data_8YAZ
# 
_entry.id   8YAZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YAZ         pdb_00008yaz 10.2210/pdb8yaz/pdb 
WWPDB D_1300043986 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'Structure model' 1 1 2025-03-26 ? 
3 'Structure model' 1 2 2025-04-02 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 
3 3 'Structure model' citation        
# 
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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.pdbx_database_id_DOI'    
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.page_last'               
11 3 'Structure model' '_citation.pdbx_database_id_PubMed' 
12 3 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YAZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-11 
_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           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              minoru.kubo@riken.jp 
_pdbx_contact_author.name_first         Minoru 
_pdbx_contact_author.name_last          Kubo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1470-942X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nagao, S.'       1  ? 
'Kuwano, W.'      2  ? 
'Tosha, T.'       3  ? 
'Yamashita, K.'   4  ? 
'Stanfield, J.K.' 5  ? 
'Kasai, C.'       6  ? 
'Ariyasu, S.'     7  ? 
'Shoji, O.'       8  ? 
'Sugimoto, H.'    9  ? 
'Kubo, M.'        10 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                63 
_citation.page_last                 63 
_citation.title                     
'XFEL crystallography reveals catalytic cycle dynamics during non-native substrate oxidation by cytochrome P450BM3.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01440-2 
_citation.pdbx_database_id_PubMed   40075209 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nagao, S.'       1  ? 
primary 'Kuwano, W.'      2  ? 
primary 'Tosha, T.'       3  ? 
primary 'Yamashita, K.'   4  ? 
primary 'Stanfield, J.K.' 5  ? 
primary 'Kasai, C.'       6  ? 
primary 'Ariyasu, S.'     7  ? 
primary 'Hirata, K.'      8  ? 
primary 'Ueno, G.'        9  ? 
primary 'Murakami, H.'    10 ? 
primary 'Ago, H.'         11 ? 
primary 'Yamamoto, M.'    12 ? 
primary 'Shoji, O.'       13 ? 
primary 'Sugimoto, H.'    14 ? 
primary 'Kubo, M.'        15 ? 
# 
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 'Bifunctional cytochrome P450/NADPH--P450 reductase'                           52084.340 2   1.14.14.1,1.6.2.4 
F87A,F393H ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                              616.487   2   ?                 ? 
? ? 
3 non-polymer syn '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' 360.490   2   ?                 ? 
? ? 
4 non-polymer syn ethenylbenzene                                                                 104.149   2   ?                 ? 
? ? 
5 non-polymer syn GLYCEROL                                                                       92.094    3   ?                 ? 
? ? 
6 water       nat water                                                                          18.015    500 ?                 ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome P450(BM-3),Cytochrome P450BM-3,Fatty acid monooxygenase,Flavocytochrome P450 BM3' 
# 
_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       
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLATSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLATSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_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 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEM 
3 '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' D0L 
4 ethenylbenzene                                                                 SYN 
5 GLYCEROL                                                                       GOL 
6 water                                                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ILE n 
1 3   LYS n 
1 4   GLU n 
1 5   MET n 
1 6   PRO n 
1 7   GLN n 
1 8   PRO n 
1 9   LYS n 
1 10  THR n 
1 11  PHE n 
1 12  GLY n 
1 13  GLU n 
1 14  LEU n 
1 15  LYS n 
1 16  ASN n 
1 17  LEU n 
1 18  PRO n 
1 19  LEU n 
1 20  LEU n 
1 21  ASN n 
1 22  THR n 
1 23  ASP n 
1 24  LYS n 
1 25  PRO n 
1 26  VAL n 
1 27  GLN n 
1 28  ALA n 
1 29  LEU n 
1 30  MET n 
1 31  LYS n 
1 32  ILE n 
1 33  ALA n 
1 34  ASP n 
1 35  GLU n 
1 36  LEU n 
1 37  GLY n 
1 38  GLU n 
1 39  ILE n 
1 40  PHE n 
1 41  LYS n 
1 42  PHE n 
1 43  GLU n 
1 44  ALA n 
1 45  PRO n 
1 46  GLY n 
1 47  ARG n 
1 48  VAL n 
1 49  THR n 
1 50  ARG n 
1 51  TYR n 
1 52  LEU n 
1 53  SER n 
1 54  SER n 
1 55  GLN n 
1 56  ARG n 
1 57  LEU n 
1 58  ILE n 
1 59  LYS n 
1 60  GLU n 
1 61  ALA n 
1 62  CYS n 
1 63  ASP n 
1 64  GLU n 
1 65  SER n 
1 66  ARG n 
1 67  PHE n 
1 68  ASP n 
1 69  LYS n 
1 70  ASN n 
1 71  LEU n 
1 72  SER n 
1 73  GLN n 
1 74  ALA n 
1 75  LEU n 
1 76  LYS n 
1 77  PHE n 
1 78  VAL n 
1 79  ARG n 
1 80  ASP n 
1 81  PHE n 
1 82  ALA n 
1 83  GLY n 
1 84  ASP n 
1 85  GLY n 
1 86  LEU n 
1 87  ALA n 
1 88  THR n 
1 89  SER n 
1 90  TRP n 
1 91  THR n 
1 92  HIS n 
1 93  GLU n 
1 94  LYS n 
1 95  ASN n 
1 96  TRP n 
1 97  LYS n 
1 98  LYS n 
1 99  ALA n 
1 100 HIS n 
1 101 ASN n 
1 102 ILE n 
1 103 LEU n 
1 104 LEU n 
1 105 PRO n 
1 106 SER n 
1 107 PHE n 
1 108 SER n 
1 109 GLN n 
1 110 GLN n 
1 111 ALA n 
1 112 MET n 
1 113 LYS n 
1 114 GLY n 
1 115 TYR n 
1 116 HIS n 
1 117 ALA n 
1 118 MET n 
1 119 MET n 
1 120 VAL n 
1 121 ASP n 
1 122 ILE n 
1 123 ALA n 
1 124 VAL n 
1 125 GLN n 
1 126 LEU n 
1 127 VAL n 
1 128 GLN n 
1 129 LYS n 
1 130 TRP n 
1 131 GLU n 
1 132 ARG n 
1 133 LEU n 
1 134 ASN n 
1 135 ALA n 
1 136 ASP n 
1 137 GLU n 
1 138 HIS n 
1 139 ILE n 
1 140 GLU n 
1 141 VAL n 
1 142 PRO n 
1 143 GLU n 
1 144 ASP n 
1 145 MET n 
1 146 THR n 
1 147 ARG n 
1 148 LEU n 
1 149 THR n 
1 150 LEU n 
1 151 ASP n 
1 152 THR n 
1 153 ILE n 
1 154 GLY n 
1 155 LEU n 
1 156 CYS n 
1 157 GLY n 
1 158 PHE n 
1 159 ASN n 
1 160 TYR n 
1 161 ARG n 
1 162 PHE n 
1 163 ASN n 
1 164 SER n 
1 165 PHE n 
1 166 TYR n 
1 167 ARG n 
1 168 ASP n 
1 169 GLN n 
1 170 PRO n 
1 171 HIS n 
1 172 PRO n 
1 173 PHE n 
1 174 ILE n 
1 175 THR n 
1 176 SER n 
1 177 MET n 
1 178 VAL n 
1 179 ARG n 
1 180 ALA n 
1 181 LEU n 
1 182 ASP n 
1 183 GLU n 
1 184 ALA n 
1 185 MET n 
1 186 ASN n 
1 187 LYS n 
1 188 LEU n 
1 189 GLN n 
1 190 ARG n 
1 191 ALA n 
1 192 ASN n 
1 193 PRO n 
1 194 ASP n 
1 195 ASP n 
1 196 PRO n 
1 197 ALA n 
1 198 TYR n 
1 199 ASP n 
1 200 GLU n 
1 201 ASN n 
1 202 LYS n 
1 203 ARG n 
1 204 GLN n 
1 205 PHE n 
1 206 GLN n 
1 207 GLU n 
1 208 ASP n 
1 209 ILE n 
1 210 LYS n 
1 211 VAL n 
1 212 MET n 
1 213 ASN n 
1 214 ASP n 
1 215 LEU n 
1 216 VAL n 
1 217 ASP n 
1 218 LYS n 
1 219 ILE n 
1 220 ILE n 
1 221 ALA n 
1 222 ASP n 
1 223 ARG n 
1 224 LYS n 
1 225 ALA n 
1 226 SER n 
1 227 GLY n 
1 228 GLU n 
1 229 GLN n 
1 230 SER n 
1 231 ASP n 
1 232 ASP n 
1 233 LEU n 
1 234 LEU n 
1 235 THR n 
1 236 HIS n 
1 237 MET n 
1 238 LEU n 
1 239 ASN n 
1 240 GLY n 
1 241 LYS n 
1 242 ASP n 
1 243 PRO n 
1 244 GLU n 
1 245 THR n 
1 246 GLY n 
1 247 GLU n 
1 248 PRO n 
1 249 LEU n 
1 250 ASP n 
1 251 ASP n 
1 252 GLU n 
1 253 ASN n 
1 254 ILE n 
1 255 ARG n 
1 256 TYR n 
1 257 GLN n 
1 258 ILE n 
1 259 ILE n 
1 260 THR n 
1 261 PHE n 
1 262 LEU n 
1 263 ILE n 
1 264 ALA n 
1 265 GLY n 
1 266 HIS n 
1 267 GLU n 
1 268 THR n 
1 269 THR n 
1 270 SER n 
1 271 GLY n 
1 272 LEU n 
1 273 LEU n 
1 274 SER n 
1 275 PHE n 
1 276 ALA n 
1 277 LEU n 
1 278 TYR n 
1 279 PHE n 
1 280 LEU n 
1 281 VAL n 
1 282 LYS n 
1 283 ASN n 
1 284 PRO n 
1 285 HIS n 
1 286 VAL n 
1 287 LEU n 
1 288 GLN n 
1 289 LYS n 
1 290 ALA n 
1 291 ALA n 
1 292 GLU n 
1 293 GLU n 
1 294 ALA n 
1 295 ALA n 
1 296 ARG n 
1 297 VAL n 
1 298 LEU n 
1 299 VAL n 
1 300 ASP n 
1 301 PRO n 
1 302 VAL n 
1 303 PRO n 
1 304 SER n 
1 305 TYR n 
1 306 LYS n 
1 307 GLN n 
1 308 VAL n 
1 309 LYS n 
1 310 GLN n 
1 311 LEU n 
1 312 LYS n 
1 313 TYR n 
1 314 VAL n 
1 315 GLY n 
1 316 MET n 
1 317 VAL n 
1 318 LEU n 
1 319 ASN n 
1 320 GLU n 
1 321 ALA n 
1 322 LEU n 
1 323 ARG n 
1 324 LEU n 
1 325 TRP n 
1 326 PRO n 
1 327 THR n 
1 328 ALA n 
1 329 PRO n 
1 330 ALA n 
1 331 PHE n 
1 332 SER n 
1 333 LEU n 
1 334 TYR n 
1 335 ALA n 
1 336 LYS n 
1 337 GLU n 
1 338 ASP n 
1 339 THR n 
1 340 VAL n 
1 341 LEU n 
1 342 GLY n 
1 343 GLY n 
1 344 GLU n 
1 345 TYR n 
1 346 PRO n 
1 347 LEU n 
1 348 GLU n 
1 349 LYS n 
1 350 GLY n 
1 351 ASP n 
1 352 GLU n 
1 353 LEU n 
1 354 MET n 
1 355 VAL n 
1 356 LEU n 
1 357 ILE n 
1 358 PRO n 
1 359 GLN n 
1 360 LEU n 
1 361 HIS n 
1 362 ARG n 
1 363 ASP n 
1 364 LYS n 
1 365 THR n 
1 366 ILE n 
1 367 TRP n 
1 368 GLY n 
1 369 ASP n 
1 370 ASP n 
1 371 VAL n 
1 372 GLU n 
1 373 GLU n 
1 374 PHE n 
1 375 ARG n 
1 376 PRO n 
1 377 GLU n 
1 378 ARG n 
1 379 PHE n 
1 380 GLU n 
1 381 ASN n 
1 382 PRO n 
1 383 SER n 
1 384 ALA n 
1 385 ILE n 
1 386 PRO n 
1 387 GLN n 
1 388 HIS n 
1 389 ALA n 
1 390 PHE n 
1 391 LYS n 
1 392 PRO n 
1 393 HIS n 
1 394 GLY n 
1 395 ASN n 
1 396 GLY n 
1 397 GLN n 
1 398 ARG n 
1 399 ALA n 
1 400 CYS n 
1 401 ILE n 
1 402 GLY n 
1 403 GLN n 
1 404 GLN n 
1 405 PHE n 
1 406 ALA n 
1 407 LEU n 
1 408 HIS n 
1 409 GLU n 
1 410 ALA n 
1 411 THR n 
1 412 LEU n 
1 413 VAL n 
1 414 LEU n 
1 415 GLY n 
1 416 MET n 
1 417 MET n 
1 418 LEU n 
1 419 LYS n 
1 420 HIS n 
1 421 PHE n 
1 422 ASP n 
1 423 PHE n 
1 424 GLU n 
1 425 ASP n 
1 426 HIS n 
1 427 THR n 
1 428 ASN n 
1 429 TYR n 
1 430 GLU n 
1 431 LEU n 
1 432 ASP n 
1 433 ILE n 
1 434 LYS n 
1 435 GLU n 
1 436 THR n 
1 437 LEU n 
1 438 THR n 
1 439 LEU n 
1 440 LYS n 
1 441 PRO n 
1 442 GLU n 
1 443 GLY n 
1 444 PHE n 
1 445 VAL n 
1 446 VAL n 
1 447 LYS n 
1 448 ALA n 
1 449 LYS n 
1 450 SER n 
1 451 LYS n 
1 452 LYS n 
1 453 ILE n 
1 454 PRO n 
1 455 LEU 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                   455 
_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                    'NBRC 15308 = ATCC 14581' 
_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      'Priestia megaterium NBRC 15308 = ATCC 14581' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1348623 
_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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
D0L non-polymer         . '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' ? 'C21 H32 N2 O3'    
360.490 
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  
GOL non-polymer         . GLYCEROL                                                                       
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEME 'C34 H32 Fe N4 O4' 
616.487 
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 
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 
SYN non-polymer         . ethenylbenzene                                                                 styrene 'C8 H8' 104.149 
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   THR 1   1   1   THR THR A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   MET 5   5   5   MET MET A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  MET 30  30  30  MET MET A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  CYS 62  62  62  CYS CYS A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TRP 90  90  90  TRP TRP A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 MET 177 177 177 MET MET A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 HIS 236 236 236 HIS HIS A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 HIS 266 266 266 HIS HIS A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 TYR 278 278 278 TYR TYR A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 HIS 285 285 285 HIS HIS A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 GLN 307 307 307 GLN GLN A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 TYR 313 313 313 TYR TYR A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 MET 316 316 316 MET MET A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 TRP 325 325 325 TRP TRP A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 MET 354 354 354 MET MET A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 TRP 367 367 367 TRP TRP A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 PHE 374 374 374 PHE PHE A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 PRO 382 382 382 PRO PRO A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 ILE 385 385 385 ILE ILE A . n 
A 1 386 PRO 386 386 386 PRO PRO A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 HIS 388 388 388 HIS HIS A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 HIS 393 393 393 HIS HIS A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 GLN 397 397 397 GLN GLN A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 CYS 400 400 400 CYS CYS A . n 
A 1 401 ILE 401 401 401 ILE ILE A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 GLN 403 403 403 GLN GLN A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 GLY 415 415 415 GLY GLY A . n 
A 1 416 MET 416 416 416 MET MET A . n 
A 1 417 MET 417 417 417 MET MET A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 LYS 419 419 419 LYS LYS A . n 
A 1 420 HIS 420 420 420 HIS HIS A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 PHE 423 423 423 PHE PHE A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 THR 427 427 427 THR THR A . n 
A 1 428 ASN 428 428 428 ASN ASN A . n 
A 1 429 TYR 429 429 429 TYR TYR A . n 
A 1 430 GLU 430 430 430 GLU GLU A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 THR 436 436 436 THR THR A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 PRO 441 441 441 PRO PRO A . n 
A 1 442 GLU 442 442 442 GLU GLU A . n 
A 1 443 GLY 443 443 443 GLY GLY A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 VAL 445 445 445 VAL VAL A . n 
A 1 446 VAL 446 446 446 VAL VAL A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 LYS 449 449 449 LYS LYS A . n 
A 1 450 SER 450 450 450 SER SER A . n 
A 1 451 LYS 451 451 451 LYS LYS A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 ILE 453 453 453 ILE ILE A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
B 1 1   THR 1   1   1   THR THR B . n 
B 1 2   ILE 2   2   2   ILE ILE B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   GLU 4   4   4   GLU GLU B . n 
B 1 5   MET 5   5   5   MET MET B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLN 7   7   7   GLN GLN B . n 
B 1 8   PRO 8   8   8   PRO PRO B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  THR 10  10  10  THR THR B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  ASN 21  21  21  ASN ASN B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  VAL 26  26  26  VAL VAL B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  MET 30  30  30  MET MET B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  CYS 62  62  62  CYS CYS B . n 
B 1 63  ASP 63  63  63  ASP ASP B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  PHE 67  67  67  PHE PHE B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  GLN 73  73  73  GLN GLN B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  PHE 77  77  77  PHE PHE B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  TRP 90  90  90  TRP TRP B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  TRP 96  96  96  TRP TRP B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 PRO 105 105 105 PRO PRO B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 MET 112 112 112 MET MET B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 HIS 116 116 116 HIS HIS B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 MET 118 118 118 MET MET B . n 
B 1 119 MET 119 119 119 MET MET B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLN 125 125 125 GLN GLN B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 GLN 128 128 128 GLN GLN B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 TRP 130 130 130 TRP TRP B . n 
B 1 131 GLU 131 131 131 GLU GLU B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 MET 145 145 145 MET MET B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 ARG 147 147 147 ARG ARG B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 ASP 151 151 151 ASP ASP B . n 
B 1 152 THR 152 152 152 THR THR B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 GLY 157 157 157 GLY GLY B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 ASN 163 163 163 ASN ASN B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 ASP 168 168 168 ASP ASP B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 SER 176 176 176 SER SER B . n 
B 1 177 MET 177 177 177 MET MET B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 ARG 190 190 190 ARG ARG B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 ASN 192 192 192 ASN ASN B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 ASP 194 194 194 ASP ASP B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 PRO 196 196 196 PRO PRO B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 GLU 200 200 200 GLU GLU B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 LYS 202 202 202 LYS LYS B . n 
B 1 203 ARG 203 203 203 ARG ARG B . n 
B 1 204 GLN 204 204 204 GLN GLN B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 GLN 206 206 206 GLN GLN B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 LYS 210 210 210 LYS LYS B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 ASP 217 217 217 ASP ASP B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 ARG 223 223 223 ARG ARG B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 HIS 236 236 236 HIS HIS B . n 
B 1 237 MET 237 237 237 MET MET B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 ASN 239 239 239 ASN ASN B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 LYS 241 241 241 LYS LYS B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 PRO 248 248 248 PRO PRO B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 ASP 250 250 250 ASP ASP B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 GLU 252 252 252 GLU GLU B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ILE 263 263 263 ILE ILE B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 HIS 266 266 266 HIS HIS B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 SER 270 270 270 SER SER B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 PHE 275 275 275 PHE PHE B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 TYR 278 278 278 TYR TYR B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 ASN 283 283 283 ASN ASN B . n 
B 1 284 PRO 284 284 284 PRO PRO B . n 
B 1 285 HIS 285 285 285 HIS HIS B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 LYS 289 289 289 LYS LYS B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 GLU 293 293 293 GLU GLU B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 LEU 298 298 298 LEU LEU B . n 
B 1 299 VAL 299 299 299 VAL VAL B . n 
B 1 300 ASP 300 300 300 ASP ASP B . n 
B 1 301 PRO 301 301 301 PRO PRO B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 TYR 305 305 305 TYR TYR B . n 
B 1 306 LYS 306 306 306 LYS LYS B . n 
B 1 307 GLN 307 307 307 GLN GLN B . n 
B 1 308 VAL 308 308 308 VAL VAL B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 GLN 310 310 310 GLN GLN B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 TYR 313 313 313 TYR TYR B . n 
B 1 314 VAL 314 314 314 VAL VAL B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 MET 316 316 316 MET MET B . n 
B 1 317 VAL 317 317 317 VAL VAL B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 ASN 319 319 319 ASN ASN B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 TRP 325 325 325 TRP TRP B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 THR 327 327 327 THR THR B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 PRO 329 329 329 PRO PRO B . n 
B 1 330 ALA 330 330 330 ALA ALA B . n 
B 1 331 PHE 331 331 331 PHE PHE B . n 
B 1 332 SER 332 332 332 SER SER B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 TYR 334 334 334 TYR TYR B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 GLU 337 337 337 GLU GLU B . n 
B 1 338 ASP 338 338 338 ASP ASP B . n 
B 1 339 THR 339 339 339 THR THR B . n 
B 1 340 VAL 340 340 340 VAL VAL B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 PRO 346 346 346 PRO PRO B . n 
B 1 347 LEU 347 347 347 LEU LEU B . n 
B 1 348 GLU 348 348 348 GLU GLU B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 ASP 351 351 351 ASP ASP B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 LEU 353 353 353 LEU LEU B . n 
B 1 354 MET 354 354 354 MET MET B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 PRO 358 358 358 PRO PRO B . n 
B 1 359 GLN 359 359 359 GLN GLN B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 HIS 361 361 361 HIS HIS B . n 
B 1 362 ARG 362 362 362 ARG ARG B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 LYS 364 364 364 LYS LYS B . n 
B 1 365 THR 365 365 365 THR THR B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 TRP 367 367 367 TRP TRP B . n 
B 1 368 GLY 368 368 368 GLY GLY B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 ASP 370 370 370 ASP ASP B . n 
B 1 371 VAL 371 371 371 VAL VAL B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 PHE 374 374 374 PHE PHE B . n 
B 1 375 ARG 375 375 375 ARG ARG B . n 
B 1 376 PRO 376 376 376 PRO PRO B . n 
B 1 377 GLU 377 377 377 GLU GLU B . n 
B 1 378 ARG 378 378 378 ARG ARG B . n 
B 1 379 PHE 379 379 379 PHE PHE B . n 
B 1 380 GLU 380 380 380 GLU GLU B . n 
B 1 381 ASN 381 381 381 ASN ASN B . n 
B 1 382 PRO 382 382 382 PRO PRO B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 ALA 384 384 384 ALA ALA B . n 
B 1 385 ILE 385 385 385 ILE ILE B . n 
B 1 386 PRO 386 386 386 PRO PRO B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 HIS 388 388 388 HIS HIS B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 LYS 391 391 391 LYS LYS B . n 
B 1 392 PRO 392 392 392 PRO PRO B . n 
B 1 393 HIS 393 393 393 HIS HIS B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 ASN 395 395 395 ASN ASN B . n 
B 1 396 GLY 396 396 396 GLY GLY B . n 
B 1 397 GLN 397 397 397 GLN GLN B . n 
B 1 398 ARG 398 398 398 ARG ARG B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 CYS 400 400 400 CYS CYS B . n 
B 1 401 ILE 401 401 401 ILE ILE B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 GLN 403 403 403 GLN GLN B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 PHE 405 405 405 PHE PHE B . n 
B 1 406 ALA 406 406 406 ALA ALA B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 HIS 408 408 408 HIS HIS B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 ALA 410 410 410 ALA ALA B . n 
B 1 411 THR 411 411 411 THR THR B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 VAL 413 413 413 VAL VAL B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 GLY 415 415 415 GLY GLY B . n 
B 1 416 MET 416 416 416 MET MET B . n 
B 1 417 MET 417 417 417 MET MET B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 LYS 419 419 419 LYS LYS B . n 
B 1 420 HIS 420 420 420 HIS HIS B . n 
B 1 421 PHE 421 421 421 PHE PHE B . n 
B 1 422 ASP 422 422 422 ASP ASP B . n 
B 1 423 PHE 423 423 423 PHE PHE B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 ASP 425 425 425 ASP ASP B . n 
B 1 426 HIS 426 426 426 HIS HIS B . n 
B 1 427 THR 427 427 427 THR THR B . n 
B 1 428 ASN 428 428 428 ASN ASN B . n 
B 1 429 TYR 429 429 429 TYR TYR B . n 
B 1 430 GLU 430 430 430 GLU GLU B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ASP 432 432 432 ASP ASP B . n 
B 1 433 ILE 433 433 433 ILE ILE B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 GLU 435 435 435 GLU GLU B . n 
B 1 436 THR 436 436 436 THR THR B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 LEU 439 439 439 LEU LEU B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 PRO 441 441 441 PRO PRO B . n 
B 1 442 GLU 442 442 442 GLU GLU B . n 
B 1 443 GLY 443 443 443 GLY GLY B . n 
B 1 444 PHE 444 444 444 PHE PHE B . n 
B 1 445 VAL 445 445 445 VAL VAL B . n 
B 1 446 VAL 446 446 446 VAL VAL B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 LYS 449 449 449 LYS LYS B . n 
B 1 450 SER 450 450 450 SER SER B . n 
B 1 451 LYS 451 451 451 LYS LYS B . n 
B 1 452 LYS 452 452 452 LYS LYS B . n 
B 1 453 ILE 453 453 453 ILE ILE B . n 
B 1 454 PRO 454 454 454 PRO PRO B . n 
B 1 455 LEU 455 455 455 LEU LEU B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SYN ? ? SYN ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 HEM 1   501 501 HEM HEM A . 
D 3 D0L 1   502 503 D0L 7PF A . 
E 4 SYN 1   503 601 SYN SYN A . 
F 5 GOL 1   504 602 GOL GOL A . 
G 5 GOL 1   505 603 GOL GOL A . 
H 2 HEM 1   501 501 HEM HEM B . 
I 3 D0L 1   502 503 D0L 7PF B . 
J 4 SYN 1   503 601 SYN SYN B . 
K 5 GOL 1   504 602 GOL GOL B . 
L 6 HOH 1   601 418 HOH HOH A . 
L 6 HOH 2   602 492 HOH HOH A . 
L 6 HOH 3   603 464 HOH HOH A . 
L 6 HOH 4   604 460 HOH HOH A . 
L 6 HOH 5   605 226 HOH HOH A . 
L 6 HOH 6   606 446 HOH HOH A . 
L 6 HOH 7   607 392 HOH HOH A . 
L 6 HOH 8   608 500 HOH HOH A . 
L 6 HOH 9   609 336 HOH HOH A . 
L 6 HOH 10  610 322 HOH HOH A . 
L 6 HOH 11  611 88  HOH HOH A . 
L 6 HOH 12  612 176 HOH HOH A . 
L 6 HOH 13  613 276 HOH HOH A . 
L 6 HOH 14  614 239 HOH HOH A . 
L 6 HOH 15  615 402 HOH HOH A . 
L 6 HOH 16  616 389 HOH HOH A . 
L 6 HOH 17  617 178 HOH HOH A . 
L 6 HOH 18  618 440 HOH HOH A . 
L 6 HOH 19  619 259 HOH HOH A . 
L 6 HOH 20  620 52  HOH HOH A . 
L 6 HOH 21  621 327 HOH HOH A . 
L 6 HOH 22  622 159 HOH HOH A . 
L 6 HOH 23  623 207 HOH HOH A . 
L 6 HOH 24  624 338 HOH HOH A . 
L 6 HOH 25  625 467 HOH HOH A . 
L 6 HOH 26  626 442 HOH HOH A . 
L 6 HOH 27  627 444 HOH HOH A . 
L 6 HOH 28  628 356 HOH HOH A . 
L 6 HOH 29  629 100 HOH HOH A . 
L 6 HOH 30  630 422 HOH HOH A . 
L 6 HOH 31  631 218 HOH HOH A . 
L 6 HOH 32  632 368 HOH HOH A . 
L 6 HOH 33  633 404 HOH HOH A . 
L 6 HOH 34  634 79  HOH HOH A . 
L 6 HOH 35  635 268 HOH HOH A . 
L 6 HOH 36  636 236 HOH HOH A . 
L 6 HOH 37  637 126 HOH HOH A . 
L 6 HOH 38  638 288 HOH HOH A . 
L 6 HOH 39  639 251 HOH HOH A . 
L 6 HOH 40  640 307 HOH HOH A . 
L 6 HOH 41  641 245 HOH HOH A . 
L 6 HOH 42  642 105 HOH HOH A . 
L 6 HOH 43  643 439 HOH HOH A . 
L 6 HOH 44  644 191 HOH HOH A . 
L 6 HOH 45  645 435 HOH HOH A . 
L 6 HOH 46  646 273 HOH HOH A . 
L 6 HOH 47  647 483 HOH HOH A . 
L 6 HOH 48  648 395 HOH HOH A . 
L 6 HOH 49  649 68  HOH HOH A . 
L 6 HOH 50  650 22  HOH HOH A . 
L 6 HOH 51  651 437 HOH HOH A . 
L 6 HOH 52  652 92  HOH HOH A . 
L 6 HOH 53  653 459 HOH HOH A . 
L 6 HOH 54  654 78  HOH HOH A . 
L 6 HOH 55  655 30  HOH HOH A . 
L 6 HOH 56  656 474 HOH HOH A . 
L 6 HOH 57  657 309 HOH HOH A . 
L 6 HOH 58  658 76  HOH HOH A . 
L 6 HOH 59  659 74  HOH HOH A . 
L 6 HOH 60  660 426 HOH HOH A . 
L 6 HOH 61  661 406 HOH HOH A . 
L 6 HOH 62  662 289 HOH HOH A . 
L 6 HOH 63  663 48  HOH HOH A . 
L 6 HOH 64  664 70  HOH HOH A . 
L 6 HOH 65  665 143 HOH HOH A . 
L 6 HOH 66  666 50  HOH HOH A . 
L 6 HOH 67  667 189 HOH HOH A . 
L 6 HOH 68  668 477 HOH HOH A . 
L 6 HOH 69  669 229 HOH HOH A . 
L 6 HOH 70  670 473 HOH HOH A . 
L 6 HOH 71  671 28  HOH HOH A . 
L 6 HOH 72  672 152 HOH HOH A . 
L 6 HOH 73  673 21  HOH HOH A . 
L 6 HOH 74  674 186 HOH HOH A . 
L 6 HOH 75  675 221 HOH HOH A . 
L 6 HOH 76  676 204 HOH HOH A . 
L 6 HOH 77  677 255 HOH HOH A . 
L 6 HOH 78  678 393 HOH HOH A . 
L 6 HOH 79  679 269 HOH HOH A . 
L 6 HOH 80  680 124 HOH HOH A . 
L 6 HOH 81  681 187 HOH HOH A . 
L 6 HOH 82  682 430 HOH HOH A . 
L 6 HOH 83  683 36  HOH HOH A . 
L 6 HOH 84  684 119 HOH HOH A . 
L 6 HOH 85  685 352 HOH HOH A . 
L 6 HOH 86  686 39  HOH HOH A . 
L 6 HOH 87  687 121 HOH HOH A . 
L 6 HOH 88  688 227 HOH HOH A . 
L 6 HOH 89  689 125 HOH HOH A . 
L 6 HOH 90  690 38  HOH HOH A . 
L 6 HOH 91  691 396 HOH HOH A . 
L 6 HOH 92  692 405 HOH HOH A . 
L 6 HOH 93  693 57  HOH HOH A . 
L 6 HOH 94  694 109 HOH HOH A . 
L 6 HOH 95  695 194 HOH HOH A . 
L 6 HOH 96  696 419 HOH HOH A . 
L 6 HOH 97  697 212 HOH HOH A . 
L 6 HOH 98  698 366 HOH HOH A . 
L 6 HOH 99  699 123 HOH HOH A . 
L 6 HOH 100 700 413 HOH HOH A . 
L 6 HOH 101 701 324 HOH HOH A . 
L 6 HOH 102 702 300 HOH HOH A . 
L 6 HOH 103 703 449 HOH HOH A . 
L 6 HOH 104 704 107 HOH HOH A . 
L 6 HOH 105 705 148 HOH HOH A . 
L 6 HOH 106 706 407 HOH HOH A . 
L 6 HOH 107 707 408 HOH HOH A . 
L 6 HOH 108 708 478 HOH HOH A . 
L 6 HOH 109 709 158 HOH HOH A . 
L 6 HOH 110 710 164 HOH HOH A . 
L 6 HOH 111 711 340 HOH HOH A . 
L 6 HOH 112 712 156 HOH HOH A . 
L 6 HOH 113 713 306 HOH HOH A . 
L 6 HOH 114 714 484 HOH HOH A . 
L 6 HOH 115 715 80  HOH HOH A . 
L 6 HOH 116 716 3   HOH HOH A . 
L 6 HOH 117 717 494 HOH HOH A . 
L 6 HOH 118 718 342 HOH HOH A . 
L 6 HOH 119 719 302 HOH HOH A . 
L 6 HOH 120 720 416 HOH HOH A . 
L 6 HOH 121 721 290 HOH HOH A . 
L 6 HOH 122 722 400 HOH HOH A . 
L 6 HOH 123 723 49  HOH HOH A . 
L 6 HOH 124 724 17  HOH HOH A . 
L 6 HOH 125 725 63  HOH HOH A . 
L 6 HOH 126 726 248 HOH HOH A . 
L 6 HOH 127 727 173 HOH HOH A . 
L 6 HOH 128 728 434 HOH HOH A . 
L 6 HOH 129 729 262 HOH HOH A . 
L 6 HOH 130 730 365 HOH HOH A . 
L 6 HOH 131 731 82  HOH HOH A . 
L 6 HOH 132 732 448 HOH HOH A . 
L 6 HOH 133 733 420 HOH HOH A . 
L 6 HOH 134 734 469 HOH HOH A . 
L 6 HOH 135 735 184 HOH HOH A . 
L 6 HOH 136 736 75  HOH HOH A . 
L 6 HOH 137 737 294 HOH HOH A . 
L 6 HOH 138 738 95  HOH HOH A . 
L 6 HOH 139 739 411 HOH HOH A . 
L 6 HOH 140 740 357 HOH HOH A . 
L 6 HOH 141 741 200 HOH HOH A . 
L 6 HOH 142 742 20  HOH HOH A . 
L 6 HOH 143 743 370 HOH HOH A . 
L 6 HOH 144 744 337 HOH HOH A . 
L 6 HOH 145 745 133 HOH HOH A . 
L 6 HOH 146 746 462 HOH HOH A . 
L 6 HOH 147 747 188 HOH HOH A . 
L 6 HOH 148 748 332 HOH HOH A . 
L 6 HOH 149 749 23  HOH HOH A . 
L 6 HOH 150 750 458 HOH HOH A . 
L 6 HOH 151 751 166 HOH HOH A . 
L 6 HOH 152 752 210 HOH HOH A . 
L 6 HOH 153 753 297 HOH HOH A . 
L 6 HOH 154 754 386 HOH HOH A . 
L 6 HOH 155 755 208 HOH HOH A . 
L 6 HOH 156 756 295 HOH HOH A . 
L 6 HOH 157 757 343 HOH HOH A . 
L 6 HOH 158 758 62  HOH HOH A . 
L 6 HOH 159 759 175 HOH HOH A . 
L 6 HOH 160 760 339 HOH HOH A . 
L 6 HOH 161 761 275 HOH HOH A . 
L 6 HOH 162 762 304 HOH HOH A . 
L 6 HOH 163 763 475 HOH HOH A . 
L 6 HOH 164 764 320 HOH HOH A . 
L 6 HOH 165 765 160 HOH HOH A . 
L 6 HOH 166 766 423 HOH HOH A . 
L 6 HOH 167 767 260 HOH HOH A . 
L 6 HOH 168 768 310 HOH HOH A . 
L 6 HOH 169 769 397 HOH HOH A . 
L 6 HOH 170 770 421 HOH HOH A . 
L 6 HOH 171 771 375 HOH HOH A . 
L 6 HOH 172 772 192 HOH HOH A . 
L 6 HOH 173 773 101 HOH HOH A . 
L 6 HOH 174 774 202 HOH HOH A . 
L 6 HOH 175 775 198 HOH HOH A . 
L 6 HOH 176 776 472 HOH HOH A . 
L 6 HOH 177 777 463 HOH HOH A . 
L 6 HOH 178 778 32  HOH HOH A . 
L 6 HOH 179 779 223 HOH HOH A . 
L 6 HOH 180 780 384 HOH HOH A . 
L 6 HOH 181 781 468 HOH HOH A . 
L 6 HOH 182 782 409 HOH HOH A . 
L 6 HOH 183 783 319 HOH HOH A . 
L 6 HOH 184 784 354 HOH HOH A . 
L 6 HOH 185 785 323 HOH HOH A . 
L 6 HOH 186 786 326 HOH HOH A . 
L 6 HOH 187 787 398 HOH HOH A . 
L 6 HOH 188 788 367 HOH HOH A . 
L 6 HOH 189 789 190 HOH HOH A . 
L 6 HOH 190 790 168 HOH HOH A . 
L 6 HOH 191 791 272 HOH HOH A . 
L 6 HOH 192 792 263 HOH HOH A . 
L 6 HOH 193 793 466 HOH HOH A . 
L 6 HOH 194 794 264 HOH HOH A . 
L 6 HOH 195 795 383 HOH HOH A . 
L 6 HOH 196 796 457 HOH HOH A . 
L 6 HOH 197 797 491 HOH HOH A . 
L 6 HOH 198 798 234 HOH HOH A . 
L 6 HOH 199 799 346 HOH HOH A . 
L 6 HOH 200 800 465 HOH HOH A . 
L 6 HOH 201 801 401 HOH HOH A . 
L 6 HOH 202 802 436 HOH HOH A . 
L 6 HOH 203 803 417 HOH HOH A . 
L 6 HOH 204 804 428 HOH HOH A . 
L 6 HOH 205 805 455 HOH HOH A . 
L 6 HOH 206 806 321 HOH HOH A . 
L 6 HOH 207 807 161 HOH HOH A . 
L 6 HOH 208 808 431 HOH HOH A . 
L 6 HOH 209 809 373 HOH HOH A . 
L 6 HOH 210 810 447 HOH HOH A . 
L 6 HOH 211 811 64  HOH HOH A . 
L 6 HOH 212 812 331 HOH HOH A . 
L 6 HOH 213 813 217 HOH HOH A . 
L 6 HOH 214 814 371 HOH HOH A . 
L 6 HOH 215 815 249 HOH HOH A . 
L 6 HOH 216 816 495 HOH HOH A . 
L 6 HOH 217 817 410 HOH HOH A . 
L 6 HOH 218 818 441 HOH HOH A . 
L 6 HOH 219 819 471 HOH HOH A . 
L 6 HOH 220 820 424 HOH HOH A . 
L 6 HOH 221 821 344 HOH HOH A . 
L 6 HOH 222 822 476 HOH HOH A . 
L 6 HOH 223 823 388 HOH HOH A . 
L 6 HOH 224 824 452 HOH HOH A . 
M 6 HOH 1   601 174 HOH HOH B . 
M 6 HOH 2   602 43  HOH HOH B . 
M 6 HOH 3   603 312 HOH HOH B . 
M 6 HOH 4   604 470 HOH HOH B . 
M 6 HOH 5   605 267 HOH HOH B . 
M 6 HOH 6   606 89  HOH HOH B . 
M 6 HOH 7   607 361 HOH HOH B . 
M 6 HOH 8   608 359 HOH HOH B . 
M 6 HOH 9   609 379 HOH HOH B . 
M 6 HOH 10  610 380 HOH HOH B . 
M 6 HOH 11  611 171 HOH HOH B . 
M 6 HOH 12  612 211 HOH HOH B . 
M 6 HOH 13  613 197 HOH HOH B . 
M 6 HOH 14  614 136 HOH HOH B . 
M 6 HOH 15  615 325 HOH HOH B . 
M 6 HOH 16  616 364 HOH HOH B . 
M 6 HOH 17  617 203 HOH HOH B . 
M 6 HOH 18  618 382 HOH HOH B . 
M 6 HOH 19  619 138 HOH HOH B . 
M 6 HOH 20  620 445 HOH HOH B . 
M 6 HOH 21  621 334 HOH HOH B . 
M 6 HOH 22  622 1   HOH HOH B . 
M 6 HOH 23  623 355 HOH HOH B . 
M 6 HOH 24  624 438 HOH HOH B . 
M 6 HOH 25  625 177 HOH HOH B . 
M 6 HOH 26  626 235 HOH HOH B . 
M 6 HOH 27  627 293 HOH HOH B . 
M 6 HOH 28  628 33  HOH HOH B . 
M 6 HOH 29  629 266 HOH HOH B . 
M 6 HOH 30  630 206 HOH HOH B . 
M 6 HOH 31  631 305 HOH HOH B . 
M 6 HOH 32  632 10  HOH HOH B . 
M 6 HOH 33  633 99  HOH HOH B . 
M 6 HOH 34  634 137 HOH HOH B . 
M 6 HOH 35  635 27  HOH HOH B . 
M 6 HOH 36  636 46  HOH HOH B . 
M 6 HOH 37  637 67  HOH HOH B . 
M 6 HOH 38  638 216 HOH HOH B . 
M 6 HOH 39  639 487 HOH HOH B . 
M 6 HOH 40  640 128 HOH HOH B . 
M 6 HOH 41  641 55  HOH HOH B . 
M 6 HOH 42  642 58  HOH HOH B . 
M 6 HOH 43  643 443 HOH HOH B . 
M 6 HOH 44  644 250 HOH HOH B . 
M 6 HOH 45  645 94  HOH HOH B . 
M 6 HOH 46  646 247 HOH HOH B . 
M 6 HOH 47  647 219 HOH HOH B . 
M 6 HOH 48  648 362 HOH HOH B . 
M 6 HOH 49  649 81  HOH HOH B . 
M 6 HOH 50  650 60  HOH HOH B . 
M 6 HOH 51  651 253 HOH HOH B . 
M 6 HOH 52  652 114 HOH HOH B . 
M 6 HOH 53  653 224 HOH HOH B . 
M 6 HOH 54  654 252 HOH HOH B . 
M 6 HOH 55  655 427 HOH HOH B . 
M 6 HOH 56  656 232 HOH HOH B . 
M 6 HOH 57  657 69  HOH HOH B . 
M 6 HOH 58  658 71  HOH HOH B . 
M 6 HOH 59  659 84  HOH HOH B . 
M 6 HOH 60  660 108 HOH HOH B . 
M 6 HOH 61  661 170 HOH HOH B . 
M 6 HOH 62  662 8   HOH HOH B . 
M 6 HOH 63  663 155 HOH HOH B . 
M 6 HOH 64  664 73  HOH HOH B . 
M 6 HOH 65  665 2   HOH HOH B . 
M 6 HOH 66  666 77  HOH HOH B . 
M 6 HOH 67  667 24  HOH HOH B . 
M 6 HOH 68  668 26  HOH HOH B . 
M 6 HOH 69  669 97  HOH HOH B . 
M 6 HOH 70  670 149 HOH HOH B . 
M 6 HOH 71  671 335 HOH HOH B . 
M 6 HOH 72  672 54  HOH HOH B . 
M 6 HOH 73  673 31  HOH HOH B . 
M 6 HOH 74  674 16  HOH HOH B . 
M 6 HOH 75  675 83  HOH HOH B . 
M 6 HOH 76  676 394 HOH HOH B . 
M 6 HOH 77  677 282 HOH HOH B . 
M 6 HOH 78  678 122 HOH HOH B . 
M 6 HOH 79  679 233 HOH HOH B . 
M 6 HOH 80  680 353 HOH HOH B . 
M 6 HOH 81  681 34  HOH HOH B . 
M 6 HOH 82  682 433 HOH HOH B . 
M 6 HOH 83  683 5   HOH HOH B . 
M 6 HOH 84  684 56  HOH HOH B . 
M 6 HOH 85  685 104 HOH HOH B . 
M 6 HOH 86  686 291 HOH HOH B . 
M 6 HOH 87  687 4   HOH HOH B . 
M 6 HOH 88  688 195 HOH HOH B . 
M 6 HOH 89  689 285 HOH HOH B . 
M 6 HOH 90  690 456 HOH HOH B . 
M 6 HOH 91  691 244 HOH HOH B . 
M 6 HOH 92  692 358 HOH HOH B . 
M 6 HOH 93  693 6   HOH HOH B . 
M 6 HOH 94  694 9   HOH HOH B . 
M 6 HOH 95  695 44  HOH HOH B . 
M 6 HOH 96  696 454 HOH HOH B . 
M 6 HOH 97  697 199 HOH HOH B . 
M 6 HOH 98  698 243 HOH HOH B . 
M 6 HOH 99  699 317 HOH HOH B . 
M 6 HOH 100 700 180 HOH HOH B . 
M 6 HOH 101 701 15  HOH HOH B . 
M 6 HOH 102 702 181 HOH HOH B . 
M 6 HOH 103 703 481 HOH HOH B . 
M 6 HOH 104 704 333 HOH HOH B . 
M 6 HOH 105 705 47  HOH HOH B . 
M 6 HOH 106 706 144 HOH HOH B . 
M 6 HOH 107 707 65  HOH HOH B . 
M 6 HOH 108 708 157 HOH HOH B . 
M 6 HOH 109 709 13  HOH HOH B . 
M 6 HOH 110 710 165 HOH HOH B . 
M 6 HOH 111 711 222 HOH HOH B . 
M 6 HOH 112 712 51  HOH HOH B . 
M 6 HOH 113 713 37  HOH HOH B . 
M 6 HOH 114 714 167 HOH HOH B . 
M 6 HOH 115 715 242 HOH HOH B . 
M 6 HOH 116 716 110 HOH HOH B . 
M 6 HOH 117 717 103 HOH HOH B . 
M 6 HOH 118 718 35  HOH HOH B . 
M 6 HOH 119 719 270 HOH HOH B . 
M 6 HOH 120 720 330 HOH HOH B . 
M 6 HOH 121 721 45  HOH HOH B . 
M 6 HOH 122 722 59  HOH HOH B . 
M 6 HOH 123 723 90  HOH HOH B . 
M 6 HOH 124 724 11  HOH HOH B . 
M 6 HOH 125 725 72  HOH HOH B . 
M 6 HOH 126 726 129 HOH HOH B . 
M 6 HOH 127 727 240 HOH HOH B . 
M 6 HOH 128 728 482 HOH HOH B . 
M 6 HOH 129 729 120 HOH HOH B . 
M 6 HOH 130 730 271 HOH HOH B . 
M 6 HOH 131 731 40  HOH HOH B . 
M 6 HOH 132 732 311 HOH HOH B . 
M 6 HOH 133 733 215 HOH HOH B . 
M 6 HOH 134 734 196 HOH HOH B . 
M 6 HOH 135 735 19  HOH HOH B . 
M 6 HOH 136 736 403 HOH HOH B . 
M 6 HOH 137 737 341 HOH HOH B . 
M 6 HOH 138 738 7   HOH HOH B . 
M 6 HOH 139 739 287 HOH HOH B . 
M 6 HOH 140 740 42  HOH HOH B . 
M 6 HOH 141 741 102 HOH HOH B . 
M 6 HOH 142 742 292 HOH HOH B . 
M 6 HOH 143 743 53  HOH HOH B . 
M 6 HOH 144 744 429 HOH HOH B . 
M 6 HOH 145 745 316 HOH HOH B . 
M 6 HOH 146 746 12  HOH HOH B . 
M 6 HOH 147 747 432 HOH HOH B . 
M 6 HOH 148 748 117 HOH HOH B . 
M 6 HOH 149 749 115 HOH HOH B . 
M 6 HOH 150 750 14  HOH HOH B . 
M 6 HOH 151 751 497 HOH HOH B . 
M 6 HOH 152 752 329 HOH HOH B . 
M 6 HOH 153 753 387 HOH HOH B . 
M 6 HOH 154 754 485 HOH HOH B . 
M 6 HOH 155 755 134 HOH HOH B . 
M 6 HOH 156 756 345 HOH HOH B . 
M 6 HOH 157 757 286 HOH HOH B . 
M 6 HOH 158 758 314 HOH HOH B . 
M 6 HOH 159 759 228 HOH HOH B . 
M 6 HOH 160 760 150 HOH HOH B . 
M 6 HOH 161 761 118 HOH HOH B . 
M 6 HOH 162 762 296 HOH HOH B . 
M 6 HOH 163 763 193 HOH HOH B . 
M 6 HOH 164 764 25  HOH HOH B . 
M 6 HOH 165 765 230 HOH HOH B . 
M 6 HOH 166 766 496 HOH HOH B . 
M 6 HOH 167 767 183 HOH HOH B . 
M 6 HOH 168 768 131 HOH HOH B . 
M 6 HOH 169 769 151 HOH HOH B . 
M 6 HOH 170 770 41  HOH HOH B . 
M 6 HOH 171 771 132 HOH HOH B . 
M 6 HOH 172 772 154 HOH HOH B . 
M 6 HOH 173 773 91  HOH HOH B . 
M 6 HOH 174 774 299 HOH HOH B . 
M 6 HOH 175 775 29  HOH HOH B . 
M 6 HOH 176 776 213 HOH HOH B . 
M 6 HOH 177 777 185 HOH HOH B . 
M 6 HOH 178 778 451 HOH HOH B . 
M 6 HOH 179 779 301 HOH HOH B . 
M 6 HOH 180 780 18  HOH HOH B . 
M 6 HOH 181 781 66  HOH HOH B . 
M 6 HOH 182 782 220 HOH HOH B . 
M 6 HOH 183 783 209 HOH HOH B . 
M 6 HOH 184 784 130 HOH HOH B . 
M 6 HOH 185 785 205 HOH HOH B . 
M 6 HOH 186 786 313 HOH HOH B . 
M 6 HOH 187 787 153 HOH HOH B . 
M 6 HOH 188 788 315 HOH HOH B . 
M 6 HOH 189 789 274 HOH HOH B . 
M 6 HOH 190 790 135 HOH HOH B . 
M 6 HOH 191 791 450 HOH HOH B . 
M 6 HOH 192 792 369 HOH HOH B . 
M 6 HOH 193 793 258 HOH HOH B . 
M 6 HOH 194 794 284 HOH HOH B . 
M 6 HOH 195 795 377 HOH HOH B . 
M 6 HOH 196 796 257 HOH HOH B . 
M 6 HOH 197 797 391 HOH HOH B . 
M 6 HOH 198 798 390 HOH HOH B . 
M 6 HOH 199 799 98  HOH HOH B . 
M 6 HOH 200 800 112 HOH HOH B . 
M 6 HOH 201 801 489 HOH HOH B . 
M 6 HOH 202 802 172 HOH HOH B . 
M 6 HOH 203 803 246 HOH HOH B . 
M 6 HOH 204 804 385 HOH HOH B . 
M 6 HOH 205 805 347 HOH HOH B . 
M 6 HOH 206 806 169 HOH HOH B . 
M 6 HOH 207 807 127 HOH HOH B . 
M 6 HOH 208 808 241 HOH HOH B . 
M 6 HOH 209 809 237 HOH HOH B . 
M 6 HOH 210 810 499 HOH HOH B . 
M 6 HOH 211 811 96  HOH HOH B . 
M 6 HOH 212 812 179 HOH HOH B . 
M 6 HOH 213 813 87  HOH HOH B . 
M 6 HOH 214 814 147 HOH HOH B . 
M 6 HOH 215 815 318 HOH HOH B . 
M 6 HOH 216 816 116 HOH HOH B . 
M 6 HOH 217 817 225 HOH HOH B . 
M 6 HOH 218 818 214 HOH HOH B . 
M 6 HOH 219 819 488 HOH HOH B . 
M 6 HOH 220 820 163 HOH HOH B . 
M 6 HOH 221 821 303 HOH HOH B . 
M 6 HOH 222 822 378 HOH HOH B . 
M 6 HOH 223 823 399 HOH HOH B . 
M 6 HOH 224 824 453 HOH HOH B . 
M 6 HOH 225 825 412 HOH HOH B . 
M 6 HOH 226 826 182 HOH HOH B . 
M 6 HOH 227 827 86  HOH HOH B . 
M 6 HOH 228 828 231 HOH HOH B . 
M 6 HOH 229 829 372 HOH HOH B . 
M 6 HOH 230 830 360 HOH HOH B . 
M 6 HOH 231 831 93  HOH HOH B . 
M 6 HOH 232 832 281 HOH HOH B . 
M 6 HOH 233 833 85  HOH HOH B . 
M 6 HOH 234 834 298 HOH HOH B . 
M 6 HOH 235 835 363 HOH HOH B . 
M 6 HOH 236 836 415 HOH HOH B . 
M 6 HOH 237 837 425 HOH HOH B . 
M 6 HOH 238 838 145 HOH HOH B . 
M 6 HOH 239 839 111 HOH HOH B . 
M 6 HOH 240 840 254 HOH HOH B . 
M 6 HOH 241 841 480 HOH HOH B . 
M 6 HOH 242 842 350 HOH HOH B . 
M 6 HOH 243 843 376 HOH HOH B . 
M 6 HOH 244 844 113 HOH HOH B . 
M 6 HOH 245 845 486 HOH HOH B . 
M 6 HOH 246 846 479 HOH HOH B . 
M 6 HOH 247 847 162 HOH HOH B . 
M 6 HOH 248 848 328 HOH HOH B . 
M 6 HOH 249 849 238 HOH HOH B . 
M 6 HOH 250 850 146 HOH HOH B . 
M 6 HOH 251 851 61  HOH HOH B . 
M 6 HOH 252 852 140 HOH HOH B . 
M 6 HOH 253 853 308 HOH HOH B . 
M 6 HOH 254 854 498 HOH HOH B . 
M 6 HOH 255 855 265 HOH HOH B . 
M 6 HOH 256 856 374 HOH HOH B . 
M 6 HOH 257 857 283 HOH HOH B . 
M 6 HOH 258 858 349 HOH HOH B . 
M 6 HOH 259 859 381 HOH HOH B . 
M 6 HOH 260 860 141 HOH HOH B . 
M 6 HOH 261 861 142 HOH HOH B . 
M 6 HOH 262 862 201 HOH HOH B . 
M 6 HOH 263 863 280 HOH HOH B . 
M 6 HOH 264 864 261 HOH HOH B . 
M 6 HOH 265 865 348 HOH HOH B . 
M 6 HOH 266 866 256 HOH HOH B . 
M 6 HOH 267 867 461 HOH HOH B . 
M 6 HOH 268 868 493 HOH HOH B . 
M 6 HOH 269 869 277 HOH HOH B . 
M 6 HOH 270 870 414 HOH HOH B . 
M 6 HOH 271 871 279 HOH HOH B . 
M 6 HOH 272 872 106 HOH HOH B . 
M 6 HOH 273 873 139 HOH HOH B . 
M 6 HOH 274 874 278 HOH HOH B . 
M 6 HOH 275 875 351 HOH HOH B . 
M 6 HOH 276 876 490 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YAZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.900 
_cell.length_a_esd                 ? 
_cell.length_b                     128.440 
_cell.length_b_esd                 ? 
_cell.length_c                     149.050 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YAZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8YAZ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.55 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.4 
_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    
'50 mM Tris-HCl buffer, 120 mM MgCl2, 16-18% PEG 8000, 200 uM N-Enanthyl-L-Prolyl-L-Phenylalanine, 1%(v/v) styrene' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300-HS' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9539 
_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                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SACLA BEAMLINE BL2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9539 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL2 
_diffrn_source.pdbx_synchrotron_site       SACLA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YAZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               10 
_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                                     96618 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                92.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.53 
_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                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.972 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.85 
_reflns_shell.d_res_low                                     1.87 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.95 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4723 
_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                               34.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.608 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YAZ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             9.98 
_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                     96521 
_refine.ls_number_reflns_R_free                  4809 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1876 
_refine.ls_R_factor_R_free                       0.2199 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1859 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 22.69 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        9.98 
_refine_hist.number_atoms_solvent             500 
_refine_hist.number_atoms_total               8000 
_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        7328 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         172 
_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 ? 7710  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.066 ? 10446 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.983 ? 1055  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.057 ? 1109  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 1368  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.85 1.87 . . 161 2970 100.00 . . . . 0.3036 . . . . . . . . . . . 0.3577 
'X-RAY DIFFRACTION' 1.87 1.89 . . 182 3027 100.00 . . . . 0.2931 . . . . . . . . . . . 0.3290 
'X-RAY DIFFRACTION' 1.89 1.92 . . 172 3003 100.00 . . . . 0.2876 . . . . . . . . . . . 0.3624 
'X-RAY DIFFRACTION' 1.92 1.94 . . 151 3008 100.00 . . . . 0.2823 . . . . . . . . . . . 0.3258 
'X-RAY DIFFRACTION' 1.94 1.97 . . 153 3054 100.00 . . . . 0.2613 . . . . . . . . . . . 0.3264 
'X-RAY DIFFRACTION' 1.97 1.99 . . 146 3018 100.00 . . . . 0.2562 . . . . . . . . . . . 0.2970 
'X-RAY DIFFRACTION' 1.99 2.02 . . 159 3050 100.00 . . . . 0.2266 . . . . . . . . . . . 0.2964 
'X-RAY DIFFRACTION' 2.02 2.05 . . 163 3034 100.00 . . . . 0.2275 . . . . . . . . . . . 0.2782 
'X-RAY DIFFRACTION' 2.05 2.08 . . 169 2988 100.00 . . . . 0.2208 . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 2.08 2.12 . . 181 3026 100.00 . . . . 0.2079 . . . . . . . . . . . 0.2527 
'X-RAY DIFFRACTION' 2.12 2.15 . . 148 3013 100.00 . . . . 0.1946 . . . . . . . . . . . 0.2446 
'X-RAY DIFFRACTION' 2.15 2.19 . . 185 3030 100.00 . . . . 0.1949 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 2.19 2.23 . . 158 3020 100.00 . . . . 0.1847 . . . . . . . . . . . 0.2404 
'X-RAY DIFFRACTION' 2.23 2.28 . . 152 3055 100.00 . . . . 0.1897 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 2.28 2.33 . . 133 3050 100.00 . . . . 0.1821 . . . . . . . . . . . 0.1904 
'X-RAY DIFFRACTION' 2.33 2.38 . . 144 3055 100.00 . . . . 0.1853 . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 2.38 2.44 . . 162 3068 100.00 . . . . 0.1871 . . . . . . . . . . . 0.2320 
'X-RAY DIFFRACTION' 2.44 2.50 . . 181 3005 100.00 . . . . 0.1870 . . . . . . . . . . . 0.2398 
'X-RAY DIFFRACTION' 2.50 2.58 . . 149 3091 100.00 . . . . 0.1882 . . . . . . . . . . . 0.2282 
'X-RAY DIFFRACTION' 2.58 2.66 . . 150 3057 100.00 . . . . 0.1913 . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 2.66 2.75 . . 156 3045 100.00 . . . . 0.1912 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 2.75 2.86 . . 179 3055 100.00 . . . . 0.1910 . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 2.86 2.98 . . 145 3090 100.00 . . . . 0.2011 . . . . . . . . . . . 0.2438 
'X-RAY DIFFRACTION' 2.98 3.14 . . 166 3069 100.00 . . . . 0.1935 . . . . . . . . . . . 0.2388 
'X-RAY DIFFRACTION' 3.14 3.33 . . 158 3082 100.00 . . . . 0.1927 . . . . . . . . . . . 0.2248 
'X-RAY DIFFRACTION' 3.33 3.57 . . 158 3098 100.00 . . . . 0.1808 . . . . . . . . . . . 0.1949 
'X-RAY DIFFRACTION' 3.57 3.91 . . 153 3120 100.00 . . . . 0.1721 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 3.91 4.43 . . 144 3140 100.00 . . . . 0.1544 . . . . . . . . . . . 0.1657 
'X-RAY DIFFRACTION' 4.43 5.43 . . 176 3146 100.00 . . . . 0.1538 . . . . . . . . . . . 0.1821 
'X-RAY DIFFRACTION' 5.43 9.98 . . 175 3245 100.00 . . . . 0.1735 . . . . . . . . . . . 0.2019 
# 
_struct.entry_id                     8YAZ 
_struct.title                        
'XFEL crystal structure of the oxidized form of F87A/F393H P450BM3 with N-enanthyl-L-prolyl-L-phenylalanine in complex with styrene' 
_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        8YAZ 
_struct_keywords.text            'Cytochrome P450, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CPXB_PRIM2 
_struct_ref.pdbx_db_accession          P14779 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_struct_ref.pdbx_align_begin           0 
# 
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 8YAZ A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 8YAZ B 1 ? 455 ? P14779 2 ? 456 ? 1 455 
# 
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 8YAZ ALA A 87  ? UNP P14779 PHE 88  'engineered mutation' 87  1 
1 8YAZ HIS A 393 ? UNP P14779 PHE 394 'engineered mutation' 393 2 
2 8YAZ ALA B 87  ? UNP P14779 PHE 88  'engineered mutation' 87  3 
2 8YAZ HIS B 393 ? UNP P14779 PHE 394 'engineered mutation' 393 4 
# 
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)' 1310  ? 
1 MORE         -22   ? 
1 'SSA (A^2)'  18950 ? 
2 'ABSA (A^2)' 1320  ? 
2 MORE         -22   ? 
2 'SSA (A^2)'  19110 ? 
# 
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   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 11  ? LYS A 15  ? PHE A 11  LYS A 15  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 16  ? ASN A 21  ? ASN A 16  ASN A 21  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 24  ? GLY A 37  ? LYS A 24  GLY A 37  1 ? 14 
HELX_P HELX_P4  AA4 SER A 54  ? CYS A 62  ? SER A 54  CYS A 62  1 ? 9  
HELX_P HELX_P5  AA5 SER A 72  ? GLY A 83  ? SER A 72  GLY A 83  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 93  ? LEU A 104 ? GLU A 93  LEU A 104 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 105 ? PHE A 107 ? PRO A 105 PHE A 107 5 ? 3  
HELX_P HELX_P8  AA8 SER A 108 ? ARG A 132 ? SER A 108 ARG A 132 1 ? 25 
HELX_P HELX_P9  AA9 VAL A 141 ? ASN A 159 ? VAL A 141 ASN A 159 1 ? 19 
HELX_P HELX_P10 AB1 ASN A 163 ? ARG A 167 ? ASN A 163 ARG A 167 5 ? 5  
HELX_P HELX_P11 AB2 HIS A 171 ? LEU A 188 ? HIS A 171 LEU A 188 1 ? 18 
HELX_P HELX_P12 AB3 ASP A 195 ? ALA A 197 ? ASP A 195 ALA A 197 5 ? 3  
HELX_P HELX_P13 AB4 TYR A 198 ? ALA A 225 ? TYR A 198 ALA A 225 1 ? 28 
HELX_P HELX_P14 AB5 ASP A 232 ? GLY A 240 ? ASP A 232 GLY A 240 1 ? 9  
HELX_P HELX_P15 AB6 ASP A 250 ? THR A 268 ? ASP A 250 THR A 268 1 ? 19 
HELX_P HELX_P16 AB7 THR A 268 ? LYS A 282 ? THR A 268 LYS A 282 1 ? 15 
HELX_P HELX_P17 AB8 ASN A 283 ? LEU A 298 ? ASN A 283 LEU A 298 1 ? 16 
HELX_P HELX_P18 AB9 SER A 304 ? GLN A 310 ? SER A 304 GLN A 310 1 ? 7  
HELX_P HELX_P19 AC1 LEU A 311 ? TRP A 325 ? LEU A 311 TRP A 325 1 ? 15 
HELX_P HELX_P20 AC2 ILE A 357 ? HIS A 361 ? ILE A 357 HIS A 361 1 ? 5  
HELX_P HELX_P21 AC3 ASP A 363 ? GLY A 368 ? ASP A 363 GLY A 368 1 ? 6  
HELX_P HELX_P22 AC4 ARG A 375 ? GLU A 380 ? ARG A 375 GLU A 380 5 ? 6  
HELX_P HELX_P23 AC5 ASN A 381 ? ILE A 385 ? ASN A 381 ILE A 385 5 ? 5  
HELX_P HELX_P24 AC6 ASN A 395 ? ALA A 399 ? ASN A 395 ALA A 399 5 ? 5  
HELX_P HELX_P25 AC7 GLY A 402 ? HIS A 420 ? GLY A 402 HIS A 420 1 ? 19 
HELX_P HELX_P26 AC8 PHE B 11  ? LYS B 15  ? PHE B 11  LYS B 15  5 ? 5  
HELX_P HELX_P27 AC9 ASN B 16  ? ASN B 21  ? ASN B 16  ASN B 21  5 ? 6  
HELX_P HELX_P28 AD1 LYS B 24  ? GLY B 37  ? LYS B 24  GLY B 37  1 ? 14 
HELX_P HELX_P29 AD2 SER B 54  ? CYS B 62  ? SER B 54  CYS B 62  1 ? 9  
HELX_P HELX_P30 AD3 SER B 72  ? GLY B 83  ? SER B 72  GLY B 83  1 ? 12 
HELX_P HELX_P31 AD4 GLU B 93  ? LEU B 104 ? GLU B 93  LEU B 104 1 ? 12 
HELX_P HELX_P32 AD5 PRO B 105 ? SER B 108 ? PRO B 105 SER B 108 5 ? 4  
HELX_P HELX_P33 AD6 GLN B 109 ? GLN B 110 ? GLN B 109 GLN B 110 5 ? 2  
HELX_P HELX_P34 AD7 ALA B 111 ? ARG B 132 ? ALA B 111 ARG B 132 1 ? 22 
HELX_P HELX_P35 AD8 VAL B 141 ? ASN B 159 ? VAL B 141 ASN B 159 1 ? 19 
HELX_P HELX_P36 AD9 ASN B 163 ? ARG B 167 ? ASN B 163 ARG B 167 5 ? 5  
HELX_P HELX_P37 AE1 HIS B 171 ? LEU B 188 ? HIS B 171 LEU B 188 1 ? 18 
HELX_P HELX_P38 AE2 ASP B 195 ? ALA B 197 ? ASP B 195 ALA B 197 5 ? 3  
HELX_P HELX_P39 AE3 TYR B 198 ? SER B 226 ? TYR B 198 SER B 226 1 ? 29 
HELX_P HELX_P40 AE4 ASP B 232 ? GLY B 240 ? ASP B 232 GLY B 240 1 ? 9  
HELX_P HELX_P41 AE5 ASP B 250 ? ASN B 283 ? ASP B 250 ASN B 283 1 ? 34 
HELX_P HELX_P42 AE6 ASN B 283 ? LEU B 298 ? ASN B 283 LEU B 298 1 ? 16 
HELX_P HELX_P43 AE7 SER B 304 ? GLN B 310 ? SER B 304 GLN B 310 1 ? 7  
HELX_P HELX_P44 AE8 LEU B 311 ? TRP B 325 ? LEU B 311 TRP B 325 1 ? 15 
HELX_P HELX_P45 AE9 GLY B 342 ? GLU B 344 ? GLY B 342 GLU B 344 5 ? 3  
HELX_P HELX_P46 AF1 ILE B 357 ? HIS B 361 ? ILE B 357 HIS B 361 1 ? 5  
HELX_P HELX_P47 AF2 ASP B 363 ? GLY B 368 ? ASP B 363 GLY B 368 1 ? 6  
HELX_P HELX_P48 AF3 ARG B 375 ? GLU B 380 ? ARG B 375 GLU B 380 5 ? 6  
HELX_P HELX_P49 AF4 ASN B 381 ? ILE B 385 ? ASN B 381 ILE B 385 5 ? 5  
HELX_P HELX_P50 AF5 ASN B 395 ? ALA B 399 ? ASN B 395 ALA B 399 5 ? 5  
HELX_P HELX_P51 AF6 GLY B 402 ? HIS B 420 ? GLY B 402 HIS B 420 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 400 SG ? ? ? 1_555 C HEM . FE ? ? A CYS 400 A HEM 501 1_555 ? ? ? ? ? ? ? 2.218 ? ? 
metalc2 metalc ? ? B CYS 400 SG ? ? ? 1_555 H HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.237 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA ? C HEM . ? A HEM 501 ? 1_555 101.0 ? 
2  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 88.1  ? 
3  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 89.4  ? 
4  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 85.7  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 172.4 ? 
6  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 87.3  ? 
7  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 99.1  ? 
8  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 90.7  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 172.7 ? 
10 NC ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 91.7  ? 
11 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NA ? H HEM . ? B HEM 501 ? 1_555 99.7  ? 
12 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 88.0  ? 
13 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 88.9  ? 
14 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 84.2  ? 
15 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 175.2 ? 
16 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 88.3  ? 
17 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 96.5  ? 
18 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 91.6  ? 
19 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 175.4 ? 
20 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 90.8  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 39  ? ALA A 44  ? ILE A 39  ALA A 44  
AA1 2 ARG A 47  ? LEU A 52  ? ARG A 47  LEU A 52  
AA1 3 GLU A 352 ? LEU A 356 ? GLU A 352 LEU A 356 
AA1 4 ALA A 330 ? ALA A 335 ? ALA A 330 ALA A 335 
AA1 5 PHE A 67  ? ASN A 70  ? PHE A 67  ASN A 70  
AA2 1 ILE A 139 ? GLU A 140 ? ILE A 139 GLU A 140 
AA2 2 VAL A 445 ? SER A 450 ? VAL A 445 SER A 450 
AA2 3 PHE A 421 ? GLU A 424 ? PHE A 421 GLU A 424 
AA3 1 THR A 339 ? LEU A 341 ? THR A 339 LEU A 341 
AA3 2 TYR A 345 ? LEU A 347 ? TYR A 345 LEU A 347 
AA4 1 ILE A 433 ? GLU A 435 ? ILE A 433 GLU A 435 
AA4 2 LEU A 439 ? PRO A 441 ? LEU A 439 PRO A 441 
AA5 1 ILE B 39  ? ALA B 44  ? ILE B 39  ALA B 44  
AA5 2 ARG B 47  ? LEU B 52  ? ARG B 47  LEU B 52  
AA5 3 GLU B 352 ? LEU B 356 ? GLU B 352 LEU B 356 
AA5 4 ALA B 330 ? ALA B 335 ? ALA B 330 ALA B 335 
AA5 5 PHE B 67  ? ASN B 70  ? PHE B 67  ASN B 70  
AA6 1 ILE B 139 ? GLU B 140 ? ILE B 139 GLU B 140 
AA6 2 VAL B 445 ? SER B 450 ? VAL B 445 SER B 450 
AA6 3 PHE B 421 ? GLU B 424 ? PHE B 421 GLU B 424 
AA7 1 THR B 339 ? LEU B 341 ? THR B 339 LEU B 341 
AA7 2 TYR B 345 ? LEU B 347 ? TYR B 345 LEU B 347 
AA8 1 ILE B 433 ? GLU B 435 ? ILE B 433 GLU B 435 
AA8 2 LEU B 439 ? PRO B 441 ? LEU B 439 PRO B 441 
# 
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 PHE A 40  ? N PHE A 40  O TYR A 51  ? O TYR A 51  
AA1 2 3 N LEU A 52  ? N LEU A 52  O MET A 354 ? O MET A 354 
AA1 3 4 O VAL A 355 ? O VAL A 355 N PHE A 331 ? N PHE A 331 
AA1 4 5 O SER A 332 ? O SER A 332 N ASN A 70  ? N ASN A 70  
AA2 1 2 N ILE A 139 ? N ILE A 139 O VAL A 446 ? O VAL A 446 
AA2 2 3 O LYS A 449 ? O LYS A 449 N ASP A 422 ? N ASP A 422 
AA3 1 2 N THR A 339 ? N THR A 339 O LEU A 347 ? O LEU A 347 
AA4 1 2 N LYS A 434 ? N LYS A 434 O LYS A 440 ? O LYS A 440 
AA5 1 2 N PHE B 42  ? N PHE B 42  O THR B 49  ? O THR B 49  
AA5 2 3 N ARG B 50  ? N ARG B 50  O MET B 354 ? O MET B 354 
AA5 3 4 O VAL B 355 ? O VAL B 355 N PHE B 331 ? N PHE B 331 
AA5 4 5 O SER B 332 ? O SER B 332 N ASN B 70  ? N ASN B 70  
AA6 1 2 N ILE B 139 ? N ILE B 139 O VAL B 446 ? O VAL B 446 
AA6 2 3 O LYS B 449 ? O LYS B 449 N ASP B 422 ? N ASP B 422 
AA7 1 2 N THR B 339 ? N THR B 339 O LEU B 347 ? O LEU B 347 
AA8 1 2 N LYS B 434 ? N LYS B 434 O LYS B 440 ? O LYS B 440 
# 
_pdbx_entry_details.entry_id                   8YAZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NH1 A ARG 47  ? ? O1 A D0L 502 ? ? 1.32 
2 1 OE2 A GLU 337 ? ? O  A HOH 601 ? ? 1.96 
# 
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 47  ? ? CZ A ARG 47  ? ? NH1 A ARG 47  ? ? 123.36 120.30 3.06  0.50 N 
2 1 CA A PRO 170 ? ? N  A PRO 170 ? ? CD  A PRO 170 ? ? 102.57 111.70 -9.13 1.40 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 LYS A 15  ? ? 61.11   -128.86 
2  1 ASP A 84  ? ? -98.16  40.15   
3  1 PHE A 158 ? ? -142.02 11.61   
4  1 PRO A 170 ? ? -38.11  146.96  
5  1 PRO A 193 ? ? -65.21  3.63    
6  1 GLU A 244 ? ? -63.61  -73.38  
7  1 THR A 268 ? ? -95.11  -61.37  
8  1 ASP A 370 ? ? -87.52  32.78   
9  1 CYS A 400 ? ? -59.25  109.65  
10 1 THR A 436 ? ? -115.56 -124.52 
11 1 LYS B 15  ? ? 56.44   -128.95 
12 1 ASP B 84  ? ? -99.14  38.77   
13 1 ASN B 192 ? ? 65.60   73.73   
14 1 ASP B 231 ? ? -81.21  44.17   
15 1 GLU B 344 ? ? -141.83 -30.22  
16 1 ASP B 370 ? ? -95.10  33.83   
17 1 THR B 436 ? ? -123.87 -121.93 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 ASP A 136 ? ? GLU A 137 ? ? 147.98 
2 1 ASP B 136 ? ? GLU B 137 ? ? 145.86 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
D0L C1   C  Y N 88  
D0L C2   C  Y N 89  
D0L C15  C  N N 90  
D0L C14  C  N N 91  
D0L C7   C  N N 92  
D0L C12  C  N N 93  
D0L C10  C  N N 94  
D0L C3   C  Y N 95  
D0L C13  C  N N 96  
D0L C11  C  N S 97  
D0L C6   C  Y N 98  
D0L C8   C  N S 99  
D0L C5   C  Y N 100 
D0L C9   C  N N 101 
D0L C4   C  Y N 102 
D0L O2   O  N N 103 
D0L O3   O  N N 104 
D0L O1   O  N N 105 
D0L N2   N  N N 106 
D0L C16  C  N N 107 
D0L C17  C  N N 108 
D0L C18  C  N N 109 
D0L C19  C  N N 110 
D0L C20  C  N N 111 
D0L C21  C  N N 112 
D0L N1   N  N N 113 
D0L H1   H  N N 114 
D0L H2   H  N N 115 
D0L H3   H  N N 116 
D0L H4   H  N N 117 
D0L H5   H  N N 118 
D0L H6   H  N N 119 
D0L H7   H  N N 120 
D0L H8   H  N N 121 
D0L H9   H  N N 122 
D0L H10  H  N N 123 
D0L H11  H  N N 124 
D0L H12  H  N N 125 
D0L H13  H  N N 126 
D0L H14  H  N N 127 
D0L H15  H  N N 128 
D0L H16  H  N N 129 
D0L H17  H  N N 130 
D0L H18  H  N N 131 
D0L H20  H  N N 132 
D0L H21  H  N N 133 
D0L H22  H  N N 134 
D0L H23  H  N N 135 
D0L H24  H  N N 136 
D0L H25  H  N N 137 
D0L H26  H  N N 138 
D0L H27  H  N N 139 
D0L H28  H  N N 140 
D0L H29  H  N N 141 
D0L H30  H  N N 142 
D0L H31  H  N N 143 
D0L H32  H  N N 144 
D0L H33  H  N N 145 
GLN N    N  N N 146 
GLN CA   C  N S 147 
GLN C    C  N N 148 
GLN O    O  N N 149 
GLN CB   C  N N 150 
GLN CG   C  N N 151 
GLN CD   C  N N 152 
GLN OE1  O  N N 153 
GLN NE2  N  N N 154 
GLN OXT  O  N N 155 
GLN H    H  N N 156 
GLN H2   H  N N 157 
GLN HA   H  N N 158 
GLN HB2  H  N N 159 
GLN HB3  H  N N 160 
GLN HG2  H  N N 161 
GLN HG3  H  N N 162 
GLN HE21 H  N N 163 
GLN HE22 H  N N 164 
GLN HXT  H  N N 165 
GLU N    N  N N 166 
GLU CA   C  N S 167 
GLU C    C  N N 168 
GLU O    O  N N 169 
GLU CB   C  N N 170 
GLU CG   C  N N 171 
GLU CD   C  N N 172 
GLU OE1  O  N N 173 
GLU OE2  O  N N 174 
GLU OXT  O  N N 175 
GLU H    H  N N 176 
GLU H2   H  N N 177 
GLU HA   H  N N 178 
GLU HB2  H  N N 179 
GLU HB3  H  N N 180 
GLU HG2  H  N N 181 
GLU HG3  H  N N 182 
GLU HE2  H  N N 183 
GLU HXT  H  N N 184 
GLY N    N  N N 185 
GLY CA   C  N N 186 
GLY C    C  N N 187 
GLY O    O  N N 188 
GLY OXT  O  N N 189 
GLY H    H  N N 190 
GLY H2   H  N N 191 
GLY HA2  H  N N 192 
GLY HA3  H  N N 193 
GLY HXT  H  N N 194 
GOL C1   C  N N 195 
GOL O1   O  N N 196 
GOL C2   C  N N 197 
GOL O2   O  N N 198 
GOL C3   C  N N 199 
GOL O3   O  N N 200 
GOL H11  H  N N 201 
GOL H12  H  N N 202 
GOL HO1  H  N N 203 
GOL H2   H  N N 204 
GOL HO2  H  N N 205 
GOL H31  H  N N 206 
GOL H32  H  N N 207 
GOL HO3  H  N N 208 
HEM CHA  C  N N 209 
HEM CHB  C  N N 210 
HEM CHC  C  N N 211 
HEM CHD  C  N N 212 
HEM C1A  C  Y N 213 
HEM C2A  C  Y N 214 
HEM C3A  C  Y N 215 
HEM C4A  C  Y N 216 
HEM CMA  C  N N 217 
HEM CAA  C  N N 218 
HEM CBA  C  N N 219 
HEM CGA  C  N N 220 
HEM O1A  O  N N 221 
HEM O2A  O  N N 222 
HEM C1B  C  N N 223 
HEM C2B  C  N N 224 
HEM C3B  C  N N 225 
HEM C4B  C  N N 226 
HEM CMB  C  N N 227 
HEM CAB  C  N N 228 
HEM CBB  C  N N 229 
HEM C1C  C  Y N 230 
HEM C2C  C  Y N 231 
HEM C3C  C  Y N 232 
HEM C4C  C  Y N 233 
HEM CMC  C  N N 234 
HEM CAC  C  N N 235 
HEM CBC  C  N N 236 
HEM C1D  C  N N 237 
HEM C2D  C  N N 238 
HEM C3D  C  N N 239 
HEM C4D  C  N N 240 
HEM CMD  C  N N 241 
HEM CAD  C  N N 242 
HEM CBD  C  N N 243 
HEM CGD  C  N N 244 
HEM O1D  O  N N 245 
HEM O2D  O  N N 246 
HEM NA   N  Y N 247 
HEM NB   N  N N 248 
HEM NC   N  Y N 249 
HEM ND   N  N N 250 
HEM FE   FE N N 251 
HEM HHB  H  N N 252 
HEM HHC  H  N N 253 
HEM HHD  H  N N 254 
HEM HMA  H  N N 255 
HEM HMAA H  N N 256 
HEM HMAB H  N N 257 
HEM HAA  H  N N 258 
HEM HAAA H  N N 259 
HEM HBA  H  N N 260 
HEM HBAA H  N N 261 
HEM HMB  H  N N 262 
HEM HMBA H  N N 263 
HEM HMBB H  N N 264 
HEM HAB  H  N N 265 
HEM HBB  H  N N 266 
HEM HBBA H  N N 267 
HEM HMC  H  N N 268 
HEM HMCA H  N N 269 
HEM HMCB H  N N 270 
HEM HAC  H  N N 271 
HEM HBC  H  N N 272 
HEM HBCA H  N N 273 
HEM HMD  H  N N 274 
HEM HMDA H  N N 275 
HEM HMDB H  N N 276 
HEM HAD  H  N N 277 
HEM HADA H  N N 278 
HEM HBD  H  N N 279 
HEM HBDA H  N N 280 
HEM H2A  H  N N 281 
HEM H2D  H  N N 282 
HEM HHA  H  N N 283 
HIS N    N  N N 284 
HIS CA   C  N S 285 
HIS C    C  N N 286 
HIS O    O  N N 287 
HIS CB   C  N N 288 
HIS CG   C  Y N 289 
HIS ND1  N  Y N 290 
HIS CD2  C  Y N 291 
HIS CE1  C  Y N 292 
HIS NE2  N  Y N 293 
HIS OXT  O  N N 294 
HIS H    H  N N 295 
HIS H2   H  N N 296 
HIS HA   H  N N 297 
HIS HB2  H  N N 298 
HIS HB3  H  N N 299 
HIS HD1  H  N N 300 
HIS HD2  H  N N 301 
HIS HE1  H  N N 302 
HIS HE2  H  N N 303 
HIS HXT  H  N N 304 
HOH O    O  N N 305 
HOH H1   H  N N 306 
HOH H2   H  N N 307 
ILE N    N  N N 308 
ILE CA   C  N S 309 
ILE C    C  N N 310 
ILE O    O  N N 311 
ILE CB   C  N S 312 
ILE CG1  C  N N 313 
ILE CG2  C  N N 314 
ILE CD1  C  N N 315 
ILE OXT  O  N N 316 
ILE H    H  N N 317 
ILE H2   H  N N 318 
ILE HA   H  N N 319 
ILE HB   H  N N 320 
ILE HG12 H  N N 321 
ILE HG13 H  N N 322 
ILE HG21 H  N N 323 
ILE HG22 H  N N 324 
ILE HG23 H  N N 325 
ILE HD11 H  N N 326 
ILE HD12 H  N N 327 
ILE HD13 H  N N 328 
ILE HXT  H  N N 329 
LEU N    N  N N 330 
LEU CA   C  N S 331 
LEU C    C  N N 332 
LEU O    O  N N 333 
LEU CB   C  N N 334 
LEU CG   C  N N 335 
LEU CD1  C  N N 336 
LEU CD2  C  N N 337 
LEU OXT  O  N N 338 
LEU H    H  N N 339 
LEU H2   H  N N 340 
LEU HA   H  N N 341 
LEU HB2  H  N N 342 
LEU HB3  H  N N 343 
LEU HG   H  N N 344 
LEU HD11 H  N N 345 
LEU HD12 H  N N 346 
LEU HD13 H  N N 347 
LEU HD21 H  N N 348 
LEU HD22 H  N N 349 
LEU HD23 H  N N 350 
LEU HXT  H  N N 351 
LYS N    N  N N 352 
LYS CA   C  N S 353 
LYS C    C  N N 354 
LYS O    O  N N 355 
LYS CB   C  N N 356 
LYS CG   C  N N 357 
LYS CD   C  N N 358 
LYS CE   C  N N 359 
LYS NZ   N  N N 360 
LYS OXT  O  N N 361 
LYS H    H  N N 362 
LYS H2   H  N N 363 
LYS HA   H  N N 364 
LYS HB2  H  N N 365 
LYS HB3  H  N N 366 
LYS HG2  H  N N 367 
LYS HG3  H  N N 368 
LYS HD2  H  N N 369 
LYS HD3  H  N N 370 
LYS HE2  H  N N 371 
LYS HE3  H  N N 372 
LYS HZ1  H  N N 373 
LYS HZ2  H  N N 374 
LYS HZ3  H  N N 375 
LYS HXT  H  N N 376 
MET N    N  N N 377 
MET CA   C  N S 378 
MET C    C  N N 379 
MET O    O  N N 380 
MET CB   C  N N 381 
MET CG   C  N N 382 
MET SD   S  N N 383 
MET CE   C  N N 384 
MET OXT  O  N N 385 
MET H    H  N N 386 
MET H2   H  N N 387 
MET HA   H  N N 388 
MET HB2  H  N N 389 
MET HB3  H  N N 390 
MET HG2  H  N N 391 
MET HG3  H  N N 392 
MET HE1  H  N N 393 
MET HE2  H  N N 394 
MET HE3  H  N N 395 
MET HXT  H  N N 396 
PHE N    N  N N 397 
PHE CA   C  N S 398 
PHE C    C  N N 399 
PHE O    O  N N 400 
PHE CB   C  N N 401 
PHE CG   C  Y N 402 
PHE CD1  C  Y N 403 
PHE CD2  C  Y N 404 
PHE CE1  C  Y N 405 
PHE CE2  C  Y N 406 
PHE CZ   C  Y N 407 
PHE OXT  O  N N 408 
PHE H    H  N N 409 
PHE H2   H  N N 410 
PHE HA   H  N N 411 
PHE HB2  H  N N 412 
PHE HB3  H  N N 413 
PHE HD1  H  N N 414 
PHE HD2  H  N N 415 
PHE HE1  H  N N 416 
PHE HE2  H  N N 417 
PHE HZ   H  N N 418 
PHE HXT  H  N N 419 
PRO N    N  N N 420 
PRO CA   C  N S 421 
PRO C    C  N N 422 
PRO O    O  N N 423 
PRO CB   C  N N 424 
PRO CG   C  N N 425 
PRO CD   C  N N 426 
PRO OXT  O  N N 427 
PRO H    H  N N 428 
PRO HA   H  N N 429 
PRO HB2  H  N N 430 
PRO HB3  H  N N 431 
PRO HG2  H  N N 432 
PRO HG3  H  N N 433 
PRO HD2  H  N N 434 
PRO HD3  H  N N 435 
PRO HXT  H  N N 436 
SER N    N  N N 437 
SER CA   C  N S 438 
SER C    C  N N 439 
SER O    O  N N 440 
SER CB   C  N N 441 
SER OG   O  N N 442 
SER OXT  O  N N 443 
SER H    H  N N 444 
SER H2   H  N N 445 
SER HA   H  N N 446 
SER HB2  H  N N 447 
SER HB3  H  N N 448 
SER HG   H  N N 449 
SER HXT  H  N N 450 
SYN CAF  C  Y N 451 
SYN CAD  C  Y N 452 
SYN CAC  C  Y N 453 
SYN CAE  C  Y N 454 
SYN CAG  C  Y N 455 
SYN CAH  C  Y N 456 
SYN CAB  C  N N 457 
SYN CAA  C  N N 458 
SYN H1   H  N N 459 
SYN H2   H  N N 460 
SYN H3   H  N N 461 
SYN H4   H  N N 462 
SYN H5   H  N N 463 
SYN H6   H  N N 464 
SYN H8   H  N N 465 
SYN H9   H  N N 466 
THR N    N  N N 467 
THR CA   C  N S 468 
THR C    C  N N 469 
THR O    O  N N 470 
THR CB   C  N R 471 
THR OG1  O  N N 472 
THR CG2  C  N N 473 
THR OXT  O  N N 474 
THR H    H  N N 475 
THR H2   H  N N 476 
THR HA   H  N N 477 
THR HB   H  N N 478 
THR HG1  H  N N 479 
THR HG21 H  N N 480 
THR HG22 H  N N 481 
THR HG23 H  N N 482 
THR HXT  H  N N 483 
TRP N    N  N N 484 
TRP CA   C  N S 485 
TRP C    C  N N 486 
TRP O    O  N N 487 
TRP CB   C  N N 488 
TRP CG   C  Y N 489 
TRP CD1  C  Y N 490 
TRP CD2  C  Y N 491 
TRP NE1  N  Y N 492 
TRP CE2  C  Y N 493 
TRP CE3  C  Y N 494 
TRP CZ2  C  Y N 495 
TRP CZ3  C  Y N 496 
TRP CH2  C  Y N 497 
TRP OXT  O  N N 498 
TRP H    H  N N 499 
TRP H2   H  N N 500 
TRP HA   H  N N 501 
TRP HB2  H  N N 502 
TRP HB3  H  N N 503 
TRP HD1  H  N N 504 
TRP HE1  H  N N 505 
TRP HE3  H  N N 506 
TRP HZ2  H  N N 507 
TRP HZ3  H  N N 508 
TRP HH2  H  N N 509 
TRP HXT  H  N N 510 
TYR N    N  N N 511 
TYR CA   C  N S 512 
TYR C    C  N N 513 
TYR O    O  N N 514 
TYR CB   C  N N 515 
TYR CG   C  Y N 516 
TYR CD1  C  Y N 517 
TYR CD2  C  Y N 518 
TYR CE1  C  Y N 519 
TYR CE2  C  Y N 520 
TYR CZ   C  Y N 521 
TYR OH   O  N N 522 
TYR OXT  O  N N 523 
TYR H    H  N N 524 
TYR H2   H  N N 525 
TYR HA   H  N N 526 
TYR HB2  H  N N 527 
TYR HB3  H  N N 528 
TYR HD1  H  N N 529 
TYR HD2  H  N N 530 
TYR HE1  H  N N 531 
TYR HE2  H  N N 532 
TYR HH   H  N N 533 
TYR HXT  H  N N 534 
VAL N    N  N N 535 
VAL CA   C  N S 536 
VAL C    C  N N 537 
VAL O    O  N N 538 
VAL CB   C  N N 539 
VAL CG1  C  N N 540 
VAL CG2  C  N N 541 
VAL OXT  O  N N 542 
VAL H    H  N N 543 
VAL H2   H  N N 544 
VAL HA   H  N N 545 
VAL HB   H  N N 546 
VAL HG11 H  N N 547 
VAL HG12 H  N N 548 
VAL HG13 H  N N 549 
VAL HG21 H  N N 550 
VAL HG22 H  N N 551 
VAL HG23 H  N N 552 
VAL HXT  H  N N 553 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
D0L C21 C20  sing N N 83  
D0L C20 C19  sing N N 84  
D0L C19 C18  sing N N 85  
D0L C18 C17  sing N N 86  
D0L C14 N2   sing N N 87  
D0L C14 C13  sing N N 88  
D0L C17 C16  sing N N 89  
D0L C15 N2   sing N N 90  
D0L C15 C16  sing N N 91  
D0L N2  C11  sing N N 92  
D0L C13 C12  sing N N 93  
D0L O2  C9   doub N N 94  
D0L C11 C12  sing N N 95  
D0L C11 C10  sing N N 96  
D0L C5  C4   doub Y N 97  
D0L C5  C6   sing Y N 98  
D0L C4  C3   sing Y N 99  
D0L C6  C1   doub Y N 100 
D0L N1  C10  sing N N 101 
D0L N1  C8   sing N N 102 
D0L C9  O1   sing N N 103 
D0L C9  C8   sing N N 104 
D0L C10 O3   doub N N 105 
D0L C3  C2   doub Y N 106 
D0L C1  C2   sing Y N 107 
D0L C8  C7   sing N N 108 
D0L C2  C7   sing N N 109 
D0L C1  H1   sing N N 110 
D0L C15 H2   sing N N 111 
D0L C15 H3   sing N N 112 
D0L C14 H4   sing N N 113 
D0L C14 H5   sing N N 114 
D0L C7  H6   sing N N 115 
D0L C7  H7   sing N N 116 
D0L C12 H8   sing N N 117 
D0L C12 H9   sing N N 118 
D0L C3  H10  sing N N 119 
D0L C13 H11  sing N N 120 
D0L C13 H12  sing N N 121 
D0L C11 H13  sing N N 122 
D0L C6  H14  sing N N 123 
D0L C8  H15  sing N N 124 
D0L C5  H16  sing N N 125 
D0L C4  H17  sing N N 126 
D0L O1  H18  sing N N 127 
D0L C16 H20  sing N N 128 
D0L C16 H21  sing N N 129 
D0L C17 H22  sing N N 130 
D0L C17 H23  sing N N 131 
D0L C18 H24  sing N N 132 
D0L C18 H25  sing N N 133 
D0L C19 H26  sing N N 134 
D0L C19 H27  sing N N 135 
D0L C20 H28  sing N N 136 
D0L C20 H29  sing N N 137 
D0L C21 H30  sing N N 138 
D0L C21 H31  sing N N 139 
D0L C21 H32  sing N N 140 
D0L N1  H33  sing N N 141 
GLN N   CA   sing N N 142 
GLN N   H    sing N N 143 
GLN N   H2   sing N N 144 
GLN CA  C    sing N N 145 
GLN CA  CB   sing N N 146 
GLN CA  HA   sing N N 147 
GLN C   O    doub N N 148 
GLN C   OXT  sing N N 149 
GLN CB  CG   sing N N 150 
GLN CB  HB2  sing N N 151 
GLN CB  HB3  sing N N 152 
GLN CG  CD   sing N N 153 
GLN CG  HG2  sing N N 154 
GLN CG  HG3  sing N N 155 
GLN CD  OE1  doub N N 156 
GLN CD  NE2  sing N N 157 
GLN NE2 HE21 sing N N 158 
GLN NE2 HE22 sing N N 159 
GLN OXT HXT  sing N N 160 
GLU N   CA   sing N N 161 
GLU N   H    sing N N 162 
GLU N   H2   sing N N 163 
GLU CA  C    sing N N 164 
GLU CA  CB   sing N N 165 
GLU CA  HA   sing N N 166 
GLU C   O    doub N N 167 
GLU C   OXT  sing N N 168 
GLU CB  CG   sing N N 169 
GLU CB  HB2  sing N N 170 
GLU CB  HB3  sing N N 171 
GLU CG  CD   sing N N 172 
GLU CG  HG2  sing N N 173 
GLU CG  HG3  sing N N 174 
GLU CD  OE1  doub N N 175 
GLU CD  OE2  sing N N 176 
GLU OE2 HE2  sing N N 177 
GLU OXT HXT  sing N N 178 
GLY N   CA   sing N N 179 
GLY N   H    sing N N 180 
GLY N   H2   sing N N 181 
GLY CA  C    sing N N 182 
GLY CA  HA2  sing N N 183 
GLY CA  HA3  sing N N 184 
GLY C   O    doub N N 185 
GLY C   OXT  sing N N 186 
GLY OXT HXT  sing N N 187 
GOL C1  O1   sing N N 188 
GOL C1  C2   sing N N 189 
GOL C1  H11  sing N N 190 
GOL C1  H12  sing N N 191 
GOL O1  HO1  sing N N 192 
GOL C2  O2   sing N N 193 
GOL C2  C3   sing N N 194 
GOL C2  H2   sing N N 195 
GOL O2  HO2  sing N N 196 
GOL C3  O3   sing N N 197 
GOL C3  H31  sing N N 198 
GOL C3  H32  sing N N 199 
GOL O3  HO3  sing N N 200 
HEM CHA C1A  sing N N 201 
HEM CHA C4D  doub N N 202 
HEM CHA HHA  sing N N 203 
HEM CHB C4A  sing N N 204 
HEM CHB C1B  doub N N 205 
HEM CHB HHB  sing N N 206 
HEM CHC C4B  sing N N 207 
HEM CHC C1C  doub N N 208 
HEM CHC HHC  sing N N 209 
HEM CHD C4C  doub N N 210 
HEM CHD C1D  sing N N 211 
HEM CHD HHD  sing N N 212 
HEM C1A C2A  doub Y N 213 
HEM C1A NA   sing Y N 214 
HEM C2A C3A  sing Y N 215 
HEM C2A CAA  sing N N 216 
HEM C3A C4A  doub Y N 217 
HEM C3A CMA  sing N N 218 
HEM C4A NA   sing Y N 219 
HEM CMA HMA  sing N N 220 
HEM CMA HMAA sing N N 221 
HEM CMA HMAB sing N N 222 
HEM CAA CBA  sing N N 223 
HEM CAA HAA  sing N N 224 
HEM CAA HAAA sing N N 225 
HEM CBA CGA  sing N N 226 
HEM CBA HBA  sing N N 227 
HEM CBA HBAA sing N N 228 
HEM CGA O1A  doub N N 229 
HEM CGA O2A  sing N N 230 
HEM C1B C2B  sing N N 231 
HEM C1B NB   sing N N 232 
HEM C2B C3B  doub N N 233 
HEM C2B CMB  sing N N 234 
HEM C3B C4B  sing N N 235 
HEM C3B CAB  sing N N 236 
HEM C4B NB   doub N N 237 
HEM CMB HMB  sing N N 238 
HEM CMB HMBA sing N N 239 
HEM CMB HMBB sing N N 240 
HEM CAB CBB  doub N N 241 
HEM CAB HAB  sing N N 242 
HEM CBB HBB  sing N N 243 
HEM CBB HBBA sing N N 244 
HEM C1C C2C  sing Y N 245 
HEM C1C NC   sing Y N 246 
HEM C2C C3C  doub Y N 247 
HEM C2C CMC  sing N N 248 
HEM C3C C4C  sing Y N 249 
HEM C3C CAC  sing N N 250 
HEM C4C NC   sing Y N 251 
HEM CMC HMC  sing N N 252 
HEM CMC HMCA sing N N 253 
HEM CMC HMCB sing N N 254 
HEM CAC CBC  doub N N 255 
HEM CAC HAC  sing N N 256 
HEM CBC HBC  sing N N 257 
HEM CBC HBCA sing N N 258 
HEM C1D C2D  sing N N 259 
HEM C1D ND   doub N N 260 
HEM C2D C3D  doub N N 261 
HEM C2D CMD  sing N N 262 
HEM C3D C4D  sing N N 263 
HEM C3D CAD  sing N N 264 
HEM C4D ND   sing N N 265 
HEM CMD HMD  sing N N 266 
HEM CMD HMDA sing N N 267 
HEM CMD HMDB sing N N 268 
HEM CAD CBD  sing N N 269 
HEM CAD HAD  sing N N 270 
HEM CAD HADA sing N N 271 
HEM CBD CGD  sing N N 272 
HEM CBD HBD  sing N N 273 
HEM CBD HBDA sing N N 274 
HEM CGD O1D  doub N N 275 
HEM CGD O2D  sing N N 276 
HEM O2A H2A  sing N N 277 
HEM O2D H2D  sing N N 278 
HEM FE  NA   sing N N 279 
HEM FE  NB   sing N N 280 
HEM FE  NC   sing N N 281 
HEM FE  ND   sing N N 282 
HIS N   CA   sing N N 283 
HIS N   H    sing N N 284 
HIS N   H2   sing N N 285 
HIS CA  C    sing N N 286 
HIS CA  CB   sing N N 287 
HIS CA  HA   sing N N 288 
HIS C   O    doub N N 289 
HIS C   OXT  sing N N 290 
HIS CB  CG   sing N N 291 
HIS CB  HB2  sing N N 292 
HIS CB  HB3  sing N N 293 
HIS CG  ND1  sing Y N 294 
HIS CG  CD2  doub Y N 295 
HIS ND1 CE1  doub Y N 296 
HIS ND1 HD1  sing N N 297 
HIS CD2 NE2  sing Y N 298 
HIS CD2 HD2  sing N N 299 
HIS CE1 NE2  sing Y N 300 
HIS CE1 HE1  sing N N 301 
HIS NE2 HE2  sing N N 302 
HIS OXT HXT  sing N N 303 
HOH O   H1   sing N N 304 
HOH O   H2   sing N N 305 
ILE N   CA   sing N N 306 
ILE N   H    sing N N 307 
ILE N   H2   sing N N 308 
ILE CA  C    sing N N 309 
ILE CA  CB   sing N N 310 
ILE CA  HA   sing N N 311 
ILE C   O    doub N N 312 
ILE C   OXT  sing N N 313 
ILE CB  CG1  sing N N 314 
ILE CB  CG2  sing N N 315 
ILE CB  HB   sing N N 316 
ILE CG1 CD1  sing N N 317 
ILE CG1 HG12 sing N N 318 
ILE CG1 HG13 sing N N 319 
ILE CG2 HG21 sing N N 320 
ILE CG2 HG22 sing N N 321 
ILE CG2 HG23 sing N N 322 
ILE CD1 HD11 sing N N 323 
ILE CD1 HD12 sing N N 324 
ILE CD1 HD13 sing N N 325 
ILE OXT HXT  sing N N 326 
LEU N   CA   sing N N 327 
LEU N   H    sing N N 328 
LEU N   H2   sing N N 329 
LEU CA  C    sing N N 330 
LEU CA  CB   sing N N 331 
LEU CA  HA   sing N N 332 
LEU C   O    doub N N 333 
LEU C   OXT  sing N N 334 
LEU CB  CG   sing N N 335 
LEU CB  HB2  sing N N 336 
LEU CB  HB3  sing N N 337 
LEU CG  CD1  sing N N 338 
LEU CG  CD2  sing N N 339 
LEU CG  HG   sing N N 340 
LEU CD1 HD11 sing N N 341 
LEU CD1 HD12 sing N N 342 
LEU CD1 HD13 sing N N 343 
LEU CD2 HD21 sing N N 344 
LEU CD2 HD22 sing N N 345 
LEU CD2 HD23 sing N N 346 
LEU OXT HXT  sing N N 347 
LYS N   CA   sing N N 348 
LYS N   H    sing N N 349 
LYS N   H2   sing N N 350 
LYS CA  C    sing N N 351 
LYS CA  CB   sing N N 352 
LYS CA  HA   sing N N 353 
LYS C   O    doub N N 354 
LYS C   OXT  sing N N 355 
LYS CB  CG   sing N N 356 
LYS CB  HB2  sing N N 357 
LYS CB  HB3  sing N N 358 
LYS CG  CD   sing N N 359 
LYS CG  HG2  sing N N 360 
LYS CG  HG3  sing N N 361 
LYS CD  CE   sing N N 362 
LYS CD  HD2  sing N N 363 
LYS CD  HD3  sing N N 364 
LYS CE  NZ   sing N N 365 
LYS CE  HE2  sing N N 366 
LYS CE  HE3  sing N N 367 
LYS NZ  HZ1  sing N N 368 
LYS NZ  HZ2  sing N N 369 
LYS NZ  HZ3  sing N N 370 
LYS OXT HXT  sing N N 371 
MET N   CA   sing N N 372 
MET N   H    sing N N 373 
MET N   H2   sing N N 374 
MET CA  C    sing N N 375 
MET CA  CB   sing N N 376 
MET CA  HA   sing N N 377 
MET C   O    doub N N 378 
MET C   OXT  sing N N 379 
MET CB  CG   sing N N 380 
MET CB  HB2  sing N N 381 
MET CB  HB3  sing N N 382 
MET CG  SD   sing N N 383 
MET CG  HG2  sing N N 384 
MET CG  HG3  sing N N 385 
MET SD  CE   sing N N 386 
MET CE  HE1  sing N N 387 
MET CE  HE2  sing N N 388 
MET CE  HE3  sing N N 389 
MET OXT HXT  sing N N 390 
PHE N   CA   sing N N 391 
PHE N   H    sing N N 392 
PHE N   H2   sing N N 393 
PHE CA  C    sing N N 394 
PHE CA  CB   sing N N 395 
PHE CA  HA   sing N N 396 
PHE C   O    doub N N 397 
PHE C   OXT  sing N N 398 
PHE CB  CG   sing N N 399 
PHE CB  HB2  sing N N 400 
PHE CB  HB3  sing N N 401 
PHE CG  CD1  doub Y N 402 
PHE CG  CD2  sing Y N 403 
PHE CD1 CE1  sing Y N 404 
PHE CD1 HD1  sing N N 405 
PHE CD2 CE2  doub Y N 406 
PHE CD2 HD2  sing N N 407 
PHE CE1 CZ   doub Y N 408 
PHE CE1 HE1  sing N N 409 
PHE CE2 CZ   sing Y N 410 
PHE CE2 HE2  sing N N 411 
PHE CZ  HZ   sing N N 412 
PHE OXT HXT  sing N N 413 
PRO N   CA   sing N N 414 
PRO N   CD   sing N N 415 
PRO N   H    sing N N 416 
PRO CA  C    sing N N 417 
PRO CA  CB   sing N N 418 
PRO CA  HA   sing N N 419 
PRO C   O    doub N N 420 
PRO C   OXT  sing N N 421 
PRO CB  CG   sing N N 422 
PRO CB  HB2  sing N N 423 
PRO CB  HB3  sing N N 424 
PRO CG  CD   sing N N 425 
PRO CG  HG2  sing N N 426 
PRO CG  HG3  sing N N 427 
PRO CD  HD2  sing N N 428 
PRO CD  HD3  sing N N 429 
PRO OXT HXT  sing N N 430 
SER N   CA   sing N N 431 
SER N   H    sing N N 432 
SER N   H2   sing N N 433 
SER CA  C    sing N N 434 
SER CA  CB   sing N N 435 
SER CA  HA   sing N N 436 
SER C   O    doub N N 437 
SER C   OXT  sing N N 438 
SER CB  OG   sing N N 439 
SER CB  HB2  sing N N 440 
SER CB  HB3  sing N N 441 
SER OG  HG   sing N N 442 
SER OXT HXT  sing N N 443 
SYN CAC CAE  doub Y N 444 
SYN CAC CAD  sing Y N 445 
SYN CAE CAG  sing Y N 446 
SYN CAD CAF  doub Y N 447 
SYN CAG CAH  doub Y N 448 
SYN CAF CAH  sing Y N 449 
SYN CAH CAB  sing N N 450 
SYN CAB CAA  doub N N 451 
SYN CAF H1   sing N N 452 
SYN CAD H2   sing N N 453 
SYN CAC H3   sing N N 454 
SYN CAE H4   sing N N 455 
SYN CAG H5   sing N N 456 
SYN CAB H6   sing N N 457 
SYN CAA H8   sing N N 458 
SYN CAA H9   sing N N 459 
THR N   CA   sing N N 460 
THR N   H    sing N N 461 
THR N   H2   sing N N 462 
THR CA  C    sing N N 463 
THR CA  CB   sing N N 464 
THR CA  HA   sing N N 465 
THR C   O    doub N N 466 
THR C   OXT  sing N N 467 
THR CB  OG1  sing N N 468 
THR CB  CG2  sing N N 469 
THR CB  HB   sing N N 470 
THR OG1 HG1  sing N N 471 
THR CG2 HG21 sing N N 472 
THR CG2 HG22 sing N N 473 
THR CG2 HG23 sing N N 474 
THR OXT HXT  sing N N 475 
TRP N   CA   sing N N 476 
TRP N   H    sing N N 477 
TRP N   H2   sing N N 478 
TRP CA  C    sing N N 479 
TRP CA  CB   sing N N 480 
TRP CA  HA   sing N N 481 
TRP C   O    doub N N 482 
TRP C   OXT  sing N N 483 
TRP CB  CG   sing N N 484 
TRP CB  HB2  sing N N 485 
TRP CB  HB3  sing N N 486 
TRP CG  CD1  doub Y N 487 
TRP CG  CD2  sing Y N 488 
TRP CD1 NE1  sing Y N 489 
TRP CD1 HD1  sing N N 490 
TRP CD2 CE2  doub Y N 491 
TRP CD2 CE3  sing Y N 492 
TRP NE1 CE2  sing Y N 493 
TRP NE1 HE1  sing N N 494 
TRP CE2 CZ2  sing Y N 495 
TRP CE3 CZ3  doub Y N 496 
TRP CE3 HE3  sing N N 497 
TRP CZ2 CH2  doub Y N 498 
TRP CZ2 HZ2  sing N N 499 
TRP CZ3 CH2  sing Y N 500 
TRP CZ3 HZ3  sing N N 501 
TRP CH2 HH2  sing N N 502 
TRP OXT HXT  sing N N 503 
TYR N   CA   sing N N 504 
TYR N   H    sing N N 505 
TYR N   H2   sing N N 506 
TYR CA  C    sing N N 507 
TYR CA  CB   sing N N 508 
TYR CA  HA   sing N N 509 
TYR C   O    doub N N 510 
TYR C   OXT  sing N N 511 
TYR CB  CG   sing N N 512 
TYR CB  HB2  sing N N 513 
TYR CB  HB3  sing N N 514 
TYR CG  CD1  doub Y N 515 
TYR CG  CD2  sing Y N 516 
TYR CD1 CE1  sing Y N 517 
TYR CD1 HD1  sing N N 518 
TYR CD2 CE2  doub Y N 519 
TYR CD2 HD2  sing N N 520 
TYR CE1 CZ   doub Y N 521 
TYR CE1 HE1  sing N N 522 
TYR CE2 CZ   sing Y N 523 
TYR CE2 HE2  sing N N 524 
TYR CZ  OH   sing N N 525 
TYR OH  HH   sing N N 526 
TYR OXT HXT  sing N N 527 
VAL N   CA   sing N N 528 
VAL N   H    sing N N 529 
VAL N   H2   sing N N 530 
VAL CA  C    sing N N 531 
VAL CA  CB   sing N N 532 
VAL CA  HA   sing N N 533 
VAL C   O    doub N N 534 
VAL C   OXT  sing N N 535 
VAL CB  CG1  sing N N 536 
VAL CB  CG2  sing N N 537 
VAL CB  HB   sing N N 538 
VAL CG1 HG11 sing N N 539 
VAL CG1 HG12 sing N N 540 
VAL CG1 HG13 sing N N 541 
VAL CG2 HG21 sing N N 542 
VAL CG2 HG22 sing N N 543 
VAL CG2 HG23 sing N N 544 
VAL OXT HXT  sing N N 545 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Science and Technology'                      Japan JPMJCR15P3 1 
'Japan Society for the Promotion of Science (JSPS)' Japan JP19H05784 2 
'Japan Society for the Promotion of Science (JSPS)' Japan JP18KK0397 3 
'Japan Society for the Promotion of Science (JSPS)' Japan JP19K22403 4 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6K58 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_data_reduction.diffrn_id             1 
_pdbx_serial_crystallography_data_reduction.frames_total          ? 
_pdbx_serial_crystallography_data_reduction.xfel_pulse_events     ? 
_pdbx_serial_crystallography_data_reduction.frame_hits            ? 
_pdbx_serial_crystallography_data_reduction.crystal_hits          18419 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        11660 
_pdbx_serial_crystallography_data_reduction.lattices_indexed      ? 
_pdbx_serial_crystallography_data_reduction.xfel_run_numbers      ? 
_pdbx_serial_crystallography_data_reduction.lattices_merged       ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 ? 
_pdbx_serial_crystallography_measurement.pulse_duration               10 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   30 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          13 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              19.313 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        4.1 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   Fixed-target 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_pdbx_serial_crystallography_sample_delivery_fixed_target.diffrn_id                       1 
_pdbx_serial_crystallography_sample_delivery_fixed_target.description                     
'microcrystals were mounted on mesh loop and flash-frozen by liquid nitrogen' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_holding                  'polyimide film' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.support_base                    'SPINE magnet base' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_unit_size                36 
_pdbx_serial_crystallography_sample_delivery_fixed_target.crystals_per_unit               50 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_solvent                  
'125 mM Tris-HCl (pH 8.3), 14% w/v PEG 8000, 60 mM MgCl2, saturated styrene, and 30% glycerol' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_dehydration_prevention   none 
_pdbx_serial_crystallography_sample_delivery_fixed_target.motion_control                  'stepper motors' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_horizontal             ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_vertical               ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.details                         ? 
# 
_atom_sites.entry_id                    8YAZ 
_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]   0.016978 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007786 
_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]   0.006709 
_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  
FE 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR A 1 1   ? -9.590  -24.644 -24.936 1.00 73.06  ? 1   THR A N   1 
ATOM   2    C  CA  . THR A 1 1   ? -10.453 -23.782 -24.132 1.00 74.18  ? 1   THR A CA  1 
ATOM   3    C  C   . THR A 1 1   ? -10.738 -24.395 -22.754 1.00 70.14  ? 1   THR A C   1 
ATOM   4    O  O   . THR A 1 1   ? -10.187 -23.951 -21.745 1.00 68.23  ? 1   THR A O   1 
ATOM   5    C  CB  . THR A 1 1   ? -11.789 -23.491 -24.857 1.00 76.86  ? 1   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 1   ? -12.707 -22.861 -23.950 1.00 77.59  ? 1   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 1   ? -12.405 -24.777 -25.422 1.00 77.71  ? 1   THR A CG2 1 
ATOM   8    N  N   . ILE A 1 2   ? -11.596 -25.413 -22.721 1.00 71.05  ? 2   ILE A N   1 
ATOM   9    C  CA  . ILE A 1 2   ? -11.885 -26.134 -21.485 1.00 66.64  ? 2   ILE A CA  1 
ATOM   10   C  C   . ILE A 1 2   ? -10.627 -26.865 -21.027 1.00 68.15  ? 2   ILE A C   1 
ATOM   11   O  O   . ILE A 1 2   ? -10.121 -27.759 -21.718 1.00 67.13  ? 2   ILE A O   1 
ATOM   12   C  CB  . ILE A 1 2   ? -13.054 -27.109 -21.686 1.00 70.37  ? 2   ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 2   ? -14.309 -26.350 -22.131 1.00 71.12  ? 2   ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 2   ? -13.311 -27.930 -20.419 1.00 66.60  ? 2   ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 2   ? -15.514 -27.238 -22.350 1.00 66.94  ? 2   ILE A CD1 1 
ATOM   16   N  N   . LYS A 1 3   ? -10.120 -26.490 -19.856 1.00 60.67  ? 3   LYS A N   1 
ATOM   17   C  CA  . LYS A 1 3   ? -8.948  -27.113 -19.254 1.00 60.07  ? 3   LYS A CA  1 
ATOM   18   C  C   . LYS A 1 3   ? -9.400  -28.124 -18.209 1.00 58.72  ? 3   LYS A C   1 
ATOM   19   O  O   . LYS A 1 3   ? -10.383 -27.896 -17.498 1.00 57.36  ? 3   LYS A O   1 
ATOM   20   C  CB  . LYS A 1 3   ? -8.058  -26.054 -18.600 1.00 55.40  ? 3   LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 3   ? -6.589  -26.175 -18.880 1.00 57.81  ? 3   LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 3   ? -5.956  -24.807 -18.842 1.00 59.71  ? 3   LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 3   ? -5.259  -24.568 -17.519 1.00 64.31  ? 3   LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 3   ? -4.487  -23.288 -17.536 1.00 64.10  ? 3   LYS A NZ  1 
ATOM   25   N  N   . GLU A 1 4   ? -8.687  -29.239 -18.107 1.00 59.32  ? 4   GLU A N   1 
ATOM   26   C  CA  . GLU A 1 4   ? -8.940  -30.172 -17.022 1.00 56.87  ? 4   GLU A CA  1 
ATOM   27   C  C   . GLU A 1 4   ? -8.011  -29.837 -15.865 1.00 54.57  ? 4   GLU A C   1 
ATOM   28   O  O   . GLU A 1 4   ? -6.801  -29.691 -16.043 1.00 52.51  ? 4   GLU A O   1 
ATOM   29   C  CB  . GLU A 1 4   ? -8.757  -31.620 -17.460 1.00 60.11  ? 4   GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 4   ? -8.199  -32.491 -16.368 1.00 63.64  ? 4   GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 4   ? -8.458  -33.950 -16.626 1.00 69.53  ? 4   GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 4   ? -9.644  -34.348 -16.584 1.00 75.86  ? 4   GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 4   ? -7.484  -34.696 -16.860 1.00 80.99  ? 4   GLU A OE2 1 
ATOM   34   N  N   . MET A 1 5   ? -8.581  -29.703 -14.697 1.00 55.20  ? 5   MET A N   1 
ATOM   35   C  CA  . MET A 1 5   ? -7.865  -29.182 -13.546 1.00 50.36  ? 5   MET A CA  1 
ATOM   36   C  C   . MET A 1 5   ? -7.151  -30.313 -12.813 1.00 39.91  ? 5   MET A C   1 
ATOM   37   O  O   . MET A 1 5   ? -7.629  -31.451 -12.803 1.00 41.11  ? 5   MET A O   1 
ATOM   38   C  CB  . MET A 1 5   ? -8.861  -28.409 -12.663 1.00 49.85  ? 5   MET A CB  1 
ATOM   39   C  CG  . MET A 1 5   ? -10.024 -29.211 -12.074 1.00 48.36  ? 5   MET A CG  1 
ATOM   40   S  SD  . MET A 1 5   ? -10.769 -28.488 -10.598 1.00 41.95  ? 5   MET A SD  1 
ATOM   41   C  CE  . MET A 1 5   ? -11.984 -27.488 -11.462 1.00 45.33  ? 5   MET A CE  1 
ATOM   42   N  N   . PRO A 1 6   ? -5.966  -30.048 -12.279 1.00 43.87  ? 6   PRO A N   1 
ATOM   43   C  CA  . PRO A 1 6   ? -5.230  -31.100 -11.569 1.00 38.69  ? 6   PRO A CA  1 
ATOM   44   C  C   . PRO A 1 6   ? -5.965  -31.506 -10.298 1.00 41.40  ? 6   PRO A C   1 
ATOM   45   O  O   . PRO A 1 6   ? -6.927  -30.873 -9.857  1.00 39.36  ? 6   PRO A O   1 
ATOM   46   C  CB  . PRO A 1 6   ? -3.882  -30.457 -11.256 1.00 40.06  ? 6   PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 6   ? -4.128  -28.974 -11.338 1.00 44.49  ? 6   PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 6   ? -5.224  -28.774 -12.332 1.00 41.89  ? 6   PRO A CD  1 
ATOM   49   N  N   . GLN A 1 7   ? -5.493  -32.599 -9.706  1.00 41.72  ? 7   GLN A N   1 
ATOM   50   C  CA  . GLN A 1 7   ? -6.062  -33.159 -8.488  1.00 39.16  ? 7   GLN A CA  1 
ATOM   51   C  C   . GLN A 1 7   ? -4.925  -33.809 -7.724  1.00 39.80  ? 7   GLN A C   1 
ATOM   52   O  O   . GLN A 1 7   ? -4.110  -34.510 -8.344  1.00 38.74  ? 7   GLN A O   1 
ATOM   53   C  CB  . GLN A 1 7   ? -7.149  -34.195 -8.791  1.00 38.01  ? 7   GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 7   ? -7.696  -34.877 -7.545  1.00 41.88  ? 7   GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 7   ? -8.829  -35.824 -7.875  1.00 45.77  ? 7   GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 7   ? -9.110  -36.082 -9.045  1.00 43.30  ? 7   GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 7   ? -9.488  -36.343 -6.849  1.00 47.36  ? 7   GLN A NE2 1 
ATOM   58   N  N   . PRO A 1 8   ? -4.828  -33.597 -6.387  1.00 40.43  ? 8   PRO A N   1 
ATOM   59   C  CA  . PRO A 1 8   ? -3.756  -34.244 -5.617  1.00 39.03  ? 8   PRO A CA  1 
ATOM   60   C  C   . PRO A 1 8   ? -3.970  -35.749 -5.489  1.00 38.42  ? 8   PRO A C   1 
ATOM   61   O  O   . PRO A 1 8   ? -4.974  -36.293 -5.960  1.00 36.03  ? 8   PRO A O   1 
ATOM   62   C  CB  . PRO A 1 8   ? -3.830  -33.541 -4.251  1.00 35.61  ? 8   PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 8   ? -5.287  -33.196 -4.100  1.00 32.89  ? 8   PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 8   ? -5.751  -32.840 -5.517  1.00 39.09  ? 8   PRO A CD  1 
ATOM   65   N  N   . LYS A 1 9   ? -3.032  -36.429 -4.835  1.00 38.65  ? 9   LYS A N   1 
ATOM   66   C  CA  . LYS A 1 9   ? -3.035  -37.887 -4.811  1.00 36.99  ? 9   LYS A CA  1 
ATOM   67   C  C   . LYS A 1 9   ? -4.259  -38.437 -4.085  1.00 36.70  ? 9   LYS A C   1 
ATOM   68   O  O   . LYS A 1 9   ? -4.731  -37.868 -3.091  1.00 37.50  ? 9   LYS A O   1 
ATOM   69   C  CB  . LYS A 1 9   ? -1.762  -38.406 -4.136  1.00 37.19  ? 9   LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 9   ? -1.544  -37.891 -2.727  1.00 39.25  ? 9   LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 9   ? -0.125  -38.213 -2.266  1.00 35.99  ? 9   LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 9   ? 0.195   -37.560 -0.923  1.00 42.03  ? 9   LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 9   ? 1.398   -38.138 -0.255  1.00 44.23  ? 9   LYS A NZ  1 
ATOM   74   N  N   . THR A 1 10  ? -4.748  -39.571 -4.575  1.00 36.73  ? 10  THR A N   1 
ATOM   75   C  CA  . THR A 1 10  ? -5.942  -40.229 -4.061  1.00 38.99  ? 10  THR A CA  1 
ATOM   76   C  C   . THR A 1 10  ? -5.593  -41.520 -3.330  1.00 35.48  ? 10  THR A C   1 
ATOM   77   O  O   . THR A 1 10  ? -4.486  -42.065 -3.446  1.00 36.00  ? 10  THR A O   1 
ATOM   78   C  CB  . THR A 1 10  ? -6.925  -40.538 -5.194  1.00 39.33  ? 10  THR A CB  1 
ATOM   79   O  OG1 . THR A 1 10  ? -6.312  -41.439 -6.128  1.00 38.30  ? 10  THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 10  ? -7.340  -39.252 -5.895  1.00 36.77  ? 10  THR A CG2 1 
ATOM   81   N  N   . PHE A 1 11  ? -6.593  -42.017 -2.597  1.00 36.17  ? 11  PHE A N   1 
ATOM   82   C  CA  . PHE A 1 11  ? -6.471  -43.146 -1.679  1.00 36.38  ? 11  PHE A CA  1 
ATOM   83   C  C   . PHE A 1 11  ? -7.618  -44.126 -1.930  1.00 37.79  ? 11  PHE A C   1 
ATOM   84   O  O   . PHE A 1 11  ? -8.405  -44.417 -1.033  1.00 41.22  ? 11  PHE A O   1 
ATOM   85   C  CB  . PHE A 1 11  ? -6.501  -42.666 -0.225  1.00 34.58  ? 11  PHE A CB  1 
ATOM   86   C  CG  . PHE A 1 11  ? -5.330  -41.821 0.145   1.00 34.32  ? 11  PHE A CG  1 
ATOM   87   C  CD1 . PHE A 1 11  ? -5.240  -40.508 -0.298  1.00 34.23  ? 11  PHE A CD1 1 
ATOM   88   C  CD2 . PHE A 1 11  ? -4.307  -42.331 0.911   1.00 34.86  ? 11  PHE A CD2 1 
ATOM   89   C  CE1 . PHE A 1 11  ? -4.134  -39.729 0.026   1.00 38.33  ? 11  PHE A CE1 1 
ATOM   90   C  CE2 . PHE A 1 11  ? -3.209  -41.558 1.244   1.00 36.63  ? 11  PHE A CE2 1 
ATOM   91   C  CZ  . PHE A 1 11  ? -3.119  -40.262 0.811   1.00 37.77  ? 11  PHE A CZ  1 
ATOM   92   N  N   . GLY A 1 12  ? -7.727  -44.627 -3.158  1.00 40.63  ? 12  GLY A N   1 
ATOM   93   C  CA  . GLY A 1 12  ? -8.819  -45.547 -3.456  1.00 41.46  ? 12  GLY A CA  1 
ATOM   94   C  C   . GLY A 1 12  ? -10.174 -44.900 -3.223  1.00 42.02  ? 12  GLY A C   1 
ATOM   95   O  O   . GLY A 1 12  ? -10.403 -43.734 -3.567  1.00 37.90  ? 12  GLY A O   1 
ATOM   96   N  N   . GLU A 1 13  ? -11.086 -45.659 -2.607  1.00 44.78  ? 13  GLU A N   1 
ATOM   97   C  CA  . GLU A 1 13  ? -12.446 -45.166 -2.377  1.00 46.02  ? 13  GLU A CA  1 
ATOM   98   C  C   . GLU A 1 13  ? -12.496 -43.969 -1.437  1.00 46.35  ? 13  GLU A C   1 
ATOM   99   O  O   . GLU A 1 13  ? -13.503 -43.254 -1.423  1.00 45.40  ? 13  GLU A O   1 
ATOM   100  C  CB  . GLU A 1 13  ? -13.323 -46.291 -1.823  1.00 48.48  ? 13  GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 13  ? -13.335 -47.511 -2.719  1.00 57.25  ? 13  GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 13  ? -14.625 -48.305 -2.612  1.00 72.10  ? 13  GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 13  ? -15.182 -48.677 -3.669  1.00 73.01  ? 13  GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 13  ? -15.064 -48.577 -1.471  1.00 70.29  ? 13  GLU A OE2 1 
ATOM   105  N  N   . LEU A 1 14  ? -11.446 -43.736 -0.650  1.00 42.41  ? 14  LEU A N   1 
ATOM   106  C  CA  . LEU A 1 14  ? -11.395 -42.564 0.210   1.00 43.32  ? 14  LEU A CA  1 
ATOM   107  C  C   . LEU A 1 14  ? -11.044 -41.297 -0.563  1.00 43.76  ? 14  LEU A C   1 
ATOM   108  O  O   . LEU A 1 14  ? -11.134 -40.203 0.003   1.00 36.09  ? 14  LEU A O   1 
ATOM   109  C  CB  . LEU A 1 14  ? -10.378 -42.780 1.332   1.00 37.25  ? 14  LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 14  ? -10.727 -43.862 2.360   1.00 48.45  ? 14  LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 14  ? -9.701  -43.915 3.497   1.00 44.31  ? 14  LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 14  ? -12.138 -43.652 2.891   1.00 46.06  ? 14  LEU A CD2 1 
ATOM   113  N  N   . LYS A 1 15  ? -10.637 -41.418 -1.827  1.00 39.01  ? 15  LYS A N   1 
ATOM   114  C  CA  . LYS A 1 15  ? -10.370 -40.252 -2.692  1.00 41.81  ? 15  LYS A CA  1 
ATOM   115  C  C   . LYS A 1 15  ? -9.247  -39.419 -2.073  1.00 40.80  ? 15  LYS A C   1 
ATOM   116  O  O   . LYS A 1 15  ? -8.180  -39.973 -1.748  1.00 38.18  ? 15  LYS A O   1 
ATOM   117  C  CB  . LYS A 1 15  ? -11.678 -39.497 -2.911  1.00 43.55  ? 15  LYS A CB  1 
ATOM   118  C  CG  . LYS A 1 15  ? -12.562 -40.010 -4.024  1.00 48.62  ? 15  LYS A CG  1 
ATOM   119  C  CD  . LYS A 1 15  ? -13.467 -41.116 -3.546  1.00 52.25  ? 15  LYS A CD  1 
ATOM   120  C  CE  . LYS A 1 15  ? -14.510 -41.496 -4.606  1.00 57.88  ? 15  LYS A CE  1 
ATOM   121  N  NZ  . LYS A 1 15  ? -15.642 -40.505 -4.671  1.00 59.10  ? 15  LYS A NZ  1 
ATOM   122  N  N   . ASN A 1 16  ? -9.427  -38.101 -1.901  1.00 34.43  ? 16  ASN A N   1 
ATOM   123  C  CA  . ASN A 1 16  ? -8.414  -37.233 -1.312  1.00 36.44  ? 16  ASN A CA  1 
ATOM   124  C  C   . ASN A 1 16  ? -8.561  -37.062 0.196   1.00 35.47  ? 16  ASN A C   1 
ATOM   125  O  O   . ASN A 1 16  ? -7.713  -36.397 0.810   1.00 35.34  ? 16  ASN A O   1 
ATOM   126  C  CB  . ASN A 1 16  ? -8.454  -35.841 -1.955  1.00 35.55  ? 16  ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 16  ? -8.183  -35.874 -3.447  1.00 39.48  ? 16  ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 16  ? -9.036  -35.489 -4.241  1.00 37.95  ? 16  ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 16  ? -6.992  -36.342 -3.839  1.00 36.81  ? 16  ASN A ND2 1 
ATOM   130  N  N   . LEU A 1 17  ? -9.611  -37.613 0.806   1.00 36.63  ? 17  LEU A N   1 
ATOM   131  C  CA  . LEU A 1 17  ? -9.858  -37.370 2.232   1.00 36.30  ? 17  LEU A CA  1 
ATOM   132  C  C   . LEU A 1 17  ? -8.649  -37.581 3.133   1.00 38.87  ? 17  LEU A C   1 
ATOM   133  O  O   . LEU A 1 17  ? -8.412  -36.732 4.007   1.00 34.99  ? 17  LEU A O   1 
ATOM   134  C  CB  . LEU A 1 17  ? -11.044 -38.220 2.707   1.00 34.39  ? 17  LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 17  ? -11.600 -37.735 4.051   1.00 42.32  ? 17  LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 17  ? -12.245 -36.376 3.930   1.00 44.53  ? 17  LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 17  ? -12.648 -38.729 4.494   1.00 43.64  ? 17  LEU A CD2 1 
ATOM   138  N  N   . PRO A 1 18  ? -7.865  -38.654 2.998   1.00 37.96  ? 18  PRO A N   1 
ATOM   139  C  CA  . PRO A 1 18  ? -6.716  -38.846 3.904   1.00 36.36  ? 18  PRO A CA  1 
ATOM   140  C  C   . PRO A 1 18  ? -5.694  -37.717 3.875   1.00 36.29  ? 18  PRO A C   1 
ATOM   141  O  O   . PRO A 1 18  ? -4.883  -37.614 4.808   1.00 36.38  ? 18  PRO A O   1 
ATOM   142  C  CB  . PRO A 1 18  ? -6.109  -40.169 3.412   1.00 38.98  ? 18  PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 18  ? -7.299  -40.908 2.846   1.00 36.22  ? 18  PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 18  ? -8.082  -39.821 2.132   1.00 34.44  ? 18  PRO A CD  1 
ATOM   145  N  N   . LEU A 1 19  ? -5.695  -36.862 2.846   1.00 36.94  ? 19  LEU A N   1 
ATOM   146  C  CA  . LEU A 1 19  ? -4.806  -35.701 2.875   1.00 37.27  ? 19  LEU A CA  1 
ATOM   147  C  C   . LEU A 1 19  ? -5.165  -34.737 4.002   1.00 38.30  ? 19  LEU A C   1 
ATOM   148  O  O   . LEU A 1 19  ? -4.320  -33.931 4.414   1.00 37.43  ? 19  LEU A O   1 
ATOM   149  C  CB  . LEU A 1 19  ? -4.845  -34.973 1.536   1.00 38.51  ? 19  LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 19  ? -4.424  -35.778 0.308   1.00 38.31  ? 19  LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 19  ? -4.584  -34.926 -0.947  1.00 37.35  ? 19  LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 19  ? -2.982  -36.252 0.482   1.00 37.44  ? 19  LEU A CD2 1 
ATOM   153  N  N   . LEU A 1 20  ? -6.398  -34.784 4.506   1.00 35.09  ? 20  LEU A N   1 
ATOM   154  C  CA  . LEU A 1 20  ? -6.774  -33.939 5.635   1.00 37.99  ? 20  LEU A CA  1 
ATOM   155  C  C   . LEU A 1 20  ? -6.502  -34.607 6.973   1.00 39.88  ? 20  LEU A C   1 
ATOM   156  O  O   . LEU A 1 20  ? -6.775  -34.005 8.015   1.00 40.68  ? 20  LEU A O   1 
ATOM   157  C  CB  . LEU A 1 20  ? -8.257  -33.561 5.575   1.00 35.19  ? 20  LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 20  ? -8.782  -32.905 4.302   1.00 41.82  ? 20  LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 20  ? -10.269 -32.632 4.486   1.00 40.91  ? 20  LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 20  ? -8.010  -31.644 3.999   1.00 43.56  ? 20  LEU A CD2 1 
ATOM   161  N  N   . ASN A 1 21  ? -5.984  -35.836 6.969   1.00 44.10  ? 21  ASN A N   1 
ATOM   162  C  CA  . ASN A 1 21  ? -5.686  -36.560 8.205   1.00 45.23  ? 21  ASN A CA  1 
ATOM   163  C  C   . ASN A 1 21  ? -4.350  -36.041 8.745   1.00 44.38  ? 21  ASN A C   1 
ATOM   164  O  O   . ASN A 1 21  ? -3.304  -36.690 8.677   1.00 42.52  ? 21  ASN A O   1 
ATOM   165  C  CB  . ASN A 1 21  ? -5.636  -38.059 7.947   1.00 44.85  ? 21  ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 21  ? -5.494  -38.862 9.219   1.00 52.58  ? 21  ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 21  ? -5.090  -38.336 10.261  1.00 48.24  ? 21  ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 21  ? -5.742  -40.161 9.123   1.00 55.17  ? 21  ASN A ND2 1 
ATOM   169  N  N   . THR A 1 22  ? -4.399  -34.818 9.264   1.00 41.98  ? 22  THR A N   1 
ATOM   170  C  CA  . THR A 1 22  ? -3.235  -34.121 9.793   1.00 43.12  ? 22  THR A CA  1 
ATOM   171  C  C   . THR A 1 22  ? -3.734  -33.045 10.741  1.00 44.76  ? 22  THR A C   1 
ATOM   172  O  O   . THR A 1 22  ? -4.910  -32.673 10.716  1.00 47.16  ? 22  THR A O   1 
ATOM   173  C  CB  . THR A 1 22  ? -2.380  -33.506 8.684   1.00 43.58  ? 22  THR A CB  1 
ATOM   174  O  OG1 . THR A 1 22  ? -1.394  -32.648 9.272   1.00 46.98  ? 22  THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 22  ? -3.247  -32.698 7.697   1.00 38.00  ? 22  THR A CG2 1 
ATOM   176  N  N   . ASP A 1 23  ? -2.842  -32.562 11.601  1.00 45.66  ? 23  ASP A N   1 
ATOM   177  C  CA  . ASP A 1 23  ? -3.284  -31.501 12.494  1.00 50.28  ? 23  ASP A CA  1 
ATOM   178  C  C   . ASP A 1 23  ? -3.140  -30.113 11.876  1.00 38.66  ? 23  ASP A C   1 
ATOM   179  O  O   . ASP A 1 23  ? -3.605  -29.139 12.476  1.00 39.57  ? 23  ASP A O   1 
ATOM   180  C  CB  . ASP A 1 23  ? -2.528  -31.582 13.819  1.00 49.22  ? 23  ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 23  ? -1.054  -31.779 13.624  1.00 59.57  ? 23  ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 23  ? -0.652  -32.929 13.313  1.00 62.80  ? 23  ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 23  ? -0.301  -30.796 13.805  1.00 61.23  ? 23  ASP A OD2 1 
ATOM   184  N  N   . LYS A 1 24  ? -2.536  -30.005 10.690  1.00 42.40  ? 24  LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? -2.367  -28.729 9.991   1.00 38.85  ? 24  LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? -2.890  -28.846 8.561   1.00 35.62  ? 24  LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? -2.140  -28.702 7.592   1.00 33.76  ? 24  LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? -0.900  -28.317 10.012  1.00 39.35  ? 24  LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? -0.340  -28.136 11.425  1.00 37.78  ? 24  LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 1.108   -27.644 11.379  1.00 41.27  ? 24  LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 1.665   -27.405 12.801  1.00 41.55  ? 24  LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 3.065   -26.878 12.757  1.00 41.35  ? 24  LYS A NZ  1 
ATOM   193  N  N   . PRO A 1 25  ? -4.193  -29.102 8.397   1.00 33.79  ? 25  PRO A N   1 
ATOM   194  C  CA  . PRO A 1 25  ? -4.721  -29.361 7.043   1.00 35.24  ? 25  PRO A CA  1 
ATOM   195  C  C   . PRO A 1 25  ? -4.720  -28.151 6.120   1.00 39.50  ? 25  PRO A C   1 
ATOM   196  O  O   . PRO A 1 25  ? -4.538  -28.314 4.905   1.00 38.93  ? 25  PRO A O   1 
ATOM   197  C  CB  . PRO A 1 25  ? -6.153  -29.858 7.315   1.00 35.03  ? 25  PRO A CB  1 
ATOM   198  C  CG  . PRO A 1 25  ? -6.511  -29.299 8.673   1.00 36.04  ? 25  PRO A CG  1 
ATOM   199  C  CD  . PRO A 1 25  ? -5.211  -29.274 9.449   1.00 37.41  ? 25  PRO A CD  1 
ATOM   200  N  N   . VAL A 1 26  ? -4.975  -26.948 6.642   1.00 36.07  ? 26  VAL A N   1 
ATOM   201  C  CA  . VAL A 1 26  ? -4.907  -25.752 5.805   1.00 32.33  ? 26  VAL A CA  1 
ATOM   202  C  C   . VAL A 1 26  ? -3.509  -25.585 5.235   1.00 38.19  ? 26  VAL A C   1 
ATOM   203  O  O   . VAL A 1 26  ? -3.332  -25.325 4.041   1.00 35.13  ? 26  VAL A O   1 
ATOM   204  C  CB  . VAL A 1 26  ? -5.322  -24.507 6.605   1.00 35.08  ? 26  VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 26  ? -4.907  -23.246 5.845   1.00 35.42  ? 26  VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 26  ? -6.835  -24.528 6.880   1.00 34.14  ? 26  VAL A CG2 1 
ATOM   207  N  N   . GLN A 1 27  ? -2.492  -25.706 6.091   1.00 35.95  ? 27  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 27  ? -1.116  -25.618 5.606   1.00 36.48  ? 27  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 27  ? -0.776  -26.752 4.644   1.00 36.44  ? 27  GLN A C   1 
ATOM   210  O  O   . GLN A 1 27  ? 0.009   -26.552 3.703   1.00 36.37  ? 27  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 27  ? -0.158  -25.589 6.795   1.00 36.92  ? 27  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 27  ? -0.240  -24.299 7.589   1.00 38.15  ? 27  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 27  ? 0.306   -24.442 8.992   1.00 39.47  ? 27  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 27  ? 1.492   -24.207 9.230   1.00 37.18  ? 27  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 27  ? -0.562  -24.803 9.939   1.00 36.65  ? 27  GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 28  ? -1.360  -27.941 4.848   1.00 36.32  ? 28  ALA A N   1 
ATOM   217  C  CA  . ALA A 1 28  ? -1.160  -29.017 3.885   1.00 38.07  ? 28  ALA A CA  1 
ATOM   218  C  C   . ALA A 1 28  ? -1.795  -28.671 2.542   1.00 39.81  ? 28  ALA A C   1 
ATOM   219  O  O   . ALA A 1 28  ? -1.212  -28.945 1.487   1.00 35.54  ? 28  ALA A O   1 
ATOM   220  C  CB  . ALA A 1 28  ? -1.714  -30.331 4.431   1.00 38.32  ? 28  ALA A CB  1 
ATOM   221  N  N   . LEU A 1 29  ? -2.987  -28.058 2.558   1.00 34.55  ? 29  LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? -3.620  -27.634 1.312   1.00 36.03  ? 29  LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? -2.837  -26.517 0.638   1.00 34.83  ? 29  LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? -2.800  -26.435 -0.598  1.00 36.15  ? 29  LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? -5.058  -27.173 1.591   1.00 35.85  ? 29  LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? -6.010  -28.308 1.932   1.00 32.87  ? 29  LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? -7.248  -27.810 2.694   1.00 36.87  ? 29  LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? -6.410  -29.035 0.656   1.00 32.70  ? 29  LEU A CD2 1 
ATOM   229  N  N   . MET A 1 30  ? -2.180  -25.663 1.420   1.00 32.60  ? 30  MET A N   1 
ATOM   230  C  CA  . MET A 1 30  ? -1.376  -24.609 0.815   1.00 31.25  ? 30  MET A CA  1 
ATOM   231  C  C   . MET A 1 30  ? -0.233  -25.221 0.013   1.00 37.83  ? 30  MET A C   1 
ATOM   232  O  O   . MET A 1 30  ? 0.073   -24.780 -1.103  1.00 36.41  ? 30  MET A O   1 
ATOM   233  C  CB  . MET A 1 30  ? -0.777  -23.691 1.875   1.00 35.08  ? 30  MET A CB  1 
ATOM   234  C  CG  . MET A 1 30  ? -1.592  -22.440 2.125   1.00 40.18  ? 30  MET A CG  1 
ATOM   235  S  SD  . MET A 1 30  ? -1.323  -21.922 3.832   1.00 35.82  ? 30  MET A SD  1 
ATOM   236  C  CE  . MET A 1 30  ? 0.008   -20.824 3.396   1.00 32.51  ? 30  MET A CE  1 
ATOM   237  N  N   . LYS A 1 31  ? 0.444   -26.216 0.596   1.00 35.23  ? 31  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 31  ? 1.544   -26.876 -0.105  1.00 37.17  ? 31  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 31  ? 1.051   -27.577 -1.375  1.00 38.65  ? 31  LYS A C   1 
ATOM   240  O  O   . LYS A 1 31  ? 1.751   -27.599 -2.398  1.00 37.50  ? 31  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 31  ? 2.228   -27.867 0.836   1.00 42.10  ? 31  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 31  ? 3.448   -28.565 0.249   1.00 51.36  ? 31  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 31  ? 4.254   -29.289 1.341   1.00 53.29  ? 31  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 31  ? 5.310   -28.386 1.966   1.00 55.65  ? 31  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 31  ? 6.387   -28.049 0.984   1.00 60.20  ? 31  LYS A NZ  1 
ATOM   246  N  N   . ILE A 1 32  ? -0.155  -28.156 -1.337  1.00 35.01  ? 32  ILE A N   1 
ATOM   247  C  CA  . ILE A 1 32  ? -0.708  -28.730 -2.563  1.00 34.14  ? 32  ILE A CA  1 
ATOM   248  C  C   . ILE A 1 32  ? -0.892  -27.647 -3.618  1.00 40.14  ? 32  ILE A C   1 
ATOM   249  O  O   . ILE A 1 32  ? -0.545  -27.842 -4.794  1.00 39.15  ? 32  ILE A O   1 
ATOM   250  C  CB  . ILE A 1 32  ? -2.018  -29.484 -2.274  1.00 34.52  ? 32  ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 32  ? -1.724  -30.751 -1.453  1.00 34.35  ? 32  ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 32  ? -2.761  -29.816 -3.603  1.00 33.26  ? 32  ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 32  ? -2.957  -31.364 -0.740  1.00 36.85  ? 32  ILE A CD1 1 
ATOM   254  N  N   . ALA A 1 33  ? -1.407  -26.474 -3.209  1.00 37.39  ? 33  ALA A N   1 
ATOM   255  C  CA  . ALA A 1 33  ? -1.576  -25.364 -4.146  1.00 36.24  ? 33  ALA A CA  1 
ATOM   256  C  C   . ALA A 1 33  ? -0.243  -24.931 -4.749  1.00 37.17  ? 33  ALA A C   1 
ATOM   257  O  O   . ALA A 1 33  ? -0.167  -24.644 -5.951  1.00 37.17  ? 33  ALA A O   1 
ATOM   258  C  CB  . ALA A 1 33  ? -2.263  -24.174 -3.457  1.00 33.46  ? 33  ALA A CB  1 
ATOM   259  N  N   . ASP A 1 34  ? 0.818   -24.862 -3.935  1.00 39.94  ? 34  ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? 2.154   -24.621 -4.489  1.00 42.24  ? 34  ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? 2.467   -25.585 -5.615  1.00 37.81  ? 34  ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? 2.992   -25.197 -6.662  1.00 46.82  ? 34  ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? 3.230   -24.754 -3.410  1.00 42.04  ? 34  ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? 3.223   -23.616 -2.448  1.00 45.85  ? 34  ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? 2.636   -22.573 -2.789  1.00 48.22  ? 34  ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? 3.812   -23.766 -1.355  1.00 48.22  ? 34  ASP A OD2 1 
ATOM   267  N  N   . GLU A 1 35  ? 2.181   -26.863 -5.396  1.00 38.61  ? 35  GLU A N   1 
ATOM   268  C  CA  . GLU A 1 35  ? 2.478   -27.881 -6.393  1.00 41.25  ? 35  GLU A CA  1 
ATOM   269  C  C   . GLU A 1 35  ? 1.573   -27.757 -7.615  1.00 43.59  ? 35  GLU A C   1 
ATOM   270  O  O   . GLU A 1 35  ? 2.044   -27.827 -8.759  1.00 41.66  ? 35  GLU A O   1 
ATOM   271  C  CB  . GLU A 1 35  ? 2.317   -29.259 -5.763  1.00 42.14  ? 35  GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 35  ? 2.811   -30.390 -6.638  1.00 50.57  ? 35  GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 35  ? 2.612   -31.742 -5.990  1.00 52.86  ? 35  GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 35  ? 2.907   -31.886 -4.784  1.00 53.36  ? 35  GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 35  ? 2.147   -32.662 -6.700  1.00 64.96  ? 35  GLU A OE2 1 
ATOM   276  N  N   . LEU A 1 36  ? 0.266   -27.597 -7.394  1.00 35.08  ? 36  LEU A N   1 
ATOM   277  C  CA  . LEU A 1 36  ? -0.725  -27.777 -8.448  1.00 36.97  ? 36  LEU A CA  1 
ATOM   278  C  C   . LEU A 1 36  ? -1.209  -26.481 -9.097  1.00 39.87  ? 36  LEU A C   1 
ATOM   279  O  O   . LEU A 1 36  ? -1.735  -26.533 -10.219 1.00 40.37  ? 36  LEU A O   1 
ATOM   280  C  CB  . LEU A 1 36  ? -1.930  -28.551 -7.888  1.00 35.72  ? 36  LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 36  ? -1.670  -30.002 -7.451  1.00 39.17  ? 36  LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 36  ? -2.988  -30.755 -7.212  1.00 35.38  ? 36  LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 36  ? -0.805  -30.761 -8.470  1.00 40.55  ? 36  LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 37  ? -1.074  -25.338 -8.432  1.00 35.25  ? 37  GLY A N   1 
ATOM   285  C  CA  . GLY A 1 37  ? -1.435  -24.055 -9.030  1.00 38.79  ? 37  GLY A CA  1 
ATOM   286  C  C   . GLY A 1 37  ? -2.742  -23.467 -8.530  1.00 41.06  ? 37  GLY A C   1 
ATOM   287  O  O   . GLY A 1 37  ? -3.237  -23.776 -7.444  1.00 38.52  ? 37  GLY A O   1 
ATOM   288  N  N   . GLU A 1 38  ? -3.318  -22.597 -9.368  1.00 39.71  ? 38  GLU A N   1 
ATOM   289  C  CA  . GLU A 1 38  ? -4.426  -21.739 -8.945  1.00 37.60  ? 38  GLU A CA  1 
ATOM   290  C  C   . GLU A 1 38  ? -5.733  -22.493 -8.693  1.00 34.87  ? 38  GLU A C   1 
ATOM   291  O  O   . GLU A 1 38  ? -6.654  -21.922 -8.095  1.00 34.33  ? 38  GLU A O   1 
ATOM   292  C  CB  . GLU A 1 38  ? -4.669  -20.658 -10.002 1.00 40.78  ? 38  GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 38  ? -5.122  -21.230 -11.340 1.00 39.18  ? 38  GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 38  ? -5.371  -20.167 -12.407 1.00 44.03  ? 38  GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 38  ? -5.485  -18.963 -12.068 1.00 38.52  ? 38  GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 38  ? -5.450  -20.543 -13.601 1.00 42.32  ? 38  GLU A OE2 1 
ATOM   297  N  N   . ILE A 1 39  ? -5.860  -23.734 -9.149  1.00 32.79  ? 39  ILE A N   1 
ATOM   298  C  CA  . ILE A 1 39  ? -7.115  -24.468 -8.986  1.00 32.51  ? 39  ILE A CA  1 
ATOM   299  C  C   . ILE A 1 39  ? -6.820  -25.960 -8.980  1.00 38.93  ? 39  ILE A C   1 
ATOM   300  O  O   . ILE A 1 39  ? -6.080  -26.457 -9.835  1.00 39.04  ? 39  ILE A O   1 
ATOM   301  C  CB  . ILE A 1 39  ? -8.129  -24.124 -10.093 1.00 36.71  ? 39  ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 39  ? -9.473  -24.790 -9.797  1.00 36.29  ? 39  ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 39  ? -7.608  -24.534 -11.472 1.00 39.85  ? 39  ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 39  ? -10.568 -24.361 -10.751 1.00 40.70  ? 39  ILE A CD1 1 
ATOM   305  N  N   . PHE A 1 40  ? -7.384  -26.678 -8.009  1.00 35.39  ? 40  PHE A N   1 
ATOM   306  C  CA  . PHE A 1 40  ? -7.304  -28.131 -8.028  1.00 39.09  ? 40  PHE A CA  1 
ATOM   307  C  C   . PHE A 1 40  ? -8.569  -28.731 -7.439  1.00 38.93  ? 40  PHE A C   1 
ATOM   308  O  O   . PHE A 1 40  ? -9.176  -28.159 -6.526  1.00 36.88  ? 40  PHE A O   1 
ATOM   309  C  CB  . PHE A 1 40  ? -6.070  -28.660 -7.285  1.00 36.80  ? 40  PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 40  ? -6.033  -28.337 -5.803  1.00 37.25  ? 40  PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 40  ? -6.691  -29.149 -4.882  1.00 37.59  ? 40  PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 40  ? -5.277  -27.275 -5.327  1.00 35.88  ? 40  PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 40  ? -6.621  -28.877 -3.511  1.00 36.17  ? 40  PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 40  ? -5.209  -26.991 -3.962  1.00 32.91  ? 40  PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 40  ? -5.875  -27.795 -3.053  1.00 34.38  ? 40  PHE A CZ  1 
ATOM   316  N  N   . LYS A 1 41  ? -8.971  -29.869 -8.008  1.00 35.41  ? 41  LYS A N   1 
ATOM   317  C  CA  . LYS A 1 41  ? -10.090 -30.669 -7.524  1.00 37.62  ? 41  LYS A CA  1 
ATOM   318  C  C   . LYS A 1 41  ? -9.721  -31.422 -6.253  1.00 35.60  ? 41  LYS A C   1 
ATOM   319  O  O   . LYS A 1 41  ? -8.581  -31.859 -6.069  1.00 35.28  ? 41  LYS A O   1 
ATOM   320  C  CB  . LYS A 1 41  ? -10.513 -31.675 -8.597  1.00 44.49  ? 41  LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 41  ? -11.896 -32.284 -8.400  1.00 42.58  ? 41  LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 41  ? -12.247 -33.154 -9.613  1.00 48.17  ? 41  LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 41  ? -13.135 -32.344 -10.579 1.00 58.71  ? 41  LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 41  ? -13.441 -32.980 -11.905 1.00 56.68  ? 41  LYS A NZ  1 
ATOM   325  N  N   . PHE A 1 42  ? -10.707 -31.578 -5.374  1.00 34.67  ? 42  PHE A N   1 
ATOM   326  C  CA  . PHE A 1 42  ? -10.523 -32.289 -4.116  1.00 37.44  ? 42  PHE A CA  1 
ATOM   327  C  C   . PHE A 1 42  ? -11.804 -33.051 -3.833  1.00 40.94  ? 42  PHE A C   1 
ATOM   328  O  O   . PHE A 1 42  ? -12.866 -32.436 -3.688  1.00 39.09  ? 42  PHE A O   1 
ATOM   329  C  CB  . PHE A 1 42  ? -10.191 -31.320 -2.978  1.00 34.52  ? 42  PHE A CB  1 
ATOM   330  C  CG  . PHE A 1 42  ? -9.760  -31.997 -1.700  1.00 38.94  ? 42  PHE A CG  1 
ATOM   331  C  CD1 . PHE A 1 42  ? -10.689 -32.619 -0.881  1.00 39.93  ? 42  PHE A CD1 1 
ATOM   332  C  CD2 . PHE A 1 42  ? -8.430  -31.993 -1.311  1.00 35.57  ? 42  PHE A CD2 1 
ATOM   333  C  CE1 . PHE A 1 42  ? -10.296 -33.236 0.310   1.00 38.81  ? 42  PHE A CE1 1 
ATOM   334  C  CE2 . PHE A 1 42  ? -8.033  -32.610 -0.123  1.00 38.62  ? 42  PHE A CE2 1 
ATOM   335  C  CZ  . PHE A 1 42  ? -8.962  -33.217 0.689   1.00 37.61  ? 42  PHE A CZ  1 
ATOM   336  N  N   . GLU A 1 43  ? -11.701 -34.381 -3.781  1.00 38.88  ? 43  GLU A N   1 
ATOM   337  C  CA  . GLU A 1 43  ? -12.836 -35.281 -3.612  1.00 40.65  ? 43  GLU A CA  1 
ATOM   338  C  C   . GLU A 1 43  ? -12.736 -36.031 -2.288  1.00 41.40  ? 43  GLU A C   1 
ATOM   339  O  O   . GLU A 1 43  ? -11.640 -36.382 -1.832  1.00 37.19  ? 43  GLU A O   1 
ATOM   340  C  CB  . GLU A 1 43  ? -12.899 -36.306 -4.746  1.00 44.24  ? 43  GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 43  ? -13.349 -35.760 -6.074  1.00 47.74  ? 43  GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 43  ? -13.261 -36.803 -7.165  1.00 53.57  ? 43  GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 43  ? -12.216 -37.496 -7.250  1.00 50.84  ? 43  GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 43  ? -14.238 -36.936 -7.926  1.00 55.77  ? 43  GLU A OE2 1 
ATOM   345  N  N   . ALA A 1 44  ? -13.884 -36.267 -1.670  1.00 39.39  ? 44  ALA A N   1 
ATOM   346  C  CA  . ALA A 1 44  ? -14.033 -37.181 -0.548  1.00 39.91  ? 44  ALA A CA  1 
ATOM   347  C  C   . ALA A 1 44  ? -15.272 -38.011 -0.822  1.00 44.58  ? 44  ALA A C   1 
ATOM   348  O  O   . ALA A 1 44  ? -16.034 -37.718 -1.750  1.00 42.07  ? 44  ALA A O   1 
ATOM   349  C  CB  . ALA A 1 44  ? -14.162 -36.425 0.784   1.00 40.63  ? 44  ALA A CB  1 
ATOM   350  N  N   . PRO A 1 45  ? -15.488 -39.089 -0.064  1.00 46.34  ? 45  PRO A N   1 
ATOM   351  C  CA  . PRO A 1 45  ? -16.733 -39.847 -0.247  1.00 49.14  ? 45  PRO A CA  1 
ATOM   352  C  C   . PRO A 1 45  ? -17.938 -38.924 -0.161  1.00 47.32  ? 45  PRO A C   1 
ATOM   353  O  O   . PRO A 1 45  ? -18.137 -38.255 0.855   1.00 46.53  ? 45  PRO A O   1 
ATOM   354  C  CB  . PRO A 1 45  ? -16.693 -40.863 0.893   1.00 48.25  ? 45  PRO A CB  1 
ATOM   355  C  CG  . PRO A 1 45  ? -15.225 -41.115 1.073   1.00 45.98  ? 45  PRO A CG  1 
ATOM   356  C  CD  . PRO A 1 45  ? -14.568 -39.763 0.870   1.00 45.91  ? 45  PRO A CD  1 
ATOM   357  N  N   . GLY A 1 46  ? -18.707 -38.845 -1.248  1.00 51.77  ? 46  GLY A N   1 
ATOM   358  C  CA  . GLY A 1 46  ? -19.898 -38.021 -1.310  1.00 50.64  ? 46  GLY A CA  1 
ATOM   359  C  C   . GLY A 1 46  ? -19.696 -36.521 -1.437  1.00 58.41  ? 46  GLY A C   1 
ATOM   360  O  O   . GLY A 1 46  ? -20.663 -35.777 -1.241  1.00 55.51  ? 46  GLY A O   1 
ATOM   361  N  N   . ARG A 1 47  ? -18.490 -36.039 -1.764  1.00 50.11  ? 47  ARG A N   1 
ATOM   362  C  CA  . ARG A 1 47  ? -18.250 -34.597 -1.813  1.00 50.37  ? 47  ARG A CA  1 
ATOM   363  C  C   . ARG A 1 47  ? -17.212 -34.302 -2.891  1.00 47.03  ? 47  ARG A C   1 
ATOM   364  O  O   . ARG A 1 47  ? -16.259 -35.063 -3.070  1.00 42.81  ? 47  ARG A O   1 
ATOM   365  C  CB  . ARG A 1 47  ? -17.808 -34.050 -0.431  1.00 48.33  ? 47  ARG A CB  1 
ATOM   366  C  CG  . ARG A 1 47  ? -18.016 -32.499 -0.155  1.00 53.08  ? 47  ARG A CG  1 
ATOM   367  C  CD  . ARG A 1 47  ? -16.791 -31.705 0.434   1.00 53.98  ? 47  ARG A CD  1 
ATOM   368  N  NE  . ARG A 1 47  ? -16.984 -30.246 0.467   1.00 53.06  ? 47  ARG A NE  1 
ATOM   369  C  CZ  . ARG A 1 47  ? -16.476 -29.355 1.335   1.00 50.78  ? 47  ARG A CZ  1 
ATOM   370  N  NH1 . ARG A 1 47  ? -15.827 -29.705 2.458   1.00 60.17  ? 47  ARG A NH1 1 
ATOM   371  N  NH2 . ARG A 1 47  ? -16.644 -28.062 1.090   1.00 48.84  ? 47  ARG A NH2 1 
ATOM   372  N  N   . VAL A 1 48  ? -17.426 -33.221 -3.637  1.00 44.06  ? 48  VAL A N   1 
ATOM   373  C  CA  . VAL A 1 48  ? -16.411 -32.674 -4.532  1.00 40.62  ? 48  VAL A CA  1 
ATOM   374  C  C   . VAL A 1 48  ? -16.346 -31.175 -4.283  1.00 42.36  ? 48  VAL A C   1 
ATOM   375  O  O   . VAL A 1 48  ? -17.383 -30.519 -4.143  1.00 38.39  ? 48  VAL A O   1 
ATOM   376  C  CB  . VAL A 1 48  ? -16.705 -32.948 -6.023  1.00 43.69  ? 48  VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 48  ? -15.798 -32.074 -6.898  1.00 43.44  ? 48  VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 48  ? -16.534 -34.425 -6.362  1.00 46.29  ? 48  VAL A CG2 1 
ATOM   379  N  N   . THR A 1 49  ? -15.133 -30.634 -4.210  1.00 38.19  ? 49  THR A N   1 
ATOM   380  C  CA  . THR A 1 49  ? -14.959 -29.190 -4.206  1.00 36.60  ? 49  THR A CA  1 
ATOM   381  C  C   . THR A 1 49  ? -13.710 -28.870 -5.017  1.00 38.90  ? 49  THR A C   1 
ATOM   382  O  O   . THR A 1 49  ? -13.001 -29.767 -5.498  1.00 38.59  ? 49  THR A O   1 
ATOM   383  C  CB  . THR A 1 49  ? -14.929 -28.637 -2.760  1.00 34.43  ? 49  THR A CB  1 
ATOM   384  O  OG1 . THR A 1 49  ? -15.069 -27.210 -2.784  1.00 37.75  ? 49  THR A OG1 1 
ATOM   385  C  CG2 . THR A 1 49  ? -13.636 -29.007 -2.047  1.00 38.71  ? 49  THR A CG2 1 
ATOM   386  N  N   . ARG A 1 50  ? -13.470 -27.582 -5.216  1.00 40.19  ? 50  ARG A N   1 
ATOM   387  C  CA  . ARG A 1 50  ? -12.348 -27.098 -6.011  1.00 36.98  ? 50  ARG A CA  1 
ATOM   388  C  C   . ARG A 1 50  ? -11.686 -25.985 -5.222  1.00 37.80  ? 50  ARG A C   1 
ATOM   389  O  O   . ARG A 1 50  ? -12.361 -25.020 -4.847  1.00 36.05  ? 50  ARG A O   1 
ATOM   390  C  CB  . ARG A 1 50  ? -12.815 -26.590 -7.379  1.00 35.61  ? 50  ARG A CB  1 
ATOM   391  C  CG  . ARG A 1 50  ? -13.571 -27.619 -8.224  1.00 38.87  ? 50  ARG A CG  1 
ATOM   392  C  CD  . ARG A 1 50  ? -14.870 -27.071 -8.813  1.00 37.64  ? 50  ARG A CD  1 
ATOM   393  N  NE  . ARG A 1 50  ? -15.654 -28.133 -9.437  1.00 40.26  ? 50  ARG A NE  1 
ATOM   394  C  CZ  . ARG A 1 50  ? -16.605 -28.837 -8.833  1.00 41.08  ? 50  ARG A CZ  1 
ATOM   395  N  NH1 . ARG A 1 50  ? -16.979 -28.577 -7.590  1.00 38.67  ? 50  ARG A NH1 1 
ATOM   396  N  NH2 . ARG A 1 50  ? -17.190 -29.834 -9.492  1.00 41.82  ? 50  ARG A NH2 1 
ATOM   397  N  N   . TYR A 1 51  ? -10.379 -26.109 -4.969  1.00 31.52  ? 51  TYR A N   1 
ATOM   398  C  CA  . TYR A 1 51  ? -9.650  -25.115 -4.187  1.00 34.03  ? 51  TYR A CA  1 
ATOM   399  C  C   . TYR A 1 51  ? -9.082  -24.034 -5.101  1.00 32.17  ? 51  TYR A C   1 
ATOM   400  O  O   . TYR A 1 51  ? -8.263  -24.325 -5.984  1.00 35.67  ? 51  TYR A O   1 
ATOM   401  C  CB  . TYR A 1 51  ? -8.532  -25.765 -3.366  1.00 32.39  ? 51  TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 51  ? -9.072  -26.450 -2.122  1.00 31.54  ? 51  TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 51  ? -9.578  -27.742 -2.188  1.00 31.75  ? 51  TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 51  ? -9.093  -25.798 -0.898  1.00 32.53  ? 51  TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 51  ? -10.094 -28.374 -1.066  1.00 38.17  ? 51  TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 51  ? -9.614  -26.421 0.232   1.00 34.20  ? 51  TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 51  ? -10.113 -27.710 0.140   1.00 37.31  ? 51  TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 51  ? -10.629 -28.335 1.258   1.00 39.29  ? 51  TYR A OH  1 
ATOM   409  N  N   . LEU A 1 52  ? -9.497  -22.793 -4.871  1.00 32.46  ? 52  LEU A N   1 
ATOM   410  C  CA  . LEU A 1 52  ? -9.034  -21.638 -5.633  1.00 32.78  ? 52  LEU A CA  1 
ATOM   411  C  C   . LEU A 1 52  ? -7.948  -20.916 -4.853  1.00 32.79  ? 52  LEU A C   1 
ATOM   412  O  O   . LEU A 1 52  ? -8.112  -20.661 -3.655  1.00 33.04  ? 52  LEU A O   1 
ATOM   413  C  CB  . LEU A 1 52  ? -10.183 -20.671 -5.909  1.00 32.98  ? 52  LEU A CB  1 
ATOM   414  C  CG  . LEU A 1 52  ? -11.346 -21.267 -6.699  1.00 37.20  ? 52  LEU A CG  1 
ATOM   415  C  CD1 . LEU A 1 52  ? -12.314 -20.141 -7.121  1.00 34.35  ? 52  LEU A CD1 1 
ATOM   416  C  CD2 . LEU A 1 52  ? -10.814 -22.046 -7.914  1.00 34.97  ? 52  LEU A CD2 1 
ATOM   417  N  N   . SER A 1 53  ? -6.854  -20.567 -5.542  1.00 32.00  ? 53  SER A N   1 
ATOM   418  C  CA  . SER A 1 53  ? -5.713  -19.889 -4.930  1.00 39.96  ? 53  SER A CA  1 
ATOM   419  C  C   . SER A 1 53  ? -5.268  -18.615 -5.641  1.00 35.52  ? 53  SER A C   1 
ATOM   420  O  O   . SER A 1 53  ? -4.404  -17.919 -5.099  1.00 34.94  ? 53  SER A O   1 
ATOM   421  C  CB  . SER A 1 53  ? -4.493  -20.832 -4.858  1.00 37.26  ? 53  SER A CB  1 
ATOM   422  O  OG  . SER A 1 53  ? -4.684  -21.817 -3.864  1.00 39.14  ? 53  SER A OG  1 
ATOM   423  N  N   . SER A 1 54  ? -5.778  -18.308 -6.844  1.00 33.32  ? 54  SER A N   1 
ATOM   424  C  CA  . SER A 1 54  ? -5.339  -17.130 -7.590  1.00 37.30  ? 54  SER A CA  1 
ATOM   425  C  C   . SER A 1 54  ? -6.391  -16.024 -7.553  1.00 33.35  ? 54  SER A C   1 
ATOM   426  O  O   . SER A 1 54  ? -7.597  -16.285 -7.575  1.00 33.50  ? 54  SER A O   1 
ATOM   427  C  CB  . SER A 1 54  ? -5.040  -17.463 -9.057  1.00 34.14  ? 54  SER A CB  1 
ATOM   428  O  OG  . SER A 1 54  ? -6.241  -17.772 -9.743  1.00 34.06  ? 54  SER A OG  1 
ATOM   429  N  N   . GLN A 1 55  ? -5.916  -14.777 -7.523  1.00 35.36  ? 55  GLN A N   1 
ATOM   430  C  CA  . GLN A 1 55  ? -6.830  -13.642 -7.636  1.00 33.59  ? 55  GLN A CA  1 
ATOM   431  C  C   . GLN A 1 55  ? -7.597  -13.689 -8.950  1.00 34.61  ? 55  GLN A C   1 
ATOM   432  O  O   . GLN A 1 55  ? -8.767  -13.283 -9.003  1.00 34.26  ? 55  GLN A O   1 
ATOM   433  C  CB  . GLN A 1 55  ? -6.042  -12.325 -7.502  1.00 34.04  ? 55  GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 55  ? -6.876  -11.014 -7.491  1.00 34.73  ? 55  GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 55  ? -7.145  -10.445 -8.894  1.00 36.23  ? 55  GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 55  ? -6.671  -10.982 -9.893  1.00 38.27  ? 55  GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 55  ? -7.896  -9.340  -8.963  1.00 32.08  ? 55  GLN A NE2 1 
ATOM   438  N  N   . ARG A 1 56  ? -6.971  -14.221 -10.010 1.00 35.40  ? 56  ARG A N   1 
ATOM   439  C  CA  . ARG A 1 56  ? -7.626  -14.282 -11.320 1.00 35.38  ? 56  ARG A CA  1 
ATOM   440  C  C   . ARG A 1 56  ? -8.958  -15.005 -11.228 1.00 37.79  ? 56  ARG A C   1 
ATOM   441  O  O   . ARG A 1 56  ? -9.948  -14.582 -11.838 1.00 35.90  ? 56  ARG A O   1 
ATOM   442  C  CB  . ARG A 1 56  ? -6.713  -14.984 -12.339 1.00 35.35  ? 56  ARG A CB  1 
ATOM   443  C  CG  . ARG A 1 56  ? -7.376  -15.258 -13.704 1.00 44.93  ? 56  ARG A CG  1 
ATOM   444  C  CD  . ARG A 1 56  ? -6.420  -15.992 -14.648 1.00 42.69  ? 56  ARG A CD  1 
ATOM   445  N  NE  . ARG A 1 56  ? -6.590  -17.444 -14.606 1.00 43.89  ? 56  ARG A NE  1 
ATOM   446  C  CZ  . ARG A 1 56  ? -7.431  -18.125 -15.378 1.00 48.60  ? 56  ARG A CZ  1 
ATOM   447  N  NH1 . ARG A 1 56  ? -8.185  -17.519 -16.283 1.00 45.34  ? 56  ARG A NH1 1 
ATOM   448  N  NH2 . ARG A 1 56  ? -7.513  -19.448 -15.243 1.00 47.03  ? 56  ARG A NH2 1 
ATOM   449  N  N   . LEU A 1 57  ? -8.999  -16.111 -10.478 1.00 33.36  ? 57  LEU A N   1 
ATOM   450  C  CA  . LEU A 1 57  ? -10.215 -16.902 -10.379 1.00 34.93  ? 57  LEU A CA  1 
ATOM   451  C  C   . LEU A 1 57  ? -11.081 -16.460 -9.212  1.00 33.78  ? 57  LEU A C   1 
ATOM   452  O  O   . LEU A 1 57  ? -12.313 -16.527 -9.291  1.00 35.37  ? 57  LEU A O   1 
ATOM   453  C  CB  . LEU A 1 57  ? -9.871  -18.390 -10.235 1.00 34.34  ? 57  LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 57  ? -9.188  -19.017 -11.459 1.00 37.47  ? 57  LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 57  ? -8.910  -20.515 -11.251 1.00 34.61  ? 57  LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 57  ? -10.012 -18.768 -12.701 1.00 36.37  ? 57  LEU A CD2 1 
ATOM   457  N  N   . ILE A 1 58  ? -10.457 -16.022 -8.122  1.00 32.01  ? 58  ILE A N   1 
ATOM   458  C  CA  . ILE A 1 58  ? -11.233 -15.679 -6.937  1.00 34.60  ? 58  ILE A CA  1 
ATOM   459  C  C   . ILE A 1 58  ? -12.040 -14.409 -7.181  1.00 34.38  ? 58  ILE A C   1 
ATOM   460  O  O   . ILE A 1 58  ? -13.135 -14.243 -6.627  1.00 33.55  ? 58  ILE A O   1 
ATOM   461  C  CB  . ILE A 1 58  ? -10.286 -15.589 -5.720  1.00 35.42  ? 58  ILE A CB  1 
ATOM   462  C  CG1 . ILE A 1 58  ? -9.894  -17.024 -5.292  1.00 35.48  ? 58  ILE A CG1 1 
ATOM   463  C  CG2 . ILE A 1 58  ? -10.945 -14.839 -4.566  1.00 32.44  ? 58  ILE A CG2 1 
ATOM   464  C  CD1 . ILE A 1 58  ? -8.617  -17.153 -4.449  1.00 32.56  ? 58  ILE A CD1 1 
ATOM   465  N  N   . LYS A 1 59  ? -11.553 -13.518 -8.050  1.00 31.95  ? 59  LYS A N   1 
ATOM   466  C  CA  . LYS A 1 59  ? -12.325 -12.323 -8.367  1.00 36.30  ? 59  LYS A CA  1 
ATOM   467  C  C   . LYS A 1 59  ? -13.636 -12.677 -9.049  1.00 35.38  ? 59  LYS A C   1 
ATOM   468  O  O   . LYS A 1 59  ? -14.640 -11.981 -8.850  1.00 36.85  ? 59  LYS A O   1 
ATOM   469  C  CB  . LYS A 1 59  ? -11.505 -11.360 -9.218  1.00 32.35  ? 59  LYS A CB  1 
ATOM   470  C  CG  . LYS A 1 59  ? -11.377 -11.737 -10.672 1.00 36.17  ? 59  LYS A CG  1 
ATOM   471  C  CD  . LYS A 1 59  ? -10.501 -10.721 -11.390 1.00 34.91  ? 59  LYS A CD  1 
ATOM   472  C  CE  . LYS A 1 59  ? -9.958  -11.259 -12.705 1.00 38.76  ? 59  LYS A CE  1 
ATOM   473  N  NZ  . LYS A 1 59  ? -8.783  -10.460 -13.125 1.00 44.83  ? 59  LYS A NZ  1 
ATOM   474  N  N   . GLU A 1 60  ? -13.669 -13.781 -9.805  1.00 34.32  ? 60  GLU A N   1 
ATOM   475  C  CA  . GLU A 1 60  ? -14.935 -14.254 -10.370 1.00 33.13  ? 60  GLU A CA  1 
ATOM   476  C  C   . GLU A 1 60  ? -15.798 -14.941 -9.322  1.00 36.23  ? 60  GLU A C   1 
ATOM   477  O  O   . GLU A 1 60  ? -17.021 -14.750 -9.292  1.00 35.57  ? 60  GLU A O   1 
ATOM   478  C  CB  . GLU A 1 60  ? -14.667 -15.210 -11.536 1.00 34.69  ? 60  GLU A CB  1 
ATOM   479  C  CG  . GLU A 1 60  ? -14.165 -14.483 -12.759 1.00 39.85  ? 60  GLU A CG  1 
ATOM   480  C  CD  . GLU A 1 60  ? -14.080 -15.374 -13.981 1.00 42.06  ? 60  GLU A CD  1 
ATOM   481  O  OE1 . GLU A 1 60  ? -15.045 -16.120 -14.230 1.00 43.95  ? 60  GLU A OE1 1 
ATOM   482  O  OE2 . GLU A 1 60  ? -13.072 -15.281 -14.716 1.00 46.05  ? 60  GLU A OE2 1 
ATOM   483  N  N   . ALA A 1 61  ? -15.189 -15.764 -8.470  1.00 32.44  ? 61  ALA A N   1 
ATOM   484  C  CA  . ALA A 1 61  ? -15.967 -16.452 -7.452  1.00 35.14  ? 61  ALA A CA  1 
ATOM   485  C  C   . ALA A 1 61  ? -16.650 -15.474 -6.503  1.00 32.15  ? 61  ALA A C   1 
ATOM   486  O  O   . ALA A 1 61  ? -17.672 -15.824 -5.897  1.00 33.05  ? 61  ALA A O   1 
ATOM   487  C  CB  . ALA A 1 61  ? -15.064 -17.421 -6.682  1.00 35.18  ? 61  ALA A CB  1 
ATOM   488  N  N   . CYS A 1 62  ? -16.111 -14.266 -6.355  1.00 29.86  ? 62  CYS A N   1 
ATOM   489  C  CA  . CYS A 1 62  ? -16.692 -13.253 -5.478  1.00 35.02  ? 62  CYS A CA  1 
ATOM   490  C  C   . CYS A 1 62  ? -17.827 -12.483 -6.125  1.00 35.84  ? 62  CYS A C   1 
ATOM   491  O  O   . CYS A 1 62  ? -18.348 -11.560 -5.492  1.00 32.49  ? 62  CYS A O   1 
ATOM   492  C  CB  . CYS A 1 62  ? -15.619 -12.264 -5.013  1.00 35.16  ? 62  CYS A CB  1 
ATOM   493  S  SG  . CYS A 1 62  ? -14.470 -12.988 -3.861  1.00 32.88  ? 62  CYS A SG  1 
ATOM   494  N  N   . ASP A 1 63  ? -18.192 -12.821 -7.360  1.00 35.57  ? 63  ASP A N   1 
ATOM   495  C  CA  . ASP A 1 63  ? -19.363 -12.258 -8.038  1.00 36.87  ? 63  ASP A CA  1 
ATOM   496  C  C   . ASP A 1 63  ? -20.617 -12.854 -7.412  1.00 33.42  ? 63  ASP A C   1 
ATOM   497  O  O   . ASP A 1 63  ? -20.906 -14.039 -7.605  1.00 34.15  ? 63  ASP A O   1 
ATOM   498  C  CB  . ASP A 1 63  ? -19.278 -12.570 -9.536  1.00 35.93  ? 63  ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 63  ? -20.461 -12.025 -10.345 1.00 36.83  ? 63  ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 63  ? -21.477 -11.586 -9.759  1.00 38.53  ? 63  ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 63  ? -20.383 -12.078 -11.595 1.00 39.51  ? 63  ASP A OD2 1 
ATOM   502  N  N   . GLU A 1 64  ? -21.351 -12.042 -6.639  1.00 30.86  ? 64  GLU A N   1 
ATOM   503  C  CA  . GLU A 1 64  ? -22.497 -12.544 -5.888  1.00 34.12  ? 64  GLU A CA  1 
ATOM   504  C  C   . GLU A 1 64  ? -23.666 -12.907 -6.786  1.00 34.02  ? 64  GLU A C   1 
ATOM   505  O  O   . GLU A 1 64  ? -24.592 -13.590 -6.332  1.00 34.81  ? 64  GLU A O   1 
ATOM   506  C  CB  . GLU A 1 64  ? -22.958 -11.510 -4.855  1.00 32.98  ? 64  GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 64  ? -21.941 -11.241 -3.781  1.00 35.56  ? 64  GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 64  ? -22.446 -10.269 -2.755  1.00 34.72  ? 64  GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 64  ? -22.381 -9.045  -2.995  1.00 37.01  ? 64  GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 64  ? -22.940 -10.738 -1.714  1.00 34.89  ? 64  GLU A OE2 1 
ATOM   511  N  N   . SER A 1 65  ? -23.666 -12.444 -8.038  1.00 34.93  ? 65  SER A N   1 
ATOM   512  C  CA  . SER A 1 65  ? -24.730 -12.874 -8.933  1.00 35.71  ? 65  SER A CA  1 
ATOM   513  C  C   . SER A 1 65  ? -24.506 -14.296 -9.418  1.00 36.94  ? 65  SER A C   1 
ATOM   514  O  O   . SER A 1 65  ? -25.464 -14.940 -9.844  1.00 36.59  ? 65  SER A O   1 
ATOM   515  C  CB  . SER A 1 65  ? -24.864 -11.927 -10.137 1.00 36.11  ? 65  SER A CB  1 
ATOM   516  O  OG  . SER A 1 65  ? -23.811 -12.098 -11.076 1.00 35.24  ? 65  SER A OG  1 
ATOM   517  N  N   . ARG A 1 66  ? -23.279 -14.810 -9.316  1.00 34.43  ? 66  ARG A N   1 
ATOM   518  C  CA  . ARG A 1 66  ? -22.935 -16.146 -9.788  1.00 35.53  ? 66  ARG A CA  1 
ATOM   519  C  C   . ARG A 1 66  ? -22.676 -17.151 -8.672  1.00 35.83  ? 66  ARG A C   1 
ATOM   520  O  O   . ARG A 1 66  ? -22.910 -18.350 -8.871  1.00 35.43  ? 66  ARG A O   1 
ATOM   521  C  CB  . ARG A 1 66  ? -21.691 -16.085 -10.693 1.00 38.26  ? 66  ARG A CB  1 
ATOM   522  C  CG  . ARG A 1 66  ? -21.858 -15.227 -11.959 1.00 41.38  ? 66  ARG A CG  1 
ATOM   523  C  CD  . ARG A 1 66  ? -20.488 -14.805 -12.580 1.00 39.50  ? 66  ARG A CD  1 
ATOM   524  N  NE  . ARG A 1 66  ? -19.779 -15.952 -13.124 1.00 38.95  ? 66  ARG A NE  1 
ATOM   525  C  CZ  . ARG A 1 66  ? -18.495 -15.976 -13.453 1.00 40.47  ? 66  ARG A CZ  1 
ATOM   526  N  NH1 . ARG A 1 66  ? -17.730 -14.898 -13.353 1.00 44.29  ? 66  ARG A NH1 1 
ATOM   527  N  NH2 . ARG A 1 66  ? -17.972 -17.103 -13.927 1.00 45.15  ? 66  ARG A NH2 1 
ATOM   528  N  N   . PHE A 1 67  ? -22.219 -16.699 -7.502  1.00 33.77  ? 67  PHE A N   1 
ATOM   529  C  CA  . PHE A 1 67  ? -21.851 -17.588 -6.408  1.00 32.29  ? 67  PHE A CA  1 
ATOM   530  C  C   . PHE A 1 67  ? -22.384 -17.045 -5.090  1.00 31.59  ? 67  PHE A C   1 
ATOM   531  O  O   . PHE A 1 67  ? -22.298 -15.840 -4.816  1.00 32.28  ? 67  PHE A O   1 
ATOM   532  C  CB  . PHE A 1 67  ? -20.307 -17.773 -6.313  1.00 32.62  ? 67  PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 67  ? -19.704 -18.358 -7.566  1.00 35.23  ? 67  PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 67  ? -19.664 -19.727 -7.754  1.00 34.72  ? 67  PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 67  ? -19.234 -17.538 -8.573  1.00 34.93  ? 67  PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 67  ? -19.144 -20.265 -8.928  1.00 36.56  ? 67  PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 67  ? -18.712 -18.070 -9.737  1.00 34.67  ? 67  PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 67  ? -18.658 -19.429 -9.910  1.00 35.49  ? 67  PHE A CZ  1 
ATOM   539  N  N   . ASP A 1 68  ? -22.895 -17.950 -4.269  1.00 30.63  ? 68  ASP A N   1 
ATOM   540  C  CA  . ASP A 1 68  ? -23.421 -17.643 -2.946  1.00 30.95  ? 68  ASP A CA  1 
ATOM   541  C  C   . ASP A 1 68  ? -22.598 -18.408 -1.916  1.00 31.40  ? 68  ASP A C   1 
ATOM   542  O  O   . ASP A 1 68  ? -21.871 -19.349 -2.251  1.00 31.09  ? 68  ASP A O   1 
ATOM   543  C  CB  . ASP A 1 68  ? -24.913 -18.017 -2.861  1.00 30.23  ? 68  ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 68  ? -25.546 -17.716 -1.504  1.00 35.10  ? 68  ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 68  ? -25.093 -16.800 -0.772  1.00 34.02  ? 68  ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 68  ? -26.534 -18.406 -1.170  1.00 34.43  ? 68  ASP A OD2 1 
ATOM   547  N  N   . LYS A 1 69  ? -22.717 -18.007 -0.651  1.00 30.67  ? 69  LYS A N   1 
ATOM   548  C  CA  . LYS A 1 69  ? -21.976 -18.692 0.406   1.00 31.35  ? 69  LYS A CA  1 
ATOM   549  C  C   . LYS A 1 69  ? -22.426 -20.148 0.545   1.00 30.50  ? 69  LYS A C   1 
ATOM   550  O  O   . LYS A 1 69  ? -23.624 -20.449 0.599   1.00 34.01  ? 69  LYS A O   1 
ATOM   551  C  CB  . LYS A 1 69  ? -22.150 -17.963 1.751   1.00 29.73  ? 69  LYS A CB  1 
ATOM   552  C  CG  . LYS A 1 69  ? -21.811 -18.863 2.955   1.00 29.03  ? 69  LYS A CG  1 
ATOM   553  C  CD  . LYS A 1 69  ? -21.420 -18.055 4.189   1.00 29.75  ? 69  LYS A CD  1 
ATOM   554  C  CE  . LYS A 1 69  ? -21.337 -18.946 5.440   1.00 30.59  ? 69  LYS A CE  1 
ATOM   555  N  NZ  . LYS A 1 69  ? -20.474 -18.345 6.513   1.00 32.06  ? 69  LYS A NZ  1 
ATOM   556  N  N   . ASN A 1 70  ? -21.455 -21.051 0.620   1.00 29.18  ? 70  ASN A N   1 
ATOM   557  C  CA  . ASN A 1 70  ? -21.704 -22.453 0.902   1.00 32.02  ? 70  ASN A CA  1 
ATOM   558  C  C   . ASN A 1 70  ? -21.238 -22.787 2.313   1.00 32.92  ? 70  ASN A C   1 
ATOM   559  O  O   . ASN A 1 70  ? -20.272 -22.206 2.809   1.00 31.94  ? 70  ASN A O   1 
ATOM   560  C  CB  . ASN A 1 70  ? -20.958 -23.340 -0.098  1.00 30.70  ? 70  ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 70  ? -21.181 -24.808 0.163   1.00 36.21  ? 70  ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 70  ? -22.323 -25.254 0.275   1.00 38.27  ? 70  ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 70  ? -20.102 -25.562 0.285   1.00 35.74  ? 70  ASN A ND2 1 
ATOM   564  N  N   . LEU A 1 71  ? -21.921 -23.735 2.962   1.00 35.29  ? 71  LEU A N   1 
ATOM   565  C  CA  . LEU A 1 71  ? -21.437 -24.258 4.240   1.00 32.51  ? 71  LEU A CA  1 
ATOM   566  C  C   . LEU A 1 71  ? -20.420 -25.358 3.942   1.00 33.84  ? 71  LEU A C   1 
ATOM   567  O  O   . LEU A 1 71  ? -20.757 -26.400 3.368   1.00 35.29  ? 71  LEU A O   1 
ATOM   568  C  CB  . LEU A 1 71  ? -22.579 -24.768 5.119   1.00 32.97  ? 71  LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 71  ? -23.670 -23.787 5.542   1.00 33.42  ? 71  LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 71  ? -24.614 -24.402 6.593   1.00 37.28  ? 71  LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 71  ? -23.114 -22.413 6.023   1.00 32.38  ? 71  LEU A CD2 1 
ATOM   572  N  N   . SER A 1 72  ? -19.159 -25.101 4.278   1.00 33.95  ? 72  SER A N   1 
ATOM   573  C  CA  . SER A 1 72  ? -18.156 -26.148 4.234   1.00 34.61  ? 72  SER A CA  1 
ATOM   574  C  C   . SER A 1 72  ? -18.540 -27.255 5.208   1.00 36.72  ? 72  SER A C   1 
ATOM   575  O  O   . SER A 1 72  ? -19.398 -27.081 6.074   1.00 35.32  ? 72  SER A O   1 
ATOM   576  C  CB  . SER A 1 72  ? -16.796 -25.579 4.603   1.00 34.05  ? 72  SER A CB  1 
ATOM   577  O  OG  . SER A 1 72  ? -16.897 -24.929 5.864   1.00 36.40  ? 72  SER A OG  1 
ATOM   578  N  N   . GLN A 1 73  ? -17.894 -28.413 5.063   1.00 37.11  ? 73  GLN A N   1 
ATOM   579  C  CA  . GLN A 1 73  ? -18.096 -29.454 6.068   1.00 37.98  ? 73  GLN A CA  1 
ATOM   580  C  C   . GLN A 1 73  ? -17.794 -28.922 7.460   1.00 36.23  ? 73  GLN A C   1 
ATOM   581  O  O   . GLN A 1 73  ? -18.517 -29.218 8.419   1.00 39.11  ? 73  GLN A O   1 
ATOM   582  C  CB  . GLN A 1 73  ? -17.234 -30.679 5.769   1.00 38.46  ? 73  GLN A CB  1 
ATOM   583  C  CG  . GLN A 1 73  ? -17.734 -31.907 6.546   1.00 41.80  ? 73  GLN A CG  1 
ATOM   584  C  CD  . GLN A 1 73  ? -19.193 -32.183 6.253   1.00 45.48  ? 73  GLN A CD  1 
ATOM   585  O  OE1 . GLN A 1 73  ? -19.589 -32.281 5.094   1.00 49.77  ? 73  GLN A OE1 1 
ATOM   586  N  NE2 . GLN A 1 73  ? -20.014 -32.247 7.299   1.00 46.67  ? 73  GLN A NE2 1 
ATOM   587  N  N   . ALA A 1 74  ? -16.734 -28.121 7.584   1.00 36.71  ? 74  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 74  ? -16.391 -27.520 8.870   1.00 37.30  ? 74  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 74  ? -17.563 -26.727 9.442   1.00 34.15  ? 74  ALA A C   1 
ATOM   590  O  O   . ALA A 1 74  ? -17.937 -26.894 10.612  1.00 35.05  ? 74  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 74  ? -15.162 -26.628 8.704   1.00 35.17  ? 74  ALA A CB  1 
ATOM   592  N  N   . LEU A 1 75  ? -18.166 -25.858 8.631   1.00 34.83  ? 75  LEU A N   1 
ATOM   593  C  CA  . LEU A 1 75  ? -19.301 -25.080 9.126   1.00 34.73  ? 75  LEU A CA  1 
ATOM   594  C  C   . LEU A 1 75  ? -20.534 -25.950 9.363   1.00 34.03  ? 75  LEU A C   1 
ATOM   595  O  O   . LEU A 1 75  ? -21.344 -25.645 10.247  1.00 37.57  ? 75  LEU A O   1 
ATOM   596  C  CB  . LEU A 1 75  ? -19.628 -23.929 8.161   1.00 31.56  ? 75  LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 75  ? -18.650 -22.737 8.116   1.00 35.41  ? 75  LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 75  ? -19.101 -21.684 7.113   1.00 34.91  ? 75  LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 75  ? -18.482 -22.084 9.478   1.00 35.95  ? 75  LEU A CD2 1 
ATOM   600  N  N   . LYS A 1 76  ? -20.708 -27.028 8.596   1.00 34.09  ? 76  LYS A N   1 
ATOM   601  C  CA  . LYS A 1 76  ? -21.829 -27.923 8.879   1.00 37.81  ? 76  LYS A CA  1 
ATOM   602  C  C   . LYS A 1 76  ? -21.694 -28.562 10.263  1.00 38.60  ? 76  LYS A C   1 
ATOM   603  O  O   . LYS A 1 76  ? -22.681 -28.705 10.999  1.00 35.81  ? 76  LYS A O   1 
ATOM   604  C  CB  . LYS A 1 76  ? -21.921 -28.981 7.787   1.00 40.24  ? 76  LYS A CB  1 
ATOM   605  C  CG  . LYS A 1 76  ? -22.541 -28.429 6.532   1.00 37.70  ? 76  LYS A CG  1 
ATOM   606  C  CD  . LYS A 1 76  ? -22.651 -29.458 5.452   1.00 45.51  ? 76  LYS A CD  1 
ATOM   607  C  CE  . LYS A 1 76  ? -23.418 -28.875 4.278   1.00 46.41  ? 76  LYS A CE  1 
ATOM   608  N  NZ  . LYS A 1 76  ? -22.803 -29.334 3.025   1.00 46.67  ? 76  LYS A NZ  1 
ATOM   609  N  N   . PHE A 1 77  ? -20.473 -28.932 10.653  1.00 40.02  ? 77  PHE A N   1 
ATOM   610  C  CA  . PHE A 1 77  ? -20.314 -29.544 11.965  1.00 38.26  ? 77  PHE A CA  1 
ATOM   611  C  C   . PHE A 1 77  ? -20.408 -28.501 13.071  1.00 40.19  ? 77  PHE A C   1 
ATOM   612  O  O   . PHE A 1 77  ? -20.953 -28.778 14.147  1.00 40.67  ? 77  PHE A O   1 
ATOM   613  C  CB  . PHE A 1 77  ? -18.990 -30.302 12.028  1.00 37.89  ? 77  PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 77  ? -18.971 -31.572 11.216  1.00 43.66  ? 77  PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 77  ? -20.114 -32.353 11.084  1.00 43.46  ? 77  PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 77  ? -17.796 -31.998 10.602  1.00 44.22  ? 77  PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 77  ? -20.092 -33.529 10.334  1.00 45.56  ? 77  PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 77  ? -17.765 -33.171 9.850   1.00 47.99  ? 77  PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 77  ? -18.913 -33.938 9.722   1.00 49.85  ? 77  PHE A CZ  1 
ATOM   620  N  N   . VAL A 1 78  ? -19.892 -27.290 12.832  1.00 37.55  ? 78  VAL A N   1 
ATOM   621  C  CA  . VAL A 1 78  ? -20.064 -26.225 13.822  1.00 32.82  ? 78  VAL A CA  1 
ATOM   622  C  C   . VAL A 1 78  ? -21.532 -25.862 13.985  1.00 34.43  ? 78  VAL A C   1 
ATOM   623  O  O   . VAL A 1 78  ? -21.970 -25.466 15.075  1.00 35.95  ? 78  VAL A O   1 
ATOM   624  C  CB  . VAL A 1 78  ? -19.233 -24.988 13.450  1.00 37.09  ? 78  VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 78  ? -19.551 -23.841 14.427  1.00 35.08  ? 78  VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 78  ? -17.742 -25.321 13.495  1.00 34.52  ? 78  VAL A CG2 1 
ATOM   627  N  N   . ARG A 1 79  ? -22.308 -25.965 12.914  1.00 33.77  ? 79  ARG A N   1 
ATOM   628  C  CA  . ARG A 1 79  ? -23.739 -25.704 13.009  1.00 35.23  ? 79  ARG A CA  1 
ATOM   629  C  C   . ARG A 1 79  ? -24.414 -26.580 14.068  1.00 39.13  ? 79  ARG A C   1 
ATOM   630  O  O   . ARG A 1 79  ? -25.459 -26.197 14.611  1.00 38.77  ? 79  ARG A O   1 
ATOM   631  C  CB  . ARG A 1 79  ? -24.369 -25.926 11.635  1.00 36.16  ? 79  ARG A CB  1 
ATOM   632  C  CG  . ARG A 1 79  ? -25.862 -25.664 11.591  1.00 41.21  ? 79  ARG A CG  1 
ATOM   633  C  CD  . ARG A 1 79  ? -26.328 -25.431 10.152  1.00 42.01  ? 79  ARG A CD  1 
ATOM   634  N  NE  . ARG A 1 79  ? -27.781 -25.509 10.061  1.00 42.33  ? 79  ARG A NE  1 
ATOM   635  C  CZ  . ARG A 1 79  ? -28.530 -24.582 9.486   1.00 42.98  ? 79  ARG A CZ  1 
ATOM   636  N  NH1 . ARG A 1 79  ? -27.990 -23.526 8.905   1.00 37.80  ? 79  ARG A NH1 1 
ATOM   637  N  NH2 . ARG A 1 79  ? -29.855 -24.698 9.527   1.00 43.74  ? 79  ARG A NH2 1 
ATOM   638  N  N   . ASP A 1 80  ? -23.838 -27.748 14.375  1.00 41.48  ? 80  ASP A N   1 
ATOM   639  C  CA  . ASP A 1 80  ? -24.399 -28.598 15.421  1.00 42.47  ? 80  ASP A CA  1 
ATOM   640  C  C   . ASP A 1 80  ? -24.542 -27.854 16.744  1.00 45.13  ? 80  ASP A C   1 
ATOM   641  O  O   . ASP A 1 80  ? -25.387 -28.225 17.568  1.00 44.36  ? 80  ASP A O   1 
ATOM   642  C  CB  . ASP A 1 80  ? -23.541 -29.847 15.599  1.00 41.35  ? 80  ASP A CB  1 
ATOM   643  C  CG  . ASP A 1 80  ? -23.823 -30.901 14.549  1.00 46.44  ? 80  ASP A CG  1 
ATOM   644  O  OD1 . ASP A 1 80  ? -24.941 -30.904 13.993  1.00 47.74  ? 80  ASP A OD1 1 
ATOM   645  O  OD2 . ASP A 1 80  ? -22.910 -31.706 14.263  1.00 55.48  ? 80  ASP A OD2 1 
ATOM   646  N  N   . PHE A 1 81  ? -23.724 -26.822 16.988  1.00 41.17  ? 81  PHE A N   1 
ATOM   647  C  CA  . PHE A 1 81  ? -23.934 -25.988 18.162  1.00 38.97  ? 81  PHE A CA  1 
ATOM   648  C  C   . PHE A 1 81  ? -24.121 -24.505 17.866  1.00 40.99  ? 81  PHE A C   1 
ATOM   649  O  O   . PHE A 1 81  ? -24.646 -23.789 18.734  1.00 35.82  ? 81  PHE A O   1 
ATOM   650  C  CB  . PHE A 1 81  ? -22.795 -26.166 19.196  1.00 38.11  ? 81  PHE A CB  1 
ATOM   651  C  CG  . PHE A 1 81  ? -21.393 -26.096 18.631  1.00 37.57  ? 81  PHE A CG  1 
ATOM   652  C  CD1 . PHE A 1 81  ? -20.818 -27.206 18.020  1.00 38.92  ? 81  PHE A CD1 1 
ATOM   653  C  CD2 . PHE A 1 81  ? -20.625 -24.945 18.767  1.00 37.60  ? 81  PHE A CD2 1 
ATOM   654  C  CE1 . PHE A 1 81  ? -19.517 -27.147 17.517  1.00 38.95  ? 81  PHE A CE1 1 
ATOM   655  C  CE2 . PHE A 1 81  ? -19.310 -24.892 18.268  1.00 35.09  ? 81  PHE A CE2 1 
ATOM   656  C  CZ  . PHE A 1 81  ? -18.770 -25.994 17.641  1.00 37.60  ? 81  PHE A CZ  1 
ATOM   657  N  N   . ALA A 1 82  ? -23.731 -24.018 16.680  1.00 38.03  ? 82  ALA A N   1 
ATOM   658  C  CA  . ALA A 1 82  ? -24.013 -22.624 16.339  1.00 36.69  ? 82  ALA A CA  1 
ATOM   659  C  C   . ALA A 1 82  ? -25.334 -22.446 15.590  1.00 38.29  ? 82  ALA A C   1 
ATOM   660  O  O   . ALA A 1 82  ? -25.724 -21.305 15.319  1.00 36.73  ? 82  ALA A O   1 
ATOM   661  C  CB  . ALA A 1 82  ? -22.866 -22.022 15.519  1.00 35.01  ? 82  ALA A CB  1 
ATOM   662  N  N   . GLY A 1 83  ? -26.019 -23.539 15.251  1.00 38.99  ? 83  GLY A N   1 
ATOM   663  C  CA  . GLY A 1 83  ? -27.380 -23.463 14.733  1.00 42.67  ? 83  GLY A CA  1 
ATOM   664  C  C   . GLY A 1 83  ? -27.481 -22.619 13.478  1.00 39.26  ? 83  GLY A C   1 
ATOM   665  O  O   . GLY A 1 83  ? -26.596 -22.636 12.607  1.00 34.44  ? 83  GLY A O   1 
ATOM   666  N  N   . ASP A 1 84  ? -28.583 -21.875 13.372  1.00 36.82  ? 84  ASP A N   1 
ATOM   667  C  CA  . ASP A 1 84  ? -28.751 -20.905 12.286  1.00 36.85  ? 84  ASP A CA  1 
ATOM   668  C  C   . ASP A 1 84  ? -28.401 -19.490 12.742  1.00 35.06  ? 84  ASP A C   1 
ATOM   669  O  O   . ASP A 1 84  ? -29.059 -18.507 12.384  1.00 34.93  ? 84  ASP A O   1 
ATOM   670  C  CB  . ASP A 1 84  ? -30.163 -20.975 11.696  1.00 37.80  ? 84  ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 84  ? -31.249 -20.696 12.712  1.00 37.37  ? 84  ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 84  ? -30.939 -20.561 13.912  1.00 36.99  ? 84  ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 84  ? -32.427 -20.624 12.307  1.00 33.15  ? 84  ASP A OD2 1 
ATOM   674  N  N   . GLY A 1 85  ? -27.340 -19.361 13.540  1.00 35.38  ? 85  GLY A N   1 
ATOM   675  C  CA  . GLY A 1 85  ? -26.726 -18.069 13.764  1.00 33.83  ? 85  GLY A CA  1 
ATOM   676  C  C   . GLY A 1 85  ? -26.116 -17.558 12.472  1.00 32.66  ? 85  GLY A C   1 
ATOM   677  O  O   . GLY A 1 85  ? -26.140 -18.256 11.446  1.00 34.45  ? 85  GLY A O   1 
ATOM   678  N  N   . LEU A 1 86  ? -25.565 -16.345 12.503  1.00 33.05  ? 86  LEU A N   1 
ATOM   679  C  CA  . LEU A 1 86  ? -25.248 -15.657 11.250  1.00 34.77  ? 86  LEU A CA  1 
ATOM   680  C  C   . LEU A 1 86  ? -24.228 -16.423 10.429  1.00 35.26  ? 86  LEU A C   1 
ATOM   681  O  O   . LEU A 1 86  ? -24.301 -16.421 9.195   1.00 35.40  ? 86  LEU A O   1 
ATOM   682  C  CB  . LEU A 1 86  ? -24.738 -14.238 11.521  1.00 28.83  ? 86  LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 86  ? -25.826 -13.196 11.791  1.00 33.25  ? 86  LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 86  ? -25.192 -11.922 12.308  1.00 35.17  ? 86  LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 86  ? -26.593 -12.930 10.487  1.00 30.34  ? 86  LEU A CD2 1 
ATOM   686  N  N   . ALA A 1 87  ? -23.248 -17.066 11.086  1.00 34.27  ? 87  ALA A N   1 
ATOM   687  C  CA  . ALA A 1 87  ? -22.115 -17.631 10.349  1.00 31.46  ? 87  ALA A CA  1 
ATOM   688  C  C   . ALA A 1 87  ? -22.382 -19.033 9.804   1.00 34.21  ? 87  ALA A C   1 
ATOM   689  O  O   . ALA A 1 87  ? -21.693 -19.466 8.876   1.00 32.61  ? 87  ALA A O   1 
ATOM   690  C  CB  . ALA A 1 87  ? -20.863 -17.664 11.237  1.00 34.16  ? 87  ALA A CB  1 
ATOM   691  N  N   . THR A 1 88  ? -23.363 -19.748 10.346  1.00 31.17  ? 88  THR A N   1 
ATOM   692  C  CA  . THR A 1 88  ? -23.628 -21.115 9.934   1.00 31.16  ? 88  THR A CA  1 
ATOM   693  C  C   . THR A 1 88  ? -24.999 -21.250 9.282   1.00 34.34  ? 88  THR A C   1 
ATOM   694  O  O   . THR A 1 88  ? -25.473 -22.367 9.088   1.00 34.37  ? 88  THR A O   1 
ATOM   695  C  CB  . THR A 1 88  ? -23.502 -22.071 11.130  1.00 33.58  ? 88  THR A CB  1 
ATOM   696  O  OG1 . THR A 1 88  ? -24.225 -21.541 12.245  1.00 32.57  ? 88  THR A OG1 1 
ATOM   697  C  CG2 . THR A 1 88  ? -22.031 -22.212 11.540  1.00 30.81  ? 88  THR A CG2 1 
ATOM   698  N  N   . SER A 1 89  ? -25.640 -20.152 8.923   1.00 30.81  ? 89  SER A N   1 
ATOM   699  C  CA  . SER A 1 89  ? -26.892 -20.241 8.184   1.00 35.96  ? 89  SER A CA  1 
ATOM   700  C  C   . SER A 1 89  ? -26.670 -19.974 6.691   1.00 37.01  ? 89  SER A C   1 
ATOM   701  O  O   . SER A 1 89  ? -25.699 -19.317 6.294   1.00 31.11  ? 89  SER A O   1 
ATOM   702  C  CB  . SER A 1 89  ? -27.922 -19.281 8.787   1.00 34.58  ? 89  SER A CB  1 
ATOM   703  O  OG  . SER A 1 89  ? -27.386 -17.977 8.879   1.00 40.49  ? 89  SER A OG  1 
ATOM   704  N  N   . TRP A 1 90  ? -27.542 -20.560 5.866   1.00 34.87  ? 90  TRP A N   1 
ATOM   705  C  CA  . TRP A 1 90  ? -27.554 -20.315 4.429   1.00 33.78  ? 90  TRP A CA  1 
ATOM   706  C  C   . TRP A 1 90  ? -28.205 -18.961 4.172   1.00 32.53  ? 90  TRP A C   1 
ATOM   707  O  O   . TRP A 1 90  ? -29.089 -18.527 4.917   1.00 33.86  ? 90  TRP A O   1 
ATOM   708  C  CB  . TRP A 1 90  ? -28.349 -21.397 3.676   1.00 33.63  ? 90  TRP A CB  1 
ATOM   709  C  CG  . TRP A 1 90  ? -27.815 -22.800 3.872   1.00 36.97  ? 90  TRP A CG  1 
ATOM   710  C  CD1 . TRP A 1 90  ? -28.199 -23.683 4.840   1.00 32.86  ? 90  TRP A CD1 1 
ATOM   711  C  CD2 . TRP A 1 90  ? -26.832 -23.485 3.074   1.00 34.91  ? 90  TRP A CD2 1 
ATOM   712  N  NE1 . TRP A 1 90  ? -27.504 -24.862 4.714   1.00 34.70  ? 90  TRP A NE1 1 
ATOM   713  C  CE2 . TRP A 1 90  ? -26.659 -24.769 3.639   1.00 33.88  ? 90  TRP A CE2 1 
ATOM   714  C  CE3 . TRP A 1 90  ? -26.076 -23.134 1.952   1.00 33.92  ? 90  TRP A CE3 1 
ATOM   715  C  CZ2 . TRP A 1 90  ? -25.752 -25.702 3.127   1.00 35.44  ? 90  TRP A CZ2 1 
ATOM   716  C  CZ3 . TRP A 1 90  ? -25.174 -24.074 1.430   1.00 34.38  ? 90  TRP A CZ3 1 
ATOM   717  C  CH2 . TRP A 1 90  ? -25.018 -25.338 2.024   1.00 35.62  ? 90  TRP A CH2 1 
ATOM   718  N  N   . THR A 1 91  ? -27.781 -18.312 3.088   1.00 32.31  ? 91  THR A N   1 
ATOM   719  C  CA  . THR A 1 91  ? -28.299 -16.991 2.759   1.00 33.43  ? 91  THR A CA  1 
ATOM   720  C  C   . THR A 1 91  ? -29.814 -17.005 2.593   1.00 31.64  ? 91  THR A C   1 
ATOM   721  O  O   . THR A 1 91  ? -30.465 -15.985 2.841   1.00 32.60  ? 91  THR A O   1 
ATOM   722  C  CB  . THR A 1 91  ? -27.629 -16.476 1.480   1.00 32.07  ? 91  THR A CB  1 
ATOM   723  O  OG1 . THR A 1 91  ? -26.198 -16.553 1.631   1.00 31.44  ? 91  THR A OG1 1 
ATOM   724  C  CG2 . THR A 1 91  ? -28.025 -15.039 1.198   1.00 33.67  ? 91  THR A CG2 1 
ATOM   725  N  N   . HIS A 1 92  ? -30.392 -18.144 2.180   1.00 31.05  ? 92  HIS A N   1 
ATOM   726  C  CA  . HIS A 1 92  ? -31.823 -18.224 1.887   1.00 33.39  ? 92  HIS A CA  1 
ATOM   727  C  C   . HIS A 1 92  ? -32.656 -18.639 3.090   1.00 33.55  ? 92  HIS A C   1 
ATOM   728  O  O   . HIS A 1 92  ? -33.893 -18.622 3.005   1.00 36.21  ? 92  HIS A O   1 
ATOM   729  C  CB  . HIS A 1 92  ? -32.075 -19.200 0.738   1.00 33.29  ? 92  HIS A CB  1 
ATOM   730  C  CG  . HIS A 1 92  ? -31.347 -20.500 0.887   1.00 32.55  ? 92  HIS A CG  1 
ATOM   731  N  ND1 . HIS A 1 92  ? -31.750 -21.481 1.770   1.00 35.32  ? 92  HIS A ND1 1 
ATOM   732  C  CD2 . HIS A 1 92  ? -30.230 -20.973 0.280   1.00 31.23  ? 92  HIS A CD2 1 
ATOM   733  C  CE1 . HIS A 1 92  ? -30.924 -22.511 1.684   1.00 32.50  ? 92  HIS A CE1 1 
ATOM   734  N  NE2 . HIS A 1 92  ? -29.989 -22.224 0.796   1.00 31.06  ? 92  HIS A NE2 1 
ATOM   735  N  N   . GLU A 1 93  ? -32.030 -19.012 4.205   1.00 33.10  ? 93  GLU A N   1 
ATOM   736  C  CA  . GLU A 1 93  ? -32.799 -19.254 5.416   1.00 34.73  ? 93  GLU A CA  1 
ATOM   737  C  C   . GLU A 1 93  ? -33.293 -17.926 5.974   1.00 37.71  ? 93  GLU A C   1 
ATOM   738  O  O   . GLU A 1 93  ? -32.539 -16.949 6.059   1.00 37.45  ? 93  GLU A O   1 
ATOM   739  C  CB  . GLU A 1 93  ? -31.961 -19.967 6.481   1.00 34.35  ? 93  GLU A CB  1 
ATOM   740  C  CG  . GLU A 1 93  ? -31.638 -21.420 6.181   1.00 34.35  ? 93  GLU A CG  1 
ATOM   741  C  CD  . GLU A 1 93  ? -30.831 -22.058 7.292   1.00 38.07  ? 93  GLU A CD  1 
ATOM   742  O  OE1 . GLU A 1 93  ? -29.603 -21.833 7.340   1.00 38.52  ? 93  GLU A OE1 1 
ATOM   743  O  OE2 . GLU A 1 93  ? -31.429 -22.780 8.123   1.00 37.60  ? 93  GLU A OE2 1 
ATOM   744  N  N   . LYS A 1 94  ? -34.566 -17.899 6.372   1.00 36.10  ? 94  LYS A N   1 
ATOM   745  C  CA  . LYS A 1 94  ? -35.183 -16.652 6.811   1.00 32.11  ? 94  LYS A CA  1 
ATOM   746  C  C   . LYS A 1 94  ? -34.400 -16.002 7.950   1.00 31.92  ? 94  LYS A C   1 
ATOM   747  O  O   . LYS A 1 94  ? -34.323 -14.770 8.022   1.00 34.44  ? 94  LYS A O   1 
ATOM   748  C  CB  . LYS A 1 94  ? -36.637 -16.913 7.234   1.00 36.16  ? 94  LYS A CB  1 
ATOM   749  C  CG  . LYS A 1 94  ? -37.349 -15.752 7.923   1.00 43.09  ? 94  LYS A CG  1 
ATOM   750  C  CD  . LYS A 1 94  ? -38.597 -16.253 8.684   1.00 44.25  ? 94  LYS A CD  1 
ATOM   751  C  CE  . LYS A 1 94  ? -39.580 -15.141 8.975   1.00 49.91  ? 94  LYS A CE  1 
ATOM   752  N  NZ  . LYS A 1 94  ? -40.912 -15.665 9.433   1.00 48.34  ? 94  LYS A NZ  1 
ATOM   753  N  N   . ASN A 1 95  ? -33.800 -16.801 8.835   1.00 32.68  ? 95  ASN A N   1 
ATOM   754  C  CA  . ASN A 1 95  ? -33.115 -16.221 9.990   1.00 33.30  ? 95  ASN A CA  1 
ATOM   755  C  C   . ASN A 1 95  ? -31.784 -15.562 9.616   1.00 32.88  ? 95  ASN A C   1 
ATOM   756  O  O   . ASN A 1 95  ? -31.249 -14.791 10.419  1.00 35.70  ? 95  ASN A O   1 
ATOM   757  C  CB  . ASN A 1 95  ? -32.873 -17.286 11.061  1.00 32.78  ? 95  ASN A CB  1 
ATOM   758  C  CG  . ASN A 1 95  ? -34.011 -17.393 12.069  1.00 39.79  ? 95  ASN A CG  1 
ATOM   759  O  OD1 . ASN A 1 95  ? -34.781 -16.453 12.267  1.00 40.05  ? 95  ASN A OD1 1 
ATOM   760  N  ND2 . ASN A 1 95  ? -34.096 -18.541 12.737  1.00 39.21  ? 95  ASN A ND2 1 
ATOM   761  N  N   . TRP A 1 96  ? -31.230 -15.832 8.430   1.00 32.38  ? 96  TRP A N   1 
ATOM   762  C  CA  . TRP A 1 96  ? -30.004 -15.117 8.068   1.00 33.72  ? 96  TRP A CA  1 
ATOM   763  C  C   . TRP A 1 96  ? -30.278 -13.630 7.835   1.00 34.52  ? 96  TRP A C   1 
ATOM   764  O  O   . TRP A 1 96  ? -29.767 -12.769 8.560   1.00 32.21  ? 96  TRP A O   1 
ATOM   765  C  CB  . TRP A 1 96  ? -29.306 -15.713 6.838   1.00 31.33  ? 96  TRP A CB  1 
ATOM   766  C  CG  . TRP A 1 96  ? -28.098 -14.830 6.629   1.00 34.34  ? 96  TRP A CG  1 
ATOM   767  C  CD1 . TRP A 1 96  ? -26.963 -14.794 7.415   1.00 33.49  ? 96  TRP A CD1 1 
ATOM   768  C  CD2 . TRP A 1 96  ? -27.961 -13.770 5.687   1.00 35.35  ? 96  TRP A CD2 1 
ATOM   769  N  NE1 . TRP A 1 96  ? -26.117 -13.797 6.986   1.00 29.84  ? 96  TRP A NE1 1 
ATOM   770  C  CE2 . TRP A 1 96  ? -26.702 -13.152 5.927   1.00 33.50  ? 96  TRP A CE2 1 
ATOM   771  C  CE3 . TRP A 1 96  ? -28.771 -13.279 4.650   1.00 34.97  ? 96  TRP A CE3 1 
ATOM   772  C  CZ2 . TRP A 1 96  ? -26.241 -12.082 5.170   1.00 34.48  ? 96  TRP A CZ2 1 
ATOM   773  C  CZ3 . TRP A 1 96  ? -28.303 -12.207 3.891   1.00 33.20  ? 96  TRP A CZ3 1 
ATOM   774  C  CH2 . TRP A 1 96  ? -27.043 -11.628 4.155   1.00 34.97  ? 96  TRP A CH2 1 
ATOM   775  N  N   . LYS A 1 97  ? -31.073 -13.301 6.816   1.00 33.61  ? 97  LYS A N   1 
ATOM   776  C  CA  . LYS A 1 97  ? -31.295 -11.892 6.506   1.00 34.04  ? 97  LYS A CA  1 
ATOM   777  C  C   . LYS A 1 97  ? -31.965 -11.163 7.662   1.00 35.87  ? 97  LYS A C   1 
ATOM   778  O  O   . LYS A 1 97  ? -31.715 -9.970  7.879   1.00 33.97  ? 97  LYS A O   1 
ATOM   779  C  CB  . LYS A 1 97  ? -32.134 -11.754 5.232   1.00 40.30  ? 97  LYS A CB  1 
ATOM   780  C  CG  . LYS A 1 97  ? -32.296 -10.310 4.743   1.00 42.75  ? 97  LYS A CG  1 
ATOM   781  C  CD  . LYS A 1 97  ? -30.979 -9.729  4.263   1.00 42.78  ? 97  LYS A CD  1 
ATOM   782  C  CE  . LYS A 1 97  ? -31.195 -8.338  3.698   1.00 48.71  ? 97  LYS A CE  1 
ATOM   783  N  NZ  . LYS A 1 97  ? -29.938 -7.792  3.141   1.00 57.73  ? 97  LYS A NZ  1 
ATOM   784  N  N   . LYS A 1 98  ? -32.817 -11.856 8.416   1.00 35.06  ? 98  LYS A N   1 
ATOM   785  C  CA  . LYS A 1 98  ? -33.492 -11.219 9.544   1.00 34.42  ? 98  LYS A CA  1 
ATOM   786  C  C   . LYS A 1 98  ? -32.495 -10.843 10.641  1.00 34.87  ? 98  LYS A C   1 
ATOM   787  O  O   . LYS A 1 98  ? -32.438 -9.688  11.075  1.00 33.26  ? 98  LYS A O   1 
ATOM   788  C  CB  . LYS A 1 98  ? -34.569 -12.163 10.062  1.00 38.52  ? 98  LYS A CB  1 
ATOM   789  C  CG  . LYS A 1 98  ? -35.330 -11.734 11.276  1.00 40.75  ? 98  LYS A CG  1 
ATOM   790  C  CD  . LYS A 1 98  ? -36.343 -12.857 11.573  1.00 47.45  ? 98  LYS A CD  1 
ATOM   791  C  CE  . LYS A 1 98  ? -37.041 -12.708 12.904  1.00 43.27  ? 98  LYS A CE  1 
ATOM   792  N  NZ  . LYS A 1 98  ? -38.051 -13.801 13.034  1.00 41.04  ? 98  LYS A NZ  1 
ATOM   793  N  N   . ALA A 1 99  ? -31.693 -11.802 11.099  1.00 34.43  ? 99  ALA A N   1 
ATOM   794  C  CA  . ALA A 1 99  ? -30.654 -11.474 12.071  1.00 35.86  ? 99  ALA A CA  1 
ATOM   795  C  C   . ALA A 1 99  ? -29.664 -10.461 11.507  1.00 33.39  ? 99  ALA A C   1 
ATOM   796  O  O   . ALA A 1 99  ? -29.167 -9.593  12.233  1.00 35.06  ? 99  ALA A O   1 
ATOM   797  C  CB  . ALA A 1 99  ? -29.921 -12.746 12.518  1.00 32.38  ? 99  ALA A CB  1 
ATOM   798  N  N   . HIS A 1 100 ? -29.332 -10.585 10.219  1.00 36.67  ? 100 HIS A N   1 
ATOM   799  C  CA  . HIS A 1 100 ? -28.440 -9.625  9.576   1.00 37.65  ? 100 HIS A CA  1 
ATOM   800  C  C   . HIS A 1 100 ? -28.985 -8.205  9.688   1.00 39.17  ? 100 HIS A C   1 
ATOM   801  O  O   . HIS A 1 100 ? -28.288 -7.297  10.149  1.00 36.48  ? 100 HIS A O   1 
ATOM   802  C  CB  . HIS A 1 100 ? -28.238 -10.023 8.113   1.00 37.25  ? 100 HIS A CB  1 
ATOM   803  C  CG  . HIS A 1 100 ? -27.398 -9.070  7.323   1.00 36.54  ? 100 HIS A CG  1 
ATOM   804  N  ND1 . HIS A 1 100 ? -26.019 -9.063  7.384   1.00 42.44  ? 100 HIS A ND1 1 
ATOM   805  C  CD2 . HIS A 1 100 ? -27.739 -8.131  6.407   1.00 42.91  ? 100 HIS A CD2 1 
ATOM   806  C  CE1 . HIS A 1 100 ? -25.549 -8.144  6.558   1.00 41.40  ? 100 HIS A CE1 1 
ATOM   807  N  NE2 . HIS A 1 100 ? -26.571 -7.570  5.947   1.00 47.98  ? 100 HIS A NE2 1 
ATOM   808  N  N   . ASN A 1 101 ? -30.240 -7.998  9.275   1.00 37.11  ? 101 ASN A N   1 
ATOM   809  C  CA  . ASN A 1 101 ? -30.857 -6.676  9.371   1.00 37.08  ? 101 ASN A CA  1 
ATOM   810  C  C   . ASN A 1 101 ? -30.878 -6.177  10.810  1.00 33.46  ? 101 ASN A C   1 
ATOM   811  O  O   . ASN A 1 101 ? -30.630 -4.993  11.065  1.00 38.29  ? 101 ASN A O   1 
ATOM   812  C  CB  . ASN A 1 101 ? -32.287 -6.711  8.815   1.00 39.36  ? 101 ASN A CB  1 
ATOM   813  C  CG  . ASN A 1 101 ? -32.326 -6.862  7.306   1.00 41.26  ? 101 ASN A CG  1 
ATOM   814  O  OD1 . ASN A 1 101 ? -31.329 -6.658  6.624   1.00 41.16  ? 101 ASN A OD1 1 
ATOM   815  N  ND2 . ASN A 1 101 ? -33.493 -7.240  6.777   1.00 41.30  ? 101 ASN A ND2 1 
ATOM   816  N  N   . ILE A 1 102 ? -31.191 -7.056  11.761  1.00 33.79  ? 102 ILE A N   1 
ATOM   817  C  CA  . ILE A 1 102 ? -31.326 -6.616  13.147  1.00 34.93  ? 102 ILE A CA  1 
ATOM   818  C  C   . ILE A 1 102 ? -29.969 -6.225  13.719  1.00 37.60  ? 102 ILE A C   1 
ATOM   819  O  O   . ILE A 1 102 ? -29.856 -5.252  14.469  1.00 36.47  ? 102 ILE A O   1 
ATOM   820  C  CB  . ILE A 1 102 ? -32.006 -7.709  13.991  1.00 33.11  ? 102 ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 102 ? -33.500 -7.805  13.639  1.00 37.81  ? 102 ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 102 ? -31.829 -7.443  15.487  1.00 37.07  ? 102 ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 102 ? -34.129 -9.100  14.087  1.00 36.82  ? 102 ILE A CD1 1 
ATOM   824  N  N   . LEU A 1 103 ? -28.917 -6.954  13.354  1.00 34.75  ? 103 LEU A N   1 
ATOM   825  C  CA  . LEU A 1 103 ? -27.628 -6.815  14.023  1.00 32.11  ? 103 LEU A CA  1 
ATOM   826  C  C   . LEU A 1 103 ? -26.647 -5.874  13.323  1.00 33.95  ? 103 LEU A C   1 
ATOM   827  O  O   . LEU A 1 103 ? -25.718 -5.383  13.975  1.00 33.89  ? 103 LEU A O   1 
ATOM   828  C  CB  . LEU A 1 103 ? -26.996 -8.208  14.194  1.00 33.24  ? 103 LEU A CB  1 
ATOM   829  C  CG  . LEU A 1 103 ? -27.533 -9.071  15.338  1.00 32.66  ? 103 LEU A CG  1 
ATOM   830  C  CD1 . LEU A 1 103 ? -27.212 -10.516 15.103  1.00 36.11  ? 103 LEU A CD1 1 
ATOM   831  C  CD2 . LEU A 1 103 ? -26.942 -8.614  16.695  1.00 31.81  ? 103 LEU A CD2 1 
ATOM   832  N  N   . LEU A 1 104 ? -26.825 -5.591  12.033  1.00 37.80  ? 104 LEU A N   1 
ATOM   833  C  CA  . LEU A 1 104 ? -25.964 -4.628  11.345  1.00 40.14  ? 104 LEU A CA  1 
ATOM   834  C  C   . LEU A 1 104 ? -25.709 -3.358  12.150  1.00 37.97  ? 104 LEU A C   1 
ATOM   835  O  O   . LEU A 1 104 ? -24.536 -2.985  12.314  1.00 36.01  ? 104 LEU A O   1 
ATOM   836  C  CB  . LEU A 1 104 ? -26.580 -4.253  9.989   1.00 33.19  ? 104 LEU A CB  1 
ATOM   837  C  CG  . LEU A 1 104 ? -25.927 -4.823  8.737   1.00 43.19  ? 104 LEU A CG  1 
ATOM   838  C  CD1 . LEU A 1 104 ? -26.486 -4.147  7.477   1.00 44.97  ? 104 LEU A CD1 1 
ATOM   839  C  CD2 . LEU A 1 104 ? -24.420 -4.700  8.830   1.00 40.55  ? 104 LEU A CD2 1 
ATOM   840  N  N   . PRO A 1 105 ? -26.727 -2.665  12.683  1.00 37.95  ? 105 PRO A N   1 
ATOM   841  C  CA  . PRO A 1 105 ? -26.457 -1.430  13.434  1.00 39.61  ? 105 PRO A CA  1 
ATOM   842  C  C   . PRO A 1 105 ? -25.663 -1.656  14.712  1.00 37.89  ? 105 PRO A C   1 
ATOM   843  O  O   . PRO A 1 105 ? -25.073 -0.701  15.230  1.00 38.07  ? 105 PRO A O   1 
ATOM   844  C  CB  . PRO A 1 105 ? -27.864 -0.891  13.741  1.00 40.64  ? 105 PRO A CB  1 
ATOM   845  C  CG  . PRO A 1 105 ? -28.757 -1.582  12.769  1.00 39.59  ? 105 PRO A CG  1 
ATOM   846  C  CD  . PRO A 1 105 ? -28.167 -2.945  12.616  1.00 36.82  ? 105 PRO A CD  1 
ATOM   847  N  N   . SER A 1 106 ? -25.644 -2.876  15.239  1.00 36.45  ? 106 SER A N   1 
ATOM   848  C  CA  . SER A 1 106 ? -24.849 -3.207  16.415  1.00 39.40  ? 106 SER A CA  1 
ATOM   849  C  C   . SER A 1 106 ? -23.362 -3.328  16.105  1.00 36.87  ? 106 SER A C   1 
ATOM   850  O  O   . SER A 1 106 ? -22.550 -3.381  17.032  1.00 38.04  ? 106 SER A O   1 
ATOM   851  C  CB  . SER A 1 106 ? -25.348 -4.525  17.015  1.00 35.64  ? 106 SER A CB  1 
ATOM   852  O  OG  . SER A 1 106 ? -26.604 -4.319  17.607  1.00 45.78  ? 106 SER A OG  1 
ATOM   853  N  N   . PHE A 1 107 ? -22.988 -3.360  14.832  1.00 36.06  ? 107 PHE A N   1 
ATOM   854  C  CA  . PHE A 1 107 ? -21.617 -3.661  14.429  1.00 34.36  ? 107 PHE A CA  1 
ATOM   855  C  C   . PHE A 1 107 ? -21.018 -2.582  13.554  1.00 38.08  ? 107 PHE A C   1 
ATOM   856  O  O   . PHE A 1 107 ? -19.934 -2.791  12.981  1.00 37.78  ? 107 PHE A O   1 
ATOM   857  C  CB  . PHE A 1 107 ? -21.582 -5.009  13.706  1.00 35.98  ? 107 PHE A CB  1 
ATOM   858  C  CG  . PHE A 1 107 ? -21.567 -6.172  14.634  1.00 38.73  ? 107 PHE A CG  1 
ATOM   859  C  CD1 . PHE A 1 107 ? -20.428 -6.464  15.371  1.00 37.17  ? 107 PHE A CD1 1 
ATOM   860  C  CD2 . PHE A 1 107 ? -22.710 -6.923  14.845  1.00 36.77  ? 107 PHE A CD2 1 
ATOM   861  C  CE1 . PHE A 1 107 ? -20.406 -7.525  16.250  1.00 37.64  ? 107 PHE A CE1 1 
ATOM   862  C  CE2 . PHE A 1 107 ? -22.696 -7.992  15.725  1.00 40.89  ? 107 PHE A CE2 1 
ATOM   863  C  CZ  . PHE A 1 107 ? -21.544 -8.290  16.436  1.00 39.11  ? 107 PHE A CZ  1 
ATOM   864  N  N   . SER A 1 108 ? -21.674 -1.430  13.455  1.00 32.79  ? 108 SER A N   1 
ATOM   865  C  CA  . SER A 1 108 ? -21.230 -0.356  12.583  1.00 39.45  ? 108 SER A CA  1 
ATOM   866  C  C   . SER A 1 108 ? -20.088 0.417   13.225  1.00 43.52  ? 108 SER A C   1 
ATOM   867  O  O   . SER A 1 108 ? -19.850 0.343   14.435  1.00 40.22  ? 108 SER A O   1 
ATOM   868  C  CB  . SER A 1 108 ? -22.366 0.618   12.298  1.00 36.39  ? 108 SER A CB  1 
ATOM   869  O  OG  . SER A 1 108 ? -22.685 1.318   13.486  1.00 40.67  ? 108 SER A OG  1 
ATOM   870  N  N   . GLN A 1 109 ? -19.387 1.190   12.396  1.00 42.27  ? 109 GLN A N   1 
ATOM   871  C  CA  . GLN A 1 109 ? -18.362 2.067   12.941  1.00 45.80  ? 109 GLN A CA  1 
ATOM   872  C  C   . GLN A 1 109 ? -18.935 2.932   14.058  1.00 40.96  ? 109 GLN A C   1 
ATOM   873  O  O   . GLN A 1 109 ? -18.304 3.097   15.110  1.00 47.70  ? 109 GLN A O   1 
ATOM   874  C  CB  . GLN A 1 109 ? -17.748 2.921   11.831  1.00 45.35  ? 109 GLN A CB  1 
ATOM   875  C  CG  . GLN A 1 109 ? -16.486 3.639   12.272  1.00 47.12  ? 109 GLN A CG  1 
ATOM   876  C  CD  . GLN A 1 109 ? -15.474 2.699   12.935  1.00 48.78  ? 109 GLN A CD  1 
ATOM   877  O  OE1 . GLN A 1 109 ? -14.902 3.027   13.975  1.00 49.13  ? 109 GLN A OE1 1 
ATOM   878  N  NE2 . GLN A 1 109 ? -15.239 1.534   12.323  1.00 46.70  ? 109 GLN A NE2 1 
ATOM   879  N  N   . GLN A 1 110 ? -20.157 3.442   13.878  1.00 44.12  ? 110 GLN A N   1 
ATOM   880  C  CA  . GLN A 1 110 ? -20.770 4.262   14.924  1.00 42.49  ? 110 GLN A CA  1 
ATOM   881  C  C   . GLN A 1 110 ? -20.994 3.486   16.219  1.00 48.62  ? 110 GLN A C   1 
ATOM   882  O  O   . GLN A 1 110 ? -20.862 4.057   17.310  1.00 46.41  ? 110 GLN A O   1 
ATOM   883  C  CB  . GLN A 1 110 ? -22.091 4.864   14.445  1.00 47.92  ? 110 GLN A CB  1 
ATOM   884  C  CG  . GLN A 1 110 ? -22.896 5.441   15.600  1.00 53.55  ? 110 GLN A CG  1 
ATOM   885  C  CD  . GLN A 1 110 ? -22.492 6.872   15.944  1.00 54.20  ? 110 GLN A CD  1 
ATOM   886  O  OE1 . GLN A 1 110 ? -21.601 7.457   15.307  1.00 46.96  ? 110 GLN A OE1 1 
ATOM   887  N  NE2 . GLN A 1 110 ? -23.101 7.418   16.994  1.00 48.71  ? 110 GLN A NE2 1 
ATOM   888  N  N   . ALA A 1 111 ? -21.378 2.200   16.131  1.00 43.63  ? 111 ALA A N   1 
ATOM   889  C  CA  . ALA A 1 111 ? -21.624 1.438   17.357  1.00 41.17  ? 111 ALA A CA  1 
ATOM   890  C  C   . ALA A 1 111 ? -20.332 1.184   18.116  1.00 39.08  ? 111 ALA A C   1 
ATOM   891  O  O   . ALA A 1 111 ? -20.360 0.840   19.307  1.00 39.51  ? 111 ALA A O   1 
ATOM   892  C  CB  . ALA A 1 111 ? -22.311 0.105   17.041  1.00 37.19  ? 111 ALA A CB  1 
ATOM   893  N  N   . MET A 1 112 ? -19.204 1.365   17.439  1.00 36.45  ? 112 MET A N   1 
ATOM   894  C  CA  . MET A 1 112 ? -17.908 1.074   18.024  1.00 37.97  ? 112 MET A CA  1 
ATOM   895  C  C   . MET A 1 112 ? -17.630 2.067   19.150  1.00 40.26  ? 112 MET A C   1 
ATOM   896  O  O   . MET A 1 112 ? -16.991 1.724   20.151  1.00 35.96  ? 112 MET A O   1 
ATOM   897  C  CB  . MET A 1 112 ? -16.849 1.192   16.929  1.00 38.88  ? 112 MET A CB  1 
ATOM   898  C  CG  . MET A 1 112 ? -16.645 -0.101  16.116  1.00 41.58  ? 112 MET A CG  1 
ATOM   899  S  SD  . MET A 1 112 ? -16.879 -1.657  16.982  1.00 41.05  ? 112 MET A SD  1 
ATOM   900  C  CE  . MET A 1 112 ? -18.383 -2.262  16.225  1.00 38.18  ? 112 MET A CE  1 
ATOM   901  N  N   . LYS A 1 113 ? -18.130 3.304   18.996  1.00 38.37  ? 113 LYS A N   1 
ATOM   902  C  CA  . LYS A 1 113 ? -17.984 4.333   20.025  1.00 38.64  ? 113 LYS A CA  1 
ATOM   903  C  C   . LYS A 1 113 ? -18.563 3.873   21.355  1.00 40.86  ? 113 LYS A C   1 
ATOM   904  O  O   . LYS A 1 113 ? -18.022 4.196   22.419  1.00 44.07  ? 113 LYS A O   1 
ATOM   905  C  CB  . LYS A 1 113 ? -18.681 5.622   19.582  1.00 42.33  ? 113 LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 113 ? -18.177 6.213   18.274  1.00 44.77  ? 113 LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 113 ? -19.066 7.379   17.845  1.00 43.29  ? 113 LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 113 ? -18.329 8.335   16.920  1.00 48.82  ? 113 LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 113 ? -19.261 8.955   15.943  1.00 47.56  ? 113 LYS A NZ  1 
ATOM   910  N  N   . GLY A 1 114 ? -19.679 3.139   21.318  1.00 37.70  ? 114 GLY A N   1 
ATOM   911  C  CA  . GLY A 1 114 ? -20.276 2.644   22.552  1.00 39.62  ? 114 GLY A CA  1 
ATOM   912  C  C   . GLY A 1 114 ? -19.539 1.467   23.172  1.00 42.55  ? 114 GLY A C   1 
ATOM   913  O  O   . GLY A 1 114 ? -19.563 1.296   24.395  1.00 43.99  ? 114 GLY A O   1 
ATOM   914  N  N   . TYR A 1 115 ? -18.889 0.632   22.350  1.00 38.71  ? 115 TYR A N   1 
ATOM   915  C  CA  . TYR A 1 115 ? -18.115 -0.486  22.889  1.00 36.58  ? 115 TYR A CA  1 
ATOM   916  C  C   . TYR A 1 115 ? -16.747 -0.063  23.393  1.00 37.35  ? 115 TYR A C   1 
ATOM   917  O  O   . TYR A 1 115 ? -16.094 -0.837  24.108  1.00 35.83  ? 115 TYR A O   1 
ATOM   918  C  CB  . TYR A 1 115 ? -17.899 -1.581  21.836  1.00 32.81  ? 115 TYR A CB  1 
ATOM   919  C  CG  . TYR A 1 115 ? -19.156 -2.162  21.254  1.00 35.92  ? 115 TYR A CG  1 
ATOM   920  C  CD1 . TYR A 1 115 ? -20.196 -2.575  22.076  1.00 34.46  ? 115 TYR A CD1 1 
ATOM   921  C  CD2 . TYR A 1 115 ? -19.292 -2.336  19.877  1.00 33.99  ? 115 TYR A CD2 1 
ATOM   922  C  CE1 . TYR A 1 115 ? -21.356 -3.124  21.542  1.00 42.66  ? 115 TYR A CE1 1 
ATOM   923  C  CE2 . TYR A 1 115 ? -20.452 -2.886  19.344  1.00 32.46  ? 115 TYR A CE2 1 
ATOM   924  C  CZ  . TYR A 1 115 ? -21.474 -3.273  20.173  1.00 38.68  ? 115 TYR A CZ  1 
ATOM   925  O  OH  . TYR A 1 115 ? -22.628 -3.815  19.643  1.00 41.04  ? 115 TYR A OH  1 
ATOM   926  N  N   . HIS A 1 116 ? -16.293 1.133   23.017  1.00 33.00  ? 116 HIS A N   1 
ATOM   927  C  CA  . HIS A 1 116 ? -14.904 1.504   23.239  1.00 31.90  ? 116 HIS A CA  1 
ATOM   928  C  C   . HIS A 1 116 ? -14.527 1.437   24.712  1.00 35.21  ? 116 HIS A C   1 
ATOM   929  O  O   . HIS A 1 116 ? -13.450 0.942   25.065  1.00 37.63  ? 116 HIS A O   1 
ATOM   930  C  CB  . HIS A 1 116 ? -14.651 2.905   22.693  1.00 37.07  ? 116 HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 116 ? -13.262 3.392   22.943  1.00 37.34  ? 116 HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 116 ? -12.208 3.085   22.112  1.00 37.87  ? 116 HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 116 ? -12.744 4.126   23.960  1.00 38.51  ? 116 HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 116 ? -11.101 3.628   22.591  1.00 36.65  ? 116 HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 116 ? -11.400 4.275   23.706  1.00 36.78  ? 116 HIS A NE2 1 
ATOM   936  N  N   . ALA A 1 117 ? -15.384 1.967   25.590  1.00 33.18  ? 117 ALA A N   1 
ATOM   937  C  CA  . ALA A 1 117 ? -15.028 2.016   27.006  1.00 37.66  ? 117 ALA A CA  1 
ATOM   938  C  C   . ALA A 1 117 ? -14.778 0.620   27.566  1.00 36.46  ? 117 ALA A C   1 
ATOM   939  O  O   . ALA A 1 117 ? -13.848 0.407   28.358  1.00 36.79  ? 117 ALA A O   1 
ATOM   940  C  CB  . ALA A 1 117 ? -16.128 2.725   27.798  1.00 38.09  ? 117 ALA A CB  1 
ATOM   941  N  N   . MET A 1 118 ? -15.605 -0.344  27.189  1.00 35.04  ? 118 MET A N   1 
ATOM   942  C  CA  . MET A 1 118 ? -15.401 -1.674  27.731  1.00 35.44  ? 118 MET A CA  1 
ATOM   943  C  C   . MET A 1 118 ? -14.293 -2.436  27.007  1.00 33.22  ? 118 MET A C   1 
ATOM   944  O  O   . MET A 1 118 ? -13.675 -3.316  27.621  1.00 31.32  ? 118 MET A O   1 
ATOM   945  C  CB  . MET A 1 118 ? -16.728 -2.443  27.744  1.00 37.89  ? 118 MET A CB  1 
ATOM   946  C  CG  . MET A 1 118 ? -17.689 -1.848  28.798  1.00 42.01  ? 118 MET A CG  1 
ATOM   947  S  SD  . MET A 1 118 ? -16.984 -1.814  30.506  1.00 52.55  ? 118 MET A SD  1 
ATOM   948  C  CE  . MET A 1 118 ? -16.910 -0.048  30.855  1.00 41.40  ? 118 MET A CE  1 
ATOM   949  N  N   . MET A 1 119 ? -13.955 -2.100  25.753  1.00 33.55  ? 119 MET A N   1 
ATOM   950  C  CA  . MET A 1 119 ? -12.715 -2.701  25.280  1.00 32.14  ? 119 MET A CA  1 
ATOM   951  C  C   . MET A 1 119 ? -11.502 -2.085  25.963  1.00 34.71  ? 119 MET A C   1 
ATOM   952  O  O   . MET A 1 119 ? -10.501 -2.782  26.157  1.00 30.49  ? 119 MET A O   1 
ATOM   953  C  CB  . MET A 1 119 ? -12.528 -2.684  23.754  1.00 35.49  ? 119 MET A CB  1 
ATOM   954  C  CG  . MET A 1 119 ? -13.753 -2.741  22.880  1.00 32.02  ? 119 MET A CG  1 
ATOM   955  S  SD  . MET A 1 119 ? -13.299 -2.429  21.149  1.00 35.50  ? 119 MET A SD  1 
ATOM   956  C  CE  . MET A 1 119 ? -14.485 -3.489  20.317  1.00 36.41  ? 119 MET A CE  1 
ATOM   957  N  N   . VAL A 1 120 ? -11.568 -0.811  26.365  1.00 31.55  ? 120 VAL A N   1 
ATOM   958  C  CA  . VAL A 1 120 ? -10.446 -0.242  27.119  1.00 33.13  ? 120 VAL A CA  1 
ATOM   959  C  C   . VAL A 1 120 ? -10.308 -0.948  28.471  1.00 32.36  ? 120 VAL A C   1 
ATOM   960  O  O   . VAL A 1 120 ? -9.196  -1.204  28.940  1.00 33.82  ? 120 VAL A O   1 
ATOM   961  C  CB  . VAL A 1 120 ? -10.613 1.285   27.276  1.00 37.17  ? 120 VAL A CB  1 
ATOM   962  C  CG1 . VAL A 1 120 ? -9.543  1.847   28.193  1.00 33.87  ? 120 VAL A CG1 1 
ATOM   963  C  CG2 . VAL A 1 120 ? -10.551 1.999   25.905  1.00 31.31  ? 120 VAL A CG2 1 
ATOM   964  N  N   . ASP A 1 121 ? -11.437 -1.290  29.103  1.00 34.58  ? 121 ASP A N   1 
ATOM   965  C  CA  . ASP A 1 121 ? -11.429 -2.027  30.372  1.00 33.58  ? 121 ASP A CA  1 
ATOM   966  C  C   . ASP A 1 121 ? -10.585 -3.293  30.274  1.00 34.31  ? 121 ASP A C   1 
ATOM   967  O  O   . ASP A 1 121 ? -9.664  -3.500  31.075  1.00 34.00  ? 121 ASP A O   1 
ATOM   968  C  CB  . ASP A 1 121 ? -12.879 -2.354  30.777  1.00 32.53  ? 121 ASP A CB  1 
ATOM   969  C  CG  . ASP A 1 121 ? -12.995 -3.063  32.143  1.00 35.38  ? 121 ASP A CG  1 
ATOM   970  O  OD1 . ASP A 1 121 ? -12.406 -4.152  32.352  1.00 32.02  ? 121 ASP A OD1 1 
ATOM   971  O  OD2 . ASP A 1 121 ? -13.730 -2.552  33.010  1.00 35.74  ? 121 ASP A OD2 1 
ATOM   972  N  N   . ILE A 1 122 ? -10.851 -4.130  29.261  1.00 32.02  ? 122 ILE A N   1 
ATOM   973  C  CA  . ILE A 1 122 ? -10.102 -5.373  29.097  1.00 31.24  ? 122 ILE A CA  1 
ATOM   974  C  C   . ILE A 1 122 ? -8.667  -5.082  28.660  1.00 32.45  ? 122 ILE A C   1 
ATOM   975  O  O   . ILE A 1 122 ? -7.716  -5.717  29.132  1.00 32.83  ? 122 ILE A O   1 
ATOM   976  C  CB  . ILE A 1 122 ? -10.812 -6.311  28.096  1.00 31.06  ? 122 ILE A CB  1 
ATOM   977  C  CG1 . ILE A 1 122 ? -12.275 -6.543  28.492  1.00 29.94  ? 122 ILE A CG1 1 
ATOM   978  C  CG2 . ILE A 1 122 ? -10.108 -7.665  28.027  1.00 28.32  ? 122 ILE A CG2 1 
ATOM   979  C  CD1 . ILE A 1 122 ? -12.481 -6.924  29.972  1.00 30.23  ? 122 ILE A CD1 1 
ATOM   980  N  N   . ALA A 1 123 ? -8.484  -4.133  27.739  1.00 32.97  ? 123 ALA A N   1 
ATOM   981  C  CA  . ALA A 1 123 ? -7.134  -3.832  27.264  1.00 32.40  ? 123 ALA A CA  1 
ATOM   982  C  C   . ALA A 1 123 ? -6.242  -3.369  28.408  1.00 32.39  ? 123 ALA A C   1 
ATOM   983  O  O   . ALA A 1 123 ? -5.055  -3.711  28.458  1.00 33.65  ? 123 ALA A O   1 
ATOM   984  C  CB  . ALA A 1 123 ? -7.184  -2.763  26.169  1.00 36.12  ? 123 ALA A CB  1 
ATOM   985  N  N   . VAL A 1 124 ? -6.795  -2.583  29.330  1.00 31.56  ? 124 VAL A N   1 
ATOM   986  C  CA  . VAL A 1 124 ? -6.019  -2.143  30.485  1.00 36.09  ? 124 VAL A CA  1 
ATOM   987  C  C   . VAL A 1 124 ? -5.658  -3.332  31.371  1.00 36.43  ? 124 VAL A C   1 
ATOM   988  O  O   . VAL A 1 124 ? -4.549  -3.400  31.915  1.00 34.58  ? 124 VAL A O   1 
ATOM   989  C  CB  . VAL A 1 124 ? -6.785  -1.049  31.258  1.00 35.06  ? 124 VAL A CB  1 
ATOM   990  C  CG1 . VAL A 1 124 ? -6.133  -0.796  32.607  1.00 34.31  ? 124 VAL A CG1 1 
ATOM   991  C  CG2 . VAL A 1 124 ? -6.804  0.232   30.450  1.00 34.62  ? 124 VAL A CG2 1 
ATOM   992  N  N   . GLN A 1 125 ? -6.575  -4.301  31.524  1.00 34.29  ? 125 GLN A N   1 
ATOM   993  C  CA  . GLN A 1 125 ? -6.224  -5.498  32.291  1.00 33.10  ? 125 GLN A CA  1 
ATOM   994  C  C   . GLN A 1 125 ? -5.037  -6.223  31.666  1.00 33.40  ? 125 GLN A C   1 
ATOM   995  O  O   . GLN A 1 125 ? -4.157  -6.717  32.384  1.00 31.38  ? 125 GLN A O   1 
ATOM   996  C  CB  . GLN A 1 125 ? -7.416  -6.450  32.411  1.00 32.85  ? 125 GLN A CB  1 
ATOM   997  C  CG  . GLN A 1 125 ? -8.527  -5.935  33.304  1.00 31.19  ? 125 GLN A CG  1 
ATOM   998  C  CD  . GLN A 1 125 ? -9.586  -6.975  33.567  1.00 33.57  ? 125 GLN A CD  1 
ATOM   999  O  OE1 . GLN A 1 125 ? -9.276  -8.097  33.967  1.00 30.58  ? 125 GLN A OE1 1 
ATOM   1000 N  NE2 . GLN A 1 125 ? -10.849 -6.613  33.344  1.00 31.76  ? 125 GLN A NE2 1 
ATOM   1001 N  N   . LEU A 1 126 ? -4.984  -6.282  30.326  1.00 32.59  ? 126 LEU A N   1 
ATOM   1002 C  CA  . LEU A 1 126 ? -3.838  -6.894  29.651  1.00 30.90  ? 126 LEU A CA  1 
ATOM   1003 C  C   . LEU A 1 126 ? -2.555  -6.137  29.956  1.00 33.61  ? 126 LEU A C   1 
ATOM   1004 O  O   . LEU A 1 126 ? -1.546  -6.736  30.362  1.00 34.96  ? 126 LEU A O   1 
ATOM   1005 C  CB  . LEU A 1 126 ? -4.068  -6.957  28.135  1.00 29.78  ? 126 LEU A CB  1 
ATOM   1006 C  CG  . LEU A 1 126 ? -2.827  -7.436  27.355  1.00 33.66  ? 126 LEU A CG  1 
ATOM   1007 C  CD1 . LEU A 1 126 ? -2.589  -8.932  27.565  1.00 35.45  ? 126 LEU A CD1 1 
ATOM   1008 C  CD2 . LEU A 1 126 ? -2.959  -7.143  25.882  1.00 41.03  ? 126 LEU A CD2 1 
ATOM   1009 N  N   . VAL A 1 127 ? -2.574  -4.815  29.788  1.00 32.23  ? 127 VAL A N   1 
ATOM   1010 C  CA  . VAL A 1 127 ? -1.355  -4.031  30.009  1.00 33.67  ? 127 VAL A CA  1 
ATOM   1011 C  C   . VAL A 1 127 ? -0.895  -4.168  31.459  1.00 35.55  ? 127 VAL A C   1 
ATOM   1012 O  O   . VAL A 1 127 ? 0.302   -4.331  31.735  1.00 35.01  ? 127 VAL A O   1 
ATOM   1013 C  CB  . VAL A 1 127 ? -1.580  -2.553  29.619  1.00 35.20  ? 127 VAL A CB  1 
ATOM   1014 C  CG1 . VAL A 1 127 ? -0.431  -1.681  30.085  1.00 36.59  ? 127 VAL A CG1 1 
ATOM   1015 C  CG2 . VAL A 1 127 ? -1.798  -2.396  28.097  1.00 30.76  ? 127 VAL A CG2 1 
ATOM   1016 N  N   . GLN A 1 128 ? -1.831  -4.107  32.411  1.00 34.09  ? 128 GLN A N   1 
ATOM   1017 C  CA  . GLN A 1 128 ? -1.443  -4.226  33.820  1.00 36.74  ? 128 GLN A CA  1 
ATOM   1018 C  C   . GLN A 1 128 ? -0.878  -5.607  34.124  1.00 34.97  ? 128 GLN A C   1 
ATOM   1019 O  O   . GLN A 1 128 ? 0.086   -5.728  34.889  1.00 35.24  ? 128 GLN A O   1 
ATOM   1020 C  CB  . GLN A 1 128 ? -2.630  -3.905  34.726  1.00 32.43  ? 128 GLN A CB  1 
ATOM   1021 C  CG  . GLN A 1 128 ? -2.997  -2.449  34.575  1.00 39.11  ? 128 GLN A CG  1 
ATOM   1022 C  CD  . GLN A 1 128 ? -3.967  -1.988  35.608  1.00 47.73  ? 128 GLN A CD  1 
ATOM   1023 O  OE1 . GLN A 1 128 ? -5.003  -2.620  35.803  1.00 50.64  ? 128 GLN A OE1 1 
ATOM   1024 N  NE2 . GLN A 1 128 ? -3.667  -0.861  36.260  1.00 47.59  ? 128 GLN A NE2 1 
ATOM   1025 N  N   . LYS A 1 129 ? -1.439  -6.661  33.523  1.00 32.81  ? 129 LYS A N   1 
ATOM   1026 C  CA  . LYS A 1 129 ? -0.830  -7.986  33.672  1.00 29.53  ? 129 LYS A CA  1 
ATOM   1027 C  C   . LYS A 1 129 ? 0.650   -7.946  33.299  1.00 35.14  ? 129 LYS A C   1 
ATOM   1028 O  O   . LYS A 1 129 ? 1.513   -8.427  34.043  1.00 31.16  ? 129 LYS A O   1 
ATOM   1029 C  CB  . LYS A 1 129 ? -1.546  -9.031  32.799  1.00 32.52  ? 129 LYS A CB  1 
ATOM   1030 C  CG  . LYS A 1 129 ? -0.941  -10.429 33.005  1.00 32.18  ? 129 LYS A CG  1 
ATOM   1031 C  CD  . LYS A 1 129 ? -1.639  -11.546 32.222  1.00 33.73  ? 129 LYS A CD  1 
ATOM   1032 C  CE  . LYS A 1 129 ? -0.868  -12.864 32.444  1.00 32.73  ? 129 LYS A CE  1 
ATOM   1033 N  NZ  . LYS A 1 129 ? -1.509  -14.062 31.850  1.00 36.91  ? 129 LYS A NZ  1 
ATOM   1034 N  N   . TRP A 1 130 ? 0.956   -7.386  32.127  1.00 32.96  ? 130 TRP A N   1 
ATOM   1035 C  CA  . TRP A 1 130 ? 2.333   -7.393  31.641  1.00 34.58  ? 130 TRP A CA  1 
ATOM   1036 C  C   . TRP A 1 130 ? 3.223   -6.471  32.469  1.00 35.04  ? 130 TRP A C   1 
ATOM   1037 O  O   . TRP A 1 130 ? 4.398   -6.783  32.689  1.00 37.82  ? 130 TRP A O   1 
ATOM   1038 C  CB  . TRP A 1 130 ? 2.343   -7.004  30.156  1.00 34.20  ? 130 TRP A CB  1 
ATOM   1039 C  CG  . TRP A 1 130 ? 1.732   -8.057  29.274  1.00 32.94  ? 130 TRP A CG  1 
ATOM   1040 C  CD1 . TRP A 1 130 ? 1.199   -9.266  29.664  1.00 32.23  ? 130 TRP A CD1 1 
ATOM   1041 C  CD2 . TRP A 1 130 ? 1.575   -7.998  27.837  1.00 34.54  ? 130 TRP A CD2 1 
ATOM   1042 N  NE1 . TRP A 1 130 ? 0.743   -9.959  28.565  1.00 33.60  ? 130 TRP A NE1 1 
ATOM   1043 C  CE2 . TRP A 1 130 ? 0.945   -9.200  27.436  1.00 33.95  ? 130 TRP A CE2 1 
ATOM   1044 C  CE3 . TRP A 1 130 ? 1.896   -7.042  26.867  1.00 34.71  ? 130 TRP A CE3 1 
ATOM   1045 C  CZ2 . TRP A 1 130 ? 0.641   -9.481  26.096  1.00 34.59  ? 130 TRP A CZ2 1 
ATOM   1046 C  CZ3 . TRP A 1 130 ? 1.593   -7.319  25.531  1.00 33.16  ? 130 TRP A CZ3 1 
ATOM   1047 C  CH2 . TRP A 1 130 ? 0.962   -8.528  25.162  1.00 31.48  ? 130 TRP A CH2 1 
ATOM   1048 N  N   . GLU A 1 131 ? 2.690   -5.326  32.921  1.00 35.31  ? 131 GLU A N   1 
ATOM   1049 C  CA  . GLU A 1 131 ? 3.459   -4.451  33.810  1.00 36.27  ? 131 GLU A CA  1 
ATOM   1050 C  C   . GLU A 1 131 ? 3.843   -5.172  35.099  1.00 38.64  ? 131 GLU A C   1 
ATOM   1051 O  O   . GLU A 1 131 ? 4.863   -4.849  35.719  1.00 35.70  ? 131 GLU A O   1 
ATOM   1052 C  CB  . GLU A 1 131 ? 2.658   -3.189  34.148  1.00 37.22  ? 131 GLU A CB  1 
ATOM   1053 C  CG  . GLU A 1 131 ? 2.351   -2.229  32.995  1.00 35.64  ? 131 GLU A CG  1 
ATOM   1054 C  CD  . GLU A 1 131 ? 3.516   -1.310  32.625  1.00 40.06  ? 131 GLU A CD  1 
ATOM   1055 O  OE1 . GLU A 1 131 ? 4.684   -1.684  32.874  1.00 39.59  ? 131 GLU A OE1 1 
ATOM   1056 O  OE2 . GLU A 1 131 ? 3.266   -0.202  32.096  1.00 42.73  ? 131 GLU A OE2 1 
ATOM   1057 N  N   . ARG A 1 132 ? 3.041   -6.143  35.516  1.00 34.74  ? 132 ARG A N   1 
ATOM   1058 C  CA  . ARG A 1 132 ? 3.227   -6.845  36.775  1.00 33.64  ? 132 ARG A CA  1 
ATOM   1059 C  C   . ARG A 1 132 ? 4.065   -8.107  36.651  1.00 32.77  ? 132 ARG A C   1 
ATOM   1060 O  O   . ARG A 1 132 ? 4.281   -8.783  37.657  1.00 34.29  ? 132 ARG A O   1 
ATOM   1061 C  CB  . ARG A 1 132 ? 1.861   -7.186  37.381  1.00 30.54  ? 132 ARG A CB  1 
ATOM   1062 C  CG  . ARG A 1 132 ? 1.177   -5.939  37.892  1.00 32.04  ? 132 ARG A CG  1 
ATOM   1063 C  CD  . ARG A 1 132 ? -0.297  -6.154  38.285  1.00 30.39  ? 132 ARG A CD  1 
ATOM   1064 N  NE  . ARG A 1 132 ? -0.825  -4.871  38.740  1.00 34.32  ? 132 ARG A NE  1 
ATOM   1065 C  CZ  . ARG A 1 132 ? -2.114  -4.567  38.830  1.00 35.94  ? 132 ARG A CZ  1 
ATOM   1066 N  NH1 . ARG A 1 132 ? -3.052  -5.396  38.408  1.00 33.77  ? 132 ARG A NH1 1 
ATOM   1067 N  NH2 . ARG A 1 132 ? -2.470  -3.400  39.357  1.00 36.57  ? 132 ARG A NH2 1 
ATOM   1068 N  N   . LEU A 1 133 ? 4.560   -8.435  35.461  1.00 35.46  ? 133 LEU A N   1 
ATOM   1069 C  CA  . LEU A 1 133 ? 5.434   -9.593  35.331  1.00 34.52  ? 133 LEU A CA  1 
ATOM   1070 C  C   . LEU A 1 133 ? 6.794   -9.287  35.945  1.00 35.87  ? 133 LEU A C   1 
ATOM   1071 O  O   . LEU A 1 133 ? 7.245   -8.142  35.949  1.00 35.53  ? 133 LEU A O   1 
ATOM   1072 C  CB  . LEU A 1 133 ? 5.588   -9.980  33.857  1.00 34.33  ? 133 LEU A CB  1 
ATOM   1073 C  CG  . LEU A 1 133 ? 4.305   -10.493 33.186  1.00 37.10  ? 133 LEU A CG  1 
ATOM   1074 C  CD1 . LEU A 1 133 ? 4.573   -10.832 31.714  1.00 37.29  ? 133 LEU A CD1 1 
ATOM   1075 C  CD2 . LEU A 1 133 ? 3.792   -11.738 33.912  1.00 38.29  ? 133 LEU A CD2 1 
ATOM   1076 N  N   . ASN A 1 134 ? 7.429   -10.318 36.493  1.00 32.45  ? 134 ASN A N   1 
ATOM   1077 C  CA  . ASN A 1 134 ? 8.756   -10.159 37.064  1.00 40.11  ? 134 ASN A CA  1 
ATOM   1078 C  C   . ASN A 1 134 ? 9.806   -10.182 35.965  1.00 42.40  ? 134 ASN A C   1 
ATOM   1079 O  O   . ASN A 1 134 ? 9.590   -10.739 34.882  1.00 41.68  ? 134 ASN A O   1 
ATOM   1080 C  CB  . ASN A 1 134 ? 9.048   -11.258 38.087  1.00 38.59  ? 134 ASN A CB  1 
ATOM   1081 C  CG  . ASN A 1 134 ? 8.087   -11.222 39.251  1.00 36.91  ? 134 ASN A CG  1 
ATOM   1082 O  OD1 . ASN A 1 134 ? 8.137   -10.303 40.067  1.00 36.52  ? 134 ASN A OD1 1 
ATOM   1083 N  ND2 . ASN A 1 134 ? 7.171   -12.182 39.302  1.00 35.59  ? 134 ASN A ND2 1 
ATOM   1084 N  N   . ALA A 1 135 ? 10.943  -9.550  36.250  1.00 44.57  ? 135 ALA A N   1 
ATOM   1085 C  CA  . ALA A 1 135 ? 12.059  -9.552  35.313  1.00 45.74  ? 135 ALA A CA  1 
ATOM   1086 C  C   . ALA A 1 135 ? 12.336  -10.970 34.839  1.00 49.26  ? 135 ALA A C   1 
ATOM   1087 O  O   . ALA A 1 135 ? 12.337  -11.919 35.628  1.00 53.04  ? 135 ALA A O   1 
ATOM   1088 C  CB  . ALA A 1 135 ? 13.306  -8.956  35.975  1.00 48.05  ? 135 ALA A CB  1 
ATOM   1089 N  N   . ASP A 1 136 ? 12.545  -11.127 33.541  1.00 53.04  ? 136 ASP A N   1 
ATOM   1090 C  CA  . ASP A 1 136 ? 12.839  -12.454 33.010  1.00 59.68  ? 136 ASP A CA  1 
ATOM   1091 C  C   . ASP A 1 136 ? 11.746  -13.473 33.377  1.00 60.04  ? 136 ASP A C   1 
ATOM   1092 O  O   . ASP A 1 136 ? 12.025  -14.652 33.617  1.00 58.39  ? 136 ASP A O   1 
ATOM   1093 C  CB  . ASP A 1 136 ? 14.226  -12.923 33.475  1.00 63.65  ? 136 ASP A CB  1 
ATOM   1094 C  CG  . ASP A 1 136 ? 15.299  -11.822 33.342  1.00 67.88  ? 136 ASP A CG  1 
ATOM   1095 O  OD1 . ASP A 1 136 ? 15.582  -11.388 32.200  1.00 69.23  ? 136 ASP A OD1 1 
ATOM   1096 O  OD2 . ASP A 1 136 ? 15.857  -11.388 34.378  1.00 70.69  ? 136 ASP A OD2 1 
ATOM   1097 N  N   . GLU A 1 137 ? 10.499  -13.010 33.482  1.00 50.53  ? 137 GLU A N   1 
ATOM   1098 C  CA  . GLU A 1 137 ? 9.345   -13.829 33.145  1.00 44.86  ? 137 GLU A CA  1 
ATOM   1099 C  C   . GLU A 1 137 ? 9.027   -13.539 31.681  1.00 39.27  ? 137 GLU A C   1 
ATOM   1100 O  O   . GLU A 1 137 ? 9.543   -12.591 31.102  1.00 41.86  ? 137 GLU A O   1 
ATOM   1101 C  CB  . GLU A 1 137 ? 8.157   -13.501 34.056  1.00 39.78  ? 137 GLU A CB  1 
ATOM   1102 C  CG  . GLU A 1 137 ? 8.147   -14.368 35.308  1.00 44.75  ? 137 GLU A CG  1 
ATOM   1103 C  CD  . GLU A 1 137 ? 7.171   -13.907 36.391  1.00 46.50  ? 137 GLU A CD  1 
ATOM   1104 O  OE1 . GLU A 1 137 ? 6.351   -12.991 36.153  1.00 42.30  ? 137 GLU A OE1 1 
ATOM   1105 O  OE2 . GLU A 1 137 ? 7.269   -14.448 37.519  1.00 50.93  ? 137 GLU A OE2 1 
ATOM   1106 N  N   . HIS A 1 138 ? 8.168   -14.340 31.066  1.00 39.10  ? 138 HIS A N   1 
ATOM   1107 C  CA  . HIS A 1 138 ? 7.824   -14.031 29.686  1.00 35.38  ? 138 HIS A CA  1 
ATOM   1108 C  C   . HIS A 1 138 ? 6.308   -14.040 29.523  1.00 37.56  ? 138 HIS A C   1 
ATOM   1109 O  O   . HIS A 1 138 ? 5.562   -14.399 30.439  1.00 34.46  ? 138 HIS A O   1 
ATOM   1110 C  CB  . HIS A 1 138 ? 8.491   -15.004 28.702  1.00 36.40  ? 138 HIS A CB  1 
ATOM   1111 C  CG  . HIS A 1 138 ? 7.980   -16.400 28.812  1.00 38.29  ? 138 HIS A CG  1 
ATOM   1112 N  ND1 . HIS A 1 138 ? 8.622   -17.369 29.546  1.00 40.59  ? 138 HIS A ND1 1 
ATOM   1113 C  CD2 . HIS A 1 138 ? 6.865   -16.982 28.311  1.00 37.71  ? 138 HIS A CD2 1 
ATOM   1114 C  CE1 . HIS A 1 138 ? 7.936   -18.495 29.480  1.00 42.58  ? 138 HIS A CE1 1 
ATOM   1115 N  NE2 . HIS A 1 138 ? 6.866   -18.289 28.732  1.00 38.81  ? 138 HIS A NE2 1 
ATOM   1116 N  N   . ILE A 1 139 ? 5.879   -13.607 28.339  1.00 35.29  ? 139 ILE A N   1 
ATOM   1117 C  CA  . ILE A 1 139 ? 4.473   -13.517 27.948  1.00 36.01  ? 139 ILE A CA  1 
ATOM   1118 C  C   . ILE A 1 139 ? 4.164   -14.682 27.020  1.00 35.45  ? 139 ILE A C   1 
ATOM   1119 O  O   . ILE A 1 139 ? 4.904   -14.931 26.062  1.00 34.71  ? 139 ILE A O   1 
ATOM   1120 C  CB  . ILE A 1 139 ? 4.195   -12.173 27.250  1.00 34.91  ? 139 ILE A CB  1 
ATOM   1121 C  CG1 . ILE A 1 139 ? 4.322   -11.011 28.243  1.00 35.78  ? 139 ILE A CG1 1 
ATOM   1122 C  CG2 . ILE A 1 139 ? 2.831   -12.196 26.485  1.00 33.70  ? 139 ILE A CG2 1 
ATOM   1123 C  CD1 . ILE A 1 139 ? 4.596   -9.678  27.570  1.00 37.27  ? 139 ILE A CD1 1 
ATOM   1124 N  N   . GLU A 1 140 ? 3.081   -15.406 27.299  1.00 33.70  ? 140 GLU A N   1 
ATOM   1125 C  CA  . GLU A 1 140 ? 2.557   -16.411 26.372  1.00 33.96  ? 140 GLU A CA  1 
ATOM   1126 C  C   . GLU A 1 140 ? 1.532   -15.695 25.491  1.00 35.13  ? 140 GLU A C   1 
ATOM   1127 O  O   . GLU A 1 140 ? 0.429   -15.373 25.933  1.00 32.12  ? 140 GLU A O   1 
ATOM   1128 C  CB  . GLU A 1 140 ? 1.949   -17.571 27.142  1.00 35.54  ? 140 GLU A CB  1 
ATOM   1129 C  CG  . GLU A 1 140 ? 2.948   -18.234 28.064  1.00 37.59  ? 140 GLU A CG  1 
ATOM   1130 C  CD  . GLU A 1 140 ? 2.357   -19.371 28.856  1.00 45.49  ? 140 GLU A CD  1 
ATOM   1131 O  OE1 . GLU A 1 140 ? 1.139   -19.349 29.135  1.00 42.34  ? 140 GLU A OE1 1 
ATOM   1132 O  OE2 . GLU A 1 140 ? 3.121   -20.283 29.215  1.00 45.34  ? 140 GLU A OE2 1 
ATOM   1133 N  N   . VAL A 1 141 ? 1.902   -15.414 24.250  1.00 34.26  ? 141 VAL A N   1 
ATOM   1134 C  CA  . VAL A 1 141 ? 1.188   -14.399 23.472  1.00 34.63  ? 141 VAL A CA  1 
ATOM   1135 C  C   . VAL A 1 141 ? -0.209  -14.859 23.051  1.00 30.71  ? 141 VAL A C   1 
ATOM   1136 O  O   . VAL A 1 141 ? -1.187  -14.160 23.355  1.00 33.50  ? 141 VAL A O   1 
ATOM   1137 C  CB  . VAL A 1 141 ? 2.009   -13.973 22.249  1.00 32.00  ? 141 VAL A CB  1 
ATOM   1138 C  CG1 . VAL A 1 141 ? 1.151   -13.119 21.328  1.00 28.43  ? 141 VAL A CG1 1 
ATOM   1139 C  CG2 . VAL A 1 141 ? 3.227   -13.195 22.716  1.00 31.12  ? 141 VAL A CG2 1 
ATOM   1140 N  N   . PRO A 1 142 ? -0.369  -15.972 22.327  1.00 31.79  ? 142 PRO A N   1 
ATOM   1141 C  CA  . PRO A 1 142 ? -1.741  -16.369 21.943  1.00 31.75  ? 142 PRO A CA  1 
ATOM   1142 C  C   . PRO A 1 142 ? -2.626  -16.621 23.134  1.00 32.60  ? 142 PRO A C   1 
ATOM   1143 O  O   . PRO A 1 142 ? -3.831  -16.338 23.076  1.00 33.16  ? 142 PRO A O   1 
ATOM   1144 C  CB  . PRO A 1 142 ? -1.540  -17.646 21.113  1.00 34.09  ? 142 PRO A CB  1 
ATOM   1145 C  CG  . PRO A 1 142 ? -0.090  -18.080 21.391  1.00 34.84  ? 142 PRO A CG  1 
ATOM   1146 C  CD  . PRO A 1 142 ? 0.654   -16.826 21.703  1.00 33.72  ? 142 PRO A CD  1 
ATOM   1147 N  N   . GLU A 1 143 ? -2.053  -17.153 24.216  1.00 31.03  ? 143 GLU A N   1 
ATOM   1148 C  CA  . GLU A 1 143 ? -2.818  -17.391 25.423  1.00 32.74  ? 143 GLU A CA  1 
ATOM   1149 C  C   . GLU A 1 143 ? -3.403  -16.092 25.955  1.00 31.75  ? 143 GLU A C   1 
ATOM   1150 O  O   . GLU A 1 143 ? -4.609  -16.007 26.241  1.00 31.84  ? 143 GLU A O   1 
ATOM   1151 C  CB  . GLU A 1 143 ? -1.921  -18.051 26.477  1.00 32.92  ? 143 GLU A CB  1 
ATOM   1152 C  CG  . GLU A 1 143 ? -1.586  -19.507 26.196  1.00 32.11  ? 143 GLU A CG  1 
ATOM   1153 C  CD  . GLU A 1 143 ? -0.468  -19.671 25.159  1.00 35.73  ? 143 GLU A CD  1 
ATOM   1154 O  OE1 . GLU A 1 143 ? 0.180   -18.671 24.785  1.00 33.49  ? 143 GLU A OE1 1 
ATOM   1155 O  OE2 . GLU A 1 143 ? -0.239  -20.806 24.723  1.00 38.66  ? 143 GLU A OE2 1 
ATOM   1156 N  N   . ASP A 1 144 ? -2.551  -15.069 26.119  1.00 30.46  ? 144 ASP A N   1 
ATOM   1157 C  CA  . ASP A 1 144 ? -3.044  -13.793 26.612  1.00 32.45  ? 144 ASP A CA  1 
ATOM   1158 C  C   . ASP A 1 144 ? -3.919  -13.099 25.585  1.00 32.30  ? 144 ASP A C   1 
ATOM   1159 O  O   . ASP A 1 144 ? -4.857  -12.388 25.958  1.00 32.57  ? 144 ASP A O   1 
ATOM   1160 C  CB  . ASP A 1 144 ? -1.893  -12.869 27.007  1.00 31.03  ? 144 ASP A CB  1 
ATOM   1161 C  CG  . ASP A 1 144 ? -1.408  -13.123 28.423  1.00 34.27  ? 144 ASP A CG  1 
ATOM   1162 O  OD1 . ASP A 1 144 ? -2.131  -13.802 29.185  1.00 31.78  ? 144 ASP A OD1 1 
ATOM   1163 O  OD2 . ASP A 1 144 ? -0.297  -12.658 28.763  1.00 31.23  ? 144 ASP A OD2 1 
ATOM   1164 N  N   . MET A 1 145 ? -3.644  -13.278 24.287  1.00 31.78  ? 145 MET A N   1 
ATOM   1165 C  CA  . MET A 1 145 ? -4.473  -12.548 23.343  1.00 31.78  ? 145 MET A CA  1 
ATOM   1166 C  C   . MET A 1 145 ? -5.880  -13.145 23.346  1.00 30.99  ? 145 MET A C   1 
ATOM   1167 O  O   . MET A 1 145 ? -6.871  -12.429 23.149  1.00 31.13  ? 145 MET A O   1 
ATOM   1168 C  CB  . MET A 1 145 ? -3.860  -12.592 21.940  1.00 31.24  ? 145 MET A CB  1 
ATOM   1169 C  CG  . MET A 1 145 ? -2.570  -11.771 21.948  1.00 30.32  ? 145 MET A CG  1 
ATOM   1170 S  SD  . MET A 1 145 ? -2.732  -10.028 22.166  1.00 33.98  ? 145 MET A SD  1 
ATOM   1171 C  CE  . MET A 1 145 ? -2.198  -9.908  23.884  1.00 37.59  ? 145 MET A CE  1 
ATOM   1172 N  N   . THR A 1 146 ? -5.973  -14.454 23.569  1.00 30.24  ? 146 THR A N   1 
ATOM   1173 C  CA  . THR A 1 146 ? -7.269  -15.129 23.649  1.00 28.87  ? 146 THR A CA  1 
ATOM   1174 C  C   . THR A 1 146 ? -8.012  -14.783 24.930  1.00 33.46  ? 146 THR A C   1 
ATOM   1175 O  O   . THR A 1 146 ? -9.238  -14.657 24.924  1.00 31.24  ? 146 THR A O   1 
ATOM   1176 C  CB  . THR A 1 146 ? -7.064  -16.634 23.530  1.00 31.77  ? 146 THR A CB  1 
ATOM   1177 O  OG1 . THR A 1 146 ? -6.392  -16.905 22.296  1.00 33.04  ? 146 THR A OG1 1 
ATOM   1178 C  CG2 . THR A 1 146 ? -8.405  -17.391 23.578  1.00 33.42  ? 146 THR A CG2 1 
ATOM   1179 N  N   . ARG A 1 147 ? -7.293  -14.624 26.045  1.00 30.90  ? 147 ARG A N   1 
ATOM   1180 C  CA  . ARG A 1 147 ? -7.923  -14.089 27.251  1.00 30.77  ? 147 ARG A CA  1 
ATOM   1181 C  C   . ARG A 1 147 ? -8.557  -12.725 26.982  1.00 30.83  ? 147 ARG A C   1 
ATOM   1182 O  O   . ARG A 1 147 ? -9.700  -12.462 27.375  1.00 32.56  ? 147 ARG A O   1 
ATOM   1183 C  CB  . ARG A 1 147 ? -6.889  -13.973 28.371  1.00 29.52  ? 147 ARG A CB  1 
ATOM   1184 C  CG  . ARG A 1 147 ? -6.451  -15.285 28.995  1.00 32.73  ? 147 ARG A CG  1 
ATOM   1185 C  CD  . ARG A 1 147 ? -5.522  -14.977 30.196  1.00 35.85  ? 147 ARG A CD  1 
ATOM   1186 N  NE  . ARG A 1 147 ? -5.139  -16.181 30.926  1.00 38.66  ? 147 ARG A NE  1 
ATOM   1187 C  CZ  . ARG A 1 147 ? -3.980  -16.803 30.754  1.00 40.37  ? 147 ARG A CZ  1 
ATOM   1188 N  NH1 . ARG A 1 147 ? -3.099  -16.387 29.855  1.00 33.67  ? 147 ARG A NH1 1 
ATOM   1189 N  NH2 . ARG A 1 147 ? -3.699  -17.869 31.498  1.00 46.49  ? 147 ARG A NH2 1 
ATOM   1190 N  N   . LEU A 1 148 ? -7.806  -11.837 26.336  1.00 30.25  ? 148 LEU A N   1 
ATOM   1191 C  CA  . LEU A 1 148 ? -8.297  -10.513 25.969  1.00 30.55  ? 148 LEU A CA  1 
ATOM   1192 C  C   . LEU A 1 148 ? -9.548  -10.582 25.100  1.00 33.19  ? 148 LEU A C   1 
ATOM   1193 O  O   . LEU A 1 148 ? -10.586 -10.006 25.445  1.00 32.19  ? 148 LEU A O   1 
ATOM   1194 C  CB  . LEU A 1 148 ? -7.193  -9.734  25.244  1.00 34.84  ? 148 LEU A CB  1 
ATOM   1195 C  CG  . LEU A 1 148 ? -7.690  -8.373  24.738  1.00 36.36  ? 148 LEU A CG  1 
ATOM   1196 C  CD1 . LEU A 1 148 ? -7.262  -7.254  25.637  1.00 33.82  ? 148 LEU A CD1 1 
ATOM   1197 C  CD2 . LEU A 1 148 ? -7.147  -8.149  23.328  1.00 39.55  ? 148 LEU A CD2 1 
ATOM   1198 N  N   . THR A 1 149 ? -9.457  -11.234 23.932  1.00 32.64  ? 149 THR A N   1 
ATOM   1199 C  CA  . THR A 1 149 ? -10.568 -11.122 22.989  1.00 34.82  ? 149 THR A CA  1 
ATOM   1200 C  C   . THR A 1 149 ? -11.816 -11.831 23.493  1.00 31.90  ? 149 THR A C   1 
ATOM   1201 O  O   . THR A 1 149 ? -12.934 -11.375 23.209  1.00 32.67  ? 149 THR A O   1 
ATOM   1202 C  CB  . THR A 1 149 ? -10.183 -11.645 21.593  1.00 31.99  ? 149 THR A CB  1 
ATOM   1203 O  OG1 . THR A 1 149 ? -9.929  -13.057 21.635  1.00 33.86  ? 149 THR A OG1 1 
ATOM   1204 C  CG2 . THR A 1 149 ? -8.967  -10.894 21.087  1.00 30.23  ? 149 THR A CG2 1 
ATOM   1205 N  N   . LEU A 1 150 ? -11.663 -12.937 24.232  1.00 32.30  ? 150 LEU A N   1 
ATOM   1206 C  CA  . LEU A 1 150 ? -12.835 -13.564 24.846  1.00 35.52  ? 150 LEU A CA  1 
ATOM   1207 C  C   . LEU A 1 150 ? -13.489 -12.629 25.859  1.00 33.54  ? 150 LEU A C   1 
ATOM   1208 O  O   . LEU A 1 150 ? -14.717 -12.441 25.859  1.00 33.49  ? 150 LEU A O   1 
ATOM   1209 C  CB  . LEU A 1 150 ? -12.457 -14.889 25.520  1.00 36.06  ? 150 LEU A CB  1 
ATOM   1210 C  CG  . LEU A 1 150 ? -13.620 -15.344 26.407  1.00 35.88  ? 150 LEU A CG  1 
ATOM   1211 C  CD1 . LEU A 1 150 ? -14.716 -15.882 25.496  1.00 39.17  ? 150 LEU A CD1 1 
ATOM   1212 C  CD2 . LEU A 1 150 ? -13.185 -16.417 27.422  1.00 43.20  ? 150 LEU A CD2 1 
ATOM   1213 N  N   . ASP A 1 151 ? -12.687 -12.041 26.745  1.00 29.54  ? 151 ASP A N   1 
ATOM   1214 C  CA  . ASP A 1 151 ? -13.249 -11.088 27.698  1.00 33.03  ? 151 ASP A CA  1 
ATOM   1215 C  C   . ASP A 1 151 ? -13.906 -9.910  26.983  1.00 30.12  ? 151 ASP A C   1 
ATOM   1216 O  O   . ASP A 1 151 ? -14.952 -9.422  27.415  1.00 30.01  ? 151 ASP A O   1 
ATOM   1217 C  CB  . ASP A 1 151 ? -12.170 -10.587 28.670  1.00 30.92  ? 151 ASP A CB  1 
ATOM   1218 C  CG  . ASP A 1 151 ? -11.950 -11.536 29.844  1.00 33.13  ? 151 ASP A CG  1 
ATOM   1219 O  OD1 . ASP A 1 151 ? -12.191 -12.748 29.686  1.00 35.33  ? 151 ASP A OD1 1 
ATOM   1220 O  OD2 . ASP A 1 151 ? -11.540 -11.062 30.923  1.00 39.05  ? 151 ASP A OD2 1 
ATOM   1221 N  N   . THR A 1 152 ? -13.311 -9.427  25.893  1.00 29.77  ? 152 THR A N   1 
ATOM   1222 C  CA  . THR A 1 152 ? -13.893 -8.259  25.235  1.00 29.09  ? 152 THR A CA  1 
ATOM   1223 C  C   . THR A 1 152 ? -15.288 -8.562  24.683  1.00 32.75  ? 152 THR A C   1 
ATOM   1224 O  O   . THR A 1 152 ? -16.237 -7.793  24.909  1.00 31.27  ? 152 THR A O   1 
ATOM   1225 C  CB  . THR A 1 152 ? -12.965 -7.760  24.135  1.00 31.61  ? 152 THR A CB  1 
ATOM   1226 O  OG1 . THR A 1 152 ? -11.753 -7.305  24.748  1.00 32.01  ? 152 THR A OG1 1 
ATOM   1227 C  CG2 . THR A 1 152 ? -13.619 -6.608  23.374  1.00 32.46  ? 152 THR A CG2 1 
ATOM   1228 N  N   . ILE A 1 153 ? -15.441 -9.691  23.973  1.00 31.17  ? 153 ILE A N   1 
ATOM   1229 C  CA  . ILE A 1 153 ? -16.756 -10.023 23.414  1.00 31.28  ? 153 ILE A CA  1 
ATOM   1230 C  C   . ILE A 1 153 ? -17.750 -10.337 24.526  1.00 33.88  ? 153 ILE A C   1 
ATOM   1231 O  O   . ILE A 1 153 ? -18.945 -10.014 24.422  1.00 33.26  ? 153 ILE A O   1 
ATOM   1232 C  CB  . ILE A 1 153 ? -16.663 -11.175 22.390  1.00 32.25  ? 153 ILE A CB  1 
ATOM   1233 C  CG1 . ILE A 1 153 ? -18.014 -11.334 21.672  1.00 31.06  ? 153 ILE A CG1 1 
ATOM   1234 C  CG2 . ILE A 1 153 ? -16.297 -12.482 23.054  1.00 35.83  ? 153 ILE A CG2 1 
ATOM   1235 C  CD1 . ILE A 1 153 ? -18.557 -10.008 21.123  1.00 33.34  ? 153 ILE A CD1 1 
ATOM   1236 N  N   . GLY A 1 154 ? -17.287 -10.986 25.600  1.00 32.87  ? 154 GLY A N   1 
ATOM   1237 C  CA  . GLY A 1 154 ? -18.170 -11.227 26.730  1.00 29.98  ? 154 GLY A CA  1 
ATOM   1238 C  C   . GLY A 1 154 ? -18.714 -9.937  27.315  1.00 34.49  ? 154 GLY A C   1 
ATOM   1239 O  O   . GLY A 1 154 ? -19.913 -9.812  27.581  1.00 35.92  ? 154 GLY A O   1 
ATOM   1240 N  N   . LEU A 1 155 ? -17.836 -8.953  27.525  1.00 30.01  ? 155 LEU A N   1 
ATOM   1241 C  CA  . LEU A 1 155 ? -18.253 -7.705  28.162  1.00 33.51  ? 155 LEU A CA  1 
ATOM   1242 C  C   . LEU A 1 155 ? -19.042 -6.833  27.196  1.00 40.01  ? 155 LEU A C   1 
ATOM   1243 O  O   . LEU A 1 155 ? -20.196 -6.475  27.464  1.00 37.28  ? 155 LEU A O   1 
ATOM   1244 C  CB  . LEU A 1 155 ? -17.031 -6.950  28.684  1.00 36.10  ? 155 LEU A CB  1 
ATOM   1245 C  CG  . LEU A 1 155 ? -17.284 -5.824  29.665  1.00 40.52  ? 155 LEU A CG  1 
ATOM   1246 C  CD1 . LEU A 1 155 ? -18.222 -6.305  30.807  1.00 34.73  ? 155 LEU A CD1 1 
ATOM   1247 C  CD2 . LEU A 1 155 ? -15.950 -5.285  30.167  1.00 38.39  ? 155 LEU A CD2 1 
ATOM   1248 N  N   . CYS A 1 156 ? -18.434 -6.489  26.051  1.00 39.82  ? 156 CYS A N   1 
ATOM   1249 C  CA  . CYS A 1 156 ? -19.105 -5.632  25.077  1.00 38.80  ? 156 CYS A CA  1 
ATOM   1250 C  C   . CYS A 1 156 ? -20.387 -6.268  24.566  1.00 39.68  ? 156 CYS A C   1 
ATOM   1251 O  O   . CYS A 1 156 ? -21.372 -5.565  24.317  1.00 47.75  ? 156 CYS A O   1 
ATOM   1252 C  CB  . CYS A 1 156 ? -18.162 -5.306  23.897  1.00 32.80  ? 156 CYS A CB  1 
ATOM   1253 S  SG  . CYS A 1 156 ? -16.729 -4.404  24.401  1.00 44.92  ? 156 CYS A SG  1 
ATOM   1254 N  N   . GLY A 1 157 ? -20.406 -7.588  24.404  1.00 41.88  ? 157 GLY A N   1 
ATOM   1255 C  CA  . GLY A 1 157 ? -21.555 -8.237  23.816  1.00 39.95  ? 157 GLY A CA  1 
ATOM   1256 C  C   . GLY A 1 157 ? -22.709 -8.507  24.763  1.00 45.84  ? 157 GLY A C   1 
ATOM   1257 O  O   . GLY A 1 157 ? -23.878 -8.423  24.369  1.00 42.66  ? 157 GLY A O   1 
ATOM   1258 N  N   . PHE A 1 158 ? -22.401 -8.861  26.015  1.00 42.70  ? 158 PHE A N   1 
ATOM   1259 C  CA  . PHE A 1 158 ? -23.418 -9.379  26.928  1.00 41.98  ? 158 PHE A CA  1 
ATOM   1260 C  C   . PHE A 1 158 ? -23.255 -8.906  28.359  1.00 39.03  ? 158 PHE A C   1 
ATOM   1261 O  O   . PHE A 1 158 ? -23.929 -9.443  29.242  1.00 37.29  ? 158 PHE A O   1 
ATOM   1262 C  CB  . PHE A 1 158 ? -23.416 -10.908 26.884  1.00 42.34  ? 158 PHE A CB  1 
ATOM   1263 C  CG  . PHE A 1 158 ? -23.143 -11.447 25.525  1.00 45.61  ? 158 PHE A CG  1 
ATOM   1264 C  CD1 . PHE A 1 158 ? -24.038 -11.193 24.486  1.00 45.30  ? 158 PHE A CD1 1 
ATOM   1265 C  CD2 . PHE A 1 158 ? -21.916 -12.008 25.223  1.00 44.11  ? 158 PHE A CD2 1 
ATOM   1266 C  CE1 . PHE A 1 158 ? -23.786 -11.648 23.192  1.00 46.51  ? 158 PHE A CE1 1 
ATOM   1267 C  CE2 . PHE A 1 158 ? -21.639 -12.443 23.933  1.00 47.70  ? 158 PHE A CE2 1 
ATOM   1268 C  CZ  . PHE A 1 158 ? -22.579 -12.261 22.912  1.00 46.43  ? 158 PHE A CZ  1 
ATOM   1269 N  N   . ASN A 1 159 ? -22.401 -7.923  28.613  1.00 39.61  ? 159 ASN A N   1 
ATOM   1270 C  CA  . ASN A 1 159 ? -22.203 -7.399  29.956  1.00 38.54  ? 159 ASN A CA  1 
ATOM   1271 C  C   . ASN A 1 159 ? -21.799 -8.504  30.921  1.00 38.35  ? 159 ASN A C   1 
ATOM   1272 O  O   . ASN A 1 159 ? -22.197 -8.501  32.088  1.00 38.95  ? 159 ASN A O   1 
ATOM   1273 C  CB  . ASN A 1 159 ? -23.459 -6.685  30.462  1.00 38.15  ? 159 ASN A CB  1 
ATOM   1274 C  CG  . ASN A 1 159 ? -23.125 -5.477  31.297  1.00 49.03  ? 159 ASN A CG  1 
ATOM   1275 O  OD1 . ASN A 1 159 ? -22.105 -4.834  31.076  1.00 47.87  ? 159 ASN A OD1 1 
ATOM   1276 N  ND2 . ASN A 1 159 ? -23.981 -5.158  32.262  1.00 52.31  ? 159 ASN A ND2 1 
ATOM   1277 N  N   . TYR A 1 160 ? -21.023 -9.468  30.434  1.00 33.39  ? 160 TYR A N   1 
ATOM   1278 C  CA  . TYR A 1 160 ? -20.582 -10.592 31.246  1.00 33.43  ? 160 TYR A CA  1 
ATOM   1279 C  C   . TYR A 1 160 ? -19.058 -10.590 31.338  1.00 34.99  ? 160 TYR A C   1 
ATOM   1280 O  O   . TYR A 1 160 ? -18.370 -10.355 30.338  1.00 35.13  ? 160 TYR A O   1 
ATOM   1281 C  CB  . TYR A 1 160 ? -21.062 -11.916 30.659  1.00 36.33  ? 160 TYR A CB  1 
ATOM   1282 C  CG  . TYR A 1 160 ? -20.774 -13.081 31.563  1.00 34.82  ? 160 TYR A CG  1 
ATOM   1283 C  CD1 . TYR A 1 160 ? -21.619 -13.371 32.633  1.00 36.62  ? 160 TYR A CD1 1 
ATOM   1284 C  CD2 . TYR A 1 160 ? -19.663 -13.881 31.368  1.00 34.89  ? 160 TYR A CD2 1 
ATOM   1285 C  CE1 . TYR A 1 160 ? -21.367 -14.435 33.476  1.00 39.75  ? 160 TYR A CE1 1 
ATOM   1286 C  CE2 . TYR A 1 160 ? -19.401 -14.956 32.206  1.00 40.74  ? 160 TYR A CE2 1 
ATOM   1287 C  CZ  . TYR A 1 160 ? -20.254 -15.218 33.263  1.00 40.71  ? 160 TYR A CZ  1 
ATOM   1288 O  OH  . TYR A 1 160 ? -20.000 -16.276 34.094  1.00 42.50  ? 160 TYR A OH  1 
ATOM   1289 N  N   . ARG A 1 161 ? -18.524 -10.843 32.536  1.00 34.52  ? 161 ARG A N   1 
ATOM   1290 C  CA  . ARG A 1 161 ? -17.076 -10.836 32.748  1.00 35.28  ? 161 ARG A CA  1 
ATOM   1291 C  C   . ARG A 1 161 ? -16.590 -12.280 32.870  1.00 33.02  ? 161 ARG A C   1 
ATOM   1292 O  O   . ARG A 1 161 ? -16.848 -12.956 33.875  1.00 35.71  ? 161 ARG A O   1 
ATOM   1293 C  CB  . ARG A 1 161 ? -16.717 -9.989  33.974  1.00 35.32  ? 161 ARG A CB  1 
ATOM   1294 C  CG  . ARG A 1 161 ? -16.874 -8.492  33.695  1.00 35.19  ? 161 ARG A CG  1 
ATOM   1295 C  CD  . ARG A 1 161 ? -16.412 -7.596  34.826  1.00 31.94  ? 161 ARG A CD  1 
ATOM   1296 N  NE  . ARG A 1 161 ? -16.628 -6.186  34.494  1.00 32.96  ? 161 ARG A NE  1 
ATOM   1297 C  CZ  . ARG A 1 161 ? -15.696 -5.392  33.982  1.00 35.36  ? 161 ARG A CZ  1 
ATOM   1298 N  NH1 . ARG A 1 161 ? -14.476 -5.841  33.704  1.00 31.74  ? 161 ARG A NH1 1 
ATOM   1299 N  NH2 . ARG A 1 161 ? -15.992 -4.121  33.733  1.00 34.69  ? 161 ARG A NH2 1 
ATOM   1300 N  N   . PHE A 1 162 ? -15.901 -12.767 31.832  1.00 31.08  ? 162 PHE A N   1 
ATOM   1301 C  CA  . PHE A 1 162 ? -15.274 -14.080 31.944  1.00 32.19  ? 162 PHE A CA  1 
ATOM   1302 C  C   . PHE A 1 162 ? -14.070 -14.051 32.874  1.00 33.76  ? 162 PHE A C   1 
ATOM   1303 O  O   . PHE A 1 162 ? -13.629 -15.109 33.334  1.00 36.11  ? 162 PHE A O   1 
ATOM   1304 C  CB  . PHE A 1 162 ? -14.851 -14.607 30.567  1.00 34.22  ? 162 PHE A CB  1 
ATOM   1305 C  CG  . PHE A 1 162 ? -16.014 -15.041 29.718  1.00 36.62  ? 162 PHE A CG  1 
ATOM   1306 C  CD1 . PHE A 1 162 ? -16.634 -16.263 29.948  1.00 36.98  ? 162 PHE A CD1 1 
ATOM   1307 C  CD2 . PHE A 1 162 ? -16.473 -14.239 28.681  1.00 35.34  ? 162 PHE A CD2 1 
ATOM   1308 C  CE1 . PHE A 1 162 ? -17.719 -16.676 29.179  1.00 36.90  ? 162 PHE A CE1 1 
ATOM   1309 C  CE2 . PHE A 1 162 ? -17.561 -14.653 27.901  1.00 33.44  ? 162 PHE A CE2 1 
ATOM   1310 C  CZ  . PHE A 1 162 ? -18.183 -15.877 28.166  1.00 33.41  ? 162 PHE A CZ  1 
ATOM   1311 N  N   . ASN A 1 163 ? -13.540 -12.868 33.155  1.00 31.33  ? 163 ASN A N   1 
ATOM   1312 C  CA  . ASN A 1 163 ? -12.424 -12.696 34.088  1.00 32.96  ? 163 ASN A CA  1 
ATOM   1313 C  C   . ASN A 1 163 ? -11.265 -13.630 33.742  1.00 30.65  ? 163 ASN A C   1 
ATOM   1314 O  O   . ASN A 1 163 ? -10.649 -14.263 34.608  1.00 33.92  ? 163 ASN A O   1 
ATOM   1315 C  CB  . ASN A 1 163 ? -12.910 -12.865 35.533  1.00 31.80  ? 163 ASN A CB  1 
ATOM   1316 C  CG  . ASN A 1 163 ? -13.749 -11.676 35.988  1.00 35.37  ? 163 ASN A CG  1 
ATOM   1317 O  OD1 . ASN A 1 163 ? -13.357 -10.530 35.777  1.00 34.58  ? 163 ASN A OD1 1 
ATOM   1318 N  ND2 . ASN A 1 163 ? -14.922 -11.938 36.586  1.00 32.68  ? 163 ASN A ND2 1 
ATOM   1319 N  N   . SER A 1 164 ? -10.939 -13.679 32.439  1.00 31.64  ? 164 SER A N   1 
ATOM   1320 C  CA  . SER A 1 164 ? -9.916  -14.604 31.956  1.00 34.03  ? 164 SER A CA  1 
ATOM   1321 C  C   . SER A 1 164 ? -8.538  -14.294 32.525  1.00 33.35  ? 164 SER A C   1 
ATOM   1322 O  O   . SER A 1 164 ? -7.708  -15.202 32.665  1.00 35.40  ? 164 SER A O   1 
ATOM   1323 C  CB  . SER A 1 164 ? -9.862  -14.584 30.425  1.00 32.30  ? 164 SER A CB  1 
ATOM   1324 O  OG  . SER A 1 164 ? -11.091 -15.048 29.873  1.00 32.90  ? 164 SER A OG  1 
ATOM   1325 N  N   . PHE A 1 165 ? -8.257  -13.031 32.819  1.00 32.67  ? 165 PHE A N   1 
ATOM   1326 C  CA  . PHE A 1 165 ? -6.950  -12.702 33.379  1.00 32.35  ? 165 PHE A CA  1 
ATOM   1327 C  C   . PHE A 1 165 ? -6.851  -13.058 34.853  1.00 38.83  ? 165 PHE A C   1 
ATOM   1328 O  O   . PHE A 1 165 ? -5.768  -12.938 35.438  1.00 39.51  ? 165 PHE A O   1 
ATOM   1329 C  CB  . PHE A 1 165 ? -6.665  -11.218 33.177  1.00 30.81  ? 165 PHE A CB  1 
ATOM   1330 C  CG  . PHE A 1 165 ? -6.392  -10.857 31.754  1.00 35.56  ? 165 PHE A CG  1 
ATOM   1331 C  CD1 . PHE A 1 165 ? -5.281  -11.374 31.086  1.00 33.04  ? 165 PHE A CD1 1 
ATOM   1332 C  CD2 . PHE A 1 165 ? -7.279  -10.043 31.059  1.00 33.51  ? 165 PHE A CD2 1 
ATOM   1333 C  CE1 . PHE A 1 165 ? -5.047  -11.051 29.747  1.00 32.11  ? 165 PHE A CE1 1 
ATOM   1334 C  CE2 . PHE A 1 165 ? -7.051  -9.719  29.707  1.00 32.81  ? 165 PHE A CE2 1 
ATOM   1335 C  CZ  . PHE A 1 165 ? -5.922  -10.224 29.063  1.00 33.52  ? 165 PHE A CZ  1 
ATOM   1336 N  N   . TYR A 1 166 ? -7.947  -13.492 35.467  1.00 34.09  ? 166 TYR A N   1 
ATOM   1337 C  CA  . TYR A 1 166 ? -7.892  -13.964 36.840  1.00 37.63  ? 166 TYR A CA  1 
ATOM   1338 C  C   . TYR A 1 166 ? -7.706  -15.473 36.909  1.00 44.21  ? 166 TYR A C   1 
ATOM   1339 O  O   . TYR A 1 166 ? -7.679  -16.031 38.004  1.00 42.72  ? 166 TYR A O   1 
ATOM   1340 C  CB  . TYR A 1 166 ? -9.163  -13.531 37.593  1.00 31.53  ? 166 TYR A CB  1 
ATOM   1341 C  CG  . TYR A 1 166 ? -9.237  -12.039 37.825  1.00 34.03  ? 166 TYR A CG  1 
ATOM   1342 C  CD1 . TYR A 1 166 ? -9.783  -11.181 36.859  1.00 31.01  ? 166 TYR A CD1 1 
ATOM   1343 C  CD2 . TYR A 1 166 ? -8.741  -11.470 38.993  1.00 31.95  ? 166 TYR A CD2 1 
ATOM   1344 C  CE1 . TYR A 1 166 ? -9.825  -9.812  37.053  1.00 33.18  ? 166 TYR A CE1 1 
ATOM   1345 C  CE2 . TYR A 1 166 ? -8.790  -10.092 39.198  1.00 31.08  ? 166 TYR A CE2 1 
ATOM   1346 C  CZ  . TYR A 1 166 ? -9.329  -9.269  38.240  1.00 32.70  ? 166 TYR A CZ  1 
ATOM   1347 O  OH  . TYR A 1 166 ? -9.373  -7.900  38.458  1.00 33.19  ? 166 TYR A OH  1 
ATOM   1348 N  N   . ARG A 1 167 ? -7.519  -16.129 35.765  1.00 45.42  ? 167 ARG A N   1 
ATOM   1349 C  CA  . ARG A 1 167 ? -7.629  -17.573 35.640  1.00 50.42  ? 167 ARG A CA  1 
ATOM   1350 C  C   . ARG A 1 167 ? -6.412  -18.163 34.948  1.00 51.07  ? 167 ARG A C   1 
ATOM   1351 O  O   . ARG A 1 167 ? -5.788  -17.521 34.093  1.00 52.42  ? 167 ARG A O   1 
ATOM   1352 C  CB  . ARG A 1 167 ? -8.849  -17.956 34.799  1.00 46.42  ? 167 ARG A CB  1 
ATOM   1353 C  CG  . ARG A 1 167 ? -10.142 -17.980 35.524  1.00 46.58  ? 167 ARG A CG  1 
ATOM   1354 C  CD  . ARG A 1 167 ? -11.274 -18.110 34.508  1.00 46.18  ? 167 ARG A CD  1 
ATOM   1355 N  NE  . ARG A 1 167 ? -12.453 -17.351 34.895  1.00 46.00  ? 167 ARG A NE  1 
ATOM   1356 C  CZ  . ARG A 1 167 ? -13.507 -17.888 35.491  1.00 49.76  ? 167 ARG A CZ  1 
ATOM   1357 N  NH1 . ARG A 1 167 ? -13.516 -19.156 35.863  1.00 53.80  ? 167 ARG A NH1 1 
ATOM   1358 N  NH2 . ARG A 1 167 ? -14.575 -17.135 35.727  1.00 46.27  ? 167 ARG A NH2 1 
ATOM   1359 N  N   . ASP A 1 168 ? -6.096  -19.406 35.312  1.00 58.24  ? 168 ASP A N   1 
ATOM   1360 C  CA  . ASP A 1 168 ? -5.372  -20.312 34.425  1.00 62.17  ? 168 ASP A CA  1 
ATOM   1361 C  C   . ASP A 1 168 ? -6.302  -21.228 33.653  1.00 58.73  ? 168 ASP A C   1 
ATOM   1362 O  O   . ASP A 1 168 ? -5.960  -21.640 32.541  1.00 66.67  ? 168 ASP A O   1 
ATOM   1363 C  CB  . ASP A 1 168 ? -4.373  -21.197 35.194  1.00 63.03  ? 168 ASP A CB  1 
ATOM   1364 C  CG  . ASP A 1 168 ? -3.328  -20.402 35.948  1.00 62.18  ? 168 ASP A CG  1 
ATOM   1365 O  OD1 . ASP A 1 168 ? -2.471  -19.790 35.277  1.00 64.94  ? 168 ASP A OD1 1 
ATOM   1366 O  OD2 . ASP A 1 168 ? -3.338  -20.426 37.202  1.00 64.06  ? 168 ASP A OD2 1 
ATOM   1367 N  N   . GLN A 1 169 ? -7.468  -21.543 34.213  1.00 58.98  ? 169 GLN A N   1 
ATOM   1368 C  CA  . GLN A 1 169 ? -8.335  -22.594 33.697  1.00 60.54  ? 169 GLN A CA  1 
ATOM   1369 C  C   . GLN A 1 169 ? -9.665  -22.006 33.237  1.00 58.60  ? 169 GLN A C   1 
ATOM   1370 O  O   . GLN A 1 169 ? -10.383 -21.391 34.048  1.00 56.27  ? 169 GLN A O   1 
ATOM   1371 C  CB  . GLN A 1 169 ? -8.539  -23.677 34.761  1.00 68.58  ? 169 GLN A CB  1 
ATOM   1372 C  CG  . GLN A 1 169 ? -7.206  -24.207 35.321  1.00 69.46  ? 169 GLN A CG  1 
ATOM   1373 C  CD  . GLN A 1 169 ? -6.398  -25.010 34.294  1.00 74.45  ? 169 GLN A CD  1 
ATOM   1374 O  OE1 . GLN A 1 169 ? -6.950  -25.573 33.342  1.00 76.89  ? 169 GLN A OE1 1 
ATOM   1375 N  NE2 . GLN A 1 169 ? -5.079  -25.030 34.469  1.00 74.51  ? 169 GLN A NE2 1 
ATOM   1376 N  N   . PRO A 1 170 ? -9.992  -22.118 31.939  1.00 60.82  ? 170 PRO A N   1 
ATOM   1377 C  CA  . PRO A 1 170 ? -11.221 -21.556 31.385  1.00 57.64  ? 170 PRO A CA  1 
ATOM   1378 C  C   . PRO A 1 170 ? -12.503 -21.611 32.210  1.00 56.50  ? 170 PRO A C   1 
ATOM   1379 O  O   . PRO A 1 170 ? -12.780 -22.563 32.943  1.00 55.46  ? 170 PRO A O   1 
ATOM   1380 C  CB  . PRO A 1 170 ? -11.375 -22.420 30.126  1.00 55.58  ? 170 PRO A CB  1 
ATOM   1381 C  CG  . PRO A 1 170 ? -9.830  -22.639 29.686  1.00 60.08  ? 170 PRO A CG  1 
ATOM   1382 C  CD  . PRO A 1 170 ? -9.038  -21.947 30.838  1.00 64.31  ? 170 PRO A CD  1 
ATOM   1383 N  N   . HIS A 1 171 ? -13.318 -20.575 32.024  1.00 51.53  ? 171 HIS A N   1 
ATOM   1384 C  CA  . HIS A 1 171 ? -14.707 -20.614 32.451  1.00 50.12  ? 171 HIS A CA  1 
ATOM   1385 C  C   . HIS A 1 171 ? -15.392 -21.853 31.866  1.00 51.47  ? 171 HIS A C   1 
ATOM   1386 O  O   . HIS A 1 171 ? -15.076 -22.257 30.735  1.00 52.13  ? 171 HIS A O   1 
ATOM   1387 C  CB  . HIS A 1 171 ? -15.401 -19.327 31.992  1.00 47.69  ? 171 HIS A CB  1 
ATOM   1388 C  CG  . HIS A 1 171 ? -16.858 -19.253 32.326  1.00 44.29  ? 171 HIS A CG  1 
ATOM   1389 N  ND1 . HIS A 1 171 ? -17.800 -20.089 31.768  1.00 43.86  ? 171 HIS A ND1 1 
ATOM   1390 C  CD2 . HIS A 1 171 ? -17.540 -18.403 33.130  1.00 47.78  ? 171 HIS A CD2 1 
ATOM   1391 C  CE1 . HIS A 1 171 ? -19.000 -19.772 32.231  1.00 50.82  ? 171 HIS A CE1 1 
ATOM   1392 N  NE2 . HIS A 1 171 ? -18.870 -18.749 33.059  1.00 49.52  ? 171 HIS A NE2 1 
ATOM   1393 N  N   . PRO A 1 172 ? -16.330 -22.476 32.596  1.00 49.19  ? 172 PRO A N   1 
ATOM   1394 C  CA  . PRO A 1 172 ? -16.910 -23.750 32.120  1.00 48.79  ? 172 PRO A CA  1 
ATOM   1395 C  C   . PRO A 1 172 ? -17.546 -23.698 30.735  1.00 51.48  ? 172 PRO A C   1 
ATOM   1396 O  O   . PRO A 1 172 ? -17.485 -24.694 29.999  1.00 47.92  ? 172 PRO A O   1 
ATOM   1397 C  CB  . PRO A 1 172 ? -17.953 -24.105 33.199  1.00 54.27  ? 172 PRO A CB  1 
ATOM   1398 C  CG  . PRO A 1 172 ? -17.753 -23.149 34.333  1.00 47.94  ? 172 PRO A CG  1 
ATOM   1399 C  CD  . PRO A 1 172 ? -16.826 -22.057 33.924  1.00 52.10  ? 172 PRO A CD  1 
ATOM   1400 N  N   . PHE A 1 173 ? -18.190 -22.589 30.363  1.00 49.82  ? 173 PHE A N   1 
ATOM   1401 C  CA  . PHE A 1 173 ? -18.758 -22.495 29.021  1.00 46.09  ? 173 PHE A CA  1 
ATOM   1402 C  C   . PHE A 1 173 ? -17.669 -22.622 27.959  1.00 42.47  ? 173 PHE A C   1 
ATOM   1403 O  O   . PHE A 1 173 ? -17.864 -23.285 26.933  1.00 39.37  ? 173 PHE A O   1 
ATOM   1404 C  CB  . PHE A 1 173 ? -19.522 -21.173 28.863  1.00 46.84  ? 173 PHE A CB  1 
ATOM   1405 C  CG  . PHE A 1 173 ? -19.924 -20.867 27.435  1.00 46.37  ? 173 PHE A CG  1 
ATOM   1406 C  CD1 . PHE A 1 173 ? -19.024 -20.273 26.562  1.00 44.39  ? 173 PHE A CD1 1 
ATOM   1407 C  CD2 . PHE A 1 173 ? -21.190 -21.195 26.967  1.00 50.23  ? 173 PHE A CD2 1 
ATOM   1408 C  CE1 . PHE A 1 173 ? -19.370 -20.003 25.265  1.00 46.51  ? 173 PHE A CE1 1 
ATOM   1409 C  CE2 . PHE A 1 173 ? -21.549 -20.927 25.672  1.00 47.80  ? 173 PHE A CE2 1 
ATOM   1410 C  CZ  . PHE A 1 173 ? -20.630 -20.328 24.809  1.00 48.03  ? 173 PHE A CZ  1 
ATOM   1411 N  N   . ILE A 1 174 ? -16.517 -21.992 28.204  1.00 45.60  ? 174 ILE A N   1 
ATOM   1412 C  CA  . ILE A 1 174 ? -15.409 -21.979 27.253  1.00 44.16  ? 174 ILE A CA  1 
ATOM   1413 C  C   . ILE A 1 174 ? -14.808 -23.375 27.111  1.00 45.30  ? 174 ILE A C   1 
ATOM   1414 O  O   . ILE A 1 174 ? -14.401 -23.786 26.019  1.00 43.65  ? 174 ILE A O   1 
ATOM   1415 C  CB  . ILE A 1 174 ? -14.360 -20.953 27.713  1.00 45.44  ? 174 ILE A CB  1 
ATOM   1416 C  CG1 . ILE A 1 174 ? -14.914 -19.529 27.646  1.00 44.74  ? 174 ILE A CG1 1 
ATOM   1417 C  CG2 . ILE A 1 174 ? -13.123 -21.023 26.835  1.00 44.83  ? 174 ILE A CG2 1 
ATOM   1418 C  CD1 . ILE A 1 174 ? -15.912 -19.301 26.558  1.00 47.04  ? 174 ILE A CD1 1 
ATOM   1419 N  N   . THR A 1 175 ? -14.741 -24.127 28.213  1.00 45.60  ? 175 THR A N   1 
ATOM   1420 C  CA  . THR A 1 175 ? -14.264 -25.504 28.139  1.00 45.48  ? 175 THR A CA  1 
ATOM   1421 C  C   . THR A 1 175 ? -15.083 -26.311 27.144  1.00 42.33  ? 175 THR A C   1 
ATOM   1422 O  O   . THR A 1 175 ? -14.525 -27.037 26.316  1.00 45.38  ? 175 THR A O   1 
ATOM   1423 C  CB  . THR A 1 175 ? -14.297 -26.155 29.526  1.00 46.42  ? 175 THR A CB  1 
ATOM   1424 O  OG1 . THR A 1 175 ? -13.300 -25.540 30.346  1.00 45.00  ? 175 THR A OG1 1 
ATOM   1425 C  CG2 . THR A 1 175 ? -14.008 -27.645 29.423  1.00 46.20  ? 175 THR A CG2 1 
ATOM   1426 N  N   . SER A 1 176 ? -16.411 -26.165 27.184  1.00 40.19  ? 176 SER A N   1 
ATOM   1427 C  CA  . SER A 1 176 ? -17.260 -26.920 26.270  1.00 44.28  ? 176 SER A CA  1 
ATOM   1428 C  C   . SER A 1 176 ? -17.180 -26.363 24.848  1.00 43.52  ? 176 SER A C   1 
ATOM   1429 O  O   . SER A 1 176 ? -17.107 -27.141 23.892  1.00 41.38  ? 176 SER A O   1 
ATOM   1430 C  CB  . SER A 1 176 ? -18.706 -26.951 26.791  1.00 48.92  ? 176 SER A CB  1 
ATOM   1431 O  OG  . SER A 1 176 ? -18.798 -27.799 27.931  1.00 47.67  ? 176 SER A OG  1 
ATOM   1432 N  N   . MET A 1 177 ? -17.205 -25.028 24.684  1.00 43.36  ? 177 MET A N   1 
ATOM   1433 C  CA  . MET A 1 177 ? -16.864 -24.417 23.392  1.00 39.68  ? 177 MET A CA  1 
ATOM   1434 C  C   . MET A 1 177 ? -15.643 -25.010 22.742  1.00 38.96  ? 177 MET A C   1 
ATOM   1435 O  O   . MET A 1 177 ? -15.670 -25.410 21.573  1.00 40.21  ? 177 MET A O   1 
ATOM   1436 C  CB  . MET A 1 177 ? -16.519 -22.943 23.483  1.00 40.58  ? 177 MET A CB  1 
ATOM   1437 C  CG  . MET A 1 177 ? -16.725 -22.238 22.153  1.00 38.51  ? 177 MET A CG  1 
ATOM   1438 S  SD  . MET A 1 177 ? -16.966 -20.472 22.257  1.00 40.72  ? 177 MET A SD  1 
ATOM   1439 C  CE  . MET A 1 177 ? -15.229 -19.978 22.338  1.00 43.10  ? 177 MET A CE  1 
ATOM   1440 N  N   . VAL A 1 178 ? -14.516 -24.904 23.443  1.00 39.36  ? 178 VAL A N   1 
ATOM   1441 C  CA  . VAL A 1 178 ? -13.253 -25.267 22.817  1.00 40.37  ? 178 VAL A CA  1 
ATOM   1442 C  C   . VAL A 1 178 ? -13.278 -26.748 22.468  1.00 42.79  ? 178 VAL A C   1 
ATOM   1443 O  O   . VAL A 1 178 ? -12.861 -27.157 21.377  1.00 41.64  ? 178 VAL A O   1 
ATOM   1444 C  CB  . VAL A 1 178 ? -12.072 -24.902 23.743  1.00 45.20  ? 178 VAL A CB  1 
ATOM   1445 C  CG1 . VAL A 1 178 ? -10.798 -25.652 23.338  1.00 42.90  ? 178 VAL A CG1 1 
ATOM   1446 C  CG2 . VAL A 1 178 ? -11.862 -23.389 23.803  1.00 42.49  ? 178 VAL A CG2 1 
ATOM   1447 N  N   . ARG A 1 179 ? -13.826 -27.571 23.372  1.00 43.05  ? 179 ARG A N   1 
ATOM   1448 C  CA  . ARG A 1 179 ? -13.938 -29.006 23.117  1.00 43.32  ? 179 ARG A CA  1 
ATOM   1449 C  C   . ARG A 1 179 ? -14.881 -29.304 21.956  1.00 40.53  ? 179 ARG A C   1 
ATOM   1450 O  O   . ARG A 1 179 ? -14.625 -30.218 21.165  1.00 40.30  ? 179 ARG A O   1 
ATOM   1451 C  CB  . ARG A 1 179 ? -14.407 -29.734 24.381  1.00 42.19  ? 179 ARG A CB  1 
ATOM   1452 C  CG  . ARG A 1 179 ? -14.157 -31.237 24.335  1.00 49.45  ? 179 ARG A CG  1 
ATOM   1453 C  CD  . ARG A 1 179 ? -14.152 -31.849 25.734  1.00 52.11  ? 179 ARG A CD  1 
ATOM   1454 N  NE  . ARG A 1 179 ? -15.271 -31.355 26.526  1.00 49.13  ? 179 ARG A NE  1 
ATOM   1455 C  CZ  . ARG A 1 179 ? -15.255 -31.217 27.845  1.00 55.19  ? 179 ARG A CZ  1 
ATOM   1456 N  NH1 . ARG A 1 179 ? -14.209 -31.586 28.567  1.00 50.16  ? 179 ARG A NH1 1 
ATOM   1457 N  NH2 . ARG A 1 179 ? -16.313 -30.685 28.452  1.00 52.97  ? 179 ARG A NH2 1 
ATOM   1458 N  N   . ALA A 1 180 ? -15.986 -28.562 21.852  1.00 41.30  ? 180 ALA A N   1 
ATOM   1459 C  CA  . ALA A 1 180 ? -16.912 -28.748 20.737  1.00 42.32  ? 180 ALA A CA  1 
ATOM   1460 C  C   . ALA A 1 180 ? -16.292 -28.301 19.416  1.00 39.87  ? 180 ALA A C   1 
ATOM   1461 O  O   . ALA A 1 180 ? -16.467 -28.958 18.384  1.00 38.79  ? 180 ALA A O   1 
ATOM   1462 C  CB  . ALA A 1 180 ? -18.203 -27.977 21.002  1.00 39.56  ? 180 ALA A CB  1 
ATOM   1463 N  N   . LEU A 1 181 ? -15.583 -27.173 19.419  1.00 42.98  ? 181 LEU A N   1 
ATOM   1464 C  CA  . LEU A 1 181 ? -14.856 -26.773 18.218  1.00 39.41  ? 181 LEU A CA  1 
ATOM   1465 C  C   . LEU A 1 181 ? -13.820 -27.822 17.837  1.00 39.93  ? 181 LEU A C   1 
ATOM   1466 O  O   . LEU A 1 181 ? -13.593 -28.089 16.652  1.00 36.43  ? 181 LEU A O   1 
ATOM   1467 C  CB  . LEU A 1 181 ? -14.183 -25.416 18.434  1.00 40.94  ? 181 LEU A CB  1 
ATOM   1468 C  CG  . LEU A 1 181 ? -15.122 -24.209 18.436  1.00 39.11  ? 181 LEU A CG  1 
ATOM   1469 C  CD1 . LEU A 1 181 ? -14.411 -23.023 19.052  1.00 38.43  ? 181 LEU A CD1 1 
ATOM   1470 C  CD2 . LEU A 1 181 ? -15.612 -23.886 17.026  1.00 39.03  ? 181 LEU A CD2 1 
ATOM   1471 N  N   . ASP A 1 182 ? -13.160 -28.417 18.830  1.00 41.23  ? 182 ASP A N   1 
ATOM   1472 C  CA  . ASP A 1 182 ? -12.145 -29.407 18.499  1.00 43.50  ? 182 ASP A CA  1 
ATOM   1473 C  C   . ASP A 1 182 ? -12.779 -30.646 17.880  1.00 43.90  ? 182 ASP A C   1 
ATOM   1474 O  O   . ASP A 1 182 ? -12.255 -31.196 16.907  1.00 43.90  ? 182 ASP A O   1 
ATOM   1475 C  CB  . ASP A 1 182 ? -11.329 -29.765 19.740  1.00 47.14  ? 182 ASP A CB  1 
ATOM   1476 C  CG  . ASP A 1 182 ? -10.307 -30.850 19.465  1.00 53.51  ? 182 ASP A CG  1 
ATOM   1477 O  OD1 . ASP A 1 182 ? -9.288  -30.559 18.797  1.00 52.05  ? 182 ASP A OD1 1 
ATOM   1478 O  OD2 . ASP A 1 182 ? -10.520 -31.989 19.924  1.00 56.80  ? 182 ASP A OD2 1 
ATOM   1479 N  N   . GLU A 1 183 ? -13.929 -31.076 18.403  1.00 43.36  ? 183 GLU A N   1 
ATOM   1480 C  CA  . GLU A 1 183 ? -14.604 -32.230 17.820  1.00 42.32  ? 183 GLU A CA  1 
ATOM   1481 C  C   . GLU A 1 183 ? -15.104 -31.927 16.414  1.00 44.17  ? 183 GLU A C   1 
ATOM   1482 O  O   . GLU A 1 183 ? -14.971 -32.760 15.508  1.00 43.07  ? 183 GLU A O   1 
ATOM   1483 C  CB  . GLU A 1 183 ? -15.764 -32.669 18.712  1.00 43.70  ? 183 GLU A CB  1 
ATOM   1484 C  CG  . GLU A 1 183 ? -16.692 -33.688 18.062  1.00 48.52  ? 183 GLU A CG  1 
ATOM   1485 C  CD  . GLU A 1 183 ? -16.039 -35.055 17.883  1.00 50.61  ? 183 GLU A CD  1 
ATOM   1486 O  OE1 . GLU A 1 183 ? -14.871 -35.226 18.297  1.00 49.58  ? 183 GLU A OE1 1 
ATOM   1487 O  OE2 . GLU A 1 183 ? -16.698 -35.955 17.323  1.00 54.15  ? 183 GLU A OE2 1 
ATOM   1488 N  N   . ALA A 1 184 ? -15.707 -30.753 16.222  1.00 45.08  ? 184 ALA A N   1 
ATOM   1489 C  CA  . ALA A 1 184 ? -16.193 -30.368 14.900  1.00 47.16  ? 184 ALA A CA  1 
ATOM   1490 C  C   . ALA A 1 184 ? -15.082 -30.466 13.855  1.00 43.73  ? 184 ALA A C   1 
ATOM   1491 O  O   . ALA A 1 184 ? -15.266 -31.057 12.786  1.00 44.69  ? 184 ALA A O   1 
ATOM   1492 C  CB  . ALA A 1 184 ? -16.779 -28.948 14.958  1.00 38.17  ? 184 ALA A CB  1 
ATOM   1493 N  N   . MET A 1 185 ? -13.918 -29.888 14.154  1.00 45.31  ? 185 MET A N   1 
ATOM   1494 C  CA  . MET A 1 185 ? -12.784 -29.934 13.233  1.00 44.38  ? 185 MET A CA  1 
ATOM   1495 C  C   . MET A 1 185 ? -12.219 -31.348 13.074  1.00 49.30  ? 185 MET A C   1 
ATOM   1496 O  O   . MET A 1 185 ? -11.898 -31.766 11.953  1.00 49.22  ? 185 MET A O   1 
ATOM   1497 C  CB  . MET A 1 185 ? -11.708 -28.953 13.715  1.00 47.60  ? 185 MET A CB  1 
ATOM   1498 C  CG  . MET A 1 185 ? -12.087 -27.431 13.722  1.00 42.65  ? 185 MET A CG  1 
ATOM   1499 S  SD  . MET A 1 185 ? -13.146 -26.751 12.394  1.00 49.51  ? 185 MET A SD  1 
ATOM   1500 C  CE  . MET A 1 185 ? -11.967 -26.785 11.070  1.00 42.96  ? 185 MET A CE  1 
ATOM   1501 N  N   . ASN A 1 186 ? -12.061 -32.098 14.173  1.00 45.53  ? 186 ASN A N   1 
ATOM   1502 C  CA  . ASN A 1 186 ? -11.501 -33.445 14.048  1.00 48.21  ? 186 ASN A CA  1 
ATOM   1503 C  C   . ASN A 1 186 ? -12.440 -34.356 13.264  1.00 48.15  ? 186 ASN A C   1 
ATOM   1504 O  O   . ASN A 1 186 ? -11.982 -35.234 12.525  1.00 51.11  ? 186 ASN A O   1 
ATOM   1505 C  CB  . ASN A 1 186 ? -11.210 -34.023 15.444  1.00 52.89  ? 186 ASN A CB  1 
ATOM   1506 C  CG  . ASN A 1 186 ? -10.949 -35.536 15.435  1.00 62.54  ? 186 ASN A CG  1 
ATOM   1507 O  OD1 . ASN A 1 186 ? -11.010 -36.186 16.481  1.00 71.59  ? 186 ASN A OD1 1 
ATOM   1508 N  ND2 . ASN A 1 186 ? -10.583 -36.082 14.279  1.00 65.45  ? 186 ASN A ND2 1 
ATOM   1509 N  N   . LYS A 1 187 ? -13.749 -34.156 13.419  1.00 45.57  ? 187 LYS A N   1 
ATOM   1510 C  CA  . LYS A 1 187 ? -14.752 -34.949 12.721  1.00 48.60  ? 187 LYS A CA  1 
ATOM   1511 C  C   . LYS A 1 187 ? -14.525 -34.952 11.208  1.00 55.65  ? 187 LYS A C   1 
ATOM   1512 O  O   . LYS A 1 187 ? -14.864 -35.931 10.525  1.00 48.46  ? 187 LYS A O   1 
ATOM   1513 C  CB  . LYS A 1 187 ? -16.124 -34.367 13.051  1.00 49.89  ? 187 LYS A CB  1 
ATOM   1514 C  CG  . LYS A 1 187 ? -17.295 -35.320 13.121  1.00 53.68  ? 187 LYS A CG  1 
ATOM   1515 C  CD  . LYS A 1 187 ? -18.547 -34.470 13.359  1.00 49.71  ? 187 LYS A CD  1 
ATOM   1516 C  CE  . LYS A 1 187 ? -18.929 -34.402 14.817  1.00 52.92  ? 187 LYS A CE  1 
ATOM   1517 N  NZ  . LYS A 1 187 ? -20.356 -34.756 15.034  1.00 58.88  ? 187 LYS A NZ  1 
ATOM   1518 N  N   . LEU A 1 188 ? -13.948 -33.862 10.679  1.00 50.46  ? 188 LEU A N   1 
ATOM   1519 C  CA  . LEU A 1 188 ? -13.766 -33.676 9.243   1.00 50.93  ? 188 LEU A CA  1 
ATOM   1520 C  C   . LEU A 1 188 ? -12.918 -34.774 8.613   1.00 51.82  ? 188 LEU A C   1 
ATOM   1521 O  O   . LEU A 1 188 ? -13.116 -35.111 7.439   1.00 45.80  ? 188 LEU A O   1 
ATOM   1522 C  CB  . LEU A 1 188 ? -13.103 -32.320 8.980   1.00 50.99  ? 188 LEU A CB  1 
ATOM   1523 C  CG  . LEU A 1 188 ? -13.898 -31.063 9.340   1.00 50.33  ? 188 LEU A CG  1 
ATOM   1524 C  CD1 . LEU A 1 188 ? -12.961 -29.882 9.535   1.00 47.74  ? 188 LEU A CD1 1 
ATOM   1525 C  CD2 . LEU A 1 188 ? -14.950 -30.766 8.271   1.00 50.42  ? 188 LEU A CD2 1 
ATOM   1526 N  N   . GLN A 1 189 ? -11.951 -35.316 9.352   1.00 54.64  ? 189 GLN A N   1 
ATOM   1527 C  CA  . GLN A 1 189 ? -10.999 -36.257 8.768   1.00 52.82  ? 189 GLN A CA  1 
ATOM   1528 C  C   . GLN A 1 189 ? -11.451 -37.711 8.844   1.00 56.73  ? 189 GLN A C   1 
ATOM   1529 O  O   . GLN A 1 189 ? -11.058 -38.518 7.990   1.00 55.71  ? 189 GLN A O   1 
ATOM   1530 C  CB  . GLN A 1 189 ? -9.642  -36.096 9.450   1.00 52.10  ? 189 GLN A CB  1 
ATOM   1531 C  CG  . GLN A 1 189 ? -9.509  -34.737 10.123  1.00 55.30  ? 189 GLN A CG  1 
ATOM   1532 C  CD  . GLN A 1 189 ? -8.234  -34.604 10.931  1.00 55.74  ? 189 GLN A CD  1 
ATOM   1533 O  OE1 . GLN A 1 189 ? -7.717  -35.589 11.463  1.00 53.52  ? 189 GLN A OE1 1 
ATOM   1534 N  NE2 . GLN A 1 189 ? -7.717  -33.377 11.022  1.00 55.92  ? 189 GLN A NE2 1 
ATOM   1535 N  N   . ARG A 1 190 ? -12.279 -38.061 9.829   1.00 54.39  ? 190 ARG A N   1 
ATOM   1536 C  CA  . ARG A 1 190 ? -12.696 -39.444 10.044  1.00 59.93  ? 190 ARG A CA  1 
ATOM   1537 C  C   . ARG A 1 190 ? -13.222 -40.120 8.786   1.00 62.84  ? 190 ARG A C   1 
ATOM   1538 O  O   . ARG A 1 190 ? -14.296 -39.774 8.280   1.00 63.22  ? 190 ARG A O   1 
ATOM   1539 C  CB  . ARG A 1 190 ? -13.745 -39.506 11.157  1.00 58.78  ? 190 ARG A CB  1 
ATOM   1540 C  CG  . ARG A 1 190 ? -13.209 -38.977 12.461  1.00 58.93  ? 190 ARG A CG  1 
ATOM   1541 C  CD  . ARG A 1 190 ? -14.235 -38.968 13.559  1.00 56.04  ? 190 ARG A CD  1 
ATOM   1542 N  NE  . ARG A 1 190 ? -13.778 -38.121 14.652  1.00 56.26  ? 190 ARG A NE  1 
ATOM   1543 C  CZ  . ARG A 1 190 ? -14.534 -37.719 15.660  1.00 49.85  ? 190 ARG A CZ  1 
ATOM   1544 N  NH1 . ARG A 1 190 ? -15.823 -37.992 15.705  1.00 50.87  ? 190 ARG A NH1 1 
ATOM   1545 N  NH2 . ARG A 1 190 ? -13.979 -37.019 16.645  1.00 55.56  ? 190 ARG A NH2 1 
ATOM   1546 N  N   . ALA A 1 191 ? -12.464 -41.097 8.282   1.00 65.69  ? 191 ALA A N   1 
ATOM   1547 C  CA  . ALA A 1 191 ? -12.940 -41.883 7.150   1.00 64.51  ? 191 ALA A CA  1 
ATOM   1548 C  C   . ALA A 1 191 ? -14.221 -42.635 7.497   1.00 72.69  ? 191 ALA A C   1 
ATOM   1549 O  O   . ALA A 1 191 ? -15.067 -42.857 6.621   1.00 72.76  ? 191 ALA A O   1 
ATOM   1550 C  CB  . ALA A 1 191 ? -11.846 -42.847 6.686   1.00 63.81  ? 191 ALA A CB  1 
ATOM   1551 N  N   . ASN A 1 192 ? -14.396 -43.018 8.763   1.00 70.37  ? 192 ASN A N   1 
ATOM   1552 C  CA  . ASN A 1 192 ? -15.614 -43.694 9.208   1.00 70.35  ? 192 ASN A CA  1 
ATOM   1553 C  C   . ASN A 1 192 ? -16.051 -43.111 10.544  1.00 71.24  ? 192 ASN A C   1 
ATOM   1554 O  O   . ASN A 1 192 ? -15.715 -43.642 11.610  1.00 71.84  ? 192 ASN A O   1 
ATOM   1555 C  CB  . ASN A 1 192 ? -15.408 -45.206 9.320   1.00 76.95  ? 192 ASN A CB  1 
ATOM   1556 C  CG  . ASN A 1 192 ? -16.687 -45.993 9.060   1.00 77.91  ? 192 ASN A CG  1 
ATOM   1557 O  OD1 . ASN A 1 192 ? -17.081 -46.188 7.908   1.00 79.07  ? 192 ASN A OD1 1 
ATOM   1558 N  ND2 . ASN A 1 192 ? -17.350 -46.427 10.127  1.00 76.12  ? 192 ASN A ND2 1 
ATOM   1559 N  N   . PRO A 1 193 ? -16.831 -42.026 10.526  1.00 71.97  ? 193 PRO A N   1 
ATOM   1560 C  CA  . PRO A 1 193 ? -17.298 -41.429 11.786  1.00 73.50  ? 193 PRO A CA  1 
ATOM   1561 C  C   . PRO A 1 193 ? -18.232 -42.325 12.584  1.00 74.88  ? 193 PRO A C   1 
ATOM   1562 O  O   . PRO A 1 193 ? -18.734 -41.893 13.630  1.00 70.08  ? 193 PRO A O   1 
ATOM   1563 C  CB  . PRO A 1 193 ? -18.024 -40.159 11.320  1.00 71.58  ? 193 PRO A CB  1 
ATOM   1564 C  CG  . PRO A 1 193 ? -18.502 -40.488 9.947   1.00 75.32  ? 193 PRO A CG  1 
ATOM   1565 C  CD  . PRO A 1 193 ? -17.485 -41.427 9.348   1.00 72.45  ? 193 PRO A CD  1 
ATOM   1566 N  N   . ASP A 1 194 ? -18.479 -43.555 12.132  1.00 77.24  ? 194 ASP A N   1 
ATOM   1567 C  CA  . ASP A 1 194 ? -19.401 -44.458 12.799  1.00 76.73  ? 194 ASP A CA  1 
ATOM   1568 C  C   . ASP A 1 194 ? -18.711 -45.575 13.572  1.00 79.92  ? 194 ASP A C   1 
ATOM   1569 O  O   . ASP A 1 194 ? -19.381 -46.279 14.339  1.00 76.20  ? 194 ASP A O   1 
ATOM   1570 C  CB  . ASP A 1 194 ? -20.372 -45.064 11.775  1.00 79.96  ? 194 ASP A CB  1 
ATOM   1571 C  CG  . ASP A 1 194 ? -21.542 -44.142 11.466  1.00 84.67  ? 194 ASP A CG  1 
ATOM   1572 O  OD1 . ASP A 1 194 ? -21.658 -43.081 12.122  1.00 84.89  ? 194 ASP A OD1 1 
ATOM   1573 O  OD2 . ASP A 1 194 ? -22.339 -44.472 10.561  1.00 84.07  ? 194 ASP A OD2 1 
ATOM   1574 N  N   . ASP A 1 195 ? -17.405 -45.751 13.402  1.00 77.70  ? 195 ASP A N   1 
ATOM   1575 C  CA  . ASP A 1 195 ? -16.687 -46.735 14.195  1.00 75.83  ? 195 ASP A CA  1 
ATOM   1576 C  C   . ASP A 1 195 ? -16.905 -46.463 15.681  1.00 76.08  ? 195 ASP A C   1 
ATOM   1577 O  O   . ASP A 1 195 ? -16.932 -45.299 16.100  1.00 76.33  ? 195 ASP A O   1 
ATOM   1578 C  CB  . ASP A 1 195 ? -15.193 -46.703 13.866  1.00 76.69  ? 195 ASP A CB  1 
ATOM   1579 C  CG  . ASP A 1 195 ? -14.440 -47.874 14.467  1.00 82.44  ? 195 ASP A CG  1 
ATOM   1580 O  OD1 . ASP A 1 195 ? -14.735 -49.027 14.081  1.00 83.68  ? 195 ASP A OD1 1 
ATOM   1581 O  OD2 . ASP A 1 195 ? -13.550 -47.642 15.317  1.00 82.48  ? 195 ASP A OD2 1 
ATOM   1582 N  N   . PRO A 1 196 ? -17.064 -47.506 16.504  1.00 77.49  ? 196 PRO A N   1 
ATOM   1583 C  CA  . PRO A 1 196 ? -17.273 -47.288 17.946  1.00 73.15  ? 196 PRO A CA  1 
ATOM   1584 C  C   . PRO A 1 196 ? -16.127 -46.572 18.629  1.00 70.47  ? 196 PRO A C   1 
ATOM   1585 O  O   . PRO A 1 196 ? -16.290 -46.153 19.783  1.00 67.33  ? 196 PRO A O   1 
ATOM   1586 C  CB  . PRO A 1 196 ? -17.434 -48.711 18.501  1.00 75.09  ? 196 PRO A CB  1 
ATOM   1587 C  CG  . PRO A 1 196 ? -17.818 -49.543 17.329  1.00 76.47  ? 196 PRO A CG  1 
ATOM   1588 C  CD  . PRO A 1 196 ? -17.130 -48.932 16.146  1.00 78.60  ? 196 PRO A CD  1 
ATOM   1589 N  N   . ALA A 1 197 ? -14.970 -46.443 17.972  1.00 71.44  ? 197 ALA A N   1 
ATOM   1590 C  CA  . ALA A 1 197 ? -13.883 -45.648 18.530  1.00 70.63  ? 197 ALA A CA  1 
ATOM   1591 C  C   . ALA A 1 197 ? -14.337 -44.233 18.870  1.00 66.41  ? 197 ALA A C   1 
ATOM   1592 O  O   . ALA A 1 197 ? -13.867 -43.643 19.850  1.00 68.39  ? 197 ALA A O   1 
ATOM   1593 C  CB  . ALA A 1 197 ? -12.713 -45.608 17.546  1.00 69.13  ? 197 ALA A CB  1 
ATOM   1594 N  N   . TYR A 1 198 ? -15.262 -43.682 18.085  1.00 68.49  ? 198 TYR A N   1 
ATOM   1595 C  CA  . TYR A 1 198 ? -15.714 -42.304 18.210  1.00 64.85  ? 198 TYR A CA  1 
ATOM   1596 C  C   . TYR A 1 198 ? -16.974 -42.185 19.051  1.00 64.39  ? 198 TYR A C   1 
ATOM   1597 O  O   . TYR A 1 198 ? -17.691 -41.185 18.948  1.00 59.75  ? 198 TYR A O   1 
ATOM   1598 C  CB  . TYR A 1 198 ? -15.945 -41.723 16.814  1.00 61.65  ? 198 TYR A CB  1 
ATOM   1599 C  CG  . TYR A 1 198 ? -14.705 -41.768 15.955  1.00 61.59  ? 198 TYR A CG  1 
ATOM   1600 C  CD1 . TYR A 1 198 ? -13.495 -41.251 16.412  1.00 61.79  ? 198 TYR A CD1 1 
ATOM   1601 C  CD2 . TYR A 1 198 ? -14.719 -42.409 14.723  1.00 63.13  ? 198 TYR A CD2 1 
ATOM   1602 C  CE1 . TYR A 1 198 ? -12.352 -41.314 15.632  1.00 61.42  ? 198 TYR A CE1 1 
ATOM   1603 C  CE2 . TYR A 1 198 ? -13.582 -42.483 13.941  1.00 62.10  ? 198 TYR A CE2 1 
ATOM   1604 C  CZ  . TYR A 1 198 ? -12.403 -41.937 14.399  1.00 60.32  ? 198 TYR A CZ  1 
ATOM   1605 O  OH  . TYR A 1 198 ? -11.273 -42.013 13.610  1.00 66.48  ? 198 TYR A OH  1 
ATOM   1606 N  N   . ASP A 1 199 ? -17.268 -43.195 19.870  1.00 64.66  ? 199 ASP A N   1 
ATOM   1607 C  CA  . ASP A 1 199 ? -18.494 -43.172 20.658  1.00 65.94  ? 199 ASP A CA  1 
ATOM   1608 C  C   . ASP A 1 199 ? -18.384 -42.188 21.816  1.00 60.76  ? 199 ASP A C   1 
ATOM   1609 O  O   . ASP A 1 199 ? -19.342 -41.470 22.122  1.00 63.51  ? 199 ASP A O   1 
ATOM   1610 C  CB  . ASP A 1 199 ? -18.799 -44.574 21.180  1.00 70.45  ? 199 ASP A CB  1 
ATOM   1611 C  CG  . ASP A 1 199 ? -19.462 -45.447 20.140  1.00 74.49  ? 199 ASP A CG  1 
ATOM   1612 O  OD1 . ASP A 1 199 ? -20.302 -44.932 19.370  1.00 71.70  ? 199 ASP A OD1 1 
ATOM   1613 O  OD2 . ASP A 1 199 ? -19.140 -46.654 20.101  1.00 78.24  ? 199 ASP A OD2 1 
ATOM   1614 N  N   . GLU A 1 200 ? -17.228 -42.159 22.480  1.00 63.01  ? 200 GLU A N   1 
ATOM   1615 C  CA  . GLU A 1 200 ? -17.014 -41.214 23.572  1.00 62.44  ? 200 GLU A CA  1 
ATOM   1616 C  C   . GLU A 1 200 ? -16.997 -39.778 23.058  1.00 61.24  ? 200 GLU A C   1 
ATOM   1617 O  O   . GLU A 1 200 ? -17.646 -38.899 23.638  1.00 60.80  ? 200 GLU A O   1 
ATOM   1618 C  CB  . GLU A 1 200 ? -15.711 -41.545 24.305  1.00 58.53  ? 200 GLU A CB  1 
ATOM   1619 C  CG  . GLU A 1 200 ? -15.382 -40.616 25.469  1.00 60.89  ? 200 GLU A CG  1 
ATOM   1620 C  CD  . GLU A 1 200 ? -16.556 -40.421 26.416  1.00 63.92  ? 200 GLU A CD  1 
ATOM   1621 O  OE1 . GLU A 1 200 ? -17.357 -41.364 26.569  1.00 65.34  ? 200 GLU A OE1 1 
ATOM   1622 O  OE2 . GLU A 1 200 ? -16.674 -39.332 27.013  1.00 65.46  ? 200 GLU A OE2 1 
ATOM   1623 N  N   . ASN A 1 201 ? -16.248 -39.516 21.979  1.00 62.45  ? 201 ASN A N   1 
ATOM   1624 C  CA  . ASN A 1 201 ? -16.300 -38.195 21.355  1.00 59.08  ? 201 ASN A CA  1 
ATOM   1625 C  C   . ASN A 1 201 ? -17.744 -37.778 21.117  1.00 54.91  ? 201 ASN A C   1 
ATOM   1626 O  O   . ASN A 1 201 ? -18.141 -36.648 21.421  1.00 52.97  ? 201 ASN A O   1 
ATOM   1627 C  CB  . ASN A 1 201 ? -15.519 -38.181 20.034  1.00 57.21  ? 201 ASN A CB  1 
ATOM   1628 C  CG  . ASN A 1 201 ? -14.122 -38.748 20.161  1.00 62.20  ? 201 ASN A CG  1 
ATOM   1629 O  OD1 . ASN A 1 201 ? -13.806 -39.791 19.586  1.00 63.93  ? 201 ASN A OD1 1 
ATOM   1630 N  ND2 . ASN A 1 201 ? -13.269 -38.054 20.908  1.00 64.43  ? 201 ASN A ND2 1 
ATOM   1631 N  N   . LYS A 1 202 ? -18.543 -38.701 20.581  1.00 59.63  ? 202 LYS A N   1 
ATOM   1632 C  CA  . LYS A 1 202 ? -19.963 -38.461 20.347  1.00 54.81  ? 202 LYS A CA  1 
ATOM   1633 C  C   . LYS A 1 202 ? -20.671 -38.125 21.653  1.00 59.42  ? 202 LYS A C   1 
ATOM   1634 O  O   . LYS A 1 202 ? -21.401 -37.132 21.744  1.00 57.16  ? 202 LYS A O   1 
ATOM   1635 C  CB  . LYS A 1 202 ? -20.572 -39.710 19.713  1.00 59.24  ? 202 LYS A CB  1 
ATOM   1636 C  CG  . LYS A 1 202 ? -20.716 -39.679 18.205  1.00 62.47  ? 202 LYS A CG  1 
ATOM   1637 C  CD  . LYS A 1 202 ? -21.167 -41.048 17.698  1.00 63.44  ? 202 LYS A CD  1 
ATOM   1638 C  CE  . LYS A 1 202 ? -21.074 -41.163 16.177  1.00 70.15  ? 202 LYS A CE  1 
ATOM   1639 N  NZ  . LYS A 1 202 ? -22.260 -41.845 15.576  1.00 73.13  ? 202 LYS A NZ  1 
ATOM   1640 N  N   . ARG A 1 203 ? -20.467 -38.956 22.679  1.00 59.96  ? 203 ARG A N   1 
ATOM   1641 C  CA  . ARG A 1 203 ? -21.035 -38.670 23.992  1.00 59.93  ? 203 ARG A CA  1 
ATOM   1642 C  C   . ARG A 1 203 ? -20.631 -37.289 24.473  1.00 56.34  ? 203 ARG A C   1 
ATOM   1643 O  O   . ARG A 1 203 ? -21.479 -36.479 24.860  1.00 55.89  ? 203 ARG A O   1 
ATOM   1644 C  CB  . ARG A 1 203 ? -20.589 -39.728 25.002  1.00 62.06  ? 203 ARG A CB  1 
ATOM   1645 C  CG  . ARG A 1 203 ? -21.557 -39.927 26.154  1.00 63.53  ? 203 ARG A CG  1 
ATOM   1646 C  CD  . ARG A 1 203 ? -20.848 -40.196 27.488  1.00 69.95  ? 203 ARG A CD  1 
ATOM   1647 N  NE  . ARG A 1 203 ? -19.621 -39.433 27.692  1.00 67.77  ? 203 ARG A NE  1 
ATOM   1648 C  CZ  . ARG A 1 203 ? -19.572 -38.243 28.279  1.00 67.42  ? 203 ARG A CZ  1 
ATOM   1649 N  NH1 . ARG A 1 203 ? -20.672 -37.625 28.684  1.00 64.31  ? 203 ARG A NH1 1 
ATOM   1650 N  NH2 . ARG A 1 203 ? -18.391 -37.661 28.469  1.00 66.91  ? 203 ARG A NH2 1 
ATOM   1651 N  N   . GLN A 1 204 ? -19.326 -37.008 24.465  1.00 58.82  ? 204 GLN A N   1 
ATOM   1652 C  CA  . GLN A 1 204 ? -18.825 -35.769 25.049  1.00 56.32  ? 204 GLN A CA  1 
ATOM   1653 C  C   . GLN A 1 204 ? -19.310 -34.560 24.251  1.00 56.58  ? 204 GLN A C   1 
ATOM   1654 O  O   . GLN A 1 204 ? -19.623 -33.509 24.825  1.00 53.76  ? 204 GLN A O   1 
ATOM   1655 C  CB  . GLN A 1 204 ? -17.299 -35.819 25.102  1.00 56.24  ? 204 GLN A CB  1 
ATOM   1656 C  CG  . GLN A 1 204 ? -16.622 -34.499 25.352  1.00 54.17  ? 204 GLN A CG  1 
ATOM   1657 C  CD  . GLN A 1 204 ? -16.807 -34.033 26.782  1.00 58.79  ? 204 GLN A CD  1 
ATOM   1658 O  OE1 . GLN A 1 204 ? -17.844 -33.470 27.143  1.00 56.14  ? 204 GLN A OE1 1 
ATOM   1659 N  NE2 . GLN A 1 204 ? -15.791 -34.266 27.610  1.00 61.10  ? 204 GLN A NE2 1 
ATOM   1660 N  N   . PHE A 1 205 ? -19.395 -34.704 22.923  1.00 55.57  ? 205 PHE A N   1 
ATOM   1661 C  CA  . PHE A 1 205 ? -19.951 -33.654 22.070  1.00 52.65  ? 205 PHE A CA  1 
ATOM   1662 C  C   . PHE A 1 205 ? -21.334 -33.219 22.540  1.00 55.18  ? 205 PHE A C   1 
ATOM   1663 O  O   . PHE A 1 205 ? -21.636 -32.021 22.595  1.00 50.85  ? 205 PHE A O   1 
ATOM   1664 C  CB  . PHE A 1 205 ? -20.024 -34.139 20.619  1.00 52.22  ? 205 PHE A CB  1 
ATOM   1665 C  CG  . PHE A 1 205 ? -20.143 -33.029 19.607  1.00 52.87  ? 205 PHE A CG  1 
ATOM   1666 C  CD1 . PHE A 1 205 ? -19.228 -31.983 19.581  1.00 49.12  ? 205 PHE A CD1 1 
ATOM   1667 C  CD2 . PHE A 1 205 ? -21.178 -33.031 18.677  1.00 53.94  ? 205 PHE A CD2 1 
ATOM   1668 C  CE1 . PHE A 1 205 ? -19.339 -30.959 18.644  1.00 46.46  ? 205 PHE A CE1 1 
ATOM   1669 C  CE2 . PHE A 1 205 ? -21.298 -32.005 17.734  1.00 50.35  ? 205 PHE A CE2 1 
ATOM   1670 C  CZ  . PHE A 1 205 ? -20.378 -30.974 17.717  1.00 49.36  ? 205 PHE A CZ  1 
ATOM   1671 N  N   . GLN A 1 206 ? -22.201 -34.186 22.861  1.00 55.40  ? 206 GLN A N   1 
ATOM   1672 C  CA  . GLN A 1 206 ? -23.577 -33.836 23.207  1.00 57.00  ? 206 GLN A CA  1 
ATOM   1673 C  C   . GLN A 1 206 ? -23.656 -33.201 24.584  1.00 53.35  ? 206 GLN A C   1 
ATOM   1674 O  O   . GLN A 1 206 ? -24.468 -32.297 24.806  1.00 59.64  ? 206 GLN A O   1 
ATOM   1675 C  CB  . GLN A 1 206 ? -24.480 -35.064 23.116  1.00 56.06  ? 206 GLN A CB  1 
ATOM   1676 C  CG  . GLN A 1 206 ? -24.492 -35.666 21.729  1.00 58.35  ? 206 GLN A CG  1 
ATOM   1677 C  CD  . GLN A 1 206 ? -25.167 -34.754 20.711  1.00 63.04  ? 206 GLN A CD  1 
ATOM   1678 O  OE1 . GLN A 1 206 ? -26.185 -34.121 21.000  1.00 63.47  ? 206 GLN A OE1 1 
ATOM   1679 N  NE2 . GLN A 1 206 ? -24.587 -34.672 19.516  1.00 60.84  ? 206 GLN A NE2 1 
ATOM   1680 N  N   . GLU A 1 207 ? -22.820 -33.652 25.520  1.00 55.96  ? 207 GLU A N   1 
ATOM   1681 C  CA  . GLU A 1 207 ? -22.718 -32.968 26.803  1.00 56.82  ? 207 GLU A CA  1 
ATOM   1682 C  C   . GLU A 1 207 ? -22.327 -31.509 26.616  1.00 56.80  ? 207 GLU A C   1 
ATOM   1683 O  O   . GLU A 1 207 ? -22.851 -30.623 27.305  1.00 53.92  ? 207 GLU A O   1 
ATOM   1684 C  CB  . GLU A 1 207 ? -21.704 -33.683 27.696  1.00 59.76  ? 207 GLU A CB  1 
ATOM   1685 C  CG  . GLU A 1 207 ? -21.348 -32.949 28.993  1.00 59.61  ? 207 GLU A CG  1 
ATOM   1686 C  CD  . GLU A 1 207 ? -20.237 -33.658 29.771  1.00 66.45  ? 207 GLU A CD  1 
ATOM   1687 O  OE1 . GLU A 1 207 ? -20.306 -34.902 29.901  1.00 71.97  ? 207 GLU A OE1 1 
ATOM   1688 O  OE2 . GLU A 1 207 ? -19.292 -32.977 30.236  1.00 64.40  ? 207 GLU A OE2 1 
ATOM   1689 N  N   . ASP A 1 208 ? -21.401 -31.240 25.688  1.00 52.67  ? 208 ASP A N   1 
ATOM   1690 C  CA  . ASP A 1 208 ? -20.887 -29.884 25.520  1.00 50.75  ? 208 ASP A CA  1 
ATOM   1691 C  C   . ASP A 1 208 ? -21.919 -28.979 24.864  1.00 49.27  ? 208 ASP A C   1 
ATOM   1692 O  O   . ASP A 1 208 ? -22.036 -27.799 25.217  1.00 48.02  ? 208 ASP A O   1 
ATOM   1693 C  CB  . ASP A 1 208 ? -19.604 -29.917 24.697  1.00 47.64  ? 208 ASP A CB  1 
ATOM   1694 C  CG  . ASP A 1 208 ? -18.409 -30.406 25.499  1.00 47.17  ? 208 ASP A CG  1 
ATOM   1695 O  OD1 . ASP A 1 208 ? -18.376 -30.194 26.730  1.00 49.97  ? 208 ASP A OD1 1 
ATOM   1696 O  OD2 . ASP A 1 208 ? -17.496 -31.008 24.893  1.00 51.13  ? 208 ASP A OD2 1 
ATOM   1697 N  N   . ILE A 1 209 ? -22.667 -29.512 23.897  1.00 49.47  ? 209 ILE A N   1 
ATOM   1698 C  CA  . ILE A 1 209 ? -23.769 -28.759 23.313  1.00 50.57  ? 209 ILE A CA  1 
ATOM   1699 C  C   . ILE A 1 209 ? -24.793 -28.413 24.385  1.00 54.67  ? 209 ILE A C   1 
ATOM   1700 O  O   . ILE A 1 209 ? -25.401 -27.338 24.351  1.00 50.32  ? 209 ILE A O   1 
ATOM   1701 C  CB  . ILE A 1 209 ? -24.405 -29.562 22.163  1.00 51.89  ? 209 ILE A CB  1 
ATOM   1702 C  CG1 . ILE A 1 209 ? -23.470 -29.590 20.948  1.00 51.50  ? 209 ILE A CG1 1 
ATOM   1703 C  CG2 . ILE A 1 209 ? -25.755 -28.964 21.782  1.00 54.25  ? 209 ILE A CG2 1 
ATOM   1704 C  CD1 . ILE A 1 209 ? -23.950 -30.496 19.829  1.00 52.23  ? 209 ILE A CD1 1 
ATOM   1705 N  N   . LYS A 1 210 ? -24.990 -29.307 25.361  1.00 57.60  ? 210 LYS A N   1 
ATOM   1706 C  CA  . LYS A 1 210 ? -25.959 -29.040 26.423  1.00 56.12  ? 210 LYS A CA  1 
ATOM   1707 C  C   . LYS A 1 210 ? -25.450 -27.990 27.404  1.00 52.64  ? 210 LYS A C   1 
ATOM   1708 O  O   . LYS A 1 210 ? -26.216 -27.123 27.839  1.00 56.59  ? 210 LYS A O   1 
ATOM   1709 C  CB  . LYS A 1 210 ? -26.301 -30.325 27.173  1.00 55.61  ? 210 LYS A CB  1 
ATOM   1710 C  CG  . LYS A 1 210 ? -27.264 -30.075 28.321  1.00 61.75  ? 210 LYS A CG  1 
ATOM   1711 C  CD  . LYS A 1 210 ? -27.104 -31.089 29.441  1.00 69.67  ? 210 LYS A CD  1 
ATOM   1712 C  CE  . LYS A 1 210 ? -28.455 -31.418 30.071  1.00 73.44  ? 210 LYS A CE  1 
ATOM   1713 N  NZ  . LYS A 1 210 ? -29.189 -30.183 30.477  1.00 68.73  ? 210 LYS A NZ  1 
ATOM   1714 N  N   . VAL A 1 211 ? -24.174 -28.068 27.791  1.00 47.93  ? 211 VAL A N   1 
ATOM   1715 C  CA  . VAL A 1 211 ? -23.594 -27.070 28.687  1.00 50.67  ? 211 VAL A CA  1 
ATOM   1716 C  C   . VAL A 1 211 ? -23.702 -25.682 28.089  1.00 53.17  ? 211 VAL A C   1 
ATOM   1717 O  O   . VAL A 1 211 ? -23.860 -24.679 28.805  1.00 48.78  ? 211 VAL A O   1 
ATOM   1718 C  CB  . VAL A 1 211 ? -22.124 -27.426 28.985  1.00 50.23  ? 211 VAL A CB  1 
ATOM   1719 C  CG1 . VAL A 1 211 ? -21.411 -26.252 29.613  1.00 49.81  ? 211 VAL A CG1 1 
ATOM   1720 C  CG2 . VAL A 1 211 ? -22.052 -28.655 29.904  1.00 50.62  ? 211 VAL A CG2 1 
ATOM   1721 N  N   . MET A 1 212 ? -23.594 -25.609 26.771  1.00 49.37  ? 212 MET A N   1 
ATOM   1722 C  CA  . MET A 1 212 ? -23.474 -24.358 26.052  1.00 46.83  ? 212 MET A CA  1 
ATOM   1723 C  C   . MET A 1 212 ? -24.869 -23.741 25.913  1.00 47.16  ? 212 MET A C   1 
ATOM   1724 O  O   . MET A 1 212 ? -25.090 -22.573 26.248  1.00 47.58  ? 212 MET A O   1 
ATOM   1725 C  CB  . MET A 1 212 ? -22.824 -24.721 24.705  1.00 48.18  ? 212 MET A CB  1 
ATOM   1726 C  CG  . MET A 1 212 ? -21.297 -24.465 24.637  1.00 46.19  ? 212 MET A CG  1 
ATOM   1727 S  SD  . MET A 1 212 ? -20.636 -24.157 22.991  1.00 44.45  ? 212 MET A SD  1 
ATOM   1728 C  CE  . MET A 1 212 ? -20.741 -25.778 22.291  1.00 37.68  ? 212 MET A CE  1 
ATOM   1729 N  N   . ASN A 1 213 ? -25.838 -24.567 25.513  1.00 44.22  ? 213 ASN A N   1 
ATOM   1730 C  CA  . ASN A 1 213 ? -27.231 -24.134 25.408  1.00 49.39  ? 213 ASN A CA  1 
ATOM   1731 C  C   . ASN A 1 213 ? -27.796 -23.720 26.764  1.00 51.96  ? 213 ASN A C   1 
ATOM   1732 O  O   . ASN A 1 213 ? -28.417 -22.657 26.889  1.00 53.22  ? 213 ASN A O   1 
ATOM   1733 C  CB  . ASN A 1 213 ? -28.062 -25.262 24.808  1.00 48.27  ? 213 ASN A CB  1 
ATOM   1734 C  CG  . ASN A 1 213 ? -27.749 -25.488 23.353  1.00 50.63  ? 213 ASN A CG  1 
ATOM   1735 O  OD1 . ASN A 1 213 ? -27.009 -24.714 22.750  1.00 51.51  ? 213 ASN A OD1 1 
ATOM   1736 N  ND2 . ASN A 1 213 ? -28.309 -26.546 22.777  1.00 44.51  ? 213 ASN A ND2 1 
ATOM   1737 N  N   . ASP A 1 214 ? -27.583 -24.551 27.796  1.00 52.58  ? 214 ASP A N   1 
ATOM   1738 C  CA  . ASP A 1 214 ? -28.149 -24.271 29.118  1.00 54.99  ? 214 ASP A CA  1 
ATOM   1739 C  C   . ASP A 1 214 ? -27.608 -22.970 29.705  1.00 53.68  ? 214 ASP A C   1 
ATOM   1740 O  O   . ASP A 1 214 ? -28.372 -22.184 30.277  1.00 50.80  ? 214 ASP A O   1 
ATOM   1741 C  CB  . ASP A 1 214 ? -27.883 -25.441 30.068  1.00 54.25  ? 214 ASP A CB  1 
ATOM   1742 C  CG  . ASP A 1 214 ? -28.717 -26.663 29.739  1.00 62.09  ? 214 ASP A CG  1 
ATOM   1743 O  OD1 . ASP A 1 214 ? -29.592 -26.565 28.846  1.00 57.14  ? 214 ASP A OD1 1 
ATOM   1744 O  OD2 . ASP A 1 214 ? -28.498 -27.727 30.369  1.00 59.92  ? 214 ASP A OD2 1 
ATOM   1745 N  N   . LEU A 1 215 ? -26.295 -22.719 29.578  1.00 51.91  ? 215 LEU A N   1 
ATOM   1746 C  CA  . LEU A 1 215 ? -25.732 -21.479 30.120  1.00 48.38  ? 215 LEU A CA  1 
ATOM   1747 C  C   . LEU A 1 215 ? -26.181 -20.256 29.330  1.00 50.58  ? 215 LEU A C   1 
ATOM   1748 O  O   . LEU A 1 215 ? -26.423 -19.195 29.918  1.00 51.36  ? 215 LEU A O   1 
ATOM   1749 C  CB  . LEU A 1 215 ? -24.199 -21.544 30.164  1.00 55.76  ? 215 LEU A CB  1 
ATOM   1750 C  CG  . LEU A 1 215 ? -23.356 -20.357 30.707  1.00 56.66  ? 215 LEU A CG  1 
ATOM   1751 C  CD1 . LEU A 1 215 ? -23.465 -19.050 29.897  1.00 55.16  ? 215 LEU A CD1 1 
ATOM   1752 C  CD2 . LEU A 1 215 ? -23.635 -20.068 32.193  1.00 67.46  ? 215 LEU A CD2 1 
ATOM   1753 N  N   . VAL A 1 216 ? -26.244 -20.357 27.997  1.00 48.02  ? 216 VAL A N   1 
ATOM   1754 C  CA  . VAL A 1 216 ? -26.704 -19.219 27.203  1.00 47.29  ? 216 VAL A CA  1 
ATOM   1755 C  C   . VAL A 1 216 ? -28.184 -18.955 27.450  1.00 43.05  ? 216 VAL A C   1 
ATOM   1756 O  O   . VAL A 1 216 ? -28.599 -17.809 27.661  1.00 41.83  ? 216 VAL A O   1 
ATOM   1757 C  CB  . VAL A 1 216 ? -26.426 -19.434 25.702  1.00 44.61  ? 216 VAL A CB  1 
ATOM   1758 C  CG1 . VAL A 1 216 ? -26.756 -18.153 24.941  1.00 41.05  ? 216 VAL A CG1 1 
ATOM   1759 C  CG2 . VAL A 1 216 ? -24.963 -19.799 25.474  1.00 45.71  ? 216 VAL A CG2 1 
ATOM   1760 N  N   . ASP A 1 217 ? -29.002 -20.009 27.406  1.00 48.99  ? 217 ASP A N   1 
ATOM   1761 C  CA  . ASP A 1 217 ? -30.432 -19.841 27.656  1.00 49.13  ? 217 ASP A CA  1 
ATOM   1762 C  C   . ASP A 1 217 ? -30.685 -19.207 29.018  1.00 51.37  ? 217 ASP A C   1 
ATOM   1763 O  O   . ASP A 1 217 ? -31.637 -18.436 29.184  1.00 53.05  ? 217 ASP A O   1 
ATOM   1764 C  CB  . ASP A 1 217 ? -31.143 -21.187 27.566  1.00 47.96  ? 217 ASP A CB  1 
ATOM   1765 C  CG  . ASP A 1 217 ? -31.130 -21.754 26.182  1.00 50.03  ? 217 ASP A CG  1 
ATOM   1766 O  OD1 . ASP A 1 217 ? -30.804 -21.011 25.235  1.00 51.19  ? 217 ASP A OD1 1 
ATOM   1767 O  OD2 . ASP A 1 217 ? -31.421 -22.957 26.045  1.00 51.15  ? 217 ASP A OD2 1 
ATOM   1768 N  N   . LYS A 1 218 ? -29.853 -19.536 30.012  1.00 50.73  ? 218 LYS A N   1 
ATOM   1769 C  CA  . LYS A 1 218 ? -29.965 -18.896 31.320  1.00 51.78  ? 218 LYS A CA  1 
ATOM   1770 C  C   . LYS A 1 218 ? -29.642 -17.412 31.246  1.00 50.11  ? 218 LYS A C   1 
ATOM   1771 O  O   . LYS A 1 218 ? -30.330 -16.589 31.858  1.00 48.19  ? 218 LYS A O   1 
ATOM   1772 C  CB  . LYS A 1 218 ? -29.044 -19.575 32.333  1.00 52.87  ? 218 LYS A CB  1 
ATOM   1773 C  CG  . LYS A 1 218 ? -29.169 -18.987 33.744  1.00 58.52  ? 218 LYS A CG  1 
ATOM   1774 C  CD  . LYS A 1 218 ? -29.068 -20.042 34.832  1.00 61.44  ? 218 LYS A CD  1 
ATOM   1775 C  CE  . LYS A 1 218 ? -30.013 -19.722 35.985  1.00 68.43  ? 218 LYS A CE  1 
ATOM   1776 N  NZ  . LYS A 1 218 ? -29.890 -18.289 36.382  1.00 67.47  ? 218 LYS A NZ  1 
ATOM   1777 N  N   . ILE A 1 219 ? -28.577 -17.048 30.531  1.00 46.37  ? 219 ILE A N   1 
ATOM   1778 C  CA  . ILE A 1 219 ? -28.233 -15.635 30.404  1.00 45.89  ? 219 ILE A CA  1 
ATOM   1779 C  C   . ILE A 1 219 ? -29.358 -14.875 29.721  1.00 43.64  ? 219 ILE A C   1 
ATOM   1780 O  O   . ILE A 1 219 ? -29.703 -13.752 30.113  1.00 47.29  ? 219 ILE A O   1 
ATOM   1781 C  CB  . ILE A 1 219 ? -26.908 -15.477 29.639  1.00 46.06  ? 219 ILE A CB  1 
ATOM   1782 C  CG1 . ILE A 1 219 ? -25.786 -16.186 30.393  1.00 49.08  ? 219 ILE A CG1 1 
ATOM   1783 C  CG2 . ILE A 1 219 ? -26.598 -14.010 29.448  1.00 54.45  ? 219 ILE A CG2 1 
ATOM   1784 C  CD1 . ILE A 1 219 ? -25.012 -15.249 31.253  1.00 47.91  ? 219 ILE A CD1 1 
ATOM   1785 N  N   . ILE A 1 220 ? -29.935 -15.464 28.675  1.00 44.32  ? 220 ILE A N   1 
ATOM   1786 C  CA  . ILE A 1 220 ? -31.044 -14.810 27.989  1.00 44.29  ? 220 ILE A CA  1 
ATOM   1787 C  C   . ILE A 1 220 ? -32.220 -14.647 28.946  1.00 51.42  ? 220 ILE A C   1 
ATOM   1788 O  O   . ILE A 1 220 ? -32.741 -13.540 29.149  1.00 48.46  ? 220 ILE A O   1 
ATOM   1789 C  CB  . ILE A 1 220 ? -31.443 -15.610 26.737  1.00 49.02  ? 220 ILE A CB  1 
ATOM   1790 C  CG1 . ILE A 1 220 ? -30.322 -15.564 25.695  1.00 45.05  ? 220 ILE A CG1 1 
ATOM   1791 C  CG2 . ILE A 1 220 ? -32.745 -15.064 26.148  1.00 48.93  ? 220 ILE A CG2 1 
ATOM   1792 C  CD1 . ILE A 1 220 ? -30.475 -16.591 24.594  1.00 45.36  ? 220 ILE A CD1 1 
ATOM   1793 N  N   . ALA A 1 221 ? -32.637 -15.754 29.566  1.00 48.98  ? 221 ALA A N   1 
ATOM   1794 C  CA  . ALA A 1 221 ? -33.744 -15.716 30.517  1.00 52.87  ? 221 ALA A CA  1 
ATOM   1795 C  C   . ALA A 1 221 ? -33.490 -14.687 31.613  1.00 50.63  ? 221 ALA A C   1 
ATOM   1796 O  O   . ALA A 1 221 ? -34.344 -13.836 31.890  1.00 57.99  ? 221 ALA A O   1 
ATOM   1797 C  CB  . ALA A 1 221 ? -33.959 -17.110 31.103  1.00 51.42  ? 221 ALA A CB  1 
ATOM   1798 N  N   . ASP A 1 222 ? -32.301 -14.729 32.225  1.00 54.39  ? 222 ASP A N   1 
ATOM   1799 C  CA  . ASP A 1 222 ? -31.979 -13.808 33.314  1.00 53.62  ? 222 ASP A CA  1 
ATOM   1800 C  C   . ASP A 1 222 ? -32.078 -12.354 32.866  1.00 57.33  ? 222 ASP A C   1 
ATOM   1801 O  O   . ASP A 1 222 ? -32.581 -11.502 33.609  1.00 56.49  ? 222 ASP A O   1 
ATOM   1802 C  CB  . ASP A 1 222 ? -30.574 -14.092 33.858  1.00 57.32  ? 222 ASP A CB  1 
ATOM   1803 C  CG  . ASP A 1 222 ? -30.487 -15.402 34.652  1.00 59.56  ? 222 ASP A CG  1 
ATOM   1804 O  OD1 . ASP A 1 222 ? -31.533 -16.017 34.958  1.00 59.07  ? 222 ASP A OD1 1 
ATOM   1805 O  OD2 . ASP A 1 222 ? -29.351 -15.816 34.971  1.00 65.49  ? 222 ASP A OD2 1 
ATOM   1806 N  N   . ARG A 1 223 ? -31.578 -12.039 31.664  1.00 52.31  ? 223 ARG A N   1 
ATOM   1807 C  CA  . ARG A 1 223 ? -31.658 -10.661 31.186  1.00 52.60  ? 223 ARG A CA  1 
ATOM   1808 C  C   . ARG A 1 223 ? -33.106 -10.223 30.983  1.00 57.38  ? 223 ARG A C   1 
ATOM   1809 O  O   . ARG A 1 223 ? -33.474 -9.088  31.311  1.00 59.62  ? 223 ARG A O   1 
ATOM   1810 C  CB  . ARG A 1 223 ? -30.886 -10.497 29.883  1.00 47.47  ? 223 ARG A CB  1 
ATOM   1811 C  CG  . ARG A 1 223 ? -31.049 -9.109  29.276  1.00 47.04  ? 223 ARG A CG  1 
ATOM   1812 C  CD  . ARG A 1 223 ? -30.318 -8.049  30.090  1.00 48.37  ? 223 ARG A CD  1 
ATOM   1813 N  NE  . ARG A 1 223 ? -28.889 -8.344  30.126  1.00 48.68  ? 223 ARG A NE  1 
ATOM   1814 C  CZ  . ARG A 1 223 ? -28.027 -7.898  29.223  1.00 48.01  ? 223 ARG A CZ  1 
ATOM   1815 N  NH1 . ARG A 1 223 ? -28.417 -7.125  28.221  1.00 48.42  ? 223 ARG A NH1 1 
ATOM   1816 N  NH2 . ARG A 1 223 ? -26.742 -8.229  29.328  1.00 45.05  ? 223 ARG A NH2 1 
ATOM   1817 N  N   . LYS A 1 224 ? -33.936 -11.107 30.423  1.00 52.52  ? 224 LYS A N   1 
ATOM   1818 C  CA  . LYS A 1 224 ? -35.326 -10.752 30.160  1.00 62.90  ? 224 LYS A CA  1 
ATOM   1819 C  C   . LYS A 1 224 ? -36.084 -10.490 31.457  1.00 64.00  ? 224 LYS A C   1 
ATOM   1820 O  O   . LYS A 1 224 ? -36.843 -9.517  31.557  1.00 66.40  ? 224 LYS A O   1 
ATOM   1821 C  CB  . LYS A 1 224 ? -35.994 -11.856 29.337  1.00 57.20  ? 224 LYS A CB  1 
ATOM   1822 C  CG  . LYS A 1 224 ? -35.916 -11.595 27.845  1.00 63.32  ? 224 LYS A CG  1 
ATOM   1823 C  CD  . LYS A 1 224 ? -35.818 -12.870 27.022  1.00 57.58  ? 224 LYS A CD  1 
ATOM   1824 C  CE  . LYS A 1 224 ? -37.085 -13.696 27.099  1.00 58.89  ? 224 LYS A CE  1 
ATOM   1825 N  NZ  . LYS A 1 224 ? -38.040 -13.291 26.030  1.00 61.43  ? 224 LYS A NZ  1 
ATOM   1826 N  N   . ALA A 1 225 ? -35.878 -11.331 32.468  1.00 62.21  ? 225 ALA A N   1 
ATOM   1827 C  CA  . ALA A 1 225 ? -36.540 -11.124 33.749  1.00 67.49  ? 225 ALA A CA  1 
ATOM   1828 C  C   . ALA A 1 225 ? -35.977 -9.940  34.517  1.00 69.83  ? 225 ALA A C   1 
ATOM   1829 O  O   . ALA A 1 225 ? -36.495 -9.623  35.592  1.00 69.96  ? 225 ALA A O   1 
ATOM   1830 C  CB  . ALA A 1 225 ? -36.435 -12.389 34.602  1.00 61.84  ? 225 ALA A CB  1 
ATOM   1831 N  N   . SER A 1 226 ? -34.943 -9.282  33.996  1.00 70.48  ? 226 SER A N   1 
ATOM   1832 C  CA  . SER A 1 226 ? -34.230 -8.238  34.719  1.00 70.78  ? 226 SER A CA  1 
ATOM   1833 C  C   . SER A 1 226 ? -34.687 -6.833  34.349  1.00 72.08  ? 226 SER A C   1 
ATOM   1834 O  O   . SER A 1 226 ? -34.774 -5.965  35.225  1.00 73.25  ? 226 SER A O   1 
ATOM   1835 C  CB  . SER A 1 226 ? -32.723 -8.371  34.466  1.00 72.13  ? 226 SER A CB  1 
ATOM   1836 O  OG  . SER A 1 226 ? -31.997 -7.342  35.113  1.00 71.11  ? 226 SER A OG  1 
ATOM   1837 N  N   . GLY A 1 227 ? -34.983 -6.585  33.071  1.00 68.53  ? 227 GLY A N   1 
ATOM   1838 C  CA  . GLY A 1 227 ? -35.299 -5.256  32.593  1.00 69.88  ? 227 GLY A CA  1 
ATOM   1839 C  C   . GLY A 1 227 ? -34.109 -4.370  32.277  1.00 74.30  ? 227 GLY A C   1 
ATOM   1840 O  O   . GLY A 1 227 ? -34.262 -3.405  31.516  1.00 72.32  ? 227 GLY A O   1 
ATOM   1841 N  N   . GLU A 1 228 ? -32.930 -4.662  32.833  1.00 77.34  ? 228 GLU A N   1 
ATOM   1842 C  CA  . GLU A 1 228 ? -31.751 -3.824  32.629  1.00 73.96  ? 228 GLU A CA  1 
ATOM   1843 C  C   . GLU A 1 228 ? -31.492 -3.615  31.142  1.00 73.29  ? 228 GLU A C   1 
ATOM   1844 O  O   . GLU A 1 228 ? -31.483 -4.570  30.360  1.00 67.42  ? 228 GLU A O   1 
ATOM   1845 C  CB  . GLU A 1 228 ? -30.535 -4.469  33.301  1.00 73.70  ? 228 GLU A CB  1 
ATOM   1846 C  CG  . GLU A 1 228 ? -29.208 -3.785  33.013  1.00 78.70  ? 228 GLU A CG  1 
ATOM   1847 C  CD  . GLU A 1 228 ? -28.022 -4.714  33.207  1.00 80.34  ? 228 GLU A CD  1 
ATOM   1848 O  OE1 . GLU A 1 228 ? -27.681 -5.001  34.376  1.00 87.55  ? 228 GLU A OE1 1 
ATOM   1849 O  OE2 . GLU A 1 228 ? -27.424 -5.149  32.195  1.00 76.82  ? 228 GLU A OE2 1 
ATOM   1850 N  N   . GLN A 1 229 ? -31.281 -2.358  30.754  1.00 69.89  ? 229 GLN A N   1 
ATOM   1851 C  CA  . GLN A 1 229 ? -31.202 -2.020  29.339  1.00 70.50  ? 229 GLN A CA  1 
ATOM   1852 C  C   . GLN A 1 229 ? -29.792 -1.627  28.921  1.00 71.21  ? 229 GLN A C   1 
ATOM   1853 O  O   . GLN A 1 229 ? -29.599 -0.592  28.274  1.00 71.65  ? 229 GLN A O   1 
ATOM   1854 C  CB  . GLN A 1 229 ? -32.171 -0.885  29.010  1.00 70.53  ? 229 GLN A CB  1 
ATOM   1855 C  CG  . GLN A 1 229 ? -33.621 -1.311  29.006  1.00 71.31  ? 229 GLN A CG  1 
ATOM   1856 C  CD  . GLN A 1 229 ? -33.980 -2.108  27.767  1.00 69.54  ? 229 GLN A CD  1 
ATOM   1857 O  OE1 . GLN A 1 229 ? -33.729 -1.677  26.641  1.00 67.70  ? 229 GLN A OE1 1 
ATOM   1858 N  NE2 . GLN A 1 229 ? -34.574 -3.282  27.971  1.00 67.87  ? 229 GLN A NE2 1 
ATOM   1859 N  N   . SER A 1 230 ? -28.803 -2.441  29.272  1.00 71.91  ? 230 SER A N   1 
ATOM   1860 C  CA  . SER A 1 230 ? -27.433 -2.123  28.900  1.00 70.85  ? 230 SER A CA  1 
ATOM   1861 C  C   . SER A 1 230 ? -27.263 -2.166  27.385  1.00 64.52  ? 230 SER A C   1 
ATOM   1862 O  O   . SER A 1 230 ? -27.880 -2.985  26.694  1.00 65.08  ? 230 SER A O   1 
ATOM   1863 C  CB  . SER A 1 230 ? -26.464 -3.084  29.588  1.00 66.14  ? 230 SER A CB  1 
ATOM   1864 O  OG  . SER A 1 230 ? -27.038 -4.370  29.725  1.00 65.71  ? 230 SER A OG  1 
ATOM   1865 N  N   . ASP A 1 231 ? -26.437 -1.255  26.865  1.00 68.83  ? 231 ASP A N   1 
ATOM   1866 C  CA  . ASP A 1 231 ? -26.141 -1.202  25.432  1.00 69.44  ? 231 ASP A CA  1 
ATOM   1867 C  C   . ASP A 1 231 ? -25.167 -2.332  25.096  1.00 67.62  ? 231 ASP A C   1 
ATOM   1868 O  O   . ASP A 1 231 ? -23.945 -2.164  25.013  1.00 68.46  ? 231 ASP A O   1 
ATOM   1869 C  CB  . ASP A 1 231 ? -25.610 0.176   25.027  1.00 73.28  ? 231 ASP A CB  1 
ATOM   1870 C  CG  . ASP A 1 231 ? -24.274 0.528   25.689  1.00 82.84  ? 231 ASP A CG  1 
ATOM   1871 O  OD1 . ASP A 1 231 ? -23.800 -0.254  26.546  1.00 82.70  ? 231 ASP A OD1 1 
ATOM   1872 O  OD2 . ASP A 1 231 ? -23.689 1.584   25.341  1.00 81.60  ? 231 ASP A OD2 1 
ATOM   1873 N  N   . ASP A 1 232 ? -25.728 -3.523  24.908  1.00 58.64  ? 232 ASP A N   1 
ATOM   1874 C  CA  . ASP A 1 232 ? -24.941 -4.652  24.444  1.00 51.85  ? 232 ASP A CA  1 
ATOM   1875 C  C   . ASP A 1 232 ? -25.772 -5.458  23.453  1.00 47.85  ? 232 ASP A C   1 
ATOM   1876 O  O   . ASP A 1 232 ? -26.979 -5.255  23.299  1.00 48.73  ? 232 ASP A O   1 
ATOM   1877 C  CB  . ASP A 1 232 ? -24.420 -5.497  25.629  1.00 44.36  ? 232 ASP A CB  1 
ATOM   1878 C  CG  . ASP A 1 232 ? -25.540 -6.208  26.422  1.00 44.72  ? 232 ASP A CG  1 
ATOM   1879 O  OD1 . ASP A 1 232 ? -26.668 -6.391  25.913  1.00 43.90  ? 232 ASP A OD1 1 
ATOM   1880 O  OD2 . ASP A 1 232 ? -25.276 -6.584  27.586  1.00 45.70  ? 232 ASP A OD2 1 
ATOM   1881 N  N   . LEU A 1 233 ? -25.096 -6.372  22.766  1.00 46.38  ? 233 LEU A N   1 
ATOM   1882 C  CA  . LEU A 1 233 ? -25.730 -7.133  21.692  1.00 42.08  ? 233 LEU A CA  1 
ATOM   1883 C  C   . LEU A 1 233 ? -26.972 -7.876  22.169  1.00 44.13  ? 233 LEU A C   1 
ATOM   1884 O  O   . LEU A 1 233 ? -27.936 -8.033  21.410  1.00 43.38  ? 233 LEU A O   1 
ATOM   1885 C  CB  . LEU A 1 233 ? -24.720 -8.117  21.103  1.00 38.66  ? 233 LEU A CB  1 
ATOM   1886 C  CG  . LEU A 1 233 ? -23.528 -7.493  20.397  1.00 42.12  ? 233 LEU A CG  1 
ATOM   1887 C  CD1 . LEU A 1 233 ? -22.472 -8.560  20.144  1.00 38.16  ? 233 LEU A CD1 1 
ATOM   1888 C  CD2 . LEU A 1 233 ? -23.985 -6.844  19.082  1.00 39.92  ? 233 LEU A CD2 1 
ATOM   1889 N  N   . LEU A 1 234 ? -26.955 -8.384  23.406  1.00 40.30  ? 234 LEU A N   1 
ATOM   1890 C  CA  . LEU A 1 234 ? -28.096 -9.153  23.883  1.00 42.66  ? 234 LEU A CA  1 
ATOM   1891 C  C   . LEU A 1 234 ? -29.339 -8.270  24.003  1.00 45.64  ? 234 LEU A C   1 
ATOM   1892 O  O   . LEU A 1 234 ? -30.446 -8.695  23.643  1.00 46.32  ? 234 LEU A O   1 
ATOM   1893 C  CB  . LEU A 1 234 ? -27.751 -9.834  25.212  1.00 41.89  ? 234 LEU A CB  1 
ATOM   1894 C  CG  . LEU A 1 234 ? -28.918 -10.489 25.963  1.00 43.46  ? 234 LEU A CG  1 
ATOM   1895 C  CD1 . LEU A 1 234 ? -29.573 -11.558 25.096  1.00 44.67  ? 234 LEU A CD1 1 
ATOM   1896 C  CD2 . LEU A 1 234 ? -28.475 -11.092 27.296  1.00 42.07  ? 234 LEU A CD2 1 
ATOM   1897 N  N   . THR A 1 235 ? -29.169 -7.026  24.462  1.00 44.39  ? 235 THR A N   1 
ATOM   1898 C  CA  . THR A 1 235 ? -30.288 -6.084  24.510  1.00 48.54  ? 235 THR A CA  1 
ATOM   1899 C  C   . THR A 1 235 ? -30.791 -5.742  23.105  1.00 42.73  ? 235 THR A C   1 
ATOM   1900 O  O   . THR A 1 235 ? -31.999 -5.767  22.856  1.00 48.02  ? 235 THR A O   1 
ATOM   1901 C  CB  . THR A 1 235 ? -29.887 -4.809  25.272  1.00 52.21  ? 235 THR A CB  1 
ATOM   1902 O  OG1 . THR A 1 235 ? -29.541 -5.131  26.631  1.00 57.84  ? 235 THR A OG1 1 
ATOM   1903 C  CG2 . THR A 1 235 ? -31.038 -3.799  25.281  1.00 54.12  ? 235 THR A CG2 1 
ATOM   1904 N  N   . HIS A 1 236 ? -29.887 -5.420  22.166  1.00 47.81  ? 236 HIS A N   1 
ATOM   1905 C  CA  . HIS A 1 236 ? -30.342 -5.126  20.803  1.00 47.11  ? 236 HIS A CA  1 
ATOM   1906 C  C   . HIS A 1 236 ? -31.105 -6.297  20.216  1.00 46.79  ? 236 HIS A C   1 
ATOM   1907 O  O   . HIS A 1 236 ? -32.036 -6.109  19.419  1.00 49.05  ? 236 HIS A O   1 
ATOM   1908 C  CB  . HIS A 1 236 ? -29.178 -4.778  19.863  1.00 48.59  ? 236 HIS A CB  1 
ATOM   1909 C  CG  . HIS A 1 236 ? -28.196 -3.798  20.428  1.00 57.45  ? 236 HIS A CG  1 
ATOM   1910 N  ND1 . HIS A 1 236 ? -26.835 -3.898  20.210  1.00 55.07  ? 236 HIS A ND1 1 
ATOM   1911 C  CD2 . HIS A 1 236 ? -28.371 -2.708  21.216  1.00 57.72  ? 236 HIS A CD2 1 
ATOM   1912 C  CE1 . HIS A 1 236 ? -26.219 -2.904  20.828  1.00 56.31  ? 236 HIS A CE1 1 
ATOM   1913 N  NE2 . HIS A 1 236 ? -27.127 -2.171  21.450  1.00 55.91  ? 236 HIS A NE2 1 
ATOM   1914 N  N   . MET A 1 237 ? -30.717 -7.510  20.590  1.00 40.90  ? 237 MET A N   1 
ATOM   1915 C  CA  . MET A 1 237 ? -31.320 -8.713  20.050  1.00 42.76  ? 237 MET A CA  1 
ATOM   1916 C  C   . MET A 1 237 ? -32.689 -8.951  20.678  1.00 49.55  ? 237 MET A C   1 
ATOM   1917 O  O   . MET A 1 237 ? -33.631 -9.376  19.995  1.00 44.62  ? 237 MET A O   1 
ATOM   1918 C  CB  . MET A 1 237 ? -30.347 -9.862  20.295  1.00 44.65  ? 237 MET A CB  1 
ATOM   1919 C  CG  . MET A 1 237 ? -29.385 -10.004 19.123  1.00 41.79  ? 237 MET A CG  1 
ATOM   1920 S  SD  . MET A 1 237 ? -28.527 -11.564 19.043  1.00 40.70  ? 237 MET A SD  1 
ATOM   1921 C  CE  . MET A 1 237 ? -27.567 -11.476 20.568  1.00 38.44  ? 237 MET A CE  1 
ATOM   1922 N  N   . LEU A 1 238 ? -32.821 -8.650  21.972  1.00 47.68  ? 238 LEU A N   1 
ATOM   1923 C  CA  . LEU A 1 238 ? -34.112 -8.765  22.639  1.00 48.87  ? 238 LEU A CA  1 
ATOM   1924 C  C   . LEU A 1 238 ? -35.070 -7.662  22.193  1.00 46.24  ? 238 LEU A C   1 
ATOM   1925 O  O   . LEU A 1 238 ? -36.289 -7.846  22.239  1.00 48.84  ? 238 LEU A O   1 
ATOM   1926 C  CB  . LEU A 1 238 ? -33.907 -8.724  24.158  1.00 47.14  ? 238 LEU A CB  1 
ATOM   1927 C  CG  . LEU A 1 238 ? -33.392 -10.004 24.833  1.00 45.95  ? 238 LEU A CG  1 
ATOM   1928 C  CD1 . LEU A 1 238 ? -33.160 -9.803  26.323  1.00 50.95  ? 238 LEU A CD1 1 
ATOM   1929 C  CD2 . LEU A 1 238 ? -34.354 -11.161 24.612  1.00 48.50  ? 238 LEU A CD2 1 
ATOM   1930 N  N   . ASN A 1 239 ? -34.544 -6.518  21.755  1.00 48.68  ? 239 ASN A N   1 
ATOM   1931 C  CA  . ASN A 1 239 ? -35.373 -5.372  21.425  1.00 53.30  ? 239 ASN A CA  1 
ATOM   1932 C  C   . ASN A 1 239 ? -35.533 -5.111  19.933  1.00 50.16  ? 239 ASN A C   1 
ATOM   1933 O  O   . ASN A 1 239 ? -36.476 -4.416  19.547  1.00 53.16  ? 239 ASN A O   1 
ATOM   1934 C  CB  . ASN A 1 239 ? -34.803 -4.095  22.060  1.00 53.31  ? 239 ASN A CB  1 
ATOM   1935 C  CG  . ASN A 1 239 ? -34.911 -4.087  23.570  1.00 54.54  ? 239 ASN A CG  1 
ATOM   1936 O  OD1 . ASN A 1 239 ? -35.575 -4.936  24.170  1.00 56.45  ? 239 ASN A OD1 1 
ATOM   1937 N  ND2 . ASN A 1 239 ? -34.270 -3.110  24.192  1.00 56.59  ? 239 ASN A ND2 1 
ATOM   1938 N  N   . GLY A 1 240 ? -34.641 -5.605  19.099  1.00 44.31  ? 240 GLY A N   1 
ATOM   1939 C  CA  . GLY A 1 240 ? -34.628 -5.168  17.725  1.00 42.70  ? 240 GLY A CA  1 
ATOM   1940 C  C   . GLY A 1 240 ? -35.701 -5.836  16.895  1.00 43.40  ? 240 GLY A C   1 
ATOM   1941 O  O   . GLY A 1 240 ? -36.176 -6.929  17.190  1.00 46.99  ? 240 GLY A O   1 
ATOM   1942 N  N   . LYS A 1 241 ? -36.080 -5.173  15.814  1.00 44.92  ? 241 LYS A N   1 
ATOM   1943 C  CA  . LYS A 1 241 ? -37.058 -5.747  14.912  1.00 46.20  ? 241 LYS A CA  1 
ATOM   1944 C  C   . LYS A 1 241 ? -36.540 -5.594  13.495  1.00 43.51  ? 241 LYS A C   1 
ATOM   1945 O  O   . LYS A 1 241 ? -35.990 -4.551  13.134  1.00 42.50  ? 241 LYS A O   1 
ATOM   1946 C  CB  . LYS A 1 241 ? -38.440 -5.087  15.104  1.00 49.14  ? 241 LYS A CB  1 
ATOM   1947 C  CG  . LYS A 1 241 ? -39.004 -5.351  16.510  1.00 51.57  ? 241 LYS A CG  1 
ATOM   1948 C  CD  . LYS A 1 241 ? -40.242 -6.233  16.504  1.00 55.78  ? 241 LYS A CD  1 
ATOM   1949 C  CE  . LYS A 1 241 ? -41.522 -5.445  16.815  1.00 62.96  ? 241 LYS A CE  1 
ATOM   1950 N  NZ  . LYS A 1 241 ? -42.743 -6.324  16.884  1.00 63.49  ? 241 LYS A NZ  1 
ATOM   1951 N  N   . ASP A 1 242 ? -36.662 -6.662  12.725  1.00 43.40  ? 242 ASP A N   1 
ATOM   1952 C  CA  . ASP A 1 242 ? -36.232 -6.669  11.336  1.00 46.06  ? 242 ASP A CA  1 
ATOM   1953 C  C   . ASP A 1 242 ? -37.137 -5.747  10.528  1.00 49.57  ? 242 ASP A C   1 
ATOM   1954 O  O   . ASP A 1 242 ? -38.361 -5.938  10.540  1.00 51.80  ? 242 ASP A O   1 
ATOM   1955 C  CB  . ASP A 1 242 ? -36.279 -8.111  10.807  1.00 44.05  ? 242 ASP A CB  1 
ATOM   1956 C  CG  . ASP A 1 242 ? -36.060 -8.206  9.295   1.00 43.49  ? 242 ASP A CG  1 
ATOM   1957 O  OD1 . ASP A 1 242 ? -35.488 -7.278  8.695   1.00 44.37  ? 242 ASP A OD1 1 
ATOM   1958 O  OD2 . ASP A 1 242 ? -36.477 -9.222  8.704   1.00 41.75  ? 242 ASP A OD2 1 
ATOM   1959 N  N   . PRO A 1 243 ? -36.606 -4.716  9.865   1.00 47.92  ? 243 PRO A N   1 
ATOM   1960 C  CA  . PRO A 1 243 ? -37.488 -3.856  9.052   1.00 51.59  ? 243 PRO A CA  1 
ATOM   1961 C  C   . PRO A 1 243 ? -38.255 -4.631  7.990   1.00 54.15  ? 243 PRO A C   1 
ATOM   1962 O  O   . PRO A 1 243 ? -39.425 -4.328  7.730   1.00 60.96  ? 243 PRO A O   1 
ATOM   1963 C  CB  . PRO A 1 243 ? -36.525 -2.839  8.420   1.00 51.96  ? 243 PRO A CB  1 
ATOM   1964 C  CG  . PRO A 1 243 ? -35.255 -2.920  9.188   1.00 52.34  ? 243 PRO A CG  1 
ATOM   1965 C  CD  . PRO A 1 243 ? -35.269 -4.132  10.079  1.00 49.19  ? 243 PRO A CD  1 
ATOM   1966 N  N   . GLU A 1 244 ? -37.626 -5.630  7.369   1.00 53.42  ? 244 GLU A N   1 
ATOM   1967 C  CA  . GLU A 1 244 ? -38.274 -6.436  6.338   1.00 52.02  ? 244 GLU A CA  1 
ATOM   1968 C  C   . GLU A 1 244 ? -39.464 -7.229  6.871   1.00 58.15  ? 244 GLU A C   1 
ATOM   1969 O  O   . GLU A 1 244 ? -40.618 -6.908  6.566   1.00 58.67  ? 244 GLU A O   1 
ATOM   1970 C  CB  . GLU A 1 244 ? -37.273 -7.401  5.705   1.00 50.45  ? 244 GLU A CB  1 
ATOM   1971 C  CG  . GLU A 1 244 ? -37.770 -8.028  4.414   1.00 59.77  ? 244 GLU A CG  1 
ATOM   1972 C  CD  . GLU A 1 244 ? -36.708 -8.857  3.713   1.00 64.26  ? 244 GLU A CD  1 
ATOM   1973 O  OE1 . GLU A 1 244 ? -35.521 -8.748  4.090   1.00 62.24  ? 244 GLU A OE1 1 
ATOM   1974 O  OE2 . GLU A 1 244 ? -37.067 -9.633  2.797   1.00 69.53  ? 244 GLU A OE2 1 
ATOM   1975 N  N   . THR A 1 245 ? -39.189 -8.289  7.642   1.00 53.94  ? 245 THR A N   1 
ATOM   1976 C  CA  . THR A 1 245 ? -40.251 -9.132  8.178   1.00 48.81  ? 245 THR A CA  1 
ATOM   1977 C  C   . THR A 1 245 ? -41.002 -8.454  9.314   1.00 50.71  ? 245 THR A C   1 
ATOM   1978 O  O   . THR A 1 245 ? -42.103 -8.896  9.660   1.00 54.87  ? 245 THR A O   1 
ATOM   1979 C  CB  . THR A 1 245 ? -39.677 -10.470 8.672   1.00 51.38  ? 245 THR A CB  1 
ATOM   1980 O  OG1 . THR A 1 245 ? -38.837 -10.243 9.814   1.00 45.74  ? 245 THR A OG1 1 
ATOM   1981 C  CG2 . THR A 1 245 ? -38.859 -11.158 7.581   1.00 51.27  ? 245 THR A CG2 1 
ATOM   1982 N  N   . GLY A 1 246 ? -40.437 -7.404  9.903   1.00 46.54  ? 246 GLY A N   1 
ATOM   1983 C  CA  . GLY A 1 246 ? -41.014 -6.765  11.072  1.00 48.48  ? 246 GLY A CA  1 
ATOM   1984 C  C   . GLY A 1 246 ? -40.910 -7.549  12.364  1.00 50.10  ? 246 GLY A C   1 
ATOM   1985 O  O   . GLY A 1 246 ? -41.338 -7.046  13.410  1.00 50.02  ? 246 GLY A O   1 
ATOM   1986 N  N   . GLU A 1 247 ? -40.332 -8.752  12.336  1.00 50.94  ? 247 GLU A N   1 
ATOM   1987 C  CA  . GLU A 1 247 ? -40.183 -9.755  13.384  1.00 47.37  ? 247 GLU A CA  1 
ATOM   1988 C  C   . GLU A 1 247 ? -38.877 -9.558  14.166  1.00 48.34  ? 247 GLU A C   1 
ATOM   1989 O  O   . GLU A 1 247 ? -37.848 -9.205  13.582  1.00 47.35  ? 247 GLU A O   1 
ATOM   1990 C  CB  . GLU A 1 247 ? -40.185 -11.155 12.777  1.00 50.01  ? 247 GLU A CB  1 
ATOM   1991 C  CG  . GLU A 1 247 ? -41.364 -11.448 11.876  1.00 50.14  ? 247 GLU A CG  1 
ATOM   1992 C  CD  . GLU A 1 247 ? -41.284 -12.829 11.267  1.00 52.62  ? 247 GLU A CD  1 
ATOM   1993 O  OE1 . GLU A 1 247 ? -40.418 -13.631 11.698  1.00 48.42  ? 247 GLU A OE1 1 
ATOM   1994 O  OE2 . GLU A 1 247 ? -42.108 -13.125 10.379  1.00 56.33  ? 247 GLU A OE2 1 
ATOM   1995 N  N   . PRO A 1 248 ? -38.896 -9.806  15.474  1.00 46.83  ? 248 PRO A N   1 
ATOM   1996 C  CA  . PRO A 1 248 ? -37.656 -9.939  16.236  1.00 44.46  ? 248 PRO A CA  1 
ATOM   1997 C  C   . PRO A 1 248 ? -37.145 -11.376 16.170  1.00 44.18  ? 248 PRO A C   1 
ATOM   1998 O  O   . PRO A 1 248 ? -37.854 -12.306 15.765  1.00 41.57  ? 248 PRO A O   1 
ATOM   1999 C  CB  . PRO A 1 248 ? -38.101 -9.572  17.657  1.00 42.32  ? 248 PRO A CB  1 
ATOM   2000 C  CG  . PRO A 1 248 ? -39.486 -10.139 17.731  1.00 42.79  ? 248 PRO A CG  1 
ATOM   2001 C  CD  . PRO A 1 248 ? -40.077 -10.000 16.336  1.00 46.24  ? 248 PRO A CD  1 
ATOM   2002 N  N   . LEU A 1 249 ? -35.884 -11.544 16.562  1.00 39.71  ? 249 LEU A N   1 
ATOM   2003 C  CA  . LEU A 1 249 ? -35.334 -12.884 16.710  1.00 40.99  ? 249 LEU A CA  1 
ATOM   2004 C  C   . LEU A 1 249 ? -36.027 -13.593 17.866  1.00 40.14  ? 249 LEU A C   1 
ATOM   2005 O  O   . LEU A 1 249 ? -36.403 -12.965 18.854  1.00 40.03  ? 249 LEU A O   1 
ATOM   2006 C  CB  . LEU A 1 249 ? -33.828 -12.813 16.981  1.00 36.08  ? 249 LEU A CB  1 
ATOM   2007 C  CG  . LEU A 1 249 ? -32.983 -12.105 15.912  1.00 35.59  ? 249 LEU A CG  1 
ATOM   2008 C  CD1 . LEU A 1 249 ? -31.472 -12.200 16.235  1.00 36.85  ? 249 LEU A CD1 1 
ATOM   2009 C  CD2 . LEU A 1 249 ? -33.258 -12.725 14.572  1.00 41.62  ? 249 LEU A CD2 1 
ATOM   2010 N  N   . ASP A 1 250 ? -36.192 -14.910 17.751  1.00 40.79  ? 250 ASP A N   1 
ATOM   2011 C  CA  . ASP A 1 250 ? -36.695 -15.647 18.902  1.00 43.06  ? 250 ASP A CA  1 
ATOM   2012 C  C   . ASP A 1 250 ? -35.532 -16.141 19.761  1.00 45.13  ? 250 ASP A C   1 
ATOM   2013 O  O   . ASP A 1 250 ? -34.357 -16.059 19.381  1.00 39.29  ? 250 ASP A O   1 
ATOM   2014 C  CB  . ASP A 1 250 ? -37.619 -16.800 18.483  1.00 45.61  ? 250 ASP A CB  1 
ATOM   2015 C  CG  . ASP A 1 250 ? -36.912 -17.903 17.702  1.00 46.64  ? 250 ASP A CG  1 
ATOM   2016 O  OD1 . ASP A 1 250 ? -35.666 -18.020 17.733  1.00 45.18  ? 250 ASP A OD1 1 
ATOM   2017 O  OD2 . ASP A 1 250 ? -37.633 -18.685 17.058  1.00 48.70  ? 250 ASP A OD2 1 
ATOM   2018 N  N   . ASP A 1 251 ? -35.878 -16.653 20.949  1.00 46.12  ? 251 ASP A N   1 
ATOM   2019 C  CA  . ASP A 1 251 ? -34.865 -16.905 21.972  1.00 44.68  ? 251 ASP A CA  1 
ATOM   2020 C  C   . ASP A 1 251 ? -33.886 -17.988 21.533  1.00 42.22  ? 251 ASP A C   1 
ATOM   2021 O  O   . ASP A 1 251 ? -32.696 -17.927 21.862  1.00 42.19  ? 251 ASP A O   1 
ATOM   2022 C  CB  . ASP A 1 251 ? -35.534 -17.302 23.294  1.00 49.94  ? 251 ASP A CB  1 
ATOM   2023 C  CG  . ASP A 1 251 ? -36.194 -16.122 24.010  1.00 51.40  ? 251 ASP A CG  1 
ATOM   2024 O  OD1 . ASP A 1 251 ? -36.009 -14.958 23.595  1.00 48.68  ? 251 ASP A OD1 1 
ATOM   2025 O  OD2 . ASP A 1 251 ? -36.909 -16.375 25.003  1.00 55.62  ? 251 ASP A OD2 1 
ATOM   2026 N  N   . GLU A 1 252 ? -34.371 -19.010 20.829  1.00 38.96  ? 252 GLU A N   1 
ATOM   2027 C  CA  . GLU A 1 252 ? -33.460 -20.016 20.299  1.00 42.97  ? 252 GLU A CA  1 
ATOM   2028 C  C   . GLU A 1 252 ? -32.441 -19.396 19.352  1.00 41.83  ? 252 GLU A C   1 
ATOM   2029 O  O   . GLU A 1 252 ? -31.248 -19.705 19.422  1.00 39.61  ? 252 GLU A O   1 
ATOM   2030 C  CB  . GLU A 1 252 ? -34.220 -21.114 19.569  1.00 41.89  ? 252 GLU A CB  1 
ATOM   2031 C  CG  . GLU A 1 252 ? -33.283 -22.223 19.091  1.00 50.70  ? 252 GLU A CG  1 
ATOM   2032 C  CD  . GLU A 1 252 ? -33.963 -23.252 18.220  1.00 52.40  ? 252 GLU A CD  1 
ATOM   2033 O  OE1 . GLU A 1 252 ? -34.783 -24.024 18.752  1.00 61.03  ? 252 GLU A OE1 1 
ATOM   2034 O  OE2 . GLU A 1 252 ? -33.670 -23.299 17.006  1.00 61.06  ? 252 GLU A OE2 1 
ATOM   2035 N  N   . ASN A 1 253 ? -32.887 -18.530 18.443  1.00 39.70  ? 253 ASN A N   1 
ATOM   2036 C  CA  . ASN A 1 253 ? -31.910 -17.954 17.524  1.00 37.90  ? 253 ASN A CA  1 
ATOM   2037 C  C   . ASN A 1 253 ? -30.975 -16.984 18.243  1.00 40.18  ? 253 ASN A C   1 
ATOM   2038 O  O   . ASN A 1 253 ? -29.773 -16.938 17.943  1.00 37.14  ? 253 ASN A O   1 
ATOM   2039 C  CB  . ASN A 1 253 ? -32.597 -17.271 16.347  1.00 35.24  ? 253 ASN A CB  1 
ATOM   2040 C  CG  . ASN A 1 253 ? -31.590 -16.773 15.318  1.00 35.59  ? 253 ASN A CG  1 
ATOM   2041 O  OD1 . ASN A 1 253 ? -31.231 -15.589 15.291  1.00 35.32  ? 253 ASN A OD1 1 
ATOM   2042 N  ND2 . ASN A 1 253 ? -31.102 -17.686 14.490  1.00 34.10  ? 253 ASN A ND2 1 
ATOM   2043 N  N   . ILE A 1 254 ? -31.487 -16.216 19.210  1.00 39.73  ? 254 ILE A N   1 
ATOM   2044 C  CA  . ILE A 1 254 ? -30.592 -15.361 19.992  1.00 41.17  ? 254 ILE A CA  1 
ATOM   2045 C  C   . ILE A 1 254 ? -29.503 -16.200 20.658  1.00 40.54  ? 254 ILE A C   1 
ATOM   2046 O  O   . ILE A 1 254 ? -28.326 -15.812 20.684  1.00 40.36  ? 254 ILE A O   1 
ATOM   2047 C  CB  . ILE A 1 254 ? -31.371 -14.525 21.028  1.00 41.58  ? 254 ILE A CB  1 
ATOM   2048 C  CG1 . ILE A 1 254 ? -32.270 -13.488 20.345  1.00 37.58  ? 254 ILE A CG1 1 
ATOM   2049 C  CG2 . ILE A 1 254 ? -30.395 -13.811 21.973  1.00 40.84  ? 254 ILE A CG2 1 
ATOM   2050 C  CD1 . ILE A 1 254 ? -33.457 -13.026 21.193  1.00 45.39  ? 254 ILE A CD1 1 
ATOM   2051 N  N   . ARG A 1 255 ? -29.872 -17.357 21.213  1.00 42.32  ? 255 ARG A N   1 
ATOM   2052 C  CA  . ARG A 1 255 ? -28.860 -18.249 21.783  1.00 40.38  ? 255 ARG A CA  1 
ATOM   2053 C  C   . ARG A 1 255 ? -27.802 -18.612 20.739  1.00 39.73  ? 255 ARG A C   1 
ATOM   2054 O  O   . ARG A 1 255 ? -26.594 -18.588 21.016  1.00 37.26  ? 255 ARG A O   1 
ATOM   2055 C  CB  . ARG A 1 255 ? -29.516 -19.514 22.343  1.00 38.92  ? 255 ARG A CB  1 
ATOM   2056 C  CG  . ARG A 1 255 ? -28.507 -20.621 22.684  1.00 37.64  ? 255 ARG A CG  1 
ATOM   2057 C  CD  . ARG A 1 255 ? -28.920 -21.948 22.112  1.00 44.61  ? 255 ARG A CD  1 
ATOM   2058 N  NE  . ARG A 1 255 ? -30.110 -22.475 22.770  1.00 46.91  ? 255 ARG A NE  1 
ATOM   2059 C  CZ  . ARG A 1 255 ? -30.743 -23.582 22.406  1.00 50.62  ? 255 ARG A CZ  1 
ATOM   2060 N  NH1 . ARG A 1 255 ? -30.362 -24.280 21.348  1.00 50.70  ? 255 ARG A NH1 1 
ATOM   2061 N  NH2 . ARG A 1 255 ? -31.784 -24.001 23.122  1.00 47.31  ? 255 ARG A NH2 1 
ATOM   2062 N  N   . TYR A 1 256 ? -28.243 -18.956 19.527  1.00 35.93  ? 256 TYR A N   1 
ATOM   2063 C  CA  . TYR A 1 256 ? -27.291 -19.298 18.475  1.00 36.27  ? 256 TYR A CA  1 
ATOM   2064 C  C   . TYR A 1 256 ? -26.389 -18.116 18.136  1.00 35.68  ? 256 TYR A C   1 
ATOM   2065 O  O   . TYR A 1 256 ? -25.177 -18.298 17.932  1.00 35.50  ? 256 TYR A O   1 
ATOM   2066 C  CB  . TYR A 1 256 ? -28.045 -19.795 17.244  1.00 34.72  ? 256 TYR A CB  1 
ATOM   2067 C  CG  . TYR A 1 256 ? -28.560 -21.200 17.435  1.00 42.38  ? 256 TYR A CG  1 
ATOM   2068 C  CD1 . TYR A 1 256 ? -27.819 -22.131 18.149  1.00 43.49  ? 256 TYR A CD1 1 
ATOM   2069 C  CD2 . TYR A 1 256 ? -29.814 -21.580 16.968  1.00 40.03  ? 256 TYR A CD2 1 
ATOM   2070 C  CE1 . TYR A 1 256 ? -28.291 -23.425 18.357  1.00 44.61  ? 256 TYR A CE1 1 
ATOM   2071 C  CE2 . TYR A 1 256 ? -30.294 -22.872 17.176  1.00 45.94  ? 256 TYR A CE2 1 
ATOM   2072 C  CZ  . TYR A 1 256 ? -29.526 -23.786 17.868  1.00 47.54  ? 256 TYR A CZ  1 
ATOM   2073 O  OH  . TYR A 1 256 ? -29.977 -25.074 18.075  1.00 55.34  ? 256 TYR A OH  1 
ATOM   2074 N  N   . GLN A 1 257 ? -26.945 -16.892 18.083  1.00 34.15  ? 257 GLN A N   1 
ATOM   2075 C  CA  . GLN A 1 257 ? -26.108 -15.728 17.794  1.00 33.10  ? 257 GLN A CA  1 
ATOM   2076 C  C   . GLN A 1 257 ? -25.046 -15.537 18.872  1.00 33.22  ? 257 GLN A C   1 
ATOM   2077 O  O   . GLN A 1 257 ? -23.876 -15.273 18.558  1.00 33.23  ? 257 GLN A O   1 
ATOM   2078 C  CB  . GLN A 1 257 ? -26.935 -14.442 17.649  1.00 37.42  ? 257 GLN A CB  1 
ATOM   2079 C  CG  . GLN A 1 257 ? -28.053 -14.452 16.597  1.00 33.84  ? 257 GLN A CG  1 
ATOM   2080 C  CD  . GLN A 1 257 ? -27.574 -14.763 15.181  1.00 37.09  ? 257 GLN A CD  1 
ATOM   2081 O  OE1 . GLN A 1 257 ? -26.366 -14.728 14.878  1.00 34.04  ? 257 GLN A OE1 1 
ATOM   2082 N  NE2 . GLN A 1 257 ? -28.531 -15.080 14.298  1.00 30.18  ? 257 GLN A NE2 1 
ATOM   2083 N  N   . ILE A 1 258 ? -25.431 -15.672 20.151  1.00 36.03  ? 258 ILE A N   1 
ATOM   2084 C  CA  . ILE A 1 258 ? -24.469 -15.477 21.237  1.00 34.68  ? 258 ILE A CA  1 
ATOM   2085 C  C   . ILE A 1 258 ? -23.360 -16.520 21.163  1.00 34.71  ? 258 ILE A C   1 
ATOM   2086 O  O   . ILE A 1 258 ? -22.176 -16.197 21.337  1.00 36.30  ? 258 ILE A O   1 
ATOM   2087 C  CB  . ILE A 1 258 ? -25.178 -15.497 22.611  1.00 37.14  ? 258 ILE A CB  1 
ATOM   2088 C  CG1 . ILE A 1 258 ? -26.080 -14.271 22.782  1.00 40.32  ? 258 ILE A CG1 1 
ATOM   2089 C  CG2 . ILE A 1 258 ? -24.155 -15.530 23.751  1.00 37.64  ? 258 ILE A CG2 1 
ATOM   2090 C  CD1 . ILE A 1 258 ? -26.965 -14.333 24.063  1.00 41.09  ? 258 ILE A CD1 1 
ATOM   2091 N  N   . ILE A 1 259 ? -23.719 -17.789 20.930  1.00 33.65  ? 259 ILE A N   1 
ATOM   2092 C  CA  . ILE A 1 259 ? -22.696 -18.815 20.750  1.00 31.93  ? 259 ILE A CA  1 
ATOM   2093 C  C   . ILE A 1 259 ? -21.781 -18.428 19.597  1.00 34.98  ? 259 ILE A C   1 
ATOM   2094 O  O   . ILE A 1 259 ? -20.550 -18.463 19.715  1.00 32.90  ? 259 ILE A O   1 
ATOM   2095 C  CB  . ILE A 1 259 ? -23.359 -20.194 20.539  1.00 36.66  ? 259 ILE A CB  1 
ATOM   2096 C  CG1 . ILE A 1 259 ? -24.029 -20.686 21.843  1.00 33.16  ? 259 ILE A CG1 1 
ATOM   2097 C  CG2 . ILE A 1 259 ? -22.381 -21.240 20.022  1.00 34.90  ? 259 ILE A CG2 1 
ATOM   2098 C  CD1 . ILE A 1 259 ? -24.869 -21.945 21.636  1.00 35.30  ? 259 ILE A CD1 1 
ATOM   2099 N  N   . THR A 1 260 ? -22.374 -17.964 18.498  1.00 33.59  ? 260 THR A N   1 
ATOM   2100 C  CA  . THR A 1 260 ? -21.608 -17.572 17.313  1.00 32.98  ? 260 THR A CA  1 
ATOM   2101 C  C   . THR A 1 260 ? -20.617 -16.446 17.612  1.00 33.74  ? 260 THR A C   1 
ATOM   2102 O  O   . THR A 1 260 ? -19.447 -16.497 17.193  1.00 33.65  ? 260 THR A O   1 
ATOM   2103 C  CB  . THR A 1 260 ? -22.579 -17.144 16.213  1.00 32.25  ? 260 THR A CB  1 
ATOM   2104 O  OG1 . THR A 1 260 ? -23.414 -18.253 15.863  1.00 33.64  ? 260 THR A OG1 1 
ATOM   2105 C  CG2 . THR A 1 260 ? -21.810 -16.656 14.982  1.00 31.18  ? 260 THR A CG2 1 
ATOM   2106 N  N   . PHE A 1 261 ? -21.078 -15.388 18.282  1.00 30.23  ? 261 PHE A N   1 
ATOM   2107 C  CA  . PHE A 1 261 ? -20.188 -14.271 18.595  1.00 33.97  ? 261 PHE A CA  1 
ATOM   2108 C  C   . PHE A 1 261 ? -19.073 -14.697 19.537  1.00 35.30  ? 261 PHE A C   1 
ATOM   2109 O  O   . PHE A 1 261 ? -17.941 -14.214 19.423  1.00 37.69  ? 261 PHE A O   1 
ATOM   2110 C  CB  . PHE A 1 261 ? -20.967 -13.113 19.220  1.00 37.33  ? 261 PHE A CB  1 
ATOM   2111 C  CG  . PHE A 1 261 ? -21.985 -12.511 18.313  1.00 37.56  ? 261 PHE A CG  1 
ATOM   2112 C  CD1 . PHE A 1 261 ? -21.697 -12.281 16.984  1.00 36.97  ? 261 PHE A CD1 1 
ATOM   2113 C  CD2 . PHE A 1 261 ? -23.243 -12.176 18.794  1.00 41.90  ? 261 PHE A CD2 1 
ATOM   2114 C  CE1 . PHE A 1 261 ? -22.644 -11.726 16.138  1.00 37.15  ? 261 PHE A CE1 1 
ATOM   2115 C  CE2 . PHE A 1 261 ? -24.196 -11.620 17.956  1.00 36.55  ? 261 PHE A CE2 1 
ATOM   2116 C  CZ  . PHE A 1 261 ? -23.897 -11.409 16.618  1.00 37.43  ? 261 PHE A CZ  1 
ATOM   2117 N  N   . LEU A 1 262 ? -19.373 -15.588 20.488  1.00 37.22  ? 262 LEU A N   1 
ATOM   2118 C  CA  . LEU A 1 262 ? -18.330 -16.020 21.415  1.00 37.66  ? 262 LEU A CA  1 
ATOM   2119 C  C   . LEU A 1 262 ? -17.295 -16.884 20.710  1.00 39.07  ? 262 LEU A C   1 
ATOM   2120 O  O   . LEU A 1 262 ? -16.097 -16.797 21.015  1.00 39.88  ? 262 LEU A O   1 
ATOM   2121 C  CB  . LEU A 1 262 ? -18.936 -16.769 22.603  1.00 40.02  ? 262 LEU A CB  1 
ATOM   2122 C  CG  . LEU A 1 262 ? -19.837 -15.924 23.505  1.00 39.17  ? 262 LEU A CG  1 
ATOM   2123 C  CD1 . LEU A 1 262 ? -20.526 -16.823 24.506  1.00 43.43  ? 262 LEU A CD1 1 
ATOM   2124 C  CD2 . LEU A 1 262 ? -19.016 -14.863 24.217  1.00 40.46  ? 262 LEU A CD2 1 
ATOM   2125 N  N   . ILE A 1 263 ? -17.731 -17.744 19.785  1.00 35.08  ? 263 ILE A N   1 
ATOM   2126 C  CA  . ILE A 1 263 ? -16.763 -18.458 18.957  1.00 36.53  ? 263 ILE A CA  1 
ATOM   2127 C  C   . ILE A 1 263 ? -15.874 -17.462 18.220  1.00 42.00  ? 263 ILE A C   1 
ATOM   2128 O  O   . ILE A 1 263 ? -14.641 -17.567 18.253  1.00 40.52  ? 263 ILE A O   1 
ATOM   2129 C  CB  . ILE A 1 263 ? -17.471 -19.417 17.983  1.00 37.58  ? 263 ILE A CB  1 
ATOM   2130 C  CG1 . ILE A 1 263 ? -18.072 -20.616 18.730  1.00 38.26  ? 263 ILE A CG1 1 
ATOM   2131 C  CG2 . ILE A 1 263 ? -16.488 -19.906 16.913  1.00 38.62  ? 263 ILE A CG2 1 
ATOM   2132 C  CD1 . ILE A 1 263 ? -19.217 -21.281 17.966  1.00 42.63  ? 263 ILE A CD1 1 
ATOM   2133 N  N   . ALA A 1 264 ? -16.483 -16.461 17.565  1.00 36.84  ? 264 ALA A N   1 
ATOM   2134 C  CA  . ALA A 1 264 ? -15.696 -15.482 16.809  1.00 37.51  ? 264 ALA A CA  1 
ATOM   2135 C  C   . ALA A 1 264 ? -14.736 -14.711 17.708  1.00 43.13  ? 264 ALA A C   1 
ATOM   2136 O  O   . ALA A 1 264 ? -13.571 -14.502 17.347  1.00 42.93  ? 264 ALA A O   1 
ATOM   2137 C  CB  . ALA A 1 264 ? -16.616 -14.510 16.072  1.00 35.55  ? 264 ALA A CB  1 
ATOM   2138 N  N   . GLY A 1 265 ? -15.205 -14.266 18.879  1.00 38.57  ? 265 GLY A N   1 
ATOM   2139 C  CA  . GLY A 1 265 ? -14.314 -13.564 19.790  1.00 43.66  ? 265 GLY A CA  1 
ATOM   2140 C  C   . GLY A 1 265 ? -13.124 -14.413 20.196  1.00 43.38  ? 265 GLY A C   1 
ATOM   2141 O  O   . GLY A 1 265 ? -11.971 -14.001 20.052  1.00 48.12  ? 265 GLY A O   1 
ATOM   2142 N  N   . HIS A 1 266 ? -13.393 -15.634 20.670  1.00 35.91  ? 266 HIS A N   1 
ATOM   2143 C  CA  . HIS A 1 266 ? -12.333 -16.520 21.134  1.00 37.96  ? 266 HIS A CA  1 
ATOM   2144 C  C   . HIS A 1 266 ? -11.288 -16.796 20.051  1.00 44.13  ? 266 HIS A C   1 
ATOM   2145 O  O   . HIS A 1 266 ? -10.088 -16.840 20.340  1.00 39.02  ? 266 HIS A O   1 
ATOM   2146 C  CB  . HIS A 1 266 ? -12.960 -17.825 21.618  1.00 41.55  ? 266 HIS A CB  1 
ATOM   2147 C  CG  . HIS A 1 266 ? -12.016 -18.714 22.356  1.00 44.71  ? 266 HIS A CG  1 
ATOM   2148 N  ND1 . HIS A 1 266 ? -11.176 -19.597 21.711  1.00 42.29  ? 266 HIS A ND1 1 
ATOM   2149 C  CD2 . HIS A 1 266 ? -11.791 -18.875 23.683  1.00 40.15  ? 266 HIS A CD2 1 
ATOM   2150 C  CE1 . HIS A 1 266 ? -10.465 -20.257 22.610  1.00 44.03  ? 266 HIS A CE1 1 
ATOM   2151 N  NE2 . HIS A 1 266 ? -10.827 -19.843 23.813  1.00 40.08  ? 266 HIS A NE2 1 
ATOM   2152 N  N   . GLU A 1 267 ? -11.714 -16.963 18.796  1.00 40.51  ? 267 GLU A N   1 
ATOM   2153 C  CA  . GLU A 1 267 ? -10.874 -17.634 17.811  1.00 40.82  ? 267 GLU A CA  1 
ATOM   2154 C  C   . GLU A 1 267 ? -10.129 -16.701 16.850  1.00 41.44  ? 267 GLU A C   1 
ATOM   2155 O  O   . GLU A 1 267 ? -8.990  -16.991 16.468  1.00 43.12  ? 267 GLU A O   1 
ATOM   2156 C  CB  . GLU A 1 267 ? -11.720 -18.615 16.984  1.00 38.05  ? 267 GLU A CB  1 
ATOM   2157 C  CG  . GLU A 1 267 ? -12.248 -19.808 17.758  1.00 42.54  ? 267 GLU A CG  1 
ATOM   2158 C  CD  . GLU A 1 267 ? -11.134 -20.795 18.073  1.00 47.94  ? 267 GLU A CD  1 
ATOM   2159 O  OE1 . GLU A 1 267 ? -10.326 -20.459 18.973  1.00 46.38  ? 267 GLU A OE1 1 
ATOM   2160 O  OE2 . GLU A 1 267 ? -11.005 -21.833 17.384  1.00 48.97  ? 267 GLU A OE2 1 
ATOM   2161 N  N   . THR A 1 268 ? -10.726 -15.598 16.409  1.00 36.68  ? 268 THR A N   1 
ATOM   2162 C  CA  . THR A 1 268 ? -10.205 -14.871 15.247  1.00 35.21  ? 268 THR A CA  1 
ATOM   2163 C  C   . THR A 1 268 ? -9.280  -13.717 15.625  1.00 35.41  ? 268 THR A C   1 
ATOM   2164 O  O   . THR A 1 268 ? -8.114  -13.679 15.215  1.00 34.83  ? 268 THR A O   1 
ATOM   2165 C  CB  . THR A 1 268 ? -11.378 -14.323 14.429  1.00 33.15  ? 268 THR A CB  1 
ATOM   2166 O  OG1 . THR A 1 268 ? -12.216 -13.559 15.306  1.00 37.72  ? 268 THR A OG1 1 
ATOM   2167 C  CG2 . THR A 1 268 ? -12.179 -15.462 13.855  1.00 38.30  ? 268 THR A CG2 1 
ATOM   2168 N  N   . THR A 1 269 ? -9.804  -12.741 16.360  1.00 30.86  ? 269 THR A N   1 
ATOM   2169 C  CA  . THR A 1 269 ? -9.035  -11.536 16.650  1.00 32.93  ? 269 THR A CA  1 
ATOM   2170 C  C   . THR A 1 269 ? -7.804  -11.852 17.495  1.00 32.78  ? 269 THR A C   1 
ATOM   2171 O  O   . THR A 1 269 ? -6.753  -11.214 17.333  1.00 31.59  ? 269 THR A O   1 
ATOM   2172 C  CB  . THR A 1 269 ? -9.934  -10.516 17.350  1.00 36.46  ? 269 THR A CB  1 
ATOM   2173 O  OG1 . THR A 1 269 ? -11.120 -10.309 16.565  1.00 36.21  ? 269 THR A OG1 1 
ATOM   2174 C  CG2 . THR A 1 269 ? -9.215  -9.193  17.541  1.00 32.80  ? 269 THR A CG2 1 
ATOM   2175 N  N   . SER A 1 270 ? -7.901  -12.841 18.386  1.00 32.13  ? 270 SER A N   1 
ATOM   2176 C  CA  . SER A 1 270 ? -6.719  -13.232 19.161  1.00 27.63  ? 270 SER A CA  1 
ATOM   2177 C  C   . SER A 1 270 ? -5.615  -13.768 18.251  1.00 35.68  ? 270 SER A C   1 
ATOM   2178 O  O   . SER A 1 270 ? -4.426  -13.492 18.467  1.00 32.95  ? 270 SER A O   1 
ATOM   2179 C  CB  . SER A 1 270 ? -7.115  -14.283 20.200  1.00 35.04  ? 270 SER A CB  1 
ATOM   2180 O  OG  . SER A 1 270 ? -7.816  -15.349 19.567  1.00 39.26  ? 270 SER A OG  1 
ATOM   2181 N  N   . GLY A 1 271 ? -5.991  -14.554 17.237  1.00 31.21  ? 271 GLY A N   1 
ATOM   2182 C  CA  . GLY A 1 271 ? -5.014  -15.007 16.260  1.00 34.96  ? 271 GLY A CA  1 
ATOM   2183 C  C   . GLY A 1 271 ? -4.361  -13.852 15.532  1.00 35.34  ? 271 GLY A C   1 
ATOM   2184 O  O   . GLY A 1 271 ? -3.135  -13.799 15.397  1.00 32.25  ? 271 GLY A O   1 
ATOM   2185 N  N   . LEU A 1 272 ? -5.177  -12.902 15.055  1.00 33.12  ? 272 LEU A N   1 
ATOM   2186 C  CA  . LEU A 1 272 ? -4.641  -11.725 14.376  1.00 35.86  ? 272 LEU A CA  1 
ATOM   2187 C  C   . LEU A 1 272 ? -3.646  -10.978 15.263  1.00 34.09  ? 272 LEU A C   1 
ATOM   2188 O  O   . LEU A 1 272 ? -2.524  -10.669 14.843  1.00 33.64  ? 272 LEU A O   1 
ATOM   2189 C  CB  . LEU A 1 272 ? -5.796  -10.810 13.933  1.00 31.56  ? 272 LEU A CB  1 
ATOM   2190 C  CG  . LEU A 1 272 ? -5.390  -9.390  13.506  1.00 29.95  ? 272 LEU A CG  1 
ATOM   2191 C  CD1 . LEU A 1 272 ? -4.344  -9.436  12.334  1.00 30.30  ? 272 LEU A CD1 1 
ATOM   2192 C  CD2 . LEU A 1 272 ? -6.591  -8.503  13.165  1.00 31.29  ? 272 LEU A CD2 1 
ATOM   2193 N  N   . LEU A 1 273 ? -4.027  -10.677 16.503  1.00 31.35  ? 273 LEU A N   1 
ATOM   2194 C  CA  . LEU A 1 273 ? -3.109  -9.955  17.371  1.00 32.68  ? 273 LEU A CA  1 
ATOM   2195 C  C   . LEU A 1 273 ? -1.818  -10.742 17.574  1.00 32.14  ? 273 LEU A C   1 
ATOM   2196 O  O   . LEU A 1 273 ? -0.730  -10.162 17.622  1.00 34.96  ? 273 LEU A O   1 
ATOM   2197 C  CB  . LEU A 1 273 ? -3.793  -9.653  18.708  1.00 32.36  ? 273 LEU A CB  1 
ATOM   2198 C  CG  . LEU A 1 273 ? -4.742  -8.455  18.641  1.00 31.81  ? 273 LEU A CG  1 
ATOM   2199 C  CD1 . LEU A 1 273 ? -5.727  -8.489  19.837  1.00 29.51  ? 273 LEU A CD1 1 
ATOM   2200 C  CD2 . LEU A 1 273 ? -3.944  -7.148  18.601  1.00 34.72  ? 273 LEU A CD2 1 
ATOM   2201 N  N   . SER A 1 274 ? -1.922  -12.066 17.694  1.00 33.40  ? 274 SER A N   1 
ATOM   2202 C  CA  . SER A 1 274 ? -0.736  -12.887 17.911  1.00 34.58  ? 274 SER A CA  1 
ATOM   2203 C  C   . SER A 1 274 ? 0.183   -12.840 16.693  1.00 36.49  ? 274 SER A C   1 
ATOM   2204 O  O   . SER A 1 274 ? 1.396   -12.646 16.824  1.00 36.01  ? 274 SER A O   1 
ATOM   2205 C  CB  . SER A 1 274 ? -1.157  -14.322 18.230  1.00 30.66  ? 274 SER A CB  1 
ATOM   2206 O  OG  . SER A 1 274 ? -1.965  -14.365 19.413  1.00 30.39  ? 274 SER A OG  1 
ATOM   2207 N  N   . PHE A 1 275 ? -0.386  -12.992 15.492  1.00 30.29  ? 275 PHE A N   1 
ATOM   2208 C  CA  . PHE A 1 275 ? 0.429   -12.897 14.276  1.00 34.41  ? 275 PHE A CA  1 
ATOM   2209 C  C   . PHE A 1 275 ? 1.015   -11.496 14.095  1.00 35.61  ? 275 PHE A C   1 
ATOM   2210 O  O   . PHE A 1 275 ? 2.150   -11.354 13.616  1.00 34.20  ? 275 PHE A O   1 
ATOM   2211 C  CB  . PHE A 1 275 ? -0.398  -13.285 13.041  1.00 30.39  ? 275 PHE A CB  1 
ATOM   2212 C  CG  . PHE A 1 275 ? -0.527  -14.777 12.825  1.00 32.41  ? 275 PHE A CG  1 
ATOM   2213 C  CD1 . PHE A 1 275 ? 0.600   -15.562 12.596  1.00 33.61  ? 275 PHE A CD1 1 
ATOM   2214 C  CD2 . PHE A 1 275 ? -1.775  -15.387 12.844  1.00 30.12  ? 275 PHE A CD2 1 
ATOM   2215 C  CE1 . PHE A 1 275 ? 0.491   -16.945 12.374  1.00 32.92  ? 275 PHE A CE1 1 
ATOM   2216 C  CE2 . PHE A 1 275 ? -1.916  -16.758 12.624  1.00 34.54  ? 275 PHE A CE2 1 
ATOM   2217 C  CZ  . PHE A 1 275 ? -0.777  -17.554 12.395  1.00 37.21  ? 275 PHE A CZ  1 
ATOM   2218 N  N   . ALA A 1 276 ? 0.259   -10.444 14.438  1.00 30.58  ? 276 ALA A N   1 
ATOM   2219 C  CA  . ALA A 1 276 ? 0.791   -9.085  14.289  1.00 33.41  ? 276 ALA A CA  1 
ATOM   2220 C  C   . ALA A 1 276 ? 2.008   -8.872  15.181  1.00 36.35  ? 276 ALA A C   1 
ATOM   2221 O  O   . ALA A 1 276 ? 3.039   -8.354  14.736  1.00 34.62  ? 276 ALA A O   1 
ATOM   2222 C  CB  . ALA A 1 276 ? -0.285  -8.037  14.595  1.00 32.90  ? 276 ALA A CB  1 
ATOM   2223 N  N   . LEU A 1 277 ? 1.922   -9.287  16.442  1.00 31.67  ? 277 LEU A N   1 
ATOM   2224 C  CA  . LEU A 1 277 ? 3.069   -9.099  17.325  1.00 31.02  ? 277 LEU A CA  1 
ATOM   2225 C  C   . LEU A 1 277 ? 4.257   -9.926  16.853  1.00 33.95  ? 277 LEU A C   1 
ATOM   2226 O  O   . LEU A 1 277 ? 5.403   -9.462  16.895  1.00 32.91  ? 277 LEU A O   1 
ATOM   2227 C  CB  . LEU A 1 277 ? 2.705   -9.456  18.761  1.00 34.72  ? 277 LEU A CB  1 
ATOM   2228 C  CG  . LEU A 1 277 ? 3.843   -9.198  19.756  1.00 37.58  ? 277 LEU A CG  1 
ATOM   2229 C  CD1 . LEU A 1 277 ? 4.210   -7.715  19.764  1.00 35.06  ? 277 LEU A CD1 1 
ATOM   2230 C  CD2 . LEU A 1 277 ? 3.434   -9.655  21.154  1.00 34.90  ? 277 LEU A CD2 1 
ATOM   2231 N  N   . TYR A 1 278 ? 4.001   -11.148 16.388  1.00 32.44  ? 278 TYR A N   1 
ATOM   2232 C  CA  . TYR A 1 278 ? 5.078   -11.956 15.823  1.00 32.87  ? 278 TYR A CA  1 
ATOM   2233 C  C   . TYR A 1 278 ? 5.763   -11.210 14.686  1.00 38.92  ? 278 TYR A C   1 
ATOM   2234 O  O   . TYR A 1 278 ? 6.993   -11.073 14.659  1.00 35.82  ? 278 TYR A O   1 
ATOM   2235 C  CB  . TYR A 1 278 ? 4.523   -13.300 15.336  1.00 35.13  ? 278 TYR A CB  1 
ATOM   2236 C  CG  . TYR A 1 278 ? 5.429   -14.022 14.349  1.00 37.42  ? 278 TYR A CG  1 
ATOM   2237 C  CD1 . TYR A 1 278 ? 6.456   -14.833 14.799  1.00 38.96  ? 278 TYR A CD1 1 
ATOM   2238 C  CD2 . TYR A 1 278 ? 5.273   -13.864 12.975  1.00 38.07  ? 278 TYR A CD2 1 
ATOM   2239 C  CE1 . TYR A 1 278 ? 7.296   -15.486 13.926  1.00 36.10  ? 278 TYR A CE1 1 
ATOM   2240 C  CE2 . TYR A 1 278 ? 6.117   -14.522 12.073  1.00 39.06  ? 278 TYR A CE2 1 
ATOM   2241 C  CZ  . TYR A 1 278 ? 7.136   -15.320 12.564  1.00 40.86  ? 278 TYR A CZ  1 
ATOM   2242 O  OH  . TYR A 1 278 ? 7.993   -15.976 11.718  1.00 36.64  ? 278 TYR A OH  1 
ATOM   2243 N  N   . PHE A 1 279 ? 4.985   -10.719 13.723  1.00 33.10  ? 279 PHE A N   1 
ATOM   2244 C  CA  . PHE A 1 279 ? 5.610   -10.015 12.605  1.00 36.61  ? 279 PHE A CA  1 
ATOM   2245 C  C   . PHE A 1 279 ? 6.334   -8.749  13.061  1.00 37.63  ? 279 PHE A C   1 
ATOM   2246 O  O   . PHE A 1 279 ? 7.373   -8.385  12.486  1.00 38.33  ? 279 PHE A O   1 
ATOM   2247 C  CB  . PHE A 1 279 ? 4.568   -9.700  11.530  1.00 35.28  ? 279 PHE A CB  1 
ATOM   2248 C  CG  . PHE A 1 279 ? 4.266   -10.869 10.641  1.00 32.95  ? 279 PHE A CG  1 
ATOM   2249 C  CD1 . PHE A 1 279 ? 5.266   -11.434 9.864   1.00 33.58  ? 279 PHE A CD1 1 
ATOM   2250 C  CD2 . PHE A 1 279 ? 2.988   -11.413 10.585  1.00 36.32  ? 279 PHE A CD2 1 
ATOM   2251 C  CE1 . PHE A 1 279 ? 4.992   -12.526 9.047   1.00 33.89  ? 279 PHE A CE1 1 
ATOM   2252 C  CE2 . PHE A 1 279 ? 2.714   -12.498 9.777   1.00 32.33  ? 279 PHE A CE2 1 
ATOM   2253 C  CZ  . PHE A 1 279 ? 3.720   -13.062 9.004   1.00 35.10  ? 279 PHE A CZ  1 
ATOM   2254 N  N   . LEU A 1 280 ? 5.830   -8.082  14.097  1.00 33.97  ? 280 LEU A N   1 
ATOM   2255 C  CA  . LEU A 1 280 ? 6.487   -6.868  14.566  1.00 35.42  ? 280 LEU A CA  1 
ATOM   2256 C  C   . LEU A 1 280 ? 7.843   -7.178  15.198  1.00 38.36  ? 280 LEU A C   1 
ATOM   2257 O  O   . LEU A 1 280 ? 8.818   -6.458  14.947  1.00 35.56  ? 280 LEU A O   1 
ATOM   2258 C  CB  . LEU A 1 280 ? 5.584   -6.114  15.542  1.00 33.35  ? 280 LEU A CB  1 
ATOM   2259 C  CG  . LEU A 1 280 ? 4.400   -5.340  14.948  1.00 33.46  ? 280 LEU A CG  1 
ATOM   2260 C  CD1 . LEU A 1 280 ? 3.582   -4.660  16.033  1.00 34.29  ? 280 LEU A CD1 1 
ATOM   2261 C  CD2 . LEU A 1 280 ? 4.879   -4.313  13.938  1.00 38.67  ? 280 LEU A CD2 1 
ATOM   2262 N  N   . VAL A 1 281 ? 7.939   -8.244  16.003  1.00 37.19  ? 281 VAL A N   1 
ATOM   2263 C  CA  . VAL A 1 281 ? 9.240   -8.542  16.617  1.00 35.92  ? 281 VAL A CA  1 
ATOM   2264 C  C   . VAL A 1 281 ? 10.219  -9.087  15.587  1.00 39.12  ? 281 VAL A C   1 
ATOM   2265 O  O   . VAL A 1 281 ? 11.434  -8.930  15.750  1.00 39.50  ? 281 VAL A O   1 
ATOM   2266 C  CB  . VAL A 1 281 ? 9.136   -9.501  17.828  1.00 38.40  ? 281 VAL A CB  1 
ATOM   2267 C  CG1 . VAL A 1 281 ? 8.266   -8.909  18.910  1.00 40.06  ? 281 VAL A CG1 1 
ATOM   2268 C  CG2 . VAL A 1 281 ? 8.656   -10.912 17.431  1.00 38.98  ? 281 VAL A CG2 1 
ATOM   2269 N  N   . LYS A 1 282 ? 9.727   -9.730  14.522  1.00 35.96  ? 282 LYS A N   1 
ATOM   2270 C  CA  . LYS A 1 282 ? 10.592  -10.168 13.428  1.00 39.37  ? 282 LYS A CA  1 
ATOM   2271 C  C   . LYS A 1 282 ? 10.955  -9.045  12.463  1.00 38.55  ? 282 LYS A C   1 
ATOM   2272 O  O   . LYS A 1 282 ? 11.775  -9.263  11.559  1.00 41.72  ? 282 LYS A O   1 
ATOM   2273 C  CB  . LYS A 1 282 ? 9.934   -11.305 12.651  1.00 37.78  ? 282 LYS A CB  1 
ATOM   2274 C  CG  . LYS A 1 282 ? 9.605   -12.551 13.499  1.00 33.97  ? 282 LYS A CG  1 
ATOM   2275 C  CD  . LYS A 1 282 ? 10.866  -13.126 14.188  1.00 35.54  ? 282 LYS A CD  1 
ATOM   2276 C  CE  . LYS A 1 282 ? 10.750  -14.624 14.422  1.00 34.43  ? 282 LYS A CE  1 
ATOM   2277 N  NZ  . LYS A 1 282 ? 11.875  -15.180 15.247  1.00 39.72  ? 282 LYS A NZ  1 
ATOM   2278 N  N   . ASN A 1 283 ? 10.365  -7.864  12.618  1.00 36.51  ? 283 ASN A N   1 
ATOM   2279 C  CA  . ASN A 1 283 ? 10.585  -6.728  11.716  1.00 37.96  ? 283 ASN A CA  1 
ATOM   2280 C  C   . ASN A 1 283 ? 10.714  -5.450  12.540  1.00 41.19  ? 283 ASN A C   1 
ATOM   2281 O  O   . ASN A 1 283 ? 9.826   -4.582  12.545  1.00 38.15  ? 283 ASN A O   1 
ATOM   2282 C  CB  . ASN A 1 283 ? 9.463   -6.646  10.679  1.00 42.38  ? 283 ASN A CB  1 
ATOM   2283 C  CG  . ASN A 1 283 ? 9.464   -7.842  9.739   1.00 42.64  ? 283 ASN A CG  1 
ATOM   2284 O  OD1 . ASN A 1 283 ? 10.177  -7.841  8.728   1.00 42.86  ? 283 ASN A OD1 1 
ATOM   2285 N  ND2 . ASN A 1 283 ? 8.699   -8.882  10.076  1.00 38.41  ? 283 ASN A ND2 1 
ATOM   2286 N  N   . PRO A 1 284 ? 11.842  -5.294  13.243  1.00 43.05  ? 284 PRO A N   1 
ATOM   2287 C  CA  . PRO A 1 284 ? 11.965  -4.193  14.218  1.00 45.16  ? 284 PRO A CA  1 
ATOM   2288 C  C   . PRO A 1 284 ? 11.761  -2.815  13.622  1.00 39.94  ? 284 PRO A C   1 
ATOM   2289 O  O   . PRO A 1 284 ? 11.243  -1.936  14.316  1.00 41.52  ? 284 PRO A O   1 
ATOM   2290 C  CB  . PRO A 1 284 ? 13.394  -4.345  14.763  1.00 46.37  ? 284 PRO A CB  1 
ATOM   2291 C  CG  . PRO A 1 284 ? 13.945  -5.633  14.204  1.00 46.26  ? 284 PRO A CG  1 
ATOM   2292 C  CD  . PRO A 1 284 ? 12.915  -6.299  13.356  1.00 43.60  ? 284 PRO A CD  1 
ATOM   2293 N  N   . HIS A 1 285 ? 12.154  -2.586  12.366  1.00 43.55  ? 285 HIS A N   1 
ATOM   2294 C  CA  . HIS A 1 285 ? 11.913  -1.276  11.763  1.00 44.43  ? 285 HIS A CA  1 
ATOM   2295 C  C   . HIS A 1 285 ? 10.422  -0.992  11.637  1.00 39.12  ? 285 HIS A C   1 
ATOM   2296 O  O   . HIS A 1 285 ? 9.983   0.152   11.805  1.00 39.11  ? 285 HIS A O   1 
ATOM   2297 C  CB  . HIS A 1 285 ? 12.595  -1.181  10.400  1.00 45.95  ? 285 HIS A CB  1 
ATOM   2298 C  CG  . HIS A 1 285 ? 14.070  -1.445  10.449  1.00 58.64  ? 285 HIS A CG  1 
ATOM   2299 N  ND1 . HIS A 1 285 ? 14.874  -0.970  11.465  1.00 59.09  ? 285 HIS A ND1 1 
ATOM   2300 C  CD2 . HIS A 1 285 ? 14.886  -2.125  9.607   1.00 61.54  ? 285 HIS A CD2 1 
ATOM   2301 C  CE1 . HIS A 1 285 ? 16.122  -1.353  11.249  1.00 65.56  ? 285 HIS A CE1 1 
ATOM   2302 N  NE2 . HIS A 1 285 ? 16.157  -2.053  10.128  1.00 64.29  ? 285 HIS A NE2 1 
ATOM   2303 N  N   . VAL A 1 286 ? 9.626   -2.021  11.368  1.00 42.65  ? 286 VAL A N   1 
ATOM   2304 C  CA  . VAL A 1 286 ? 8.173   -1.841  11.338  1.00 37.75  ? 286 VAL A CA  1 
ATOM   2305 C  C   . VAL A 1 286 ? 7.644   -1.582  12.746  1.00 35.77  ? 286 VAL A C   1 
ATOM   2306 O  O   . VAL A 1 286 ? 6.833   -0.670  12.967  1.00 36.13  ? 286 VAL A O   1 
ATOM   2307 C  CB  . VAL A 1 286 ? 7.515   -3.066  10.673  1.00 38.54  ? 286 VAL A CB  1 
ATOM   2308 C  CG1 . VAL A 1 286 ? 5.976   -2.930  10.631  1.00 35.28  ? 286 VAL A CG1 1 
ATOM   2309 C  CG2 . VAL A 1 286 ? 8.079   -3.251  9.272   1.00 36.88  ? 286 VAL A CG2 1 
ATOM   2310 N  N   . LEU A 1 287 ? 8.111   -2.356  13.728  1.00 39.69  ? 287 LEU A N   1 
ATOM   2311 C  CA  . LEU A 1 287 ? 7.711   -2.084  15.105  1.00 36.60  ? 287 LEU A CA  1 
ATOM   2312 C  C   . LEU A 1 287 ? 8.013   -0.635  15.479  1.00 40.03  ? 287 LEU A C   1 
ATOM   2313 O  O   . LEU A 1 287 ? 7.160   0.071   16.030  1.00 39.14  ? 287 LEU A O   1 
ATOM   2314 C  CB  . LEU A 1 287 ? 8.405   -3.067  16.058  1.00 40.25  ? 287 LEU A CB  1 
ATOM   2315 C  CG  . LEU A 1 287 ? 7.771   -3.259  17.457  1.00 37.54  ? 287 LEU A CG  1 
ATOM   2316 C  CD1 . LEU A 1 287 ? 8.357   -4.469  18.162  1.00 37.19  ? 287 LEU A CD1 1 
ATOM   2317 C  CD2 . LEU A 1 287 ? 7.964   -2.018  18.298  1.00 42.12  ? 287 LEU A CD2 1 
ATOM   2318 N  N   . GLN A 1 288 ? 9.231   -0.171  15.176  1.00 40.79  ? 288 GLN A N   1 
ATOM   2319 C  CA  . GLN A 1 288 ? 9.592   1.223   15.427  1.00 41.73  ? 288 GLN A CA  1 
ATOM   2320 C  C   . GLN A 1 288 ? 8.578   2.201   14.851  1.00 39.56  ? 288 GLN A C   1 
ATOM   2321 O  O   . GLN A 1 288 ? 8.102   3.106   15.551  1.00 37.97  ? 288 GLN A O   1 
ATOM   2322 C  CB  . GLN A 1 288 ? 10.962  1.523   14.836  1.00 43.50  ? 288 GLN A CB  1 
ATOM   2323 C  CG  . GLN A 1 288 ? 11.396  2.944   15.138  1.00 50.16  ? 288 GLN A CG  1 
ATOM   2324 C  CD  . GLN A 1 288 ? 12.881  3.122   15.032  1.00 58.79  ? 288 GLN A CD  1 
ATOM   2325 O  OE1 . GLN A 1 288 ? 13.614  2.175   14.733  1.00 62.30  ? 288 GLN A OE1 1 
ATOM   2326 N  NE2 . GLN A 1 288 ? 13.341  4.345   15.253  1.00 63.89  ? 288 GLN A NE2 1 
ATOM   2327 N  N   . LYS A 1 289 ? 8.278   2.068   13.552  1.00 40.52  ? 289 LYS A N   1 
ATOM   2328 C  CA  . LYS A 1 289 ? 7.333   2.980   12.902  1.00 41.95  ? 289 LYS A CA  1 
ATOM   2329 C  C   . LYS A 1 289 ? 5.980   2.956   13.603  1.00 35.48  ? 289 LYS A C   1 
ATOM   2330 O  O   . LYS A 1 289 ? 5.379   4.007   13.868  1.00 40.34  ? 289 LYS A O   1 
ATOM   2331 C  CB  . LYS A 1 289 ? 7.188   2.604   11.422  1.00 38.52  ? 289 LYS A CB  1 
ATOM   2332 C  CG  . LYS A 1 289 ? 6.347   3.551   10.583  1.00 43.21  ? 289 LYS A CG  1 
ATOM   2333 C  CD  . LYS A 1 289 ? 6.716   3.428   9.084   1.00 42.58  ? 289 LYS A CD  1 
ATOM   2334 C  CE  . LYS A 1 289 ? 5.758   4.219   8.181   1.00 44.05  ? 289 LYS A CE  1 
ATOM   2335 N  NZ  . LYS A 1 289 ? 5.857   3.828   6.732   1.00 44.58  ? 289 LYS A NZ  1 
ATOM   2336 N  N   . ALA A 1 290 ? 5.492   1.758   13.923  1.00 37.84  ? 290 ALA A N   1 
ATOM   2337 C  CA  . ALA A 1 290 ? 4.208   1.638   14.607  1.00 35.99  ? 290 ALA A CA  1 
ATOM   2338 C  C   . ALA A 1 290 ? 4.278   2.172   16.037  1.00 33.61  ? 290 ALA A C   1 
ATOM   2339 O  O   . ALA A 1 290 ? 3.329   2.806   16.516  1.00 38.22  ? 290 ALA A O   1 
ATOM   2340 C  CB  . ALA A 1 290 ? 3.757   0.183   14.595  1.00 34.13  ? 290 ALA A CB  1 
ATOM   2341 N  N   . ALA A 1 291 ? 5.377   1.908   16.746  1.00 37.55  ? 291 ALA A N   1 
ATOM   2342 C  CA  . ALA A 1 291 ? 5.496   2.428   18.108  1.00 36.35  ? 291 ALA A CA  1 
ATOM   2343 C  C   . ALA A 1 291 ? 5.533   3.951   18.094  1.00 40.17  ? 291 ALA A C   1 
ATOM   2344 O  O   . ALA A 1 291 ? 4.947   4.611   18.965  1.00 39.21  ? 291 ALA A O   1 
ATOM   2345 C  CB  . ALA A 1 291 ? 6.745   1.854   18.790  1.00 37.79  ? 291 ALA A CB  1 
ATOM   2346 N  N   . GLU A 1 292 ? 6.192   4.525   17.083  1.00 40.96  ? 292 GLU A N   1 
ATOM   2347 C  CA  . GLU A 1 292 ? 6.246   5.975   16.956  1.00 38.62  ? 292 GLU A CA  1 
ATOM   2348 C  C   . GLU A 1 292 ? 4.844   6.549   16.752  1.00 39.60  ? 292 GLU A C   1 
ATOM   2349 O  O   . GLU A 1 292 ? 4.496   7.592   17.324  1.00 37.57  ? 292 GLU A O   1 
ATOM   2350 C  CB  . GLU A 1 292 ? 7.172   6.337   15.785  1.00 41.35  ? 292 GLU A CB  1 
ATOM   2351 C  CG  . GLU A 1 292 ? 8.614   6.701   16.178  1.00 47.72  ? 292 GLU A CG  1 
ATOM   2352 C  CD  . GLU A 1 292 ? 9.615   6.371   15.058  1.00 56.99  ? 292 GLU A CD  1 
ATOM   2353 O  OE1 . GLU A 1 292 ? 9.173   6.228   13.894  1.00 54.15  ? 292 GLU A OE1 1 
ATOM   2354 O  OE2 . GLU A 1 292 ? 10.835  6.264   15.325  1.00 54.65  ? 292 GLU A OE2 1 
ATOM   2355 N  N   . GLU A 1 293 ? 4.016   5.882   15.940  1.00 37.39  ? 293 GLU A N   1 
ATOM   2356 C  CA  . GLU A 1 293 ? 2.634   6.333   15.788  1.00 36.77  ? 293 GLU A CA  1 
ATOM   2357 C  C   . GLU A 1 293 ? 1.889   6.219   17.105  1.00 39.50  ? 293 GLU A C   1 
ATOM   2358 O  O   . GLU A 1 293 ? 1.158   7.139   17.507  1.00 42.34  ? 293 GLU A O   1 
ATOM   2359 C  CB  . GLU A 1 293 ? 1.917   5.527   14.706  1.00 35.45  ? 293 GLU A CB  1 
ATOM   2360 C  CG  . GLU A 1 293 ? 0.505   6.059   14.461  1.00 36.36  ? 293 GLU A CG  1 
ATOM   2361 C  CD  . GLU A 1 293 ? -0.268  5.229   13.480  1.00 38.11  ? 293 GLU A CD  1 
ATOM   2362 O  OE1 . GLU A 1 293 ? -0.611  4.078   13.823  1.00 37.09  ? 293 GLU A OE1 1 
ATOM   2363 O  OE2 . GLU A 1 293 ? -0.517  5.717   12.351  1.00 39.19  ? 293 GLU A OE2 1 
ATOM   2364 N  N   . ALA A 1 294 ? 2.061   5.084   17.790  1.00 37.81  ? 294 ALA A N   1 
ATOM   2365 C  CA  . ALA A 1 294 ? 1.379   4.869   19.060  1.00 39.48  ? 294 ALA A CA  1 
ATOM   2366 C  C   . ALA A 1 294 ? 1.724   5.969   20.052  1.00 35.61  ? 294 ALA A C   1 
ATOM   2367 O  O   . ALA A 1 294 ? 0.838   6.536   20.700  1.00 37.58  ? 294 ALA A O   1 
ATOM   2368 C  CB  . ALA A 1 294 ? 1.745   3.500   19.626  1.00 37.81  ? 294 ALA A CB  1 
ATOM   2369 N  N   . ALA A 1 295 ? 3.012   6.298   20.169  1.00 40.81  ? 295 ALA A N   1 
ATOM   2370 C  CA  . ALA A 1 295 ? 3.417   7.333   21.119  1.00 40.92  ? 295 ALA A CA  1 
ATOM   2371 C  C   . ALA A 1 295 ? 2.882   8.697   20.710  1.00 41.32  ? 295 ALA A C   1 
ATOM   2372 O  O   . ALA A 1 295 ? 2.455   9.487   21.560  1.00 42.90  ? 295 ALA A O   1 
ATOM   2373 C  CB  . ALA A 1 295 ? 4.943   7.361   21.246  1.00 40.64  ? 295 ALA A CB  1 
ATOM   2374 N  N   A ARG A 1 296 ? 2.877   8.991   19.408  0.51 42.13  ? 296 ARG A N   1 
ATOM   2375 N  N   B ARG A 1 296 ? 2.875   8.986   19.409  0.49 42.09  ? 296 ARG A N   1 
ATOM   2376 C  CA  A ARG A 1 296 ? 2.443   10.309  18.963  0.51 39.71  ? 296 ARG A CA  1 
ATOM   2377 C  CA  B ARG A 1 296 ? 2.449   10.305  18.965  0.49 39.73  ? 296 ARG A CA  1 
ATOM   2378 C  C   A ARG A 1 296 ? 0.932   10.477  19.089  0.51 41.15  ? 296 ARG A C   1 
ATOM   2379 C  C   B ARG A 1 296 ? 0.936   10.477  19.085  0.49 41.12  ? 296 ARG A C   1 
ATOM   2380 O  O   A ARG A 1 296 ? 0.452   11.585  19.360  0.51 40.18  ? 296 ARG A O   1 
ATOM   2381 O  O   B ARG A 1 296 ? 0.459   11.585  19.360  0.49 40.19  ? 296 ARG A O   1 
ATOM   2382 C  CB  A ARG A 1 296 ? 2.929   10.538  17.527  0.51 43.59  ? 296 ARG A CB  1 
ATOM   2383 C  CB  B ARG A 1 296 ? 2.954   10.532  17.534  0.49 43.55  ? 296 ARG A CB  1 
ATOM   2384 C  CG  A ARG A 1 296 ? 2.137   11.523  16.688  0.51 44.00  ? 296 ARG A CG  1 
ATOM   2385 C  CG  B ARG A 1 296 ? 2.102   11.398  16.643  0.49 44.00  ? 296 ARG A CG  1 
ATOM   2386 C  CD  A ARG A 1 296 ? 2.668   11.546  15.237  0.51 44.76  ? 296 ARG A CD  1 
ATOM   2387 C  CD  B ARG A 1 296 ? 2.807   11.674  15.293  0.49 44.70  ? 296 ARG A CD  1 
ATOM   2388 N  NE  A ARG A 1 296 ? 1.880   10.739  14.308  0.51 44.27  ? 296 ARG A NE  1 
ATOM   2389 N  NE  B ARG A 1 296 ? 2.824   10.529  14.384  0.49 43.94  ? 296 ARG A NE  1 
ATOM   2390 C  CZ  A ARG A 1 296 ? 0.611   10.969  14.005  0.51 40.92  ? 296 ARG A CZ  1 
ATOM   2391 C  CZ  B ARG A 1 296 ? 3.875   9.752   14.151  0.49 43.43  ? 296 ARG A CZ  1 
ATOM   2392 N  NH1 A ARG A 1 296 ? -0.059  11.971  14.551  0.51 45.16  ? 296 ARG A NH1 1 
ATOM   2393 N  NH1 B ARG A 1 296 ? 5.040   9.966   14.740  0.49 42.53  ? 296 ARG A NH1 1 
ATOM   2394 N  NH2 A ARG A 1 296 ? 0.002   10.182  13.125  0.51 40.41  ? 296 ARG A NH2 1 
ATOM   2395 N  NH2 B ARG A 1 296 ? 3.756   8.741   13.293  0.49 41.59  ? 296 ARG A NH2 1 
ATOM   2396 N  N   . VAL A 1 297 ? 0.169   9.395   18.946  1.00 40.47  ? 297 VAL A N   1 
ATOM   2397 C  CA  . VAL A 1 297 ? -1.289  9.500   18.938  1.00 36.31  ? 297 VAL A CA  1 
ATOM   2398 C  C   . VAL A 1 297 ? -1.899  9.264   20.323  1.00 38.89  ? 297 VAL A C   1 
ATOM   2399 O  O   . VAL A 1 297 ? -2.849  9.945   20.715  1.00 38.33  ? 297 VAL A O   1 
ATOM   2400 C  CB  . VAL A 1 297 ? -1.858  8.528   17.885  1.00 39.08  ? 297 VAL A CB  1 
ATOM   2401 C  CG1 . VAL A 1 297 ? -3.347  8.337   18.092  1.00 35.50  ? 297 VAL A CG1 1 
ATOM   2402 C  CG2 . VAL A 1 297 ? -1.568  9.066   16.453  1.00 35.84  ? 297 VAL A CG2 1 
ATOM   2403 N  N   . LEU A 1 298 ? -1.388  8.305   21.088  1.00 39.67  ? 298 LEU A N   1 
ATOM   2404 C  CA  . LEU A 1 298 ? -2.042  7.902   22.334  1.00 39.16  ? 298 LEU A CA  1 
ATOM   2405 C  C   . LEU A 1 298 ? -1.468  8.746   23.474  1.00 41.61  ? 298 LEU A C   1 
ATOM   2406 O  O   . LEU A 1 298 ? -0.647  8.297   24.283  1.00 41.20  ? 298 LEU A O   1 
ATOM   2407 C  CB  . LEU A 1 298 ? -1.859  6.402   22.563  1.00 39.74  ? 298 LEU A CB  1 
ATOM   2408 C  CG  . LEU A 1 298 ? -2.462  5.473   21.491  1.00 39.41  ? 298 LEU A CG  1 
ATOM   2409 C  CD1 . LEU A 1 298 ? -2.121  4.006   21.757  1.00 36.96  ? 298 LEU A CD1 1 
ATOM   2410 C  CD2 . LEU A 1 298 ? -3.958  5.663   21.370  1.00 41.21  ? 298 LEU A CD2 1 
ATOM   2411 N  N   . VAL A 1 299 ? -1.941  10.000  23.544  1.00 43.48  ? 299 VAL A N   1 
ATOM   2412 C  CA  . VAL A 1 299 ? -1.344  11.012  24.414  1.00 45.80  ? 299 VAL A CA  1 
ATOM   2413 C  C   . VAL A 1 299 ? -2.015  11.099  25.775  1.00 48.33  ? 299 VAL A C   1 
ATOM   2414 O  O   . VAL A 1 299 ? -1.589  11.908  26.613  1.00 45.71  ? 299 VAL A O   1 
ATOM   2415 C  CB  . VAL A 1 299 ? -1.358  12.397  23.723  1.00 42.65  ? 299 VAL A CB  1 
ATOM   2416 C  CG1 . VAL A 1 299 ? -0.570  12.340  22.417  1.00 42.32  ? 299 VAL A CG1 1 
ATOM   2417 C  CG2 . VAL A 1 299 ? -2.787  12.847  23.447  1.00 42.75  ? 299 VAL A CG2 1 
ATOM   2418 N  N   . ASP A 1 300 ? -3.037  10.290  26.028  1.00 43.48  ? 300 ASP A N   1 
ATOM   2419 C  CA  . ASP A 1 300 ? -3.748  10.229  27.292  1.00 45.58  ? 300 ASP A CA  1 
ATOM   2420 C  C   . ASP A 1 300 ? -3.563  8.852   27.934  1.00 46.97  ? 300 ASP A C   1 
ATOM   2421 O  O   . ASP A 1 300 ? -3.234  7.875   27.249  1.00 44.55  ? 300 ASP A O   1 
ATOM   2422 C  CB  . ASP A 1 300 ? -5.240  10.510  27.078  1.00 46.04  ? 300 ASP A CB  1 
ATOM   2423 C  CG  . ASP A 1 300 ? -5.490  11.880  26.477  1.00 48.60  ? 300 ASP A CG  1 
ATOM   2424 O  OD1 . ASP A 1 300 ? -4.809  12.842  26.903  1.00 46.95  ? 300 ASP A OD1 1 
ATOM   2425 O  OD2 . ASP A 1 300 ? -6.355  11.991  25.576  1.00 49.78  ? 300 ASP A OD2 1 
ATOM   2426 N  N   . PRO A 1 301 ? -3.770  8.739   29.249  1.00 48.33  ? 301 PRO A N   1 
ATOM   2427 C  CA  . PRO A 1 301 ? -3.559  7.435   29.912  1.00 48.63  ? 301 PRO A CA  1 
ATOM   2428 C  C   . PRO A 1 301 ? -4.519  6.353   29.439  1.00 45.00  ? 301 PRO A C   1 
ATOM   2429 O  O   . PRO A 1 301 ? -4.150  5.171   29.458  1.00 45.97  ? 301 PRO A O   1 
ATOM   2430 C  CB  . PRO A 1 301 ? -3.749  7.739   31.406  1.00 46.96  ? 301 PRO A CB  1 
ATOM   2431 C  CG  . PRO A 1 301 ? -4.173  9.163   31.514  1.00 52.14  ? 301 PRO A CG  1 
ATOM   2432 C  CD  . PRO A 1 301 ? -4.165  9.818   30.170  1.00 51.72  ? 301 PRO A CD  1 
ATOM   2433 N  N   . VAL A 1 302 ? -5.726  6.714   29.012  1.00 47.38  ? 302 VAL A N   1 
ATOM   2434 C  CA  . VAL A 1 302 ? -6.660  5.789   28.381  1.00 52.15  ? 302 VAL A CA  1 
ATOM   2435 C  C   . VAL A 1 302 ? -6.884  6.260   26.949  1.00 48.55  ? 302 VAL A C   1 
ATOM   2436 O  O   . VAL A 1 302 ? -7.157  7.441   26.735  1.00 47.56  ? 302 VAL A O   1 
ATOM   2437 C  CB  . VAL A 1 302 ? -8.005  5.700   29.127  1.00 53.20  ? 302 VAL A CB  1 
ATOM   2438 C  CG1 . VAL A 1 302 ? -7.781  5.640   30.639  1.00 55.54  ? 302 VAL A CG1 1 
ATOM   2439 C  CG2 . VAL A 1 302 ? -8.933  6.847   28.740  1.00 53.35  ? 302 VAL A CG2 1 
ATOM   2440 N  N   . PRO A 1 303 ? -6.783  5.391   25.946  1.00 49.01  ? 303 PRO A N   1 
ATOM   2441 C  CA  . PRO A 1 303 ? -7.108  5.813   24.577  1.00 38.83  ? 303 PRO A CA  1 
ATOM   2442 C  C   . PRO A 1 303 ? -8.578  6.191   24.428  1.00 42.17  ? 303 PRO A C   1 
ATOM   2443 O  O   . PRO A 1 303 ? -9.463  5.637   25.085  1.00 36.94  ? 303 PRO A O   1 
ATOM   2444 C  CB  . PRO A 1 303 ? -6.774  4.572   23.745  1.00 43.77  ? 303 PRO A CB  1 
ATOM   2445 C  CG  . PRO A 1 303 ? -5.735  3.882   24.538  1.00 42.43  ? 303 PRO A CG  1 
ATOM   2446 C  CD  . PRO A 1 303 ? -6.200  4.039   25.960  1.00 43.23  ? 303 PRO A CD  1 
ATOM   2447 N  N   . SER A 1 304 ? -8.834  7.136   23.529  1.00 40.74  ? 304 SER A N   1 
ATOM   2448 C  CA  . SER A 1 304 ? -10.192 7.494   23.141  1.00 41.26  ? 304 SER A CA  1 
ATOM   2449 C  C   . SER A 1 304 ? -10.555 6.853   21.811  1.00 35.12  ? 304 SER A C   1 
ATOM   2450 O  O   . SER A 1 304 ? -9.689  6.407   21.051  1.00 38.54  ? 304 SER A O   1 
ATOM   2451 C  CB  . SER A 1 304 ? -10.350 9.011   23.035  1.00 41.76  ? 304 SER A CB  1 
ATOM   2452 O  OG  . SER A 1 304 ? -9.528  9.524   22.001  1.00 42.69  ? 304 SER A OG  1 
ATOM   2453 N  N   . TYR A 1 305 ? -11.862 6.822   21.533  1.00 38.06  ? 305 TYR A N   1 
ATOM   2454 C  CA  . TYR A 1 305 ? -12.324 6.342   20.236  1.00 37.53  ? 305 TYR A CA  1 
ATOM   2455 C  C   . TYR A 1 305 ? -11.659 7.113   19.101  1.00 42.01  ? 305 TYR A C   1 
ATOM   2456 O  O   . TYR A 1 305 ? -11.170 6.516   18.130  1.00 41.75  ? 305 TYR A O   1 
ATOM   2457 C  CB  . TYR A 1 305 ? -13.848 6.454   20.132  1.00 41.87  ? 305 TYR A CB  1 
ATOM   2458 C  CG  . TYR A 1 305 ? -14.358 6.150   18.737  1.00 45.68  ? 305 TYR A CG  1 
ATOM   2459 C  CD1 . TYR A 1 305 ? -14.561 4.833   18.325  1.00 43.40  ? 305 TYR A CD1 1 
ATOM   2460 C  CD2 . TYR A 1 305 ? -14.614 7.175   17.822  1.00 45.36  ? 305 TYR A CD2 1 
ATOM   2461 C  CE1 . TYR A 1 305 ? -15.023 4.540   17.044  1.00 42.33  ? 305 TYR A CE1 1 
ATOM   2462 C  CE2 . TYR A 1 305 ? -15.068 6.886   16.531  1.00 44.38  ? 305 TYR A CE2 1 
ATOM   2463 C  CZ  . TYR A 1 305 ? -15.269 5.565   16.153  1.00 42.96  ? 305 TYR A CZ  1 
ATOM   2464 O  OH  . TYR A 1 305 ? -15.717 5.254   14.890  1.00 47.16  ? 305 TYR A OH  1 
ATOM   2465 N  N   . LYS A 1 306 ? -11.636 8.448   19.205  1.00 40.58  ? 306 LYS A N   1 
ATOM   2466 C  CA  . LYS A 1 306 ? -11.034 9.270   18.156  1.00 42.05  ? 306 LYS A CA  1 
ATOM   2467 C  C   . LYS A 1 306 ? -9.579  8.904   17.923  1.00 37.56  ? 306 LYS A C   1 
ATOM   2468 O  O   . LYS A 1 306 ? -9.139  8.783   16.774  1.00 44.74  ? 306 LYS A O   1 
ATOM   2469 C  CB  . LYS A 1 306 ? -11.144 10.757  18.501  1.00 44.44  ? 306 LYS A CB  1 
ATOM   2470 C  CG  . LYS A 1 306 ? -12.531 11.241  18.859  1.00 50.95  ? 306 LYS A CG  1 
ATOM   2471 C  CD  . LYS A 1 306 ? -12.783 12.594  18.208  1.00 58.82  ? 306 LYS A CD  1 
ATOM   2472 C  CE  . LYS A 1 306 ? -13.912 13.333  18.894  1.00 61.72  ? 306 LYS A CE  1 
ATOM   2473 N  NZ  . LYS A 1 306 ? -15.128 13.350  18.048  1.00 68.52  ? 306 LYS A NZ  1 
ATOM   2474 N  N   . GLN A 1 307 ? -8.809  8.734   19.000  1.00 39.70  ? 307 GLN A N   1 
ATOM   2475 C  CA  . GLN A 1 307 ? -7.388  8.416   18.854  1.00 38.19  ? 307 GLN A CA  1 
ATOM   2476 C  C   . GLN A 1 307 ? -7.170  7.053   18.208  1.00 37.45  ? 307 GLN A C   1 
ATOM   2477 O  O   . GLN A 1 307 ? -6.290  6.902   17.349  1.00 39.66  ? 307 GLN A O   1 
ATOM   2478 C  CB  . GLN A 1 307 ? -6.669  8.494   20.217  1.00 40.52  ? 307 GLN A CB  1 
ATOM   2479 C  CG  . GLN A 1 307 ? -6.932  9.774   20.985  1.00 40.54  ? 307 GLN A CG  1 
ATOM   2480 C  CD  . GLN A 1 307 ? -6.422  9.753   22.417  1.00 43.17  ? 307 GLN A CD  1 
ATOM   2481 O  OE1 . GLN A 1 307 ? -6.498  8.735   23.099  1.00 44.01  ? 307 GLN A OE1 1 
ATOM   2482 N  NE2 . GLN A 1 307 ? -5.918  10.895  22.888  1.00 45.81  ? 307 GLN A NE2 1 
ATOM   2483 N  N   . VAL A 1 308 ? -7.949  6.046   18.598  1.00 39.47  ? 308 VAL A N   1 
ATOM   2484 C  CA  . VAL A 1 308 ? -7.806  4.750   17.942  1.00 37.80  ? 308 VAL A CA  1 
ATOM   2485 C  C   . VAL A 1 308 ? -8.005  4.900   16.440  1.00 38.50  ? 308 VAL A C   1 
ATOM   2486 O  O   . VAL A 1 308 ? -7.312  4.260   15.640  1.00 37.40  ? 308 VAL A O   1 
ATOM   2487 C  CB  . VAL A 1 308 ? -8.783  3.731   18.548  1.00 34.34  ? 308 VAL A CB  1 
ATOM   2488 C  CG1 . VAL A 1 308 ? -8.756  2.425   17.739  1.00 38.30  ? 308 VAL A CG1 1 
ATOM   2489 C  CG2 . VAL A 1 308 ? -8.451  3.491   20.026  1.00 36.02  ? 308 VAL A CG2 1 
ATOM   2490 N  N   . LYS A 1 309 ? -8.943  5.768   16.035  1.00 37.27  ? 309 LYS A N   1 
ATOM   2491 C  CA  . LYS A 1 309 ? -9.205  6.006   14.620  1.00 40.77  ? 309 LYS A CA  1 
ATOM   2492 C  C   . LYS A 1 309 ? -8.000  6.600   13.905  1.00 36.97  ? 309 LYS A C   1 
ATOM   2493 O  O   . LYS A 1 309 ? -7.898  6.472   12.683  1.00 39.62  ? 309 LYS A O   1 
ATOM   2494 C  CB  . LYS A 1 309 ? -10.411 6.939   14.458  1.00 42.60  ? 309 LYS A CB  1 
ATOM   2495 C  CG  . LYS A 1 309 ? -11.784 6.304   14.709  1.00 42.25  ? 309 LYS A CG  1 
ATOM   2496 C  CD  . LYS A 1 309 ? -12.007 4.981   13.958  1.00 50.39  ? 309 LYS A CD  1 
ATOM   2497 C  CE  . LYS A 1 309 ? -12.108 3.791   14.920  1.00 48.73  ? 309 LYS A CE  1 
ATOM   2498 N  NZ  . LYS A 1 309 ? -12.184 2.451   14.226  1.00 50.23  ? 309 LYS A NZ  1 
ATOM   2499 N  N   . GLN A 1 310 ? -7.086  7.245   14.628  1.00 36.36  ? 310 GLN A N   1 
ATOM   2500 C  CA  . GLN A 1 310 ? -5.915  7.868   14.012  1.00 41.66  ? 310 GLN A CA  1 
ATOM   2501 C  C   . GLN A 1 310 ? -4.686  6.967   14.024  1.00 39.68  ? 310 GLN A C   1 
ATOM   2502 O  O   . GLN A 1 310 ? -3.625  7.380   13.541  1.00 37.80  ? 310 GLN A O   1 
ATOM   2503 C  CB  . GLN A 1 310 ? -5.587  9.208   14.701  1.00 37.49  ? 310 GLN A CB  1 
ATOM   2504 C  CG  . GLN A 1 310 ? -6.648  10.302  14.479  1.00 38.85  ? 310 GLN A CG  1 
ATOM   2505 C  CD  . GLN A 1 310 ? -7.051  10.446  13.009  1.00 44.50  ? 310 GLN A CD  1 
ATOM   2506 O  OE1 . GLN A 1 310 ? -6.195  10.529  12.135  1.00 42.95  ? 310 GLN A OE1 1 
ATOM   2507 N  NE2 . GLN A 1 310 ? -8.356  10.485  12.740  1.00 47.00  ? 310 GLN A NE2 1 
ATOM   2508 N  N   . LEU A 1 311 ? -4.803  5.745   14.557  1.00 35.43  ? 311 LEU A N   1 
ATOM   2509 C  CA  . LEU A 1 311 ? -3.712  4.764   14.533  1.00 37.34  ? 311 LEU A CA  1 
ATOM   2510 C  C   . LEU A 1 311 ? -3.702  4.073   13.166  1.00 39.12  ? 311 LEU A C   1 
ATOM   2511 O  O   . LEU A 1 311 ? -3.953  2.872   13.015  1.00 37.13  ? 311 LEU A O   1 
ATOM   2512 C  CB  . LEU A 1 311 ? -3.857  3.769   15.671  1.00 37.92  ? 311 LEU A CB  1 
ATOM   2513 C  CG  . LEU A 1 311 ? -3.657  4.401   17.050  1.00 34.48  ? 311 LEU A CG  1 
ATOM   2514 C  CD1 . LEU A 1 311 ? -3.994  3.379   18.124  1.00 35.38  ? 311 LEU A CD1 1 
ATOM   2515 C  CD2 . LEU A 1 311 ? -2.214  4.878   17.178  1.00 34.88  ? 311 LEU A CD2 1 
ATOM   2516 N  N   . LYS A 1 312 ? -3.375  4.875   12.153  1.00 37.68  ? 312 LYS A N   1 
ATOM   2517 C  CA  . LYS A 1 312 ? -3.547  4.445   10.772  1.00 35.68  ? 312 LYS A CA  1 
ATOM   2518 C  C   . LYS A 1 312 ? -2.487  3.428   10.369  1.00 36.90  ? 312 LYS A C   1 
ATOM   2519 O  O   . LYS A 1 312 ? -2.789  2.463   9.662   1.00 33.60  ? 312 LYS A O   1 
ATOM   2520 C  CB  . LYS A 1 312 ? -3.524  5.680   9.870   1.00 37.52  ? 312 LYS A CB  1 
ATOM   2521 C  CG  . LYS A 1 312 ? -4.901  6.344   9.840   1.00 44.58  ? 312 LYS A CG  1 
ATOM   2522 C  CD  . LYS A 1 312 ? -5.026  7.437   8.796   1.00 53.26  ? 312 LYS A CD  1 
ATOM   2523 C  CE  . LYS A 1 312 ? -5.868  8.570   9.351   1.00 53.84  ? 312 LYS A CE  1 
ATOM   2524 N  NZ  . LYS A 1 312 ? -7.313  8.222   9.337   1.00 51.46  ? 312 LYS A NZ  1 
ATOM   2525 N  N   . TYR A 1 313 ? -1.243  3.613   10.818  1.00 36.21  ? 313 TYR A N   1 
ATOM   2526 C  CA  . TYR A 1 313 ? -0.205  2.645   10.486  1.00 35.77  ? 313 TYR A CA  1 
ATOM   2527 C  C   . TYR A 1 313 ? -0.427  1.340   11.233  1.00 35.30  ? 313 TYR A C   1 
ATOM   2528 O  O   . TYR A 1 313 ? -0.212  0.250   10.683  1.00 34.23  ? 313 TYR A O   1 
ATOM   2529 C  CB  . TYR A 1 313 ? 1.181   3.202   10.813  1.00 34.42  ? 313 TYR A CB  1 
ATOM   2530 C  CG  . TYR A 1 313 ? 2.294   2.361   10.234  1.00 31.89  ? 313 TYR A CG  1 
ATOM   2531 C  CD1 . TYR A 1 313 ? 2.573   2.393   8.861   1.00 36.18  ? 313 TYR A CD1 1 
ATOM   2532 C  CD2 . TYR A 1 313 ? 3.072   1.536   11.043  1.00 36.20  ? 313 TYR A CD2 1 
ATOM   2533 C  CE1 . TYR A 1 313 ? 3.593   1.614   8.320   1.00 36.87  ? 313 TYR A CE1 1 
ATOM   2534 C  CE2 . TYR A 1 313 ? 4.093   0.743   10.506  1.00 33.93  ? 313 TYR A CE2 1 
ATOM   2535 C  CZ  . TYR A 1 313 ? 4.351   0.795   9.147   1.00 38.04  ? 313 TYR A CZ  1 
ATOM   2536 O  OH  . TYR A 1 313 ? 5.368   0.028   8.614   1.00 38.07  ? 313 TYR A OH  1 
ATOM   2537 N  N   . VAL A 1 314 ? -0.843  1.428   12.498  1.00 31.97  ? 314 VAL A N   1 
ATOM   2538 C  CA  . VAL A 1 314 ? -1.196  0.211   13.218  1.00 32.45  ? 314 VAL A CA  1 
ATOM   2539 C  C   . VAL A 1 314 ? -2.227  -0.575  12.413  1.00 34.74  ? 314 VAL A C   1 
ATOM   2540 O  O   . VAL A 1 314 ? -2.150  -1.805  12.306  1.00 32.06  ? 314 VAL A O   1 
ATOM   2541 C  CB  . VAL A 1 314 ? -1.694  0.560   14.630  1.00 36.55  ? 314 VAL A CB  1 
ATOM   2542 C  CG1 . VAL A 1 314 ? -2.257  -0.695  15.345  1.00 35.45  ? 314 VAL A CG1 1 
ATOM   2543 C  CG2 . VAL A 1 314 ? -0.549  1.211   15.436  1.00 34.47  ? 314 VAL A CG2 1 
ATOM   2544 N  N   . GLY A 1 315 ? -3.171  0.137   11.787  1.00 32.15  ? 315 GLY A N   1 
ATOM   2545 C  CA  . GLY A 1 315 ? -4.168  -0.528  10.964  1.00 34.16  ? 315 GLY A CA  1 
ATOM   2546 C  C   . GLY A 1 315 ? -3.568  -1.251  9.770   1.00 34.03  ? 315 GLY A C   1 
ATOM   2547 O  O   . GLY A 1 315 ? -3.993  -2.358  9.428   1.00 33.83  ? 315 GLY A O   1 
ATOM   2548 N  N   . MET A 1 316 ? -2.589  -0.637  9.095   1.00 33.62  ? 316 MET A N   1 
ATOM   2549 C  CA  . MET A 1 316 ? -1.994  -1.384  7.990   1.00 35.75  ? 316 MET A CA  1 
ATOM   2550 C  C   . MET A 1 316 ? -1.101  -2.515  8.472   1.00 33.58  ? 316 MET A C   1 
ATOM   2551 O  O   . MET A 1 316 ? -0.975  -3.517  7.766   1.00 34.10  ? 316 MET A O   1 
ATOM   2552 C  CB  . MET A 1 316 ? -1.266  -0.491  6.964   1.00 36.06  ? 316 MET A CB  1 
ATOM   2553 C  CG  . MET A 1 316 ? -1.786  0.919   6.762   1.00 41.55  ? 316 MET A CG  1 
ATOM   2554 S  SD  . MET A 1 316 ? -0.588  2.021   5.955   1.00 48.01  ? 316 MET A SD  1 
ATOM   2555 C  CE  . MET A 1 316 ? -1.689  3.354   5.489   1.00 50.31  ? 316 MET A CE  1 
ATOM   2556 N  N   . VAL A 1 317 ? -0.494  -2.394  9.656   1.00 30.41  ? 317 VAL A N   1 
ATOM   2557 C  CA  . VAL A 1 317 ? 0.186   -3.545  10.257  1.00 33.61  ? 317 VAL A CA  1 
ATOM   2558 C  C   . VAL A 1 317 ? -0.786  -4.707  10.410  1.00 36.86  ? 317 VAL A C   1 
ATOM   2559 O  O   . VAL A 1 317 ? -0.474  -5.861  10.086  1.00 34.13  ? 317 VAL A O   1 
ATOM   2560 C  CB  . VAL A 1 317 ? 0.805   -3.165  11.617  1.00 33.53  ? 317 VAL A CB  1 
ATOM   2561 C  CG1 . VAL A 1 317 ? 1.147   -4.418  12.423  1.00 32.53  ? 317 VAL A CG1 1 
ATOM   2562 C  CG2 . VAL A 1 317 ? 2.050   -2.316  11.422  1.00 37.86  ? 317 VAL A CG2 1 
ATOM   2563 N  N   . LEU A 1 318 ? -1.979  -4.419  10.936  1.00 33.42  ? 318 LEU A N   1 
ATOM   2564 C  CA  . LEU A 1 318 ? -2.961  -5.476  11.108  1.00 32.58  ? 318 LEU A CA  1 
ATOM   2565 C  C   . LEU A 1 318 ? -3.369  -6.057  9.765   1.00 32.96  ? 318 LEU A C   1 
ATOM   2566 O  O   . LEU A 1 318 ? -3.484  -7.280  9.613   1.00 31.47  ? 318 LEU A O   1 
ATOM   2567 C  CB  . LEU A 1 318 ? -4.170  -4.927  11.862  1.00 29.71  ? 318 LEU A CB  1 
ATOM   2568 C  CG  . LEU A 1 318 ? -3.824  -4.613  13.323  1.00 29.47  ? 318 LEU A CG  1 
ATOM   2569 C  CD1 . LEU A 1 318 ? -4.977  -3.829  13.964  1.00 29.93  ? 318 LEU A CD1 1 
ATOM   2570 C  CD2 . LEU A 1 318 ? -3.535  -5.893  14.110  1.00 30.44  ? 318 LEU A CD2 1 
ATOM   2571 N  N   . ASN A 1 319 ? -3.589  -5.198  8.771   1.00 33.98  ? 319 ASN A N   1 
ATOM   2572 C  CA  . ASN A 1 319 ? -3.976  -5.719  7.465   1.00 30.40  ? 319 ASN A CA  1 
ATOM   2573 C  C   . ASN A 1 319 ? -2.888  -6.598  6.866   1.00 33.33  ? 319 ASN A C   1 
ATOM   2574 O  O   . ASN A 1 319 ? -3.182  -7.615  6.231   1.00 32.50  ? 319 ASN A O   1 
ATOM   2575 C  CB  . ASN A 1 319 ? -4.335  -4.570  6.536   1.00 32.75  ? 319 ASN A CB  1 
ATOM   2576 C  CG  . ASN A 1 319 ? -5.743  -4.098  6.771   1.00 38.50  ? 319 ASN A CG  1 
ATOM   2577 O  OD1 . ASN A 1 319 ? -6.593  -4.886  7.157   1.00 36.13  ? 319 ASN A OD1 1 
ATOM   2578 N  ND2 . ASN A 1 319 ? -5.995  -2.824  6.560   1.00 38.04  ? 319 ASN A ND2 1 
ATOM   2579 N  N   . GLU A 1 320 ? -1.622  -6.226  7.056   1.00 33.29  ? 320 GLU A N   1 
ATOM   2580 C  CA  . GLU A 1 320 ? -0.539  -7.025  6.490   1.00 28.33  ? 320 GLU A CA  1 
ATOM   2581 C  C   . GLU A 1 320 ? -0.389  -8.349  7.225   1.00 33.86  ? 320 GLU A C   1 
ATOM   2582 O  O   . GLU A 1 320 ? -0.039  -9.363  6.607   1.00 32.22  ? 320 GLU A O   1 
ATOM   2583 C  CB  . GLU A 1 320 ? 0.761   -6.207  6.510   1.00 30.69  ? 320 GLU A CB  1 
ATOM   2584 C  CG  . GLU A 1 320 ? 2.010   -6.927  5.980   1.00 30.60  ? 320 GLU A CG  1 
ATOM   2585 C  CD  . GLU A 1 320 ? 2.026   -7.110  4.469   1.00 38.72  ? 320 GLU A CD  1 
ATOM   2586 O  OE1 . GLU A 1 320 ? 0.959   -7.001  3.829   1.00 36.93  ? 320 GLU A OE1 1 
ATOM   2587 O  OE2 . GLU A 1 320 ? 3.118   -7.362  3.922   1.00 38.47  ? 320 GLU A OE2 1 
ATOM   2588 N  N   . ALA A 1 321 ? -0.675  -8.372  8.534   1.00 31.95  ? 321 ALA A N   1 
ATOM   2589 C  CA  . ALA A 1 321 ? -0.710  -9.647  9.246   1.00 28.99  ? 321 ALA A CA  1 
ATOM   2590 C  C   . ALA A 1 321 ? -1.854  -10.517 8.745   1.00 32.32  ? 321 ALA A C   1 
ATOM   2591 O  O   . ALA A 1 321 ? -1.700  -11.737 8.601   1.00 32.57  ? 321 ALA A O   1 
ATOM   2592 C  CB  . ALA A 1 321 ? -0.840  -9.419  10.764  1.00 32.88  ? 321 ALA A CB  1 
ATOM   2593 N  N   . LEU A 1 322 ? -3.019  -9.909  8.484   1.00 32.73  ? 322 LEU A N   1 
ATOM   2594 C  CA  . LEU A 1 322 ? -4.121  -10.671 7.900   1.00 32.36  ? 322 LEU A CA  1 
ATOM   2595 C  C   . LEU A 1 322 ? -3.797  -11.166 6.499   1.00 33.99  ? 322 LEU A C   1 
ATOM   2596 O  O   . LEU A 1 322 ? -4.369  -12.173 6.047   1.00 33.30  ? 322 LEU A O   1 
ATOM   2597 C  CB  . LEU A 1 322 ? -5.384  -9.816  7.838   1.00 31.30  ? 322 LEU A CB  1 
ATOM   2598 C  CG  . LEU A 1 322 ? -6.139  -9.610  9.147   1.00 30.95  ? 322 LEU A CG  1 
ATOM   2599 C  CD1 . LEU A 1 322 ? -7.281  -8.636  8.858   1.00 33.13  ? 322 LEU A CD1 1 
ATOM   2600 C  CD2 . LEU A 1 322 ? -6.653  -10.942 9.705   1.00 28.86  ? 322 LEU A CD2 1 
ATOM   2601 N  N   . ARG A 1 323 ? -2.940  -10.441 5.768   1.00 30.15  ? 323 ARG A N   1 
ATOM   2602 C  CA  . ARG A 1 323 ? -2.576  -10.892 4.430   1.00 31.57  ? 323 ARG A CA  1 
ATOM   2603 C  C   . ARG A 1 323 ? -1.787  -12.184 4.501   1.00 31.33  ? 323 ARG A C   1 
ATOM   2604 O  O   . ARG A 1 323 ? -2.145  -13.179 3.861   1.00 31.18  ? 323 ARG A O   1 
ATOM   2605 C  CB  . ARG A 1 323 ? -1.773  -9.818  3.676   1.00 29.85  ? 323 ARG A CB  1 
ATOM   2606 C  CG  . ARG A 1 323 ? -1.453  -10.249 2.205   1.00 32.47  ? 323 ARG A CG  1 
ATOM   2607 C  CD  . ARG A 1 323 ? -0.591  -9.229  1.443   1.00 34.91  ? 323 ARG A CD  1 
ATOM   2608 N  NE  . ARG A 1 323 ? 0.749   -9.123  2.020   1.00 34.59  ? 323 ARG A NE  1 
ATOM   2609 C  CZ  . ARG A 1 323 ? 1.732   -9.974  1.769   1.00 38.95  ? 323 ARG A CZ  1 
ATOM   2610 N  NH1 . ARG A 1 323 ? 1.560   -11.008 0.958   1.00 36.98  ? 323 ARG A NH1 1 
ATOM   2611 N  NH2 . ARG A 1 323 ? 2.918   -9.786  2.348   1.00 37.85  ? 323 ARG A NH2 1 
ATOM   2612 N  N   . LEU A 1 324 ? -0.714  -12.198 5.292   1.00 35.79  ? 324 LEU A N   1 
ATOM   2613 C  CA  . LEU A 1 324 ? 0.155   -13.372 5.313   1.00 33.22  ? 324 LEU A CA  1 
ATOM   2614 C  C   . LEU A 1 324 ? -0.473  -14.541 6.061   1.00 32.36  ? 324 LEU A C   1 
ATOM   2615 O  O   . LEU A 1 324 ? -0.290  -15.700 5.667   1.00 34.58  ? 324 LEU A O   1 
ATOM   2616 C  CB  . LEU A 1 324 ? 1.519   -13.006 5.908   1.00 33.64  ? 324 LEU A CB  1 
ATOM   2617 C  CG  . LEU A 1 324 ? 2.363   -12.244 4.889   1.00 35.82  ? 324 LEU A CG  1 
ATOM   2618 C  CD1 . LEU A 1 324 ? 3.470   -11.439 5.556   1.00 40.84  ? 324 LEU A CD1 1 
ATOM   2619 C  CD2 . LEU A 1 324 ? 2.927   -13.225 3.869   1.00 38.28  ? 324 LEU A CD2 1 
ATOM   2620 N  N   . TRP A 1 325 ? -1.248  -14.275 7.118   1.00 34.49  ? 325 TRP A N   1 
ATOM   2621 C  CA  . TRP A 1 325 ? -1.870  -15.345 7.905   1.00 29.44  ? 325 TRP A CA  1 
ATOM   2622 C  C   . TRP A 1 325 ? -3.305  -14.992 8.268   1.00 33.14  ? 325 TRP A C   1 
ATOM   2623 O  O   . TRP A 1 325 ? -3.617  -14.722 9.432   1.00 33.45  ? 325 TRP A O   1 
ATOM   2624 C  CB  . TRP A 1 325 ? -1.020  -15.655 9.146   1.00 31.12  ? 325 TRP A CB  1 
ATOM   2625 C  CG  . TRP A 1 325 ? 0.183   -16.429 8.710   1.00 29.52  ? 325 TRP A CG  1 
ATOM   2626 C  CD1 . TRP A 1 325 ? 1.485   -16.037 8.777   1.00 34.79  ? 325 TRP A CD1 1 
ATOM   2627 C  CD2 . TRP A 1 325 ? 0.176   -17.687 8.033   1.00 34.13  ? 325 TRP A CD2 1 
ATOM   2628 N  NE1 . TRP A 1 325 ? 2.296   -16.991 8.209   1.00 35.73  ? 325 TRP A NE1 1 
ATOM   2629 C  CE2 . TRP A 1 325 ? 1.514   -18.016 7.747   1.00 35.78  ? 325 TRP A CE2 1 
ATOM   2630 C  CE3 . TRP A 1 325 ? -0.833  -18.581 7.662   1.00 35.12  ? 325 TRP A CE3 1 
ATOM   2631 C  CZ2 . TRP A 1 325 ? 1.868   -19.193 7.099   1.00 36.93  ? 325 TRP A CZ2 1 
ATOM   2632 C  CZ3 . TRP A 1 325 ? -0.477  -19.756 7.022   1.00 39.12  ? 325 TRP A CZ3 1 
ATOM   2633 C  CH2 . TRP A 1 325 ? 0.859   -20.050 6.748   1.00 41.25  ? 325 TRP A CH2 1 
ATOM   2634 N  N   . PRO A 1 326 ? -4.220  -15.042 7.294   1.00 32.71  ? 326 PRO A N   1 
ATOM   2635 C  CA  . PRO A 1 326 ? -5.634  -14.755 7.582   1.00 34.00  ? 326 PRO A CA  1 
ATOM   2636 C  C   . PRO A 1 326 ? -6.195  -15.797 8.534   1.00 34.61  ? 326 PRO A C   1 
ATOM   2637 O  O   . PRO A 1 326 ? -6.245  -16.988 8.219   1.00 29.82  ? 326 PRO A O   1 
ATOM   2638 C  CB  . PRO A 1 326 ? -6.302  -14.805 6.203   1.00 33.55  ? 326 PRO A CB  1 
ATOM   2639 C  CG  . PRO A 1 326 ? -5.391  -15.686 5.358   1.00 32.41  ? 326 PRO A CG  1 
ATOM   2640 C  CD  . PRO A 1 326 ? -3.997  -15.408 5.876   1.00 32.54  ? 326 PRO A CD  1 
ATOM   2641 N  N   . THR A 1 327 ? -6.612  -15.341 9.720   1.00 34.15  ? 327 THR A N   1 
ATOM   2642 C  CA  . THR A 1 327 ? -6.819  -16.298 10.805  1.00 31.54  ? 327 THR A CA  1 
ATOM   2643 C  C   . THR A 1 327 ? -8.029  -17.191 10.555  1.00 35.31  ? 327 THR A C   1 
ATOM   2644 O  O   . THR A 1 327 ? -8.071  -18.322 11.058  1.00 33.03  ? 327 THR A O   1 
ATOM   2645 C  CB  . THR A 1 327 ? -6.950  -15.580 12.150  1.00 36.52  ? 327 THR A CB  1 
ATOM   2646 O  OG1 . THR A 1 327 ? -7.777  -14.424 12.015  1.00 37.33  ? 327 THR A OG1 1 
ATOM   2647 C  CG2 . THR A 1 327 ? -5.574  -15.081 12.572  1.00 39.05  ? 327 THR A CG2 1 
ATOM   2648 N  N   . ALA A 1 328 ? -9.036  -16.703 9.816   1.00 30.44  ? 328 ALA A N   1 
ATOM   2649 C  CA  . ALA A 1 328 ? -10.080 -17.581 9.304   1.00 29.68  ? 328 ALA A CA  1 
ATOM   2650 C  C   . ALA A 1 328 ? -9.681  -17.938 7.881   1.00 33.76  ? 328 ALA A C   1 
ATOM   2651 O  O   . ALA A 1 328 ? -9.868  -17.118 6.967   1.00 38.35  ? 328 ALA A O   1 
ATOM   2652 C  CB  . ALA A 1 328 ? -11.450 -16.898 9.325   1.00 38.61  ? 328 ALA A CB  1 
ATOM   2653 N  N   . PRO A 1 329 ? -9.098  -19.109 7.635   1.00 32.21  ? 329 PRO A N   1 
ATOM   2654 C  CA  . PRO A 1 329 ? -8.263  -19.275 6.438   1.00 31.40  ? 329 PRO A CA  1 
ATOM   2655 C  C   . PRO A 1 329 ? -9.004  -19.691 5.178   1.00 30.21  ? 329 PRO A C   1 
ATOM   2656 O  O   . PRO A 1 329 ? -8.378  -19.744 4.112   1.00 29.66  ? 329 PRO A O   1 
ATOM   2657 C  CB  . PRO A 1 329 ? -7.282  -20.364 6.886   1.00 32.79  ? 329 PRO A CB  1 
ATOM   2658 C  CG  . PRO A 1 329 ? -8.112  -21.232 7.764   1.00 33.90  ? 329 PRO A CG  1 
ATOM   2659 C  CD  . PRO A 1 329 ? -9.030  -20.292 8.511   1.00 33.25  ? 329 PRO A CD  1 
ATOM   2660 N  N   . ALA A 1 330 ? -10.307 -19.950 5.234   1.00 29.64  ? 330 ALA A N   1 
ATOM   2661 C  CA  . ALA A 1 330 ? -11.003 -20.302 4.005   1.00 34.56  ? 330 ALA A CA  1 
ATOM   2662 C  C   . ALA A 1 330 ? -12.467 -19.919 4.115   1.00 32.37  ? 330 ALA A C   1 
ATOM   2663 O  O   . ALA A 1 330 ? -12.987 -19.670 5.204   1.00 33.12  ? 330 ALA A O   1 
ATOM   2664 C  CB  . ALA A 1 330 ? -10.884 -21.796 3.701   1.00 34.03  ? 330 ALA A CB  1 
ATOM   2665 N  N   . PHE A 1 331 ? -13.125 -19.887 2.958   1.00 31.07  ? 331 PHE A N   1 
ATOM   2666 C  CA  . PHE A 1 331 ? -14.575 -19.908 2.911   1.00 29.92  ? 331 PHE A CA  1 
ATOM   2667 C  C   . PHE A 1 331 ? -15.000 -20.618 1.632   1.00 34.80  ? 331 PHE A C   1 
ATOM   2668 O  O   . PHE A 1 331 ? -14.220 -20.767 0.685   1.00 32.70  ? 331 PHE A O   1 
ATOM   2669 C  CB  . PHE A 1 331 ? -15.180 -18.495 3.032   1.00 33.76  ? 331 PHE A CB  1 
ATOM   2670 C  CG  . PHE A 1 331 ? -14.690 -17.492 2.002   1.00 34.81  ? 331 PHE A CG  1 
ATOM   2671 C  CD1 . PHE A 1 331 ? -13.556 -16.719 2.239   1.00 33.84  ? 331 PHE A CD1 1 
ATOM   2672 C  CD2 . PHE A 1 331 ? -15.410 -17.268 0.827   1.00 35.05  ? 331 PHE A CD2 1 
ATOM   2673 C  CE1 . PHE A 1 331 ? -13.128 -15.763 1.313   1.00 34.47  ? 331 PHE A CE1 1 
ATOM   2674 C  CE2 . PHE A 1 331 ? -14.980 -16.309 -0.111  1.00 36.26  ? 331 PHE A CE2 1 
ATOM   2675 C  CZ  . PHE A 1 331 ? -13.844 -15.563 0.133   1.00 34.56  ? 331 PHE A CZ  1 
ATOM   2676 N  N   . SER A 1 332 ? -16.248 -21.072 1.635   1.00 31.77  ? 332 SER A N   1 
ATOM   2677 C  CA  . SER A 1 332 ? -16.813 -21.932 0.611   1.00 29.68  ? 332 SER A CA  1 
ATOM   2678 C  C   . SER A 1 332 ? -17.944 -21.217 -0.124  1.00 32.82  ? 332 SER A C   1 
ATOM   2679 O  O   . SER A 1 332 ? -18.662 -20.390 0.451   1.00 31.49  ? 332 SER A O   1 
ATOM   2680 C  CB  . SER A 1 332 ? -17.341 -23.220 1.249   1.00 35.48  ? 332 SER A CB  1 
ATOM   2681 O  OG  . SER A 1 332 ? -17.723 -24.172 0.284   1.00 39.26  ? 332 SER A OG  1 
ATOM   2682 N  N   . LEU A 1 333 ? -18.118 -21.571 -1.397  1.00 32.05  ? 333 LEU A N   1 
ATOM   2683 C  CA  . LEU A 1 333 ? -19.110 -20.957 -2.266  1.00 32.84  ? 333 LEU A CA  1 
ATOM   2684 C  C   . LEU A 1 333 ? -19.733 -22.064 -3.096  1.00 33.60  ? 333 LEU A C   1 
ATOM   2685 O  O   . LEU A 1 333 ? -19.131 -23.127 -3.273  1.00 35.67  ? 333 LEU A O   1 
ATOM   2686 C  CB  . LEU A 1 333 ? -18.487 -19.902 -3.198  1.00 32.16  ? 333 LEU A CB  1 
ATOM   2687 C  CG  . LEU A 1 333 ? -17.772 -18.718 -2.522  1.00 35.38  ? 333 LEU A CG  1 
ATOM   2688 C  CD1 . LEU A 1 333 ? -16.756 -18.039 -3.465  1.00 32.38  ? 333 LEU A CD1 1 
ATOM   2689 C  CD2 . LEU A 1 333 ? -18.775 -17.713 -2.003  1.00 31.86  ? 333 LEU A CD2 1 
ATOM   2690 N  N   . TYR A 1 334 ? -20.955 -21.821 -3.592  1.00 32.22  ? 334 TYR A N   1 
ATOM   2691 C  CA  . TYR A 1 334 ? -21.559 -22.703 -4.586  1.00 33.90  ? 334 TYR A CA  1 
ATOM   2692 C  C   . TYR A 1 334 ? -22.078 -21.877 -5.755  1.00 34.83  ? 334 TYR A C   1 
ATOM   2693 O  O   . TYR A 1 334 ? -22.467 -20.711 -5.601  1.00 33.80  ? 334 TYR A O   1 
ATOM   2694 C  CB  . TYR A 1 334 ? -22.708 -23.565 -4.006  1.00 33.35  ? 334 TYR A CB  1 
ATOM   2695 C  CG  . TYR A 1 334 ? -23.933 -22.765 -3.633  1.00 33.98  ? 334 TYR A CG  1 
ATOM   2696 C  CD1 . TYR A 1 334 ? -24.061 -22.209 -2.362  1.00 33.48  ? 334 TYR A CD1 1 
ATOM   2697 C  CD2 . TYR A 1 334 ? -24.963 -22.560 -4.548  1.00 37.69  ? 334 TYR A CD2 1 
ATOM   2698 C  CE1 . TYR A 1 334 ? -25.190 -21.460 -2.019  1.00 31.00  ? 334 TYR A CE1 1 
ATOM   2699 C  CE2 . TYR A 1 334 ? -26.086 -21.827 -4.215  1.00 35.47  ? 334 TYR A CE2 1 
ATOM   2700 C  CZ  . TYR A 1 334 ? -26.195 -21.279 -2.954  1.00 32.99  ? 334 TYR A CZ  1 
ATOM   2701 O  OH  . TYR A 1 334 ? -27.307 -20.537 -2.629  1.00 35.13  ? 334 TYR A OH  1 
ATOM   2702 N  N   . ALA A 1 335 ? -22.074 -22.499 -6.929  1.00 35.54  ? 335 ALA A N   1 
ATOM   2703 C  CA  . ALA A 1 335 ? -22.519 -21.834 -8.149  1.00 34.67  ? 335 ALA A CA  1 
ATOM   2704 C  C   . ALA A 1 335 ? -24.036 -21.695 -8.138  1.00 34.37  ? 335 ALA A C   1 
ATOM   2705 O  O   . ALA A 1 335 ? -24.754 -22.688 -7.998  1.00 36.39  ? 335 ALA A O   1 
ATOM   2706 C  CB  . ALA A 1 335 ? -22.067 -22.622 -9.374  1.00 37.21  ? 335 ALA A CB  1 
ATOM   2707 N  N   . LYS A 1 336 ? -24.525 -20.467 -8.304  1.00 34.15  ? 336 LYS A N   1 
ATOM   2708 C  CA  . LYS A 1 336 ? -25.968 -20.262 -8.351  1.00 37.08  ? 336 LYS A CA  1 
ATOM   2709 C  C   . LYS A 1 336 ? -26.564 -20.794 -9.651  1.00 42.52  ? 336 LYS A C   1 
ATOM   2710 O  O   . LYS A 1 336 ? -27.735 -21.213 -9.675  1.00 41.88  ? 336 LYS A O   1 
ATOM   2711 C  CB  . LYS A 1 336 ? -26.286 -18.784 -8.176  1.00 36.65  ? 336 LYS A CB  1 
ATOM   2712 C  CG  . LYS A 1 336 ? -25.945 -18.271 -6.780  1.00 38.82  ? 336 LYS A CG  1 
ATOM   2713 C  CD  . LYS A 1 336 ? -25.910 -16.733 -6.718  1.00 32.98  ? 336 LYS A CD  1 
ATOM   2714 C  CE  . LYS A 1 336 ? -27.191 -16.102 -7.239  1.00 40.39  ? 336 LYS A CE  1 
ATOM   2715 N  NZ  . LYS A 1 336 ? -28.332 -16.291 -6.289  1.00 37.82  ? 336 LYS A NZ  1 
ATOM   2716 N  N   . GLU A 1 337 ? -25.768 -20.819 -10.719 1.00 35.92  ? 337 GLU A N   1 
ATOM   2717 C  CA  . GLU A 1 337 ? -26.239 -21.274 -12.019 1.00 42.98  ? 337 GLU A CA  1 
ATOM   2718 C  C   . GLU A 1 337 ? -25.032 -21.869 -12.732 1.00 43.17  ? 337 GLU A C   1 
ATOM   2719 O  O   . GLU A 1 337 ? -23.889 -21.614 -12.347 1.00 42.47  ? 337 GLU A O   1 
ATOM   2720 C  CB  . GLU A 1 337 ? -26.813 -20.103 -12.829 1.00 44.79  ? 337 GLU A CB  1 
ATOM   2721 C  CG  . GLU A 1 337 ? -28.278 -19.789 -12.497 1.00 48.64  ? 337 GLU A CG  1 
ATOM   2722 C  CD  . GLU A 1 337 ? -29.196 -21.000 -12.495 1.00 55.41  ? 337 GLU A CD  1 
ATOM   2723 O  OE1 . GLU A 1 337 ? -30.226 -20.936 -11.786 1.00 53.95  ? 337 GLU A OE1 1 
ATOM   2724 O  OE2 . GLU A 1 337 ? -28.906 -21.995 -13.195 1.00 61.82  ? 337 GLU A OE2 1 
ATOM   2725 N  N   . ASP A 1 338 ? -25.275 -22.647 -13.787 1.00 45.14  ? 338 ASP A N   1 
ATOM   2726 C  CA  . ASP A 1 338 ? -24.166 -23.043 -14.655 1.00 43.45  ? 338 ASP A CA  1 
ATOM   2727 C  C   . ASP A 1 338 ? -23.354 -21.811 -15.031 1.00 39.10  ? 338 ASP A C   1 
ATOM   2728 O  O   . ASP A 1 338 ? -23.914 -20.752 -15.327 1.00 46.03  ? 338 ASP A O   1 
ATOM   2729 C  CB  . ASP A 1 338 ? -24.680 -23.720 -15.932 1.00 45.06  ? 338 ASP A CB  1 
ATOM   2730 C  CG  . ASP A 1 338 ? -25.403 -25.015 -15.662 1.00 45.24  ? 338 ASP A CG  1 
ATOM   2731 O  OD1 . ASP A 1 338 ? -25.326 -25.521 -14.528 1.00 48.74  ? 338 ASP A OD1 1 
ATOM   2732 O  OD2 . ASP A 1 338 ? -26.063 -25.529 -16.590 1.00 53.86  ? 338 ASP A OD2 1 
ATOM   2733 N  N   . THR A 1 339 ? -22.030 -21.941 -15.014 1.00 41.17  ? 339 THR A N   1 
ATOM   2734 C  CA  . THR A 1 339 ? -21.169 -20.802 -15.311 1.00 43.38  ? 339 THR A CA  1 
ATOM   2735 C  C   . THR A 1 339 ? -19.767 -21.317 -15.611 1.00 42.69  ? 339 THR A C   1 
ATOM   2736 O  O   . THR A 1 339 ? -19.412 -22.449 -15.273 1.00 45.16  ? 339 THR A O   1 
ATOM   2737 C  CB  . THR A 1 339 ? -21.154 -19.793 -14.146 1.00 44.16  ? 339 THR A CB  1 
ATOM   2738 O  OG1 . THR A 1 339 ? -20.567 -18.561 -14.561 1.00 41.33  ? 339 THR A OG1 1 
ATOM   2739 C  CG2 . THR A 1 339 ? -20.342 -20.337 -12.966 1.00 39.41  ? 339 THR A CG2 1 
ATOM   2740 N  N   . VAL A 1 340 ? -18.969 -20.471 -16.248 1.00 46.72  ? 340 VAL A N   1 
ATOM   2741 C  CA  . VAL A 1 340 ? -17.618 -20.840 -16.650 1.00 45.26  ? 340 VAL A CA  1 
ATOM   2742 C  C   . VAL A 1 340 ? -16.657 -19.947 -15.886 1.00 44.78  ? 340 VAL A C   1 
ATOM   2743 O  O   . VAL A 1 340 ? -16.749 -18.717 -15.957 1.00 46.19  ? 340 VAL A O   1 
ATOM   2744 C  CB  . VAL A 1 340 ? -17.415 -20.723 -18.170 1.00 44.63  ? 340 VAL A CB  1 
ATOM   2745 C  CG1 . VAL A 1 340 ? -15.946 -20.919 -18.523 1.00 45.36  ? 340 VAL A CG1 1 
ATOM   2746 C  CG2 . VAL A 1 340 ? -18.285 -21.756 -18.900 1.00 41.63  ? 340 VAL A CG2 1 
ATOM   2747 N  N   . LEU A 1 341 ? -15.755 -20.563 -15.136 1.00 45.99  ? 341 LEU A N   1 
ATOM   2748 C  CA  . LEU A 1 341 ? -14.797 -19.835 -14.324 1.00 43.32  ? 341 LEU A CA  1 
ATOM   2749 C  C   . LEU A 1 341 ? -13.534 -19.572 -15.133 1.00 41.01  ? 341 LEU A C   1 
ATOM   2750 O  O   . LEU A 1 341 ? -12.946 -20.504 -15.688 1.00 43.37  ? 341 LEU A O   1 
ATOM   2751 C  CB  . LEU A 1 341 ? -14.475 -20.651 -13.073 1.00 43.14  ? 341 LEU A CB  1 
ATOM   2752 C  CG  . LEU A 1 341 ? -13.924 -19.964 -11.839 1.00 49.97  ? 341 LEU A CG  1 
ATOM   2753 C  CD1 . LEU A 1 341 ? -14.935 -18.958 -11.270 1.00 39.42  ? 341 LEU A CD1 1 
ATOM   2754 C  CD2 . LEU A 1 341 ? -13.586 -21.051 -10.829 1.00 39.84  ? 341 LEU A CD2 1 
ATOM   2755 N  N   . GLY A 1 342 ? -13.121 -18.308 -15.195 1.00 42.96  ? 342 GLY A N   1 
ATOM   2756 C  CA  . GLY A 1 342 ? -11.884 -17.956 -15.859 1.00 43.86  ? 342 GLY A CA  1 
ATOM   2757 C  C   . GLY A 1 342 ? -11.807 -18.368 -17.310 1.00 51.01  ? 342 GLY A C   1 
ATOM   2758 O  O   . GLY A 1 342 ? -10.702 -18.547 -17.833 1.00 49.68  ? 342 GLY A O   1 
ATOM   2759 N  N   . GLY A 1 343 ? -12.948 -18.540 -17.977 1.00 42.55  ? 343 GLY A N   1 
ATOM   2760 C  CA  . GLY A 1 343 ? -12.954 -18.973 -19.367 1.00 48.57  ? 343 GLY A CA  1 
ATOM   2761 C  C   . GLY A 1 343 ? -12.444 -20.373 -19.618 1.00 49.78  ? 343 GLY A C   1 
ATOM   2762 O  O   . GLY A 1 343 ? -12.286 -20.761 -20.780 1.00 46.68  ? 343 GLY A O   1 
ATOM   2763 N  N   . GLU A 1 344 ? -12.199 -21.160 -18.574 1.00 46.16  ? 344 GLU A N   1 
ATOM   2764 C  CA  . GLU A 1 344 ? -11.508 -22.433 -18.739 1.00 50.19  ? 344 GLU A CA  1 
ATOM   2765 C  C   . GLU A 1 344 ? -12.181 -23.576 -17.991 1.00 49.97  ? 344 GLU A C   1 
ATOM   2766 O  O   . GLU A 1 344 ? -12.047 -24.740 -18.388 1.00 52.30  ? 344 GLU A O   1 
ATOM   2767 C  CB  . GLU A 1 344 ? -10.052 -22.306 -18.271 1.00 49.17  ? 344 GLU A CB  1 
ATOM   2768 C  CG  . GLU A 1 344 ? -9.089  -21.746 -19.310 1.00 56.98  ? 344 GLU A CG  1 
ATOM   2769 C  CD  . GLU A 1 344 ? -7.749  -21.345 -18.718 1.00 58.56  ? 344 GLU A CD  1 
ATOM   2770 O  OE1 . GLU A 1 344 ? -7.671  -21.169 -17.484 1.00 57.91  ? 344 GLU A OE1 1 
ATOM   2771 O  OE2 . GLU A 1 344 ? -6.759  -21.247 -19.478 1.00 66.21  ? 344 GLU A OE2 1 
ATOM   2772 N  N   . TYR A 1 345 ? -12.882 -23.271 -16.899 1.00 45.57  ? 345 TYR A N   1 
ATOM   2773 C  CA  . TYR A 1 345 ? -13.415 -24.311 -16.019 1.00 44.27  ? 345 TYR A CA  1 
ATOM   2774 C  C   . TYR A 1 345 ? -14.925 -24.207 -15.914 1.00 47.54  ? 345 TYR A C   1 
ATOM   2775 O  O   . TYR A 1 345 ? -15.447 -23.400 -15.124 1.00 42.65  ? 345 TYR A O   1 
ATOM   2776 C  CB  . TYR A 1 345 ? -12.766 -24.227 -14.641 1.00 44.36  ? 345 TYR A CB  1 
ATOM   2777 C  CG  . TYR A 1 345 ? -11.265 -24.310 -14.739 1.00 41.55  ? 345 TYR A CG  1 
ATOM   2778 C  CD1 . TYR A 1 345 ? -10.641 -25.515 -15.018 1.00 46.19  ? 345 TYR A CD1 1 
ATOM   2779 C  CD2 . TYR A 1 345 ? -10.475 -23.178 -14.585 1.00 41.67  ? 345 TYR A CD2 1 
ATOM   2780 C  CE1 . TYR A 1 345 ? -9.268  -25.602 -15.128 1.00 42.69  ? 345 TYR A CE1 1 
ATOM   2781 C  CE2 . TYR A 1 345 ? -9.108  -23.251 -14.691 1.00 43.40  ? 345 TYR A CE2 1 
ATOM   2782 C  CZ  . TYR A 1 345 ? -8.507  -24.467 -14.969 1.00 45.22  ? 345 TYR A CZ  1 
ATOM   2783 O  OH  . TYR A 1 345 ? -7.138  -24.541 -15.067 1.00 45.50  ? 345 TYR A OH  1 
ATOM   2784 N  N   . PRO A 1 346 ? -15.665 -24.997 -16.686 1.00 47.99  ? 346 PRO A N   1 
ATOM   2785 C  CA  . PRO A 1 346 ? -17.127 -24.956 -16.594 1.00 44.26  ? 346 PRO A CA  1 
ATOM   2786 C  C   . PRO A 1 346 ? -17.631 -25.577 -15.297 1.00 46.35  ? 346 PRO A C   1 
ATOM   2787 O  O   . PRO A 1 346 ? -17.130 -26.607 -14.840 1.00 42.21  ? 346 PRO A O   1 
ATOM   2788 C  CB  . PRO A 1 346 ? -17.578 -25.757 -17.822 1.00 47.36  ? 346 PRO A CB  1 
ATOM   2789 C  CG  . PRO A 1 346 ? -16.429 -26.659 -18.118 1.00 49.39  ? 346 PRO A CG  1 
ATOM   2790 C  CD  . PRO A 1 346 ? -15.204 -25.839 -17.802 1.00 45.90  ? 346 PRO A CD  1 
ATOM   2791 N  N   . LEU A 1 347 ? -18.633 -24.923 -14.704 1.00 40.41  ? 347 LEU A N   1 
ATOM   2792 C  CA  . LEU A 1 347 ? -19.255 -25.370 -13.470 1.00 40.42  ? 347 LEU A CA  1 
ATOM   2793 C  C   . LEU A 1 347 ? -20.746 -25.502 -13.697 1.00 40.32  ? 347 LEU A C   1 
ATOM   2794 O  O   . LEU A 1 347 ? -21.355 -24.708 -14.424 1.00 40.50  ? 347 LEU A O   1 
ATOM   2795 C  CB  . LEU A 1 347 ? -19.004 -24.391 -12.318 1.00 39.11  ? 347 LEU A CB  1 
ATOM   2796 C  CG  . LEU A 1 347 ? -17.532 -24.140 -11.977 1.00 39.97  ? 347 LEU A CG  1 
ATOM   2797 C  CD1 . LEU A 1 347 ? -17.399 -23.020 -10.959 1.00 40.82  ? 347 LEU A CD1 1 
ATOM   2798 C  CD2 . LEU A 1 347 ? -16.882 -25.416 -11.466 1.00 40.94  ? 347 LEU A CD2 1 
ATOM   2799 N  N   . GLU A 1 348 ? -21.331 -26.500 -13.052 1.00 37.61  ? 348 GLU A N   1 
ATOM   2800 C  CA  . GLU A 1 348 ? -22.770 -26.687 -13.037 1.00 40.97  ? 348 GLU A CA  1 
ATOM   2801 C  C   . GLU A 1 348 ? -23.354 -26.081 -11.766 1.00 43.52  ? 348 GLU A C   1 
ATOM   2802 O  O   . GLU A 1 348 ? -22.685 -25.996 -10.735 1.00 41.28  ? 348 GLU A O   1 
ATOM   2803 C  CB  . GLU A 1 348 ? -23.115 -28.177 -13.122 1.00 45.94  ? 348 GLU A CB  1 
ATOM   2804 C  CG  . GLU A 1 348 ? -22.579 -28.822 -14.387 1.00 48.24  ? 348 GLU A CG  1 
ATOM   2805 C  CD  . GLU A 1 348 ? -23.049 -30.249 -14.549 1.00 57.64  ? 348 GLU A CD  1 
ATOM   2806 O  OE1 . GLU A 1 348 ? -22.540 -31.129 -13.833 1.00 61.52  ? 348 GLU A OE1 1 
ATOM   2807 O  OE2 . GLU A 1 348 ? -23.937 -30.485 -15.389 1.00 62.64  ? 348 GLU A OE2 1 
ATOM   2808 N  N   . LYS A 1 349 ? -24.605 -25.640 -11.857 1.00 40.21  ? 349 LYS A N   1 
ATOM   2809 C  CA  . LYS A 1 349 ? -25.333 -25.193 -10.680 1.00 40.45  ? 349 LYS A CA  1 
ATOM   2810 C  C   . LYS A 1 349 ? -25.138 -26.174 -9.535  1.00 41.06  ? 349 LYS A C   1 
ATOM   2811 O  O   . LYS A 1 349 ? -25.226 -27.390 -9.720  1.00 42.06  ? 349 LYS A O   1 
ATOM   2812 C  CB  . LYS A 1 349 ? -26.815 -25.051 -11.021 1.00 40.50  ? 349 LYS A CB  1 
ATOM   2813 C  CG  . LYS A 1 349 ? -27.695 -24.520 -9.922  1.00 44.80  ? 349 LYS A CG  1 
ATOM   2814 C  CD  . LYS A 1 349 ? -29.148 -24.843 -10.249 1.00 50.15  ? 349 LYS A CD  1 
ATOM   2815 C  CE  . LYS A 1 349 ? -30.086 -23.719 -9.830  1.00 52.18  ? 349 LYS A CE  1 
ATOM   2816 N  NZ  . LYS A 1 349 ? -31.409 -24.270 -9.414  1.00 60.43  ? 349 LYS A NZ  1 
ATOM   2817 N  N   . GLY A 1 350 ? -24.832 -25.643 -8.355  1.00 42.42  ? 350 GLY A N   1 
ATOM   2818 C  CA  . GLY A 1 350 ? -24.585 -26.454 -7.185  1.00 36.62  ? 350 GLY A CA  1 
ATOM   2819 C  C   . GLY A 1 350 ? -23.126 -26.761 -6.915  1.00 41.33  ? 350 GLY A C   1 
ATOM   2820 O  O   . GLY A 1 350 ? -22.785 -27.104 -5.776  1.00 39.95  ? 350 GLY A O   1 
ATOM   2821 N  N   . ASP A 1 351 ? -22.259 -26.644 -7.922  1.00 39.87  ? 351 ASP A N   1 
ATOM   2822 C  CA  . ASP A 1 351 ? -20.848 -26.971 -7.742  1.00 38.43  ? 351 ASP A CA  1 
ATOM   2823 C  C   . ASP A 1 351 ? -20.220 -26.044 -6.709  1.00 37.14  ? 351 ASP A C   1 
ATOM   2824 O  O   . ASP A 1 351 ? -20.499 -24.840 -6.682  1.00 33.46  ? 351 ASP A O   1 
ATOM   2825 C  CB  . ASP A 1 351 ? -20.088 -26.851 -9.066  1.00 36.64  ? 351 ASP A CB  1 
ATOM   2826 C  CG  . ASP A 1 351 ? -20.353 -28.021 -10.012 1.00 43.04  ? 351 ASP A CG  1 
ATOM   2827 O  OD1 . ASP A 1 351 ? -21.080 -28.959 -9.628  1.00 40.71  ? 351 ASP A OD1 1 
ATOM   2828 O  OD2 . ASP A 1 351 ? -19.823 -27.995 -11.142 1.00 40.61  ? 351 ASP A OD2 1 
ATOM   2829 N  N   . GLU A 1 352 ? -19.353 -26.612 -5.872  1.00 36.52  ? 352 GLU A N   1 
ATOM   2830 C  CA  . GLU A 1 352 ? -18.743 -25.921 -4.742  1.00 37.47  ? 352 GLU A CA  1 
ATOM   2831 C  C   . GLU A 1 352 ? -17.332 -25.453 -5.072  1.00 39.20  ? 352 GLU A C   1 
ATOM   2832 O  O   . GLU A 1 352 ? -16.617 -26.084 -5.855  1.00 37.93  ? 352 GLU A O   1 
ATOM   2833 C  CB  . GLU A 1 352 ? -18.673 -26.845 -3.528  1.00 40.28  ? 352 GLU A CB  1 
ATOM   2834 C  CG  . GLU A 1 352 ? -19.938 -27.574 -3.263  1.00 42.91  ? 352 GLU A CG  1 
ATOM   2835 C  CD  . GLU A 1 352 ? -19.943 -28.250 -1.914  1.00 49.09  ? 352 GLU A CD  1 
ATOM   2836 O  OE1 . GLU A 1 352 ? -18.934 -28.137 -1.178  1.00 44.70  ? 352 GLU A OE1 1 
ATOM   2837 O  OE2 . GLU A 1 352 ? -20.957 -28.914 -1.608  1.00 52.53  ? 352 GLU A OE2 1 
ATOM   2838 N  N   . LEU A 1 353 ? -16.935 -24.347 -4.433  1.00 34.88  ? 353 LEU A N   1 
ATOM   2839 C  CA  . LEU A 1 353 ? -15.582 -23.825 -4.467  1.00 34.57  ? 353 LEU A CA  1 
ATOM   2840 C  C   . LEU A 1 353 ? -15.119 -23.624 -3.035  1.00 33.07  ? 353 LEU A C   1 
ATOM   2841 O  O   . LEU A 1 353 ? -15.923 -23.288 -2.159  1.00 34.90  ? 353 LEU A O   1 
ATOM   2842 C  CB  . LEU A 1 353 ? -15.483 -22.471 -5.200  1.00 33.75  ? 353 LEU A CB  1 
ATOM   2843 C  CG  . LEU A 1 353 ? -15.997 -22.398 -6.629  1.00 35.20  ? 353 LEU A CG  1 
ATOM   2844 C  CD1 . LEU A 1 353 ? -16.006 -20.957 -7.085  1.00 37.28  ? 353 LEU A CD1 1 
ATOM   2845 C  CD2 . LEU A 1 353 ? -15.143 -23.267 -7.550  1.00 34.77  ? 353 LEU A CD2 1 
ATOM   2846 N  N   . MET A 1 354 ? -13.818 -23.795 -2.812  1.00 30.57  ? 354 MET A N   1 
ATOM   2847 C  CA  . MET A 1 354 ? -13.164 -23.398 -1.571  1.00 33.21  ? 354 MET A CA  1 
ATOM   2848 C  C   . MET A 1 354 ? -12.164 -22.290 -1.889  1.00 30.95  ? 354 MET A C   1 
ATOM   2849 O  O   . MET A 1 354 ? -11.316 -22.456 -2.768  1.00 34.02  ? 354 MET A O   1 
ATOM   2850 C  CB  . MET A 1 354 ? -12.417 -24.567 -0.917  1.00 33.97  ? 354 MET A CB  1 
ATOM   2851 C  CG  . MET A 1 354 ? -13.219 -25.642 -0.184  1.00 37.19  ? 354 MET A CG  1 
ATOM   2852 S  SD  . MET A 1 354 ? -14.461 -25.017 0.959   1.00 39.23  ? 354 MET A SD  1 
ATOM   2853 C  CE  . MET A 1 354 ? -13.381 -24.487 2.278   1.00 32.01  ? 354 MET A CE  1 
ATOM   2854 N  N   . VAL A 1 355 ? -12.238 -21.173 -1.172  1.00 31.95  ? 355 VAL A N   1 
ATOM   2855 C  CA  . VAL A 1 355 ? -11.274 -20.090 -1.358  1.00 31.90  ? 355 VAL A CA  1 
ATOM   2856 C  C   . VAL A 1 355 ? -10.182 -20.247 -0.299  1.00 31.75  ? 355 VAL A C   1 
ATOM   2857 O  O   . VAL A 1 355 ? -10.439 -20.119 0.898   1.00 30.92  ? 355 VAL A O   1 
ATOM   2858 C  CB  . VAL A 1 355 ? -11.943 -18.710 -1.288  1.00 33.88  ? 355 VAL A CB  1 
ATOM   2859 C  CG1 . VAL A 1 355 ? -10.877 -17.604 -1.346  1.00 31.23  ? 355 VAL A CG1 1 
ATOM   2860 C  CG2 . VAL A 1 355 ? -12.946 -18.560 -2.456  1.00 29.90  ? 355 VAL A CG2 1 
ATOM   2861 N  N   . LEU A 1 356 ? -8.958  -20.534 -0.740  1.00 31.11  ? 356 LEU A N   1 
ATOM   2862 C  CA  . LEU A 1 356 ? -7.844  -20.800 0.171   1.00 32.45  ? 356 LEU A CA  1 
ATOM   2863 C  C   . LEU A 1 356 ? -7.137  -19.472 0.398   1.00 33.98  ? 356 LEU A C   1 
ATOM   2864 O  O   . LEU A 1 356 ? -6.272  -19.068 -0.378  1.00 33.26  ? 356 LEU A O   1 
ATOM   2865 C  CB  . LEU A 1 356 ? -6.918  -21.858 -0.423  1.00 34.12  ? 356 LEU A CB  1 
ATOM   2866 C  CG  . LEU A 1 356 ? -5.801  -22.488 0.415   1.00 37.96  ? 356 LEU A CG  1 
ATOM   2867 C  CD1 . LEU A 1 356 ? -6.375  -23.178 1.667   1.00 38.17  ? 356 LEU A CD1 1 
ATOM   2868 C  CD2 . LEU A 1 356 ? -4.995  -23.482 -0.442  1.00 35.96  ? 356 LEU A CD2 1 
ATOM   2869 N  N   . ILE A 1 357 ? -7.544  -18.757 1.457   1.00 34.06  ? 357 ILE A N   1 
ATOM   2870 C  CA  . ILE A 1 357 ? -7.165  -17.343 1.582   1.00 29.27  ? 357 ILE A CA  1 
ATOM   2871 C  C   . ILE A 1 357 ? -5.662  -17.152 1.704   1.00 30.22  ? 357 ILE A C   1 
ATOM   2872 O  O   . ILE A 1 357 ? -5.129  -16.221 1.081   1.00 30.82  ? 357 ILE A O   1 
ATOM   2873 C  CB  . ILE A 1 357 ? -7.933  -16.683 2.734   1.00 29.27  ? 357 ILE A CB  1 
ATOM   2874 C  CG1 . ILE A 1 357 ? -9.428  -16.983 2.625   1.00 25.20  ? 357 ILE A CG1 1 
ATOM   2875 C  CG2 . ILE A 1 357 ? -7.695  -15.181 2.684   1.00 29.97  ? 357 ILE A CG2 1 
ATOM   2876 C  CD1 . ILE A 1 357 ? -10.211 -16.516 3.857   1.00 30.23  ? 357 ILE A CD1 1 
ATOM   2877 N  N   . PRO A 1 358 ? -4.929  -17.929 2.507   1.00 31.18  ? 358 PRO A N   1 
ATOM   2878 C  CA  . PRO A 1 358 ? -3.486  -17.660 2.641   1.00 32.90  ? 358 PRO A CA  1 
ATOM   2879 C  C   . PRO A 1 358 ? -2.764  -17.763 1.308   1.00 31.97  ? 358 PRO A C   1 
ATOM   2880 O  O   . PRO A 1 358 ? -1.765  -17.065 1.074   1.00 33.86  ? 358 PRO A O   1 
ATOM   2881 C  CB  . PRO A 1 358 ? -3.018  -18.741 3.631   1.00 32.65  ? 358 PRO A CB  1 
ATOM   2882 C  CG  . PRO A 1 358 ? -4.296  -19.117 4.418   1.00 31.91  ? 358 PRO A CG  1 
ATOM   2883 C  CD  . PRO A 1 358 ? -5.353  -19.077 3.327   1.00 30.91  ? 358 PRO A CD  1 
ATOM   2884 N  N   . GLN A 1 359 ? -3.250  -18.627 0.420   1.00 35.32  ? 359 GLN A N   1 
ATOM   2885 C  CA  . GLN A 1 359 ? -2.612  -18.780 -0.880  1.00 33.71  ? 359 GLN A CA  1 
ATOM   2886 C  C   . GLN A 1 359 ? -2.993  -17.635 -1.813  1.00 34.56  ? 359 GLN A C   1 
ATOM   2887 O  O   . GLN A 1 359 ? -2.163  -17.173 -2.603  1.00 36.69  ? 359 GLN A O   1 
ATOM   2888 C  CB  . GLN A 1 359 ? -2.996  -20.139 -1.471  1.00 37.50  ? 359 GLN A CB  1 
ATOM   2889 C  CG  . GLN A 1 359 ? -1.991  -20.733 -2.433  1.00 41.91  ? 359 GLN A CG  1 
ATOM   2890 C  CD  . GLN A 1 359 ? -0.656  -21.071 -1.786  1.00 41.57  ? 359 GLN A CD  1 
ATOM   2891 O  OE1 . GLN A 1 359 ? -0.525  -21.138 -0.548  1.00 39.62  ? 359 GLN A OE1 1 
ATOM   2892 N  NE2 . GLN A 1 359 ? 0.352   -21.290 -2.631  1.00 45.14  ? 359 GLN A NE2 1 
ATOM   2893 N  N   . LEU A 1 360 ? -4.249  -17.174 -1.750  1.00 35.60  ? 360 LEU A N   1 
ATOM   2894 C  CA  . LEU A 1 360 ? -4.639  -15.991 -2.510  1.00 31.54  ? 360 LEU A CA  1 
ATOM   2895 C  C   . LEU A 1 360 ? -3.725  -14.822 -2.165  1.00 32.91  ? 360 LEU A C   1 
ATOM   2896 O  O   . LEU A 1 360 ? -3.254  -14.089 -3.041  1.00 33.82  ? 360 LEU A O   1 
ATOM   2897 C  CB  . LEU A 1 360 ? -6.109  -15.626 -2.213  1.00 31.10  ? 360 LEU A CB  1 
ATOM   2898 C  CG  . LEU A 1 360 ? -6.563  -14.190 -2.561  1.00 31.96  ? 360 LEU A CG  1 
ATOM   2899 C  CD1 . LEU A 1 360 ? -6.709  -14.018 -4.063  1.00 32.84  ? 360 LEU A CD1 1 
ATOM   2900 C  CD2 . LEU A 1 360 ? -7.892  -13.804 -1.884  1.00 30.45  ? 360 LEU A CD2 1 
ATOM   2901 N  N   . HIS A 1 361 ? -3.479  -14.623 -0.874  1.00 28.97  ? 361 HIS A N   1 
ATOM   2902 C  CA  . HIS A 1 361 ? -2.712  -13.488 -0.419  1.00 29.36  ? 361 HIS A CA  1 
ATOM   2903 C  C   . HIS A 1 361 ? -1.232  -13.625 -0.732  1.00 30.70  ? 361 HIS A C   1 
ATOM   2904 O  O   . HIS A 1 361 ? -0.474  -12.718 -0.374  1.00 32.09  ? 361 HIS A O   1 
ATOM   2905 C  CB  . HIS A 1 361 ? -2.913  -13.314 1.084   1.00 30.36  ? 361 HIS A CB  1 
ATOM   2906 C  CG  . HIS A 1 361 ? -4.299  -12.870 1.462   1.00 30.47  ? 361 HIS A CG  1 
ATOM   2907 N  ND1 . HIS A 1 361 ? -4.731  -12.830 2.770   1.00 31.36  ? 361 HIS A ND1 1 
ATOM   2908 C  CD2 . HIS A 1 361 ? -5.331  -12.422 0.710   1.00 28.61  ? 361 HIS A CD2 1 
ATOM   2909 C  CE1 . HIS A 1 361 ? -5.974  -12.372 2.811   1.00 28.71  ? 361 HIS A CE1 1 
ATOM   2910 N  NE2 . HIS A 1 361 ? -6.366  -12.120 1.573   1.00 28.91  ? 361 HIS A NE2 1 
ATOM   2911 N  N   . ARG A 1 362 ? -0.813  -14.737 -1.343  1.00 35.37  ? 362 ARG A N   1 
ATOM   2912 C  CA  . ARG A 1 362 ? 0.562   -14.915 -1.795  1.00 34.02  ? 362 ARG A CA  1 
ATOM   2913 C  C   . ARG A 1 362 ? 0.652   -14.915 -3.308  1.00 37.71  ? 362 ARG A C   1 
ATOM   2914 O  O   . ARG A 1 362 ? 1.657   -15.357 -3.865  1.00 33.44  ? 362 ARG A O   1 
ATOM   2915 C  CB  . ARG A 1 362 ? 1.170   -16.203 -1.232  1.00 33.37  ? 362 ARG A CB  1 
ATOM   2916 C  CG  . ARG A 1 362 ? 1.524   -16.119 0.236   1.00 34.87  ? 362 ARG A CG  1 
ATOM   2917 C  CD  . ARG A 1 362 ? 1.626   -17.510 0.881   1.00 38.02  ? 362 ARG A CD  1 
ATOM   2918 N  NE  . ARG A 1 362 ? 2.179   -17.405 2.225   1.00 36.08  ? 362 ARG A NE  1 
ATOM   2919 C  CZ  . ARG A 1 362 ? 1.475   -17.011 3.282   1.00 41.01  ? 362 ARG A CZ  1 
ATOM   2920 N  NH1 . ARG A 1 362 ? 0.180   -16.748 3.191   1.00 35.26  ? 362 ARG A NH1 1 
ATOM   2921 N  NH2 . ARG A 1 362 ? 2.085   -16.868 4.460   1.00 33.59  ? 362 ARG A NH2 1 
ATOM   2922 N  N   . ASP A 1 363 ? -0.392  -14.441 -3.985  1.00 32.51  ? 363 ASP A N   1 
ATOM   2923 C  CA  . ASP A 1 363 ? -0.410  -14.421 -5.443  1.00 37.05  ? 363 ASP A CA  1 
ATOM   2924 C  C   . ASP A 1 363 ? 0.615   -13.402 -5.913  1.00 37.53  ? 363 ASP A C   1 
ATOM   2925 O  O   . ASP A 1 363 ? 0.435   -12.198 -5.710  1.00 37.12  ? 363 ASP A O   1 
ATOM   2926 C  CB  . ASP A 1 363 ? -1.825  -14.095 -5.932  1.00 33.80  ? 363 ASP A CB  1 
ATOM   2927 C  CG  . ASP A 1 363 ? -1.965  -14.142 -7.435  1.00 38.28  ? 363 ASP A CG  1 
ATOM   2928 O  OD1 . ASP A 1 363 ? -0.959  -13.956 -8.173  1.00 33.90  ? 363 ASP A OD1 1 
ATOM   2929 O  OD2 . ASP A 1 363 ? -3.119  -14.338 -7.877  1.00 31.91  ? 363 ASP A OD2 1 
ATOM   2930 N  N   . LYS A 1 364 ? 1.717   -13.882 -6.512  1.00 41.49  ? 364 LYS A N   1 
ATOM   2931 C  CA  . LYS A 1 364 ? 2.797   -12.970 -6.884  1.00 38.90  ? 364 LYS A CA  1 
ATOM   2932 C  C   . LYS A 1 364 ? 2.407   -12.042 -8.018  1.00 35.48  ? 364 LYS A C   1 
ATOM   2933 O  O   . LYS A 1 364 ? 2.973   -10.950 -8.127  1.00 36.19  ? 364 LYS A O   1 
ATOM   2934 C  CB  . LYS A 1 364 ? 4.077   -13.730 -7.268  1.00 40.53  ? 364 LYS A CB  1 
ATOM   2935 C  CG  . LYS A 1 364 ? 4.902   -14.203 -6.077  1.00 50.04  ? 364 LYS A CG  1 
ATOM   2936 C  CD  . LYS A 1 364 ? 6.308   -14.657 -6.509  1.00 58.01  ? 364 LYS A CD  1 
ATOM   2937 C  CE  . LYS A 1 364 ? 6.819   -15.860 -5.717  1.00 61.60  ? 364 LYS A CE  1 
ATOM   2938 N  NZ  . LYS A 1 364 ? 5.983   -17.079 -5.934  1.00 64.78  ? 364 LYS A NZ  1 
ATOM   2939 N  N   . THR A 1 365 ? 1.451   -12.427 -8.857  1.00 37.04  ? 365 THR A N   1 
ATOM   2940 C  CA  . THR A 1 365 ? 1.025   -11.464 -9.864  1.00 38.04  ? 365 THR A CA  1 
ATOM   2941 C  C   . THR A 1 365 ? 0.356   -10.248 -9.248  1.00 41.40  ? 365 THR A C   1 
ATOM   2942 O  O   . THR A 1 365 ? 0.205   -9.235  -9.937  1.00 38.15  ? 365 THR A O   1 
ATOM   2943 C  CB  . THR A 1 365 ? 0.079   -12.103 -10.878 1.00 39.14  ? 365 THR A CB  1 
ATOM   2944 O  OG1 . THR A 1 365 ? -1.186  -12.331 -10.251 1.00 39.84  ? 365 THR A OG1 1 
ATOM   2945 C  CG2 . THR A 1 365 ? 0.633   -13.407 -11.418 1.00 35.79  ? 365 THR A CG2 1 
ATOM   2946 N  N   . ILE A 1 366 ? -0.052  -10.314 -7.986  1.00 37.68  ? 366 ILE A N   1 
ATOM   2947 C  CA  . ILE A 1 366 ? -0.729  -9.205  -7.332  1.00 32.88  ? 366 ILE A CA  1 
ATOM   2948 C  C   . ILE A 1 366 ? 0.230   -8.400  -6.485  1.00 34.71  ? 366 ILE A C   1 
ATOM   2949 O  O   . ILE A 1 366 ? 0.296   -7.175  -6.596  1.00 37.13  ? 366 ILE A O   1 
ATOM   2950 C  CB  . ILE A 1 366 ? -1.905  -9.714  -6.470  1.00 36.05  ? 366 ILE A CB  1 
ATOM   2951 C  CG1 . ILE A 1 366 ? -3.024  -10.278 -7.336  1.00 35.27  ? 366 ILE A CG1 1 
ATOM   2952 C  CG2 . ILE A 1 366 ? -2.414  -8.576  -5.595  1.00 34.88  ? 366 ILE A CG2 1 
ATOM   2953 C  CD1 . ILE A 1 366 ? -3.626  -9.276  -8.307  1.00 37.28  ? 366 ILE A CD1 1 
ATOM   2954 N  N   . TRP A 1 367 ? 0.966   -9.081  -5.604  1.00 35.74  ? 367 TRP A N   1 
ATOM   2955 C  CA  . TRP A 1 367 ? 1.748   -8.426  -4.578  1.00 35.79  ? 367 TRP A CA  1 
ATOM   2956 C  C   . TRP A 1 367 ? 3.208   -8.240  -4.976  1.00 42.20  ? 367 TRP A C   1 
ATOM   2957 O  O   . TRP A 1 367 ? 3.924   -7.508  -4.291  1.00 43.15  ? 367 TRP A O   1 
ATOM   2958 C  CB  . TRP A 1 367 ? 1.644   -9.221  -3.262  1.00 36.70  ? 367 TRP A CB  1 
ATOM   2959 C  CG  . TRP A 1 367 ? 0.204   -9.444  -2.847  1.00 35.99  ? 367 TRP A CG  1 
ATOM   2960 C  CD1 . TRP A 1 367 ? -0.544  -10.573 -3.036  1.00 35.38  ? 367 TRP A CD1 1 
ATOM   2961 C  CD2 . TRP A 1 367 ? -0.659  -8.490  -2.208  1.00 35.75  ? 367 TRP A CD2 1 
ATOM   2962 N  NE1 . TRP A 1 367 ? -1.816  -10.384 -2.548  1.00 33.33  ? 367 TRP A NE1 1 
ATOM   2963 C  CE2 . TRP A 1 367 ? -1.908  -9.113  -2.030  1.00 35.96  ? 367 TRP A CE2 1 
ATOM   2964 C  CE3 . TRP A 1 367 ? -0.494  -7.170  -1.775  1.00 36.15  ? 367 TRP A CE3 1 
ATOM   2965 C  CZ2 . TRP A 1 367 ? -2.992  -8.460  -1.432  1.00 34.55  ? 367 TRP A CZ2 1 
ATOM   2966 C  CZ3 . TRP A 1 367 ? -1.562  -6.523  -1.175  1.00 37.19  ? 367 TRP A CZ3 1 
ATOM   2967 C  CH2 . TRP A 1 367 ? -2.798  -7.171  -1.009  1.00 36.81  ? 367 TRP A CH2 1 
ATOM   2968 N  N   . GLY A 1 368 ? 3.653   -8.842  -6.076  1.00 41.73  ? 368 GLY A N   1 
ATOM   2969 C  CA  . GLY A 1 368 ? 5.036   -8.703  -6.491  1.00 45.69  ? 368 GLY A CA  1 
ATOM   2970 C  C   . GLY A 1 368 ? 5.918   -9.781  -5.898  1.00 50.39  ? 368 GLY A C   1 
ATOM   2971 O  O   . GLY A 1 368 ? 5.458   -10.740 -5.271  1.00 48.12  ? 368 GLY A O   1 
ATOM   2972 N  N   . ASP A 1 369 ? 7.224   -9.621  -6.101  1.00 50.48  ? 369 ASP A N   1 
ATOM   2973 C  CA  . ASP A 1 369 ? 8.117   -10.693 -5.689  1.00 57.86  ? 369 ASP A CA  1 
ATOM   2974 C  C   . ASP A 1 369 ? 8.456   -10.650 -4.205  1.00 50.59  ? 369 ASP A C   1 
ATOM   2975 O  O   . ASP A 1 369 ? 8.922   -11.660 -3.674  1.00 55.80  ? 369 ASP A O   1 
ATOM   2976 C  CB  . ASP A 1 369 ? 9.390   -10.673 -6.531  1.00 58.25  ? 369 ASP A CB  1 
ATOM   2977 C  CG  . ASP A 1 369 ? 9.190   -11.343 -7.875  1.00 66.75  ? 369 ASP A CG  1 
ATOM   2978 O  OD1 . ASP A 1 369 ? 9.069   -12.589 -7.912  1.00 71.27  ? 369 ASP A OD1 1 
ATOM   2979 O  OD2 . ASP A 1 369 ? 9.124   -10.619 -8.890  1.00 71.40  ? 369 ASP A OD2 1 
ATOM   2980 N  N   . ASP A 1 370 ? 8.212   -9.529  -3.525  1.00 54.46  ? 370 ASP A N   1 
ATOM   2981 C  CA  . ASP A 1 370 ? 8.466   -9.440  -2.089  1.00 52.02  ? 370 ASP A CA  1 
ATOM   2982 C  C   . ASP A 1 370 ? 7.252   -9.914  -1.291  1.00 52.79  ? 370 ASP A C   1 
ATOM   2983 O  O   . ASP A 1 370 ? 7.008   -9.444  -0.173  1.00 51.99  ? 370 ASP A O   1 
ATOM   2984 C  CB  . ASP A 1 370 ? 8.873   -8.008  -1.715  1.00 47.63  ? 370 ASP A CB  1 
ATOM   2985 C  CG  . ASP A 1 370 ? 7.706   -7.036  -1.712  1.00 55.06  ? 370 ASP A CG  1 
ATOM   2986 O  OD1 . ASP A 1 370 ? 6.658   -7.333  -2.328  1.00 57.35  ? 370 ASP A OD1 1 
ATOM   2987 O  OD2 . ASP A 1 370 ? 7.844   -5.954  -1.108  1.00 60.11  ? 370 ASP A OD2 1 
ATOM   2988 N  N   . VAL A 1 371 ? 6.520   -10.888 -1.842  1.00 50.34  ? 371 VAL A N   1 
ATOM   2989 C  CA  . VAL A 1 371 ? 5.221   -11.284 -1.288  1.00 47.63  ? 371 VAL A CA  1 
ATOM   2990 C  C   . VAL A 1 371 ? 5.338   -11.858 0.127   1.00 49.09  ? 371 VAL A C   1 
ATOM   2991 O  O   . VAL A 1 371 ? 4.421   -11.694 0.948   1.00 44.82  ? 371 VAL A O   1 
ATOM   2992 C  CB  . VAL A 1 371 ? 4.530   -12.271 -2.249  1.00 48.94  ? 371 VAL A CB  1 
ATOM   2993 C  CG1 . VAL A 1 371 ? 5.283   -13.580 -2.289  1.00 49.24  ? 371 VAL A CG1 1 
ATOM   2994 C  CG2 . VAL A 1 371 ? 3.101   -12.509 -1.799  1.00 48.20  ? 371 VAL A CG2 1 
ATOM   2995 N  N   . GLU A 1 372 ? 6.445   -12.541 0.442   1.00 47.68  ? 372 GLU A N   1 
ATOM   2996 C  CA  . GLU A 1 372 ? 6.623   -13.118 1.774   1.00 44.67  ? 372 GLU A CA  1 
ATOM   2997 C  C   . GLU A 1 372 ? 7.112   -12.098 2.796   1.00 41.24  ? 372 GLU A C   1 
ATOM   2998 O  O   . GLU A 1 372 ? 7.181   -12.419 3.983   1.00 47.25  ? 372 GLU A O   1 
ATOM   2999 C  CB  . GLU A 1 372 ? 7.611   -14.285 1.715   1.00 47.15  ? 372 GLU A CB  1 
ATOM   3000 C  CG  . GLU A 1 372 ? 7.024   -15.591 1.198   1.00 50.37  ? 372 GLU A CG  1 
ATOM   3001 C  CD  . GLU A 1 372 ? 5.970   -16.213 2.112   1.00 48.09  ? 372 GLU A CD  1 
ATOM   3002 O  OE1 . GLU A 1 372 ? 6.028   -16.011 3.345   1.00 50.54  ? 372 GLU A OE1 1 
ATOM   3003 O  OE2 . GLU A 1 372 ? 5.075   -16.920 1.587   1.00 52.25  ? 372 GLU A OE2 1 
ATOM   3004 N  N   . GLU A 1 373 ? 7.438   -10.887 2.362   1.00 39.73  ? 373 GLU A N   1 
ATOM   3005 C  CA  . GLU A 1 373 ? 7.939   -9.826  3.222   1.00 45.80  ? 373 GLU A CA  1 
ATOM   3006 C  C   . GLU A 1 373 ? 6.782   -9.186  3.978   1.00 44.21  ? 373 GLU A C   1 
ATOM   3007 O  O   . GLU A 1 373 ? 5.662   -9.089  3.469   1.00 41.84  ? 373 GLU A O   1 
ATOM   3008 C  CB  . GLU A 1 373 ? 8.632   -8.766  2.370   1.00 48.47  ? 373 GLU A CB  1 
ATOM   3009 C  CG  . GLU A 1 373 ? 10.137  -8.887  2.249   1.00 56.61  ? 373 GLU A CG  1 
ATOM   3010 C  CD  . GLU A 1 373 ? 10.777  -7.571  1.805   1.00 64.25  ? 373 GLU A CD  1 
ATOM   3011 O  OE1 . GLU A 1 373 ? 10.088  -6.520  1.812   1.00 67.55  ? 373 GLU A OE1 1 
ATOM   3012 O  OE2 . GLU A 1 373 ? 11.964  -7.593  1.423   1.00 69.08  ? 373 GLU A OE2 1 
ATOM   3013 N  N   . PHE A 1 374 ? 7.062   -8.733  5.194   1.00 39.07  ? 374 PHE A N   1 
ATOM   3014 C  CA  . PHE A 1 374 ? 6.065   -8.020  5.991   1.00 38.90  ? 374 PHE A CA  1 
ATOM   3015 C  C   . PHE A 1 374 ? 6.238   -6.530  5.736   1.00 40.62  ? 374 PHE A C   1 
ATOM   3016 O  O   . PHE A 1 374 ? 7.128   -5.884  6.297   1.00 38.63  ? 374 PHE A O   1 
ATOM   3017 C  CB  . PHE A 1 374 ? 6.205   -8.350  7.473   1.00 35.27  ? 374 PHE A CB  1 
ATOM   3018 C  CG  . PHE A 1 374 ? 5.035   -7.912  8.294   1.00 34.03  ? 374 PHE A CG  1 
ATOM   3019 C  CD1 . PHE A 1 374 ? 3.867   -8.657  8.311   1.00 35.71  ? 374 PHE A CD1 1 
ATOM   3020 C  CD2 . PHE A 1 374 ? 5.080   -6.732  9.015   1.00 35.85  ? 374 PHE A CD2 1 
ATOM   3021 C  CE1 . PHE A 1 374 ? 2.766   -8.245  9.071   1.00 31.26  ? 374 PHE A CE1 1 
ATOM   3022 C  CE2 . PHE A 1 374 ? 3.990   -6.313  9.776   1.00 35.26  ? 374 PHE A CE2 1 
ATOM   3023 C  CZ  . PHE A 1 374 ? 2.830   -7.084  9.791   1.00 33.08  ? 374 PHE A CZ  1 
ATOM   3024 N  N   . ARG A 1 375 ? 5.371   -5.967  4.902   1.00 36.56  ? 375 ARG A N   1 
ATOM   3025 C  CA  . ARG A 1 375 ? 5.468   -4.565  4.510   1.00 36.96  ? 375 ARG A CA  1 
ATOM   3026 C  C   . ARG A 1 375 ? 4.093   -3.913  4.580   1.00 36.98  ? 375 ARG A C   1 
ATOM   3027 O  O   . ARG A 1 375 ? 3.335   -3.930  3.597   1.00 37.89  ? 375 ARG A O   1 
ATOM   3028 C  CB  . ARG A 1 375 ? 6.081   -4.453  3.112   1.00 40.90  ? 375 ARG A CB  1 
ATOM   3029 C  CG  . ARG A 1 375 ? 6.199   -3.033  2.589   1.00 45.95  ? 375 ARG A CG  1 
ATOM   3030 C  CD  . ARG A 1 375 ? 7.222   -2.947  1.443   1.00 49.89  ? 375 ARG A CD  1 
ATOM   3031 N  NE  . ARG A 1 375 ? 6.704   -3.543  0.218   1.00 53.20  ? 375 ARG A NE  1 
ATOM   3032 C  CZ  . ARG A 1 375 ? 5.872   -2.947  -0.624  1.00 54.68  ? 375 ARG A CZ  1 
ATOM   3033 N  NH1 . ARG A 1 375 ? 5.372   -1.745  -0.370  1.00 50.42  ? 375 ARG A NH1 1 
ATOM   3034 N  NH2 . ARG A 1 375 ? 5.517   -3.582  -1.741  1.00 51.79  ? 375 ARG A NH2 1 
ATOM   3035 N  N   . PRO A 1 376 ? 3.731   -3.334  5.729   1.00 37.43  ? 376 PRO A N   1 
ATOM   3036 C  CA  . PRO A 1 376 ? 2.390   -2.738  5.858   1.00 37.97  ? 376 PRO A CA  1 
ATOM   3037 C  C   . PRO A 1 376 ? 2.100   -1.662  4.826   1.00 38.06  ? 376 PRO A C   1 
ATOM   3038 O  O   . PRO A 1 376 ? 0.923   -1.411  4.521   1.00 37.62  ? 376 PRO A O   1 
ATOM   3039 C  CB  . PRO A 1 376 ? 2.402   -2.157  7.284   1.00 39.10  ? 376 PRO A CB  1 
ATOM   3040 C  CG  . PRO A 1 376 ? 3.409   -3.028  8.032   1.00 38.12  ? 376 PRO A CG  1 
ATOM   3041 C  CD  . PRO A 1 376 ? 4.486   -3.269  6.997   1.00 37.14  ? 376 PRO A CD  1 
ATOM   3042 N  N   . GLU A 1 377 ? 3.135   -1.008  4.284   1.00 36.18  ? 377 GLU A N   1 
ATOM   3043 C  CA  . GLU A 1 377 ? 2.953   0.049   3.295   1.00 40.02  ? 377 GLU A CA  1 
ATOM   3044 C  C   . GLU A 1 377 ? 2.275   -0.440  2.006   1.00 35.74  ? 377 GLU A C   1 
ATOM   3045 O  O   . GLU A 1 377 ? 1.822   0.392   1.218   1.00 36.50  ? 377 GLU A O   1 
ATOM   3046 C  CB  . GLU A 1 377 ? 4.318   0.694   2.991   1.00 39.19  ? 377 GLU A CB  1 
ATOM   3047 C  CG  . GLU A 1 377 ? 4.945   1.443   4.194   1.00 40.32  ? 377 GLU A CG  1 
ATOM   3048 C  CD  . GLU A 1 377 ? 5.640   0.511   5.214   1.00 43.04  ? 377 GLU A CD  1 
ATOM   3049 O  OE1 . GLU A 1 377 ? 5.760   -0.702  4.939   1.00 40.80  ? 377 GLU A OE1 1 
ATOM   3050 O  OE2 . GLU A 1 377 ? 6.074   1.005   6.282   1.00 41.81  ? 377 GLU A OE2 1 
ATOM   3051 N  N   . ARG A 1 378 ? 2.197   -1.752  1.774   1.00 34.38  ? 378 ARG A N   1 
ATOM   3052 C  CA  . ARG A 1 378 ? 1.345   -2.298  0.712   1.00 36.28  ? 378 ARG A CA  1 
ATOM   3053 C  C   . ARG A 1 378 ? -0.058  -1.727  0.750   1.00 35.14  ? 378 ARG A C   1 
ATOM   3054 O  O   . ARG A 1 378 ? -0.732  -1.663  -0.284  1.00 36.74  ? 378 ARG A O   1 
ATOM   3055 C  CB  . ARG A 1 378 ? 1.227   -3.817  0.855   1.00 39.73  ? 378 ARG A CB  1 
ATOM   3056 C  CG  . ARG A 1 378 ? 2.440   -4.571  0.540   1.00 43.97  ? 378 ARG A CG  1 
ATOM   3057 C  CD  . ARG A 1 378 ? 2.168   -6.044  0.658   1.00 37.30  ? 378 ARG A CD  1 
ATOM   3058 N  NE  . ARG A 1 378 ? 3.352   -6.717  1.158   1.00 39.64  ? 378 ARG A NE  1 
ATOM   3059 C  CZ  . ARG A 1 378 ? 4.302   -7.181  0.357   1.00 47.43  ? 378 ARG A CZ  1 
ATOM   3060 N  NH1 . ARG A 1 378 ? 4.218   -7.046  -0.962  1.00 47.73  ? 378 ARG A NH1 1 
ATOM   3061 N  NH2 . ARG A 1 378 ? 5.361   -7.783  0.887   1.00 47.92  ? 378 ARG A NH2 1 
ATOM   3062 N  N   . PHE A 1 379 ? -0.532  -1.355  1.931   1.00 32.23  ? 379 PHE A N   1 
ATOM   3063 C  CA  . PHE A 1 379 ? -1.929  -0.981  2.121   1.00 36.64  ? 379 PHE A CA  1 
ATOM   3064 C  C   . PHE A 1 379 ? -2.141  0.524   2.138   1.00 37.40  ? 379 PHE A C   1 
ATOM   3065 O  O   . PHE A 1 379 ? -3.247  0.981   2.435   1.00 36.84  ? 379 PHE A O   1 
ATOM   3066 C  CB  . PHE A 1 379 ? -2.472  -1.639  3.398   1.00 38.45  ? 379 PHE A CB  1 
ATOM   3067 C  CG  . PHE A 1 379 ? -2.658  -3.115  3.240   1.00 34.37  ? 379 PHE A CG  1 
ATOM   3068 C  CD1 . PHE A 1 379 ? -3.817  -3.617  2.658   1.00 34.15  ? 379 PHE A CD1 1 
ATOM   3069 C  CD2 . PHE A 1 379 ? -1.635  -4.001  3.566   1.00 36.76  ? 379 PHE A CD2 1 
ATOM   3070 C  CE1 . PHE A 1 379 ? -3.976  -4.988  2.451   1.00 37.01  ? 379 PHE A CE1 1 
ATOM   3071 C  CE2 . PHE A 1 379 ? -1.785  -5.366  3.373   1.00 33.34  ? 379 PHE A CE2 1 
ATOM   3072 C  CZ  . PHE A 1 379 ? -2.955  -5.866  2.815   1.00 37.64  ? 379 PHE A CZ  1 
ATOM   3073 N  N   . GLU A 1 380 ? -1.123  1.295   1.760   1.00 36.30  ? 380 GLU A N   1 
ATOM   3074 C  CA  . GLU A 1 380 ? -1.246  2.746   1.737   1.00 39.71  ? 380 GLU A CA  1 
ATOM   3075 C  C   . GLU A 1 380 ? -2.408  3.190   0.858   1.00 38.02  ? 380 GLU A C   1 
ATOM   3076 O  O   . GLU A 1 380 ? -3.107  4.153   1.187   1.00 39.32  ? 380 GLU A O   1 
ATOM   3077 C  CB  . GLU A 1 380 ? 0.063   3.355   1.234   1.00 37.72  ? 380 GLU A CB  1 
ATOM   3078 C  CG  . GLU A 1 380 ? 1.252   2.839   2.050   1.00 49.41  ? 380 GLU A CG  1 
ATOM   3079 C  CD  . GLU A 1 380 ? 2.319   3.868   2.379   1.00 56.34  ? 380 GLU A CD  1 
ATOM   3080 O  OE1 . GLU A 1 380 ? 2.105   4.692   3.290   1.00 56.35  ? 380 GLU A OE1 1 
ATOM   3081 O  OE2 . GLU A 1 380 ? 3.385   3.834   1.726   1.00 64.64  ? 380 GLU A OE2 1 
ATOM   3082 N  N   . ASN A 1 381 ? -2.624  2.518   -0.271  1.00 34.68  ? 381 ASN A N   1 
ATOM   3083 C  CA  . ASN A 1 381 ? -3.612  2.958   -1.260  1.00 37.76  ? 381 ASN A CA  1 
ATOM   3084 C  C   . ASN A 1 381 ? -4.488  1.796   -1.718  1.00 35.26  ? 381 ASN A C   1 
ATOM   3085 O  O   . ASN A 1 381 ? -4.104  1.045   -2.635  1.00 32.03  ? 381 ASN A O   1 
ATOM   3086 C  CB  . ASN A 1 381 ? -2.924  3.605   -2.458  1.00 33.62  ? 381 ASN A CB  1 
ATOM   3087 C  CG  . ASN A 1 381 ? -3.916  4.200   -3.446  1.00 37.55  ? 381 ASN A CG  1 
ATOM   3088 O  OD1 . ASN A 1 381 ? -5.128  4.217   -3.196  1.00 38.13  ? 381 ASN A OD1 1 
ATOM   3089 N  ND2 . ASN A 1 381 ? -3.407  4.707   -4.559  1.00 34.81  ? 381 ASN A ND2 1 
ATOM   3090 N  N   . PRO A 1 382 ? -5.662  1.607   -1.106  1.00 33.21  ? 382 PRO A N   1 
ATOM   3091 C  CA  . PRO A 1 382 ? -6.520  0.486   -1.515  1.00 35.70  ? 382 PRO A CA  1 
ATOM   3092 C  C   . PRO A 1 382 ? -6.918  0.551   -2.976  1.00 31.89  ? 382 PRO A C   1 
ATOM   3093 O  O   . PRO A 1 382 ? -7.248  -0.489  -3.562  1.00 32.09  ? 382 PRO A O   1 
ATOM   3094 C  CB  . PRO A 1 382 ? -7.742  0.624   -0.594  1.00 35.72  ? 382 PRO A CB  1 
ATOM   3095 C  CG  . PRO A 1 382 ? -7.175  1.319   0.649   1.00 35.39  ? 382 PRO A CG  1 
ATOM   3096 C  CD  . PRO A 1 382 ? -6.220  2.333   0.052   1.00 33.09  ? 382 PRO A CD  1 
ATOM   3097 N  N   . SER A 1 383 ? -6.917  1.739   -3.583  1.00 34.26  ? 383 SER A N   1 
ATOM   3098 C  CA  . SER A 1 383 ? -7.233  1.825   -5.000  1.00 33.35  ? 383 SER A CA  1 
ATOM   3099 C  C   . SER A 1 383 ? -6.150  1.189   -5.861  1.00 31.83  ? 383 SER A C   1 
ATOM   3100 O  O   . SER A 1 383 ? -6.407  0.894   -7.023  1.00 34.79  ? 383 SER A O   1 
ATOM   3101 C  CB  . SER A 1 383 ? -7.446  3.290   -5.416  1.00 35.03  ? 383 SER A CB  1 
ATOM   3102 O  OG  . SER A 1 383 ? -8.531  3.878   -4.692  1.00 33.70  ? 383 SER A OG  1 
ATOM   3103 N  N   . ALA A 1 384 ? -4.944  0.993   -5.333  1.00 32.95  ? 384 ALA A N   1 
ATOM   3104 C  CA  . ALA A 1 384 ? -3.880  0.367   -6.106  1.00 34.37  ? 384 ALA A CA  1 
ATOM   3105 C  C   . ALA A 1 384 ? -3.873  -1.147  -5.944  1.00 38.19  ? 384 ALA A C   1 
ATOM   3106 O  O   . ALA A 1 384 ? -3.025  -1.824  -6.538  1.00 35.50  ? 384 ALA A O   1 
ATOM   3107 C  CB  . ALA A 1 384 ? -2.507  0.957   -5.715  1.00 35.64  ? 384 ALA A CB  1 
ATOM   3108 N  N   . ILE A 1 385 ? -4.810  -1.685  -5.173  1.00 34.09  ? 385 ILE A N   1 
ATOM   3109 C  CA  . ILE A 1 385 ? -4.934  -3.119  -4.938  1.00 32.46  ? 385 ILE A CA  1 
ATOM   3110 C  C   . ILE A 1 385 ? -6.060  -3.636  -5.828  1.00 33.76  ? 385 ILE A C   1 
ATOM   3111 O  O   . ILE A 1 385 ? -7.188  -3.141  -5.719  1.00 34.85  ? 385 ILE A O   1 
ATOM   3112 C  CB  . ILE A 1 385 ? -5.222  -3.421  -3.457  1.00 31.49  ? 385 ILE A CB  1 
ATOM   3113 C  CG1 . ILE A 1 385 ? -4.086  -2.857  -2.579  1.00 36.36  ? 385 ILE A CG1 1 
ATOM   3114 C  CG2 . ILE A 1 385 ? -5.385  -4.921  -3.265  1.00 31.43  ? 385 ILE A CG2 1 
ATOM   3115 C  CD1 . ILE A 1 385 ? -4.220  -3.133  -1.087  1.00 32.86  ? 385 ILE A CD1 1 
ATOM   3116 N  N   . PRO A 1 386 ? -5.806  -4.614  -6.704  1.00 33.64  ? 386 PRO A N   1 
ATOM   3117 C  CA  . PRO A 1 386 ? -6.857  -5.122  -7.597  1.00 35.52  ? 386 PRO A CA  1 
ATOM   3118 C  C   . PRO A 1 386 ? -8.047  -5.690  -6.827  1.00 33.50  ? 386 PRO A C   1 
ATOM   3119 O  O   . PRO A 1 386 ? -7.950  -6.049  -5.655  1.00 33.27  ? 386 PRO A O   1 
ATOM   3120 C  CB  . PRO A 1 386 ? -6.138  -6.218  -8.394  1.00 34.70  ? 386 PRO A CB  1 
ATOM   3121 C  CG  . PRO A 1 386 ? -4.670  -5.836  -8.312  1.00 32.15  ? 386 PRO A CG  1 
ATOM   3122 C  CD  . PRO A 1 386 ? -4.508  -5.272  -6.938  1.00 35.84  ? 386 PRO A CD  1 
ATOM   3123 N  N   . GLN A 1 387 ? -9.192  -5.785  -7.511  1.00 33.36  ? 387 GLN A N   1 
ATOM   3124 C  CA  . GLN A 1 387 ? -10.395 -6.279  -6.848  1.00 32.79  ? 387 GLN A CA  1 
ATOM   3125 C  C   . GLN A 1 387 ? -10.211 -7.702  -6.337  1.00 33.68  ? 387 GLN A C   1 
ATOM   3126 O  O   . GLN A 1 387 ? -9.667  -8.570  -7.033  1.00 35.17  ? 387 GLN A O   1 
ATOM   3127 C  CB  . GLN A 1 387 ? -11.593 -6.252  -7.802  1.00 33.63  ? 387 GLN A CB  1 
ATOM   3128 C  CG  . GLN A 1 387 ? -12.002 -4.855  -8.226  1.00 32.82  ? 387 GLN A CG  1 
ATOM   3129 C  CD  . GLN A 1 387 ? -13.415 -4.838  -8.744  1.00 34.99  ? 387 GLN A CD  1 
ATOM   3130 O  OE1 . GLN A 1 387 ? -14.388 -4.844  -7.971  1.00 32.03  ? 387 GLN A OE1 1 
ATOM   3131 N  NE2 . GLN A 1 387 ? -13.542 -4.889  -10.063 1.00 30.18  ? 387 GLN A NE2 1 
ATOM   3132 N  N   . HIS A 1 388 ? -10.699 -7.937  -5.115  1.00 32.15  ? 388 HIS A N   1 
ATOM   3133 C  CA  . HIS A 1 388 ? -10.790 -9.255  -4.499  1.00 31.26  ? 388 HIS A CA  1 
ATOM   3134 C  C   . HIS A 1 388 ? -9.435  -9.926  -4.302  1.00 31.31  ? 388 HIS A C   1 
ATOM   3135 O  O   . HIS A 1 388 ? -9.370  -11.143 -4.169  1.00 34.31  ? 388 HIS A O   1 
ATOM   3136 C  CB  . HIS A 1 388 ? -11.728 -10.156 -5.307  1.00 33.85  ? 388 HIS A CB  1 
ATOM   3137 C  CG  . HIS A 1 388 ? -13.065 -9.528  -5.526  1.00 36.66  ? 388 HIS A CG  1 
ATOM   3138 N  ND1 . HIS A 1 388 ? -13.877 -9.173  -4.473  1.00 33.52  ? 388 HIS A ND1 1 
ATOM   3139 C  CD2 . HIS A 1 388 ? -13.707 -9.132  -6.651  1.00 37.67  ? 388 HIS A CD2 1 
ATOM   3140 C  CE1 . HIS A 1 388 ? -14.977 -8.607  -4.940  1.00 40.13  ? 388 HIS A CE1 1 
ATOM   3141 N  NE2 . HIS A 1 388 ? -14.903 -8.576  -6.260  1.00 34.85  ? 388 HIS A NE2 1 
ATOM   3142 N  N   . ALA A 1 389 ? -8.351  -9.142  -4.251  1.00 32.05  ? 389 ALA A N   1 
ATOM   3143 C  CA  . ALA A 1 389 ? -7.039  -9.687  -3.926  1.00 33.17  ? 389 ALA A CA  1 
ATOM   3144 C  C   . ALA A 1 389 ? -6.850  -9.943  -2.431  1.00 33.11  ? 389 ALA A C   1 
ATOM   3145 O  O   . ALA A 1 389 ? -5.948  -10.704 -2.051  1.00 31.65  ? 389 ALA A O   1 
ATOM   3146 C  CB  . ALA A 1 389 ? -5.954  -8.727  -4.406  1.00 32.17  ? 389 ALA A CB  1 
ATOM   3147 N  N   . PHE A 1 390 ? -7.680  -9.342  -1.583  1.00 27.53  ? 390 PHE A N   1 
ATOM   3148 C  CA  . PHE A 1 390 ? -7.472  -9.316  -0.131  1.00 30.41  ? 390 PHE A CA  1 
ATOM   3149 C  C   . PHE A 1 390 ? -8.814  -9.634  0.510   1.00 33.65  ? 390 PHE A C   1 
ATOM   3150 O  O   . PHE A 1 390 ? -9.726  -8.799  0.471   1.00 31.00  ? 390 PHE A O   1 
ATOM   3151 C  CB  . PHE A 1 390 ? -6.967  -7.935  0.295   1.00 32.04  ? 390 PHE A CB  1 
ATOM   3152 C  CG  . PHE A 1 390 ? -6.658  -7.784  1.776   1.00 33.19  ? 390 PHE A CG  1 
ATOM   3153 C  CD1 . PHE A 1 390 ? -5.665  -8.549  2.397   1.00 30.35  ? 390 PHE A CD1 1 
ATOM   3154 C  CD2 . PHE A 1 390 ? -7.351  -6.853  2.540   1.00 29.61  ? 390 PHE A CD2 1 
ATOM   3155 C  CE1 . PHE A 1 390 ? -5.375  -8.384  3.756   1.00 34.03  ? 390 PHE A CE1 1 
ATOM   3156 C  CE2 . PHE A 1 390 ? -7.063  -6.683  3.898   1.00 32.87  ? 390 PHE A CE2 1 
ATOM   3157 C  CZ  . PHE A 1 390 ? -6.074  -7.440  4.503   1.00 31.44  ? 390 PHE A CZ  1 
ATOM   3158 N  N   . LYS A 1 391 ? -8.960  -10.848 1.046   1.00 30.01  ? 391 LYS A N   1 
ATOM   3159 C  CA  . LYS A 1 391 ? -10.285 -11.319 1.468   1.00 31.19  ? 391 LYS A CA  1 
ATOM   3160 C  C   . LYS A 1 391 ? -10.275 -11.933 2.868   1.00 29.64  ? 391 LYS A C   1 
ATOM   3161 O  O   . LYS A 1 391 ? -10.922 -12.972 3.088   1.00 30.11  ? 391 LYS A O   1 
ATOM   3162 C  CB  . LYS A 1 391 ? -10.834 -12.378 0.500   1.00 26.90  ? 391 LYS A CB  1 
ATOM   3163 C  CG  . LYS A 1 391 ? -10.870 -11.988 -0.991  1.00 32.14  ? 391 LYS A CG  1 
ATOM   3164 C  CD  . LYS A 1 391 ? -11.703 -10.730 -1.228  1.00 33.52  ? 391 LYS A CD  1 
ATOM   3165 C  CE  . LYS A 1 391 ? -13.174 -10.990 -0.985  1.00 34.34  ? 391 LYS A CE  1 
ATOM   3166 N  NZ  . LYS A 1 391 ? -14.044 -9.897  -1.576  1.00 37.07  ? 391 LYS A NZ  1 
ATOM   3167 N  N   . PRO A 1 392 ? -9.588  -11.335 3.839   1.00 26.87  ? 392 PRO A N   1 
ATOM   3168 C  CA  . PRO A 1 392 ? -9.547  -11.955 5.169   1.00 27.77  ? 392 PRO A CA  1 
ATOM   3169 C  C   . PRO A 1 392 ? -10.879 -11.933 5.906   1.00 32.10  ? 392 PRO A C   1 
ATOM   3170 O  O   . PRO A 1 392 ? -11.017 -12.655 6.901   1.00 32.01  ? 392 PRO A O   1 
ATOM   3171 C  CB  . PRO A 1 392 ? -8.490  -11.126 5.904   1.00 30.35  ? 392 PRO A CB  1 
ATOM   3172 C  CG  . PRO A 1 392 ? -8.639  -9.765  5.298   1.00 29.58  ? 392 PRO A CG  1 
ATOM   3173 C  CD  . PRO A 1 392 ? -8.871  -10.048 3.815   1.00 27.15  ? 392 PRO A CD  1 
ATOM   3174 N  N   . HIS A 1 393 ? -11.846 -11.122 5.477   1.00 28.30  ? 393 HIS A N   1 
ATOM   3175 C  CA  . HIS A 1 393 ? -13.158 -11.068 6.129   1.00 29.16  ? 393 HIS A CA  1 
ATOM   3176 C  C   . HIS A 1 393 ? -14.267 -11.644 5.253   1.00 30.95  ? 393 HIS A C   1 
ATOM   3177 O  O   . HIS A 1 393 ? -15.460 -11.392 5.503   1.00 31.36  ? 393 HIS A O   1 
ATOM   3178 C  CB  . HIS A 1 393 ? -13.469 -9.633  6.545   1.00 31.34  ? 393 HIS A CB  1 
ATOM   3179 C  CG  . HIS A 1 393 ? -12.503 -9.087  7.551   1.00 33.11  ? 393 HIS A CG  1 
ATOM   3180 N  ND1 . HIS A 1 393 ? -12.511 -9.474  8.875   1.00 42.22  ? 393 HIS A ND1 1 
ATOM   3181 C  CD2 . HIS A 1 393 ? -11.501 -8.183  7.429   1.00 36.62  ? 393 HIS A CD2 1 
ATOM   3182 C  CE1 . HIS A 1 393 ? -11.551 -8.834  9.524   1.00 39.93  ? 393 HIS A CE1 1 
ATOM   3183 N  NE2 . HIS A 1 393 ? -10.931 -8.037  8.670   1.00 38.71  ? 393 HIS A NE2 1 
ATOM   3184 N  N   . GLY A 1 394 ? -13.902 -12.454 4.256   1.00 31.07  ? 394 GLY A N   1 
ATOM   3185 C  CA  . GLY A 1 394 ? -14.908 -13.035 3.382   1.00 27.62  ? 394 GLY A CA  1 
ATOM   3186 C  C   . GLY A 1 394 ? -15.352 -12.045 2.317   1.00 32.53  ? 394 GLY A C   1 
ATOM   3187 O  O   . GLY A 1 394 ? -14.617 -11.117 1.965   1.00 31.07  ? 394 GLY A O   1 
ATOM   3188 N  N   . ASN A 1 395 ? -16.587 -12.238 1.814   1.00 29.32  ? 395 ASN A N   1 
ATOM   3189 C  CA  . ASN A 1 395 ? -17.033 -11.570 0.597   1.00 29.82  ? 395 ASN A CA  1 
ATOM   3190 C  C   . ASN A 1 395 ? -18.485 -11.115 0.666   1.00 31.67  ? 395 ASN A C   1 
ATOM   3191 O  O   . ASN A 1 395 ? -19.362 -11.859 1.131   1.00 29.80  ? 395 ASN A O   1 
ATOM   3192 C  CB  . ASN A 1 395 ? -16.894 -12.490 -0.613  1.00 29.37  ? 395 ASN A CB  1 
ATOM   3193 C  CG  . ASN A 1 395 ? -17.245 -11.769 -1.898  1.00 30.41  ? 395 ASN A CG  1 
ATOM   3194 O  OD1 . ASN A 1 395 ? -16.575 -10.799 -2.262  1.00 32.13  ? 395 ASN A OD1 1 
ATOM   3195 N  ND2 . ASN A 1 395 ? -18.321 -12.198 -2.554  1.00 31.79  ? 395 ASN A ND2 1 
ATOM   3196 N  N   . GLY A 1 396 ? -18.727 -9.888  0.194   1.00 33.06  ? 396 GLY A N   1 
ATOM   3197 C  CA  . GLY A 1 396 ? -20.083 -9.474  -0.139  1.00 34.90  ? 396 GLY A CA  1 
ATOM   3198 C  C   . GLY A 1 396 ? -20.986 -9.450  1.081   1.00 31.12  ? 396 GLY A C   1 
ATOM   3199 O  O   . GLY A 1 396 ? -20.549 -9.165  2.196   1.00 29.31  ? 396 GLY A O   1 
ATOM   3200 N  N   . GLN A 1 397 ? -22.277 -9.764  0.867   1.00 29.63  ? 397 GLN A N   1 
ATOM   3201 C  CA  . GLN A 1 397 ? -23.238 -9.684  1.969   1.00 33.09  ? 397 GLN A CA  1 
ATOM   3202 C  C   . GLN A 1 397 ? -22.959 -10.706 3.060   1.00 32.29  ? 397 GLN A C   1 
ATOM   3203 O  O   . GLN A 1 397 ? -23.459 -10.554 4.178   1.00 30.97  ? 397 GLN A O   1 
ATOM   3204 C  CB  . GLN A 1 397 ? -24.677 -9.855  1.449   1.00 33.62  ? 397 GLN A CB  1 
ATOM   3205 C  CG  . GLN A 1 397 ? -25.095 -11.283 1.029   1.00 32.79  ? 397 GLN A CG  1 
ATOM   3206 C  CD  . GLN A 1 397 ? -26.496 -11.294 0.413   1.00 35.38  ? 397 GLN A CD  1 
ATOM   3207 O  OE1 . GLN A 1 397 ? -27.321 -10.433 0.732   1.00 36.01  ? 397 GLN A OE1 1 
ATOM   3208 N  NE2 . GLN A 1 397 ? -26.774 -12.270 -0.442  1.00 34.07  ? 397 GLN A NE2 1 
ATOM   3209 N  N   . ARG A 1 398 ? -22.195 -11.749 2.756   1.00 29.58  ? 398 ARG A N   1 
ATOM   3210 C  CA  . ARG A 1 398 ? -21.825 -12.749 3.748   1.00 29.58  ? 398 ARG A CA  1 
ATOM   3211 C  C   . ARG A 1 398 ? -20.430 -12.491 4.301   1.00 32.59  ? 398 ARG A C   1 
ATOM   3212 O  O   . ARG A 1 398 ? -19.805 -13.408 4.842   1.00 31.25  ? 398 ARG A O   1 
ATOM   3213 C  CB  . ARG A 1 398 ? -21.915 -14.161 3.157   1.00 28.17  ? 398 ARG A CB  1 
ATOM   3214 C  CG  . ARG A 1 398 ? -23.307 -14.566 2.651   1.00 29.38  ? 398 ARG A CG  1 
ATOM   3215 C  CD  . ARG A 1 398 ? -24.368 -14.332 3.718   1.00 29.78  ? 398 ARG A CD  1 
ATOM   3216 N  NE  . ARG A 1 398 ? -24.088 -15.053 4.958   1.00 29.41  ? 398 ARG A NE  1 
ATOM   3217 C  CZ  . ARG A 1 398 ? -24.469 -16.303 5.202   1.00 32.70  ? 398 ARG A CZ  1 
ATOM   3218 N  NH1 . ARG A 1 398 ? -25.096 -17.028 4.290   1.00 31.16  ? 398 ARG A NH1 1 
ATOM   3219 N  NH2 . ARG A 1 398 ? -24.215 -16.839 6.391   1.00 31.97  ? 398 ARG A NH2 1 
ATOM   3220 N  N   . ALA A 1 399 ? -19.918 -11.271 4.141   1.00 30.31  ? 399 ALA A N   1 
ATOM   3221 C  CA  . ALA A 1 399 ? -18.645 -10.919 4.750   1.00 30.33  ? 399 ALA A CA  1 
ATOM   3222 C  C   . ALA A 1 399 ? -18.794 -10.836 6.272   1.00 34.60  ? 399 ALA A C   1 
ATOM   3223 O  O   . ALA A 1 399 ? -19.900 -10.820 6.830   1.00 31.42  ? 399 ALA A O   1 
ATOM   3224 C  CB  . ALA A 1 399 ? -18.130 -9.589  4.185   1.00 31.57  ? 399 ALA A CB  1 
ATOM   3225 N  N   . CYS A 1 400 ? -17.653 -10.773 6.951   1.00 29.33  ? 400 CYS A N   1 
ATOM   3226 C  CA  . CYS A 1 400 ? -17.613 -10.750 8.410   1.00 28.77  ? 400 CYS A CA  1 
ATOM   3227 C  C   . CYS A 1 400 ? -18.373 -9.564  8.995   1.00 33.63  ? 400 CYS A C   1 
ATOM   3228 O  O   . CYS A 1 400 ? -17.922 -8.419  8.892   1.00 31.00  ? 400 CYS A O   1 
ATOM   3229 C  CB  . CYS A 1 400 ? -16.158 -10.696 8.888   1.00 27.82  ? 400 CYS A CB  1 
ATOM   3230 S  SG  . CYS A 1 400 ? -16.051 -10.611 10.688  1.00 32.34  ? 400 CYS A SG  1 
ATOM   3231 N  N   . ILE A 1 401 ? -19.519 -9.805  9.637   1.00 33.61  ? 401 ILE A N   1 
ATOM   3232 C  CA  . ILE A 1 401 ? -20.239 -8.677  10.213  1.00 31.54  ? 401 ILE A CA  1 
ATOM   3233 C  C   . ILE A 1 401 ? -19.450 -8.012  11.336  1.00 33.82  ? 401 ILE A C   1 
ATOM   3234 O  O   . ILE A 1 401 ? -19.686 -6.841  11.636  1.00 35.15  ? 401 ILE A O   1 
ATOM   3235 C  CB  . ILE A 1 401 ? -21.632 -9.097  10.717  1.00 31.74  ? 401 ILE A CB  1 
ATOM   3236 C  CG1 . ILE A 1 401 ? -22.478 -7.837  11.024  1.00 35.28  ? 401 ILE A CG1 1 
ATOM   3237 C  CG2 . ILE A 1 401 ? -21.509 -9.968  11.934  1.00 31.46  ? 401 ILE A CG2 1 
ATOM   3238 C  CD1 . ILE A 1 401 ? -23.958 -8.125  11.403  1.00 34.29  ? 401 ILE A CD1 1 
ATOM   3239 N  N   . GLY A 1 402 ? -18.507 -8.727  11.951  1.00 32.66  ? 402 GLY A N   1 
ATOM   3240 C  CA  . GLY A 1 402 ? -17.726 -8.196  13.053  1.00 32.21  ? 402 GLY A CA  1 
ATOM   3241 C  C   . GLY A 1 402 ? -16.425 -7.532  12.641  1.00 33.92  ? 402 GLY A C   1 
ATOM   3242 O  O   . GLY A 1 402 ? -15.536 -7.341  13.470  1.00 31.96  ? 402 GLY A O   1 
ATOM   3243 N  N   . GLN A 1 403 ? -16.307 -7.135  11.376  1.00 32.45  ? 403 GLN A N   1 
ATOM   3244 C  CA  . GLN A 1 403 ? -15.012 -6.664  10.878  1.00 33.85  ? 403 GLN A CA  1 
ATOM   3245 C  C   . GLN A 1 403 ? -14.570 -5.374  11.566  1.00 37.47  ? 403 GLN A C   1 
ATOM   3246 O  O   . GLN A 1 403 ? -13.394 -5.230  11.915  1.00 34.52  ? 403 GLN A O   1 
ATOM   3247 C  CB  . GLN A 1 403 ? -15.063 -6.463  9.357   1.00 37.90  ? 403 GLN A CB  1 
ATOM   3248 C  CG  . GLN A 1 403 ? -13.923 -5.591  8.805   1.00 37.86  ? 403 GLN A CG  1 
ATOM   3249 C  CD  . GLN A 1 403 ? -13.929 -5.506  7.281   1.00 45.92  ? 403 GLN A CD  1 
ATOM   3250 O  OE1 . GLN A 1 403 ? -14.659 -6.228  6.606   1.00 46.19  ? 403 GLN A OE1 1 
ATOM   3251 N  NE2 . GLN A 1 403 ? -13.110 -4.618  6.739   1.00 44.37  ? 403 GLN A NE2 1 
ATOM   3252 N  N   . GLN A 1 404 ? -15.483 -4.414  11.750  1.00 33.42  ? 404 GLN A N   1 
ATOM   3253 C  CA  . GLN A 1 404 ? -15.107 -3.168  12.428  1.00 35.43  ? 404 GLN A CA  1 
ATOM   3254 C  C   . GLN A 1 404 ? -14.804 -3.410  13.898  1.00 32.37  ? 404 GLN A C   1 
ATOM   3255 O  O   . GLN A 1 404 ? -13.866 -2.817  14.451  1.00 36.04  ? 404 GLN A O   1 
ATOM   3256 C  CB  . GLN A 1 404 ? -16.215 -2.117  12.302  1.00 38.84  ? 404 GLN A CB  1 
ATOM   3257 C  CG  . GLN A 1 404 ? -16.770 -1.967  10.910  1.00 47.24  ? 404 GLN A CG  1 
ATOM   3258 C  CD  . GLN A 1 404 ? -15.701 -1.546  9.943   1.00 47.95  ? 404 GLN A CD  1 
ATOM   3259 O  OE1 . GLN A 1 404 ? -15.095 -0.485  10.104  1.00 56.66  ? 404 GLN A OE1 1 
ATOM   3260 N  NE2 . GLN A 1 404 ? -15.455 -2.374  8.927   1.00 54.67  ? 404 GLN A NE2 1 
ATOM   3261 N  N   . PHE A 1 405 ? -15.607 -4.255  14.546  1.00 32.33  ? 405 PHE A N   1 
ATOM   3262 C  CA  . PHE A 1 405 ? -15.363 -4.623  15.938  1.00 34.51  ? 405 PHE A CA  1 
ATOM   3263 C  C   . PHE A 1 405 ? -13.950 -5.164  16.117  1.00 33.34  ? 405 PHE A C   1 
ATOM   3264 O  O   . PHE A 1 405 ? -13.207 -4.729  17.006  1.00 35.61  ? 405 PHE A O   1 
ATOM   3265 C  CB  . PHE A 1 405 ? -16.399 -5.673  16.368  1.00 31.77  ? 405 PHE A CB  1 
ATOM   3266 C  CG  . PHE A 1 405 ? -16.429 -5.962  17.851  1.00 35.11  ? 405 PHE A CG  1 
ATOM   3267 C  CD1 . PHE A 1 405 ? -15.494 -6.825  18.432  1.00 35.37  ? 405 PHE A CD1 1 
ATOM   3268 C  CD2 . PHE A 1 405 ? -17.435 -5.428  18.648  1.00 31.40  ? 405 PHE A CD2 1 
ATOM   3269 C  CE1 . PHE A 1 405 ? -15.546 -7.135  19.810  1.00 34.53  ? 405 PHE A CE1 1 
ATOM   3270 C  CE2 . PHE A 1 405 ? -17.498 -5.723  20.021  1.00 36.18  ? 405 PHE A CE2 1 
ATOM   3271 C  CZ  . PHE A 1 405 ? -16.555 -6.577  20.602  1.00 33.55  ? 405 PHE A CZ  1 
ATOM   3272 N  N   . ALA A 1 406 ? -13.575 -6.135  15.279  1.00 32.92  ? 406 ALA A N   1 
ATOM   3273 C  CA  . ALA A 1 406 ? -12.259 -6.757  15.398  1.00 34.63  ? 406 ALA A CA  1 
ATOM   3274 C  C   . ALA A 1 406 ? -11.149 -5.747  15.172  1.00 33.95  ? 406 ALA A C   1 
ATOM   3275 O  O   . ALA A 1 406 ? -10.164 -5.717  15.920  1.00 34.05  ? 406 ALA A O   1 
ATOM   3276 C  CB  . ALA A 1 406 ? -12.129 -7.915  14.407  1.00 34.55  ? 406 ALA A CB  1 
ATOM   3277 N  N   . LEU A 1 407 ? -11.275 -4.918  14.138  1.00 35.20  ? 407 LEU A N   1 
ATOM   3278 C  CA  . LEU A 1 407 ? -10.191 -3.981  13.846  1.00 35.92  ? 407 LEU A CA  1 
ATOM   3279 C  C   . LEU A 1 407 ? -10.125 -2.854  14.874  1.00 37.07  ? 407 LEU A C   1 
ATOM   3280 O  O   . LEU A 1 407 ? -9.031  -2.381  15.193  1.00 34.87  ? 407 LEU A O   1 
ATOM   3281 C  CB  . LEU A 1 407 ? -10.325 -3.445  12.416  1.00 34.24  ? 407 LEU A CB  1 
ATOM   3282 C  CG  . LEU A 1 407 ? -10.238 -4.557  11.350  1.00 42.95  ? 407 LEU A CG  1 
ATOM   3283 C  CD1 . LEU A 1 407 ? -10.569 -4.067  9.918   1.00 44.35  ? 407 LEU A CD1 1 
ATOM   3284 C  CD2 . LEU A 1 407 ? -8.857  -5.219  11.363  1.00 43.73  ? 407 LEU A CD2 1 
ATOM   3285 N  N   . HIS A 1 408 ? -11.258 -2.431  15.441  1.00 32.81  ? 408 HIS A N   1 
ATOM   3286 C  CA  . HIS A 1 408 ? -11.182 -1.470  16.536  1.00 33.65  ? 408 HIS A CA  1 
ATOM   3287 C  C   . HIS A 1 408 ? -10.498 -2.086  17.751  1.00 36.36  ? 408 HIS A C   1 
ATOM   3288 O  O   . HIS A 1 408 ? -9.580  -1.485  18.324  1.00 36.32  ? 408 HIS A O   1 
ATOM   3289 C  CB  . HIS A 1 408 ? -12.562 -0.939  16.914  1.00 38.29  ? 408 HIS A CB  1 
ATOM   3290 C  CG  . HIS A 1 408 ? -12.502 0.296   17.756  1.00 37.36  ? 408 HIS A CG  1 
ATOM   3291 N  ND1 . HIS A 1 408 ? -12.249 1.543   17.228  1.00 34.42  ? 408 HIS A ND1 1 
ATOM   3292 C  CD2 . HIS A 1 408 ? -12.626 0.471   19.093  1.00 38.39  ? 408 HIS A CD2 1 
ATOM   3293 C  CE1 . HIS A 1 408 ? -12.239 2.438   18.200  1.00 35.67  ? 408 HIS A CE1 1 
ATOM   3294 N  NE2 . HIS A 1 408 ? -12.455 1.811   19.344  1.00 36.21  ? 408 HIS A NE2 1 
ATOM   3295 N  N   . GLU A 1 409 ? -10.911 -3.295  18.152  1.00 32.35  ? 409 GLU A N   1 
ATOM   3296 C  CA  . GLU A 1 409 ? -10.281 -3.907  19.319  1.00 33.48  ? 409 GLU A CA  1 
ATOM   3297 C  C   . GLU A 1 409 ? -8.800  -4.173  19.054  1.00 35.40  ? 409 GLU A C   1 
ATOM   3298 O  O   . GLU A 1 409 ? -7.942  -3.873  19.893  1.00 32.20  ? 409 GLU A O   1 
ATOM   3299 C  CB  . GLU A 1 409 ? -11.001 -5.201  19.710  1.00 36.13  ? 409 GLU A CB  1 
ATOM   3300 C  CG  . GLU A 1 409 ? -10.197 -6.007  20.734  1.00 40.95  ? 409 GLU A CG  1 
ATOM   3301 C  CD  . GLU A 1 409 ? -10.859 -7.308  21.146  1.00 39.97  ? 409 GLU A CD  1 
ATOM   3302 O  OE1 . GLU A 1 409 ? -11.736 -7.821  20.394  1.00 36.82  ? 409 GLU A OE1 1 
ATOM   3303 O  OE2 . GLU A 1 409 ? -10.498 -7.792  22.252  1.00 35.78  ? 409 GLU A OE2 1 
ATOM   3304 N  N   . ALA A 1 410 ? -8.475  -4.706  17.880  1.00 33.15  ? 410 ALA A N   1 
ATOM   3305 C  CA  . ALA A 1 410 ? -7.080  -5.047  17.602  1.00 32.09  ? 410 ALA A CA  1 
ATOM   3306 C  C   . ALA A 1 410 ? -6.209  -3.797  17.508  1.00 35.93  ? 410 ALA A C   1 
ATOM   3307 O  O   . ALA A 1 410 ? -5.060  -3.792  17.979  1.00 33.77  ? 410 ALA A O   1 
ATOM   3308 C  CB  . ALA A 1 410 ? -6.988  -5.878  16.319  1.00 30.99  ? 410 ALA A CB  1 
ATOM   3309 N  N   . THR A 1 411 ? -6.737  -2.727  16.914  1.00 35.03  ? 411 THR A N   1 
ATOM   3310 C  CA  . THR A 1 411 ? -5.981  -1.484  16.806  1.00 32.48  ? 411 THR A CA  1 
ATOM   3311 C  C   . THR A 1 411 ? -5.744  -0.875  18.182  1.00 34.72  ? 411 THR A C   1 
ATOM   3312 O  O   . THR A 1 411 ? -4.628  -0.453  18.504  1.00 33.32  ? 411 THR A O   1 
ATOM   3313 C  CB  . THR A 1 411 ? -6.721  -0.488  15.913  1.00 32.47  ? 411 THR A CB  1 
ATOM   3314 O  OG1 . THR A 1 411 ? -6.888  -1.048  14.601  1.00 32.23  ? 411 THR A OG1 1 
ATOM   3315 C  CG2 . THR A 1 411 ? -5.909  0.818   15.782  1.00 35.13  ? 411 THR A CG2 1 
ATOM   3316 N  N   . LEU A 1 412 ? -6.796  -0.813  19.004  1.00 31.94  ? 412 LEU A N   1 
ATOM   3317 C  CA  . LEU A 1 412 ? -6.665  -0.249  20.343  1.00 35.32  ? 412 LEU A CA  1 
ATOM   3318 C  C   . LEU A 1 412 ? -5.618  -1.001  21.155  1.00 31.65  ? 412 LEU A C   1 
ATOM   3319 O  O   . LEU A 1 412 ? -4.742  -0.391  21.783  1.00 33.83  ? 412 LEU A O   1 
ATOM   3320 C  CB  . LEU A 1 412 ? -8.019  -0.289  21.053  1.00 33.01  ? 412 LEU A CB  1 
ATOM   3321 C  CG  . LEU A 1 412 ? -7.985  -0.132  22.570  1.00 37.93  ? 412 LEU A CG  1 
ATOM   3322 C  CD1 . LEU A 1 412 ? -7.568  1.283   22.915  1.00 38.54  ? 412 LEU A CD1 1 
ATOM   3323 C  CD2 . LEU A 1 412 ? -9.355  -0.419  23.141  1.00 34.01  ? 412 LEU A CD2 1 
ATOM   3324 N  N   . VAL A 1 413 ? -5.689  -2.334  21.141  1.00 33.41  ? 413 VAL A N   1 
ATOM   3325 C  CA  . VAL A 1 413 ? -4.837  -3.145  22.004  1.00 32.52  ? 413 VAL A CA  1 
ATOM   3326 C  C   . VAL A 1 413 ? -3.389  -3.094  21.531  1.00 35.29  ? 413 VAL A C   1 
ATOM   3327 O  O   . VAL A 1 413 ? -2.464  -2.905  22.332  1.00 34.64  ? 413 VAL A O   1 
ATOM   3328 C  CB  . VAL A 1 413 ? -5.364  -4.594  22.056  1.00 36.08  ? 413 VAL A CB  1 
ATOM   3329 C  CG1 . VAL A 1 413 ? -4.372  -5.508  22.750  1.00 40.13  ? 413 VAL A CG1 1 
ATOM   3330 C  CG2 . VAL A 1 413 ? -6.716  -4.645  22.761  1.00 39.66  ? 413 VAL A CG2 1 
ATOM   3331 N  N   . LEU A 1 414 ? -3.164  -3.274  20.225  1.00 33.47  ? 414 LEU A N   1 
ATOM   3332 C  CA  . LEU A 1 414 ? -1.796  -3.192  19.712  1.00 36.24  ? 414 LEU A CA  1 
ATOM   3333 C  C   . LEU A 1 414 ? -1.222  -1.793  19.908  1.00 34.92  ? 414 LEU A C   1 
ATOM   3334 O  O   . LEU A 1 414 ? -0.038  -1.630  20.233  1.00 37.03  ? 414 LEU A O   1 
ATOM   3335 C  CB  . LEU A 1 414 ? -1.765  -3.586  18.230  1.00 34.99  ? 414 LEU A CB  1 
ATOM   3336 C  CG  . LEU A 1 414 ? -0.374  -3.802  17.620  1.00 35.01  ? 414 LEU A CG  1 
ATOM   3337 C  CD1 . LEU A 1 414 ? 0.455   -4.747  18.481  1.00 36.58  ? 414 LEU A CD1 1 
ATOM   3338 C  CD2 . LEU A 1 414 ? -0.490  -4.351  16.195  1.00 35.33  ? 414 LEU A CD2 1 
ATOM   3339 N  N   . GLY A 1 415 ? -2.043  -0.767  19.693  1.00 34.23  ? 415 GLY A N   1 
ATOM   3340 C  CA  . GLY A 1 415 ? -1.612  0.584   20.008  1.00 33.71  ? 415 GLY A CA  1 
ATOM   3341 C  C   . GLY A 1 415 ? -1.124  0.729   21.438  1.00 37.23  ? 415 GLY A C   1 
ATOM   3342 O  O   . GLY A 1 415 ? -0.069  1.319   21.689  1.00 36.01  ? 415 GLY A O   1 
ATOM   3343 N  N   . MET A 1 416 ? -1.887  0.195   22.404  1.00 35.33  ? 416 MET A N   1 
ATOM   3344 C  CA  . MET A 1 416 ? -1.481  0.354   23.796  1.00 33.44  ? 416 MET A CA  1 
ATOM   3345 C  C   . MET A 1 416 ? -0.249  -0.486  24.106  1.00 36.87  ? 416 MET A C   1 
ATOM   3346 O  O   . MET A 1 416 ? 0.656   -0.055  24.835  1.00 35.13  ? 416 MET A O   1 
ATOM   3347 C  CB  . MET A 1 416 ? -2.618  -0.020  24.742  1.00 33.11  ? 416 MET A CB  1 
ATOM   3348 C  CG  . MET A 1 416 ? -3.689  1.028   24.823  1.00 35.97  ? 416 MET A CG  1 
ATOM   3349 S  SD  . MET A 1 416 ? -5.096  0.416   25.772  1.00 41.84  ? 416 MET A SD  1 
ATOM   3350 C  CE  . MET A 1 416 ? -4.569  0.945   27.391  1.00 39.09  ? 416 MET A CE  1 
ATOM   3351 N  N   . MET A 1 417 ? -0.201  -1.681  23.540  1.00 34.22  ? 417 MET A N   1 
ATOM   3352 C  CA  . MET A 1 417 ? 0.957   -2.551  23.661  1.00 35.56  ? 417 MET A CA  1 
ATOM   3353 C  C   . MET A 1 417 ? 2.232   -1.814  23.230  1.00 40.26  ? 417 MET A C   1 
ATOM   3354 O  O   . MET A 1 417 ? 3.240   -1.799  23.951  1.00 36.24  ? 417 MET A O   1 
ATOM   3355 C  CB  . MET A 1 417 ? 0.679   -3.768  22.790  1.00 34.16  ? 417 MET A CB  1 
ATOM   3356 C  CG  . MET A 1 417 ? -0.057  -4.889  23.514  1.00 38.33  ? 417 MET A CG  1 
ATOM   3357 S  SD  . MET A 1 417 ? -0.637  -6.120  22.339  1.00 37.30  ? 417 MET A SD  1 
ATOM   3358 C  CE  . MET A 1 417 ? 0.929   -6.686  21.663  1.00 34.92  ? 417 MET A CE  1 
ATOM   3359 N  N   . LEU A 1 418 ? 2.187   -1.160  22.055  1.00 36.40  ? 418 LEU A N   1 
ATOM   3360 C  CA  . LEU A 1 418 ? 3.344   -0.434  21.535  1.00 34.64  ? 418 LEU A CA  1 
ATOM   3361 C  C   . LEU A 1 418 ? 3.615   0.865   22.298  1.00 37.38  ? 418 LEU A C   1 
ATOM   3362 O  O   . LEU A 1 418 ? 4.758   1.332   22.335  1.00 39.49  ? 418 LEU A O   1 
ATOM   3363 C  CB  . LEU A 1 418 ? 3.128   -0.132  20.047  1.00 36.82  ? 418 LEU A CB  1 
ATOM   3364 C  CG  . LEU A 1 418 ? 2.938   -1.356  19.137  1.00 42.03  ? 418 LEU A CG  1 
ATOM   3365 C  CD1 . LEU A 1 418 ? 2.527   -0.921  17.731  1.00 40.33  ? 418 LEU A CD1 1 
ATOM   3366 C  CD2 . LEU A 1 418 ? 4.205   -2.197  19.083  1.00 40.45  ? 418 LEU A CD2 1 
ATOM   3367 N  N   . LYS A 1 419 ? 2.589   1.476   22.887  1.00 39.19  ? 419 LYS A N   1 
ATOM   3368 C  CA  . LYS A 1 419 ? 2.815   2.651   23.724  1.00 37.31  ? 419 LYS A CA  1 
ATOM   3369 C  C   . LYS A 1 419 ? 3.586   2.300   24.992  1.00 39.88  ? 419 LYS A C   1 
ATOM   3370 O  O   . LYS A 1 419 ? 4.451   3.069   25.429  1.00 36.96  ? 419 LYS A O   1 
ATOM   3371 C  CB  . LYS A 1 419 ? 1.484   3.313   24.090  1.00 40.62  ? 419 LYS A CB  1 
ATOM   3372 C  CG  . LYS A 1 419 ? 1.632   4.460   25.105  1.00 38.31  ? 419 LYS A CG  1 
ATOM   3373 C  CD  . LYS A 1 419 ? 0.295   5.121   25.393  1.00 38.67  ? 419 LYS A CD  1 
ATOM   3374 C  CE  . LYS A 1 419 ? 0.394   6.113   26.545  1.00 37.85  ? 419 LYS A CE  1 
ATOM   3375 N  NZ  . LYS A 1 419 ? -0.853  6.928   26.695  1.00 40.88  ? 419 LYS A NZ  1 
ATOM   3376 N  N   . HIS A 1 420 ? 3.301   1.142   25.593  1.00 38.89  ? 420 HIS A N   1 
ATOM   3377 C  CA  . HIS A 1 420 ? 3.703   0.896   26.974  1.00 37.31  ? 420 HIS A CA  1 
ATOM   3378 C  C   . HIS A 1 420 ? 4.907   -0.026  27.126  1.00 38.61  ? 420 HIS A C   1 
ATOM   3379 O  O   . HIS A 1 420 ? 5.514   -0.045  28.208  1.00 42.76  ? 420 HIS A O   1 
ATOM   3380 C  CB  . HIS A 1 420 ? 2.513   0.335   27.766  1.00 37.00  ? 420 HIS A CB  1 
ATOM   3381 C  CG  . HIS A 1 420 ? 1.498   1.379   28.115  1.00 37.35  ? 420 HIS A CG  1 
ATOM   3382 N  ND1 . HIS A 1 420 ? 1.638   2.219   29.197  1.00 37.78  ? 420 HIS A ND1 1 
ATOM   3383 C  CD2 . HIS A 1 420 ? 0.359   1.762   27.486  1.00 35.58  ? 420 HIS A CD2 1 
ATOM   3384 C  CE1 . HIS A 1 420 ? 0.610   3.050   29.246  1.00 39.11  ? 420 HIS A CE1 1 
ATOM   3385 N  NE2 . HIS A 1 420 ? -0.176  2.802   28.210  1.00 37.31  ? 420 HIS A NE2 1 
ATOM   3386 N  N   . PHE A 1 421 ? 5.293   -0.762  26.086  1.00 37.00  ? 421 PHE A N   1 
ATOM   3387 C  CA  . PHE A 1 421 ? 6.335   -1.770  26.217  1.00 38.12  ? 421 PHE A CA  1 
ATOM   3388 C  C   . PHE A 1 421 ? 7.244   -1.784  25.001  1.00 40.74  ? 421 PHE A C   1 
ATOM   3389 O  O   . PHE A 1 421 ? 6.808   -1.545  23.874  1.00 38.35  ? 421 PHE A O   1 
ATOM   3390 C  CB  . PHE A 1 421 ? 5.759   -3.180  26.376  1.00 38.82  ? 421 PHE A CB  1 
ATOM   3391 C  CG  . PHE A 1 421 ? 4.773   -3.308  27.503  1.00 38.12  ? 421 PHE A CG  1 
ATOM   3392 C  CD1 . PHE A 1 421 ? 5.200   -3.601  28.786  1.00 35.51  ? 421 PHE A CD1 1 
ATOM   3393 C  CD2 . PHE A 1 421 ? 3.420   -3.154  27.265  1.00 38.03  ? 421 PHE A CD2 1 
ATOM   3394 C  CE1 . PHE A 1 421 ? 4.299   -3.719  29.829  1.00 36.66  ? 421 PHE A CE1 1 
ATOM   3395 C  CE2 . PHE A 1 421 ? 2.509   -3.270  28.287  1.00 35.41  ? 421 PHE A CE2 1 
ATOM   3396 C  CZ  . PHE A 1 421 ? 2.953   -3.556  29.583  1.00 38.59  ? 421 PHE A CZ  1 
ATOM   3397 N  N   . ASP A 1 422 ? 8.512   -2.106  25.249  1.00 40.75  ? 422 ASP A N   1 
ATOM   3398 C  CA  . ASP A 1 422 ? 9.393   -2.653  24.228  1.00 42.19  ? 422 ASP A CA  1 
ATOM   3399 C  C   . ASP A 1 422 ? 9.296   -4.173  24.269  1.00 41.20  ? 422 ASP A C   1 
ATOM   3400 O  O   . ASP A 1 422 ? 9.102   -4.767  25.332  1.00 42.52  ? 422 ASP A O   1 
ATOM   3401 C  CB  . ASP A 1 422 ? 10.837  -2.205  24.466  1.00 42.80  ? 422 ASP A CB  1 
ATOM   3402 C  CG  . ASP A 1 422 ? 11.029  -0.730  24.210  1.00 45.56  ? 422 ASP A CG  1 
ATOM   3403 O  OD1 . ASP A 1 422 ? 10.712  -0.280  23.092  1.00 48.22  ? 422 ASP A OD1 1 
ATOM   3404 O  OD2 . ASP A 1 422 ? 11.496  -0.021  25.125  1.00 50.35  ? 422 ASP A OD2 1 
ATOM   3405 N  N   . PHE A 1 423 ? 9.410   -4.805  23.108  1.00 37.26  ? 423 PHE A N   1 
ATOM   3406 C  CA  . PHE A 1 423 ? 9.260   -6.252  23.003  1.00 39.94  ? 423 PHE A CA  1 
ATOM   3407 C  C   . PHE A 1 423 ? 10.545  -6.896  22.510  1.00 40.63  ? 423 PHE A C   1 
ATOM   3408 O  O   . PHE A 1 423 ? 11.224  -6.356  21.632  1.00 43.67  ? 423 PHE A O   1 
ATOM   3409 C  CB  . PHE A 1 423 ? 8.098   -6.612  22.083  1.00 39.98  ? 423 PHE A CB  1 
ATOM   3410 C  CG  . PHE A 1 423 ? 6.771   -6.171  22.625  1.00 39.09  ? 423 PHE A CG  1 
ATOM   3411 C  CD1 . PHE A 1 423 ? 6.082   -6.977  23.526  1.00 38.89  ? 423 PHE A CD1 1 
ATOM   3412 C  CD2 . PHE A 1 423 ? 6.246   -4.932  22.284  1.00 36.99  ? 423 PHE A CD2 1 
ATOM   3413 C  CE1 . PHE A 1 423 ? 4.874   -6.565  24.054  1.00 36.78  ? 423 PHE A CE1 1 
ATOM   3414 C  CE2 . PHE A 1 423 ? 5.039   -4.507  22.802  1.00 34.98  ? 423 PHE A CE2 1 
ATOM   3415 C  CZ  . PHE A 1 423 ? 4.351   -5.326  23.692  1.00 38.45  ? 423 PHE A CZ  1 
ATOM   3416 N  N   . GLU A 1 424 ? 10.865  -8.059  23.075  1.00 35.98  ? 424 GLU A N   1 
ATOM   3417 C  CA  . GLU A 1 424 ? 12.067  -8.806  22.714  1.00 40.88  ? 424 GLU A CA  1 
ATOM   3418 C  C   . GLU A 1 424 ? 11.699  -10.233 22.354  1.00 36.36  ? 424 GLU A C   1 
ATOM   3419 O  O   . GLU A 1 424 ? 11.101  -10.949 23.164  1.00 39.44  ? 424 GLU A O   1 
ATOM   3420 C  CB  . GLU A 1 424 ? 13.096  -8.802  23.851  1.00 38.45  ? 424 GLU A CB  1 
ATOM   3421 C  CG  . GLU A 1 424 ? 14.220  -9.781  23.621  1.00 43.06  ? 424 GLU A CG  1 
ATOM   3422 C  CD  . GLU A 1 424 ? 15.180  -9.867  24.800  1.00 46.77  ? 424 GLU A CD  1 
ATOM   3423 O  OE1 . GLU A 1 424 ? 14.757  -9.627  25.947  1.00 50.48  ? 424 GLU A OE1 1 
ATOM   3424 O  OE2 . GLU A 1 424 ? 16.357  -10.207 24.575  1.00 53.01  ? 424 GLU A OE2 1 
ATOM   3425 N  N   . ASP A 1 425 ? 12.072  -10.650 21.145  1.00 35.24  ? 425 ASP A N   1 
ATOM   3426 C  CA  . ASP A 1 425 ? 11.933  -12.044 20.719  1.00 33.59  ? 425 ASP A CA  1 
ATOM   3427 C  C   . ASP A 1 425 ? 13.089  -12.823 21.344  1.00 41.03  ? 425 ASP A C   1 
ATOM   3428 O  O   . ASP A 1 425 ? 14.072  -13.184 20.698  1.00 39.32  ? 425 ASP A O   1 
ATOM   3429 C  CB  . ASP A 1 425 ? 11.903  -12.112 19.193  1.00 39.80  ? 425 ASP A CB  1 
ATOM   3430 C  CG  . ASP A 1 425 ? 11.923  -13.518 18.641  1.00 32.70  ? 425 ASP A CG  1 
ATOM   3431 O  OD1 . ASP A 1 425 ? 11.458  -14.468 19.303  1.00 35.54  ? 425 ASP A OD1 1 
ATOM   3432 O  OD2 . ASP A 1 425 ? 12.383  -13.663 17.485  1.00 36.04  ? 425 ASP A OD2 1 
ATOM   3433 N  N   . HIS A 1 426 ? 12.957  -13.097 22.644  1.00 38.37  ? 426 HIS A N   1 
ATOM   3434 C  CA  . HIS A 1 426 ? 14.103  -13.603 23.392  1.00 42.32  ? 426 HIS A CA  1 
ATOM   3435 C  C   . HIS A 1 426 ? 14.443  -15.052 23.052  1.00 40.29  ? 426 HIS A C   1 
ATOM   3436 O  O   . HIS A 1 426 ? 15.580  -15.464 23.279  1.00 42.09  ? 426 HIS A O   1 
ATOM   3437 C  CB  . HIS A 1 426 ? 13.862  -13.430 24.898  1.00 40.93  ? 426 HIS A CB  1 
ATOM   3438 C  CG  . HIS A 1 426 ? 12.723  -14.242 25.423  1.00 44.14  ? 426 HIS A CG  1 
ATOM   3439 N  ND1 . HIS A 1 426 ? 11.413  -14.017 25.048  1.00 41.53  ? 426 HIS A ND1 1 
ATOM   3440 C  CD2 . HIS A 1 426 ? 12.696  -15.283 26.287  1.00 39.81  ? 426 HIS A CD2 1 
ATOM   3441 C  CE1 . HIS A 1 426 ? 10.630  -14.888 25.659  1.00 43.31  ? 426 HIS A CE1 1 
ATOM   3442 N  NE2 . HIS A 1 426 ? 11.384  -15.667 26.418  1.00 40.48  ? 426 HIS A NE2 1 
ATOM   3443 N  N   . THR A 1 427 ? 13.516  -15.828 22.484  1.00 39.52  ? 427 THR A N   1 
ATOM   3444 C  CA  . THR A 1 427 ? 13.785  -17.218 22.119  1.00 37.48  ? 427 THR A CA  1 
ATOM   3445 C  C   . THR A 1 427 ? 14.087  -17.403 20.630  1.00 39.16  ? 427 THR A C   1 
ATOM   3446 O  O   . THR A 1 427 ? 14.235  -18.538 20.177  1.00 38.26  ? 427 THR A O   1 
ATOM   3447 C  CB  . THR A 1 427 ? 12.610  -18.122 22.492  1.00 39.93  ? 427 THR A CB  1 
ATOM   3448 O  OG1 . THR A 1 427 ? 11.534  -17.941 21.549  1.00 39.79  ? 427 THR A OG1 1 
ATOM   3449 C  CG2 . THR A 1 427 ? 12.121  -17.835 23.927  1.00 40.53  ? 427 THR A CG2 1 
ATOM   3450 N  N   . ASN A 1 428 ? 14.156  -16.328 19.859  1.00 35.19  ? 428 ASN A N   1 
ATOM   3451 C  CA  . ASN A 1 428 ? 14.233  -16.446 18.408  1.00 38.22  ? 428 ASN A CA  1 
ATOM   3452 C  C   . ASN A 1 428 ? 13.178  -17.429 17.915  1.00 39.58  ? 428 ASN A C   1 
ATOM   3453 O  O   . ASN A 1 428 ? 13.471  -18.465 17.313  1.00 38.18  ? 428 ASN A O   1 
ATOM   3454 C  CB  . ASN A 1 428 ? 15.623  -16.872 17.950  1.00 35.15  ? 428 ASN A CB  1 
ATOM   3455 C  CG  . ASN A 1 428 ? 15.841  -16.566 16.484  1.00 42.28  ? 428 ASN A CG  1 
ATOM   3456 O  OD1 . ASN A 1 428 ? 15.122  -15.748 15.915  1.00 42.83  ? 428 ASN A OD1 1 
ATOM   3457 N  ND2 . ASN A 1 428 ? 16.807  -17.219 15.865  1.00 38.65  ? 428 ASN A ND2 1 
ATOM   3458 N  N   . TYR A 1 429 ? 11.928  -17.088 18.210  1.00 37.51  ? 429 TYR A N   1 
ATOM   3459 C  CA  . TYR A 1 429 ? 10.831  -18.032 18.044  1.00 35.26  ? 429 TYR A CA  1 
ATOM   3460 C  C   . TYR A 1 429 ? 10.674  -18.449 16.585  1.00 38.34  ? 429 TYR A C   1 
ATOM   3461 O  O   . TYR A 1 429 ? 10.696  -17.611 15.676  1.00 40.80  ? 429 TYR A O   1 
ATOM   3462 C  CB  . TYR A 1 429 ? 9.542   -17.395 18.572  1.00 34.34  ? 429 TYR A CB  1 
ATOM   3463 C  CG  . TYR A 1 429 ? 8.278   -18.095 18.148  1.00 35.66  ? 429 TYR A CG  1 
ATOM   3464 C  CD1 . TYR A 1 429 ? 7.871   -19.269 18.763  1.00 36.91  ? 429 TYR A CD1 1 
ATOM   3465 C  CD2 . TYR A 1 429 ? 7.479   -17.569 17.143  1.00 37.11  ? 429 TYR A CD2 1 
ATOM   3466 C  CE1 . TYR A 1 429 ? 6.686   -19.907 18.384  1.00 37.79  ? 429 TYR A CE1 1 
ATOM   3467 C  CE2 . TYR A 1 429 ? 6.301   -18.194 16.754  1.00 36.50  ? 429 TYR A CE2 1 
ATOM   3468 C  CZ  . TYR A 1 429 ? 5.906   -19.358 17.375  1.00 37.36  ? 429 TYR A CZ  1 
ATOM   3469 O  OH  . TYR A 1 429 ? 4.734   -19.987 16.972  1.00 36.11  ? 429 TYR A OH  1 
ATOM   3470 N  N   . GLU A 1 430 ? 10.544  -19.754 16.367  1.00 35.30  ? 430 GLU A N   1 
ATOM   3471 C  CA  . GLU A 1 430 ? 10.274  -20.312 15.050  1.00 40.07  ? 430 GLU A CA  1 
ATOM   3472 C  C   . GLU A 1 430 ? 8.765   -20.455 14.905  1.00 38.61  ? 430 GLU A C   1 
ATOM   3473 O  O   . GLU A 1 430 ? 8.130   -21.139 15.718  1.00 40.70  ? 430 GLU A O   1 
ATOM   3474 C  CB  . GLU A 1 430 ? 10.954  -21.671 14.886  1.00 40.69  ? 430 GLU A CB  1 
ATOM   3475 C  CG  . GLU A 1 430 ? 10.814  -22.270 13.488  1.00 51.18  ? 430 GLU A CG  1 
ATOM   3476 C  CD  . GLU A 1 430 ? 11.459  -23.648 13.369  1.00 62.85  ? 430 GLU A CD  1 
ATOM   3477 O  OE1 . GLU A 1 430 ? 12.232  -24.030 14.280  1.00 65.03  ? 430 GLU A OE1 1 
ATOM   3478 O  OE2 . GLU A 1 430 ? 11.191  -24.349 12.365  1.00 61.89  ? 430 GLU A OE2 1 
ATOM   3479 N  N   . LEU A 1 431 ? 8.190   -19.808 13.889  1.00 37.75  ? 431 LEU A N   1 
ATOM   3480 C  CA  . LEU A 1 431 ? 6.733   -19.772 13.778  1.00 37.46  ? 431 LEU A CA  1 
ATOM   3481 C  C   . LEU A 1 431 ? 6.174   -21.178 13.622  1.00 41.16  ? 431 LEU A C   1 
ATOM   3482 O  O   . LEU A 1 431 ? 6.660   -21.963 12.804  1.00 37.67  ? 431 LEU A O   1 
ATOM   3483 C  CB  . LEU A 1 431 ? 6.309   -18.890 12.601  1.00 39.60  ? 431 LEU A CB  1 
ATOM   3484 C  CG  . LEU A 1 431 ? 4.804   -18.774 12.339  1.00 42.32  ? 431 LEU A CG  1 
ATOM   3485 C  CD1 . LEU A 1 431 ? 4.068   -18.226 13.550  1.00 36.91  ? 431 LEU A CD1 1 
ATOM   3486 C  CD2 . LEU A 1 431 ? 4.569   -17.887 11.129  1.00 41.39  ? 431 LEU A CD2 1 
ATOM   3487 N  N   . ASP A 1 432 ? 5.153   -21.497 14.426  1.00 35.83  ? 432 ASP A N   1 
ATOM   3488 C  CA  . ASP A 1 432 ? 4.507   -22.808 14.426  1.00 37.29  ? 432 ASP A CA  1 
ATOM   3489 C  C   . ASP A 1 432 ? 3.008   -22.548 14.492  1.00 37.63  ? 432 ASP A C   1 
ATOM   3490 O  O   . ASP A 1 432 ? 2.535   -21.943 15.455  1.00 36.35  ? 432 ASP A O   1 
ATOM   3491 C  CB  . ASP A 1 432 ? 4.996   -23.650 15.620  1.00 36.37  ? 432 ASP A CB  1 
ATOM   3492 C  CG  . ASP A 1 432 ? 4.309   -25.014 15.734  1.00 43.80  ? 432 ASP A CG  1 
ATOM   3493 O  OD1 . ASP A 1 432 ? 3.569   -25.432 14.820  1.00 42.60  ? 432 ASP A OD1 1 
ATOM   3494 O  OD2 . ASP A 1 432 ? 4.560   -25.699 16.748  1.00 47.86  ? 432 ASP A OD2 1 
ATOM   3495 N  N   . ILE A 1 433 ? 2.262   -22.936 13.460  1.00 38.70  ? 433 ILE A N   1 
ATOM   3496 C  CA  . ILE A 1 433 ? 0.871   -22.501 13.337  1.00 35.55  ? 433 ILE A CA  1 
ATOM   3497 C  C   . ILE A 1 433 ? -0.054  -23.660 13.670  1.00 39.06  ? 433 ILE A C   1 
ATOM   3498 O  O   . ILE A 1 433 ? -0.105  -24.664 12.948  1.00 38.28  ? 433 ILE A O   1 
ATOM   3499 C  CB  . ILE A 1 433 ? 0.562   -21.930 11.949  1.00 32.63  ? 433 ILE A CB  1 
ATOM   3500 C  CG1 . ILE A 1 433 ? 1.324   -20.622 11.735  1.00 37.76  ? 433 ILE A CG1 1 
ATOM   3501 C  CG2 . ILE A 1 433 ? -0.963  -21.692 11.795  1.00 34.50  ? 433 ILE A CG2 1 
ATOM   3502 C  CD1 . ILE A 1 433 ? 1.313   -20.154 10.301  1.00 40.56  ? 433 ILE A CD1 1 
ATOM   3503 N  N   . LYS A 1 434 ? -0.803  -23.498 14.753  1.00 35.03  ? 434 LYS A N   1 
ATOM   3504 C  CA  . LYS A 1 434 ? -1.790  -24.468 15.185  1.00 34.98  ? 434 LYS A CA  1 
ATOM   3505 C  C   . LYS A 1 434 ? -3.147  -24.143 14.581  1.00 38.07  ? 434 LYS A C   1 
ATOM   3506 O  O   . LYS A 1 434 ? -3.544  -22.978 14.512  1.00 37.91  ? 434 LYS A O   1 
ATOM   3507 C  CB  . LYS A 1 434 ? -1.864  -24.473 16.713  1.00 39.53  ? 434 LYS A CB  1 
ATOM   3508 C  CG  . LYS A 1 434 ? -2.707  -25.574 17.325  1.00 42.41  ? 434 LYS A CG  1 
ATOM   3509 C  CD  . LYS A 1 434 ? -2.975  -25.210 18.783  1.00 48.08  ? 434 LYS A CD  1 
ATOM   3510 C  CE  . LYS A 1 434 ? -3.769  -26.266 19.524  1.00 52.58  ? 434 LYS A CE  1 
ATOM   3511 N  NZ  . LYS A 1 434 ? -5.064  -25.704 19.990  1.00 56.53  ? 434 LYS A NZ  1 
ATOM   3512 N  N   . GLU A 1 435 ? -3.856  -25.176 14.140  1.00 35.74  ? 435 GLU A N   1 
ATOM   3513 C  CA  . GLU A 1 435 ? -5.124  -25.003 13.443  1.00 36.61  ? 435 GLU A CA  1 
ATOM   3514 C  C   . GLU A 1 435 ? -6.257  -25.533 14.305  1.00 34.65  ? 435 GLU A C   1 
ATOM   3515 O  O   . GLU A 1 435 ? -6.278  -26.719 14.650  1.00 37.75  ? 435 GLU A O   1 
ATOM   3516 C  CB  . GLU A 1 435 ? -5.107  -25.710 12.088  1.00 36.53  ? 435 GLU A CB  1 
ATOM   3517 C  CG  . GLU A 1 435 ? -3.855  -25.419 11.268  1.00 31.89  ? 435 GLU A CG  1 
ATOM   3518 C  CD  . GLU A 1 435 ? -4.037  -25.727 9.791   1.00 37.32  ? 435 GLU A CD  1 
ATOM   3519 O  OE1 . GLU A 1 435 ? -5.159  -26.103 9.402   1.00 37.51  ? 435 GLU A OE1 1 
ATOM   3520 O  OE2 . GLU A 1 435 ? -3.058  -25.599 9.025   1.00 33.86  ? 435 GLU A OE2 1 
ATOM   3521 N  N   . THR A 1 436 ? -7.191  -24.654 14.647  1.00 40.03  ? 436 THR A N   1 
ATOM   3522 C  CA  . THR A 1 436 ? -8.462  -25.071 15.229  1.00 41.89  ? 436 THR A CA  1 
ATOM   3523 C  C   . THR A 1 436 ? -9.570  -24.692 14.251  1.00 43.28  ? 436 THR A C   1 
ATOM   3524 O  O   . THR A 1 436 ? -9.511  -25.083 13.073  1.00 40.55  ? 436 THR A O   1 
ATOM   3525 C  CB  . THR A 1 436 ? -8.659  -24.446 16.617  1.00 42.48  ? 436 THR A CB  1 
ATOM   3526 O  OG1 . THR A 1 436 ? -8.553  -23.015 16.543  1.00 40.19  ? 436 THR A OG1 1 
ATOM   3527 C  CG2 . THR A 1 436 ? -7.616  -24.982 17.590  1.00 39.83  ? 436 THR A CG2 1 
ATOM   3528 N  N   . LEU A 1 437 ? -10.569 -23.923 14.700  1.00 38.39  ? 437 LEU A N   1 
ATOM   3529 C  CA  . LEU A 1 437 ? -11.417 -23.221 13.733  1.00 44.38  ? 437 LEU A CA  1 
ATOM   3530 C  C   . LEU A 1 437 ? -10.567 -22.309 12.856  1.00 41.04  ? 437 LEU A C   1 
ATOM   3531 O  O   . LEU A 1 437 ? -10.814 -22.156 11.652  1.00 41.26  ? 437 LEU A O   1 
ATOM   3532 C  CB  . LEU A 1 437 ? -12.479 -22.390 14.464  1.00 41.98  ? 437 LEU A CB  1 
ATOM   3533 C  CG  . LEU A 1 437 ? -13.916 -22.255 13.936  1.00 46.07  ? 437 LEU A CG  1 
ATOM   3534 C  CD1 . LEU A 1 437 ? -14.408 -20.822 14.096  1.00 39.26  ? 437 LEU A CD1 1 
ATOM   3535 C  CD2 . LEU A 1 437 ? -14.082 -22.739 12.500  1.00 49.73  ? 437 LEU A CD2 1 
ATOM   3536 N  N   . THR A 1 438 ? -9.547  -21.714 13.452  1.00 41.14  ? 438 THR A N   1 
ATOM   3537 C  CA  . THR A 1 438 ? -8.777  -20.627 12.887  1.00 38.53  ? 438 THR A CA  1 
ATOM   3538 C  C   . THR A 1 438 ? -7.300  -20.981 12.990  1.00 38.51  ? 438 THR A C   1 
ATOM   3539 O  O   . THR A 1 438 ? -6.933  -22.065 13.454  1.00 34.70  ? 438 THR A O   1 
ATOM   3540 C  CB  . THR A 1 438 ? -9.088  -19.340 13.653  1.00 38.93  ? 438 THR A CB  1 
ATOM   3541 O  OG1 . THR A 1 438 ? -8.942  -19.623 15.052  1.00 38.32  ? 438 THR A OG1 1 
ATOM   3542 C  CG2 . THR A 1 438 ? -10.548 -18.916 13.388  1.00 34.24  ? 438 THR A CG2 1 
ATOM   3543 N  N   . LEU A 1 439 ? -6.451  -20.055 12.559  1.00 35.77  ? 439 LEU A N   1 
ATOM   3544 C  CA  . LEU A 1 439 ? -5.006  -20.207 12.641  1.00 33.01  ? 439 LEU A CA  1 
ATOM   3545 C  C   . LEU A 1 439 ? -4.465  -19.325 13.757  1.00 35.70  ? 439 LEU A C   1 
ATOM   3546 O  O   . LEU A 1 439 ? -4.882  -18.171 13.902  1.00 31.20  ? 439 LEU A O   1 
ATOM   3547 C  CB  . LEU A 1 439 ? -4.355  -19.831 11.305  1.00 32.04  ? 439 LEU A CB  1 
ATOM   3548 C  CG  . LEU A 1 439 ? -4.887  -20.480 10.021  1.00 31.54  ? 439 LEU A CG  1 
ATOM   3549 C  CD1 . LEU A 1 439 ? -4.129  -19.922 8.807   1.00 34.63  ? 439 LEU A CD1 1 
ATOM   3550 C  CD2 . LEU A 1 439 ? -4.764  -22.008 10.036  1.00 30.68  ? 439 LEU A CD2 1 
ATOM   3551 N  N   . LYS A 1 440 ? -3.519  -19.864 14.540  1.00 34.59  ? 440 LYS A N   1 
ATOM   3552 C  CA  . LYS A 1 440 ? -2.894  -19.114 15.629  1.00 35.52  ? 440 LYS A CA  1 
ATOM   3553 C  C   . LYS A 1 440 ? -1.445  -19.560 15.738  1.00 36.10  ? 440 LYS A C   1 
ATOM   3554 O  O   . LYS A 1 440 ? -1.174  -20.757 15.585  1.00 38.68  ? 440 LYS A O   1 
ATOM   3555 C  CB  . LYS A 1 440 ? -3.598  -19.368 16.973  1.00 42.38  ? 440 LYS A CB  1 
ATOM   3556 C  CG  . LYS A 1 440 ? -4.985  -18.739 17.115  1.00 41.04  ? 440 LYS A CG  1 
ATOM   3557 C  CD  . LYS A 1 440 ? -5.455  -18.747 18.584  1.00 41.25  ? 440 LYS A CD  1 
ATOM   3558 C  CE  . LYS A 1 440 ? -6.927  -18.336 18.680  1.00 42.24  ? 440 LYS A CE  1 
ATOM   3559 N  NZ  . LYS A 1 440 ? -7.409  -18.343 20.108  1.00 38.73  ? 440 LYS A NZ  1 
ATOM   3560 N  N   . PRO A 1 441 ? -0.500  -18.659 16.025  1.00 36.89  ? 441 PRO A N   1 
ATOM   3561 C  CA  . PRO A 1 441 ? 0.833   -19.138 16.399  1.00 36.95  ? 441 PRO A CA  1 
ATOM   3562 C  C   . PRO A 1 441 ? 0.701   -19.960 17.676  1.00 44.88  ? 441 PRO A C   1 
ATOM   3563 O  O   . PRO A 1 441 ? -0.153  -19.680 18.527  1.00 47.58  ? 441 PRO A O   1 
ATOM   3564 C  CB  . PRO A 1 441 ? 1.653   -17.858 16.618  1.00 38.68  ? 441 PRO A CB  1 
ATOM   3565 C  CG  . PRO A 1 441 ? 0.745   -16.703 16.407  1.00 36.04  ? 441 PRO A CG  1 
ATOM   3566 C  CD  . PRO A 1 441 ? -0.642  -17.194 16.128  1.00 36.18  ? 441 PRO A CD  1 
ATOM   3567 N  N   . GLU A 1 442 ? 1.489   -21.025 17.772  1.00 38.64  ? 442 GLU A N   1 
ATOM   3568 C  CA  . GLU A 1 442 ? 1.539   -21.840 18.977  1.00 41.00  ? 442 GLU A CA  1 
ATOM   3569 C  C   . GLU A 1 442 ? 2.917   -21.716 19.604  1.00 36.16  ? 442 GLU A C   1 
ATOM   3570 O  O   . GLU A 1 442 ? 3.930   -21.747 18.900  1.00 34.88  ? 442 GLU A O   1 
ATOM   3571 C  CB  . GLU A 1 442 ? 1.232   -23.316 18.704  1.00 38.25  ? 442 GLU A CB  1 
ATOM   3572 C  CG  . GLU A 1 442 ? 1.186   -24.109 20.023  1.00 44.67  ? 442 GLU A CG  1 
ATOM   3573 C  CD  . GLU A 1 442 ? 0.780   -25.569 19.868  1.00 50.51  ? 442 GLU A CD  1 
ATOM   3574 O  OE1 . GLU A 1 442 ? 1.069   -26.186 18.818  1.00 46.00  ? 442 GLU A OE1 1 
ATOM   3575 O  OE2 . GLU A 1 442 ? 0.160   -26.098 20.817  1.00 54.16  ? 442 GLU A OE2 1 
ATOM   3576 N  N   . GLY A 1 443 ? 2.948   -21.549 20.924  1.00 35.42  ? 443 GLY A N   1 
ATOM   3577 C  CA  . GLY A 1 443 ? 4.219   -21.444 21.613  1.00 38.62  ? 443 GLY A CA  1 
ATOM   3578 C  C   . GLY A 1 443 ? 4.933   -20.125 21.434  1.00 37.51  ? 443 GLY A C   1 
ATOM   3579 O  O   . GLY A 1 443 ? 6.094   -19.999 21.841  1.00 36.15  ? 443 GLY A O   1 
ATOM   3580 N  N   . PHE A 1 444 ? 4.281   -19.135 20.838  1.00 36.21  ? 444 PHE A N   1 
ATOM   3581 C  CA  . PHE A 1 444 ? 4.905   -17.830 20.645  1.00 37.34  ? 444 PHE A CA  1 
ATOM   3582 C  C   . PHE A 1 444 ? 5.025   -17.090 21.983  1.00 37.63  ? 444 PHE A C   1 
ATOM   3583 O  O   . PHE A 1 444 ? 4.019   -16.814 22.648  1.00 33.54  ? 444 PHE A O   1 
ATOM   3584 C  CB  . PHE A 1 444 ? 4.096   -17.034 19.616  1.00 34.53  ? 444 PHE A CB  1 
ATOM   3585 C  CG  . PHE A 1 444 ? 4.603   -15.641 19.371  1.00 35.44  ? 444 PHE A CG  1 
ATOM   3586 C  CD1 . PHE A 1 444 ? 5.958   -15.356 19.390  1.00 36.19  ? 444 PHE A CD1 1 
ATOM   3587 C  CD2 . PHE A 1 444 ? 3.709   -14.607 19.139  1.00 31.66  ? 444 PHE A CD2 1 
ATOM   3588 C  CE1 . PHE A 1 444 ? 6.411   -14.057 19.174  1.00 34.71  ? 444 PHE A CE1 1 
ATOM   3589 C  CE2 . PHE A 1 444 ? 4.149   -13.312 18.932  1.00 32.51  ? 444 PHE A CE2 1 
ATOM   3590 C  CZ  . PHE A 1 444 ? 5.501   -13.033 18.943  1.00 34.45  ? 444 PHE A CZ  1 
ATOM   3591 N  N   . VAL A 1 445 ? 6.260   -16.780 22.386  1.00 34.80  ? 445 VAL A N   1 
ATOM   3592 C  CA  . VAL A 1 445 ? 6.549   -16.122 23.656  1.00 36.19  ? 445 VAL A CA  1 
ATOM   3593 C  C   . VAL A 1 445 ? 7.464   -14.937 23.369  1.00 39.07  ? 445 VAL A C   1 
ATOM   3594 O  O   . VAL A 1 445 ? 8.271   -14.969 22.433  1.00 36.35  ? 445 VAL A O   1 
ATOM   3595 C  CB  . VAL A 1 445 ? 7.225   -17.084 24.665  1.00 36.74  ? 445 VAL A CB  1 
ATOM   3596 C  CG1 . VAL A 1 445 ? 6.273   -18.204 25.077  1.00 34.88  ? 445 VAL A CG1 1 
ATOM   3597 C  CG2 . VAL A 1 445 ? 8.525   -17.665 24.066  1.00 34.85  ? 445 VAL A CG2 1 
ATOM   3598 N  N   . VAL A 1 446 ? 7.329   -13.880 24.169  1.00 37.12  ? 446 VAL A N   1 
ATOM   3599 C  CA  . VAL A 1 446 ? 8.194   -12.709 24.079  1.00 37.13  ? 446 VAL A CA  1 
ATOM   3600 C  C   . VAL A 1 446 ? 8.430   -12.188 25.486  1.00 38.81  ? 446 VAL A C   1 
ATOM   3601 O  O   . VAL A 1 446 ? 7.770   -12.588 26.448  1.00 39.59  ? 446 VAL A O   1 
ATOM   3602 C  CB  . VAL A 1 446 ? 7.608   -11.573 23.207  1.00 39.14  ? 446 VAL A CB  1 
ATOM   3603 C  CG1 . VAL A 1 446 ? 7.379   -12.025 21.751  1.00 34.61  ? 446 VAL A CG1 1 
ATOM   3604 C  CG2 . VAL A 1 446 ? 6.342   -11.003 23.859  1.00 33.43  ? 446 VAL A CG2 1 
ATOM   3605 N  N   . LYS A 1 447 ? 9.372   -11.266 25.587  1.00 42.77  ? 447 LYS A N   1 
ATOM   3606 C  CA  . LYS A 1 447 ? 9.611   -10.520 26.806  1.00 37.15  ? 447 LYS A CA  1 
ATOM   3607 C  C   . LYS A 1 447 ? 9.210   -9.083  26.537  1.00 39.01  ? 447 LYS A C   1 
ATOM   3608 O  O   . LYS A 1 447 ? 9.457   -8.557  25.446  1.00 43.02  ? 447 LYS A O   1 
ATOM   3609 C  CB  . LYS A 1 447 ? 11.089  -10.604 27.210  1.00 37.00  ? 447 LYS A CB  1 
ATOM   3610 C  CG  . LYS A 1 447 ? 11.370  -11.629 28.272  1.00 44.73  ? 447 LYS A CG  1 
ATOM   3611 C  CD  . LYS A 1 447 ? 12.847  -11.610 28.654  1.00 51.27  ? 447 LYS A CD  1 
ATOM   3612 C  CE  . LYS A 1 447 ? 13.125  -12.500 29.850  1.00 60.10  ? 447 LYS A CE  1 
ATOM   3613 N  NZ  . LYS A 1 447 ? 13.282  -13.909 29.387  1.00 56.29  ? 447 LYS A NZ  1 
ATOM   3614 N  N   . ALA A 1 448 ? 8.552   -8.460  27.506  1.00 37.71  ? 448 ALA A N   1 
ATOM   3615 C  CA  . ALA A 1 448 ? 8.205   -7.051  27.428  1.00 40.64  ? 448 ALA A CA  1 
ATOM   3616 C  C   . ALA A 1 448 ? 9.025   -6.283  28.452  1.00 47.54  ? 448 ALA A C   1 
ATOM   3617 O  O   . ALA A 1 448 ? 9.148   -6.710  29.605  1.00 51.52  ? 448 ALA A O   1 
ATOM   3618 C  CB  . ALA A 1 448 ? 6.712   -6.826  27.669  1.00 44.78  ? 448 ALA A CB  1 
ATOM   3619 N  N   . LYS A 1 449 ? 9.597   -5.170  28.017  1.00 44.14  ? 449 LYS A N   1 
ATOM   3620 C  CA  . LYS A 1 449 ? 10.319  -4.232  28.864  1.00 45.04  ? 449 LYS A CA  1 
ATOM   3621 C  C   . LYS A 1 449 ? 9.436   -2.998  28.996  1.00 41.80  ? 449 LYS A C   1 
ATOM   3622 O  O   . LYS A 1 449 ? 9.193   -2.297  28.011  1.00 42.78  ? 449 LYS A O   1 
ATOM   3623 C  CB  . LYS A 1 449 ? 11.670  -3.891  28.236  1.00 47.57  ? 449 LYS A CB  1 
ATOM   3624 C  CG  . LYS A 1 449 ? 12.887  -4.428  28.964  1.00 61.35  ? 449 LYS A CG  1 
ATOM   3625 C  CD  . LYS A 1 449 ? 13.333  -3.477  30.070  1.00 62.17  ? 449 LYS A CD  1 
ATOM   3626 C  CE  . LYS A 1 449 ? 14.289  -4.153  31.046  1.00 70.60  ? 449 LYS A CE  1 
ATOM   3627 N  NZ  . LYS A 1 449 ? 14.239  -3.534  32.409  1.00 78.98  ? 449 LYS A NZ  1 
ATOM   3628 N  N   . SER A 1 450 ? 8.947   -2.733  30.200  1.00 41.48  ? 450 SER A N   1 
ATOM   3629 C  CA  . SER A 1 450 ? 8.022   -1.625  30.369  1.00 42.23  ? 450 SER A CA  1 
ATOM   3630 C  C   . SER A 1 450 ? 8.704   -0.297  30.045  1.00 44.65  ? 450 SER A C   1 
ATOM   3631 O  O   . SER A 1 450 ? 9.847   -0.055  30.430  1.00 44.58  ? 450 SER A O   1 
ATOM   3632 C  CB  . SER A 1 450 ? 7.478   -1.612  31.803  1.00 38.95  ? 450 SER A CB  1 
ATOM   3633 O  OG  . SER A 1 450 ? 6.649   -0.482  32.027  1.00 42.25  ? 450 SER A OG  1 
ATOM   3634 N  N   . LYS A 1 451 ? 8.001   0.563   29.312  1.00 39.57  ? 451 LYS A N   1 
ATOM   3635 C  CA  . LYS A 1 451 ? 8.406   1.957   29.196  1.00 43.12  ? 451 LYS A CA  1 
ATOM   3636 C  C   . LYS A 1 451 ? 8.034   2.770   30.431  1.00 46.91  ? 451 LYS A C   1 
ATOM   3637 O  O   . LYS A 1 451 ? 8.345   3.963   30.493  1.00 44.69  ? 451 LYS A O   1 
ATOM   3638 C  CB  . LYS A 1 451 ? 7.780   2.588   27.951  1.00 44.55  ? 451 LYS A CB  1 
ATOM   3639 C  CG  . LYS A 1 451 ? 8.316   2.009   26.651  1.00 43.78  ? 451 LYS A CG  1 
ATOM   3640 C  CD  . LYS A 1 451 ? 7.664   2.687   25.452  1.00 42.46  ? 451 LYS A CD  1 
ATOM   3641 C  CE  . LYS A 1 451 ? 8.111   2.050   24.158  1.00 41.52  ? 451 LYS A CE  1 
ATOM   3642 N  NZ  . LYS A 1 451 ? 9.469   2.539   23.777  1.00 48.66  ? 451 LYS A NZ  1 
ATOM   3643 N  N   . LYS A 1 452 ? 7.372   2.147   31.404  1.00 44.67  ? 452 LYS A N   1 
ATOM   3644 C  CA  . LYS A 1 452 ? 7.044   2.776   32.676  1.00 47.02  ? 452 LYS A CA  1 
ATOM   3645 C  C   . LYS A 1 452 ? 6.201   4.028   32.461  1.00 53.21  ? 452 LYS A C   1 
ATOM   3646 O  O   . LYS A 1 452 ? 6.435   5.077   33.067  1.00 53.62  ? 452 LYS A O   1 
ATOM   3647 C  CB  . LYS A 1 452 ? 8.312   3.089   33.471  1.00 51.69  ? 452 LYS A CB  1 
ATOM   3648 C  CG  . LYS A 1 452 ? 8.714   1.984   34.435  1.00 53.15  ? 452 LYS A CG  1 
ATOM   3649 C  CD  . LYS A 1 452 ? 10.228  1.820   34.496  1.00 61.73  ? 452 LYS A CD  1 
ATOM   3650 C  CE  . LYS A 1 452 ? 10.638  0.560   35.265  1.00 67.14  ? 452 LYS A CE  1 
ATOM   3651 N  NZ  . LYS A 1 452 ? 11.965  0.022   34.821  1.00 77.01  ? 452 LYS A NZ  1 
ATOM   3652 N  N   . ILE A 1 453 ? 5.204   3.919   31.593  1.00 48.00  ? 453 ILE A N   1 
ATOM   3653 C  CA  . ILE A 1 453 ? 4.300   5.024   31.294  1.00 42.32  ? 453 ILE A CA  1 
ATOM   3654 C  C   . ILE A 1 453 ? 2.993   4.762   32.037  1.00 47.66  ? 453 ILE A C   1 
ATOM   3655 O  O   . ILE A 1 453 ? 2.375   3.709   31.817  1.00 46.90  ? 453 ILE A O   1 
ATOM   3656 C  CB  . ILE A 1 453 ? 4.059   5.152   29.785  1.00 46.76  ? 453 ILE A CB  1 
ATOM   3657 C  CG1 . ILE A 1 453 ? 5.372   5.532   29.080  1.00 45.10  ? 453 ILE A CG1 1 
ATOM   3658 C  CG2 . ILE A 1 453 ? 2.994   6.213   29.531  1.00 44.20  ? 453 ILE A CG2 1 
ATOM   3659 C  CD1 . ILE A 1 453 ? 5.240   5.735   27.577  1.00 44.45  ? 453 ILE A CD1 1 
ATOM   3660 N  N   . PRO A 1 454 ? 2.540   5.670   32.906  1.00 50.19  ? 454 PRO A N   1 
ATOM   3661 C  CA  . PRO A 1 454 ? 1.394   5.365   33.775  1.00 48.66  ? 454 PRO A CA  1 
ATOM   3662 C  C   . PRO A 1 454 ? 0.086   5.231   33.012  1.00 48.50  ? 454 PRO A C   1 
ATOM   3663 O  O   . PRO A 1 454 ? -0.127  5.860   31.971  1.00 49.55  ? 454 PRO A O   1 
ATOM   3664 C  CB  . PRO A 1 454 ? 1.341   6.565   34.735  1.00 52.18  ? 454 PRO A CB  1 
ATOM   3665 C  CG  . PRO A 1 454 ? 2.664   7.252   34.605  1.00 52.99  ? 454 PRO A CG  1 
ATOM   3666 C  CD  . PRO A 1 454 ? 3.149   6.976   33.218  1.00 51.38  ? 454 PRO A CD  1 
ATOM   3667 N  N   . LEU A 1 455 ? -0.811  4.415   33.567  1.00 43.86  ? 455 LEU A N   1 
ATOM   3668 C  CA  . LEU A 1 455 ? -2.152  4.250   33.003  1.00 48.79  ? 455 LEU A CA  1 
ATOM   3669 C  C   . LEU A 1 455 ? -3.151  5.158   33.727  1.00 54.08  ? 455 LEU A C   1 
ATOM   3670 O  O   . LEU A 1 455 ? -2.802  5.848   34.688  1.00 54.71  ? 455 LEU A O   1 
ATOM   3671 C  CB  . LEU A 1 455 ? -2.611  2.795   33.100  1.00 50.27  ? 455 LEU A CB  1 
ATOM   3672 C  CG  . LEU A 1 455 ? -1.966  1.753   32.186  1.00 44.57  ? 455 LEU A CG  1 
ATOM   3673 C  CD1 . LEU A 1 455 ? -2.185  0.370   32.784  1.00 42.56  ? 455 LEU A CD1 1 
ATOM   3674 C  CD2 . LEU A 1 455 ? -2.525  1.833   30.785  1.00 43.67  ? 455 LEU A CD2 1 
ATOM   3675 O  OXT . LEU A 1 455 ? -4.335  5.227   33.388  1.00 53.75  ? 455 LEU A OXT 1 
ATOM   3676 N  N   . THR B 1 1   ? 2.442   -23.380 99.318  1.00 76.81  ? 1   THR B N   1 
ATOM   3677 C  CA  . THR B 1 1   ? 1.069   -23.820 99.072  1.00 79.97  ? 1   THR B CA  1 
ATOM   3678 C  C   . THR B 1 1   ? 0.983   -24.625 97.771  1.00 73.66  ? 1   THR B C   1 
ATOM   3679 O  O   . THR B 1 1   ? 0.106   -24.399 96.925  1.00 70.04  ? 1   THR B O   1 
ATOM   3680 C  CB  . THR B 1 1   ? 0.093   -22.617 99.029  1.00 80.84  ? 1   THR B CB  1 
ATOM   3681 O  OG1 . THR B 1 1   ? -1.225  -23.074 98.697  1.00 83.23  ? 1   THR B OG1 1 
ATOM   3682 C  CG2 . THR B 1 1   ? 0.556   -21.560 98.024  1.00 72.11  ? 1   THR B CG2 1 
ATOM   3683 N  N   . ILE B 1 2   ? 1.887   -25.596 97.657  1.00 71.00  ? 2   ILE B N   1 
ATOM   3684 C  CA  . ILE B 1 2   ? 2.157   -26.284 96.397  1.00 67.72  ? 2   ILE B CA  1 
ATOM   3685 C  C   . ILE B 1 2   ? 0.977   -27.171 96.013  1.00 69.86  ? 2   ILE B C   1 
ATOM   3686 O  O   . ILE B 1 2   ? 0.645   -28.132 96.718  1.00 71.69  ? 2   ILE B O   1 
ATOM   3687 C  CB  . ILE B 1 2   ? 3.458   -27.092 96.500  1.00 68.28  ? 2   ILE B CB  1 
ATOM   3688 C  CG1 . ILE B 1 2   ? 4.614   -26.191 96.978  1.00 68.41  ? 2   ILE B CG1 1 
ATOM   3689 C  CG2 . ILE B 1 2   ? 3.772   -27.788 95.181  1.00 68.85  ? 2   ILE B CG2 1 
ATOM   3690 C  CD1 . ILE B 1 2   ? 4.486   -24.712 96.574  1.00 67.69  ? 2   ILE B CD1 1 
ATOM   3691 N  N   . LYS B 1 3   ? 0.352   -26.859 94.875  1.00 67.86  ? 3   LYS B N   1 
ATOM   3692 C  CA  . LYS B 1 3   ? -0.773  -27.589 94.297  1.00 65.99  ? 3   LYS B CA  1 
ATOM   3693 C  C   . LYS B 1 3   ? -0.302  -28.653 93.301  1.00 63.42  ? 3   LYS B C   1 
ATOM   3694 O  O   . LYS B 1 3   ? 0.792   -28.573 92.731  1.00 60.71  ? 3   LYS B O   1 
ATOM   3695 C  CB  . LYS B 1 3   ? -1.728  -26.631 93.572  1.00 61.05  ? 3   LYS B CB  1 
ATOM   3696 C  CG  . LYS B 1 3   ? -2.982  -26.209 94.322  1.00 63.22  ? 3   LYS B CG  1 
ATOM   3697 C  CD  . LYS B 1 3   ? -3.350  -24.778 93.941  1.00 63.48  ? 3   LYS B CD  1 
ATOM   3698 C  CE  . LYS B 1 3   ? -4.787  -24.419 94.297  1.00 68.24  ? 3   LYS B CE  1 
ATOM   3699 N  NZ  . LYS B 1 3   ? -5.760  -25.071 93.365  1.00 66.78  ? 3   LYS B NZ  1 
ATOM   3700 N  N   . GLU B 1 4   ? -1.171  -29.637 93.075  1.00 61.15  ? 4   GLU B N   1 
ATOM   3701 C  CA  . GLU B 1 4   ? -0.999  -30.658 92.049  1.00 58.83  ? 4   GLU B CA  1 
ATOM   3702 C  C   . GLU B 1 4   ? -1.921  -30.381 90.865  1.00 53.03  ? 4   GLU B C   1 
ATOM   3703 O  O   . GLU B 1 4   ? -3.073  -29.959 91.030  1.00 49.80  ? 4   GLU B O   1 
ATOM   3704 C  CB  . GLU B 1 4   ? -1.269  -32.058 92.609  1.00 60.11  ? 4   GLU B CB  1 
ATOM   3705 C  CG  . GLU B 1 4   ? -2.719  -32.299 93.000  1.00 65.86  ? 4   GLU B CG  1 
ATOM   3706 C  CD  . GLU B 1 4   ? -3.135  -31.514 94.243  1.00 73.06  ? 4   GLU B CD  1 
ATOM   3707 O  OE1 . GLU B 1 4   ? -4.298  -31.659 94.676  1.00 77.39  ? 4   GLU B OE1 1 
ATOM   3708 O  OE2 . GLU B 1 4   ? -2.304  -30.748 94.783  1.00 73.35  ? 4   GLU B OE2 1 
ATOM   3709 N  N   . MET B 1 5   ? -1.427  -30.644 89.705  1.00 47.11  ? 5   MET B N   1 
ATOM   3710 C  CA  . MET B 1 5   ? -1.983  -30.073 88.494  1.00 44.86  ? 5   MET B CA  1 
ATOM   3711 C  C   . MET B 1 5   ? -2.854  -31.097 87.770  1.00 41.05  ? 5   MET B C   1 
ATOM   3712 O  O   . MET B 1 5   ? -2.471  -32.274 87.657  1.00 39.67  ? 5   MET B O   1 
ATOM   3713 C  CB  . MET B 1 5   ? -0.821  -29.595 87.623  1.00 45.99  ? 5   MET B CB  1 
ATOM   3714 C  CG  . MET B 1 5   ? -1.025  -29.419 86.175  1.00 44.85  ? 5   MET B CG  1 
ATOM   3715 S  SD  . MET B 1 5   ? 0.583   -28.949 85.493  1.00 41.31  ? 5   MET B SD  1 
ATOM   3716 C  CE  . MET B 1 5   ? 1.367   -28.104 86.848  1.00 40.58  ? 5   MET B CE  1 
ATOM   3717 N  N   . PRO B 1 6   ? -4.051  -30.730 87.322  1.00 39.87  ? 6   PRO B N   1 
ATOM   3718 C  CA  . PRO B 1 6   ? -4.911  -31.704 86.640  1.00 40.77  ? 6   PRO B CA  1 
ATOM   3719 C  C   . PRO B 1 6   ? -4.301  -32.132 85.310  1.00 36.19  ? 6   PRO B C   1 
ATOM   3720 O  O   . PRO B 1 6   ? -3.383  -31.511 84.774  1.00 37.34  ? 6   PRO B O   1 
ATOM   3721 C  CB  . PRO B 1 6   ? -6.228  -30.955 86.436  1.00 35.59  ? 6   PRO B CB  1 
ATOM   3722 C  CG  . PRO B 1 6   ? -5.867  -29.528 86.519  1.00 40.67  ? 6   PRO B CG  1 
ATOM   3723 C  CD  . PRO B 1 6   ? -4.680  -29.407 87.429  1.00 37.91  ? 6   PRO B CD  1 
ATOM   3724 N  N   . GLN B 1 7   ? -4.813  -33.240 84.795  1.00 36.92  ? 7   GLN B N   1 
ATOM   3725 C  CA  . GLN B 1 7   ? -4.317  -33.810 83.559  1.00 38.92  ? 7   GLN B CA  1 
ATOM   3726 C  C   . GLN B 1 7   ? -5.505  -34.442 82.853  1.00 39.54  ? 7   GLN B C   1 
ATOM   3727 O  O   . GLN B 1 7   ? -6.354  -35.061 83.522  1.00 35.47  ? 7   GLN B O   1 
ATOM   3728 C  CB  . GLN B 1 7   ? -3.242  -34.861 83.811  1.00 36.47  ? 7   GLN B CB  1 
ATOM   3729 C  CG  . GLN B 1 7   ? -2.726  -35.570 82.572  1.00 38.76  ? 7   GLN B CG  1 
ATOM   3730 C  CD  . GLN B 1 7   ? -1.613  -36.527 82.943  1.00 44.64  ? 7   GLN B CD  1 
ATOM   3731 O  OE1 . GLN B 1 7   ? -1.400  -36.790 84.125  1.00 48.39  ? 7   GLN B OE1 1 
ATOM   3732 N  NE2 . GLN B 1 7   ? -0.887  -37.034 81.950  1.00 35.77  ? 7   GLN B NE2 1 
ATOM   3733 N  N   . PRO B 1 8   ? -5.596  -34.297 81.527  1.00 33.53  ? 8   PRO B N   1 
ATOM   3734 C  CA  . PRO B 1 8   ? -6.687  -34.923 80.764  1.00 37.60  ? 8   PRO B CA  1 
ATOM   3735 C  C   . PRO B 1 8   ? -6.550  -36.439 80.613  1.00 34.50  ? 8   PRO B C   1 
ATOM   3736 O  O   . PRO B 1 8   ? -5.565  -37.048 81.048  1.00 32.75  ? 8   PRO B O   1 
ATOM   3737 C  CB  . PRO B 1 8   ? -6.594  -34.227 79.402  1.00 35.55  ? 8   PRO B CB  1 
ATOM   3738 C  CG  . PRO B 1 8   ? -5.144  -33.867 79.276  1.00 35.94  ? 8   PRO B CG  1 
ATOM   3739 C  CD  . PRO B 1 8   ? -4.719  -33.469 80.672  1.00 35.96  ? 8   PRO B CD  1 
ATOM   3740 N  N   . LYS B 1 9   ? -7.537  -37.057 79.981  1.00 35.94  ? 9   LYS B N   1 
ATOM   3741 C  CA  . LYS B 1 9   ? -7.595  -38.514 79.935  1.00 33.60  ? 9   LYS B CA  1 
ATOM   3742 C  C   . LYS B 1 9   ? -6.384  -39.098 79.213  1.00 39.63  ? 9   LYS B C   1 
ATOM   3743 O  O   . LYS B 1 9   ? -5.827  -38.503 78.283  1.00 36.36  ? 9   LYS B O   1 
ATOM   3744 C  CB  . LYS B 1 9   ? -8.884  -38.978 79.256  1.00 35.38  ? 9   LYS B CB  1 
ATOM   3745 C  CG  . LYS B 1 9   ? -9.059  -38.485 77.828  1.00 37.48  ? 9   LYS B CG  1 
ATOM   3746 C  CD  . LYS B 1 9   ? -10.462 -38.765 77.300  1.00 37.08  ? 9   LYS B CD  1 
ATOM   3747 C  CE  . LYS B 1 9   ? -10.552 -38.440 75.819  1.00 43.88  ? 9   LYS B CE  1 
ATOM   3748 N  NZ  . LYS B 1 9   ? -11.945 -38.119 75.418  1.00 45.67  ? 9   LYS B NZ  1 
ATOM   3749 N  N   . THR B 1 10  ? -5.995  -40.296 79.637  1.00 34.76  ? 10  THR B N   1 
ATOM   3750 C  CA  . THR B 1 10  ? -4.811  -40.972 79.132  1.00 33.70  ? 10  THR B CA  1 
ATOM   3751 C  C   . THR B 1 10  ? -5.153  -42.238 78.353  1.00 37.17  ? 10  THR B C   1 
ATOM   3752 O  O   . THR B 1 10  ? -6.275  -42.775 78.402  1.00 35.12  ? 10  THR B O   1 
ATOM   3753 C  CB  . THR B 1 10  ? -3.858  -41.292 80.291  1.00 37.92  ? 10  THR B CB  1 
ATOM   3754 O  OG1 . THR B 1 10  ? -4.496  -42.236 81.166  1.00 38.68  ? 10  THR B OG1 1 
ATOM   3755 C  CG2 . THR B 1 10  ? -3.458  -40.021 81.048  1.00 38.00  ? 10  THR B CG2 1 
ATOM   3756 N  N   . PHE B 1 11  ? -4.139  -42.710 77.624  1.00 34.70  ? 11  PHE B N   1 
ATOM   3757 C  CA  . PHE B 1 11  ? -4.266  -43.787 76.647  1.00 34.24  ? 11  PHE B CA  1 
ATOM   3758 C  C   . PHE B 1 11  ? -3.151  -44.812 76.891  1.00 38.63  ? 11  PHE B C   1 
ATOM   3759 O  O   . PHE B 1 11  ? -2.372  -45.143 76.000  1.00 37.62  ? 11  PHE B O   1 
ATOM   3760 C  CB  . PHE B 1 11  ? -4.166  -43.254 75.210  1.00 34.36  ? 11  PHE B CB  1 
ATOM   3761 C  CG  . PHE B 1 11  ? -5.330  -42.391 74.798  1.00 34.25  ? 11  PHE B CG  1 
ATOM   3762 C  CD1 . PHE B 1 11  ? -5.442  -41.086 75.284  1.00 33.73  ? 11  PHE B CD1 1 
ATOM   3763 C  CD2 . PHE B 1 11  ? -6.330  -42.883 73.981  1.00 37.60  ? 11  PHE B CD2 1 
ATOM   3764 C  CE1 . PHE B 1 11  ? -6.516  -40.277 74.921  1.00 33.85  ? 11  PHE B CE1 1 
ATOM   3765 C  CE2 . PHE B 1 11  ? -7.424  -42.080 73.613  1.00 37.97  ? 11  PHE B CE2 1 
ATOM   3766 C  CZ  . PHE B 1 11  ? -7.511  -40.780 74.083  1.00 35.19  ? 11  PHE B CZ  1 
ATOM   3767 N  N   . GLY B 1 12  ? -3.063  -45.308 78.117  1.00 38.28  ? 12  GLY B N   1 
ATOM   3768 C  CA  . GLY B 1 12  ? -2.015  -46.268 78.433  1.00 37.24  ? 12  GLY B CA  1 
ATOM   3769 C  C   . GLY B 1 12  ? -0.635  -45.654 78.231  1.00 42.37  ? 12  GLY B C   1 
ATOM   3770 O  O   . GLY B 1 12  ? -0.365  -44.514 78.638  1.00 41.81  ? 12  GLY B O   1 
ATOM   3771 N  N   . GLU B 1 13  ? 0.257   -46.409 77.580  1.00 42.96  ? 13  GLU B N   1 
ATOM   3772 C  CA  . GLU B 1 13  ? 1.627   -45.937 77.380  1.00 47.17  ? 13  GLU B CA  1 
ATOM   3773 C  C   . GLU B 1 13  ? 1.735   -44.775 76.406  1.00 41.80  ? 13  GLU B C   1 
ATOM   3774 O  O   . GLU B 1 13  ? 2.803   -44.156 76.336  1.00 41.97  ? 13  GLU B O   1 
ATOM   3775 C  CB  . GLU B 1 13  ? 2.532   -47.086 76.924  1.00 46.29  ? 13  GLU B CB  1 
ATOM   3776 C  CG  . GLU B 1 13  ? 2.733   -48.141 78.002  1.00 54.00  ? 13  GLU B CG  1 
ATOM   3777 C  CD  . GLU B 1 13  ? 3.213   -47.519 79.312  1.00 59.75  ? 13  GLU B CD  1 
ATOM   3778 O  OE1 . GLU B 1 13  ? 4.444   -47.374 79.483  1.00 67.97  ? 13  GLU B OE1 1 
ATOM   3779 O  OE2 . GLU B 1 13  ? 2.369   -47.157 80.167  1.00 63.57  ? 13  GLU B OE2 1 
ATOM   3780 N  N   . LEU B 1 14  ? 0.683   -44.463 75.654  1.00 36.35  ? 14  LEU B N   1 
ATOM   3781 C  CA  . LEU B 1 14  ? 0.711   -43.269 74.814  1.00 40.56  ? 14  LEU B CA  1 
ATOM   3782 C  C   . LEU B 1 14  ? 0.342   -41.999 75.585  1.00 38.76  ? 14  LEU B C   1 
ATOM   3783 O  O   . LEU B 1 14  ? 0.395   -40.900 75.010  1.00 39.31  ? 14  LEU B O   1 
ATOM   3784 C  CB  . LEU B 1 14  ? -0.211  -43.463 73.607  1.00 36.49  ? 14  LEU B CB  1 
ATOM   3785 C  CG  . LEU B 1 14  ? 0.198   -44.535 72.584  1.00 39.13  ? 14  LEU B CG  1 
ATOM   3786 C  CD1 . LEU B 1 14  ? -0.913  -44.740 71.582  1.00 44.94  ? 14  LEU B CD1 1 
ATOM   3787 C  CD2 . LEU B 1 14  ? 1.493   -44.167 71.854  1.00 38.99  ? 14  LEU B CD2 1 
ATOM   3788 N  N   . LYS B 1 15  ? 0.023   -42.119 76.871  1.00 36.34  ? 15  LYS B N   1 
ATOM   3789 C  CA  . LYS B 1 15  ? -0.220  -40.979 77.764  1.00 38.87  ? 15  LYS B CA  1 
ATOM   3790 C  C   . LYS B 1 15  ? -1.330  -40.124 77.154  1.00 38.91  ? 15  LYS B C   1 
ATOM   3791 O  O   . LYS B 1 15  ? -2.397  -40.662 76.817  1.00 38.83  ? 15  LYS B O   1 
ATOM   3792 C  CB  . LYS B 1 15  ? 1.104   -40.256 78.018  1.00 42.98  ? 15  LYS B CB  1 
ATOM   3793 C  CG  . LYS B 1 15  ? 2.318   -41.154 78.353  1.00 44.59  ? 15  LYS B CG  1 
ATOM   3794 C  CD  . LYS B 1 15  ? 3.048   -40.608 79.566  1.00 47.69  ? 15  LYS B CD  1 
ATOM   3795 C  CE  . LYS B 1 15  ? 4.536   -40.932 79.588  1.00 56.16  ? 15  LYS B CE  1 
ATOM   3796 N  NZ  . LYS B 1 15  ? 4.843   -42.100 80.454  1.00 60.85  ? 15  LYS B NZ  1 
ATOM   3797 N  N   . ASN B 1 16  ? -1.142  -38.813 77.007  1.00 36.50  ? 16  ASN B N   1 
ATOM   3798 C  CA  . ASN B 1 16  ? -2.150  -37.946 76.410  1.00 35.83  ? 16  ASN B CA  1 
ATOM   3799 C  C   . ASN B 1 16  ? -2.001  -37.784 74.899  1.00 37.46  ? 16  ASN B C   1 
ATOM   3800 O  O   . ASN B 1 16  ? -2.839  -37.114 74.280  1.00 36.94  ? 16  ASN B O   1 
ATOM   3801 C  CB  . ASN B 1 16  ? -2.095  -36.558 77.058  1.00 34.64  ? 16  ASN B CB  1 
ATOM   3802 C  CG  . ASN B 1 16  ? -2.330  -36.595 78.552  1.00 37.73  ? 16  ASN B CG  1 
ATOM   3803 O  OD1 . ASN B 1 16  ? -1.494  -36.141 79.338  1.00 33.90  ? 16  ASN B OD1 1 
ATOM   3804 N  ND2 . ASN B 1 16  ? -3.470  -37.149 78.958  1.00 35.53  ? 16  ASN B ND2 1 
ATOM   3805 N  N   . LEU B 1 17  ? -0.955  -38.335 74.288  1.00 36.83  ? 17  LEU B N   1 
ATOM   3806 C  CA  . LEU B 1 17  ? -0.678  -38.030 72.882  1.00 35.72  ? 17  LEU B CA  1 
ATOM   3807 C  C   . LEU B 1 17  ? -1.871  -38.238 71.942  1.00 37.11  ? 17  LEU B C   1 
ATOM   3808 O  O   . LEU B 1 17  ? -2.053  -37.418 71.026  1.00 36.15  ? 17  LEU B O   1 
ATOM   3809 C  CB  . LEU B 1 17  ? 0.523   -38.858 72.400  1.00 36.64  ? 17  LEU B CB  1 
ATOM   3810 C  CG  . LEU B 1 17  ? 0.962   -38.549 70.956  1.00 41.62  ? 17  LEU B CG  1 
ATOM   3811 C  CD1 . LEU B 1 17  ? 1.262   -37.056 70.767  1.00 43.79  ? 17  LEU B CD1 1 
ATOM   3812 C  CD2 . LEU B 1 17  ? 2.160   -39.407 70.545  1.00 45.87  ? 17  LEU B CD2 1 
ATOM   3813 N  N   . PRO B 1 18  ? -2.697  -39.274 72.083  1.00 37.72  ? 18  PRO B N   1 
ATOM   3814 C  CA  . PRO B 1 18  ? -3.812  -39.442 71.131  1.00 32.17  ? 18  PRO B CA  1 
ATOM   3815 C  C   . PRO B 1 18  ? -4.856  -38.339 71.200  1.00 35.18  ? 18  PRO B C   1 
ATOM   3816 O  O   . PRO B 1 18  ? -5.670  -38.222 70.271  1.00 35.08  ? 18  PRO B O   1 
ATOM   3817 C  CB  . PRO B 1 18  ? -4.406  -40.806 71.520  1.00 35.55  ? 18  PRO B CB  1 
ATOM   3818 C  CG  . PRO B 1 18  ? -3.289  -41.512 72.225  1.00 34.72  ? 18  PRO B CG  1 
ATOM   3819 C  CD  . PRO B 1 18  ? -2.575  -40.431 72.989  1.00 35.77  ? 18  PRO B CD  1 
ATOM   3820 N  N   . LEU B 1 19  ? -4.861  -37.514 72.250  1.00 33.68  ? 19  LEU B N   1 
ATOM   3821 C  CA  . LEU B 1 19  ? -5.750  -36.354 72.262  1.00 35.38  ? 19  LEU B CA  1 
ATOM   3822 C  C   . LEU B 1 19  ? -5.465  -35.417 71.092  1.00 38.83  ? 19  LEU B C   1 
ATOM   3823 O  O   . LEU B 1 19  ? -6.351  -34.669 70.655  1.00 34.97  ? 19  LEU B O   1 
ATOM   3824 C  CB  . LEU B 1 19  ? -5.620  -35.604 73.596  1.00 35.29  ? 19  LEU B CB  1 
ATOM   3825 C  CG  . LEU B 1 19  ? -6.116  -36.379 74.814  1.00 34.94  ? 19  LEU B CG  1 
ATOM   3826 C  CD1 . LEU B 1 19  ? -5.854  -35.594 76.074  1.00 33.22  ? 19  LEU B CD1 1 
ATOM   3827 C  CD2 . LEU B 1 19  ? -7.599  -36.681 74.644  1.00 34.36  ? 19  LEU B CD2 1 
ATOM   3828 N  N   . LEU B 1 20  ? -4.242  -35.428 70.576  1.00 36.09  ? 20  LEU B N   1 
ATOM   3829 C  CA  . LEU B 1 20  ? -3.908  -34.569 69.450  1.00 35.91  ? 20  LEU B CA  1 
ATOM   3830 C  C   . LEU B 1 20  ? -4.075  -35.257 68.113  1.00 36.05  ? 20  LEU B C   1 
ATOM   3831 O  O   . LEU B 1 20  ? -3.800  -34.639 67.080  1.00 38.18  ? 20  LEU B O   1 
ATOM   3832 C  CB  . LEU B 1 20  ? -2.475  -34.040 69.581  1.00 37.70  ? 20  LEU B CB  1 
ATOM   3833 C  CG  . LEU B 1 20  ? -2.154  -33.342 70.901  1.00 36.98  ? 20  LEU B CG  1 
ATOM   3834 C  CD1 . LEU B 1 20  ? -0.806  -32.715 70.825  1.00 43.14  ? 20  LEU B CD1 1 
ATOM   3835 C  CD2 . LEU B 1 20  ? -3.198  -32.282 71.193  1.00 39.31  ? 20  LEU B CD2 1 
ATOM   3836 N  N   . ASN B 1 21  ? -4.521  -36.514 68.098  1.00 34.30  ? 21  ASN B N   1 
ATOM   3837 C  CA  . ASN B 1 21  ? -4.800  -37.208 66.837  1.00 36.36  ? 21  ASN B CA  1 
ATOM   3838 C  C   . ASN B 1 21  ? -6.178  -36.775 66.326  1.00 40.92  ? 21  ASN B C   1 
ATOM   3839 O  O   . ASN B 1 21  ? -7.160  -37.520 66.335  1.00 38.37  ? 21  ASN B O   1 
ATOM   3840 C  CB  . ASN B 1 21  ? -4.705  -38.717 67.023  1.00 37.02  ? 21  ASN B CB  1 
ATOM   3841 C  CG  . ASN B 1 21  ? -4.851  -39.476 65.717  1.00 48.53  ? 21  ASN B CG  1 
ATOM   3842 O  OD1 . ASN B 1 21  ? -4.818  -38.889 64.633  1.00 47.54  ? 21  ASN B OD1 1 
ATOM   3843 N  ND2 . ASN B 1 21  ? -4.991  -40.795 65.814  1.00 53.36  ? 21  ASN B ND2 1 
ATOM   3844 N  N   . THR B 1 22  ? -6.231  -35.525 65.876  1.00 38.47  ? 22  THR B N   1 
ATOM   3845 C  CA  . THR B 1 22  ? -7.451  -34.904 65.368  1.00 37.37  ? 22  THR B CA  1 
ATOM   3846 C  C   . THR B 1 22  ? -7.037  -33.780 64.431  1.00 38.01  ? 22  THR B C   1 
ATOM   3847 O  O   . THR B 1 22  ? -5.910  -33.288 64.491  1.00 38.19  ? 22  THR B O   1 
ATOM   3848 C  CB  . THR B 1 22  ? -8.332  -34.345 66.488  1.00 41.25  ? 22  THR B CB  1 
ATOM   3849 O  OG1 . THR B 1 22  ? -9.363  -33.528 65.907  1.00 44.14  ? 22  THR B OG1 1 
ATOM   3850 C  CG2 . THR B 1 22  ? -7.490  -33.474 67.460  1.00 37.25  ? 22  THR B CG2 1 
ATOM   3851 N  N   . ASP B 1 23  ? -7.952  -33.378 63.551  1.00 41.17  ? 23  ASP B N   1 
ATOM   3852 C  CA  . ASP B 1 23  ? -7.588  -32.289 62.653  1.00 42.38  ? 23  ASP B CA  1 
ATOM   3853 C  C   . ASP B 1 23  ? -7.681  -30.918 63.311  1.00 36.75  ? 23  ASP B C   1 
ATOM   3854 O  O   . ASP B 1 23  ? -7.253  -29.927 62.697  1.00 35.71  ? 23  ASP B O   1 
ATOM   3855 C  CB  . ASP B 1 23  ? -8.457  -32.288 61.392  1.00 45.11  ? 23  ASP B CB  1 
ATOM   3856 C  CG  . ASP B 1 23  ? -9.932  -32.301 61.705  1.00 48.40  ? 23  ASP B CG  1 
ATOM   3857 O  OD1 . ASP B 1 23  ? -10.299 -32.542 62.876  1.00 54.78  ? 23  ASP B OD1 1 
ATOM   3858 O  OD2 . ASP B 1 23  ? -10.730 -32.029 60.781  1.00 60.21  ? 23  ASP B OD2 1 
ATOM   3859 N  N   . LYS B 1 24  ? -8.241  -30.824 64.513  1.00 34.63  ? 24  LYS B N   1 
ATOM   3860 C  CA  . LYS B 1 24  ? -8.394  -29.548 65.219  1.00 36.16  ? 24  LYS B CA  1 
ATOM   3861 C  C   . LYS B 1 24  ? -7.827  -29.677 66.628  1.00 34.51  ? 24  LYS B C   1 
ATOM   3862 O  O   . LYS B 1 24  ? -8.555  -29.604 67.625  1.00 32.88  ? 24  LYS B O   1 
ATOM   3863 C  CB  . LYS B 1 24  ? -9.859  -29.106 65.224  1.00 36.26  ? 24  LYS B CB  1 
ATOM   3864 C  CG  . LYS B 1 24  ? -10.519 -29.245 63.853  1.00 37.54  ? 24  LYS B CG  1 
ATOM   3865 C  CD  . LYS B 1 24  ? -11.965 -28.755 63.861  1.00 37.60  ? 24  LYS B CD  1 
ATOM   3866 C  CE  . LYS B 1 24  ? -12.491 -28.436 62.455  1.00 38.44  ? 24  LYS B CE  1 
ATOM   3867 N  NZ  . LYS B 1 24  ? -13.888 -27.881 62.558  1.00 38.64  ? 24  LYS B NZ  1 
ATOM   3868 N  N   . PRO B 1 25  ? -6.511  -29.868 66.744  1.00 32.33  ? 25  PRO B N   1 
ATOM   3869 C  CA  . PRO B 1 25  ? -5.940  -30.093 68.084  1.00 32.17  ? 25  PRO B CA  1 
ATOM   3870 C  C   . PRO B 1 25  ? -5.983  -28.875 69.000  1.00 33.44  ? 25  PRO B C   1 
ATOM   3871 O  O   . PRO B 1 25  ? -6.182  -29.043 70.214  1.00 34.24  ? 25  PRO B O   1 
ATOM   3872 C  CB  . PRO B 1 25  ? -4.502  -30.545 67.779  1.00 33.75  ? 25  PRO B CB  1 
ATOM   3873 C  CG  . PRO B 1 25  ? -4.202  -29.991 66.413  1.00 32.92  ? 25  PRO B CG  1 
ATOM   3874 C  CD  . PRO B 1 25  ? -5.515  -30.030 65.667  1.00 33.02  ? 25  PRO B CD  1 
ATOM   3875 N  N   . VAL B 1 26  ? -5.783  -27.658 68.480  1.00 34.73  ? 26  VAL B N   1 
ATOM   3876 C  CA  . VAL B 1 26  ? -5.816  -26.491 69.365  1.00 30.78  ? 26  VAL B CA  1 
ATOM   3877 C  C   . VAL B 1 26  ? -7.219  -26.301 69.939  1.00 31.71  ? 26  VAL B C   1 
ATOM   3878 O  O   . VAL B 1 26  ? -7.388  -26.034 71.131  1.00 32.01  ? 26  VAL B O   1 
ATOM   3879 C  CB  . VAL B 1 26  ? -5.322  -25.227 68.635  1.00 35.43  ? 26  VAL B CB  1 
ATOM   3880 C  CG1 . VAL B 1 26  ? -5.576  -23.999 69.504  1.00 30.56  ? 26  VAL B CG1 1 
ATOM   3881 C  CG2 . VAL B 1 26  ? -3.807  -25.344 68.325  1.00 35.11  ? 26  VAL B CG2 1 
ATOM   3882 N  N   . GLN B 1 27  ? -8.246  -26.463 69.109  1.00 33.02  ? 27  GLN B N   1 
ATOM   3883 C  CA  . GLN B 1 27  ? -9.616  -26.384 69.608  1.00 32.73  ? 27  GLN B CA  1 
ATOM   3884 C  C   . GLN B 1 27  ? -9.920  -27.502 70.604  1.00 31.43  ? 27  GLN B C   1 
ATOM   3885 O  O   . GLN B 1 27  ? -10.671 -27.287 71.564  1.00 33.82  ? 27  GLN B O   1 
ATOM   3886 C  CB  . GLN B 1 27  ? -10.572 -26.414 68.412  1.00 31.86  ? 27  GLN B CB  1 
ATOM   3887 C  CG  . GLN B 1 27  ? -10.480 -25.133 67.577  1.00 35.07  ? 27  GLN B CG  1 
ATOM   3888 C  CD  . GLN B 1 27  ? -11.147 -25.247 66.210  1.00 34.83  ? 27  GLN B CD  1 
ATOM   3889 O  OE1 . GLN B 1 27  ? -12.361 -25.119 66.077  1.00 33.91  ? 27  GLN B OE1 1 
ATOM   3890 N  NE2 . GLN B 1 27  ? -10.341 -25.513 65.186  1.00 30.73  ? 27  GLN B NE2 1 
ATOM   3891 N  N   . ALA B 1 28  ? -9.337  -28.691 70.414  1.00 31.88  ? 28  ALA B N   1 
ATOM   3892 C  CA  . ALA B 1 28  ? -9.477  -29.734 71.427  1.00 33.34  ? 28  ALA B CA  1 
ATOM   3893 C  C   . ALA B 1 28  ? -8.837  -29.307 72.743  1.00 36.64  ? 28  ALA B C   1 
ATOM   3894 O  O   . ALA B 1 28  ? -9.396  -29.535 73.819  1.00 33.45  ? 28  ALA B O   1 
ATOM   3895 C  CB  . ALA B 1 28  ? -8.857  -31.044 70.932  1.00 34.14  ? 28  ALA B CB  1 
ATOM   3896 N  N   . LEU B 1 29  ? -7.653  -28.696 72.674  1.00 32.58  ? 29  LEU B N   1 
ATOM   3897 C  CA  . LEU B 1 29  ? -6.985  -28.236 73.886  1.00 31.67  ? 29  LEU B CA  1 
ATOM   3898 C  C   . LEU B 1 29  ? -7.781  -27.127 74.562  1.00 32.87  ? 29  LEU B C   1 
ATOM   3899 O  O   . LEU B 1 29  ? -7.846  -27.065 75.805  1.00 33.04  ? 29  LEU B O   1 
ATOM   3900 C  CB  . LEU B 1 29  ? -5.569  -27.769 73.543  1.00 30.00  ? 29  LEU B CB  1 
ATOM   3901 C  CG  . LEU B 1 29  ? -4.631  -28.904 73.179  1.00 32.65  ? 29  LEU B CG  1 
ATOM   3902 C  CD1 . LEU B 1 29  ? -3.466  -28.371 72.345  1.00 31.38  ? 29  LEU B CD1 1 
ATOM   3903 C  CD2 . LEU B 1 29  ? -4.152  -29.572 74.475  1.00 32.01  ? 29  LEU B CD2 1 
ATOM   3904 N  N   . MET B 1 30  ? -8.401  -26.244 73.769  1.00 32.17  ? 30  MET B N   1 
ATOM   3905 C  CA  . MET B 1 30  ? -9.287  -25.257 74.373  1.00 34.81  ? 30  MET B CA  1 
ATOM   3906 C  C   . MET B 1 30  ? -10.403 -25.913 75.159  1.00 35.35  ? 30  MET B C   1 
ATOM   3907 O  O   . MET B 1 30  ? -10.750 -25.452 76.251  1.00 33.63  ? 30  MET B O   1 
ATOM   3908 C  CB  . MET B 1 30  ? -9.868  -24.286 73.333  1.00 32.39  ? 30  MET B CB  1 
ATOM   3909 C  CG  . MET B 1 30  ? -8.827  -23.394 72.654  1.00 33.49  ? 30  MET B CG  1 
ATOM   3910 S  SD  . MET B 1 30  ? -9.468  -22.652 71.152  1.00 34.52  ? 30  MET B SD  1 
ATOM   3911 C  CE  . MET B 1 30  ? -10.747 -21.614 71.826  1.00 33.47  ? 30  MET B CE  1 
ATOM   3912 N  N   . LYS B 1 31  ? -10.981 -26.986 74.626  1.00 36.21  ? 31  LYS B N   1 
ATOM   3913 C  CA  . LYS B 1 31  ? -12.072 -27.621 75.357  1.00 37.21  ? 31  LYS B CA  1 
ATOM   3914 C  C   . LYS B 1 31  ? -11.558 -28.291 76.630  1.00 36.39  ? 31  LYS B C   1 
ATOM   3915 O  O   . LYS B 1 31  ? -12.219 -28.248 77.674  1.00 32.87  ? 31  LYS B O   1 
ATOM   3916 C  CB  . LYS B 1 31  ? -12.784 -28.608 74.438  1.00 39.93  ? 31  LYS B CB  1 
ATOM   3917 C  CG  . LYS B 1 31  ? -13.920 -27.936 73.698  1.00 49.06  ? 31  LYS B CG  1 
ATOM   3918 C  CD  . LYS B 1 31  ? -14.701 -28.884 72.797  1.00 52.87  ? 31  LYS B CD  1 
ATOM   3919 C  CE  . LYS B 1 31  ? -15.783 -28.109 72.075  1.00 56.87  ? 31  LYS B CE  1 
ATOM   3920 N  NZ  . LYS B 1 31  ? -15.341 -27.841 70.681  1.00 65.25  ? 31  LYS B NZ  1 
ATOM   3921 N  N   . ILE B 1 32  ? -10.374 -28.907 76.564  1.00 35.48  ? 32  ILE B N   1 
ATOM   3922 C  CA  . ILE B 1 32  ? -9.745  -29.469 77.760  1.00 35.16  ? 32  ILE B CA  1 
ATOM   3923 C  C   . ILE B 1 32  ? -9.514  -28.379 78.803  1.00 33.10  ? 32  ILE B C   1 
ATOM   3924 O  O   . ILE B 1 32  ? -9.812  -28.559 80.000  1.00 34.61  ? 32  ILE B O   1 
ATOM   3925 C  CB  . ILE B 1 32  ? -8.433  -30.191 77.381  1.00 30.85  ? 32  ILE B CB  1 
ATOM   3926 C  CG1 . ILE B 1 32  ? -8.738  -31.473 76.594  1.00 34.16  ? 32  ILE B CG1 1 
ATOM   3927 C  CG2 . ILE B 1 32  ? -7.631  -30.532 78.640  1.00 30.14  ? 32  ILE B CG2 1 
ATOM   3928 C  CD1 . ILE B 1 32  ? -7.525  -32.067 75.885  1.00 34.07  ? 32  ILE B CD1 1 
ATOM   3929 N  N   . ALA B 1 33  ? -9.000  -27.222 78.374  1.00 33.45  ? 33  ALA B N   1 
ATOM   3930 C  CA  . ALA B 1 33  ? -8.801  -26.121 79.319  1.00 34.39  ? 33  ALA B CA  1 
ATOM   3931 C  C   . ALA B 1 33  ? -10.125 -25.685 79.941  1.00 36.50  ? 33  ALA B C   1 
ATOM   3932 O  O   . ALA B 1 33  ? -10.193 -25.399 81.142  1.00 35.43  ? 33  ALA B O   1 
ATOM   3933 C  CB  . ALA B 1 33  ? -8.127  -24.938 78.630  1.00 31.74  ? 33  ALA B CB  1 
ATOM   3934 N  N   . ASP B 1 34  ? -11.191 -25.643 79.147  1.00 37.20  ? 34  ASP B N   1 
ATOM   3935 C  CA  . ASP B 1 34  ? -12.497 -25.306 79.714  1.00 33.17  ? 34  ASP B CA  1 
ATOM   3936 C  C   . ASP B 1 34  ? -12.869 -26.252 80.842  1.00 38.49  ? 34  ASP B C   1 
ATOM   3937 O  O   . ASP B 1 34  ? -13.465 -25.836 81.841  1.00 41.53  ? 34  ASP B O   1 
ATOM   3938 C  CB  . ASP B 1 34  ? -13.561 -25.333 78.625  1.00 36.06  ? 34  ASP B CB  1 
ATOM   3939 C  CG  . ASP B 1 34  ? -13.623 -24.035 77.860  1.00 41.13  ? 34  ASP B CG  1 
ATOM   3940 O  OD1 . ASP B 1 34  ? -13.140 -23.005 78.391  1.00 44.89  ? 34  ASP B OD1 1 
ATOM   3941 O  OD2 . ASP B 1 34  ? -14.143 -24.040 76.727  1.00 42.85  ? 34  ASP B OD2 1 
ATOM   3942 N  N   A GLU B 1 35  ? -12.545 -27.537 80.689  0.52 37.15  ? 35  GLU B N   1 
ATOM   3943 N  N   B GLU B 1 35  ? -12.517 -27.529 80.714  0.48 37.14  ? 35  GLU B N   1 
ATOM   3944 C  CA  A GLU B 1 35  ? -12.879 -28.531 81.702  0.52 36.58  ? 35  GLU B CA  1 
ATOM   3945 C  CA  B GLU B 1 35  ? -12.905 -28.490 81.735  0.48 36.55  ? 35  GLU B CA  1 
ATOM   3946 C  C   A GLU B 1 35  ? -11.942 -28.464 82.903  0.52 37.34  ? 35  GLU B C   1 
ATOM   3947 C  C   B GLU B 1 35  ? -11.932 -28.542 82.903  0.48 37.38  ? 35  GLU B C   1 
ATOM   3948 O  O   A GLU B 1 35  ? -12.399 -28.556 84.045  0.52 35.91  ? 35  GLU B O   1 
ATOM   3949 O  O   B GLU B 1 35  ? -12.359 -28.812 84.029  0.48 35.93  ? 35  GLU B O   1 
ATOM   3950 C  CB  A GLU B 1 35  ? -12.872 -29.934 81.080  0.52 38.03  ? 35  GLU B CB  1 
ATOM   3951 C  CB  B GLU B 1 35  ? -13.050 -29.892 81.136  0.48 38.12  ? 35  GLU B CB  1 
ATOM   3952 C  CG  A GLU B 1 35  ? -13.971 -30.157 80.030  0.52 39.87  ? 35  GLU B CG  1 
ATOM   3953 C  CG  B GLU B 1 35  ? -13.048 -30.989 82.189  0.48 37.73  ? 35  GLU B CG  1 
ATOM   3954 C  CD  A GLU B 1 35  ? -13.961 -31.567 79.449  0.52 42.41  ? 35  GLU B CD  1 
ATOM   3955 C  CD  B GLU B 1 35  ? -12.844 -32.367 81.612  0.48 40.45  ? 35  GLU B CD  1 
ATOM   3956 O  OE1 A GLU B 1 35  ? -12.911 -32.233 79.522  0.52 43.89  ? 35  GLU B OE1 1 
ATOM   3957 O  OE1 B GLU B 1 35  ? -13.092 -32.542 80.403  0.48 39.97  ? 35  GLU B OE1 1 
ATOM   3958 O  OE2 A GLU B 1 35  ? -15.019 -32.032 78.979  0.52 41.29  ? 35  GLU B OE2 1 
ATOM   3959 O  OE2 B GLU B 1 35  ? -12.418 -33.272 82.367  0.48 40.91  ? 35  GLU B OE2 1 
ATOM   3960 N  N   . LEU B 1 36  ? -10.639 -28.281 82.673  1.00 34.60  ? 36  LEU B N   1 
ATOM   3961 C  CA  . LEU B 1 36  ? -9.640  -28.445 83.722  1.00 37.99  ? 36  LEU B CA  1 
ATOM   3962 C  C   . LEU B 1 36  ? -9.205  -27.147 84.388  1.00 40.11  ? 36  LEU B C   1 
ATOM   3963 O  O   . LEU B 1 36  ? -8.678  -27.199 85.506  1.00 37.88  ? 36  LEU B O   1 
ATOM   3964 C  CB  . LEU B 1 36  ? -8.402  -29.153 83.157  1.00 33.57  ? 36  LEU B CB  1 
ATOM   3965 C  CG  . LEU B 1 36  ? -8.710  -30.563 82.646  1.00 35.10  ? 36  LEU B CG  1 
ATOM   3966 C  CD1 . LEU B 1 36  ? -7.421  -31.310 82.259  1.00 32.72  ? 36  LEU B CD1 1 
ATOM   3967 C  CD2 . LEU B 1 36  ? -9.504  -31.365 83.682  1.00 38.90  ? 36  LEU B CD2 1 
ATOM   3968 N  N   . GLY B 1 37  ? -9.374  -26.000 83.729  1.00 36.59  ? 37  GLY B N   1 
ATOM   3969 C  CA  . GLY B 1 37  ? -9.020  -24.726 84.333  1.00 34.94  ? 37  GLY B CA  1 
ATOM   3970 C  C   . GLY B 1 37  ? -7.747  -24.099 83.786  1.00 38.23  ? 37  GLY B C   1 
ATOM   3971 O  O   . GLY B 1 37  ? -7.357  -24.347 82.631  1.00 38.12  ? 37  GLY B O   1 
ATOM   3972 N  N   . GLU B 1 38  ? -7.080  -23.299 84.619  1.00 33.61  ? 38  GLU B N   1 
ATOM   3973 C  CA  . GLU B 1 38  ? -6.029  -22.413 84.131  1.00 36.10  ? 38  GLU B CA  1 
ATOM   3974 C  C   . GLU B 1 38  ? -4.725  -23.130 83.826  1.00 34.77  ? 38  GLU B C   1 
ATOM   3975 O  O   . GLU B 1 38  ? -3.831  -22.507 83.230  1.00 31.21  ? 38  GLU B O   1 
ATOM   3976 C  CB  . GLU B 1 38  ? -5.685  -21.307 85.129  1.00 35.40  ? 38  GLU B CB  1 
ATOM   3977 C  CG  . GLU B 1 38  ? -4.999  -21.822 86.398  1.00 37.85  ? 38  GLU B CG  1 
ATOM   3978 C  CD  . GLU B 1 38  ? -4.985  -20.812 87.542  1.00 44.64  ? 38  GLU B CD  1 
ATOM   3979 O  OE1 . GLU B 1 38  ? -5.029  -19.593 87.272  1.00 37.89  ? 38  GLU B OE1 1 
ATOM   3980 O  OE2 . GLU B 1 38  ? -4.853  -21.232 88.709  1.00 45.38  ? 38  GLU B OE2 1 
ATOM   3981 N  N   . ILE B 1 39  ? -4.562  -24.375 84.267  1.00 33.68  ? 39  ILE B N   1 
ATOM   3982 C  CA  . ILE B 1 39  ? -3.321  -25.076 83.962  1.00 34.27  ? 39  ILE B CA  1 
ATOM   3983 C  C   . ILE B 1 39  ? -3.567  -26.582 83.960  1.00 35.77  ? 39  ILE B C   1 
ATOM   3984 O  O   . ILE B 1 39  ? -4.221  -27.120 84.861  1.00 34.84  ? 39  ILE B O   1 
ATOM   3985 C  CB  . ILE B 1 39  ? -2.222  -24.675 84.961  1.00 31.93  ? 39  ILE B CB  1 
ATOM   3986 C  CG1 . ILE B 1 39  ? -0.928  -25.432 84.666  1.00 35.62  ? 39  ILE B CG1 1 
ATOM   3987 C  CG2 . ILE B 1 39  ? -2.670  -25.035 86.389  1.00 37.41  ? 39  ILE B CG2 1 
ATOM   3988 C  CD1 . ILE B 1 39  ? 0.195   -25.099 85.641  1.00 39.44  ? 39  ILE B CD1 1 
ATOM   3989 N  N   . PHE B 1 40  ? -3.046  -27.284 82.952  1.00 31.46  ? 40  PHE B N   1 
ATOM   3990 C  CA  . PHE B 1 40  ? -3.087  -28.737 82.988  1.00 33.81  ? 40  PHE B CA  1 
ATOM   3991 C  C   . PHE B 1 40  ? -1.807  -29.300 82.401  1.00 34.83  ? 40  PHE B C   1 
ATOM   3992 O  O   . PHE B 1 40  ? -1.173  -28.691 81.530  1.00 34.06  ? 40  PHE B O   1 
ATOM   3993 C  CB  . PHE B 1 40  ? -4.319  -29.329 82.271  1.00 35.26  ? 40  PHE B CB  1 
ATOM   3994 C  CG  . PHE B 1 40  ? -4.418  -29.006 80.797  1.00 36.77  ? 40  PHE B CG  1 
ATOM   3995 C  CD1 . PHE B 1 40  ? -3.829  -29.839 79.852  1.00 34.08  ? 40  PHE B CD1 1 
ATOM   3996 C  CD2 . PHE B 1 40  ? -5.159  -27.906 80.355  1.00 32.87  ? 40  PHE B CD2 1 
ATOM   3997 C  CE1 . PHE B 1 40  ? -3.928  -29.556 78.494  1.00 33.89  ? 40  PHE B CE1 1 
ATOM   3998 C  CE2 . PHE B 1 40  ? -5.270  -27.612 79.009  1.00 34.16  ? 40  PHE B CE2 1 
ATOM   3999 C  CZ  . PHE B 1 40  ? -4.670  -28.441 78.064  1.00 34.60  ? 40  PHE B CZ  1 
ATOM   4000 N  N   . LYS B 1 41  ? -1.429  -30.468 82.901  1.00 34.24  ? 41  LYS B N   1 
ATOM   4001 C  CA  . LYS B 1 41  ? -0.229  -31.141 82.438  1.00 32.07  ? 41  LYS B CA  1 
ATOM   4002 C  C   . LYS B 1 41  ? -0.587  -32.005 81.235  1.00 35.16  ? 41  LYS B C   1 
ATOM   4003 O  O   . LYS B 1 41  ? -1.691  -32.547 81.147  1.00 34.69  ? 41  LYS B O   1 
ATOM   4004 C  CB  . LYS B 1 41  ? 0.381   -31.971 83.575  1.00 40.01  ? 41  LYS B CB  1 
ATOM   4005 C  CG  . LYS B 1 41  ? 0.999   -33.286 83.164  1.00 45.20  ? 41  LYS B CG  1 
ATOM   4006 C  CD  . LYS B 1 41  ? 1.851   -33.834 84.297  1.00 48.32  ? 41  LYS B CD  1 
ATOM   4007 C  CE  . LYS B 1 41  ? 1.056   -34.758 85.196  1.00 53.12  ? 41  LYS B CE  1 
ATOM   4008 N  NZ  . LYS B 1 41  ? 1.895   -35.908 85.675  1.00 58.18  ? 41  LYS B NZ  1 
ATOM   4009 N  N   . PHE B 1 42  ? 0.326   -32.092 80.276  1.00 34.95  ? 42  PHE B N   1 
ATOM   4010 C  CA  . PHE B 1 42  ? 0.098   -32.911 79.092  1.00 34.21  ? 42  PHE B CA  1 
ATOM   4011 C  C   . PHE B 1 42  ? 1.341   -33.749 78.869  1.00 36.50  ? 42  PHE B C   1 
ATOM   4012 O  O   . PHE B 1 42  ? 2.430   -33.197 78.698  1.00 34.66  ? 42  PHE B O   1 
ATOM   4013 C  CB  . PHE B 1 42  ? -0.204  -32.041 77.875  1.00 32.33  ? 42  PHE B CB  1 
ATOM   4014 C  CG  . PHE B 1 42  ? -0.631  -32.811 76.656  1.00 33.34  ? 42  PHE B CG  1 
ATOM   4015 C  CD1 . PHE B 1 42  ? 0.294   -33.559 75.926  1.00 37.87  ? 42  PHE B CD1 1 
ATOM   4016 C  CD2 . PHE B 1 42  ? -1.944  -32.753 76.206  1.00 36.59  ? 42  PHE B CD2 1 
ATOM   4017 C  CE1 . PHE B 1 42  ? -0.097  -34.270 74.784  1.00 37.78  ? 42  PHE B CE1 1 
ATOM   4018 C  CE2 . PHE B 1 42  ? -2.339  -33.454 75.068  1.00 35.51  ? 42  PHE B CE2 1 
ATOM   4019 C  CZ  . PHE B 1 42  ? -1.401  -34.207 74.348  1.00 35.38  ? 42  PHE B CZ  1 
ATOM   4020 N  N   . GLU B 1 43  ? 1.174   -35.063 78.860  1.00 35.39  ? 43  GLU B N   1 
ATOM   4021 C  CA  . GLU B 1 43  ? 2.276   -36.002 78.734  1.00 38.82  ? 43  GLU B CA  1 
ATOM   4022 C  C   . GLU B 1 43  ? 2.170   -36.781 77.435  1.00 38.44  ? 43  GLU B C   1 
ATOM   4023 O  O   . GLU B 1 43  ? 1.078   -37.177 77.020  1.00 34.07  ? 43  GLU B O   1 
ATOM   4024 C  CB  . GLU B 1 43  ? 2.300   -36.989 79.898  1.00 40.00  ? 43  GLU B CB  1 
ATOM   4025 C  CG  . GLU B 1 43  ? 2.782   -36.391 81.195  1.00 45.13  ? 43  GLU B CG  1 
ATOM   4026 C  CD  . GLU B 1 43  ? 2.809   -37.406 82.311  1.00 47.01  ? 43  GLU B CD  1 
ATOM   4027 O  OE1 . GLU B 1 43  ? 1.895   -38.259 82.377  1.00 49.07  ? 43  GLU B OE1 1 
ATOM   4028 O  OE2 . GLU B 1 43  ? 3.753   -37.350 83.116  1.00 53.06  ? 43  GLU B OE2 1 
ATOM   4029 N  N   . ALA B 1 44  ? 3.307   -36.998 76.801  1.00 39.34  ? 44  ALA B N   1 
ATOM   4030 C  CA  . ALA B 1 44  ? 3.448   -37.914 75.680  1.00 35.53  ? 44  ALA B CA  1 
ATOM   4031 C  C   . ALA B 1 44  ? 4.675   -38.752 75.967  1.00 38.14  ? 44  ALA B C   1 
ATOM   4032 O  O   . ALA B 1 44  ? 5.449   -38.440 76.878  1.00 43.28  ? 44  ALA B O   1 
ATOM   4033 C  CB  . ALA B 1 44  ? 3.582   -37.158 74.345  1.00 37.48  ? 44  ALA B CB  1 
ATOM   4034 N  N   . PRO B 1 45  ? 4.863   -39.870 75.243  1.00 40.88  ? 45  PRO B N   1 
ATOM   4035 C  CA  . PRO B 1 45  ? 6.103   -40.636 75.410  1.00 38.36  ? 45  PRO B CA  1 
ATOM   4036 C  C   . PRO B 1 45  ? 7.304   -39.723 75.242  1.00 40.37  ? 45  PRO B C   1 
ATOM   4037 O  O   . PRO B 1 45  ? 7.458   -39.092 74.194  1.00 37.44  ? 45  PRO B O   1 
ATOM   4038 C  CB  . PRO B 1 45  ? 6.030   -41.689 74.302  1.00 41.71  ? 45  PRO B CB  1 
ATOM   4039 C  CG  . PRO B 1 45  ? 4.560   -41.850 74.008  1.00 40.43  ? 45  PRO B CG  1 
ATOM   4040 C  CD  . PRO B 1 45  ? 3.878   -40.557 74.388  1.00 41.97  ? 45  PRO B CD  1 
ATOM   4041 N  N   . GLY B 1 46  ? 8.115   -39.593 76.289  1.00 42.49  ? 46  GLY B N   1 
ATOM   4042 C  CA  . GLY B 1 46  ? 9.326   -38.805 76.219  1.00 43.00  ? 46  GLY B CA  1 
ATOM   4043 C  C   . GLY B 1 46  ? 9.170   -37.308 76.382  1.00 49.17  ? 46  GLY B C   1 
ATOM   4044 O  O   . GLY B 1 46  ? 10.126  -36.577 76.094  1.00 42.79  ? 46  GLY B O   1 
ATOM   4045 N  N   . ARG B 1 47  ? 8.014   -36.811 76.828  1.00 39.46  ? 47  ARG B N   1 
ATOM   4046 C  CA  . ARG B 1 47  ? 7.933   -35.359 76.942  1.00 42.62  ? 47  ARG B CA  1 
ATOM   4047 C  C   . ARG B 1 47  ? 6.745   -34.950 77.807  1.00 40.20  ? 47  ARG B C   1 
ATOM   4048 O  O   . ARG B 1 47  ? 5.743   -35.662 77.901  1.00 36.40  ? 47  ARG B O   1 
ATOM   4049 C  CB  . ARG B 1 47  ? 7.829   -34.702 75.564  1.00 44.43  ? 47  ARG B CB  1 
ATOM   4050 C  CG  . ARG B 1 47  ? 6.455   -34.786 74.985  1.00 47.28  ? 47  ARG B CG  1 
ATOM   4051 C  CD  . ARG B 1 47  ? 6.257   -33.763 73.876  1.00 53.85  ? 47  ARG B CD  1 
ATOM   4052 N  NE  . ARG B 1 47  ? 5.087   -34.085 73.067  1.00 53.29  ? 47  ARG B NE  1 
ATOM   4053 C  CZ  . ARG B 1 47  ? 3.908   -33.489 73.202  1.00 48.44  ? 47  ARG B CZ  1 
ATOM   4054 N  NH1 . ARG B 1 47  ? 3.723   -32.508 74.071  1.00 45.17  ? 47  ARG B NH1 1 
ATOM   4055 N  NH2 . ARG B 1 47  ? 2.890   -33.889 72.450  1.00 48.66  ? 47  ARG B NH2 1 
ATOM   4056 N  N   . VAL B 1 48  ? 6.881   -33.794 78.440  1.00 38.60  ? 48  VAL B N   1 
ATOM   4057 C  CA  . VAL B 1 48  ? 5.815   -33.214 79.245  1.00 39.07  ? 48  VAL B CA  1 
ATOM   4058 C  C   . VAL B 1 48  ? 5.782   -31.717 78.977  1.00 42.41  ? 48  VAL B C   1 
ATOM   4059 O  O   . VAL B 1 48  ? 6.829   -31.065 78.868  1.00 39.17  ? 48  VAL B O   1 
ATOM   4060 C  CB  . VAL B 1 48  ? 6.017   -33.492 80.749  1.00 40.98  ? 48  VAL B CB  1 
ATOM   4061 C  CG1 . VAL B 1 48  ? 7.433   -33.125 81.165  1.00 44.93  ? 48  VAL B CG1 1 
ATOM   4062 C  CG2 . VAL B 1 48  ? 4.965   -32.747 81.593  1.00 40.86  ? 48  VAL B CG2 1 
ATOM   4063 N  N   . THR B 1 49  ? 4.580   -31.166 78.867  1.00 34.62  ? 49  THR B N   1 
ATOM   4064 C  CA  . THR B 1 49  ? 4.435   -29.722 78.921  1.00 37.58  ? 49  THR B CA  1 
ATOM   4065 C  C   . THR B 1 49  ? 3.219   -29.385 79.765  1.00 36.60  ? 49  THR B C   1 
ATOM   4066 O  O   . THR B 1 49  ? 2.480   -30.271 80.220  1.00 36.23  ? 49  THR B O   1 
ATOM   4067 C  CB  . THR B 1 49  ? 4.360   -29.093 77.519  1.00 34.97  ? 49  THR B CB  1 
ATOM   4068 O  OG1 . THR B 1 49  ? 4.496   -27.667 77.635  1.00 38.04  ? 49  THR B OG1 1 
ATOM   4069 C  CG2 . THR B 1 49  ? 3.057   -29.433 76.822  1.00 37.87  ? 49  THR B CG2 1 
ATOM   4070 N  N   . ARG B 1 50  ? 3.047   -28.088 79.999  1.00 32.11  ? 50  ARG B N   1 
ATOM   4071 C  CA  . ARG B 1 50  ? 1.975   -27.551 80.834  1.00 32.62  ? 50  ARG B CA  1 
ATOM   4072 C  C   . ARG B 1 50  ? 1.258   -26.459 80.047  1.00 36.57  ? 50  ARG B C   1 
ATOM   4073 O  O   . ARG B 1 50  ? 1.891   -25.488 79.621  1.00 34.88  ? 50  ARG B O   1 
ATOM   4074 C  CB  . ARG B 1 50  ? 2.545   -26.985 82.143  1.00 37.29  ? 50  ARG B CB  1 
ATOM   4075 C  CG  . ARG B 1 50  ? 3.192   -28.041 83.057  1.00 39.36  ? 50  ARG B CG  1 
ATOM   4076 C  CD  . ARG B 1 50  ? 4.518   -27.547 83.661  1.00 40.16  ? 50  ARG B CD  1 
ATOM   4077 N  NE  . ARG B 1 50  ? 5.352   -28.645 84.135  1.00 40.90  ? 50  ARG B NE  1 
ATOM   4078 C  CZ  . ARG B 1 50  ? 6.276   -29.260 83.408  1.00 43.81  ? 50  ARG B CZ  1 
ATOM   4079 N  NH1 . ARG B 1 50  ? 6.577   -28.857 82.175  1.00 37.18  ? 50  ARG B NH1 1 
ATOM   4080 N  NH2 . ARG B 1 50  ? 6.916   -30.304 83.928  1.00 38.22  ? 50  ARG B NH2 1 
ATOM   4081 N  N   . TYR B 1 51  ? -0.056  -26.610 79.861  1.00 33.46  ? 51  TYR B N   1 
ATOM   4082 C  CA  . TYR B 1 51  ? -0.862  -25.641 79.121  1.00 36.35  ? 51  TYR B CA  1 
ATOM   4083 C  C   . TYR B 1 51  ? -1.454  -24.618 80.085  1.00 34.65  ? 51  TYR B C   1 
ATOM   4084 O  O   . TYR B 1 51  ? -2.159  -24.991 81.026  1.00 34.52  ? 51  TYR B O   1 
ATOM   4085 C  CB  . TYR B 1 51  ? -1.978  -26.351 78.352  1.00 32.69  ? 51  TYR B CB  1 
ATOM   4086 C  CG  . TYR B 1 51  ? -1.453  -27.059 77.132  1.00 34.67  ? 51  TYR B CG  1 
ATOM   4087 C  CD1 . TYR B 1 51  ? -0.973  -28.356 77.221  1.00 33.14  ? 51  TYR B CD1 1 
ATOM   4088 C  CD2 . TYR B 1 51  ? -1.429  -26.430 75.895  1.00 34.62  ? 51  TYR B CD2 1 
ATOM   4089 C  CE1 . TYR B 1 51  ? -0.480  -29.015 76.108  1.00 37.27  ? 51  TYR B CE1 1 
ATOM   4090 C  CE2 . TYR B 1 51  ? -0.931  -27.085 74.767  1.00 32.34  ? 51  TYR B CE2 1 
ATOM   4091 C  CZ  . TYR B 1 51  ? -0.458  -28.370 74.881  1.00 34.15  ? 51  TYR B CZ  1 
ATOM   4092 O  OH  . TYR B 1 51  ? 0.036   -29.030 73.768  1.00 33.21  ? 51  TYR B OH  1 
ATOM   4093 N  N   . LEU B 1 52  ? -1.175  -23.336 79.834  1.00 35.42  ? 52  LEU B N   1 
ATOM   4094 C  CA  . LEU B 1 52  ? -1.627  -22.216 80.651  1.00 34.03  ? 52  LEU B CA  1 
ATOM   4095 C  C   . LEU B 1 52  ? -2.731  -21.447 79.935  1.00 33.76  ? 52  LEU B C   1 
ATOM   4096 O  O   . LEU B 1 52  ? -2.611  -21.136 78.744  1.00 32.59  ? 52  LEU B O   1 
ATOM   4097 C  CB  . LEU B 1 52  ? -0.482  -21.253 80.930  1.00 34.14  ? 52  LEU B CB  1 
ATOM   4098 C  CG  . LEU B 1 52  ? 0.723   -21.831 81.656  1.00 34.55  ? 52  LEU B CG  1 
ATOM   4099 C  CD1 . LEU B 1 52  ? 1.592   -20.662 82.063  1.00 38.38  ? 52  LEU B CD1 1 
ATOM   4100 C  CD2 . LEU B 1 52  ? 0.261   -22.626 82.851  1.00 36.01  ? 52  LEU B CD2 1 
ATOM   4101 N  N   . SER B 1 53  ? -3.774  -21.084 80.689  1.00 31.92  ? 53  SER B N   1 
ATOM   4102 C  CA  . SER B 1 53  ? -4.965  -20.446 80.133  1.00 33.60  ? 53  SER B CA  1 
ATOM   4103 C  C   . SER B 1 53  ? -5.409  -19.182 80.857  1.00 34.14  ? 53  SER B C   1 
ATOM   4104 O  O   . SER B 1 53  ? -6.279  -18.478 80.331  1.00 34.29  ? 53  SER B O   1 
ATOM   4105 C  CB  . SER B 1 53  ? -6.151  -21.429 80.137  1.00 33.42  ? 53  SER B CB  1 
ATOM   4106 O  OG  . SER B 1 53  ? -5.953  -22.425 79.153  1.00 36.86  ? 53  SER B OG  1 
ATOM   4107 N  N   . SER B 1 54  ? -4.874  -18.880 82.042  1.00 33.12  ? 54  SER B N   1 
ATOM   4108 C  CA  . SER B 1 54  ? -5.298  -17.713 82.812  1.00 35.24  ? 54  SER B CA  1 
ATOM   4109 C  C   . SER B 1 54  ? -4.273  -16.589 82.720  1.00 33.80  ? 54  SER B C   1 
ATOM   4110 O  O   . SER B 1 54  ? -3.060  -16.830 82.653  1.00 32.79  ? 54  SER B O   1 
ATOM   4111 C  CB  . SER B 1 54  ? -5.544  -18.085 84.282  1.00 35.18  ? 54  SER B CB  1 
ATOM   4112 O  OG  . SER B 1 54  ? -4.322  -18.396 84.909  1.00 34.64  ? 54  SER B OG  1 
ATOM   4113 N  N   . GLN B 1 55  ? -4.777  -15.354 82.703  1.00 33.42  ? 55  GLN B N   1 
ATOM   4114 C  CA  . GLN B 1 55  ? -3.898  -14.193 82.727  1.00 34.57  ? 55  GLN B CA  1 
ATOM   4115 C  C   . GLN B 1 55  ? -3.042  -14.198 83.983  1.00 33.72  ? 55  GLN B C   1 
ATOM   4116 O  O   . GLN B 1 55  ? -1.887  -13.754 83.957  1.00 33.32  ? 55  GLN B O   1 
ATOM   4117 C  CB  . GLN B 1 55  ? -4.742  -12.916 82.634  1.00 36.78  ? 55  GLN B CB  1 
ATOM   4118 C  CG  . GLN B 1 55  ? -3.957  -11.623 82.436  1.00 35.56  ? 55  GLN B CG  1 
ATOM   4119 C  CD  . GLN B 1 55  ? -3.468  -11.005 83.755  1.00 39.31  ? 55  GLN B CD  1 
ATOM   4120 O  OE1 . GLN B 1 55  ? -3.917  -11.384 84.839  1.00 33.37  ? 55  GLN B OE1 1 
ATOM   4121 N  NE2 . GLN B 1 55  ? -2.522  -10.076 83.659  1.00 35.47  ? 55  GLN B NE2 1 
ATOM   4122 N  N   . ARG B 1 56  ? -3.564  -14.757 85.072  1.00 30.85  ? 56  ARG B N   1 
ATOM   4123 C  CA  . ARG B 1 56  ? -2.819  -14.753 86.327  1.00 36.19  ? 56  ARG B CA  1 
ATOM   4124 C  C   . ARG B 1 56  ? -1.521  -15.543 86.188  1.00 36.57  ? 56  ARG B C   1 
ATOM   4125 O  O   . ARG B 1 56  ? -0.466  -15.112 86.673  1.00 36.75  ? 56  ARG B O   1 
ATOM   4126 C  CB  . ARG B 1 56  ? -3.679  -15.343 87.446  1.00 37.93  ? 56  ARG B CB  1 
ATOM   4127 C  CG  . ARG B 1 56  ? -2.881  -15.902 88.593  1.00 44.59  ? 56  ARG B CG  1 
ATOM   4128 C  CD  . ARG B 1 56  ? -3.779  -16.467 89.710  1.00 48.26  ? 56  ARG B CD  1 
ATOM   4129 N  NE  . ARG B 1 56  ? -3.808  -17.929 89.676  1.00 44.45  ? 56  ARG B NE  1 
ATOM   4130 C  CZ  . ARG B 1 56  ? -2.966  -18.706 90.349  1.00 48.06  ? 56  ARG B CZ  1 
ATOM   4131 N  NH1 . ARG B 1 56  ? -2.050  -18.198 91.160  1.00 44.01  ? 56  ARG B NH1 1 
ATOM   4132 N  NH2 . ARG B 1 56  ? -3.024  -20.025 90.187  1.00 45.45  ? 56  ARG B NH2 1 
ATOM   4133 N  N   . LEU B 1 57  ? -1.570  -16.700 85.514  1.00 32.90  ? 57  LEU B N   1 
ATOM   4134 C  CA  . LEU B 1 57  ? -0.349  -17.481 85.330  1.00 32.81  ? 57  LEU B CA  1 
ATOM   4135 C  C   . LEU B 1 57  ? 0.448   -17.031 84.109  1.00 33.92  ? 57  LEU B C   1 
ATOM   4136 O  O   . LEU B 1 57  ? 1.681   -17.111 84.112  1.00 34.04  ? 57  LEU B O   1 
ATOM   4137 C  CB  . LEU B 1 57  ? -0.669  -18.972 85.211  1.00 33.14  ? 57  LEU B CB  1 
ATOM   4138 C  CG  . LEU B 1 57  ? -1.279  -19.652 86.430  1.00 35.77  ? 57  LEU B CG  1 
ATOM   4139 C  CD1 . LEU B 1 57  ? -1.635  -21.099 86.091  1.00 33.57  ? 57  LEU B CD1 1 
ATOM   4140 C  CD2 . LEU B 1 57  ? -0.340  -19.580 87.636  1.00 35.31  ? 57  LEU B CD2 1 
ATOM   4141 N  N   . ILE B 1 58  ? -0.229  -16.562 83.062  1.00 35.29  ? 58  ILE B N   1 
ATOM   4142 C  CA  . ILE B 1 58  ? 0.488   -16.210 81.841  1.00 30.96  ? 58  ILE B CA  1 
ATOM   4143 C  C   . ILE B 1 58  ? 1.293   -14.931 82.034  1.00 32.06  ? 58  ILE B C   1 
ATOM   4144 O  O   . ILE B 1 58  ? 2.376   -14.784 81.460  1.00 33.03  ? 58  ILE B O   1 
ATOM   4145 C  CB  . ILE B 1 58  ? -0.514  -16.139 80.671  1.00 32.19  ? 58  ILE B CB  1 
ATOM   4146 C  CG1 . ILE B 1 58  ? -0.943  -17.576 80.314  1.00 31.08  ? 58  ILE B CG1 1 
ATOM   4147 C  CG2 . ILE B 1 58  ? 0.097   -15.409 79.468  1.00 30.13  ? 58  ILE B CG2 1 
ATOM   4148 C  CD1 . ILE B 1 58  ? -2.230  -17.676 79.457  1.00 30.97  ? 58  ILE B CD1 1 
ATOM   4149 N  N   . LYS B 1 59  ? 0.824   -14.006 82.878  1.00 31.77  ? 59  LYS B N   1 
ATOM   4150 C  CA  . LYS B 1 59  ? 1.658   -12.844 83.167  1.00 35.53  ? 59  LYS B CA  1 
ATOM   4151 C  C   . LYS B 1 59  ? 2.981   -13.259 83.801  1.00 30.99  ? 59  LYS B C   1 
ATOM   4152 O  O   . LYS B 1 59  ? 4.015   -12.639 83.532  1.00 36.45  ? 59  LYS B O   1 
ATOM   4153 C  CB  . LYS B 1 59  ? 0.902   -11.838 84.055  1.00 35.89  ? 59  LYS B CB  1 
ATOM   4154 C  CG  . LYS B 1 59  ? 0.760   -12.234 85.498  1.00 37.96  ? 59  LYS B CG  1 
ATOM   4155 C  CD  . LYS B 1 59  ? -0.017  -11.182 86.294  1.00 38.99  ? 59  LYS B CD  1 
ATOM   4156 C  CE  . LYS B 1 59  ? -0.155  -11.601 87.751  1.00 41.83  ? 59  LYS B CE  1 
ATOM   4157 N  NZ  . LYS B 1 59  ? -0.846  -10.526 88.542  1.00 42.58  ? 59  LYS B NZ  1 
ATOM   4158 N  N   . GLU B 1 60  ? 2.989   -14.328 84.588  1.00 34.37  ? 60  GLU B N   1 
ATOM   4159 C  CA  . GLU B 1 60  ? 4.257   -14.809 85.143  1.00 36.34  ? 60  GLU B CA  1 
ATOM   4160 C  C   . GLU B 1 60  ? 5.110   -15.466 84.071  1.00 37.91  ? 60  GLU B C   1 
ATOM   4161 O  O   . GLU B 1 60  ? 6.336   -15.289 84.044  1.00 35.44  ? 60  GLU B O   1 
ATOM   4162 C  CB  . GLU B 1 60  ? 4.005   -15.797 86.283  1.00 37.12  ? 60  GLU B CB  1 
ATOM   4163 C  CG  . GLU B 1 60  ? 3.566   -15.127 87.564  1.00 42.89  ? 60  GLU B CG  1 
ATOM   4164 C  CD  . GLU B 1 60  ? 3.589   -16.063 88.775  1.00 44.39  ? 60  GLU B CD  1 
ATOM   4165 O  OE1 . GLU B 1 60  ? 4.509   -16.897 88.895  1.00 39.54  ? 60  GLU B OE1 1 
ATOM   4166 O  OE2 . GLU B 1 60  ? 2.663   -15.964 89.604  1.00 43.04  ? 60  GLU B OE2 1 
ATOM   4167 N  N   . ALA B 1 61  ? 4.486   -16.244 83.191  1.00 32.26  ? 61  ALA B N   1 
ATOM   4168 C  CA  . ALA B 1 61  ? 5.246   -16.926 82.153  1.00 34.11  ? 61  ALA B CA  1 
ATOM   4169 C  C   . ALA B 1 61  ? 5.881   -15.920 81.212  1.00 35.30  ? 61  ALA B C   1 
ATOM   4170 O  O   . ALA B 1 61  ? 6.915   -16.205 80.588  1.00 33.96  ? 61  ALA B O   1 
ATOM   4171 C  CB  . ALA B 1 61  ? 4.326   -17.890 81.389  1.00 36.80  ? 61  ALA B CB  1 
ATOM   4172 N  N   . CYS B 1 62  ? 5.270   -14.739 81.098  1.00 33.25  ? 62  CYS B N   1 
ATOM   4173 C  CA  . CYS B 1 62  ? 5.754   -13.651 80.260  1.00 32.32  ? 62  CYS B CA  1 
ATOM   4174 C  C   . CYS B 1 62  ? 6.833   -12.814 80.932  1.00 36.89  ? 62  CYS B C   1 
ATOM   4175 O  O   . CYS B 1 62  ? 7.275   -11.822 80.342  1.00 34.85  ? 62  CYS B O   1 
ATOM   4176 C  CB  . CYS B 1 62  ? 4.577   -12.749 79.851  1.00 34.83  ? 62  CYS B CB  1 
ATOM   4177 S  SG  . CYS B 1 62  ? 3.474   -13.533 78.626  1.00 36.00  ? 62  CYS B SG  1 
ATOM   4178 N  N   . ASP B 1 63  ? 7.267   -13.183 82.136  1.00 32.71  ? 63  ASP B N   1 
ATOM   4179 C  CA  . ASP B 1 63  ? 8.396   -12.521 82.788  1.00 34.66  ? 63  ASP B CA  1 
ATOM   4180 C  C   . ASP B 1 63  ? 9.699   -13.053 82.197  1.00 31.65  ? 63  ASP B C   1 
ATOM   4181 O  O   . ASP B 1 63  ? 10.100  -14.188 82.480  1.00 35.89  ? 63  ASP B O   1 
ATOM   4182 C  CB  . ASP B 1 63  ? 8.318   -12.768 84.294  1.00 34.33  ? 63  ASP B CB  1 
ATOM   4183 C  CG  . ASP B 1 63  ? 9.481   -12.164 85.059  1.00 36.70  ? 63  ASP B CG  1 
ATOM   4184 O  OD1 . ASP B 1 63  ? 10.513  -11.809 84.455  1.00 34.86  ? 63  ASP B OD1 1 
ATOM   4185 O  OD2 . ASP B 1 63  ? 9.351   -12.082 86.290  1.00 40.34  ? 63  ASP B OD2 1 
ATOM   4186 N  N   . GLU B 1 64  ? 10.374  -12.235 81.391  1.00 34.23  ? 64  GLU B N   1 
ATOM   4187 C  CA  . GLU B 1 64  ? 11.523  -12.725 80.630  1.00 32.19  ? 64  GLU B CA  1 
ATOM   4188 C  C   . GLU B 1 64  ? 12.732  -12.993 81.501  1.00 36.96  ? 64  GLU B C   1 
ATOM   4189 O  O   . GLU B 1 64  ? 13.686  -13.609 81.013  1.00 33.99  ? 64  GLU B O   1 
ATOM   4190 C  CB  . GLU B 1 64  ? 11.917  -11.724 79.547  1.00 38.35  ? 64  GLU B CB  1 
ATOM   4191 C  CG  . GLU B 1 64  ? 10.861  -11.541 78.508  1.00 40.01  ? 64  GLU B CG  1 
ATOM   4192 C  CD  . GLU B 1 64  ? 11.223  -10.459 77.538  1.00 37.69  ? 64  GLU B CD  1 
ATOM   4193 O  OE1 . GLU B 1 64  ? 11.190  -9.283  77.934  1.00 44.14  ? 64  GLU B OE1 1 
ATOM   4194 O  OE2 . GLU B 1 64  ? 11.539  -10.783 76.384  1.00 34.37  ? 64  GLU B OE2 1 
ATOM   4195 N  N   . SER B 1 65  ? 12.732  -12.511 82.754  1.00 36.20  ? 65  SER B N   1 
ATOM   4196 C  CA  . SER B 1 65  ? 13.788  -12.896 83.681  1.00 37.96  ? 65  SER B CA  1 
ATOM   4197 C  C   . SER B 1 65  ? 13.615  -14.333 84.123  1.00 38.68  ? 65  SER B C   1 
ATOM   4198 O  O   . SER B 1 65  ? 14.572  -14.948 84.607  1.00 41.73  ? 65  SER B O   1 
ATOM   4199 C  CB  . SER B 1 65  ? 13.804  -11.986 84.918  1.00 37.47  ? 65  SER B CB  1 
ATOM   4200 O  OG  . SER B 1 65  ? 12.697  -12.242 85.780  1.00 37.37  ? 65  SER B OG  1 
ATOM   4201 N  N   . ARG B 1 66  ? 12.420  -14.887 83.941  1.00 33.61  ? 66  ARG B N   1 
ATOM   4202 C  CA  . ARG B 1 66  ? 12.114  -16.207 84.448  1.00 33.58  ? 66  ARG B CA  1 
ATOM   4203 C  C   . ARG B 1 66  ? 11.945  -17.255 83.356  1.00 33.79  ? 66  ARG B C   1 
ATOM   4204 O  O   . ARG B 1 66  ? 12.295  -18.416 83.586  1.00 34.87  ? 66  ARG B O   1 
ATOM   4205 C  CB  . ARG B 1 66  ? 10.835  -16.133 85.287  1.00 35.09  ? 66  ARG B CB  1 
ATOM   4206 C  CG  . ARG B 1 66  ? 11.100  -15.550 86.687  1.00 37.60  ? 66  ARG B CG  1 
ATOM   4207 C  CD  . ARG B 1 66  ? 9.776   -15.253 87.382  1.00 38.44  ? 66  ARG B CD  1 
ATOM   4208 N  NE  . ARG B 1 66  ? 9.261   -16.470 87.987  1.00 37.14  ? 66  ARG B NE  1 
ATOM   4209 C  CZ  . ARG B 1 66  ? 7.994   -16.677 88.313  1.00 40.60  ? 66  ARG B CZ  1 
ATOM   4210 N  NH1 . ARG B 1 66  ? 7.059   -15.774 88.066  1.00 41.26  ? 66  ARG B NH1 1 
ATOM   4211 N  NH2 . ARG B 1 66  ? 7.661   -17.817 88.910  1.00 43.02  ? 66  ARG B NH2 1 
ATOM   4212 N  N   . PHE B 1 67  ? 11.444  -16.869 82.175  1.00 33.16  ? 67  PHE B N   1 
ATOM   4213 C  CA  . PHE B 1 67  ? 11.087  -17.791 81.095  1.00 32.59  ? 67  PHE B CA  1 
ATOM   4214 C  C   . PHE B 1 67  ? 11.588  -17.223 79.772  1.00 32.26  ? 67  PHE B C   1 
ATOM   4215 O  O   . PHE B 1 67  ? 11.478  -16.016 79.527  1.00 34.74  ? 67  PHE B O   1 
ATOM   4216 C  CB  . PHE B 1 67  ? 9.556   -17.949 81.046  1.00 34.32  ? 67  PHE B CB  1 
ATOM   4217 C  CG  . PHE B 1 67  ? 8.985   -18.545 82.311  1.00 31.62  ? 67  PHE B CG  1 
ATOM   4218 C  CD1 . PHE B 1 67  ? 9.014   -19.915 82.534  1.00 34.16  ? 67  PHE B CD1 1 
ATOM   4219 C  CD2 . PHE B 1 67  ? 8.524   -17.710 83.332  1.00 34.99  ? 67  PHE B CD2 1 
ATOM   4220 C  CE1 . PHE B 1 67  ? 8.514   -20.451 83.728  1.00 33.97  ? 67  PHE B CE1 1 
ATOM   4221 C  CE2 . PHE B 1 67  ? 8.048   -18.240 84.524  1.00 36.76  ? 67  PHE B CE2 1 
ATOM   4222 C  CZ  . PHE B 1 67  ? 8.042   -19.612 84.713  1.00 36.30  ? 67  PHE B CZ  1 
ATOM   4223 N  N   . ASP B 1 68  ? 12.105  -18.081 78.903  1.00 33.24  ? 68  ASP B N   1 
ATOM   4224 C  CA  . ASP B 1 68  ? 12.503  -17.608 77.587  1.00 32.81  ? 68  ASP B CA  1 
ATOM   4225 C  C   . ASP B 1 68  ? 11.733  -18.441 76.564  1.00 32.58  ? 68  ASP B C   1 
ATOM   4226 O  O   . ASP B 1 68  ? 11.069  -19.416 76.924  1.00 31.35  ? 68  ASP B O   1 
ATOM   4227 C  CB  . ASP B 1 68  ? 14.046  -17.651 77.473  1.00 33.87  ? 68  ASP B CB  1 
ATOM   4228 C  CG  . ASP B 1 68  ? 14.562  -17.563 76.051  1.00 38.41  ? 68  ASP B CG  1 
ATOM   4229 O  OD1 . ASP B 1 68  ? 14.082  -16.660 75.324  1.00 35.55  ? 68  ASP B OD1 1 
ATOM   4230 O  OD2 . ASP B 1 68  ? 15.561  -18.253 75.721  1.00 32.99  ? 68  ASP B OD2 1 
ATOM   4231 N  N   . LYS B 1 69  ? 11.759  -18.021 75.290  1.00 33.07  ? 69  LYS B N   1 
ATOM   4232 C  CA  . LYS B 1 69  ? 11.012  -18.730 74.248  1.00 31.40  ? 69  LYS B CA  1 
ATOM   4233 C  C   . LYS B 1 69  ? 11.540  -20.154 74.043  1.00 35.38  ? 69  LYS B C   1 
ATOM   4234 O  O   . LYS B 1 69  ? 12.751  -20.383 73.919  1.00 32.48  ? 69  LYS B O   1 
ATOM   4235 C  CB  . LYS B 1 69  ? 11.074  -17.951 72.920  1.00 29.17  ? 69  LYS B CB  1 
ATOM   4236 C  CG  . LYS B 1 69  ? 10.816  -18.817 71.664  1.00 31.36  ? 69  LYS B CG  1 
ATOM   4237 C  CD  . LYS B 1 69  ? 10.335  -17.981 70.481  1.00 29.87  ? 69  LYS B CD  1 
ATOM   4238 C  CE  . LYS B 1 69  ? 10.211  -18.873 69.237  1.00 30.64  ? 69  LYS B CE  1 
ATOM   4239 N  NZ  . LYS B 1 69  ? 9.316   -18.255 68.200  1.00 31.48  ? 69  LYS B NZ  1 
ATOM   4240 N  N   . ASN B 1 70  ? 10.618  -21.110 74.000  1.00 30.90  ? 70  ASN B N   1 
ATOM   4241 C  CA  . ASN B 1 70  ? 10.917  -22.486 73.648  1.00 31.18  ? 70  ASN B CA  1 
ATOM   4242 C  C   . ASN B 1 70  ? 10.461  -22.749 72.217  1.00 32.21  ? 70  ASN B C   1 
ATOM   4243 O  O   . ASN B 1 70  ? 9.482   -22.167 71.739  1.00 30.79  ? 70  ASN B O   1 
ATOM   4244 C  CB  . ASN B 1 70  ? 10.216  -23.467 74.609  1.00 32.01  ? 70  ASN B CB  1 
ATOM   4245 C  CG  . ASN B 1 70  ? 10.530  -24.924 74.296  1.00 35.26  ? 70  ASN B CG  1 
ATOM   4246 O  OD1 . ASN B 1 70  ? 11.692  -25.294 74.134  1.00 34.80  ? 70  ASN B OD1 1 
ATOM   4247 N  ND2 . ASN B 1 70  ? 9.497   -25.754 74.190  1.00 30.80  ? 70  ASN B ND2 1 
ATOM   4248 N  N   . LEU B 1 71  ? 11.175  -23.629 71.520  1.00 34.23  ? 71  LEU B N   1 
ATOM   4249 C  CA  . LEU B 1 71  ? 10.706  -24.077 70.215  1.00 32.69  ? 71  LEU B CA  1 
ATOM   4250 C  C   . LEU B 1 71  ? 9.753   -25.236 70.482  1.00 34.23  ? 71  LEU B C   1 
ATOM   4251 O  O   . LEU B 1 71  ? 10.189  -26.322 70.885  1.00 32.40  ? 71  LEU B O   1 
ATOM   4252 C  CB  . LEU B 1 71  ? 11.858  -24.522 69.316  1.00 35.38  ? 71  LEU B CB  1 
ATOM   4253 C  CG  . LEU B 1 71  ? 12.857  -23.479 68.799  1.00 34.99  ? 71  LEU B CG  1 
ATOM   4254 C  CD1 . LEU B 1 71  ? 13.762  -24.123 67.731  1.00 35.10  ? 71  LEU B CD1 1 
ATOM   4255 C  CD2 . LEU B 1 71  ? 12.237  -22.143 68.347  1.00 35.05  ? 71  LEU B CD2 1 
ATOM   4256 N  N   . SER B 1 72  ? 8.451   -25.002 70.289  1.00 33.31  ? 72  SER B N   1 
ATOM   4257 C  CA  . SER B 1 72  ? 7.490   -26.095 70.319  1.00 35.44  ? 72  SER B CA  1 
ATOM   4258 C  C   . SER B 1 72  ? 7.909   -27.166 69.305  1.00 33.21  ? 72  SER B C   1 
ATOM   4259 O  O   . SER B 1 72  ? 8.749   -26.943 68.437  1.00 36.28  ? 72  SER B O   1 
ATOM   4260 C  CB  . SER B 1 72  ? 6.085   -25.569 70.002  1.00 29.78  ? 72  SER B CB  1 
ATOM   4261 O  OG  . SER B 1 72  ? 6.113   -24.886 68.747  1.00 33.87  ? 72  SER B OG  1 
ATOM   4262 N  N   . GLN B 1 73  ? 7.297   -28.343 69.404  1.00 36.79  ? 73  GLN B N   1 
ATOM   4263 C  CA  . GLN B 1 73  ? 7.568   -29.336 68.371  1.00 36.72  ? 73  GLN B CA  1 
ATOM   4264 C  C   . GLN B 1 73  ? 7.109   -28.836 67.007  1.00 34.13  ? 73  GLN B C   1 
ATOM   4265 O  O   . GLN B 1 73  ? 7.768   -29.093 65.988  1.00 34.72  ? 73  GLN B O   1 
ATOM   4266 C  CB  . GLN B 1 73  ? 6.911   -30.668 68.733  1.00 40.16  ? 73  GLN B CB  1 
ATOM   4267 C  CG  . GLN B 1 73  ? 7.308   -31.770 67.754  1.00 42.69  ? 73  GLN B CG  1 
ATOM   4268 C  CD  . GLN B 1 73  ? 8.768   -32.134 67.912  1.00 45.95  ? 73  GLN B CD  1 
ATOM   4269 O  OE1 . GLN B 1 73  ? 9.212   -32.513 68.992  1.00 49.29  ? 73  GLN B OE1 1 
ATOM   4270 N  NE2 . GLN B 1 73  ? 9.542   -31.938 66.850  1.00 43.67  ? 73  GLN B NE2 1 
ATOM   4271 N  N   . ALA B 1 74  ? 6.011   -28.077 66.973  1.00 34.97  ? 74  ALA B N   1 
ATOM   4272 C  CA  . ALA B 1 74  ? 5.586   -27.460 65.721  1.00 33.50  ? 74  ALA B CA  1 
ATOM   4273 C  C   . ALA B 1 74  ? 6.696   -26.588 65.133  1.00 32.00  ? 74  ALA B C   1 
ATOM   4274 O  O   . ALA B 1 74  ? 7.023   -26.689 63.944  1.00 34.78  ? 74  ALA B O   1 
ATOM   4275 C  CB  . ALA B 1 74  ? 4.308   -26.650 65.954  1.00 33.19  ? 74  ALA B CB  1 
ATOM   4276 N  N   . LEU B 1 75  ? 7.302   -25.731 65.955  1.00 32.17  ? 75  LEU B N   1 
ATOM   4277 C  CA  . LEU B 1 75  ? 8.361   -24.882 65.424  1.00 33.67  ? 75  LEU B CA  1 
ATOM   4278 C  C   . LEU B 1 75  ? 9.602   -25.699 65.069  1.00 35.06  ? 75  LEU B C   1 
ATOM   4279 O  O   . LEU B 1 75  ? 10.292  -25.379 64.094  1.00 33.56  ? 75  LEU B O   1 
ATOM   4280 C  CB  . LEU B 1 75  ? 8.698   -23.766 66.420  1.00 31.27  ? 75  LEU B CB  1 
ATOM   4281 C  CG  . LEU B 1 75  ? 7.622   -22.670 66.531  1.00 31.30  ? 75  LEU B CG  1 
ATOM   4282 C  CD1 . LEU B 1 75  ? 8.088   -21.594 67.536  1.00 31.54  ? 75  LEU B CD1 1 
ATOM   4283 C  CD2 . LEU B 1 75  ? 7.330   -22.065 65.171  1.00 31.95  ? 75  LEU B CD2 1 
ATOM   4284 N  N   . LYS B 1 76  ? 9.882   -26.774 65.817  1.00 33.33  ? 76  LYS B N   1 
ATOM   4285 C  CA  . LYS B 1 76  ? 11.041  -27.594 65.478  1.00 36.86  ? 76  LYS B CA  1 
ATOM   4286 C  C   . LYS B 1 76  ? 10.868  -28.237 64.109  1.00 35.81  ? 76  LYS B C   1 
ATOM   4287 O  O   . LYS B 1 76  ? 11.819  -28.316 63.323  1.00 33.72  ? 76  LYS B O   1 
ATOM   4288 C  CB  . LYS B 1 76  ? 11.261  -28.647 66.554  1.00 37.19  ? 76  LYS B CB  1 
ATOM   4289 C  CG  . LYS B 1 76  ? 11.801  -28.049 67.846  1.00 36.51  ? 76  LYS B CG  1 
ATOM   4290 C  CD  . LYS B 1 76  ? 12.052  -29.139 68.867  1.00 38.92  ? 76  LYS B CD  1 
ATOM   4291 C  CE  . LYS B 1 76  ? 12.769  -28.570 70.070  1.00 39.23  ? 76  LYS B CE  1 
ATOM   4292 N  NZ  . LYS B 1 76  ? 12.927  -29.641 71.061  1.00 45.06  ? 76  LYS B NZ  1 
ATOM   4293 N  N   . PHE B 1 77  ? 9.646   -28.658 63.788  1.00 32.80  ? 77  PHE B N   1 
ATOM   4294 C  CA  . PHE B 1 77  ? 9.381   -29.219 62.463  1.00 38.16  ? 77  PHE B CA  1 
ATOM   4295 C  C   . PHE B 1 77  ? 9.469   -28.151 61.374  1.00 37.82  ? 77  PHE B C   1 
ATOM   4296 O  O   . PHE B 1 77  ? 10.003  -28.408 60.288  1.00 39.11  ? 77  PHE B O   1 
ATOM   4297 C  CB  . PHE B 1 77  ? 8.014   -29.893 62.477  1.00 36.69  ? 77  PHE B CB  1 
ATOM   4298 C  CG  . PHE B 1 77  ? 8.025   -31.239 63.142  1.00 41.44  ? 77  PHE B CG  1 
ATOM   4299 C  CD1 . PHE B 1 77  ? 9.169   -32.017 63.131  1.00 43.84  ? 77  PHE B CD1 1 
ATOM   4300 C  CD2 . PHE B 1 77  ? 6.921   -31.687 63.847  1.00 42.42  ? 77  PHE B CD2 1 
ATOM   4301 C  CE1 . PHE B 1 77  ? 9.195   -33.251 63.753  1.00 47.87  ? 77  PHE B CE1 1 
ATOM   4302 C  CE2 . PHE B 1 77  ? 6.943   -32.921 64.481  1.00 44.67  ? 77  PHE B CE2 1 
ATOM   4303 C  CZ  . PHE B 1 77  ? 8.084   -33.699 64.436  1.00 45.65  ? 77  PHE B CZ  1 
ATOM   4304 N  N   . VAL B 1 78  ? 8.987   -26.937 61.654  1.00 32.82  ? 78  VAL B N   1 
ATOM   4305 C  CA  . VAL B 1 78  ? 9.066   -25.862 60.662  1.00 29.64  ? 78  VAL B CA  1 
ATOM   4306 C  C   . VAL B 1 78  ? 10.512  -25.427 60.468  1.00 33.15  ? 78  VAL B C   1 
ATOM   4307 O  O   . VAL B 1 78  ? 10.912  -25.031 59.366  1.00 33.68  ? 78  VAL B O   1 
ATOM   4308 C  CB  . VAL B 1 78  ? 8.179   -24.675 61.079  1.00 34.77  ? 78  VAL B CB  1 
ATOM   4309 C  CG1 . VAL B 1 78  ? 8.439   -23.446 60.193  1.00 31.86  ? 78  VAL B CG1 1 
ATOM   4310 C  CG2 . VAL B 1 78  ? 6.687   -25.066 61.037  1.00 32.24  ? 78  VAL B CG2 1 
ATOM   4311 N  N   . ARG B 1 79  ? 11.316  -25.500 61.526  1.00 32.32  ? 79  ARG B N   1 
ATOM   4312 C  CA  . ARG B 1 79  ? 12.739  -25.181 61.419  1.00 34.50  ? 79  ARG B CA  1 
ATOM   4313 C  C   . ARG B 1 79  ? 13.453  -25.999 60.351  1.00 36.95  ? 79  ARG B C   1 
ATOM   4314 O  O   . ARG B 1 79  ? 14.504  -25.568 59.844  1.00 36.34  ? 79  ARG B O   1 
ATOM   4315 C  CB  . ARG B 1 79  ? 13.421  -25.422 62.763  1.00 31.17  ? 79  ARG B CB  1 
ATOM   4316 C  CG  . ARG B 1 79  ? 14.938  -25.139 62.706  1.00 33.54  ? 79  ARG B CG  1 
ATOM   4317 C  CD  . ARG B 1 79  ? 15.514  -24.991 64.114  1.00 33.36  ? 79  ARG B CD  1 
ATOM   4318 N  NE  . ARG B 1 79  ? 16.968  -24.882 64.076  1.00 36.68  ? 79  ARG B NE  1 
ATOM   4319 C  CZ  . ARG B 1 79  ? 17.665  -23.981 64.756  1.00 41.60  ? 79  ARG B CZ  1 
ATOM   4320 N  NH1 . ARG B 1 79  ? 17.067  -23.052 65.484  1.00 35.94  ? 79  ARG B NH1 1 
ATOM   4321 N  NH2 . ARG B 1 79  ? 18.998  -24.003 64.693  1.00 36.60  ? 79  ARG B NH2 1 
ATOM   4322 N  N   . ASP B 1 80  ? 12.921  -27.177 60.003  1.00 38.04  ? 80  ASP B N   1 
ATOM   4323 C  CA  . ASP B 1 80  ? 13.525  -27.966 58.933  1.00 38.89  ? 80  ASP B CA  1 
ATOM   4324 C  C   . ASP B 1 80  ? 13.543  -27.221 57.611  1.00 38.88  ? 80  ASP B C   1 
ATOM   4325 O  O   . ASP B 1 80  ? 14.368  -27.546 56.745  1.00 40.08  ? 80  ASP B O   1 
ATOM   4326 C  CB  . ASP B 1 80  ? 12.792  -29.296 58.755  1.00 41.95  ? 80  ASP B CB  1 
ATOM   4327 C  CG  . ASP B 1 80  ? 13.206  -30.328 59.788  1.00 44.80  ? 80  ASP B CG  1 
ATOM   4328 O  OD1 . ASP B 1 80  ? 14.258  -30.146 60.440  1.00 45.89  ? 80  ASP B OD1 1 
ATOM   4329 O  OD2 . ASP B 1 80  ? 12.487  -31.330 59.942  1.00 48.68  ? 80  ASP B OD2 1 
ATOM   4330 N  N   . PHE B 1 81  ? 12.647  -26.246 57.412  1.00 34.68  ? 81  PHE B N   1 
ATOM   4331 C  CA  . PHE B 1 81  ? 12.747  -25.389 56.241  1.00 37.82  ? 81  PHE B CA  1 
ATOM   4332 C  C   . PHE B 1 81  ? 12.867  -23.905 56.562  1.00 36.09  ? 81  PHE B C   1 
ATOM   4333 O  O   . PHE B 1 81  ? 13.308  -23.148 55.693  1.00 34.58  ? 81  PHE B O   1 
ATOM   4334 C  CB  . PHE B 1 81  ? 11.565  -25.613 55.268  1.00 39.87  ? 81  PHE B CB  1 
ATOM   4335 C  CG  . PHE B 1 81  ? 10.188  -25.596 55.909  1.00 36.80  ? 81  PHE B CG  1 
ATOM   4336 C  CD1 . PHE B 1 81  ? 9.682   -26.727 56.540  1.00 35.04  ? 81  PHE B CD1 1 
ATOM   4337 C  CD2 . PHE B 1 81  ? 9.376   -24.476 55.803  1.00 39.45  ? 81  PHE B CD2 1 
ATOM   4338 C  CE1 . PHE B 1 81  ? 8.406   -26.726 57.101  1.00 41.47  ? 81  PHE B CE1 1 
ATOM   4339 C  CE2 . PHE B 1 81  ? 8.100   -24.463 56.359  1.00 36.89  ? 81  PHE B CE2 1 
ATOM   4340 C  CZ  . PHE B 1 81  ? 7.612   -25.589 57.011  1.00 38.37  ? 81  PHE B CZ  1 
ATOM   4341 N  N   . ALA B 1 82  ? 12.522  -23.469 57.782  1.00 34.70  ? 82  ALA B N   1 
ATOM   4342 C  CA  . ALA B 1 82  ? 12.725  -22.076 58.157  1.00 33.54  ? 82  ALA B CA  1 
ATOM   4343 C  C   . ALA B 1 82  ? 14.076  -21.834 58.827  1.00 36.65  ? 82  ALA B C   1 
ATOM   4344 O  O   . ALA B 1 82  ? 14.433  -20.671 59.051  1.00 37.76  ? 82  ALA B O   1 
ATOM   4345 C  CB  . ALA B 1 82  ? 11.598  -21.587 59.085  1.00 30.52  ? 82  ALA B CB  1 
ATOM   4346 N  N   . GLY B 1 83  ? 14.815  -22.896 59.158  1.00 36.67  ? 83  GLY B N   1 
ATOM   4347 C  CA  . GLY B 1 83  ? 16.190  -22.774 59.645  1.00 37.49  ? 83  GLY B CA  1 
ATOM   4348 C  C   . GLY B 1 83  ? 16.312  -21.913 60.888  1.00 35.70  ? 83  GLY B C   1 
ATOM   4349 O  O   . GLY B 1 83  ? 15.480  -21.964 61.810  1.00 32.24  ? 83  GLY B O   1 
ATOM   4350 N  N   . ASP B 1 84  ? 17.380  -21.116 60.942  1.00 35.40  ? 84  ASP B N   1 
ATOM   4351 C  CA  . ASP B 1 84  ? 17.550  -20.195 62.065  1.00 35.34  ? 84  ASP B CA  1 
ATOM   4352 C  C   . ASP B 1 84  ? 17.105  -18.794 61.687  1.00 35.76  ? 84  ASP B C   1 
ATOM   4353 O  O   . ASP B 1 84  ? 17.713  -17.785 62.069  1.00 33.84  ? 84  ASP B O   1 
ATOM   4354 C  CB  . ASP B 1 84  ? 18.986  -20.216 62.605  1.00 35.63  ? 84  ASP B CB  1 
ATOM   4355 C  CG  . ASP B 1 84  ? 20.039  -19.873 61.556  1.00 37.25  ? 84  ASP B CG  1 
ATOM   4356 O  OD1 . ASP B 1 84  ? 19.686  -19.662 60.378  1.00 35.18  ? 84  ASP B OD1 1 
ATOM   4357 O  OD2 . ASP B 1 84  ? 21.243  -19.818 61.932  1.00 34.99  ? 84  ASP B OD2 1 
ATOM   4358 N  N   . GLY B 1 85  ? 16.019  -18.709 60.920  1.00 35.66  ? 85  GLY B N   1 
ATOM   4359 C  CA  . GLY B 1 85  ? 15.327  -17.457 60.769  1.00 31.42  ? 85  GLY B CA  1 
ATOM   4360 C  C   . GLY B 1 85  ? 14.724  -17.052 62.099  1.00 31.06  ? 85  GLY B C   1 
ATOM   4361 O  O   . GLY B 1 85  ? 14.776  -17.778 63.094  1.00 33.02  ? 85  GLY B O   1 
ATOM   4362 N  N   . LEU B 1 86  ? 14.123  -15.859 62.111  1.00 28.69  ? 86  LEU B N   1 
ATOM   4363 C  CA  . LEU B 1 86  ? 13.786  -15.214 63.386  1.00 31.22  ? 86  LEU B CA  1 
ATOM   4364 C  C   . LEU B 1 86  ? 12.784  -16.017 64.196  1.00 35.44  ? 86  LEU B C   1 
ATOM   4365 O  O   . LEU B 1 86  ? 12.841  -16.012 65.431  1.00 31.09  ? 86  LEU B O   1 
ATOM   4366 C  CB  . LEU B 1 86  ? 13.232  -13.806 63.151  1.00 30.21  ? 86  LEU B CB  1 
ATOM   4367 C  CG  . LEU B 1 86  ? 14.237  -12.683 62.899  1.00 31.67  ? 86  LEU B CG  1 
ATOM   4368 C  CD1 . LEU B 1 86  ? 13.480  -11.427 62.484  1.00 32.20  ? 86  LEU B CD1 1 
ATOM   4369 C  CD2 . LEU B 1 86  ? 15.074  -12.412 64.135  1.00 32.24  ? 86  LEU B CD2 1 
ATOM   4370 N  N   . ALA B 1 87  ? 11.818  -16.666 63.535  1.00 32.63  ? 87  ALA B N   1 
ATOM   4371 C  CA  . ALA B 1 87  ? 10.734  -17.305 64.291  1.00 31.66  ? 87  ALA B CA  1 
ATOM   4372 C  C   . ALA B 1 87  ? 11.107  -18.695 64.809  1.00 29.37  ? 87  ALA B C   1 
ATOM   4373 O  O   . ALA B 1 87  ? 10.477  -19.186 65.759  1.00 32.50  ? 87  ALA B O   1 
ATOM   4374 C  CB  . ALA B 1 87  ? 9.475   -17.382 63.419  1.00 32.83  ? 87  ALA B CB  1 
ATOM   4375 N  N   . THR B 1 88  ? 12.129  -19.337 64.234  1.00 31.84  ? 88  THR B N   1 
ATOM   4376 C  CA  . THR B 1 88  ? 12.500  -20.696 64.616  1.00 30.27  ? 88  THR B CA  1 
ATOM   4377 C  C   . THR B 1 88  ? 13.903  -20.804 65.211  1.00 32.19  ? 88  THR B C   1 
ATOM   4378 O  O   . THR B 1 88  ? 14.411  -21.924 65.353  1.00 32.44  ? 88  THR B O   1 
ATOM   4379 C  CB  . THR B 1 88  ? 12.383  -21.657 63.431  1.00 32.62  ? 88  THR B CB  1 
ATOM   4380 O  OG1 . THR B 1 88  ? 13.041  -21.105 62.281  1.00 32.50  ? 88  THR B OG1 1 
ATOM   4381 C  CG2 . THR B 1 88  ? 10.903  -21.945 63.110  1.00 32.15  ? 88  THR B CG2 1 
ATOM   4382 N  N   . SER B 1 89  ? 14.534  -19.688 65.568  1.00 32.77  ? 89  SER B N   1 
ATOM   4383 C  CA  . SER B 1 89  ? 15.815  -19.734 66.261  1.00 31.66  ? 89  SER B CA  1 
ATOM   4384 C  C   . SER B 1 89  ? 15.589  -19.620 67.766  1.00 33.81  ? 89  SER B C   1 
ATOM   4385 O  O   . SER B 1 89  ? 14.609  -19.027 68.228  1.00 31.48  ? 89  SER B O   1 
ATOM   4386 C  CB  . SER B 1 89  ? 16.741  -18.605 65.821  1.00 35.02  ? 89  SER B CB  1 
ATOM   4387 O  OG  . SER B 1 89  ? 16.012  -17.412 65.611  1.00 39.64  ? 89  SER B OG  1 
ATOM   4388 N  N   . TRP B 1 90  ? 16.518  -20.187 68.527  1.00 32.09  ? 90  TRP B N   1 
ATOM   4389 C  CA  . TRP B 1 90  ? 16.565  -19.961 69.964  1.00 33.48  ? 90  TRP B CA  1 
ATOM   4390 C  C   . TRP B 1 90  ? 17.121  -18.570 70.247  1.00 35.11  ? 90  TRP B C   1 
ATOM   4391 O  O   . TRP B 1 90  ? 17.939  -18.036 69.489  1.00 33.01  ? 90  TRP B O   1 
ATOM   4392 C  CB  . TRP B 1 90  ? 17.434  -21.022 70.639  1.00 29.11  ? 90  TRP B CB  1 
ATOM   4393 C  CG  . TRP B 1 90  ? 16.981  -22.425 70.375  1.00 33.31  ? 90  TRP B CG  1 
ATOM   4394 C  CD1 . TRP B 1 90  ? 17.336  -23.222 69.321  1.00 34.39  ? 90  TRP B CD1 1 
ATOM   4395 C  CD2 . TRP B 1 90  ? 16.071  -23.201 71.175  1.00 34.66  ? 90  TRP B CD2 1 
ATOM   4396 N  NE1 . TRP B 1 90  ? 16.704  -24.443 69.418  1.00 32.60  ? 90  TRP B NE1 1 
ATOM   4397 C  CE2 . TRP B 1 90  ? 15.927  -24.458 70.546  1.00 35.87  ? 90  TRP B CE2 1 
ATOM   4398 C  CE3 . TRP B 1 90  ? 15.361  -22.953 72.356  1.00 35.72  ? 90  TRP B CE3 1 
ATOM   4399 C  CZ2 . TRP B 1 90  ? 15.102  -25.464 71.061  1.00 36.16  ? 90  TRP B CZ2 1 
ATOM   4400 C  CZ3 . TRP B 1 90  ? 14.533  -23.960 72.868  1.00 33.84  ? 90  TRP B CZ3 1 
ATOM   4401 C  CH2 . TRP B 1 90  ? 14.418  -25.194 72.226  1.00 33.90  ? 90  TRP B CH2 1 
ATOM   4402 N  N   . THR B 1 91  ? 16.692  -17.993 71.366  1.00 30.67  ? 91  THR B N   1 
ATOM   4403 C  CA  . THR B 1 91  ? 17.155  -16.658 71.727  1.00 32.41  ? 91  THR B CA  1 
ATOM   4404 C  C   . THR B 1 91  ? 18.677  -16.585 71.843  1.00 32.69  ? 91  THR B C   1 
ATOM   4405 O  O   . THR B 1 91  ? 19.261  -15.517 71.636  1.00 33.62  ? 91  THR B O   1 
ATOM   4406 C  CB  . THR B 1 91  ? 16.518  -16.238 73.048  1.00 32.50  ? 91  THR B CB  1 
ATOM   4407 O  OG1 . THR B 1 91  ? 15.095  -16.328 72.932  1.00 33.09  ? 91  THR B OG1 1 
ATOM   4408 C  CG2 . THR B 1 91  ? 16.910  -14.797 73.381  1.00 37.31  ? 91  THR B CG2 1 
ATOM   4409 N  N   . HIS B 1 92  ? 19.329  -17.691 72.191  1.00 30.77  ? 92  HIS B N   1 
ATOM   4410 C  CA  . HIS B 1 92  ? 20.771  -17.693 72.432  1.00 33.59  ? 92  HIS B CA  1 
ATOM   4411 C  C   . HIS B 1 92  ? 21.594  -18.003 71.191  1.00 33.26  ? 92  HIS B C   1 
ATOM   4412 O  O   . HIS B 1 92  ? 22.832  -17.974 71.255  1.00 32.37  ? 92  HIS B O   1 
ATOM   4413 C  CB  . HIS B 1 92  ? 21.109  -18.703 73.536  1.00 33.22  ? 92  HIS B CB  1 
ATOM   4414 C  CG  . HIS B 1 92  ? 20.483  -20.043 73.318  1.00 31.25  ? 92  HIS B CG  1 
ATOM   4415 N  ND1 . HIS B 1 92  ? 20.934  -20.925 72.364  1.00 32.45  ? 92  HIS B ND1 1 
ATOM   4416 C  CD2 . HIS B 1 92  ? 19.437  -20.650 73.930  1.00 34.94  ? 92  HIS B CD2 1 
ATOM   4417 C  CE1 . HIS B 1 92  ? 20.192  -22.020 72.392  1.00 35.24  ? 92  HIS B CE1 1 
ATOM   4418 N  NE2 . HIS B 1 92  ? 19.275  -21.877 73.332  1.00 33.40  ? 92  HIS B NE2 1 
ATOM   4419 N  N   . GLU B 1 93  ? 20.962  -18.308 70.064  1.00 32.15  ? 93  GLU B N   1 
ATOM   4420 C  CA  . GLU B 1 93  ? 21.714  -18.509 68.839  1.00 32.67  ? 93  GLU B CA  1 
ATOM   4421 C  C   . GLU B 1 93  ? 22.158  -17.157 68.306  1.00 35.33  ? 93  GLU B C   1 
ATOM   4422 O  O   . GLU B 1 93  ? 21.361  -16.220 68.231  1.00 34.45  ? 93  GLU B O   1 
ATOM   4423 C  CB  . GLU B 1 93  ? 20.871  -19.234 67.798  1.00 33.90  ? 93  GLU B CB  1 
ATOM   4424 C  CG  . GLU B 1 93  ? 20.691  -20.709 68.058  1.00 35.00  ? 93  GLU B CG  1 
ATOM   4425 C  CD  . GLU B 1 93  ? 19.874  -21.358 66.959  1.00 37.71  ? 93  GLU B CD  1 
ATOM   4426 O  OE1 . GLU B 1 93  ? 18.630  -21.266 67.003  1.00 33.30  ? 93  GLU B OE1 1 
ATOM   4427 O  OE2 . GLU B 1 93  ? 20.466  -21.948 66.040  1.00 39.17  ? 93  GLU B OE2 1 
ATOM   4428 N  N   . LYS B 1 94  ? 23.443  -17.055 67.952  1.00 32.79  ? 94  LYS B N   1 
ATOM   4429 C  CA  . LYS B 1 94  ? 23.988  -15.788 67.479  1.00 33.90  ? 94  LYS B CA  1 
ATOM   4430 C  C   . LYS B 1 94  ? 23.097  -15.151 66.412  1.00 32.29  ? 94  LYS B C   1 
ATOM   4431 O  O   . LYS B 1 94  ? 22.913  -13.930 66.397  1.00 32.33  ? 94  LYS B O   1 
ATOM   4432 C  CB  . LYS B 1 94  ? 25.399  -16.009 66.930  1.00 33.30  ? 94  LYS B CB  1 
ATOM   4433 C  CG  . LYS B 1 94  ? 26.027  -14.794 66.256  1.00 38.50  ? 94  LYS B CG  1 
ATOM   4434 C  CD  . LYS B 1 94  ? 27.420  -15.173 65.702  1.00 33.40  ? 94  LYS B CD  1 
ATOM   4435 C  CE  . LYS B 1 94  ? 28.162  -13.948 65.214  1.00 42.38  ? 94  LYS B CE  1 
ATOM   4436 N  NZ  . LYS B 1 94  ? 29.565  -14.271 64.738  1.00 38.33  ? 94  LYS B NZ  1 
ATOM   4437 N  N   . ASN B 1 95  ? 22.536  -15.962 65.513  1.00 33.65  ? 95  ASN B N   1 
ATOM   4438 C  CA  . ASN B 1 95  ? 21.765  -15.408 64.407  1.00 33.80  ? 95  ASN B CA  1 
ATOM   4439 C  C   . ASN B 1 95  ? 20.427  -14.819 64.832  1.00 33.13  ? 95  ASN B C   1 
ATOM   4440 O  O   . ASN B 1 95  ? 19.832  -14.066 64.046  1.00 32.55  ? 95  ASN B O   1 
ATOM   4441 C  CB  . ASN B 1 95  ? 21.518  -16.462 63.334  1.00 33.16  ? 95  ASN B CB  1 
ATOM   4442 C  CG  . ASN B 1 95  ? 22.604  -16.485 62.304  1.00 39.06  ? 95  ASN B CG  1 
ATOM   4443 O  OD1 . ASN B 1 95  ? 23.344  -15.508 62.160  1.00 34.43  ? 95  ASN B OD1 1 
ATOM   4444 N  ND2 . ASN B 1 95  ? 22.701  -17.583 61.560  1.00 37.59  ? 95  ASN B ND2 1 
ATOM   4445 N  N   . TRP B 1 96  ? 19.917  -15.146 66.023  1.00 33.41  ? 96  TRP B N   1 
ATOM   4446 C  CA  . TRP B 1 96  ? 18.661  -14.519 66.439  1.00 34.42  ? 96  TRP B CA  1 
ATOM   4447 C  C   . TRP B 1 96  ? 18.858  -13.025 66.692  1.00 34.38  ? 96  TRP B C   1 
ATOM   4448 O  O   . TRP B 1 96  ? 18.217  -12.184 66.053  1.00 30.35  ? 96  TRP B O   1 
ATOM   4449 C  CB  . TRP B 1 96  ? 18.056  -15.165 67.694  1.00 30.91  ? 96  TRP B CB  1 
ATOM   4450 C  CG  . TRP B 1 96  ? 16.816  -14.396 67.966  1.00 30.46  ? 96  TRP B CG  1 
ATOM   4451 C  CD1 . TRP B 1 96  ? 15.675  -14.387 67.194  1.00 31.51  ? 96  TRP B CD1 1 
ATOM   4452 C  CD2 . TRP B 1 96  ? 16.653  -13.335 68.914  1.00 32.93  ? 96  TRP B CD2 1 
ATOM   4453 N  NE1 . TRP B 1 96  ? 14.784  -13.455 67.669  1.00 32.08  ? 96  TRP B NE1 1 
ATOM   4454 C  CE2 . TRP B 1 96  ? 15.361  -12.783 68.712  1.00 32.01  ? 96  TRP B CE2 1 
ATOM   4455 C  CE3 . TRP B 1 96  ? 17.458  -12.812 69.933  1.00 34.65  ? 96  TRP B CE3 1 
ATOM   4456 C  CZ2 . TRP B 1 96  ? 14.852  -11.755 69.507  1.00 34.59  ? 96  TRP B CZ2 1 
ATOM   4457 C  CZ3 . TRP B 1 96  ? 16.956  -11.774 70.714  1.00 33.92  ? 96  TRP B CZ3 1 
ATOM   4458 C  CH2 . TRP B 1 96  ? 15.660  -11.263 70.500  1.00 35.07  ? 96  TRP B CH2 1 
ATOM   4459 N  N   . LYS B 1 97  ? 19.739  -12.675 67.635  1.00 31.87  ? 97  LYS B N   1 
ATOM   4460 C  CA  . LYS B 1 97  ? 19.895  -11.266 67.995  1.00 30.11  ? 97  LYS B CA  1 
ATOM   4461 C  C   . LYS B 1 97  ? 20.470  -10.476 66.837  1.00 32.63  ? 97  LYS B C   1 
ATOM   4462 O  O   . LYS B 1 97  ? 20.107  -9.311  66.627  1.00 34.13  ? 97  LYS B O   1 
ATOM   4463 C  CB  . LYS B 1 97  ? 20.785  -11.121 69.239  1.00 32.05  ? 97  LYS B CB  1 
ATOM   4464 C  CG  . LYS B 1 97  ? 20.794  -9.705  69.802  1.00 38.45  ? 97  LYS B CG  1 
ATOM   4465 C  CD  . LYS B 1 97  ? 19.382  -9.237  70.163  1.00 38.84  ? 97  LYS B CD  1 
ATOM   4466 C  CE  . LYS B 1 97  ? 19.370  -7.803  70.690  1.00 38.92  ? 97  LYS B CE  1 
ATOM   4467 N  NZ  . LYS B 1 97  ? 19.984  -7.696  72.032  1.00 38.21  ? 97  LYS B NZ  1 
ATOM   4468 N  N   . LYS B 1 98  ? 21.341  -11.100 66.052  1.00 33.64  ? 98  LYS B N   1 
ATOM   4469 C  CA  . LYS B 1 98  ? 21.938  -10.389 64.937  1.00 32.39  ? 98  LYS B CA  1 
ATOM   4470 C  C   . LYS B 1 98  ? 20.877  -10.035 63.891  1.00 34.86  ? 98  LYS B C   1 
ATOM   4471 O  O   . LYS B 1 98  ? 20.791  -8.880  63.453  1.00 33.83  ? 98  LYS B O   1 
ATOM   4472 C  CB  . LYS B 1 98  ? 23.084  -11.230 64.373  1.00 37.02  ? 98  LYS B CB  1 
ATOM   4473 C  CG  . LYS B 1 98  ? 23.339  -11.081 62.925  1.00 41.30  ? 98  LYS B CG  1 
ATOM   4474 C  CD  . LYS B 1 98  ? 24.430  -12.054 62.494  1.00 42.22  ? 98  LYS B CD  1 
ATOM   4475 C  CE  . LYS B 1 98  ? 25.398  -11.421 61.556  1.00 35.16  ? 98  LYS B CE  1 
ATOM   4476 N  NZ  . LYS B 1 98  ? 26.361  -12.452 61.103  1.00 36.52  ? 98  LYS B NZ  1 
ATOM   4477 N  N   . ALA B 1 99  ? 20.014  -10.991 63.527  1.00 30.14  ? 99  ALA B N   1 
ATOM   4478 C  CA  . ALA B 1 99  ? 18.927  -10.671 62.596  1.00 34.87  ? 99  ALA B CA  1 
ATOM   4479 C  C   . ALA B 1 99  ? 17.914  -9.723  63.232  1.00 33.35  ? 99  ALA B C   1 
ATOM   4480 O  O   . ALA B 1 99  ? 17.427  -8.792  62.574  1.00 33.65  ? 99  ALA B O   1 
ATOM   4481 C  CB  . ALA B 1 99  ? 18.234  -11.947 62.112  1.00 32.20  ? 99  ALA B CB  1 
ATOM   4482 N  N   . HIS B 1 100 ? 17.557  -9.967  64.494  1.00 33.80  ? 100 HIS B N   1 
ATOM   4483 C  CA  . HIS B 1 100 ? 16.734  -9.022  65.239  1.00 33.00  ? 100 HIS B CA  1 
ATOM   4484 C  C   . HIS B 1 100 ? 17.230  -7.591  65.101  1.00 38.43  ? 100 HIS B C   1 
ATOM   4485 O  O   . HIS B 1 100 ? 16.474  -6.699  64.711  1.00 35.89  ? 100 HIS B O   1 
ATOM   4486 C  CB  . HIS B 1 100 ? 16.674  -9.408  66.711  1.00 36.88  ? 100 HIS B CB  1 
ATOM   4487 C  CG  . HIS B 1 100 ? 15.736  -8.558  67.513  1.00 38.83  ? 100 HIS B CG  1 
ATOM   4488 N  ND1 . HIS B 1 100 ? 14.371  -8.543  67.320  1.00 39.92  ? 100 HIS B ND1 1 
ATOM   4489 C  CD2 . HIS B 1 100 ? 15.989  -7.651  68.490  1.00 39.44  ? 100 HIS B CD2 1 
ATOM   4490 C  CE1 . HIS B 1 100 ? 13.822  -7.681  68.158  1.00 39.75  ? 100 HIS B CE1 1 
ATOM   4491 N  NE2 . HIS B 1 100 ? 14.783  -7.124  68.877  1.00 41.49  ? 100 HIS B NE2 1 
ATOM   4492 N  N   . ASN B 1 101 ? 18.490  -7.344  65.471  1.00 33.26  ? 101 ASN B N   1 
ATOM   4493 C  CA  . ASN B 1 101 ? 19.020  -5.985  65.409  1.00 37.42  ? 101 ASN B CA  1 
ATOM   4494 C  C   . ASN B 1 101 ? 18.948  -5.429  63.994  1.00 33.60  ? 101 ASN B C   1 
ATOM   4495 O  O   . ASN B 1 101 ? 18.625  -4.251  63.798  1.00 37.13  ? 101 ASN B O   1 
ATOM   4496 C  CB  . ASN B 1 101 ? 20.465  -5.952  65.915  1.00 33.45  ? 101 ASN B CB  1 
ATOM   4497 C  CG  . ASN B 1 101 ? 20.558  -6.105  67.424  1.00 37.16  ? 101 ASN B CG  1 
ATOM   4498 O  OD1 . ASN B 1 101 ? 19.564  -5.946  68.138  1.00 37.22  ? 101 ASN B OD1 1 
ATOM   4499 N  ND2 . ASN B 1 101 ? 21.761  -6.404  67.923  1.00 35.40  ? 101 ASN B ND2 1 
ATOM   4500 N  N   . ILE B 1 102 ? 19.272  -6.248  62.998  1.00 33.79  ? 102 ILE B N   1 
ATOM   4501 C  CA  . ILE B 1 102 ? 19.332  -5.749  61.632  1.00 35.10  ? 102 ILE B CA  1 
ATOM   4502 C  C   . ILE B 1 102 ? 17.938  -5.407  61.122  1.00 37.96  ? 102 ILE B C   1 
ATOM   4503 O  O   . ILE B 1 102 ? 17.749  -4.391  60.448  1.00 35.87  ? 102 ILE B O   1 
ATOM   4504 C  CB  . ILE B 1 102 ? 20.043  -6.760  60.719  1.00 33.90  ? 102 ILE B CB  1 
ATOM   4505 C  CG1 . ILE B 1 102 ? 21.541  -6.801  61.041  1.00 33.59  ? 102 ILE B CG1 1 
ATOM   4506 C  CG2 . ILE B 1 102 ? 19.831  -6.422  59.235  1.00 35.23  ? 102 ILE B CG2 1 
ATOM   4507 C  CD1 . ILE B 1 102 ? 22.216  -8.017  60.509  1.00 33.29  ? 102 ILE B CD1 1 
ATOM   4508 N  N   . LEU B 1 103 ? 16.938  -6.219  61.469  1.00 35.19  ? 103 LEU B N   1 
ATOM   4509 C  CA  . LEU B 1 103 ? 15.624  -6.114  60.843  1.00 34.06  ? 103 LEU B CA  1 
ATOM   4510 C  C   . LEU B 1 103 ? 14.611  -5.292  61.635  1.00 36.29  ? 103 LEU B C   1 
ATOM   4511 O  O   . LEU B 1 103 ? 13.634  -4.817  61.041  1.00 33.26  ? 103 LEU B O   1 
ATOM   4512 C  CB  . LEU B 1 103 ? 15.056  -7.519  60.581  1.00 32.02  ? 103 LEU B CB  1 
ATOM   4513 C  CG  . LEU B 1 103 ? 15.602  -8.275  59.361  1.00 37.82  ? 103 LEU B CG  1 
ATOM   4514 C  CD1 . LEU B 1 103 ? 15.388  -9.784  59.493  1.00 36.92  ? 103 LEU B CD1 1 
ATOM   4515 C  CD2 . LEU B 1 103 ? 14.966  -7.778  58.084  1.00 33.82  ? 103 LEU B CD2 1 
ATOM   4516 N  N   . LEU B 1 104 ? 14.808  -5.088  62.937  1.00 34.11  ? 104 LEU B N   1 
ATOM   4517 C  CA  . LEU B 1 104 ? 13.856  -4.290  63.716  1.00 35.72  ? 104 LEU B CA  1 
ATOM   4518 C  C   . LEU B 1 104 ? 13.514  -2.951  63.072  1.00 39.52  ? 104 LEU B C   1 
ATOM   4519 O  O   . LEU B 1 104 ? 12.318  -2.616  62.988  1.00 40.17  ? 104 LEU B O   1 
ATOM   4520 C  CB  . LEU B 1 104 ? 14.391  -4.049  65.134  1.00 36.39  ? 104 LEU B CB  1 
ATOM   4521 C  CG  . LEU B 1 104 ? 13.310  -3.789  66.197  1.00 41.54  ? 104 LEU B CG  1 
ATOM   4522 C  CD1 . LEU B 1 104 ? 12.159  -4.782  66.132  1.00 39.15  ? 104 LEU B CD1 1 
ATOM   4523 C  CD2 . LEU B 1 104 ? 13.880  -3.672  67.638  1.00 43.20  ? 104 LEU B CD2 1 
ATOM   4524 N  N   . PRO B 1 105 ? 14.479  -2.147  62.618  1.00 40.74  ? 105 PRO B N   1 
ATOM   4525 C  CA  . PRO B 1 105 ? 14.118  -0.861  62.002  1.00 43.71  ? 105 PRO B CA  1 
ATOM   4526 C  C   . PRO B 1 105 ? 13.230  -0.998  60.774  1.00 41.85  ? 105 PRO B C   1 
ATOM   4527 O  O   . PRO B 1 105 ? 12.433  -0.091  60.503  1.00 45.88  ? 105 PRO B O   1 
ATOM   4528 C  CB  . PRO B 1 105 ? 15.485  -0.245  61.649  1.00 40.19  ? 105 PRO B CB  1 
ATOM   4529 C  CG  . PRO B 1 105 ? 16.471  -0.964  62.534  1.00 46.01  ? 105 PRO B CG  1 
ATOM   4530 C  CD  . PRO B 1 105 ? 15.940  -2.348  62.680  1.00 39.56  ? 105 PRO B CD  1 
ATOM   4531 N  N   . SER B 1 106 ? 13.353  -2.093  60.020  1.00 33.77  ? 106 SER B N   1 
ATOM   4532 C  CA  . SER B 1 106 ? 12.563  -2.314  58.819  1.00 35.19  ? 106 SER B CA  1 
ATOM   4533 C  C   . SER B 1 106 ? 11.097  -2.606  59.116  1.00 35.87  ? 106 SER B C   1 
ATOM   4534 O  O   . SER B 1 106 ? 10.296  -2.659  58.180  1.00 37.61  ? 106 SER B O   1 
ATOM   4535 C  CB  . SER B 1 106 ? 13.150  -3.478  58.025  1.00 42.02  ? 106 SER B CB  1 
ATOM   4536 O  OG  . SER B 1 106 ? 14.391  -3.112  57.449  1.00 45.90  ? 106 SER B OG  1 
ATOM   4537 N  N   . PHE B 1 107 ? 10.734  -2.805  60.380  1.00 35.22  ? 107 PHE B N   1 
ATOM   4538 C  CA  . PHE B 1 107 ? 9.397   -3.255  60.756  1.00 36.18  ? 107 PHE B CA  1 
ATOM   4539 C  C   . PHE B 1 107 ? 8.703   -2.279  61.689  1.00 39.08  ? 107 PHE B C   1 
ATOM   4540 O  O   . PHE B 1 107 ? 7.624   -2.594  62.215  1.00 37.08  ? 107 PHE B O   1 
ATOM   4541 C  CB  . PHE B 1 107 ? 9.477   -4.639  61.397  1.00 31.76  ? 107 PHE B CB  1 
ATOM   4542 C  CG  . PHE B 1 107 ? 9.540   -5.743  60.399  1.00 36.81  ? 107 PHE B CG  1 
ATOM   4543 C  CD1 . PHE B 1 107 ? 8.403   -6.116  59.695  1.00 35.87  ? 107 PHE B CD1 1 
ATOM   4544 C  CD2 . PHE B 1 107 ? 10.743  -6.368  60.103  1.00 39.40  ? 107 PHE B CD2 1 
ATOM   4545 C  CE1 . PHE B 1 107 ? 8.452   -7.114  58.750  1.00 36.49  ? 107 PHE B CE1 1 
ATOM   4546 C  CE2 . PHE B 1 107 ? 10.803  -7.376  59.142  1.00 39.17  ? 107 PHE B CE2 1 
ATOM   4547 C  CZ  . PHE B 1 107 ? 9.652   -7.751  58.472  1.00 42.86  ? 107 PHE B CZ  1 
ATOM   4548 N  N   . SER B 1 108 ? 9.304   -1.108  61.910  1.00 38.34  ? 108 SER B N   1 
ATOM   4549 C  CA  . SER B 1 108 ? 8.758   -0.110  62.812  1.00 39.20  ? 108 SER B CA  1 
ATOM   4550 C  C   . SER B 1 108 ? 7.499   0.508   62.226  1.00 40.61  ? 108 SER B C   1 
ATOM   4551 O  O   . SER B 1 108 ? 7.211   0.394   61.028  1.00 42.11  ? 108 SER B O   1 
ATOM   4552 C  CB  . SER B 1 108 ? 9.780   1.000   63.058  1.00 41.08  ? 108 SER B CB  1 
ATOM   4553 O  OG  . SER B 1 108 ? 10.004  1.717   61.840  1.00 38.82  ? 108 SER B OG  1 
ATOM   4554 N  N   . GLN B 1 109 ? 6.753   1.197   63.085  1.00 42.55  ? 109 GLN B N   1 
ATOM   4555 C  CA  . GLN B 1 109 ? 5.621   1.973   62.596  1.00 44.51  ? 109 GLN B CA  1 
ATOM   4556 C  C   . GLN B 1 109 ? 6.070   2.967   61.532  1.00 40.01  ? 109 GLN B C   1 
ATOM   4557 O  O   . GLN B 1 109 ? 5.421   3.109   60.489  1.00 41.87  ? 109 GLN B O   1 
ATOM   4558 C  CB  . GLN B 1 109 ? 4.927   2.675   63.765  1.00 42.20  ? 109 GLN B CB  1 
ATOM   4559 C  CG  . GLN B 1 109 ? 3.553   3.262   63.449  1.00 46.66  ? 109 GLN B CG  1 
ATOM   4560 C  CD  . GLN B 1 109 ? 2.623   2.307   62.718  1.00 47.64  ? 109 GLN B CD  1 
ATOM   4561 O  OE1 . GLN B 1 109 ? 2.067   2.654   61.666  1.00 48.50  ? 109 GLN B OE1 1 
ATOM   4562 N  NE2 . GLN B 1 109 ? 2.424   1.108   63.278  1.00 43.90  ? 109 GLN B NE2 1 
ATOM   4563 N  N   . GLN B 1 110 ? 7.194   3.649   61.761  1.00 45.00  ? 110 GLN B N   1 
ATOM   4564 C  CA  . GLN B 1 110 ? 7.688   4.579   60.754  1.00 44.62  ? 110 GLN B CA  1 
ATOM   4565 C  C   . GLN B 1 110 ? 8.007   3.877   59.438  1.00 46.64  ? 110 GLN B C   1 
ATOM   4566 O  O   . GLN B 1 110 ? 7.763   4.435   58.361  1.00 47.06  ? 110 GLN B O   1 
ATOM   4567 C  CB  . GLN B 1 110 ? 8.901   5.339   61.286  1.00 52.59  ? 110 GLN B CB  1 
ATOM   4568 C  CG  . GLN B 1 110 ? 9.490   6.257   60.240  1.00 59.87  ? 110 GLN B CG  1 
ATOM   4569 C  CD  . GLN B 1 110 ? 8.773   7.597   60.162  1.00 60.08  ? 110 GLN B CD  1 
ATOM   4570 O  OE1 . GLN B 1 110 ? 7.843   7.879   60.933  1.00 55.79  ? 110 GLN B OE1 1 
ATOM   4571 N  NE2 . GLN B 1 110 ? 9.192   8.424   59.209  1.00 60.63  ? 110 GLN B NE2 1 
ATOM   4572 N  N   . ALA B 1 111 ? 8.539   2.648   59.497  1.00 41.24  ? 111 ALA B N   1 
ATOM   4573 C  CA  . ALA B 1 111 ? 8.799   1.894   58.272  1.00 39.17  ? 111 ALA B CA  1 
ATOM   4574 C  C   . ALA B 1 111 ? 7.529   1.625   57.471  1.00 34.56  ? 111 ALA B C   1 
ATOM   4575 O  O   . ALA B 1 111 ? 7.605   1.395   56.259  1.00 33.15  ? 111 ALA B O   1 
ATOM   4576 C  CB  . ALA B 1 111 ? 9.474   0.561   58.599  1.00 40.87  ? 111 ALA B CB  1 
ATOM   4577 N  N   . MET B 1 112 ? 6.363   1.664   58.117  1.00 34.83  ? 112 MET B N   1 
ATOM   4578 C  CA  . MET B 1 112 ? 5.120   1.331   57.433  1.00 39.35  ? 112 MET B CA  1 
ATOM   4579 C  C   . MET B 1 112 ? 4.793   2.345   56.350  1.00 38.67  ? 112 MET B C   1 
ATOM   4580 O  O   . MET B 1 112 ? 4.076   2.021   55.391  1.00 37.10  ? 112 MET B O   1 
ATOM   4581 C  CB  . MET B 1 112 ? 3.980   1.289   58.443  1.00 39.78  ? 112 MET B CB  1 
ATOM   4582 C  CG  . MET B 1 112 ? 3.858   -0.007  59.246  1.00 39.80  ? 112 MET B CG  1 
ATOM   4583 S  SD  . MET B 1 112 ? 4.419   -1.502  58.438  1.00 40.16  ? 112 MET B SD  1 
ATOM   4584 C  CE  . MET B 1 112 ? 5.937   -1.828  59.353  1.00 41.27  ? 112 MET B CE  1 
ATOM   4585 N  N   . LYS B 1 113 ? 5.292   3.576   56.505  1.00 38.96  ? 113 LYS B N   1 
ATOM   4586 C  CA  . LYS B 1 113 ? 5.102   4.616   55.501  1.00 35.79  ? 113 LYS B CA  1 
ATOM   4587 C  C   . LYS B 1 113 ? 5.675   4.184   54.162  1.00 38.65  ? 113 LYS B C   1 
ATOM   4588 O  O   . LYS B 1 113 ? 5.093   4.462   53.103  1.00 34.39  ? 113 LYS B O   1 
ATOM   4589 C  CB  . LYS B 1 113 ? 5.782   5.906   55.970  1.00 38.58  ? 113 LYS B CB  1 
ATOM   4590 C  CG  . LYS B 1 113 ? 5.084   6.596   57.136  1.00 43.03  ? 113 LYS B CG  1 
ATOM   4591 C  CD  . LYS B 1 113 ? 5.931   7.787   57.628  1.00 45.27  ? 113 LYS B CD  1 
ATOM   4592 C  CE  . LYS B 1 113 ? 5.539   8.222   59.025  1.00 54.31  ? 113 LYS B CE  1 
ATOM   4593 N  NZ  . LYS B 1 113 ? 5.254   9.683   59.101  1.00 56.28  ? 113 LYS B NZ  1 
ATOM   4594 N  N   . GLY B 1 114 ? 6.820   3.500   54.191  1.00 33.87  ? 114 GLY B N   1 
ATOM   4595 C  CA  . GLY B 1 114 ? 7.459   3.088   52.957  1.00 39.55  ? 114 GLY B CA  1 
ATOM   4596 C  C   . GLY B 1 114 ? 6.826   1.875   52.311  1.00 41.41  ? 114 GLY B C   1 
ATOM   4597 O  O   . GLY B 1 114 ? 6.939   1.695   51.096  1.00 43.21  ? 114 GLY B O   1 
ATOM   4598 N  N   . TYR B 1 115 ? 6.167   1.022   53.102  1.00 37.76  ? 115 TYR B N   1 
ATOM   4599 C  CA  . TYR B 1 115 ? 5.459   -0.129  52.545  1.00 36.35  ? 115 TYR B CA  1 
ATOM   4600 C  C   . TYR B 1 115 ? 4.076   0.231   52.039  1.00 37.14  ? 115 TYR B C   1 
ATOM   4601 O  O   . TYR B 1 115 ? 3.490   -0.544  51.265  1.00 33.71  ? 115 TYR B O   1 
ATOM   4602 C  CB  . TYR B 1 115 ? 5.310   -1.235  53.593  1.00 31.20  ? 115 TYR B CB  1 
ATOM   4603 C  CG  . TYR B 1 115 ? 6.617   -1.781  54.100  1.00 37.20  ? 115 TYR B CG  1 
ATOM   4604 C  CD1 . TYR B 1 115 ? 7.616   -2.172  53.210  1.00 39.23  ? 115 TYR B CD1 1 
ATOM   4605 C  CD2 . TYR B 1 115 ? 6.854   -1.924  55.454  1.00 36.05  ? 115 TYR B CD2 1 
ATOM   4606 C  CE1 . TYR B 1 115 ? 8.816   -2.689  53.667  1.00 38.89  ? 115 TYR B CE1 1 
ATOM   4607 C  CE2 . TYR B 1 115 ? 8.056   -2.443  55.924  1.00 37.42  ? 115 TYR B CE2 1 
ATOM   4608 C  CZ  . TYR B 1 115 ? 9.030   -2.814  55.026  1.00 39.35  ? 115 TYR B CZ  1 
ATOM   4609 O  OH  . TYR B 1 115 ? 10.220  -3.321  55.488  1.00 40.22  ? 115 TYR B OH  1 
ATOM   4610 N  N   . HIS B 1 116 ? 3.558   1.393   52.437  1.00 34.97  ? 116 HIS B N   1 
ATOM   4611 C  CA  . HIS B 1 116 ? 2.137   1.681   52.246  1.00 35.77  ? 116 HIS B CA  1 
ATOM   4612 C  C   . HIS B 1 116 ? 1.735   1.629   50.776  1.00 34.05  ? 116 HIS B C   1 
ATOM   4613 O  O   . HIS B 1 116 ? 0.684   1.074   50.427  1.00 33.29  ? 116 HIS B O   1 
ATOM   4614 C  CB  . HIS B 1 116 ? 1.783   3.044   52.836  1.00 37.35  ? 116 HIS B CB  1 
ATOM   4615 C  CG  . HIS B 1 116 ? 0.349   3.420   52.616  1.00 35.88  ? 116 HIS B CG  1 
ATOM   4616 N  ND1 . HIS B 1 116 ? -0.655  3.057   53.487  1.00 36.31  ? 116 HIS B ND1 1 
ATOM   4617 C  CD2 . HIS B 1 116 ? -0.255  4.076   51.596  1.00 36.87  ? 116 HIS B CD2 1 
ATOM   4618 C  CE1 . HIS B 1 116 ? -1.814  3.488   53.023  1.00 36.22  ? 116 HIS B CE1 1 
ATOM   4619 N  NE2 . HIS B 1 116 ? -1.600  4.111   51.877  1.00 36.14  ? 116 HIS B NE2 1 
ATOM   4620 N  N   . ALA B 1 117 ? 2.530   2.250   49.900  1.00 33.63  ? 117 ALA B N   1 
ATOM   4621 C  CA  . ALA B 1 117 ? 2.150   2.306   48.492  1.00 34.62  ? 117 ALA B CA  1 
ATOM   4622 C  C   . ALA B 1 117 ? 2.000   0.910   47.894  1.00 35.30  ? 117 ALA B C   1 
ATOM   4623 O  O   . ALA B 1 117 ? 1.075   0.660   47.107  1.00 36.09  ? 117 ALA B O   1 
ATOM   4624 C  CB  . ALA B 1 117 ? 3.171   3.127   47.701  1.00 36.11  ? 117 ALA B CB  1 
ATOM   4625 N  N   . MET B 1 118 ? 2.901   -0.016  48.235  1.00 32.57  ? 118 MET B N   1 
ATOM   4626 C  CA  . MET B 1 118 ? 2.818   -1.335  47.602  1.00 36.52  ? 118 MET B CA  1 
ATOM   4627 C  C   . MET B 1 118 ? 1.729   -2.183  48.257  1.00 32.79  ? 118 MET B C   1 
ATOM   4628 O  O   . MET B 1 118 ? 1.162   -3.094  47.630  1.00 33.60  ? 118 MET B O   1 
ATOM   4629 C  CB  . MET B 1 118 ? 4.161   -2.051  47.685  1.00 37.14  ? 118 MET B CB  1 
ATOM   4630 C  CG  . MET B 1 118 ? 5.142   -1.580  46.593  1.00 37.16  ? 118 MET B CG  1 
ATOM   4631 S  SD  . MET B 1 118 ? 4.558   -1.557  44.891  1.00 50.10  ? 118 MET B SD  1 
ATOM   4632 C  CE  . MET B 1 118 ? 4.115   0.155   44.651  1.00 40.35  ? 118 MET B CE  1 
ATOM   4633 N  N   . MET B 1 119 ? 1.456   -1.909  49.527  1.00 31.45  ? 119 MET B N   1 
ATOM   4634 C  CA  . MET B 1 119 ? 0.292   -2.463  50.212  1.00 32.17  ? 119 MET B CA  1 
ATOM   4635 C  C   . MET B 1 119 ? -0.992  -2.090  49.467  1.00 29.20  ? 119 MET B C   1 
ATOM   4636 O  O   . MET B 1 119 ? -1.859  -2.942  49.193  1.00 30.86  ? 119 MET B O   1 
ATOM   4637 C  CB  . MET B 1 119 ? 0.345   -1.871  51.617  1.00 34.59  ? 119 MET B CB  1 
ATOM   4638 C  CG  . MET B 1 119 ? 1.245   -2.679  52.568  1.00 32.37  ? 119 MET B CG  1 
ATOM   4639 S  SD  . MET B 1 119 ? 0.721   -2.570  54.278  1.00 35.14  ? 119 MET B SD  1 
ATOM   4640 C  CE  . MET B 1 119 ? 2.236   -3.115  55.076  1.00 31.86  ? 119 MET B CE  1 
ATOM   4641 N  N   . VAL B 1 120 ? -1.107  -0.813  49.095  1.00 29.79  ? 120 VAL B N   1 
ATOM   4642 C  CA  . VAL B 1 120 ? -2.261  -0.322  48.333  1.00 31.86  ? 120 VAL B CA  1 
ATOM   4643 C  C   . VAL B 1 120 ? -2.339  -1.005  46.965  1.00 32.61  ? 120 VAL B C   1 
ATOM   4644 O  O   . VAL B 1 120 ? -3.429  -1.314  46.461  1.00 32.52  ? 120 VAL B O   1 
ATOM   4645 C  CB  . VAL B 1 120 ? -2.178  1.212   48.194  1.00 32.48  ? 120 VAL B CB  1 
ATOM   4646 C  CG1 . VAL B 1 120 ? -3.238  1.741   47.199  1.00 36.03  ? 120 VAL B CG1 1 
ATOM   4647 C  CG2 . VAL B 1 120 ? -2.310  1.905   49.562  1.00 33.28  ? 120 VAL B CG2 1 
ATOM   4648 N  N   . ASP B 1 121 ? -1.187  -1.245  46.339  1.00 33.70  ? 121 ASP B N   1 
ATOM   4649 C  CA  . ASP B 1 121 ? -1.169  -1.886  45.023  1.00 36.38  ? 121 ASP B CA  1 
ATOM   4650 C  C   . ASP B 1 121 ? -1.912  -3.226  45.053  1.00 34.27  ? 121 ASP B C   1 
ATOM   4651 O  O   . ASP B 1 121 ? -2.768  -3.505  44.201  1.00 33.23  ? 121 ASP B O   1 
ATOM   4652 C  CB  . ASP B 1 121 ? 0.294   -2.068  44.576  1.00 35.53  ? 121 ASP B CB  1 
ATOM   4653 C  CG  . ASP B 1 121 ? 0.432   -2.728  43.199  1.00 39.25  ? 121 ASP B CG  1 
ATOM   4654 O  OD1 . ASP B 1 121 ? -0.029  -3.890  43.048  1.00 34.46  ? 121 ASP B OD1 1 
ATOM   4655 O  OD2 . ASP B 1 121 ? 1.044   -2.107  42.292  1.00 36.27  ? 121 ASP B OD2 1 
ATOM   4656 N  N   . ILE B 1 122 ? -1.603  -4.066  46.044  1.00 32.83  ? 122 ILE B N   1 
ATOM   4657 C  CA  . ILE B 1 122 ? -2.230  -5.385  46.133  1.00 32.65  ? 122 ILE B CA  1 
ATOM   4658 C  C   . ILE B 1 122 ? -3.685  -5.257  46.578  1.00 31.57  ? 122 ILE B C   1 
ATOM   4659 O  O   . ILE B 1 122 ? -4.573  -5.969  46.078  1.00 32.08  ? 122 ILE B O   1 
ATOM   4660 C  CB  . ILE B 1 122 ? -1.430  -6.294  47.085  1.00 33.01  ? 122 ILE B CB  1 
ATOM   4661 C  CG1 . ILE B 1 122 ? 0.031   -6.403  46.636  1.00 33.23  ? 122 ILE B CG1 1 
ATOM   4662 C  CG2 . ILE B 1 122 ? -2.071  -7.666  47.142  1.00 30.09  ? 122 ILE B CG2 1 
ATOM   4663 C  CD1 . ILE B 1 122 ? 0.198   -6.837  45.141  1.00 32.21  ? 122 ILE B CD1 1 
ATOM   4664 N  N   . ALA B 1 123 ? -3.953  -4.340  47.512  1.00 32.10  ? 123 ALA B N   1 
ATOM   4665 C  CA  . ALA B 1 123 ? -5.319  -4.145  47.995  1.00 34.15  ? 123 ALA B CA  1 
ATOM   4666 C  C   . ALA B 1 123 ? -6.238  -3.695  46.868  1.00 32.53  ? 123 ALA B C   1 
ATOM   4667 O  O   . ALA B 1 123 ? -7.375  -4.167  46.757  1.00 35.34  ? 123 ALA B O   1 
ATOM   4668 C  CB  . ALA B 1 123 ? -5.332  -3.128  49.137  1.00 35.00  ? 123 ALA B CB  1 
ATOM   4669 N  N   . VAL B 1 124 ? -5.774  -2.760  46.038  1.00 30.88  ? 124 VAL B N   1 
ATOM   4670 C  CA  . VAL B 1 124 ? -6.562  -2.335  44.879  1.00 35.30  ? 124 VAL B CA  1 
ATOM   4671 C  C   . VAL B 1 124 ? -6.840  -3.525  43.961  1.00 32.99  ? 124 VAL B C   1 
ATOM   4672 O  O   . VAL B 1 124 ? -7.926  -3.635  43.369  1.00 32.68  ? 124 VAL B O   1 
ATOM   4673 C  CB  . VAL B 1 124 ? -5.842  -1.184  44.145  1.00 35.96  ? 124 VAL B CB  1 
ATOM   4674 C  CG1 . VAL B 1 124 ? -6.442  -0.932  42.762  1.00 35.49  ? 124 VAL B CG1 1 
ATOM   4675 C  CG2 . VAL B 1 124 ? -5.874  0.103   44.974  1.00 31.65  ? 124 VAL B CG2 1 
ATOM   4676 N  N   . GLN B 1 125 ? -5.869  -4.438  43.821  1.00 31.62  ? 125 GLN B N   1 
ATOM   4677 C  CA  . GLN B 1 125 ? -6.106  -5.634  43.009  1.00 32.63  ? 125 GLN B CA  1 
ATOM   4678 C  C   . GLN B 1 125 ? -7.229  -6.479  43.587  1.00 32.07  ? 125 GLN B C   1 
ATOM   4679 O  O   . GLN B 1 125 ? -8.045  -7.031  42.846  1.00 33.70  ? 125 GLN B O   1 
ATOM   4680 C  CB  . GLN B 1 125 ? -4.844  -6.476  42.892  1.00 34.56  ? 125 GLN B CB  1 
ATOM   4681 C  CG  . GLN B 1 125 ? -3.769  -5.820  42.026  1.00 32.65  ? 125 GLN B CG  1 
ATOM   4682 C  CD  . GLN B 1 125 ? -2.702  -6.794  41.664  1.00 33.35  ? 125 GLN B CD  1 
ATOM   4683 O  OE1 . GLN B 1 125 ? -2.988  -7.933  41.253  1.00 31.57  ? 125 GLN B OE1 1 
ATOM   4684 N  NE2 . GLN B 1 125 ? -1.450  -6.378  41.825  1.00 32.93  ? 125 GLN B NE2 1 
ATOM   4685 N  N   . LEU B 1 126 ? -7.267  -6.612  44.913  1.00 30.57  ? 126 LEU B N   1 
ATOM   4686 C  CA  . LEU B 1 126 ? -8.360  -7.332  45.557  1.00 30.80  ? 126 LEU B CA  1 
ATOM   4687 C  C   . LEU B 1 126 ? -9.701  -6.664  45.269  1.00 31.00  ? 126 LEU B C   1 
ATOM   4688 O  O   . LEU B 1 126 ? -10.671 -7.325  44.873  1.00 30.18  ? 126 LEU B O   1 
ATOM   4689 C  CB  . LEU B 1 126 ? -8.112  -7.399  47.063  1.00 27.60  ? 126 LEU B CB  1 
ATOM   4690 C  CG  . LEU B 1 126 ? -9.321  -7.994  47.806  1.00 33.12  ? 126 LEU B CG  1 
ATOM   4691 C  CD1 . LEU B 1 126 ? -9.340  -9.515  47.669  1.00 32.10  ? 126 LEU B CD1 1 
ATOM   4692 C  CD2 . LEU B 1 126 ? -9.287  -7.577  49.259  1.00 39.30  ? 126 LEU B CD2 1 
ATOM   4693 N  N   . VAL B 1 127 ? -9.777  -5.348  45.470  1.00 29.26  ? 127 VAL B N   1 
ATOM   4694 C  CA  . VAL B 1 127 ? -11.040 -4.647  45.266  1.00 31.24  ? 127 VAL B CA  1 
ATOM   4695 C  C   . VAL B 1 127 ? -11.483 -4.766  43.809  1.00 33.43  ? 127 VAL B C   1 
ATOM   4696 O  O   . VAL B 1 127 ? -12.673 -4.933  43.517  1.00 32.74  ? 127 VAL B O   1 
ATOM   4697 C  CB  . VAL B 1 127 ? -10.919 -3.175  45.707  1.00 32.14  ? 127 VAL B CB  1 
ATOM   4698 C  CG1 . VAL B 1 127 ? -12.160 -2.384  45.301  1.00 33.49  ? 127 VAL B CG1 1 
ATOM   4699 C  CG2 . VAL B 1 127 ? -10.720 -3.098  47.211  1.00 34.56  ? 127 VAL B CG2 1 
ATOM   4700 N  N   . GLN B 1 128 ? -10.548 -4.661  42.869  1.00 33.62  ? 128 GLN B N   1 
ATOM   4701 C  CA  . GLN B 1 128 ? -10.953 -4.766  41.470  1.00 30.47  ? 128 GLN B CA  1 
ATOM   4702 C  C   . GLN B 1 128 ? -11.444 -6.168  41.134  1.00 33.94  ? 128 GLN B C   1 
ATOM   4703 O  O   . GLN B 1 128 ? -12.400 -6.317  40.365  1.00 33.76  ? 128 GLN B O   1 
ATOM   4704 C  CB  . GLN B 1 128 ? -9.823  -4.325  40.543  1.00 32.92  ? 128 GLN B CB  1 
ATOM   4705 C  CG  . GLN B 1 128 ? -9.555  -2.839  40.724  1.00 34.53  ? 128 GLN B CG  1 
ATOM   4706 C  CD  . GLN B 1 128 ? -8.673  -2.224  39.681  1.00 47.14  ? 128 GLN B CD  1 
ATOM   4707 O  OE1 . GLN B 1 128 ? -7.560  -2.693  39.433  1.00 50.40  ? 128 GLN B OE1 1 
ATOM   4708 N  NE2 . GLN B 1 128 ? -9.160  -1.138  39.064  1.00 44.03  ? 128 GLN B NE2 1 
ATOM   4709 N  N   . LYS B 1 129 ? -10.837 -7.206  41.719  1.00 31.13  ? 129 LYS B N   1 
ATOM   4710 C  CA  . LYS B 1 129 ? -11.354 -8.560  41.507  1.00 31.37  ? 129 LYS B CA  1 
ATOM   4711 C  C   . LYS B 1 129 ? -12.822 -8.659  41.918  1.00 32.05  ? 129 LYS B C   1 
ATOM   4712 O  O   . LYS B 1 129 ? -13.651 -9.200  41.182  1.00 30.25  ? 129 LYS B O   1 
ATOM   4713 C  CB  . LYS B 1 129 ? -10.528 -9.591  42.285  1.00 30.17  ? 129 LYS B CB  1 
ATOM   4714 C  CG  . LYS B 1 129 ? -11.153 -11.001 42.196  1.00 32.00  ? 129 LYS B CG  1 
ATOM   4715 C  CD  . LYS B 1 129 ? -10.244 -12.099 42.681  1.00 33.69  ? 129 LYS B CD  1 
ATOM   4716 C  CE  . LYS B 1 129 ? -11.019 -13.412 42.765  1.00 36.84  ? 129 LYS B CE  1 
ATOM   4717 N  NZ  . LYS B 1 129 ? -10.193 -14.533 43.255  1.00 34.48  ? 129 LYS B NZ  1 
ATOM   4718 N  N   . TRP B 1 130 ? -13.160 -8.141  43.100  1.00 31.69  ? 130 TRP B N   1 
ATOM   4719 C  CA  . TRP B 1 130 ? -14.532 -8.263  43.587  1.00 30.05  ? 130 TRP B CA  1 
ATOM   4720 C  C   . TRP B 1 130 ? -15.493 -7.378  42.790  1.00 31.02  ? 130 TRP B C   1 
ATOM   4721 O  O   . TRP B 1 130 ? -16.652 -7.754  42.559  1.00 32.48  ? 130 TRP B O   1 
ATOM   4722 C  CB  . TRP B 1 130 ? -14.569 -7.931  45.085  1.00 28.62  ? 130 TRP B CB  1 
ATOM   4723 C  CG  . TRP B 1 130 ? -13.887 -8.984  45.920  1.00 33.10  ? 130 TRP B CG  1 
ATOM   4724 C  CD1 . TRP B 1 130 ? -13.296 -10.143 45.471  1.00 26.40  ? 130 TRP B CD1 1 
ATOM   4725 C  CD2 . TRP B 1 130 ? -13.698 -8.964  47.335  1.00 31.39  ? 130 TRP B CD2 1 
ATOM   4726 N  NE1 . TRP B 1 130 ? -12.777 -10.853 46.529  1.00 34.22  ? 130 TRP B NE1 1 
ATOM   4727 C  CE2 . TRP B 1 130 ? -13.003 -10.151 47.683  1.00 30.77  ? 130 TRP B CE2 1 
ATOM   4728 C  CE3 . TRP B 1 130 ? -14.055 -8.067  48.345  1.00 29.75  ? 130 TRP B CE3 1 
ATOM   4729 C  CZ2 . TRP B 1 130 ? -12.664 -10.464 49.000  1.00 31.04  ? 130 TRP B CZ2 1 
ATOM   4730 C  CZ3 . TRP B 1 130 ? -13.711 -8.385  49.662  1.00 29.58  ? 130 TRP B CZ3 1 
ATOM   4731 C  CH2 . TRP B 1 130 ? -13.020 -9.569  49.969  1.00 34.58  ? 130 TRP B CH2 1 
ATOM   4732 N  N   . GLU B 1 131 ? -15.044 -6.192  42.381  1.00 30.32  ? 131 GLU B N   1 
ATOM   4733 C  CA  . GLU B 1 131 ? -15.863 -5.341  41.519  1.00 34.35  ? 131 GLU B CA  1 
ATOM   4734 C  C   . GLU B 1 131 ? -16.239 -6.059  40.230  1.00 36.25  ? 131 GLU B C   1 
ATOM   4735 O  O   . GLU B 1 131 ? -17.297 -5.786  39.642  1.00 31.46  ? 131 GLU B O   1 
ATOM   4736 C  CB  . GLU B 1 131 ? -15.110 -4.052  41.172  1.00 33.86  ? 131 GLU B CB  1 
ATOM   4737 C  CG  . GLU B 1 131 ? -14.852 -3.085  42.320  1.00 36.46  ? 131 GLU B CG  1 
ATOM   4738 C  CD  . GLU B 1 131 ? -16.069 -2.269  42.702  1.00 40.97  ? 131 GLU B CD  1 
ATOM   4739 O  OE1 . GLU B 1 131 ? -17.203 -2.733  42.463  1.00 38.25  ? 131 GLU B OE1 1 
ATOM   4740 O  OE2 . GLU B 1 131 ? -15.888 -1.157  43.229  1.00 40.44  ? 131 GLU B OE2 1 
ATOM   4741 N  N   . ARG B 1 132 ? -15.380 -6.952  39.760  1.00 31.48  ? 132 ARG B N   1 
ATOM   4742 C  CA  . ARG B 1 132 ? -15.541 -7.566  38.447  1.00 32.77  ? 132 ARG B CA  1 
ATOM   4743 C  C   . ARG B 1 132 ? -16.266 -8.900  38.501  1.00 36.79  ? 132 ARG B C   1 
ATOM   4744 O  O   . ARG B 1 132 ? -16.455 -9.526  37.455  1.00 34.18  ? 132 ARG B O   1 
ATOM   4745 C  CB  . ARG B 1 132 ? -14.170 -7.734  37.785  1.00 32.47  ? 132 ARG B CB  1 
ATOM   4746 C  CG  . ARG B 1 132 ? -13.535 -6.392  37.443  1.00 33.50  ? 132 ARG B CG  1 
ATOM   4747 C  CD  . ARG B 1 132 ? -12.043 -6.493  37.043  1.00 34.23  ? 132 ARG B CD  1 
ATOM   4748 N  NE  . ARG B 1 132 ? -11.573 -5.184  36.599  1.00 33.16  ? 132 ARG B NE  1 
ATOM   4749 C  CZ  . ARG B 1 132 ? -10.304 -4.845  36.426  1.00 37.62  ? 132 ARG B CZ  1 
ATOM   4750 N  NH1 . ARG B 1 132 ? -9.325  -5.709  36.632  1.00 35.79  ? 132 ARG B NH1 1 
ATOM   4751 N  NH2 . ARG B 1 132 ? -10.013 -3.610  36.022  1.00 36.80  ? 132 ARG B NH2 1 
ATOM   4752 N  N   . LEU B 1 133 ? -16.673 -9.352  39.684  1.00 32.95  ? 133 LEU B N   1 
ATOM   4753 C  CA  . LEU B 1 133 ? -17.495 -10.548 39.764  1.00 35.03  ? 133 LEU B CA  1 
ATOM   4754 C  C   . LEU B 1 133 ? -18.871 -10.265 39.164  1.00 37.15  ? 133 LEU B C   1 
ATOM   4755 O  O   . LEU B 1 133 ? -19.382 -9.142  39.227  1.00 35.81  ? 133 LEU B O   1 
ATOM   4756 C  CB  . LEU B 1 133 ? -17.647 -11.010 41.217  1.00 33.30  ? 133 LEU B CB  1 
ATOM   4757 C  CG  . LEU B 1 133 ? -16.344 -11.400 41.929  1.00 33.07  ? 133 LEU B CG  1 
ATOM   4758 C  CD1 . LEU B 1 133 ? -16.612 -11.839 43.357  1.00 31.32  ? 133 LEU B CD1 1 
ATOM   4759 C  CD2 . LEU B 1 133 ? -15.600 -12.484 41.154  1.00 38.03  ? 133 LEU B CD2 1 
ATOM   4760 N  N   . ASN B 1 134 ? -19.466 -11.302 38.584  1.00 32.18  ? 134 ASN B N   1 
ATOM   4761 C  CA  . ASN B 1 134 ? -20.799 -11.209 38.016  1.00 36.41  ? 134 ASN B CA  1 
ATOM   4762 C  C   . ASN B 1 134 ? -21.861 -11.382 39.106  1.00 39.19  ? 134 ASN B C   1 
ATOM   4763 O  O   . ASN B 1 134 ? -21.584 -11.841 40.211  1.00 37.42  ? 134 ASN B O   1 
ATOM   4764 C  CB  . ASN B 1 134 ? -20.970 -12.255 36.919  1.00 33.84  ? 134 ASN B CB  1 
ATOM   4765 C  CG  . ASN B 1 134 ? -19.938 -12.095 35.800  1.00 35.84  ? 134 ASN B CG  1 
ATOM   4766 O  OD1 . ASN B 1 134 ? -19.964 -11.110 35.058  1.00 33.85  ? 134 ASN B OD1 1 
ATOM   4767 N  ND2 . ASN B 1 134 ? -19.033 -13.060 35.681  1.00 32.07  ? 134 ASN B ND2 1 
ATOM   4768 N  N   . ALA B 1 135 ? -23.097 -11.009 38.770  1.00 38.82  ? 135 ALA B N   1 
ATOM   4769 C  CA  . ALA B 1 135 ? -24.209 -11.108 39.708  1.00 41.28  ? 135 ALA B CA  1 
ATOM   4770 C  C   . ALA B 1 135 ? -24.244 -12.466 40.394  1.00 42.43  ? 135 ALA B C   1 
ATOM   4771 O  O   . ALA B 1 135 ? -24.186 -13.515 39.749  1.00 47.37  ? 135 ALA B O   1 
ATOM   4772 C  CB  . ALA B 1 135 ? -25.532 -10.862 38.977  1.00 44.33  ? 135 ALA B CB  1 
ATOM   4773 N  N   . ASP B 1 136 ? -24.339 -12.436 41.716  1.00 44.68  ? 136 ASP B N   1 
ATOM   4774 C  CA  . ASP B 1 136 ? -24.471 -13.654 42.517  1.00 58.10  ? 136 ASP B CA  1 
ATOM   4775 C  C   . ASP B 1 136 ? -23.421 -14.726 42.181  1.00 55.15  ? 136 ASP B C   1 
ATOM   4776 O  O   . ASP B 1 136 ? -23.644 -15.924 42.389  1.00 60.94  ? 136 ASP B O   1 
ATOM   4777 C  CB  . ASP B 1 136 ? -25.898 -14.200 42.409  1.00 60.97  ? 136 ASP B CB  1 
ATOM   4778 C  CG  . ASP B 1 136 ? -26.947 -13.126 42.701  1.00 62.95  ? 136 ASP B CG  1 
ATOM   4779 O  OD1 . ASP B 1 136 ? -26.994 -12.651 43.863  1.00 59.17  ? 136 ASP B OD1 1 
ATOM   4780 O  OD2 . ASP B 1 136 ? -27.713 -12.756 41.777  1.00 62.48  ? 136 ASP B OD2 1 
ATOM   4781 N  N   . GLU B 1 137 ? -22.255 -14.323 41.675  1.00 47.91  ? 137 GLU B N   1 
ATOM   4782 C  CA  . GLU B 1 137 ? -21.067 -15.081 42.042  1.00 42.60  ? 137 GLU B CA  1 
ATOM   4783 C  C   . GLU B 1 137 ? -20.761 -14.783 43.509  1.00 39.81  ? 137 GLU B C   1 
ATOM   4784 O  O   . GLU B 1 137 ? -21.331 -13.864 44.100  1.00 42.69  ? 137 GLU B O   1 
ATOM   4785 C  CB  . GLU B 1 137 ? -19.888 -14.725 41.135  1.00 41.49  ? 137 GLU B CB  1 
ATOM   4786 C  CG  . GLU B 1 137 ? -20.094 -15.274 39.742  1.00 47.47  ? 137 GLU B CG  1 
ATOM   4787 C  CD  . GLU B 1 137 ? -19.116 -14.768 38.705  1.00 44.42  ? 137 GLU B CD  1 
ATOM   4788 O  OE1 . GLU B 1 137 ? -18.151 -14.056 39.044  1.00 39.98  ? 137 GLU B OE1 1 
ATOM   4789 O  OE2 . GLU B 1 137 ? -19.318 -15.109 37.517  1.00 46.57  ? 137 GLU B OE2 1 
ATOM   4790 N  N   . HIS B 1 138 ? -19.860 -15.554 44.116  1.00 37.51  ? 138 HIS B N   1 
ATOM   4791 C  CA  . HIS B 1 138 ? -19.521 -15.245 45.501  1.00 36.67  ? 138 HIS B CA  1 
ATOM   4792 C  C   . HIS B 1 138 ? -18.008 -15.159 45.672  1.00 37.73  ? 138 HIS B C   1 
ATOM   4793 O  O   . HIS B 1 138 ? -17.223 -15.413 44.748  1.00 33.59  ? 138 HIS B O   1 
ATOM   4794 C  CB  . HIS B 1 138 ? -20.070 -16.270 46.502  1.00 37.67  ? 138 HIS B CB  1 
ATOM   4795 C  CG  . HIS B 1 138 ? -19.649 -17.678 46.226  1.00 35.54  ? 138 HIS B CG  1 
ATOM   4796 N  ND1 . HIS B 1 138 ? -20.129 -18.410 45.163  1.00 42.08  ? 138 HIS B ND1 1 
ATOM   4797 C  CD2 . HIS B 1 138 ? -18.678 -18.435 46.794  1.00 40.52  ? 138 HIS B CD2 1 
ATOM   4798 C  CE1 . HIS B 1 138 ? -19.543 -19.596 45.149  1.00 43.42  ? 138 HIS B CE1 1 
ATOM   4799 N  NE2 . HIS B 1 138 ? -18.649 -19.633 46.122  1.00 41.89  ? 138 HIS B NE2 1 
ATOM   4800 N  N   . ILE B 1 139 ? -17.611 -14.798 46.886  1.00 32.18  ? 139 ILE B N   1 
ATOM   4801 C  CA  . ILE B 1 139 ? -16.214 -14.599 47.258  1.00 32.67  ? 139 ILE B CA  1 
ATOM   4802 C  C   . ILE B 1 139 ? -15.810 -15.756 48.153  1.00 33.70  ? 139 ILE B C   1 
ATOM   4803 O  O   . ILE B 1 139 ? -16.536 -16.094 49.094  1.00 30.28  ? 139 ILE B O   1 
ATOM   4804 C  CB  . ILE B 1 139 ? -16.026 -13.253 47.987  1.00 33.29  ? 139 ILE B CB  1 
ATOM   4805 C  CG1 . ILE B 1 139 ? -16.254 -12.088 47.009  1.00 31.31  ? 139 ILE B CG1 1 
ATOM   4806 C  CG2 . ILE B 1 139 ? -14.654 -13.189 48.683  1.00 31.40  ? 139 ILE B CG2 1 
ATOM   4807 C  CD1 . ILE B 1 139 ? -16.594 -10.743 47.720  1.00 31.23  ? 139 ILE B CD1 1 
ATOM   4808 N  N   . GLU B 1 140 ? -14.671 -16.376 47.861  1.00 27.90  ? 140 GLU B N   1 
ATOM   4809 C  CA  . GLU B 1 140 ? -14.076 -17.348 48.780  1.00 28.71  ? 140 GLU B CA  1 
ATOM   4810 C  C   . GLU B 1 140 ? -13.095 -16.572 49.648  1.00 32.12  ? 140 GLU B C   1 
ATOM   4811 O  O   . GLU B 1 140 ? -12.037 -16.155 49.166  1.00 30.57  ? 140 GLU B O   1 
ATOM   4812 C  CB  . GLU B 1 140 ? -13.396 -18.477 48.002  1.00 32.76  ? 140 GLU B CB  1 
ATOM   4813 C  CG  . GLU B 1 140 ? -14.383 -19.270 47.121  1.00 35.33  ? 140 GLU B CG  1 
ATOM   4814 C  CD  . GLU B 1 140 ? -13.705 -20.323 46.266  1.00 44.36  ? 140 GLU B CD  1 
ATOM   4815 O  OE1 . GLU B 1 140 ? -12.562 -20.086 45.828  1.00 39.71  ? 140 GLU B OE1 1 
ATOM   4816 O  OE2 . GLU B 1 140 ? -14.327 -21.376 46.004  1.00 44.44  ? 140 GLU B OE2 1 
ATOM   4817 N  N   . VAL B 1 141 ? -13.457 -16.342 50.909  1.00 30.62  ? 141 VAL B N   1 
ATOM   4818 C  CA  . VAL B 1 141 ? -12.831 -15.288 51.708  1.00 29.10  ? 141 VAL B CA  1 
ATOM   4819 C  C   . VAL B 1 141 ? -11.402 -15.659 52.092  1.00 28.28  ? 141 VAL B C   1 
ATOM   4820 O  O   . VAL B 1 141 ? -10.469 -14.903 51.773  1.00 31.40  ? 141 VAL B O   1 
ATOM   4821 C  CB  . VAL B 1 141 ? -13.677 -14.964 52.953  1.00 30.77  ? 141 VAL B CB  1 
ATOM   4822 C  CG1 . VAL B 1 141 ? -12.911 -14.015 53.864  1.00 28.06  ? 141 VAL B CG1 1 
ATOM   4823 C  CG2 . VAL B 1 141 ? -15.044 -14.332 52.534  1.00 29.28  ? 141 VAL B CG2 1 
ATOM   4824 N  N   . PRO B 1 142 ? -11.161 -16.771 52.792  1.00 29.94  ? 142 PRO B N   1 
ATOM   4825 C  CA  . PRO B 1 142 ? -9.765  -17.072 53.154  1.00 29.39  ? 142 PRO B CA  1 
ATOM   4826 C  C   . PRO B 1 142 ? -8.889  -17.254 51.934  1.00 33.38  ? 142 PRO B C   1 
ATOM   4827 O  O   . PRO B 1 142 ? -7.696  -16.918 51.969  1.00 33.85  ? 142 PRO B O   1 
ATOM   4828 C  CB  . PRO B 1 142 ? -9.868  -18.352 54.002  1.00 34.66  ? 142 PRO B CB  1 
ATOM   4829 C  CG  . PRO B 1 142 ? -11.278 -18.903 53.734  1.00 33.55  ? 142 PRO B CG  1 
ATOM   4830 C  CD  . PRO B 1 142 ? -12.119 -17.705 53.409  1.00 32.43  ? 142 PRO B CD  1 
ATOM   4831 N  N   . GLU B 1 143 ? -9.472  -17.735 50.836  1.00 33.05  ? 143 GLU B N   1 
ATOM   4832 C  CA  . GLU B 1 143 ? -8.723  -17.913 49.604  1.00 32.90  ? 143 GLU B CA  1 
ATOM   4833 C  C   . GLU B 1 143 ? -8.210  -16.579 49.087  1.00 33.75  ? 143 GLU B C   1 
ATOM   4834 O  O   . GLU B 1 143 ? -7.008  -16.423 48.827  1.00 30.85  ? 143 GLU B O   1 
ATOM   4835 C  CB  . GLU B 1 143 ? -9.615  -18.619 48.583  1.00 31.00  ? 143 GLU B CB  1 
ATOM   4836 C  CG  . GLU B 1 143 ? -9.731  -20.111 48.883  1.00 35.14  ? 143 GLU B CG  1 
ATOM   4837 C  CD  . GLU B 1 143 ? -10.844 -20.429 49.900  1.00 34.26  ? 143 GLU B CD  1 
ATOM   4838 O  OE1 . GLU B 1 143 ? -11.540 -19.503 50.379  1.00 33.86  ? 143 GLU B OE1 1 
ATOM   4839 O  OE2 . GLU B 1 143 ? -11.008 -21.604 50.244  1.00 37.94  ? 143 GLU B OE2 1 
ATOM   4840 N  N   . ASP B 1 144 ? -9.103  -15.587 48.958  1.00 30.37  ? 144 ASP B N   1 
ATOM   4841 C  CA  . ASP B 1 144 ? -8.681  -14.283 48.459  1.00 28.33  ? 144 ASP B CA  1 
ATOM   4842 C  C   . ASP B 1 144 ? -7.837  -13.531 49.481  1.00 33.40  ? 144 ASP B C   1 
ATOM   4843 O  O   . ASP B 1 144 ? -6.933  -12.780 49.104  1.00 30.45  ? 144 ASP B O   1 
ATOM   4844 C  CB  . ASP B 1 144 ? -9.896  -13.442 48.066  1.00 29.39  ? 144 ASP B CB  1 
ATOM   4845 C  CG  . ASP B 1 144 ? -10.351 -13.710 46.631  1.00 34.64  ? 144 ASP B CG  1 
ATOM   4846 O  OD1 . ASP B 1 144 ? -9.570  -14.294 45.856  1.00 32.89  ? 144 ASP B OD1 1 
ATOM   4847 O  OD2 . ASP B 1 144 ? -11.483 -13.327 46.290  1.00 32.37  ? 144 ASP B OD2 1 
ATOM   4848 N  N   . MET B 1 145 ? -8.124  -13.711 50.771  1.00 28.76  ? 145 MET B N   1 
ATOM   4849 C  CA  . MET B 1 145 ? -7.372  -13.016 51.805  1.00 29.97  ? 145 MET B CA  1 
ATOM   4850 C  C   . MET B 1 145 ? -5.919  -13.500 51.776  1.00 29.61  ? 145 MET B C   1 
ATOM   4851 O  O   . MET B 1 145 ? -4.983  -12.728 52.009  1.00 29.78  ? 145 MET B O   1 
ATOM   4852 C  CB  . MET B 1 145 ? -8.047  -13.326 53.147  1.00 30.84  ? 145 MET B CB  1 
ATOM   4853 C  CG  . MET B 1 145 ? -9.238  -12.398 53.530  1.00 28.73  ? 145 MET B CG  1 
ATOM   4854 S  SD  . MET B 1 145 ? -9.266  -10.688 52.982  1.00 31.82  ? 145 MET B SD  1 
ATOM   4855 C  CE  . MET B 1 145 ? -10.140 -10.811 51.404  1.00 38.17  ? 145 MET B CE  1 
ATOM   4856 N  N   . THR B 1 146 ? -5.724  -14.793 51.489  1.00 29.74  ? 146 THR B N   1 
ATOM   4857 C  CA  . THR B 1 146 ? -4.386  -15.386 51.403  1.00 31.58  ? 146 THR B CA  1 
ATOM   4858 C  C   . THR B 1 146 ? -3.667  -14.968 50.128  1.00 32.46  ? 146 THR B C   1 
ATOM   4859 O  O   . THR B 1 146 ? -2.460  -14.708 50.149  1.00 32.95  ? 146 THR B O   1 
ATOM   4860 C  CB  . THR B 1 146 ? -4.494  -16.912 51.469  1.00 33.65  ? 146 THR B CB  1 
ATOM   4861 O  OG1 . THR B 1 146 ? -5.113  -17.299 52.701  1.00 32.76  ? 146 THR B OG1 1 
ATOM   4862 C  CG2 . THR B 1 146 ? -3.114  -17.575 51.366  1.00 39.94  ? 146 THR B CG2 1 
ATOM   4863 N  N   . ARG B 1 147 ? -4.379  -14.928 48.998  1.00 30.27  ? 147 ARG B N   1 
ATOM   4864 C  CA  . ARG B 1 147 ? -3.796  -14.327 47.803  1.00 34.03  ? 147 ARG B CA  1 
ATOM   4865 C  C   . ARG B 1 147 ? -3.232  -12.941 48.119  1.00 32.07  ? 147 ARG B C   1 
ATOM   4866 O  O   . ARG B 1 147 ? -2.101  -12.607 47.744  1.00 35.64  ? 147 ARG B O   1 
ATOM   4867 C  CB  . ARG B 1 147 ? -4.849  -14.230 46.692  1.00 29.80  ? 147 ARG B CB  1 
ATOM   4868 C  CG  . ARG B 1 147 ? -5.320  -15.568 46.127  1.00 30.57  ? 147 ARG B CG  1 
ATOM   4869 C  CD  . ARG B 1 147 ? -6.217  -15.325 44.889  1.00 37.00  ? 147 ARG B CD  1 
ATOM   4870 N  NE  . ARG B 1 147 ? -6.583  -16.550 44.174  1.00 41.67  ? 147 ARG B NE  1 
ATOM   4871 C  CZ  . ARG B 1 147 ? -7.662  -17.285 44.416  1.00 44.59  ? 147 ARG B CZ  1 
ATOM   4872 N  NH1 . ARG B 1 147 ? -8.560  -16.928 45.322  1.00 37.22  ? 147 ARG B NH1 1 
ATOM   4873 N  NH2 . ARG B 1 147 ? -7.862  -18.399 43.713  1.00 47.10  ? 147 ARG B NH2 1 
ATOM   4874 N  N   . LEU B 1 148 ? -4.023  -12.116 48.814  1.00 32.99  ? 148 LEU B N   1 
ATOM   4875 C  CA  . LEU B 1 148 ? -3.605  -10.750 49.110  1.00 33.65  ? 148 LEU B CA  1 
ATOM   4876 C  C   . LEU B 1 148 ? -2.383  -10.719 50.024  1.00 31.77  ? 148 LEU B C   1 
ATOM   4877 O  O   . LEU B 1 148 ? -1.417  -10.007 49.743  1.00 33.03  ? 148 LEU B O   1 
ATOM   4878 C  CB  . LEU B 1 148 ? -4.757  -9.972  49.745  1.00 31.86  ? 148 LEU B CB  1 
ATOM   4879 C  CG  . LEU B 1 148 ? -4.394  -8.558  50.214  1.00 33.49  ? 148 LEU B CG  1 
ATOM   4880 C  CD1 . LEU B 1 148 ? -5.390  -7.572  49.626  1.00 35.26  ? 148 LEU B CD1 1 
ATOM   4881 C  CD2 . LEU B 1 148 ? -4.406  -8.466  51.705  1.00 35.39  ? 148 LEU B CD2 1 
ATOM   4882 N  N   . THR B 1 149 ? -2.405  -11.471 51.131  1.00 30.58  ? 149 THR B N   1 
ATOM   4883 C  CA  . THR B 1 149 ? -1.311  -11.326 52.098  1.00 33.02  ? 149 THR B CA  1 
ATOM   4884 C  C   . THR B 1 149 ? -0.015  -11.896 51.552  1.00 32.51  ? 149 THR B C   1 
ATOM   4885 O  O   . THR B 1 149 ? 1.068   -11.325 51.778  1.00 31.28  ? 149 THR B O   1 
ATOM   4886 C  CB  . THR B 1 149 ? -1.663  -11.965 53.449  1.00 33.18  ? 149 THR B CB  1 
ATOM   4887 O  OG1 . THR B 1 149 ? -1.877  -13.379 53.306  1.00 31.67  ? 149 THR B OG1 1 
ATOM   4888 C  CG2 . THR B 1 149 ? -2.908  -11.297 54.043  1.00 32.14  ? 149 THR B CG2 1 
ATOM   4889 N  N   . LEU B 1 150 ? -0.096  -13.015 50.834  1.00 31.09  ? 150 LEU B N   1 
ATOM   4890 C  CA  . LEU B 1 150 ? 1.092   -13.518 50.149  1.00 35.16  ? 150 LEU B CA  1 
ATOM   4891 C  C   . LEU B 1 150 ? 1.655   -12.481 49.189  1.00 35.47  ? 150 LEU B C   1 
ATOM   4892 O  O   . LEU B 1 150 ? 2.857   -12.172 49.217  1.00 32.95  ? 150 LEU B O   1 
ATOM   4893 C  CB  . LEU B 1 150 ? 0.784   -14.829 49.424  1.00 33.13  ? 150 LEU B CB  1 
ATOM   4894 C  CG  . LEU B 1 150 ? 2.018   -15.211 48.612  1.00 35.07  ? 150 LEU B CG  1 
ATOM   4895 C  CD1 . LEU B 1 150 ? 2.998   -15.919 49.531  1.00 45.15  ? 150 LEU B CD1 1 
ATOM   4896 C  CD2 . LEU B 1 150 ? 1.624   -16.116 47.457  1.00 42.03  ? 150 LEU B CD2 1 
ATOM   4897 N  N   . ASP B 1 151 ? 0.800   -11.899 48.348  1.00 31.26  ? 151 ASP B N   1 
ATOM   4898 C  CA  . ASP B 1 151 ? 1.311   -10.932 47.385  1.00 35.00  ? 151 ASP B CA  1 
ATOM   4899 C  C   . ASP B 1 151 ? 1.888   -9.702  48.079  1.00 33.21  ? 151 ASP B C   1 
ATOM   4900 O  O   . ASP B 1 151 ? 2.904   -9.149  47.636  1.00 32.81  ? 151 ASP B O   1 
ATOM   4901 C  CB  . ASP B 1 151 ? 0.214   -10.549 46.397  1.00 33.22  ? 151 ASP B CB  1 
ATOM   4902 C  CG  . ASP B 1 151 ? 0.098   -11.555 45.263  1.00 31.24  ? 151 ASP B CG  1 
ATOM   4903 O  OD1 . ASP B 1 151 ? 0.466   -12.732 45.483  1.00 36.18  ? 151 ASP B OD1 1 
ATOM   4904 O  OD2 . ASP B 1 151 ? -0.333  -11.154 44.169  1.00 35.93  ? 151 ASP B OD2 1 
ATOM   4905 N  N   . THR B 1 152 ? 1.268   -9.269  49.175  1.00 31.70  ? 152 THR B N   1 
ATOM   4906 C  CA  . THR B 1 152 ? 1.743   -8.073  49.859  1.00 32.29  ? 152 THR B CA  1 
ATOM   4907 C  C   . THR B 1 152 ? 3.142   -8.283  50.424  1.00 32.72  ? 152 THR B C   1 
ATOM   4908 O  O   . THR B 1 152 ? 4.016   -7.412  50.291  1.00 30.94  ? 152 THR B O   1 
ATOM   4909 C  CB  . THR B 1 152 ? 0.774   -7.688  50.974  1.00 31.93  ? 152 THR B CB  1 
ATOM   4910 O  OG1 . THR B 1 152 ? -0.501  -7.371  50.398  1.00 32.77  ? 152 THR B OG1 1 
ATOM   4911 C  CG2 . THR B 1 152 ? 1.296   -6.475  51.728  1.00 34.55  ? 152 THR B CG2 1 
ATOM   4912 N  N   . ILE B 1 153 ? 3.368   -9.423  51.088  1.00 31.51  ? 153 ILE B N   1 
ATOM   4913 C  CA  . ILE B 1 153 ? 4.702   -9.675  51.634  1.00 32.67  ? 153 ILE B CA  1 
ATOM   4914 C  C   . ILE B 1 153 ? 5.708   -9.879  50.509  1.00 35.36  ? 153 ILE B C   1 
ATOM   4915 O  O   . ILE B 1 153 ? 6.843   -9.385  50.582  1.00 36.08  ? 153 ILE B O   1 
ATOM   4916 C  CB  . ILE B 1 153 ? 4.694   -10.854 52.628  1.00 32.24  ? 153 ILE B CB  1 
ATOM   4917 C  CG1 . ILE B 1 153 ? 6.071   -10.971 53.292  1.00 36.38  ? 153 ILE B CG1 1 
ATOM   4918 C  CG2 . ILE B 1 153 ? 4.347   -12.160 51.931  1.00 40.60  ? 153 ILE B CG2 1 
ATOM   4919 C  CD1 . ILE B 1 153 ? 6.458   -9.706  54.005  1.00 43.71  ? 153 ILE B CD1 1 
ATOM   4920 N  N   . GLY B 1 154 ? 5.322   -10.603 49.451  1.00 32.29  ? 154 GLY B N   1 
ATOM   4921 C  CA  . GLY B 1 154 ? 6.204   -10.716 48.296  1.00 32.00  ? 154 GLY B CA  1 
ATOM   4922 C  C   . GLY B 1 154 ? 6.657   -9.367  47.773  1.00 37.16  ? 154 GLY B C   1 
ATOM   4923 O  O   . GLY B 1 154 ? 7.850   -9.142  47.542  1.00 36.66  ? 154 GLY B O   1 
ATOM   4924 N  N   . LEU B 1 155 ? 5.705   -8.450  47.566  1.00 33.65  ? 155 LEU B N   1 
ATOM   4925 C  CA  . LEU B 1 155 ? 6.010   -7.155  46.958  1.00 34.65  ? 155 LEU B CA  1 
ATOM   4926 C  C   . LEU B 1 155 ? 6.733   -6.239  47.927  1.00 37.87  ? 155 LEU B C   1 
ATOM   4927 O  O   . LEU B 1 155 ? 7.808   -5.708  47.612  1.00 36.67  ? 155 LEU B O   1 
ATOM   4928 C  CB  . LEU B 1 155 ? 4.723   -6.477  46.480  1.00 36.50  ? 155 LEU B CB  1 
ATOM   4929 C  CG  . LEU B 1 155 ? 4.787   -5.294  45.508  1.00 34.55  ? 155 LEU B CG  1 
ATOM   4930 C  CD1 . LEU B 1 155 ? 5.891   -5.414  44.438  1.00 36.70  ? 155 LEU B CD1 1 
ATOM   4931 C  CD2 . LEU B 1 155 ? 3.437   -5.072  44.886  1.00 35.09  ? 155 LEU B CD2 1 
ATOM   4932 N  N   . CYS B 1 156 ? 6.131   -6.012  49.102  1.00 36.97  ? 156 CYS B N   1 
ATOM   4933 C  CA  . CYS B 1 156 ? 6.713   -5.100  50.079  1.00 40.10  ? 156 CYS B CA  1 
ATOM   4934 C  C   . CYS B 1 156 ? 8.066   -5.603  50.529  1.00 38.92  ? 156 CYS B C   1 
ATOM   4935 O  O   . CYS B 1 156 ? 9.027   -4.828  50.625  1.00 44.91  ? 156 CYS B O   1 
ATOM   4936 C  CB  . CYS B 1 156 ? 5.779   -4.940  51.292  1.00 33.54  ? 156 CYS B CB  1 
ATOM   4937 S  SG  . CYS B 1 156 ? 4.294   -4.068  50.885  1.00 39.77  ? 156 CYS B SG  1 
ATOM   4938 N  N   . GLY B 1 157 ? 8.162   -6.907  50.790  1.00 37.86  ? 157 GLY B N   1 
ATOM   4939 C  CA  . GLY B 1 157 ? 9.381   -7.447  51.357  1.00 40.39  ? 157 GLY B CA  1 
ATOM   4940 C  C   . GLY B 1 157 ? 10.512  -7.574  50.352  1.00 44.74  ? 157 GLY B C   1 
ATOM   4941 O  O   . GLY B 1 157 ? 11.671  -7.293  50.679  1.00 43.84  ? 157 GLY B O   1 
ATOM   4942 N  N   . PHE B 1 158 ? 10.200  -8.000  49.109  1.00 40.04  ? 158 PHE B N   1 
ATOM   4943 C  CA  . PHE B 1 158 ? 11.247  -8.410  48.177  1.00 37.84  ? 158 PHE B CA  1 
ATOM   4944 C  C   . PHE B 1 158 ? 11.010  -7.955  46.746  1.00 37.54  ? 158 PHE B C   1 
ATOM   4945 O  O   . PHE B 1 158 ? 11.682  -8.457  45.837  1.00 40.86  ? 158 PHE B O   1 
ATOM   4946 C  CB  . PHE B 1 158 ? 11.389  -9.932  48.226  1.00 39.96  ? 158 PHE B CB  1 
ATOM   4947 C  CG  . PHE B 1 158 ? 11.339  -10.457 49.607  1.00 46.80  ? 158 PHE B CG  1 
ATOM   4948 C  CD1 . PHE B 1 158 ? 12.427  -10.290 50.464  1.00 43.10  ? 158 PHE B CD1 1 
ATOM   4949 C  CD2 . PHE B 1 158 ? 10.155  -10.968 50.110  1.00 41.87  ? 158 PHE B CD2 1 
ATOM   4950 C  CE1 . PHE B 1 158 ? 12.365  -10.722 51.776  1.00 43.84  ? 158 PHE B CE1 1 
ATOM   4951 C  CE2 . PHE B 1 158 ? 10.076  -11.392 51.424  1.00 47.07  ? 158 PHE B CE2 1 
ATOM   4952 C  CZ  . PHE B 1 158 ? 11.190  -11.270 52.263  1.00 43.95  ? 158 PHE B CZ  1 
ATOM   4953 N  N   . ASN B 1 159 ? 10.096  -7.023  46.517  1.00 37.41  ? 159 ASN B N   1 
ATOM   4954 C  CA  . ASN B 1 159 ? 9.826   -6.519  45.184  1.00 40.96  ? 159 ASN B CA  1 
ATOM   4955 C  C   . ASN B 1 159 ? 9.580   -7.668  44.204  1.00 36.95  ? 159 ASN B C   1 
ATOM   4956 O  O   . ASN B 1 159 ? 9.950   -7.603  43.030  1.00 38.68  ? 159 ASN B O   1 
ATOM   4957 C  CB  . ASN B 1 159 ? 10.970  -5.622  44.709  1.00 44.34  ? 159 ASN B CB  1 
ATOM   4958 C  CG  . ASN B 1 159 ? 10.532  -4.654  43.657  1.00 50.05  ? 159 ASN B CG  1 
ATOM   4959 O  OD1 . ASN B 1 159 ? 9.390   -4.198  43.664  1.00 54.04  ? 159 ASN B OD1 1 
ATOM   4960 N  ND2 . ASN B 1 159 ? 11.425  -4.352  42.715  1.00 52.67  ? 159 ASN B ND2 1 
ATOM   4961 N  N   . TYR B 1 160 ? 8.941   -8.733  44.687  1.00 36.11  ? 160 TYR B N   1 
ATOM   4962 C  CA  . TYR B 1 160 ? 8.568   -9.864  43.845  1.00 38.08  ? 160 TYR B CA  1 
ATOM   4963 C  C   . TYR B 1 160 ? 7.046   -9.965  43.768  1.00 35.52  ? 160 TYR B C   1 
ATOM   4964 O  O   . TYR B 1 160 ? 6.358   -9.905  44.796  1.00 31.94  ? 160 TYR B O   1 
ATOM   4965 C  CB  . TYR B 1 160 ? 9.167   -11.174 44.368  1.00 36.03  ? 160 TYR B CB  1 
ATOM   4966 C  CG  . TYR B 1 160 ? 8.979   -12.325 43.398  1.00 36.54  ? 160 TYR B CG  1 
ATOM   4967 C  CD1 . TYR B 1 160 ? 9.904   -12.567 42.377  1.00 38.96  ? 160 TYR B CD1 1 
ATOM   4968 C  CD2 . TYR B 1 160 ? 7.855   -13.134 43.464  1.00 38.54  ? 160 TYR B CD2 1 
ATOM   4969 C  CE1 . TYR B 1 160 ? 9.719   -13.610 41.470  1.00 42.04  ? 160 TYR B CE1 1 
ATOM   4970 C  CE2 . TYR B 1 160 ? 7.662   -14.167 42.566  1.00 41.37  ? 160 TYR B CE2 1 
ATOM   4971 C  CZ  . TYR B 1 160 ? 8.595   -14.409 41.574  1.00 46.05  ? 160 TYR B CZ  1 
ATOM   4972 O  OH  . TYR B 1 160 ? 8.387   -15.453 40.694  1.00 48.78  ? 160 TYR B OH  1 
ATOM   4973 N  N   . ARG B 1 161 ? 6.520   -10.161 42.565  1.00 34.84  ? 161 ARG B N   1 
ATOM   4974 C  CA  . ARG B 1 161 ? 5.068   -10.254 42.372  1.00 32.26  ? 161 ARG B CA  1 
ATOM   4975 C  C   . ARG B 1 161 ? 4.684   -11.715 42.173  1.00 33.79  ? 161 ARG B C   1 
ATOM   4976 O  O   . ARG B 1 161 ? 4.976   -12.306 41.131  1.00 32.82  ? 161 ARG B O   1 
ATOM   4977 C  CB  . ARG B 1 161 ? 4.632   -9.387  41.195  1.00 32.66  ? 161 ARG B CB  1 
ATOM   4978 C  CG  . ARG B 1 161 ? 4.724   -7.901  41.546  1.00 34.35  ? 161 ARG B CG  1 
ATOM   4979 C  CD  . ARG B 1 161 ? 4.153   -7.021  40.464  1.00 38.24  ? 161 ARG B CD  1 
ATOM   4980 N  NE  . ARG B 1 161 ? 4.288   -5.608  40.791  1.00 33.77  ? 161 ARG B NE  1 
ATOM   4981 C  CZ  . ARG B 1 161 ? 3.299   -4.872  41.267  1.00 32.49  ? 161 ARG B CZ  1 
ATOM   4982 N  NH1 . ARG B 1 161 ? 2.097   -5.393  41.475  1.00 32.59  ? 161 ARG B NH1 1 
ATOM   4983 N  NH2 . ARG B 1 161 ? 3.512   -3.581  41.519  1.00 31.84  ? 161 ARG B NH2 1 
ATOM   4984 N  N   . PHE B 1 162 ? 4.035   -12.307 43.180  1.00 28.73  ? 162 PHE B N   1 
ATOM   4985 C  CA  . PHE B 1 162 ? 3.506   -13.652 42.996  1.00 29.11  ? 162 PHE B CA  1 
ATOM   4986 C  C   . PHE B 1 162 ? 2.306   -13.653 42.047  1.00 34.14  ? 162 PHE B C   1 
ATOM   4987 O  O   . PHE B 1 162 ? 1.957   -14.706 41.507  1.00 35.04  ? 162 PHE B O   1 
ATOM   4988 C  CB  . PHE B 1 162 ? 3.116   -14.257 44.339  1.00 34.22  ? 162 PHE B CB  1 
ATOM   4989 C  CG  . PHE B 1 162 ? 4.299   -14.632 45.201  1.00 34.88  ? 162 PHE B CG  1 
ATOM   4990 C  CD1 . PHE B 1 162 ? 5.106   -15.718 44.869  1.00 37.97  ? 162 PHE B CD1 1 
ATOM   4991 C  CD2 . PHE B 1 162 ? 4.607   -13.897 46.332  1.00 35.20  ? 162 PHE B CD2 1 
ATOM   4992 C  CE1 . PHE B 1 162 ? 6.198   -16.062 45.665  1.00 39.34  ? 162 PHE B CE1 1 
ATOM   4993 C  CE2 . PHE B 1 162 ? 5.712   -14.234 47.128  1.00 38.19  ? 162 PHE B CE2 1 
ATOM   4994 C  CZ  . PHE B 1 162 ? 6.500   -15.313 46.788  1.00 39.06  ? 162 PHE B CZ  1 
ATOM   4995 N  N   . ASN B 1 163 ? 1.693   -12.496 41.822  1.00 32.37  ? 163 ASN B N   1 
ATOM   4996 C  CA  . ASN B 1 163 ? 0.552   -12.382 40.899  1.00 30.12  ? 163 ASN B CA  1 
ATOM   4997 C  C   . ASN B 1 163 ? -0.522  -13.434 41.201  1.00 34.61  ? 163 ASN B C   1 
ATOM   4998 O  O   . ASN B 1 163 ? -1.055  -14.099 40.305  1.00 36.63  ? 163 ASN B O   1 
ATOM   4999 C  CB  . ASN B 1 163 ? 1.045   -12.453 39.443  1.00 31.37  ? 163 ASN B CB  1 
ATOM   5000 C  CG  . ASN B 1 163 ? 1.761   -11.172 39.025  1.00 34.50  ? 163 ASN B CG  1 
ATOM   5001 O  OD1 . ASN B 1 163 ? 1.297   -10.066 39.335  1.00 35.31  ? 163 ASN B OD1 1 
ATOM   5002 N  ND2 . ASN B 1 163 ? 2.901   -11.306 38.339  1.00 36.17  ? 163 ASN B ND2 1 
ATOM   5003 N  N   . SER B 1 164 ? -0.867  -13.554 42.497  1.00 29.46  ? 164 SER B N   1 
ATOM   5004 C  CA  . SER B 1 164 ? -1.828  -14.564 42.945  1.00 34.14  ? 164 SER B CA  1 
ATOM   5005 C  C   . SER B 1 164 ? -3.225  -14.323 42.379  1.00 34.79  ? 164 SER B C   1 
ATOM   5006 O  O   . SER B 1 164 ? -4.014  -15.271 42.254  1.00 33.16  ? 164 SER B O   1 
ATOM   5007 C  CB  . SER B 1 164 ? -1.908  -14.594 44.473  1.00 31.95  ? 164 SER B CB  1 
ATOM   5008 O  OG  . SER B 1 164 ? -0.656  -14.948 45.029  1.00 33.31  ? 164 SER B OG  1 
ATOM   5009 N  N   . PHE B 1 165 ? -3.566  -13.077 42.083  1.00 34.24  ? 165 PHE B N   1 
ATOM   5010 C  CA  . PHE B 1 165 ? -4.878  -12.784 41.519  1.00 36.72  ? 165 PHE B CA  1 
ATOM   5011 C  C   . PHE B 1 165 ? -4.940  -13.037 40.026  1.00 36.70  ? 165 PHE B C   1 
ATOM   5012 O  O   . PHE B 1 165 ? -6.001  -12.843 39.431  1.00 39.13  ? 165 PHE B O   1 
ATOM   5013 C  CB  . PHE B 1 165 ? -5.279  -11.335 41.806  1.00 32.67  ? 165 PHE B CB  1 
ATOM   5014 C  CG  . PHE B 1 165 ? -5.593  -11.075 43.245  1.00 35.09  ? 165 PHE B CG  1 
ATOM   5015 C  CD1 . PHE B 1 165 ? -6.622  -11.753 43.879  1.00 37.94  ? 165 PHE B CD1 1 
ATOM   5016 C  CD2 . PHE B 1 165 ? -4.867  -10.138 43.966  1.00 36.20  ? 165 PHE B CD2 1 
ATOM   5017 C  CE1 . PHE B 1 165 ? -6.912  -11.500 45.231  1.00 37.32  ? 165 PHE B CE1 1 
ATOM   5018 C  CE2 . PHE B 1 165 ? -5.144  -9.886  45.311  1.00 36.50  ? 165 PHE B CE2 1 
ATOM   5019 C  CZ  . PHE B 1 165 ? -6.167  -10.569 45.944  1.00 33.24  ? 165 PHE B CZ  1 
ATOM   5020 N  N   . TYR B 1 166 ? -3.835  -13.442 39.405  1.00 35.13  ? 166 TYR B N   1 
ATOM   5021 C  CA  . TYR B 1 166 ? -3.841  -13.851 38.009  1.00 39.43  ? 166 TYR B CA  1 
ATOM   5022 C  C   . TYR B 1 166 ? -3.857  -15.363 37.851  1.00 45.20  ? 166 TYR B C   1 
ATOM   5023 O  O   . TYR B 1 166 ? -3.801  -15.855 36.722  1.00 45.53  ? 166 TYR B O   1 
ATOM   5024 C  CB  . TYR B 1 166 ? -2.616  -13.269 37.282  1.00 36.73  ? 166 TYR B CB  1 
ATOM   5025 C  CG  . TYR B 1 166 ? -2.656  -11.764 37.151  1.00 35.77  ? 166 TYR B CG  1 
ATOM   5026 C  CD1 . TYR B 1 166 ? -2.179  -10.939 38.172  1.00 33.25  ? 166 TYR B CD1 1 
ATOM   5027 C  CD2 . TYR B 1 166 ? -3.175  -11.164 36.008  1.00 36.95  ? 166 TYR B CD2 1 
ATOM   5028 C  CE1 . TYR B 1 166 ? -2.210  -9.545  38.050  1.00 30.61  ? 166 TYR B CE1 1 
ATOM   5029 C  CE2 . TYR B 1 166 ? -3.223  -9.793  35.879  1.00 29.84  ? 166 TYR B CE2 1 
ATOM   5030 C  CZ  . TYR B 1 166 ? -2.741  -8.987  36.902  1.00 31.57  ? 166 TYR B CZ  1 
ATOM   5031 O  OH  . TYR B 1 166 ? -2.806  -7.625  36.735  1.00 34.95  ? 166 TYR B OH  1 
ATOM   5032 N  N   . ARG B 1 167 ? -3.948  -16.107 38.952  1.00 42.19  ? 167 ARG B N   1 
ATOM   5033 C  CA  . ARG B 1 167 ? -3.619  -17.522 38.953  1.00 53.12  ? 167 ARG B CA  1 
ATOM   5034 C  C   . ARG B 1 167 ? -4.755  -18.327 39.555  1.00 51.09  ? 167 ARG B C   1 
ATOM   5035 O  O   . ARG B 1 167 ? -5.443  -17.867 40.473  1.00 53.97  ? 167 ARG B O   1 
ATOM   5036 C  CB  . ARG B 1 167 ? -2.375  -17.795 39.789  1.00 50.40  ? 167 ARG B CB  1 
ATOM   5037 C  CG  . ARG B 1 167 ? -1.074  -17.402 39.165  1.00 53.45  ? 167 ARG B CG  1 
ATOM   5038 C  CD  . ARG B 1 167 ? 0.000   -17.483 40.239  1.00 47.41  ? 167 ARG B CD  1 
ATOM   5039 N  NE  . ARG B 1 167 ? 1.256   -16.879 39.811  1.00 53.33  ? 167 ARG B NE  1 
ATOM   5040 C  CZ  . ARG B 1 167 ? 2.228   -17.526 39.185  1.00 53.50  ? 167 ARG B CZ  1 
ATOM   5041 N  NH1 . ARG B 1 167 ? 2.106   -18.799 38.849  1.00 50.50  ? 167 ARG B NH1 1 
ATOM   5042 N  NH2 . ARG B 1 167 ? 3.349   -16.877 38.889  1.00 56.54  ? 167 ARG B NH2 1 
ATOM   5043 N  N   . ASP B 1 168 ? -4.930  -19.543 39.031  1.00 57.30  ? 168 ASP B N   1 
ATOM   5044 C  CA  . ASP B 1 168 ? -5.620  -20.613 39.742  1.00 57.86  ? 168 ASP B CA  1 
ATOM   5045 C  C   . ASP B 1 168 ? -4.631  -21.422 40.575  1.00 61.61  ? 168 ASP B C   1 
ATOM   5046 O  O   . ASP B 1 168 ? -4.853  -21.645 41.768  1.00 60.68  ? 168 ASP B O   1 
ATOM   5047 C  CB  . ASP B 1 168 ? -6.346  -21.550 38.762  1.00 58.42  ? 168 ASP B CB  1 
ATOM   5048 C  CG  . ASP B 1 168 ? -7.507  -20.880 38.042  1.00 58.26  ? 168 ASP B CG  1 
ATOM   5049 O  OD1 . ASP B 1 168 ? -8.435  -20.389 38.723  1.00 55.13  ? 168 ASP B OD1 1 
ATOM   5050 O  OD2 . ASP B 1 168 ? -7.503  -20.875 36.793  1.00 60.99  ? 168 ASP B OD2 1 
ATOM   5051 N  N   . GLN B 1 169 ? -3.531  -21.856 39.949  1.00 59.55  ? 169 GLN B N   1 
ATOM   5052 C  CA  . GLN B 1 169 ? -2.501  -22.636 40.627  1.00 63.95  ? 169 GLN B CA  1 
ATOM   5053 C  C   . GLN B 1 169 ? -1.426  -21.703 41.174  1.00 60.86  ? 169 GLN B C   1 
ATOM   5054 O  O   . GLN B 1 169 ? -0.855  -20.916 40.403  1.00 57.22  ? 169 GLN B O   1 
ATOM   5055 C  CB  . GLN B 1 169 ? -1.877  -23.644 39.674  1.00 66.15  ? 169 GLN B CB  1 
ATOM   5056 C  CG  . GLN B 1 169 ? -2.676  -24.941 39.484  1.00 73.27  ? 169 GLN B CG  1 
ATOM   5057 C  CD  . GLN B 1 169 ? -3.497  -25.333 40.710  1.00 77.05  ? 169 GLN B CD  1 
ATOM   5058 O  OE1 . GLN B 1 169 ? -4.648  -24.914 40.864  1.00 76.31  ? 169 GLN B OE1 1 
ATOM   5059 N  NE2 . GLN B 1 169 ? -2.904  -26.137 41.589  1.00 79.30  ? 169 GLN B NE2 1 
ATOM   5060 N  N   . PRO B 1 170 ? -1.123  -21.755 42.473  1.00 60.61  ? 170 PRO B N   1 
ATOM   5061 C  CA  . PRO B 1 170 ? -0.137  -20.834 43.052  1.00 54.30  ? 170 PRO B CA  1 
ATOM   5062 C  C   . PRO B 1 170 ? 1.243   -20.967 42.425  1.00 52.04  ? 170 PRO B C   1 
ATOM   5063 O  O   . PRO B 1 170 ? 1.603   -21.982 41.823  1.00 53.15  ? 170 PRO B O   1 
ATOM   5064 C  CB  . PRO B 1 170 ? -0.094  -21.237 44.529  1.00 56.02  ? 170 PRO B CB  1 
ATOM   5065 C  CG  . PRO B 1 170 ? -1.401  -21.916 44.800  1.00 56.84  ? 170 PRO B CG  1 
ATOM   5066 C  CD  . PRO B 1 170 ? -1.986  -22.380 43.490  1.00 61.24  ? 170 PRO B CD  1 
ATOM   5067 N  N   . HIS B 1 171 ? 2.027   -19.915 42.610  1.00 51.37  ? 171 HIS B N   1 
ATOM   5068 C  CA  . HIS B 1 171 ? 3.436   -19.946 42.256  1.00 52.60  ? 171 HIS B CA  1 
ATOM   5069 C  C   . HIS B 1 171 ? 4.091   -21.205 42.832  1.00 53.63  ? 171 HIS B C   1 
ATOM   5070 O  O   . HIS B 1 171 ? 3.707   -21.661 43.922  1.00 51.19  ? 171 HIS B O   1 
ATOM   5071 C  CB  . HIS B 1 171 ? 4.115   -18.677 42.783  1.00 48.79  ? 171 HIS B CB  1 
ATOM   5072 C  CG  . HIS B 1 171 ? 5.565   -18.565 42.430  1.00 51.30  ? 171 HIS B CG  1 
ATOM   5073 N  ND1 . HIS B 1 171 ? 6.525   -19.402 42.957  1.00 50.42  ? 171 HIS B ND1 1 
ATOM   5074 C  CD2 . HIS B 1 171 ? 6.221   -17.703 41.617  1.00 51.21  ? 171 HIS B CD2 1 
ATOM   5075 C  CE1 . HIS B 1 171 ? 7.710   -19.070 42.474  1.00 51.10  ? 171 HIS B CE1 1 
ATOM   5076 N  NE2 . HIS B 1 171 ? 7.554   -18.036 41.665  1.00 49.41  ? 171 HIS B NE2 1 
ATOM   5077 N  N   . PRO B 1 172 ? 5.055   -21.809 42.122  1.00 51.12  ? 172 PRO B N   1 
ATOM   5078 C  CA  . PRO B 1 172 ? 5.638   -23.079 42.594  1.00 49.24  ? 172 PRO B CA  1 
ATOM   5079 C  C   . PRO B 1 172 ? 6.279   -23.008 43.969  1.00 51.47  ? 172 PRO B C   1 
ATOM   5080 O  O   . PRO B 1 172 ? 6.326   -24.035 44.661  1.00 46.11  ? 172 PRO B O   1 
ATOM   5081 C  CB  . PRO B 1 172 ? 6.688   -23.403 41.523  1.00 48.09  ? 172 PRO B CB  1 
ATOM   5082 C  CG  . PRO B 1 172 ? 6.211   -22.714 40.286  1.00 51.64  ? 172 PRO B CG  1 
ATOM   5083 C  CD  . PRO B 1 172 ? 5.329   -21.559 40.693  1.00 50.64  ? 172 PRO B CD  1 
ATOM   5084 N  N   . PHE B 1 173 ? 6.822   -21.854 44.375  1.00 47.32  ? 173 PHE B N   1 
ATOM   5085 C  CA  . PHE B 1 173 ? 7.329   -21.751 45.743  1.00 46.98  ? 173 PHE B CA  1 
ATOM   5086 C  C   . PHE B 1 173 ? 6.208   -21.959 46.748  1.00 46.93  ? 173 PHE B C   1 
ATOM   5087 O  O   . PHE B 1 173 ? 6.392   -22.644 47.762  1.00 47.11  ? 173 PHE B O   1 
ATOM   5088 C  CB  . PHE B 1 173 ? 7.989   -20.394 45.994  1.00 50.47  ? 173 PHE B CB  1 
ATOM   5089 C  CG  . PHE B 1 173 ? 8.416   -20.192 47.436  1.00 46.41  ? 173 PHE B CG  1 
ATOM   5090 C  CD1 . PHE B 1 173 ? 7.521   -19.677 48.375  1.00 47.08  ? 173 PHE B CD1 1 
ATOM   5091 C  CD2 . PHE B 1 173 ? 9.701   -20.534 47.854  1.00 45.47  ? 173 PHE B CD2 1 
ATOM   5092 C  CE1 . PHE B 1 173 ? 7.892   -19.509 49.703  1.00 43.49  ? 173 PHE B CE1 1 
ATOM   5093 C  CE2 . PHE B 1 173 ? 10.090  -20.358 49.177  1.00 45.60  ? 173 PHE B CE2 1 
ATOM   5094 C  CZ  . PHE B 1 173 ? 9.176   -19.842 50.109  1.00 45.47  ? 173 PHE B CZ  1 
ATOM   5095 N  N   . ILE B 1 174 ? 5.043   -21.362 46.483  1.00 46.54  ? 174 ILE B N   1 
ATOM   5096 C  CA  . ILE B 1 174 ? 3.939   -21.403 47.438  1.00 48.13  ? 174 ILE B CA  1 
ATOM   5097 C  C   . ILE B 1 174 ? 3.418   -22.825 47.582  1.00 49.71  ? 174 ILE B C   1 
ATOM   5098 O  O   . ILE B 1 174 ? 3.101   -23.282 48.690  1.00 44.83  ? 174 ILE B O   1 
ATOM   5099 C  CB  . ILE B 1 174 ? 2.839   -20.419 46.992  1.00 46.66  ? 174 ILE B CB  1 
ATOM   5100 C  CG1 . ILE B 1 174 ? 3.385   -19.001 47.090  1.00 45.95  ? 174 ILE B CG1 1 
ATOM   5101 C  CG2 . ILE B 1 174 ? 1.573   -20.556 47.848  1.00 44.87  ? 174 ILE B CG2 1 
ATOM   5102 C  CD1 . ILE B 1 174 ? 4.067   -18.734 48.435  1.00 49.20  ? 174 ILE B CD1 1 
ATOM   5103 N  N   . THR B 1 175 ? 3.341   -23.554 46.465  1.00 47.15  ? 175 THR B N   1 
ATOM   5104 C  CA  . THR B 1 175 ? 2.886   -24.939 46.503  1.00 45.87  ? 175 THR B CA  1 
ATOM   5105 C  C   . THR B 1 175 ? 3.768   -25.765 47.431  1.00 46.79  ? 175 THR B C   1 
ATOM   5106 O  O   . THR B 1 175 ? 3.275   -26.549 48.250  1.00 45.42  ? 175 THR B O   1 
ATOM   5107 C  CB  . THR B 1 175 ? 2.901   -25.525 45.087  1.00 47.98  ? 175 THR B CB  1 
ATOM   5108 O  OG1 . THR B 1 175 ? 1.732   -25.086 44.392  1.00 49.97  ? 175 THR B OG1 1 
ATOM   5109 C  CG2 . THR B 1 175 ? 2.888   -27.037 45.151  1.00 49.56  ? 175 THR B CG2 1 
ATOM   5110 N  N   . SER B 1 176 ? 5.084   -25.599 47.309  1.00 42.92  ? 176 SER B N   1 
ATOM   5111 C  CA  . SER B 1 176 ? 5.986   -26.315 48.197  1.00 44.74  ? 176 SER B CA  1 
ATOM   5112 C  C   . SER B 1 176 ? 5.867   -25.820 49.634  1.00 40.83  ? 176 SER B C   1 
ATOM   5113 O  O   . SER B 1 176 ? 5.938   -26.623 50.576  1.00 40.29  ? 176 SER B O   1 
ATOM   5114 C  CB  . SER B 1 176 ? 7.423   -26.195 47.694  1.00 44.48  ? 176 SER B CB  1 
ATOM   5115 O  OG  . SER B 1 176 ? 7.572   -26.943 46.503  1.00 46.28  ? 176 SER B OG  1 
ATOM   5116 N  N   . MET B 1 177 ? 5.693   -24.515 49.845  1.00 38.88  ? 177 MET B N   1 
ATOM   5117 C  CA  . MET B 1 177 ? 5.781   -24.107 51.243  1.00 41.64  ? 177 MET B CA  1 
ATOM   5118 C  C   . MET B 1 177 ? 4.487   -24.468 51.958  1.00 41.81  ? 177 MET B C   1 
ATOM   5119 O  O   . MET B 1 177 ? 4.510   -24.815 53.143  1.00 41.06  ? 177 MET B O   1 
ATOM   5120 C  CB  . MET B 1 177 ? 6.109   -22.613 51.385  1.00 39.81  ? 177 MET B CB  1 
ATOM   5121 C  CG  . MET B 1 177 ? 5.506   -21.895 52.602  1.00 34.88  ? 177 MET B CG  1 
ATOM   5122 S  SD  . MET B 1 177 ? 5.286   -20.113 52.494  1.00 42.31  ? 177 MET B SD  1 
ATOM   5123 C  CE  . MET B 1 177 ? 3.545   -20.006 52.078  1.00 41.17  ? 177 MET B CE  1 
ATOM   5124 N  N   . VAL B 1 178 ? 3.359   -24.445 51.239  1.00 40.38  ? 178 VAL B N   1 
ATOM   5125 C  CA  . VAL B 1 178 ? 2.096   -24.879 51.832  1.00 39.85  ? 178 VAL B CA  1 
ATOM   5126 C  C   . VAL B 1 178 ? 2.159   -26.367 52.161  1.00 42.27  ? 178 VAL B C   1 
ATOM   5127 O  O   . VAL B 1 178 ? 1.699   -26.810 53.222  1.00 42.03  ? 178 VAL B O   1 
ATOM   5128 C  CB  . VAL B 1 178 ? 0.924   -24.559 50.883  1.00 44.37  ? 178 VAL B CB  1 
ATOM   5129 C  CG1 . VAL B 1 178 ? -0.282  -25.451 51.201  1.00 47.60  ? 178 VAL B CG1 1 
ATOM   5130 C  CG2 . VAL B 1 178 ? 0.562   -23.080 50.925  1.00 46.10  ? 178 VAL B CG2 1 
ATOM   5131 N  N   . ARG B 1 179 ? 2.746   -27.163 51.261  1.00 39.43  ? 179 ARG B N   1 
ATOM   5132 C  CA  . ARG B 1 179 ? 2.860   -28.600 51.497  1.00 40.25  ? 179 ARG B CA  1 
ATOM   5133 C  C   . ARG B 1 179 ? 3.845   -28.905 52.614  1.00 40.47  ? 179 ARG B C   1 
ATOM   5134 O  O   . ARG B 1 179 ? 3.642   -29.856 53.379  1.00 39.39  ? 179 ARG B O   1 
ATOM   5135 C  CB  . ARG B 1 179 ? 3.284   -29.314 50.211  1.00 44.51  ? 179 ARG B CB  1 
ATOM   5136 C  CG  . ARG B 1 179 ? 3.002   -30.800 50.194  1.00 48.86  ? 179 ARG B CG  1 
ATOM   5137 C  CD  . ARG B 1 179 ? 2.854   -31.284 48.766  1.00 47.69  ? 179 ARG B CD  1 
ATOM   5138 N  NE  . ARG B 1 179 ? 4.040   -30.930 47.996  1.00 50.37  ? 179 ARG B NE  1 
ATOM   5139 C  CZ  . ARG B 1 179 ? 4.034   -30.649 46.700  1.00 54.36  ? 179 ARG B CZ  1 
ATOM   5140 N  NH1 . ARG B 1 179 ? 2.921   -30.714 45.985  1.00 53.47  ? 179 ARG B NH1 1 
ATOM   5141 N  NH2 . ARG B 1 179 ? 5.172   -30.288 46.109  1.00 46.11  ? 179 ARG B NH2 1 
ATOM   5142 N  N   . ALA B 1 180 ? 4.908   -28.108 52.731  1.00 39.24  ? 180 ALA B N   1 
ATOM   5143 C  CA  . ALA B 1 180 ? 5.840   -28.297 53.835  1.00 40.95  ? 180 ALA B CA  1 
ATOM   5144 C  C   . ALA B 1 180 ? 5.164   -27.993 55.170  1.00 39.11  ? 180 ALA B C   1 
ATOM   5145 O  O   . ALA B 1 180 ? 5.290   -28.762 56.135  1.00 40.60  ? 180 ALA B O   1 
ATOM   5146 C  CB  . ALA B 1 180 ? 7.073   -27.419 53.628  1.00 41.87  ? 180 ALA B CB  1 
ATOM   5147 N  N   . LEU B 1 181 ? 4.435   -26.875 55.240  1.00 39.31  ? 181 LEU B N   1 
ATOM   5148 C  CA  . LEU B 1 181 ? 3.709   -26.533 56.462  1.00 42.48  ? 181 LEU B CA  1 
ATOM   5149 C  C   . LEU B 1 181 ? 2.721   -27.629 56.824  1.00 40.74  ? 181 LEU B C   1 
ATOM   5150 O  O   . LEU B 1 181 ? 2.542   -27.965 58.002  1.00 37.98  ? 181 LEU B O   1 
ATOM   5151 C  CB  . LEU B 1 181 ? 2.985   -25.197 56.283  1.00 40.32  ? 181 LEU B CB  1 
ATOM   5152 C  CG  . LEU B 1 181 ? 3.898   -23.975 56.247  1.00 38.88  ? 181 LEU B CG  1 
ATOM   5153 C  CD1 . LEU B 1 181 ? 3.185   -22.759 55.641  1.00 37.57  ? 181 LEU B CD1 1 
ATOM   5154 C  CD2 . LEU B 1 181 ? 4.419   -23.680 57.651  1.00 37.03  ? 181 LEU B CD2 1 
ATOM   5155 N  N   . ASP B 1 182 ? 2.074   -28.199 55.814  1.00 41.34  ? 182 ASP B N   1 
ATOM   5156 C  CA  . ASP B 1 182 ? 1.105   -29.263 56.049  1.00 45.33  ? 182 ASP B CA  1 
ATOM   5157 C  C   . ASP B 1 182 ? 1.778   -30.511 56.606  1.00 43.59  ? 182 ASP B C   1 
ATOM   5158 O  O   . ASP B 1 182 ? 1.257   -31.142 57.539  1.00 42.68  ? 182 ASP B O   1 
ATOM   5159 C  CB  . ASP B 1 182 ? 0.363   -29.562 54.744  1.00 45.53  ? 182 ASP B CB  1 
ATOM   5160 C  CG  . ASP B 1 182 ? -1.119  -29.768 54.959  1.00 59.50  ? 182 ASP B CG  1 
ATOM   5161 O  OD1 . ASP B 1 182 ? -1.488  -30.775 55.600  1.00 58.89  ? 182 ASP B OD1 1 
ATOM   5162 O  OD2 . ASP B 1 182 ? -1.909  -28.903 54.512  1.00 68.49  ? 182 ASP B OD2 1 
ATOM   5163 N  N   . GLU B 1 183 ? 2.948   -30.876 56.067  1.00 44.40  ? 183 GLU B N   1 
ATOM   5164 C  CA  . GLU B 1 183 ? 3.679   -32.022 56.607  1.00 44.75  ? 183 GLU B CA  1 
ATOM   5165 C  C   . GLU B 1 183 ? 4.164   -31.750 58.030  1.00 48.98  ? 183 GLU B C   1 
ATOM   5166 O  O   . GLU B 1 183 ? 4.085   -32.630 58.902  1.00 46.92  ? 183 GLU B O   1 
ATOM   5167 C  CB  . GLU B 1 183 ? 4.860   -32.382 55.697  1.00 43.38  ? 183 GLU B CB  1 
ATOM   5168 C  CG  . GLU B 1 183 ? 5.860   -33.377 56.316  1.00 46.87  ? 183 GLU B CG  1 
ATOM   5169 C  CD  . GLU B 1 183 ? 5.302   -34.803 56.497  1.00 54.24  ? 183 GLU B CD  1 
ATOM   5170 O  OE1 . GLU B 1 183 ? 4.120   -35.056 56.157  1.00 52.28  ? 183 GLU B OE1 1 
ATOM   5171 O  OE2 . GLU B 1 183 ? 6.044   -35.659 57.028  1.00 54.17  ? 183 GLU B OE2 1 
ATOM   5172 N  N   . ALA B 1 184 ? 4.671   -30.537 58.286  1.00 45.95  ? 184 ALA B N   1 
ATOM   5173 C  CA  . ALA B 1 184 ? 5.167   -30.214 59.621  1.00 47.25  ? 184 ALA B CA  1 
ATOM   5174 C  C   . ALA B 1 184 ? 4.084   -30.415 60.673  1.00 45.14  ? 184 ALA B C   1 
ATOM   5175 O  O   . ALA B 1 184 ? 4.346   -30.957 61.752  1.00 45.58  ? 184 ALA B O   1 
ATOM   5176 C  CB  . ALA B 1 184 ? 5.685   -28.775 59.661  1.00 41.58  ? 184 ALA B CB  1 
ATOM   5177 N  N   . MET B 1 185 ? 2.860   -29.994 60.381  1.00 43.07  ? 185 MET B N   1 
ATOM   5178 C  CA  . MET B 1 185 ? 1.831   -30.110 61.403  1.00 49.13  ? 185 MET B CA  1 
ATOM   5179 C  C   . MET B 1 185 ? 1.172   -31.487 61.446  1.00 52.84  ? 185 MET B C   1 
ATOM   5180 O  O   . MET B 1 185 ? 0.727   -31.902 62.520  1.00 50.33  ? 185 MET B O   1 
ATOM   5181 C  CB  . MET B 1 185 ? 0.811   -28.989 61.226  1.00 46.53  ? 185 MET B CB  1 
ATOM   5182 C  CG  . MET B 1 185 ? 1.521   -27.640 60.998  1.00 46.00  ? 185 MET B CG  1 
ATOM   5183 S  SD  . MET B 1 185 ? 2.248   -26.994 62.549  1.00 51.96  ? 185 MET B SD  1 
ATOM   5184 C  CE  . MET B 1 185 ? 2.566   -25.321 62.066  1.00 51.81  ? 185 MET B CE  1 
ATOM   5185 N  N   . ASN B 1 186 ? 1.145   -32.229 60.329  1.00 46.75  ? 186 ASN B N   1 
ATOM   5186 C  CA  . ASN B 1 186 ? 0.736   -33.637 60.377  1.00 49.45  ? 186 ASN B CA  1 
ATOM   5187 C  C   . ASN B 1 186 ? 1.721   -34.482 61.180  1.00 53.84  ? 186 ASN B C   1 
ATOM   5188 O  O   . ASN B 1 186 ? 1.329   -35.445 61.852  1.00 50.68  ? 186 ASN B O   1 
ATOM   5189 C  CB  . ASN B 1 186 ? 0.609   -34.192 58.959  1.00 52.36  ? 186 ASN B CB  1 
ATOM   5190 C  CG  . ASN B 1 186 ? -0.699  -33.806 58.303  1.00 62.43  ? 186 ASN B CG  1 
ATOM   5191 O  OD1 . ASN B 1 186 ? -1.650  -33.403 58.983  1.00 68.37  ? 186 ASN B OD1 1 
ATOM   5192 N  ND2 . ASN B 1 186 ? -0.748  -33.893 56.973  1.00 62.14  ? 186 ASN B ND2 1 
ATOM   5193 N  N   . LYS B 1 187 ? 3.008   -34.137 61.110  1.00 51.28  ? 187 LYS B N   1 
ATOM   5194 C  CA  . LYS B 1 187 ? 4.033   -34.858 61.854  1.00 48.10  ? 187 LYS B CA  1 
ATOM   5195 C  C   . LYS B 1 187 ? 3.711   -34.914 63.345  1.00 52.55  ? 187 LYS B C   1 
ATOM   5196 O  O   . LYS B 1 187 ? 3.978   -35.923 64.010  1.00 52.76  ? 187 LYS B O   1 
ATOM   5197 C  CB  . LYS B 1 187 ? 5.381   -34.174 61.629  1.00 45.56  ? 187 LYS B CB  1 
ATOM   5198 C  CG  . LYS B 1 187 ? 6.486   -35.071 61.134  1.00 55.50  ? 187 LYS B CG  1 
ATOM   5199 C  CD  . LYS B 1 187 ? 7.730   -34.258 60.769  1.00 49.46  ? 187 LYS B CD  1 
ATOM   5200 C  CE  . LYS B 1 187 ? 8.119   -34.482 59.318  1.00 58.94  ? 187 LYS B CE  1 
ATOM   5201 N  NZ  . LYS B 1 187 ? 9.063   -33.452 58.800  1.00 59.58  ? 187 LYS B NZ  1 
ATOM   5202 N  N   . LEU B 1 188 ? 3.145   -33.834 63.890  1.00 50.28  ? 188 LEU B N   1 
ATOM   5203 C  CA  . LEU B 1 188 ? 2.896   -33.773 65.326  1.00 51.58  ? 188 LEU B CA  1 
ATOM   5204 C  C   . LEU B 1 188 ? 1.990   -34.903 65.800  1.00 53.59  ? 188 LEU B C   1 
ATOM   5205 O  O   . LEU B 1 188 ? 2.075   -35.311 66.964  1.00 56.36  ? 188 LEU B O   1 
ATOM   5206 C  CB  . LEU B 1 188 ? 2.288   -32.416 65.707  1.00 51.27  ? 188 LEU B CB  1 
ATOM   5207 C  CG  . LEU B 1 188 ? 3.098   -31.166 65.362  1.00 44.21  ? 188 LEU B CG  1 
ATOM   5208 C  CD1 . LEU B 1 188 ? 2.248   -29.902 65.456  1.00 45.56  ? 188 LEU B CD1 1 
ATOM   5209 C  CD2 . LEU B 1 188 ? 4.313   -31.070 66.276  1.00 45.80  ? 188 LEU B CD2 1 
ATOM   5210 N  N   . GLN B 1 189 ? 1.130   -35.426 64.919  1.00 60.49  ? 189 GLN B N   1 
ATOM   5211 C  CA  . GLN B 1 189 ? 0.103   -36.397 65.290  1.00 61.71  ? 189 GLN B CA  1 
ATOM   5212 C  C   . GLN B 1 189 ? 0.467   -37.832 64.922  1.00 66.66  ? 189 GLN B C   1 
ATOM   5213 O  O   . GLN B 1 189 ? -0.431  -38.646 64.678  1.00 68.98  ? 189 GLN B O   1 
ATOM   5214 C  CB  . GLN B 1 189 ? -1.225  -36.066 64.621  1.00 53.68  ? 189 GLN B CB  1 
ATOM   5215 C  CG  . GLN B 1 189 ? -1.486  -34.623 64.332  1.00 58.33  ? 189 GLN B CG  1 
ATOM   5216 C  CD  . GLN B 1 189 ? -2.761  -34.491 63.540  1.00 54.20  ? 189 GLN B CD  1 
ATOM   5217 O  OE1 . GLN B 1 189 ? -3.518  -35.463 63.421  1.00 56.32  ? 189 GLN B OE1 1 
ATOM   5218 N  NE2 . GLN B 1 189 ? -3.011  -33.308 62.987  1.00 54.43  ? 189 GLN B NE2 1 
ATOM   5219 N  N   . ARG B 1 190 ? 1.748   -38.171 64.853  1.00 67.00  ? 190 ARG B N   1 
ATOM   5220 C  CA  . ARG B 1 190 ? 2.137   -39.505 64.400  1.00 71.87  ? 190 ARG B CA  1 
ATOM   5221 C  C   . ARG B 1 190 ? 2.807   -40.260 65.540  1.00 75.78  ? 190 ARG B C   1 
ATOM   5222 O  O   . ARG B 1 190 ? 4.023   -40.172 65.731  1.00 79.77  ? 190 ARG B O   1 
ATOM   5223 C  CB  . ARG B 1 190 ? 3.046   -39.441 63.171  1.00 67.80  ? 190 ARG B CB  1 
ATOM   5224 C  CG  . ARG B 1 190 ? 2.356   -38.911 61.932  1.00 63.04  ? 190 ARG B CG  1 
ATOM   5225 C  CD  . ARG B 1 190 ? 3.344   -38.744 60.798  1.00 60.36  ? 190 ARG B CD  1 
ATOM   5226 N  NE  . ARG B 1 190 ? 2.743   -38.059 59.660  1.00 60.45  ? 190 ARG B NE  1 
ATOM   5227 C  CZ  . ARG B 1 190 ? 3.437   -37.521 58.667  1.00 57.44  ? 190 ARG B CZ  1 
ATOM   5228 N  NH1 . ARG B 1 190 ? 4.758   -37.584 58.636  1.00 56.60  ? 190 ARG B NH1 1 
ATOM   5229 N  NH2 . ARG B 1 190 ? 2.791   -36.901 57.685  1.00 56.40  ? 190 ARG B NH2 1 
ATOM   5230 N  N   . ALA B 1 191 ? 2.007   -41.005 66.301  1.00 76.01  ? 191 ALA B N   1 
ATOM   5231 C  CA  . ALA B 1 191 ? 2.564   -42.120 67.047  1.00 78.70  ? 191 ALA B CA  1 
ATOM   5232 C  C   . ALA B 1 191 ? 3.141   -43.108 66.042  1.00 80.78  ? 191 ALA B C   1 
ATOM   5233 O  O   . ALA B 1 191 ? 2.453   -43.525 65.103  1.00 79.29  ? 191 ALA B O   1 
ATOM   5234 C  CB  . ALA B 1 191 ? 1.498   -42.782 67.915  1.00 72.13  ? 191 ALA B CB  1 
ATOM   5235 N  N   . ASN B 1 192 ? 4.421   -43.447 66.219  1.00 80.92  ? 192 ASN B N   1 
ATOM   5236 C  CA  . ASN B 1 192 ? 5.184   -44.186 65.219  1.00 80.06  ? 192 ASN B CA  1 
ATOM   5237 C  C   . ASN B 1 192 ? 5.353   -43.336 63.964  1.00 77.90  ? 192 ASN B C   1 
ATOM   5238 O  O   . ASN B 1 192 ? 4.699   -43.586 62.941  1.00 70.60  ? 192 ASN B O   1 
ATOM   5239 C  CB  . ASN B 1 192 ? 4.521   -45.524 64.876  1.00 82.55  ? 192 ASN B CB  1 
ATOM   5240 C  CG  . ASN B 1 192 ? 4.035   -46.269 66.104  1.00 82.56  ? 192 ASN B CG  1 
ATOM   5241 O  OD1 . ASN B 1 192 ? 4.832   -46.685 66.946  1.00 83.66  ? 192 ASN B OD1 1 
ATOM   5242 N  ND2 . ASN B 1 192 ? 2.721   -46.442 66.210  1.00 81.52  ? 192 ASN B ND2 1 
ATOM   5243 N  N   . PRO B 1 193 ? 6.214   -42.315 64.009  1.00 80.04  ? 193 PRO B N   1 
ATOM   5244 C  CA  . PRO B 1 193 ? 6.533   -41.572 62.782  1.00 77.60  ? 193 PRO B CA  1 
ATOM   5245 C  C   . PRO B 1 193 ? 7.397   -42.360 61.810  1.00 74.23  ? 193 PRO B C   1 
ATOM   5246 O  O   . PRO B 1 193 ? 7.431   -42.018 60.623  1.00 71.52  ? 193 PRO B O   1 
ATOM   5247 C  CB  . PRO B 1 193 ? 7.266   -40.334 63.310  1.00 78.75  ? 193 PRO B CB  1 
ATOM   5248 C  CG  . PRO B 1 193 ? 7.939   -40.827 64.551  1.00 81.05  ? 193 PRO B CG  1 
ATOM   5249 C  CD  . PRO B 1 193 ? 6.981   -41.824 65.168  1.00 77.21  ? 193 PRO B CD  1 
ATOM   5250 N  N   . ASP B 1 194 ? 8.095   -43.400 62.275  1.00 75.93  ? 194 ASP B N   1 
ATOM   5251 C  CA  . ASP B 1 194 ? 8.875   -44.274 61.405  1.00 75.82  ? 194 ASP B CA  1 
ATOM   5252 C  C   . ASP B 1 194 ? 8.008   -45.190 60.550  1.00 76.82  ? 194 ASP B C   1 
ATOM   5253 O  O   . ASP B 1 194 ? 8.551   -45.974 59.760  1.00 72.32  ? 194 ASP B O   1 
ATOM   5254 C  CB  . ASP B 1 194 ? 9.834   -45.129 62.238  1.00 81.08  ? 194 ASP B CB  1 
ATOM   5255 C  CG  . ASP B 1 194 ? 10.916  -44.313 62.902  1.00 79.70  ? 194 ASP B CG  1 
ATOM   5256 O  OD1 . ASP B 1 194 ? 11.398  -43.340 62.278  1.00 79.19  ? 194 ASP B OD1 1 
ATOM   5257 O  OD2 . ASP B 1 194 ? 11.286  -44.659 64.046  1.00 78.34  ? 194 ASP B OD2 1 
ATOM   5258 N  N   . ASP B 1 195 ? 6.692   -45.124 60.696  1.00 74.27  ? 195 ASP B N   1 
ATOM   5259 C  CA  . ASP B 1 195 ? 5.805   -45.970 59.915  1.00 73.09  ? 195 ASP B CA  1 
ATOM   5260 C  C   . ASP B 1 195 ? 6.092   -45.795 58.423  1.00 69.06  ? 195 ASP B C   1 
ATOM   5261 O  O   . ASP B 1 195 ? 6.387   -44.678 57.975  1.00 70.00  ? 195 ASP B O   1 
ATOM   5262 C  CB  . ASP B 1 195 ? 4.348   -45.617 60.222  1.00 68.74  ? 195 ASP B CB  1 
ATOM   5263 C  CG  . ASP B 1 195 ? 3.369   -46.490 59.473  1.00 73.62  ? 195 ASP B CG  1 
ATOM   5264 O  OD1 . ASP B 1 195 ? 3.283   -47.693 59.793  1.00 75.30  ? 195 ASP B OD1 1 
ATOM   5265 O  OD2 . ASP B 1 195 ? 2.701   -45.982 58.546  1.00 76.84  ? 195 ASP B OD2 1 
ATOM   5266 N  N   . PRO B 1 196 ? 6.005   -46.863 57.619  1.00 68.66  ? 196 PRO B N   1 
ATOM   5267 C  CA  . PRO B 1 196 ? 6.284   -46.714 56.182  1.00 65.10  ? 196 PRO B CA  1 
ATOM   5268 C  C   . PRO B 1 196 ? 5.180   -46.011 55.410  1.00 58.46  ? 196 PRO B C   1 
ATOM   5269 O  O   . PRO B 1 196 ? 5.448   -45.507 54.312  1.00 54.75  ? 196 PRO B O   1 
ATOM   5270 C  CB  . PRO B 1 196 ? 6.477   -48.161 55.704  1.00 62.08  ? 196 PRO B CB  1 
ATOM   5271 C  CG  . PRO B 1 196 ? 5.920   -49.044 56.794  1.00 63.64  ? 196 PRO B CG  1 
ATOM   5272 C  CD  . PRO B 1 196 ? 5.433   -48.182 57.927  1.00 66.75  ? 196 PRO B CD  1 
ATOM   5273 N  N   . ALA B 1 197 ? 3.957   -45.948 55.942  1.00 62.22  ? 197 ALA B N   1 
ATOM   5274 C  CA  . ALA B 1 197 ? 2.911   -45.161 55.295  1.00 64.52  ? 197 ALA B CA  1 
ATOM   5275 C  C   . ALA B 1 197 ? 3.282   -43.684 55.168  1.00 61.52  ? 197 ALA B C   1 
ATOM   5276 O  O   . ALA B 1 197 ? 2.613   -42.950 54.429  1.00 59.62  ? 197 ALA B O   1 
ATOM   5277 C  CB  . ALA B 1 197 ? 1.595   -45.308 56.066  1.00 65.69  ? 197 ALA B CB  1 
ATOM   5278 N  N   . TYR B 1 198 ? 4.334   -43.242 55.862  1.00 62.35  ? 198 TYR B N   1 
ATOM   5279 C  CA  . TYR B 1 198 ? 4.810   -41.867 55.817  1.00 58.87  ? 198 TYR B CA  1 
ATOM   5280 C  C   . TYR B 1 198 ? 6.039   -41.693 54.942  1.00 59.87  ? 198 TYR B C   1 
ATOM   5281 O  O   . TYR B 1 198 ? 6.513   -40.560 54.802  1.00 59.12  ? 198 TYR B O   1 
ATOM   5282 C  CB  . TYR B 1 198 ? 5.155   -41.391 57.224  1.00 59.03  ? 198 TYR B CB  1 
ATOM   5283 C  CG  . TYR B 1 198 ? 4.009   -41.514 58.178  1.00 64.31  ? 198 TYR B CG  1 
ATOM   5284 C  CD1 . TYR B 1 198 ? 2.724   -41.160 57.798  1.00 59.50  ? 198 TYR B CD1 1 
ATOM   5285 C  CD2 . TYR B 1 198 ? 4.202   -42.044 59.445  1.00 66.39  ? 198 TYR B CD2 1 
ATOM   5286 C  CE1 . TYR B 1 198 ? 1.666   -41.293 58.669  1.00 61.94  ? 198 TYR B CE1 1 
ATOM   5287 C  CE2 . TYR B 1 198 ? 3.149   -42.185 60.322  1.00 67.79  ? 198 TYR B CE2 1 
ATOM   5288 C  CZ  . TYR B 1 198 ? 1.884   -41.807 59.927  1.00 64.61  ? 198 TYR B CZ  1 
ATOM   5289 O  OH  . TYR B 1 198 ? 0.836   -41.946 60.803  1.00 68.38  ? 198 TYR B OH  1 
ATOM   5290 N  N   . ASP B 1 199 ? 6.586   -42.779 54.384  1.00 54.38  ? 199 ASP B N   1 
ATOM   5291 C  CA  . ASP B 1 199 ? 7.777   -42.650 53.550  1.00 54.67  ? 199 ASP B CA  1 
ATOM   5292 C  C   . ASP B 1 199 ? 7.562   -41.640 52.433  1.00 50.34  ? 199 ASP B C   1 
ATOM   5293 O  O   . ASP B 1 199 ? 8.428   -40.800 52.167  1.00 54.63  ? 199 ASP B O   1 
ATOM   5294 C  CB  . ASP B 1 199 ? 8.174   -44.009 52.967  1.00 54.13  ? 199 ASP B CB  1 
ATOM   5295 C  CG  . ASP B 1 199 ? 8.429   -45.059 54.033  1.00 58.79  ? 199 ASP B CG  1 
ATOM   5296 O  OD1 . ASP B 1 199 ? 8.670   -44.694 55.211  1.00 53.87  ? 199 ASP B OD1 1 
ATOM   5297 O  OD2 . ASP B 1 199 ? 8.411   -46.256 53.680  1.00 57.27  ? 199 ASP B OD2 1 
ATOM   5298 N  N   . GLU B 1 200 ? 6.415   -41.715 51.756  1.00 54.76  ? 200 GLU B N   1 
ATOM   5299 C  CA  . GLU B 1 200 ? 6.160   -40.788 50.661  1.00 54.87  ? 200 GLU B CA  1 
ATOM   5300 C  C   . GLU B 1 200 ? 6.153   -39.345 51.154  1.00 56.40  ? 200 GLU B C   1 
ATOM   5301 O  O   . GLU B 1 200 ? 6.710   -38.456 50.496  1.00 56.60  ? 200 GLU B O   1 
ATOM   5302 C  CB  . GLU B 1 200 ? 4.842   -41.140 49.973  1.00 54.24  ? 200 GLU B CB  1 
ATOM   5303 C  CG  . GLU B 1 200 ? 4.556   -40.333 48.718  1.00 53.10  ? 200 GLU B CG  1 
ATOM   5304 C  CD  . GLU B 1 200 ? 5.805   -40.044 47.902  1.00 60.50  ? 200 GLU B CD  1 
ATOM   5305 O  OE1 . GLU B 1 200 ? 6.771   -40.836 47.975  1.00 60.44  ? 200 GLU B OE1 1 
ATOM   5306 O  OE2 . GLU B 1 200 ? 5.822   -39.014 47.189  1.00 58.98  ? 200 GLU B OE2 1 
ATOM   5307 N  N   . ASN B 1 201 ? 5.542   -39.097 52.318  1.00 54.74  ? 201 ASN B N   1 
ATOM   5308 C  CA  . ASN B 1 201 ? 5.531   -37.747 52.881  1.00 56.87  ? 201 ASN B CA  1 
ATOM   5309 C  C   . ASN B 1 201 ? 6.948   -37.262 53.168  1.00 52.66  ? 201 ASN B C   1 
ATOM   5310 O  O   . ASN B 1 201 ? 7.304   -36.122 52.843  1.00 54.43  ? 201 ASN B O   1 
ATOM   5311 C  CB  . ASN B 1 201 ? 4.693   -37.709 54.161  1.00 56.62  ? 201 ASN B CB  1 
ATOM   5312 C  CG  . ASN B 1 201 ? 3.286   -38.206 53.954  1.00 60.51  ? 201 ASN B CG  1 
ATOM   5313 O  OD1 . ASN B 1 201 ? 2.947   -39.312 54.365  1.00 63.81  ? 201 ASN B OD1 1 
ATOM   5314 N  ND2 . ASN B 1 201 ? 2.463   -37.406 53.291  1.00 63.72  ? 201 ASN B ND2 1 
ATOM   5315 N  N   . LYS B 1 202 ? 7.764   -38.114 53.801  1.00 55.33  ? 202 LYS B N   1 
ATOM   5316 C  CA  . LYS B 1 202 ? 9.182   -37.815 53.997  1.00 58.31  ? 202 LYS B CA  1 
ATOM   5317 C  C   . LYS B 1 202 ? 9.827   -37.326 52.709  1.00 51.06  ? 202 LYS B C   1 
ATOM   5318 O  O   . LYS B 1 202 ? 10.478  -36.277 52.688  1.00 53.06  ? 202 LYS B O   1 
ATOM   5319 C  CB  . LYS B 1 202 ? 9.939   -39.054 54.489  1.00 57.19  ? 202 LYS B CB  1 
ATOM   5320 C  CG  . LYS B 1 202 ? 9.965   -39.321 55.990  1.00 60.50  ? 202 LYS B CG  1 
ATOM   5321 C  CD  . LYS B 1 202 ? 8.587   -39.371 56.611  1.00 60.76  ? 202 LYS B CD  1 
ATOM   5322 C  CE  . LYS B 1 202 ? 8.679   -39.853 58.051  1.00 63.37  ? 202 LYS B CE  1 
ATOM   5323 N  NZ  . LYS B 1 202 ? 9.732   -40.915 58.192  1.00 63.50  ? 202 LYS B NZ  1 
ATOM   5324 N  N   . ARG B 1 203 ? 9.689   -38.103 51.629  1.00 53.54  ? 203 ARG B N   1 
ATOM   5325 C  CA  . ARG B 1 203 ? 10.385  -37.769 50.388  1.00 52.84  ? 203 ARG B CA  1 
ATOM   5326 C  C   . ARG B 1 203 ? 9.891   -36.440 49.834  1.00 54.56  ? 203 ARG B C   1 
ATOM   5327 O  O   . ARG B 1 203 ? 10.690  -35.558 49.502  1.00 55.39  ? 203 ARG B O   1 
ATOM   5328 C  CB  . ARG B 1 203 ? 10.199  -38.876 49.346  1.00 56.88  ? 203 ARG B CB  1 
ATOM   5329 C  CG  . ARG B 1 203 ? 10.427  -38.362 47.930  1.00 55.85  ? 203 ARG B CG  1 
ATOM   5330 C  CD  . ARG B 1 203 ? 9.777   -39.221 46.847  1.00 65.28  ? 203 ARG B CD  1 
ATOM   5331 N  NE  . ARG B 1 203 ? 8.523   -38.617 46.404  1.00 65.18  ? 203 ARG B NE  1 
ATOM   5332 C  CZ  . ARG B 1 203 ? 8.443   -37.498 45.697  1.00 66.11  ? 203 ARG B CZ  1 
ATOM   5333 N  NH1 . ARG B 1 203 ? 9.529   -36.830 45.335  1.00 64.03  ? 203 ARG B NH1 1 
ATOM   5334 N  NH2 . ARG B 1 203 ? 7.245   -37.019 45.372  1.00 63.78  ? 203 ARG B NH2 1 
ATOM   5335 N  N   . GLN B 1 204 ? 8.567   -36.290 49.712  1.00 54.80  ? 204 GLN B N   1 
ATOM   5336 C  CA  . GLN B 1 204 ? 7.986   -35.018 49.300  1.00 51.80  ? 204 GLN B CA  1 
ATOM   5337 C  C   . GLN B 1 204 ? 8.547   -33.856 50.123  1.00 51.60  ? 204 GLN B C   1 
ATOM   5338 O  O   . GLN B 1 204 ? 8.941   -32.821 49.570  1.00 47.31  ? 204 GLN B O   1 
ATOM   5339 C  CB  . GLN B 1 204 ? 6.463   -35.089 49.428  1.00 48.91  ? 204 GLN B CB  1 
ATOM   5340 C  CG  . GLN B 1 204 ? 5.729   -33.889 48.872  1.00 50.29  ? 204 GLN B CG  1 
ATOM   5341 C  CD  . GLN B 1 204 ? 6.057   -33.615 47.432  1.00 53.58  ? 204 GLN B CD  1 
ATOM   5342 O  OE1 . GLN B 1 204 ? 6.939   -32.813 47.121  1.00 54.34  ? 204 GLN B OE1 1 
ATOM   5343 N  NE2 . GLN B 1 204 ? 5.329   -34.263 46.534  1.00 54.33  ? 204 GLN B NE2 1 
ATOM   5344 N  N   . PHE B 1 205 ? 8.578   -34.014 51.452  1.00 51.64  ? 205 PHE B N   1 
ATOM   5345 C  CA  . PHE B 1 205 ? 9.109   -32.973 52.333  1.00 49.53  ? 205 PHE B CA  1 
ATOM   5346 C  C   . PHE B 1 205 ? 10.483  -32.503 51.875  1.00 49.85  ? 205 PHE B C   1 
ATOM   5347 O  O   . PHE B 1 205 ? 10.709  -31.300 51.691  1.00 50.11  ? 205 PHE B O   1 
ATOM   5348 C  CB  . PHE B 1 205 ? 9.174   -33.485 53.774  1.00 45.36  ? 205 PHE B CB  1 
ATOM   5349 C  CG  . PHE B 1 205 ? 9.213   -32.384 54.833  1.00 50.19  ? 205 PHE B CG  1 
ATOM   5350 C  CD1 . PHE B 1 205 ? 8.297   -31.334 54.827  1.00 45.48  ? 205 PHE B CD1 1 
ATOM   5351 C  CD2 . PHE B 1 205 ? 10.174  -32.413 55.841  1.00 46.63  ? 205 PHE B CD2 1 
ATOM   5352 C  CE1 . PHE B 1 205 ? 8.337   -30.336 55.817  1.00 46.73  ? 205 PHE B CE1 1 
ATOM   5353 C  CE2 . PHE B 1 205 ? 10.226  -31.412 56.825  1.00 43.38  ? 205 PHE B CE2 1 
ATOM   5354 C  CZ  . PHE B 1 205 ? 9.307   -30.380 56.820  1.00 40.60  ? 205 PHE B CZ  1 
ATOM   5355 N  N   . GLN B 1 206 ? 11.416  -33.443 51.682  1.00 53.03  ? 206 GLN B N   1 
ATOM   5356 C  CA  . GLN B 1 206 ? 12.757  -33.076 51.224  1.00 54.18  ? 206 GLN B CA  1 
ATOM   5357 C  C   . GLN B 1 206 ? 12.724  -32.391 49.868  1.00 53.08  ? 206 GLN B C   1 
ATOM   5358 O  O   . GLN B 1 206 ? 13.491  -31.449 49.622  1.00 51.63  ? 206 GLN B O   1 
ATOM   5359 C  CB  . GLN B 1 206 ? 13.658  -34.308 51.172  1.00 54.53  ? 206 GLN B CB  1 
ATOM   5360 C  CG  . GLN B 1 206 ? 13.796  -34.999 52.504  1.00 54.59  ? 206 GLN B CG  1 
ATOM   5361 C  CD  . GLN B 1 206 ? 14.314  -34.042 53.562  1.00 60.06  ? 206 GLN B CD  1 
ATOM   5362 O  OE1 . GLN B 1 206 ? 15.248  -33.275 53.311  1.00 56.32  ? 206 GLN B OE1 1 
ATOM   5363 N  NE2 . GLN B 1 206 ? 13.712  -34.078 54.746  1.00 56.13  ? 206 GLN B NE2 1 
ATOM   5364 N  N   . GLU B 1 207 ? 11.853  -32.855 48.966  1.00 52.68  ? 207 GLU B N   1 
ATOM   5365 C  CA  . GLU B 1 207 ? 11.747  -32.213 47.658  1.00 53.10  ? 207 GLU B CA  1 
ATOM   5366 C  C   . GLU B 1 207 ? 11.223  -30.785 47.788  1.00 50.82  ? 207 GLU B C   1 
ATOM   5367 O  O   . GLU B 1 207 ? 11.660  -29.885 47.060  1.00 52.18  ? 207 GLU B O   1 
ATOM   5368 C  CB  . GLU B 1 207 ? 10.858  -33.063 46.743  1.00 55.18  ? 207 GLU B CB  1 
ATOM   5369 C  CG  . GLU B 1 207 ? 10.377  -32.392 45.459  1.00 60.79  ? 207 GLU B CG  1 
ATOM   5370 C  CD  . GLU B 1 207 ? 9.467   -33.309 44.636  1.00 68.48  ? 207 GLU B CD  1 
ATOM   5371 O  OE1 . GLU B 1 207 ? 8.255   -33.010 44.507  1.00 67.16  ? 207 GLU B OE1 1 
ATOM   5372 O  OE2 . GLU B 1 207 ? 9.971   -34.336 44.123  1.00 72.82  ? 207 GLU B OE2 1 
ATOM   5373 N  N   . ASP B 1 208 ? 10.306  -30.550 48.731  1.00 50.51  ? 208 ASP B N   1 
ATOM   5374 C  CA  . ASP B 1 208 ? 9.762   -29.206 48.903  1.00 50.42  ? 208 ASP B CA  1 
ATOM   5375 C  C   . ASP B 1 208 ? 10.781  -28.279 49.551  1.00 44.99  ? 208 ASP B C   1 
ATOM   5376 O  O   . ASP B 1 208 ? 10.844  -27.091 49.219  1.00 47.53  ? 208 ASP B O   1 
ATOM   5377 C  CB  . ASP B 1 208 ? 8.485   -29.264 49.740  1.00 44.75  ? 208 ASP B CB  1 
ATOM   5378 C  CG  . ASP B 1 208 ? 7.305   -29.785 48.958  1.00 47.28  ? 208 ASP B CG  1 
ATOM   5379 O  OD1 . ASP B 1 208 ? 7.257   -29.564 47.730  1.00 45.69  ? 208 ASP B OD1 1 
ATOM   5380 O  OD2 . ASP B 1 208 ? 6.432   -30.425 49.577  1.00 46.46  ? 208 ASP B OD2 1 
ATOM   5381 N  N   . ILE B 1 209 ? 11.579  -28.803 50.485  1.00 48.72  ? 209 ILE B N   1 
ATOM   5382 C  CA  . ILE B 1 209 ? 12.658  -28.014 51.071  1.00 45.02  ? 209 ILE B CA  1 
ATOM   5383 C  C   . ILE B 1 209 ? 13.678  -27.621 50.009  1.00 50.01  ? 209 ILE B C   1 
ATOM   5384 O  O   . ILE B 1 209 ? 14.187  -26.493 50.006  1.00 49.50  ? 209 ILE B O   1 
ATOM   5385 C  CB  . ILE B 1 209 ? 13.320  -28.772 52.236  1.00 49.25  ? 209 ILE B CB  1 
ATOM   5386 C  CG1 . ILE B 1 209 ? 12.298  -29.113 53.325  1.00 46.67  ? 209 ILE B CG1 1 
ATOM   5387 C  CG2 . ILE B 1 209 ? 14.496  -27.977 52.809  1.00 49.99  ? 209 ILE B CG2 1 
ATOM   5388 C  CD1 . ILE B 1 209 ? 12.840  -30.081 54.372  1.00 47.05  ? 209 ILE B CD1 1 
ATOM   5389 N  N   . LYS B 1 210 ? 13.992  -28.532 49.085  1.00 51.51  ? 210 LYS B N   1 
ATOM   5390 C  CA  . LYS B 1 210 ? 14.951  -28.164 48.048  1.00 52.62  ? 210 LYS B CA  1 
ATOM   5391 C  C   . LYS B 1 210 ? 14.342  -27.187 47.046  1.00 49.34  ? 210 LYS B C   1 
ATOM   5392 O  O   . LYS B 1 210 ? 15.053  -26.330 46.511  1.00 53.74  ? 210 LYS B O   1 
ATOM   5393 C  CB  . LYS B 1 210 ? 15.500  -29.412 47.348  1.00 51.39  ? 210 LYS B CB  1 
ATOM   5394 C  CG  . LYS B 1 210 ? 16.307  -29.085 46.091  1.00 56.56  ? 210 LYS B CG  1 
ATOM   5395 C  CD  . LYS B 1 210 ? 17.126  -30.286 45.590  1.00 58.45  ? 210 LYS B CD  1 
ATOM   5396 C  CE  . LYS B 1 210 ? 18.248  -29.827 44.662  1.00 56.98  ? 210 LYS B CE  1 
ATOM   5397 N  NZ  . LYS B 1 210 ? 17.957  -30.168 43.239  1.00 62.82  ? 210 LYS B NZ  1 
ATOM   5398 N  N   . VAL B 1 211 ? 13.032  -27.274 46.797  1.00 51.67  ? 211 VAL B N   1 
ATOM   5399 C  CA  . VAL B 1 211 ? 12.370  -26.279 45.952  1.00 47.73  ? 211 VAL B CA  1 
ATOM   5400 C  C   . VAL B 1 211 ? 12.458  -24.898 46.589  1.00 51.12  ? 211 VAL B C   1 
ATOM   5401 O  O   . VAL B 1 211 ? 12.803  -23.900 45.940  1.00 43.97  ? 211 VAL B O   1 
ATOM   5402 C  CB  . VAL B 1 211 ? 10.908  -26.683 45.693  1.00 46.40  ? 211 VAL B CB  1 
ATOM   5403 C  CG1 . VAL B 1 211 ? 10.118  -25.516 45.128  1.00 44.39  ? 211 VAL B CG1 1 
ATOM   5404 C  CG2 . VAL B 1 211 ? 10.846  -27.869 44.722  1.00 50.79  ? 211 VAL B CG2 1 
ATOM   5405 N  N   . MET B 1 212 ? 12.112  -24.824 47.872  1.00 48.49  ? 212 MET B N   1 
ATOM   5406 C  CA  . MET B 1 212 ? 12.150  -23.566 48.609  1.00 45.68  ? 212 MET B CA  1 
ATOM   5407 C  C   . MET B 1 212 ? 13.554  -22.966 48.620  1.00 46.45  ? 212 MET B C   1 
ATOM   5408 O  O   . MET B 1 212 ? 13.736  -21.794 48.277  1.00 44.06  ? 212 MET B O   1 
ATOM   5409 C  CB  . MET B 1 212 ? 11.615  -23.847 50.013  1.00 43.72  ? 212 MET B CB  1 
ATOM   5410 C  CG  . MET B 1 212 ? 10.092  -23.987 49.983  1.00 47.77  ? 212 MET B CG  1 
ATOM   5411 S  SD  . MET B 1 212 ? 9.313   -23.742 51.576  1.00 45.78  ? 212 MET B SD  1 
ATOM   5412 C  CE  . MET B 1 212 ? 9.723   -25.300 52.323  1.00 39.33  ? 212 MET B CE  1 
ATOM   5413 N  N   . ASN B 1 213 ? 14.565  -23.764 48.985  1.00 47.07  ? 213 ASN B N   1 
ATOM   5414 C  CA  . ASN B 1 213 ? 15.936  -23.248 49.021  1.00 50.15  ? 213 ASN B CA  1 
ATOM   5415 C  C   . ASN B 1 213 ? 16.413  -22.797 47.648  1.00 50.68  ? 213 ASN B C   1 
ATOM   5416 O  O   . ASN B 1 213 ? 16.897  -21.669 47.492  1.00 49.74  ? 213 ASN B O   1 
ATOM   5417 C  CB  . ASN B 1 213 ? 16.890  -24.289 49.606  1.00 46.42  ? 213 ASN B CB  1 
ATOM   5418 C  CG  . ASN B 1 213 ? 16.539  -24.660 51.030  1.00 50.68  ? 213 ASN B CG  1 
ATOM   5419 O  OD1 . ASN B 1 213 ? 15.735  -23.984 51.667  1.00 50.44  ? 213 ASN B OD1 1 
ATOM   5420 N  ND2 . ASN B 1 213 ? 17.163  -25.714 51.548  1.00 47.77  ? 213 ASN B ND2 1 
ATOM   5421 N  N   . ASP B 1 214 ? 16.311  -23.671 46.640  1.00 50.37  ? 214 ASP B N   1 
ATOM   5422 C  CA  . ASP B 1 214 ? 16.834  -23.310 45.325  1.00 53.98  ? 214 ASP B CA  1 
ATOM   5423 C  C   . ASP B 1 214 ? 16.218  -22.013 44.816  1.00 46.13  ? 214 ASP B C   1 
ATOM   5424 O  O   . ASP B 1 214 ? 16.922  -21.167 44.260  1.00 49.35  ? 214 ASP B O   1 
ATOM   5425 C  CB  . ASP B 1 214 ? 16.614  -24.451 44.332  1.00 51.27  ? 214 ASP B CB  1 
ATOM   5426 C  CG  . ASP B 1 214 ? 17.346  -25.714 44.734  1.00 56.28  ? 214 ASP B CG  1 
ATOM   5427 O  OD1 . ASP B 1 214 ? 18.161  -25.661 45.684  1.00 59.30  ? 214 ASP B OD1 1 
ATOM   5428 O  OD2 . ASP B 1 214 ? 17.100  -26.768 44.112  1.00 58.57  ? 214 ASP B OD2 1 
ATOM   5429 N  N   . LEU B 1 215 ? 14.913  -21.811 45.041  1.00 50.75  ? 215 LEU B N   1 
ATOM   5430 C  CA  . LEU B 1 215 ? 14.235  -20.654 44.453  1.00 41.28  ? 215 LEU B CA  1 
ATOM   5431 C  C   . LEU B 1 215 ? 14.552  -19.352 45.194  1.00 47.94  ? 215 LEU B C   1 
ATOM   5432 O  O   . LEU B 1 215 ? 14.710  -18.299 44.560  1.00 45.46  ? 215 LEU B O   1 
ATOM   5433 C  CB  . LEU B 1 215 ? 12.726  -20.898 44.425  1.00 48.18  ? 215 LEU B CB  1 
ATOM   5434 C  CG  . LEU B 1 215 ? 12.310  -22.093 43.555  1.00 52.20  ? 215 LEU B CG  1 
ATOM   5435 C  CD1 . LEU B 1 215 ? 10.818  -22.395 43.696  1.00 50.50  ? 215 LEU B CD1 1 
ATOM   5436 C  CD2 . LEU B 1 215 ? 12.693  -21.857 42.093  1.00 51.42  ? 215 LEU B CD2 1 
ATOM   5437 N  N   . VAL B 1 216 ? 14.592  -19.389 46.534  1.00 46.78  ? 216 VAL B N   1 
ATOM   5438 C  CA  . VAL B 1 216 ? 15.003  -18.213 47.302  1.00 48.70  ? 216 VAL B CA  1 
ATOM   5439 C  C   . VAL B 1 216 ? 16.496  -17.934 47.113  1.00 44.77  ? 216 VAL B C   1 
ATOM   5440 O  O   . VAL B 1 216 ? 16.917  -16.775 47.025  1.00 43.93  ? 216 VAL B O   1 
ATOM   5441 C  CB  . VAL B 1 216 ? 14.645  -18.389 48.793  1.00 46.51  ? 216 VAL B CB  1 
ATOM   5442 C  CG1 . VAL B 1 216 ? 14.949  -17.115 49.562  1.00 45.60  ? 216 VAL B CG1 1 
ATOM   5443 C  CG2 . VAL B 1 216 ? 13.150  -18.729 48.958  1.00 42.04  ? 216 VAL B CG2 1 
ATOM   5444 N  N   . ASP B 1 217 ? 17.322  -18.985 47.075  1.00 46.02  ? 217 ASP B N   1 
ATOM   5445 C  CA  . ASP B 1 217 ? 18.745  -18.767 46.826  1.00 48.55  ? 217 ASP B CA  1 
ATOM   5446 C  C   . ASP B 1 217 ? 18.968  -18.042 45.503  1.00 49.24  ? 217 ASP B C   1 
ATOM   5447 O  O   . ASP B 1 217 ? 19.825  -17.159 45.416  1.00 48.48  ? 217 ASP B O   1 
ATOM   5448 C  CB  . ASP B 1 217 ? 19.509  -20.088 46.840  1.00 44.60  ? 217 ASP B CB  1 
ATOM   5449 C  CG  . ASP B 1 217 ? 19.700  -20.634 48.229  1.00 50.52  ? 217 ASP B CG  1 
ATOM   5450 O  OD1 . ASP B 1 217 ? 19.475  -19.872 49.187  1.00 49.41  ? 217 ASP B OD1 1 
ATOM   5451 O  OD2 . ASP B 1 217 ? 20.090  -21.818 48.363  1.00 46.78  ? 217 ASP B OD2 1 
ATOM   5452 N  N   . LYS B 1 218 ? 18.191  -18.381 44.465  1.00 47.85  ? 218 LYS B N   1 
ATOM   5453 C  CA  . LYS B 1 218 ? 18.368  -17.705 43.179  1.00 49.10  ? 218 LYS B CA  1 
ATOM   5454 C  C   . LYS B 1 218 ? 17.851  -16.275 43.227  1.00 52.47  ? 218 LYS B C   1 
ATOM   5455 O  O   . LYS B 1 218 ? 18.411  -15.389 42.574  1.00 53.16  ? 218 LYS B O   1 
ATOM   5456 C  CB  . LYS B 1 218 ? 17.670  -18.464 42.050  1.00 55.78  ? 218 LYS B CB  1 
ATOM   5457 C  CG  . LYS B 1 218 ? 17.865  -17.793 40.679  1.00 56.98  ? 218 LYS B CG  1 
ATOM   5458 C  CD  . LYS B 1 218 ? 17.174  -18.565 39.577  1.00 68.42  ? 218 LYS B CD  1 
ATOM   5459 C  CE  . LYS B 1 218 ? 17.369  -20.058 39.771  1.00 70.87  ? 218 LYS B CE  1 
ATOM   5460 N  NZ  . LYS B 1 218 ? 16.108  -20.819 39.521  1.00 79.32  ? 218 LYS B NZ  1 
ATOM   5461 N  N   . ILE B 1 219 ? 16.770  -16.031 43.976  1.00 47.73  ? 219 ILE B N   1 
ATOM   5462 C  CA  . ILE B 1 219 ? 16.309  -14.662 44.194  1.00 46.26  ? 219 ILE B CA  1 
ATOM   5463 C  C   . ILE B 1 219 ? 17.420  -13.819 44.807  1.00 51.87  ? 219 ILE B C   1 
ATOM   5464 O  O   . ILE B 1 219 ? 17.692  -12.692 44.365  1.00 47.84  ? 219 ILE B O   1 
ATOM   5465 C  CB  . ILE B 1 219 ? 15.050  -14.664 45.079  1.00 51.96  ? 219 ILE B CB  1 
ATOM   5466 C  CG1 . ILE B 1 219 ? 13.854  -15.148 44.261  1.00 49.62  ? 219 ILE B CG1 1 
ATOM   5467 C  CG2 . ILE B 1 219 ? 14.812  -13.308 45.684  1.00 49.94  ? 219 ILE B CG2 1 
ATOM   5468 C  CD1 . ILE B 1 219 ? 13.389  -14.107 43.304  1.00 51.48  ? 219 ILE B CD1 1 
ATOM   5469 N  N   . ILE B 1 220 ? 18.066  -14.353 45.848  1.00 46.11  ? 220 ILE B N   1 
ATOM   5470 C  CA  . ILE B 1 220 ? 19.166  -13.642 46.497  1.00 47.98  ? 220 ILE B CA  1 
ATOM   5471 C  C   . ILE B 1 220 ? 20.294  -13.402 45.507  1.00 50.51  ? 220 ILE B C   1 
ATOM   5472 O  O   . ILE B 1 220 ? 20.768  -12.274 45.340  1.00 49.48  ? 220 ILE B O   1 
ATOM   5473 C  CB  . ILE B 1 220 ? 19.660  -14.421 47.729  1.00 48.74  ? 220 ILE B CB  1 
ATOM   5474 C  CG1 . ILE B 1 220 ? 18.489  -14.810 48.641  1.00 48.37  ? 220 ILE B CG1 1 
ATOM   5475 C  CG2 . ILE B 1 220 ? 20.709  -13.614 48.486  1.00 48.50  ? 220 ILE B CG2 1 
ATOM   5476 C  CD1 . ILE B 1 220 ? 18.926  -15.376 49.998  1.00 43.18  ? 220 ILE B CD1 1 
ATOM   5477 N  N   . ALA B 1 221 ? 20.744  -14.462 44.837  1.00 50.73  ? 221 ALA B N   1 
ATOM   5478 C  CA  . ALA B 1 221 ? 21.826  -14.310 43.870  1.00 53.88  ? 221 ALA B CA  1 
ATOM   5479 C  C   . ALA B 1 221 ? 21.469  -13.260 42.820  1.00 58.17  ? 221 ALA B C   1 
ATOM   5480 O  O   . ALA B 1 221 ? 22.220  -12.299 42.604  1.00 57.62  ? 221 ALA B O   1 
ATOM   5481 C  CB  . ALA B 1 221 ? 22.140  -15.659 43.230  1.00 52.51  ? 221 ALA B CB  1 
ATOM   5482 N  N   . ASP B 1 222 ? 20.297  -13.406 42.189  1.00 56.73  ? 222 ASP B N   1 
ATOM   5483 C  CA  . ASP B 1 222 ? 19.853  -12.454 41.172  1.00 55.06  ? 222 ASP B CA  1 
ATOM   5484 C  C   . ASP B 1 222 ? 20.015  -11.014 41.649  1.00 58.45  ? 222 ASP B C   1 
ATOM   5485 O  O   . ASP B 1 222 ? 20.596  -10.180 40.949  1.00 62.35  ? 222 ASP B O   1 
ATOM   5486 C  CB  . ASP B 1 222 ? 18.395  -12.726 40.807  1.00 57.94  ? 222 ASP B CB  1 
ATOM   5487 C  CG  . ASP B 1 222 ? 18.224  -13.958 39.927  1.00 60.16  ? 222 ASP B CG  1 
ATOM   5488 O  OD1 . ASP B 1 222 ? 19.230  -14.621 39.600  1.00 61.87  ? 222 ASP B OD1 1 
ATOM   5489 O  OD2 . ASP B 1 222 ? 17.067  -14.274 39.576  1.00 65.86  ? 222 ASP B OD2 1 
ATOM   5490 N  N   . ARG B 1 223 ? 19.498  -10.701 42.842  1.00 50.39  ? 223 ARG B N   1 
ATOM   5491 C  CA  . ARG B 1 223 ? 19.623  -9.351  43.383  1.00 53.97  ? 223 ARG B CA  1 
ATOM   5492 C  C   . ARG B 1 223 ? 21.079  -8.961  43.603  1.00 58.81  ? 223 ARG B C   1 
ATOM   5493 O  O   . ARG B 1 223 ? 21.400  -7.768  43.630  1.00 60.12  ? 223 ARG B O   1 
ATOM   5494 C  CB  . ARG B 1 223 ? 18.857  -9.244  44.704  1.00 49.98  ? 223 ARG B CB  1 
ATOM   5495 C  CG  . ARG B 1 223 ? 18.914  -7.881  45.365  1.00 49.95  ? 223 ARG B CG  1 
ATOM   5496 C  CD  . ARG B 1 223 ? 18.027  -6.873  44.654  1.00 52.71  ? 223 ARG B CD  1 
ATOM   5497 N  NE  . ARG B 1 223 ? 16.611  -7.203  44.778  1.00 54.37  ? 223 ARG B NE  1 
ATOM   5498 C  CZ  . ARG B 1 223 ? 15.802  -6.734  45.721  1.00 50.04  ? 223 ARG B CZ  1 
ATOM   5499 N  NH1 . ARG B 1 223 ? 16.237  -5.920  46.669  1.00 53.22  ? 223 ARG B NH1 1 
ATOM   5500 N  NH2 . ARG B 1 223 ? 14.522  -7.089  45.712  1.00 51.37  ? 223 ARG B NH2 1 
ATOM   5501 N  N   . LYS B 1 224 ? 21.961  -9.945  43.775  1.00 57.80  ? 224 LYS B N   1 
ATOM   5502 C  CA  . LYS B 1 224 ? 23.379  -9.664  43.955  1.00 61.43  ? 224 LYS B CA  1 
ATOM   5503 C  C   . LYS B 1 224 ? 24.102  -9.501  42.621  1.00 62.57  ? 224 LYS B C   1 
ATOM   5504 O  O   . LYS B 1 224 ? 25.063  -8.729  42.535  1.00 68.05  ? 224 LYS B O   1 
ATOM   5505 C  CB  . LYS B 1 224 ? 24.022  -10.777 44.785  1.00 58.51  ? 224 LYS B CB  1 
ATOM   5506 C  CG  . LYS B 1 224 ? 23.900  -10.565 46.275  1.00 50.03  ? 224 LYS B CG  1 
ATOM   5507 C  CD  . LYS B 1 224 ? 24.422  -11.749 47.055  1.00 54.73  ? 224 LYS B CD  1 
ATOM   5508 C  CE  . LYS B 1 224 ? 25.656  -11.355 47.847  1.00 56.20  ? 224 LYS B CE  1 
ATOM   5509 N  NZ  . LYS B 1 224 ? 26.533  -12.520 48.131  1.00 58.34  ? 224 LYS B NZ  1 
ATOM   5510 N  N   . ALA B 1 225 ? 23.651  -10.203 41.575  1.00 63.38  ? 225 ALA B N   1 
ATOM   5511 C  CA  . ALA B 1 225 ? 24.242  -10.046 40.248  1.00 62.57  ? 225 ALA B CA  1 
ATOM   5512 C  C   . ALA B 1 225 ? 23.972  -8.660  39.670  1.00 67.83  ? 225 ALA B C   1 
ATOM   5513 O  O   . ALA B 1 225 ? 24.759  -8.163  38.855  1.00 72.26  ? 225 ALA B O   1 
ATOM   5514 C  CB  . ALA B 1 225 ? 23.710  -11.128 39.308  1.00 61.09  ? 225 ALA B CB  1 
ATOM   5515 N  N   . SER B 1 226 ? 22.863  -8.038  40.055  1.00 70.25  ? 226 SER B N   1 
ATOM   5516 C  CA  . SER B 1 226 ? 22.601  -6.634  39.790  1.00 73.39  ? 226 SER B CA  1 
ATOM   5517 C  C   . SER B 1 226 ? 23.010  -5.821  41.020  1.00 71.37  ? 226 SER B C   1 
ATOM   5518 O  O   . SER B 1 226 ? 23.636  -6.339  41.950  1.00 74.85  ? 226 SER B O   1 
ATOM   5519 C  CB  . SER B 1 226 ? 21.131  -6.448  39.420  1.00 70.19  ? 226 SER B CB  1 
ATOM   5520 O  OG  . SER B 1 226 ? 20.299  -6.800  40.510  1.00 67.35  ? 226 SER B OG  1 
ATOM   5521 N  N   . GLY B 1 227 ? 22.655  -4.539  41.046  1.00 74.80  ? 227 GLY B N   1 
ATOM   5522 C  CA  . GLY B 1 227 ? 23.030  -3.716  42.182  1.00 77.85  ? 227 GLY B CA  1 
ATOM   5523 C  C   . GLY B 1 227 ? 21.922  -2.825  42.703  1.00 82.58  ? 227 GLY B C   1 
ATOM   5524 O  O   . GLY B 1 227 ? 22.110  -2.082  43.674  1.00 80.70  ? 227 GLY B O   1 
ATOM   5525 N  N   . GLU B 1 228 ? 20.755  -2.904  42.071  1.00 83.66  ? 228 GLU B N   1 
ATOM   5526 C  CA  . GLU B 1 228 ? 19.666  -1.982  42.367  1.00 85.34  ? 228 GLU B CA  1 
ATOM   5527 C  C   . GLU B 1 228 ? 19.296  -2.013  43.846  1.00 81.87  ? 228 GLU B C   1 
ATOM   5528 O  O   . GLU B 1 228 ? 18.932  -3.064  44.383  1.00 79.40  ? 228 GLU B O   1 
ATOM   5529 C  CB  . GLU B 1 228 ? 18.454  -2.334  41.509  1.00 88.65  ? 228 GLU B CB  1 
ATOM   5530 C  CG  . GLU B 1 228 ? 18.366  -1.560  40.206  1.00 97.32  ? 228 GLU B CG  1 
ATOM   5531 C  CD  . GLU B 1 228 ? 17.829  -2.409  39.071  1.00 101.08 ? 228 GLU B CD  1 
ATOM   5532 O  OE1 . GLU B 1 228 ? 16.978  -3.285  39.337  1.00 99.44  ? 228 GLU B OE1 1 
ATOM   5533 O  OE2 . GLU B 1 228 ? 18.257  -2.198  37.916  1.00 103.06 ? 228 GLU B OE2 1 
ATOM   5534 N  N   . GLN B 1 229 ? 19.392  -0.855  44.504  1.00 82.27  ? 229 GLN B N   1 
ATOM   5535 C  CA  . GLN B 1 229 ? 18.782  -0.681  45.817  1.00 80.07  ? 229 GLN B CA  1 
ATOM   5536 C  C   . GLN B 1 229 ? 17.272  -0.786  45.659  1.00 78.17  ? 229 GLN B C   1 
ATOM   5537 O  O   . GLN B 1 229 ? 16.778  -0.899  44.533  1.00 83.41  ? 229 GLN B O   1 
ATOM   5538 C  CB  . GLN B 1 229 ? 19.169  0.664   46.440  1.00 82.35  ? 229 GLN B CB  1 
ATOM   5539 C  CG  . GLN B 1 229 ? 20.661  0.878   46.576  1.00 84.61  ? 229 GLN B CG  1 
ATOM   5540 C  CD  . GLN B 1 229 ? 21.363  -0.324  47.172  1.00 83.19  ? 229 GLN B CD  1 
ATOM   5541 O  OE1 . GLN B 1 229 ? 21.339  -0.530  48.388  1.00 79.56  ? 229 GLN B OE1 1 
ATOM   5542 N  NE2 . GLN B 1 229 ? 21.997  -1.124  46.319  1.00 77.60  ? 229 GLN B NE2 1 
ATOM   5543 N  N   . SER B 1 230 ? 16.524  -0.765  46.759  1.00 79.81  ? 230 SER B N   1 
ATOM   5544 C  CA  . SER B 1 230 ? 15.073  -0.854  46.653  1.00 73.70  ? 230 SER B CA  1 
ATOM   5545 C  C   . SER B 1 230 ? 14.441  -0.581  48.010  1.00 72.99  ? 230 SER B C   1 
ATOM   5546 O  O   . SER B 1 230 ? 15.119  -0.455  49.032  1.00 75.63  ? 230 SER B O   1 
ATOM   5547 C  CB  . SER B 1 230 ? 14.612  -2.217  46.116  1.00 71.18  ? 230 SER B CB  1 
ATOM   5548 O  OG  . SER B 1 230 ? 15.489  -2.743  45.136  1.00 74.20  ? 230 SER B OG  1 
ATOM   5549 N  N   . ASP B 1 231 ? 13.117  -0.479  47.990  1.00 76.87  ? 231 ASP B N   1 
ATOM   5550 C  CA  . ASP B 1 231 ? 12.278  -0.321  49.174  1.00 76.87  ? 231 ASP B CA  1 
ATOM   5551 C  C   . ASP B 1 231 ? 12.014  -1.642  49.873  1.00 69.83  ? 231 ASP B C   1 
ATOM   5552 O  O   . ASP B 1 231 ? 10.867  -1.918  50.241  1.00 69.39  ? 231 ASP B O   1 
ATOM   5553 C  CB  . ASP B 1 231 ? 10.955  0.323   48.756  1.00 79.19  ? 231 ASP B CB  1 
ATOM   5554 C  CG  . ASP B 1 231 ? 10.884  1.811   49.068  1.00 85.27  ? 231 ASP B CG  1 
ATOM   5555 O  OD1 . ASP B 1 231 ? 11.122  2.203   50.235  1.00 85.39  ? 231 ASP B OD1 1 
ATOM   5556 O  OD2 . ASP B 1 231 ? 10.568  2.586   48.138  1.00 87.32  ? 231 ASP B OD2 1 
ATOM   5557 N  N   . ASP B 1 232 ? 13.014  -2.503  50.059  1.00 68.20  ? 232 ASP B N   1 
ATOM   5558 C  CA  . ASP B 1 232 ? 12.634  -3.856  50.432  1.00 57.32  ? 232 ASP B CA  1 
ATOM   5559 C  C   . ASP B 1 232 ? 13.631  -4.526  51.376  1.00 51.82  ? 232 ASP B C   1 
ATOM   5560 O  O   . ASP B 1 232 ? 14.797  -4.136  51.501  1.00 51.99  ? 232 ASP B O   1 
ATOM   5561 C  CB  . ASP B 1 232 ? 12.320  -4.671  49.158  1.00 49.95  ? 232 ASP B CB  1 
ATOM   5562 C  CG  . ASP B 1 232 ? 13.540  -5.266  48.478  1.00 52.69  ? 232 ASP B CG  1 
ATOM   5563 O  OD1 . ASP B 1 232 ? 14.619  -5.412  49.091  1.00 54.32  ? 232 ASP B OD1 1 
ATOM   5564 O  OD2 . ASP B 1 232 ? 13.399  -5.591  47.276  1.00 49.51  ? 232 ASP B OD2 1 
ATOM   5565 N  N   . LEU B 1 233 ? 13.111  -5.545  52.060  1.00 47.45  ? 233 LEU B N   1 
ATOM   5566 C  CA  . LEU B 1 233 ? 13.830  -6.221  53.130  1.00 45.86  ? 233 LEU B CA  1 
ATOM   5567 C  C   . LEU B 1 233 ? 15.045  -6.952  52.603  1.00 46.34  ? 233 LEU B C   1 
ATOM   5568 O  O   . LEU B 1 233 ? 16.005  -7.171  53.349  1.00 47.46  ? 233 LEU B O   1 
ATOM   5569 C  CB  . LEU B 1 233 ? 12.897  -7.213  53.833  1.00 45.76  ? 233 LEU B CB  1 
ATOM   5570 C  CG  . LEU B 1 233 ? 11.669  -6.654  54.562  1.00 42.16  ? 233 LEU B CG  1 
ATOM   5571 C  CD1 . LEU B 1 233 ? 10.629  -7.754  54.789  1.00 47.22  ? 233 LEU B CD1 1 
ATOM   5572 C  CD2 . LEU B 1 233 ? 12.020  -5.977  55.874  1.00 41.41  ? 233 LEU B CD2 1 
ATOM   5573 N  N   . LEU B 1 234 ? 15.018  -7.368  51.335  1.00 44.33  ? 234 LEU B N   1 
ATOM   5574 C  CA  . LEU B 1 234 ? 16.158  -8.099  50.799  1.00 42.94  ? 234 LEU B CA  1 
ATOM   5575 C  C   . LEU B 1 234 ? 17.356  -7.177  50.627  1.00 52.97  ? 234 LEU B C   1 
ATOM   5576 O  O   . LEU B 1 234 ? 18.488  -7.550  50.963  1.00 44.15  ? 234 LEU B O   1 
ATOM   5577 C  CB  . LEU B 1 234 ? 15.786  -8.774  49.482  1.00 46.62  ? 234 LEU B CB  1 
ATOM   5578 C  CG  . LEU B 1 234 ? 16.925  -9.494  48.759  1.00 47.51  ? 234 LEU B CG  1 
ATOM   5579 C  CD1 . LEU B 1 234 ? 17.542  -10.589 49.628  1.00 46.66  ? 234 LEU B CD1 1 
ATOM   5580 C  CD2 . LEU B 1 234 ? 16.426  -10.093 47.448  1.00 45.94  ? 234 LEU B CD2 1 
ATOM   5581 N  N   . THR B 1 235 ? 17.120  -5.964  50.124  1.00 50.82  ? 235 THR B N   1 
ATOM   5582 C  CA  . THR B 1 235 ? 18.203  -4.995  49.981  1.00 54.62  ? 235 THR B CA  1 
ATOM   5583 C  C   . THR B 1 235 ? 18.871  -4.735  51.326  1.00 53.18  ? 235 THR B C   1 
ATOM   5584 O  O   . THR B 1 235 ? 20.099  -4.802  51.448  1.00 51.09  ? 235 THR B O   1 
ATOM   5585 C  CB  . THR B 1 235 ? 17.669  -3.686  49.392  1.00 59.31  ? 235 THR B CB  1 
ATOM   5586 O  OG1 . THR B 1 235 ? 17.429  -3.845  47.986  1.00 62.10  ? 235 THR B OG1 1 
ATOM   5587 C  CG2 . THR B 1 235 ? 18.700  -2.588  49.572  1.00 62.36  ? 235 THR B CG2 1 
ATOM   5588 N  N   . HIS B 1 236 ? 18.070  -4.445  52.353  1.00 49.28  ? 236 HIS B N   1 
ATOM   5589 C  CA  . HIS B 1 236 ? 18.634  -4.203  53.680  1.00 54.26  ? 236 HIS B CA  1 
ATOM   5590 C  C   . HIS B 1 236 ? 19.376  -5.419  54.221  1.00 53.48  ? 236 HIS B C   1 
ATOM   5591 O  O   . HIS B 1 236 ? 20.451  -5.290  54.821  1.00 52.14  ? 236 HIS B O   1 
ATOM   5592 C  CB  . HIS B 1 236 ? 17.548  -3.788  54.663  1.00 50.60  ? 236 HIS B CB  1 
ATOM   5593 C  CG  . HIS B 1 236 ? 18.108  -3.254  55.940  1.00 59.29  ? 236 HIS B CG  1 
ATOM   5594 N  ND1 . HIS B 1 236 ? 17.608  -3.599  57.178  1.00 57.56  ? 236 HIS B ND1 1 
ATOM   5595 C  CD2 . HIS B 1 236 ? 19.176  -2.453  56.172  1.00 55.19  ? 236 HIS B CD2 1 
ATOM   5596 C  CE1 . HIS B 1 236 ? 18.325  -3.004  58.117  1.00 56.18  ? 236 HIS B CE1 1 
ATOM   5597 N  NE2 . HIS B 1 236 ? 19.283  -2.306  57.533  1.00 54.82  ? 236 HIS B NE2 1 
ATOM   5598 N  N   . MET B 1 237 ? 18.805  -6.604  54.051  1.00 47.22  ? 237 MET B N   1 
ATOM   5599 C  CA  . MET B 1 237 ? 19.456  -7.799  54.562  1.00 47.26  ? 237 MET B CA  1 
ATOM   5600 C  C   . MET B 1 237 ? 20.805  -8.002  53.884  1.00 50.73  ? 237 MET B C   1 
ATOM   5601 O  O   . MET B 1 237 ? 21.748  -8.512  54.502  1.00 45.27  ? 237 MET B O   1 
ATOM   5602 C  CB  . MET B 1 237 ? 18.522  -8.983  54.342  1.00 41.09  ? 237 MET B CB  1 
ATOM   5603 C  CG  . MET B 1 237 ? 17.507  -9.106  55.463  1.00 40.97  ? 237 MET B CG  1 
ATOM   5604 S  SD  . MET B 1 237 ? 16.636  -10.681 55.539  1.00 40.93  ? 237 MET B SD  1 
ATOM   5605 C  CE  . MET B 1 237 ? 15.672  -10.647 54.023  1.00 37.82  ? 237 MET B CE  1 
ATOM   5606 N  N   . LEU B 1 238 ? 20.923  -7.566  52.624  1.00 47.62  ? 238 LEU B N   1 
ATOM   5607 C  CA  . LEU B 1 238 ? 22.178  -7.686  51.894  1.00 48.89  ? 238 LEU B CA  1 
ATOM   5608 C  C   . LEU B 1 238 ? 23.196  -6.644  52.332  1.00 50.69  ? 238 LEU B C   1 
ATOM   5609 O  O   . LEU B 1 238 ? 24.405  -6.878  52.227  1.00 57.89  ? 238 LEU B O   1 
ATOM   5610 C  CB  . LEU B 1 238 ? 21.924  -7.547  50.392  1.00 48.48  ? 238 LEU B CB  1 
ATOM   5611 C  CG  . LEU B 1 238 ? 21.306  -8.751  49.685  1.00 50.82  ? 238 LEU B CG  1 
ATOM   5612 C  CD1 . LEU B 1 238 ? 20.894  -8.371  48.260  1.00 53.10  ? 238 LEU B CD1 1 
ATOM   5613 C  CD2 . LEU B 1 238 ? 22.236  -9.957  49.691  1.00 52.07  ? 238 LEU B CD2 1 
ATOM   5614 N  N   . ASN B 1 239 ? 22.736  -5.493  52.798  1.00 47.76  ? 239 ASN B N   1 
ATOM   5615 C  CA  . ASN B 1 239 ? 23.614  -4.376  53.106  1.00 54.92  ? 239 ASN B CA  1 
ATOM   5616 C  C   . ASN B 1 239 ? 23.781  -4.139  54.596  1.00 47.15  ? 239 ASN B C   1 
ATOM   5617 O  O   . ASN B 1 239 ? 24.892  -3.828  55.035  1.00 47.82  ? 239 ASN B O   1 
ATOM   5618 C  CB  . ASN B 1 239 ? 23.087  -3.084  52.461  1.00 52.40  ? 239 ASN B CB  1 
ATOM   5619 C  CG  . ASN B 1 239 ? 23.196  -3.092  50.939  1.00 58.46  ? 239 ASN B CG  1 
ATOM   5620 O  OD1 . ASN B 1 239 ? 23.926  -3.894  50.353  1.00 57.19  ? 239 ASN B OD1 1 
ATOM   5621 N  ND2 . ASN B 1 239 ? 22.473  -2.178  50.295  1.00 60.69  ? 239 ASN B ND2 1 
ATOM   5622 N  N   . GLY B 1 240 ? 22.709  -4.292  55.378  1.00 44.49  ? 240 GLY B N   1 
ATOM   5623 C  CA  . GLY B 1 240 ? 22.726  -3.854  56.767  1.00 40.31  ? 240 GLY B CA  1 
ATOM   5624 C  C   . GLY B 1 240 ? 23.707  -4.634  57.630  1.00 41.68  ? 240 GLY B C   1 
ATOM   5625 O  O   . GLY B 1 240 ? 24.019  -5.797  57.377  1.00 41.17  ? 240 GLY B O   1 
ATOM   5626 N  N   . LYS B 1 241 ? 24.195  -3.966  58.677  1.00 40.91  ? 241 LYS B N   1 
ATOM   5627 C  CA  . LYS B 1 241 ? 25.137  -4.532  59.635  1.00 40.21  ? 241 LYS B CA  1 
ATOM   5628 C  C   . LYS B 1 241 ? 24.501  -4.532  61.012  1.00 36.46  ? 241 LYS B C   1 
ATOM   5629 O  O   . LYS B 1 241 ? 23.871  -3.546  61.408  1.00 40.15  ? 241 LYS B O   1 
ATOM   5630 C  CB  . LYS B 1 241 ? 26.448  -3.727  59.718  1.00 41.91  ? 241 LYS B CB  1 
ATOM   5631 C  CG  . LYS B 1 241 ? 27.152  -3.498  58.396  1.00 44.77  ? 241 LYS B CG  1 
ATOM   5632 C  CD  . LYS B 1 241 ? 27.544  -4.781  57.717  1.00 47.21  ? 241 LYS B CD  1 
ATOM   5633 C  CE  . LYS B 1 241 ? 28.718  -4.536  56.789  1.00 50.23  ? 241 LYS B CE  1 
ATOM   5634 N  NZ  . LYS B 1 241 ? 29.518  -3.375  57.278  1.00 61.41  ? 241 LYS B NZ  1 
ATOM   5635 N  N   . ASP B 1 242 ? 24.692  -5.624  61.741  1.00 36.64  ? 242 ASP B N   1 
ATOM   5636 C  CA  . ASP B 1 242 ? 24.326  -5.682  63.150  1.00 35.19  ? 242 ASP B CA  1 
ATOM   5637 C  C   . ASP B 1 242 ? 25.283  -4.818  63.963  1.00 38.69  ? 242 ASP B C   1 
ATOM   5638 O  O   . ASP B 1 242 ? 26.501  -5.056  63.924  1.00 36.62  ? 242 ASP B O   1 
ATOM   5639 C  CB  . ASP B 1 242 ? 24.375  -7.123  63.658  1.00 35.95  ? 242 ASP B CB  1 
ATOM   5640 C  CG  . ASP B 1 242 ? 24.341  -7.210  65.182  1.00 33.61  ? 242 ASP B CG  1 
ATOM   5641 O  OD1 . ASP B 1 242 ? 23.686  -6.354  65.821  1.00 35.52  ? 242 ASP B OD1 1 
ATOM   5642 O  OD2 . ASP B 1 242 ? 24.991  -8.126  65.755  1.00 34.20  ? 242 ASP B OD2 1 
ATOM   5643 N  N   . PRO B 1 243 ? 24.791  -3.827  64.713  1.00 34.55  ? 243 PRO B N   1 
ATOM   5644 C  CA  . PRO B 1 243 ? 25.700  -2.969  65.500  1.00 38.73  ? 243 PRO B CA  1 
ATOM   5645 C  C   . PRO B 1 243 ? 26.489  -3.718  66.552  1.00 38.85  ? 243 PRO B C   1 
ATOM   5646 O  O   . PRO B 1 243 ? 27.610  -3.303  66.873  1.00 37.07  ? 243 PRO B O   1 
ATOM   5647 C  CB  . PRO B 1 243 ? 24.760  -1.944  66.154  1.00 40.38  ? 243 PRO B CB  1 
ATOM   5648 C  CG  . PRO B 1 243 ? 23.527  -1.958  65.323  1.00 41.66  ? 243 PRO B CG  1 
ATOM   5649 C  CD  . PRO B 1 243 ? 23.402  -3.342  64.735  1.00 38.97  ? 243 PRO B CD  1 
ATOM   5650 N  N   . GLU B 1 244 ? 25.947  -4.801  67.113  1.00 35.02  ? 244 GLU B N   1 
ATOM   5651 C  CA  . GLU B 1 244 ? 26.677  -5.523  68.150  1.00 36.52  ? 244 GLU B CA  1 
ATOM   5652 C  C   . GLU B 1 244 ? 27.847  -6.311  67.559  1.00 40.64  ? 244 GLU B C   1 
ATOM   5653 O  O   . GLU B 1 244 ? 29.009  -6.072  67.906  1.00 39.37  ? 244 GLU B O   1 
ATOM   5654 C  CB  . GLU B 1 244 ? 25.741  -6.452  68.920  1.00 36.08  ? 244 GLU B CB  1 
ATOM   5655 C  CG  . GLU B 1 244 ? 26.470  -7.241  69.994  1.00 40.07  ? 244 GLU B CG  1 
ATOM   5656 C  CD  . GLU B 1 244 ? 25.539  -8.090  70.834  1.00 47.15  ? 244 GLU B CD  1 
ATOM   5657 O  OE1 . GLU B 1 244 ? 24.531  -8.575  70.300  1.00 43.95  ? 244 GLU B OE1 1 
ATOM   5658 O  OE2 . GLU B 1 244 ? 25.803  -8.249  72.040  1.00 58.61  ? 244 GLU B OE2 1 
ATOM   5659 N  N   . THR B 1 245 ? 27.559  -7.273  66.679  1.00 35.60  ? 245 THR B N   1 
ATOM   5660 C  CA  . THR B 1 245 ? 28.629  -8.046  66.058  1.00 33.57  ? 245 THR B CA  1 
ATOM   5661 C  C   . THR B 1 245 ? 29.330  -7.262  64.965  1.00 38.54  ? 245 THR B C   1 
ATOM   5662 O  O   . THR B 1 245 ? 30.458  -7.612  64.603  1.00 38.65  ? 245 THR B O   1 
ATOM   5663 C  CB  . THR B 1 245 ? 28.098  -9.359  65.470  1.00 36.90  ? 245 THR B CB  1 
ATOM   5664 O  OG1 . THR B 1 245 ? 27.267  -9.068  64.349  1.00 34.69  ? 245 THR B OG1 1 
ATOM   5665 C  CG2 . THR B 1 245 ? 27.301  -10.171 66.506  1.00 38.44  ? 245 THR B CG2 1 
ATOM   5666 N  N   . GLY B 1 246 ? 28.695  -6.205  64.445  1.00 32.51  ? 246 GLY B N   1 
ATOM   5667 C  CA  . GLY B 1 246 ? 29.194  -5.491  63.286  1.00 33.42  ? 246 GLY B CA  1 
ATOM   5668 C  C   . GLY B 1 246 ? 29.095  -6.253  61.989  1.00 36.88  ? 246 GLY B C   1 
ATOM   5669 O  O   . GLY B 1 246 ? 29.638  -5.801  60.971  1.00 35.19  ? 246 GLY B O   1 
ATOM   5670 N  N   . GLU B 1 247 ? 28.429  -7.452  61.996  1.00 36.83  ? 247 GLU B N   1 
ATOM   5671 C  CA  . GLU B 1 247 ? 28.390  -8.249  60.778  1.00 36.75  ? 247 GLU B CA  1 
ATOM   5672 C  C   . GLU B 1 247 ? 27.031  -8.127  60.095  1.00 37.48  ? 247 GLU B C   1 
ATOM   5673 O  O   . GLU B 1 247 ? 26.029  -7.825  60.750  1.00 32.54  ? 247 GLU B O   1 
ATOM   5674 C  CB  . GLU B 1 247 ? 28.657  -9.731  61.075  1.00 36.28  ? 247 GLU B CB  1 
ATOM   5675 C  CG  . GLU B 1 247 ? 29.594  -10.017 62.240  1.00 40.43  ? 247 GLU B CG  1 
ATOM   5676 C  CD  . GLU B 1 247 ? 29.575  -11.483 62.653  1.00 41.51  ? 247 GLU B CD  1 
ATOM   5677 O  OE1 . GLU B 1 247 ? 28.631  -12.203 62.245  1.00 41.19  ? 247 GLU B OE1 1 
ATOM   5678 O  OE2 . GLU B 1 247 ? 30.464  -11.901 63.435  1.00 39.22  ? 247 GLU B OE2 1 
ATOM   5679 N  N   . PRO B 1 248 ? 26.980  -8.353  58.786  1.00 39.23  ? 248 PRO B N   1 
ATOM   5680 C  CA  . PRO B 1 248 ? 25.698  -8.532  58.102  1.00 39.10  ? 248 PRO B CA  1 
ATOM   5681 C  C   . PRO B 1 248 ? 25.270  -9.993  58.180  1.00 37.39  ? 248 PRO B C   1 
ATOM   5682 O  O   . PRO B 1 248 ? 26.035  -10.872 58.571  1.00 34.96  ? 248 PRO B O   1 
ATOM   5683 C  CB  . PRO B 1 248 ? 26.025  -8.134  56.657  1.00 37.96  ? 248 PRO B CB  1 
ATOM   5684 C  CG  . PRO B 1 248 ? 27.433  -8.658  56.480  1.00 41.69  ? 248 PRO B CG  1 
ATOM   5685 C  CD  . PRO B 1 248 ? 28.120  -8.438  57.850  1.00 37.20  ? 248 PRO B CD  1 
ATOM   5686 N  N   . LEU B 1 249 ? 24.017  -10.239 57.797  1.00 40.25  ? 249 LEU B N   1 
ATOM   5687 C  CA  . LEU B 1 249 ? 23.526  -11.606 57.675  1.00 39.39  ? 249 LEU B CA  1 
ATOM   5688 C  C   . LEU B 1 249 ? 24.256  -12.316 56.543  1.00 36.98  ? 249 LEU B C   1 
ATOM   5689 O  O   . LEU B 1 249 ? 24.566  -11.701 55.523  1.00 37.99  ? 249 LEU B O   1 
ATOM   5690 C  CB  . LEU B 1 249 ? 22.026  -11.585 57.374  1.00 37.75  ? 249 LEU B CB  1 
ATOM   5691 C  CG  . LEU B 1 249 ? 21.128  -10.971 58.440  1.00 37.72  ? 249 LEU B CG  1 
ATOM   5692 C  CD1 . LEU B 1 249 ? 19.664  -11.183 58.057  1.00 40.69  ? 249 LEU B CD1 1 
ATOM   5693 C  CD2 . LEU B 1 249 ? 21.387  -11.636 59.762  1.00 37.48  ? 249 LEU B CD2 1 
ATOM   5694 N  N   . ASP B 1 250 ? 24.504  -13.617 56.690  1.00 36.26  ? 250 ASP B N   1 
ATOM   5695 C  CA  . ASP B 1 250 ? 25.056  -14.313 55.531  1.00 44.40  ? 250 ASP B CA  1 
ATOM   5696 C  C   . ASP B 1 250 ? 23.916  -14.792 54.617  1.00 44.76  ? 250 ASP B C   1 
ATOM   5697 O  O   . ASP B 1 250 ? 22.733  -14.731 54.973  1.00 39.33  ? 250 ASP B O   1 
ATOM   5698 C  CB  . ASP B 1 250 ? 26.003  -15.451 55.954  1.00 45.38  ? 250 ASP B CB  1 
ATOM   5699 C  CG  . ASP B 1 250 ? 25.314  -16.607 56.671  1.00 48.46  ? 250 ASP B CG  1 
ATOM   5700 O  OD1 . ASP B 1 250 ? 24.087  -16.793 56.555  1.00 51.48  ? 250 ASP B OD1 1 
ATOM   5701 O  OD2 . ASP B 1 250 ? 26.034  -17.357 57.364  1.00 58.46  ? 250 ASP B OD2 1 
ATOM   5702 N  N   . ASP B 1 251 ? 24.277  -15.224 53.396  1.00 44.33  ? 251 ASP B N   1 
ATOM   5703 C  CA  . ASP B 1 251 ? 23.241  -15.499 52.396  1.00 45.20  ? 251 ASP B CA  1 
ATOM   5704 C  C   . ASP B 1 251 ? 22.327  -16.635 52.820  1.00 40.85  ? 251 ASP B C   1 
ATOM   5705 O  O   . ASP B 1 251 ? 21.147  -16.637 52.457  1.00 44.38  ? 251 ASP B O   1 
ATOM   5706 C  CB  . ASP B 1 251 ? 23.836  -15.832 51.023  1.00 44.59  ? 251 ASP B CB  1 
ATOM   5707 C  CG  . ASP B 1 251 ? 24.503  -14.648 50.356  1.00 49.25  ? 251 ASP B CG  1 
ATOM   5708 O  OD1 . ASP B 1 251 ? 24.086  -13.495 50.598  1.00 47.21  ? 251 ASP B OD1 1 
ATOM   5709 O  OD2 . ASP B 1 251 ? 25.396  -14.881 49.514  1.00 55.44  ? 251 ASP B OD2 1 
ATOM   5710 N  N   . GLU B 1 252 ? 22.848  -17.622 53.552  1.00 40.67  ? 252 GLU B N   1 
ATOM   5711 C  CA  . GLU B 1 252 ? 22.002  -18.729 53.980  1.00 41.86  ? 252 GLU B CA  1 
ATOM   5712 C  C   . GLU B 1 252 ? 20.948  -18.260 54.979  1.00 43.63  ? 252 GLU B C   1 
ATOM   5713 O  O   . GLU B 1 252 ? 19.768  -18.631 54.876  1.00 37.37  ? 252 GLU B O   1 
ATOM   5714 C  CB  . GLU B 1 252 ? 22.845  -19.848 54.583  1.00 43.72  ? 252 GLU B CB  1 
ATOM   5715 C  CG  . GLU B 1 252 ? 21.994  -21.024 55.012  1.00 45.72  ? 252 GLU B CG  1 
ATOM   5716 C  CD  . GLU B 1 252 ? 22.741  -22.059 55.815  1.00 49.93  ? 252 GLU B CD  1 
ATOM   5717 O  OE1 . GLU B 1 252 ? 23.658  -22.702 55.264  1.00 56.93  ? 252 GLU B OE1 1 
ATOM   5718 O  OE2 . GLU B 1 252 ? 22.414  -22.233 57.003  1.00 54.87  ? 252 GLU B OE2 1 
ATOM   5719 N  N   . ASN B 1 253 ? 21.351  -17.451 55.964  1.00 40.38  ? 253 ASN B N   1 
ATOM   5720 C  CA  . ASN B 1 253 ? 20.361  -16.937 56.911  1.00 35.33  ? 253 ASN B CA  1 
ATOM   5721 C  C   . ASN B 1 253 ? 19.369  -16.006 56.218  1.00 38.03  ? 253 ASN B C   1 
ATOM   5722 O  O   . ASN B 1 253 ? 18.171  -16.003 56.548  1.00 34.86  ? 253 ASN B O   1 
ATOM   5723 C  CB  . ASN B 1 253 ? 21.050  -16.217 58.079  1.00 38.37  ? 253 ASN B CB  1 
ATOM   5724 C  CG  . ASN B 1 253 ? 20.060  -15.807 59.167  1.00 32.63  ? 253 ASN B CG  1 
ATOM   5725 O  OD1 . ASN B 1 253 ? 19.682  -14.646 59.269  1.00 35.18  ? 253 ASN B OD1 1 
ATOM   5726 N  ND2 . ASN B 1 253 ? 19.613  -16.771 59.950  1.00 34.72  ? 253 ASN B ND2 1 
ATOM   5727 N  N   . ILE B 1 254 ? 19.847  -15.206 55.255  1.00 37.19  ? 254 ILE B N   1 
ATOM   5728 C  CA  . ILE B 1 254 ? 18.956  -14.339 54.490  1.00 37.11  ? 254 ILE B CA  1 
ATOM   5729 C  C   . ILE B 1 254 ? 17.845  -15.166 53.854  1.00 36.89  ? 254 ILE B C   1 
ATOM   5730 O  O   . ILE B 1 254 ? 16.675  -14.767 53.837  1.00 39.08  ? 254 ILE B O   1 
ATOM   5731 C  CB  . ILE B 1 254 ? 19.741  -13.569 53.413  1.00 38.71  ? 254 ILE B CB  1 
ATOM   5732 C  CG1 . ILE B 1 254 ? 20.731  -12.594 54.052  1.00 38.75  ? 254 ILE B CG1 1 
ATOM   5733 C  CG2 . ILE B 1 254 ? 18.754  -12.798 52.539  1.00 37.64  ? 254 ILE B CG2 1 
ATOM   5734 C  CD1 . ILE B 1 254 ? 21.092  -11.421 53.177  1.00 47.38  ? 254 ILE B CD1 1 
ATOM   5735 N  N   . ARG B 1 255 ? 18.209  -16.320 53.295  1.00 37.08  ? 255 ARG B N   1 
ATOM   5736 C  CA  . ARG B 1 255 ? 17.214  -17.212 52.710  1.00 43.23  ? 255 ARG B CA  1 
ATOM   5737 C  C   . ARG B 1 255 ? 16.225  -17.717 53.759  1.00 38.93  ? 255 ARG B C   1 
ATOM   5738 O  O   . ARG B 1 255 ? 15.014  -17.750 53.520  1.00 36.72  ? 255 ARG B O   1 
ATOM   5739 C  CB  . ARG B 1 255 ? 17.941  -18.356 52.015  1.00 41.12  ? 255 ARG B CB  1 
ATOM   5740 C  CG  . ARG B 1 255 ? 17.210  -19.682 51.885  1.00 40.72  ? 255 ARG B CG  1 
ATOM   5741 C  CD  . ARG B 1 255 ? 18.328  -20.602 51.499  1.00 50.32  ? 255 ARG B CD  1 
ATOM   5742 N  NE  . ARG B 1 255 ? 18.372  -21.805 52.301  1.00 49.02  ? 255 ARG B NE  1 
ATOM   5743 C  CZ  . ARG B 1 255 ? 19.304  -22.734 52.175  1.00 51.45  ? 255 ARG B CZ  1 
ATOM   5744 N  NH1 . ARG B 1 255 ? 20.219  -22.670 51.217  1.00 47.58  ? 255 ARG B NH1 1 
ATOM   5745 N  NH2 . ARG B 1 255 ? 19.340  -23.732 53.052  1.00 51.01  ? 255 ARG B NH2 1 
ATOM   5746 N  N   . TYR B 1 256 ? 16.719  -18.084 54.937  1.00 39.04  ? 256 TYR B N   1 
ATOM   5747 C  CA  . TYR B 1 256 ? 15.816  -18.487 56.008  1.00 37.69  ? 256 TYR B CA  1 
ATOM   5748 C  C   . TYR B 1 256 ? 14.896  -17.347 56.431  1.00 35.87  ? 256 TYR B C   1 
ATOM   5749 O  O   . TYR B 1 256 ? 13.717  -17.578 56.748  1.00 32.52  ? 256 TYR B O   1 
ATOM   5750 C  CB  . TYR B 1 256 ? 16.625  -19.020 57.186  1.00 39.54  ? 256 TYR B CB  1 
ATOM   5751 C  CG  . TYR B 1 256 ? 17.166  -20.396 56.907  1.00 41.53  ? 256 TYR B CG  1 
ATOM   5752 C  CD1 . TYR B 1 256 ? 16.378  -21.335 56.259  1.00 36.22  ? 256 TYR B CD1 1 
ATOM   5753 C  CD2 . TYR B 1 256 ? 18.473  -20.749 57.250  1.00 41.51  ? 256 TYR B CD2 1 
ATOM   5754 C  CE1 . TYR B 1 256 ? 16.851  -22.604 55.984  1.00 44.66  ? 256 TYR B CE1 1 
ATOM   5755 C  CE2 . TYR B 1 256 ? 18.961  -22.029 56.969  1.00 45.52  ? 256 TYR B CE2 1 
ATOM   5756 C  CZ  . TYR B 1 256 ? 18.140  -22.947 56.336  1.00 46.32  ? 256 TYR B CZ  1 
ATOM   5757 O  OH  . TYR B 1 256 ? 18.588  -24.217 56.050  1.00 50.22  ? 256 TYR B OH  1 
ATOM   5758 N  N   . GLN B 1 257 ? 15.403  -16.109 56.456  1.00 31.32  ? 257 GLN B N   1 
ATOM   5759 C  CA  . GLN B 1 257 ? 14.523  -14.998 56.802  1.00 34.68  ? 257 GLN B CA  1 
ATOM   5760 C  C   . GLN B 1 257 ? 13.433  -14.799 55.749  1.00 35.24  ? 257 GLN B C   1 
ATOM   5761 O  O   . GLN B 1 257 ? 12.276  -14.532 56.096  1.00 35.14  ? 257 GLN B O   1 
ATOM   5762 C  CB  . GLN B 1 257 ? 15.307  -13.695 57.007  1.00 34.02  ? 257 GLN B CB  1 
ATOM   5763 C  CG  . GLN B 1 257 ? 16.468  -13.772 58.016  1.00 33.03  ? 257 GLN B CG  1 
ATOM   5764 C  CD  . GLN B 1 257 ? 16.044  -14.140 59.424  1.00 34.96  ? 257 GLN B CD  1 
ATOM   5765 O  OE1 . GLN B 1 257 ? 14.847  -14.234 59.733  1.00 29.52  ? 257 GLN B OE1 1 
ATOM   5766 N  NE2 . GLN B 1 257 ? 17.035  -14.379 60.295  1.00 33.79  ? 257 GLN B NE2 1 
ATOM   5767 N  N   . ILE B 1 258 ? 13.783  -14.896 54.466  1.00 33.79  ? 258 ILE B N   1 
ATOM   5768 C  CA  . ILE B 1 258 ? 12.781  -14.733 53.409  1.00 37.25  ? 258 ILE B CA  1 
ATOM   5769 C  C   . ILE B 1 258 ? 11.692  -15.794 53.540  1.00 32.35  ? 258 ILE B C   1 
ATOM   5770 O  O   . ILE B 1 258 ? 10.491  -15.482 53.544  1.00 37.26  ? 258 ILE B O   1 
ATOM   5771 C  CB  . ILE B 1 258 ? 13.442  -14.774 52.015  1.00 37.75  ? 258 ILE B CB  1 
ATOM   5772 C  CG1 . ILE B 1 258 ? 14.386  -13.583 51.809  1.00 40.55  ? 258 ILE B CG1 1 
ATOM   5773 C  CG2 . ILE B 1 258 ? 12.379  -14.775 50.919  1.00 38.68  ? 258 ILE B CG2 1 
ATOM   5774 C  CD1 . ILE B 1 258 ? 15.421  -13.829 50.740  1.00 41.74  ? 258 ILE B CD1 1 
ATOM   5775 N  N   . ILE B 1 259 ? 12.091  -17.064 53.642  1.00 35.37  ? 259 ILE B N   1 
ATOM   5776 C  CA  . ILE B 1 259 ? 11.117  -18.137 53.871  1.00 35.87  ? 259 ILE B CA  1 
ATOM   5777 C  C   . ILE B 1 259 ? 10.278  -17.822 55.108  1.00 36.36  ? 259 ILE B C   1 
ATOM   5778 O  O   . ILE B 1 259 ? 9.045   -17.981 55.109  1.00 31.85  ? 259 ILE B O   1 
ATOM   5779 C  CB  . ILE B 1 259 ? 11.851  -19.489 54.005  1.00 33.90  ? 259 ILE B CB  1 
ATOM   5780 C  CG1 . ILE B 1 259 ? 12.472  -19.901 52.666  1.00 38.88  ? 259 ILE B CG1 1 
ATOM   5781 C  CG2 . ILE B 1 259 ? 10.932  -20.600 54.510  1.00 31.59  ? 259 ILE B CG2 1 
ATOM   5782 C  CD1 . ILE B 1 259 ? 13.379  -21.123 52.760  1.00 38.43  ? 259 ILE B CD1 1 
ATOM   5783 N  N   . THR B 1 260 ? 10.936  -17.344 56.173  1.00 32.45  ? 260 THR B N   1 
ATOM   5784 C  CA  . THR B 1 260 ? 10.224  -17.034 57.416  1.00 32.55  ? 260 THR B CA  1 
ATOM   5785 C  C   . THR B 1 260 ? 9.175   -15.941 57.212  1.00 33.12  ? 260 THR B C   1 
ATOM   5786 O  O   . THR B 1 260 ? 8.052   -16.046 57.716  1.00 34.60  ? 260 THR B O   1 
ATOM   5787 C  CB  . THR B 1 260 ? 11.225  -16.617 58.495  1.00 31.89  ? 260 THR B CB  1 
ATOM   5788 O  OG1 . THR B 1 260 ? 12.087  -17.719 58.795  1.00 32.94  ? 260 THR B OG1 1 
ATOM   5789 C  CG2 . THR B 1 260 ? 10.508  -16.176 59.760  1.00 32.80  ? 260 THR B CG2 1 
ATOM   5790 N  N   . PHE B 1 261 ? 9.518   -14.876 56.488  1.00 31.60  ? 261 PHE B N   1 
ATOM   5791 C  CA  . PHE B 1 261 ? 8.547   -13.799 56.309  1.00 36.72  ? 261 PHE B CA  1 
ATOM   5792 C  C   . PHE B 1 261 ? 7.371   -14.262 55.461  1.00 38.45  ? 261 PHE B C   1 
ATOM   5793 O  O   . PHE B 1 261 ? 6.218   -13.933 55.761  1.00 41.07  ? 261 PHE B O   1 
ATOM   5794 C  CB  . PHE B 1 261 ? 9.216   -12.572 55.681  1.00 40.98  ? 261 PHE B CB  1 
ATOM   5795 C  CG  . PHE B 1 261 ? 10.224  -11.916 56.583  1.00 36.53  ? 261 PHE B CG  1 
ATOM   5796 C  CD1 . PHE B 1 261 ? 9.931   -11.695 57.918  1.00 39.30  ? 261 PHE B CD1 1 
ATOM   5797 C  CD2 . PHE B 1 261 ? 11.456  -11.539 56.105  1.00 40.32  ? 261 PHE B CD2 1 
ATOM   5798 C  CE1 . PHE B 1 261 ? 10.848  -11.108 58.765  1.00 42.39  ? 261 PHE B CE1 1 
ATOM   5799 C  CE2 . PHE B 1 261 ? 12.390  -10.944 56.956  1.00 37.41  ? 261 PHE B CE2 1 
ATOM   5800 C  CZ  . PHE B 1 261 ? 12.079  -10.740 58.282  1.00 40.52  ? 261 PHE B CZ  1 
ATOM   5801 N  N   . LEU B 1 262 ? 7.638   -15.050 54.418  1.00 38.85  ? 262 LEU B N   1 
ATOM   5802 C  CA  . LEU B 1 262 ? 6.545   -15.528 53.578  1.00 43.23  ? 262 LEU B CA  1 
ATOM   5803 C  C   . LEU B 1 262 ? 5.633   -16.468 54.350  1.00 43.37  ? 262 LEU B C   1 
ATOM   5804 O  O   . LEU B 1 262 ? 4.406   -16.424 54.189  1.00 46.35  ? 262 LEU B O   1 
ATOM   5805 C  CB  . LEU B 1 262 ? 7.089   -16.216 52.325  1.00 36.06  ? 262 LEU B CB  1 
ATOM   5806 C  CG  . LEU B 1 262 ? 7.873   -15.302 51.373  1.00 40.23  ? 262 LEU B CG  1 
ATOM   5807 C  CD1 . LEU B 1 262 ? 8.684   -16.119 50.376  1.00 40.28  ? 262 LEU B CD1 1 
ATOM   5808 C  CD2 . LEU B 1 262 ? 6.963   -14.329 50.644  1.00 43.88  ? 262 LEU B CD2 1 
ATOM   5809 N  N   . ILE B 1 263 ? 6.205   -17.335 55.183  1.00 37.41  ? 263 ILE B N   1 
ATOM   5810 C  CA  . ILE B 1 263 ? 5.357   -18.225 55.973  1.00 38.72  ? 263 ILE B CA  1 
ATOM   5811 C  C   . ILE B 1 263 ? 4.409   -17.399 56.838  1.00 49.97  ? 263 ILE B C   1 
ATOM   5812 O  O   . ILE B 1 263 ? 3.218   -17.714 56.950  1.00 50.31  ? 263 ILE B O   1 
ATOM   5813 C  CB  . ILE B 1 263 ? 6.213   -19.178 56.825  1.00 40.49  ? 263 ILE B CB  1 
ATOM   5814 C  CG1 . ILE B 1 263 ? 6.735   -20.347 55.984  1.00 40.73  ? 263 ILE B CG1 1 
ATOM   5815 C  CG2 . ILE B 1 263 ? 5.386   -19.740 57.952  1.00 42.30  ? 263 ILE B CG2 1 
ATOM   5816 C  CD1 . ILE B 1 263 ? 7.992   -20.975 56.594  1.00 43.93  ? 263 ILE B CD1 1 
ATOM   5817 N  N   . ALA B 1 264 ? 4.918   -16.305 57.434  1.00 46.21  ? 264 ALA B N   1 
ATOM   5818 C  CA  . ALA B 1 264 ? 4.073   -15.404 58.229  1.00 41.31  ? 264 ALA B CA  1 
ATOM   5819 C  C   . ALA B 1 264 ? 3.076   -14.637 57.361  1.00 52.69  ? 264 ALA B C   1 
ATOM   5820 O  O   . ALA B 1 264 ? 1.887   -14.537 57.698  1.00 49.42  ? 264 ALA B O   1 
ATOM   5821 C  CB  . ALA B 1 264 ? 4.942   -14.425 59.008  1.00 40.98  ? 264 ALA B CB  1 
ATOM   5822 N  N   . GLY B 1 265 ? 3.532   -14.082 56.238  1.00 51.84  ? 265 GLY B N   1 
ATOM   5823 C  CA  . GLY B 1 265 ? 2.619   -13.304 55.420  1.00 51.18  ? 265 GLY B CA  1 
ATOM   5824 C  C   . GLY B 1 265 ? 1.434   -14.111 54.924  1.00 51.80  ? 265 GLY B C   1 
ATOM   5825 O  O   . GLY B 1 265 ? 0.359   -13.556 54.669  1.00 51.90  ? 265 GLY B O   1 
ATOM   5826 N  N   . HIS B 1 266 ? 1.601   -15.423 54.791  1.00 49.90  ? 266 HIS B N   1 
ATOM   5827 C  CA  . HIS B 1 266 ? 0.649   -16.213 54.034  1.00 46.12  ? 266 HIS B CA  1 
ATOM   5828 C  C   . HIS B 1 266 ? -0.448  -16.826 54.910  1.00 53.79  ? 266 HIS B C   1 
ATOM   5829 O  O   . HIS B 1 266 ? -1.518  -17.159 54.379  1.00 54.38  ? 266 HIS B O   1 
ATOM   5830 C  CB  . HIS B 1 266 ? 1.407   -17.291 53.245  1.00 49.35  ? 266 HIS B CB  1 
ATOM   5831 C  CG  . HIS B 1 266 ? 0.570   -18.464 52.837  1.00 53.00  ? 266 HIS B CG  1 
ATOM   5832 N  ND1 . HIS B 1 266 ? 0.154   -19.436 53.723  1.00 54.86  ? 266 HIS B ND1 1 
ATOM   5833 C  CD2 . HIS B 1 266 ? 0.093   -18.832 51.622  1.00 55.41  ? 266 HIS B CD2 1 
ATOM   5834 C  CE1 . HIS B 1 266 ? -0.564  -20.339 53.075  1.00 57.17  ? 266 HIS B CE1 1 
ATOM   5835 N  NE2 . HIS B 1 266 ? -0.612  -19.997 51.798  1.00 60.70  ? 266 HIS B NE2 1 
ATOM   5836 N  N   . GLU B 1 267 ? -0.253  -16.938 56.241  1.00 46.82  ? 267 GLU B N   1 
ATOM   5837 C  CA  . GLU B 1 267 ? -1.267  -17.586 57.076  1.00 46.71  ? 267 GLU B CA  1 
ATOM   5838 C  C   . GLU B 1 267 ? -1.790  -16.743 58.230  1.00 43.12  ? 267 GLU B C   1 
ATOM   5839 O  O   . GLU B 1 267 ? -2.984  -16.825 58.544  1.00 49.05  ? 267 GLU B O   1 
ATOM   5840 C  CB  . GLU B 1 267 ? -0.739  -18.909 57.646  1.00 53.16  ? 267 GLU B CB  1 
ATOM   5841 C  CG  . GLU B 1 267 ? -0.310  -19.930 56.583  1.00 62.36  ? 267 GLU B CG  1 
ATOM   5842 C  CD  . GLU B 1 267 ? -0.049  -21.296 57.182  1.00 59.60  ? 267 GLU B CD  1 
ATOM   5843 O  OE1 . GLU B 1 267 ? 0.543   -21.349 58.284  1.00 61.07  ? 267 GLU B OE1 1 
ATOM   5844 O  OE2 . GLU B 1 267 ? -0.450  -22.309 56.571  1.00 65.64  ? 267 GLU B OE2 1 
ATOM   5845 N  N   . THR B 1 268 ? -0.951  -15.932 58.865  1.00 40.24  ? 268 THR B N   1 
ATOM   5846 C  CA  . THR B 1 268 ? -1.383  -15.205 60.054  1.00 37.81  ? 268 THR B CA  1 
ATOM   5847 C  C   . THR B 1 268 ? -2.357  -14.088 59.701  1.00 39.05  ? 268 THR B C   1 
ATOM   5848 O  O   . THR B 1 268 ? -3.469  -14.020 60.242  1.00 37.64  ? 268 THR B O   1 
ATOM   5849 C  CB  . THR B 1 268 ? -0.157  -14.649 60.783  1.00 36.26  ? 268 THR B CB  1 
ATOM   5850 O  OG1 . THR B 1 268 ? 0.527   -13.757 59.902  1.00 34.67  ? 268 THR B OG1 1 
ATOM   5851 C  CG2 . THR B 1 268 ? 0.767   -15.768 61.193  1.00 39.94  ? 268 THR B CG2 1 
ATOM   5852 N  N   . THR B 1 269 ? -1.951  -13.192 58.801  1.00 32.55  ? 269 THR B N   1 
ATOM   5853 C  CA  . THR B 1 269 ? -2.766  -12.018 58.515  1.00 33.17  ? 269 THR B CA  1 
ATOM   5854 C  C   . THR B 1 269 ? -3.989  -12.370 57.689  1.00 34.99  ? 269 THR B C   1 
ATOM   5855 O  O   . THR B 1 269 ? -5.059  -11.770 57.862  1.00 30.89  ? 269 THR B O   1 
ATOM   5856 C  CB  . THR B 1 269 ? -1.923  -10.972 57.794  1.00 35.17  ? 269 THR B CB  1 
ATOM   5857 O  OG1 . THR B 1 269 ? -0.719  -10.778 58.538  1.00 35.67  ? 269 THR B OG1 1 
ATOM   5858 C  CG2 . THR B 1 269 ? -2.679  -9.659  57.664  1.00 33.33  ? 269 THR B CG2 1 
ATOM   5859 N  N   A SER B 1 270 ? -3.852  -13.319 56.762  0.27 30.90  ? 270 SER B N   1 
ATOM   5860 N  N   B SER B 1 270 ? -3.847  -13.324 56.768  0.73 30.93  ? 270 SER B N   1 
ATOM   5861 C  CA  A SER B 1 270 ? -5.014  -13.726 55.980  0.27 31.67  ? 270 SER B CA  1 
ATOM   5862 C  CA  B SER B 1 270 ? -5.000  -13.741 55.976  0.73 31.66  ? 270 SER B CA  1 
ATOM   5863 C  C   A SER B 1 270 ? -6.092  -14.313 56.877  0.27 31.73  ? 270 SER B C   1 
ATOM   5864 C  C   B SER B 1 270 ? -6.086  -14.319 56.869  0.73 31.77  ? 270 SER B C   1 
ATOM   5865 O  O   A SER B 1 270 ? -7.290  -14.107 56.641  0.27 31.30  ? 270 SER B O   1 
ATOM   5866 O  O   B SER B 1 270 ? -7.282  -14.105 56.626  0.73 31.32  ? 270 SER B O   1 
ATOM   5867 C  CB  A SER B 1 270 ? -4.607  -14.734 54.910  0.27 32.38  ? 270 SER B CB  1 
ATOM   5868 C  CB  B SER B 1 270 ? -4.570  -14.764 54.926  0.73 32.37  ? 270 SER B CB  1 
ATOM   5869 O  OG  A SER B 1 270 ? -5.723  -15.525 54.550  0.27 30.53  ? 270 SER B OG  1 
ATOM   5870 O  OG  B SER B 1 270 ? -4.096  -15.945 55.543  0.73 32.50  ? 270 SER B OG  1 
ATOM   5871 N  N   . GLY B 1 271 ? -5.687  -15.055 57.908  1.00 29.03  ? 271 GLY B N   1 
ATOM   5872 C  CA  . GLY B 1 271 ? -6.660  -15.576 58.855  1.00 31.44  ? 271 GLY B CA  1 
ATOM   5873 C  C   . GLY B 1 271 ? -7.361  -14.474 59.629  1.00 30.79  ? 271 GLY B C   1 
ATOM   5874 O  O   . GLY B 1 271 ? -8.577  -14.522 59.837  1.00 32.14  ? 271 GLY B O   1 
ATOM   5875 N  N   . LEU B 1 272 ? -6.599  -13.479 60.086  1.00 31.80  ? 272 LEU B N   1 
ATOM   5876 C  CA  . LEU B 1 272 ? -7.193  -12.335 60.775  1.00 33.73  ? 272 LEU B CA  1 
ATOM   5877 C  C   . LEU B 1 272 ? -8.259  -11.662 59.914  1.00 32.43  ? 272 LEU B C   1 
ATOM   5878 O  O   . LEU B 1 272 ? -9.385  -11.404 60.369  1.00 29.05  ? 272 LEU B O   1 
ATOM   5879 C  CB  . LEU B 1 272 ? -6.099  -11.336 61.153  1.00 30.75  ? 272 LEU B CB  1 
ATOM   5880 C  CG  . LEU B 1 272 ? -6.584  -9.959  61.607  1.00 30.20  ? 272 LEU B CG  1 
ATOM   5881 C  CD1 . LEU B 1 272 ? -7.594  -10.113 62.767  1.00 29.79  ? 272 LEU B CD1 1 
ATOM   5882 C  CD2 . LEU B 1 272 ? -5.402  -9.070  62.020  1.00 30.07  ? 272 LEU B CD2 1 
ATOM   5883 N  N   . LEU B 1 273 ? -7.924  -11.358 58.663  1.00 27.82  ? 273 LEU B N   1 
ATOM   5884 C  CA  . LEU B 1 273 ? -8.897  -10.675 57.819  1.00 28.53  ? 273 LEU B CA  1 
ATOM   5885 C  C   . LEU B 1 273 ? -10.134 -11.535 57.635  1.00 28.86  ? 273 LEU B C   1 
ATOM   5886 O  O   . LEU B 1 273 ? -11.267 -11.032 57.637  1.00 30.23  ? 273 LEU B O   1 
ATOM   5887 C  CB  . LEU B 1 273 ? -8.266  -10.329 56.470  1.00 30.29  ? 273 LEU B CB  1 
ATOM   5888 C  CG  . LEU B 1 273 ? -7.356  -9.086  56.506  1.00 29.68  ? 273 LEU B CG  1 
ATOM   5889 C  CD1 . LEU B 1 273 ? -6.397  -9.056  55.306  1.00 29.83  ? 273 LEU B CD1 1 
ATOM   5890 C  CD2 . LEU B 1 273 ? -8.223  -7.846  56.506  1.00 32.46  ? 273 LEU B CD2 1 
ATOM   5891 N  N   . SER B 1 274 ? -9.936  -12.841 57.470  1.00 26.77  ? 274 SER B N   1 
ATOM   5892 C  CA  . SER B 1 274 ? -11.071 -13.732 57.265  1.00 29.77  ? 274 SER B CA  1 
ATOM   5893 C  C   . SER B 1 274 ? -11.949 -13.794 58.508  1.00 30.97  ? 274 SER B C   1 
ATOM   5894 O  O   . SER B 1 274 ? -13.180 -13.715 58.402  1.00 31.61  ? 274 SER B O   1 
ATOM   5895 C  CB  . SER B 1 274 ? -10.579 -15.127 56.885  1.00 29.17  ? 274 SER B CB  1 
ATOM   5896 O  OG  . SER B 1 274 ? -9.742  -15.081 55.744  1.00 30.29  ? 274 SER B OG  1 
ATOM   5897 N  N   . PHE B 1 275 ? -11.340 -13.948 59.695  1.00 28.83  ? 275 PHE B N   1 
ATOM   5898 C  CA  . PHE B 1 275 ? -12.126 -13.953 60.936  1.00 32.02  ? 275 PHE B CA  1 
ATOM   5899 C  C   . PHE B 1 275 ? -12.835 -12.613 61.141  1.00 32.13  ? 275 PHE B C   1 
ATOM   5900 O  O   . PHE B 1 275 ? -14.002 -12.561 61.569  1.00 30.20  ? 275 PHE B O   1 
ATOM   5901 C  CB  . PHE B 1 275 ? -11.198 -14.257 62.127  1.00 31.22  ? 275 PHE B CB  1 
ATOM   5902 C  CG  . PHE B 1 275 ? -10.995 -15.741 62.396  1.00 32.59  ? 275 PHE B CG  1 
ATOM   5903 C  CD1 . PHE B 1 275 ? -12.071 -16.592 62.598  1.00 32.04  ? 275 PHE B CD1 1 
ATOM   5904 C  CD2 . PHE B 1 275 ? -9.712  -16.290 62.343  1.00 30.44  ? 275 PHE B CD2 1 
ATOM   5905 C  CE1 . PHE B 1 275 ? -11.873 -17.959 62.843  1.00 31.13  ? 275 PHE B CE1 1 
ATOM   5906 C  CE2 . PHE B 1 275 ? -9.493  -17.648 62.567  1.00 30.61  ? 275 PHE B CE2 1 
ATOM   5907 C  CZ  . PHE B 1 275 ? -10.564 -18.491 62.810  1.00 31.88  ? 275 PHE B CZ  1 
ATOM   5908 N  N   . ALA B 1 276 ? -12.133 -11.513 60.859  1.00 29.60  ? 276 ALA B N   1 
ATOM   5909 C  CA  . ALA B 1 276 ? -12.729 -10.184 60.976  1.00 28.88  ? 276 ALA B CA  1 
ATOM   5910 C  C   . ALA B 1 276 ? -13.991 -10.060 60.122  1.00 33.03  ? 276 ALA B C   1 
ATOM   5911 O  O   . ALA B 1 276 ? -15.043 -9.612  60.601  1.00 31.18  ? 276 ALA B O   1 
ATOM   5912 C  CB  . ALA B 1 276 ? -11.701 -9.130  60.571  1.00 28.87  ? 276 ALA B CB  1 
ATOM   5913 N  N   . LEU B 1 277 ? -13.907 -10.447 58.845  1.00 30.92  ? 277 LEU B N   1 
ATOM   5914 C  CA  . LEU B 1 277 ? -15.095 -10.343 57.992  1.00 31.87  ? 277 LEU B CA  1 
ATOM   5915 C  C   . LEU B 1 277 ? -16.199 -11.295 58.460  1.00 30.50  ? 277 LEU B C   1 
ATOM   5916 O  O   . LEU B 1 277 ? -17.382 -10.938 58.442  1.00 32.31  ? 277 LEU B O   1 
ATOM   5917 C  CB  . LEU B 1 277 ? -14.722 -10.612 56.534  1.00 28.14  ? 277 LEU B CB  1 
ATOM   5918 C  CG  . LEU B 1 277 ? -15.866 -10.364 55.525  1.00 33.90  ? 277 LEU B CG  1 
ATOM   5919 C  CD1 . LEU B 1 277 ? -16.222 -8.878  55.485  1.00 31.03  ? 277 LEU B CD1 1 
ATOM   5920 C  CD2 . LEU B 1 277 ? -15.477 -10.858 54.128  1.00 31.36  ? 277 LEU B CD2 1 
ATOM   5921 N  N   . TYR B 1 278 ? -15.838 -12.511 58.878  1.00 30.16  ? 278 TYR B N   1 
ATOM   5922 C  CA  . TYR B 1 278 ? -16.832 -13.406 59.465  1.00 30.82  ? 278 TYR B CA  1 
ATOM   5923 C  C   . TYR B 1 278 ? -17.574 -12.724 60.617  1.00 32.91  ? 278 TYR B C   1 
ATOM   5924 O  O   . TYR B 1 278 ? -18.812 -12.692 60.650  1.00 32.08  ? 278 TYR B O   1 
ATOM   5925 C  CB  . TYR B 1 278 ? -16.170 -14.698 59.944  1.00 28.90  ? 278 TYR B CB  1 
ATOM   5926 C  CG  . TYR B 1 278 ? -17.059 -15.477 60.889  1.00 32.62  ? 278 TYR B CG  1 
ATOM   5927 C  CD1 . TYR B 1 278 ? -17.979 -16.395 60.404  1.00 34.76  ? 278 TYR B CD1 1 
ATOM   5928 C  CD2 . TYR B 1 278 ? -16.976 -15.290 62.268  1.00 32.33  ? 278 TYR B CD2 1 
ATOM   5929 C  CE1 . TYR B 1 278 ? -18.811 -17.107 61.275  1.00 31.35  ? 278 TYR B CE1 1 
ATOM   5930 C  CE2 . TYR B 1 278 ? -17.800 -15.982 63.134  1.00 36.41  ? 278 TYR B CE2 1 
ATOM   5931 C  CZ  . TYR B 1 278 ? -18.712 -16.887 62.627  1.00 32.64  ? 278 TYR B CZ  1 
ATOM   5932 O  OH  . TYR B 1 278 ? -19.520 -17.571 63.498  1.00 35.67  ? 278 TYR B OH  1 
ATOM   5933 N  N   . PHE B 1 279 ? -16.836 -12.171 61.587  1.00 28.83  ? 279 PHE B N   1 
ATOM   5934 C  CA  . PHE B 1 279 ? -17.524 -11.537 62.714  1.00 28.95  ? 279 PHE B CA  1 
ATOM   5935 C  C   . PHE B 1 279 ? -18.346 -10.325 62.278  1.00 29.95  ? 279 PHE B C   1 
ATOM   5936 O  O   . PHE B 1 279 ? -19.419 -10.074 62.835  1.00 31.35  ? 279 PHE B O   1 
ATOM   5937 C  CB  . PHE B 1 279 ? -16.525 -11.142 63.803  1.00 29.73  ? 279 PHE B CB  1 
ATOM   5938 C  CG  . PHE B 1 279 ? -16.083 -12.304 64.652  1.00 32.74  ? 279 PHE B CG  1 
ATOM   5939 C  CD1 . PHE B 1 279 ? -17.011 -13.027 65.402  1.00 30.21  ? 279 PHE B CD1 1 
ATOM   5940 C  CD2 . PHE B 1 279 ? -14.749 -12.688 64.692  1.00 31.41  ? 279 PHE B CD2 1 
ATOM   5941 C  CE1 . PHE B 1 279 ? -16.613 -14.095 66.184  1.00 32.13  ? 279 PHE B CE1 1 
ATOM   5942 C  CE2 . PHE B 1 279 ? -14.346 -13.754 65.470  1.00 33.55  ? 279 PHE B CE2 1 
ATOM   5943 C  CZ  . PHE B 1 279 ? -15.283 -14.464 66.226  1.00 36.57  ? 279 PHE B CZ  1 
ATOM   5944 N  N   . LEU B 1 280 ? -17.874 -9.572  61.287  1.00 26.92  ? 280 LEU B N   1 
ATOM   5945 C  CA  . LEU B 1 280 ? -18.632 -8.415  60.827  1.00 31.61  ? 280 LEU B CA  1 
ATOM   5946 C  C   . LEU B 1 280 ? -19.972 -8.830  60.219  1.00 30.24  ? 280 LEU B C   1 
ATOM   5947 O  O   . LEU B 1 280 ? -21.007 -8.235  60.542  1.00 36.55  ? 280 LEU B O   1 
ATOM   5948 C  CB  . LEU B 1 280 ? -17.812 -7.598  59.821  1.00 30.69  ? 280 LEU B CB  1 
ATOM   5949 C  CG  . LEU B 1 280 ? -16.656 -6.805  60.449  1.00 31.68  ? 280 LEU B CG  1 
ATOM   5950 C  CD1 . LEU B 1 280 ? -15.809 -6.146  59.385  1.00 34.09  ? 280 LEU B CD1 1 
ATOM   5951 C  CD2 . LEU B 1 280 ? -17.190 -5.767  61.420  1.00 35.57  ? 280 LEU B CD2 1 
ATOM   5952 N  N   . VAL B 1 281 ? -19.988 -9.854  59.357  1.00 30.23  ? 281 VAL B N   1 
ATOM   5953 C  CA  . VAL B 1 281 ? -21.278 -10.228 58.776  1.00 32.45  ? 281 VAL B CA  1 
ATOM   5954 C  C   . VAL B 1 281 ? -22.174 -10.916 59.797  1.00 31.38  ? 281 VAL B C   1 
ATOM   5955 O  O   . VAL B 1 281 ? -23.402 -10.892 59.643  1.00 34.88  ? 281 VAL B O   1 
ATOM   5956 C  CB  . VAL B 1 281 ? -21.124 -11.090 57.502  1.00 32.98  ? 281 VAL B CB  1 
ATOM   5957 C  CG1 . VAL B 1 281 ? -20.256 -10.366 56.504  1.00 35.11  ? 281 VAL B CG1 1 
ATOM   5958 C  CG2 . VAL B 1 281 ? -20.596 -12.528 57.820  1.00 31.66  ? 281 VAL B CG2 1 
ATOM   5959 N  N   . LYS B 1 282 ? -21.608 -11.501 60.854  1.00 29.16  ? 282 LYS B N   1 
ATOM   5960 C  CA  . LYS B 1 282 ? -22.440 -12.073 61.910  1.00 33.48  ? 282 LYS B CA  1 
ATOM   5961 C  C   . LYS B 1 282 ? -22.933 -11.023 62.906  1.00 34.37  ? 282 LYS B C   1 
ATOM   5962 O  O   . LYS B 1 282 ? -23.791 -11.330 63.759  1.00 33.11  ? 282 LYS B O   1 
ATOM   5963 C  CB  . LYS B 1 282 ? -21.657 -13.166 62.652  1.00 31.60  ? 282 LYS B CB  1 
ATOM   5964 C  CG  . LYS B 1 282 ? -21.316 -14.388 61.786  1.00 33.52  ? 282 LYS B CG  1 
ATOM   5965 C  CD  . LYS B 1 282 ? -22.554 -15.064 61.156  1.00 30.87  ? 282 LYS B CD  1 
ATOM   5966 C  CE  . LYS B 1 282 ? -22.240 -16.520 60.786  1.00 33.27  ? 282 LYS B CE  1 
ATOM   5967 N  NZ  . LYS B 1 282 ? -23.359 -17.178 60.017  1.00 33.96  ? 282 LYS B NZ  1 
ATOM   5968 N  N   . ASN B 1 283 ? -22.419 -9.799  62.830  1.00 30.08  ? 283 ASN B N   1 
ATOM   5969 C  CA  . ASN B 1 283 ? -22.732 -8.747  63.806  1.00 29.11  ? 283 ASN B CA  1 
ATOM   5970 C  C   . ASN B 1 283 ? -22.984 -7.447  63.060  1.00 30.17  ? 283 ASN B C   1 
ATOM   5971 O  O   . ASN B 1 283 ? -22.140 -6.545  63.039  1.00 31.54  ? 283 ASN B O   1 
ATOM   5972 C  CB  . ASN B 1 283 ? -21.601 -8.598  64.836  1.00 30.88  ? 283 ASN B CB  1 
ATOM   5973 C  CG  . ASN B 1 283 ? -21.474 -9.816  65.745  1.00 36.69  ? 283 ASN B CG  1 
ATOM   5974 O  OD1 . ASN B 1 283 ? -22.169 -9.921  66.763  1.00 35.86  ? 283 ASN B OD1 1 
ATOM   5975 N  ND2 . ASN B 1 283 ? -20.570 -10.741 65.394  1.00 32.01  ? 283 ASN B ND2 1 
ATOM   5976 N  N   . PRO B 1 284 ? -24.175 -7.298  62.467  1.00 32.82  ? 284 PRO B N   1 
ATOM   5977 C  CA  . PRO B 1 284 ? -24.432 -6.155  61.567  1.00 32.80  ? 284 PRO B CA  1 
ATOM   5978 C  C   . PRO B 1 284 ? -24.296 -4.788  62.211  1.00 32.15  ? 284 PRO B C   1 
ATOM   5979 O  O   . PRO B 1 284 ? -23.928 -3.833  61.516  1.00 33.07  ? 284 PRO B O   1 
ATOM   5980 C  CB  . PRO B 1 284 ? -25.882 -6.388  61.103  1.00 38.37  ? 284 PRO B CB  1 
ATOM   5981 C  CG  . PRO B 1 284 ? -26.173 -7.812  61.378  1.00 36.07  ? 284 PRO B CG  1 
ATOM   5982 C  CD  . PRO B 1 284 ? -25.293 -8.260  62.504  1.00 35.12  ? 284 PRO B CD  1 
ATOM   5983 N  N   . HIS B 1 285 ? -24.650 -4.638  63.494  1.00 30.93  ? 285 HIS B N   1 
ATOM   5984 C  CA  . HIS B 1 285 ? -24.393 -3.372  64.179  1.00 31.53  ? 285 HIS B CA  1 
ATOM   5985 C  C   . HIS B 1 285 ? -22.920 -2.997  64.117  1.00 30.13  ? 285 HIS B C   1 
ATOM   5986 O  O   . HIS B 1 285 ? -22.579 -1.837  63.872  1.00 29.92  ? 285 HIS B O   1 
ATOM   5987 C  CB  . HIS B 1 285 ? -24.870 -3.424  65.631  1.00 31.39  ? 285 HIS B CB  1 
ATOM   5988 C  CG  . HIS B 1 285 ? -26.361 -3.392  65.769  1.00 36.06  ? 285 HIS B CG  1 
ATOM   5989 N  ND1 . HIS B 1 285 ? -27.076 -4.325  66.488  1.00 42.46  ? 285 HIS B ND1 1 
ATOM   5990 C  CD2 . HIS B 1 285 ? -27.266 -2.502  65.299  1.00 29.74  ? 285 HIS B CD2 1 
ATOM   5991 C  CE1 . HIS B 1 285 ? -28.363 -4.021  66.437  1.00 32.69  ? 285 HIS B CE1 1 
ATOM   5992 N  NE2 . HIS B 1 285 ? -28.505 -2.927  65.713  1.00 33.76  ? 285 HIS B NE2 1 
ATOM   5993 N  N   . VAL B 1 286 ? -22.037 -3.957  64.378  1.00 30.87  ? 286 VAL B N   1 
ATOM   5994 C  CA  . VAL B 1 286 ? -20.597 -3.677  64.309  1.00 27.80  ? 286 VAL B CA  1 
ATOM   5995 C  C   . VAL B 1 286 ? -20.176 -3.348  62.881  1.00 30.78  ? 286 VAL B C   1 
ATOM   5996 O  O   . VAL B 1 286 ? -19.354 -2.450  62.642  1.00 31.49  ? 286 VAL B O   1 
ATOM   5997 C  CB  . VAL B 1 286 ? -19.810 -4.869  64.857  1.00 30.94  ? 286 VAL B CB  1 
ATOM   5998 C  CG1 . VAL B 1 286 ? -18.293 -4.606  64.728  1.00 27.53  ? 286 VAL B CG1 1 
ATOM   5999 C  CG2 . VAL B 1 286 ? -20.222 -5.136  66.298  1.00 27.75  ? 286 VAL B CG2 1 
ATOM   6000 N  N   . LEU B 1 287 ? -20.713 -4.078  61.905  1.00 30.09  ? 287 LEU B N   1 
ATOM   6001 C  CA  . LEU B 1 287 ? -20.318 -3.822  60.527  1.00 32.56  ? 287 LEU B CA  1 
ATOM   6002 C  C   . LEU B 1 287 ? -20.696 -2.405  60.122  1.00 33.80  ? 287 LEU B C   1 
ATOM   6003 O  O   . LEU B 1 287 ? -19.931 -1.723  59.437  1.00 31.03  ? 287 LEU B O   1 
ATOM   6004 C  CB  . LEU B 1 287 ? -20.962 -4.864  59.607  1.00 29.03  ? 287 LEU B CB  1 
ATOM   6005 C  CG  . LEU B 1 287 ? -21.009 -4.617  58.103  1.00 38.16  ? 287 LEU B CG  1 
ATOM   6006 C  CD1 . LEU B 1 287 ? -19.649 -4.271  57.614  1.00 41.26  ? 287 LEU B CD1 1 
ATOM   6007 C  CD2 . LEU B 1 287 ? -21.498 -5.887  57.395  1.00 45.23  ? 287 LEU B CD2 1 
ATOM   6008 N  N   . GLN B 1 288 ? -21.877 -1.938  60.553  1.00 32.68  ? 288 GLN B N   1 
ATOM   6009 C  CA  . GLN B 1 288 ? -22.337 -0.593  60.198  1.00 33.09  ? 288 GLN B CA  1 
ATOM   6010 C  C   . GLN B 1 288 ? -21.422 0.466   60.796  1.00 33.99  ? 288 GLN B C   1 
ATOM   6011 O  O   . GLN B 1 288 ? -21.093 1.466   60.141  1.00 31.26  ? 288 GLN B O   1 
ATOM   6012 C  CB  . GLN B 1 288 ? -23.768 -0.385  60.705  1.00 36.74  ? 288 GLN B CB  1 
ATOM   6013 C  CG  . GLN B 1 288 ? -24.247 1.065   60.715  1.00 40.22  ? 288 GLN B CG  1 
ATOM   6014 C  CD  . GLN B 1 288 ? -25.600 1.207   61.389  1.00 50.68  ? 288 GLN B CD  1 
ATOM   6015 O  OE1 . GLN B 1 288 ? -26.641 0.932   60.787  1.00 57.48  ? 288 GLN B OE1 1 
ATOM   6016 N  NE2 . GLN B 1 288 ? -25.593 1.656   62.640  1.00 52.81  ? 288 GLN B NE2 1 
ATOM   6017 N  N   . LYS B 1 289 ? -21.018 0.268   62.057  1.00 30.37  ? 289 LYS B N   1 
ATOM   6018 C  CA  . LYS B 1 289 ? -20.074 1.181   62.686  1.00 31.51  ? 289 LYS B CA  1 
ATOM   6019 C  C   . LYS B 1 289 ? -18.741 1.169   61.954  1.00 31.79  ? 289 LYS B C   1 
ATOM   6020 O  O   . LYS B 1 289 ? -18.129 2.218   61.748  1.00 30.79  ? 289 LYS B O   1 
ATOM   6021 C  CB  . LYS B 1 289 ? -19.870 0.810   64.163  1.00 28.78  ? 289 LYS B CB  1 
ATOM   6022 C  CG  . LYS B 1 289 ? -20.978 1.275   65.086  1.00 43.43  ? 289 LYS B CG  1 
ATOM   6023 C  CD  . LYS B 1 289 ? -20.668 0.920   66.543  1.00 34.94  ? 289 LYS B CD  1 
ATOM   6024 C  CE  . LYS B 1 289 ? -19.597 1.784   67.157  1.00 33.47  ? 289 LYS B CE  1 
ATOM   6025 N  NZ  . LYS B 1 289 ? -19.793 1.836   68.659  1.00 33.88  ? 289 LYS B NZ  1 
ATOM   6026 N  N   . ALA B 1 290 ? -18.261 -0.012  61.572  1.00 31.54  ? 290 ALA B N   1 
ATOM   6027 C  CA  . ALA B 1 290 ? -16.968 -0.052  60.895  1.00 31.28  ? 290 ALA B CA  1 
ATOM   6028 C  C   . ALA B 1 290 ? -17.072 0.545   59.497  1.00 31.11  ? 290 ALA B C   1 
ATOM   6029 O  O   . ALA B 1 290 ? -16.159 1.238   59.037  1.00 30.64  ? 290 ALA B O   1 
ATOM   6030 C  CB  . ALA B 1 290 ? -16.447 -1.488  60.855  1.00 29.68  ? 290 ALA B CB  1 
ATOM   6031 N  N   . ALA B 1 291 ? -18.200 0.322   58.819  1.00 30.12  ? 291 ALA B N   1 
ATOM   6032 C  CA  . ALA B 1 291 ? -18.353 0.850   57.468  1.00 32.03  ? 291 ALA B CA  1 
ATOM   6033 C  C   . ALA B 1 291 ? -18.566 2.367   57.479  1.00 30.36  ? 291 ALA B C   1 
ATOM   6034 O  O   . ALA B 1 291 ? -18.090 3.068   56.581  1.00 30.83  ? 291 ALA B O   1 
ATOM   6035 C  CB  . ALA B 1 291 ? -19.505 0.126   56.759  1.00 32.32  ? 291 ALA B CB  1 
ATOM   6036 N  N   . GLU B 1 292 ? -19.269 2.897   58.489  1.00 32.20  ? 292 GLU B N   1 
ATOM   6037 C  CA  . GLU B 1 292 ? -19.378 4.351   58.638  1.00 33.11  ? 292 GLU B CA  1 
ATOM   6038 C  C   . GLU B 1 292 ? -17.994 4.980   58.678  1.00 32.16  ? 292 GLU B C   1 
ATOM   6039 O  O   . GLU B 1 292 ? -17.718 5.979   58.005  1.00 29.59  ? 292 GLU B O   1 
ATOM   6040 C  CB  . GLU B 1 292 ? -20.143 4.694   59.927  1.00 35.91  ? 292 GLU B CB  1 
ATOM   6041 C  CG  . GLU B 1 292 ? -20.500 6.178   60.087  1.00 36.71  ? 292 GLU B CG  1 
ATOM   6042 C  CD  . GLU B 1 292 ? -19.327 7.078   60.475  1.00 38.55  ? 292 GLU B CD  1 
ATOM   6043 O  OE1 . GLU B 1 292 ? -18.395 6.616   61.189  1.00 33.39  ? 292 GLU B OE1 1 
ATOM   6044 O  OE2 . GLU B 1 292 ? -19.337 8.256   60.034  1.00 39.76  ? 292 GLU B OE2 1 
ATOM   6045 N  N   . GLU B 1 293 ? -17.111 4.397   59.475  1.00 30.59  ? 293 GLU B N   1 
ATOM   6046 C  CA  . GLU B 1 293 ? -15.776 4.963   59.641  1.00 30.64  ? 293 GLU B CA  1 
ATOM   6047 C  C   . GLU B 1 293 ? -14.998 4.906   58.337  1.00 33.20  ? 293 GLU B C   1 
ATOM   6048 O  O   . GLU B 1 293 ? -14.379 5.895   57.925  1.00 30.65  ? 293 GLU B O   1 
ATOM   6049 C  CB  . GLU B 1 293 ? -15.026 4.215   60.735  1.00 29.40  ? 293 GLU B CB  1 
ATOM   6050 C  CG  . GLU B 1 293 ? -13.662 4.846   61.047  1.00 30.91  ? 293 GLU B CG  1 
ATOM   6051 C  CD  . GLU B 1 293 ? -12.948 4.086   62.136  1.00 31.46  ? 293 GLU B CD  1 
ATOM   6052 O  OE1 . GLU B 1 293 ? -12.408 3.014   61.818  1.00 31.31  ? 293 GLU B OE1 1 
ATOM   6053 O  OE2 . GLU B 1 293 ? -12.937 4.543   63.302  1.00 30.73  ? 293 GLU B OE2 1 
ATOM   6054 N  N   . ALA B 1 294 ? -15.012 3.743   57.683  1.00 29.50  ? 294 ALA B N   1 
ATOM   6055 C  CA  . ALA B 1 294 ? -14.270 3.595   56.435  1.00 32.03  ? 294 ALA B CA  1 
ATOM   6056 C  C   . ALA B 1 294 ? -14.747 4.595   55.394  1.00 31.35  ? 294 ALA B C   1 
ATOM   6057 O  O   . ALA B 1 294 ? -13.932 5.251   54.731  1.00 32.69  ? 294 ALA B O   1 
ATOM   6058 C  CB  . ALA B 1 294 ? -14.407 2.163   55.915  1.00 28.95  ? 294 ALA B CB  1 
ATOM   6059 N  N   . ALA B 1 295 ? -16.067 4.746   55.248  1.00 35.30  ? 295 ALA B N   1 
ATOM   6060 C  CA  . ALA B 1 295 ? -16.584 5.689   54.260  1.00 32.94  ? 295 ALA B CA  1 
ATOM   6061 C  C   . ALA B 1 295 ? -16.203 7.126   54.619  1.00 33.13  ? 295 ALA B C   1 
ATOM   6062 O  O   . ALA B 1 295 ? -15.859 7.924   53.739  1.00 38.07  ? 295 ALA B O   1 
ATOM   6063 C  CB  . ALA B 1 295 ? -18.107 5.534   54.131  1.00 32.41  ? 295 ALA B CB  1 
ATOM   6064 N  N   . ARG B 1 296 ? -16.223 7.468   55.911  1.00 31.94  ? 296 ARG B N   1 
ATOM   6065 C  CA  . ARG B 1 296 ? -15.935 8.844   56.323  1.00 32.71  ? 296 ARG B CA  1 
ATOM   6066 C  C   . ARG B 1 296 ? -14.452 9.172   56.206  1.00 34.87  ? 296 ARG B C   1 
ATOM   6067 O  O   . ARG B 1 296 ? -14.083 10.302  55.858  1.00 35.88  ? 296 ARG B O   1 
ATOM   6068 C  CB  . ARG B 1 296 ? -16.378 9.068   57.773  1.00 36.10  ? 296 ARG B CB  1 
ATOM   6069 C  CG  . ARG B 1 296 ? -15.844 10.354  58.369  1.00 33.89  ? 296 ARG B CG  1 
ATOM   6070 C  CD  . ARG B 1 296 ? -16.634 10.718  59.624  1.00 37.32  ? 296 ARG B CD  1 
ATOM   6071 N  NE  . ARG B 1 296 ? -16.804 9.562   60.496  1.00 39.38  ? 296 ARG B NE  1 
ATOM   6072 C  CZ  . ARG B 1 296 ? -15.974 9.248   61.483  1.00 38.49  ? 296 ARG B CZ  1 
ATOM   6073 N  NH1 . ARG B 1 296 ? -14.900 9.980   61.741  1.00 39.28  ? 296 ARG B NH1 1 
ATOM   6074 N  NH2 . ARG B 1 296 ? -16.226 8.174   62.224  1.00 33.97  ? 296 ARG B NH2 1 
ATOM   6075 N  N   . VAL B 1 297 ? -13.586 8.218   56.532  1.00 33.16  ? 297 VAL B N   1 
ATOM   6076 C  CA  . VAL B 1 297 ? -12.152 8.512   56.598  1.00 31.42  ? 297 VAL B CA  1 
ATOM   6077 C  C   . VAL B 1 297 ? -11.469 8.338   55.245  1.00 35.62  ? 297 VAL B C   1 
ATOM   6078 O  O   . VAL B 1 297 ? -10.618 9.149   54.865  1.00 30.99  ? 297 VAL B O   1 
ATOM   6079 C  CB  . VAL B 1 297 ? -11.498 7.625   57.675  1.00 34.35  ? 297 VAL B CB  1 
ATOM   6080 C  CG1 . VAL B 1 297 ? -9.942  7.668   57.558  1.00 33.97  ? 297 VAL B CG1 1 
ATOM   6081 C  CG2 . VAL B 1 297 ? -11.986 8.044   59.059  1.00 35.40  ? 297 VAL B CG2 1 
ATOM   6082 N  N   . LEU B 1 298 ? -11.808 7.292   54.489  1.00 34.07  ? 298 LEU B N   1 
ATOM   6083 C  CA  . LEU B 1 298 ? -11.103 7.004   53.233  1.00 32.79  ? 298 LEU B CA  1 
ATOM   6084 C  C   . LEU B 1 298 ? -11.734 7.799   52.086  1.00 36.27  ? 298 LEU B C   1 
ATOM   6085 O  O   . LEU B 1 298 ? -12.441 7.265   51.229  1.00 34.71  ? 298 LEU B O   1 
ATOM   6086 C  CB  . LEU B 1 298 ? -11.116 5.506   52.958  1.00 30.61  ? 298 LEU B CB  1 
ATOM   6087 C  CG  . LEU B 1 298 ? -10.455 4.650   54.034  1.00 28.98  ? 298 LEU B CG  1 
ATOM   6088 C  CD1 . LEU B 1 298 ? -10.581 3.131   53.727  1.00 27.96  ? 298 LEU B CD1 1 
ATOM   6089 C  CD2 . LEU B 1 298 ? -8.975  5.053   54.210  1.00 31.67  ? 298 LEU B CD2 1 
ATOM   6090 N  N   . VAL B 1 299 ? -11.471 9.115   52.092  1.00 35.97  ? 299 VAL B N   1 
ATOM   6091 C  CA  . VAL B 1 299 ? -12.189 10.016  51.188  1.00 38.33  ? 299 VAL B CA  1 
ATOM   6092 C  C   . VAL B 1 299 ? -11.593 10.058  49.790  1.00 40.94  ? 299 VAL B C   1 
ATOM   6093 O  O   . VAL B 1 299 ? -12.205 10.636  48.888  1.00 40.71  ? 299 VAL B O   1 
ATOM   6094 C  CB  . VAL B 1 299 ? -12.267 11.445  51.768  1.00 41.61  ? 299 VAL B CB  1 
ATOM   6095 C  CG1 . VAL B 1 299 ? -13.177 11.455  52.984  1.00 43.62  ? 299 VAL B CG1 1 
ATOM   6096 C  CG2 . VAL B 1 299 ? -10.880 11.994  52.129  1.00 39.62  ? 299 VAL B CG2 1 
ATOM   6097 N  N   . ASP B 1 300 ? -10.425 9.455   49.582  1.00 38.00  ? 300 ASP B N   1 
ATOM   6098 C  CA  . ASP B 1 300 ? -9.716  9.461   48.319  1.00 39.55  ? 300 ASP B CA  1 
ATOM   6099 C  C   . ASP B 1 300 ? -9.729  8.075   47.687  1.00 38.48  ? 300 ASP B C   1 
ATOM   6100 O  O   . ASP B 1 300 ? -9.793  7.065   48.394  1.00 38.47  ? 300 ASP B O   1 
ATOM   6101 C  CB  . ASP B 1 300 ? -8.264  9.910   48.519  1.00 39.81  ? 300 ASP B CB  1 
ATOM   6102 C  CG  . ASP B 1 300 ? -8.179  11.315  49.064  1.00 43.29  ? 300 ASP B CG  1 
ATOM   6103 O  OD1 . ASP B 1 300 ? -8.872  12.191  48.520  1.00 40.85  ? 300 ASP B OD1 1 
ATOM   6104 O  OD2 . ASP B 1 300 ? -7.458  11.534  50.054  1.00 42.85  ? 300 ASP B OD2 1 
ATOM   6105 N  N   . PRO B 1 301 ? -9.647  7.996   46.359  1.00 40.41  ? 301 PRO B N   1 
ATOM   6106 C  CA  . PRO B 1 301 ? -9.619  6.671   45.710  1.00 40.98  ? 301 PRO B CA  1 
ATOM   6107 C  C   . PRO B 1 301 ? -8.443  5.828   46.156  1.00 41.03  ? 301 PRO B C   1 
ATOM   6108 O  O   . PRO B 1 301 ? -8.573  4.605   46.269  1.00 41.72  ? 301 PRO B O   1 
ATOM   6109 C  CB  . PRO B 1 301 ? -9.539  7.008   44.212  1.00 43.54  ? 301 PRO B CB  1 
ATOM   6110 C  CG  . PRO B 1 301 ? -10.001 8.436   44.096  1.00 45.75  ? 301 PRO B CG  1 
ATOM   6111 C  CD  . PRO B 1 301 ? -9.695  9.111   45.399  1.00 42.61  ? 301 PRO B CD  1 
ATOM   6112 N  N   . VAL B 1 302 ? -7.293  6.457   46.394  1.00 39.46  ? 302 VAL B N   1 
ATOM   6113 C  CA  . VAL B 1 302 ? -6.094  5.798   46.908  1.00 42.73  ? 302 VAL B CA  1 
ATOM   6114 C  C   . VAL B 1 302 ? -5.976  6.146   48.392  1.00 40.82  ? 302 VAL B C   1 
ATOM   6115 O  O   . VAL B 1 302 ? -5.729  7.320   48.721  1.00 41.34  ? 302 VAL B O   1 
ATOM   6116 C  CB  . VAL B 1 302 ? -4.834  6.229   46.137  1.00 40.00  ? 302 VAL B CB  1 
ATOM   6117 C  CG1 . VAL B 1 302 ? -3.626  5.425   46.578  1.00 44.08  ? 302 VAL B CG1 1 
ATOM   6118 C  CG2 . VAL B 1 302 ? -5.042  6.048   44.630  1.00 46.73  ? 302 VAL B CG2 1 
ATOM   6119 N  N   . PRO B 1 303 ? -6.152  5.189   49.306  1.00 40.59  ? 303 PRO B N   1 
ATOM   6120 C  CA  . PRO B 1 303 ? -5.947  5.492   50.727  1.00 38.26  ? 303 PRO B CA  1 
ATOM   6121 C  C   . PRO B 1 303 ? -4.512  5.930   50.983  1.00 38.14  ? 303 PRO B C   1 
ATOM   6122 O  O   . PRO B 1 303 ? -3.565  5.383   50.415  1.00 35.31  ? 303 PRO B O   1 
ATOM   6123 C  CB  . PRO B 1 303 ? -6.262  4.165   51.425  1.00 38.72  ? 303 PRO B CB  1 
ATOM   6124 C  CG  . PRO B 1 303 ? -7.227  3.473   50.487  1.00 33.85  ? 303 PRO B CG  1 
ATOM   6125 C  CD  . PRO B 1 303 ? -6.710  3.839   49.102  1.00 34.62  ? 303 PRO B CD  1 
ATOM   6126 N  N   . SER B 1 304 ? -4.360  6.929   51.848  1.00 38.07  ? 304 SER B N   1 
ATOM   6127 C  CA  . SER B 1 304 ? -3.049  7.373   52.305  1.00 39.94  ? 304 SER B CA  1 
ATOM   6128 C  C   . SER B 1 304 ? -2.694  6.717   53.639  1.00 36.45  ? 304 SER B C   1 
ATOM   6129 O  O   . SER B 1 304 ? -3.560  6.236   54.382  1.00 32.90  ? 304 SER B O   1 
ATOM   6130 C  CB  . SER B 1 304 ? -3.017  8.896   52.470  1.00 36.50  ? 304 SER B CB  1 
ATOM   6131 O  OG  . SER B 1 304 ? -3.776  9.269   53.612  1.00 35.88  ? 304 SER B OG  1 
ATOM   6132 N  N   . TYR B 1 305 ? -1.393  6.726   53.946  1.00 33.34  ? 305 TYR B N   1 
ATOM   6133 C  CA  . TYR B 1 305 ? -0.939  6.196   55.229  1.00 35.39  ? 305 TYR B CA  1 
ATOM   6134 C  C   . TYR B 1 305 ? -1.642  6.906   56.381  1.00 34.26  ? 305 TYR B C   1 
ATOM   6135 O  O   . TYR B 1 305 ? -2.115  6.264   57.329  1.00 38.32  ? 305 TYR B O   1 
ATOM   6136 C  CB  . TYR B 1 305 ? 0.580   6.352   55.335  1.00 36.39  ? 305 TYR B CB  1 
ATOM   6137 C  CG  . TYR B 1 305 ? 1.124   6.099   56.708  1.00 34.72  ? 305 TYR B CG  1 
ATOM   6138 C  CD1 . TYR B 1 305 ? 1.512   4.824   57.090  1.00 35.79  ? 305 TYR B CD1 1 
ATOM   6139 C  CD2 . TYR B 1 305 ? 1.231   7.135   57.640  1.00 40.01  ? 305 TYR B CD2 1 
ATOM   6140 C  CE1 . TYR B 1 305 ? 2.010   4.578   58.360  1.00 40.14  ? 305 TYR B CE1 1 
ATOM   6141 C  CE2 . TYR B 1 305 ? 1.718   6.898   58.925  1.00 35.24  ? 305 TYR B CE2 1 
ATOM   6142 C  CZ  . TYR B 1 305 ? 2.105   5.612   59.275  1.00 41.73  ? 305 TYR B CZ  1 
ATOM   6143 O  OH  . TYR B 1 305 ? 2.591   5.351   60.544  1.00 46.65  ? 305 TYR B OH  1 
ATOM   6144 N  N   . LYS B 1 306 ? -1.701  8.243   56.316  1.00 33.07  ? 306 LYS B N   1 
ATOM   6145 C  CA  . LYS B 1 306 ? -2.378  9.035   57.342  1.00 37.41  ? 306 LYS B CA  1 
ATOM   6146 C  C   . LYS B 1 306 ? -3.817  8.579   57.530  1.00 33.80  ? 306 LYS B C   1 
ATOM   6147 O  O   . LYS B 1 306 ? -4.307  8.482   58.658  1.00 33.21  ? 306 LYS B O   1 
ATOM   6148 C  CB  . LYS B 1 306 ? -2.367  10.523  56.958  1.00 42.19  ? 306 LYS B CB  1 
ATOM   6149 C  CG  . LYS B 1 306 ? -1.425  11.413  57.758  1.00 51.54  ? 306 LYS B CG  1 
ATOM   6150 C  CD  . LYS B 1 306 ? -0.950  12.620  56.928  1.00 59.66  ? 306 LYS B CD  1 
ATOM   6151 C  CE  . LYS B 1 306 ? 0.166   13.391  57.636  1.00 61.47  ? 306 LYS B CE  1 
ATOM   6152 N  NZ  . LYS B 1 306 ? 1.201   13.923  56.700  1.00 68.50  ? 306 LYS B NZ  1 
ATOM   6153 N  N   . GLN B 1 307 ? -4.516  8.320   56.432  1.00 33.63  ? 307 GLN B N   1 
ATOM   6154 C  CA  . GLN B 1 307 ? -5.925  7.944   56.537  1.00 35.74  ? 307 GLN B CA  1 
ATOM   6155 C  C   . GLN B 1 307 ? -6.107  6.570   57.179  1.00 33.42  ? 307 GLN B C   1 
ATOM   6156 O  O   . GLN B 1 307 ? -7.041  6.364   57.969  1.00 34.12  ? 307 GLN B O   1 
ATOM   6157 C  CB  . GLN B 1 307 ? -6.565  7.980   55.155  1.00 33.38  ? 307 GLN B CB  1 
ATOM   6158 C  CG  . GLN B 1 307 ? -6.719  9.385   54.608  1.00 34.36  ? 307 GLN B CG  1 
ATOM   6159 C  CD  . GLN B 1 307 ? -7.070  9.380   53.136  1.00 38.33  ? 307 GLN B CD  1 
ATOM   6160 O  OE1 . GLN B 1 307 ? -6.881  8.372   52.456  1.00 37.53  ? 307 GLN B OE1 1 
ATOM   6161 N  NE2 . GLN B 1 307 ? -7.610  10.496  52.637  1.00 37.51  ? 307 GLN B NE2 1 
ATOM   6162 N  N   . VAL B 1 308 ? -5.246  5.608   56.841  1.00 30.58  ? 308 VAL B N   1 
ATOM   6163 C  CA  . VAL B 1 308 ? -5.322  4.300   57.486  1.00 32.49  ? 308 VAL B CA  1 
ATOM   6164 C  C   . VAL B 1 308 ? -5.147  4.438   59.000  1.00 34.58  ? 308 VAL B C   1 
ATOM   6165 O  O   . VAL B 1 308 ? -5.804  3.740   59.777  1.00 32.59  ? 308 VAL B O   1 
ATOM   6166 C  CB  . VAL B 1 308 ? -4.283  3.344   56.872  1.00 33.18  ? 308 VAL B CB  1 
ATOM   6167 C  CG1 . VAL B 1 308 ? -4.212  2.031   57.650  1.00 32.85  ? 308 VAL B CG1 1 
ATOM   6168 C  CG2 . VAL B 1 308 ? -4.622  3.076   55.388  1.00 33.69  ? 308 VAL B CG2 1 
ATOM   6169 N  N   . LYS B 1 309 ? -4.277  5.350   59.446  1.00 32.39  ? 309 LYS B N   1 
ATOM   6170 C  CA  . LYS B 1 309 ? -4.027  5.451   60.878  1.00 34.96  ? 309 LYS B CA  1 
ATOM   6171 C  C   . LYS B 1 309 ? -5.247  6.015   61.603  1.00 36.69  ? 309 LYS B C   1 
ATOM   6172 O  O   . LYS B 1 309 ? -5.372  5.860   62.825  1.00 32.72  ? 309 LYS B O   1 
ATOM   6173 C  CB  . LYS B 1 309 ? -2.812  6.339   61.150  1.00 37.31  ? 309 LYS B CB  1 
ATOM   6174 C  CG  . LYS B 1 309 ? -1.481  5.699   60.685  1.00 37.42  ? 309 LYS B CG  1 
ATOM   6175 C  CD  . LYS B 1 309 ? -0.943  4.525   61.506  1.00 44.56  ? 309 LYS B CD  1 
ATOM   6176 C  CE  . LYS B 1 309 ? -0.964  3.279   60.569  1.00 48.31  ? 309 LYS B CE  1 
ATOM   6177 N  NZ  . LYS B 1 309 ? -0.507  1.901   61.046  1.00 44.02  ? 309 LYS B NZ  1 
ATOM   6178 N  N   . GLN B 1 310 ? -6.152  6.654   60.865  1.00 31.57  ? 310 GLN B N   1 
ATOM   6179 C  CA  . GLN B 1 310 ? -7.402  7.201   61.385  1.00 32.80  ? 310 GLN B CA  1 
ATOM   6180 C  C   . GLN B 1 310 ? -8.522  6.176   61.529  1.00 31.39  ? 310 GLN B C   1 
ATOM   6181 O  O   . GLN B 1 310 ? -9.582  6.521   62.069  1.00 34.51  ? 310 GLN B O   1 
ATOM   6182 C  CB  . GLN B 1 310 ? -7.877  8.310   60.445  1.00 34.07  ? 310 GLN B CB  1 
ATOM   6183 C  CG  . GLN B 1 310 ? -7.281  9.668   60.716  1.00 37.67  ? 310 GLN B CG  1 
ATOM   6184 C  CD  . GLN B 1 310 ? -7.803  10.692  59.736  1.00 38.85  ? 310 GLN B CD  1 
ATOM   6185 O  OE1 . GLN B 1 310 ? -7.648  10.526  58.527  1.00 39.89  ? 310 GLN B OE1 1 
ATOM   6186 N  NE2 . GLN B 1 310 ? -8.440  11.738  60.241  1.00 40.89  ? 310 GLN B NE2 1 
ATOM   6187 N  N   . LEU B 1 311 ? -8.339  4.940   61.056  1.00 32.66  ? 311 LEU B N   1 
ATOM   6188 C  CA  . LEU B 1 311 ? -9.389  3.906   61.078  1.00 31.94  ? 311 LEU B CA  1 
ATOM   6189 C  C   . LEU B 1 311 ? -9.366  3.190   62.435  1.00 32.46  ? 311 LEU B C   1 
ATOM   6190 O  O   . LEU B 1 311 ? -9.029  2.011   62.563  1.00 31.54  ? 311 LEU B O   1 
ATOM   6191 C  CB  . LEU B 1 311 ? -9.184  2.927   59.919  1.00 31.03  ? 311 LEU B CB  1 
ATOM   6192 C  CG  . LEU B 1 311 ? -9.320  3.491   58.496  1.00 31.63  ? 311 LEU B CG  1 
ATOM   6193 C  CD1 . LEU B 1 311 ? -8.920  2.461   57.462  1.00 28.45  ? 311 LEU B CD1 1 
ATOM   6194 C  CD2 . LEU B 1 311 ? -10.753 3.967   58.234  1.00 29.88  ? 311 LEU B CD2 1 
ATOM   6195 N  N   . LYS B 1 312 ? -9.722  3.953   63.470  1.00 36.85  ? 312 LYS B N   1 
ATOM   6196 C  CA  . LYS B 1 312 ? -9.614  3.469   64.849  1.00 33.08  ? 312 LYS B CA  1 
ATOM   6197 C  C   . LYS B 1 312 ? -10.553 2.300   65.114  1.00 31.87  ? 312 LYS B C   1 
ATOM   6198 O  O   . LYS B 1 312 ? -10.153 1.277   65.688  1.00 30.86  ? 312 LYS B O   1 
ATOM   6199 C  CB  . LYS B 1 312 ? -9.909  4.625   65.810  1.00 35.74  ? 312 LYS B CB  1 
ATOM   6200 C  CG  . LYS B 1 312 ? -9.122  4.588   67.081  1.00 47.58  ? 312 LYS B CG  1 
ATOM   6201 C  CD  . LYS B 1 312 ? -10.028 4.416   68.268  1.00 51.25  ? 312 LYS B CD  1 
ATOM   6202 C  CE  . LYS B 1 312 ? -9.344  4.914   69.543  1.00 46.02  ? 312 LYS B CE  1 
ATOM   6203 N  NZ  . LYS B 1 312 ? -10.070 4.467   70.738  1.00 46.58  ? 312 LYS B NZ  1 
ATOM   6204 N  N   . TYR B 1 313 ? -11.813 2.430   64.700  1.00 32.90  ? 313 TYR B N   1 
ATOM   6205 C  CA  . TYR B 1 313 ? -12.771 1.360   64.964  1.00 32.50  ? 313 TYR B CA  1 
ATOM   6206 C  C   . TYR B 1 313 ? -12.477 0.120   64.120  1.00 30.65  ? 313 TYR B C   1 
ATOM   6207 O  O   . TYR B 1 313 ? -12.635 -1.012  64.593  1.00 30.94  ? 313 TYR B O   1 
ATOM   6208 C  CB  . TYR B 1 313 ? -14.195 1.869   64.729  1.00 28.91  ? 313 TYR B CB  1 
ATOM   6209 C  CG  . TYR B 1 313 ? -15.255 0.927   65.289  1.00 29.84  ? 313 TYR B CG  1 
ATOM   6210 C  CD1 . TYR B 1 313 ? -15.617 0.973   66.635  1.00 33.80  ? 313 TYR B CD1 1 
ATOM   6211 C  CD2 . TYR B 1 313 ? -15.871 -0.022  64.477  1.00 31.43  ? 313 TYR B CD2 1 
ATOM   6212 C  CE1 . TYR B 1 313 ? -16.579 0.102   67.158  1.00 31.34  ? 313 TYR B CE1 1 
ATOM   6213 C  CE2 . TYR B 1 313 ? -16.831 -0.900  64.983  1.00 30.85  ? 313 TYR B CE2 1 
ATOM   6214 C  CZ  . TYR B 1 313 ? -17.182 -0.841  66.322  1.00 32.61  ? 313 TYR B CZ  1 
ATOM   6215 O  OH  . TYR B 1 313 ? -18.150 -1.717  66.815  1.00 30.77  ? 313 TYR B OH  1 
ATOM   6216 N  N   . VAL B 1 314 ? -12.043 0.303   62.869  1.00 30.31  ? 314 VAL B N   1 
ATOM   6217 C  CA  . VAL B 1 314 ? -11.554 -0.835  62.093  1.00 30.44  ? 314 VAL B CA  1 
ATOM   6218 C  C   . VAL B 1 314 ? -10.441 -1.561  62.857  1.00 32.23  ? 314 VAL B C   1 
ATOM   6219 O  O   . VAL B 1 314 ? -10.430 -2.797  62.946  1.00 28.80  ? 314 VAL B O   1 
ATOM   6220 C  CB  . VAL B 1 314 ? -11.102 -0.368  60.690  1.00 31.48  ? 314 VAL B CB  1 
ATOM   6221 C  CG1 . VAL B 1 314 ? -10.469 -1.519  59.917  1.00 30.48  ? 314 VAL B CG1 1 
ATOM   6222 C  CG2 . VAL B 1 314 ? -12.301 0.166   59.892  1.00 28.50  ? 314 VAL B CG2 1 
ATOM   6223 N  N   . GLY B 1 315 ? -9.497  -0.808  63.436  1.00 32.95  ? 315 GLY B N   1 
ATOM   6224 C  CA  . GLY B 1 315 ? -8.448  -1.443  64.233  1.00 32.78  ? 315 GLY B CA  1 
ATOM   6225 C  C   . GLY B 1 315 ? -9.001  -2.191  65.435  1.00 31.60  ? 315 GLY B C   1 
ATOM   6226 O  O   . GLY B 1 315 ? -8.498  -3.254  65.819  1.00 31.20  ? 315 GLY B O   1 
ATOM   6227 N  N   . MET B 1 316 ? -10.040 -1.634  66.050  1.00 28.81  ? 316 MET B N   1 
ATOM   6228 C  CA  . MET B 1 316 ? -10.703 -2.270  67.183  1.00 31.15  ? 316 MET B CA  1 
ATOM   6229 C  C   . MET B 1 316 ? -11.357 -3.586  66.775  1.00 30.51  ? 316 MET B C   1 
ATOM   6230 O  O   . MET B 1 316 ? -11.321 -4.571  67.518  1.00 32.39  ? 316 MET B O   1 
ATOM   6231 C  CB  . MET B 1 316 ? -11.735 -1.273  67.712  1.00 32.15  ? 316 MET B CB  1 
ATOM   6232 C  CG  . MET B 1 316 ? -11.127 -0.192  68.597  1.00 32.92  ? 316 MET B CG  1 
ATOM   6233 S  SD  . MET B 1 316 ? -12.293 1.164   68.850  1.00 34.88  ? 316 MET B SD  1 
ATOM   6234 C  CE  . MET B 1 316 ? -13.614 0.365   69.723  1.00 34.41  ? 316 MET B CE  1 
ATOM   6235 N  N   . VAL B 1 317 ? -12.012 -3.595  65.612  1.00 28.68  ? 317 VAL B N   1 
ATOM   6236 C  CA  . VAL B 1 317 ? -12.547 -4.820  65.026  1.00 31.07  ? 317 VAL B CA  1 
ATOM   6237 C  C   . VAL B 1 317 ? -11.446 -5.859  64.870  1.00 31.03  ? 317 VAL B C   1 
ATOM   6238 O  O   . VAL B 1 317 ? -11.605 -7.027  65.237  1.00 29.54  ? 317 VAL B O   1 
ATOM   6239 C  CB  . VAL B 1 317 ? -13.194 -4.494  63.660  1.00 30.09  ? 317 VAL B CB  1 
ATOM   6240 C  CG1 . VAL B 1 317 ? -13.469 -5.763  62.856  1.00 27.12  ? 317 VAL B CG1 1 
ATOM   6241 C  CG2 . VAL B 1 317 ? -14.471 -3.701  63.868  1.00 29.72  ? 317 VAL B CG2 1 
ATOM   6242 N  N   . LEU B 1 318 ? -10.315 -5.447  64.295  1.00 29.84  ? 318 LEU B N   1 
ATOM   6243 C  CA  . LEU B 1 318 ? -9.218  -6.386  64.093  1.00 28.39  ? 318 LEU B CA  1 
ATOM   6244 C  C   . LEU B 1 318 ? -8.730  -6.948  65.431  1.00 31.44  ? 318 LEU B C   1 
ATOM   6245 O  O   . LEU B 1 318 ? -8.503  -8.156  65.559  1.00 29.26  ? 318 LEU B O   1 
ATOM   6246 C  CB  . LEU B 1 318 ? -8.088  -5.676  63.327  1.00 29.99  ? 318 LEU B CB  1 
ATOM   6247 C  CG  . LEU B 1 318 ? -8.478  -5.392  61.859  1.00 30.20  ? 318 LEU B CG  1 
ATOM   6248 C  CD1 . LEU B 1 318 ? -7.430  -4.532  61.178  1.00 26.98  ? 318 LEU B CD1 1 
ATOM   6249 C  CD2 . LEU B 1 318 ? -8.663  -6.691  61.062  1.00 28.12  ? 318 LEU B CD2 1 
ATOM   6250 N  N   . ASN B 1 319 ? -8.577  -6.088  66.445  1.00 27.48  ? 319 ASN B N   1 
ATOM   6251 C  CA  . ASN B 1 319 ? -8.095  -6.568  67.738  1.00 29.76  ? 319 ASN B CA  1 
ATOM   6252 C  C   . ASN B 1 319 ? -9.101  -7.502  68.394  1.00 30.75  ? 319 ASN B C   1 
ATOM   6253 O  O   . ASN B 1 319 ? -8.717  -8.491  69.031  1.00 27.73  ? 319 ASN B O   1 
ATOM   6254 C  CB  . ASN B 1 319 ? -7.781  -5.385  68.651  1.00 28.53  ? 319 ASN B CB  1 
ATOM   6255 C  CG  . ASN B 1 319 ? -6.443  -4.770  68.331  1.00 35.15  ? 319 ASN B CG  1 
ATOM   6256 O  OD1 . ASN B 1 319 ? -5.503  -5.479  67.968  1.00 34.60  ? 319 ASN B OD1 1 
ATOM   6257 N  ND2 . ASN B 1 319 ? -6.350  -3.452  68.438  1.00 35.81  ? 319 ASN B ND2 1 
ATOM   6258 N  N   . GLU B 1 320 ? -10.395 -7.210  68.249  1.00 28.55  ? 320 GLU B N   1 
ATOM   6259 C  CA  . GLU B 1 320 ? -11.396 -8.102  68.812  1.00 29.03  ? 320 GLU B CA  1 
ATOM   6260 C  C   . GLU B 1 320 ? -11.413 -9.443  68.086  1.00 29.90  ? 320 GLU B C   1 
ATOM   6261 O  O   . GLU B 1 320 ? -11.635 -10.479 68.713  1.00 30.01  ? 320 GLU B O   1 
ATOM   6262 C  CB  . GLU B 1 320 ? -12.776 -7.429  68.772  1.00 33.07  ? 320 GLU B CB  1 
ATOM   6263 C  CG  . GLU B 1 320 ? -13.890 -8.266  69.310  1.00 30.13  ? 320 GLU B CG  1 
ATOM   6264 C  CD  . GLU B 1 320 ? -13.869 -8.418  70.834  1.00 32.39  ? 320 GLU B CD  1 
ATOM   6265 O  OE1 . GLU B 1 320 ? -12.795 -8.219  71.453  1.00 30.69  ? 320 GLU B OE1 1 
ATOM   6266 O  OE2 . GLU B 1 320 ? -14.933 -8.763  71.417  1.00 33.02  ? 320 GLU B OE2 1 
ATOM   6267 N  N   . ALA B 1 321 ? -11.154 -9.454  66.774  1.00 30.92  ? 321 ALA B N   1 
ATOM   6268 C  CA  . ALA B 1 321 ? -11.046 -10.731 66.082  1.00 29.97  ? 321 ALA B CA  1 
ATOM   6269 C  C   . ALA B 1 321 ? -9.802  -11.491 66.520  1.00 29.22  ? 321 ALA B C   1 
ATOM   6270 O  O   . ALA B 1 321 ? -9.843  -12.719 66.632  1.00 28.42  ? 321 ALA B O   1 
ATOM   6271 C  CB  . ALA B 1 321 ? -11.029 -10.533 64.567  1.00 30.32  ? 321 ALA B CB  1 
ATOM   6272 N  N   . LEU B 1 322 ? -8.676  -10.786 66.714  1.00 28.66  ? 322 LEU B N   1 
ATOM   6273 C  CA  . LEU B 1 322 ? -7.495  -11.429 67.293  1.00 30.34  ? 322 LEU B CA  1 
ATOM   6274 C  C   . LEU B 1 322 ? -7.760  -11.917 68.705  1.00 31.82  ? 322 LEU B C   1 
ATOM   6275 O  O   . LEU B 1 322 ? -7.109  -12.871 69.161  1.00 32.12  ? 322 LEU B O   1 
ATOM   6276 C  CB  . LEU B 1 322 ? -6.291  -10.474 67.328  1.00 31.37  ? 322 LEU B CB  1 
ATOM   6277 C  CG  . LEU B 1 322 ? -5.626  -10.168 65.991  1.00 33.86  ? 322 LEU B CG  1 
ATOM   6278 C  CD1 . LEU B 1 322 ? -4.494  -9.159  66.193  1.00 33.79  ? 322 LEU B CD1 1 
ATOM   6279 C  CD2 . LEU B 1 322 ? -5.131  -11.458 65.382  1.00 32.91  ? 322 LEU B CD2 1 
ATOM   6280 N  N   . ARG B 1 323 ? -8.674  -11.270 69.434  1.00 30.21  ? 323 ARG B N   1 
ATOM   6281 C  CA  . ARG B 1 323 ? -8.924  -11.737 70.791  1.00 29.69  ? 323 ARG B CA  1 
ATOM   6282 C  C   . ARG B 1 323 ? -9.622  -13.092 70.759  1.00 31.00  ? 323 ARG B C   1 
ATOM   6283 O  O   . ARG B 1 323 ? -9.183  -14.033 71.414  1.00 27.74  ? 323 ARG B O   1 
ATOM   6284 C  CB  . ARG B 1 323 ? -9.729  -10.705 71.601  1.00 30.88  ? 323 ARG B CB  1 
ATOM   6285 C  CG  . ARG B 1 323 ? -10.177 -11.236 72.977  1.00 30.76  ? 323 ARG B CG  1 
ATOM   6286 C  CD  . ARG B 1 323 ? -11.080 -10.269 73.775  1.00 32.41  ? 323 ARG B CD  1 
ATOM   6287 N  NE  . ARG B 1 323 ? -12.457 -10.317 73.273  1.00 31.34  ? 323 ARG B NE  1 
ATOM   6288 C  CZ  . ARG B 1 323 ? -13.333 -11.278 73.542  1.00 35.94  ? 323 ARG B CZ  1 
ATOM   6289 N  NH1 . ARG B 1 323 ? -13.036 -12.288 74.357  1.00 32.77  ? 323 ARG B NH1 1 
ATOM   6290 N  NH2 . ARG B 1 323 ? -14.524 -11.251 72.945  1.00 30.96  ? 323 ARG B NH2 1 
ATOM   6291 N  N   . LEU B 1 324 ? -10.685 -13.230 69.957  1.00 27.61  ? 324 LEU B N   1 
ATOM   6292 C  CA  . LEU B 1 324 ? -11.428 -14.486 69.954  1.00 31.23  ? 324 LEU B CA  1 
ATOM   6293 C  C   . LEU B 1 324 ? -10.658 -15.599 69.241  1.00 28.91  ? 324 LEU B C   1 
ATOM   6294 O  O   . LEU B 1 324 ? -10.623 -16.745 69.721  1.00 34.35  ? 324 LEU B O   1 
ATOM   6295 C  CB  . LEU B 1 324 ? -12.811 -14.263 69.335  1.00 31.01  ? 324 LEU B CB  1 
ATOM   6296 C  CG  . LEU B 1 324 ? -13.761 -13.548 70.307  1.00 33.39  ? 324 LEU B CG  1 
ATOM   6297 C  CD1 . LEU B 1 324 ? -14.945 -12.953 69.561  1.00 33.23  ? 324 LEU B CD1 1 
ATOM   6298 C  CD2 . LEU B 1 324 ? -14.231 -14.500 71.426  1.00 32.54  ? 324 LEU B CD2 1 
ATOM   6299 N  N   . TRP B 1 325 ? -10.007 -15.286 68.123  1.00 31.29  ? 325 TRP B N   1 
ATOM   6300 C  CA  . TRP B 1 325 ? -9.336  -16.294 67.296  1.00 29.04  ? 325 TRP B CA  1 
ATOM   6301 C  C   . TRP B 1 325 ? -7.943  -15.814 66.913  1.00 30.66  ? 325 TRP B C   1 
ATOM   6302 O  O   . TRP B 1 325 ? -7.665  -15.484 65.753  1.00 30.96  ? 325 TRP B O   1 
ATOM   6303 C  CB  . TRP B 1 325 ? -10.192 -16.636 66.073  1.00 30.87  ? 325 TRP B CB  1 
ATOM   6304 C  CG  . TRP B 1 325 ? -11.384 -17.412 66.531  1.00 31.91  ? 325 TRP B CG  1 
ATOM   6305 C  CD1 . TRP B 1 325 ? -12.696 -17.015 66.494  1.00 36.14  ? 325 TRP B CD1 1 
ATOM   6306 C  CD2 . TRP B 1 325 ? -11.370 -18.692 67.189  1.00 32.47  ? 325 TRP B CD2 1 
ATOM   6307 N  NE1 . TRP B 1 325 ? -13.494 -17.981 67.066  1.00 31.95  ? 325 TRP B NE1 1 
ATOM   6308 C  CE2 . TRP B 1 325 ? -12.709 -19.018 67.499  1.00 32.44  ? 325 TRP B CE2 1 
ATOM   6309 C  CE3 . TRP B 1 325 ? -10.355 -19.606 67.520  1.00 31.52  ? 325 TRP B CE3 1 
ATOM   6310 C  CZ2 . TRP B 1 325 ? -13.060 -20.214 68.121  1.00 32.99  ? 325 TRP B CZ2 1 
ATOM   6311 C  CZ3 . TRP B 1 325 ? -10.708 -20.798 68.141  1.00 36.09  ? 325 TRP B CZ3 1 
ATOM   6312 C  CH2 . TRP B 1 325 ? -12.049 -21.090 68.434  1.00 36.01  ? 325 TRP B CH2 1 
ATOM   6313 N  N   . PRO B 1 326 ? -7.019  -15.789 67.873  1.00 30.48  ? 326 PRO B N   1 
ATOM   6314 C  CA  . PRO B 1 326 ? -5.644  -15.387 67.542  1.00 28.69  ? 326 PRO B CA  1 
ATOM   6315 C  C   . PRO B 1 326 ? -5.046  -16.429 66.607  1.00 32.42  ? 326 PRO B C   1 
ATOM   6316 O  O   . PRO B 1 326 ? -5.005  -17.615 66.928  1.00 28.92  ? 326 PRO B O   1 
ATOM   6317 C  CB  . PRO B 1 326 ? -4.941  -15.340 68.909  1.00 29.80  ? 326 PRO B CB  1 
ATOM   6318 C  CG  . PRO B 1 326 ? -5.791  -16.259 69.819  1.00 31.01  ? 326 PRO B CG  1 
ATOM   6319 C  CD  . PRO B 1 326 ? -7.206  -16.129 69.293  1.00 29.37  ? 326 PRO B CD  1 
ATOM   6320 N  N   . THR B 1 327 ? -4.625  -15.990 65.420  1.00 31.11  ? 327 THR B N   1 
ATOM   6321 C  CA  . THR B 1 327 ? -4.432  -16.950 64.337  1.00 30.69  ? 327 THR B CA  1 
ATOM   6322 C  C   . THR B 1 327 ? -3.138  -17.744 64.453  1.00 31.43  ? 327 THR B C   1 
ATOM   6323 O  O   . THR B 1 327 ? -3.020  -18.792 63.813  1.00 32.48  ? 327 THR B O   1 
ATOM   6324 C  CB  . THR B 1 327 ? -4.502  -16.231 62.984  1.00 34.00  ? 327 THR B CB  1 
ATOM   6325 O  OG1 . THR B 1 327 ? -3.594  -15.129 62.988  1.00 34.68  ? 327 THR B OG1 1 
ATOM   6326 C  CG2 . THR B 1 327 ? -5.909  -15.666 62.789  1.00 33.44  ? 327 THR B CG2 1 
ATOM   6327 N  N   . ALA B 1 328 ? -2.168  -17.286 65.250  1.00 30.31  ? 328 ALA B N   1 
ATOM   6328 C  CA  . ALA B 1 328 ? -1.046  -18.126 65.668  1.00 28.57  ? 328 ALA B CA  1 
ATOM   6329 C  C   . ALA B 1 328 ? -1.329  -18.465 67.129  1.00 31.41  ? 328 ALA B C   1 
ATOM   6330 O  O   . ALA B 1 328 ? -0.952  -17.707 68.030  1.00 33.55  ? 328 ALA B O   1 
ATOM   6331 C  CB  . ALA B 1 328 ? 0.310   -17.417 65.504  1.00 31.05  ? 328 ALA B CB  1 
ATOM   6332 N  N   . PRO B 1 329 ? -2.003  -19.583 67.414  1.00 30.72  ? 329 PRO B N   1 
ATOM   6333 C  CA  . PRO B 1 329 ? -2.800  -19.683 68.646  1.00 29.70  ? 329 PRO B CA  1 
ATOM   6334 C  C   . PRO B 1 329 ? -2.030  -20.063 69.901  1.00 33.10  ? 329 PRO B C   1 
ATOM   6335 O  O   . PRO B 1 329 ? -2.629  -20.107 70.982  1.00 29.37  ? 329 PRO B O   1 
ATOM   6336 C  CB  . PRO B 1 329 ? -3.835  -20.759 68.275  1.00 32.39  ? 329 PRO B CB  1 
ATOM   6337 C  CG  . PRO B 1 329 ? -3.095  -21.657 67.356  1.00 35.10  ? 329 PRO B CG  1 
ATOM   6338 C  CD  . PRO B 1 329 ? -2.268  -20.714 66.499  1.00 32.11  ? 329 PRO B CD  1 
ATOM   6339 N  N   . ALA B 1 330 ? -0.728  -20.318 69.822  1.00 28.37  ? 330 ALA B N   1 
ATOM   6340 C  CA  . ALA B 1 330 ? -0.032  -20.699 71.042  1.00 31.55  ? 330 ALA B CA  1 
ATOM   6341 C  C   . ALA B 1 330 ? 1.431   -20.351 70.857  1.00 33.25  ? 330 ALA B C   1 
ATOM   6342 O  O   . ALA B 1 330 ? 1.906   -20.208 69.725  1.00 32.52  ? 330 ALA B O   1 
ATOM   6343 C  CB  . ALA B 1 330 ? -0.207  -22.195 71.340  1.00 31.82  ? 330 ALA B CB  1 
ATOM   6344 N  N   . PHE B 1 331 ? 2.137   -20.207 71.978  1.00 29.41  ? 331 PHE B N   1 
ATOM   6345 C  CA  . PHE B 1 331 ? 3.598   -20.143 71.948  1.00 30.91  ? 331 PHE B CA  1 
ATOM   6346 C  C   . PHE B 1 331 ? 4.136   -20.868 73.174  1.00 35.67  ? 331 PHE B C   1 
ATOM   6347 O  O   . PHE B 1 331 ? 3.407   -21.114 74.137  1.00 33.00  ? 331 PHE B O   1 
ATOM   6348 C  CB  . PHE B 1 331 ? 4.137   -18.691 71.857  1.00 31.69  ? 331 PHE B CB  1 
ATOM   6349 C  CG  . PHE B 1 331 ? 3.658   -17.733 72.956  1.00 35.57  ? 331 PHE B CG  1 
ATOM   6350 C  CD1 . PHE B 1 331 ? 2.469   -17.022 72.818  1.00 33.29  ? 331 PHE B CD1 1 
ATOM   6351 C  CD2 . PHE B 1 331 ? 4.453   -17.472 74.071  1.00 33.88  ? 331 PHE B CD2 1 
ATOM   6352 C  CE1 . PHE B 1 331 ? 2.046   -16.120 73.779  1.00 32.42  ? 331 PHE B CE1 1 
ATOM   6353 C  CE2 . PHE B 1 331 ? 4.034   -16.571 75.066  1.00 35.34  ? 331 PHE B CE2 1 
ATOM   6354 C  CZ  . PHE B 1 331 ? 2.833   -15.887 74.921  1.00 35.59  ? 331 PHE B CZ  1 
ATOM   6355 N  N   . SER B 1 332 ? 5.423   -21.221 73.121  1.00 33.12  ? 332 SER B N   1 
ATOM   6356 C  CA  . SER B 1 332 ? 6.040   -22.079 74.123  1.00 33.91  ? 332 SER B CA  1 
ATOM   6357 C  C   . SER B 1 332 ? 7.178   -21.354 74.845  1.00 30.67  ? 332 SER B C   1 
ATOM   6358 O  O   . SER B 1 332 ? 7.859   -20.504 74.264  1.00 30.73  ? 332 SER B O   1 
ATOM   6359 C  CB  . SER B 1 332 ? 6.543   -23.385 73.459  1.00 31.52  ? 332 SER B CB  1 
ATOM   6360 O  OG  . SER B 1 332 ? 6.989   -24.310 74.427  1.00 34.57  ? 332 SER B OG  1 
ATOM   6361 N  N   . LEU B 1 333 ? 7.371   -21.708 76.124  1.00 29.87  ? 333 LEU B N   1 
ATOM   6362 C  CA  . LEU B 1 333 ? 8.377   -21.118 76.998  1.00 33.52  ? 333 LEU B CA  1 
ATOM   6363 C  C   . LEU B 1 333 ? 9.073   -22.228 77.781  1.00 32.37  ? 333 LEU B C   1 
ATOM   6364 O  O   . LEU B 1 333 ? 8.502   -23.293 78.010  1.00 33.55  ? 333 LEU B O   1 
ATOM   6365 C  CB  . LEU B 1 333 ? 7.742   -20.125 77.979  1.00 36.46  ? 333 LEU B CB  1 
ATOM   6366 C  CG  . LEU B 1 333 ? 6.923   -19.026 77.283  1.00 35.42  ? 333 LEU B CG  1 
ATOM   6367 C  CD1 . LEU B 1 333 ? 5.889   -18.439 78.227  1.00 37.98  ? 333 LEU B CD1 1 
ATOM   6368 C  CD2 . LEU B 1 333 ? 7.831   -17.946 76.672  1.00 30.51  ? 333 LEU B CD2 1 
ATOM   6369 N  N   . TYR B 1 334 ? 10.308  -21.969 78.223  1.00 34.12  ? 334 TYR B N   1 
ATOM   6370 C  CA  . TYR B 1 334 ? 10.960  -22.866 79.176  1.00 34.55  ? 334 TYR B CA  1 
ATOM   6371 C  C   . TYR B 1 334 ? 11.440  -22.059 80.373  1.00 35.33  ? 334 TYR B C   1 
ATOM   6372 O  O   . TYR B 1 334 ? 11.757  -20.870 80.253  1.00 33.54  ? 334 TYR B O   1 
ATOM   6373 C  CB  . TYR B 1 334 ? 12.144  -23.641 78.566  1.00 31.93  ? 334 TYR B CB  1 
ATOM   6374 C  CG  . TYR B 1 334 ? 13.319  -22.756 78.198  1.00 33.86  ? 334 TYR B CG  1 
ATOM   6375 C  CD1 . TYR B 1 334 ? 13.386  -22.136 76.958  1.00 33.93  ? 334 TYR B CD1 1 
ATOM   6376 C  CD2 . TYR B 1 334 ? 14.362  -22.532 79.102  1.00 36.31  ? 334 TYR B CD2 1 
ATOM   6377 C  CE1 . TYR B 1 334 ? 14.460  -21.316 76.615  1.00 32.12  ? 334 TYR B CE1 1 
ATOM   6378 C  CE2 . TYR B 1 334 ? 15.435  -21.700 78.773  1.00 35.74  ? 334 TYR B CE2 1 
ATOM   6379 C  CZ  . TYR B 1 334 ? 15.477  -21.097 77.531  1.00 35.96  ? 334 TYR B CZ  1 
ATOM   6380 O  OH  . TYR B 1 334 ? 16.533  -20.279 77.186  1.00 36.72  ? 334 TYR B OH  1 
ATOM   6381 N  N   . ALA B 1 335 ? 11.495  -22.718 81.529  1.00 31.44  ? 335 ALA B N   1 
ATOM   6382 C  CA  . ALA B 1 335 ? 11.985  -22.074 82.741  1.00 33.57  ? 335 ALA B CA  1 
ATOM   6383 C  C   . ALA B 1 335 ? 13.503  -21.962 82.678  1.00 35.44  ? 335 ALA B C   1 
ATOM   6384 O  O   . ALA B 1 335 ? 14.208  -22.968 82.526  1.00 35.28  ? 335 ALA B O   1 
ATOM   6385 C  CB  . ALA B 1 335 ? 11.554  -22.851 83.981  1.00 37.23  ? 335 ALA B CB  1 
ATOM   6386 N  N   . LYS B 1 336 ? 14.004  -20.732 82.781  1.00 36.17  ? 336 LYS B N   1 
ATOM   6387 C  CA  . LYS B 1 336 ? 15.451  -20.520 82.784  1.00 37.28  ? 336 LYS B CA  1 
ATOM   6388 C  C   . LYS B 1 336 ? 16.112  -21.115 84.027  1.00 37.64  ? 336 LYS B C   1 
ATOM   6389 O  O   . LYS B 1 336 ? 17.243  -21.607 83.951  1.00 40.87  ? 336 LYS B O   1 
ATOM   6390 C  CB  . LYS B 1 336 ? 15.742  -19.020 82.691  1.00 38.15  ? 336 LYS B CB  1 
ATOM   6391 C  CG  . LYS B 1 336 ? 15.460  -18.408 81.317  1.00 35.54  ? 336 LYS B CG  1 
ATOM   6392 C  CD  . LYS B 1 336 ? 15.044  -16.947 81.454  1.00 35.15  ? 336 LYS B CD  1 
ATOM   6393 C  CE  . LYS B 1 336 ? 16.249  -16.019 81.644  1.00 40.24  ? 336 LYS B CE  1 
ATOM   6394 N  NZ  . LYS B 1 336 ? 17.465  -16.498 80.917  1.00 40.62  ? 336 LYS B NZ  1 
ATOM   6395 N  N   . GLU B 1 337 ? 15.422  -21.082 85.165  1.00 34.96  ? 337 GLU B N   1 
ATOM   6396 C  CA  . GLU B 1 337 ? 15.937  -21.532 86.456  1.00 39.41  ? 337 GLU B CA  1 
ATOM   6397 C  C   . GLU B 1 337 ? 14.767  -22.199 87.168  1.00 41.08  ? 337 GLU B C   1 
ATOM   6398 O  O   . GLU B 1 337 ? 13.605  -21.992 86.795  1.00 37.80  ? 337 GLU B O   1 
ATOM   6399 C  CB  . GLU B 1 337 ? 16.445  -20.329 87.280  1.00 36.36  ? 337 GLU B CB  1 
ATOM   6400 C  CG  . GLU B 1 337 ? 17.820  -19.721 86.949  1.00 40.56  ? 337 GLU B CG  1 
ATOM   6401 C  CD  . GLU B 1 337 ? 18.935  -20.666 86.528  1.00 37.37  ? 337 GLU B CD  1 
ATOM   6402 O  OE1 . GLU B 1 337 ? 18.955  -21.854 86.914  1.00 38.58  ? 337 GLU B OE1 1 
ATOM   6403 O  OE2 . GLU B 1 337 ? 19.801  -20.200 85.765  1.00 42.81  ? 337 GLU B OE2 1 
ATOM   6404 N  N   . ASP B 1 338 ? 15.052  -23.008 88.195  1.00 41.99  ? 338 ASP B N   1 
ATOM   6405 C  CA  . ASP B 1 338 ? 13.963  -23.465 89.057  1.00 38.09  ? 338 ASP B CA  1 
ATOM   6406 C  C   . ASP B 1 338 ? 13.143  -22.260 89.497  1.00 39.60  ? 338 ASP B C   1 
ATOM   6407 O  O   . ASP B 1 338 ? 13.690  -21.197 89.807  1.00 40.42  ? 338 ASP B O   1 
ATOM   6408 C  CB  . ASP B 1 338 ? 14.474  -24.182 90.311  1.00 44.38  ? 338 ASP B CB  1 
ATOM   6409 C  CG  . ASP B 1 338 ? 15.281  -25.432 90.013  1.00 42.47  ? 338 ASP B CG  1 
ATOM   6410 O  OD1 . ASP B 1 338 ? 15.195  -26.006 88.908  1.00 38.18  ? 338 ASP B OD1 1 
ATOM   6411 O  OD2 . ASP B 1 338 ? 16.010  -25.844 90.931  1.00 42.81  ? 338 ASP B OD2 1 
ATOM   6412 N  N   . THR B 1 339 ? 11.826  -22.435 89.563  1.00 37.45  ? 339 THR B N   1 
ATOM   6413 C  CA  . THR B 1 339 ? 10.969  -21.324 89.942  1.00 38.88  ? 339 THR B CA  1 
ATOM   6414 C  C   . THR B 1 339 ? 9.589   -21.880 90.270  1.00 41.07  ? 339 THR B C   1 
ATOM   6415 O  O   . THR B 1 339 ? 9.242   -23.001 89.877  1.00 42.92  ? 339 THR B O   1 
ATOM   6416 C  CB  . THR B 1 339 ? 10.915  -20.280 88.816  1.00 40.35  ? 339 THR B CB  1 
ATOM   6417 O  OG1 . THR B 1 339 ? 10.380  -19.043 89.298  1.00 40.72  ? 339 THR B OG1 1 
ATOM   6418 C  CG2 . THR B 1 339 ? 10.079  -20.804 87.650  1.00 39.04  ? 339 THR B CG2 1 
ATOM   6419 N  N   . VAL B 1 340 ? 8.811   -21.100 91.016  1.00 40.85  ? 340 VAL B N   1 
ATOM   6420 C  CA  . VAL B 1 340 ? 7.474   -21.515 91.432  1.00 40.26  ? 340 VAL B CA  1 
ATOM   6421 C  C   . VAL B 1 340 ? 6.444   -20.663 90.693  1.00 37.76  ? 340 VAL B C   1 
ATOM   6422 O  O   . VAL B 1 340 ? 6.416   -19.431 90.829  1.00 40.59  ? 340 VAL B O   1 
ATOM   6423 C  CB  . VAL B 1 340 ? 7.297   -21.416 92.957  1.00 45.01  ? 340 VAL B CB  1 
ATOM   6424 C  CG1 . VAL B 1 340 ? 5.847   -21.733 93.353  1.00 39.73  ? 340 VAL B CG1 1 
ATOM   6425 C  CG2 . VAL B 1 340 ? 8.272   -22.364 93.655  1.00 43.24  ? 340 VAL B CG2 1 
ATOM   6426 N  N   . LEU B 1 341 ? 5.588   -21.322 89.918  1.00 41.08  ? 341 LEU B N   1 
ATOM   6427 C  CA  . LEU B 1 341 ? 4.574   -20.626 89.140  1.00 38.10  ? 341 LEU B CA  1 
ATOM   6428 C  C   . LEU B 1 341 ? 3.326   -20.396 89.991  1.00 35.87  ? 341 LEU B C   1 
ATOM   6429 O  O   . LEU B 1 341 ? 2.748   -21.343 90.531  1.00 37.10  ? 341 LEU B O   1 
ATOM   6430 C  CB  . LEU B 1 341 ? 4.235   -21.427 87.884  1.00 39.27  ? 341 LEU B CB  1 
ATOM   6431 C  CG  . LEU B 1 341 ? 3.332   -20.783 86.831  1.00 39.82  ? 341 LEU B CG  1 
ATOM   6432 C  CD1 . LEU B 1 341 ? 4.027   -19.586 86.180  1.00 38.39  ? 341 LEU B CD1 1 
ATOM   6433 C  CD2 . LEU B 1 341 ? 2.942   -21.830 85.783  1.00 37.63  ? 341 LEU B CD2 1 
ATOM   6434 N  N   . GLY B 1 342 ? 2.920   -19.136 90.112  1.00 36.88  ? 342 GLY B N   1 
ATOM   6435 C  CA  . GLY B 1 342 ? 1.654   -18.822 90.734  1.00 37.53  ? 342 GLY B CA  1 
ATOM   6436 C  C   . GLY B 1 342 ? 1.591   -19.140 92.203  1.00 42.51  ? 342 GLY B C   1 
ATOM   6437 O  O   . GLY B 1 342 ? 0.499   -19.356 92.734  1.00 43.63  ? 342 GLY B O   1 
ATOM   6438 N  N   . GLY B 1 343 ? 2.738   -19.188 92.878  1.00 42.97  ? 343 GLY B N   1 
ATOM   6439 C  CA  . GLY B 1 343 ? 2.758   -19.574 94.272  1.00 42.39  ? 343 GLY B CA  1 
ATOM   6440 C  C   . GLY B 1 343 ? 2.370   -21.008 94.528  1.00 46.59  ? 343 GLY B C   1 
ATOM   6441 O  O   . GLY B 1 343 ? 2.236   -21.398 95.690  1.00 46.97  ? 343 GLY B O   1 
ATOM   6442 N  N   . GLU B 1 344 ? 2.236   -21.822 93.483  1.00 37.55  ? 344 GLU B N   1 
ATOM   6443 C  CA  . GLU B 1 344 ? 1.536   -23.094 93.602  1.00 44.75  ? 344 GLU B CA  1 
ATOM   6444 C  C   . GLU B 1 344 ? 2.157   -24.232 92.807  1.00 46.69  ? 344 GLU B C   1 
ATOM   6445 O  O   . GLU B 1 344 ? 2.047   -25.383 93.237  1.00 44.47  ? 344 GLU B O   1 
ATOM   6446 C  CB  . GLU B 1 344 ? 0.086   -22.896 93.151  1.00 45.62  ? 344 GLU B CB  1 
ATOM   6447 C  CG  . GLU B 1 344 ? -0.789  -22.287 94.231  1.00 55.12  ? 344 GLU B CG  1 
ATOM   6448 C  CD  . GLU B 1 344 ? -2.186  -21.957 93.740  1.00 56.79  ? 344 GLU B CD  1 
ATOM   6449 O  OE1 . GLU B 1 344 ? -2.384  -21.916 92.505  1.00 52.67  ? 344 GLU B OE1 1 
ATOM   6450 O  OE2 . GLU B 1 344 ? -3.087  -21.755 94.585  1.00 61.55  ? 344 GLU B OE2 1 
ATOM   6451 N  N   . TYR B 1 345 ? 2.807   -23.966 91.679  1.00 37.38  ? 345 TYR B N   1 
ATOM   6452 C  CA  . TYR B 1 345 ? 3.281   -25.010 90.771  1.00 40.18  ? 345 TYR B CA  1 
ATOM   6453 C  C   . TYR B 1 345 ? 4.791   -24.904 90.641  1.00 42.41  ? 345 TYR B C   1 
ATOM   6454 O  O   . TYR B 1 345 ? 5.295   -24.028 89.916  1.00 38.53  ? 345 TYR B O   1 
ATOM   6455 C  CB  . TYR B 1 345 ? 2.599   -24.873 89.410  1.00 41.51  ? 345 TYR B CB  1 
ATOM   6456 C  CG  . TYR B 1 345 ? 1.106   -24.989 89.555  1.00 37.78  ? 345 TYR B CG  1 
ATOM   6457 C  CD1 . TYR B 1 345 ? 0.522   -26.216 89.852  1.00 41.38  ? 345 TYR B CD1 1 
ATOM   6458 C  CD2 . TYR B 1 345 ? 0.287   -23.871 89.478  1.00 41.97  ? 345 TYR B CD2 1 
ATOM   6459 C  CE1 . TYR B 1 345 ? -0.844  -26.344 90.018  1.00 41.81  ? 345 TYR B CE1 1 
ATOM   6460 C  CE2 . TYR B 1 345 ? -1.089  -23.983 89.647  1.00 40.36  ? 345 TYR B CE2 1 
ATOM   6461 C  CZ  . TYR B 1 345 ? -1.644  -25.229 89.920  1.00 41.27  ? 345 TYR B CZ  1 
ATOM   6462 O  OH  . TYR B 1 345 ? -3.009  -25.358 90.087  1.00 46.94  ? 345 TYR B OH  1 
ATOM   6463 N  N   . PRO B 1 346 ? 5.550   -25.722 91.369  1.00 42.22  ? 346 PRO B N   1 
ATOM   6464 C  CA  . PRO B 1 346 ? 7.010   -25.683 91.232  1.00 43.58  ? 346 PRO B CA  1 
ATOM   6465 C  C   . PRO B 1 346 ? 7.453   -26.223 89.884  1.00 34.69  ? 346 PRO B C   1 
ATOM   6466 O  O   . PRO B 1 346 ? 6.974   -27.262 89.421  1.00 37.50  ? 346 PRO B O   1 
ATOM   6467 C  CB  . PRO B 1 346 ? 7.509   -26.563 92.388  1.00 45.17  ? 346 PRO B CB  1 
ATOM   6468 C  CG  . PRO B 1 346 ? 6.350   -26.665 93.328  1.00 46.06  ? 346 PRO B CG  1 
ATOM   6469 C  CD  . PRO B 1 346 ? 5.118   -26.568 92.495  1.00 44.69  ? 346 PRO B CD  1 
ATOM   6470 N  N   . LEU B 1 347 ? 8.395   -25.505 89.275  1.00 38.52  ? 347 LEU B N   1 
ATOM   6471 C  CA  . LEU B 1 347 ? 8.975   -25.832 87.981  1.00 39.10  ? 347 LEU B CA  1 
ATOM   6472 C  C   . LEU B 1 347 ? 10.482  -25.966 88.139  1.00 41.71  ? 347 LEU B C   1 
ATOM   6473 O  O   . LEU B 1 347 ? 11.105  -25.217 88.899  1.00 37.27  ? 347 LEU B O   1 
ATOM   6474 C  CB  . LEU B 1 347 ? 8.663   -24.729 86.956  1.00 36.42  ? 347 LEU B CB  1 
ATOM   6475 C  CG  . LEU B 1 347 ? 7.202   -24.468 86.595  1.00 38.53  ? 347 LEU B CG  1 
ATOM   6476 C  CD1 . LEU B 1 347 ? 7.118   -23.532 85.397  1.00 35.66  ? 347 LEU B CD1 1 
ATOM   6477 C  CD2 . LEU B 1 347 ? 6.460   -25.764 86.301  1.00 38.53  ? 347 LEU B CD2 1 
ATOM   6478 N  N   . GLU B 1 348 ? 11.066  -26.923 87.437  1.00 39.72  ? 348 GLU B N   1 
ATOM   6479 C  CA  . GLU B 1 348 ? 12.513  -27.020 87.376  1.00 39.34  ? 348 GLU B CA  1 
ATOM   6480 C  C   . GLU B 1 348 ? 13.043  -26.345 86.124  1.00 38.11  ? 348 GLU B C   1 
ATOM   6481 O  O   . GLU B 1 348 ? 12.365  -26.280 85.096  1.00 37.85  ? 348 GLU B O   1 
ATOM   6482 C  CB  . GLU B 1 348 ? 12.981  -28.476 87.412  1.00 43.10  ? 348 GLU B CB  1 
ATOM   6483 C  CG  . GLU B 1 348 ? 12.191  -29.349 88.363  1.00 51.68  ? 348 GLU B CG  1 
ATOM   6484 C  CD  . GLU B 1 348 ? 12.676  -30.775 88.321  1.00 57.36  ? 348 GLU B CD  1 
ATOM   6485 O  OE1 . GLU B 1 348 ? 13.723  -31.067 88.945  1.00 62.45  ? 348 GLU B OE1 1 
ATOM   6486 O  OE2 . GLU B 1 348 ? 12.011  -31.599 87.667  1.00 58.51  ? 348 GLU B OE2 1 
ATOM   6487 N  N   . LYS B 1 349 ? 14.271  -25.843 86.226  1.00 37.18  ? 349 LYS B N   1 
ATOM   6488 C  CA  . LYS B 1 349 ? 14.974  -25.333 85.066  1.00 34.79  ? 349 LYS B CA  1 
ATOM   6489 C  C   . LYS B 1 349 ? 14.775  -26.283 83.896  1.00 37.60  ? 349 LYS B C   1 
ATOM   6490 O  O   . LYS B 1 349 ? 14.895  -27.506 84.043  1.00 35.88  ? 349 LYS B O   1 
ATOM   6491 C  CB  . LYS B 1 349 ? 16.463  -25.164 85.400  1.00 35.91  ? 349 LYS B CB  1 
ATOM   6492 C  CG  . LYS B 1 349 ? 17.392  -24.980 84.214  1.00 40.65  ? 349 LYS B CG  1 
ATOM   6493 C  CD  . LYS B 1 349 ? 18.825  -25.043 84.718  1.00 42.19  ? 349 LYS B CD  1 
ATOM   6494 C  CE  . LYS B 1 349 ? 19.728  -24.085 83.997  1.00 49.12  ? 349 LYS B CE  1 
ATOM   6495 N  NZ  . LYS B 1 349 ? 21.046  -24.705 83.716  1.00 48.61  ? 349 LYS B NZ  1 
ATOM   6496 N  N   . GLY B 1 350 ? 14.411  -25.721 82.744  1.00 34.12  ? 350 GLY B N   1 
ATOM   6497 C  CA  . GLY B 1 350 ? 14.146  -26.507 81.561  1.00 33.37  ? 350 GLY B CA  1 
ATOM   6498 C  C   . GLY B 1 350 ? 12.692  -26.898 81.355  1.00 34.98  ? 350 GLY B C   1 
ATOM   6499 O  O   . GLY B 1 350 ? 12.314  -27.218 80.223  1.00 34.67  ? 350 GLY B O   1 
ATOM   6500 N  N   . ASP B 1 351 ? 11.867  -26.876 82.406  1.00 37.50  ? 351 ASP B N   1 
ATOM   6501 C  CA  . ASP B 1 351 ? 10.463  -27.255 82.261  1.00 35.48  ? 351 ASP B CA  1 
ATOM   6502 C  C   . ASP B 1 351 ? 9.766   -26.327 81.279  1.00 36.09  ? 351 ASP B C   1 
ATOM   6503 O  O   . ASP B 1 351 ? 9.989   -25.111 81.292  1.00 35.39  ? 351 ASP B O   1 
ATOM   6504 C  CB  . ASP B 1 351 ? 9.730   -27.174 83.598  1.00 35.01  ? 351 ASP B CB  1 
ATOM   6505 C  CG  . ASP B 1 351 ? 9.961   -28.388 84.483  1.00 40.94  ? 351 ASP B CG  1 
ATOM   6506 O  OD1 . ASP B 1 351 ? 10.635  -29.353 84.055  1.00 37.52  ? 351 ASP B OD1 1 
ATOM   6507 O  OD2 . ASP B 1 351 ? 9.452   -28.357 85.622  1.00 40.58  ? 351 ASP B OD2 1 
ATOM   6508 N  N   . GLU B 1 352 ? 8.867   -26.891 80.471  1.00 35.55  ? 352 GLU B N   1 
ATOM   6509 C  CA  . GLU B 1 352 ? 8.215   -26.154 79.399  1.00 38.18  ? 352 GLU B CA  1 
ATOM   6510 C  C   . GLU B 1 352 ? 6.760   -25.822 79.707  1.00 36.89  ? 352 GLU B C   1 
ATOM   6511 O  O   . GLU B 1 352 ? 6.081   -26.528 80.465  1.00 34.60  ? 352 GLU B O   1 
ATOM   6512 C  CB  . GLU B 1 352 ? 8.287   -26.931 78.087  1.00 37.97  ? 352 GLU B CB  1 
ATOM   6513 C  CG  . GLU B 1 352 ? 9.661   -27.474 77.832  1.00 41.48  ? 352 GLU B CG  1 
ATOM   6514 C  CD  . GLU B 1 352 ? 9.719   -28.267 76.565  1.00 45.72  ? 352 GLU B CD  1 
ATOM   6515 O  OE1 . GLU B 1 352 ? 8.667   -28.360 75.886  1.00 42.72  ? 352 GLU B OE1 1 
ATOM   6516 O  OE2 . GLU B 1 352 ? 10.814  -28.782 76.251  1.00 50.67  ? 352 GLU B OE2 1 
ATOM   6517 N  N   . LEU B 1 353 ? 6.304   -24.729 79.085  1.00 36.20  ? 353 LEU B N   1 
ATOM   6518 C  CA  . LEU B 1 353 ? 4.949   -24.199 79.196  1.00 33.26  ? 353 LEU B CA  1 
ATOM   6519 C  C   . LEU B 1 353 ? 4.402   -23.922 77.802  1.00 33.19  ? 353 LEU B C   1 
ATOM   6520 O  O   . LEU B 1 353 ? 5.139   -23.468 76.917  1.00 34.32  ? 353 LEU B O   1 
ATOM   6521 C  CB  . LEU B 1 353 ? 4.925   -22.883 79.984  1.00 29.84  ? 353 LEU B CB  1 
ATOM   6522 C  CG  . LEU B 1 353 ? 5.540   -22.853 81.381  1.00 31.92  ? 353 LEU B CG  1 
ATOM   6523 C  CD1 . LEU B 1 353 ? 5.590   -21.425 81.837  1.00 32.03  ? 353 LEU B CD1 1 
ATOM   6524 C  CD2 . LEU B 1 353 ? 4.705   -23.695 82.336  1.00 32.09  ? 353 LEU B CD2 1 
ATOM   6525 N  N   . MET B 1 354 ? 3.108   -24.158 77.611  1.00 30.45  ? 354 MET B N   1 
ATOM   6526 C  CA  . MET B 1 354 ? 2.425   -23.689 76.411  1.00 30.95  ? 354 MET B CA  1 
ATOM   6527 C  C   . MET B 1 354 ? 1.359   -22.688 76.805  1.00 33.82  ? 354 MET B C   1 
ATOM   6528 O  O   . MET B 1 354 ? 0.549   -22.955 77.693  1.00 34.78  ? 354 MET B O   1 
ATOM   6529 C  CB  . MET B 1 354 ? 1.799   -24.817 75.576  1.00 31.99  ? 354 MET B CB  1 
ATOM   6530 C  CG  . MET B 1 354 ? 2.790   -25.890 75.275  1.00 34.51  ? 354 MET B CG  1 
ATOM   6531 S  SD  . MET B 1 354 ? 3.721   -25.417 73.783  1.00 36.56  ? 354 MET B SD  1 
ATOM   6532 C  CE  . MET B 1 354 ? 2.527   -24.528 72.805  1.00 32.37  ? 354 MET B CE  1 
ATOM   6533 N  N   . VAL B 1 355 ? 1.391   -21.532 76.161  1.00 32.08  ? 355 VAL B N   1 
ATOM   6534 C  CA  . VAL B 1 355 ? 0.406   -20.487 76.390  1.00 31.51  ? 355 VAL B CA  1 
ATOM   6535 C  C   . VAL B 1 355 ? -0.696  -20.693 75.367  1.00 30.79  ? 355 VAL B C   1 
ATOM   6536 O  O   . VAL B 1 355 ? -0.447  -20.609 74.161  1.00 29.52  ? 355 VAL B O   1 
ATOM   6537 C  CB  . VAL B 1 355 ? 1.039   -19.097 76.242  1.00 31.75  ? 355 VAL B CB  1 
ATOM   6538 C  CG1 . VAL B 1 355 ? -0.023  -18.006 76.380  1.00 31.28  ? 355 VAL B CG1 1 
ATOM   6539 C  CG2 . VAL B 1 355 ? 2.163   -18.908 77.247  1.00 29.97  ? 355 VAL B CG2 1 
ATOM   6540 N  N   . LEU B 1 356 ? -1.912  -20.946 75.836  1.00 32.69  ? 356 LEU B N   1 
ATOM   6541 C  CA  . LEU B 1 356 ? -3.041  -21.201 74.940  1.00 33.38  ? 356 LEU B CA  1 
ATOM   6542 C  C   . LEU B 1 356 ? -3.750  -19.865 74.731  1.00 31.25  ? 356 LEU B C   1 
ATOM   6543 O  O   . LEU B 1 356 ? -4.647  -19.496 75.495  1.00 34.66  ? 356 LEU B O   1 
ATOM   6544 C  CB  . LEU B 1 356 ? -3.967  -22.238 75.564  1.00 32.86  ? 356 LEU B CB  1 
ATOM   6545 C  CG  . LEU B 1 356 ? -4.064  -23.642 74.985  1.00 45.31  ? 356 LEU B CG  1 
ATOM   6546 C  CD1 . LEU B 1 356 ? -5.111  -24.425 75.800  1.00 40.50  ? 356 LEU B CD1 1 
ATOM   6547 C  CD2 . LEU B 1 356 ? -4.328  -23.664 73.478  1.00 42.99  ? 356 LEU B CD2 1 
ATOM   6548 N  N   . ILE B 1 357 ? -3.338  -19.119 73.694  1.00 29.74  ? 357 ILE B N   1 
ATOM   6549 C  CA  . ILE B 1 357 ? -3.793  -17.723 73.559  1.00 29.98  ? 357 ILE B CA  1 
ATOM   6550 C  C   . ILE B 1 357 ? -5.309  -17.610 73.506  1.00 32.52  ? 357 ILE B C   1 
ATOM   6551 O  O   . ILE B 1 357 ? -5.863  -16.679 74.119  1.00 30.93  ? 357 ILE B O   1 
ATOM   6552 C  CB  . ILE B 1 357 ? -3.112  -17.057 72.354  1.00 30.47  ? 357 ILE B CB  1 
ATOM   6553 C  CG1 . ILE B 1 357 ? -1.601  -17.267 72.366  1.00 29.81  ? 357 ILE B CG1 1 
ATOM   6554 C  CG2 . ILE B 1 357 ? -3.420  -15.535 72.330  1.00 28.79  ? 357 ILE B CG2 1 
ATOM   6555 C  CD1 . ILE B 1 357 ? -0.954  -16.645 71.116  1.00 28.22  ? 357 ILE B CD1 1 
ATOM   6556 N  N   . PRO B 1 358 ? -6.043  -18.461 72.778  1.00 33.89  ? 358 PRO B N   1 
ATOM   6557 C  CA  . PRO B 1 358 ? -7.509  -18.285 72.740  1.00 31.21  ? 358 PRO B CA  1 
ATOM   6558 C  C   . PRO B 1 358 ? -8.146  -18.386 74.116  1.00 31.16  ? 358 PRO B C   1 
ATOM   6559 O  O   . PRO B 1 358 ? -9.186  -17.754 74.366  1.00 34.85  ? 358 PRO B O   1 
ATOM   6560 C  CB  . PRO B 1 358 ? -7.978  -19.419 71.812  1.00 29.03  ? 358 PRO B CB  1 
ATOM   6561 C  CG  . PRO B 1 358 ? -6.738  -19.748 70.957  1.00 31.23  ? 358 PRO B CG  1 
ATOM   6562 C  CD  . PRO B 1 358 ? -5.596  -19.586 71.939  1.00 30.16  ? 358 PRO B CD  1 
ATOM   6563 N  N   . GLN B 1 359 ? -7.557  -19.176 75.017  1.00 33.76  ? 359 GLN B N   1 
ATOM   6564 C  CA  . GLN B 1 359 ? -8.122  -19.309 76.355  1.00 33.22  ? 359 GLN B CA  1 
ATOM   6565 C  C   . GLN B 1 359 ? -7.771  -18.106 77.201  1.00 35.11  ? 359 GLN B C   1 
ATOM   6566 O  O   . GLN B 1 359 ? -8.619  -17.601 77.940  1.00 34.76  ? 359 GLN B O   1 
ATOM   6567 C  CB  . GLN B 1 359 ? -7.620  -20.595 77.024  1.00 35.85  ? 359 GLN B CB  1 
ATOM   6568 C  CG  . GLN B 1 359 ? -8.163  -21.854 76.390  1.00 37.13  ? 359 GLN B CG  1 
ATOM   6569 C  CD  . GLN B 1 359 ? -9.679  -21.872 76.387  1.00 35.68  ? 359 GLN B CD  1 
ATOM   6570 O  OE1 . GLN B 1 359 ? -10.309 -21.855 75.335  1.00 37.36  ? 359 GLN B OE1 1 
ATOM   6571 N  NE2 . GLN B 1 359 ? -10.266 -21.932 77.577  1.00 38.89  ? 359 GLN B NE2 1 
ATOM   6572 N  N   . LEU B 1 360 ? -6.510  -17.661 77.135  1.00 32.59  ? 360 LEU B N   1 
ATOM   6573 C  CA  . LEU B 1 360 ? -6.134  -16.413 77.785  1.00 31.99  ? 360 LEU B CA  1 
ATOM   6574 C  C   . LEU B 1 360 ? -7.158  -15.332 77.448  1.00 32.68  ? 360 LEU B C   1 
ATOM   6575 O  O   . LEU B 1 360 ? -7.642  -14.606 78.327  1.00 34.21  ? 360 LEU B O   1 
ATOM   6576 C  CB  . LEU B 1 360 ? -4.728  -15.987 77.321  1.00 27.95  ? 360 LEU B CB  1 
ATOM   6577 C  CG  . LEU B 1 360 ? -4.327  -14.538 77.640  1.00 33.10  ? 360 LEU B CG  1 
ATOM   6578 C  CD1 . LEU B 1 360 ? -4.167  -14.374 79.162  1.00 34.59  ? 360 LEU B CD1 1 
ATOM   6579 C  CD2 . LEU B 1 360 ? -3.039  -14.125 76.946  1.00 31.84  ? 360 LEU B CD2 1 
ATOM   6580 N  N   . HIS B 1 361 ? -7.499  -15.216 76.162  1.00 30.34  ? 361 HIS B N   1 
ATOM   6581 C  CA  . HIS B 1 361 ? -8.388  -14.160 75.685  1.00 32.11  ? 361 HIS B CA  1 
ATOM   6582 C  C   . HIS B 1 361 ? -9.839  -14.396 76.071  1.00 34.01  ? 361 HIS B C   1 
ATOM   6583 O  O   . HIS B 1 361 ? -10.697 -13.572 75.720  1.00 33.04  ? 361 HIS B O   1 
ATOM   6584 C  CB  . HIS B 1 361 ? -8.259  -14.018 74.161  1.00 28.75  ? 361 HIS B CB  1 
ATOM   6585 C  CG  . HIS B 1 361 ? -6.930  -13.480 73.721  1.00 28.80  ? 361 HIS B CG  1 
ATOM   6586 N  ND1 . HIS B 1 361 ? -6.547  -13.424 72.395  1.00 30.67  ? 361 HIS B ND1 1 
ATOM   6587 C  CD2 . HIS B 1 361 ? -5.897  -12.970 74.436  1.00 30.61  ? 361 HIS B CD2 1 
ATOM   6588 C  CE1 . HIS B 1 361 ? -5.335  -12.893 72.314  1.00 31.30  ? 361 HIS B CE1 1 
ATOM   6589 N  NE2 . HIS B 1 361 ? -4.918  -12.604 73.539  1.00 29.59  ? 361 HIS B NE2 1 
ATOM   6590 N  N   . ARG B 1 362 ? -10.125 -15.494 76.775  1.00 33.77  ? 362 ARG B N   1 
ATOM   6591 C  CA  . ARG B 1 362 ? -11.462 -15.771 77.286  1.00 32.02  ? 362 ARG B CA  1 
ATOM   6592 C  C   . ARG B 1 362 ? -11.489 -15.801 78.810  1.00 35.88  ? 362 ARG B C   1 
ATOM   6593 O  O   . ARG B 1 362 ? -12.448 -16.307 79.396  1.00 33.85  ? 362 ARG B O   1 
ATOM   6594 C  CB  . ARG B 1 362 ? -11.993 -17.093 76.718  1.00 32.08  ? 362 ARG B CB  1 
ATOM   6595 C  CG  . ARG B 1 362 ? -12.374 -17.039 75.230  1.00 35.10  ? 362 ARG B CG  1 
ATOM   6596 C  CD  . ARG B 1 362 ? -12.556 -18.449 74.626  1.00 32.99  ? 362 ARG B CD  1 
ATOM   6597 N  NE  . ARG B 1 362 ? -13.105 -18.408 73.273  1.00 32.60  ? 362 ARG B NE  1 
ATOM   6598 C  CZ  . ARG B 1 362 ? -12.414 -18.036 72.202  1.00 33.61  ? 362 ARG B CZ  1 
ATOM   6599 N  NH1 . ARG B 1 362 ? -11.156 -17.641 72.294  1.00 29.86  ? 362 ARG B NH1 1 
ATOM   6600 N  NH2 . ARG B 1 362 ? -12.998 -18.067 71.009  1.00 33.91  ? 362 ARG B NH2 1 
ATOM   6601 N  N   . ASP B 1 363 ? -10.449 -15.297 79.465  1.00 32.83  ? 363 ASP B N   1 
ATOM   6602 C  CA  . ASP B 1 363 ? -10.394 -15.251 80.925  1.00 32.74  ? 363 ASP B CA  1 
ATOM   6603 C  C   . ASP B 1 363 ? -11.451 -14.272 81.432  1.00 35.45  ? 363 ASP B C   1 
ATOM   6604 O  O   . ASP B 1 363 ? -11.317 -13.058 81.256  1.00 32.19  ? 363 ASP B O   1 
ATOM   6605 C  CB  . ASP B 1 363 ? -8.980  -14.853 81.342  1.00 31.58  ? 363 ASP B CB  1 
ATOM   6606 C  CG  . ASP B 1 363 ? -8.774  -14.889 82.828  1.00 38.90  ? 363 ASP B CG  1 
ATOM   6607 O  OD1 . ASP B 1 363 ? -9.776  -14.842 83.568  1.00 35.60  ? 363 ASP B OD1 1 
ATOM   6608 O  OD2 . ASP B 1 363 ? -7.602  -14.967 83.251  1.00 34.71  ? 363 ASP B OD2 1 
ATOM   6609 N  N   . LYS B 1 364 ? -12.531 -14.797 82.030  1.00 34.45  ? 364 LYS B N   1 
ATOM   6610 C  CA  . LYS B 1 364 ? -13.625 -13.928 82.457  1.00 35.01  ? 364 LYS B CA  1 
ATOM   6611 C  C   . LYS B 1 364 ? -13.217 -12.956 83.555  1.00 36.50  ? 364 LYS B C   1 
ATOM   6612 O  O   . LYS B 1 364 ? -13.829 -11.887 83.677  1.00 36.46  ? 364 LYS B O   1 
ATOM   6613 C  CB  . LYS B 1 364 ? -14.821 -14.761 82.921  1.00 40.84  ? 364 LYS B CB  1 
ATOM   6614 C  CG  . LYS B 1 364 ? -15.337 -15.704 81.863  1.00 42.98  ? 364 LYS B CG  1 
ATOM   6615 C  CD  . LYS B 1 364 ? -16.473 -16.561 82.377  1.00 49.47  ? 364 LYS B CD  1 
ATOM   6616 C  CE  . LYS B 1 364 ? -17.268 -17.152 81.222  1.00 53.98  ? 364 LYS B CE  1 
ATOM   6617 N  NZ  . LYS B 1 364 ? -18.465 -17.903 81.723  1.00 53.06  ? 364 LYS B NZ  1 
ATOM   6618 N  N   . THR B 1 365 ? -12.212 -13.298 84.374  1.00 36.14  ? 365 THR B N   1 
ATOM   6619 C  CA  . THR B 1 365 ? -11.767 -12.350 85.399  1.00 34.30  ? 365 THR B CA  1 
ATOM   6620 C  C   . THR B 1 365 ? -11.136 -11.104 84.797  1.00 38.15  ? 365 THR B C   1 
ATOM   6621 O  O   . THR B 1 365 ? -10.995 -10.103 85.505  1.00 37.13  ? 365 THR B O   1 
ATOM   6622 C  CB  . THR B 1 365 ? -10.769 -13.002 86.368  1.00 39.19  ? 365 THR B CB  1 
ATOM   6623 O  OG1 . THR B 1 365 ? -9.495  -13.126 85.732  1.00 37.89  ? 365 THR B OG1 1 
ATOM   6624 C  CG2 . THR B 1 365 ? -11.250 -14.389 86.825  1.00 37.38  ? 365 THR B CG2 1 
ATOM   6625 N  N   . ILE B 1 366 ? -10.761 -11.148 83.520  1.00 37.71  ? 366 ILE B N   1 
ATOM   6626 C  CA  . ILE B 1 366 ? -10.231 -9.994  82.786  1.00 31.41  ? 366 ILE B CA  1 
ATOM   6627 C  C   . ILE B 1 366 ? -11.314 -9.337  81.941  1.00 36.23  ? 366 ILE B C   1 
ATOM   6628 O  O   . ILE B 1 366 ? -11.522 -8.124  82.003  1.00 34.05  ? 366 ILE B O   1 
ATOM   6629 C  CB  . ILE B 1 366 ? -9.049  -10.439 81.894  1.00 32.42  ? 366 ILE B CB  1 
ATOM   6630 C  CG1 . ILE B 1 366 ? -7.854  -10.933 82.710  1.00 34.08  ? 366 ILE B CG1 1 
ATOM   6631 C  CG2 . ILE B 1 366 ? -8.626  -9.320  80.953  1.00 34.61  ? 366 ILE B CG2 1 
ATOM   6632 C  CD1 . ILE B 1 366 ? -7.151  -9.862  83.539  1.00 37.32  ? 366 ILE B CD1 1 
ATOM   6633 N  N   . TRP B 1 367 ? -12.013 -10.134 81.138  1.00 31.93  ? 367 TRP B N   1 
ATOM   6634 C  CA  . TRP B 1 367 ? -12.870 -9.610  80.090  1.00 34.92  ? 367 TRP B CA  1 
ATOM   6635 C  C   . TRP B 1 367 ? -14.341 -9.524  80.489  1.00 39.26  ? 367 TRP B C   1 
ATOM   6636 O  O   . TRP B 1 367 ? -15.115 -8.867  79.784  1.00 39.48  ? 367 TRP B O   1 
ATOM   6637 C  CB  . TRP B 1 367 ? -12.710 -10.466 78.828  1.00 34.57  ? 367 TRP B CB  1 
ATOM   6638 C  CG  . TRP B 1 367 ? -11.262 -10.506 78.342  1.00 35.71  ? 367 TRP B CG  1 
ATOM   6639 C  CD1 . TRP B 1 367 ? -10.342 -11.479 78.598  1.00 37.04  ? 367 TRP B CD1 1 
ATOM   6640 C  CD2 . TRP B 1 367 ? -10.586 -9.516  77.542  1.00 34.81  ? 367 TRP B CD2 1 
ATOM   6641 N  NE1 . TRP B 1 367 ? -9.134  -11.165 78.000  1.00 34.05  ? 367 TRP B NE1 1 
ATOM   6642 C  CE2 . TRP B 1 367 ? -9.262  -9.964  77.351  1.00 34.37  ? 367 TRP B CE2 1 
ATOM   6643 C  CE3 . TRP B 1 367 ? -10.972 -8.294  76.974  1.00 35.76  ? 367 TRP B CE3 1 
ATOM   6644 C  CZ2 . TRP B 1 367 ? -8.325  -9.238  76.608  1.00 32.89  ? 367 TRP B CZ2 1 
ATOM   6645 C  CZ3 . TRP B 1 367 ? -10.039 -7.573  76.245  1.00 35.35  ? 367 TRP B CZ3 1 
ATOM   6646 C  CH2 . TRP B 1 367 ? -8.731  -8.051  76.064  1.00 34.69  ? 367 TRP B CH2 1 
ATOM   6647 N  N   . GLY B 1 368 ? -14.744 -10.149 81.592  1.00 39.61  ? 368 GLY B N   1 
ATOM   6648 C  CA  . GLY B 1 368 ? -16.130 -10.089 82.031  1.00 38.06  ? 368 GLY B CA  1 
ATOM   6649 C  C   . GLY B 1 368 ? -16.916 -11.283 81.538  1.00 43.48  ? 368 GLY B C   1 
ATOM   6650 O  O   . GLY B 1 368 ? -16.379 -12.221 80.946  1.00 43.20  ? 368 GLY B O   1 
ATOM   6651 N  N   . ASP B 1 369 ? -18.230 -11.229 81.774  1.00 41.35  ? 369 ASP B N   1 
ATOM   6652 C  CA  . ASP B 1 369 ? -19.074 -12.401 81.546  1.00 43.36  ? 369 ASP B CA  1 
ATOM   6653 C  C   . ASP B 1 369 ? -19.328 -12.681 80.066  1.00 39.59  ? 369 ASP B C   1 
ATOM   6654 O  O   . ASP B 1 369 ? -19.632 -13.821 79.714  1.00 48.09  ? 369 ASP B O   1 
ATOM   6655 C  CB  . ASP B 1 369 ? -20.422 -12.230 82.236  1.00 44.61  ? 369 ASP B CB  1 
ATOM   6656 C  CG  . ASP B 1 369 ? -20.306 -12.207 83.732  1.00 54.55  ? 369 ASP B CG  1 
ATOM   6657 O  OD1 . ASP B 1 369 ? -19.733 -13.163 84.287  1.00 56.59  ? 369 ASP B OD1 1 
ATOM   6658 O  OD2 . ASP B 1 369 ? -20.812 -11.240 84.347  1.00 58.89  ? 369 ASP B OD2 1 
ATOM   6659 N  N   . ASP B 1 370 ? -19.231 -11.670 79.205  1.00 41.23  ? 370 ASP B N   1 
ATOM   6660 C  CA  . ASP B 1 370 ? -19.613 -11.775 77.801  1.00 45.52  ? 370 ASP B CA  1 
ATOM   6661 C  C   . ASP B 1 370 ? -18.440 -12.101 76.866  1.00 37.52  ? 370 ASP B C   1 
ATOM   6662 O  O   . ASP B 1 370 ? -18.448 -11.654 75.719  1.00 35.57  ? 370 ASP B O   1 
ATOM   6663 C  CB  . ASP B 1 370 ? -20.283 -10.476 77.337  1.00 43.55  ? 370 ASP B CB  1 
ATOM   6664 C  CG  . ASP B 1 370 ? -19.369 -9.256  77.484  1.00 46.43  ? 370 ASP B CG  1 
ATOM   6665 O  OD1 . ASP B 1 370 ? -18.170 -9.443  77.816  1.00 45.98  ? 370 ASP B OD1 1 
ATOM   6666 O  OD2 . ASP B 1 370 ? -19.805 -8.126  77.142  1.00 50.09  ? 370 ASP B OD2 1 
ATOM   6667 N  N   . VAL B 1 371 ? -17.455 -12.888 77.308  1.00 37.02  ? 371 VAL B N   1 
ATOM   6668 C  CA  . VAL B 1 371 ? -16.236 -13.079 76.515  1.00 39.82  ? 371 VAL B CA  1 
ATOM   6669 C  C   . VAL B 1 371 ? -16.463 -13.687 75.131  1.00 39.18  ? 371 VAL B C   1 
ATOM   6670 O  O   . VAL B 1 371 ? -15.612 -13.511 74.251  1.00 39.07  ? 371 VAL B O   1 
ATOM   6671 C  CB  . VAL B 1 371 ? -15.202 -13.915 77.310  1.00 40.02  ? 371 VAL B CB  1 
ATOM   6672 C  CG1 . VAL B 1 371 ? -15.042 -13.358 78.704  1.00 44.45  ? 371 VAL B CG1 1 
ATOM   6673 C  CG2 . VAL B 1 371 ? -15.686 -15.362 77.432  1.00 39.52  ? 371 VAL B CG2 1 
ATOM   6674 N  N   . GLU B 1 372 ? -17.577 -14.395 74.888  1.00 35.52  ? 372 GLU B N   1 
ATOM   6675 C  CA  . GLU B 1 372 ? -17.735 -14.980 73.555  1.00 36.98  ? 372 GLU B CA  1 
ATOM   6676 C  C   . GLU B 1 372 ? -18.382 -14.032 72.559  1.00 35.74  ? 372 GLU B C   1 
ATOM   6677 O  O   . GLU B 1 372 ? -18.412 -14.339 71.368  1.00 34.40  ? 372 GLU B O   1 
ATOM   6678 C  CB  . GLU B 1 372 ? -18.534 -16.288 73.614  1.00 37.20  ? 372 GLU B CB  1 
ATOM   6679 C  CG  . GLU B 1 372 ? -17.784 -17.337 74.410  1.00 43.94  ? 372 GLU B CG  1 
ATOM   6680 C  CD  . GLU B 1 372 ? -16.724 -18.044 73.589  1.00 40.40  ? 372 GLU B CD  1 
ATOM   6681 O  OE1 . GLU B 1 372 ? -16.813 -18.072 72.341  1.00 43.84  ? 372 GLU B OE1 1 
ATOM   6682 O  OE2 . GLU B 1 372 ? -15.751 -18.530 74.197  1.00 43.02  ? 372 GLU B OE2 1 
ATOM   6683 N  N   . GLU B 1 373 ? -18.862 -12.885 73.013  1.00 32.31  ? 373 GLU B N   1 
ATOM   6684 C  CA  . GLU B 1 373 ? -19.481 -11.902 72.146  1.00 35.02  ? 373 GLU B CA  1 
ATOM   6685 C  C   . GLU B 1 373 ? -18.427 -11.067 71.425  1.00 36.00  ? 373 GLU B C   1 
ATOM   6686 O  O   . GLU B 1 373 ? -17.376 -10.742 71.989  1.00 30.84  ? 373 GLU B O   1 
ATOM   6687 C  CB  . GLU B 1 373 ? -20.399 -11.020 72.993  1.00 35.78  ? 373 GLU B CB  1 
ATOM   6688 C  CG  . GLU B 1 373 ? -21.499 -11.892 73.623  1.00 37.08  ? 373 GLU B CG  1 
ATOM   6689 C  CD  . GLU B 1 373 ? -22.593 -11.129 74.337  1.00 44.46  ? 373 GLU B CD  1 
ATOM   6690 O  OE1 . GLU B 1 373 ? -22.404 -9.938  74.655  1.00 42.90  ? 373 GLU B OE1 1 
ATOM   6691 O  OE2 . GLU B 1 373 ? -23.647 -11.751 74.600  1.00 48.95  ? 373 GLU B OE2 1 
ATOM   6692 N  N   . PHE B 1 374 ? -18.722 -10.701 70.178  1.00 32.65  ? 374 PHE B N   1 
ATOM   6693 C  CA  . PHE B 1 374 ? -17.784 -9.909  69.382  1.00 31.70  ? 374 PHE B CA  1 
ATOM   6694 C  C   . PHE B 1 374 ? -18.112 -8.443  69.621  1.00 32.95  ? 374 PHE B C   1 
ATOM   6695 O  O   . PHE B 1 374 ? -19.113 -7.924  69.120  1.00 32.30  ? 374 PHE B O   1 
ATOM   6696 C  CB  . PHE B 1 374 ? -17.881 -10.281 67.904  1.00 31.98  ? 374 PHE B CB  1 
ATOM   6697 C  CG  . PHE B 1 374 ? -16.875 -9.587  67.058  1.00 29.96  ? 374 PHE B CG  1 
ATOM   6698 C  CD1 . PHE B 1 374 ? -15.606 -10.130 66.918  1.00 29.93  ? 374 PHE B CD1 1 
ATOM   6699 C  CD2 . PHE B 1 374 ? -17.184 -8.418  66.390  1.00 30.98  ? 374 PHE B CD2 1 
ATOM   6700 C  CE1 . PHE B 1 374 ? -14.653 -9.492  66.140  1.00 29.67  ? 374 PHE B CE1 1 
ATOM   6701 C  CE2 . PHE B 1 374 ? -16.245 -7.785  65.602  1.00 31.58  ? 374 PHE B CE2 1 
ATOM   6702 C  CZ  . PHE B 1 374 ? -14.974 -8.315  65.492  1.00 30.74  ? 374 PHE B CZ  1 
ATOM   6703 N  N   . ARG B 1 375 ? -17.278 -7.773  70.412  1.00 31.40  ? 375 ARG B N   1 
ATOM   6704 C  CA  . ARG B 1 375 ? -17.545 -6.402  70.843  1.00 31.86  ? 375 ARG B CA  1 
ATOM   6705 C  C   . ARG B 1 375 ? -16.281 -5.577  70.719  1.00 32.12  ? 375 ARG B C   1 
ATOM   6706 O  O   . ARG B 1 375 ? -15.485 -5.495  71.663  1.00 31.25  ? 375 ARG B O   1 
ATOM   6707 C  CB  . ARG B 1 375 ? -18.069 -6.366  72.280  1.00 31.10  ? 375 ARG B CB  1 
ATOM   6708 C  CG  . ARG B 1 375 ? -19.532 -6.789  72.401  1.00 36.89  ? 375 ARG B CG  1 
ATOM   6709 C  CD  . ARG B 1 375 ? -19.999 -6.807  73.871  1.00 41.49  ? 375 ARG B CD  1 
ATOM   6710 N  NE  . ARG B 1 375 ? -21.307 -7.443  73.971  1.00 44.52  ? 375 ARG B NE  1 
ATOM   6711 C  CZ  . ARG B 1 375 ? -22.423 -6.895  73.500  1.00 47.15  ? 375 ARG B CZ  1 
ATOM   6712 N  NH1 . ARG B 1 375 ? -22.420 -5.695  72.937  1.00 40.02  ? 375 ARG B NH1 1 
ATOM   6713 N  NH2 . ARG B 1 375 ? -23.573 -7.562  73.604  1.00 41.92  ? 375 ARG B NH2 1 
ATOM   6714 N  N   . PRO B 1 376 ? -16.056 -4.953  69.557  1.00 34.09  ? 376 PRO B N   1 
ATOM   6715 C  CA  . PRO B 1 376 ? -14.830 -4.163  69.383  1.00 31.99  ? 376 PRO B CA  1 
ATOM   6716 C  C   . PRO B 1 376 ? -14.698 -3.049  70.396  1.00 33.56  ? 376 PRO B C   1 
ATOM   6717 O  O   . PRO B 1 376 ? -13.575 -2.601  70.658  1.00 32.97  ? 376 PRO B O   1 
ATOM   6718 C  CB  . PRO B 1 376 ? -14.965 -3.611  67.956  1.00 29.80  ? 376 PRO B CB  1 
ATOM   6719 C  CG  . PRO B 1 376 ? -15.827 -4.663  67.247  1.00 29.42  ? 376 PRO B CG  1 
ATOM   6720 C  CD  . PRO B 1 376 ? -16.862 -4.995  68.325  1.00 29.98  ? 376 PRO B CD  1 
ATOM   6721 N  N   . GLU B 1 377 ? -15.816 -2.592  70.976  1.00 30.43  ? 377 GLU B N   1 
ATOM   6722 C  CA  . GLU B 1 377 ? -15.778 -1.525  71.974  1.00 34.18  ? 377 GLU B CA  1 
ATOM   6723 C  C   . GLU B 1 377 ? -14.901 -1.870  73.175  1.00 35.25  ? 377 GLU B C   1 
ATOM   6724 O  O   . GLU B 1 377 ? -14.478 -0.956  73.897  1.00 30.76  ? 377 GLU B O   1 
ATOM   6725 C  CB  . GLU B 1 377 ? -17.209 -1.209  72.424  1.00 38.37  ? 377 GLU B CB  1 
ATOM   6726 C  CG  . GLU B 1 377 ? -18.060 -0.545  71.322  1.00 33.68  ? 377 GLU B CG  1 
ATOM   6727 C  CD  . GLU B 1 377 ? -18.582 -1.531  70.272  1.00 33.35  ? 377 GLU B CD  1 
ATOM   6728 O  OE1 . GLU B 1 377 ? -18.560 -2.761  70.510  1.00 32.42  ? 377 GLU B OE1 1 
ATOM   6729 O  OE2 . GLU B 1 377 ? -19.033 -1.072  69.207  1.00 32.73  ? 377 GLU B OE2 1 
ATOM   6730 N  N   . ARG B 1 378 ? -14.625 -3.162  73.414  1.00 34.69  ? 378 ARG B N   1 
ATOM   6731 C  CA  . ARG B 1 378 ? -13.679 -3.540  74.468  1.00 38.49  ? 378 ARG B CA  1 
ATOM   6732 C  C   . ARG B 1 378 ? -12.343 -2.849  74.294  1.00 36.98  ? 378 ARG B C   1 
ATOM   6733 O  O   . ARG B 1 378 ? -11.572 -2.729  75.249  1.00 33.94  ? 378 ARG B O   1 
ATOM   6734 C  CB  . ARG B 1 378 ? -13.402 -5.046  74.470  1.00 37.39  ? 378 ARG B CB  1 
ATOM   6735 C  CG  . ARG B 1 378 ? -14.554 -5.944  74.691  1.00 37.60  ? 378 ARG B CG  1 
ATOM   6736 C  CD  . ARG B 1 378 ? -14.061 -7.358  74.529  1.00 32.16  ? 378 ARG B CD  1 
ATOM   6737 N  NE  . ARG B 1 378 ? -15.138 -8.221  74.093  1.00 30.39  ? 378 ARG B NE  1 
ATOM   6738 C  CZ  . ARG B 1 378 ? -16.023 -8.754  74.918  1.00 35.87  ? 378 ARG B CZ  1 
ATOM   6739 N  NH1 . ARG B 1 378 ? -15.968 -8.528  76.224  1.00 35.43  ? 378 ARG B NH1 1 
ATOM   6740 N  NH2 . ARG B 1 378 ? -16.978 -9.537  74.425  1.00 36.86  ? 378 ARG B NH2 1 
ATOM   6741 N  N   . PHE B 1 379 ? -12.012 -2.465  73.070  1.00 36.21  ? 379 PHE B N   1 
ATOM   6742 C  CA  . PHE B 1 379 ? -10.699 -1.930  72.768  1.00 35.79  ? 379 PHE B CA  1 
ATOM   6743 C  C   . PHE B 1 379 ? -10.738 -0.417  72.587  1.00 37.07  ? 379 PHE B C   1 
ATOM   6744 O  O   . PHE B 1 379 ? -9.761  0.173   72.126  1.00 35.45  ? 379 PHE B O   1 
ATOM   6745 C  CB  . PHE B 1 379 ? -10.122 -2.648  71.531  1.00 36.11  ? 379 PHE B CB  1 
ATOM   6746 C  CG  . PHE B 1 379 ? -9.663  -4.067  71.816  1.00 33.82  ? 379 PHE B CG  1 
ATOM   6747 C  CD1 . PHE B 1 379 ? -8.389  -4.316  72.315  1.00 32.73  ? 379 PHE B CD1 1 
ATOM   6748 C  CD2 . PHE B 1 379 ? -10.511 -5.145  71.610  1.00 32.89  ? 379 PHE B CD2 1 
ATOM   6749 C  CE1 . PHE B 1 379 ? -7.963  -5.610  72.601  1.00 32.15  ? 379 PHE B CE1 1 
ATOM   6750 C  CE2 . PHE B 1 379 ? -10.086 -6.457  71.893  1.00 33.48  ? 379 PHE B CE2 1 
ATOM   6751 C  CZ  . PHE B 1 379 ? -8.812  -6.683  72.390  1.00 30.06  ? 379 PHE B CZ  1 
ATOM   6752 N  N   . GLU B 1 380 ? -11.853 0.221   72.951  1.00 38.45  ? 380 GLU B N   1 
ATOM   6753 C  CA  . GLU B 1 380 ? -11.960 1.674   72.837  1.00 39.92  ? 380 GLU B CA  1 
ATOM   6754 C  C   . GLU B 1 380 ? -10.786 2.350   73.524  1.00 44.20  ? 380 GLU B C   1 
ATOM   6755 O  O   . GLU B 1 380 ? -10.169 3.276   72.983  1.00 44.05  ? 380 GLU B O   1 
ATOM   6756 C  CB  . GLU B 1 380 ? -13.256 2.139   73.485  1.00 41.99  ? 380 GLU B CB  1 
ATOM   6757 C  CG  . GLU B 1 380 ? -14.283 2.741   72.592  1.00 52.19  ? 380 GLU B CG  1 
ATOM   6758 C  CD  . GLU B 1 380 ? -15.639 2.709   73.269  1.00 51.07  ? 380 GLU B CD  1 
ATOM   6759 O  OE1 . GLU B 1 380 ? -15.650 2.711   74.522  1.00 58.01  ? 380 GLU B OE1 1 
ATOM   6760 O  OE2 . GLU B 1 380 ? -16.677 2.636   72.568  1.00 54.84  ? 380 GLU B OE2 1 
ATOM   6761 N  N   . ASN B 1 381 ? -10.471 1.880   74.727  1.00 43.44  ? 381 ASN B N   1 
ATOM   6762 C  CA  . ASN B 1 381 ? -9.434  2.443   75.591  1.00 43.01  ? 381 ASN B CA  1 
ATOM   6763 C  C   . ASN B 1 381 ? -8.323  1.424   75.795  1.00 43.33  ? 381 ASN B C   1 
ATOM   6764 O  O   . ASN B 1 381 ? -8.424  0.557   76.681  1.00 40.62  ? 381 ASN B O   1 
ATOM   6765 C  CB  . ASN B 1 381 ? -10.063 2.856   76.924  1.00 46.06  ? 381 ASN B CB  1 
ATOM   6766 C  CG  . ASN B 1 381 ? -9.082  3.526   77.859  1.00 49.05  ? 381 ASN B CG  1 
ATOM   6767 O  OD1 . ASN B 1 381 ? -8.011  3.968   77.444  1.00 54.42  ? 381 ASN B OD1 1 
ATOM   6768 N  ND2 . ASN B 1 381 ? -9.459  3.622   79.138  1.00 49.51  ? 381 ASN B ND2 1 
ATOM   6769 N  N   . PRO B 1 382 ? -7.253  1.480   74.998  1.00 45.22  ? 382 PRO B N   1 
ATOM   6770 C  CA  . PRO B 1 382 ? -6.194  0.472   75.119  1.00 45.17  ? 382 PRO B CA  1 
ATOM   6771 C  C   . PRO B 1 382 ? -5.623  0.386   76.514  1.00 44.39  ? 382 PRO B C   1 
ATOM   6772 O  O   . PRO B 1 382 ? -5.207  -0.697  76.941  1.00 44.81  ? 382 PRO B O   1 
ATOM   6773 C  CB  . PRO B 1 382 ? -5.131  0.950   74.118  1.00 45.74  ? 382 PRO B CB  1 
ATOM   6774 C  CG  . PRO B 1 382 ? -5.824  1.909   73.231  1.00 47.66  ? 382 PRO B CG  1 
ATOM   6775 C  CD  . PRO B 1 382 ? -6.960  2.495   73.973  1.00 46.74  ? 382 PRO B CD  1 
ATOM   6776 N  N   . SER B 1 383 ? -5.609  1.500   77.244  1.00 48.21  ? 383 SER B N   1 
ATOM   6777 C  CA  . SER B 1 383 ? -4.987  1.530   78.562  1.00 48.72  ? 383 SER B CA  1 
ATOM   6778 C  C   . SER B 1 383 ? -5.761  0.709   79.579  1.00 45.59  ? 383 SER B C   1 
ATOM   6779 O  O   . SER B 1 383 ? -5.210  0.373   80.628  1.00 43.36  ? 383 SER B O   1 
ATOM   6780 C  CB  . SER B 1 383 ? -4.854  2.976   79.052  1.00 43.15  ? 383 SER B CB  1 
ATOM   6781 O  OG  . SER B 1 383 ? -6.125  3.511   79.348  1.00 49.19  ? 383 SER B OG  1 
ATOM   6782 N  N   . ALA B 1 384 ? -7.015  0.371   79.292  1.00 45.10  ? 384 ALA B N   1 
ATOM   6783 C  CA  . ALA B 1 384 ? -7.800  -0.453  80.200  1.00 43.82  ? 384 ALA B CA  1 
ATOM   6784 C  C   . ALA B 1 384 ? -7.488  -1.946  80.090  1.00 41.59  ? 384 ALA B C   1 
ATOM   6785 O  O   . ALA B 1 384 ? -7.977  -2.722  80.919  1.00 40.99  ? 384 ALA B O   1 
ATOM   6786 C  CB  . ALA B 1 384 ? -9.287  -0.215  79.951  1.00 40.47  ? 384 ALA B CB  1 
ATOM   6787 N  N   . ILE B 1 385 ? -6.709  -2.372  79.099  1.00 40.35  ? 385 ILE B N   1 
ATOM   6788 C  CA  . ILE B 1 385 ? -6.317  -3.777  78.963  1.00 41.79  ? 385 ILE B CA  1 
ATOM   6789 C  C   . ILE B 1 385 ? -5.159  -4.056  79.913  1.00 40.57  ? 385 ILE B C   1 
ATOM   6790 O  O   . ILE B 1 385 ? -4.079  -3.481  79.724  1.00 42.05  ? 385 ILE B O   1 
ATOM   6791 C  CB  . ILE B 1 385 ? -5.898  -4.118  77.520  1.00 42.35  ? 385 ILE B CB  1 
ATOM   6792 C  CG1 . ILE B 1 385 ? -6.865  -3.530  76.484  1.00 40.44  ? 385 ILE B CG1 1 
ATOM   6793 C  CG2 . ILE B 1 385 ? -5.739  -5.635  77.353  1.00 44.18  ? 385 ILE B CG2 1 
ATOM   6794 C  CD1 . ILE B 1 385 ? -8.234  -4.160  76.470  1.00 44.66  ? 385 ILE B CD1 1 
ATOM   6795 N  N   . PRO B 1 386 ? -5.311  -4.921  80.927  1.00 42.87  ? 386 PRO B N   1 
ATOM   6796 C  CA  . PRO B 1 386 ? -4.167  -5.231  81.798  1.00 41.45  ? 386 PRO B CA  1 
ATOM   6797 C  C   . PRO B 1 386 ? -2.997  -5.792  81.000  1.00 40.29  ? 386 PRO B C   1 
ATOM   6798 O  O   . PRO B 1 386 ? -3.173  -6.396  79.943  1.00 36.84  ? 386 PRO B O   1 
ATOM   6799 C  CB  . PRO B 1 386 ? -4.728  -6.281  82.769  1.00 40.31  ? 386 PRO B CB  1 
ATOM   6800 C  CG  . PRO B 1 386 ? -6.201  -6.073  82.735  1.00 39.15  ? 386 PRO B CG  1 
ATOM   6801 C  CD  . PRO B 1 386 ? -6.510  -5.675  81.315  1.00 40.17  ? 386 PRO B CD  1 
ATOM   6802 N  N   . GLN B 1 387 ? -1.791  -5.608  81.538  1.00 40.88  ? 387 GLN B N   1 
ATOM   6803 C  CA  . GLN B 1 387 ? -0.599  -6.144  80.898  1.00 42.89  ? 387 GLN B CA  1 
ATOM   6804 C  C   . GLN B 1 387 ? -0.702  -7.664  80.802  1.00 38.75  ? 387 GLN B C   1 
ATOM   6805 O  O   . GLN B 1 387 ? -1.129  -8.333  81.744  1.00 33.18  ? 387 GLN B O   1 
ATOM   6806 C  CB  . GLN B 1 387 ? 0.654   -5.746  81.694  1.00 41.56  ? 387 GLN B CB  1 
ATOM   6807 C  CG  . GLN B 1 387 ? 1.981   -6.263  81.133  1.00 45.87  ? 387 GLN B CG  1 
ATOM   6808 C  CD  . GLN B 1 387 ? 3.209   -5.806  81.949  1.00 49.91  ? 387 GLN B CD  1 
ATOM   6809 O  OE1 . GLN B 1 387 ? 3.111   -5.559  83.146  1.00 56.21  ? 387 GLN B OE1 1 
ATOM   6810 N  NE2 . GLN B 1 387 ? 4.357   -5.687  81.291  1.00 52.00  ? 387 GLN B NE2 1 
ATOM   6811 N  N   . HIS B 1 388 ? -0.303  -8.206  79.650  1.00 34.82  ? 388 HIS B N   1 
ATOM   6812 C  CA  . HIS B 1 388 ? -0.242  -9.643  79.400  1.00 35.83  ? 388 HIS B CA  1 
ATOM   6813 C  C   . HIS B 1 388 ? -1.618  -10.290 79.369  1.00 32.78  ? 388 HIS B C   1 
ATOM   6814 O  O   . HIS B 1 388 ? -1.727  -11.502 79.518  1.00 35.45  ? 388 HIS B O   1 
ATOM   6815 C  CB  . HIS B 1 388 ? 0.626   -10.382 80.428  1.00 38.90  ? 388 HIS B CB  1 
ATOM   6816 C  CG  . HIS B 1 388 ? 2.029   -9.870  80.519  1.00 41.08  ? 388 HIS B CG  1 
ATOM   6817 N  ND1 . HIS B 1 388 ? 2.772   -9.539  79.407  1.00 41.25  ? 388 HIS B ND1 1 
ATOM   6818 C  CD2 . HIS B 1 388 ? 2.833   -9.658  81.588  1.00 43.68  ? 388 HIS B CD2 1 
ATOM   6819 C  CE1 . HIS B 1 388 ? 3.970   -9.131  79.788  1.00 46.37  ? 388 HIS B CE1 1 
ATOM   6820 N  NE2 . HIS B 1 388 ? 4.031   -9.191  81.106  1.00 45.21  ? 388 HIS B NE2 1 
ATOM   6821 N  N   . ALA B 1 389 ? -2.676  -9.501  79.194  1.00 33.46  ? 389 ALA B N   1 
ATOM   6822 C  CA  . ALA B 1 389 ? -4.016  -10.049 79.024  1.00 36.38  ? 389 ALA B CA  1 
ATOM   6823 C  C   . ALA B 1 389 ? -4.364  -10.326 77.568  1.00 33.92  ? 389 ALA B C   1 
ATOM   6824 O  O   . ALA B 1 389 ? -5.238  -11.162 77.304  1.00 35.15  ? 389 ALA B O   1 
ATOM   6825 C  CB  . ALA B 1 389 ? -5.067  -9.090  79.580  1.00 33.37  ? 389 ALA B CB  1 
ATOM   6826 N  N   . PHE B 1 390 ? -3.709  -9.640  76.640  1.00 29.69  ? 390 PHE B N   1 
ATOM   6827 C  CA  . PHE B 1 390 ? -4.021  -9.682  75.205  1.00 30.70  ? 390 PHE B CA  1 
ATOM   6828 C  C   . PHE B 1 390 ? -2.698  -9.914  74.476  1.00 31.08  ? 390 PHE B C   1 
ATOM   6829 O  O   . PHE B 1 390 ? -1.887  -8.988  74.373  1.00 31.19  ? 390 PHE B O   1 
ATOM   6830 C  CB  . PHE B 1 390 ? -4.695  -8.369  74.789  1.00 32.65  ? 390 PHE B CB  1 
ATOM   6831 C  CG  . PHE B 1 390 ? -5.052  -8.287  73.330  1.00 33.61  ? 390 PHE B CG  1 
ATOM   6832 C  CD1 . PHE B 1 390 ? -5.966  -9.158  72.780  1.00 31.76  ? 390 PHE B CD1 1 
ATOM   6833 C  CD2 . PHE B 1 390 ? -4.476  -7.323  72.518  1.00 33.42  ? 390 PHE B CD2 1 
ATOM   6834 C  CE1 . PHE B 1 390 ? -6.303  -9.072  71.428  1.00 33.97  ? 390 PHE B CE1 1 
ATOM   6835 C  CE2 . PHE B 1 390 ? -4.802  -7.233  71.180  1.00 34.33  ? 390 PHE B CE2 1 
ATOM   6836 C  CZ  . PHE B 1 390 ? -5.722  -8.112  70.633  1.00 33.61  ? 390 PHE B CZ  1 
ATOM   6837 N  N   . LYS B 1 391 ? -2.456  -11.150 73.996  1.00 32.26  ? 391 LYS B N   1 
ATOM   6838 C  CA  . LYS B 1 391 ? -1.124  -11.555 73.516  1.00 32.83  ? 391 LYS B CA  1 
ATOM   6839 C  C   . LYS B 1 391 ? -1.159  -12.260 72.158  1.00 31.66  ? 391 LYS B C   1 
ATOM   6840 O  O   . LYS B 1 391 ? -0.504  -13.283 71.957  1.00 29.52  ? 391 LYS B O   1 
ATOM   6841 C  CB  . LYS B 1 391 ? -0.473  -12.464 74.546  1.00 29.78  ? 391 LYS B CB  1 
ATOM   6842 C  CG  . LYS B 1 391 ? -0.485  -11.892 75.967  1.00 32.84  ? 391 LYS B CG  1 
ATOM   6843 C  CD  . LYS B 1 391 ? 0.456   -10.732 76.033  1.00 36.12  ? 391 LYS B CD  1 
ATOM   6844 C  CE  . LYS B 1 391 ? 1.885   -11.232 76.215  1.00 37.76  ? 391 LYS B CE  1 
ATOM   6845 N  NZ  . LYS B 1 391 ? 2.835   -10.084 76.232  1.00 37.79  ? 391 LYS B NZ  1 
ATOM   6846 N  N   . PRO B 1 392 ? -1.906  -11.736 71.188  1.00 31.66  ? 392 PRO B N   1 
ATOM   6847 C  CA  . PRO B 1 392 ? -1.950  -12.418 69.889  1.00 28.75  ? 392 PRO B CA  1 
ATOM   6848 C  C   . PRO B 1 392 ? -0.637  -12.325 69.131  1.00 32.10  ? 392 PRO B C   1 
ATOM   6849 O  O   . PRO B 1 392 ? -0.489  -13.026 68.134  1.00 31.12  ? 392 PRO B O   1 
ATOM   6850 C  CB  . PRO B 1 392 ? -3.077  -11.689 69.143  1.00 32.13  ? 392 PRO B CB  1 
ATOM   6851 C  CG  . PRO B 1 392 ? -2.964  -10.293 69.684  1.00 33.71  ? 392 PRO B CG  1 
ATOM   6852 C  CD  . PRO B 1 392 ? -2.659  -10.470 71.171  1.00 29.54  ? 392 PRO B CD  1 
ATOM   6853 N  N   . HIS B 1 393 ? 0.306   -11.479 69.561  1.00 31.12  ? 393 HIS B N   1 
ATOM   6854 C  CA  . HIS B 1 393 ? 1.590   -11.324 68.877  1.00 30.70  ? 393 HIS B CA  1 
ATOM   6855 C  C   . HIS B 1 393 ? 2.759   -11.771 69.747  1.00 33.14  ? 393 HIS B C   1 
ATOM   6856 O  O   . HIS B 1 393 ? 3.919   -11.417 69.467  1.00 32.23  ? 393 HIS B O   1 
ATOM   6857 C  CB  . HIS B 1 393 ? 1.775   -9.878  68.417  1.00 34.02  ? 393 HIS B CB  1 
ATOM   6858 C  CG  . HIS B 1 393 ? 0.833   -9.486  67.319  1.00 36.50  ? 393 HIS B CG  1 
ATOM   6859 N  ND1 . HIS B 1 393 ? 0.995   -9.890  66.009  1.00 38.19  ? 393 HIS B ND1 1 
ATOM   6860 C  CD2 . HIS B 1 393 ? -0.312  -8.767  67.352  1.00 34.05  ? 393 HIS B CD2 1 
ATOM   6861 C  CE1 . HIS B 1 393 ? 0.007   -9.406  65.276  1.00 36.49  ? 393 HIS B CE1 1 
ATOM   6862 N  NE2 . HIS B 1 393 ? -0.797  -8.717  66.068  1.00 42.96  ? 393 HIS B NE2 1 
ATOM   6863 N  N   . GLY B 1 394 ? 2.478   -12.569 70.775  1.00 30.28  ? 394 GLY B N   1 
ATOM   6864 C  CA  . GLY B 1 394 ? 3.535   -13.155 71.571  1.00 33.14  ? 394 GLY B CA  1 
ATOM   6865 C  C   . GLY B 1 394 ? 4.022   -12.177 72.626  1.00 33.71  ? 394 GLY B C   1 
ATOM   6866 O  O   . GLY B 1 394 ? 3.316   -11.248 73.014  1.00 31.07  ? 394 GLY B O   1 
ATOM   6867 N  N   . ASN B 1 395 ? 5.268   -12.367 73.063  1.00 29.22  ? 395 ASN B N   1 
ATOM   6868 C  CA  . ASN B 1 395 ? 5.705   -11.696 74.276  1.00 30.67  ? 395 ASN B CA  1 
ATOM   6869 C  C   . ASN B 1 395 ? 7.144   -11.232 74.155  1.00 31.46  ? 395 ASN B C   1 
ATOM   6870 O  O   . ASN B 1 395 ? 7.992   -11.969 73.651  1.00 29.81  ? 395 ASN B O   1 
ATOM   6871 C  CB  . ASN B 1 395 ? 5.608   -12.613 75.483  1.00 30.95  ? 395 ASN B CB  1 
ATOM   6872 C  CG  . ASN B 1 395 ? 5.998   -11.912 76.758  1.00 34.92  ? 395 ASN B CG  1 
ATOM   6873 O  OD1 . ASN B 1 395 ? 5.336   -10.955 77.171  1.00 35.77  ? 395 ASN B OD1 1 
ATOM   6874 N  ND2 . ASN B 1 395 ? 7.080   -12.367 77.382  1.00 32.63  ? 395 ASN B ND2 1 
ATOM   6875 N  N   . GLY B 1 396 ? 7.395   -10.012 74.634  1.00 31.06  ? 396 GLY B N   1 
ATOM   6876 C  CA  . GLY B 1 396 ? 8.735   -9.551  74.954  1.00 34.96  ? 396 GLY B CA  1 
ATOM   6877 C  C   . GLY B 1 396 ? 9.608   -9.416  73.721  1.00 31.60  ? 396 GLY B C   1 
ATOM   6878 O  O   . GLY B 1 396 ? 9.143   -9.114  72.616  1.00 30.79  ? 396 GLY B O   1 
ATOM   6879 N  N   . GLN B 1 397 ? 10.902  -9.677  73.906  1.00 30.12  ? 397 GLN B N   1 
ATOM   6880 C  CA  . GLN B 1 397 ? 11.819  -9.546  72.777  1.00 31.96  ? 397 GLN B CA  1 
ATOM   6881 C  C   . GLN B 1 397 ? 11.552  -10.566 71.677  1.00 30.93  ? 397 GLN B C   1 
ATOM   6882 O  O   . GLN B 1 397 ? 12.013  -10.369 70.542  1.00 31.72  ? 397 GLN B O   1 
ATOM   6883 C  CB  . GLN B 1 397 ? 13.276  -9.657  73.251  1.00 33.34  ? 397 GLN B CB  1 
ATOM   6884 C  CG  . GLN B 1 397 ? 13.734  -11.074 73.676  1.00 33.56  ? 397 GLN B CG  1 
ATOM   6885 C  CD  . GLN B 1 397 ? 15.157  -11.056 74.231  1.00 36.48  ? 397 GLN B CD  1 
ATOM   6886 O  OE1 . GLN B 1 397 ? 15.955  -10.198 73.861  1.00 38.36  ? 397 GLN B OE1 1 
ATOM   6887 N  NE2 . GLN B 1 397 ? 15.470  -11.988 75.128  1.00 33.75  ? 397 GLN B NE2 1 
ATOM   6888 N  N   . ARG B 1 398 ? 10.850  -11.654 71.986  1.00 30.27  ? 398 ARG B N   1 
ATOM   6889 C  CA  . ARG B 1 398 ? 10.461  -12.648 70.993  1.00 32.58  ? 398 ARG B CA  1 
ATOM   6890 C  C   . ARG B 1 398 ? 9.033   -12.442 70.505  1.00 29.07  ? 398 ARG B C   1 
ATOM   6891 O  O   . ARG B 1 398 ? 8.445   -13.364 69.927  1.00 32.54  ? 398 ARG B O   1 
ATOM   6892 C  CB  . ARG B 1 398 ? 10.616  -14.068 71.553  1.00 33.81  ? 398 ARG B CB  1 
ATOM   6893 C  CG  . ARG B 1 398 ? 12.043  -14.447 71.991  1.00 30.74  ? 398 ARG B CG  1 
ATOM   6894 C  CD  . ARG B 1 398 ? 13.063  -14.155 70.887  1.00 31.46  ? 398 ARG B CD  1 
ATOM   6895 N  NE  . ARG B 1 398 ? 12.811  -14.875 69.636  1.00 32.81  ? 398 ARG B NE  1 
ATOM   6896 C  CZ  . ARG B 1 398 ? 13.222  -16.111 69.367  1.00 30.62  ? 398 ARG B CZ  1 
ATOM   6897 N  NH1 . ARG B 1 398 ? 13.835  -16.852 70.275  1.00 30.50  ? 398 ARG B NH1 1 
ATOM   6898 N  NH2 . ARG B 1 398 ? 13.033  -16.607 68.144  1.00 28.93  ? 398 ARG B NH2 1 
ATOM   6899 N  N   . ALA B 1 399 ? 8.469   -11.255 70.713  1.00 29.82  ? 399 ALA B N   1 
ATOM   6900 C  CA  . ALA B 1 399 ? 7.153   -10.942 70.162  1.00 31.09  ? 399 ALA B CA  1 
ATOM   6901 C  C   . ALA B 1 399 ? 7.223   -10.819 68.634  1.00 33.10  ? 399 ALA B C   1 
ATOM   6902 O  O   . ALA B 1 399 ? 8.294   -10.778 68.026  1.00 30.45  ? 399 ALA B O   1 
ATOM   6903 C  CB  . ALA B 1 399 ? 6.604   -9.654  70.789  1.00 26.21  ? 399 ALA B CB  1 
ATOM   6904 N  N   . CYS B 1 400 ? 6.054   -10.720 68.011  1.00 27.37  ? 400 CYS B N   1 
ATOM   6905 C  CA  . CYS B 1 400 ? 5.968   -10.737 66.557  1.00 28.57  ? 400 CYS B CA  1 
ATOM   6906 C  C   . CYS B 1 400 ? 6.635   -9.500  65.971  1.00 30.87  ? 400 CYS B C   1 
ATOM   6907 O  O   . CYS B 1 400 ? 6.152   -8.384  66.187  1.00 31.47  ? 400 CYS B O   1 
ATOM   6908 C  CB  . CYS B 1 400 ? 4.496   -10.797 66.118  1.00 29.96  ? 400 CYS B CB  1 
ATOM   6909 S  SG  . CYS B 1 400 ? 4.322   -10.721 64.309  1.00 32.49  ? 400 CYS B SG  1 
ATOM   6910 N  N   . ILE B 1 401 ? 7.733   -9.668  65.225  1.00 31.05  ? 401 ILE B N   1 
ATOM   6911 C  CA  . ILE B 1 401 ? 8.367   -8.489  64.656  1.00 31.09  ? 401 ILE B CA  1 
ATOM   6912 C  C   . ILE B 1 401 ? 7.480   -7.882  63.576  1.00 32.68  ? 401 ILE B C   1 
ATOM   6913 O  O   . ILE B 1 401 ? 7.588   -6.686  63.288  1.00 32.01  ? 401 ILE B O   1 
ATOM   6914 C  CB  . ILE B 1 401 ? 9.773   -8.819  64.106  1.00 31.00  ? 401 ILE B CB  1 
ATOM   6915 C  CG1 . ILE B 1 401 ? 10.550  -7.540  63.782  1.00 34.94  ? 401 ILE B CG1 1 
ATOM   6916 C  CG2 . ILE B 1 401 ? 9.681   -9.649  62.823  1.00 31.21  ? 401 ILE B CG2 1 
ATOM   6917 C  CD1 . ILE B 1 401 ? 12.035  -7.814  63.408  1.00 31.76  ? 401 ILE B CD1 1 
ATOM   6918 N  N   . GLY B 1 402 ? 6.573   -8.669  63.004  1.00 35.67  ? 402 GLY B N   1 
ATOM   6919 C  CA  . GLY B 1 402 ? 5.708   -8.179  61.943  1.00 30.14  ? 402 GLY B CA  1 
ATOM   6920 C  C   . GLY B 1 402 ? 4.410   -7.578  62.440  1.00 33.37  ? 402 GLY B C   1 
ATOM   6921 O  O   . GLY B 1 402 ? 3.488   -7.375  61.646  1.00 29.63  ? 402 GLY B O   1 
ATOM   6922 N  N   . GLN B 1 403 ? 4.325   -7.250  63.736  1.00 31.70  ? 403 GLN B N   1 
ATOM   6923 C  CA  . GLN B 1 403 ? 3.038   -6.825  64.294  1.00 33.46  ? 403 GLN B CA  1 
ATOM   6924 C  C   . GLN B 1 403 ? 2.507   -5.564  63.608  1.00 32.24  ? 403 GLN B C   1 
ATOM   6925 O  O   . GLN B 1 403 ? 1.337   -5.519  63.189  1.00 32.39  ? 403 GLN B O   1 
ATOM   6926 C  CB  . GLN B 1 403 ? 3.146   -6.627  65.813  1.00 34.05  ? 403 GLN B CB  1 
ATOM   6927 C  CG  . GLN B 1 403 ? 1.788   -6.267  66.446  1.00 38.02  ? 403 GLN B CG  1 
ATOM   6928 C  CD  . GLN B 1 403 ? 1.905   -5.840  67.912  1.00 46.65  ? 403 GLN B CD  1 
ATOM   6929 O  OE1 . GLN B 1 403 ? 2.733   -6.368  68.649  1.00 43.20  ? 403 GLN B OE1 1 
ATOM   6930 N  NE2 . GLN B 1 403 ? 1.128   -4.836  68.311  1.00 44.49  ? 403 GLN B NE2 1 
ATOM   6931 N  N   . GLN B 1 404 ? 3.351   -4.533  63.472  1.00 32.44  ? 404 GLN B N   1 
ATOM   6932 C  CA  . GLN B 1 404 ? 2.910   -3.289  62.836  1.00 35.28  ? 404 GLN B CA  1 
ATOM   6933 C  C   . GLN B 1 404 ? 2.525   -3.536  61.392  1.00 31.76  ? 404 GLN B C   1 
ATOM   6934 O  O   . GLN B 1 404 ? 1.537   -2.975  60.898  1.00 31.21  ? 404 GLN B O   1 
ATOM   6935 C  CB  . GLN B 1 404 ? 4.009   -2.222  62.842  1.00 40.79  ? 404 GLN B CB  1 
ATOM   6936 C  CG  . GLN B 1 404 ? 4.179   -1.454  64.118  1.00 44.24  ? 404 GLN B CG  1 
ATOM   6937 C  CD  . GLN B 1 404 ? 4.372   -2.381  65.256  1.00 50.21  ? 404 GLN B CD  1 
ATOM   6938 O  OE1 . GLN B 1 404 ? 5.507   -2.703  65.610  1.00 59.17  ? 404 GLN B OE1 1 
ATOM   6939 N  NE2 . GLN B 1 404 ? 3.270   -2.864  65.826  1.00 54.61  ? 404 GLN B NE2 1 
ATOM   6940 N  N   . PHE B 1 405 ? 3.351   -4.317  60.686  1.00 31.61  ? 405 PHE B N   1 
ATOM   6941 C  CA  . PHE B 1 405 ? 3.097   -4.639  59.288  1.00 30.71  ? 405 PHE B CA  1 
ATOM   6942 C  C   . PHE B 1 405 ? 1.728   -5.275  59.134  1.00 30.59  ? 405 PHE B C   1 
ATOM   6943 O  O   . PHE B 1 405 ? 0.914   -4.845  58.309  1.00 30.81  ? 405 PHE B O   1 
ATOM   6944 C  CB  . PHE B 1 405 ? 4.217   -5.562  58.784  1.00 31.10  ? 405 PHE B CB  1 
ATOM   6945 C  CG  . PHE B 1 405 ? 4.220   -5.804  57.290  1.00 32.65  ? 405 PHE B CG  1 
ATOM   6946 C  CD1 . PHE B 1 405 ? 3.347   -6.737  56.720  1.00 29.40  ? 405 PHE B CD1 1 
ATOM   6947 C  CD2 . PHE B 1 405 ? 5.127   -5.145  56.463  1.00 30.43  ? 405 PHE B CD2 1 
ATOM   6948 C  CE1 . PHE B 1 405 ? 3.346   -6.987  55.328  1.00 30.10  ? 405 PHE B CE1 1 
ATOM   6949 C  CE2 . PHE B 1 405 ? 5.143   -5.377  55.068  1.00 34.45  ? 405 PHE B CE2 1 
ATOM   6950 C  CZ  . PHE B 1 405 ? 4.245   -6.301  54.498  1.00 34.50  ? 405 PHE B CZ  1 
ATOM   6951 N  N   . ALA B 1 406 ? 1.459   -6.304  59.935  1.00 30.95  ? 406 ALA B N   1 
ATOM   6952 C  CA  . ALA B 1 406 ? 0.195   -7.025  59.829  1.00 31.27  ? 406 ALA B CA  1 
ATOM   6953 C  C   . ALA B 1 406 ? -0.988  -6.104  60.088  1.00 33.11  ? 406 ALA B C   1 
ATOM   6954 O  O   . ALA B 1 406 ? -1.999  -6.175  59.382  1.00 31.26  ? 406 ALA B O   1 
ATOM   6955 C  CB  . ALA B 1 406 ? 0.168   -8.196  60.814  1.00 32.91  ? 406 ALA B CB  1 
ATOM   6956 N  N   . LEU B 1 407 ? -0.904  -5.262  61.117  1.00 33.86  ? 407 LEU B N   1 
ATOM   6957 C  CA  . LEU B 1 407 ? -2.071  -4.448  61.473  1.00 29.19  ? 407 LEU B CA  1 
ATOM   6958 C  C   . LEU B 1 407 ? -2.259  -3.301  60.484  1.00 32.10  ? 407 LEU B C   1 
ATOM   6959 O  O   . LEU B 1 407 ? -3.393  -2.921  60.179  1.00 34.46  ? 407 LEU B O   1 
ATOM   6960 C  CB  . LEU B 1 407 ? -1.929  -3.943  62.915  1.00 36.86  ? 407 LEU B CB  1 
ATOM   6961 C  CG  . LEU B 1 407 ? -2.030  -5.068  63.979  1.00 38.73  ? 407 LEU B CG  1 
ATOM   6962 C  CD1 . LEU B 1 407 ? -1.995  -4.548  65.429  1.00 43.50  ? 407 LEU B CD1 1 
ATOM   6963 C  CD2 . LEU B 1 407 ? -3.233  -5.980  63.757  1.00 41.67  ? 407 LEU B CD2 1 
ATOM   6964 N  N   . HIS B 1 408 ? -1.175  -2.773  59.908  1.00 31.68  ? 408 HIS B N   1 
ATOM   6965 C  CA  . HIS B 1 408 ? -1.367  -1.770  58.870  1.00 31.56  ? 408 HIS B CA  1 
ATOM   6966 C  C   . HIS B 1 408 ? -2.010  -2.385  57.631  1.00 31.32  ? 408 HIS B C   1 
ATOM   6967 O  O   . HIS B 1 408 ? -2.947  -1.811  57.059  1.00 32.30  ? 408 HIS B O   1 
ATOM   6968 C  CB  . HIS B 1 408 ? -0.040  -1.102  58.498  1.00 33.12  ? 408 HIS B CB  1 
ATOM   6969 C  CG  . HIS B 1 408 ? -0.211  0.140   57.676  1.00 34.68  ? 408 HIS B CG  1 
ATOM   6970 N  ND1 . HIS B 1 408 ? -0.574  1.350   58.228  1.00 35.30  ? 408 HIS B ND1 1 
ATOM   6971 C  CD2 . HIS B 1 408 ? -0.106  0.352   56.343  1.00 33.84  ? 408 HIS B CD2 1 
ATOM   6972 C  CE1 . HIS B 1 408 ? -0.664  2.258   57.273  1.00 35.54  ? 408 HIS B CE1 1 
ATOM   6973 N  NE2 . HIS B 1 408 ? -0.385  1.679   56.117  1.00 35.15  ? 408 HIS B NE2 1 
ATOM   6974 N  N   . GLU B 1 409 ? -1.526  -3.556  57.205  1.00 30.57  ? 409 GLU B N   1 
ATOM   6975 C  CA  . GLU B 1 409 ? -2.096  -4.175  56.011  1.00 32.28  ? 409 GLU B CA  1 
ATOM   6976 C  C   . GLU B 1 409 ? -3.546  -4.590  56.256  1.00 32.98  ? 409 GLU B C   1 
ATOM   6977 O  O   . GLU B 1 409 ? -4.414  -4.362  55.405  1.00 32.44  ? 409 GLU B O   1 
ATOM   6978 C  CB  . GLU B 1 409 ? -1.240  -5.367  55.567  1.00 30.82  ? 409 GLU B CB  1 
ATOM   6979 C  CG  . GLU B 1 409 ? -1.854  -6.047  54.329  1.00 42.64  ? 409 GLU B CG  1 
ATOM   6980 C  CD  . GLU B 1 409 ? -1.267  -7.407  54.003  1.00 42.48  ? 409 GLU B CD  1 
ATOM   6981 O  OE1 . GLU B 1 409 ? -0.459  -7.939  54.811  1.00 42.33  ? 409 GLU B OE1 1 
ATOM   6982 O  OE2 . GLU B 1 409 ? -1.601  -7.924  52.905  1.00 35.26  ? 409 GLU B OE2 1 
ATOM   6983 N  N   . ALA B 1 410 ? -3.837  -5.171  57.425  1.00 31.11  ? 410 ALA B N   1 
ATOM   6984 C  CA  . ALA B 1 410 ? -5.218  -5.585  57.694  1.00 30.95  ? 410 ALA B CA  1 
ATOM   6985 C  C   . ALA B 1 410 ? -6.149  -4.383  57.834  1.00 32.46  ? 410 ALA B C   1 
ATOM   6986 O  O   . ALA B 1 410 ? -7.305  -4.442  57.394  1.00 33.21  ? 410 ALA B O   1 
ATOM   6987 C  CB  . ALA B 1 410 ? -5.282  -6.472  58.941  1.00 26.19  ? 410 ALA B CB  1 
ATOM   6988 N  N   . THR B 1 411 ? -5.678  -3.283  58.445  1.00 29.65  ? 411 THR B N   1 
ATOM   6989 C  CA  . THR B 1 411 ? -6.520  -2.086  58.575  1.00 30.59  ? 411 THR B CA  1 
ATOM   6990 C  C   . THR B 1 411 ? -6.756  -1.438  57.212  1.00 33.51  ? 411 THR B C   1 
ATOM   6991 O  O   . THR B 1 411 ? -7.894  -1.077  56.870  1.00 31.23  ? 411 THR B O   1 
ATOM   6992 C  CB  . THR B 1 411 ? -5.887  -1.088  59.565  1.00 30.40  ? 411 THR B CB  1 
ATOM   6993 O  OG1 . THR B 1 411 ? -5.703  -1.727  60.836  1.00 32.22  ? 411 THR B OG1 1 
ATOM   6994 C  CG2 . THR B 1 411 ? -6.769  0.160   59.761  1.00 30.15  ? 411 THR B CG2 1 
ATOM   6995 N  N   . LEU B 1 412 ? -5.708  -1.347  56.389  1.00 31.08  ? 412 LEU B N   1 
ATOM   6996 C  CA  . LEU B 1 412 ? -5.883  -0.807  55.041  1.00 32.01  ? 412 LEU B CA  1 
ATOM   6997 C  C   . LEU B 1 412 ? -6.914  -1.608  54.250  1.00 32.63  ? 412 LEU B C   1 
ATOM   6998 O  O   . LEU B 1 412 ? -7.877  -1.047  53.707  1.00 33.89  ? 412 LEU B O   1 
ATOM   6999 C  CB  . LEU B 1 412 ? -4.547  -0.805  54.309  1.00 28.19  ? 412 LEU B CB  1 
ATOM   7000 C  CG  . LEU B 1 412 ? -4.624  -0.594  52.792  1.00 30.97  ? 412 LEU B CG  1 
ATOM   7001 C  CD1 . LEU B 1 412 ? -4.983  0.842   52.484  1.00 32.57  ? 412 LEU B CD1 1 
ATOM   7002 C  CD2 . LEU B 1 412 ? -3.277  -0.954  52.154  1.00 36.17  ? 412 LEU B CD2 1 
ATOM   7003 N  N   . VAL B 1 413 ? -6.724  -2.928  54.180  1.00 33.94  ? 413 VAL B N   1 
ATOM   7004 C  CA  . VAL B 1 413 ? -7.542  -3.786  53.325  1.00 30.77  ? 413 VAL B CA  1 
ATOM   7005 C  C   . VAL B 1 413 ? -8.978  -3.853  53.836  1.00 33.16  ? 413 VAL B C   1 
ATOM   7006 O  O   . VAL B 1 413 ? -9.936  -3.772  53.060  1.00 31.91  ? 413 VAL B O   1 
ATOM   7007 C  CB  . VAL B 1 413 ? -6.908  -5.191  53.245  1.00 33.33  ? 413 VAL B CB  1 
ATOM   7008 C  CG1 . VAL B 1 413 ? -7.850  -6.181  52.587  1.00 39.53  ? 413 VAL B CG1 1 
ATOM   7009 C  CG2 . VAL B 1 413 ? -5.576  -5.122  52.479  1.00 37.92  ? 413 VAL B CG2 1 
ATOM   7010 N  N   . LEU B 1 414 ? -9.148  -4.051  55.141  1.00 29.60  ? 414 LEU B N   1 
ATOM   7011 C  CA  . LEU B 1 414 ? -10.504 -4.119  55.690  1.00 31.95  ? 414 LEU B CA  1 
ATOM   7012 C  C   . LEU B 1 414 ? -11.226 -2.790  55.509  1.00 31.11  ? 414 LEU B C   1 
ATOM   7013 O  O   . LEU B 1 414 ? -12.433 -2.761  55.205  1.00 32.31  ? 414 LEU B O   1 
ATOM   7014 C  CB  . LEU B 1 414 ? -10.451 -4.518  57.164  1.00 31.96  ? 414 LEU B CB  1 
ATOM   7015 C  CG  . LEU B 1 414 ? -11.808 -4.781  57.848  1.00 31.07  ? 414 LEU B CG  1 
ATOM   7016 C  CD1 . LEU B 1 414 ? -12.639 -5.767  57.028  1.00 34.56  ? 414 LEU B CD1 1 
ATOM   7017 C  CD2 . LEU B 1 414 ? -11.570 -5.296  59.253  1.00 28.40  ? 414 LEU B CD2 1 
ATOM   7018 N  N   . GLY B 1 415 ? -10.505 -1.675  55.675  1.00 31.33  ? 415 GLY B N   1 
ATOM   7019 C  CA  . GLY B 1 415 ? -11.118 -0.374  55.427  1.00 33.30  ? 415 GLY B CA  1 
ATOM   7020 C  C   . GLY B 1 415 ? -11.593 -0.229  53.992  1.00 31.41  ? 415 GLY B C   1 
ATOM   7021 O  O   . GLY B 1 415 ? -12.714 0.232   53.730  1.00 29.59  ? 415 GLY B O   1 
ATOM   7022 N  N   . MET B 1 416 ? -10.739 -0.611  53.035  1.00 29.52  ? 416 MET B N   1 
ATOM   7023 C  CA  . MET B 1 416 ? -11.128 -0.541  51.630  1.00 31.47  ? 416 MET B CA  1 
ATOM   7024 C  C   . MET B 1 416 ? -12.300 -1.472  51.336  1.00 31.10  ? 416 MET B C   1 
ATOM   7025 O  O   . MET B 1 416 ? -13.210 -1.121  50.572  1.00 31.63  ? 416 MET B O   1 
ATOM   7026 C  CB  . MET B 1 416 ? -9.917  -0.877  50.752  1.00 29.29  ? 416 MET B CB  1 
ATOM   7027 C  CG  . MET B 1 416 ? -8.950  0.290   50.682  1.00 30.10  ? 416 MET B CG  1 
ATOM   7028 S  SD  . MET B 1 416 ? -7.544  -0.044  49.597  1.00 37.18  ? 416 MET B SD  1 
ATOM   7029 C  CE  . MET B 1 416 ? -8.338  0.350   48.041  1.00 35.77  ? 416 MET B CE  1 
ATOM   7030 N  N   . MET B 1 417 ? -12.272 -2.679  51.907  1.00 29.55  ? 417 MET B N   1 
ATOM   7031 C  CA  . MET B 1 417 ? -13.366 -3.631  51.717  1.00 28.85  ? 417 MET B CA  1 
ATOM   7032 C  C   . MET B 1 417 ? -14.689 -3.029  52.170  1.00 35.08  ? 417 MET B C   1 
ATOM   7033 O  O   . MET B 1 417 ? -15.700 -3.122  51.464  1.00 30.62  ? 417 MET B O   1 
ATOM   7034 C  CB  . MET B 1 417 ? -13.061 -4.905  52.501  1.00 31.27  ? 417 MET B CB  1 
ATOM   7035 C  CG  . MET B 1 417 ? -11.984 -5.740  51.857  1.00 33.16  ? 417 MET B CG  1 
ATOM   7036 S  SD  . MET B 1 417 ? -11.483 -7.119  52.888  1.00 37.60  ? 417 MET B SD  1 
ATOM   7037 C  CE  . MET B 1 417 ? -13.006 -8.022  53.120  1.00 36.59  ? 417 MET B CE  1 
ATOM   7038 N  N   . LEU B 1 418 ? -14.695 -2.396  53.351  1.00 31.61  ? 418 LEU B N   1 
ATOM   7039 C  CA  . LEU B 1 418 ? -15.932 -1.836  53.889  1.00 34.01  ? 418 LEU B CA  1 
ATOM   7040 C  C   . LEU B 1 418 ? -16.341 -0.577  53.150  1.00 34.63  ? 418 LEU B C   1 
ATOM   7041 O  O   . LEU B 1 418 ? -17.535 -0.250  53.092  1.00 34.77  ? 418 LEU B O   1 
ATOM   7042 C  CB  . LEU B 1 418 ? -15.769 -1.544  55.386  1.00 31.71  ? 418 LEU B CB  1 
ATOM   7043 C  CG  . LEU B 1 418 ? -15.484 -2.795  56.235  1.00 36.84  ? 418 LEU B CG  1 
ATOM   7044 C  CD1 . LEU B 1 418 ? -15.107 -2.411  57.651  1.00 35.31  ? 418 LEU B CD1 1 
ATOM   7045 C  CD2 . LEU B 1 418 ? -16.664 -3.756  56.250  1.00 37.60  ? 418 LEU B CD2 1 
ATOM   7046 N  N   . LYS B 1 419 ? -15.371 0.148   52.592  1.00 30.84  ? 419 LYS B N   1 
ATOM   7047 C  CA  . LYS B 1 419 ? -15.701 1.349   51.832  1.00 33.87  ? 419 LYS B CA  1 
ATOM   7048 C  C   . LYS B 1 419 ? -16.409 1.000   50.530  1.00 33.03  ? 419 LYS B C   1 
ATOM   7049 O  O   . LYS B 1 419 ? -17.333 1.704   50.106  1.00 33.42  ? 419 LYS B O   1 
ATOM   7050 C  CB  . LYS B 1 419 ? -14.433 2.148   51.532  1.00 34.33  ? 419 LYS B CB  1 
ATOM   7051 C  CG  . LYS B 1 419 ? -14.609 3.165   50.393  1.00 35.52  ? 419 LYS B CG  1 
ATOM   7052 C  CD  . LYS B 1 419 ? -13.304 3.943   50.158  1.00 32.07  ? 419 LYS B CD  1 
ATOM   7053 C  CE  . LYS B 1 419 ? -13.483 5.009   49.066  1.00 34.04  ? 419 LYS B CE  1 
ATOM   7054 N  NZ  . LYS B 1 419 ? -12.200 5.734   48.805  1.00 33.48  ? 419 LYS B NZ  1 
ATOM   7055 N  N   . HIS B 1 420 ? -15.988 -0.078  49.881  1.00 29.81  ? 420 HIS B N   1 
ATOM   7056 C  CA  . HIS B 1 420 ? -16.371 -0.314  48.499  1.00 35.07  ? 420 HIS B CA  1 
ATOM   7057 C  C   . HIS B 1 420 ? -17.519 -1.303  48.319  1.00 30.25  ? 420 HIS B C   1 
ATOM   7058 O  O   . HIS B 1 420 ? -18.075 -1.366  47.219  1.00 33.27  ? 420 HIS B O   1 
ATOM   7059 C  CB  . HIS B 1 420 ? -15.145 -0.790  47.706  1.00 31.65  ? 420 HIS B CB  1 
ATOM   7060 C  CG  . HIS B 1 420 ? -14.194 0.318   47.360  1.00 33.63  ? 420 HIS B CG  1 
ATOM   7061 N  ND1 . HIS B 1 420 ? -14.406 1.167   46.291  1.00 33.37  ? 420 HIS B ND1 1 
ATOM   7062 C  CD2 . HIS B 1 420 ? -13.032 0.718   47.937  1.00 33.95  ? 420 HIS B CD2 1 
ATOM   7063 C  CE1 . HIS B 1 420 ? -13.415 2.045   46.229  1.00 39.38  ? 420 HIS B CE1 1 
ATOM   7064 N  NE2 . HIS B 1 420 ? -12.566 1.793   47.215  1.00 33.38  ? 420 HIS B NE2 1 
ATOM   7065 N  N   . PHE B 1 421 ? -17.906 -2.057  49.350  1.00 31.33  ? 421 PHE B N   1 
ATOM   7066 C  CA  . PHE B 1 421 ? -18.888 -3.127  49.195  1.00 31.02  ? 421 PHE B CA  1 
ATOM   7067 C  C   . PHE B 1 421 ? -19.770 -3.227  50.431  1.00 32.69  ? 421 PHE B C   1 
ATOM   7068 O  O   . PHE B 1 421 ? -19.311 -2.996  51.553  1.00 33.00  ? 421 PHE B O   1 
ATOM   7069 C  CB  . PHE B 1 421 ? -18.216 -4.496  49.033  1.00 32.00  ? 421 PHE B CB  1 
ATOM   7070 C  CG  . PHE B 1 421 ? -17.278 -4.579  47.873  1.00 31.66  ? 421 PHE B CG  1 
ATOM   7071 C  CD1 . PHE B 1 421 ? -17.740 -4.754  46.581  1.00 32.78  ? 421 PHE B CD1 1 
ATOM   7072 C  CD2 . PHE B 1 421 ? -15.912 -4.409  48.088  1.00 31.54  ? 421 PHE B CD2 1 
ATOM   7073 C  CE1 . PHE B 1 421 ? -16.859 -4.799  45.505  1.00 33.68  ? 421 PHE B CE1 1 
ATOM   7074 C  CE2 . PHE B 1 421 ? -15.017 -4.447  47.014  1.00 32.98  ? 421 PHE B CE2 1 
ATOM   7075 C  CZ  . PHE B 1 421 ? -15.502 -4.640  45.718  1.00 31.03  ? 421 PHE B CZ  1 
ATOM   7076 N  N   . ASP B 1 422 ? -21.022 -3.636  50.222  1.00 35.49  ? 422 ASP B N   1 
ATOM   7077 C  CA  . ASP B 1 422 ? -21.814 -4.264  51.277  1.00 37.89  ? 422 ASP B CA  1 
ATOM   7078 C  C   . ASP B 1 422 ? -21.654 -5.779  51.176  1.00 36.16  ? 422 ASP B C   1 
ATOM   7079 O  O   . ASP B 1 422 ? -21.426 -6.315  50.096  1.00 37.42  ? 422 ASP B O   1 
ATOM   7080 C  CB  . ASP B 1 422 ? -23.290 -3.906  51.146  1.00 36.72  ? 422 ASP B CB  1 
ATOM   7081 C  CG  . ASP B 1 422 ? -23.564 -2.479  51.509  1.00 41.34  ? 422 ASP B CG  1 
ATOM   7082 O  OD1 . ASP B 1 422 ? -23.306 -2.099  52.663  1.00 46.77  ? 422 ASP B OD1 1 
ATOM   7083 O  OD2 . ASP B 1 422 ? -23.996 -1.739  50.619  1.00 41.28  ? 422 ASP B OD2 1 
ATOM   7084 N  N   . PHE B 1 423 ? -21.796 -6.472  52.293  1.00 31.71  ? 423 PHE B N   1 
ATOM   7085 C  CA  . PHE B 1 423 ? -21.511 -7.903  52.337  1.00 33.80  ? 423 PHE B CA  1 
ATOM   7086 C  C   . PHE B 1 423 ? -22.720 -8.692  52.819  1.00 36.25  ? 423 PHE B C   1 
ATOM   7087 O  O   . PHE B 1 423 ? -23.428 -8.267  53.736  1.00 39.17  ? 423 PHE B O   1 
ATOM   7088 C  CB  . PHE B 1 423 ? -20.309 -8.184  53.236  1.00 34.87  ? 423 PHE B CB  1 
ATOM   7089 C  CG  . PHE B 1 423 ? -19.017 -7.664  52.664  1.00 37.88  ? 423 PHE B CG  1 
ATOM   7090 C  CD1 . PHE B 1 423 ? -18.325 -8.402  51.718  1.00 38.28  ? 423 PHE B CD1 1 
ATOM   7091 C  CD2 . PHE B 1 423 ? -18.529 -6.420  53.032  1.00 36.88  ? 423 PHE B CD2 1 
ATOM   7092 C  CE1 . PHE B 1 423 ? -17.146 -7.916  51.164  1.00 35.46  ? 423 PHE B CE1 1 
ATOM   7093 C  CE2 . PHE B 1 423 ? -17.356 -5.929  52.483  1.00 34.58  ? 423 PHE B CE2 1 
ATOM   7094 C  CZ  . PHE B 1 423 ? -16.665 -6.672  51.556  1.00 33.50  ? 423 PHE B CZ  1 
ATOM   7095 N  N   . GLU B 1 424 ? -22.950 -9.844  52.203  1.00 35.47  ? 424 GLU B N   1 
ATOM   7096 C  CA  . GLU B 1 424 ? -24.047 -10.713 52.592  1.00 37.14  ? 424 GLU B CA  1 
ATOM   7097 C  C   . GLU B 1 424 ? -23.497 -12.085 52.942  1.00 38.04  ? 424 GLU B C   1 
ATOM   7098 O  O   . GLU B 1 424 ? -22.725 -12.675 52.174  1.00 35.23  ? 424 GLU B O   1 
ATOM   7099 C  CB  . GLU B 1 424 ? -25.095 -10.832 51.482  1.00 37.43  ? 424 GLU B CB  1 
ATOM   7100 C  CG  . GLU B 1 424 ? -26.251 -11.759 51.866  1.00 37.94  ? 424 GLU B CG  1 
ATOM   7101 C  CD  . GLU B 1 424 ? -27.150 -12.119 50.695  1.00 46.93  ? 424 GLU B CD  1 
ATOM   7102 O  OE1 . GLU B 1 424 ? -26.885 -11.639 49.572  1.00 44.85  ? 424 GLU B OE1 1 
ATOM   7103 O  OE2 . GLU B 1 424 ? -28.109 -12.890 50.903  1.00 45.96  ? 424 GLU B OE2 1 
ATOM   7104 N  N   . ASP B 1 425 ? -23.887 -12.573 54.112  1.00 31.02  ? 425 ASP B N   1 
ATOM   7105 C  CA  . ASP B 1 425 ? -23.613 -13.941 54.554  1.00 33.17  ? 425 ASP B CA  1 
ATOM   7106 C  C   . ASP B 1 425 ? -24.707 -14.835 53.968  1.00 36.19  ? 425 ASP B C   1 
ATOM   7107 O  O   . ASP B 1 425 ? -25.607 -15.323 54.651  1.00 34.14  ? 425 ASP B O   1 
ATOM   7108 C  CB  . ASP B 1 425 ? -23.577 -13.984 56.080  1.00 35.71  ? 425 ASP B CB  1 
ATOM   7109 C  CG  . ASP B 1 425 ? -23.527 -15.390 56.650  1.00 35.74  ? 425 ASP B CG  1 
ATOM   7110 O  OD1 . ASP B 1 425 ? -22.989 -16.309 56.001  1.00 34.13  ? 425 ASP B OD1 1 
ATOM   7111 O  OD2 . ASP B 1 425 ? -24.014 -15.564 57.788  1.00 35.03  ? 425 ASP B OD2 1 
ATOM   7112 N  N   . HIS B 1 426 ? -24.622 -15.023 52.654  1.00 35.65  ? 426 HIS B N   1 
ATOM   7113 C  CA  . HIS B 1 426 ? -25.739 -15.589 51.906  1.00 38.68  ? 426 HIS B CA  1 
ATOM   7114 C  C   . HIS B 1 426 ? -25.976 -17.070 52.202  1.00 36.35  ? 426 HIS B C   1 
ATOM   7115 O  O   . HIS B 1 426 ? -27.071 -17.570 51.928  1.00 38.87  ? 426 HIS B O   1 
ATOM   7116 C  CB  . HIS B 1 426 ? -25.501 -15.375 50.406  1.00 39.00  ? 426 HIS B CB  1 
ATOM   7117 C  CG  . HIS B 1 426 ? -24.307 -16.112 49.871  1.00 37.89  ? 426 HIS B CG  1 
ATOM   7118 N  ND1 . HIS B 1 426 ? -23.012 -15.822 50.259  1.00 34.80  ? 426 HIS B ND1 1 
ATOM   7119 C  CD2 . HIS B 1 426 ? -24.213 -17.132 48.982  1.00 36.82  ? 426 HIS B CD2 1 
ATOM   7120 C  CE1 . HIS B 1 426 ? -22.176 -16.633 49.634  1.00 35.96  ? 426 HIS B CE1 1 
ATOM   7121 N  NE2 . HIS B 1 426 ? -22.878 -17.435 48.850  1.00 36.85  ? 426 HIS B NE2 1 
ATOM   7122 N  N   . THR B 1 427 ? -24.985 -17.796 52.706  1.00 33.12  ? 427 THR B N   1 
ATOM   7123 C  CA  . THR B 1 427 ? -25.171 -19.196 53.089  1.00 31.46  ? 427 THR B CA  1 
ATOM   7124 C  C   . THR B 1 427 ? -25.450 -19.379 54.573  1.00 32.01  ? 427 THR B C   1 
ATOM   7125 O  O   . THR B 1 427 ? -25.593 -20.520 55.029  1.00 34.73  ? 427 THR B O   1 
ATOM   7126 C  CB  . THR B 1 427 ? -23.939 -20.031 52.706  1.00 34.45  ? 427 THR B CB  1 
ATOM   7127 O  OG1 . THR B 1 427 ? -22.862 -19.736 53.609  1.00 35.76  ? 427 THR B OG1 1 
ATOM   7128 C  CG2 . THR B 1 427 ? -23.495 -19.720 51.288  1.00 35.65  ? 427 THR B CG2 1 
ATOM   7129 N  N   . ASN B 1 428 ? -25.549 -18.299 55.339  1.00 32.13  ? 428 ASN B N   1 
ATOM   7130 C  CA  . ASN B 1 428 ? -25.572 -18.385 56.799  1.00 34.14  ? 428 ASN B CA  1 
ATOM   7131 C  C   . ASN B 1 428 ? -24.469 -19.325 57.293  1.00 40.07  ? 428 ASN B C   1 
ATOM   7132 O  O   . ASN B 1 428 ? -24.706 -20.340 57.952  1.00 37.29  ? 428 ASN B O   1 
ATOM   7133 C  CB  . ASN B 1 428 ? -26.952 -18.806 57.314  1.00 36.09  ? 428 ASN B CB  1 
ATOM   7134 C  CG  . ASN B 1 428 ? -27.043 -18.706 58.816  1.00 47.54  ? 428 ASN B CG  1 
ATOM   7135 O  OD1 . ASN B 1 428 ? -26.374 -17.873 59.423  1.00 39.69  ? 428 ASN B OD1 1 
ATOM   7136 N  ND2 . ASN B 1 428 ? -27.909 -19.513 59.422  1.00 49.18  ? 428 ASN B ND2 1 
ATOM   7137 N  N   . TYR B 1 429 ? -23.235 -18.934 56.967  1.00 35.56  ? 429 TYR B N   1 
ATOM   7138 C  CA  . TYR B 1 429 ? -22.070 -19.792 57.149  1.00 34.43  ? 429 TYR B CA  1 
ATOM   7139 C  C   . TYR B 1 429 ? -21.890 -20.240 58.597  1.00 34.38  ? 429 TYR B C   1 
ATOM   7140 O  O   . TYR B 1 429 ? -21.992 -19.442 59.530  1.00 35.20  ? 429 TYR B O   1 
ATOM   7141 C  CB  . TYR B 1 429 ? -20.827 -19.041 56.664  1.00 33.33  ? 429 TYR B CB  1 
ATOM   7142 C  CG  . TYR B 1 429 ? -19.507 -19.663 57.082  1.00 34.00  ? 429 TYR B CG  1 
ATOM   7143 C  CD1 . TYR B 1 429 ? -19.000 -20.784 56.432  1.00 32.62  ? 429 TYR B CD1 1 
ATOM   7144 C  CD2 . TYR B 1 429 ? -18.765 -19.102 58.123  1.00 32.79  ? 429 TYR B CD2 1 
ATOM   7145 C  CE1 . TYR B 1 429 ? -17.773 -21.326 56.804  1.00 33.21  ? 429 TYR B CE1 1 
ATOM   7146 C  CE2 . TYR B 1 429 ? -17.560 -19.632 58.503  1.00 30.76  ? 429 TYR B CE2 1 
ATOM   7147 C  CZ  . TYR B 1 429 ? -17.066 -20.749 57.851  1.00 29.74  ? 429 TYR B CZ  1 
ATOM   7148 O  OH  . TYR B 1 429 ? -15.835 -21.262 58.250  1.00 33.55  ? 429 TYR B OH  1 
ATOM   7149 N  N   . GLU B 1 430 ? -21.622 -21.532 58.779  1.00 33.26  ? 430 GLU B N   1 
ATOM   7150 C  CA  . GLU B 1 430 ? -21.278 -22.084 60.086  1.00 33.93  ? 430 GLU B CA  1 
ATOM   7151 C  C   . GLU B 1 430 ? -19.762 -22.090 60.267  1.00 36.50  ? 430 GLU B C   1 
ATOM   7152 O  O   . GLU B 1 430 ? -19.033 -22.698 59.467  1.00 34.53  ? 430 GLU B O   1 
ATOM   7153 C  CB  . GLU B 1 430 ? -21.817 -23.504 60.247  1.00 35.88  ? 430 GLU B CB  1 
ATOM   7154 C  CG  . GLU B 1 430 ? -22.069 -23.862 61.685  1.00 42.15  ? 430 GLU B CG  1 
ATOM   7155 C  CD  . GLU B 1 430 ? -22.544 -25.277 61.839  1.00 59.22  ? 430 GLU B CD  1 
ATOM   7156 O  OE1 . GLU B 1 430 ? -23.745 -25.472 62.112  1.00 62.17  ? 430 GLU B OE1 1 
ATOM   7157 O  OE2 . GLU B 1 430 ? -21.716 -26.196 61.669  1.00 65.27  ? 430 GLU B OE2 1 
ATOM   7158 N  N   . LEU B 1 431 ? -19.291 -21.431 61.319  1.00 34.51  ? 431 LEU B N   1 
ATOM   7159 C  CA  . LEU B 1 431 ? -17.852 -21.349 61.542  1.00 35.80  ? 431 LEU B CA  1 
ATOM   7160 C  C   . LEU B 1 431 ? -17.221 -22.741 61.574  1.00 32.63  ? 431 LEU B C   1 
ATOM   7161 O  O   . LEU B 1 431 ? -17.647 -23.631 62.321  1.00 32.42  ? 431 LEU B O   1 
ATOM   7162 C  CB  . LEU B 1 431 ? -17.555 -20.599 62.833  1.00 37.18  ? 431 LEU B CB  1 
ATOM   7163 C  CG  . LEU B 1 431 ? -16.078 -20.220 63.030  1.00 36.23  ? 431 LEU B CG  1 
ATOM   7164 C  CD1 . LEU B 1 431 ? -15.511 -19.458 61.815  1.00 32.50  ? 431 LEU B CD1 1 
ATOM   7165 C  CD2 . LEU B 1 431 ? -15.954 -19.419 64.316  1.00 38.60  ? 431 LEU B CD2 1 
ATOM   7166 N  N   . ASP B 1 432 ? -16.197 -22.923 60.753  1.00 33.28  ? 432 ASP B N   1 
ATOM   7167 C  CA  . ASP B 1 432 ? -15.458 -24.176 60.689  1.00 35.90  ? 432 ASP B CA  1 
ATOM   7168 C  C   . ASP B 1 432 ? -13.984 -23.798 60.626  1.00 33.03  ? 432 ASP B C   1 
ATOM   7169 O  O   . ASP B 1 432 ? -13.533 -23.249 59.612  1.00 33.91  ? 432 ASP B O   1 
ATOM   7170 C  CB  . ASP B 1 432 ? -15.889 -24.979 59.462  1.00 37.62  ? 432 ASP B CB  1 
ATOM   7171 C  CG  . ASP B 1 432 ? -15.139 -26.271 59.319  1.00 37.63  ? 432 ASP B CG  1 
ATOM   7172 O  OD1 . ASP B 1 432 ? -14.349 -26.626 60.227  1.00 37.38  ? 432 ASP B OD1 1 
ATOM   7173 O  OD2 . ASP B 1 432 ? -15.364 -26.938 58.299  1.00 39.60  ? 432 ASP B OD2 1 
ATOM   7174 N  N   . ILE B 1 433 ? -13.246 -24.019 61.713  1.00 32.50  ? 433 ILE B N   1 
ATOM   7175 C  CA  . ILE B 1 433 ? -11.886 -23.496 61.817  1.00 30.33  ? 433 ILE B CA  1 
ATOM   7176 C  C   . ILE B 1 433 ? -10.892 -24.593 61.460  1.00 32.98  ? 433 ILE B C   1 
ATOM   7177 O  O   . ILE B 1 433 ? -10.709 -25.559 62.212  1.00 33.64  ? 433 ILE B O   1 
ATOM   7178 C  CB  . ILE B 1 433 ? -11.594 -22.896 63.197  1.00 32.87  ? 433 ILE B CB  1 
ATOM   7179 C  CG1 . ILE B 1 433 ? -12.524 -21.719 63.498  1.00 31.40  ? 433 ILE B CG1 1 
ATOM   7180 C  CG2 . ILE B 1 433 ? -10.129 -22.465 63.301  1.00 32.55  ? 433 ILE B CG2 1 
ATOM   7181 C  CD1 . ILE B 1 433 ? -12.562 -21.361 64.976  1.00 31.26  ? 433 ILE B CD1 1 
ATOM   7182 N  N   . LYS B 1 434 ? -10.235 -24.417 60.311  1.00 34.94  ? 434 LYS B N   1 
ATOM   7183 C  CA  . LYS B 1 434 ? -9.125  -25.269 59.892  1.00 36.71  ? 434 LYS B CA  1 
ATOM   7184 C  C   . LYS B 1 434 ? -7.836  -24.894 60.605  1.00 34.42  ? 434 LYS B C   1 
ATOM   7185 O  O   . LYS B 1 434 ? -7.484  -23.718 60.701  1.00 34.32  ? 434 LYS B O   1 
ATOM   7186 C  CB  . LYS B 1 434 ? -8.909  -25.161 58.382  1.00 35.91  ? 434 LYS B CB  1 
ATOM   7187 C  CG  . LYS B 1 434 ? -8.026  -26.233 57.766  1.00 38.76  ? 434 LYS B CG  1 
ATOM   7188 C  CD  . LYS B 1 434 ? -7.892  -25.969 56.254  1.00 47.21  ? 434 LYS B CD  1 
ATOM   7189 C  CE  . LYS B 1 434 ? -7.014  -27.005 55.527  1.00 51.40  ? 434 LYS B CE  1 
ATOM   7190 N  NZ  . LYS B 1 434 ? -7.243  -28.408 55.959  1.00 51.21  ? 434 LYS B NZ  1 
ATOM   7191 N  N   . GLU B 1 435 ? -7.111  -25.907 61.059  1.00 34.64  ? 435 GLU B N   1 
ATOM   7192 C  CA  . GLU B 1 435 ? -5.841  -25.722 61.751  1.00 31.85  ? 435 GLU B CA  1 
ATOM   7193 C  C   . GLU B 1 435 ? -4.705  -26.206 60.859  1.00 34.66  ? 435 GLU B C   1 
ATOM   7194 O  O   . GLU B 1 435 ? -4.670  -27.381 60.478  1.00 36.15  ? 435 GLU B O   1 
ATOM   7195 C  CB  . GLU B 1 435 ? -5.841  -26.467 63.082  1.00 33.53  ? 435 GLU B CB  1 
ATOM   7196 C  CG  . GLU B 1 435 ? -7.058  -26.122 63.927  1.00 33.46  ? 435 GLU B CG  1 
ATOM   7197 C  CD  . GLU B 1 435 ? -6.881  -26.502 65.381  1.00 33.93  ? 435 GLU B CD  1 
ATOM   7198 O  OE1 . GLU B 1 435 ? -5.756  -26.890 65.786  1.00 33.28  ? 435 GLU B OE1 1 
ATOM   7199 O  OE2 . GLU B 1 435 ? -7.859  -26.376 66.125  1.00 32.88  ? 435 GLU B OE2 1 
ATOM   7200 N  N   . THR B 1 436 ? -3.776  -25.298 60.538  1.00 35.93  ? 436 THR B N   1 
ATOM   7201 C  CA  . THR B 1 436 ? -2.514  -25.667 59.904  1.00 40.07  ? 436 THR B CA  1 
ATOM   7202 C  C   . THR B 1 436 ? -1.395  -25.129 60.800  1.00 39.05  ? 436 THR B C   1 
ATOM   7203 O  O   . THR B 1 436 ? -1.343  -25.486 61.973  1.00 35.53  ? 436 THR B O   1 
ATOM   7204 C  CB  . THR B 1 436 ? -2.486  -25.213 58.457  1.00 43.58  ? 436 THR B CB  1 
ATOM   7205 O  OG1 . THR B 1 436 ? -2.470  -23.774 58.393  1.00 45.98  ? 436 THR B OG1 1 
ATOM   7206 C  CG2 . THR B 1 436 ? -3.721  -25.743 57.756  1.00 35.75  ? 436 THR B CG2 1 
ATOM   7207 N  N   . LEU B 1 437 ? -0.505  -24.280 60.291  1.00 40.28  ? 437 LEU B N   1 
ATOM   7208 C  CA  . LEU B 1 437 ? 0.358   -23.586 61.255  1.00 50.28  ? 437 LEU B CA  1 
ATOM   7209 C  C   . LEU B 1 437 ? -0.475  -22.700 62.172  1.00 43.99  ? 437 LEU B C   1 
ATOM   7210 O  O   . LEU B 1 437 ? -0.057  -22.373 63.285  1.00 47.49  ? 437 LEU B O   1 
ATOM   7211 C  CB  . LEU B 1 437 ? 1.446   -22.758 60.529  1.00 50.34  ? 437 LEU B CB  1 
ATOM   7212 C  CG  . LEU B 1 437 ? 2.402   -21.838 61.320  1.00 53.29  ? 437 LEU B CG  1 
ATOM   7213 C  CD1 . LEU B 1 437 ? 3.555   -22.601 61.965  1.00 52.50  ? 437 LEU B CD1 1 
ATOM   7214 C  CD2 . LEU B 1 437 ? 2.991   -20.717 60.439  1.00 47.96  ? 437 LEU B CD2 1 
ATOM   7215 N  N   . THR B 1 438 ? -1.677  -22.375 61.739  1.00 40.92  ? 438 THR B N   1 
ATOM   7216 C  CA  . THR B 1 438 ? -2.416  -21.227 62.208  1.00 34.77  ? 438 THR B CA  1 
ATOM   7217 C  C   . THR B 1 438 ? -3.877  -21.563 62.000  1.00 32.88  ? 438 THR B C   1 
ATOM   7218 O  O   . THR B 1 438 ? -4.205  -22.625 61.482  1.00 36.32  ? 438 THR B O   1 
ATOM   7219 C  CB  . THR B 1 438 ? -2.020  -19.997 61.409  1.00 41.07  ? 438 THR B CB  1 
ATOM   7220 O  OG1 . THR B 1 438 ? -2.078  -20.348 60.018  1.00 38.22  ? 438 THR B OG1 1 
ATOM   7221 C  CG2 . THR B 1 438 ? -0.582  -19.576 61.749  1.00 36.82  ? 438 THR B CG2 1 
ATOM   7222 N  N   . LEU B 1 439 ? -4.757  -20.657 62.396  1.00 33.52  ? 439 LEU B N   1 
ATOM   7223 C  CA  . LEU B 1 439 ? -6.186  -20.894 62.287  1.00 29.66  ? 439 LEU B CA  1 
ATOM   7224 C  C   . LEU B 1 439 ? -6.780  -20.020 61.196  1.00 32.02  ? 439 LEU B C   1 
ATOM   7225 O  O   . LEU B 1 439 ? -6.382  -18.859 61.022  1.00 33.67  ? 439 LEU B O   1 
ATOM   7226 C  CB  . LEU B 1 439 ? -6.890  -20.635 63.623  1.00 32.25  ? 439 LEU B CB  1 
ATOM   7227 C  CG  . LEU B 1 439 ? -6.258  -21.184 64.892  1.00 26.67  ? 439 LEU B CG  1 
ATOM   7228 C  CD1 . LEU B 1 439 ? -7.019  -20.648 66.102  1.00 30.46  ? 439 LEU B CD1 1 
ATOM   7229 C  CD2 . LEU B 1 439 ? -6.283  -22.720 64.880  1.00 28.33  ? 439 LEU B CD2 1 
ATOM   7230 N  N   . LYS B 1 440 ? -7.739  -20.579 60.466  1.00 33.10  ? 440 LYS B N   1 
ATOM   7231 C  CA  . LYS B 1 440 ? -8.480  -19.812 59.480  1.00 34.28  ? 440 LYS B CA  1 
ATOM   7232 C  C   . LYS B 1 440 ? -9.854  -20.437 59.366  1.00 36.16  ? 440 LYS B C   1 
ATOM   7233 O  O   . LYS B 1 440 ? -9.995  -21.653 59.536  1.00 34.74  ? 440 LYS B O   1 
ATOM   7234 C  CB  . LYS B 1 440 ? -7.804  -19.813 58.103  1.00 37.85  ? 440 LYS B CB  1 
ATOM   7235 C  CG  . LYS B 1 440 ? -7.825  -21.170 57.413  1.00 47.27  ? 440 LYS B CG  1 
ATOM   7236 C  CD  . LYS B 1 440 ? -6.787  -21.268 56.289  1.00 55.91  ? 440 LYS B CD  1 
ATOM   7237 C  CE  . LYS B 1 440 ? -7.253  -22.254 55.218  1.00 62.09  ? 440 LYS B CE  1 
ATOM   7238 N  NZ  . LYS B 1 440 ? -8.754  -22.234 55.084  1.00 50.08  ? 440 LYS B NZ  1 
ATOM   7239 N  N   . PRO B 1 441 ? -10.882 -19.649 59.083  1.00 32.63  ? 441 PRO B N   1 
ATOM   7240 C  CA  . PRO B 1 441 ? -12.173 -20.256 58.765  1.00 31.10  ? 441 PRO B CA  1 
ATOM   7241 C  C   . PRO B 1 441 ? -12.087 -20.900 57.393  1.00 38.86  ? 441 PRO B C   1 
ATOM   7242 O  O   . PRO B 1 441 ? -11.443 -20.377 56.478  1.00 47.36  ? 441 PRO B O   1 
ATOM   7243 C  CB  . PRO B 1 441 ? -13.153 -19.082 58.823  1.00 33.82  ? 441 PRO B CB  1 
ATOM   7244 C  CG  . PRO B 1 441 ? -12.324 -17.840 58.683  1.00 38.91  ? 441 PRO B CG  1 
ATOM   7245 C  CD  . PRO B 1 441 ? -10.850 -18.209 58.791  1.00 31.81  ? 441 PRO B CD  1 
ATOM   7246 N  N   . GLU B 1 442 ? -12.610 -22.106 57.292  1.00 34.85  ? 442 GLU B N   1 
ATOM   7247 C  CA  . GLU B 1 442 ? -12.557 -22.836 56.043  1.00 35.53  ? 442 GLU B CA  1 
ATOM   7248 C  C   . GLU B 1 442 ? -13.958 -22.803 55.441  1.00 34.04  ? 442 GLU B C   1 
ATOM   7249 O  O   . GLU B 1 442 ? -14.954 -22.888 56.168  1.00 33.47  ? 442 GLU B O   1 
ATOM   7250 C  CB  . GLU B 1 442 ? -12.078 -24.274 56.265  1.00 38.18  ? 442 GLU B CB  1 
ATOM   7251 C  CG  . GLU B 1 442 ? -12.672 -25.272 55.314  1.00 42.35  ? 442 GLU B CG  1 
ATOM   7252 C  CD  . GLU B 1 442 ? -11.835 -26.518 55.249  1.00 44.74  ? 442 GLU B CD  1 
ATOM   7253 O  OE1 . GLU B 1 442 ? -11.336 -26.940 56.305  1.00 47.18  ? 442 GLU B OE1 1 
ATOM   7254 O  OE2 . GLU B 1 442 ? -11.599 -27.023 54.143  1.00 51.31  ? 442 GLU B OE2 1 
ATOM   7255 N  N   . GLY B 1 443 ? -14.032 -22.615 54.127  1.00 33.63  ? 443 GLY B N   1 
ATOM   7256 C  CA  . GLY B 1 443 ? -15.329 -22.568 53.478  1.00 31.84  ? 443 GLY B CA  1 
ATOM   7257 C  C   . GLY B 1 443 ? -16.122 -21.300 53.695  1.00 35.13  ? 443 GLY B C   1 
ATOM   7258 O  O   . GLY B 1 443 ? -17.279 -21.227 53.256  1.00 32.98  ? 443 GLY B O   1 
ATOM   7259 N  N   . PHE B 1 444 ? -15.553 -20.298 54.366  1.00 32.60  ? 444 PHE B N   1 
ATOM   7260 C  CA  . PHE B 1 444 ? -16.257 -19.032 54.547  1.00 32.55  ? 444 PHE B CA  1 
ATOM   7261 C  C   . PHE B 1 444 ? -16.437 -18.335 53.196  1.00 33.46  ? 444 PHE B C   1 
ATOM   7262 O  O   . PHE B 1 444 ? -15.464 -18.078 52.482  1.00 31.19  ? 444 PHE B O   1 
ATOM   7263 C  CB  . PHE B 1 444 ? -15.484 -18.156 55.525  1.00 32.09  ? 444 PHE B CB  1 
ATOM   7264 C  CG  . PHE B 1 444 ? -16.110 -16.808 55.792  1.00 30.66  ? 444 PHE B CG  1 
ATOM   7265 C  CD1 . PHE B 1 444 ? -17.486 -16.651 55.871  1.00 32.55  ? 444 PHE B CD1 1 
ATOM   7266 C  CD2 . PHE B 1 444 ? -15.299 -15.699 55.995  1.00 33.14  ? 444 PHE B CD2 1 
ATOM   7267 C  CE1 . PHE B 1 444 ? -18.034 -15.406 56.127  1.00 33.07  ? 444 PHE B CE1 1 
ATOM   7268 C  CE2 . PHE B 1 444 ? -15.835 -14.452 56.242  1.00 32.80  ? 444 PHE B CE2 1 
ATOM   7269 C  CZ  . PHE B 1 444 ? -17.203 -14.299 56.314  1.00 32.14  ? 444 PHE B CZ  1 
ATOM   7270 N  N   . VAL B 1 445 ? -17.682 -18.035 52.836  1.00 32.29  ? 445 VAL B N   1 
ATOM   7271 C  CA  . VAL B 1 445 ? -17.998 -17.388 51.572  1.00 31.98  ? 445 VAL B CA  1 
ATOM   7272 C  C   . VAL B 1 445 ? -19.019 -16.298 51.862  1.00 35.57  ? 445 VAL B C   1 
ATOM   7273 O  O   . VAL B 1 445 ? -19.821 -16.408 52.794  1.00 33.86  ? 445 VAL B O   1 
ATOM   7274 C  CB  . VAL B 1 445 ? -18.559 -18.377 50.517  1.00 34.61  ? 445 VAL B CB  1 
ATOM   7275 C  CG1 . VAL B 1 445 ? -17.497 -19.393 50.081  1.00 35.19  ? 445 VAL B CG1 1 
ATOM   7276 C  CG2 . VAL B 1 445 ? -19.795 -19.099 51.060  1.00 39.76  ? 445 VAL B CG2 1 
ATOM   7277 N  N   . VAL B 1 446 ? -18.997 -15.249 51.040  1.00 32.18  ? 446 VAL B N   1 
ATOM   7278 C  CA  . VAL B 1 446 ? -19.940 -14.137 51.117  1.00 32.48  ? 446 VAL B CA  1 
ATOM   7279 C  C   . VAL B 1 446 ? -20.246 -13.669 49.701  1.00 34.78  ? 446 VAL B C   1 
ATOM   7280 O  O   . VAL B 1 446 ? -19.544 -14.002 48.741  1.00 34.63  ? 446 VAL B O   1 
ATOM   7281 C  CB  . VAL B 1 446 ? -19.390 -12.946 51.933  1.00 36.00  ? 446 VAL B CB  1 
ATOM   7282 C  CG1 . VAL B 1 446 ? -19.052 -13.371 53.367  1.00 33.57  ? 446 VAL B CG1 1 
ATOM   7283 C  CG2 . VAL B 1 446 ? -18.168 -12.364 51.235  1.00 31.77  ? 446 VAL B CG2 1 
ATOM   7284 N  N   . LYS B 1 447 ? -21.295 -12.865 49.586  1.00 34.41  ? 447 LYS B N   1 
ATOM   7285 C  CA  . LYS B 1 447 ? -21.555 -12.090 48.384  1.00 36.13  ? 447 LYS B CA  1 
ATOM   7286 C  C   . LYS B 1 447 ? -21.329 -10.627 48.700  1.00 34.89  ? 447 LYS B C   1 
ATOM   7287 O  O   . LYS B 1 447 ? -21.747 -10.145 49.756  1.00 38.41  ? 447 LYS B O   1 
ATOM   7288 C  CB  . LYS B 1 447 ? -22.988 -12.300 47.883  1.00 35.48  ? 447 LYS B CB  1 
ATOM   7289 C  CG  . LYS B 1 447 ? -23.224 -13.661 47.291  1.00 42.08  ? 447 LYS B CG  1 
ATOM   7290 C  CD  . LYS B 1 447 ? -24.672 -13.807 46.798  1.00 45.46  ? 447 LYS B CD  1 
ATOM   7291 C  CE  . LYS B 1 447 ? -24.812 -14.993 45.869  1.00 48.80  ? 447 LYS B CE  1 
ATOM   7292 N  NZ  . LYS B 1 447 ? -26.234 -15.239 45.455  1.00 56.90  ? 447 LYS B NZ  1 
ATOM   7293 N  N   . ALA B 1 448 ? -20.653 -9.926  47.800  1.00 35.11  ? 448 ALA B N   1 
ATOM   7294 C  CA  . ALA B 1 448 ? -20.405 -8.500  47.955  1.00 37.74  ? 448 ALA B CA  1 
ATOM   7295 C  C   . ALA B 1 448 ? -21.284 -7.741  46.972  1.00 44.33  ? 448 ALA B C   1 
ATOM   7296 O  O   . ALA B 1 448 ? -21.420 -8.146  45.812  1.00 49.84  ? 448 ALA B O   1 
ATOM   7297 C  CB  . ALA B 1 448 ? -18.921 -8.166  47.739  1.00 33.19  ? 448 ALA B CB  1 
ATOM   7298 N  N   . LYS B 1 449 ? -21.906 -6.665  47.441  1.00 39.73  ? 449 LYS B N   1 
ATOM   7299 C  CA  . LYS B 1 449 ? -22.654 -5.762  46.573  1.00 43.48  ? 449 LYS B CA  1 
ATOM   7300 C  C   . LYS B 1 449 ? -21.882 -4.459  46.472  1.00 36.64  ? 449 LYS B C   1 
ATOM   7301 O  O   . LYS B 1 449 ? -21.704 -3.760  47.475  1.00 36.81  ? 449 LYS B O   1 
ATOM   7302 C  CB  . LYS B 1 449 ? -24.071 -5.530  47.103  1.00 45.22  ? 449 LYS B CB  1 
ATOM   7303 C  CG  . LYS B 1 449 ? -25.060 -5.114  46.022  1.00 52.59  ? 449 LYS B CG  1 
ATOM   7304 C  CD  . LYS B 1 449 ? -26.507 -5.398  46.420  1.00 57.82  ? 449 LYS B CD  1 
ATOM   7305 C  CE  . LYS B 1 449 ? -26.980 -6.717  45.801  1.00 62.40  ? 449 LYS B CE  1 
ATOM   7306 N  NZ  . LYS B 1 449 ? -28.204 -7.262  46.449  1.00 62.56  ? 449 LYS B NZ  1 
ATOM   7307 N  N   . SER B 1 450 ? -21.403 -4.149  45.273  1.00 35.32  ? 450 SER B N   1 
ATOM   7308 C  CA  . SER B 1 450 ? -20.584 -2.961  45.092  1.00 40.00  ? 450 SER B CA  1 
ATOM   7309 C  C   . SER B 1 450 ? -21.355 -1.703  45.466  1.00 39.28  ? 450 SER B C   1 
ATOM   7310 O  O   . SER B 1 450 ? -22.521 -1.534  45.098  1.00 36.87  ? 450 SER B O   1 
ATOM   7311 C  CB  . SER B 1 450 ? -20.104 -2.860  43.643  1.00 39.38  ? 450 SER B CB  1 
ATOM   7312 O  OG  . SER B 1 450 ? -19.394 -1.655  43.462  1.00 37.21  ? 450 SER B OG  1 
ATOM   7313 N  N   . LYS B 1 451 ? -20.704 -0.817  46.219  1.00 32.97  ? 451 LYS B N   1 
ATOM   7314 C  CA  . LYS B 1 451 ? -21.223 0.535   46.373  1.00 36.33  ? 451 LYS B CA  1 
ATOM   7315 C  C   . LYS B 1 451 ? -20.887 1.431   45.186  1.00 40.54  ? 451 LYS B C   1 
ATOM   7316 O  O   . LYS B 1 451 ? -21.235 2.615   45.211  1.00 42.80  ? 451 LYS B O   1 
ATOM   7317 C  CB  . LYS B 1 451 ? -20.695 1.167   47.659  1.00 37.40  ? 451 LYS B CB  1 
ATOM   7318 C  CG  . LYS B 1 451 ? -20.988 0.332   48.899  1.00 38.43  ? 451 LYS B CG  1 
ATOM   7319 C  CD  . LYS B 1 451 ? -20.540 1.049   50.156  1.00 41.35  ? 451 LYS B CD  1 
ATOM   7320 C  CE  . LYS B 1 451 ? -20.946 0.267   51.369  1.00 41.37  ? 451 LYS B CE  1 
ATOM   7321 N  NZ  . LYS B 1 451 ? -22.412 0.448   51.596  1.00 51.84  ? 451 LYS B NZ  1 
ATOM   7322 N  N   . LYS B 1 452 ? -20.207 0.902   44.167  1.00 38.13  ? 452 LYS B N   1 
ATOM   7323 C  CA  . LYS B 1 452 ? -19.883 1.645   42.938  1.00 42.69  ? 452 LYS B CA  1 
ATOM   7324 C  C   . LYS B 1 452 ? -19.151 2.952   43.232  1.00 43.43  ? 452 LYS B C   1 
ATOM   7325 O  O   . LYS B 1 452 ? -19.466 4.007   42.673  1.00 41.84  ? 452 LYS B O   1 
ATOM   7326 C  CB  . LYS B 1 452 ? -21.136 1.904   42.094  1.00 44.18  ? 452 LYS B CB  1 
ATOM   7327 C  CG  . LYS B 1 452 ? -21.855 0.632   41.683  1.00 45.17  ? 452 LYS B CG  1 
ATOM   7328 C  CD  . LYS B 1 452 ? -20.945 -0.188  40.768  1.00 50.52  ? 452 LYS B CD  1 
ATOM   7329 C  CE  . LYS B 1 452 ? -21.593 -1.491  40.289  1.00 51.46  ? 452 LYS B CE  1 
ATOM   7330 N  NZ  . LYS B 1 452 ? -20.870 -2.078  39.111  1.00 53.32  ? 452 LYS B NZ  1 
ATOM   7331 N  N   . ILE B 1 453 ? -18.147 2.875   44.100  1.00 39.38  ? 453 ILE B N   1 
ATOM   7332 C  CA  . ILE B 1 453 ? -17.264 4.002   44.394  1.00 38.12  ? 453 ILE B CA  1 
ATOM   7333 C  C   . ILE B 1 453 ? -15.989 3.825   43.574  1.00 45.10  ? 453 ILE B C   1 
ATOM   7334 O  O   . ILE B 1 453 ? -15.270 2.826   43.771  1.00 39.69  ? 453 ILE B O   1 
ATOM   7335 C  CB  . ILE B 1 453 ? -16.948 4.109   45.894  1.00 43.12  ? 453 ILE B CB  1 
ATOM   7336 C  CG1 . ILE B 1 453 ? -18.221 4.430   46.687  1.00 42.83  ? 453 ILE B CG1 1 
ATOM   7337 C  CG2 . ILE B 1 453 ? -15.889 5.190   46.143  1.00 40.30  ? 453 ILE B CG2 1 
ATOM   7338 C  CD1 . ILE B 1 453 ? -18.083 4.161   48.153  1.00 45.59  ? 453 ILE B CD1 1 
ATOM   7339 N  N   . PRO B 1 454 ? -15.672 4.742   42.658  1.00 46.45  ? 454 PRO B N   1 
ATOM   7340 C  CA  . PRO B 1 454 ? -14.523 4.530   41.771  1.00 43.92  ? 454 PRO B CA  1 
ATOM   7341 C  C   . PRO B 1 454 ? -13.214 4.423   42.540  1.00 43.14  ? 454 PRO B C   1 
ATOM   7342 O  O   . PRO B 1 454 ? -13.036 5.016   43.605  1.00 42.54  ? 454 PRO B O   1 
ATOM   7343 C  CB  . PRO B 1 454 ? -14.531 5.775   40.865  1.00 47.27  ? 454 PRO B CB  1 
ATOM   7344 C  CG  . PRO B 1 454 ? -15.408 6.771   41.564  1.00 49.49  ? 454 PRO B CG  1 
ATOM   7345 C  CD  . PRO B 1 454 ? -16.418 5.967   42.320  1.00 48.40  ? 454 PRO B CD  1 
ATOM   7346 N  N   . LEU B 1 455 ? -12.284 3.667   41.966  1.00 44.04  ? 455 LEU B N   1 
ATOM   7347 C  CA  . LEU B 1 455 ? -10.910 3.630   42.445  1.00 44.98  ? 455 LEU B CA  1 
ATOM   7348 C  C   . LEU B 1 455 ? -10.033 4.626   41.693  1.00 50.15  ? 455 LEU B C   1 
ATOM   7349 O  O   . LEU B 1 455 ? -10.491 5.289   40.758  1.00 47.78  ? 455 LEU B O   1 
ATOM   7350 C  CB  . LEU B 1 455 ? -10.338 2.230   42.292  1.00 44.16  ? 455 LEU B CB  1 
ATOM   7351 C  CG  . LEU B 1 455 ? -10.847 1.233   43.324  1.00 44.23  ? 455 LEU B CG  1 
ATOM   7352 C  CD1 . LEU B 1 455 ? -10.578 -0.186  42.820  1.00 42.13  ? 455 LEU B CD1 1 
ATOM   7353 C  CD2 . LEU B 1 455 ? -10.148 1.508   44.661  1.00 40.78  ? 455 LEU B CD2 1 
ATOM   7354 O  OXT . LEU B 1 455 ? -8.839  4.773   41.993  1.00 50.86  ? 455 LEU B OXT 1 
HETATM 7355 C  CHA . HEM C 2 .   ? -17.925 -14.235 9.061   1.00 32.97  ? 501 HEM A CHA 1 
HETATM 7356 C  CHB . HEM C 2 .   ? -13.146 -13.413 9.320   1.00 32.65  ? 501 HEM A CHB 1 
HETATM 7357 C  CHC . HEM C 2 .   ? -13.722 -11.339 13.733  1.00 30.81  ? 501 HEM A CHC 1 
HETATM 7358 C  CHD . HEM C 2 .   ? -18.452 -12.344 13.508  1.00 30.75  ? 501 HEM A CHD 1 
HETATM 7359 C  C1A . HEM C 2 .   ? -16.578 -14.178 8.786   1.00 30.08  ? 501 HEM A C1A 1 
HETATM 7360 C  C2A . HEM C 2 .   ? -16.015 -14.676 7.580   1.00 32.10  ? 501 HEM A C2A 1 
HETATM 7361 C  C3A . HEM C 2 .   ? -14.676 -14.457 7.640   1.00 28.27  ? 501 HEM A C3A 1 
HETATM 7362 C  C4A . HEM C 2 .   ? -14.403 -13.820 8.878   1.00 31.27  ? 501 HEM A C4A 1 
HETATM 7363 C  CMA . HEM C 2 .   ? -13.643 -14.824 6.586   1.00 28.96  ? 501 HEM A CMA 1 
HETATM 7364 C  CAA . HEM C 2 .   ? -16.767 -15.337 6.440   1.00 30.59  ? 501 HEM A CAA 1 
HETATM 7365 C  CBA . HEM C 2 .   ? -16.830 -16.863 6.629   1.00 29.36  ? 501 HEM A CBA 1 
HETATM 7366 C  CGA . HEM C 2 .   ? -17.578 -17.520 5.486   1.00 31.27  ? 501 HEM A CGA 1 
HETATM 7367 O  O1A . HEM C 2 .   ? -17.938 -18.725 5.604   1.00 31.69  ? 501 HEM A O1A 1 
HETATM 7368 O  O2A . HEM C 2 .   ? -17.845 -16.874 4.430   1.00 30.74  ? 501 HEM A O2A 1 
HETATM 7369 C  C1B . HEM C 2 .   ? -12.920 -12.779 10.561  1.00 33.29  ? 501 HEM A C1B 1 
HETATM 7370 C  C2B . HEM C 2 .   ? -11.620 -12.379 10.994  1.00 29.75  ? 501 HEM A C2B 1 
HETATM 7371 C  C3B . HEM C 2 .   ? -11.764 -11.795 12.229  1.00 30.16  ? 501 HEM A C3B 1 
HETATM 7372 C  C4B . HEM C 2 .   ? -13.209 -11.845 12.539  1.00 32.82  ? 501 HEM A C4B 1 
HETATM 7373 C  CMB . HEM C 2 .   ? -10.355 -12.600 10.184  1.00 34.44  ? 501 HEM A CMB 1 
HETATM 7374 C  CAB . HEM C 2 .   ? -10.763 -11.211 13.148  1.00 34.96  ? 501 HEM A CAB 1 
HETATM 7375 C  CBB . HEM C 2 .   ? -9.812  -10.391 12.688  1.00 35.74  ? 501 HEM A CBB 1 
HETATM 7376 C  C1C . HEM C 2 .   ? -15.076 -11.432 14.063  1.00 31.75  ? 501 HEM A C1C 1 
HETATM 7377 C  C2C . HEM C 2 .   ? -15.665 -10.961 15.253  1.00 31.67  ? 501 HEM A C2C 1 
HETATM 7378 C  C3C . HEM C 2 .   ? -17.016 -11.255 15.187  1.00 32.87  ? 501 HEM A C3C 1 
HETATM 7379 C  C4C . HEM C 2 .   ? -17.238 -11.890 13.933  1.00 30.38  ? 501 HEM A C4C 1 
HETATM 7380 C  CMC . HEM C 2 .   ? -14.920 -10.281 16.373  1.00 33.92  ? 501 HEM A CMC 1 
HETATM 7381 C  CAC . HEM C 2 .   ? -18.073 -10.946 16.181  1.00 34.58  ? 501 HEM A CAC 1 
HETATM 7382 C  CBC . HEM C 2 .   ? -17.828 -10.851 17.482  1.00 37.41  ? 501 HEM A CBC 1 
HETATM 7383 C  C1D . HEM C 2 .   ? -18.626 -12.946 12.260  1.00 30.73  ? 501 HEM A C1D 1 
HETATM 7384 C  C2D . HEM C 2 .   ? -19.976 -13.384 11.841  1.00 33.84  ? 501 HEM A C2D 1 
HETATM 7385 C  C3D . HEM C 2 .   ? -19.841 -13.910 10.611  1.00 29.85  ? 501 HEM A C3D 1 
HETATM 7386 C  C4D . HEM C 2 .   ? -18.407 -13.779 10.273  1.00 29.42  ? 501 HEM A C4D 1 
HETATM 7387 C  CMD . HEM C 2 .   ? -21.255 -13.241 12.657  1.00 32.92  ? 501 HEM A CMD 1 
HETATM 7388 C  CAD . HEM C 2 .   ? -20.954 -14.434 9.727   1.00 30.26  ? 501 HEM A CAD 1 
HETATM 7389 C  CBD . HEM C 2 .   ? -21.567 -13.170 9.096   1.00 28.29  ? 501 HEM A CBD 1 
HETATM 7390 C  CGD . HEM C 2 .   ? -22.703 -13.447 8.109   1.00 31.22  ? 501 HEM A CGD 1 
HETATM 7391 O  O1D . HEM C 2 .   ? -22.597 -14.335 7.245   1.00 32.61  ? 501 HEM A O1D 1 
HETATM 7392 O  O2D . HEM C 2 .   ? -23.757 -12.763 8.154   1.00 31.54  ? 501 HEM A O2D 1 
HETATM 7393 N  NA  . HEM C 2 .   ? -15.578 -13.640 9.575   1.00 29.67  ? 501 HEM A NA  1 
HETATM 7394 N  NB  . HEM C 2 .   ? -13.815 -12.429 11.499  1.00 31.01  ? 501 HEM A NB  1 
HETATM 7395 N  NC  . HEM C 2 .   ? -16.038 -11.981 13.277  1.00 32.41  ? 501 HEM A NC  1 
HETATM 7396 N  ND  . HEM C 2 .   ? -17.720 -13.206 11.300  1.00 28.38  ? 501 HEM A ND  1 
HETATM 7397 FE FE  . HEM C 2 .   ? -15.874 -12.726 11.333  1.00 30.84  ? 501 HEM A FE  1 
HETATM 7398 C  C1  . D0L D 3 .   ? -12.955 -30.567 1.719   1.00 45.11  ? 502 D0L A C1  1 
HETATM 7399 C  C2  . D0L D 3 .   ? -12.963 -30.740 3.107   1.00 42.22  ? 502 D0L A C2  1 
HETATM 7400 C  C15 . D0L D 3 .   ? -11.285 -25.130 7.365   1.00 39.97  ? 502 D0L A C15 1 
HETATM 7401 C  C14 . D0L D 3 .   ? -10.269 -27.270 7.943   1.00 43.79  ? 502 D0L A C14 1 
HETATM 7402 C  C7  . D0L D 3 .   ? -12.331 -29.708 4.012   1.00 42.07  ? 502 D0L A C7  1 
HETATM 7403 C  C12 . D0L D 3 .   ? -9.092  -27.485 5.884   1.00 42.13  ? 502 D0L A C12 1 
HETATM 7404 C  C10 . D0L D 3 .   ? -11.144 -26.978 4.527   1.00 43.09  ? 502 D0L A C10 1 
HETATM 7405 C  C3  . D0L D 3 .   ? -13.532 -31.881 3.664   1.00 48.64  ? 502 D0L A C3  1 
HETATM 7406 C  C13 . D0L D 3 .   ? -9.469  -28.278 7.132   1.00 45.20  ? 502 D0L A C13 1 
HETATM 7407 C  C11 . D0L D 3 .   ? -10.260 -26.518 5.666   1.00 44.98  ? 502 D0L A C11 1 
HETATM 7408 C  C6  . D0L D 3 .   ? -13.536 -31.534 0.898   1.00 47.56  ? 502 D0L A C6  1 
HETATM 7409 C  C8  . D0L D 3 .   ? -13.033 -28.358 3.902   1.00 39.13  ? 502 D0L A C8  1 
HETATM 7410 C  C5  . D0L D 3 .   ? -14.105 -32.685 1.456   1.00 46.92  ? 502 D0L A C5  1 
HETATM 7411 C  C9  . D0L D 3 .   ? -14.499 -28.495 4.247   1.00 37.98  ? 502 D0L A C9  1 
HETATM 7412 C  C4  . D0L D 3 .   ? -14.099 -32.849 2.835   1.00 43.77  ? 502 D0L A C4  1 
HETATM 7413 O  O2  . D0L D 3 .   ? -14.759 -28.203 5.446   1.00 43.12  ? 502 D0L A O2  1 
HETATM 7414 O  O3  . D0L D 3 .   ? -10.777 -26.905 3.356   1.00 40.21  ? 502 D0L A O3  1 
HETATM 7415 O  O1  . D0L D 3 .   ? -15.359 -28.910 3.396   1.00 44.05  ? 502 D0L A O1  1 
HETATM 7416 N  N2  . D0L D 3 .   ? -11.028 -26.508 6.933   1.00 44.88  ? 502 D0L A N2  1 
HETATM 7417 C  C16 . D0L D 3 .   ? -12.653 -24.722 6.826   1.00 41.40  ? 502 D0L A C16 1 
HETATM 7418 C  C17 . D0L D 3 .   ? -12.961 -23.236 7.019   1.00 45.92  ? 502 D0L A C17 1 
HETATM 7419 C  C18 . D0L D 3 .   ? -13.261 -22.843 8.464   1.00 45.51  ? 502 D0L A C18 1 
HETATM 7420 C  C19 . D0L D 3 .   ? -12.977 -21.354 8.614   1.00 44.93  ? 502 D0L A C19 1 
HETATM 7421 C  C20 . D0L D 3 .   ? -13.350 -20.801 9.976   1.00 49.85  ? 502 D0L A C20 1 
HETATM 7422 C  C21 . D0L D 3 .   ? -14.848 -20.781 10.145  1.00 55.56  ? 502 D0L A C21 1 
HETATM 7423 N  N1  . D0L D 3 .   ? -12.339 -27.489 4.832   1.00 39.36  ? 502 D0L A N1  1 
HETATM 7424 C  CAF A SYN E 4 .   ? -17.457 -16.946 13.245  0.72 39.69  ? 503 SYN A CAF 1 
HETATM 7425 C  CAD A SYN E 4 .   ? -16.734 -16.256 12.286  0.72 38.76  ? 503 SYN A CAD 1 
HETATM 7426 C  CAC A SYN E 4 .   ? -16.358 -16.882 11.116  0.72 38.53  ? 503 SYN A CAC 1 
HETATM 7427 C  CAE A SYN E 4 .   ? -16.708 -18.193 10.899  0.72 39.82  ? 503 SYN A CAE 1 
HETATM 7428 C  CAG A SYN E 4 .   ? -17.435 -18.886 11.851  0.72 33.40  ? 503 SYN A CAG 1 
HETATM 7429 C  CAH A SYN E 4 .   ? -17.823 -18.275 13.042  0.72 40.08  ? 503 SYN A CAH 1 
HETATM 7430 C  CAB A SYN E 4 .   ? -18.598 -19.017 14.051  0.72 39.09  ? 503 SYN A CAB 1 
HETATM 7431 C  CAA A SYN E 4 .   ? -19.005 -20.248 13.967  0.72 37.62  ? 503 SYN A CAA 1 
HETATM 7432 C  C1  . GOL F 5 .   ? 8.974   -7.064  33.261  1.00 46.36  ? 504 GOL A C1  1 
HETATM 7433 O  O1  . GOL F 5 .   ? 9.421   -7.070  34.596  1.00 51.29  ? 504 GOL A O1  1 
HETATM 7434 C  C2  . GOL F 5 .   ? 7.764   -6.109  33.250  1.00 43.90  ? 504 GOL A C2  1 
HETATM 7435 O  O2  . GOL F 5 .   ? 8.123   -4.808  33.666  1.00 52.64  ? 504 GOL A O2  1 
HETATM 7436 C  C3  . GOL F 5 .   ? 7.250   -6.086  31.807  1.00 48.19  ? 504 GOL A C3  1 
HETATM 7437 O  O3  . GOL F 5 .   ? 6.544   -7.307  31.547  1.00 50.34  ? 504 GOL A O3  1 
HETATM 7438 H  H11 . GOL F 5 .   ? 8.706   -7.941  32.946  1.00 55.66  ? 504 GOL A H11 1 
HETATM 7439 H  H12 . GOL F 5 .   ? 9.648   -6.752  32.636  1.00 55.66  ? 504 GOL A H12 1 
HETATM 7440 H  HO1 . GOL F 5 .   ? 9.809   -6.323  34.725  1.00 61.58  ? 504 GOL A HO1 1 
HETATM 7441 H  H2  . GOL F 5 .   ? 7.087   -6.441  33.859  1.00 52.71  ? 504 GOL A H2  1 
HETATM 7442 H  HO2 . GOL F 5 .   ? 8.764   -4.543  33.166  1.00 63.20  ? 504 GOL A HO2 1 
HETATM 7443 H  H31 . GOL F 5 .   ? 8.008   -5.953  31.216  1.00 57.86  ? 504 GOL A H31 1 
HETATM 7444 H  H32 . GOL F 5 .   ? 6.696   -5.297  31.694  1.00 57.86  ? 504 GOL A H32 1 
HETATM 7445 H  HO3 . GOL F 5 .   ? 7.090   -7.812  31.127  1.00 60.44  ? 504 GOL A HO3 1 
HETATM 7446 C  C1  . GOL G 5 .   ? -13.918 -2.352  36.069  1.00 45.43  ? 505 GOL A C1  1 
HETATM 7447 O  O1  . GOL G 5 .   ? -13.027 -3.225  35.489  1.00 42.79  ? 505 GOL A O1  1 
HETATM 7448 C  C2  . GOL G 5 .   ? -13.203 -1.828  37.297  1.00 55.33  ? 505 GOL A C2  1 
HETATM 7449 O  O2  . GOL G 5 .   ? -12.382 -0.747  36.976  1.00 60.73  ? 505 GOL A O2  1 
HETATM 7450 C  C3  . GOL G 5 .   ? -14.361 -1.499  38.247  1.00 57.11  ? 505 GOL A C3  1 
HETATM 7451 O  O3  . GOL G 5 .   ? -15.421 -2.295  37.792  1.00 59.54  ? 505 GOL A O3  1 
HETATM 7452 C  CHA . HEM H 2 .   ? 6.449   -14.180 65.816  1.00 32.74  ? 501 HEM B CHA 1 
HETATM 7453 C  CHB . HEM H 2 .   ? 1.623   -13.708 65.692  1.00 30.70  ? 501 HEM B CHB 1 
HETATM 7454 C  CHC . HEM H 2 .   ? 1.980   -11.486 61.353  1.00 32.52  ? 501 HEM B CHC 1 
HETATM 7455 C  CHD . HEM H 2 .   ? 6.755   -12.216 61.391  1.00 30.97  ? 501 HEM B CHD 1 
HETATM 7456 C  C1A . HEM H 2 .   ? 5.107   -14.212 66.137  1.00 31.61  ? 501 HEM B C1A 1 
HETATM 7457 C  C2A . HEM H 2 .   ? 4.620   -14.751 67.351  1.00 30.61  ? 501 HEM B C2A 1 
HETATM 7458 C  C3A . HEM H 2 .   ? 3.265   -14.636 67.319  1.00 30.51  ? 501 HEM B C3A 1 
HETATM 7459 C  C4A . HEM H 2 .   ? 2.905   -14.007 66.102  1.00 30.67  ? 501 HEM B C4A 1 
HETATM 7460 C  CMA . HEM H 2 .   ? 2.331   -15.061 68.430  1.00 28.81  ? 501 HEM B CMA 1 
HETATM 7461 C  CAA . HEM H 2 .   ? 5.439   -15.348 68.492  1.00 28.48  ? 501 HEM B CAA 1 
HETATM 7462 C  CBA . HEM H 2 .   ? 5.587   -16.865 68.291  1.00 29.98  ? 501 HEM B CBA 1 
HETATM 7463 C  CGA . HEM H 2 .   ? 6.370   -17.588 69.371  1.00 29.95  ? 501 HEM B CGA 1 
HETATM 7464 O  O1A . HEM H 2 .   ? 6.790   -18.755 69.131  1.00 30.97  ? 501 HEM B O1A 1 
HETATM 7465 O  O2A . HEM H 2 .   ? 6.589   -17.069 70.500  1.00 30.85  ? 501 HEM B O2A 1 
HETATM 7466 C  C1B . HEM H 2 .   ? 1.328   -13.057 64.485  1.00 28.96  ? 501 HEM B C1B 1 
HETATM 7467 C  C2B . HEM H 2 .   ? -0.009  -12.740 64.087  1.00 27.53  ? 501 HEM B C2B 1 
HETATM 7468 C  C3B . HEM H 2 .   ? 0.079   -12.106 62.874  1.00 29.91  ? 501 HEM B C3B 1 
HETATM 7469 C  C4B . HEM H 2 .   ? 1.517   -12.066 62.535  1.00 31.65  ? 501 HEM B C4B 1 
HETATM 7470 C  CMB . HEM H 2 .   ? -1.248  -13.056 64.905  1.00 29.45  ? 501 HEM B CMB 1 
HETATM 7471 C  CAB . HEM H 2 .   ? -0.962  -11.554 61.989  1.00 34.73  ? 501 HEM B CAB 1 
HETATM 7472 C  CBB . HEM H 2 .   ? -2.088  -11.059 62.508  1.00 30.65  ? 501 HEM B CBB 1 
HETATM 7473 C  C1C . HEM H 2 .   ? 3.317   -11.484 60.969  1.00 35.03  ? 501 HEM B C1C 1 
HETATM 7474 C  C2C . HEM H 2 .   ? 3.842   -10.962 59.771  1.00 34.49  ? 501 HEM B C2C 1 
HETATM 7475 C  C3C . HEM H 2 .   ? 5.212   -11.190 59.790  1.00 32.35  ? 501 HEM B C3C 1 
HETATM 7476 C  C4C . HEM H 2 .   ? 5.501   -11.827 61.026  1.00 33.20  ? 501 HEM B C4C 1 
HETATM 7477 C  CMC . HEM H 2 .   ? 3.029   -10.310 58.678  1.00 30.97  ? 501 HEM B CMC 1 
HETATM 7478 C  CAC . HEM H 2 .   ? 6.234   -10.842 58.781  1.00 32.83  ? 501 HEM B CAC 1 
HETATM 7479 C  CBC . HEM H 2 .   ? 6.151   -9.714  58.091  1.00 40.52  ? 501 HEM B CBC 1 
HETATM 7480 C  C1D . HEM H 2 .   ? 7.004   -12.818 62.624  1.00 30.97  ? 501 HEM B C1D 1 
HETATM 7481 C  C2D . HEM H 2 .   ? 8.380   -13.189 62.993  1.00 31.94  ? 501 HEM B C2D 1 
HETATM 7482 C  C3D . HEM H 2 .   ? 8.305   -13.739 64.215  1.00 29.82  ? 501 HEM B C3D 1 
HETATM 7483 C  C4D . HEM H 2 .   ? 6.874   -13.696 64.589  1.00 32.33  ? 501 HEM B C4D 1 
HETATM 7484 C  CMD . HEM H 2 .   ? 9.637   -13.004 62.157  1.00 31.34  ? 501 HEM B CMD 1 
HETATM 7485 C  CAD . HEM H 2 .   ? 9.480   -14.226 65.040  1.00 31.90  ? 501 HEM B CAD 1 
HETATM 7486 C  CBD . HEM H 2 .   ? 10.000  -12.975 65.789  1.00 29.15  ? 501 HEM B CBD 1 
HETATM 7487 C  CGD . HEM H 2 .   ? 11.226  -13.219 66.660  1.00 33.64  ? 501 HEM B CGD 1 
HETATM 7488 O  O1D . HEM H 2 .   ? 11.223  -14.107 67.527  1.00 33.75  ? 501 HEM B O1D 1 
HETATM 7489 O  O2D . HEM H 2 .   ? 12.263  -12.514 66.528  1.00 31.49  ? 501 HEM B O2D 1 
HETATM 7490 N  NA  . HEM H 2 .   ? 4.044   -13.766 65.365  1.00 30.85  ? 501 HEM B NA  1 
HETATM 7491 N  NB  . HEM H 2 .   ? 2.162   -12.655 63.532  1.00 29.87  ? 501 HEM B NB  1 
HETATM 7492 N  NC  . HEM H 2 .   ? 4.322   -12.001 61.714  1.00 31.49  ? 501 HEM B NC  1 
HETATM 7493 N  ND  . HEM H 2 .   ? 6.132   -13.146 63.595  1.00 27.50  ? 501 HEM B ND  1 
HETATM 7494 FE FE  . HEM H 2 .   ? 4.234   -12.844 63.610  1.00 31.02  ? 501 HEM B FE  1 
HETATM 7495 C  C1  . D0L I 3 .   ? 4.027   -31.457 70.959  1.00 47.30  ? 502 D0L B C1  1 
HETATM 7496 C  C2  . D0L I 3 .   ? 2.781   -30.837 70.948  1.00 47.72  ? 502 D0L B C2  1 
HETATM 7497 C  C15 . D0L I 3 .   ? 0.122   -25.790 67.599  1.00 39.65  ? 502 D0L B C15 1 
HETATM 7498 C  C14 . D0L I 3 .   ? -0.489  -28.040 67.067  1.00 36.89  ? 502 D0L B C14 1 
HETATM 7499 C  C7  . D0L I 3 .   ? 2.529   -29.615 71.795  1.00 48.90  ? 502 D0L B C7  1 
HETATM 7500 C  C12 . D0L I 3 .   ? -1.346  -28.614 69.226  1.00 42.17  ? 502 D0L B C12 1 
HETATM 7501 C  C10 . D0L I 3 .   ? 0.500   -27.646 70.427  1.00 34.13  ? 502 D0L B C10 1 
HETATM 7502 C  C3  . D0L I 3 .   ? 1.776   -31.324 70.129  1.00 47.63  ? 502 D0L B C3  1 
HETATM 7503 C  C13 . D0L I 3 .   ? -0.968  -29.223 67.882  1.00 37.24  ? 502 D0L B C13 1 
HETATM 7504 C  C11 . D0L I 3 .   ? -0.490  -27.359 69.351  1.00 37.22  ? 502 D0L B C11 1 
HETATM 7505 C  C6  . D0L I 3 .   ? 4.270   -32.574 70.169  1.00 50.02  ? 502 D0L B C6  1 
HETATM 7506 C  C8  . D0L I 3 .   ? 2.756   -28.351 70.965  1.00 37.30  ? 502 D0L B C8  1 
HETATM 7507 C  C5  . D0L I 3 .   ? 3.258   -33.080 69.358  1.00 50.10  ? 502 D0L B C5  1 
HETATM 7508 C  C9  . D0L I 3 .   ? 4.065   -28.446 70.254  1.00 38.94  ? 502 D0L B C9  1 
HETATM 7509 C  C4  . D0L I 3 .   ? 2.012   -32.451 69.335  1.00 50.50  ? 502 D0L B C4  1 
HETATM 7510 O  O2  . D0L I 3 .   ? 5.081   -28.666 70.943  1.00 39.33  ? 502 D0L B O2  1 
HETATM 7511 O  O3  . D0L I 3 .   ? 0.194   -27.489 71.599  1.00 36.03  ? 502 D0L B O3  1 
HETATM 7512 O  O1  . D0L I 3 .   ? 4.095   -28.288 69.014  1.00 36.58  ? 502 D0L B O1  1 
HETATM 7513 N  N2  . D0L I 3 .   ? 0.187   -27.184 68.043  1.00 43.69  ? 502 D0L B N2  1 
HETATM 7514 C  C16 . D0L I 3 .   ? 1.254   -25.000 68.246  1.00 41.42  ? 502 D0L B C16 1 
HETATM 7515 C  C17 . D0L I 3 .   ? 1.112   -23.505 67.936  1.00 42.53  ? 502 D0L B C17 1 
HETATM 7516 C  C18 . D0L I 3 .   ? 1.808   -23.077 66.652  1.00 43.51  ? 502 D0L B C18 1 
HETATM 7517 C  C19 . D0L I 3 .   ? 1.580   -21.586 66.409  1.00 39.62  ? 502 D0L B C19 1 
HETATM 7518 C  C20 . D0L I 3 .   ? 2.226   -21.166 65.100  1.00 45.95  ? 502 D0L B C20 1 
HETATM 7519 C  C21 . D0L I 3 .   ? 3.538   -21.898 64.969  1.00 50.27  ? 502 D0L B C21 1 
HETATM 7520 N  N1  . D0L I 3 .   ? 1.675   -28.122 70.033  1.00 38.05  ? 502 D0L B N1  1 
HETATM 7521 C  CAF A SYN J 4 .   ? 5.510   -16.868 62.131  0.65 42.81  ? 503 SYN B CAF 1 
HETATM 7522 C  CAD A SYN J 4 .   ? 4.718   -16.507 63.207  0.65 40.41  ? 503 SYN B CAD 1 
HETATM 7523 C  CAC A SYN J 4 .   ? 4.536   -17.376 64.260  0.65 35.50  ? 503 SYN B CAC 1 
HETATM 7524 C  CAE A SYN J 4 .   ? 5.136   -18.613 64.232  0.65 45.76  ? 503 SYN B CAE 1 
HETATM 7525 C  CAG A SYN J 4 .   ? 5.924   -18.983 63.155  0.65 39.66  ? 503 SYN B CAG 1 
HETATM 7526 C  CAH A SYN J 4 .   ? 6.132   -18.116 62.086  0.65 43.74  ? 503 SYN B CAH 1 
HETATM 7527 C  CAB A SYN J 4 .   ? 6.981   -18.509 60.948  0.65 40.35  ? 503 SYN B CAB 1 
HETATM 7528 C  CAA A SYN J 4 .   ? 7.625   -19.630 60.807  0.65 39.80  ? 503 SYN B CAA 1 
HETATM 7529 C  C1  . GOL K 5 .   ? 3.587   -7.400  71.834  1.00 52.42  ? 504 GOL B C1  1 
HETATM 7530 O  O1  . GOL K 5 .   ? 2.298   -6.972  71.429  1.00 50.19  ? 504 GOL B O1  1 
HETATM 7531 C  C2  . GOL K 5 .   ? 3.710   -7.266  73.398  1.00 46.96  ? 504 GOL B C2  1 
HETATM 7532 O  O2  . GOL K 5 .   ? 2.649   -7.845  74.075  1.00 46.44  ? 504 GOL B O2  1 
HETATM 7533 C  C3  . GOL K 5 .   ? 5.079   -7.924  73.743  1.00 43.67  ? 504 GOL B C3  1 
HETATM 7534 O  O3  . GOL K 5 .   ? 5.116   -8.229  75.125  1.00 39.70  ? 504 GOL B O3  1 
HETATM 7535 O  O   . HOH L 6 .   ? -27.816 -23.194 -14.290 1.00 47.77  ? 601 HOH A O   1 
HETATM 7536 O  O   . HOH L 6 .   ? -22.004 4.255   19.332  1.00 45.39  ? 602 HOH A O   1 
HETATM 7537 O  O   . HOH L 6 .   ? 11.543  -13.809 36.866  1.00 52.66  ? 603 HOH A O   1 
HETATM 7538 O  O   . HOH L 6 .   ? 5.369   -20.464 28.398  1.00 49.39  ? 604 HOH A O   1 
HETATM 7539 O  O   . HOH L 6 .   ? -12.632 -8.640  18.302  1.00 38.61  ? 605 HOH A O   1 
HETATM 7540 O  O   . HOH L 6 .   ? -5.439  -22.856 -14.684 1.00 49.16  ? 606 HOH A O   1 
HETATM 7541 O  O   . HOH L 6 .   ? -16.905 -26.812 -0.972  1.00 39.07  ? 607 HOH A O   1 
HETATM 7542 O  O   . HOH L 6 .   ? -18.474 0.407   26.395  1.00 40.66  ? 608 HOH A O   1 
HETATM 7543 O  O   . HOH L 6 .   ? -28.690 -3.819  16.399  1.00 45.00  ? 609 HOH A O   1 
HETATM 7544 O  O   . HOH L 6 .   ? 2.222   8.895   23.957  1.00 43.83  ? 610 HOH A O   1 
HETATM 7545 O  O   . HOH L 6 .   ? 1.464   -40.452 0.638   1.00 42.47  ? 611 HOH A O   1 
HETATM 7546 O  O   . HOH L 6 .   ? -35.396 -10.320 6.755   1.00 44.52  ? 612 HOH A O   1 
HETATM 7547 O  O   . HOH L 6 .   ? -6.321  -10.755 -12.367 1.00 45.60  ? 613 HOH A O   1 
HETATM 7548 O  O   . HOH L 6 .   ? 10.863  -15.297 21.599  1.00 36.69  ? 614 HOH A O   1 
HETATM 7549 O  O   . HOH L 6 .   ? -10.005 10.409  14.643  1.00 45.45  ? 615 HOH A O   1 
HETATM 7550 O  O   . HOH L 6 .   ? -8.795  -23.405 10.778  1.00 42.96  ? 616 HOH A O   1 
HETATM 7551 O  O   . HOH L 6 .   ? 0.687   -21.750 22.565  1.00 35.31  ? 617 HOH A O   1 
HETATM 7552 O  O   . HOH L 6 .   ? -18.076 -27.361 30.323  1.00 47.44  ? 618 HOH A O   1 
HETATM 7553 O  O   . HOH L 6 .   ? -2.870  -27.949 14.595  1.00 41.83  ? 619 HOH A O   1 
HETATM 7554 O  O   . HOH L 6 .   ? -4.967  2.111   8.386   1.00 40.03  ? 620 HOH A O   1 
HETATM 7555 O  O   . HOH L 6 .   ? -23.564 -29.350 -9.156  1.00 49.15  ? 621 HOH A O   1 
HETATM 7556 O  O   . HOH L 6 .   ? -32.339 -14.879 4.549   1.00 37.17  ? 622 HOH A O   1 
HETATM 7557 O  O   . HOH L 6 .   ? -1.779  -34.130 4.048   1.00 40.85  ? 623 HOH A O   1 
HETATM 7558 O  O   . HOH L 6 .   ? -26.367 -28.720 -11.625 1.00 45.54  ? 624 HOH A O   1 
HETATM 7559 O  O   . HOH L 6 .   ? -10.439 -48.087 -1.983  1.00 48.17  ? 625 HOH A O   1 
HETATM 7560 O  O   . HOH L 6 .   ? 8.967   -4.145  5.737   1.00 43.87  ? 626 HOH A O   1 
HETATM 7561 O  O   . HOH L 6 .   ? -18.117 -11.917 -12.844 1.00 47.01  ? 627 HOH A O   1 
HETATM 7562 O  O   . HOH L 6 .   ? 6.856   -0.557  21.474  1.00 38.42  ? 628 HOH A O   1 
HETATM 7563 O  O   . HOH L 6 .   ? -7.567  -2.421  35.446  1.00 38.81  ? 629 HOH A O   1 
HETATM 7564 O  O   . HOH L 6 .   ? 1.367   1.387   32.885  1.00 44.56  ? 630 HOH A O   1 
HETATM 7565 O  O   . HOH L 6 .   ? -1.196  0.482   -1.689  1.00 47.42  ? 631 HOH A O   1 
HETATM 7566 O  O   . HOH L 6 .   ? -4.105  -25.395 -11.168 1.00 33.33  ? 632 HOH A O   1 
HETATM 7567 O  O   . HOH L 6 .   ? 8.305   -21.302 22.314  1.00 43.73  ? 633 HOH A O   1 
HETATM 7568 O  O   . HOH L 6 .   ? -22.199 -9.617  6.527   1.00 41.92  ? 634 HOH A O   1 
HETATM 7569 O  O   . HOH L 6 .   ? -7.729  -26.117 9.902   1.00 40.94  ? 635 HOH A O   1 
HETATM 7570 O  O   . HOH L 6 .   ? 3.106   -24.544 11.265  1.00 38.94  ? 636 HOH A O   1 
HETATM 7571 O  O   . HOH L 6 .   ? -23.937 -10.182 8.585   1.00 40.30  ? 637 HOH A O   1 
HETATM 7572 O  O   . HOH L 6 .   ? -17.539 3.923   24.983  1.00 36.36  ? 638 HOH A O   1 
HETATM 7573 O  O   . HOH L 6 .   ? -4.104  -14.098 -10.305 1.00 34.09  ? 639 HOH A O   1 
HETATM 7574 O  O   . HOH L 6 .   ? -29.948 -10.614 0.555   1.00 48.52  ? 640 HOH A O   1 
HETATM 7575 O  O   . HOH L 6 .   ? -30.161 -3.123  9.262   1.00 43.95  ? 641 HOH A O   1 
HETATM 7576 O  O   . HOH L 6 .   ? 4.281   1.519   30.370  1.00 40.69  ? 642 HOH A O   1 
HETATM 7577 O  O   . HOH L 6 .   ? -26.534 -6.290  3.632   1.00 50.29  ? 643 HOH A O   1 
HETATM 7578 O  O   . HOH L 6 .   ? 3.135   -14.503 31.489  1.00 41.90  ? 644 HOH A O   1 
HETATM 7579 O  O   . HOH L 6 .   ? 8.164   -1.115  5.967   1.00 45.44  ? 645 HOH A O   1 
HETATM 7580 O  O   . HOH L 6 .   ? -19.111 -29.536 -5.892  1.00 38.96  ? 646 HOH A O   1 
HETATM 7581 O  O   . HOH L 6 .   ? -19.978 -30.811 2.922   1.00 56.40  ? 647 HOH A O   1 
HETATM 7582 O  O   . HOH L 6 .   ? -34.598 -9.403  17.525  1.00 44.39  ? 648 HOH A O   1 
HETATM 7583 O  O   . HOH L 6 .   ? -4.712  -7.121  34.949  1.00 32.17  ? 649 HOH A O   1 
HETATM 7584 O  O   . HOH L 6 .   ? -17.989 -14.528 3.184   1.00 30.28  ? 650 HOH A O   1 
HETATM 7585 O  O   . HOH L 6 .   ? 4.718   -17.878 4.725   1.00 42.29  ? 651 HOH A O   1 
HETATM 7586 O  O   . HOH L 6 .   ? -33.595 -24.203 7.488   1.00 36.96  ? 652 HOH A O   1 
HETATM 7587 O  O   . HOH L 6 .   ? -23.473 -19.118 -11.496 1.00 42.96  ? 653 HOH A O   1 
HETATM 7588 O  O   . HOH L 6 .   ? -6.818  -44.053 -5.891  1.00 32.48  ? 654 HOH A O   1 
HETATM 7589 O  O   . HOH L 6 .   ? -10.138 -10.675 33.166  1.00 32.39  ? 655 HOH A O   1 
HETATM 7590 O  O   . HOH L 6 .   ? -14.516 -26.809 -14.305 1.00 46.45  ? 656 HOH A O   1 
HETATM 7591 O  O   . HOH L 6 .   ? -10.655 -14.177 -14.388 1.00 40.17  ? 657 HOH A O   1 
HETATM 7592 O  O   . HOH L 6 .   ? -16.203 -22.443 5.148   1.00 33.65  ? 658 HOH A O   1 
HETATM 7593 O  O   . HOH L 6 .   ? -20.376 -15.646 6.516   1.00 31.20  ? 659 HOH A O   1 
HETATM 7594 O  O   . HOH L 6 .   ? -6.649  -41.283 6.863   1.00 52.42  ? 660 HOH A O   1 
HETATM 7595 O  O   . HOH L 6 .   ? -37.437 -16.312 11.912  1.00 46.15  ? 661 HOH A O   1 
HETATM 7596 O  O   . HOH L 6 .   ? -9.319  12.186  22.285  1.00 46.13  ? 662 HOH A O   1 
HETATM 7597 O  O   . HOH L 6 .   ? -9.276  -5.006  -3.565  1.00 37.59  ? 663 HOH A O   1 
HETATM 7598 O  O   . HOH L 6 .   ? -18.139 -20.704 3.796   1.00 31.80  ? 664 HOH A O   1 
HETATM 7599 O  O   . HOH L 6 .   ? -16.516 -15.391 35.079  1.00 41.52  ? 665 HOH A O   1 
HETATM 7600 O  O   . HOH L 6 .   ? -9.496  -2.089  33.360  1.00 36.10  ? 666 HOH A O   1 
HETATM 7601 O  O   . HOH L 6 .   ? -9.211  -4.840  6.535   1.00 43.95  ? 667 HOH A O   1 
HETATM 7602 O  O   . HOH L 6 .   ? 12.802  -7.604  17.652  1.00 48.82  ? 668 HOH A O   1 
HETATM 7603 O  O   . HOH L 6 .   ? -24.649 -12.401 -13.621 1.00 43.54  ? 669 HOH A O   1 
HETATM 7604 O  O   . HOH L 6 .   ? -7.419  0.460   12.429  1.00 47.56  ? 670 HOH A O   1 
HETATM 7605 O  O   . HOH L 6 .   ? -8.001  6.512   -4.942  1.00 34.05  ? 671 HOH A O   1 
HETATM 7606 O  O   . HOH L 6 .   ? -26.112 -19.703 1.338   1.00 33.41  ? 672 HOH A O   1 
HETATM 7607 O  O   . HOH L 6 .   ? -15.706 -10.531 29.901  1.00 34.37  ? 673 HOH A O   1 
HETATM 7608 O  O   . HOH L 6 .   ? -6.050  -18.170 26.995  1.00 39.21  ? 674 HOH A O   1 
HETATM 7609 O  O   . HOH L 6 .   ? -15.267 -17.164 -17.735 1.00 46.81  ? 675 HOH A O   1 
HETATM 7610 O  O   . HOH L 6 .   ? -2.364  4.354   27.590  1.00 42.29  ? 676 HOH A O   1 
HETATM 7611 O  O   . HOH L 6 .   ? -27.611 -15.859 -3.706  1.00 41.84  ? 677 HOH A O   1 
HETATM 7612 O  O   . HOH L 6 .   ? 6.408   -2.794  34.841  1.00 44.11  ? 678 HOH A O   1 
HETATM 7613 O  O   . HOH L 6 .   ? -12.620 -9.691  3.132   1.00 29.33  ? 679 HOH A O   1 
HETATM 7614 O  O   . HOH L 6 .   ? -14.175 -4.492  -5.285  1.00 38.12  ? 680 HOH A O   1 
HETATM 7615 O  O   . HOH L 6 .   ? -8.655  -2.446  -2.303  1.00 38.69  ? 681 HOH A O   1 
HETATM 7616 O  O   . HOH L 6 .   ? -11.871 -27.637 26.293  1.00 44.65  ? 682 HOH A O   1 
HETATM 7617 O  O   . HOH L 6 .   ? -18.141 -4.844  13.061  1.00 34.19  ? 683 HOH A O   1 
HETATM 7618 O  O   . HOH L 6 .   ? 0.476   -31.087 1.367   1.00 37.79  ? 684 HOH A O   1 
HETATM 7619 O  O   . HOH L 6 .   ? -4.101  -11.612 -3.847  1.00 35.97  ? 685 HOH A O   1 
HETATM 7620 O  O   . HOH L 6 .   ? -13.922 -10.090 31.846  1.00 30.94  ? 686 HOH A O   1 
HETATM 7621 O  O   . HOH L 6 .   ? -13.420 -9.954  20.921  1.00 35.21  ? 687 HOH A O   1 
HETATM 7622 O  O   . HOH L 6 .   ? -0.671  4.642   -4.520  1.00 39.15  ? 688 HOH A O   1 
HETATM 7623 O  O   . HOH L 6 .   ? -28.753 -15.911 11.571  1.00 33.31  ? 689 HOH A O   1 
HETATM 7624 O  O   . HOH L 6 .   ? -13.086 -8.498  33.956  1.00 35.55  ? 690 HOH A O   1 
HETATM 7625 O  O   . HOH L 6 .   ? 8.379   -22.982 17.734  1.00 41.20  ? 691 HOH A O   1 
HETATM 7626 O  O   . HOH L 6 .   ? -16.593 -6.766  -7.440  1.00 44.97  ? 692 HOH A O   1 
HETATM 7627 O  O   . HOH L 6 .   ? -25.512 -14.238 -3.830  1.00 33.71  ? 693 HOH A O   1 
HETATM 7628 O  O   . HOH L 6 .   ? -5.443  -22.423 16.413  1.00 40.72  ? 694 HOH A O   1 
HETATM 7629 O  O   . HOH L 6 .   ? -17.198 -31.941 22.328  1.00 43.30  ? 695 HOH A O   1 
HETATM 7630 O  O   . HOH L 6 .   ? 5.237   5.435   24.278  1.00 41.29  ? 696 HOH A O   1 
HETATM 7631 O  O   . HOH L 6 .   ? -22.236 -13.092 -0.485  1.00 31.42  ? 697 HOH A O   1 
HETATM 7632 O  O   . HOH L 6 .   ? -4.250  8.122   24.556  1.00 40.57  ? 698 HOH A O   1 
HETATM 7633 O  O   . HOH L 6 .   ? -35.729 -12.997 6.462   1.00 39.93  ? 699 HOH A O   1 
HETATM 7634 O  O   . HOH L 6 .   ? -13.003 2.016   30.424  1.00 41.63  ? 700 HOH A O   1 
HETATM 7635 O  O   . HOH L 6 .   ? -33.640 -18.511 27.298  1.00 50.85  ? 701 HOH A O   1 
HETATM 7636 O  O   . HOH L 6 .   ? 9.727   -18.009 12.379  1.00 41.36  ? 702 HOH A O   1 
HETATM 7637 O  O   . HOH L 6 .   ? -5.081  -37.742 -8.301  1.00 43.49  ? 703 HOH A O   1 
HETATM 7638 O  O   . HOH L 6 .   ? 1.048   -10.275 36.033  1.00 36.26  ? 704 HOH A O   1 
HETATM 7639 O  O   . HOH L 6 .   ? 4.842   6.299   12.436  1.00 42.46  ? 705 HOH A O   1 
HETATM 7640 O  O   . HOH L 6 .   ? 6.330   9.412   18.283  1.00 40.72  ? 706 HOH A O   1 
HETATM 7641 O  O   . HOH L 6 .   ? 13.615  -8.928  19.644  1.00 43.60  ? 707 HOH A O   1 
HETATM 7642 O  O   . HOH L 6 .   ? 2.311   -16.531 -6.991  1.00 46.07  ? 708 HOH A O   1 
HETATM 7643 O  O   . HOH L 6 .   ? -9.117  -14.492 7.690   1.00 34.72  ? 709 HOH A O   1 
HETATM 7644 O  O   . HOH L 6 .   ? -3.440  -12.536 11.110  1.00 36.01  ? 710 HOH A O   1 
HETATM 7645 O  O   . HOH L 6 .   ? -5.389  -23.853 -5.592  1.00 36.48  ? 711 HOH A O   1 
HETATM 7646 O  O   . HOH L 6 .   ? 2.709   -19.228 23.813  1.00 35.92  ? 712 HOH A O   1 
HETATM 7647 O  O   . HOH L 6 .   ? -27.557 -7.814  1.591   1.00 45.98  ? 713 HOH A O   1 
HETATM 7648 O  O   B HOH L 6 .   ? -15.377 -14.646 12.145  0.46 33.42  ? 714 HOH A O   1 
HETATM 7649 O  O   . HOH L 6 .   ? -19.976 -14.173 -1.542  1.00 31.03  ? 715 HOH A O   1 
HETATM 7650 O  O   . HOH L 6 .   ? -6.996  -8.453  35.499  1.00 34.15  ? 716 HOH A O   1 
HETATM 7651 O  O   . HOH L 6 .   ? 11.423  -8.146  38.589  1.00 43.53  ? 717 HOH A O   1 
HETATM 7652 O  O   . HOH L 6 .   ? -22.739 -9.141  -10.081 1.00 43.99  ? 718 HOH A O   1 
HETATM 7653 O  O   . HOH L 6 .   ? -16.457 6.479   22.554  1.00 46.72  ? 719 HOH A O   1 
HETATM 7654 O  O   . HOH L 6 .   ? 10.458  -20.462 21.135  1.00 39.39  ? 720 HOH A O   1 
HETATM 7655 O  O   . HOH L 6 .   ? -22.777 -6.984  -1.181  1.00 49.46  ? 721 HOH A O   1 
HETATM 7656 O  O   . HOH L 6 .   ? -12.264 -17.099 31.332  1.00 41.50  ? 722 HOH A O   1 
HETATM 7657 O  O   . HOH L 6 .   ? 1.331   -14.766 29.557  1.00 33.70  ? 723 HOH A O   1 
HETATM 7658 O  O   . HOH L 6 .   ? -18.788 -18.018 1.898   1.00 30.60  ? 724 HOH A O   1 
HETATM 7659 O  O   . HOH L 6 .   ? -24.578 -14.126 -1.342  1.00 35.85  ? 725 HOH A O   1 
HETATM 7660 O  O   . HOH L 6 .   ? -16.482 -8.259  -0.071  1.00 40.43  ? 726 HOH A O   1 
HETATM 7661 O  O   . HOH L 6 .   ? -23.283 -19.076 13.172  1.00 35.01  ? 727 HOH A O   1 
HETATM 7662 O  O   . HOH L 6 .   ? 9.616   -9.224  6.238   1.00 43.39  ? 728 HOH A O   1 
HETATM 7663 O  O   . HOH L 6 .   ? -15.082 -6.467  3.843   1.00 54.52  ? 729 HOH A O   1 
HETATM 7664 O  O   . HOH L 6 .   ? -34.726 -19.427 9.197   1.00 35.86  ? 730 HOH A O   1 
HETATM 7665 O  O   . HOH L 6 .   ? -10.227 -4.848  24.260  1.00 36.95  ? 731 HOH A O   1 
HETATM 7666 O  O   . HOH L 6 .   ? -1.982  -22.203 -11.818 1.00 43.18  ? 732 HOH A O   1 
HETATM 7667 O  O   . HOH L 6 .   ? -26.887 -27.836 -14.121 1.00 48.72  ? 733 HOH A O   1 
HETATM 7668 O  O   . HOH L 6 .   ? -20.070 -32.229 -3.545  1.00 50.68  ? 734 HOH A O   1 
HETATM 7669 O  O   . HOH L 6 .   ? -13.281 9.679   21.147  1.00 44.49  ? 735 HOH A O   1 
HETATM 7670 O  O   . HOH L 6 .   ? -16.596 -37.649 3.154   1.00 48.05  ? 736 HOH A O   1 
HETATM 7671 O  O   . HOH L 6 .   ? -33.118 -20.835 15.715  1.00 45.34  ? 737 HOH A O   1 
HETATM 7672 O  O   . HOH L 6 .   ? -12.177 -5.894  -3.810  1.00 35.58  ? 738 HOH A O   1 
HETATM 7673 O  O   . HOH L 6 .   ? 8.701   -11.420 8.802   1.00 42.97  ? 739 HOH A O   1 
HETATM 7674 O  O   . HOH L 6 .   ? -11.051 -25.795 19.661  1.00 39.36  ? 740 HOH A O   1 
HETATM 7675 O  O   . HOH L 6 .   ? -38.578 -16.550 21.831  1.00 45.27  ? 741 HOH A O   1 
HETATM 7676 O  O   . HOH L 6 .   ? -19.768 -14.682 -4.228  1.00 31.09  ? 742 HOH A O   1 
HETATM 7677 O  O   . HOH L 6 .   ? -4.031  12.260  19.554  1.00 39.31  ? 743 HOH A O   1 
HETATM 7678 O  O   . HOH L 6 .   ? 5.749   3.941   21.742  1.00 41.92  ? 744 HOH A O   1 
HETATM 7679 O  O   . HOH L 6 .   ? -0.090  -16.933 30.032  1.00 39.06  ? 745 HOH A O   1 
HETATM 7680 O  O   . HOH L 6 .   ? -16.434 -31.201 -11.882 1.00 52.68  ? 746 HOH A O   1 
HETATM 7681 O  O   . HOH L 6 .   ? -39.992 -14.129 16.300  1.00 49.08  ? 747 HOH A O   1 
HETATM 7682 O  O   . HOH L 6 .   ? -14.851 -28.931 -12.067 1.00 47.12  ? 748 HOH A O   1 
HETATM 7683 O  O   . HOH L 6 .   ? -12.981 -0.332  13.327  1.00 41.84  ? 749 HOH A O   1 
HETATM 7684 O  O   . HOH L 6 .   ? -16.515 -37.772 -4.657  1.00 50.44  ? 750 HOH A O   1 
HETATM 7685 O  O   . HOH L 6 .   ? -20.765 -9.231  -6.638  1.00 39.73  ? 751 HOH A O   1 
HETATM 7686 O  O   . HOH L 6 .   ? -13.909 7.711   23.341  1.00 46.70  ? 752 HOH A O   1 
HETATM 7687 O  O   . HOH L 6 .   ? -8.761  9.750   26.146  1.00 49.25  ? 753 HOH A O   1 
HETATM 7688 O  O   . HOH L 6 .   ? -9.498  -20.633 26.238  1.00 54.86  ? 754 HOH A O   1 
HETATM 7689 O  O   . HOH L 6 .   ? -0.190  -16.436 32.806  1.00 39.23  ? 755 HOH A O   1 
HETATM 7690 O  O   . HOH L 6 .   ? -35.793 -15.680 14.852  1.00 40.87  ? 756 HOH A O   1 
HETATM 7691 O  O   . HOH L 6 .   ? 2.537   -5.469  -2.784  1.00 41.98  ? 757 HOH A O   1 
HETATM 7692 O  O   . HOH L 6 .   ? -8.959  -5.218  -10.345 1.00 32.39  ? 758 HOH A O   1 
HETATM 7693 O  O   . HOH L 6 .   ? 7.743   -9.814  29.942  1.00 41.89  ? 759 HOH A O   1 
HETATM 7694 O  O   . HOH L 6 .   ? -25.555 -33.117 17.264  1.00 55.14  ? 760 HOH A O   1 
HETATM 7695 O  O   . HOH L 6 .   ? -35.379 -19.661 15.355  1.00 40.24  ? 761 HOH A O   1 
HETATM 7696 O  O   . HOH L 6 .   ? -15.553 -20.181 6.489   1.00 36.31  ? 762 HOH A O   1 
HETATM 7697 O  O   . HOH L 6 .   ? -22.212 -3.040  10.552  1.00 44.71  ? 763 HOH A O   1 
HETATM 7698 O  O   . HOH L 6 .   ? -8.086  -17.815 31.415  1.00 44.25  ? 764 HOH A O   1 
HETATM 7699 O  O   . HOH L 6 .   ? -18.049 -8.602  -3.503  1.00 44.80  ? 765 HOH A O   1 
HETATM 7700 O  O   . HOH L 6 .   ? -19.886 -18.210 -17.866 1.00 47.82  ? 766 HOH A O   1 
HETATM 7701 O  O   . HOH L 6 .   ? -28.107 -27.013 15.572  1.00 53.13  ? 767 HOH A O   1 
HETATM 7702 O  O   . HOH L 6 .   ? -16.517 -9.928  -9.781  1.00 47.46  ? 768 HOH A O   1 
HETATM 7703 O  O   . HOH L 6 .   ? -0.653  -34.871 -4.109  1.00 42.41  ? 769 HOH A O   1 
HETATM 7704 O  O   . HOH L 6 .   ? -19.465 -28.592 1.734   1.00 42.95  ? 770 HOH A O   1 
HETATM 7705 O  O   . HOH L 6 .   ? -20.509 -4.642  9.838   1.00 45.36  ? 771 HOH A O   1 
HETATM 7706 O  O   . HOH L 6 .   ? -3.826  -14.323 33.673  1.00 39.44  ? 772 HOH A O   1 
HETATM 7707 O  O   . HOH L 6 .   ? -5.965  -5.199  38.916  1.00 37.15  ? 773 HOH A O   1 
HETATM 7708 O  O   . HOH L 6 .   ? -2.290  -21.253 19.857  1.00 45.91  ? 774 HOH A O   1 
HETATM 7709 O  O   . HOH L 6 .   ? 10.608  -3.050  21.033  1.00 43.52  ? 775 HOH A O   1 
HETATM 7710 O  O   . HOH L 6 .   ? -35.655 -16.595 27.687  1.00 55.68  ? 776 HOH A O   1 
HETATM 7711 O  O   . HOH L 6 .   ? -3.317  -33.813 -11.352 1.00 44.02  ? 777 HOH A O   1 
HETATM 7712 O  O   . HOH L 6 .   ? -9.731  -7.126  -2.009  1.00 35.90  ? 778 HOH A O   1 
HETATM 7713 O  O   . HOH L 6 .   ? -27.387 -28.218 -16.671 1.00 60.55  ? 779 HOH A O   1 
HETATM 7714 O  O   . HOH L 6 .   ? -10.427 -23.355 19.911  1.00 46.61  ? 780 HOH A O   1 
HETATM 7715 O  O   . HOH L 6 .   ? 10.777  -21.525 18.786  1.00 43.66  ? 781 HOH A O   1 
HETATM 7716 O  O   . HOH L 6 .   ? -29.598 -12.257 -1.482  1.00 43.33  ? 782 HOH A O   1 
HETATM 7717 O  O   . HOH L 6 .   ? -0.585  -28.448 15.669  1.00 40.55  ? 783 HOH A O   1 
HETATM 7718 O  O   . HOH L 6 .   ? -8.176  -7.784  -11.540 1.00 35.59  ? 784 HOH A O   1 
HETATM 7719 O  O   . HOH L 6 .   ? -1.415  -17.578 -5.507  1.00 45.32  ? 785 HOH A O   1 
HETATM 7720 O  O   . HOH L 6 .   ? 13.474  -19.053 14.341  1.00 48.22  ? 786 HOH A O   1 
HETATM 7721 O  O   . HOH L 6 .   ? 5.229   -16.337 7.792   1.00 41.21  ? 787 HOH A O   1 
HETATM 7722 O  O   . HOH L 6 .   ? -21.565 3.926   11.229  1.00 45.27  ? 788 HOH A O   1 
HETATM 7723 O  O   . HOH L 6 .   ? -37.359 -19.599 20.441  1.00 43.56  ? 789 HOH A O   1 
HETATM 7724 O  O   . HOH L 6 .   ? -28.087 -27.421 6.309   1.00 44.98  ? 790 HOH A O   1 
HETATM 7725 O  O   . HOH L 6 .   ? -4.020  -11.518 -11.354 1.00 47.58  ? 791 HOH A O   1 
HETATM 7726 O  O   . HOH L 6 .   ? -1.014  -21.681 -5.901  1.00 49.53  ? 792 HOH A O   1 
HETATM 7727 O  O   . HOH L 6 .   ? -7.085  9.369   29.791  1.00 54.17  ? 793 HOH A O   1 
HETATM 7728 O  O   . HOH L 6 .   ? -27.549 -26.832 19.791  1.00 46.37  ? 794 HOH A O   1 
HETATM 7729 O  O   . HOH L 6 .   ? -5.910  13.452  21.108  1.00 43.75  ? 795 HOH A O   1 
HETATM 7730 O  O   . HOH L 6 .   ? 12.429  -16.969 12.732  1.00 50.64  ? 796 HOH A O   1 
HETATM 7731 O  O   . HOH L 6 .   ? 6.516   -16.618 32.518  1.00 46.63  ? 797 HOH A O   1 
HETATM 7732 O  O   . HOH L 6 .   ? -5.631  6.356   -6.251  1.00 41.35  ? 798 HOH A O   1 
HETATM 7733 O  O   . HOH L 6 .   ? -0.057  -4.354  -5.007  1.00 55.55  ? 799 HOH A O   1 
HETATM 7734 O  O   . HOH L 6 .   ? -38.887 -16.289 15.042  1.00 46.30  ? 800 HOH A O   1 
HETATM 7735 O  O   . HOH L 6 .   ? -8.695  -28.034 11.822  1.00 45.03  ? 801 HOH A O   1 
HETATM 7736 O  O   . HOH L 6 .   ? -7.124  -0.038  36.505  1.00 46.93  ? 802 HOH A O   1 
HETATM 7737 O  O   . HOH L 6 .   ? -9.906  -5.389  0.391   1.00 49.08  ? 803 HOH A O   1 
HETATM 7738 O  O   . HOH L 6 .   ? 2.337   -35.352 -2.130  1.00 45.37  ? 804 HOH A O   1 
HETATM 7739 O  O   . HOH L 6 .   ? -9.165  -44.427 -6.999  1.00 42.29  ? 805 HOH A O   1 
HETATM 7740 O  O   . HOH L 6 .   ? -31.839 -2.974  6.756   1.00 58.58  ? 806 HOH A O   1 
HETATM 7741 O  O   . HOH L 6 .   ? -19.052 -15.573 0.741   1.00 32.23  ? 807 HOH A O   1 
HETATM 7742 O  O   . HOH L 6 .   ? -4.973  -22.022 18.846  1.00 47.87  ? 808 HOH A O   1 
HETATM 7743 O  O   . HOH L 6 .   ? 3.915   -20.936 25.465  1.00 42.59  ? 809 HOH A O   1 
HETATM 7744 O  O   . HOH L 6 .   ? 4.248   7.791   24.675  1.00 47.93  ? 810 HOH A O   1 
HETATM 7745 O  O   . HOH L 6 .   ? -12.822 -13.782 39.422  1.00 47.09  ? 811 HOH A O   1 
HETATM 7746 O  O   . HOH L 6 .   ? 2.031   -31.478 -0.873  1.00 45.51  ? 812 HOH A O   1 
HETATM 7747 O  O   . HOH L 6 .   ? -3.340  -8.634  -11.735 1.00 46.81  ? 813 HOH A O   1 
HETATM 7748 O  O   . HOH L 6 .   ? -34.762 -13.935 3.887   1.00 42.21  ? 814 HOH A O   1 
HETATM 7749 O  O   . HOH L 6 .   ? 2.184   -15.025 33.756  1.00 46.10  ? 815 HOH A O   1 
HETATM 7750 O  O   . HOH L 6 .   ? -5.177  3.870   6.376   1.00 46.75  ? 816 HOH A O   1 
HETATM 7751 O  O   . HOH L 6 .   ? 0.371   -33.320 5.304   1.00 41.79  ? 817 HOH A O   1 
HETATM 7752 O  O   . HOH L 6 .   ? -5.243  11.488  17.352  1.00 43.61  ? 818 HOH A O   1 
HETATM 7753 O  O   . HOH L 6 .   ? -0.033  -34.077 -1.319  1.00 45.35  ? 819 HOH A O   1 
HETATM 7754 O  O   . HOH L 6 .   ? 1.806   -31.338 3.693   1.00 41.20  ? 820 HOH A O   1 
HETATM 7755 O  O   . HOH L 6 .   ? 18.106  -14.214 18.970  1.00 46.31  ? 821 HOH A O   1 
HETATM 7756 O  O   . HOH L 6 .   ? -37.407 -19.641 9.881   1.00 47.13  ? 822 HOH A O   1 
HETATM 7757 O  O   . HOH L 6 .   ? -5.714  -7.208  -12.507 1.00 45.08  ? 823 HOH A O   1 
HETATM 7758 O  O   . HOH L 6 .   ? -0.528  -33.611 1.290   1.00 40.31  ? 824 HOH A O   1 
HETATM 7759 O  O   . HOH M 6 .   ? -12.476 -32.435 63.783  1.00 47.38  ? 601 HOH B O   1 
HETATM 7760 O  O   . HOH M 6 .   ? -16.610 -21.727 46.523  1.00 46.90  ? 602 HOH B O   1 
HETATM 7761 O  O   . HOH M 6 .   ? 3.560   7.023   61.938  1.00 53.56  ? 603 HOH B O   1 
HETATM 7762 O  O   . HOH M 6 .   ? 15.115  -24.612 53.912  1.00 47.97  ? 604 HOH B O   1 
HETATM 7763 O  O   . HOH M 6 .   ? 22.081  -20.596 64.083  1.00 40.86  ? 605 HOH B O   1 
HETATM 7764 O  O   . HOH M 6 .   ? 17.742  -23.232 88.543  1.00 43.94  ? 606 HOH B O   1 
HETATM 7765 O  O   . HOH M 6 .   ? 10.033  -31.322 60.035  1.00 47.88  ? 607 HOH B O   1 
HETATM 7766 O  O   . HOH M 6 .   ? 0.367   -8.648  57.016  1.00 42.67  ? 608 HOH B O   1 
HETATM 7767 O  O   . HOH M 6 .   ? 0.254   2.104   45.292  1.00 45.70  ? 609 HOH B O   1 
HETATM 7768 O  O   . HOH M 6 .   ? 21.394  -18.690 50.192  1.00 49.93  ? 610 HOH B O   1 
HETATM 7769 O  O   . HOH M 6 .   ? 13.012  -29.551 83.396  1.00 39.38  ? 611 HOH B O   1 
HETATM 7770 O  O   . HOH M 6 .   ? 1.678   0.286   42.214  1.00 44.50  ? 612 HOH B O   1 
HETATM 7771 O  O   . HOH M 6 .   ? 7.285   -12.858 87.417  1.00 43.77  ? 613 HOH B O   1 
HETATM 7772 O  O   . HOH M 6 .   ? -8.780  -34.774 71.164  1.00 42.66  ? 614 HOH B O   1 
HETATM 7773 O  O   . HOH M 6 .   ? 0.608   -14.595 89.305  1.00 47.71  ? 615 HOH B O   1 
HETATM 7774 O  O   . HOH M 6 .   ? -21.284 -16.312 36.575  1.00 43.99  ? 616 HOH B O   1 
HETATM 7775 O  O   . HOH M 6 .   ? -14.318 0.640   42.460  1.00 44.49  ? 617 HOH B O   1 
HETATM 7776 O  O   . HOH M 6 .   ? 8.346   -29.362 89.552  1.00 45.17  ? 618 HOH B O   1 
HETATM 7777 O  O   . HOH M 6 .   ? -4.223  11.744  53.518  1.00 47.81  ? 619 HOH B O   1 
HETATM 7778 O  O   . HOH M 6 .   ? -4.786  -23.502 89.840  1.00 47.71  ? 620 HOH B O   1 
HETATM 7779 O  O   . HOH M 6 .   ? -13.939 -24.286 67.898  1.00 45.64  ? 621 HOH B O   1 
HETATM 7780 O  O   . HOH M 6 .   ? 12.331  -9.978  66.254  1.00 34.93  ? 622 HOH B O   1 
HETATM 7781 O  O   . HOH M 6 .   ? 5.070   -7.399  68.521  1.00 40.85  ? 623 HOH B O   1 
HETATM 7782 O  O   . HOH M 6 .   ? 16.477  -28.188 88.524  1.00 47.52  ? 624 HOH B O   1 
HETATM 7783 O  O   . HOH M 6 .   ? -14.856 -15.336 43.765  1.00 38.61  ? 625 HOH B O   1 
HETATM 7784 O  O   . HOH M 6 .   ? 5.250   -17.969 92.585  1.00 45.83  ? 626 HOH B O   1 
HETATM 7785 O  O   . HOH M 6 .   ? -15.325 -19.561 70.861  1.00 44.27  ? 627 HOH B O   1 
HETATM 7786 O  O   . HOH M 6 .   ? 11.064  -13.010 75.137  1.00 32.67  ? 628 HOH B O   1 
HETATM 7787 O  O   . HOH M 6 .   ? -7.792  -1.350  68.936  1.00 42.82  ? 629 HOH B O   1 
HETATM 7788 O  O   . HOH M 6 .   ? 22.566  -8.226  56.951  1.00 38.19  ? 630 HOH B O   1 
HETATM 7789 O  O   . HOH M 6 .   ? -8.914  -35.515 83.591  1.00 46.63  ? 631 HOH B O   1 
HETATM 7790 O  O   . HOH M 6 .   ? 23.943  -9.422  67.762  1.00 31.99  ? 632 HOH B O   1 
HETATM 7791 O  O   . HOH M 6 .   ? 8.742   -29.854 80.166  1.00 41.36  ? 633 HOH B O   1 
HETATM 7792 O  O   . HOH M 6 .   ? -4.999  -2.513  39.936  1.00 38.66  ? 634 HOH B O   1 
HETATM 7793 O  O   . HOH M 6 .   ? 3.704   -10.165 45.360  1.00 35.23  ? 635 HOH B O   1 
HETATM 7794 O  O   . HOH M 6 .   ? 1.832   -9.966  43.296  1.00 31.48  ? 636 HOH B O   1 
HETATM 7795 O  O   . HOH M 6 .   ? -16.974 0.265   45.151  1.00 35.22  ? 637 HOH B O   1 
HETATM 7796 O  O   . HOH M 6 .   ? -5.759  -12.360 86.437  1.00 42.09  ? 638 HOH B O   1 
HETATM 7797 O  O   . HOH M 6 .   ? -8.020  -28.544 60.596  1.00 36.59  ? 639 HOH B O   1 
HETATM 7798 O  O   . HOH M 6 .   ? 4.497   -27.917 88.818  1.00 41.66  ? 640 HOH B O   1 
HETATM 7799 O  O   . HOH M 6 .   ? -3.170  -2.016  42.065  1.00 35.56  ? 641 HOH B O   1 
HETATM 7800 O  O   . HOH M 6 .   ? -6.543  -14.891 85.663  1.00 37.40  ? 642 HOH B O   1 
HETATM 7801 O  O   . HOH M 6 .   ? -22.677 -17.855 43.900  1.00 48.65  ? 643 HOH B O   1 
HETATM 7802 O  O   . HOH M 6 .   ? -21.831 -1.905  54.845  1.00 45.53  ? 644 HOH B O   1 
HETATM 7803 O  O   . HOH M 6 .   ? 14.407  -14.024 78.500  1.00 38.83  ? 645 HOH B O   1 
HETATM 7804 O  O   . HOH M 6 .   ? -17.333 -16.536 70.247  1.00 46.12  ? 646 HOH B O   1 
HETATM 7805 O  O   . HOH M 6 .   ? -12.969 7.649   47.140  1.00 42.88  ? 647 HOH B O   1 
HETATM 7806 O  O   . HOH M 6 .   ? 6.107   -31.444 52.004  1.00 40.96  ? 648 HOH B O   1 
HETATM 7807 O  O   . HOH M 6 .   ? -8.847  7.297   51.037  1.00 33.99  ? 649 HOH B O   1 
HETATM 7808 O  O   . HOH M 6 .   ? -22.287 -17.109 53.571  1.00 33.10  ? 650 HOH B O   1 
HETATM 7809 O  O   . HOH M 6 .   ? 4.546   4.334   50.510  1.00 39.70  ? 651 HOH B O   1 
HETATM 7810 O  O   . HOH M 6 .   ? -12.897 -22.282 74.920  1.00 38.03  ? 652 HOH B O   1 
HETATM 7811 O  O   . HOH M 6 .   ? -14.449 -18.057 79.414  1.00 45.74  ? 653 HOH B O   1 
HETATM 7812 O  O   . HOH M 6 .   ? -23.960 -1.758  47.959  1.00 49.98  ? 654 HOH B O   1 
HETATM 7813 O  O   . HOH M 6 .   ? 6.177   -28.706 73.367  1.00 43.95  ? 655 HOH B O   1 
HETATM 7814 O  O   . HOH M 6 .   ? 4.084   -13.530 37.481  1.00 47.71  ? 656 HOH B O   1 
HETATM 7815 O  O   . HOH M 6 .   ? -5.121  -0.318  63.019  1.00 33.51  ? 657 HOH B O   1 
HETATM 7816 O  O   . HOH M 6 .   ? -7.469  -7.264  40.254  1.00 31.96  ? 658 HOH B O   1 
HETATM 7817 O  O   . HOH M 6 .   ? -2.011  -15.115 67.476  1.00 32.24  ? 659 HOH B O   1 
HETATM 7818 O  O   . HOH M 6 .   ? -18.513 3.830   51.209  1.00 38.78  ? 660 HOH B O   1 
HETATM 7819 O  O   . HOH M 6 .   ? -15.916 -14.329 37.606  1.00 41.04  ? 661 HOH B O   1 
HETATM 7820 O  O   . HOH M 6 .   ? 0.708   -2.480  39.664  1.00 35.64  ? 662 HOH B O   1 
HETATM 7821 O  O   . HOH M 6 .   ? -19.335 -22.857 52.728  1.00 44.53  ? 663 HOH B O   1 
HETATM 7822 O  O   . HOH M 6 .   ? -11.990 -27.399 58.860  1.00 40.02  ? 664 HOH B O   1 
HETATM 7823 O  O   . HOH M 6 .   ? -4.220  -44.870 80.764  1.00 35.03  ? 665 HOH B O   1 
HETATM 7824 O  O   . HOH M 6 .   ? 5.293   -22.477 69.584  1.00 29.95  ? 666 HOH B O   1 
HETATM 7825 O  O   . HOH M 6 .   ? -6.192  -26.022 86.306  1.00 34.94  ? 667 HOH B O   1 
HETATM 7826 O  O   . HOH M 6 .   ? -20.973 -19.741 62.899  1.00 36.63  ? 668 HOH B O   1 
HETATM 7827 O  O   . HOH M 6 .   ? 5.880   -38.514 72.106  1.00 44.86  ? 669 HOH B O   1 
HETATM 7828 O  O   . HOH M 6 .   ? -11.835 -22.624 52.584  1.00 37.86  ? 670 HOH B O   1 
HETATM 7829 O  O   . HOH M 6 .   ? -18.877 -3.797  40.654  1.00 45.98  ? 671 HOH B O   1 
HETATM 7830 O  O   . HOH M 6 .   ? -19.505 -2.131  54.092  1.00 36.03  ? 672 HOH B O   1 
HETATM 7831 O  O   . HOH M 6 .   ? 22.719  -23.298 66.631  1.00 38.86  ? 673 HOH B O   1 
HETATM 7832 O  O   . HOH M 6 .   ? -18.148 4.615   62.978  1.00 31.21  ? 674 HOH B O   1 
HETATM 7833 O  O   . HOH M 6 .   ? -24.662 -3.734  58.925  1.00 36.73  ? 675 HOH B O   1 
HETATM 7834 O  O   . HOH M 6 .   ? -5.751  -35.954 61.993  1.00 52.32  ? 676 HOH B O   1 
HETATM 7835 O  O   . HOH M 6 .   ? -11.827 -9.762  88.047  1.00 45.00  ? 677 HOH B O   1 
HETATM 7836 O  O   . HOH M 6 .   ? 15.414  -19.505 73.201  1.00 35.12  ? 678 HOH B O   1 
HETATM 7837 O  O   . HOH M 6 .   ? 5.568   0.871   48.920  1.00 34.85  ? 679 HOH B O   1 
HETATM 7838 O  O   . HOH M 6 .   ? 1.378   -9.835  54.239  1.00 37.95  ? 680 HOH B O   1 
HETATM 7839 O  O   . HOH M 6 .   ? 12.011  -18.714 61.308  1.00 31.24  ? 681 HOH B O   1 
HETATM 7840 O  O   . HOH M 6 .   ? -21.013 9.408   58.251  1.00 45.66  ? 682 HOH B O   1 
HETATM 7841 O  O   . HOH M 6 .   ? -5.132  -8.333  39.651  1.00 32.46  ? 683 HOH B O   1 
HETATM 7842 O  O   . HOH M 6 .   ? 9.056   -15.536 68.292  1.00 31.97  ? 684 HOH B O   1 
HETATM 7843 O  O   . HOH M 6 .   ? -1.999  -5.059  50.873  1.00 39.04  ? 685 HOH B O   1 
HETATM 7844 O  O   . HOH M 6 .   ? 3.859   -16.093 92.029  1.00 44.15  ? 686 HOH B O   1 
HETATM 7845 O  O   . HOH M 6 .   ? -18.724 -8.707  44.023  1.00 41.64  ? 687 HOH B O   1 
HETATM 7846 O  O   . HOH M 6 .   ? -6.049  -28.983 58.325  1.00 53.22  ? 688 HOH B O   1 
HETATM 7847 O  O   . HOH M 6 .   ? 9.690   0.888   54.600  1.00 45.23  ? 689 HOH B O   1 
HETATM 7848 O  O   . HOH M 6 .   ? 0.660   -27.270 48.318  1.00 45.46  ? 690 HOH B O   1 
HETATM 7849 O  O   . HOH M 6 .   ? -9.720  -28.891 87.354  1.00 45.42  ? 691 HOH B O   1 
HETATM 7850 O  O   . HOH M 6 .   ? 10.640  -9.451  68.357  1.00 36.54  ? 692 HOH B O   1 
HETATM 7851 O  O   . HOH M 6 .   ? 5.991   -4.753  61.981  1.00 34.29  ? 693 HOH B O   1 
HETATM 7852 O  O   . HOH M 6 .   ? 0.897   -8.131  41.201  1.00 34.74  ? 694 HOH B O   1 
HETATM 7853 O  O   . HOH M 6 .   ? -8.436  -13.554 64.000  1.00 33.78  ? 695 HOH B O   1 
HETATM 7854 O  O   . HOH M 6 .   ? 28.172  -1.006  68.217  1.00 42.64  ? 696 HOH B O   1 
HETATM 7855 O  O   . HOH M 6 .   ? -11.272 -0.292  76.420  1.00 43.54  ? 697 HOH B O   1 
HETATM 7856 O  O   . HOH M 6 .   ? -5.157  -24.527 80.689  1.00 32.94  ? 698 HOH B O   1 
HETATM 7857 O  O   . HOH M 6 .   ? -7.398  3.520   43.934  1.00 48.43  ? 699 HOH B O   1 
HETATM 7858 O  O   . HOH M 6 .   ? 6.237   -27.096 75.618  1.00 36.80  ? 700 HOH B O   1 
HETATM 7859 O  O   . HOH M 6 .   ? 17.332  -15.235 62.952  1.00 29.86  ? 701 HOH B O   1 
HETATM 7860 O  O   . HOH M 6 .   ? 5.532   -17.670 37.454  1.00 58.71  ? 702 HOH B O   1 
HETATM 7861 O  O   . HOH M 6 .   ? 5.672   -10.561 84.158  1.00 49.81  ? 703 HOH B O   1 
HETATM 7862 O  O   . HOH M 6 .   ? -13.048 7.226   63.799  1.00 43.44  ? 704 HOH B O   1 
HETATM 7863 O  O   . HOH M 6 .   ? -7.806  0.872   67.029  1.00 37.49  ? 705 HOH B O   1 
HETATM 7864 O  O   . HOH M 6 .   ? 21.115  -14.177 70.032  1.00 36.22  ? 706 HOH B O   1 
HETATM 7865 O  O   . HOH M 6 .   ? -3.526  9.954   60.827  1.00 36.13  ? 707 HOH B O   1 
HETATM 7866 O  O   . HOH M 6 .   ? -17.712 3.047   69.964  1.00 47.89  ? 708 HOH B O   1 
HETATM 7867 O  O   . HOH M 6 .   ? 6.683   -14.604 71.696  1.00 29.48  ? 709 HOH B O   1 
HETATM 7868 O  O   . HOH M 6 .   ? -14.170 -6.975  78.039  1.00 35.13  ? 710 HOH B O   1 
HETATM 7869 O  O   . HOH M 6 .   ? -5.988  -38.532 83.315  1.00 44.21  ? 711 HOH B O   1 
HETATM 7870 O  O   . HOH M 6 .   ? -11.415 -17.710 45.059  1.00 39.70  ? 712 HOH B O   1 
HETATM 7871 O  O   . HOH M 6 .   ? -21.438 -10.992 69.188  1.00 34.59  ? 713 HOH B O   1 
HETATM 7872 O  O   . HOH M 6 .   ? -19.255 -24.467 57.372  1.00 38.91  ? 714 HOH B O   1 
HETATM 7873 O  O   . HOH M 6 .   ? 4.957   -14.785 39.668  1.00 44.64  ? 715 HOH B O   1 
HETATM 7874 O  O   . HOH M 6 .   ? 12.963  -19.261 86.119  1.00 38.49  ? 716 HOH B O   1 
HETATM 7875 O  O   . HOH M 6 .   ? -6.791  -12.167 79.343  1.00 34.83  ? 717 HOH B O   1 
HETATM 7876 O  O   . HOH M 6 .   ? 24.486  -12.285 67.946  1.00 36.31  ? 718 HOH B O   1 
HETATM 7877 O  O   . HOH M 6 .   ? 9.195   -31.626 83.129  1.00 46.20  ? 719 HOH B O   1 
HETATM 7878 O  O   . HOH M 6 .   ? -10.332 -33.127 80.575  1.00 46.42  ? 720 HOH B O   1 
HETATM 7879 O  O   . HOH M 6 .   ? -10.511 3.502   47.890  1.00 37.61  ? 721 HOH B O   1 
HETATM 7880 O  O   . HOH M 6 .   ? 7.162   -20.806 70.935  1.00 29.97  ? 722 HOH B O   1 
HETATM 7881 O  O   . HOH M 6 .   ? -12.750 -25.527 71.118  1.00 43.98  ? 723 HOH B O   1 
HETATM 7882 O  O   . HOH M 6 .   ? 8.993   -14.955 78.951  1.00 32.25  ? 724 HOH B O   1 
HETATM 7883 O  O   . HOH M 6 .   ? -14.054 -20.206 51.285  1.00 31.78  ? 725 HOH B O   1 
HETATM 7884 O  O   . HOH M 6 .   ? -9.767  11.439  56.158  1.00 45.76  ? 726 HOH B O   1 
HETATM 7885 O  O   . HOH M 6 .   ? -11.531 -16.769 42.326  1.00 41.81  ? 727 HOH B O   1 
HETATM 7886 O  O   . HOH M 6 .   ? -24.938 -9.744  57.648  1.00 46.25  ? 728 HOH B O   1 
HETATM 7887 O  O   . HOH M 6 .   ? -14.188 -25.565 64.043  1.00 32.96  ? 729 HOH B O   1 
HETATM 7888 O  O   . HOH M 6 .   ? 17.028  -13.671 84.590  1.00 48.95  ? 730 HOH B O   1 
HETATM 7889 O  O   . HOH M 6 .   ? -13.006 -10.986 39.167  1.00 33.36  ? 731 HOH B O   1 
HETATM 7890 O  O   . HOH M 6 .   ? -25.663 -9.559  48.205  1.00 49.01  ? 732 HOH B O   1 
HETATM 7891 O  O   . HOH M 6 .   ? -19.050 -23.305 64.692  1.00 53.41  ? 733 HOH B O   1 
HETATM 7892 O  O   . HOH M 6 .   ? 26.364  -19.962 56.466  1.00 61.53  ? 734 HOH B O   1 
HETATM 7893 O  O   . HOH M 6 .   ? -6.606  -5.212  36.366  1.00 36.65  ? 735 HOH B O   1 
HETATM 7894 O  O   . HOH M 6 .   ? 6.888   -4.992  40.024  1.00 48.41  ? 736 HOH B O   1 
HETATM 7895 O  O   . HOH M 6 .   ? -0.384  -6.998  72.163  1.00 52.32  ? 737 HOH B O   1 
HETATM 7896 O  O   . HOH M 6 .   ? 7.711   -18.112 72.842  1.00 31.24  ? 738 HOH B O   1 
HETATM 7897 O  O   . HOH M 6 .   ? 13.180  -27.562 77.596  1.00 45.80  ? 739 HOH B O   1 
HETATM 7898 O  O   . HOH M 6 .   ? -15.250 7.294   51.092  1.00 38.52  ? 740 HOH B O   1 
HETATM 7899 O  O   . HOH M 6 .   ? 1.160   -9.943  71.821  1.00 31.12  ? 741 HOH B O   1 
HETATM 7900 O  O   . HOH M 6 .   ? 18.669  -18.996 80.609  1.00 52.67  ? 742 HOH B O   1 
HETATM 7901 O  O   . HOH M 6 .   ? -21.485 -22.153 53.839  1.00 36.74  ? 743 HOH B O   1 
HETATM 7902 O  O   . HOH M 6 .   ? -15.679 12.489  55.159  1.00 47.08  ? 744 HOH B O   1 
HETATM 7903 O  O   . HOH M 6 .   ? -8.175  -14.612 41.320  1.00 39.71  ? 745 HOH B O   1 
HETATM 7904 O  O   . HOH M 6 .   ? -11.118 -31.739 73.858  1.00 35.80  ? 746 HOH B O   1 
HETATM 7905 O  O   . HOH M 6 .   ? -1.350  -3.838  83.659  1.00 49.55  ? 747 HOH B O   1 
HETATM 7906 O  O   . HOH M 6 .   ? -2.804  -5.306  68.694  1.00 42.50  ? 748 HOH B O   1 
HETATM 7907 O  O   . HOH M 6 .   ? -18.818 2.144   53.778  1.00 37.67  ? 749 HOH B O   1 
HETATM 7908 O  O   . HOH M 6 .   ? -1.912  -10.595 41.920  1.00 32.78  ? 750 HOH B O   1 
HETATM 7909 O  O   . HOH M 6 .   ? -22.872 -4.913  54.372  1.00 46.57  ? 751 HOH B O   1 
HETATM 7910 O  O   . HOH M 6 .   ? -17.609 -7.566  79.924  1.00 45.62  ? 752 HOH B O   1 
HETATM 7911 O  O   . HOH M 6 .   ? 18.754  -10.445 74.063  1.00 46.30  ? 753 HOH B O   1 
HETATM 7912 O  O   B HOH M 6 .   ? 3.976   -14.776 62.734  0.58 32.49  ? 754 HOH B O   1 
HETATM 7913 O  O   . HOH M 6 .   ? -16.690 -25.110 56.162  1.00 46.73  ? 755 HOH B O   1 
HETATM 7914 O  O   . HOH M 6 .   ? -3.068  -26.304 65.159  1.00 40.90  ? 756 HOH B O   1 
HETATM 7915 O  O   . HOH M 6 .   ? -11.098 -30.722 68.137  1.00 43.48  ? 757 HOH B O   1 
HETATM 7916 O  O   . HOH M 6 .   ? -0.357  -48.990 76.603  1.00 44.31  ? 758 HOH B O   1 
HETATM 7917 O  O   . HOH M 6 .   ? 14.754  -32.505 56.856  1.00 49.24  ? 759 HOH B O   1 
HETATM 7918 O  O   . HOH M 6 .   ? 0.481   -0.666  62.229  1.00 38.42  ? 760 HOH B O   1 
HETATM 7919 O  O   . HOH M 6 .   ? -19.683 -11.085 45.401  1.00 38.89  ? 761 HOH B O   1 
HETATM 7920 O  O   . HOH M 6 .   ? -24.072 -2.833  43.111  1.00 53.01  ? 762 HOH B O   1 
HETATM 7921 O  O   . HOH M 6 .   ? -19.059 -6.892  37.530  1.00 41.70  ? 763 HOH B O   1 
HETATM 7922 O  O   . HOH M 6 .   ? -20.556 -13.319 66.582  1.00 35.94  ? 764 HOH B O   1 
HETATM 7923 O  O   . HOH M 6 .   ? -12.676 -17.564 82.653  1.00 36.93  ? 765 HOH B O   1 
HETATM 7924 O  O   . HOH M 6 .   ? 24.011  -18.814 58.727  1.00 48.39  ? 766 HOH B O   1 
HETATM 7925 O  O   . HOH M 6 .   ? -9.085  -18.322 80.752  1.00 38.92  ? 767 HOH B O   1 
HETATM 7926 O  O   . HOH M 6 .   ? 0.613   7.754   52.213  1.00 43.51  ? 768 HOH B O   1 
HETATM 7927 O  O   . HOH M 6 .   ? -19.725 -15.168 76.588  1.00 43.54  ? 769 HOH B O   1 
HETATM 7928 O  O   . HOH M 6 .   ? 13.412  -13.957 75.921  1.00 34.80  ? 770 HOH B O   1 
HETATM 7929 O  O   . HOH M 6 .   ? 16.446  -29.071 85.849  1.00 44.67  ? 771 HOH B O   1 
HETATM 7930 O  O   . HOH M 6 .   ? 9.622   -9.491  81.211  1.00 42.62  ? 772 HOH B O   1 
HETATM 7931 O  O   . HOH M 6 .   ? -13.045 -15.632 45.637  1.00 33.51  ? 773 HOH B O   1 
HETATM 7932 O  O   . HOH M 6 .   ? -22.521 -5.273  42.900  1.00 53.41  ? 774 HOH B O   1 
HETATM 7933 O  O   . HOH M 6 .   ? 4.697   -29.449 86.798  1.00 43.02  ? 775 HOH B O   1 
HETATM 7934 O  O   . HOH M 6 .   ? -5.364  -18.680 48.215  1.00 41.44  ? 776 HOH B O   1 
HETATM 7935 O  O   . HOH M 6 .   ? 4.457   -20.180 68.292  1.00 34.04  ? 777 HOH B O   1 
HETATM 7936 O  O   . HOH M 6 .   ? 22.424  -6.704  70.788  1.00 46.88  ? 778 HOH B O   1 
HETATM 7937 O  O   . HOH M 6 .   ? -10.395 -17.385 84.724  1.00 54.19  ? 779 HOH B O   1 
HETATM 7938 O  O   . HOH M 6 .   ? 23.560  -18.594 65.040  1.00 35.46  ? 780 HOH B O   1 
HETATM 7939 O  O   . HOH M 6 .   ? -24.861 -6.785  65.381  1.00 40.94  ? 781 HOH B O   1 
HETATM 7940 O  O   . HOH M 6 .   ? -25.530 -13.574 59.217  1.00 53.37  ? 782 HOH B O   1 
HETATM 7941 O  O   . HOH M 6 .   ? -19.840 7.624   56.956  1.00 43.45  ? 783 HOH B O   1 
HETATM 7942 O  O   . HOH M 6 .   ? 8.855   -14.323 76.226  1.00 31.55  ? 784 HOH B O   1 
HETATM 7943 O  O   . HOH M 6 .   ? -12.889 2.624   39.344  1.00 52.52  ? 785 HOH B O   1 
HETATM 7944 O  O   . HOH M 6 .   ? -13.466 -22.532 43.502  1.00 58.77  ? 786 HOH B O   1 
HETATM 7945 O  O   . HOH M 6 .   ? -21.684 -23.397 56.561  1.00 40.74  ? 787 HOH B O   1 
HETATM 7946 O  O   . HOH M 6 .   ? -12.121 -35.896 73.566  1.00 49.84  ? 788 HOH B O   1 
HETATM 7947 O  O   . HOH M 6 .   ? 7.186   -9.000  78.256  1.00 48.76  ? 789 HOH B O   1 
HETATM 7948 O  O   . HOH M 6 .   ? 17.327  -26.755 67.769  1.00 44.79  ? 790 HOH B O   1 
HETATM 7949 O  O   . HOH M 6 .   ? -6.536  -34.849 86.498  1.00 45.48  ? 791 HOH B O   1 
HETATM 7950 O  O   . HOH M 6 .   ? 9.999   -2.541  64.742  1.00 40.41  ? 792 HOH B O   1 
HETATM 7951 O  O   . HOH M 6 .   ? -10.955 8.688   63.440  1.00 45.74  ? 793 HOH B O   1 
HETATM 7952 O  O   . HOH M 6 .   ? -24.812 -21.054 60.774  1.00 48.61  ? 794 HOH B O   1 
HETATM 7953 O  O   . HOH M 6 .   ? 1.213   -6.923  77.517  1.00 47.32  ? 795 HOH B O   1 
HETATM 7954 O  O   . HOH M 6 .   ? -18.884 -17.586 66.346  1.00 53.23  ? 796 HOH B O   1 
HETATM 7955 O  O   . HOH M 6 .   ? -21.294 -8.510  34.900  1.00 54.43  ? 797 HOH B O   1 
HETATM 7956 O  O   . HOH M 6 .   ? -3.716  -17.920 43.458  1.00 45.67  ? 798 HOH B O   1 
HETATM 7957 O  O   . HOH M 6 .   ? -13.441 12.025  60.238  1.00 42.06  ? 799 HOH B O   1 
HETATM 7958 O  O   . HOH M 6 .   ? 10.790  -25.120 91.808  1.00 45.75  ? 800 HOH B O   1 
HETATM 7959 O  O   . HOH M 6 .   ? -5.503  -23.021 58.661  1.00 37.97  ? 801 HOH B O   1 
HETATM 7960 O  O   . HOH M 6 .   ? -22.401 -20.029 47.575  1.00 47.99  ? 802 HOH B O   1 
HETATM 7961 O  O   . HOH M 6 .   ? -8.457  -22.926 87.181  1.00 39.29  ? 803 HOH B O   1 
HETATM 7962 O  O   . HOH M 6 .   ? -1.136  -15.466 91.726  1.00 48.21  ? 804 HOH B O   1 
HETATM 7963 O  O   . HOH M 6 .   ? 5.966   -38.389 79.771  1.00 49.77  ? 805 HOH B O   1 
HETATM 7964 O  O   . HOH M 6 .   ? -8.119  12.534  54.698  1.00 46.90  ? 806 HOH B O   1 
HETATM 7965 O  O   . HOH M 6 .   ? 6.739   -8.621  82.132  1.00 53.46  ? 807 HOH B O   1 
HETATM 7966 O  O   . HOH M 6 .   ? 8.357   -4.603  65.237  1.00 37.23  ? 808 HOH B O   1 
HETATM 7967 O  O   . HOH M 6 .   ? -25.771 -11.073 55.828  1.00 44.72  ? 809 HOH B O   1 
HETATM 7968 O  O   . HOH M 6 .   ? 18.242  -12.483 76.063  1.00 54.56  ? 810 HOH B O   1 
HETATM 7969 O  O   . HOH M 6 .   ? -24.434 0.161   65.049  1.00 42.56  ? 811 HOH B O   1 
HETATM 7970 O  O   . HOH M 6 .   ? 24.420  -14.712 59.508  1.00 41.09  ? 812 HOH B O   1 
HETATM 7971 O  O   . HOH M 6 .   ? -9.883  -35.396 79.215  1.00 38.50  ? 813 HOH B O   1 
HETATM 7972 O  O   . HOH M 6 .   ? 27.102  -14.890 52.520  1.00 46.93  ? 814 HOH B O   1 
HETATM 7973 O  O   . HOH M 6 .   ? 17.257  -26.435 59.115  1.00 48.23  ? 815 HOH B O   1 
HETATM 7974 O  O   . HOH M 6 .   ? -0.058  9.867   54.438  1.00 35.85  ? 816 HOH B O   1 
HETATM 7975 O  O   . HOH M 6 .   ? -0.763  -42.833 81.081  1.00 45.84  ? 817 HOH B O   1 
HETATM 7976 O  O   . HOH M 6 .   ? 25.696  -18.477 53.943  1.00 52.69  ? 818 HOH B O   1 
HETATM 7977 O  O   . HOH M 6 .   ? 16.745  -15.591 78.141  1.00 43.05  ? 819 HOH B O   1 
HETATM 7978 O  O   . HOH M 6 .   ? -16.438 -17.740 67.676  1.00 37.88  ? 820 HOH B O   1 
HETATM 7979 O  O   . HOH M 6 .   ? 3.250   6.867   52.980  1.00 42.83  ? 821 HOH B O   1 
HETATM 7980 O  O   . HOH M 6 .   ? 7.405   0.886   66.034  1.00 47.56  ? 822 HOH B O   1 
HETATM 7981 O  O   . HOH M 6 .   ? -10.374 -29.187 59.736  1.00 42.14  ? 823 HOH B O   1 
HETATM 7982 O  O   . HOH M 6 .   ? 9.740   -30.854 71.522  1.00 54.37  ? 824 HOH B O   1 
HETATM 7983 O  O   . HOH M 6 .   ? -20.343 -3.366  72.937  1.00 40.62  ? 825 HOH B O   1 
HETATM 7984 O  O   . HOH M 6 .   ? 9.701   -18.559 92.527  1.00 48.38  ? 826 HOH B O   1 
HETATM 7985 O  O   . HOH M 6 .   ? -6.118  1.683   63.541  1.00 47.38  ? 827 HOH B O   1 
HETATM 7986 O  O   . HOH M 6 .   ? -13.127 -35.734 76.995  1.00 46.57  ? 828 HOH B O   1 
HETATM 7987 O  O   . HOH M 6 .   ? 6.261   -30.904 74.878  1.00 46.12  ? 829 HOH B O   1 
HETATM 7988 O  O   . HOH M 6 .   ? -1.931  -7.103  77.158  1.00 38.34  ? 830 HOH B O   1 
HETATM 7989 O  O   . HOH M 6 .   ? 9.163   -28.739 72.619  1.00 46.07  ? 831 HOH B O   1 
HETATM 7990 O  O   . HOH M 6 .   ? -24.337 -18.602 62.650  1.00 60.89  ? 832 HOH B O   1 
HETATM 7991 O  O   . HOH M 6 .   ? -5.999  -10.294 37.576  1.00 33.39  ? 833 HOH B O   1 
HETATM 7992 O  O   . HOH M 6 .   ? -12.057 -26.447 86.365  1.00 55.72  ? 834 HOH B O   1 
HETATM 7993 O  O   . HOH M 6 .   ? -1.717  -20.802 48.921  1.00 49.70  ? 835 HOH B O   1 
HETATM 7994 O  O   . HOH M 6 .   ? 8.448   3.857   64.686  1.00 45.14  ? 836 HOH B O   1 
HETATM 7995 O  O   . HOH M 6 .   ? 30.994  -6.652  58.207  1.00 41.78  ? 837 HOH B O   1 
HETATM 7996 O  O   . HOH M 6 .   ? -6.400  9.388   45.487  1.00 39.60  ? 838 HOH B O   1 
HETATM 7997 O  O   . HOH M 6 .   ? -9.439  -22.227 81.113  1.00 43.23  ? 839 HOH B O   1 
HETATM 7998 O  O   . HOH M 6 .   ? -8.783  -25.573 53.363  1.00 59.75  ? 840 HOH B O   1 
HETATM 7999 O  O   . HOH M 6 .   ? -12.234 -4.264  78.082  1.00 52.18  ? 841 HOH B O   1 
HETATM 8000 O  O   . HOH M 6 .   ? -24.319 -7.980  49.671  1.00 44.71  ? 842 HOH B O   1 
HETATM 8001 O  O   . HOH M 6 .   ? -18.047 -17.784 42.319  1.00 47.92  ? 843 HOH B O   1 
HETATM 8002 O  O   . HOH M 6 .   ? -12.976 -39.441 72.465  1.00 46.86  ? 844 HOH B O   1 
HETATM 8003 O  O   . HOH M 6 .   ? -1.854  -28.690 63.023  1.00 43.78  ? 845 HOH B O   1 
HETATM 8004 O  O   . HOH M 6 .   ? -7.041  -20.261 52.190  1.00 49.24  ? 846 HOH B O   1 
HETATM 8005 O  O   . HOH M 6 .   ? -1.127  -7.135  69.508  1.00 42.95  ? 847 HOH B O   1 
HETATM 8006 O  O   . HOH M 6 .   ? -22.432 -9.110  70.741  1.00 45.26  ? 848 HOH B O   1 
HETATM 8007 O  O   . HOH M 6 .   ? 12.296  -22.667 93.108  1.00 52.23  ? 849 HOH B O   1 
HETATM 8008 O  O   . HOH M 6 .   ? -20.587 -7.442  42.171  1.00 57.30  ? 850 HOH B O   1 
HETATM 8009 O  O   . HOH M 6 .   ? 7.881   -15.577 74.128  1.00 32.92  ? 851 HOH B O   1 
HETATM 8010 O  O   . HOH M 6 .   ? 0.924   -13.084 35.849  1.00 47.07  ? 852 HOH B O   1 
HETATM 8011 O  O   . HOH M 6 .   ? 5.110   -11.482 86.935  1.00 51.97  ? 853 HOH B O   1 
HETATM 8012 O  O   . HOH M 6 .   ? -24.136 4.861   61.266  1.00 42.73  ? 854 HOH B O   1 
HETATM 8013 O  O   . HOH M 6 .   ? -0.058  5.721   48.814  1.00 54.06  ? 855 HOH B O   1 
HETATM 8014 O  O   . HOH M 6 .   ? -1.845  -45.349 82.050  1.00 42.69  ? 856 HOH B O   1 
HETATM 8015 O  O   . HOH M 6 .   ? -23.608 -1.484  57.084  1.00 46.36  ? 857 HOH B O   1 
HETATM 8016 O  O   . HOH M 6 .   ? -5.597  -20.463 50.412  1.00 47.65  ? 858 HOH B O   1 
HETATM 8017 O  O   . HOH M 6 .   ? -22.382 3.790   63.461  1.00 38.48  ? 859 HOH B O   1 
HETATM 8018 O  O   . HOH M 6 .   ? -15.108 -22.022 49.821  1.00 40.04  ? 860 HOH B O   1 
HETATM 8019 O  O   . HOH M 6 .   ? -11.064 -33.635 69.474  1.00 49.30  ? 861 HOH B O   1 
HETATM 8020 O  O   . HOH M 6 .   ? -7.748  -16.158 87.661  1.00 43.65  ? 862 HOH B O   1 
HETATM 8021 O  O   . HOH M 6 .   ? -17.524 6.414   50.383  1.00 47.99  ? 863 HOH B O   1 
HETATM 8022 O  O   . HOH M 6 .   ? 13.857  -17.424 88.024  1.00 50.12  ? 864 HOH B O   1 
HETATM 8023 O  O   . HOH M 6 .   ? 24.317  -21.905 63.645  1.00 52.39  ? 865 HOH B O   1 
HETATM 8024 O  O   . HOH M 6 .   ? 23.475  -12.963 70.483  1.00 43.51  ? 866 HOH B O   1 
HETATM 8025 O  O   . HOH M 6 .   ? -25.914 -6.601  50.619  1.00 46.51  ? 867 HOH B O   1 
HETATM 8026 O  O   . HOH M 6 .   ? -13.873 -15.573 41.169  1.00 49.76  ? 868 HOH B O   1 
HETATM 8027 O  O   . HOH M 6 .   ? 5.472   -40.844 70.598  1.00 51.23  ? 869 HOH B O   1 
HETATM 8028 O  O   . HOH M 6 .   ? -21.435 6.096   55.521  1.00 48.65  ? 870 HOH B O   1 
HETATM 8029 O  O   . HOH M 6 .   ? 26.054  -18.945 64.371  1.00 49.44  ? 871 HOH B O   1 
HETATM 8030 O  O   . HOH M 6 .   ? -10.060 -34.241 73.599  1.00 43.97  ? 872 HOH B O   1 
HETATM 8031 O  O   . HOH M 6 .   ? -12.651 -31.988 71.512  1.00 42.24  ? 873 HOH B O   1 
HETATM 8032 O  O   . HOH M 6 .   ? 26.971  -12.404 69.059  1.00 47.10  ? 874 HOH B O   1 
HETATM 8033 O  O   . HOH M 6 .   ? -11.706 11.396  43.646  1.00 60.98  ? 875 HOH B O   1 
HETATM 8034 O  O   . HOH M 6 .   ? 10.262  -13.727 47.141  1.00 45.48  ? 876 HOH B O   1 
# 
