A O   1 
HETATM 9291 O  O   . HOH   L 7 .   ? -22.244 14.742  45.919  1.00 18.75 ? 999  HOH   A O   1 
HETATM 9292 O  O   . HOH   L 7 .   ? -15.834 -5.935  30.328  1.00 9.32  ? 1000 HOH   A O   1 
HETATM 9293 O  O   . HOH   L 7 .   ? -18.702 -7.751  53.361  1.00 36.64 ? 1001 HOH   A O   1 
HETATM 9294 O  O   . HOH   L 7 .   ? -31.408 4.915   20.108  1.00 16.86 ? 1002 HOH   A O   1 
HETATM 9295 O  O   . HOH   L 7 .   ? -33.348 12.586  28.576  1.00 18.19 ? 1003 HOH   A O   1 
HETATM 9296 O  O   . HOH   L 7 .   ? -34.309 5.082   32.641  1.00 14.64 ? 1004 HOH   A O   1 
HETATM 9297 O  O   . HOH   L 7 .   ? -3.184  11.780  19.039  1.00 7.30  ? 1005 HOH   A O   1 
HETATM 9298 O  O   . HOH   L 7 .   ? -21.356 18.588  41.992  1.00 24.85 ? 1006 HOH   A O   1 
HETATM 9299 O  O   . HOH   L 7 .   ? 2.940   2.440   33.337  1.00 26.77 ? 1007 HOH   A O   1 
HETATM 9300 O  O   . HOH   L 7 .   ? 10.031  1.396   19.460  1.00 16.12 ? 1008 HOH   A O   1 
HETATM 9301 O  O   . HOH   L 7 .   ? -5.330  -10.571 9.793   1.00 10.62 ? 1009 HOH   A O   1 
HETATM 9302 O  O   . HOH   L 7 .   ? -21.732 15.996  33.186  1.00 12.78 ? 1010 HOH   A O   1 
HETATM 9303 O  O   . HOH   L 7 .   ? -20.669 12.734  55.283  1.00 25.06 ? 1011 HOH   A O   1 
HETATM 9304 O  O   . HOH   L 7 .   ? -29.142 14.105  -1.166  1.00 25.85 ? 1012 HOH   A O   1 
HETATM 9305 O  O   . HOH   L 7 .   ? -21.372 24.267  7.437   1.00 26.69 ? 1013 HOH   A O   1 
HETATM 9306 O  O   . HOH   L 7 .   ? 0.315   -9.253  28.506  1.00 25.38 ? 1014 HOH   A O   1 
HETATM 9307 O  O   . HOH   L 7 .   ? 0.230   -9.529  41.748  1.00 20.99 ? 1015 HOH   A O   1 
HETATM 9308 O  O   . HOH   L 7 .   ? -8.276  22.054  37.748  1.00 35.03 ? 1016 HOH   A O   1 
HETATM 9309 O  O   . HOH   L 7 .   ? -32.797 10.307  0.390   1.00 15.44 ? 1017 HOH   A O   1 
HETATM 9310 O  O   . HOH   L 7 .   ? -8.470  18.584  2.931   1.00 32.83 ? 1018 HOH   A O   1 
HETATM 9311 O  O   . HOH   L 7 .   ? 1.483   1.230   51.173  1.00 24.10 ? 1019 HOH   A O   1 
HETATM 9312 O  O   . HOH   L 7 .   ? -6.397  -16.495 54.283  1.00 21.35 ? 1020 HOH   A O   1 
HETATM 9313 O  O   . HOH   L 7 .   ? -16.829 19.086  2.111   1.00 22.73 ? 1021 HOH   A O   1 
HETATM 9314 O  O   . HOH   L 7 .   ? -18.794 2.038   28.118  1.00 14.04 ? 1022 HOH   A O   1 
HETATM 9315 O  O   . HOH   L 7 .   ? -16.742 -0.594  54.121  1.00 27.93 ? 1023 HOH   A O   1 
HETATM 9316 O  O   . HOH   L 7 .   ? -7.070  -20.517 48.959  1.00 37.57 ? 1024 HOH   A O   1 
HETATM 9317 O  O   . HOH   L 7 .   ? -3.527  -26.904 39.179  1.00 31.12 ? 1025 HOH   A O   1 
HETATM 9318 O  O   . HOH   L 7 .   ? -16.488 3.415   56.368  1.00 27.03 ? 1026 HOH   A O   1 
HETATM 9319 O  O   . HOH   L 7 .   ? -7.473  -10.812 33.232  1.00 20.04 ? 1027 HOH   A O   1 
HETATM 9320 O  O   . HOH   L 7 .   ? -2.080  16.910  48.976  1.00 31.79 ? 1028 HOH   A O   1 
HETATM 9321 O  O   . HOH   L 7 .   ? -29.691 4.344   38.651  1.00 12.58 ? 1029 HOH   A O   1 
HETATM 9322 O  O   . HOH   L 7 .   ? -0.568  -12.956 47.352  1.00 18.49 ? 1030 HOH   A O   1 
HETATM 9323 O  O   . HOH   L 7 .   ? -13.350 -25.824 22.385  1.00 13.26 ? 1031 HOH   A O   1 
HETATM 9324 O  O   . HOH   L 7 .   ? -6.567  -15.180 33.931  1.00 11.94 ? 1032 HOH   A O   1 
HETATM 9325 O  O   . HOH   L 7 .   ? -30.363 -3.272  31.081  1.00 15.56 ? 1033 HOH   A O   1 
HETATM 9326 O  O   . HOH   L 7 .   ? -1.442  18.401  7.685   1.00 31.90 ? 1034 HOH   A O   1 
HETATM 9327 O  O   . HOH   L 7 .   ? -23.187 24.822  14.824  1.00 14.53 ? 1035 HOH   A O   1 
HETATM 9328 O  O   . HOH   L 7 .   ? -24.253 25.220  10.462  1.00 24.65 ? 1036 HOH   A O   1 
HETATM 9329 O  O   . HOH   L 7 .   ? -6.398  10.053  31.933  1.00 8.55  ? 1037 HOH   A O   1 
HETATM 9330 O  O   . HOH   L 7 .   ? 2.860   -14.074 34.040  1.00 12.76 ? 1038 HOH   A O   1 
HETATM 9331 O  O   . HOH   L 7 .   ? -5.400  -12.923 11.305  1.00 13.75 ? 1039 HOH   A O   1 
HETATM 9332 O  O   . HOH   L 7 .   ? -19.596 -32.676 22.591  1.00 10.76 ? 1040 HOH   A O   1 
HETATM 9333 O  O   . HOH   L 7 .   ? -20.118 1.166   55.485  1.00 30.30 ? 1041 HOH   A O   1 
HETATM 9334 O  O   . HOH   L 7 .   ? -7.722  13.196  41.146  1.00 10.75 ? 1042 HOH   A O   1 
HETATM 9335 O  O   . HOH   L 7 .   ? -2.996  -14.116 55.002  1.00 40.45 ? 1043 HOH   A O   1 
HETATM 9336 O  O   . HOH   L 7 .   ? 6.260   -8.802  13.656  1.00 26.33 ? 1044 HOH   A O   1 
HETATM 9337 O  O   . HOH   L 7 .   ? -1.621  22.743  27.225  1.00 15.18 ? 1045 HOH   A O   1 
HETATM 9338 O  O   . HOH   L 7 .   ? -25.844 -2.316  35.459  1.00 9.90  ? 1046 HOH   A O   1 
HETATM 9339 O  O   . HOH   L 7 .   ? -3.812  3.227   52.419  1.00 16.48 ? 1047 HOH   A O   1 
HETATM 9340 O  O   . HOH   L 7 .   ? -33.493 18.658  26.520  1.00 16.64 ? 1048 HOH   A O   1 
HETATM 9341 O  O   . HOH   L 7 .   ? -10.131 11.852  -7.187  1.00 25.16 ? 1049 HOH   A O   1 
HETATM 9342 O  O   . HOH   L 7 .   ? -7.139  -2.090  27.279  1.00 13.28 ? 1050 HOH   A O   1 
HETATM 9343 O  O   . HOH   L 7 .   ? -0.800  -31.737 18.783  1.00 30.18 ? 1051 HOH   A O   1 
HETATM 9344 O  O   . HOH   L 7 .   ? -2.879  8.759   7.512   1.00 9.93  ? 1052 HOH   A O   1 
HETATM 9345 O  O   . HOH   L 7 .   ? 3.647   -30.257 29.842  1.00 33.70 ? 1053 HOH   A O   1 
HETATM 9346 O  O   . HOH   L 7 .   ? 1.957   15.034  27.289  1.00 12.41 ? 1054 HOH   A O   1 
HETATM 9347 O  O   . HOH   L 7 .   ? -28.439 22.387  14.729  1.00 38.08 ? 1055 HOH   A O   1 
HETATM 9348 O  O   . HOH   L 7 .   ? 1.446   1.248   35.554  1.00 12.00 ? 1056 HOH   A O   1 
HETATM 9349 O  O   . HOH   L 7 .   ? -2.416  21.015  8.516   1.00 26.54 ? 1057 HOH   A O   1 
HETATM 9350 O  O   . HOH   L 7 .   ? -21.288 8.218   22.314  1.00 10.46 ? 1058 HOH   A O   1 
HETATM 9351 O  O   . HOH   L 7 .   ? -4.623  -24.684 43.243  1.00 31.89 ? 1059 HOH   A O   1 
HETATM 9352 O  O   . HOH   L 7 .   ? -19.563 5.942   6.761   1.00 8.42  ? 1060 HOH   A O   1 
HETATM 9353 O  O   . HOH   L 7 .   ? -2.456  -6.865  8.335   1.00 20.95 ? 1061 HOH   A O   1 
HETATM 9354 O  O   . HOH   L 7 .   ? -31.773 17.395  29.163  1.00 36.99 ? 1062 HOH   A O   1 
HETATM 9355 O  O   . HOH   L 7 .   ? -6.875  -11.227 23.184  1.00 12.88 ? 1063 HOH   A O   1 
HETATM 9356 O  O   . HOH   L 7 .   ? -11.573 -7.897  -3.760  1.00 24.87 ? 1064 HOH   A O   1 
HETATM 9357 O  O   . HOH   L 7 .   ? -18.875 21.384  4.003   1.00 26.55 ? 1065 HOH   A O   1 
HETATM 9358 O  O   . HOH   L 7 .   ? -3.323  8.208   56.410  1.00 18.75 ? 1066 HOH   A O   1 
HETATM 9359 O  O   . HOH   L 7 .   ? -3.207  9.256   20.224  1.00 9.86  ? 1067 HOH   A O   1 
HETATM 9360 O  O   . HOH   L 7 .   ? -16.896 23.652  33.328  1.00 19.37 ? 1068 HOH   A O   1 
HETATM 9361 O  O   . HOH   L 7 .   ? -20.415 9.116   19.727  1.00 6.31  ? 1069 HOH   A O   1 
HETATM 9362 O  O   . HOH   L 7 .   ? 3.831   -15.901 19.772  1.00 23.15 ? 1070 HOH   A O   1 
HETATM 9363 O  O   . HOH   L 7 .   ? -23.212 1.813   -7.124  1.00 24.77 ? 1071 HOH   A O   1 
HETATM 9364 O  O   . HOH   L 7 .   ? -8.973  -31.204 12.881  1.00 22.56 ? 1072 HOH   A O   1 
HETATM 9365 O  O   . HOH   L 7 .   ? 8.755   13.452  16.940  1.00 19.77 ? 1073 HOH   A O   1 
HETATM 9366 O  O   . HOH   L 7 .   ? -21.468 -4.106  30.447  1.00 12.84 ? 1074 HOH   A O   1 
HETATM 9367 O  O   . HOH   L 7 .   ? -2.204  -24.447 42.386  1.00 22.86 ? 1075 HOH   A O   1 
HETATM 9368 O  O   . HOH   L 7 .   ? 0.176   18.523  20.125  1.00 33.03 ? 1076 HOH   A O   1 
HETATM 9369 O  O   . HOH   L 7 .   ? -22.041 -13.080 32.071  1.00 16.66 ? 1077 HOH   A O   1 
HETATM 9370 O  O   . HOH   L 7 .   ? -30.535 11.791  -0.332  1.00 17.45 ? 1078 HOH   A O   1 
HETATM 9371 O  O   . HOH   L 7 .   ? 2.402   10.715  31.894  1.00 18.48 ? 1079 HOH   A O   1 
HETATM 9372 O  O   . HOH   L 7 .   ? -15.473 -23.820 42.682  1.00 22.93 ? 1080 HOH   A O   1 
HETATM 9373 O  O   . HOH   L 7 .   ? -11.226 -7.049  34.072  1.00 11.73 ? 1081 HOH   A O   1 
HETATM 9374 O  O   . HOH   L 7 .   ? -18.632 -19.258 50.770  1.00 31.02 ? 1082 HOH   A O   1 
HETATM 9375 O  O   . HOH   L 7 .   ? 3.565   2.253   4.105   1.00 22.02 ? 1083 HOH   A O   1 
HETATM 9376 O  O   . HOH   L 7 .   ? -23.588 14.459  31.591  1.00 10.88 ? 1084 HOH   A O   1 
HETATM 9377 O  O   . HOH   L 7 .   ? -1.140  10.418  45.400  1.00 31.63 ? 1085 HOH   A O   1 
HETATM 9378 O  O   . HOH   L 7 .   ? -6.371  -33.355 34.969  1.00 31.22 ? 1086 HOH   A O   1 
HETATM 9379 O  O   . HOH   L 7 .   ? -39.275 11.430  22.744  1.00 40.96 ? 1087 HOH   A O   1 
HETATM 9380 O  O   . HOH   L 7 .   ? -8.410  -27.906 24.940  1.00 27.21 ? 1088 HOH   A O   1 
HETATM 9381 O  O   . HOH   L 7 .   ? -29.114 5.122   -1.303  1.00 26.03 ? 1089 HOH   A O   1 
HETATM 9382 O  O   . HOH   L 7 .   ? -3.449  -10.181 16.814  1.00 11.19 ? 1090 HOH   A O   1 
HETATM 9383 O  O   . HOH   L 7 .   ? -27.261 8.291   -9.358  1.00 19.26 ? 1091 HOH   A O   1 
HETATM 9384 O  O   . HOH   L 7 .   ? -31.632 -1.668  22.814  1.00 19.33 ? 1092 HOH   A O   1 
HETATM 9385 O  O   . HOH   L 7 .   ? -13.971 -9.490  24.818  1.00 8.82  ? 1093 HOH   A O   1 
HETATM 9386 O  O   . HOH   L 7 .   ? -1.311  -0.791  44.141  1.00 9.77  ? 1094 HOH   A O   1 
HETATM 9387 O  O   . HOH   L 7 .   ? -36.169 10.955  10.554  1.00 21.91 ? 1095 HOH   A O   1 
HETATM 9388 O  O   . HOH   L 7 .   ? -18.048 -15.960 26.888  1.00 20.80 ? 1096 HOH   A O   1 
HETATM 9389 O  O   . HOH   L 7 .   ? -23.405 -15.646 12.518  1.00 33.61 ? 1097 HOH   A O   1 
HETATM 9390 O  O   . HOH   L 7 .   ? -19.344 20.871  39.216  1.00 12.94 ? 1098 HOH   A O   1 
HETATM 9391 O  O   . HOH   L 7 .   ? -27.905 15.054  13.794  1.00 10.80 ? 1099 HOH   A O   1 
HETATM 9392 O  O   . HOH   L 7 .   ? -6.661  11.617  54.620  1.00 15.90 ? 1100 HOH   A O   1 
HETATM 9393 O  O   . HOH   L 7 .   ? -12.698 -10.679 27.091  1.00 7.57  ? 1101 HOH   A O   1 
HETATM 9394 O  O   . HOH   L 7 .   ? -13.522 -14.352 1.569   1.00 27.82 ? 1102 HOH   A O   1 
HETATM 9395 O  O   . HOH   L 7 .   ? -20.658 -12.098 41.345  1.00 25.63 ? 1103 HOH   A O   1 
HETATM 9396 O  O   . HOH   L 7 .   ? -7.458  15.851  52.300  1.00 16.32 ? 1104 HOH   A O   1 
HETATM 9397 O  O   . HOH   L 7 .   ? -19.717 -0.075  51.564  1.00 20.73 ? 1105 HOH   A O   1 
HETATM 9398 O  O   . HOH   L 7 .   ? -27.594 7.751   41.026  1.00 14.62 ? 1106 HOH   A O   1 
HETATM 9399 O  O   . HOH   L 7 .   ? -36.924 5.036   10.876  1.00 22.93 ? 1107 HOH   A O   1 
HETATM 9400 O  O   . HOH   L 7 .   ? -0.860  -5.810  4.235   1.00 22.05 ? 1108 HOH   A O   1 
HETATM 9401 O  O   . HOH   L 7 .   ? -30.697 22.110  14.997  1.00 20.89 ? 1109 HOH   A O   1 
HETATM 9402 O  O   . HOH   L 7 .   ? 2.522   -5.571  41.264  1.00 24.21 ? 1110 HOH   A O   1 
HETATM 9403 O  O   . HOH   L 7 .   ? -5.997  10.027  57.872  1.00 29.15 ? 1111 HOH   A O   1 
HETATM 9404 O  O   . HOH   L 7 .   ? -17.588 -18.732 5.469   1.00 13.37 ? 1112 HOH   A O   1 
HETATM 9405 O  O   . HOH   L 7 .   ? -20.041 2.931   25.632  1.00 8.62  ? 1113 HOH   A O   1 
HETATM 9406 O  O   . HOH   L 7 .   ? -17.259 -0.211  32.144  1.00 10.68 ? 1114 HOH   A O   1 
HETATM 9407 O  O   . HOH   L 7 .   ? -0.650  -15.301 54.309  1.00 35.36 ? 1115 HOH   A O   1 
HETATM 9408 O  O   . HOH   L 7 .   ? -12.187 -4.740  30.439  1.00 10.45 ? 1116 HOH   A O   1 
HETATM 9409 O  O   . HOH   L 7 .   ? -2.521  5.536   52.903  1.00 21.44 ? 1117 HOH   A O   1 
HETATM 9410 O  O   . HOH   L 7 .   ? 7.768   7.120   5.749   1.00 38.21 ? 1118 HOH   A O   1 
HETATM 9411 O  O   . HOH   L 7 .   ? -1.596  -6.225  29.531  1.00 24.83 ? 1119 HOH   A O   1 
HETATM 9412 O  O   . HOH   L 7 .   ? -4.397  -26.952 7.880   1.00 48.65 ? 1120 HOH   A O   1 
HETATM 9413 O  O   . HOH   L 7 .   ? -2.508  13.275  2.083   1.00 17.65 ? 1121 HOH   A O   1 
HETATM 9414 O  O   . HOH   L 7 .   ? -30.480 -1.487  19.713  1.00 20.95 ? 1122 HOH   A O   1 
HETATM 9415 O  O   . HOH   L 7 .   ? -30.400 16.810  20.220  1.00 10.63 ? 1123 HOH   A O   1 
HETATM 9416 O  O   . HOH   L 7 .   ? 9.131   8.912   13.627  1.00 11.95 ? 1124 HOH   A O   1 
HETATM 9417 O  O   . HOH   L 7 .   ? -13.046 24.136  36.853  1.00 36.09 ? 1125 HOH   A O   1 
HETATM 9418 O  O   . HOH   L 7 .   ? -15.426 12.957  50.776  1.00 24.66 ? 1126 HOH   A O   1 
HETATM 9419 O  O   . HOH   L 7 .   ? 7.423   2.237   27.156  1.00 25.70 ? 1127 HOH   A O   1 
HETATM 9420 O  O   . HOH   L 7 .   ? -5.636  8.122   18.161  1.00 14.48 ? 1128 HOH   A O   1 
HETATM 9421 O  O   . HOH   L 7 .   ? -1.392  -7.000  -3.830  1.00 34.98 ? 1129 HOH   A O   1 
HETATM 9422 O  O   . HOH   L 7 .   ? -12.711 19.584  6.881   1.00 25.50 ? 1130 HOH   A O   1 
HETATM 9423 O  O   . HOH   L 7 .   ? -23.970 8.886   47.505  1.00 13.54 ? 1131 HOH   A O   1 
HETATM 9424 O  O   . HOH   L 7 .   ? -8.077  21.713  27.249  1.00 29.80 ? 1132 HOH   A O   1 
HETATM 9425 O  O   . HOH   L 7 .   ? -35.982 13.371  3.940   1.00 16.79 ? 1133 HOH   A O   1 
HETATM 9426 O  O   . HOH   L 7 .   ? 7.414   7.078   32.627  1.00 24.55 ? 1134 HOH   A O   1 
HETATM 9427 O  O   . HOH   L 7 .   ? 7.635   10.725  11.648  1.00 17.99 ? 1135 HOH   A O   1 
HETATM 9428 O  O   . HOH   L 7 .   ? -25.021 -9.772  12.661  1.00 38.60 ? 1136 HOH   A O   1 
HETATM 9429 O  O   . HOH   L 7 .   ? 1.146   20.218  22.237  1.00 25.94 ? 1137 HOH   A O   1 
HETATM 9430 O  O   . HOH   L 7 .   ? 9.758   1.680   14.930  1.00 12.45 ? 1138 HOH   A O   1 
HETATM 9431 O  O   . HOH   L 7 .   ? -22.926 -12.344 27.439  1.00 20.22 ? 1139 HOH   A O   1 
HETATM 9432 O  O   . HOH   L 7 .   ? -25.182 -8.816  10.097  1.00 29.31 ? 1140 HOH   A O   1 
HETATM 9433 O  O   . HOH   L 7 .   ? -33.181 7.638   0.941   1.00 21.35 ? 1141 HOH   A O   1 
HETATM 9434 O  O   . HOH   L 7 .   ? -33.152 15.460  27.858  1.00 23.42 ? 1142 HOH   A O   1 
HETATM 9435 O  O   . HOH   L 7 .   ? 0.803   -14.139 14.350  1.00 26.51 ? 1143 HOH   A O   1 
HETATM 9436 O  O   . HOH   L 7 .   ? -19.218 -10.143 45.752  1.00 40.17 ? 1144 HOH   A O   1 
HETATM 9437 O  O   . HOH   L 7 .   ? -1.178  -11.215 17.891  1.00 11.92 ? 1145 HOH   A O   1 
HETATM 9438 O  O   . HOH   L 7 .   ? 5.802   16.116  15.376  1.00 26.84 ? 1146 HOH   A O   1 
HETATM 9439 O  O   . HOH   L 7 .   ? -24.199 16.839  42.362  1.00 40.75 ? 1147 HOH   A O   1 
HETATM 9440 O  O   . HOH   L 7 .   ? -36.977 1.039   12.182  1.00 24.11 ? 1148 HOH   A O   1 
HETATM 9441 O  O   . HOH   L 7 .   ? 0.530   -12.441 33.201  1.00 28.25 ? 1149 HOH   A O   1 
HETATM 9442 O  O   . HOH   L 7 .   ? -7.210  -2.355  53.054  1.00 10.67 ? 1150 HOH   A O   1 
HETATM 9443 O  O   . HOH   L 7 .   ? -33.867 3.441   22.670  1.00 33.49 ? 1151 HOH   A O   1 
HETATM 9444 O  O   . HOH   L 7 .   ? -8.614  -7.093  34.935  1.00 11.13 ? 1152 HOH   A O   1 
HETATM 9445 O  O   . HOH   L 7 .   ? -23.008 9.293   50.101  1.00 13.33 ? 1153 HOH   A O   1 
HETATM 9446 O  O   . HOH   L 7 .   ? -1.495  9.165   -4.279  1.00 31.17 ? 1154 HOH   A O   1 
HETATM 9447 O  O   . HOH   L 7 .   ? -22.405 -14.963 18.640  1.00 14.65 ? 1155 HOH   A O   1 
HETATM 9448 O  O   . HOH   L 7 .   ? -11.835 -7.329  31.483  1.00 11.52 ? 1156 HOH   A O   1 
HETATM 9449 O  O   . HOH   L 7 .   ? -7.202  -31.631 15.046  1.00 19.42 ? 1157 HOH   A O   1 
HETATM 9450 O  O   . HOH   L 7 .   ? -0.766  -24.804 39.875  1.00 20.83 ? 1158 HOH   A O   1 
HETATM 9451 O  O   . HOH   L 7 .   ? -14.419 4.915   57.576  1.00 28.48 ? 1159 HOH   A O   1 
HETATM 9452 O  O   . HOH   L 7 .   ? -18.949 19.490  41.485  1.00 12.30 ? 1160 HOH   A O   1 
HETATM 9453 O  O   . HOH   L 7 .   ? -14.923 -10.531 3.186   1.00 26.78 ? 1161 HOH   A O   1 
HETATM 9454 O  O   . HOH   L 7 .   ? -24.968 22.758  2.552   1.00 32.86 ? 1162 HOH   A O   1 
HETATM 9455 O  O   . HOH   L 7 .   ? -19.847 22.210  28.374  1.00 18.70 ? 1163 HOH   A O   1 
HETATM 9456 O  O   . HOH   L 7 .   ? -19.218 -14.663 5.395   1.00 26.74 ? 1164 HOH   A O   1 
HETATM 9457 O  O   . HOH   L 7 .   ? -12.421 12.275  56.567  1.00 40.41 ? 1165 HOH   A O   1 
HETATM 9458 O  O   . HOH   L 7 .   ? -21.860 21.649  38.361  1.00 15.49 ? 1166 HOH   A O   1 
HETATM 9459 O  O   . HOH   L 7 .   ? -24.723 -16.227 18.855  1.00 26.37 ? 1167 HOH   A O   1 
HETATM 9460 O  O   . HOH   L 7 .   ? -20.728 28.186  30.373  1.00 41.49 ? 1168 HOH   A O   1 
HETATM 9461 O  O   . HOH   L 7 .   ? -28.350 -5.304  30.617  1.00 17.35 ? 1169 HOH   A O   1 
HETATM 9462 O  O   . HOH   L 7 .   ? 2.542   -1.017  7.674   1.00 24.54 ? 1170 HOH   A O   1 
HETATM 9463 O  O   . HOH   L 7 .   ? -18.761 -18.165 41.323  1.00 39.43 ? 1171 HOH   A O   1 
HETATM 9464 O  O   . HOH   L 7 .   ? -15.153 -13.330 3.493   1.00 17.67 ? 1172 HOH   A O   1 
HETATM 9465 O  O   . HOH   L 7 .   ? -26.643 9.134   55.960  1.00 30.52 ? 1173 HOH   A O   1 
HETATM 9466 O  O   . HOH   L 7 .   ? -17.004 -14.592 56.049  1.00 46.73 ? 1174 HOH   A O   1 
HETATM 9467 O  O   . HOH   L 7 .   ? 0.906   10.563  20.859  1.00 10.86 ? 1175 HOH   A O   1 
HETATM 9468 O  O   . HOH   L 7 .   ? 2.280   -26.013 15.224  1.00 27.84 ? 1176 HOH   A O   1 
HETATM 9469 O  O   . HOH   L 7 .   ? -16.860 -2.894  32.901  1.00 9.89  ? 1177 HOH   A O   1 
HETATM 9470 O  O   . HOH   L 7 .   ? -30.950 -3.152  42.864  1.00 19.65 ? 1178 HOH   A O   1 
HETATM 9471 O  O   . HOH   L 7 .   ? -9.899  -10.511 26.666  1.00 25.41 ? 1179 HOH   A O   1 
HETATM 9472 O  O   . HOH   L 7 .   ? -37.474 13.912  27.432  1.00 40.88 ? 1180 HOH   A O   1 
HETATM 9473 O  O   . HOH   L 7 .   ? -14.633 -11.251 60.202  1.00 42.80 ? 1181 HOH   A O   1 
HETATM 9474 O  O   . HOH   L 7 .   ? -25.096 15.629  48.049  1.00 43.95 ? 1182 HOH   A O   1 
HETATM 9475 O  O   . HOH   L 7 .   ? -7.357  -25.055 38.154  1.00 29.81 ? 1183 HOH   A O   1 
HETATM 9476 O  O   . HOH   L 7 .   ? -5.443  12.180  -1.302  1.00 22.69 ? 1184 HOH   A O   1 
HETATM 9477 O  O   . HOH   L 7 .   ? -0.341  9.123   0.589   1.00 21.48 ? 1185 HOH   A O   1 
HETATM 9478 O  O   . HOH   L 7 .   ? -5.205  -8.691  58.199  1.00 35.71 ? 1186 HOH   A O   1 
HETATM 9479 O  O   . HOH   L 7 .   ? -1.737  -6.437  35.536  1.00 24.29 ? 1187 HOH   A O   1 
HETATM 9480 O  O   . HOH   L 7 .   ? -18.332 -2.135  52.583  1.00 20.95 ? 1188 HOH   A O   1 
HETATM 9481 O  O   . HOH   L 7 .   ? -21.498 -1.245  30.479  1.00 10.47 ? 1189 HOH   A O   1 
HETATM 9482 O  O   . HOH   L 7 .   ? -9.615  15.037  0.680   1.00 30.07 ? 1190 HOH   A O   1 
HETATM 9483 O  O   . HOH   L 7 .   ? -29.345 -4.528  43.847  1.00 37.40 ? 1191 HOH   A O   1 
HETATM 9484 O  O   . HOH   L 7 .   ? -19.094 -19.458 20.075  1.00 33.85 ? 1192 HOH   A O   1 
HETATM 9485 O  O   . HOH   L 7 .   ? 2.552   15.996  6.768   1.00 28.14 ? 1193 HOH   A O   1 
HETATM 9486 O  O   . HOH   L 7 .   ? -37.485 21.334  13.143  1.00 36.61 ? 1194 HOH   A O   1 
HETATM 9487 O  O   . HOH   L 7 .   ? -23.230 17.153  45.967  1.00 35.79 ? 1195 HOH   A O   1 
HETATM 9488 O  O   . HOH   L 7 .   ? -26.164 -18.886 11.514  1.00 45.60 ? 1196 HOH   A O   1 
HETATM 9489 O  O   . HOH   L 7 .   ? 0.359   12.493  34.373  1.00 28.69 ? 1197 HOH   A O   1 
HETATM 9490 O  O   . HOH   L 7 .   ? -15.798 28.010  23.499  1.00 29.60 ? 1198 HOH   A O   1 
HETATM 9491 O  O   . HOH   L 7 .   ? -21.434 -18.232 16.202  1.00 19.44 ? 1199 HOH   A O   1 
HETATM 9492 O  O   . HOH   L 7 .   ? -18.091 -17.371 33.266  1.00 41.16 ? 1200 HOH   A O   1 
HETATM 9493 O  O   . HOH   L 7 .   ? -14.559 -4.520  32.297  1.00 8.10  ? 1201 HOH   A O   1 
HETATM 9494 O  O   . HOH   L 7 .   ? 7.494   -6.254  17.726  1.00 19.93 ? 1202 HOH   A O   1 
HETATM 9495 O  O   . HOH   L 7 .   ? -24.302 12.957  47.713  1.00 26.48 ? 1203 HOH   A O   1 
HETATM 9496 O  O   . HOH   L 7 .   ? -7.760  19.713  47.734  1.00 37.55 ? 1204 HOH   A O   1 
HETATM 9497 O  O   . HOH   L 7 .   ? -19.389 0.121   30.202  1.00 15.42 ? 1205 HOH   A O   1 
HETATM 9498 O  O   . HOH   L 7 .   ? 9.340   -0.913  14.411  1.00 17.94 ? 1206 HOH   A O   1 
HETATM 9499 O  O   . HOH   L 7 .   ? -22.168 -7.567  -5.411  1.00 39.07 ? 1207 HOH   A O   1 
HETATM 9500 O  O   . HOH   L 7 .   ? -7.404  -0.023  56.899  1.00 26.80 ? 1208 HOH   A O   1 
HETATM 9501 O  O   . HOH   L 7 .   ? -22.688 -5.635  6.776   1.00 31.55 ? 1209 HOH   A O   1 
HETATM 9502 O  O   . HOH   L 7 .   ? -9.421  -12.543 15.126  1.00 24.95 ? 1210 HOH   A O   1 
HETATM 9503 O  O   . HOH   L 7 .   ? -18.265 18.500  -0.904  1.00 33.46 ? 1211 HOH   A O   1 
HETATM 9504 O  O   . HOH   L 7 .   ? 4.180   -15.824 27.822  1.00 15.36 ? 1212 HOH   A O   1 
HETATM 9505 O  O   . HOH   L 7 .   ? -26.141 27.981  24.579  1.00 28.57 ? 1213 HOH   A O   1 
HETATM 9506 O  O   . HOH   L 7 .   ? 4.662   10.119  32.902  1.00 30.19 ? 1214 HOH   A O   1 
HETATM 9507 O  O   . HOH   L 7 .   ? -37.681 14.270  2.229   1.00 36.15 ? 1215 HOH   A O   1 
HETATM 9508 O  O   . HOH   L 7 .   ? 4.016   -17.726 29.077  1.00 1.37  ? 1216 HOH   A O   1 
HETATM 9509 O  O   . HOH   L 7 .   ? 2.376   -36.292 34.623  1.00 31.04 ? 1217 HOH   A O   1 
HETATM 9510 O  O   . HOH   L 7 .   ? 5.288   -10.572 15.330  1.00 46.78 ? 1218 HOH   A O   1 
HETATM 9511 O  O   . HOH   L 7 .   ? -31.428 -2.355  3.107   1.00 37.70 ? 1219 HOH   A O   1 
HETATM 9512 O  O   . HOH   L 7 .   ? -19.370 -9.672  50.547  1.00 38.40 ? 1220 HOH   A O   1 
HETATM 9513 O  O   . HOH   L 7 .   ? -18.274 -5.011  31.857  1.00 17.14 ? 1221 HOH   A O   1 
HETATM 9514 O  O   . HOH   L 7 .   ? -29.805 7.026   39.383  1.00 17.76 ? 1222 HOH   A O   1 
HETATM 9515 O  O   . HOH   L 7 .   ? 11.207  2.538   12.996  1.00 24.52 ? 1223 HOH   A O   1 
HETATM 9516 O  O   . HOH   L 7 .   ? -9.387  -8.433  30.890  1.00 20.94 ? 1224 HOH   A O   1 
HETATM 9517 O  O   . HOH   L 7 .   ? -1.598  6.854   50.234  1.00 23.56 ? 1225 HOH   A O   1 
HETATM 9518 O  O   . HOH   L 7 .   ? -3.717  -11.854 4.939   1.00 33.55 ? 1226 HOH   A O   1 
HETATM 9519 O  O   . HOH   L 7 .   ? -26.226 -12.056 17.386  1.00 30.38 ? 1227 HOH   A O   1 
HETATM 9520 O  O   . HOH   L 7 .   ? -5.135  -11.187 2.772   1.00 21.37 ? 1228 HOH   A O   1 
HETATM 9521 O  O   . HOH   L 7 .   ? -22.599 -20.516 16.433  1.00 32.97 ? 1229 HOH   A O   1 
HETATM 9522 O  O   . HOH   L 7 .   ? -1.591  8.227   43.659  1.00 16.81 ? 1230 HOH   A O   1 
HETATM 9523 O  O   . HOH   L 7 .   ? -21.391 -15.333 33.121  1.00 28.87 ? 1231 HOH   A O   1 
HETATM 9524 O  O   . HOH   L 7 .   ? -11.854 13.227  54.379  1.00 46.02 ? 1232 HOH   A O   1 
HETATM 9525 O  O   . HOH   L 7 .   ? -36.317 11.961  28.725  1.00 36.33 ? 1233 HOH   A O   1 
HETATM 9526 O  O   . HOH   L 7 .   ? -18.768 -15.048 29.299  1.00 27.44 ? 1234 HOH   A O   1 
HETATM 9527 O  O   . HOH   L 7 .   ? -14.833 -1.149  -7.570  1.00 38.77 ? 1235 HOH   A O   1 
HETATM 9528 O  O   . HOH   L 7 .   ? -3.962  -14.836 4.744   1.00 28.21 ? 1236 HOH   A O   1 
HETATM 9529 O  O   . HOH   L 7 .   ? 9.525   -2.632  16.584  1.00 15.36 ? 1237 HOH   A O   1 
HETATM 9530 O  O   . HOH   L 7 .   ? 3.201   -11.321 16.369  1.00 33.16 ? 1238 HOH   A O   1 
HETATM 9531 O  O   . HOH   L 7 .   ? 0.402   -13.658 38.714  1.00 30.40 ? 1239 HOH   A O   1 
HETATM 9532 O  O   . HOH   L 7 .   ? 0.693   -11.824 15.654  1.00 19.13 ? 1240 HOH   A O   1 
HETATM 9533 O  O   . HOH   L 7 .   ? -17.401 -14.745 3.687   1.00 27.32 ? 1241 HOH   A O   1 
HETATM 9534 O  O   . HOH   L 7 .   ? -13.122 21.689  10.341  1.00 40.34 ? 1242 HOH   A O   1 
HETATM 9535 O  O   . HOH   L 7 .   ? -41.279 4.428   8.100   1.00 37.02 ? 1243 HOH   A O   1 
HETATM 9536 O  O   . HOH   L 7 .   ? -11.869 -24.655 36.772  1.00 43.66 ? 1244 HOH   A O   1 
HETATM 9537 O  O   . HOH   L 7 .   ? 7.815   -3.140  20.551  1.00 17.02 ? 1245 HOH   A O   1 
HETATM 9538 O  O   . HOH   L 7 .   ? -13.678 -17.132 0.752   1.00 43.70 ? 1246 HOH   A O   1 
HETATM 9539 O  O   . HOH   M 7 .   ? -42.654 0.193   12.787  1.00 19.57 ? 801  HOH   B O   1 
HETATM 9540 O  O   . HOH   M 7 .   ? -44.170 17.142  21.273  1.00 27.29 ? 802  HOH   B O   1 
HETATM 9541 O  O   . HOH   M 7 .   ? -56.325 1.242   62.772  1.00 40.34 ? 803  HOH   B O   1 
HETATM 9542 O  O   . HOH   M 7 .   ? -69.233 4.310   56.943  1.00 29.33 ? 804  HOH   B O   1 
HETATM 9543 O  O   . HOH   M 7 .   ? -65.741 8.883   20.044  1.00 32.19 ? 805  HOH   B O   1 
HETATM 9544 O  O   . HOH   M 7 .   ? -39.091 -1.910  17.298  1.00 27.66 ? 806  HOH   B O   1 
HETATM 9545 O  O   . HOH   M 7 .   ? -48.886 -24.150 41.035  1.00 32.52 ? 807  HOH   B O   1 
HETATM 9546 O  O   . HOH   M 7 .   ? -71.265 -4.036  51.554  1.00 22.86 ? 808  HOH   B O   1 
HETATM 9547 O  O   . HOH   M 7 .   ? -42.126 -1.989  14.613  1.00 20.75 ? 809  HOH   B O   1 
HETATM 9548 O  O   . HOH   M 7 .   ? -42.142 -30.096 22.407  1.00 23.20 ? 810  HOH   B O   1 
HETATM 9549 O  O   . HOH   M 7 .   ? -62.204 -8.836  7.603   1.00 37.25 ? 811  HOH   B O   1 
HETATM 9550 O  O   . HOH   M 7 .   ? -33.038 -2.760  30.666  1.00 22.63 ? 812  HOH   B O   1 
HETATM 9551 O  O   . HOH   M 7 .   ? -49.182 -13.446 48.296  1.00 23.09 ? 813  HOH   B O   1 
HETATM 9552 O  O   . HOH   M 7 .   ? -57.250 2.414   67.257  1.00 44.09 ? 814  HOH   B O   1 
HETATM 9553 O  O   . HOH   M 7 .   ? -54.173 21.526  44.273  1.00 35.09 ? 815  HOH   B O   1 
HETATM 9554 O  O   . HOH   M 7 .   ? -46.492 21.740  23.181  1.00 24.92 ? 816  HOH   B O   1 
HETATM 9555 O  O   . HOH   M 7 .   ? -56.460 -28.279 22.075  1.00 28.72 ? 817  HOH   B O   1 
HETATM 9556 O  O   . HOH   M 7 .   ? -36.747 2.119   25.630  1.00 36.97 ? 818  HOH   B O   1 
HETATM 9557 O  O   . HOH   M 7 .   ? -53.321 -3.645  29.817  1.00 12.89 ? 819  HOH   B O   1 
HETATM 9558 O  O   . HOH   M 7 .   ? -65.415 -2.638  41.553  1.00 13.64 ? 820  HOH   B O   1 
HETATM 9559 O  O   . HOH   M 7 .   ? -40.725 -28.738 38.565  1.00 43.78 ? 821  HOH   B O   1 
HETATM 9560 O  O   . HOH   M 7 .   ? -44.006 18.598  23.413  1.00 31.04 ? 822  HOH   B O   1 
HETATM 9561 O  O   . HOH   M 7 .   ? -61.982 3.827   16.512  1.00 18.94 ? 823  HOH   B O   1 
HETATM 9562 O  O   . HOH   M 7 .   ? -51.539 -12.021 7.521   1.00 8.81  ? 824  HOH   B O   1 
HETATM 9563 O  O   . HOH   M 7 .   ? -39.717 -24.091 39.766  1.00 18.96 ? 825  HOH   B O   1 
HETATM 9564 O  O   . HOH   M 7 .   ? -30.153 -17.282 13.867  1.00 20.66 ? 826  HOH   B O   1 
HETATM 9565 O  O   . HOH   M 7 .   ? -34.209 -3.650  45.962  1.00 49.55 ? 827  HOH   B O   1 
HETATM 9566 O  O   . HOH   M 7 .   ? -30.853 -8.995  39.497  1.00 19.64 ? 828  HOH   B O   1 
HETATM 9567 O  O   . HOH   M 7 .   ? -69.009 -5.005  24.911  1.00 22.13 ? 829  HOH   B O   1 
HETATM 9568 O  O   . HOH   M 7 .   ? -57.027 15.042  2.633   1.00 41.22 ? 830  HOH   B O   1 
HETATM 9569 O  O   . HOH   M 7 .   ? -59.772 -22.033 43.465  1.00 23.51 ? 831  HOH   B O   1 
HETATM 9570 O  O   . HOH   M 7 .   ? -55.954 -2.983  48.609  1.00 19.57 ? 832  HOH   B O   1 
HETATM 9571 O  O   . HOH   M 7 .   ? -56.437 15.984  38.182  1.00 21.07 ? 833  HOH   B O   1 
HETATM 9572 O  O   . HOH   M 7 .   ? -69.114 -21.231 26.719  1.00 28.46 ? 834  HOH   B O   1 
HETATM 9573 O  O   . HOH   M 7 .   ? -59.261 -18.151 33.254  1.00 15.56 ? 835  HOH   B O   1 
HETATM 9574 O  O   . HOH   M 7 .   ? -61.727 -11.929 41.060  1.00 12.21 ? 836  HOH   B O   1 
HETATM 9575 O  O   . HOH   M 7 .   ? -51.041 -4.936  58.130  1.00 31.96 ? 837  HOH   B O   1 
HETATM 9576 O  O   . HOH   M 7 .   ? -26.995 -17.920 22.505  1.00 22.81 ? 838  HOH   B O   1 
HETATM 9577 O  O   . HOH   M 7 .   ? -63.641 -10.382 8.616   1.00 30.61 ? 839  HOH   B O   1 
HETATM 9578 O  O   . HOH   M 7 .   ? -52.508 -24.814 25.915  1.00 26.84 ? 840  HOH   B O   1 
HETATM 9579 O  O   . HOH   M 7 .   ? -62.686 -14.589 46.128  1.00 17.87 ? 841  HOH   B O   1 
HETATM 9580 O  O   . HOH   M 7 .   ? -45.842 -8.510  33.532  1.00 12.79 ? 842  HOH   B O   1 
HETATM 9581 O  O   . HOH   M 7 .   ? -39.832 2.183   12.086  1.00 29.92 ? 843  HOH   B O   1 
HETATM 9582 O  O   . HOH   M 7 .   ? -55.241 -11.970 0.379   1.00 16.62 ? 844  HOH   B O   1 
HETATM 9583 O  O   . HOH   M 7 .   ? -64.157 -13.516 7.396   1.00 20.21 ? 845  HOH   B O   1 
HETATM 9584 O  O   . HOH   M 7 .   ? -36.549 -13.691 44.579  1.00 23.61 ? 846  HOH   B O   1 
HETATM 9585 O  O   . HOH   M 7 .   ? -49.183 13.311  31.024  1.00 33.77 ? 847  HOH   B O   1 
HETATM 9586 O  O   . HOH   M 7 .   ? -72.991 -3.509  25.750  1.00 28.75 ? 848  HOH   B O   1 
HETATM 9587 O  O   . HOH   M 7 .   ? -39.919 9.506   19.493  1.00 31.35 ? 849  HOH   B O   1 
HETATM 9588 O  O   . HOH   M 7 .   ? -61.056 -12.454 14.327  1.00 10.48 ? 850  HOH   B O   1 
HETATM 9589 O  O   . HOH   M 7 .   ? -51.556 21.418  22.734  1.00 26.38 ? 851  HOH   B O   1 
HETATM 9590 O  O   . HOH   M 7 .   ? -47.694 4.995   40.072  1.00 30.47 ? 852  HOH   B O   1 
HETATM 9591 O  O   . HOH   M 7 .   ? -69.531 -6.312  60.323  1.00 39.10 ? 853  HOH   B O   1 
HETATM 9592 O  O   . HOH   M 7 .   ? -48.621 -20.216 12.720  1.00 11.94 ? 854  HOH   B O   1 
HETATM 9593 O  O   . HOH   M 7 .   ? -46.174 -5.332  31.355  1.00 12.24 ? 855  HOH   B O   1 
HETATM 9594 O  O   . HOH   M 7 .   ? -41.736 8.934   13.041  1.00 16.68 ? 856  HOH   B O   1 
HETATM 9595 O  O   . HOH   M 7 .   ? -58.094 -15.035 47.426  1.00 19.02 ? 857  HOH   B O   1 
HETATM 9596 O  O   . HOH   M 7 .   ? -72.329 -0.038  27.860  1.00 29.26 ? 858  HOH   B O   1 
HETATM 9597 O  O   . HOH   M 7 .   ? -49.454 17.658  5.658   1.00 31.54 ? 859  HOH   B O   1 
HETATM 9598 O  O   . HOH   M 7 .   ? -36.692 -4.880  17.299  1.00 22.77 ? 860  HOH   B O   1 
HETATM 9599 O  O   . HOH   M 7 .   ? -39.952 4.635   12.984  1.00 30.35 ? 861  HOH   B O   1 
HETATM 9600 O  O   . HOH   M 7 .   ? -75.775 -13.419 24.104  1.00 10.55 ? 862  HOH   B O   1 
HETATM 9601 O  O   . HOH   M 7 .   ? -58.284 1.653   35.098  1.00 21.44 ? 863  HOH   B O   1 
HETATM 9602 O  O   . HOH   M 7 .   ? -50.464 -21.395 40.351  1.00 23.54 ? 864  HOH   B O   1 
HETATM 9603 O  O   . HOH   M 7 .   ? -55.234 4.611   27.627  1.00 13.25 ? 865  HOH   B O   1 
HETATM 9604 O  O   . HOH   M 7 .   ? -39.301 -17.563 38.376  1.00 15.17 ? 866  HOH   B O   1 
HETATM 9605 O  O   . HOH   M 7 .   ? -30.591 -5.431  23.388  1.00 24.05 ? 867  HOH   B O   1 
HETATM 9606 O  O   . HOH   M 7 .   ? -74.766 -14.166 36.301  1.00 20.23 ? 868  HOH   B O   1 
HETATM 9607 O  O   . HOH   M 7 .   ? -71.614 -20.308 24.478  1.00 23.29 ? 869  HOH   B O   1 
HETATM 9608 O  O   . HOH   M 7 .   ? -56.355 6.824   27.067  1.00 24.29 ? 870  HOH   B O   1 
HETATM 9609 O  O   . HOH   M 7 .   ? -60.793 -16.154 7.406   1.00 26.36 ? 871  HOH   B O   1 
HETATM 9610 O  O   . HOH   M 7 .   ? -42.332 -3.166  50.568  1.00 32.39 ? 872  HOH   B O   1 
HETATM 9611 O  O   . HOH   M 7 .   ? -41.314 -19.293 39.432  1.00 18.38 ? 873  HOH   B O   1 
HETATM 9612 O  O   . HOH   M 7 .   ? -27.073 -11.204 25.366  1.00 14.93 ? 874  HOH   B O   1 
HETATM 9613 O  O   . HOH   M 7 .   ? -43.521 -30.006 29.991  1.00 32.45 ? 875  HOH   B O   1 
HETATM 9614 O  O   . HOH   M 7 .   ? -39.347 -19.235 27.602  1.00 12.41 ? 876  HOH   B O   1 
HETATM 9615 O  O   . HOH   M 7 .   ? -66.314 13.255  36.149  1.00 34.47 ? 877  HOH   B O   1 
HETATM 9616 O  O   . HOH   M 7 .   ? -66.147 17.065  19.998  1.00 16.90 ? 878  HOH   B O   1 
HETATM 9617 O  O   . HOH   M 7 .   ? -62.978 11.045  17.693  1.00 21.05 ? 879  HOH   B O   1 
HETATM 9618 O  O   . HOH   M 7 .   ? -56.708 6.532   18.849  1.00 20.22 ? 880  HOH   B O   1 
HETATM 9619 O  O   . HOH   M 7 .   ? -42.200 8.794   23.281  1.00 23.97 ? 881  HOH   B O   1 
HETATM 9620 O  O   . HOH   M 7 .   ? -56.952 21.545  38.053  1.00 27.97 ? 882  HOH   B O   1 
HETATM 9621 O  O   . HOH   M 7 .   ? -50.364 6.202   40.700  1.00 23.24 ? 883  HOH   B O   1 
HETATM 9622 O  O   . HOH   M 7 .   ? -47.444 -11.735 47.428  1.00 28.12 ? 884  HOH   B O   1 
HETATM 9623 O  O   . HOH   M 7 .   ? -74.851 19.166  28.561  1.00 27.95 ? 885  HOH   B O   1 
HETATM 9624 O  O   . HOH   M 7 .   ? -45.141 -13.509 0.309   1.00 23.25 ? 886  HOH   B O   1 
HETATM 9625 O  O   . HOH   M 7 .   ? -62.582 -1.663  38.756  1.00 15.66 ? 887  HOH   B O   1 
HETATM 9626 O  O   . HOH   M 7 .   ? -48.174 -18.718 7.176   1.00 31.23 ? 888  HOH   B O   1 
HETATM 9627 O  O   . HOH   M 7 .   ? -43.981 8.342   47.422  1.00 34.20 ? 889  HOH   B O   1 
HETATM 9628 O  O   . HOH   M 7 .   ? -56.305 1.248   32.135  1.00 15.07 ? 890  HOH   B O   1 
HETATM 9629 O  O   . HOH   M 7 .   ? -60.485 2.143   22.670  1.00 15.50 ? 891  HOH   B O   1 
HETATM 9630 O  O   . HOH   M 7 .   ? -36.021 -27.241 32.390  1.00 26.72 ? 892  HOH   B O   1 
HETATM 9631 O  O   . HOH   M 7 .   ? -47.475 -9.061  2.342   1.00 14.85 ? 893  HOH   B O   1 
HETATM 9632 O  O   . HOH   M 7 .   ? -60.072 -12.185 43.567  1.00 18.09 ? 894  HOH   B O   1 
HETATM 9633 O  O   . HOH   M 7 .   ? -52.512 -11.119 57.744  1.00 32.24 ? 895  HOH   B O   1 
HETATM 9634 O  O   . HOH   M 7 .   ? -76.505 -12.652 20.137  1.00 24.23 ? 896  HOH   B O   1 
HETATM 9635 O  O   . HOH   M 7 .   ? -56.023 5.104   39.543  1.00 20.32 ? 897  HOH   B O   1 
HETATM 9636 O  O   . HOH   M 7 .   ? -48.103 -14.831 42.516  1.00 19.85 ? 898  HOH   B O   1 
HETATM 9637 O  O   . HOH   M 7 .   ? -45.390 -4.572  33.857  1.00 16.53 ? 899  HOH   B O   1 
HETATM 9638 O  O   . HOH   M 7 .   ? -46.318 18.549  12.505  1.00 32.16 ? 900  HOH   B O   1 
HETATM 9639 O  O   . HOH   M 7 .   ? -37.050 0.546   19.450  1.00 25.34 ? 901  HOH   B O   1 
HETATM 9640 O  O   . HOH   M 7 .   ? -35.413 -22.195 12.205  1.00 29.24 ? 902  HOH   B O   1 
HETATM 9641 O  O   . HOH   M 7 .   ? -61.034 -21.351 12.164  1.00 22.04 ? 903  HOH   B O   1 
HETATM 9642 O  O   . HOH   M 7 .   ? -73.147 -2.957  40.230  1.00 32.58 ? 904  HOH   B O   1 
HETATM 9643 O  O   . HOH   M 7 .   ? -76.801 -15.701 21.745  1.00 13.08 ? 905  HOH   B O   1 
HETATM 9644 O  O   . HOH   M 7 .   ? -51.114 7.878   53.179  1.00 33.14 ? 906  HOH   B O   1 
HETATM 9645 O  O   . HOH   M 7 .   ? -42.892 -30.664 24.999  1.00 27.18 ? 907  HOH   B O   1 
HETATM 9646 O  O   . HOH   M 7 .   ? -62.169 22.082  36.025  1.00 25.99 ? 908  HOH   B O   1 
HETATM 9647 O  O   . HOH   M 7 .   ? -41.629 -22.150 40.587  1.00 22.20 ? 909  HOH   B O   1 
HETATM 9648 O  O   . HOH   M 7 .   ? -48.866 7.876   47.190  1.00 24.58 ? 910  HOH   B O   1 
HETATM 9649 O  O   . HOH   M 7 .   ? -76.132 -7.969  34.653  1.00 20.48 ? 911  HOH   B O   1 
HETATM 9650 O  O   . HOH   M 7 .   ? -52.385 -6.928  -2.549  1.00 18.84 ? 912  HOH   B O   1 
HETATM 9651 O  O   . HOH   M 7 .   ? -52.913 -23.611 23.576  1.00 20.84 ? 913  HOH   B O   1 
HETATM 9652 O  O   . HOH   M 7 .   ? -52.989 8.696   19.717  1.00 24.09 ? 914  HOH   B O   1 
HETATM 9653 O  O   . HOH   M 7 .   ? -61.249 7.724   25.673  1.00 24.12 ? 915  HOH   B O   1 
HETATM 9654 O  O   . HOH   M 7 .   ? -50.948 -19.030 45.360  1.00 27.93 ? 916  HOH   B O   1 
HETATM 9655 O  O   . HOH   M 7 .   ? -34.574 -7.356  34.299  1.00 28.27 ? 917  HOH   B O   1 
HETATM 9656 O  O   . HOH   M 7 .   ? -58.625 -0.327  11.589  1.00 27.59 ? 918  HOH   B O   1 
HETATM 9657 O  O   . HOH   M 7 .   ? -61.542 31.809  18.427  1.00 34.83 ? 919  HOH   B O   1 
HETATM 9658 O  O   . HOH   M 7 .   ? -67.775 -9.508  33.968  1.00 12.01 ? 920  HOH   B O   1 
HETATM 9659 O  O   . HOH   M 7 .   ? -52.385 -5.794  44.172  1.00 20.41 ? 921  HOH   B O   1 
HETATM 9660 O  O   . HOH   M 7 .   ? -55.650 -12.163 34.832  1.00 10.80 ? 922  HOH   B O   1 
HETATM 9661 O  O   . HOH   M 7 .   ? -53.228 -7.803  60.525  1.00 29.78 ? 923  HOH   B O   1 
HETATM 9662 O  O   . HOH   M 7 .   ? -52.813 5.898   26.921  1.00 15.00 ? 924  HOH   B O   1 
HETATM 9663 O  O   . HOH   M 7 .   ? -46.969 11.373  16.620  1.00 16.13 ? 925  HOH   B O   1 
HETATM 9664 O  O   . HOH   M 7 .   ? -54.634 -13.003 2.690   1.00 14.81 ? 926  HOH   B O   1 
HETATM 9665 O  O   . HOH   M 7 .   ? -48.441 -4.369  11.608  1.00 11.43 ? 927  HOH   B O   1 
HETATM 9666 O  O   . HOH   M 7 .   ? -36.238 -5.275  46.715  1.00 27.15 ? 928  HOH   B O   1 
HETATM 9667 O  O   . HOH   M 7 .   ? -67.002 11.869  38.525  1.00 30.07 ? 929  HOH   B O   1 
HETATM 9668 O  O   . HOH   M 7 .   ? -73.002 -19.893 37.903  1.00 38.87 ? 930  HOH   B O   1 
HETATM 9669 O  O   . HOH   M 7 .   ? -52.948 -25.025 21.131  1.00 26.73 ? 931  HOH   B O   1 
HETATM 9670 O  O   . HOH   M 7 .   ? -56.205 3.426   13.164  1.00 15.93 ? 932  HOH   B O   1 
HETATM 9671 O  O   . HOH   M 7 .   ? -37.695 -20.223 30.183  1.00 15.17 ? 933  HOH   B O   1 
HETATM 9672 O  O   . HOH   M 7 .   ? -66.304 -16.101 36.045  1.00 16.68 ? 934  HOH   B O   1 
HETATM 9673 O  O   . HOH   M 7 .   ? -47.342 2.889   38.410  1.00 23.42 ? 935  HOH   B O   1 
HETATM 9674 O  O   . HOH   M 7 .   ? -28.290 -7.943  19.005  1.00 13.58 ? 936  HOH   B O   1 
HETATM 9675 O  O   . HOH   M 7 .   ? -63.960 -4.397  34.514  1.00 12.33 ? 937  HOH   B O   1 
HETATM 9676 O  O   . HOH   M 7 .   ? -51.502 -20.257 43.348  1.00 21.16 ? 938  HOH   B O   1 
HETATM 9677 O  O   . HOH   M 7 .   ? -54.714 -24.454 26.922  1.00 23.79 ? 939  HOH   B O   1 
HETATM 9678 O  O   . HOH   M 7 .   ? -37.205 5.334   28.511  1.00 38.75 ? 940  HOH   B O   1 
HETATM 9679 O  O   . HOH   M 7 .   ? -64.341 -7.857  36.402  1.00 12.11 ? 941  HOH   B O   1 
HETATM 9680 O  O   . HOH   M 7 .   ? -49.403 -15.723 46.393  1.00 27.05 ? 942  HOH   B O   1 
HETATM 9681 O  O   . HOH   M 7 .   ? -35.107 -13.992 12.728  1.00 13.10 ? 943  HOH   B O   1 
HETATM 9682 O  O   . HOH   M 7 .   ? -65.705 -12.403 19.832  1.00 10.22 ? 944  HOH   B O   1 
HETATM 9683 O  O   . HOH   M 7 .   ? -63.021 -10.596 39.064  1.00 12.53 ? 945  HOH   B O   1 
HETATM 9684 O  O   . HOH   M 7 .   ? -40.093 3.741   44.882  1.00 29.78 ? 946  HOH   B O   1 
HETATM 9685 O  O   . HOH   M 7 .   ? -39.168 -2.512  19.810  1.00 22.23 ? 947  HOH   B O   1 
HETATM 9686 O  O   . HOH   M 7 .   ? -58.982 3.085   32.952  1.00 20.74 ? 948  HOH   B O   1 
HETATM 9687 O  O   . HOH   M 7 .   ? -47.920 -19.349 10.121  1.00 10.26 ? 949  HOH   B O   1 
HETATM 9688 O  O   . HOH   M 7 .   ? -54.931 8.358   8.332   1.00 19.65 ? 950  HOH   B O   1 
HETATM 9689 O  O   . HOH   M 7 .   ? -52.467 1.821   8.640   1.00 10.85 ? 951  HOH   B O   1 
HETATM 9690 O  O   . HOH   M 7 .   ? -28.729 -17.469 28.228  1.00 14.35 ? 952  HOH   B O   1 
HETATM 9691 O  O   . HOH   M 7 .   ? -62.365 14.233  34.068  1.00 25.11 ? 953  HOH   B O   1 
HETATM 9692 O  O   . HOH   M 7 .   ? -57.255 -18.386 6.994   1.00 15.45 ? 954  HOH   B O   1 
HETATM 9693 O  O   . HOH   M 7 .   ? -58.741 2.051   42.695  1.00 16.27 ? 955  HOH   B O   1 
HETATM 9694 O  O   . HOH   M 7 .   ? -36.713 -24.374 17.711  1.00 15.84 ? 956  HOH   B O   1 
HETATM 9695 O  O   . HOH   M 7 .   ? -72.539 -18.076 34.046  1.00 25.00 ? 957  HOH   B O   1 
HETATM 9696 O  O   . HOH   M 7 .   ? -41.420 -26.692 17.758  1.00 22.42 ? 958  HOH   B O   1 
HETATM 9697 O  O   . HOH   M 7 .   ? -53.184 -12.169 33.681  1.00 13.56 ? 959  HOH   B O   1 
HETATM 9698 O  O   . HOH   M 7 .   ? -38.963 2.055   42.067  1.00 27.71 ? 960  HOH   B O   1 
HETATM 9699 O  O   . HOH   M 7 .   ? -49.628 -3.410  37.058  1.00 22.22 ? 961  HOH   B O   1 
HETATM 9700 O  O   . HOH   M 7 .   ? -36.759 7.345   17.581  1.00 14.01 ? 962  HOH   B O   1 
HETATM 9701 O  O   . HOH   M 7 .   ? -60.357 -8.420  59.767  1.00 32.03 ? 963  HOH   B O   1 
HETATM 9702 O  O   . HOH   M 7 .   ? -44.868 2.675   44.861  1.00 23.23 ? 964  HOH   B O   1 
HETATM 9703 O  O   . HOH   M 7 .   ? -36.521 -2.725  20.375  1.00 19.68 ? 965  HOH   B O   1 
HETATM 9704 O  O   . HOH   M 7 .   ? -62.406 -15.669 26.782  1.00 10.81 ? 966  HOH   B O   1 
HETATM 9705 O  O   . HOH   M 7 .   ? -37.821 -13.864 4.973   1.00 20.17 ? 967  HOH   B O   1 
HETATM 9706 O  O   . HOH   M 7 .   ? -70.127 -11.190 33.942  1.00 10.04 ? 968  HOH   B O   1 
HETATM 9707 O  O   . HOH   M 7 .   ? -56.909 4.793   16.894  1.00 22.32 ? 969  HOH   B O   1 
HETATM 9708 O  O   . HOH   M 7 .   ? -71.539 13.187  31.289  1.00 19.71 ? 970  HOH   B O   1 
HETATM 9709 O  O   . HOH   M 7 .   ? -57.954 -23.938 27.060  1.00 17.13 ? 971  HOH   B O   1 
HETATM 9710 O  O   . HOH   M 7 .   ? -70.895 -1.550  18.295  1.00 11.31 ? 972  HOH   B O   1 
HETATM 9711 O  O   . HOH   M 7 .   ? -58.974 -22.846 49.384  1.00 35.01 ? 973  HOH   B O   1 
HETATM 9712 O  O   . HOH   M 7 .   ? -58.590 7.507   25.526  1.00 20.86 ? 974  HOH   B O   1 
HETATM 9713 O  O   . HOH   M 7 .   ? -71.339 -11.476 36.490  1.00 19.64 ? 975  HOH   B O   1 
HETATM 9714 O  O   . HOH   M 7 .   ? -27.168 -21.555 22.346  1.00 20.84 ? 976  HOH   B O   1 
HETATM 9715 O  O   . HOH   M 7 .   ? -33.746 -9.323  8.094   1.00 28.20 ? 977  HOH   B O   1 
HETATM 9716 O  O   . HOH   M 7 .   ? -57.478 -1.128  34.458  1.00 16.86 ? 978  HOH   B O   1 
HETATM 9717 O  O   . HOH   M 7 .   ? -72.421 -14.363 17.245  1.00 13.81 ? 979  HOH   B O   1 
HETATM 9718 O  O   . HOH   M 7 .   ? -42.844 -13.322 18.947  1.00 9.27  ? 980  HOH   B O   1 
HETATM 9719 O  O   . HOH   M 7 .   ? -42.710 10.426  10.789  1.00 22.34 ? 981  HOH   B O   1 
HETATM 9720 O  O   . HOH   M 7 .   ? -68.498 2.486   13.572  1.00 30.14 ? 982  HOH   B O   1 
HETATM 9721 O  O   . HOH   M 7 .   ? -65.765 -8.649  11.394  1.00 21.67 ? 983  HOH   B O   1 
HETATM 9722 O  O   . HOH   M 7 .   ? -30.209 -14.190 16.525  1.00 18.31 ? 984  HOH   B O   1 
HETATM 9723 O  O   . HOH   M 7 .   ? -56.104 3.345   35.765  1.00 17.49 ? 985  HOH   B O   1 
HETATM 9724 O  O   . HOH   M 7 .   ? -56.474 -3.367  0.825   1.00 29.19 ? 986  HOH   B O   1 
HETATM 9725 O  O   . HOH   M 7 .   ? -55.385 21.187  32.688  1.00 25.58 ? 987  HOH   B O   1 
HETATM 9726 O  O   . HOH   M 7 .   ? -69.186 -3.842  48.015  1.00 20.92 ? 988  HOH   B O   1 
HETATM 9727 O  O   . HOH   M 7 .   ? -60.031 21.788  38.208  1.00 26.30 ? 989  HOH   B O   1 
HETATM 9728 O  O   . HOH   M 7 .   ? -48.468 -22.113 38.714  1.00 20.75 ? 990  HOH   B O   1 
HETATM 9729 O  O   . HOH   M 7 .   ? -37.321 -20.018 37.195  1.00 24.96 ? 991  HOH   B O   1 
HETATM 9730 O  O   . HOH   M 7 .   ? -64.750 -11.233 48.562  1.00 20.92 ? 992  HOH   B O   1 
HETATM 9731 O  O   . HOH   M 7 .   ? -28.546 -16.212 16.453  1.00 24.78 ? 993  HOH   B O   1 
HETATM 9732 O  O   . HOH   M 7 .   ? -72.379 -13.886 54.250  1.00 32.29 ? 994  HOH   B O   1 
HETATM 9733 O  O   . HOH   M 7 .   ? -62.587 -12.851 27.213  1.00 10.59 ? 995  HOH   B O   1 
HETATM 9734 O  O   . HOH   M 7 .   ? -68.069 3.918   28.870  1.00 22.29 ? 996  HOH   B O   1 
HETATM 9735 O  O   . HOH   M 7 .   ? -29.219 -26.992 33.379  1.00 34.03 ? 997  HOH   B O   1 
HETATM 9736 O  O   . HOH   M 7 .   ? -59.258 -15.911 15.341  1.00 9.76  ? 998  HOH   B O   1 
HETATM 9737 O  O   . HOH   M 7 .   ? -43.949 -28.813 20.489  1.00 22.65 ? 999  HOH   B O   1 
HETATM 9738 O  O   . HOH   M 7 .   ? -46.655 -27.294 40.018  1.00 28.05 ? 1000 HOH   B O   1 
HETATM 9739 O  O   . HOH   M 7 .   ? -35.017 -26.314 34.396  1.00 36.09 ? 1001 HOH   B O   1 
HETATM 9740 O  O   . HOH   M 7 .   ? -68.173 -11.710 59.728  1.00 30.17 ? 1002 HOH   B O   1 
HETATM 9741 O  O   . HOH   M 7 .   ? -33.829 -1.157  24.286  1.00 28.30 ? 1003 HOH   B O   1 
HETATM 9742 O  O   . HOH   M 7 .   ? -74.098 -4.469  28.526  1.00 22.69 ? 1004 HOH   B O   1 
HETATM 9743 O  O   . HOH   M 7 .   ? -70.925 0.023   30.037  1.00 19.68 ? 1005 HOH   B O   1 
HETATM 9744 O  O   . HOH   M 7 .   ? -47.066 -28.839 18.242  1.00 25.03 ? 1006 HOH   B O   1 
HETATM 9745 O  O   . HOH   M 7 .   ? -61.573 -9.282  0.856   1.00 34.35 ? 1007 HOH   B O   1 
HETATM 9746 O  O   . HOH   M 7 .   ? -62.556 6.130   19.230  1.00 14.51 ? 1008 HOH   B O   1 
HETATM 9747 O  O   . HOH   M 7 .   ? -71.197 -1.168  37.766  1.00 20.06 ? 1009 HOH   B O   1 
HETATM 9748 O  O   . HOH   M 7 .   ? -52.511 4.491   36.312  1.00 17.05 ? 1010 HOH   B O   1 
HETATM 9749 O  O   . HOH   M 7 .   ? -53.065 19.804  32.375  1.00 22.93 ? 1011 HOH   B O   1 
HETATM 9750 O  O   . HOH   M 7 .   ? -46.052 -12.759 31.865  1.00 11.75 ? 1012 HOH   B O   1 
HETATM 9751 O  O   . HOH   M 7 .   ? -74.191 -6.103  20.129  1.00 13.14 ? 1013 HOH   B O   1 
HETATM 9752 O  O   . HOH   M 7 .   ? -61.344 9.881   34.882  1.00 32.31 ? 1014 HOH   B O   1 
HETATM 9753 O  O   . HOH   M 7 .   ? -65.229 -15.095 28.857  1.00 10.39 ? 1015 HOH   B O   1 
HETATM 9754 O  O   . HOH   M 7 .   ? -67.419 6.736   28.708  1.00 28.14 ? 1016 HOH   B O   1 
HETATM 9755 O  O   . HOH   M 7 .   ? -73.083 -2.864  49.187  1.00 39.69 ? 1017 HOH   B O   1 
HETATM 9756 O  O   . HOH   M 7 .   ? -46.240 -2.803  3.345   1.00 26.17 ? 1018 HOH   B O   1 
HETATM 9757 O  O   . HOH   M 7 .   ? -56.035 -9.508  0.292   1.00 24.87 ? 1019 HOH   B O   1 
HETATM 9758 O  O   . HOH   M 7 .   ? -30.935 -23.229 37.514  1.00 27.60 ? 1020 HOH   B O   1 
HETATM 9759 O  O   . HOH   M 7 .   ? -43.283 4.484   41.910  1.00 29.01 ? 1021 HOH   B O   1 
HETATM 9760 O  O   . HOH   M 7 .   ? -28.785 -29.370 25.226  1.00 18.91 ? 1022 HOH   B O   1 
HETATM 9761 O  O   . HOH   M 7 .   ? -60.169 4.902   19.028  1.00 15.29 ? 1023 HOH   B O   1 
HETATM 9762 O  O   . HOH   M 7 .   ? -54.710 25.099  12.726  1.00 26.87 ? 1024 HOH   B O   1 
HETATM 9763 O  O   . HOH   M 7 .   ? -56.072 -16.469 46.224  1.00 22.80 ? 1025 HOH   B O   1 
HETATM 9764 O  O   . HOH   M 7 .   ? -67.902 6.546   55.549  1.00 30.03 ? 1026 HOH   B O   1 
HETATM 9765 O  O   . HOH   M 7 .   ? -63.178 7.799   14.320  1.00 27.14 ? 1027 HOH   B O   1 
HETATM 9766 O  O   . HOH   M 7 .   ? -58.024 6.480   38.038  1.00 19.88 ? 1028 HOH   B O   1 
HETATM 9767 O  O   . HOH   M 7 .   ? -61.675 -23.153 40.484  1.00 46.65 ? 1029 HOH   B O   1 
HETATM 9768 O  O   . HOH   M 7 .   ? -32.565 -6.779  43.600  1.00 38.69 ? 1030 HOH   B O   1 
HETATM 9769 O  O   . HOH   M 7 .   ? -40.766 4.151   40.408  1.00 21.63 ? 1031 HOH   B O   1 
HETATM 9770 O  O   . HOH   M 7 .   ? -49.514 -14.327 55.498  1.00 47.84 ? 1032 HOH   B O   1 
HETATM 9771 O  O   . HOH   M 7 .   ? -47.711 -5.150  35.467  1.00 16.73 ? 1033 HOH   B O   1 
HETATM 9772 O  O   . HOH   M 7 .   ? -43.280 -1.254  7.900   1.00 25.11 ? 1034 HOH   B O   1 
HETATM 9773 O  O   . HOH   M 7 .   ? -54.360 8.142   30.925  1.00 14.13 ? 1035 HOH   B O   1 
HETATM 9774 O  O   . HOH   M 7 .   ? -54.476 -23.290 47.071  1.00 33.15 ? 1036 HOH   B O   1 
HETATM 9775 O  O   . HOH   M 7 .   ? -45.451 -26.196 14.677  1.00 22.80 ? 1037 HOH   B O   1 
HETATM 9776 O  O   . HOH   M 7 .   ? -29.406 -6.939  16.874  1.00 17.22 ? 1038 HOH   B O   1 
HETATM 9777 O  O   . HOH   M 7 .   ? -68.107 -1.876  34.864  1.00 21.97 ? 1039 HOH   B O   1 
HETATM 9778 O  O   . HOH   M 7 .   ? -52.047 -4.154  -2.655  1.00 40.55 ? 1040 HOH   B O   1 
HETATM 9779 O  O   . HOH   M 7 .   ? -59.512 6.986   30.336  1.00 30.53 ? 1041 HOH   B O   1 
HETATM 9780 O  O   . HOH   M 7 .   ? -35.170 -13.405 5.777   1.00 20.49 ? 1042 HOH   B O   1 
HETATM 9781 O  O   . HOH   M 7 .   ? -50.472 -26.515 20.603  1.00 27.61 ? 1043 HOH   B O   1 
HETATM 9782 O  O   . HOH   M 7 .   ? -31.510 -14.809 14.269  1.00 22.80 ? 1044 HOH   B O   1 
HETATM 9783 O  O   . HOH   M 7 .   ? -38.519 -17.795 45.982  1.00 43.15 ? 1045 HOH   B O   1 
HETATM 9784 O  O   . HOH   M 7 .   ? -48.881 -26.897 38.357  1.00 28.35 ? 1046 HOH   B O   1 
HETATM 9785 O  O   . HOH   M 7 .   ? -52.062 -0.615  39.809  1.00 23.40 ? 1047 HOH   B O   1 
HETATM 9786 O  O   . HOH   M 7 .   ? -64.586 -22.911 14.904  1.00 30.61 ? 1048 HOH   B O   1 
HETATM 9787 O  O   . HOH   M 7 .   ? -25.856 -26.987 26.073  1.00 31.21 ? 1049 HOH   B O   1 
HETATM 9788 O  O   . HOH   M 7 .   ? -72.709 -7.143  16.241  1.00 13.68 ? 1050 HOH   B O   1 
HETATM 9789 O  O   . HOH   M 7 .   ? -45.123 -27.244 17.230  1.00 18.25 ? 1051 HOH   B O   1 
HETATM 9790 O  O   . HOH   M 7 .   ? -62.676 -16.095 5.356   1.00 40.08 ? 1052 HOH   B O   1 
HETATM 9791 O  O   . HOH   M 7 .   ? -45.927 -11.287 34.085  1.00 13.68 ? 1053 HOH   B O   1 
HETATM 9792 O  O   . HOH   M 7 .   ? -60.222 0.065   31.793  1.00 17.76 ? 1054 HOH   B O   1 
HETATM 9793 O  O   . HOH   M 7 .   ? -47.076 -14.698 44.942  1.00 21.46 ? 1055 HOH   B O   1 
HETATM 9794 O  O   . HOH   M 7 .   ? -52.513 6.556   29.739  1.00 15.51 ? 1056 HOH   B O   1 
HETATM 9795 O  O   . HOH   M 7 .   ? -56.134 6.071   13.891  1.00 21.59 ? 1057 HOH   B O   1 
HETATM 9796 O  O   . HOH   M 7 .   ? -46.286 28.355  23.804  1.00 45.63 ? 1058 HOH   B O   1 
HETATM 9797 O  O   . HOH   M 7 .   ? -74.911 -5.640  34.502  1.00 36.10 ? 1059 HOH   B O   1 
HETATM 9798 O  O   . HOH   M 7 .   ? -60.433 9.923   27.358  1.00 24.58 ? 1060 HOH   B O   1 
HETATM 9799 O  O   . HOH   M 7 .   ? -43.179 -29.180 32.421  1.00 23.78 ? 1061 HOH   B O   1 
HETATM 9800 O  O   . HOH   M 7 .   ? -69.954 -16.689 33.577  1.00 13.95 ? 1062 HOH   B O   1 
HETATM 9801 O  O   . HOH   M 7 .   ? -33.242 -3.113  21.147  1.00 19.98 ? 1063 HOH   B O   1 
HETATM 9802 O  O   . HOH   M 7 .   ? -53.768 -18.850 52.222  1.00 34.68 ? 1064 HOH   B O   1 
HETATM 9803 O  O   . HOH   M 7 .   ? -37.303 -1.751  12.944  1.00 21.53 ? 1065 HOH   B O   1 
HETATM 9804 O  O   . HOH   M 7 .   ? -73.050 -18.269 21.512  1.00 24.24 ? 1066 HOH   B O   1 
HETATM 9805 O  O   . HOH   M 7 .   ? -70.323 -20.578 21.954  1.00 24.14 ? 1067 HOH   B O   1 
HETATM 9806 O  O   . HOH   M 7 .   ? -31.088 -22.038 16.450  1.00 42.13 ? 1068 HOH   B O   1 
HETATM 9807 O  O   . HOH   M 7 .   ? -57.526 -27.799 15.177  1.00 46.41 ? 1069 HOH   B O   1 
HETATM 9808 O  O   . HOH   M 7 .   ? -46.950 12.321  37.983  1.00 30.97 ? 1070 HOH   B O   1 
HETATM 9809 O  O   . HOH   M 7 .   ? -76.178 6.160   52.612  1.00 40.04 ? 1071 HOH   B O   1 
HETATM 9810 O  O   . HOH   M 7 .   ? -48.824 16.338  40.040  1.00 33.66 ? 1072 HOH   B O   1 
HETATM 9811 O  O   . HOH   M 7 .   ? -70.831 2.871   45.848  1.00 25.38 ? 1073 HOH   B O   1 
HETATM 9812 O  O   . HOH   M 7 .   ? -51.552 -23.857 12.960  1.00 24.09 ? 1074 HOH   B O   1 
HETATM 9813 O  O   . HOH   M 7 .   ? -44.045 -24.499 8.128   1.00 28.43 ? 1075 HOH   B O   1 
HETATM 9814 O  O   . HOH   M 7 .   ? -58.111 -23.343 42.582  1.00 35.10 ? 1076 HOH   B O   1 
HETATM 9815 O  O   . HOH   M 7 .   ? -47.134 11.553  34.746  1.00 36.57 ? 1077 HOH   B O   1 
HETATM 9816 O  O   . HOH   M 7 .   ? -59.605 -12.375 25.696  1.00 16.65 ? 1078 HOH   B O   1 
HETATM 9817 O  O   . HOH   M 7 .   ? -70.504 -16.867 16.535  1.00 19.08 ? 1079 HOH   B O   1 
HETATM 9818 O  O   . HOH   M 7 .   ? -42.383 12.960  21.609  1.00 29.37 ? 1080 HOH   B O   1 
HETATM 9819 O  O   . HOH   M 7 .   ? -56.693 6.098   35.621  1.00 19.83 ? 1081 HOH   B O   1 
HETATM 9820 O  O   . HOH   M 7 .   ? -27.827 -23.972 31.664  1.00 19.74 ? 1082 HOH   B O   1 
HETATM 9821 O  O   . HOH   M 7 .   ? -30.410 -10.596 34.436  1.00 31.37 ? 1083 HOH   B O   1 
HETATM 9822 O  O   . HOH   M 7 .   ? -44.194 -24.814 10.756  1.00 41.36 ? 1084 HOH   B O   1 
HETATM 9823 O  O   . HOH   M 7 .   ? -60.848 6.813   37.879  1.00 23.28 ? 1085 HOH   B O   1 
HETATM 9824 O  O   . HOH   M 7 .   ? -33.158 -0.601  19.572  1.00 30.67 ? 1086 HOH   B O   1 
HETATM 9825 O  O   . HOH   M 7 .   ? -52.567 -16.057 55.434  1.00 33.13 ? 1087 HOH   B O   1 
HETATM 9826 O  O   . HOH   M 7 .   ? -54.629 -17.108 54.032  1.00 30.06 ? 1088 HOH   B O   1 
HETATM 9827 O  O   . HOH   M 7 .   ? -32.323 -6.629  33.004  1.00 25.50 ? 1089 HOH   B O   1 
HETATM 9828 O  O   . HOH   M 7 .   ? -31.594 -4.695  40.482  1.00 22.72 ? 1090 HOH   B O   1 
HETATM 9829 O  O   . HOH   M 7 .   ? -38.168 13.843  19.347  1.00 22.65 ? 1091 HOH   B O   1 
HETATM 9830 O  O   . HOH   M 7 .   ? -53.745 -25.481 34.437  1.00 31.49 ? 1092 HOH   B O   1 
HETATM 9831 O  O   . HOH   M 7 .   ? -40.532 18.480  18.383  1.00 44.52 ? 1093 HOH   B O   1 
HETATM 9832 O  O   . HOH   M 7 .   ? -59.126 -2.114  9.820   1.00 29.06 ? 1094 HOH   B O   1 
HETATM 9833 O  O   . HOH   M 7 .   ? -35.838 -20.437 44.358  1.00 33.74 ? 1095 HOH   B O   1 
HETATM 9834 O  O   . HOH   M 7 .   ? -37.441 -3.009  15.283  1.00 25.11 ? 1096 HOH   B O   1 
HETATM 9835 O  O   . HOH   M 7 .   ? -36.638 -16.015 44.867  1.00 28.84 ? 1097 HOH   B O   1 
HETATM 9836 O  O   . HOH   M 7 .   ? -35.858 -21.911 9.319   1.00 37.15 ? 1098 HOH   B O   1 
HETATM 9837 O  O   . HOH   M 7 .   ? -52.618 2.426   39.733  1.00 23.30 ? 1099 HOH   B O   1 
HETATM 9838 O  O   . HOH   M 7 .   ? -54.010 6.603   18.669  1.00 21.81 ? 1100 HOH   B O   1 
HETATM 9839 O  O   . HOH   M 7 .   ? -68.106 -15.433 9.595   1.00 39.32 ? 1101 HOH   B O   1 
HETATM 9840 O  O   . HOH   M 7 .   ? -47.594 0.113   39.405  1.00 20.97 ? 1102 HOH   B O   1 
HETATM 9841 O  O   . HOH   M 7 .   ? -66.110 4.285   30.968  1.00 27.20 ? 1103 HOH   B O   1 
HETATM 9842 O  O   . HOH   M 7 .   ? -68.722 -4.184  12.307  1.00 31.91 ? 1104 HOH   B O   1 
HETATM 9843 O  O   . HOH   M 7 .   ? -54.545 3.660   37.997  1.00 19.22 ? 1105 HOH   B O   1 
HETATM 9844 O  O   . HOH   M 7 .   ? -70.602 17.232  37.255  1.00 43.34 ? 1106 HOH   B O   1 
HETATM 9845 O  O   . HOH   M 7 .   ? -66.785 -14.060 26.883  1.00 12.28 ? 1107 HOH   B O   1 
HETATM 9846 O  O   . HOH   M 7 .   ? -44.584 4.566   9.789   1.00 18.66 ? 1108 HOH   B O   1 
HETATM 9847 O  O   . HOH   M 7 .   ? -53.070 -26.055 14.613  1.00 36.11 ? 1109 HOH   B O   1 
HETATM 9848 O  O   . HOH   M 7 .   ? -27.615 -4.325  34.752  1.00 11.35 ? 1110 HOH   B O   1 
HETATM 9849 O  O   . HOH   M 7 .   ? -59.720 -12.906 57.407  1.00 46.30 ? 1111 HOH   B O   1 
HETATM 9850 O  O   . HOH   M 7 .   ? -26.538 -19.948 24.401  1.00 19.64 ? 1112 HOH   B O   1 
HETATM 9851 O  O   . HOH   M 7 .   ? -67.729 6.095   36.659  1.00 27.32 ? 1113 HOH   B O   1 
HETATM 9852 O  O   . HOH   M 7 .   ? -49.651 -1.373  38.832  1.00 20.33 ? 1114 HOH   B O   1 
HETATM 9853 O  O   . HOH   M 7 .   ? -71.494 -15.295 48.462  1.00 40.53 ? 1115 HOH   B O   1 
HETATM 9854 O  O   . HOH   M 7 .   ? -40.933 4.783   35.881  1.00 37.61 ? 1116 HOH   B O   1 
HETATM 9855 O  O   . HOH   M 7 .   ? -71.948 -4.859  15.092  1.00 15.37 ? 1117 HOH   B O   1 
HETATM 9856 O  O   . HOH   M 7 .   ? -71.210 1.269   17.220  1.00 33.47 ? 1118 HOH   B O   1 
HETATM 9857 O  O   . HOH   M 7 .   ? -69.030 24.997  35.314  1.00 35.81 ? 1119 HOH   B O   1 
HETATM 9858 O  O   . HOH   M 7 .   ? -71.436 -13.731 40.361  1.00 39.88 ? 1120 HOH   B O   1 
HETATM 9859 O  O   . HOH   M 7 .   ? -66.592 23.071  46.987  1.00 45.98 ? 1121 HOH   B O   1 
HETATM 9860 O  O   . HOH   M 7 .   ? -57.592 3.115   10.526  1.00 26.18 ? 1122 HOH   B O   1 
HETATM 9861 O  O   . HOH   M 7 .   ? -45.683 -10.229 -2.787  1.00 40.97 ? 1123 HOH   B O   1 
HETATM 9862 O  O   . HOH   M 7 .   ? -78.087 20.538  26.296  1.00 39.09 ? 1124 HOH   B O   1 
HETATM 9863 O  O   . HOH   M 7 .   ? -41.136 2.257   9.747   1.00 27.68 ? 1125 HOH   B O   1 
HETATM 9864 O  O   . HOH   M 7 .   ? -57.970 10.313  27.570  1.00 28.74 ? 1126 HOH   B O   1 
HETATM 9865 O  O   . HOH   M 7 .   ? -56.788 8.029   29.730  1.00 24.35 ? 1127 HOH   B O   1 
HETATM 9866 O  O   . HOH   M 7 .   ? -34.679 1.214   24.153  1.00 39.10 ? 1128 HOH   B O   1 
HETATM 9867 O  O   . HOH   M 7 .   ? -73.428 -8.909  14.152  1.00 26.05 ? 1129 HOH   B O   1 
HETATM 9868 O  O   . HOH   M 7 .   ? -41.141 6.681   12.211  1.00 31.79 ? 1130 HOH   B O   1 
HETATM 9869 O  O   . HOH   M 7 .   ? -27.101 -15.103 28.455  1.00 36.51 ? 1131 HOH   B O   1 
HETATM 9870 O  O   . HOH   M 7 .   ? -44.954 -7.551  2.136   1.00 36.03 ? 1132 HOH   B O   1 
HETATM 9871 O  O   . HOH   M 7 .   ? -51.290 19.622  34.207  1.00 44.17 ? 1133 HOH   B O   1 
HETATM 9872 O  O   . HOH   M 7 .   ? -43.461 2.037   10.711  1.00 32.62 ? 1134 HOH   B O   1 
HETATM 9873 O  O   . HOH   M 7 .   ? -29.492 -7.162  40.768  1.00 39.30 ? 1135 HOH   B O   1 
HETATM 9874 O  O   . HOH   M 7 .   ? -24.693 -18.430 20.449  1.00 31.68 ? 1136 HOH   B O   1 
HETATM 9875 O  O   . HOH   M 7 .   ? -75.121 -14.142 17.790  1.00 37.16 ? 1137 HOH   B O   1 
HETATM 9876 O  O   . HOH   M 7 .   ? -63.731 8.411   18.528  1.00 26.57 ? 1138 HOH   B O   1 
HETATM 9877 O  O   . HOH   M 7 .   ? -50.786 4.160   38.531  1.00 27.56 ? 1139 HOH   B O   1 
HETATM 9878 O  O   . HOH   M 7 .   ? -30.246 -8.342  32.855  1.00 20.69 ? 1140 HOH   B O   1 
HETATM 9879 O  O   . HOH   M 7 .   ? -40.080 6.062   38.508  1.00 31.92 ? 1141 HOH   B O   1 
HETATM 9880 O  O   . HOH   M 7 .   ? -71.682 -4.373  12.588  1.00 35.80 ? 1142 HOH   B O   1 
HETATM 9881 O  O   . HOH   M 7 .   ? -37.615 9.316   11.657  1.00 37.41 ? 1143 HOH   B O   1 
HETATM 9882 O  O   . HOH   M 7 .   ? -35.271 -0.065  21.538  1.00 34.05 ? 1144 HOH   B O   1 
HETATM 9883 O  O   . HOH   M 7 .   ? -42.664 4.285   44.525  1.00 19.70 ? 1145 HOH   B O   1 
HETATM 9884 O  O   . HOH   M 7 .   ? -54.286 2.040   6.573   1.00 20.94 ? 1146 HOH   B O   1 
HETATM 9885 O  O   . HOH   M 7 .   ? -42.206 6.954   45.424  1.00 31.48 ? 1147 HOH   B O   1 
HETATM 9886 O  O   . HOH   M 7 .   ? -63.501 6.125   16.272  1.00 24.78 ? 1148 HOH   B O   1 
HETATM 9887 O  O   . HOH   M 7 .   ? -75.663 -3.551  33.589  1.00 41.61 ? 1149 HOH   B O   1 
HETATM 9888 O  O   . HOH   M 7 .   ? -72.237 -1.308  20.548  1.00 16.17 ? 1150 HOH   B O   1 
HETATM 9889 O  O   . HOH   M 7 .   ? -42.574 6.042   9.770   1.00 28.22 ? 1151 HOH   B O   1 
# 
