data_9EVJ
# 
_entry.id   9EVJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EVJ         pdb_00009evj 10.2210/pdb9evj/pdb 
WWPDB D_1292135910 ?            ?                   
# 
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 2025-04-09 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.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.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EVJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        SASBDB 
_pdbx_database_related.details        '(draft ID 5562)' 
_pdbx_database_related.db_id          SAS5562 
_pdbx_database_related.content_type   'associated SAS data' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              federico.forneris@unipv.it 
_pdbx_contact_author.name_first         Federico 
_pdbx_contact_author.name_last          Forneris 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7818-1804 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'De Marco, M.'  1 0000-0002-6637-0683 
'Scietti, L.'   2 0000-0001-8691-9429 
'Rai, S.R.'     3 ?                   
'Mattoteia, D.' 4 0000-0003-1089-0126 
'Pinnola, A.'   5 0000-0001-8373-7638 
'Forneris, F.'  6 0000-0002-7818-1804 
# 
_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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3624 
_citation.page_last                 3624 
_citation.title                     
'Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59017-5 
_citation.pdbx_database_id_PubMed   40240392 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'De Marco, M.'     1  0000-0002-6637-0683 
primary 'Rai, S.R.'        2  ?                   
primary 'Scietti, L.'      3  ?                   
primary 'Mattoteia, D.'    4  0000-0003-1089-0126 
primary 'Liberi, S.'       5  ?                   
primary 'Moroni, E.'       6  0000-0002-7705-7457 
primary 'Pinnola, A.'      7  0000-0001-8373-7638 
primary 'Vetrano, A.'      8  0000-0002-9844-5942 
primary 'Iacobucci, C.'    9  ?                   
primary 'Santambrogio, C.' 10 0000-0003-3986-6971 
primary 'Colombo, G.'      11 0000-0002-1318-668X 
primary 'Forneris, F.'     12 0000-0002-7818-1804 
# 
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 'Procollagen galactosyltransferase 1'  68589.164 2   2.4.1.50 ? ? 
'N-terminal GS and C-terminal AAA are restriction scars from recombinant expression vector - Residues not modeled are flexible' 
2 non-polymer nat "GALACTOSE-URIDINE-5'-DIPHOSPHATE"     566.302   2   ?        ? ? ? 
3 non-polymer syn "URIDINE-5'-DIPHOSPHATE"               404.161   1   ?        ? ? ? 
4 non-polymer syn 'MANGANESE (II) ION'                   54.938    1   ?        ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   2   ?        ? ? ? 
6 non-polymer syn 'CHLORIDE ION'                         35.453    6   ?        ? ? ? 
7 non-polymer syn 'CALCIUM ION'                          40.078    2   ?        ? ? ? 
8 non-polymer syn 'SODIUM ION'                           22.990    1   ?        ? ? ? 
9 water       nat water                                  18.015    136 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Collagen beta(1-O)galactosyltransferase 1,ColGalT 1,Glycosyltransferase 25 family member 1,Hydroxylysine galactosyltransferase 1' 
# 
_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       
;GSAPPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVA
VKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTV
VAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDII
VFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMIN
LRRRQDRRERMLRALQAQEIECRLVEAVDGKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRG
LQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGAR
KLLAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWD
RAKSQKMREQQALSREAKNSDVLQSPLDSAAAAA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSAPPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVA
VKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTV
VAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDII
VFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMIN
LRRRQDRRERMLRALQAQEIECRLVEAVDGKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRG
LQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGAR
KLLAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWD
RAKSQKMREQQALSREAKNSDVLQSPLDSAAAAA
;
_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 "GALACTOSE-URIDINE-5'-DIPHOSPHATE"     GDU 
3 "URIDINE-5'-DIPHOSPHATE"               UDP 
4 'MANGANESE (II) ION'                   MN  
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
6 'CHLORIDE ION'                         CL  
7 'CALCIUM ION'                          CA  
8 'SODIUM ION'                           NA  
9 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ALA n 
1 4   PRO n 
1 5   PRO n 
1 6   GLY n 
1 7   ALA n 
1 8   ASP n 
1 9   ALA n 
1 10  TYR n 
1 11  PHE n 
1 12  PRO n 
1 13  GLU n 
1 14  GLU n 
1 15  ARG n 
1 16  TRP n 
1 17  SER n 
1 18  PRO n 
1 19  GLU n 
1 20  SER n 
1 21  PRO n 
1 22  LEU n 
1 23  GLN n 
1 24  ALA n 
1 25  PRO n 
1 26  ARG n 
1 27  VAL n 
1 28  LEU n 
1 29  ILE n 
1 30  ALA n 
1 31  LEU n 
1 32  LEU n 
1 33  ALA n 
1 34  ARG n 
1 35  ASN n 
1 36  ALA n 
1 37  ALA n 
1 38  HIS n 
1 39  ALA n 
1 40  LEU n 
1 41  PRO n 
1 42  THR n 
1 43  THR n 
1 44  LEU n 
1 45  GLY n 
1 46  ALA n 
1 47  LEU n 
1 48  GLU n 
1 49  ARG n 
1 50  LEU n 
1 51  ARG n 
1 52  HIS n 
1 53  PRO n 
1 54  ARG n 
1 55  GLU n 
1 56  ARG n 
1 57  THR n 
1 58  ALA n 
1 59  LEU n 
1 60  TRP n 
1 61  VAL n 
1 62  ALA n 
1 63  THR n 
1 64  ASP n 
1 65  HIS n 
1 66  ASN n 
1 67  MET n 
1 68  ASP n 
1 69  ASN n 
1 70  THR n 
1 71  SER n 
1 72  THR n 
1 73  VAL n 
1 74  LEU n 
1 75  ARG n 
1 76  GLU n 
1 77  TRP n 
1 78  LEU n 
1 79  VAL n 
1 80  ALA n 
1 81  VAL n 
1 82  LYS n 
1 83  SER n 
1 84  LEU n 
1 85  TYR n 
1 86  HIS n 
1 87  SER n 
1 88  VAL n 
1 89  GLU n 
1 90  TRP n 
1 91  ARG n 
1 92  PRO n 
1 93  ALA n 
1 94  GLU n 
1 95  GLU n 
1 96  PRO n 
1 97  ARG n 
1 98  SER n 
1 99  TYR n 
1 100 PRO n 
1 101 ASP n 
1 102 GLU n 
1 103 GLU n 
1 104 GLY n 
1 105 PRO n 
1 106 LYS n 
1 107 HIS n 
1 108 TRP n 
1 109 SER n 
1 110 ASP n 
1 111 SER n 
1 112 ARG n 
1 113 TYR n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 MET n 
1 118 LYS n 
1 119 LEU n 
1 120 ARG n 
1 121 GLN n 
1 122 ALA n 
1 123 ALA n 
1 124 LEU n 
1 125 LYS n 
1 126 SER n 
1 127 ALA n 
1 128 ARG n 
1 129 ASP n 
1 130 MET n 
1 131 TRP n 
1 132 ALA n 
1 133 ASP n 
1 134 TYR n 
1 135 ILE n 
1 136 LEU n 
1 137 PHE n 
1 138 VAL n 
1 139 ASP n 
1 140 ALA n 
1 141 ASP n 
1 142 ASN n 
1 143 LEU n 
1 144 ILE n 
1 145 LEU n 
1 146 ASN n 
1 147 PRO n 
1 148 ASP n 
1 149 THR n 
1 150 LEU n 
1 151 SER n 
1 152 LEU n 
1 153 LEU n 
1 154 ILE n 
1 155 ALA n 
1 156 GLU n 
1 157 ASN n 
1 158 LYS n 
1 159 THR n 
1 160 VAL n 
1 161 VAL n 
1 162 ALA n 
1 163 PRO n 
1 164 MET n 
1 165 LEU n 
1 166 ASP n 
1 167 SER n 
1 168 ARG n 
1 169 ALA n 
1 170 ALA n 
1 171 TYR n 
1 172 SER n 
1 173 ASN n 
1 174 PHE n 
1 175 TRP n 
1 176 CYS n 
1 177 GLY n 
1 178 MET n 
1 179 THR n 
1 180 SER n 
1 181 GLN n 
1 182 GLY n 
1 183 TYR n 
1 184 TYR n 
1 185 LYS n 
1 186 ARG n 
1 187 THR n 
1 188 PRO n 
1 189 ALA n 
1 190 TYR n 
1 191 ILE n 
1 192 PRO n 
1 193 ILE n 
1 194 ARG n 
1 195 LYS n 
1 196 ARG n 
1 197 ASP n 
1 198 ARG n 
1 199 ARG n 
1 200 GLY n 
1 201 CYS n 
1 202 PHE n 
1 203 ALA n 
1 204 VAL n 
1 205 PRO n 
1 206 MET n 
1 207 VAL n 
1 208 HIS n 
1 209 SER n 
1 210 THR n 
1 211 PHE n 
1 212 LEU n 
1 213 ILE n 
1 214 ASP n 
1 215 LEU n 
1 216 ARG n 
1 217 LYS n 
1 218 ALA n 
1 219 ALA n 
1 220 SER n 
1 221 ARG n 
1 222 ASN n 
1 223 LEU n 
1 224 ALA n 
1 225 PHE n 
1 226 TYR n 
1 227 PRO n 
1 228 PRO n 
1 229 HIS n 
1 230 PRO n 
1 231 ASP n 
1 232 TYR n 
1 233 THR n 
1 234 TRP n 
1 235 SER n 
1 236 PHE n 
1 237 ASP n 
1 238 ASP n 
1 239 ILE n 
1 240 ILE n 
1 241 VAL n 
1 242 PHE n 
1 243 ALA n 
1 244 PHE n 
1 245 SER n 
1 246 CYS n 
1 247 LYS n 
1 248 GLN n 
1 249 ALA n 
1 250 GLU n 
1 251 VAL n 
1 252 GLN n 
1 253 MET n 
1 254 TYR n 
1 255 VAL n 
1 256 CYS n 
1 257 ASN n 
1 258 LYS n 
1 259 GLU n 
1 260 GLU n 
1 261 TYR n 
1 262 GLY n 
1 263 PHE n 
1 264 LEU n 
1 265 PRO n 
1 266 VAL n 
1 267 PRO n 
1 268 LEU n 
1 269 ARG n 
1 270 ALA n 
1 271 HIS n 
1 272 SER n 
1 273 THR n 
1 274 LEU n 
1 275 GLN n 
1 276 ASP n 
1 277 GLU n 
1 278 ALA n 
1 279 GLU n 
1 280 SER n 
1 281 PHE n 
1 282 MET n 
1 283 HIS n 
1 284 VAL n 
1 285 GLN n 
1 286 LEU n 
1 287 GLU n 
1 288 VAL n 
1 289 MET n 
1 290 VAL n 
1 291 LYS n 
1 292 HIS n 
1 293 PRO n 
1 294 PRO n 
1 295 ALA n 
1 296 GLU n 
1 297 PRO n 
1 298 SER n 
1 299 ARG n 
1 300 PHE n 
1 301 ILE n 
1 302 SER n 
1 303 ALA n 
1 304 PRO n 
1 305 THR n 
1 306 LYS n 
1 307 THR n 
1 308 PRO n 
1 309 ASP n 
1 310 LYS n 
1 311 MET n 
1 312 GLY n 
1 313 PHE n 
1 314 ASP n 
1 315 GLU n 
1 316 VAL n 
1 317 PHE n 
1 318 MET n 
1 319 ILE n 
1 320 ASN n 
1 321 LEU n 
1 322 ARG n 
1 323 ARG n 
1 324 ARG n 
1 325 GLN n 
1 326 ASP n 
1 327 ARG n 
1 328 ARG n 
1 329 GLU n 
1 330 ARG n 
1 331 MET n 
1 332 LEU n 
1 333 ARG n 
1 334 ALA n 
1 335 LEU n 
1 336 GLN n 
1 337 ALA n 
1 338 GLN n 
1 339 GLU n 
1 340 ILE n 
1 341 GLU n 
1 342 CYS n 
1 343 ARG n 
1 344 LEU n 
1 345 VAL n 
1 346 GLU n 
1 347 ALA n 
1 348 VAL n 
1 349 ASP n 
1 350 GLY n 
1 351 LYS n 
1 352 ALA n 
1 353 MET n 
1 354 ASN n 
1 355 THR n 
1 356 SER n 
1 357 GLN n 
1 358 VAL n 
1 359 GLU n 
1 360 ALA n 
1 361 LEU n 
1 362 GLY n 
1 363 ILE n 
1 364 GLN n 
1 365 MET n 
1 366 LEU n 
1 367 PRO n 
1 368 GLY n 
1 369 TYR n 
1 370 ARG n 
1 371 ASP n 
1 372 PRO n 
1 373 TYR n 
1 374 HIS n 
1 375 GLY n 
1 376 ARG n 
1 377 PRO n 
1 378 LEU n 
1 379 THR n 
1 380 LYS n 
1 381 GLY n 
1 382 GLU n 
1 383 LEU n 
1 384 GLY n 
1 385 CYS n 
1 386 PHE n 
1 387 LEU n 
1 388 SER n 
1 389 HIS n 
1 390 TYR n 
1 391 ASN n 
1 392 ILE n 
1 393 TRP n 
1 394 LYS n 
1 395 GLU n 
1 396 VAL n 
1 397 VAL n 
1 398 ASP n 
1 399 ARG n 
1 400 GLY n 
1 401 LEU n 
1 402 GLN n 
1 403 LYS n 
1 404 SER n 
1 405 LEU n 
1 406 VAL n 
1 407 PHE n 
1 408 GLU n 
1 409 ASP n 
1 410 ASP n 
1 411 LEU n 
1 412 ARG n 
1 413 PHE n 
1 414 GLU n 
1 415 ILE n 
1 416 PHE n 
1 417 PHE n 
1 418 LYS n 
1 419 ARG n 
1 420 ARG n 
1 421 LEU n 
1 422 MET n 
1 423 ASN n 
1 424 LEU n 
1 425 MET n 
1 426 ARG n 
1 427 ASP n 
1 428 VAL n 
1 429 GLU n 
1 430 ARG n 
1 431 GLU n 
1 432 GLY n 
1 433 LEU n 
1 434 ASP n 
1 435 TRP n 
1 436 ASP n 
1 437 LEU n 
1 438 ILE n 
1 439 TYR n 
1 440 VAL n 
1 441 GLY n 
1 442 ARG n 
1 443 LYS n 
1 444 ARG n 
1 445 MET n 
1 446 GLN n 
1 447 VAL n 
1 448 GLU n 
1 449 HIS n 
1 450 PRO n 
1 451 GLU n 
1 452 LYS n 
1 453 ALA n 
1 454 VAL n 
1 455 PRO n 
1 456 ARG n 
1 457 VAL n 
1 458 ARG n 
1 459 ASN n 
1 460 LEU n 
1 461 VAL n 
1 462 GLU n 
1 463 ALA n 
1 464 ASP n 
1 465 TYR n 
1 466 SER n 
1 467 TYR n 
1 468 TRP n 
1 469 THR n 
1 470 LEU n 
1 471 ALA n 
1 472 TYR n 
1 473 VAL n 
1 474 ILE n 
1 475 SER n 
1 476 LEU n 
1 477 GLN n 
1 478 GLY n 
1 479 ALA n 
1 480 ARG n 
1 481 LYS n 
1 482 LEU n 
1 483 LEU n 
1 484 ALA n 
1 485 ALA n 
1 486 GLU n 
1 487 PRO n 
1 488 LEU n 
1 489 SER n 
1 490 LYS n 
1 491 MET n 
1 492 LEU n 
1 493 PRO n 
1 494 VAL n 
1 495 ASP n 
1 496 GLU n 
1 497 PHE n 
1 498 LEU n 
1 499 PRO n 
1 500 VAL n 
1 501 MET n 
1 502 PHE n 
1 503 ASP n 
1 504 LYS n 
1 505 HIS n 
1 506 PRO n 
1 507 VAL n 
1 508 SER n 
1 509 GLU n 
1 510 TYR n 
1 511 LYS n 
1 512 ALA n 
1 513 HIS n 
1 514 PHE n 
1 515 SER n 
1 516 LEU n 
1 517 ARG n 
1 518 ASN n 
1 519 LEU n 
1 520 HIS n 
1 521 ALA n 
1 522 PHE n 
1 523 SER n 
1 524 VAL n 
1 525 GLU n 
1 526 PRO n 
1 527 LEU n 
1 528 LEU n 
1 529 ILE n 
1 530 TYR n 
1 531 PRO n 
1 532 THR n 
1 533 HIS n 
1 534 TYR n 
1 535 THR n 
1 536 GLY n 
1 537 ASP n 
1 538 ASP n 
1 539 GLY n 
1 540 TYR n 
1 541 VAL n 
1 542 SER n 
1 543 ASP n 
1 544 THR n 
1 545 GLU n 
1 546 THR n 
1 547 SER n 
1 548 VAL n 
1 549 VAL n 
1 550 TRP n 
1 551 ASN n 
1 552 ASN n 
1 553 GLU n 
1 554 HIS n 
1 555 VAL n 
1 556 LYS n 
1 557 THR n 
1 558 ASP n 
1 559 TRP n 
1 560 ASP n 
1 561 ARG n 
1 562 ALA n 
1 563 LYS n 
1 564 SER n 
1 565 GLN n 
1 566 LYS n 
1 567 MET n 
1 568 ARG n 
1 569 GLU n 
1 570 GLN n 
1 571 GLN n 
1 572 ALA n 
1 573 LEU n 
1 574 SER n 
1 575 ARG n 
1 576 GLU n 
1 577 ALA n 
1 578 LYS n 
1 579 ASN n 
1 580 SER n 
1 581 ASP n 
1 582 VAL n 
1 583 LEU n 
1 584 GLN n 
1 585 SER n 
1 586 PRO n 
1 587 LEU n 
1 588 ASP n 
1 589 SER n 
1 590 ALA n 
1 591 ALA n 
1 592 ALA n 
1 593 ALA n 
1 594 ALA 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                   594 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'COLGALT1, GLT25D1, PSEC0241' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          pET-SUMO 
_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 
CA  non-polymer         . 'CALCIUM ION'                          ?                     'Ca 2'              40.078  
CL  non-polymer         . 'CHLORIDE ION'                         ?                     'Cl -1'             35.453  
CYS 'L-peptide linking' y CYSTEINE                               ?                     'C3 H7 N O2 S'      121.158 
GDU non-polymer         . "GALACTOSE-URIDINE-5'-DIPHOSPHATE"     UDP-D-GALACTOPYRANOSE 'C15 H24 N2 O17 P2' 566.302 
GLN 'L-peptide linking' y GLUTAMINE                              ?                     'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                        ?                     'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                ?                     'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                              ?                     'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                  ?                     'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                             ?                     'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                ?                     'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                 ?                     'C6 H15 N2 O2 1'    147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ?                     'C6 H13 N O4 S'     195.237 
MET 'L-peptide linking' y METHIONINE                             ?                     'C5 H11 N O2 S'     149.211 
MN  non-polymer         . 'MANGANESE (II) ION'                   ?                     'Mn 2'              54.938  
NA  non-polymer         . 'SODIUM ION'                           ?                     'Na 1'              22.990  
PHE 'L-peptide linking' y PHENYLALANINE                          ?                     'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                ?                     'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                 ?                     'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                              ?                     'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                             ?                     'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                               ?                     'C9 H11 N O3'       181.189 
UDP 'RNA linking'       . "URIDINE-5'-DIPHOSPHATE"               ?                     'C9 H14 N2 O12 P2'  404.161 
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   GLY 1   28  ?   ?   ?   A . n 
A 1 2   SER 2   29  ?   ?   ?   A . n 
A 1 3   ALA 3   30  ?   ?   ?   A . n 
A 1 4   PRO 4   31  ?   ?   ?   A . n 
A 1 5   PRO 5   32  ?   ?   ?   A . n 
A 1 6   GLY 6   33  ?   ?   ?   A . n 
A 1 7   ALA 7   34  ?   ?   ?   A . n 
A 1 8   ASP 8   35  ?   ?   ?   A . n 
A 1 9   ALA 9   36  ?   ?   ?   A . n 
A 1 10  TYR 10  37  ?   ?   ?   A . n 
A 1 11  PHE 11  38  ?   ?   ?   A . n 
A 1 12  PRO 12  39  ?   ?   ?   A . n 
A 1 13  GLU 13  40  ?   ?   ?   A . n 
A 1 14  GLU 14  41  ?   ?   ?   A . n 
A 1 15  ARG 15  42  ?   ?   ?   A . n 
A 1 16  TRP 16  43  ?   ?   ?   A . n 
A 1 17  SER 17  44  44  SER SER A . n 
A 1 18  PRO 18  45  45  PRO PRO A . n 
A 1 19  GLU 19  46  46  GLU GLU A . n 
A 1 20  SER 20  47  47  SER SER A . n 
A 1 21  PRO 21  48  48  PRO PRO A . n 
A 1 22  LEU 22  49  49  LEU LEU A . n 
A 1 23  GLN 23  50  50  GLN GLN A . n 
A 1 24  ALA 24  51  51  ALA ALA A . n 
A 1 25  PRO 25  52  52  PRO PRO A . n 
A 1 26  ARG 26  53  53  ARG ARG A . n 
A 1 27  VAL 27  54  54  VAL VAL A . n 
A 1 28  LEU 28  55  55  LEU LEU A . n 
A 1 29  ILE 29  56  56  ILE ILE A . n 
A 1 30  ALA 30  57  57  ALA ALA A . n 
A 1 31  LEU 31  58  58  LEU LEU A . n 
A 1 32  LEU 32  59  59  LEU LEU A . n 
A 1 33  ALA 33  60  60  ALA ALA A . n 
A 1 34  ARG 34  61  61  ARG ARG A . n 
A 1 35  ASN 35  62  62  ASN ASN A . n 
A 1 36  ALA 36  63  63  ALA ALA A . n 
A 1 37  ALA 37  64  64  ALA ALA A . n 
A 1 38  HIS 38  65  65  HIS HIS A . n 
A 1 39  ALA 39  66  66  ALA ALA A . n 
A 1 40  LEU 40  67  67  LEU LEU A . n 
A 1 41  PRO 41  68  68  PRO PRO A . n 
A 1 42  THR 42  69  69  THR THR A . n 
A 1 43  THR 43  70  70  THR THR A . n 
A 1 44  LEU 44  71  71  LEU LEU A . n 
A 1 45  GLY 45  72  72  GLY GLY A . n 
A 1 46  ALA 46  73  73  ALA ALA A . n 
A 1 47  LEU 47  74  74  LEU LEU A . n 
A 1 48  GLU 48  75  75  GLU GLU A . n 
A 1 49  ARG 49  76  76  ARG ARG A . n 
A 1 50  LEU 50  77  77  LEU LEU A . n 
A 1 51  ARG 51  78  78  ARG ARG A . n 
A 1 52  HIS 52  79  79  HIS HIS A . n 
A 1 53  PRO 53  80  80  PRO PRO A . n 
A 1 54  ARG 54  81  81  ARG ARG A . n 
A 1 55  GLU 55  82  82  GLU GLU A . n 
A 1 56  ARG 56  83  83  ARG ARG A . n 
A 1 57  THR 57  84  84  THR THR A . n 
A 1 58  ALA 58  85  85  ALA ALA A . n 
A 1 59  LEU 59  86  86  LEU LEU A . n 
A 1 60  TRP 60  87  87  TRP TRP A . n 
A 1 61  VAL 61  88  88  VAL VAL A . n 
A 1 62  ALA 62  89  89  ALA ALA A . n 
A 1 63  THR 63  90  90  THR THR A . n 
A 1 64  ASP 64  91  91  ASP ASP A . n 
A 1 65  HIS 65  92  92  HIS HIS A . n 
A 1 66  ASN 66  93  93  ASN ASN A . n 
A 1 67  MET 67  94  94  MET MET A . n 
A 1 68  ASP 68  95  95  ASP ASP A . n 
A 1 69  ASN 69  96  96  ASN ASN A . n 
A 1 70  THR 70  97  97  THR THR A . n 
A 1 71  SER 71  98  98  SER SER A . n 
A 1 72  THR 72  99  99  THR THR A . n 
A 1 73  VAL 73  100 100 VAL VAL A . n 
A 1 74  LEU 74  101 101 LEU LEU A . n 
A 1 75  ARG 75  102 102 ARG ARG A . n 
A 1 76  GLU 76  103 103 GLU GLU A . n 
A 1 77  TRP 77  104 104 TRP TRP A . n 
A 1 78  LEU 78  105 105 LEU LEU A . n 
A 1 79  VAL 79  106 106 VAL VAL A . n 
A 1 80  ALA 80  107 107 ALA ALA A . n 
A 1 81  VAL 81  108 108 VAL VAL A . n 
A 1 82  LYS 82  109 109 LYS LYS A . n 
A 1 83  SER 83  110 110 SER SER A . n 
A 1 84  LEU 84  111 111 LEU LEU A . n 
A 1 85  TYR 85  112 112 TYR TYR A . n 
A 1 86  HIS 86  113 113 HIS HIS A . n 
A 1 87  SER 87  114 114 SER SER A . n 
A 1 88  VAL 88  115 115 VAL VAL A . n 
A 1 89  GLU 89  116 116 GLU GLU A . n 
A 1 90  TRP 90  117 117 TRP TRP A . n 
A 1 91  ARG 91  118 118 ARG ARG A . n 
A 1 92  PRO 92  119 119 PRO PRO A . n 
A 1 93  ALA 93  120 120 ALA ALA A . n 
A 1 94  GLU 94  121 121 GLU GLU A . n 
A 1 95  GLU 95  122 122 GLU GLU A . n 
A 1 96  PRO 96  123 123 PRO PRO A . n 
A 1 97  ARG 97  124 124 ARG ARG A . n 
A 1 98  SER 98  125 125 SER SER A . n 
A 1 99  TYR 99  126 126 TYR TYR A . n 
A 1 100 PRO 100 127 127 PRO PRO A . n 
A 1 101 ASP 101 128 128 ASP ASP A . n 
A 1 102 GLU 102 129 129 GLU GLU A . n 
A 1 103 GLU 103 130 130 GLU GLU A . n 
A 1 104 GLY 104 131 131 GLY GLY A . n 
A 1 105 PRO 105 132 132 PRO PRO A . n 
A 1 106 LYS 106 133 133 LYS LYS A . n 
A 1 107 HIS 107 134 134 HIS HIS A . n 
A 1 108 TRP 108 135 135 TRP TRP A . n 
A 1 109 SER 109 136 136 SER SER A . n 
A 1 110 ASP 110 137 137 ASP ASP A . n 
A 1 111 SER 111 138 138 SER SER A . n 
A 1 112 ARG 112 139 139 ARG ARG A . n 
A 1 113 TYR 113 140 140 TYR TYR A . n 
A 1 114 GLU 114 141 141 GLU GLU A . n 
A 1 115 HIS 115 142 142 HIS HIS A . n 
A 1 116 VAL 116 143 143 VAL VAL A . n 
A 1 117 MET 117 144 144 MET MET A . n 
A 1 118 LYS 118 145 145 LYS LYS A . n 
A 1 119 LEU 119 146 146 LEU LEU A . n 
A 1 120 ARG 120 147 147 ARG ARG A . n 
A 1 121 GLN 121 148 148 GLN GLN A . n 
A 1 122 ALA 122 149 149 ALA ALA A . n 
A 1 123 ALA 123 150 150 ALA ALA A . n 
A 1 124 LEU 124 151 151 LEU LEU A . n 
A 1 125 LYS 125 152 152 LYS LYS A . n 
A 1 126 SER 126 153 153 SER SER A . n 
A 1 127 ALA 127 154 154 ALA ALA A . n 
A 1 128 ARG 128 155 155 ARG ARG A . n 
A 1 129 ASP 129 156 156 ASP ASP A . n 
A 1 130 MET 130 157 157 MET MET A . n 
A 1 131 TRP 131 158 158 TRP TRP A . n 
A 1 132 ALA 132 159 159 ALA ALA A . n 
A 1 133 ASP 133 160 160 ASP ASP A . n 
A 1 134 TYR 134 161 161 TYR TYR A . n 
A 1 135 ILE 135 162 162 ILE ILE A . n 
A 1 136 LEU 136 163 163 LEU LEU A . n 
A 1 137 PHE 137 164 164 PHE PHE A . n 
A 1 138 VAL 138 165 165 VAL VAL A . n 
A 1 139 ASP 139 166 166 ASP ASP A . n 
A 1 140 ALA 140 167 167 ALA ALA A . n 
A 1 141 ASP 141 168 168 ASP ASP A . n 
A 1 142 ASN 142 169 169 ASN ASN A . n 
A 1 143 LEU 143 170 170 LEU LEU A . n 
A 1 144 ILE 144 171 171 ILE ILE A . n 
A 1 145 LEU 145 172 172 LEU LEU A . n 
A 1 146 ASN 146 173 173 ASN ASN A . n 
A 1 147 PRO 147 174 174 PRO PRO A . n 
A 1 148 ASP 148 175 175 ASP ASP A . n 
A 1 149 THR 149 176 176 THR THR A . n 
A 1 150 LEU 150 177 177 LEU LEU A . n 
A 1 151 SER 151 178 178 SER SER A . n 
A 1 152 LEU 152 179 179 LEU LEU A . n 
A 1 153 LEU 153 180 180 LEU LEU A . n 
A 1 154 ILE 154 181 181 ILE ILE A . n 
A 1 155 ALA 155 182 182 ALA ALA A . n 
A 1 156 GLU 156 183 183 GLU GLU A . n 
A 1 157 ASN 157 184 184 ASN ASN A . n 
A 1 158 LYS 158 185 185 LYS LYS A . n 
A 1 159 THR 159 186 186 THR THR A . n 
A 1 160 VAL 160 187 187 VAL VAL A . n 
A 1 161 VAL 161 188 188 VAL VAL A . n 
A 1 162 ALA 162 189 189 ALA ALA A . n 
A 1 163 PRO 163 190 190 PRO PRO A . n 
A 1 164 MET 164 191 191 MET MET A . n 
A 1 165 LEU 165 192 192 LEU LEU A . n 
A 1 166 ASP 166 193 193 ASP ASP A . n 
A 1 167 SER 167 194 194 SER SER A . n 
A 1 168 ARG 168 195 195 ARG ARG A . n 
A 1 169 ALA 169 196 196 ALA ALA A . n 
A 1 170 ALA 170 197 197 ALA ALA A . n 
A 1 171 TYR 171 198 198 TYR TYR A . n 
A 1 172 SER 172 199 199 SER SER A . n 
A 1 173 ASN 173 200 200 ASN ASN A . n 
A 1 174 PHE 174 201 201 PHE PHE A . n 
A 1 175 TRP 175 202 202 TRP TRP A . n 
A 1 176 CYS 176 203 203 CYS CYS A . n 
A 1 177 GLY 177 204 204 GLY GLY A . n 
A 1 178 MET 178 205 205 MET MET A . n 
A 1 179 THR 179 206 206 THR THR A . n 
A 1 180 SER 180 207 207 SER SER A . n 
A 1 181 GLN 181 208 208 GLN GLN A . n 
A 1 182 GLY 182 209 209 GLY GLY A . n 
A 1 183 TYR 183 210 210 TYR TYR A . n 
A 1 184 TYR 184 211 211 TYR TYR A . n 
A 1 185 LYS 185 212 212 LYS LYS A . n 
A 1 186 ARG 186 213 213 ARG ARG A . n 
A 1 187 THR 187 214 214 THR THR A . n 
A 1 188 PRO 188 215 215 PRO PRO A . n 
A 1 189 ALA 189 216 216 ALA ALA A . n 
A 1 190 TYR 190 217 217 TYR TYR A . n 
A 1 191 ILE 191 218 218 ILE ILE A . n 
A 1 192 PRO 192 219 219 PRO PRO A . n 
A 1 193 ILE 193 220 220 ILE ILE A . n 
A 1 194 ARG 194 221 221 ARG ARG A . n 
A 1 195 LYS 195 222 222 LYS LYS A . n 
A 1 196 ARG 196 223 223 ARG ARG A . n 
A 1 197 ASP 197 224 224 ASP ASP A . n 
A 1 198 ARG 198 225 225 ARG ARG A . n 
A 1 199 ARG 199 226 226 ARG ARG A . n 
A 1 200 GLY 200 227 227 GLY GLY A . n 
A 1 201 CYS 201 228 228 CYS CYS A . n 
A 1 202 PHE 202 229 229 PHE PHE A . n 
A 1 203 ALA 203 230 230 ALA ALA A . n 
A 1 204 VAL 204 231 231 VAL VAL A . n 
A 1 205 PRO 205 232 232 PRO PRO A . n 
A 1 206 MET 206 233 233 MET MET A . n 
A 1 207 VAL 207 234 234 VAL VAL A . n 
A 1 208 HIS 208 235 235 HIS HIS A . n 
A 1 209 SER 209 236 236 SER SER A . n 
A 1 210 THR 210 237 237 THR THR A . n 
A 1 211 PHE 211 238 238 PHE PHE A . n 
A 1 212 LEU 212 239 239 LEU LEU A . n 
A 1 213 ILE 213 240 240 ILE ILE A . n 
A 1 214 ASP 214 241 241 ASP ASP A . n 
A 1 215 LEU 215 242 242 LEU LEU A . n 
A 1 216 ARG 216 243 243 ARG ARG A . n 
A 1 217 LYS 217 244 244 LYS LYS A . n 
A 1 218 ALA 218 245 245 ALA ALA A . n 
A 1 219 ALA 219 246 246 ALA ALA A . n 
A 1 220 SER 220 247 247 SER SER A . n 
A 1 221 ARG 221 248 248 ARG ARG A . n 
A 1 222 ASN 222 249 249 ASN ASN A . n 
A 1 223 LEU 223 250 250 LEU LEU A . n 
A 1 224 ALA 224 251 251 ALA ALA A . n 
A 1 225 PHE 225 252 252 PHE PHE A . n 
A 1 226 TYR 226 253 253 TYR TYR A . n 
A 1 227 PRO 227 254 254 PRO PRO A . n 
A 1 228 PRO 228 255 255 PRO PRO A . n 
A 1 229 HIS 229 256 256 HIS HIS A . n 
A 1 230 PRO 230 257 257 PRO PRO A . n 
A 1 231 ASP 231 258 258 ASP ASP A . n 
A 1 232 TYR 232 259 259 TYR TYR A . n 
A 1 233 THR 233 260 260 THR THR A . n 
A 1 234 TRP 234 261 261 TRP TRP A . n 
A 1 235 SER 235 262 262 SER SER A . n 
A 1 236 PHE 236 263 263 PHE PHE A . n 
A 1 237 ASP 237 264 264 ASP ASP A . n 
A 1 238 ASP 238 265 265 ASP ASP A . n 
A 1 239 ILE 239 266 266 ILE ILE A . n 
A 1 240 ILE 240 267 267 ILE ILE A . n 
A 1 241 VAL 241 268 268 VAL VAL A . n 
A 1 242 PHE 242 269 269 PHE PHE A . n 
A 1 243 ALA 243 270 270 ALA ALA A . n 
A 1 244 PHE 244 271 271 PHE PHE A . n 
A 1 245 SER 245 272 272 SER SER A . n 
A 1 246 CYS 246 273 273 CYS CYS A . n 
A 1 247 LYS 247 274 274 LYS LYS A . n 
A 1 248 GLN 248 275 275 GLN GLN A . n 
A 1 249 ALA 249 276 276 ALA ALA A . n 
A 1 250 GLU 250 277 277 GLU GLU A . n 
A 1 251 VAL 251 278 278 VAL VAL A . n 
A 1 252 GLN 252 279 279 GLN GLN A . n 
A 1 253 MET 253 280 280 MET MET A . n 
A 1 254 TYR 254 281 281 TYR TYR A . n 
A 1 255 VAL 255 282 282 VAL VAL A . n 
A 1 256 CYS 256 283 283 CYS CYS A . n 
A 1 257 ASN 257 284 284 ASN ASN A . n 
A 1 258 LYS 258 285 285 LYS LYS A . n 
A 1 259 GLU 259 286 286 GLU GLU A . n 
A 1 260 GLU 260 287 287 GLU GLU A . n 
A 1 261 TYR 261 288 288 TYR TYR A . n 
A 1 262 GLY 262 289 289 GLY GLY A . n 
A 1 263 PHE 263 290 290 PHE PHE A . n 
A 1 264 LEU 264 291 291 LEU LEU A . n 
A 1 265 PRO 265 292 292 PRO PRO A . n 
A 1 266 VAL 266 293 293 VAL VAL A . n 
A 1 267 PRO 267 294 294 PRO PRO A . n 
A 1 268 LEU 268 295 295 LEU LEU A . n 
A 1 269 ARG 269 296 296 ARG ARG A . n 
A 1 270 ALA 270 297 297 ALA ALA A . n 
A 1 271 HIS 271 298 298 HIS HIS A . n 
A 1 272 SER 272 299 299 SER SER A . n 
A 1 273 THR 273 300 300 THR THR A . n 
A 1 274 LEU 274 301 301 LEU LEU A . n 
A 1 275 GLN 275 302 302 GLN GLN A . n 
A 1 276 ASP 276 303 303 ASP ASP A . n 
A 1 277 GLU 277 304 304 GLU GLU A . n 
A 1 278 ALA 278 305 305 ALA ALA A . n 
A 1 279 GLU 279 306 306 GLU GLU A . n 
A 1 280 SER 280 307 307 SER SER A . n 
A 1 281 PHE 281 308 308 PHE PHE A . n 
A 1 282 MET 282 309 309 MET MET A . n 
A 1 283 HIS 283 310 310 HIS HIS A . n 
A 1 284 VAL 284 311 311 VAL VAL A . n 
A 1 285 GLN 285 312 312 GLN GLN A . n 
A 1 286 LEU 286 313 313 LEU LEU A . n 
A 1 287 GLU 287 314 314 GLU GLU A . n 
A 1 288 VAL 288 315 315 VAL VAL A . n 
A 1 289 MET 289 316 316 MET MET A . n 
A 1 290 VAL 290 317 317 VAL VAL A . n 
A 1 291 LYS 291 318 318 LYS LYS A . n 
A 1 292 HIS 292 319 319 HIS HIS A . n 
A 1 293 PRO 293 320 320 PRO PRO A . n 
A 1 294 PRO 294 321 321 PRO PRO A . n 
A 1 295 ALA 295 322 322 ALA ALA A . n 
A 1 296 GLU 296 323 323 GLU GLU A . n 
A 1 297 PRO 297 324 324 PRO PRO A . n 
A 1 298 SER 298 325 325 SER SER A . n 
A 1 299 ARG 299 326 326 ARG ARG A . n 
A 1 300 PHE 300 327 327 PHE PHE A . n 
A 1 301 ILE 301 328 328 ILE ILE A . n 
A 1 302 SER 302 329 329 SER SER A . n 
A 1 303 ALA 303 330 330 ALA ALA A . n 
A 1 304 PRO 304 331 331 PRO PRO A . n 
A 1 305 THR 305 332 332 THR THR A . n 
A 1 306 LYS 306 333 333 LYS LYS A . n 
A 1 307 THR 307 334 334 THR THR A . n 
A 1 308 PRO 308 335 335 PRO PRO A . n 
A 1 309 ASP 309 336 336 ASP ASP A . n 
A 1 310 LYS 310 337 337 LYS LYS A . n 
A 1 311 MET 311 338 338 MET MET A . n 
A 1 312 GLY 312 339 339 GLY GLY A . n 
A 1 313 PHE 313 340 340 PHE PHE A . n 
A 1 314 ASP 314 341 341 ASP ASP A . n 
A 1 315 GLU 315 342 342 GLU GLU A . n 
A 1 316 VAL 316 343 343 VAL VAL A . n 
A 1 317 PHE 317 344 344 PHE PHE A . n 
A 1 318 MET 318 345 345 MET MET A . n 
A 1 319 ILE 319 346 346 ILE ILE A . n 
A 1 320 ASN 320 347 347 ASN ASN A . n 
A 1 321 LEU 321 348 348 LEU LEU A . n 
A 1 322 ARG 322 349 349 ARG ARG A . n 
A 1 323 ARG 323 350 350 ARG ARG A . n 
A 1 324 ARG 324 351 351 ARG ARG A . n 
A 1 325 GLN 325 352 352 GLN GLN A . n 
A 1 326 ASP 326 353 353 ASP ASP A . n 
A 1 327 ARG 327 354 354 ARG ARG A . n 
A 1 328 ARG 328 355 355 ARG ARG A . n 
A 1 329 GLU 329 356 356 GLU GLU A . n 
A 1 330 ARG 330 357 357 ARG ARG A . n 
A 1 331 MET 331 358 358 MET MET A . n 
A 1 332 LEU 332 359 359 LEU LEU A . n 
A 1 333 ARG 333 360 360 ARG ARG A . n 
A 1 334 ALA 334 361 361 ALA ALA A . n 
A 1 335 LEU 335 362 362 LEU LEU A . n 
A 1 336 GLN 336 363 363 GLN GLN A . n 
A 1 337 ALA 337 364 364 ALA ALA A . n 
A 1 338 GLN 338 365 365 GLN GLN A . n 
A 1 339 GLU 339 366 366 GLU GLU A . n 
A 1 340 ILE 340 367 367 ILE ILE A . n 
A 1 341 GLU 341 368 368 GLU GLU A . n 
A 1 342 CYS 342 369 369 CYS CYS A . n 
A 1 343 ARG 343 370 370 ARG ARG A . n 
A 1 344 LEU 344 371 371 LEU LEU A . n 
A 1 345 VAL 345 372 372 VAL VAL A . n 
A 1 346 GLU 346 373 373 GLU GLU A . n 
A 1 347 ALA 347 374 374 ALA ALA A . n 
A 1 348 VAL 348 375 375 VAL VAL A . n 
A 1 349 ASP 349 376 376 ASP ASP A . n 
A 1 350 GLY 350 377 377 GLY GLY A . n 
A 1 351 LYS 351 378 378 LYS LYS A . n 
A 1 352 ALA 352 379 379 ALA ALA A . n 
A 1 353 MET 353 380 380 MET MET A . n 
A 1 354 ASN 354 381 381 ASN ASN A . n 
A 1 355 THR 355 382 382 THR THR A . n 
A 1 356 SER 356 383 383 SER SER A . n 
A 1 357 GLN 357 384 384 GLN GLN A . n 
A 1 358 VAL 358 385 385 VAL VAL A . n 
A 1 359 GLU 359 386 386 GLU GLU A . n 
A 1 360 ALA 360 387 387 ALA ALA A . n 
A 1 361 LEU 361 388 388 LEU LEU A . n 
A 1 362 GLY 362 389 389 GLY GLY A . n 
A 1 363 ILE 363 390 390 ILE ILE A . n 
A 1 364 GLN 364 391 391 GLN GLN A . n 
A 1 365 MET 365 392 392 MET MET A . n 
A 1 366 LEU 366 393 393 LEU LEU A . n 
A 1 367 PRO 367 394 394 PRO PRO A . n 
A 1 368 GLY 368 395 395 GLY GLY A . n 
A 1 369 TYR 369 396 396 TYR TYR A . n 
A 1 370 ARG 370 397 397 ARG ARG A . n 
A 1 371 ASP 371 398 398 ASP ASP A . n 
A 1 372 PRO 372 399 399 PRO PRO A . n 
A 1 373 TYR 373 400 400 TYR TYR A . n 
A 1 374 HIS 374 401 401 HIS HIS A . n 
A 1 375 GLY 375 402 402 GLY GLY A . n 
A 1 376 ARG 376 403 403 ARG ARG A . n 
A 1 377 PRO 377 404 404 PRO PRO A . n 
A 1 378 LEU 378 405 405 LEU LEU A . n 
A 1 379 THR 379 406 406 THR THR A . n 
A 1 380 LYS 380 407 407 LYS LYS A . n 
A 1 381 GLY 381 408 408 GLY GLY A . n 
A 1 382 GLU 382 409 409 GLU GLU A . n 
A 1 383 LEU 383 410 410 LEU LEU A . n 
A 1 384 GLY 384 411 411 GLY GLY A . n 
A 1 385 CYS 385 412 412 CYS CYS A . n 
A 1 386 PHE 386 413 413 PHE PHE A . n 
A 1 387 LEU 387 414 414 LEU LEU A . n 
A 1 388 SER 388 415 415 SER SER A . n 
A 1 389 HIS 389 416 416 HIS HIS A . n 
A 1 390 TYR 390 417 417 TYR TYR A . n 
A 1 391 ASN 391 418 418 ASN ASN A . n 
A 1 392 ILE 392 419 419 ILE ILE A . n 
A 1 393 TRP 393 420 420 TRP TRP A . n 
A 1 394 LYS 394 421 421 LYS LYS A . n 
A 1 395 GLU 395 422 422 GLU GLU A . n 
A 1 396 VAL 396 423 423 VAL VAL A . n 
A 1 397 VAL 397 424 424 VAL VAL A . n 
A 1 398 ASP 398 425 425 ASP ASP A . n 
A 1 399 ARG 399 426 426 ARG ARG A . n 
A 1 400 GLY 400 427 427 GLY GLY A . n 
A 1 401 LEU 401 428 428 LEU LEU A . n 
A 1 402 GLN 402 429 429 GLN GLN A . n 
A 1 403 LYS 403 430 430 LYS LYS A . n 
A 1 404 SER 404 431 431 SER SER A . n 
A 1 405 LEU 405 432 432 LEU LEU A . n 
A 1 406 VAL 406 433 433 VAL VAL A . n 
A 1 407 PHE 407 434 434 PHE PHE A . n 
A 1 408 GLU 408 435 435 GLU GLU A . n 
A 1 409 ASP 409 436 436 ASP ASP A . n 
A 1 410 ASP 410 437 437 ASP ASP A . n 
A 1 411 LEU 411 438 438 LEU LEU A . n 
A 1 412 ARG 412 439 439 ARG ARG A . n 
A 1 413 PHE 413 440 440 PHE PHE A . n 
A 1 414 GLU 414 441 441 GLU GLU A . n 
A 1 415 ILE 415 442 442 ILE ILE A . n 
A 1 416 PHE 416 443 443 PHE PHE A . n 
A 1 417 PHE 417 444 444 PHE PHE A . n 
A 1 418 LYS 418 445 445 LYS LYS A . n 
A 1 419 ARG 419 446 446 ARG ARG A . n 
A 1 420 ARG 420 447 447 ARG ARG A . n 
A 1 421 LEU 421 448 448 LEU LEU A . n 
A 1 422 MET 422 449 449 MET MET A . n 
A 1 423 ASN 423 450 450 ASN ASN A . n 
A 1 424 LEU 424 451 451 LEU LEU A . n 
A 1 425 MET 425 452 452 MET MET A . n 
A 1 426 ARG 426 453 453 ARG ARG A . n 
A 1 427 ASP 427 454 454 ASP ASP A . n 
A 1 428 VAL 428 455 455 VAL VAL A . n 
A 1 429 GLU 429 456 456 GLU GLU A . n 
A 1 430 ARG 430 457 457 ARG ARG A . n 
A 1 431 GLU 431 458 458 GLU GLU A . n 
A 1 432 GLY 432 459 459 GLY GLY A . n 
A 1 433 LEU 433 460 460 LEU LEU A . n 
A 1 434 ASP 434 461 461 ASP ASP A . n 
A 1 435 TRP 435 462 462 TRP TRP A . n 
A 1 436 ASP 436 463 463 ASP ASP A . n 
A 1 437 LEU 437 464 464 LEU LEU A . n 
A 1 438 ILE 438 465 465 ILE ILE A . n 
A 1 439 TYR 439 466 466 TYR TYR A . n 
A 1 440 VAL 440 467 467 VAL VAL A . n 
A 1 441 GLY 441 468 468 GLY GLY A . n 
A 1 442 ARG 442 469 469 ARG ARG A . n 
A 1 443 LYS 443 470 470 LYS LYS A . n 
A 1 444 ARG 444 471 471 ARG ARG A . n 
A 1 445 MET 445 472 472 MET MET A . n 
A 1 446 GLN 446 473 473 GLN GLN A . n 
A 1 447 VAL 447 474 474 VAL VAL A . n 
A 1 448 GLU 448 475 475 GLU GLU A . n 
A 1 449 HIS 449 476 476 HIS HIS A . n 
A 1 450 PRO 450 477 477 PRO PRO A . n 
A 1 451 GLU 451 478 478 GLU GLU A . n 
A 1 452 LYS 452 479 479 LYS LYS A . n 
A 1 453 ALA 453 480 480 ALA ALA A . n 
A 1 454 VAL 454 481 481 VAL VAL A . n 
A 1 455 PRO 455 482 482 PRO PRO A . n 
A 1 456 ARG 456 483 483 ARG ARG A . n 
A 1 457 VAL 457 484 484 VAL VAL A . n 
A 1 458 ARG 458 485 485 ARG ARG A . n 
A 1 459 ASN 459 486 486 ASN ASN A . n 
A 1 460 LEU 460 487 487 LEU LEU A . n 
A 1 461 VAL 461 488 488 VAL VAL A . n 
A 1 462 GLU 462 489 489 GLU GLU A . n 
A 1 463 ALA 463 490 490 ALA ALA A . n 
A 1 464 ASP 464 491 491 ASP ASP A . n 
A 1 465 TYR 465 492 492 TYR TYR A . n 
A 1 466 SER 466 493 493 SER SER A . n 
A 1 467 TYR 467 494 494 TYR TYR A . n 
A 1 468 TRP 468 495 495 TRP TRP A . n 
A 1 469 THR 469 496 496 THR THR A . n 
A 1 470 LEU 470 497 497 LEU LEU A . n 
A 1 471 ALA 471 498 498 ALA ALA A . n 
A 1 472 TYR 472 499 499 TYR TYR A . n 
A 1 473 VAL 473 500 500 VAL VAL A . n 
A 1 474 ILE 474 501 501 ILE ILE A . n 
A 1 475 SER 475 502 502 SER SER A . n 
A 1 476 LEU 476 503 503 LEU LEU A . n 
A 1 477 GLN 477 504 504 GLN GLN A . n 
A 1 478 GLY 478 505 505 GLY GLY A . n 
A 1 479 ALA 479 506 506 ALA ALA A . n 
A 1 480 ARG 480 507 507 ARG ARG A . n 
A 1 481 LYS 481 508 508 LYS LYS A . n 
A 1 482 LEU 482 509 509 LEU LEU A . n 
A 1 483 LEU 483 510 510 LEU LEU A . n 
A 1 484 ALA 484 511 511 ALA ALA A . n 
A 1 485 ALA 485 512 512 ALA ALA A . n 
A 1 486 GLU 486 513 513 GLU GLU A . n 
A 1 487 PRO 487 514 514 PRO PRO A . n 
A 1 488 LEU 488 515 515 LEU LEU A . n 
A 1 489 SER 489 516 516 SER SER A . n 
A 1 490 LYS 490 517 517 LYS LYS A . n 
A 1 491 MET 491 518 518 MET MET A . n 
A 1 492 LEU 492 519 519 LEU LEU A . n 
A 1 493 PRO 493 520 520 PRO PRO A . n 
A 1 494 VAL 494 521 521 VAL VAL A . n 
A 1 495 ASP 495 522 522 ASP ASP A . n 
A 1 496 GLU 496 523 523 GLU GLU A . n 
A 1 497 PHE 497 524 524 PHE PHE A . n 
A 1 498 LEU 498 525 525 LEU LEU A . n 
A 1 499 PRO 499 526 526 PRO PRO A . n 
A 1 500 VAL 500 527 527 VAL VAL A . n 
A 1 501 MET 501 528 528 MET MET A . n 
A 1 502 PHE 502 529 529 PHE PHE A . n 
A 1 503 ASP 503 530 530 ASP ASP A . n 
A 1 504 LYS 504 531 531 LYS LYS A . n 
A 1 505 HIS 505 532 532 HIS HIS A . n 
A 1 506 PRO 506 533 533 PRO PRO A . n 
A 1 507 VAL 507 534 534 VAL VAL A . n 
A 1 508 SER 508 535 535 SER SER A . n 
A 1 509 GLU 509 536 536 GLU GLU A . n 
A 1 510 TYR 510 537 537 TYR TYR A . n 
A 1 511 LYS 511 538 538 LYS LYS A . n 
A 1 512 ALA 512 539 539 ALA ALA A . n 
A 1 513 HIS 513 540 540 HIS HIS A . n 
A 1 514 PHE 514 541 541 PHE PHE A . n 
A 1 515 SER 515 542 542 SER SER A . n 
A 1 516 LEU 516 543 543 LEU LEU A . n 
A 1 517 ARG 517 544 544 ARG ARG A . n 
A 1 518 ASN 518 545 545 ASN ASN A . n 
A 1 519 LEU 519 546 546 LEU LEU A . n 
A 1 520 HIS 520 547 547 HIS HIS A . n 
A 1 521 ALA 521 548 548 ALA ALA A . n 
A 1 522 PHE 522 549 549 PHE PHE A . n 
A 1 523 SER 523 550 550 SER SER A . n 
A 1 524 VAL 524 551 551 VAL VAL A . n 
A 1 525 GLU 525 552 552 GLU GLU A . n 
A 1 526 PRO 526 553 553 PRO PRO A . n 
A 1 527 LEU 527 554 554 LEU LEU A . n 
A 1 528 LEU 528 555 555 LEU LEU A . n 
A 1 529 ILE 529 556 556 ILE ILE A . n 
A 1 530 TYR 530 557 557 TYR TYR A . n 
A 1 531 PRO 531 558 558 PRO PRO A . n 
A 1 532 THR 532 559 559 THR THR A . n 
A 1 533 HIS 533 560 560 HIS HIS A . n 
A 1 534 TYR 534 561 561 TYR TYR A . n 
A 1 535 THR 535 562 562 THR THR A . n 
A 1 536 GLY 536 563 563 GLY GLY A . n 
A 1 537 ASP 537 564 564 ASP ASP A . n 
A 1 538 ASP 538 565 565 ASP ASP A . n 
A 1 539 GLY 539 566 566 GLY GLY A . n 
A 1 540 TYR 540 567 567 TYR TYR A . n 
A 1 541 VAL 541 568 568 VAL VAL A . n 
A 1 542 SER 542 569 569 SER SER A . n 
A 1 543 ASP 543 570 570 ASP ASP A . n 
A 1 544 THR 544 571 571 THR THR A . n 
A 1 545 GLU 545 572 572 GLU GLU A . n 
A 1 546 THR 546 573 573 THR THR A . n 
A 1 547 SER 547 574 574 SER SER A . n 
A 1 548 VAL 548 575 575 VAL VAL A . n 
A 1 549 VAL 549 576 576 VAL VAL A . n 
A 1 550 TRP 550 577 577 TRP TRP A . n 
A 1 551 ASN 551 578 578 ASN ASN A . n 
A 1 552 ASN 552 579 579 ASN ASN A . n 
A 1 553 GLU 553 580 580 GLU GLU A . n 
A 1 554 HIS 554 581 ?   ?   ?   A . n 
A 1 555 VAL 555 582 ?   ?   ?   A . n 
A 1 556 LYS 556 583 ?   ?   ?   A . n 
A 1 557 THR 557 584 ?   ?   ?   A . n 
A 1 558 ASP 558 585 ?   ?   ?   A . n 
A 1 559 TRP 559 586 ?   ?   ?   A . n 
A 1 560 ASP 560 587 ?   ?   ?   A . n 
A 1 561 ARG 561 588 ?   ?   ?   A . n 
A 1 562 ALA 562 589 ?   ?   ?   A . n 
A 1 563 LYS 563 590 ?   ?   ?   A . n 
A 1 564 SER 564 591 ?   ?   ?   A . n 
A 1 565 GLN 565 592 ?   ?   ?   A . n 
A 1 566 LYS 566 593 ?   ?   ?   A . n 
A 1 567 MET 567 594 ?   ?   ?   A . n 
A 1 568 ARG 568 595 ?   ?   ?   A . n 
A 1 569 GLU 569 596 ?   ?   ?   A . n 
A 1 570 GLN 570 597 ?   ?   ?   A . n 
A 1 571 GLN 571 598 ?   ?   ?   A . n 
A 1 572 ALA 572 599 ?   ?   ?   A . n 
A 1 573 LEU 573 600 ?   ?   ?   A . n 
A 1 574 SER 574 601 ?   ?   ?   A . n 
A 1 575 ARG 575 602 ?   ?   ?   A . n 
A 1 576 GLU 576 603 ?   ?   ?   A . n 
A 1 577 ALA 577 604 ?   ?   ?   A . n 
A 1 578 LYS 578 605 ?   ?   ?   A . n 
A 1 579 ASN 579 606 ?   ?   ?   A . n 
A 1 580 SER 580 607 ?   ?   ?   A . n 
A 1 581 ASP 581 608 ?   ?   ?   A . n 
A 1 582 VAL 582 609 ?   ?   ?   A . n 
A 1 583 LEU 583 610 ?   ?   ?   A . n 
A 1 584 GLN 584 611 ?   ?   ?   A . n 
A 1 585 SER 585 612 ?   ?   ?   A . n 
A 1 586 PRO 586 613 ?   ?   ?   A . n 
A 1 587 LEU 587 614 ?   ?   ?   A . n 
A 1 588 ASP 588 615 ?   ?   ?   A . n 
A 1 589 SER 589 616 ?   ?   ?   A . n 
A 1 590 ALA 590 617 ?   ?   ?   A . n 
A 1 591 ALA 591 618 ?   ?   ?   A . n 
A 1 592 ALA 592 619 ?   ?   ?   A . n 
A 1 593 ALA 593 620 ?   ?   ?   A . n 
A 1 594 ALA 594 621 ?   ?   ?   A . n 
B 1 1   GLY 1   28  ?   ?   ?   B . n 
B 1 2   SER 2   29  ?   ?   ?   B . n 
B 1 3   ALA 3   30  ?   ?   ?   B . n 
B 1 4   PRO 4   31  ?   ?   ?   B . n 
B 1 5   PRO 5   32  ?   ?   ?   B . n 
B 1 6   GLY 6   33  ?   ?   ?   B . n 
B 1 7   ALA 7   34  ?   ?   ?   B . n 
B 1 8   ASP 8   35  ?   ?   ?   B . n 
B 1 9   ALA 9   36  ?   ?   ?   B . n 
B 1 10  TYR 10  37  ?   ?   ?   B . n 
B 1 11  PHE 11  38  ?   ?   ?   B . n 
B 1 12  PRO 12  39  ?   ?   ?   B . n 
B 1 13  GLU 13  40  ?   ?   ?   B . n 
B 1 14  GLU 14  41  ?   ?   ?   B . n 
B 1 15  ARG 15  42  42  ARG ARG B . n 
B 1 16  TRP 16  43  43  TRP TRP B . n 
B 1 17  SER 17  44  44  SER SER B . n 
B 1 18  PRO 18  45  45  PRO PRO B . n 
B 1 19  GLU 19  46  46  GLU GLU B . n 
B 1 20  SER 20  47  47  SER SER B . n 
B 1 21  PRO 21  48  48  PRO PRO B . n 
B 1 22  LEU 22  49  49  LEU LEU B . n 
B 1 23  GLN 23  50  50  GLN GLN B . n 
B 1 24  ALA 24  51  51  ALA ALA B . n 
B 1 25  PRO 25  52  52  PRO PRO B . n 
B 1 26  ARG 26  53  53  ARG ARG B . n 
B 1 27  VAL 27  54  54  VAL VAL B . n 
B 1 28  LEU 28  55  55  LEU LEU B . n 
B 1 29  ILE 29  56  56  ILE ILE B . n 
B 1 30  ALA 30  57  57  ALA ALA B . n 
B 1 31  LEU 31  58  58  LEU LEU B . n 
B 1 32  LEU 32  59  59  LEU LEU B . n 
B 1 33  ALA 33  60  60  ALA ALA B . n 
B 1 34  ARG 34  61  61  ARG ARG B . n 
B 1 35  ASN 35  62  62  ASN ASN B . n 
B 1 36  ALA 36  63  63  ALA ALA B . n 
B 1 37  ALA 37  64  64  ALA ALA B . n 
B 1 38  HIS 38  65  65  HIS HIS B . n 
B 1 39  ALA 39  66  66  ALA ALA B . n 
B 1 40  LEU 40  67  67  LEU LEU B . n 
B 1 41  PRO 41  68  68  PRO PRO B . n 
B 1 42  THR 42  69  69  THR THR B . n 
B 1 43  THR 43  70  70  THR THR B . n 
B 1 44  LEU 44  71  71  LEU LEU B . n 
B 1 45  GLY 45  72  72  GLY GLY B . n 
B 1 46  ALA 46  73  73  ALA ALA B . n 
B 1 47  LEU 47  74  74  LEU LEU B . n 
B 1 48  GLU 48  75  75  GLU GLU B . n 
B 1 49  ARG 49  76  76  ARG ARG B . n 
B 1 50  LEU 50  77  77  LEU LEU B . n 
B 1 51  ARG 51  78  78  ARG ARG B . n 
B 1 52  HIS 52  79  79  HIS HIS B . n 
B 1 53  PRO 53  80  80  PRO PRO B . n 
B 1 54  ARG 54  81  81  ARG ARG B . n 
B 1 55  GLU 55  82  82  GLU GLU B . n 
B 1 56  ARG 56  83  83  ARG ARG B . n 
B 1 57  THR 57  84  84  THR THR B . n 
B 1 58  ALA 58  85  85  ALA ALA B . n 
B 1 59  LEU 59  86  86  LEU LEU B . n 
B 1 60  TRP 60  87  87  TRP TRP B . n 
B 1 61  VAL 61  88  88  VAL VAL B . n 
B 1 62  ALA 62  89  89  ALA ALA B . n 
B 1 63  THR 63  90  90  THR THR B . n 
B 1 64  ASP 64  91  91  ASP ASP B . n 
B 1 65  HIS 65  92  92  HIS HIS B . n 
B 1 66  ASN 66  93  93  ASN ASN B . n 
B 1 67  MET 67  94  94  MET MET B . n 
B 1 68  ASP 68  95  95  ASP ASP B . n 
B 1 69  ASN 69  96  96  ASN ASN B . n 
B 1 70  THR 70  97  97  THR THR B . n 
B 1 71  SER 71  98  98  SER SER B . n 
B 1 72  THR 72  99  99  THR THR B . n 
B 1 73  VAL 73  100 100 VAL VAL B . n 
B 1 74  LEU 74  101 101 LEU LEU B . n 
B 1 75  ARG 75  102 102 ARG ARG B . n 
B 1 76  GLU 76  103 103 GLU GLU B . n 
B 1 77  TRP 77  104 104 TRP TRP B . n 
B 1 78  LEU 78  105 105 LEU LEU B . n 
B 1 79  VAL 79  106 106 VAL VAL B . n 
B 1 80  ALA 80  107 107 ALA ALA B . n 
B 1 81  VAL 81  108 108 VAL VAL B . n 
B 1 82  LYS 82  109 109 LYS LYS B . n 
B 1 83  SER 83  110 110 SER SER B . n 
B 1 84  LEU 84  111 111 LEU LEU B . n 
B 1 85  TYR 85  112 112 TYR TYR B . n 
B 1 86  HIS 86  113 113 HIS HIS B . n 
B 1 87  SER 87  114 114 SER SER B . n 
B 1 88  VAL 88  115 115 VAL VAL B . n 
B 1 89  GLU 89  116 116 GLU GLU B . n 
B 1 90  TRP 90  117 117 TRP TRP B . n 
B 1 91  ARG 91  118 118 ARG ARG B . n 
B 1 92  PRO 92  119 119 PRO PRO B . n 
B 1 93  ALA 93  120 120 ALA ALA B . n 
B 1 94  GLU 94  121 121 GLU GLU B . n 
B 1 95  GLU 95  122 122 GLU GLU B . n 
B 1 96  PRO 96  123 123 PRO PRO B . n 
B 1 97  ARG 97  124 124 ARG ARG B . n 
B 1 98  SER 98  125 125 SER SER B . n 
B 1 99  TYR 99  126 126 TYR TYR B . n 
B 1 100 PRO 100 127 127 PRO PRO B . n 
B 1 101 ASP 101 128 128 ASP ASP B . n 
B 1 102 GLU 102 129 129 GLU GLU B . n 
B 1 103 GLU 103 130 130 GLU GLU B . n 
B 1 104 GLY 104 131 131 GLY GLY B . n 
B 1 105 PRO 105 132 132 PRO PRO B . n 
B 1 106 LYS 106 133 133 LYS LYS B . n 
B 1 107 HIS 107 134 134 HIS HIS B . n 
B 1 108 TRP 108 135 135 TRP TRP B . n 
B 1 109 SER 109 136 136 SER SER B . n 
B 1 110 ASP 110 137 137 ASP ASP B . n 
B 1 111 SER 111 138 138 SER SER B . n 
B 1 112 ARG 112 139 139 ARG ARG B . n 
B 1 113 TYR 113 140 140 TYR TYR B . n 
B 1 114 GLU 114 141 141 GLU GLU B . n 
B 1 115 HIS 115 142 142 HIS HIS B . n 
B 1 116 VAL 116 143 143 VAL VAL B . n 
B 1 117 MET 117 144 144 MET MET B . n 
B 1 118 LYS 118 145 145 LYS LYS B . n 
B 1 119 LEU 119 146 146 LEU LEU B . n 
B 1 120 ARG 120 147 147 ARG ARG B . n 
B 1 121 GLN 121 148 148 GLN GLN B . n 
B 1 122 ALA 122 149 149 ALA ALA B . n 
B 1 123 ALA 123 150 150 ALA ALA B . n 
B 1 124 LEU 124 151 151 LEU LEU B . n 
B 1 125 LYS 125 152 152 LYS LYS B . n 
B 1 126 SER 126 153 153 SER SER B . n 
B 1 127 ALA 127 154 154 ALA ALA B . n 
B 1 128 ARG 128 155 155 ARG ARG B . n 
B 1 129 ASP 129 156 156 ASP ASP B . n 
B 1 130 MET 130 157 157 MET MET B . n 
B 1 131 TRP 131 158 158 TRP TRP B . n 
B 1 132 ALA 132 159 159 ALA ALA B . n 
B 1 133 ASP 133 160 160 ASP ASP B . n 
B 1 134 TYR 134 161 161 TYR TYR B . n 
B 1 135 ILE 135 162 162 ILE ILE B . n 
B 1 136 LEU 136 163 163 LEU LEU B . n 
B 1 137 PHE 137 164 164 PHE PHE B . n 
B 1 138 VAL 138 165 165 VAL VAL B . n 
B 1 139 ASP 139 166 166 ASP ASP B . n 
B 1 140 ALA 140 167 167 ALA ALA B . n 
B 1 141 ASP 141 168 168 ASP ASP B . n 
B 1 142 ASN 142 169 169 ASN ASN B . n 
B 1 143 LEU 143 170 170 LEU LEU B . n 
B 1 144 ILE 144 171 171 ILE ILE B . n 
B 1 145 LEU 145 172 172 LEU LEU B . n 
B 1 146 ASN 146 173 173 ASN ASN B . n 
B 1 147 PRO 147 174 174 PRO PRO B . n 
B 1 148 ASP 148 175 175 ASP ASP B . n 
B 1 149 THR 149 176 176 THR THR B . n 
B 1 150 LEU 150 177 177 LEU LEU B . n 
B 1 151 SER 151 178 178 SER SER B . n 
B 1 152 LEU 152 179 179 LEU LEU B . n 
B 1 153 LEU 153 180 180 LEU LEU B . n 
B 1 154 ILE 154 181 181 ILE ILE B . n 
B 1 155 ALA 155 182 182 ALA ALA B . n 
B 1 156 GLU 156 183 183 GLU GLU B . n 
B 1 157 ASN 157 184 184 ASN ASN B . n 
B 1 158 LYS 158 185 185 LYS LYS B . n 
B 1 159 THR 159 186 186 THR THR B . n 
B 1 160 VAL 160 187 187 VAL VAL B . n 
B 1 161 VAL 161 188 188 VAL VAL B . n 
B 1 162 ALA 162 189 189 ALA ALA B . n 
B 1 163 PRO 163 190 190 PRO PRO B . n 
B 1 164 MET 164 191 191 MET MET B . n 
B 1 165 LEU 165 192 192 LEU LEU B . n 
B 1 166 ASP 166 193 193 ASP ASP B . n 
B 1 167 SER 167 194 194 SER SER B . n 
B 1 168 ARG 168 195 195 ARG ARG B . n 
B 1 169 ALA 169 196 196 ALA ALA B . n 
B 1 170 ALA 170 197 197 ALA ALA B . n 
B 1 171 TYR 171 198 198 TYR TYR B . n 
B 1 172 SER 172 199 199 SER SER B . n 
B 1 173 ASN 173 200 200 ASN ASN B . n 
B 1 174 PHE 174 201 201 PHE PHE B . n 
B 1 175 TRP 175 202 202 TRP TRP B . n 
B 1 176 CYS 176 203 203 CYS CYS B . n 
B 1 177 GLY 177 204 204 GLY GLY B . n 
B 1 178 MET 178 205 205 MET MET B . n 
B 1 179 THR 179 206 206 THR THR B . n 
B 1 180 SER 180 207 207 SER SER B . n 
B 1 181 GLN 181 208 208 GLN GLN B . n 
B 1 182 GLY 182 209 209 GLY GLY B . n 
B 1 183 TYR 183 210 210 TYR TYR B . n 
B 1 184 TYR 184 211 211 TYR TYR B . n 
B 1 185 LYS 185 212 212 LYS LYS B . n 
B 1 186 ARG 186 213 213 ARG ARG B . n 
B 1 187 THR 187 214 214 THR THR B . n 
B 1 188 PRO 188 215 215 PRO PRO B . n 
B 1 189 ALA 189 216 216 ALA ALA B . n 
B 1 190 TYR 190 217 217 TYR TYR B . n 
B 1 191 ILE 191 218 218 ILE ILE B . n 
B 1 192 PRO 192 219 219 PRO PRO B . n 
B 1 193 ILE 193 220 220 ILE ILE B . n 
B 1 194 ARG 194 221 221 ARG ARG B . n 
B 1 195 LYS 195 222 222 LYS LYS B . n 
B 1 196 ARG 196 223 223 ARG ARG B . n 
B 1 197 ASP 197 224 224 ASP ASP B . n 
B 1 198 ARG 198 225 225 ARG ARG B . n 
B 1 199 ARG 199 226 226 ARG ARG B . n 
B 1 200 GLY 200 227 227 GLY GLY B . n 
B 1 201 CYS 201 228 228 CYS CYS B . n 
B 1 202 PHE 202 229 229 PHE PHE B . n 
B 1 203 ALA 203 230 230 ALA ALA B . n 
B 1 204 VAL 204 231 231 VAL VAL B . n 
B 1 205 PRO 205 232 232 PRO PRO B . n 
B 1 206 MET 206 233 233 MET MET B . n 
B 1 207 VAL 207 234 234 VAL VAL B . n 
B 1 208 HIS 208 235 235 HIS HIS B . n 
B 1 209 SER 209 236 236 SER SER B . n 
B 1 210 THR 210 237 237 THR THR B . n 
B 1 211 PHE 211 238 238 PHE PHE B . n 
B 1 212 LEU 212 239 239 LEU LEU B . n 
B 1 213 ILE 213 240 240 ILE ILE B . n 
B 1 214 ASP 214 241 241 ASP ASP B . n 
B 1 215 LEU 215 242 242 LEU LEU B . n 
B 1 216 ARG 216 243 243 ARG ARG B . n 
B 1 217 LYS 217 244 244 LYS LYS B . n 
B 1 218 ALA 218 245 245 ALA ALA B . n 
B 1 219 ALA 219 246 246 ALA ALA B . n 
B 1 220 SER 220 247 247 SER SER B . n 
B 1 221 ARG 221 248 248 ARG ARG B . n 
B 1 222 ASN 222 249 249 ASN ASN B . n 
B 1 223 LEU 223 250 250 LEU LEU B . n 
B 1 224 ALA 224 251 251 ALA ALA B . n 
B 1 225 PHE 225 252 252 PHE PHE B . n 
B 1 226 TYR 226 253 253 TYR TYR B . n 
B 1 227 PRO 227 254 254 PRO PRO B . n 
B 1 228 PRO 228 255 255 PRO PRO B . n 
B 1 229 HIS 229 256 256 HIS HIS B . n 
B 1 230 PRO 230 257 257 PRO PRO B . n 
B 1 231 ASP 231 258 258 ASP ASP B . n 
B 1 232 TYR 232 259 259 TYR TYR B . n 
B 1 233 THR 233 260 260 THR THR B . n 
B 1 234 TRP 234 261 261 TRP TRP B . n 
B 1 235 SER 235 262 262 SER SER B . n 
B 1 236 PHE 236 263 263 PHE PHE B . n 
B 1 237 ASP 237 264 264 ASP ASP B . n 
B 1 238 ASP 238 265 265 ASP ASP B . n 
B 1 239 ILE 239 266 266 ILE ILE B . n 
B 1 240 ILE 240 267 267 ILE ILE B . n 
B 1 241 VAL 241 268 268 VAL VAL B . n 
B 1 242 PHE 242 269 269 PHE PHE B . n 
B 1 243 ALA 243 270 270 ALA ALA B . n 
B 1 244 PHE 244 271 271 PHE PHE B . n 
B 1 245 SER 245 272 272 SER SER B . n 
B 1 246 CYS 246 273 273 CYS CYS B . n 
B 1 247 LYS 247 274 274 LYS LYS B . n 
B 1 248 GLN 248 275 275 GLN GLN B . n 
B 1 249 ALA 249 276 276 ALA ALA B . n 
B 1 250 GLU 250 277 277 GLU GLU B . n 
B 1 251 VAL 251 278 278 VAL VAL B . n 
B 1 252 GLN 252 279 279 GLN GLN B . n 
B 1 253 MET 253 280 280 MET MET B . n 
B 1 254 TYR 254 281 281 TYR TYR B . n 
B 1 255 VAL 255 282 282 VAL VAL B . n 
B 1 256 CYS 256 283 283 CYS CYS B . n 
B 1 257 ASN 257 284 284 ASN ASN B . n 
B 1 258 LYS 258 285 285 LYS LYS B . n 
B 1 259 GLU 259 286 286 GLU GLU B . n 
B 1 260 GLU 260 287 287 GLU GLU B . n 
B 1 261 TYR 261 288 288 TYR TYR B . n 
B 1 262 GLY 262 289 289 GLY GLY B . n 
B 1 263 PHE 263 290 290 PHE PHE B . n 
B 1 264 LEU 264 291 291 LEU LEU B . n 
B 1 265 PRO 265 292 292 PRO PRO B . n 
B 1 266 VAL 266 293 293 VAL VAL B . n 
B 1 267 PRO 267 294 294 PRO PRO B . n 
B 1 268 LEU 268 295 295 LEU LEU B . n 
B 1 269 ARG 269 296 296 ARG ARG B . n 
B 1 270 ALA 270 297 297 ALA ALA B . n 
B 1 271 HIS 271 298 298 HIS HIS B . n 
B 1 272 SER 272 299 299 SER SER B . n 
B 1 273 THR 273 300 300 THR THR B . n 
B 1 274 LEU 274 301 301 LEU LEU B . n 
B 1 275 GLN 275 302 302 GLN GLN B . n 
B 1 276 ASP 276 303 303 ASP ASP B . n 
B 1 277 GLU 277 304 304 GLU GLU B . n 
B 1 278 ALA 278 305 305 ALA ALA B . n 
B 1 279 GLU 279 306 306 GLU GLU B . n 
B 1 280 SER 280 307 307 SER SER B . n 
B 1 281 PHE 281 308 308 PHE PHE B . n 
B 1 282 MET 282 309 309 MET MET B . n 
B 1 283 HIS 283 310 310 HIS HIS B . n 
B 1 284 VAL 284 311 311 VAL VAL B . n 
B 1 285 GLN 285 312 312 GLN GLN B . n 
B 1 286 LEU 286 313 313 LEU LEU B . n 
B 1 287 GLU 287 314 314 GLU GLU B . n 
B 1 288 VAL 288 315 315 VAL VAL B . n 
B 1 289 MET 289 316 316 MET MET B . n 
B 1 290 VAL 290 317 317 VAL VAL B . n 
B 1 291 LYS 291 318 318 LYS LYS B . n 
B 1 292 HIS 292 319 319 HIS HIS B . n 
B 1 293 PRO 293 320 320 PRO PRO B . n 
B 1 294 PRO 294 321 321 PRO PRO B . n 
B 1 295 ALA 295 322 322 ALA ALA B . n 
B 1 296 GLU 296 323 323 GLU GLU B . n 
B 1 297 PRO 297 324 324 PRO PRO B . n 
B 1 298 SER 298 325 325 SER SER B . n 
B 1 299 ARG 299 326 326 ARG ARG B . n 
B 1 300 PHE 300 327 327 PHE PHE B . n 
B 1 301 ILE 301 328 328 ILE ILE B . n 
B 1 302 SER 302 329 329 SER SER B . n 
B 1 303 ALA 303 330 330 ALA ALA B . n 
B 1 304 PRO 304 331 331 PRO PRO B . n 
B 1 305 THR 305 332 332 THR THR B . n 
B 1 306 LYS 306 333 333 LYS LYS B . n 
B 1 307 THR 307 334 334 THR THR B . n 
B 1 308 PRO 308 335 335 PRO PRO B . n 
B 1 309 ASP 309 336 336 ASP ASP B . n 
B 1 310 LYS 310 337 337 LYS LYS B . n 
B 1 311 MET 311 338 338 MET MET B . n 
B 1 312 GLY 312 339 339 GLY GLY B . n 
B 1 313 PHE 313 340 340 PHE PHE B . n 
B 1 314 ASP 314 341 341 ASP ASP B . n 
B 1 315 GLU 315 342 342 GLU GLU B . n 
B 1 316 VAL 316 343 343 VAL VAL B . n 
B 1 317 PHE 317 344 344 PHE PHE B . n 
B 1 318 MET 318 345 345 MET MET B . n 
B 1 319 ILE 319 346 346 ILE ILE B . n 
B 1 320 ASN 320 347 347 ASN ASN B . n 
B 1 321 LEU 321 348 348 LEU LEU B . n 
B 1 322 ARG 322 349 349 ARG ARG B . n 
B 1 323 ARG 323 350 350 ARG ARG B . n 
B 1 324 ARG 324 351 351 ARG ARG B . n 
B 1 325 GLN 325 352 352 GLN GLN B . n 
B 1 326 ASP 326 353 353 ASP ASP B . n 
B 1 327 ARG 327 354 354 ARG ARG B . n 
B 1 328 ARG 328 355 355 ARG ARG B . n 
B 1 329 GLU 329 356 356 GLU GLU B . n 
B 1 330 ARG 330 357 357 ARG ARG B . n 
B 1 331 MET 331 358 358 MET MET B . n 
B 1 332 LEU 332 359 359 LEU LEU B . n 
B 1 333 ARG 333 360 360 ARG ARG B . n 
B 1 334 ALA 334 361 361 ALA ALA B . n 
B 1 335 LEU 335 362 362 LEU LEU B . n 
B 1 336 GLN 336 363 363 GLN GLN B . n 
B 1 337 ALA 337 364 364 ALA ALA B . n 
B 1 338 GLN 338 365 365 GLN GLN B . n 
B 1 339 GLU 339 366 366 GLU GLU B . n 
B 1 340 ILE 340 367 367 ILE ILE B . n 
B 1 341 GLU 341 368 368 GLU GLU B . n 
B 1 342 CYS 342 369 369 CYS CYS B . n 
B 1 343 ARG 343 370 370 ARG ARG B . n 
B 1 344 LEU 344 371 371 LEU LEU B . n 
B 1 345 VAL 345 372 372 VAL VAL B . n 
B 1 346 GLU 346 373 373 GLU GLU B . n 
B 1 347 ALA 347 374 374 ALA ALA B . n 
B 1 348 VAL 348 375 375 VAL VAL B . n 
B 1 349 ASP 349 376 376 ASP ASP B . n 
B 1 350 GLY 350 377 377 GLY GLY B . n 
B 1 351 LYS 351 378 378 LYS LYS B . n 
B 1 352 ALA 352 379 379 ALA ALA B . n 
B 1 353 MET 353 380 380 MET MET B . n 
B 1 354 ASN 354 381 381 ASN ASN B . n 
B 1 355 THR 355 382 382 THR THR B . n 
B 1 356 SER 356 383 383 SER SER B . n 
B 1 357 GLN 357 384 384 GLN GLN B . n 
B 1 358 VAL 358 385 385 VAL VAL B . n 
B 1 359 GLU 359 386 386 GLU GLU B . n 
B 1 360 ALA 360 387 387 ALA ALA B . n 
B 1 361 LEU 361 388 388 LEU LEU B . n 
B 1 362 GLY 362 389 389 GLY GLY B . n 
B 1 363 ILE 363 390 390 ILE ILE B . n 
B 1 364 GLN 364 391 391 GLN GLN B . n 
B 1 365 MET 365 392 392 MET MET B . n 
B 1 366 LEU 366 393 393 LEU LEU B . n 
B 1 367 PRO 367 394 394 PRO PRO B . n 
B 1 368 GLY 368 395 395 GLY GLY B . n 
B 1 369 TYR 369 396 396 TYR TYR B . n 
B 1 370 ARG 370 397 397 ARG ARG B . n 
B 1 371 ASP 371 398 398 ASP ASP B . n 
B 1 372 PRO 372 399 399 PRO PRO B . n 
B 1 373 TYR 373 400 400 TYR TYR B . n 
B 1 374 HIS 374 401 401 HIS HIS B . n 
B 1 375 GLY 375 402 402 GLY GLY B . n 
B 1 376 ARG 376 403 403 ARG ARG B . n 
B 1 377 PRO 377 404 404 PRO PRO B . n 
B 1 378 LEU 378 405 405 LEU LEU B . n 
B 1 379 THR 379 406 406 THR THR B . n 
B 1 380 LYS 380 407 407 LYS LYS B . n 
B 1 381 GLY 381 408 408 GLY GLY B . n 
B 1 382 GLU 382 409 409 GLU GLU B . n 
B 1 383 LEU 383 410 410 LEU LEU B . n 
B 1 384 GLY 384 411 411 GLY GLY B . n 
B 1 385 CYS 385 412 412 CYS CYS B . n 
B 1 386 PHE 386 413 413 PHE PHE B . n 
B 1 387 LEU 387 414 414 LEU LEU B . n 
B 1 388 SER 388 415 415 SER SER B . n 
B 1 389 HIS 389 416 416 HIS HIS B . n 
B 1 390 TYR 390 417 417 TYR TYR B . n 
B 1 391 ASN 391 418 418 ASN ASN B . n 
B 1 392 ILE 392 419 419 ILE ILE B . n 
B 1 393 TRP 393 420 420 TRP TRP B . n 
B 1 394 LYS 394 421 421 LYS LYS B . n 
B 1 395 GLU 395 422 422 GLU GLU B . n 
B 1 396 VAL 396 423 423 VAL VAL B . n 
B 1 397 VAL 397 424 424 VAL VAL B . n 
B 1 398 ASP 398 425 425 ASP ASP B . n 
B 1 399 ARG 399 426 426 ARG ARG B . n 
B 1 400 GLY 400 427 427 GLY GLY B . n 
B 1 401 LEU 401 428 428 LEU LEU B . n 
B 1 402 GLN 402 429 429 GLN GLN B . n 
B 1 403 LYS 403 430 430 LYS LYS B . n 
B 1 404 SER 404 431 431 SER SER B . n 
B 1 405 LEU 405 432 432 LEU LEU B . n 
B 1 406 VAL 406 433 433 VAL VAL B . n 
B 1 407 PHE 407 434 434 PHE PHE B . n 
B 1 408 GLU 408 435 435 GLU GLU B . n 
B 1 409 ASP 409 436 436 ASP ASP B . n 
B 1 410 ASP 410 437 437 ASP ASP B . n 
B 1 411 LEU 411 438 438 LEU LEU B . n 
B 1 412 ARG 412 439 439 ARG ARG B . n 
B 1 413 PHE 413 440 440 PHE PHE B . n 
B 1 414 GLU 414 441 441 GLU GLU B . n 
B 1 415 ILE 415 442 442 ILE ILE B . n 
B 1 416 PHE 416 443 443 PHE PHE B . n 
B 1 417 PHE 417 444 444 PHE PHE B . n 
B 1 418 LYS 418 445 445 LYS LYS B . n 
B 1 419 ARG 419 446 446 ARG ARG B . n 
B 1 420 ARG 420 447 447 ARG ARG B . n 
B 1 421 LEU 421 448 448 LEU LEU B . n 
B 1 422 MET 422 449 449 MET MET B . n 
B 1 423 ASN 423 450 450 ASN ASN B . n 
B 1 424 LEU 424 451 451 LEU LEU B . n 
B 1 425 MET 425 452 452 MET MET B . n 
B 1 426 ARG 426 453 453 ARG ARG B . n 
B 1 427 ASP 427 454 454 ASP ASP B . n 
B 1 428 VAL 428 455 455 VAL VAL B . n 
B 1 429 GLU 429 456 456 GLU GLU B . n 
B 1 430 ARG 430 457 457 ARG ARG B . n 
B 1 431 GLU 431 458 458 GLU GLU B . n 
B 1 432 GLY 432 459 459 GLY GLY B . n 
B 1 433 LEU 433 460 460 LEU LEU B . n 
B 1 434 ASP 434 461 461 ASP ASP B . n 
B 1 435 TRP 435 462 462 TRP TRP B . n 
B 1 436 ASP 436 463 463 ASP ASP B . n 
B 1 437 LEU 437 464 464 LEU LEU B . n 
B 1 438 ILE 438 465 465 ILE ILE B . n 
B 1 439 TYR 439 466 466 TYR TYR B . n 
B 1 440 VAL 440 467 467 VAL VAL B . n 
B 1 441 GLY 441 468 468 GLY GLY B . n 
B 1 442 ARG 442 469 469 ARG ARG B . n 
B 1 443 LYS 443 470 470 LYS LYS B . n 
B 1 444 ARG 444 471 471 ARG ARG B . n 
B 1 445 MET 445 472 472 MET MET B . n 
B 1 446 GLN 446 473 473 GLN GLN B . n 
B 1 447 VAL 447 474 474 VAL VAL B . n 
B 1 448 GLU 448 475 475 GLU GLU B . n 
B 1 449 HIS 449 476 476 HIS HIS B . n 
B 1 450 PRO 450 477 477 PRO PRO B . n 
B 1 451 GLU 451 478 478 GLU GLU B . n 
B 1 452 LYS 452 479 479 LYS LYS B . n 
B 1 453 ALA 453 480 480 ALA ALA B . n 
B 1 454 VAL 454 481 481 VAL VAL B . n 
B 1 455 PRO 455 482 482 PRO PRO B . n 
B 1 456 ARG 456 483 483 ARG ARG B . n 
B 1 457 VAL 457 484 484 VAL VAL B . n 
B 1 458 ARG 458 485 485 ARG ARG B . n 
B 1 459 ASN 459 486 486 ASN ASN B . n 
B 1 460 LEU 460 487 487 LEU LEU B . n 
B 1 461 VAL 461 488 488 VAL VAL B . n 
B 1 462 GLU 462 489 489 GLU GLU B . n 
B 1 463 ALA 463 490 490 ALA ALA B . n 
B 1 464 ASP 464 491 491 ASP ASP B . n 
B 1 465 TYR 465 492 492 TYR TYR B . n 
B 1 466 SER 466 493 493 SER SER B . n 
B 1 467 TYR 467 494 494 TYR TYR B . n 
B 1 468 TRP 468 495 495 TRP TRP B . n 
B 1 469 THR 469 496 496 THR THR B . n 
B 1 470 LEU 470 497 497 LEU LEU B . n 
B 1 471 ALA 471 498 498 ALA ALA B . n 
B 1 472 TYR 472 499 499 TYR TYR B . n 
B 1 473 VAL 473 500 500 VAL VAL B . n 
B 1 474 ILE 474 501 501 ILE ILE B . n 
B 1 475 SER 475 502 502 SER SER B . n 
B 1 476 LEU 476 503 503 LEU LEU B . n 
B 1 477 GLN 477 504 504 GLN GLN B . n 
B 1 478 GLY 478 505 505 GLY GLY B . n 
B 1 479 ALA 479 506 506 ALA ALA B . n 
B 1 480 ARG 480 507 507 ARG ARG B . n 
B 1 481 LYS 481 508 508 LYS LYS B . n 
B 1 482 LEU 482 509 509 LEU LEU B . n 
B 1 483 LEU 483 510 510 LEU LEU B . n 
B 1 484 ALA 484 511 511 ALA ALA B . n 
B 1 485 ALA 485 512 512 ALA ALA B . n 
B 1 486 GLU 486 513 513 GLU GLU B . n 
B 1 487 PRO 487 514 514 PRO PRO B . n 
B 1 488 LEU 488 515 515 LEU LEU B . n 
B 1 489 SER 489 516 516 SER SER B . n 
B 1 490 LYS 490 517 517 LYS LYS B . n 
B 1 491 MET 491 518 518 MET MET B . n 
B 1 492 LEU 492 519 519 LEU LEU B . n 
B 1 493 PRO 493 520 520 PRO PRO B . n 
B 1 494 VAL 494 521 521 VAL VAL B . n 
B 1 495 ASP 495 522 522 ASP ASP B . n 
B 1 496 GLU 496 523 523 GLU GLU B . n 
B 1 497 PHE 497 524 524 PHE PHE B . n 
B 1 498 LEU 498 525 525 LEU LEU B . n 
B 1 499 PRO 499 526 526 PRO PRO B . n 
B 1 500 VAL 500 527 527 VAL VAL B . n 
B 1 501 MET 501 528 528 MET MET B . n 
B 1 502 PHE 502 529 529 PHE PHE B . n 
B 1 503 ASP 503 530 530 ASP ASP B . n 
B 1 504 LYS 504 531 531 LYS LYS B . n 
B 1 505 HIS 505 532 532 HIS HIS B . n 
B 1 506 PRO 506 533 533 PRO PRO B . n 
B 1 507 VAL 507 534 534 VAL VAL B . n 
B 1 508 SER 508 535 535 SER SER B . n 
B 1 509 GLU 509 536 536 GLU GLU B . n 
B 1 510 TYR 510 537 537 TYR TYR B . n 
B 1 511 LYS 511 538 538 LYS LYS B . n 
B 1 512 ALA 512 539 539 ALA ALA B . n 
B 1 513 HIS 513 540 540 HIS HIS B . n 
B 1 514 PHE 514 541 541 PHE PHE B . n 
B 1 515 SER 515 542 542 SER SER B . n 
B 1 516 LEU 516 543 543 LEU LEU B . n 
B 1 517 ARG 517 544 544 ARG ARG B . n 
B 1 518 ASN 518 545 545 ASN ASN B . n 
B 1 519 LEU 519 546 546 LEU LEU B . n 
B 1 520 HIS 520 547 547 HIS HIS B . n 
B 1 521 ALA 521 548 548 ALA ALA B . n 
B 1 522 PHE 522 549 549 PHE PHE B . n 
B 1 523 SER 523 550 550 SER SER B . n 
B 1 524 VAL 524 551 551 VAL VAL B . n 
B 1 525 GLU 525 552 552 GLU GLU B . n 
B 1 526 PRO 526 553 553 PRO PRO B . n 
B 1 527 LEU 527 554 554 LEU LEU B . n 
B 1 528 LEU 528 555 555 LEU LEU B . n 
B 1 529 ILE 529 556 556 ILE ILE B . n 
B 1 530 TYR 530 557 557 TYR TYR B . n 
B 1 531 PRO 531 558 558 PRO PRO B . n 
B 1 532 THR 532 559 559 THR THR B . n 
B 1 533 HIS 533 560 560 HIS HIS B . n 
B 1 534 TYR 534 561 561 TYR TYR B . n 
B 1 535 THR 535 562 562 THR THR B . n 
B 1 536 GLY 536 563 ?   ?   ?   B . n 
B 1 537 ASP 537 564 ?   ?   ?   B . n 
B 1 538 ASP 538 565 ?   ?   ?   B . n 
B 1 539 GLY 539 566 ?   ?   ?   B . n 
B 1 540 TYR 540 567 ?   ?   ?   B . n 
B 1 541 VAL 541 568 ?   ?   ?   B . n 
B 1 542 SER 542 569 ?   ?   ?   B . n 
B 1 543 ASP 543 570 ?   ?   ?   B . n 
B 1 544 THR 544 571 ?   ?   ?   B . n 
B 1 545 GLU 545 572 ?   ?   ?   B . n 
B 1 546 THR 546 573 ?   ?   ?   B . n 
B 1 547 SER 547 574 ?   ?   ?   B . n 
B 1 548 VAL 548 575 ?   ?   ?   B . n 
B 1 549 VAL 549 576 ?   ?   ?   B . n 
B 1 550 TRP 550 577 ?   ?   ?   B . n 
B 1 551 ASN 551 578 ?   ?   ?   B . n 
B 1 552 ASN 552 579 ?   ?   ?   B . n 
B 1 553 GLU 553 580 ?   ?   ?   B . n 
B 1 554 HIS 554 581 ?   ?   ?   B . n 
B 1 555 VAL 555 582 ?   ?   ?   B . n 
B 1 556 LYS 556 583 ?   ?   ?   B . n 
B 1 557 THR 557 584 ?   ?   ?   B . n 
B 1 558 ASP 558 585 ?   ?   ?   B . n 
B 1 559 TRP 559 586 ?   ?   ?   B . n 
B 1 560 ASP 560 587 ?   ?   ?   B . n 
B 1 561 ARG 561 588 ?   ?   ?   B . n 
B 1 562 ALA 562 589 ?   ?   ?   B . n 
B 1 563 LYS 563 590 ?   ?   ?   B . n 
B 1 564 SER 564 591 ?   ?   ?   B . n 
B 1 565 GLN 565 592 ?   ?   ?   B . n 
B 1 566 LYS 566 593 ?   ?   ?   B . n 
B 1 567 MET 567 594 ?   ?   ?   B . n 
B 1 568 ARG 568 595 ?   ?   ?   B . n 
B 1 569 GLU 569 596 ?   ?   ?   B . n 
B 1 570 GLN 570 597 ?   ?   ?   B . n 
B 1 571 GLN 571 598 ?   ?   ?   B . n 
B 1 572 ALA 572 599 ?   ?   ?   B . n 
B 1 573 LEU 573 600 ?   ?   ?   B . n 
B 1 574 SER 574 601 ?   ?   ?   B . n 
B 1 575 ARG 575 602 ?   ?   ?   B . n 
B 1 576 GLU 576 603 ?   ?   ?   B . n 
B 1 577 ALA 577 604 ?   ?   ?   B . n 
B 1 578 LYS 578 605 ?   ?   ?   B . n 
B 1 579 ASN 579 606 ?   ?   ?   B . n 
B 1 580 SER 580 607 ?   ?   ?   B . n 
B 1 581 ASP 581 608 ?   ?   ?   B . n 
B 1 582 VAL 582 609 ?   ?   ?   B . n 
B 1 583 LEU 583 610 ?   ?   ?   B . n 
B 1 584 GLN 584 611 ?   ?   ?   B . n 
B 1 585 SER 585 612 ?   ?   ?   B . n 
B 1 586 PRO 586 613 ?   ?   ?   B . n 
B 1 587 LEU 587 614 ?   ?   ?   B . n 
B 1 588 ASP 588 615 ?   ?   ?   B . n 
B 1 589 SER 589 616 ?   ?   ?   B . n 
B 1 590 ALA 590 617 ?   ?   ?   B . n 
B 1 591 ALA 591 618 ?   ?   ?   B . n 
B 1 592 ALA 592 619 ?   ?   ?   B . n 
B 1 593 ALA 593 620 ?   ?   ?   B . n 
B 1 594 ALA 594 621 ?   ?   ?   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 CA  ? ? CA  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GDU ? ? GDU ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 UDP ? ? UDP ? ? '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 GDU 1  701 600 GDU GDU A . 
D 3 UDP 1  702 601 UDP UDP A . 
E 4 MN  1  703 611 MN  MN  A . 
F 5 MES 1  704 612 MES MES A . 
G 5 MES 1  705 613 MES MES A . 
H 6 CL  1  706 2   CL  CL  A . 
I 6 CL  1  707 3   CL  CL  A . 
J 6 CL  1  708 7   CL  CL  A . 
K 7 CA  1  709 1   CA  CA  A . 
L 2 GDU 1  701 600 GDU GDU B . 
M 6 CL  1  702 4   CL  CL  B . 
N 6 CL  1  703 5   CL  CL  B . 
O 6 CL  1  704 6   CL  CL  B . 
P 8 NA  1  705 1   NA  NA  B . 
Q 7 CA  1  706 2   CA  CA  B . 
R 9 HOH 1  801 65  HOH HOH A . 
R 9 HOH 2  802 113 HOH HOH A . 
R 9 HOH 3  803 62  HOH HOH A . 
R 9 HOH 4  804 29  HOH HOH A . 
R 9 HOH 5  805 19  HOH HOH A . 
R 9 HOH 6  806 23  HOH HOH A . 
R 9 HOH 7  807 37  HOH HOH A . 
R 9 HOH 8  808 93  HOH HOH A . 
R 9 HOH 9  809 67  HOH HOH A . 
R 9 HOH 10 810 9   HOH HOH A . 
R 9 HOH 11 811 17  HOH HOH A . 
R 9 HOH 12 812 122 HOH HOH A . 
R 9 HOH 13 813 112 HOH HOH A . 
R 9 HOH 14 814 127 HOH HOH A . 
R 9 HOH 15 815 121 HOH HOH A . 
R 9 HOH 16 816 54  HOH HOH A . 
R 9 HOH 17 817 90  HOH HOH A . 
R 9 HOH 18 818 31  HOH HOH A . 
R 9 HOH 19 819 107 HOH HOH A . 
R 9 HOH 20 820 74  HOH HOH A . 
R 9 HOH 21 821 2   HOH HOH A . 
R 9 HOH 22 822 6   HOH HOH A . 
R 9 HOH 23 823 52  HOH HOH A . 
R 9 HOH 24 824 77  HOH HOH A . 
R 9 HOH 25 825 71  HOH HOH A . 
R 9 HOH 26 826 120 HOH HOH A . 
R 9 HOH 27 827 125 HOH HOH A . 
R 9 HOH 28 828 73  HOH HOH A . 
R 9 HOH 29 829 22  HOH HOH A . 
R 9 HOH 30 830 118 HOH HOH A . 
R 9 HOH 31 831 102 HOH HOH A . 
R 9 HOH 32 832 103 HOH HOH A . 
R 9 HOH 33 833 26  HOH HOH A . 
R 9 HOH 34 834 41  HOH HOH A . 
R 9 HOH 35 835 72  HOH HOH A . 
R 9 HOH 36 836 63  HOH HOH A . 
R 9 HOH 37 837 140 HOH HOH A . 
R 9 HOH 38 838 44  HOH HOH A . 
R 9 HOH 39 839 13  HOH HOH A . 
R 9 HOH 40 840 76  HOH HOH A . 
R 9 HOH 41 841 126 HOH HOH A . 
R 9 HOH 42 842 34  HOH HOH A . 
R 9 HOH 43 843 56  HOH HOH A . 
R 9 HOH 44 844 105 HOH HOH A . 
R 9 HOH 45 845 45  HOH HOH A . 
R 9 HOH 46 846 95  HOH HOH A . 
R 9 HOH 47 847 48  HOH HOH A . 
R 9 HOH 48 848 141 HOH HOH A . 
R 9 HOH 49 849 89  HOH HOH A . 
R 9 HOH 50 850 5   HOH HOH A . 
R 9 HOH 51 851 86  HOH HOH A . 
R 9 HOH 52 852 49  HOH HOH A . 
R 9 HOH 53 853 101 HOH HOH A . 
R 9 HOH 54 854 96  HOH HOH A . 
R 9 HOH 55 855 55  HOH HOH A . 
R 9 HOH 56 856 79  HOH HOH A . 
R 9 HOH 57 857 64  HOH HOH A . 
R 9 HOH 58 858 124 HOH HOH A . 
R 9 HOH 59 859 85  HOH HOH A . 
R 9 HOH 60 860 119 HOH HOH A . 
R 9 HOH 61 861 104 HOH HOH A . 
R 9 HOH 62 862 4   HOH HOH A . 
R 9 HOH 63 863 114 HOH HOH A . 
R 9 HOH 64 864 91  HOH HOH A . 
R 9 HOH 65 865 11  HOH HOH A . 
R 9 HOH 66 866 128 HOH HOH A . 
S 9 HOH 1  801 132 HOH HOH B . 
S 9 HOH 2  802 28  HOH HOH B . 
S 9 HOH 3  803 106 HOH HOH B . 
S 9 HOH 4  804 25  HOH HOH B . 
S 9 HOH 5  805 66  HOH HOH B . 
S 9 HOH 6  806 142 HOH HOH B . 
S 9 HOH 7  807 51  HOH HOH B . 
S 9 HOH 8  808 27  HOH HOH B . 
S 9 HOH 9  809 80  HOH HOH B . 
S 9 HOH 10 810 82  HOH HOH B . 
S 9 HOH 11 811 78  HOH HOH B . 
S 9 HOH 12 812 40  HOH HOH B . 
S 9 HOH 13 813 20  HOH HOH B . 
S 9 HOH 14 814 7   HOH HOH B . 
S 9 HOH 15 815 8   HOH HOH B . 
S 9 HOH 16 816 46  HOH HOH B . 
S 9 HOH 17 817 115 HOH HOH B . 
S 9 HOH 18 818 61  HOH HOH B . 
S 9 HOH 19 819 35  HOH HOH B . 
S 9 HOH 20 820 24  HOH HOH B . 
S 9 HOH 21 821 60  HOH HOH B . 
S 9 HOH 22 822 84  HOH HOH B . 
S 9 HOH 23 823 70  HOH HOH B . 
S 9 HOH 24 824 131 HOH HOH B . 
S 9 HOH 25 825 14  HOH HOH B . 
S 9 HOH 26 826 30  HOH HOH B . 
S 9 HOH 27 827 18  HOH HOH B . 
S 9 HOH 28 828 130 HOH HOH B . 
S 9 HOH 29 829 36  HOH HOH B . 
S 9 HOH 30 830 53  HOH HOH B . 
S 9 HOH 31 831 1   HOH HOH B . 
S 9 HOH 32 832 16  HOH HOH B . 
S 9 HOH 33 833 94  HOH HOH B . 
S 9 HOH 34 834 123 HOH HOH B . 
S 9 HOH 35 835 38  HOH HOH B . 
S 9 HOH 36 836 39  HOH HOH B . 
S 9 HOH 37 837 69  HOH HOH B . 
S 9 HOH 38 838 75  HOH HOH B . 
S 9 HOH 39 839 43  HOH HOH B . 
S 9 HOH 40 840 10  HOH HOH B . 
S 9 HOH 41 841 33  HOH HOH B . 
S 9 HOH 42 842 143 HOH HOH B . 
S 9 HOH 43 843 12  HOH HOH B . 
S 9 HOH 44 844 59  HOH HOH B . 
S 9 HOH 45 845 81  HOH HOH B . 
S 9 HOH 46 846 138 HOH HOH B . 
S 9 HOH 47 847 87  HOH HOH B . 
S 9 HOH 48 848 32  HOH HOH B . 
S 9 HOH 49 849 47  HOH HOH B . 
S 9 HOH 50 850 42  HOH HOH B . 
S 9 HOH 51 851 3   HOH HOH B . 
S 9 HOH 52 852 50  HOH HOH B . 
S 9 HOH 53 853 15  HOH HOH B . 
S 9 HOH 54 854 83  HOH HOH B . 
S 9 HOH 55 855 129 HOH HOH B . 
S 9 HOH 56 856 139 HOH HOH B . 
S 9 HOH 57 857 92  HOH HOH B . 
S 9 HOH 58 858 137 HOH HOH B . 
S 9 HOH 59 859 100 HOH HOH B . 
S 9 HOH 60 860 116 HOH HOH B . 
S 9 HOH 61 861 135 HOH HOH B . 
S 9 HOH 62 862 99  HOH HOH B . 
S 9 HOH 63 863 21  HOH HOH B . 
S 9 HOH 64 864 88  HOH HOH B . 
S 9 HOH 65 865 117 HOH HOH B . 
S 9 HOH 66 866 97  HOH HOH B . 
S 9 HOH 67 867 68  HOH HOH B . 
S 9 HOH 68 868 57  HOH HOH B . 
S 9 HOH 69 869 98  HOH HOH B . 
S 9 HOH 70 870 136 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_4459: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EVJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     220.855 
_cell.length_a_esd                 ? 
_cell.length_b                     220.855 
_cell.length_b_esd                 ? 
_cell.length_c                     220.855 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         9EVJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                197 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 3' 
_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                   9EVJ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    
'8% poly-ethylene-glycol (PEG) MW 4000, 100 mM 2-(N-morpholino)ethanesulfonic acid (MES)/NaOH, 20% glycerol, pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-10-22 
_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   0.9999 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EVJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.7 
_reflns.d_resolution_low                               49.38 
_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                                     49018 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.058 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.11 
_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                                    2.7 
_reflns_shell.d_res_low                                     2.79 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4444 
_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                               5.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.920 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.395 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.251 
_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                                 9EVJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.70 
_refine.ls_d_res_low                             49.38 
_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                     49006 
_refine.ls_number_reflns_R_free                  2445 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1873 
_refine.ls_R_factor_R_free                       0.2225 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1855 
_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                 24.58 
_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                            0.39 
_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                       2.70 
_refine_hist.d_res_low                        49.38 
_refine_hist.number_atoms_solvent             136 
_refine_hist.number_atoms_total               8923 
_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        8562 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         225 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? 9017  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.532  ? 12253 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.927 ? 3373  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 1311  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 1564  ? 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' 2.70 2.76  . . 118 2709 99.00  . . . . 0.3516 . . . . . . . . . . . 0.4403 
'X-RAY DIFFRACTION' 2.76 2.81  . . 134 2717 100.00 . . . . 0.3237 . . . . . . . . . . . 0.3359 
'X-RAY DIFFRACTION' 2.82 2.88  . . 133 2719 100.00 . . . . 0.2709 . . . . . . . . . . . 0.2839 
'X-RAY DIFFRACTION' 2.88 2.95  . . 161 2694 100.00 . . . . 0.2582 . . . . . . . . . . . 0.3207 
'X-RAY DIFFRACTION' 2.95 3.03  . . 145 2750 100.00 . . . . 0.2463 . . . . . . . . . . . 0.2840 
'X-RAY DIFFRACTION' 3.03 3.12  . . 147 2713 100.00 . . . . 0.2324 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 3.12 3.22  . . 166 2676 100.00 . . . . 0.2329 . . . . . . . . . . . 0.3277 
'X-RAY DIFFRACTION' 3.22 3.34  . . 136 2743 100.00 . . . . 0.2283 . . . . . . . . . . . 0.2526 
'X-RAY DIFFRACTION' 3.34 3.47  . . 154 2733 100.00 . . . . 0.2298 . . . . . . . . . . . 0.2950 
'X-RAY DIFFRACTION' 3.47 3.63  . . 144 2741 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2108 
'X-RAY DIFFRACTION' 3.63 3.82  . . 157 2727 100.00 . . . . 0.1730 . . . . . . . . . . . 0.2315 
'X-RAY DIFFRACTION' 3.82 4.06  . . 139 2729 100.00 . . . . 0.1647 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 4.06 4.37  . . 145 2739 100.00 . . . . 0.1572 . . . . . . . . . . . 0.1874 
'X-RAY DIFFRACTION' 4.37 4.81  . . 141 2776 100.00 . . . . 0.1413 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 4.81 5.51  . . 150 2738 100.00 . . . . 0.1561 . . . . . . . . . . . 0.1956 
'X-RAY DIFFRACTION' 5.51 6.94  . . 123 2816 100.00 . . . . 0.1734 . . . . . . . . . . . 0.2051 
'X-RAY DIFFRACTION' 6.94 49.38 . . 152 2841 100.00 . . . . 0.1495 . . . . . . . . . . . 0.1706 
# 
_struct.entry_id                     9EVJ 
_struct.title                        
'Crystal Structure of human Collagen Hydroxylysine Galactosyltransferase GLT25D1/COLGALT1: complex with Mn2+ and UDP-Gal' 
_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        9EVJ 
_struct_keywords.text            
'Collagen Biosynthesis; Extracellular Matrix; Post-translational modifications, Glycosyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 6 ? 
I N N 6 ? 
J N N 6 ? 
K N N 7 ? 
L N N 2 ? 
M N N 6 ? 
N N N 6 ? 
O N N 6 ? 
P N N 8 ? 
Q N N 7 ? 
R N N 9 ? 
S N N 9 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    GT251_HUMAN 
_struct_ref.pdbx_db_accession          Q8NBJ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVAVK
SLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTVVA
PMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVF
AFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMINLR
RRQDRRERMLRALQAQEIECRLVEAVDGKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRGLQ
KSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGARKL
LAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWDRA
KSQKMREQQALSREAKNSDVLQSPLDSAA
;
_struct_ref.pdbx_align_begin           30 
# 
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 9EVJ A 3 ? 591 ? Q8NBJ5 30 ? 618 ? 30 618 
2 1 9EVJ B 3 ? 591 ? Q8NBJ5 30 ? 618 ? 30 618 
# 
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 9EVJ GLY A 1   ? UNP Q8NBJ5 ? ? 'expression tag' 28  1  
1 9EVJ SER A 2   ? UNP Q8NBJ5 ? ? 'expression tag' 29  2  
1 9EVJ ALA A 592 ? UNP Q8NBJ5 ? ? 'expression tag' 619 3  
1 9EVJ ALA A 593 ? UNP Q8NBJ5 ? ? 'expression tag' 620 4  
1 9EVJ ALA A 594 ? UNP Q8NBJ5 ? ? 'expression tag' 621 5  
2 9EVJ GLY B 1   ? UNP Q8NBJ5 ? ? 'expression tag' 28  6  
2 9EVJ SER B 2   ? UNP Q8NBJ5 ? ? 'expression tag' 29  7  
2 9EVJ ALA B 592 ? UNP Q8NBJ5 ? ? 'expression tag' 619 8  
2 9EVJ ALA B 593 ? UNP Q8NBJ5 ? ? 'expression tag' 620 9  
2 9EVJ ALA B 594 ? UNP Q8NBJ5 ? ? 'expression tag' 621 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7230  ? 
1 MORE         -114  ? 
1 'SSA (A^2)'  45330 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 SAXS               'SEC-SAXS confirms elongated dimeric assembly' 
2 1 'light scattering' 'SEC-MALS confirms dimers'                     
3 1 microscopy         'Mass Photometry confirms dimers'              
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 39  ? ARG A 49  ? ALA A 66  ARG A 76  1 ? 11 
HELX_P HELX_P2  AA2 PRO A 53  ? GLU A 55  ? PRO A 80  GLU A 82  5 ? 3  
HELX_P HELX_P3  AA3 ASN A 69  ? LYS A 82  ? ASN A 96  LYS A 109 1 ? 14 
HELX_P HELX_P4  AA4 SER A 83  ? TYR A 85  ? SER A 110 TYR A 112 5 ? 3  
HELX_P HELX_P5  AA5 SER A 109 ? MET A 130 ? SER A 136 MET A 157 1 ? 22 
HELX_P HELX_P6  AA6 ASP A 148 ? GLU A 156 ? ASP A 175 GLU A 183 1 ? 9  
HELX_P HELX_P7  AA7 ALA A 189 ? LYS A 195 ? ALA A 216 LYS A 222 1 ? 7  
HELX_P HELX_P8  AA8 LYS A 217 ? LEU A 223 ? LYS A 244 LEU A 250 5 ? 7  
HELX_P HELX_P9  AA9 ASP A 237 ? ALA A 249 ? ASP A 264 ALA A 276 1 ? 13 
HELX_P HELX_P10 AB1 THR A 273 ? HIS A 292 ? THR A 300 HIS A 319 1 ? 20 
HELX_P HELX_P11 AB2 ARG A 324 ? GLN A 338 ? ARG A 351 GLN A 365 1 ? 15 
HELX_P HELX_P12 AB3 ASN A 354 ? LEU A 361 ? ASN A 381 LEU A 388 1 ? 8  
HELX_P HELX_P13 AB4 THR A 379 ? GLY A 400 ? THR A 406 GLY A 427 1 ? 22 
HELX_P HELX_P14 AB5 PHE A 416 ? GLY A 432 ? PHE A 443 GLY A 459 1 ? 17 
HELX_P HELX_P15 AB6 LEU A 476 ? GLU A 486 ? LEU A 503 GLU A 513 1 ? 11 
HELX_P HELX_P16 AB7 PRO A 487 ? MET A 491 ? PRO A 514 MET A 518 5 ? 5  
HELX_P HELX_P17 AB8 PRO A 493 ? PHE A 502 ? PRO A 520 PHE A 529 1 ? 10 
HELX_P HELX_P18 AB9 VAL A 507 ? HIS A 513 ? VAL A 534 HIS A 540 1 ? 7  
HELX_P HELX_P19 AC1 ALA B 39  ? ARG B 49  ? ALA B 66  ARG B 76  1 ? 11 
HELX_P HELX_P20 AC2 PRO B 53  ? GLU B 55  ? PRO B 80  GLU B 82  5 ? 3  
HELX_P HELX_P21 AC3 ASN B 69  ? LYS B 82  ? ASN B 96  LYS B 109 1 ? 14 
HELX_P HELX_P22 AC4 SER B 83  ? TYR B 85  ? SER B 110 TYR B 112 5 ? 3  
HELX_P HELX_P23 AC5 SER B 109 ? MET B 130 ? SER B 136 MET B 157 1 ? 22 
HELX_P HELX_P24 AC6 ASP B 148 ? GLU B 156 ? ASP B 175 GLU B 183 1 ? 9  
HELX_P HELX_P25 AC7 ALA B 189 ? LYS B 195 ? ALA B 216 LYS B 222 1 ? 7  
HELX_P HELX_P26 AC8 LYS B 217 ? LEU B 223 ? LYS B 244 LEU B 250 5 ? 7  
HELX_P HELX_P27 AC9 ASP B 237 ? ALA B 249 ? ASP B 264 ALA B 276 1 ? 13 
HELX_P HELX_P28 AD1 THR B 273 ? HIS B 292 ? THR B 300 HIS B 319 1 ? 20 
HELX_P HELX_P29 AD2 ARG B 324 ? GLN B 338 ? ARG B 351 GLN B 365 1 ? 15 
HELX_P HELX_P30 AD3 ASP B 349 ? MET B 353 ? ASP B 376 MET B 380 5 ? 5  
HELX_P HELX_P31 AD4 ASN B 354 ? LEU B 361 ? ASN B 381 LEU B 388 1 ? 8  
HELX_P HELX_P32 AD5 THR B 379 ? GLY B 400 ? THR B 406 GLY B 427 1 ? 22 
HELX_P HELX_P33 AD6 PHE B 416 ? GLY B 432 ? PHE B 443 GLY B 459 1 ? 17 
HELX_P HELX_P34 AD7 LEU B 476 ? ALA B 485 ? LEU B 503 ALA B 512 1 ? 10 
HELX_P HELX_P35 AD8 PRO B 493 ? PHE B 502 ? PRO B 520 PHE B 529 1 ? 10 
HELX_P HELX_P36 AD9 VAL B 507 ? HIS B 513 ? VAL B 534 HIS B 540 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 201 SG  ? ? ? 1_555 A CYS 256 SG ? ? A CYS 228 A CYS 283 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf2  disulf ? ? B CYS 201 SG  ? ? ? 1_555 B CYS 256 SG ? ? B CYS 228 B CYS 283 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc1  metalc ? ? A ASP 141 OD1 ? ? ? 1_555 K CA  .   CA ? ? A ASP 168 A CA  709 1_555 ? ? ? ? ? ? ? 2.707 ? ? 
metalc2  metalc ? ? A ASP 141 OD2 ? ? ? 1_555 K CA  .   CA ? ? A ASP 168 A CA  709 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
metalc3  metalc ? ? A ASP 410 OD2 ? ? ? 1_555 E MN  .   MN ? ? A ASP 437 A MN  703 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc4  metalc ? ? C GDU .   O1A ? ? ? 1_555 K CA  .   CA ? ? A GDU 701 A CA  709 1_555 ? ? ? ? ? ? ? 2.536 ? ? 
metalc5  metalc ? ? C GDU .   O3A ? ? ? 1_555 K CA  .   CA ? ? A GDU 701 A CA  709 1_555 ? ? ? ? ? ? ? 3.173 ? ? 
metalc6  metalc ? ? C GDU .   O1B ? ? ? 1_555 K CA  .   CA ? ? A GDU 701 A CA  709 1_555 ? ? ? ? ? ? ? 2.187 ? ? 
metalc7  metalc ? ? D UDP .   O1A ? ? ? 1_555 E MN  .   MN ? ? A UDP 702 A MN  703 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc8  metalc ? ? D UDP .   O2B ? ? ? 1_555 E MN  .   MN ? ? A UDP 702 A MN  703 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc9  metalc ? ? K CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  709 A HOH 817 1_555 ? ? ? ? ? ? ? 2.850 ? ? 
metalc10 metalc ? ? K CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  709 A HOH 837 1_555 ? ? ? ? ? ? ? 2.709 ? ? 
metalc11 metalc ? ? K CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  709 A HOH 848 1_555 ? ? ? ? ? ? ? 2.596 ? ? 
metalc12 metalc ? ? B ASP 141 OD2 ? ? ? 1_555 Q CA  .   CA ? ? B ASP 168 B CA  706 1_555 ? ? ? ? ? ? ? 2.231 ? ? 
metalc13 metalc ? ? L GDU .   O1A ? ? ? 1_555 Q CA  .   CA ? ? B GDU 701 B CA  706 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc14 metalc ? ? L GDU .   O2B ? ? ? 1_555 Q CA  .   CA ? ? B GDU 701 B CA  706 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc15 metalc ? ? Q CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  706 B HOH 806 1_555 ? ? ? ? ? ? ? 2.775 ? ? 
metalc16 metalc ? ? Q CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  706 B HOH 842 1_555 ? ? ? ? ? ? ? 2.389 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 OD2 ? A ASP 141 ? A ASP 168 ? 1_555 51.7  ? 
2  OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O1A ? C GDU .   ? A GDU 701 ? 1_555 91.6  ? 
3  OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O1A ? C GDU .   ? A GDU 701 ? 1_555 89.8  ? 
4  OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O3A ? C GDU .   ? A GDU 701 ? 1_555 132.0 ? 
5  OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O3A ? C GDU .   ? A GDU 701 ? 1_555 139.3 ? 
6  O1A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O3A ? C GDU .   ? A GDU 701 ? 1_555 52.6  ? 
7  OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O1B ? C GDU .   ? A GDU 701 ? 1_555 172.2 ? 
8  OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O1B ? C GDU .   ? A GDU 701 ? 1_555 127.6 ? 
9  O1A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O1B ? C GDU .   ? A GDU 701 ? 1_555 96.2  ? 
10 O3A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O1B ? C GDU .   ? A GDU 701 ? 1_555 54.6  ? 
11 OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 817 ? 1_555 120.2 ? 
12 OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 817 ? 1_555 69.4  ? 
13 O1A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 817 ? 1_555 98.3  ? 
14 O3A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 817 ? 1_555 98.2  ? 
15 O1B ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 817 ? 1_555 58.2  ? 
16 OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 837 ? 1_555 88.1  ? 
17 OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 837 ? 1_555 96.2  ? 
18 O1A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 837 ? 1_555 172.1 ? 
19 O3A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 837 ? 1_555 122.9 ? 
20 O1B ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 837 ? 1_555 84.3  ? 
21 O   ? R HOH .   ? A HOH 817 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 837 ? 1_555 88.6  ? 
22 OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 848 ? 1_555 87.0  ? 
23 OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 848 ? 1_555 135.3 ? 
24 O1A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 848 ? 1_555 110.0 ? 
25 O3A ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 848 ? 1_555 79.0  ? 
26 O1B ? C GDU .   ? A GDU 701 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 848 ? 1_555 90.8  ? 
27 O   ? R HOH .   ? A HOH 817 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 848 ? 1_555 140.4 ? 
28 O   ? R HOH .   ? A HOH 837 ? 1_555 CA ? K CA . ? A CA 709 ? 1_555 O   ? R HOH .   ? A HOH 848 ? 1_555 62.1  ? 
29 OD2 ? A ASP 410 ? A ASP 437 ? 1_555 MN ? E MN . ? A MN 703 ? 1_555 O1A ? D UDP .   ? A UDP 702 ? 1_555 72.5  ? 
30 OD2 ? A ASP 410 ? A ASP 437 ? 1_555 MN ? E MN . ? A MN 703 ? 1_555 O2B ? D UDP .   ? A UDP 702 ? 1_555 142.5 ? 
31 O1A ? D UDP .   ? A UDP 702 ? 1_555 MN ? E MN . ? A MN 703 ? 1_555 O2B ? D UDP .   ? A UDP 702 ? 1_555 70.2  ? 
32 OD2 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O1A ? L GDU .   ? B GDU 701 ? 1_555 80.8  ? 
33 OD2 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O2B ? L GDU .   ? B GDU 701 ? 1_555 126.6 ? 
34 O1A ? L GDU .   ? B GDU 701 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O2B ? L GDU .   ? B GDU 701 ? 1_555 73.3  ? 
35 OD2 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O   ? S HOH .   ? B HOH 806 ? 1_555 55.7  ? 
36 O1A ? L GDU .   ? B GDU 701 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O   ? S HOH .   ? B HOH 806 ? 1_555 70.8  ? 
37 O2B ? L GDU .   ? B GDU 701 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O   ? S HOH .   ? B HOH 806 ? 1_555 71.8  ? 
38 OD2 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O   ? S HOH .   ? B HOH 842 ? 1_555 76.0  ? 
39 O1A ? L GDU .   ? B GDU 701 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O   ? S HOH .   ? B HOH 842 ? 1_555 146.1 ? 
40 O2B ? L GDU .   ? B GDU 701 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O   ? S HOH .   ? B HOH 842 ? 1_555 101.4 ? 
41 O   ? S HOH .   ? B HOH 806 ? 1_555 CA ? Q CA . ? B CA 706 ? 1_555 O   ? S HOH .   ? B HOH 842 ? 1_555 75.7  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 201 ? CYS A 256 ? CYS A 228 ? 1_555 CYS A 283 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 201 ? CYS B 256 ? CYS B 228 ? 1_555 CYS B 283 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 95  A . ? GLU 122 A PRO 96  A ? PRO 123 A 1 -0.98 
2 TYR 226 A . ? TYR 253 A PRO 227 A ? PRO 254 A 1 -2.06 
3 GLU 525 A . ? GLU 552 A PRO 526 A ? PRO 553 A 1 0.67  
4 GLU 95  B . ? GLU 122 B PRO 96  B ? PRO 123 B 1 -1.55 
5 TYR 226 B . ? TYR 253 B PRO 227 B ? PRO 254 B 1 -4.10 
6 GLU 525 B . ? GLU 552 B PRO 526 B ? PRO 553 B 1 0.94  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 2 ? 
AA6 ? 8 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? parallel      
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? parallel      
AA6 7 8 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? parallel      
AA9 6 7 ? anti-parallel 
AB1 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 VAL A 88  ? ARG A 91  ? VAL A 115 ARG A 118 
AA1 2 THR A 57  ? THR A 63  ? THR A 84  THR A 90  
AA1 3 VAL A 27  ? ALA A 33  ? VAL A 54  ALA A 60  
AA1 4 TYR A 134 ? VAL A 138 ? TYR A 161 VAL A 165 
AA1 5 THR A 210 ? ASP A 214 ? THR A 237 ASP A 241 
AA1 6 VAL A 160 ? PRO A 163 ? VAL A 187 PRO A 190 
AA1 7 MET A 253 ? CYS A 256 ? MET A 280 CYS A 283 
AA1 8 CYS A 201 ? ALA A 203 ? CYS A 228 ALA A 230 
AA2 1 PHE A 174 ? TRP A 175 ? PHE A 201 TRP A 202 
AA2 2 MET A 206 ? VAL A 207 ? MET A 233 VAL A 234 
AA3 1 GLY A 177 ? MET A 178 ? GLY A 204 MET A 205 
AA3 2 TYR A 184 ? LYS A 185 ? TYR A 211 LYS A 212 
AA4 1 ARG A 343 ? GLU A 346 ? ARG A 370 GLU A 373 
AA4 2 GLU A 315 ? ASN A 320 ? GLU A 342 ASN A 347 
AA4 3 LYS A 403 ? PHE A 407 ? LYS A 430 PHE A 434 
AA4 4 ALA A 471 ? SER A 475 ? ALA A 498 SER A 502 
AA4 5 LEU A 437 ? GLY A 441 ? LEU A 464 GLY A 468 
AA4 6 ALA A 521 ? VAL A 524 ? ALA A 548 VAL A 551 
AA4 7 LEU A 460 ? GLU A 462 ? LEU A 487 GLU A 489 
AA5 1 LEU A 411 ? PHE A 413 ? LEU A 438 PHE A 440 
AA5 2 ILE A 529 ? PRO A 531 ? ILE A 556 PRO A 558 
AA6 1 SER B 87  ? ALA B 93  ? SER B 114 ALA B 120 
AA6 2 THR B 57  ? ASP B 64  ? THR B 84  ASP B 91  
AA6 3 VAL B 27  ? ALA B 33  ? VAL B 54  ALA B 60  
AA6 4 TYR B 134 ? ASP B 139 ? TYR B 161 ASP B 166 
AA6 5 PHE B 211 ? ASP B 214 ? PHE B 238 ASP B 241 
AA6 6 VAL B 160 ? PRO B 163 ? VAL B 187 PRO B 190 
AA6 7 MET B 253 ? CYS B 256 ? MET B 280 CYS B 283 
AA6 8 CYS B 201 ? VAL B 204 ? CYS B 228 VAL B 231 
AA7 1 PHE B 174 ? TRP B 175 ? PHE B 201 TRP B 202 
AA7 2 MET B 206 ? VAL B 207 ? MET B 233 VAL B 234 
AA8 1 GLY B 177 ? MET B 178 ? GLY B 204 MET B 205 
AA8 2 TYR B 184 ? LYS B 185 ? TYR B 211 LYS B 212 
AA9 1 ARG B 343 ? GLU B 346 ? ARG B 370 GLU B 373 
AA9 2 GLU B 315 ? ASN B 320 ? GLU B 342 ASN B 347 
AA9 3 LYS B 403 ? PHE B 407 ? LYS B 430 PHE B 434 
AA9 4 ALA B 471 ? SER B 475 ? ALA B 498 SER B 502 
AA9 5 LEU B 437 ? GLY B 441 ? LEU B 464 GLY B 468 
AA9 6 ALA B 521 ? VAL B 524 ? ALA B 548 VAL B 551 
AA9 7 LEU B 460 ? GLU B 462 ? LEU B 487 GLU B 489 
AB1 1 LEU B 411 ? PHE B 413 ? LEU B 438 PHE B 440 
AB1 2 ILE B 529 ? PRO B 531 ? ILE B 556 PRO B 558 
# 
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 O GLU A 89  ? O GLU A 116 N VAL A 61  ? N VAL A 88  
AA1 2 3 O TRP A 60  ? O TRP A 87  N LEU A 31  ? N LEU A 58  
AA1 3 4 N LEU A 28  ? N LEU A 55  O LEU A 136 ? O LEU A 163 
AA1 4 5 N ILE A 135 ? N ILE A 162 O ILE A 213 ? O ILE A 240 
AA1 5 6 O LEU A 212 ? O LEU A 239 N VAL A 161 ? N VAL A 188 
AA1 6 7 N ALA A 162 ? N ALA A 189 O TYR A 254 ? O TYR A 281 
AA1 7 8 O VAL A 255 ? O VAL A 282 N PHE A 202 ? N PHE A 229 
AA2 1 2 N TRP A 175 ? N TRP A 202 O MET A 206 ? O MET A 233 
AA3 1 2 N GLY A 177 ? N GLY A 204 O LYS A 185 ? O LYS A 212 
AA4 1 2 O ARG A 343 ? O ARG A 370 N VAL A 316 ? N VAL A 343 
AA4 2 3 N PHE A 317 ? N PHE A 344 O LEU A 405 ? O LEU A 432 
AA4 3 4 N VAL A 406 ? N VAL A 433 O TYR A 472 ? O TYR A 499 
AA4 4 5 O VAL A 473 ? O VAL A 500 N ILE A 438 ? N ILE A 465 
AA4 5 6 N TYR A 439 ? N TYR A 466 O PHE A 522 ? O PHE A 549 
AA4 6 7 O SER A 523 ? O SER A 550 N VAL A 461 ? N VAL A 488 
AA5 1 2 N ARG A 412 ? N ARG A 439 O TYR A 530 ? O TYR A 557 
AA6 1 2 O GLU B 89  ? O GLU B 116 N LEU B 59  ? N LEU B 86  
AA6 2 3 O TRP B 60  ? O TRP B 87  N LEU B 31  ? N LEU B 58  
AA6 3 4 N LEU B 28  ? N LEU B 55  O LEU B 136 ? O LEU B 163 
AA6 4 5 N PHE B 137 ? N PHE B 164 O PHE B 211 ? O PHE B 238 
AA6 5 6 O LEU B 212 ? O LEU B 239 N VAL B 161 ? N VAL B 188 
AA6 6 7 N ALA B 162 ? N ALA B 189 O TYR B 254 ? O TYR B 281 
AA6 7 8 O VAL B 255 ? O VAL B 282 N PHE B 202 ? N PHE B 229 
AA7 1 2 N TRP B 175 ? N TRP B 202 O MET B 206 ? O MET B 233 
AA8 1 2 N GLY B 177 ? N GLY B 204 O LYS B 185 ? O LYS B 212 
AA9 1 2 O ARG B 343 ? O ARG B 370 N VAL B 316 ? N VAL B 343 
AA9 2 3 N PHE B 317 ? N PHE B 344 O LEU B 405 ? O LEU B 432 
AA9 3 4 N VAL B 406 ? N VAL B 433 O TYR B 472 ? O TYR B 499 
AA9 4 5 O VAL B 473 ? O VAL B 500 N ILE B 438 ? N ILE B 465 
AA9 5 6 N TYR B 439 ? N TYR B 466 O VAL B 524 ? O VAL B 551 
AA9 6 7 O SER B 523 ? O SER B 550 N VAL B 461 ? N VAL B 488 
AB1 1 2 N ARG B 412 ? N ARG B 439 O TYR B 530 ? O TYR B 557 
# 
_pdbx_entry_details.entry_id                   9EVJ 
_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   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    304 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    801 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.16 
# 
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 ASN A 96  ? ? -90.34  38.82   
2  1 ALA A 120 ? ? -161.34 104.54  
3  1 ALA A 196 ? ? -125.96 -164.44 
4  1 ASN A 200 ? ? -92.81  49.04   
5  1 SER A 236 ? ? 69.54   -61.58  
6  1 TYR A 400 ? ? -109.41 -62.22  
7  1 PRO A 404 ? ? -69.87  -177.21 
8  1 ASP A 437 ? ? -151.73 61.70   
9  1 ASP A 491 ? ? -87.23  -156.84 
10 1 TYR A 494 ? ? -154.80 55.19   
11 1 ASP B 95  ? ? -105.96 -169.99 
12 1 ASN B 96  ? ? -93.65  46.53   
13 1 ASN B 200 ? ? -82.56  35.57   
14 1 SER B 236 ? ? 65.85   -85.22  
15 1 TRP B 261 ? ? -106.52 -168.54 
16 1 PRO B 399 ? ? -59.34  -7.32   
17 1 ARG B 483 ? ? 65.94   -4.16   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 68.1589  25.1511 60.7338  0.5602 ? 0.0820  ? 0.1183  ? 0.3176 ? 0.0708  ? 0.3331 ? 2.1840 ? 
0.2262  ? -0.0447 ? 3.5219 ? 1.2325  ? 2.2387 ? -0.1571 ? -0.2357 ? -0.3288 ? 0.0700  ? 0.0715  ? 0.1647  ? 0.2360  ? 0.1806  ? 
0.0815  ? 
2  'X-RAY DIFFRACTION' ? refined 59.6916  32.7859 46.0550  0.8075 ? 0.0354  ? -0.0364 ? 0.3059 ? -0.0070 ? 0.4039 ? 3.0113 ? 
-0.8618 ? -1.0242 ? 3.4270 ? 0.9995  ? 2.5082 ? -0.0483 ? 0.5067  ? -0.2193 ? -0.9204 ? -0.0507 ? 0.3750  ? -0.3804 ? -0.2072 ? 
0.0656  ? 
3  'X-RAY DIFFRACTION' ? refined 67.3339  28.1652 45.2637  0.7465 ? 0.0077  ? 0.0677  ? 0.3684 ? 0.0636  ? 0.2885 ? 3.0115 ? 
-1.2327 ? -0.7701 ? 4.5714 ? 0.9659  ? 2.6063 ? -0.0607 ? -0.2966 ? -0.1709 ? -0.8891 ? 0.2685  ? 0.0864  ? -0.2505 ? 0.2392  ? 
-0.0318 ? 
4  'X-RAY DIFFRACTION' ? refined 87.5045  11.7033 43.6916  0.6708 ? 0.1582  ? 0.1083  ? 0.5674 ? 0.0003  ? 0.6305 ? 2.1855 ? 
-1.5228 ? -1.7890 ? 2.4099 ? 2.3273  ? 3.8204 ? -0.0413 ? -0.2609 ? -0.1015 ? -0.1107 ? 0.2282  ? -0.4954 ? 0.4045  ? 0.8140  ? 
-0.1572 ? 
5  'X-RAY DIFFRACTION' ? refined 105.3011 15.8011 17.4590  1.2989 ? 0.1464  ? 0.6545  ? 1.2766 ? 0.0483  ? 1.4161 ? 1.0520 ? 
-0.3109 ? -0.4882 ? 1.2294 ? 0.2157  ? 2.0161 ? -0.0667 ? 0.2827  ? 0.5105  ? -0.9927 ? 0.2484  ? -1.0925 ? -0.1861 ? 0.7897  ? 
-0.1262 ? 
6  'X-RAY DIFFRACTION' ? refined 87.4277  5.5413  22.1591  1.0899 ? 0.2389  ? 0.2825  ? 0.6529 ? -0.0584 ? 0.7715 ? 2.4412 ? 
-0.1651 ? 0.1008  ? 2.4248 ? 0.5849  ? 3.3423 ? 0.1856  ? 0.4846  ? -0.2274 ? -1.0668 ? -0.0857 ? -0.5532 ? 0.2736  ? 0.7560  ? 
-0.0754 ? 
7  'X-RAY DIFFRACTION' ? refined 87.3397  13.9287 23.8732  1.2675 ? 0.2368  ? 0.3081  ? 0.7143 ? -0.0702 ? 0.7125 ? 2.3265 ? 
-0.9453 ? -0.7275 ? 2.2091 ? 2.4571  ? 4.7944 ? -0.0135 ? 0.4653  ? 0.2700  ? -1.2291 ? 0.2469  ? -0.4756 ? -0.2069 ? 1.0313  ? 
-0.4505 ? 
8  'X-RAY DIFFRACTION' ? refined 107.5190 21.3016 19.1274  1.7005 ? -0.1789 ? 0.4584  ? 1.8923 ? -0.1166 ? 1.7494 ? 6.7222 ? 
-1.4897 ? -6.2369 ? 2.0361 ? 1.6470  ? 5.8859 ? 0.1201  ? 2.9503  ? -0.9988 ? -1.6390 ? -0.3118 ? -0.9511 ? -0.5307 ? 0.2474  ? 
0.2046  ? 
9  'X-RAY DIFFRACTION' ? refined 67.4910  51.6161 88.7204  0.5003 ? 0.0701  ? 0.0225  ? 0.4209 ? 0.0023  ? 0.2635 ? 1.2600 ? 
-0.2185 ? -0.4025 ? 1.3991 ? 0.0836  ? 1.9620 ? -0.0272 ? -0.3289 ? 0.0968  ? 0.1161  ? 0.0569  ? -0.0728 ? -0.1192 ? 0.2389  ? 
-0.0137 ? 
10 'X-RAY DIFFRACTION' ? refined 43.6980  68.5346 100.9146 0.7295 ? 0.1164  ? 0.1100  ? 0.5620 ? -0.0452 ? 0.5053 ? 0.4287 ? 
-0.6162 ? -0.5466 ? 2.3241 ? 1.0639  ? 2.1736 ? -0.1768 ? 0.0901  ? -0.0155 ? 0.4012  ? -0.0192 ? 0.8308  ? -0.0652 ? -0.1395 ? 
0.0418  ? 
11 'X-RAY DIFFRACTION' ? refined 51.4228  86.1790 112.7096 1.1469 ? 0.0246  ? 0.0495  ? 0.6885 ? -0.2166 ? 0.6348 ? 2.2255 ? 
-0.7143 ? -0.1551 ? 2.9243 ? 1.0796  ? 2.5674 ? -0.2707 ? -0.4600 ? 0.6018  ? 0.4271  ? 0.4588  ? -0.1376 ? -0.7828 ? 0.4585  ? 
-0.1547 ? 
12 'X-RAY DIFFRACTION' ? refined 59.9368  82.4140 97.5593  1.7853 ? 0.2264  ? 0.3263  ? 1.7990 ? 0.3795  ? 1.1686 ? 6.1916 ? 
-1.6345 ? 5.7060  ? 2.6435 ? -2.0248 ? 7.6838 ? 1.5377  ? -5.9486 ? -1.6407 ? 0.9941  ? -2.8287 ? -1.5752 ? 5.9820  ? 2.4265  ? 
1.2669  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 44 through 190 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 191 through 276 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 277 through 300 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 301 through 373 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 374 through 406 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 407 through 540 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 541 through 571 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 572 through 580 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 42 through 318 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 319 through 373 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 374 through 560 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 561 through 562 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLY 28  ? A GLY 1   
2   1 Y 1 A SER 29  ? A SER 2   
3   1 Y 1 A ALA 30  ? A ALA 3   
4   1 Y 1 A PRO 31  ? A PRO 4   
5   1 Y 1 A PRO 32  ? A PRO 5   
6   1 Y 1 A GLY 33  ? A GLY 6   
7   1 Y 1 A ALA 34  ? A ALA 7   
8   1 Y 1 A ASP 35  ? A ASP 8   
9   1 Y 1 A ALA 36  ? A ALA 9   
10  1 Y 1 A TYR 37  ? A TYR 10  
11  1 Y 1 A PHE 38  ? A PHE 11  
12  1 Y 1 A PRO 39  ? A PRO 12  
13  1 Y 1 A GLU 40  ? A GLU 13  
14  1 Y 1 A GLU 41  ? A GLU 14  
15  1 Y 1 A ARG 42  ? A ARG 15  
16  1 Y 1 A TRP 43  ? A TRP 16  
17  1 Y 1 A HIS 581 ? A HIS 554 
18  1 Y 1 A VAL 582 ? A VAL 555 
19  1 Y 1 A LYS 583 ? A LYS 556 
20  1 Y 1 A THR 584 ? A THR 557 
21  1 Y 1 A ASP 585 ? A ASP 558 
22  1 Y 1 A TRP 586 ? A TRP 559 
23  1 Y 1 A ASP 587 ? A ASP 560 
24  1 Y 1 A ARG 588 ? A ARG 561 
25  1 Y 1 A ALA 589 ? A ALA 562 
26  1 Y 1 A LYS 590 ? A LYS 563 
27  1 Y 1 A SER 591 ? A SER 564 
28  1 Y 1 A GLN 592 ? A GLN 565 
29  1 Y 1 A LYS 593 ? A LYS 566 
30  1 Y 1 A MET 594 ? A MET 567 
31  1 Y 1 A ARG 595 ? A ARG 568 
32  1 Y 1 A GLU 596 ? A GLU 569 
33  1 Y 1 A GLN 597 ? A GLN 570 
34  1 Y 1 A GLN 598 ? A GLN 571 
35  1 Y 1 A ALA 599 ? A ALA 572 
36  1 Y 1 A LEU 600 ? A LEU 573 
37  1 Y 1 A SER 601 ? A SER 574 
38  1 Y 1 A ARG 602 ? A ARG 575 
39  1 Y 1 A GLU 603 ? A GLU 576 
40  1 Y 1 A ALA 604 ? A ALA 577 
41  1 Y 1 A LYS 605 ? A LYS 578 
42  1 Y 1 A ASN 606 ? A ASN 579 
43  1 Y 1 A SER 607 ? A SER 580 
44  1 Y 1 A ASP 608 ? A ASP 581 
45  1 Y 1 A VAL 609 ? A VAL 582 
46  1 Y 1 A LEU 610 ? A LEU 583 
47  1 Y 1 A GLN 611 ? A GLN 584 
48  1 Y 1 A SER 612 ? A SER 585 
49  1 Y 1 A PRO 613 ? A PRO 586 
50  1 Y 1 A LEU 614 ? A LEU 587 
51  1 Y 1 A ASP 615 ? A ASP 588 
52  1 Y 1 A SER 616 ? A SER 589 
53  1 Y 1 A ALA 617 ? A ALA 590 
54  1 Y 1 A ALA 618 ? A ALA 591 
55  1 Y 1 A ALA 619 ? A ALA 592 
56  1 Y 1 A ALA 620 ? A ALA 593 
57  1 Y 1 A ALA 621 ? A ALA 594 
58  1 Y 1 B GLY 28  ? B GLY 1   
59  1 Y 1 B SER 29  ? B SER 2   
60  1 Y 1 B ALA 30  ? B ALA 3   
61  1 Y 1 B PRO 31  ? B PRO 4   
62  1 Y 1 B PRO 32  ? B PRO 5   
63  1 Y 1 B GLY 33  ? B GLY 6   
64  1 Y 1 B ALA 34  ? B ALA 7   
65  1 Y 1 B ASP 35  ? B ASP 8   
66  1 Y 1 B ALA 36  ? B ALA 9   
67  1 Y 1 B TYR 37  ? B TYR 10  
68  1 Y 1 B PHE 38  ? B PHE 11  
69  1 Y 1 B PRO 39  ? B PRO 12  
70  1 Y 1 B GLU 40  ? B GLU 13  
71  1 Y 1 B GLU 41  ? B GLU 14  
72  1 Y 1 B GLY 563 ? B GLY 536 
73  1 Y 1 B ASP 564 ? B ASP 537 
74  1 Y 1 B ASP 565 ? B ASP 538 
75  1 Y 1 B GLY 566 ? B GLY 539 
76  1 Y 1 B TYR 567 ? B TYR 540 
77  1 Y 1 B VAL 568 ? B VAL 541 
78  1 Y 1 B SER 569 ? B SER 542 
79  1 Y 1 B ASP 570 ? B ASP 543 
80  1 Y 1 B THR 571 ? B THR 544 
81  1 Y 1 B GLU 572 ? B GLU 545 
82  1 Y 1 B THR 573 ? B THR 546 
83  1 Y 1 B SER 574 ? B SER 547 
84  1 Y 1 B VAL 575 ? B VAL 548 
85  1 Y 1 B VAL 576 ? B VAL 549 
86  1 Y 1 B TRP 577 ? B TRP 550 
87  1 Y 1 B ASN 578 ? B ASN 551 
88  1 Y 1 B ASN 579 ? B ASN 552 
89  1 Y 1 B GLU 580 ? B GLU 553 
90  1 Y 1 B HIS 581 ? B HIS 554 
91  1 Y 1 B VAL 582 ? B VAL 555 
92  1 Y 1 B LYS 583 ? B LYS 556 
93  1 Y 1 B THR 584 ? B THR 557 
94  1 Y 1 B ASP 585 ? B ASP 558 
95  1 Y 1 B TRP 586 ? B TRP 559 
96  1 Y 1 B ASP 587 ? B ASP 560 
97  1 Y 1 B ARG 588 ? B ARG 561 
98  1 Y 1 B ALA 589 ? B ALA 562 
99  1 Y 1 B LYS 590 ? B LYS 563 
100 1 Y 1 B SER 591 ? B SER 564 
101 1 Y 1 B GLN 592 ? B GLN 565 
102 1 Y 1 B LYS 593 ? B LYS 566 
103 1 Y 1 B MET 594 ? B MET 567 
104 1 Y 1 B ARG 595 ? B ARG 568 
105 1 Y 1 B GLU 596 ? B GLU 569 
106 1 Y 1 B GLN 597 ? B GLN 570 
107 1 Y 1 B GLN 598 ? B GLN 571 
108 1 Y 1 B ALA 599 ? B ALA 572 
109 1 Y 1 B LEU 600 ? B LEU 573 
110 1 Y 1 B SER 601 ? B SER 574 
111 1 Y 1 B ARG 602 ? B ARG 575 
112 1 Y 1 B GLU 603 ? B GLU 576 
113 1 Y 1 B ALA 604 ? B ALA 577 
114 1 Y 1 B LYS 605 ? B LYS 578 
115 1 Y 1 B ASN 606 ? B ASN 579 
116 1 Y 1 B SER 607 ? B SER 580 
117 1 Y 1 B ASP 608 ? B ASP 581 
118 1 Y 1 B VAL 609 ? B VAL 582 
119 1 Y 1 B LEU 610 ? B LEU 583 
120 1 Y 1 B GLN 611 ? B GLN 584 
121 1 Y 1 B SER 612 ? B SER 585 
122 1 Y 1 B PRO 613 ? B PRO 586 
123 1 Y 1 B LEU 614 ? B LEU 587 
124 1 Y 1 B ASP 615 ? B ASP 588 
125 1 Y 1 B SER 616 ? B SER 589 
126 1 Y 1 B ALA 617 ? B ALA 590 
127 1 Y 1 B ALA 618 ? B ALA 591 
128 1 Y 1 B ALA 619 ? B ALA 592 
129 1 Y 1 B ALA 620 ? B ALA 593 
130 1 Y 1 B ALA 621 ? B ALA 594 
# 
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  
CA  CA     CA N N 74  
CL  CL     CL N N 75  
CYS N      N  N N 76  
CYS CA     C  N R 77  
CYS C      C  N N 78  
CYS O      O  N N 79  
CYS CB     C  N N 80  
CYS SG     S  N N 81  
CYS OXT    O  N N 82  
CYS H      H  N N 83  
CYS H2     H  N N 84  
CYS HA     H  N N 85  
CYS HB2    H  N N 86  
CYS HB3    H  N N 87  
CYS HG     H  N N 88  
CYS HXT    H  N N 89  
GDU N1     N  N N 90  
GDU C2     C  N N 91  
GDU N3     N  N N 92  
GDU C4     C  N N 93  
GDU C5     C  N N 94  
GDU C6     C  N N 95  
GDU O2     O  N N 96  
GDU O4     O  N N 97  
GDU C1D    C  N R 98  
GDU C2D    C  N R 99  
GDU O2D    O  N N 100 
GDU C3D    C  N S 101 
GDU C4D    C  N R 102 
GDU O4D    O  N N 103 
GDU O3D    O  N N 104 
GDU C5D    C  N N 105 
GDU O5D    O  N N 106 
GDU PA     P  N R 107 
GDU O1A    O  N N 108 
GDU O2A    O  N N 109 
GDU O3A    O  N N 110 
GDU PB     P  N S 111 
GDU O1B    O  N N 112 
GDU O2B    O  N N 113 
GDU O3B    O  N N 114 
GDU "C1'"  C  N R 115 
GDU "C2'"  C  N R 116 
GDU "C3'"  C  N S 117 
GDU "C4'"  C  N R 118 
GDU "C5'"  C  N R 119 
GDU "C6'"  C  N N 120 
GDU "O2'"  O  N N 121 
GDU "O3'"  O  N N 122 
GDU "O4'"  O  N N 123 
GDU "O5'"  O  N N 124 
GDU "O6'"  O  N N 125 
GDU HN3    H  N N 126 
GDU H5     H  N N 127 
GDU H6     H  N N 128 
GDU H1D    H  N N 129 
GDU H2D    H  N N 130 
GDU "HO2'" H  N N 131 
GDU H3D    H  N N 132 
GDU H4D    H  N N 133 
GDU "HO3'" H  N N 134 
GDU "H5'1" H  N N 135 
GDU "H5'2" H  N N 136 
GDU HOA2   H  N N 137 
GDU HOB2   H  N N 138 
GDU "H1'"  H  N N 139 
GDU "H2'"  H  N N 140 
GDU "H3'"  H  N N 141 
GDU "H4'"  H  N N 142 
GDU "H5'"  H  N N 143 
GDU "H6'1" H  N N 144 
GDU "H6'2" H  N N 145 
GDU HO2A   H  N N 146 
GDU HO3A   H  N N 147 
GDU "HO4'" H  N N 148 
GDU "HO6'" H  N N 149 
GLN N      N  N N 150 
GLN CA     C  N S 151 
GLN C      C  N N 152 
GLN O      O  N N 153 
GLN CB     C  N N 154 
GLN CG     C  N N 155 
GLN CD     C  N N 156 
GLN OE1    O  N N 157 
GLN NE2    N  N N 158 
GLN OXT    O  N N 159 
GLN H      H  N N 160 
GLN H2     H  N N 161 
GLN HA     H  N N 162 
GLN HB2    H  N N 163 
GLN HB3    H  N N 164 
GLN HG2    H  N N 165 
GLN HG3    H  N N 166 
GLN HE21   H  N N 167 
GLN HE22   H  N N 168 
GLN HXT    H  N N 169 
GLU N      N  N N 170 
GLU CA     C  N S 171 
GLU C      C  N N 172 
GLU O      O  N N 173 
GLU CB     C  N N 174 
GLU CG     C  N N 175 
GLU CD     C  N N 176 
GLU OE1    O  N N 177 
GLU OE2    O  N N 178 
GLU OXT    O  N N 179 
GLU H      H  N N 180 
GLU H2     H  N N 181 
GLU HA     H  N N 182 
GLU HB2    H  N N 183 
GLU HB3    H  N N 184 
GLU HG2    H  N N 185 
GLU HG3    H  N N 186 
GLU HE2    H  N N 187 
GLU HXT    H  N N 188 
GLY N      N  N N 189 
GLY CA     C  N N 190 
GLY C      C  N N 191 
GLY O      O  N N 192 
GLY OXT    O  N N 193 
GLY H      H  N N 194 
GLY H2     H  N N 195 
GLY HA2    H  N N 196 
GLY HA3    H  N N 197 
GLY HXT    H  N N 198 
HIS N      N  N N 199 
HIS CA     C  N S 200 
HIS C      C  N N 201 
HIS O      O  N N 202 
HIS CB     C  N N 203 
HIS CG     C  Y N 204 
HIS ND1    N  Y N 205 
HIS CD2    C  Y N 206 
HIS CE1    C  Y N 207 
HIS NE2    N  Y N 208 
HIS OXT    O  N N 209 
HIS H      H  N N 210 
HIS H2     H  N N 211 
HIS HA     H  N N 212 
HIS HB2    H  N N 213 
HIS HB3    H  N N 214 
HIS HD1    H  N N 215 
HIS HD2    H  N N 216 
HIS HE1    H  N N 217 
HIS HE2    H  N N 218 
HIS HXT    H  N N 219 
HOH O      O  N N 220 
HOH H1     H  N N 221 
HOH H2     H  N N 222 
ILE N      N  N N 223 
ILE CA     C  N S 224 
ILE C      C  N N 225 
ILE O      O  N N 226 
ILE CB     C  N S 227 
ILE CG1    C  N N 228 
ILE CG2    C  N N 229 
ILE CD1    C  N N 230 
ILE OXT    O  N N 231 
ILE H      H  N N 232 
ILE H2     H  N N 233 
ILE HA     H  N N 234 
ILE HB     H  N N 235 
ILE HG12   H  N N 236 
ILE HG13   H  N N 237 
ILE HG21   H  N N 238 
ILE HG22   H  N N 239 
ILE HG23   H  N N 240 
ILE HD11   H  N N 241 
ILE HD12   H  N N 242 
ILE HD13   H  N N 243 
ILE HXT    H  N N 244 
LEU N      N  N N 245 
LEU CA     C  N S 246 
LEU C      C  N N 247 
LEU O      O  N N 248 
LEU CB     C  N N 249 
LEU CG     C  N N 250 
LEU CD1    C  N N 251 
LEU CD2    C  N N 252 
LEU OXT    O  N N 253 
LEU H      H  N N 254 
LEU H2     H  N N 255 
LEU HA     H  N N 256 
LEU HB2    H  N N 257 
LEU HB3    H  N N 258 
LEU HG     H  N N 259 
LEU HD11   H  N N 260 
LEU HD12   H  N N 261 
LEU HD13   H  N N 262 
LEU HD21   H  N N 263 
LEU HD22   H  N N 264 
LEU HD23   H  N N 265 
LEU HXT    H  N N 266 
LYS N      N  N N 267 
LYS CA     C  N S 268 
LYS C      C  N N 269 
LYS O      O  N N 270 
LYS CB     C  N N 271 
LYS CG     C  N N 272 
LYS CD     C  N N 273 
LYS CE     C  N N 274 
LYS NZ     N  N N 275 
LYS OXT    O  N N 276 
LYS H      H  N N 277 
LYS H2     H  N N 278 
LYS HA     H  N N 279 
LYS HB2    H  N N 280 
LYS HB3    H  N N 281 
LYS HG2    H  N N 282 
LYS HG3    H  N N 283 
LYS HD2    H  N N 284 
LYS HD3    H  N N 285 
LYS HE2    H  N N 286 
LYS HE3    H  N N 287 
LYS HZ1    H  N N 288 
LYS HZ2    H  N N 289 
LYS HZ3    H  N N 290 
LYS HXT    H  N N 291 
MES O1     O  N N 292 
MES C2     C  N N 293 
MES C3     C  N N 294 
MES N4     N  N N 295 
MES C5     C  N N 296 
MES C6     C  N N 297 
MES C7     C  N N 298 
MES C8     C  N N 299 
MES S      S  N N 300 
MES O1S    O  N N 301 
MES O2S    O  N N 302 
MES O3S    O  N N 303 
MES H21    H  N N 304 
MES H22    H  N N 305 
MES H31    H  N N 306 
MES H32    H  N N 307 
MES HN4    H  N N 308 
MES H51    H  N N 309 
MES H52    H  N N 310 
MES H61    H  N N 311 
MES H62    H  N N 312 
MES H71    H  N N 313 
MES H72    H  N N 314 
MES H81    H  N N 315 
MES H82    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
MN  MN     MN N N 337 
NA  NA     NA N N 338 
PHE N      N  N N 339 
PHE CA     C  N S 340 
PHE C      C  N N 341 
PHE O      O  N N 342 
PHE CB     C  N N 343 
PHE CG     C  Y N 344 
PHE CD1    C  Y N 345 
PHE CD2    C  Y N 346 
PHE CE1    C  Y N 347 
PHE CE2    C  Y N 348 
PHE CZ     C  Y N 349 
PHE OXT    O  N N 350 
PHE H      H  N N 351 
PHE H2     H  N N 352 
PHE HA     H  N N 353 
PHE HB2    H  N N 354 
PHE HB3    H  N N 355 
PHE HD1    H  N N 356 
PHE HD2    H  N N 357 
PHE HE1    H  N N 358 
PHE HE2    H  N N 359 
PHE HZ     H  N N 360 
PHE HXT    H  N N 361 
PRO N      N  N N 362 
PRO CA     C  N S 363 
PRO C      C  N N 364 
PRO O      O  N N 365 
PRO CB     C  N N 366 
PRO CG     C  N N 367 
PRO CD     C  N N 368 
PRO OXT    O  N N 369 
PRO H      H  N N 370 
PRO HA     H  N N 371 
PRO HB2    H  N N 372 
PRO HB3    H  N N 373 
PRO HG2    H  N N 374 
PRO HG3    H  N N 375 
PRO HD2    H  N N 376 
PRO HD3    H  N N 377 
PRO HXT    H  N N 378 
SER N      N  N N 379 
SER CA     C  N S 380 
SER C      C  N N 381 
SER O      O  N N 382 
SER CB     C  N N 383 
SER OG     O  N N 384 
SER OXT    O  N N 385 
SER H      H  N N 386 
SER H2     H  N N 387 
SER HA     H  N N 388 
SER HB2    H  N N 389 
SER HB3    H  N N 390 
SER HG     H  N N 391 
SER HXT    H  N N 392 
THR N      N  N N 393 
THR CA     C  N S 394 
THR C      C  N N 395 
THR O      O  N N 396 
THR CB     C  N R 397 
THR OG1    O  N N 398 
THR CG2    C  N N 399 
THR OXT    O  N N 400 
THR H      H  N N 401 
THR H2     H  N N 402 
THR HA     H  N N 403 
THR HB     H  N N 404 
THR HG1    H  N N 405 
THR HG21   H  N N 406 
THR HG22   H  N N 407 
THR HG23   H  N N 408 
THR HXT    H  N N 409 
TRP N      N  N N 410 
TRP CA     C  N S 411 
TRP C      C  N N 412 
TRP O      O  N N 413 
TRP CB     C  N N 414 
TRP CG     C  Y N 415 
TRP CD1    C  Y N 416 
TRP CD2    C  Y N 417 
TRP NE1    N  Y N 418 
TRP CE2    C  Y N 419 
TRP CE3    C  Y N 420 
TRP CZ2    C  Y N 421 
TRP CZ3    C  Y N 422 
TRP CH2    C  Y N 423 
TRP OXT    O  N N 424 
TRP H      H  N N 425 
TRP H2     H  N N 426 
TRP HA     H  N N 427 
TRP HB2    H  N N 428 
TRP HB3    H  N N 429 
TRP HD1    H  N N 430 
TRP HE1    H  N N 431 
TRP HE3    H  N N 432 
TRP HZ2    H  N N 433 
TRP HZ3    H  N N 434 
TRP HH2    H  N N 435 
TRP HXT    H  N N 436 
TYR N      N  N N 437 
TYR CA     C  N S 438 
TYR C      C  N N 439 
TYR O      O  N N 440 
TYR CB     C  N N 441 
TYR CG     C  Y N 442 
TYR CD1    C  Y N 443 
TYR CD2    C  Y N 444 
TYR CE1    C  Y N 445 
TYR CE2    C  Y N 446 
TYR CZ     C  Y N 447 
TYR OH     O  N N 448 
TYR OXT    O  N N 449 
TYR H      H  N N 450 
TYR H2     H  N N 451 
TYR HA     H  N N 452 
TYR HB2    H  N N 453 
TYR HB3    H  N N 454 
TYR HD1    H  N N 455 
TYR HD2    H  N N 456 
TYR HE1    H  N N 457 
TYR HE2    H  N N 458 
TYR HH     H  N N 459 
TYR HXT    H  N N 460 
UDP N1     N  N N 461 
UDP C2     C  N N 462 
UDP N3     N  N N 463 
UDP C4     C  N N 464 
UDP C5     C  N N 465 
UDP C6     C  N N 466 
UDP O2     O  N N 467 
UDP O4     O  N N 468 
UDP "C1'"  C  N R 469 
UDP "C2'"  C  N R 470 
UDP "O2'"  O  N N 471 
UDP "C3'"  C  N S 472 
UDP "C4'"  C  N R 473 
UDP "O4'"  O  N N 474 
UDP "O3'"  O  N N 475 
UDP "C5'"  C  N N 476 
UDP "O5'"  O  N N 477 
UDP PA     P  N N 478 
UDP O1A    O  N N 479 
UDP O2A    O  N N 480 
UDP O3A    O  N N 481 
UDP PB     P  N N 482 
UDP O1B    O  N N 483 
UDP O2B    O  N N 484 
UDP O3B    O  N N 485 
UDP HN3    H  N N 486 
UDP H5     H  N N 487 
UDP H6     H  N N 488 
UDP "H1'"  H  N N 489 
UDP "H2'"  H  N N 490 
UDP "HO2'" H  N N 491 
UDP "H3'"  H  N N 492 
UDP "H4'"  H  N N 493 
UDP "HO3'" H  N N 494 
UDP "H5'1" H  N N 495 
UDP "H5'2" H  N N 496 
UDP HOA2   H  N N 497 
UDP HOB2   H  N N 498 
UDP HOB3   H  N N 499 
VAL N      N  N N 500 
VAL CA     C  N S 501 
VAL C      C  N N 502 
VAL O      O  N N 503 
VAL CB     C  N N 504 
VAL CG1    C  N N 505 
VAL CG2    C  N N 506 
VAL OXT    O  N N 507 
VAL H      H  N N 508 
VAL H2     H  N N 509 
VAL HA     H  N N 510 
VAL HB     H  N N 511 
VAL HG11   H  N N 512 
VAL HG12   H  N N 513 
VAL HG13   H  N N 514 
VAL HG21   H  N N 515 
VAL HG22   H  N N 516 
VAL HG23   H  N N 517 
VAL HXT    H  N N 518 
# 
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  
GDU N1    C2     sing N N 83  
GDU N1    C6     sing N N 84  
GDU N1    C1D    sing N N 85  
GDU C2    N3     sing N N 86  
GDU C2    O2     doub N N 87  
GDU N3    C4     sing N N 88  
GDU N3    HN3    sing N N 89  
GDU C4    C5     sing N N 90  
GDU C4    O4     doub N N 91  
GDU C5    C6     doub N N 92  
GDU C5    H5     sing N N 93  
GDU C6    H6     sing N N 94  
GDU C1D   C2D    sing N N 95  
GDU C1D   O4D    sing N N 96  
GDU C1D   H1D    sing N N 97  
GDU C2D   O2D    sing N N 98  
GDU C2D   C3D    sing N N 99  
GDU C2D   H2D    sing N N 100 
GDU O2D   "HO2'" sing N N 101 
GDU C3D   C4D    sing N N 102 
GDU C3D   O3D    sing N N 103 
GDU C3D   H3D    sing N N 104 
GDU C4D   O4D    sing N N 105 
GDU C4D   C5D    sing N N 106 
GDU C4D   H4D    sing N N 107 
GDU O3D   "HO3'" sing N N 108 
GDU C5D   O5D    sing N N 109 
GDU C5D   "H5'1" sing N N 110 
GDU C5D   "H5'2" sing N N 111 
GDU O5D   PA     sing N N 112 
GDU PA    O1A    doub N N 113 
GDU PA    O2A    sing N N 114 
GDU PA    O3A    sing N N 115 
GDU O2A   HOA2   sing N N 116 
GDU O3A   PB     sing N N 117 
GDU PB    O1B    doub N N 118 
GDU PB    O2B    sing N N 119 
GDU PB    O3B    sing N N 120 
GDU O2B   HOB2   sing N N 121 
GDU O3B   "C1'"  sing N N 122 
GDU "C1'" "C2'"  sing N N 123 
GDU "C1'" "O5'"  sing N N 124 
GDU "C1'" "H1'"  sing N N 125 
GDU "C2'" "C3'"  sing N N 126 
GDU "C2'" "O2'"  sing N N 127 
GDU "C2'" "H2'"  sing N N 128 
GDU "C3'" "C4'"  sing N N 129 
GDU "C3'" "O3'"  sing N N 130 
GDU "C3'" "H3'"  sing N N 131 
GDU "C4'" "C5'"  sing N N 132 
GDU "C4'" "O4'"  sing N N 133 
GDU "C4'" "H4'"  sing N N 134 
GDU "C5'" "C6'"  sing N N 135 
GDU "C5'" "O5'"  sing N N 136 
GDU "C5'" "H5'"  sing N N 137 
GDU "C6'" "O6'"  sing N N 138 
GDU "C6'" "H6'1" sing N N 139 
GDU "C6'" "H6'2" sing N N 140 
GDU "O2'" HO2A   sing N N 141 
GDU "O3'" HO3A   sing N N 142 
GDU "O4'" "HO4'" sing N N 143 
GDU "O6'" "HO6'" sing N N 144 
GLN N     CA     sing N N 145 
GLN N     H      sing N N 146 
GLN N     H2     sing N N 147 
GLN CA    C      sing N N 148 
GLN CA    CB     sing N N 149 
GLN CA    HA     sing N N 150 
GLN C     O      doub N N 151 
GLN C     OXT    sing N N 152 
GLN CB    CG     sing N N 153 
GLN CB    HB2    sing N N 154 
GLN CB    HB3    sing N N 155 
GLN CG    CD     sing N N 156 
GLN CG    HG2    sing N N 157 
GLN CG    HG3    sing N N 158 
GLN CD    OE1    doub N N 159 
GLN CD    NE2    sing N N 160 
GLN NE2   HE21   sing N N 161 
GLN NE2   HE22   sing N N 162 
GLN OXT   HXT    sing N N 163 
GLU N     CA     sing N N 164 
GLU N     H      sing N N 165 
GLU N     H2     sing N N 166 
GLU CA    C      sing N N 167 
GLU CA    CB     sing N N 168 
GLU CA    HA     sing N N 169 
GLU C     O      doub N N 170 
GLU C     OXT    sing N N 171 
GLU CB    CG     sing N N 172 
GLU CB    HB2    sing N N 173 
GLU CB    HB3    sing N N 174 
GLU CG    CD     sing N N 175 
GLU CG    HG2    sing N N 176 
GLU CG    HG3    sing N N 177 
GLU CD    OE1    doub N N 178 
GLU CD    OE2    sing N N 179 
GLU OE2   HE2    sing N N 180 
GLU OXT   HXT    sing N N 181 
GLY N     CA     sing N N 182 
GLY N     H      sing N N 183 
GLY N     H2     sing N N 184 
GLY CA    C      sing N N 185 
GLY CA    HA2    sing N N 186 
GLY CA    HA3    sing N N 187 
GLY C     O      doub N N 188 
GLY C     OXT    sing N N 189 
GLY OXT   HXT    sing N N 190 
HIS N     CA     sing N N 191 
HIS N     H      sing N N 192 
HIS N     H2     sing N N 193 
HIS CA    C      sing N N 194 
HIS CA    CB     sing N N 195 
HIS CA    HA     sing N N 196 
HIS C     O      doub N N 197 
HIS C     OXT    sing N N 198 
HIS CB    CG     sing N N 199 
HIS CB    HB2    sing N N 200 
HIS CB    HB3    sing N N 201 
HIS CG    ND1    sing Y N 202 
HIS CG    CD2    doub Y N 203 
HIS ND1   CE1    doub Y N 204 
HIS ND1   HD1    sing N N 205 
HIS CD2   NE2    sing Y N 206 
HIS CD2   HD2    sing N N 207 
HIS CE1   NE2    sing Y N 208 
HIS CE1   HE1    sing N N 209 
HIS NE2   HE2    sing N N 210 
HIS OXT   HXT    sing N N 211 
HOH O     H1     sing N N 212 
HOH O     H2     sing N N 213 
ILE N     CA     sing N N 214 
ILE N     H      sing N N 215 
ILE N     H2     sing N N 216 
ILE CA    C      sing N N 217 
ILE CA    CB     sing N N 218 
ILE CA    HA     sing N N 219 
ILE C     O      doub N N 220 
ILE C     OXT    sing N N 221 
ILE CB    CG1    sing N N 222 
ILE CB    CG2    sing N N 223 
ILE CB    HB     sing N N 224 
ILE CG1   CD1    sing N N 225 
ILE CG1   HG12   sing N N 226 
ILE CG1   HG13   sing N N 227 
ILE CG2   HG21   sing N N 228 
ILE CG2   HG22   sing N N 229 
ILE CG2   HG23   sing N N 230 
ILE CD1   HD11   sing N N 231 
ILE CD1   HD12   sing N N 232 
ILE CD1   HD13   sing N N 233 
ILE OXT   HXT    sing N N 234 
LEU N     CA     sing N N 235 
LEU N     H      sing N N 236 
LEU N     H2     sing N N 237 
LEU CA    C      sing N N 238 
LEU CA    CB     sing N N 239 
LEU CA    HA     sing N N 240 
LEU C     O      doub N N 241 
LEU C     OXT    sing N N 242 
LEU CB    CG     sing N N 243 
LEU CB    HB2    sing N N 244 
LEU CB    HB3    sing N N 245 
LEU CG    CD1    sing N N 246 
LEU CG    CD2    sing N N 247 
LEU CG    HG     sing N N 248 
LEU CD1   HD11   sing N N 249 
LEU CD1   HD12   sing N N 250 
LEU CD1   HD13   sing N N 251 
LEU CD2   HD21   sing N N 252 
LEU CD2   HD22   sing N N 253 
LEU CD2   HD23   sing N N 254 
LEU OXT   HXT    sing N N 255 
LYS N     CA     sing N N 256 
LYS N     H      sing N N 257 
LYS N     H2     sing N N 258 
LYS CA    C      sing N N 259 
LYS CA    CB     sing N N 260 
LYS CA    HA     sing N N 261 
LYS C     O      doub N N 262 
LYS C     OXT    sing N N 263 
LYS CB    CG     sing N N 264 
LYS CB    HB2    sing N N 265 
LYS CB    HB3    sing N N 266 
LYS CG    CD     sing N N 267 
LYS CG    HG2    sing N N 268 
LYS CG    HG3    sing N N 269 
LYS CD    CE     sing N N 270 
LYS CD    HD2    sing N N 271 
LYS CD    HD3    sing N N 272 
LYS CE    NZ     sing N N 273 
LYS CE    HE2    sing N N 274 
LYS CE    HE3    sing N N 275 
LYS NZ    HZ1    sing N N 276 
LYS NZ    HZ2    sing N N 277 
LYS NZ    HZ3    sing N N 278 
LYS OXT   HXT    sing N N 279 
MES O1    C2     sing N N 280 
MES O1    C6     sing N N 281 
MES C2    C3     sing N N 282 
MES C2    H21    sing N N 283 
MES C2    H22    sing N N 284 
MES C3    N4     sing N N 285 
MES C3    H31    sing N N 286 
MES C3    H32    sing N N 287 
MES N4    C5     sing N N 288 
MES N4    C7     sing N N 289 
MES N4    HN4    sing N N 290 
MES C5    C6     sing N N 291 
MES C5    H51    sing N N 292 
MES C5    H52    sing N N 293 
MES C6    H61    sing N N 294 
MES C6    H62    sing N N 295 
MES C7    C8     sing N N 296 
MES C7    H71    sing N N 297 
MES C7    H72    sing N N 298 
MES C8    S      sing N N 299 
MES C8    H81    sing N N 300 
MES C8    H82    sing N N 301 
MES S     O1S    doub N N 302 
MES S     O2S    doub N N 303 
MES S     O3S    sing N N 304 
MET N     CA     sing N N 305 
MET N     H      sing N N 306 
MET N     H2     sing N N 307 
MET CA    C      sing N N 308 
MET CA    CB     sing N N 309 
MET CA    HA     sing N N 310 
MET C     O      doub N N 311 
MET C     OXT    sing N N 312 
MET CB    CG     sing N N 313 
MET CB    HB2    sing N N 314 
MET CB    HB3    sing N N 315 
MET CG    SD     sing N N 316 
MET CG    HG2    sing N N 317 
MET CG    HG3    sing N N 318 
MET SD    CE     sing N N 319 
MET CE    HE1    sing N N 320 
MET CE    HE2    sing N N 321 
MET CE    HE3    sing N N 322 
MET OXT   HXT    sing N N 323 
PHE N     CA     sing N N 324 
PHE N     H      sing N N 325 
PHE N     H2     sing N N 326 
PHE CA    C      sing N N 327 
PHE CA    CB     sing N N 328 
PHE CA    HA     sing N N 329 
PHE C     O      doub N N 330 
PHE C     OXT    sing N N 331 
PHE CB    CG     sing N N 332 
PHE CB    HB2    sing N N 333 
PHE CB    HB3    sing N N 334 
PHE CG    CD1    doub Y N 335 
PHE CG    CD2    sing Y N 336 
PHE CD1   CE1    sing Y N 337 
PHE CD1   HD1    sing N N 338 
PHE CD2   CE2    doub Y N 339 
PHE CD2   HD2    sing N N 340 
PHE CE1   CZ     doub Y N 341 
PHE CE1   HE1    sing N N 342 
PHE CE2   CZ     sing Y N 343 
PHE CE2   HE2    sing N N 344 
PHE CZ    HZ     sing N N 345 
PHE OXT   HXT    sing N N 346 
PRO N     CA     sing N N 347 
PRO N     CD     sing N N 348 
PRO N     H      sing N N 349 
PRO CA    C      sing N N 350 
PRO CA    CB     sing N N 351 
PRO CA    HA     sing N N 352 
PRO C     O      doub N N 353 
PRO C     OXT    sing N N 354 
PRO CB    CG     sing N N 355 
PRO CB    HB2    sing N N 356 
PRO CB    HB3    sing N N 357 
PRO CG    CD     sing N N 358 
PRO CG    HG2    sing N N 359 
PRO CG    HG3    sing N N 360 
PRO CD    HD2    sing N N 361 
PRO CD    HD3    sing N N 362 
PRO OXT   HXT    sing N N 363 
SER N     CA     sing N N 364 
SER N     H      sing N N 365 
SER N     H2     sing N N 366 
SER CA    C      sing N N 367 
SER CA    CB     sing N N 368 
SER CA    HA     sing N N 369 
SER C     O      doub N N 370 
SER C     OXT    sing N N 371 
SER CB    OG     sing N N 372 
SER CB    HB2    sing N N 373 
SER CB    HB3    sing N N 374 
SER OG    HG     sing N N 375 
SER OXT   HXT    sing N N 376 
THR N     CA     sing N N 377 
THR N     H      sing N N 378 
THR N     H2     sing N N 379 
THR CA    C      sing N N 380 
THR CA    CB     sing N N 381 
THR CA    HA     sing N N 382 
THR C     O      doub N N 383 
THR C     OXT    sing N N 384 
THR CB    OG1    sing N N 385 
THR CB    CG2    sing N N 386 
THR CB    HB     sing N N 387 
THR OG1   HG1    sing N N 388 
THR CG2   HG21   sing N N 389 
THR CG2   HG22   sing N N 390 
THR CG2   HG23   sing N N 391 
THR OXT   HXT    sing N N 392 
TRP N     CA     sing N N 393 
TRP N     H      sing N N 394 
TRP N     H2     sing N N 395 
TRP CA    C      sing N N 396 
TRP CA    CB     sing N N 397 
TRP CA    HA     sing N N 398 
TRP C     O      doub N N 399 
TRP C     OXT    sing N N 400 
TRP CB    CG     sing N N 401 
TRP CB    HB2    sing N N 402 
TRP CB    HB3    sing N N 403 
TRP CG    CD1    doub Y N 404 
TRP CG    CD2    sing Y N 405 
TRP CD1   NE1    sing Y N 406 
TRP CD1   HD1    sing N N 407 
TRP CD2   CE2    doub Y N 408 
TRP CD2   CE3    sing Y N 409 
TRP NE1   CE2    sing Y N 410 
TRP NE1   HE1    sing N N 411 
TRP CE2   CZ2    sing Y N 412 
TRP CE3   CZ3    doub Y N 413 
TRP CE3   HE3    sing N N 414 
TRP CZ2   CH2    doub Y N 415 
TRP CZ2   HZ2    sing N N 416 
TRP CZ3   CH2    sing Y N 417 
TRP CZ3   HZ3    sing N N 418 
TRP CH2   HH2    sing N N 419 
TRP OXT   HXT    sing N N 420 
TYR N     CA     sing N N 421 
TYR N     H      sing N N 422 
TYR N     H2     sing N N 423 
TYR CA    C      sing N N 424 
TYR CA    CB     sing N N 425 
TYR CA    HA     sing N N 426 
TYR C     O      doub N N 427 
TYR C     OXT    sing N N 428 
TYR CB    CG     sing N N 429 
TYR CB    HB2    sing N N 430 
TYR CB    HB3    sing N N 431 
TYR CG    CD1    doub Y N 432 
TYR CG    CD2    sing Y N 433 
TYR CD1   CE1    sing Y N 434 
TYR CD1   HD1    sing N N 435 
TYR CD2   CE2    doub Y N 436 
TYR CD2   HD2    sing N N 437 
TYR CE1   CZ     doub Y N 438 
TYR CE1   HE1    sing N N 439 
TYR CE2   CZ     sing Y N 440 
TYR CE2   HE2    sing N N 441 
TYR CZ    OH     sing N N 442 
TYR OH    HH     sing N N 443 
TYR OXT   HXT    sing N N 444 
UDP N1    C2     sing N N 445 
UDP N1    C6     sing N N 446 
UDP N1    "C1'"  sing N N 447 
UDP C2    N3     sing N N 448 
UDP C2    O2     doub N N 449 
UDP N3    C4     sing N N 450 
UDP N3    HN3    sing N N 451 
UDP C4    C5     sing N N 452 
UDP C4    O4     doub N N 453 
UDP C5    C6     doub N N 454 
UDP C5    H5     sing N N 455 
UDP C6    H6     sing N N 456 
UDP "C1'" "C2'"  sing N N 457 
UDP "C1'" "O4'"  sing N N 458 
UDP "C1'" "H1'"  sing N N 459 
UDP "C2'" "O2'"  sing N N 460 
UDP "C2'" "C3'"  sing N N 461 
UDP "C2'" "H2'"  sing N N 462 
UDP "O2'" "HO2'" sing N N 463 
UDP "C3'" "C4'"  sing N N 464 
UDP "C3'" "O3'"  sing N N 465 
UDP "C3'" "H3'"  sing N N 466 
UDP "C4'" "O4'"  sing N N 467 
UDP "C4'" "C5'"  sing N N 468 
UDP "C4'" "H4'"  sing N N 469 
UDP "O3'" "HO3'" sing N N 470 
UDP "C5'" "O5'"  sing N N 471 
UDP "C5'" "H5'1" sing N N 472 
UDP "C5'" "H5'2" sing N N 473 
UDP "O5'" PA     sing N N 474 
UDP PA    O1A    doub N N 475 
UDP PA    O2A    sing N N 476 
UDP PA    O3A    sing N N 477 
UDP O2A   HOA2   sing N N 478 
UDP O3A   PB     sing N N 479 
UDP PB    O1B    doub N N 480 
UDP PB    O2B    sing N N 481 
UDP PB    O3B    sing N N 482 
UDP O2B   HOB2   sing N N 483 
UDP O3B   HOB3   sing N N 484 
VAL N     CA     sing N N 485 
VAL N     H      sing N N 486 
VAL N     H2     sing N N 487 
VAL CA    C      sing N N 488 
VAL CA    CB     sing N N 489 
VAL CA    HA     sing N N 490 
VAL C     O      doub N N 491 
VAL C     OXT    sing N N 492 
VAL CB    CG1    sing N N 493 
VAL CB    CG2    sing N N 494 
VAL CB    HB     sing N N 495 
VAL CG1   HG11   sing N N 496 
VAL CG1   HG12   sing N N 497 
VAL CG1   HG13   sing N N 498 
VAL CG2   HG21   sing N N 499 
VAL CG2   HG22   sing N N 500 
VAL CG2   HG23   sing N N 501 
VAL OXT   HXT    sing N N 502 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Italian Association for Cancer Research'  Italy           'MFAG 20075'   1 
'Italian Association for Cancer Research'  Italy           'BRIDGE 27004' 2 
'The Giovanni Armenise-Harvard Foundation' 'United States' 'CDA 2013'     3 
'Mizutani Foundation for Glycoscience'     Japan           200039         4 
'The Ehlers-Danlos Society'                'United States' ?              5 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   XXXX 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EVJ 
_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]   0.004528 
_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]   0.004528 
_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]   0.004528 
_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  
CA 
CL 
MN 
N  
NA 
O  
P  
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     . SER A 1 17  ? 85.052  60.417  74.440  1.00 107.89 ? 44  SER A N     1 
ATOM   2    C  CA    . SER A 1 17  ? 84.494  59.230  75.072  1.00 112.81 ? 44  SER A CA    1 
ATOM   3    C  C     . SER A 1 17  ? 83.714  58.414  74.050  1.00 118.32 ? 44  SER A C     1 
ATOM   4    O  O     . SER A 1 17  ? 82.546  58.694  73.788  1.00 116.25 ? 44  SER A O     1 
ATOM   5    C  CB    . SER A 1 17  ? 83.595  59.617  76.243  1.00 115.85 ? 44  SER A CB    1 
ATOM   6    O  OG    . SER A 1 17  ? 83.338  58.492  77.062  1.00 123.57 ? 44  SER A OG    1 
ATOM   7    N  N     . PRO A 1 18  ? 84.361  57.405  73.475  1.00 104.10 ? 45  PRO A N     1 
ATOM   8    C  CA    . PRO A 1 18  ? 83.759  56.705  72.337  1.00 83.19  ? 45  PRO A CA    1 
ATOM   9    C  C     . PRO A 1 18  ? 82.835  55.579  72.774  1.00 82.18  ? 45  PRO A C     1 
ATOM   10   O  O     . PRO A 1 18  ? 83.100  54.863  73.743  1.00 88.43  ? 45  PRO A O     1 
ATOM   11   C  CB    . PRO A 1 18  ? 84.979  56.162  71.584  1.00 64.80  ? 45  PRO A CB    1 
ATOM   12   C  CG    . PRO A 1 18  ? 85.957  55.882  72.680  1.00 87.75  ? 45  PRO A CG    1 
ATOM   13   C  CD    . PRO A 1 18  ? 85.730  56.934  73.750  1.00 93.89  ? 45  PRO A CD    1 
ATOM   14   N  N     . GLU A 1 19  ? 81.732  55.434  72.045  1.00 63.76  ? 46  GLU A N     1 
ATOM   15   C  CA    . GLU A 1 19  ? 80.852  54.291  72.231  1.00 55.90  ? 46  GLU A CA    1 
ATOM   16   C  C     . GLU A 1 19  ? 81.438  53.076  71.529  1.00 54.53  ? 46  GLU A C     1 
ATOM   17   O  O     . GLU A 1 19  ? 81.977  53.182  70.424  1.00 71.65  ? 46  GLU A O     1 
ATOM   18   C  CB    . GLU A 1 19  ? 79.455  54.591  71.687  1.00 54.46  ? 46  GLU A CB    1 
ATOM   19   C  CG    . GLU A 1 19  ? 78.670  55.601  72.507  1.00 68.75  ? 46  GLU A CG    1 
ATOM   20   C  CD    . GLU A 1 19  ? 78.348  55.097  73.900  1.00 77.83  ? 46  GLU A CD    1 
ATOM   21   O  OE1   . GLU A 1 19  ? 77.981  53.908  74.030  1.00 65.63  ? 46  GLU A OE1   1 
ATOM   22   O  OE2   . GLU A 1 19  ? 78.466  55.887  74.865  1.00 62.24  ? 46  GLU A OE2   1 
ATOM   23   N  N     . SER A 1 20  ? 81.337  51.921  72.176  1.00 60.26  ? 47  SER A N     1 
ATOM   24   C  CA    . SER A 1 20  ? 81.861  50.695  71.602  1.00 52.43  ? 47  SER A CA    1 
ATOM   25   C  C     . SER A 1 20  ? 81.078  50.318  70.346  1.00 50.22  ? 47  SER A C     1 
ATOM   26   O  O     . SER A 1 20  ? 79.970  50.814  70.123  1.00 55.59  ? 47  SER A O     1 
ATOM   27   C  CB    . SER A 1 20  ? 81.796  49.563  72.626  1.00 52.10  ? 47  SER A CB    1 
ATOM   28   O  OG    . SER A 1 20  ? 80.458  49.301  73.007  1.00 59.57  ? 47  SER A OG    1 
ATOM   29   N  N     . PRO A 1 21  ? 81.641  49.456  69.499  1.00 52.37  ? 48  PRO A N     1 
ATOM   30   C  CA    . PRO A 1 21  ? 80.882  48.964  68.344  1.00 47.46  ? 48  PRO A CA    1 
ATOM   31   C  C     . PRO A 1 21  ? 79.643  48.200  68.780  1.00 50.89  ? 48  PRO A C     1 
ATOM   32   O  O     . PRO A 1 21  ? 79.557  47.675  69.891  1.00 57.55  ? 48  PRO A O     1 
ATOM   33   C  CB    . PRO A 1 21  ? 81.874  48.040  67.631  1.00 47.38  ? 48  PRO A CB    1 
ATOM   34   C  CG    . PRO A 1 21  ? 83.208  48.537  68.050  1.00 49.73  ? 48  PRO A CG    1 
ATOM   35   C  CD    . PRO A 1 21  ? 83.048  49.023  69.456  1.00 50.76  ? 48  PRO A CD    1 
ATOM   36   N  N     . LEU A 1 22  ? 78.667  48.142  67.883  1.00 56.55  ? 49  LEU A N     1 
ATOM   37   C  CA    . LEU A 1 22  ? 77.490  47.325  68.133  1.00 42.59  ? 49  LEU A CA    1 
ATOM   38   C  C     . LEU A 1 22  ? 77.824  45.855  67.921  1.00 41.54  ? 49  LEU A C     1 
ATOM   39   O  O     . LEU A 1 22  ? 78.646  45.505  67.070  1.00 48.15  ? 49  LEU A O     1 
ATOM   40   C  CB    . LEU A 1 22  ? 76.343  47.737  67.206  1.00 41.66  ? 49  LEU A CB    1 
ATOM   41   C  CG    . LEU A 1 22  ? 75.765  49.139  67.381  1.00 55.50  ? 49  LEU A CG    1 
ATOM   42   C  CD1   . LEU A 1 22  ? 74.623  49.360  66.405  1.00 41.92  ? 49  LEU A CD1   1 
ATOM   43   C  CD2   . LEU A 1 22  ? 75.292  49.330  68.806  1.00 56.29  ? 49  LEU A CD2   1 
ATOM   44   N  N     . GLN A 1 23  ? 77.196  44.991  68.710  1.00 47.55  ? 50  GLN A N     1 
ATOM   45   C  CA    . GLN A 1 23  ? 77.293  43.570  68.435  1.00 43.43  ? 50  GLN A CA    1 
ATOM   46   C  C     . GLN A 1 23  ? 76.569  43.249  67.134  1.00 38.35  ? 50  GLN A C     1 
ATOM   47   O  O     . GLN A 1 23  ? 75.695  43.991  66.680  1.00 54.40  ? 50  GLN A O     1 
ATOM   48   C  CB    . GLN A 1 23  ? 76.699  42.744  69.579  1.00 42.08  ? 50  GLN A CB    1 
ATOM   49   C  CG    . GLN A 1 23  ? 77.349  42.976  70.931  1.00 48.60  ? 50  GLN A CG    1 
ATOM   50   C  CD    . GLN A 1 23  ? 76.868  41.992  71.983  1.00 54.17  ? 50  GLN A CD    1 
ATOM   51   O  OE1   . GLN A 1 23  ? 76.955  40.777  71.799  1.00 51.10  ? 50  GLN A OE1   1 
ATOM   52   N  NE2   . GLN A 1 23  ? 76.355  42.513  73.093  1.00 51.96  ? 50  GLN A NE2   1 
ATOM   53   N  N     . ALA A 1 24  ? 76.950  42.124  66.528  1.00 47.91  ? 51  ALA A N     1 
ATOM   54   C  CA    . ALA A 1 24  ? 76.309  41.700  65.297  1.00 36.46  ? 51  ALA A CA    1 
ATOM   55   C  C     . ALA A 1 24  ? 74.847  41.352  65.570  1.00 49.62  ? 51  ALA A C     1 
ATOM   56   O  O     . ALA A 1 24  ? 74.476  41.037  66.704  1.00 41.77  ? 51  ALA A O     1 
ATOM   57   C  CB    . ALA A 1 24  ? 77.046  40.501  64.700  1.00 45.06  ? 51  ALA A CB    1 
ATOM   58   N  N     . PRO A 1 25  ? 73.993  41.423  64.548  1.00 51.55  ? 52  PRO A N     1 
ATOM   59   C  CA    . PRO A 1 25  ? 72.581  41.077  64.751  1.00 48.12  ? 52  PRO A CA    1 
ATOM   60   C  C     . PRO A 1 25  ? 72.404  39.623  65.167  1.00 44.28  ? 52  PRO A C     1 
ATOM   61   O  O     . PRO A 1 25  ? 73.235  38.761  64.876  1.00 43.54  ? 52  PRO A O     1 
ATOM   62   C  CB    . PRO A 1 25  ? 71.945  41.351  63.381  1.00 43.53  ? 52  PRO A CB    1 
ATOM   63   C  CG    . PRO A 1 25  ? 73.086  41.413  62.421  1.00 53.13  ? 52  PRO A CG    1 
ATOM   64   C  CD    . PRO A 1 25  ? 74.234  41.961  63.199  1.00 35.87  ? 52  PRO A CD    1 
ATOM   65   N  N     . ARG A 1 26  ? 71.300  39.367  65.868  1.00 47.17  ? 53  ARG A N     1 
ATOM   66   C  CA    . ARG A 1 26  ? 70.995  38.052  66.420  1.00 47.54  ? 53  ARG A CA    1 
ATOM   67   C  C     . ARG A 1 26  ? 70.260  37.223  65.374  1.00 49.25  ? 53  ARG A C     1 
ATOM   68   O  O     . ARG A 1 26  ? 69.217  37.644  64.863  1.00 51.36  ? 53  ARG A O     1 
ATOM   69   C  CB    . ARG A 1 26  ? 70.155  38.194  67.688  1.00 40.04  ? 53  ARG A CB    1 
ATOM   70   C  CG    . ARG A 1 26  ? 70.821  39.020  68.781  1.00 44.15  ? 53  ARG A CG    1 
ATOM   71   C  CD    . ARG A 1 26  ? 69.826  39.897  69.543  1.00 41.46  ? 53  ARG A CD    1 
ATOM   72   N  NE    . ARG A 1 26  ? 69.704  41.228  68.965  1.00 54.03  ? 53  ARG A NE    1 
ATOM   73   C  CZ    . ARG A 1 26  ? 69.477  42.333  69.660  1.00 46.59  ? 53  ARG A CZ    1 
ATOM   74   N  NH1   . ARG A 1 26  ? 69.348  42.309  70.976  1.00 51.58  ? 53  ARG A NH1   1 
ATOM   75   N  NH2   . ARG A 1 26  ? 69.390  43.495  69.019  1.00 63.37  ? 53  ARG A NH2   1 
ATOM   76   N  N     . VAL A 1 27  ? 70.799  36.047  65.061  1.00 54.25  ? 54  VAL A N     1 
ATOM   77   C  CA    . VAL A 1 27  ? 70.288  35.202  63.990  1.00 49.18  ? 54  VAL A CA    1 
ATOM   78   C  C     . VAL A 1 27  ? 69.997  33.816  64.546  1.00 46.30  ? 54  VAL A C     1 
ATOM   79   O  O     . VAL A 1 27  ? 70.830  33.236  65.251  1.00 47.81  ? 54  VAL A O     1 
ATOM   80   C  CB    . VAL A 1 27  ? 71.281  35.109  62.816  1.00 38.44  ? 54  VAL A CB    1 
ATOM   81   C  CG1   . VAL A 1 27  ? 70.718  34.231  61.710  1.00 40.87  ? 54  VAL A CG1   1 
ATOM   82   C  CG2   . VAL A 1 27  ? 71.609  36.491  62.290  1.00 47.16  ? 54  VAL A CG2   1 
ATOM   83   N  N     . LEU A 1 28  ? 68.818  33.289  64.224  1.00 48.28  ? 55  LEU A N     1 
ATOM   84   C  CA    . LEU A 1 28  ? 68.468  31.904  64.501  1.00 48.26  ? 55  LEU A CA    1 
ATOM   85   C  C     . LEU A 1 28  ? 68.516  31.122  63.194  1.00 46.03  ? 55  LEU A C     1 
ATOM   86   O  O     . LEU A 1 28  ? 67.798  31.450  62.244  1.00 45.23  ? 55  LEU A O     1 
ATOM   87   C  CB    . LEU A 1 28  ? 67.079  31.795  65.129  1.00 40.80  ? 55  LEU A CB    1 
ATOM   88   C  CG    . LEU A 1 28  ? 66.572  30.358  65.291  1.00 48.68  ? 55  LEU A CG    1 
ATOM   89   C  CD1   . LEU A 1 28  ? 67.265  29.676  66.458  1.00 45.62  ? 55  LEU A CD1   1 
ATOM   90   C  CD2   . LEU A 1 28  ? 65.063  30.313  65.453  1.00 45.57  ? 55  LEU A CD2   1 
ATOM   91   N  N     . ILE A 1 29  ? 69.362  30.101  63.146  1.00 40.89  ? 56  ILE A N     1 
ATOM   92   C  CA    . ILE A 1 29  ? 69.459  29.219  61.991  1.00 44.52  ? 56  ILE A CA    1 
ATOM   93   C  C     . ILE A 1 29  ? 68.506  28.050  62.205  1.00 46.88  ? 56  ILE A C     1 
ATOM   94   O  O     . ILE A 1 29  ? 68.682  27.252  63.133  1.00 54.00  ? 56  ILE A O     1 
ATOM   95   C  CB    . ILE A 1 29  ? 70.899  28.731  61.785  1.00 54.69  ? 56  ILE A CB    1 
ATOM   96   C  CG1   . ILE A 1 29  ? 71.850  29.917  61.708  1.00 50.85  ? 56  ILE A CG1   1 
ATOM   97   C  CG2   . ILE A 1 29  ? 70.997  27.893  60.524  1.00 45.79  ? 56  ILE A CG2   1 
ATOM   98   C  CD1   . ILE A 1 29  ? 73.273  29.522  61.456  1.00 39.94  ? 56  ILE A CD1   1 
ATOM   99   N  N     . ALA A 1 30  ? 67.491  27.954  61.353  1.00 46.91  ? 57  ALA A N     1 
ATOM   100  C  CA    . ALA A 1 30  ? 66.469  26.921  61.454  1.00 42.49  ? 57  ALA A CA    1 
ATOM   101  C  C     . ALA A 1 30  ? 66.789  25.816  60.453  1.00 46.28  ? 57  ALA A C     1 
ATOM   102  O  O     . ALA A 1 30  ? 66.883  26.071  59.247  1.00 47.67  ? 57  ALA A O     1 
ATOM   103  C  CB    . ALA A 1 30  ? 65.079  27.505  61.201  1.00 37.87  ? 57  ALA A CB    1 
ATOM   104  N  N     . LEU A 1 31  ? 66.937  24.590  60.951  1.00 51.64  ? 58  LEU A N     1 
ATOM   105  C  CA    . LEU A 1 31  ? 67.375  23.451  60.144  1.00 47.77  ? 58  LEU A CA    1 
ATOM   106  C  C     . LEU A 1 31  ? 66.383  22.303  60.304  1.00 51.35  ? 58  LEU A C     1 
ATOM   107  O  O     . LEU A 1 31  ? 66.358  21.635  61.342  1.00 50.80  ? 58  LEU A O     1 
ATOM   108  C  CB    . LEU A 1 31  ? 68.780  23.014  60.545  1.00 39.15  ? 58  LEU A CB    1 
ATOM   109  C  CG    . LEU A 1 31  ? 69.319  21.757  59.859  1.00 62.61  ? 58  LEU A CG    1 
ATOM   110  C  CD1   . LEU A 1 31  ? 69.583  22.021  58.386  1.00 60.70  ? 58  LEU A CD1   1 
ATOM   111  C  CD2   . LEU A 1 31  ? 70.575  21.264  60.556  1.00 59.51  ? 58  LEU A CD2   1 
ATOM   112  N  N     . LEU A 1 32  ? 65.574  22.071  59.272  1.00 47.21  ? 59  LEU A N     1 
ATOM   113  C  CA    . LEU A 1 32  ? 64.755  20.869  59.182  1.00 53.10  ? 59  LEU A CA    1 
ATOM   114  C  C     . LEU A 1 32  ? 65.538  19.808  58.419  1.00 53.44  ? 59  LEU A C     1 
ATOM   115  O  O     . LEU A 1 32  ? 66.014  20.061  57.306  1.00 52.01  ? 59  LEU A O     1 
ATOM   116  C  CB    . LEU A 1 32  ? 63.426  21.151  58.477  1.00 50.68  ? 59  LEU A CB    1 
ATOM   117  C  CG    . LEU A 1 32  ? 62.642  22.434  58.763  1.00 50.79  ? 59  LEU A CG    1 
ATOM   118  C  CD1   . LEU A 1 32  ? 61.259  22.343  58.134  1.00 56.36  ? 59  LEU A CD1   1 
ATOM   119  C  CD2   . LEU A 1 32  ? 62.534  22.710  60.247  1.00 57.60  ? 59  LEU A CD2   1 
ATOM   120  N  N     . ALA A 1 33  ? 65.675  18.623  59.012  1.00 42.82  ? 60  ALA A N     1 
ATOM   121  C  CA    . ALA A 1 33  ? 66.504  17.568  58.440  1.00 44.83  ? 60  ALA A CA    1 
ATOM   122  C  C     . ALA A 1 33  ? 65.730  16.260  58.398  1.00 52.15  ? 60  ALA A C     1 
ATOM   123  O  O     . ALA A 1 33  ? 65.377  15.711  59.447  1.00 51.36  ? 60  ALA A O     1 
ATOM   124  C  CB    . ALA A 1 33  ? 67.798  17.393  59.239  1.00 57.71  ? 60  ALA A CB    1 
ATOM   125  N  N     . ARG A 1 34  ? 65.477  15.759  57.188  1.00 52.22  ? 61  ARG A N     1 
ATOM   126  C  CA    . ARG A 1 34  ? 64.951  14.413  56.986  1.00 54.82  ? 61  ARG A CA    1 
ATOM   127  C  C     . ARG A 1 34  ? 65.823  13.706  55.962  1.00 52.62  ? 61  ARG A C     1 
ATOM   128  O  O     . ARG A 1 34  ? 65.980  14.197  54.840  1.00 55.71  ? 61  ARG A O     1 
ATOM   129  C  CB    . ARG A 1 34  ? 63.495  14.427  56.512  1.00 46.10  ? 61  ARG A CB    1 
ATOM   130  C  CG    . ARG A 1 34  ? 62.950  13.027  56.271  1.00 47.94  ? 61  ARG A CG    1 
ATOM   131  C  CD    . ARG A 1 34  ? 61.612  13.015  55.550  1.00 43.54  ? 61  ARG A CD    1 
ATOM   132  N  NE    . ARG A 1 34  ? 61.155  11.646  55.335  1.00 53.82  ? 61  ARG A NE    1 
ATOM   133  C  CZ    . ARG A 1 34  ? 60.103  11.305  54.603  1.00 52.83  ? 61  ARG A CZ    1 
ATOM   134  N  NH1   . ARG A 1 34  ? 59.362  12.214  53.993  1.00 59.48  ? 61  ARG A NH1   1 
ATOM   135  N  NH2   . ARG A 1 34  ? 59.792  10.018  54.477  1.00 51.85  ? 61  ARG A NH2   1 
ATOM   136  N  N     . ASN A 1 35  ? 66.377  12.557  56.347  1.00 52.31  ? 62  ASN A N     1 
ATOM   137  C  CA    . ASN A 1 35  ? 67.208  11.737  55.467  1.00 54.16  ? 62  ASN A CA    1 
ATOM   138  C  C     . ASN A 1 35  ? 68.327  12.572  54.843  1.00 59.74  ? 62  ASN A C     1 
ATOM   139  O  O     . ASN A 1 35  ? 68.483  12.650  53.623  1.00 51.44  ? 62  ASN A O     1 
ATOM   140  C  CB    . ASN A 1 35  ? 66.353  11.061  54.392  1.00 50.32  ? 62  ASN A CB    1 
ATOM   141  C  CG    . ASN A 1 35  ? 65.344  10.086  54.974  1.00 54.37  ? 62  ASN A CG    1 
ATOM   142  O  OD1   . ASN A 1 35  ? 65.667  9.293   55.858  1.00 59.73  ? 62  ASN A OD1   1 
ATOM   143  N  ND2   . ASN A 1 35  ? 64.113  10.143  54.478  1.00 63.37  ? 62  ASN A ND2   1 
ATOM   144  N  N     . ALA A 1 36  ? 69.106  13.213  55.714  1.00 52.97  ? 63  ALA A N     1 
ATOM   145  C  CA    . ALA A 1 36  ? 70.152  14.133  55.287  1.00 55.07  ? 63  ALA A CA    1 
ATOM   146  C  C     . ALA A 1 36  ? 71.537  13.724  55.770  1.00 55.67  ? 63  ALA A C     1 
ATOM   147  O  O     . ALA A 1 36  ? 72.487  14.500  55.615  1.00 59.05  ? 63  ALA A O     1 
ATOM   148  C  CB    . ALA A 1 36  ? 69.836  15.551  55.766  1.00 49.06  ? 63  ALA A CB    1 
ATOM   149  N  N     . ALA A 1 37  ? 71.680  12.524  56.339  1.00 62.09  ? 64  ALA A N     1 
ATOM   150  C  CA    . ALA A 1 37  ? 72.958  12.125  56.922  1.00 63.29  ? 64  ALA A CA    1 
ATOM   151  C  C     . ALA A 1 37  ? 74.083  12.136  55.896  1.00 56.86  ? 64  ALA A C     1 
ATOM   152  O  O     . ALA A 1 37  ? 75.247  12.346  56.257  1.00 62.67  ? 64  ALA A O     1 
ATOM   153  C  CB    . ALA A 1 37  ? 72.832  10.741  57.556  1.00 54.92  ? 64  ALA A CB    1 
ATOM   154  N  N     . HIS A 1 38  ? 73.760  11.915  54.620  1.00 54.87  ? 65  HIS A N     1 
ATOM   155  C  CA    . HIS A 1 38  ? 74.777  11.970  53.575  1.00 45.74  ? 65  HIS A CA    1 
ATOM   156  C  C     . HIS A 1 38  ? 75.337  13.375  53.405  1.00 54.25  ? 65  HIS A C     1 
ATOM   157  O  O     . HIS A 1 38  ? 76.485  13.539  52.978  1.00 56.43  ? 65  HIS A O     1 
ATOM   158  C  CB    . HIS A 1 38  ? 74.189  11.482  52.251  1.00 49.08  ? 65  HIS A CB    1 
ATOM   159  C  CG    . HIS A 1 38  ? 73.027  12.296  51.778  1.00 50.67  ? 65  HIS A CG    1 
ATOM   160  N  ND1   . HIS A 1 38  ? 71.750  12.119  52.264  1.00 64.43  ? 65  HIS A ND1   1 
ATOM   161  C  CD2   . HIS A 1 38  ? 72.949  13.299  50.872  1.00 58.32  ? 65  HIS A CD2   1 
ATOM   162  C  CE1   . HIS A 1 38  ? 70.934  12.974  51.674  1.00 63.70  ? 65  HIS A CE1   1 
ATOM   163  N  NE2   . HIS A 1 38  ? 71.636  13.701  50.824  1.00 64.22  ? 65  HIS A NE2   1 
ATOM   164  N  N     . ALA A 1 39  ? 74.547  14.395  53.734  1.00 59.92  ? 66  ALA A N     1 
ATOM   165  C  CA    . ALA A 1 39  ? 74.915  15.783  53.495  1.00 55.87  ? 66  ALA A CA    1 
ATOM   166  C  C     . ALA A 1 39  ? 75.316  16.546  54.747  1.00 59.04  ? 66  ALA A C     1 
ATOM   167  O  O     . ALA A 1 39  ? 76.147  17.452  54.656  1.00 52.94  ? 66  ALA A O     1 
ATOM   168  C  CB    . ALA A 1 39  ? 73.757  16.527  52.815  1.00 44.47  ? 66  ALA A CB    1 
ATOM   169  N  N     . LEU A 1 40  ? 74.748  16.204  55.905  1.00 53.06  ? 67  LEU A N     1 
ATOM   170  C  CA    . LEU A 1 40  ? 74.988  16.957  57.137  1.00 54.78  ? 67  LEU A CA    1 
ATOM   171  C  C     . LEU A 1 40  ? 76.460  17.206  57.445  1.00 52.11  ? 67  LEU A C     1 
ATOM   172  O  O     . LEU A 1 40  ? 76.795  18.340  57.820  1.00 51.48  ? 67  LEU A O     1 
ATOM   173  C  CB    . LEU A 1 40  ? 74.308  16.244  58.314  1.00 52.70  ? 67  LEU A CB    1 
ATOM   174  C  CG    . LEU A 1 40  ? 72.780  16.255  58.332  1.00 58.18  ? 67  LEU A CG    1 
ATOM   175  C  CD1   . LEU A 1 40  ? 72.263  15.448  59.509  1.00 55.00  ? 67  LEU A CD1   1 
ATOM   176  C  CD2   . LEU A 1 40  ? 72.258  17.681  58.385  1.00 41.88  ? 67  LEU A CD2   1 
ATOM   177  N  N     . PRO A 1 41  ? 77.376  16.230  57.326  1.00 61.22  ? 68  PRO A N     1 
ATOM   178  C  CA    . PRO A 1 41  ? 78.787  16.529  57.639  1.00 61.10  ? 68  PRO A CA    1 
ATOM   179  C  C     . PRO A 1 41  ? 79.346  17.718  56.879  1.00 60.90  ? 68  PRO A C     1 
ATOM   180  O  O     . PRO A 1 41  ? 80.079  18.528  57.458  1.00 68.79  ? 68  PRO A O     1 
ATOM   181  C  CB    . PRO A 1 41  ? 79.505  15.228  57.259  1.00 45.89  ? 68  PRO A CB    1 
ATOM   182  C  CG    . PRO A 1 41  ? 78.489  14.181  57.466  1.00 46.16  ? 68  PRO A CG    1 
ATOM   183  C  CD    . PRO A 1 41  ? 77.187  14.795  57.037  1.00 55.26  ? 68  PRO A CD    1 
ATOM   184  N  N     . THR A 1 42  ? 79.009  17.852  55.598  1.00 53.11  ? 69  THR A N     1 
ATOM   185  C  CA    . THR A 1 42  ? 79.465  19.003  54.828  1.00 55.65  ? 69  THR A CA    1 
ATOM   186  C  C     . THR A 1 42  ? 78.580  20.223  55.067  1.00 58.77  ? 69  THR A C     1 
ATOM   187  O  O     . THR A 1 42  ? 79.086  21.340  55.221  1.00 58.45  ? 69  THR A O     1 
ATOM   188  C  CB    . THR A 1 42  ? 79.504  18.649  53.340  1.00 52.70  ? 69  THR A CB    1 
ATOM   189  O  OG1   . THR A 1 42  ? 80.464  17.608  53.123  1.00 61.98  ? 69  THR A OG1   1 
ATOM   190  C  CG2   . THR A 1 42  ? 79.889  19.857  52.509  1.00 62.21  ? 69  THR A CG2   1 
ATOM   191  N  N     . THR A 1 43  ? 77.261  20.023  55.118  1.00 60.40  ? 70  THR A N     1 
ATOM   192  C  CA    . THR A 1 43  ? 76.342  21.140  55.318  1.00 47.94  ? 70  THR A CA    1 
ATOM   193  C  C     . THR A 1 43  ? 76.538  21.775  56.687  1.00 52.01  ? 70  THR A C     1 
ATOM   194  O  O     . THR A 1 43  ? 76.690  22.997  56.801  1.00 47.80  ? 70  THR A O     1 
ATOM   195  C  CB    . THR A 1 43  ? 74.900  20.667  55.144  1.00 47.77  ? 70  THR A CB    1 
ATOM   196  O  OG1   . THR A 1 43  ? 74.626  20.480  53.752  1.00 58.74  ? 70  THR A OG1   1 
ATOM   197  C  CG2   . THR A 1 43  ? 73.934  21.693  55.714  1.00 75.48  ? 70  THR A CG2   1 
ATOM   198  N  N     . LEU A 1 44  ? 76.546  20.956  57.743  1.00 51.61  ? 71  LEU A N     1 
ATOM   199  C  CA    . LEU A 1 44  ? 76.797  21.484  59.080  1.00 56.69  ? 71  LEU A CA    1 
ATOM   200  C  C     . LEU A 1 44  ? 78.212  22.031  59.206  1.00 63.90  ? 71  LEU A C     1 
ATOM   201  O  O     . LEU A 1 44  ? 78.442  22.981  59.962  1.00 51.90  ? 71  LEU A O     1 
ATOM   202  C  CB    . LEU A 1 44  ? 76.547  20.405  60.136  1.00 52.43  ? 71  LEU A CB    1 
ATOM   203  C  CG    . LEU A 1 44  ? 75.117  19.867  60.162  1.00 54.34  ? 71  LEU A CG    1 
ATOM   204  C  CD1   . LEU A 1 44  ? 74.983  18.719  61.143  1.00 48.03  ? 71  LEU A CD1   1 
ATOM   205  C  CD2   . LEU A 1 44  ? 74.156  20.989  60.508  1.00 54.01  ? 71  LEU A CD2   1 
ATOM   206  N  N     . GLY A 1 45  ? 79.166  21.453  58.472  1.00 55.29  ? 72  GLY A N     1 
ATOM   207  C  CA    . GLY A 1 45  ? 80.514  21.997  58.472  1.00 57.56  ? 72  GLY A CA    1 
ATOM   208  C  C     . GLY A 1 45  ? 80.571  23.394  57.886  1.00 61.32  ? 72  GLY A C     1 
ATOM   209  O  O     . GLY A 1 45  ? 81.312  24.253  58.370  1.00 57.55  ? 72  GLY A O     1 
ATOM   210  N  N     . ALA A 1 46  ? 79.776  23.645  56.846  1.00 58.10  ? 73  ALA A N     1 
ATOM   211  C  CA    . ALA A 1 46  ? 79.718  24.984  56.275  1.00 52.86  ? 73  ALA A CA    1 
ATOM   212  C  C     . ALA A 1 46  ? 79.068  25.965  57.241  1.00 54.01  ? 73  ALA A C     1 
ATOM   213  O  O     . ALA A 1 46  ? 79.551  27.090  57.409  1.00 61.61  ? 73  ALA A O     1 
ATOM   214  C  CB    . ALA A 1 46  ? 78.960  24.960  54.949  1.00 41.14  ? 73  ALA A CB    1 
ATOM   215  N  N     . LEU A 1 47  ? 77.978  25.550  57.892  1.00 53.23  ? 74  LEU A N     1 
ATOM   216  C  CA    . LEU A 1 47  ? 77.257  26.450  58.787  1.00 55.27  ? 74  LEU A CA    1 
ATOM   217  C  C     . LEU A 1 47  ? 78.111  26.847  59.984  1.00 56.59  ? 74  LEU A C     1 
ATOM   218  O  O     . LEU A 1 47  ? 78.124  28.017  60.384  1.00 50.50  ? 74  LEU A O     1 
ATOM   219  C  CB    . LEU A 1 47  ? 75.956  25.797  59.256  1.00 50.87  ? 74  LEU A CB    1 
ATOM   220  C  CG    . LEU A 1 47  ? 74.881  25.522  58.203  1.00 57.53  ? 74  LEU A CG    1 
ATOM   221  C  CD1   . LEU A 1 47  ? 73.663  24.882  58.847  1.00 49.81  ? 74  LEU A CD1   1 
ATOM   222  C  CD2   . LEU A 1 47  ? 74.495  26.805  57.491  1.00 45.33  ? 74  LEU A CD2   1 
ATOM   223  N  N     . GLU A 1 48  ? 78.834  25.887  60.569  1.00 55.79  ? 75  GLU A N     1 
ATOM   224  C  CA    . GLU A 1 48  ? 79.649  26.183  61.741  1.00 58.67  ? 75  GLU A CA    1 
ATOM   225  C  C     . GLU A 1 48  ? 80.813  27.112  61.420  1.00 64.79  ? 75  GLU A C     1 
ATOM   226  O  O     . GLU A 1 48  ? 81.357  27.742  62.333  1.00 70.67  ? 75  GLU A O     1 
ATOM   227  C  CB    . GLU A 1 48  ? 80.172  24.888  62.364  1.00 47.30  ? 75  GLU A CB    1 
ATOM   228  C  CG    . GLU A 1 48  ? 81.295  24.221  61.584  1.00 66.56  ? 75  GLU A CG    1 
ATOM   229  C  CD    . GLU A 1 48  ? 81.687  22.878  62.166  1.00 73.94  ? 75  GLU A CD    1 
ATOM   230  O  OE1   . GLU A 1 48  ? 80.818  22.224  62.780  1.00 58.82  ? 75  GLU A OE1   1 
ATOM   231  O  OE2   . GLU A 1 48  ? 82.864  22.481  62.016  1.00 70.31  ? 75  GLU A OE2   1 
ATOM   232  N  N     . ARG A 1 49  ? 81.199  27.218  60.149  1.00 56.01  ? 76  ARG A N     1 
ATOM   233  C  CA    . ARG A 1 49  ? 82.290  28.088  59.733  1.00 56.65  ? 76  ARG A CA    1 
ATOM   234  C  C     . ARG A 1 49  ? 81.802  29.407  59.143  1.00 56.91  ? 76  ARG A C     1 
ATOM   235  O  O     . ARG A 1 49  ? 82.594  30.129  58.530  1.00 47.91  ? 76  ARG A O     1 
ATOM   236  C  CB    . ARG A 1 49  ? 83.190  27.363  58.729  1.00 45.94  ? 76  ARG A CB    1 
ATOM   237  C  CG    . ARG A 1 49  ? 83.928  26.170  59.321  1.00 59.15  ? 76  ARG A CG    1 
ATOM   238  C  CD    . ARG A 1 49  ? 84.961  25.603  58.359  1.00 52.80  ? 76  ARG A CD    1 
ATOM   239  N  NE    . ARG A 1 49  ? 84.350  24.929  57.219  1.00 71.99  ? 76  ARG A NE    1 
ATOM   240  C  CZ    . ARG A 1 49  ? 84.100  23.627  57.165  1.00 72.93  ? 76  ARG A CZ    1 
ATOM   241  N  NH1   . ARG A 1 49  ? 84.396  22.824  58.174  1.00 66.28  ? 76  ARG A NH1   1 
ATOM   242  N  NH2   . ARG A 1 49  ? 83.540  23.120  56.070  1.00 67.53  ? 76  ARG A NH2   1 
ATOM   243  N  N     . LEU A 1 50  ? 80.522  29.735  59.311  1.00 58.45  ? 77  LEU A N     1 
ATOM   244  C  CA    . LEU A 1 50  ? 80.020  31.029  58.870  1.00 55.30  ? 77  LEU A CA    1 
ATOM   245  C  C     . LEU A 1 50  ? 80.718  32.152  59.623  1.00 43.98  ? 77  LEU A C     1 
ATOM   246  O  O     . LEU A 1 50  ? 80.958  32.056  60.829  1.00 60.10  ? 77  LEU A O     1 
ATOM   247  C  CB    . LEU A 1 50  ? 78.510  31.118  59.089  1.00 51.37  ? 77  LEU A CB    1 
ATOM   248  C  CG    . LEU A 1 50  ? 77.593  30.478  58.047  1.00 54.05  ? 77  LEU A CG    1 
ATOM   249  C  CD1   . LEU A 1 50  ? 76.139  30.624  58.462  1.00 39.64  ? 77  LEU A CD1   1 
ATOM   250  C  CD2   . LEU A 1 50  ? 77.825  31.114  56.690  1.00 44.68  ? 77  LEU A CD2   1 
ATOM   251  N  N     . ARG A 1 51  ? 81.048  33.224  58.902  1.00 53.59  ? 78  ARG A N     1 
ATOM   252  C  CA    . ARG A 1 51  ? 81.672  34.401  59.511  1.00 56.78  ? 78  ARG A CA    1 
ATOM   253  C  C     . ARG A 1 51  ? 80.581  35.321  60.062  1.00 62.59  ? 78  ARG A C     1 
ATOM   254  O  O     . ARG A 1 51  ? 80.277  36.394  59.533  1.00 62.75  ? 78  ARG A O     1 
ATOM   255  C  CB    . ARG A 1 51  ? 82.573  35.112  58.510  1.00 50.62  ? 78  ARG A CB    1 
ATOM   256  C  CG    . ARG A 1 51  ? 83.949  34.478  58.384  1.00 48.69  ? 78  ARG A CG    1 
ATOM   257  C  CD    . ARG A 1 51  ? 84.903  35.352  57.587  1.00 59.15  ? 78  ARG A CD    1 
ATOM   258  N  NE    . ARG A 1 51  ? 84.611  35.334  56.159  1.00 65.38  ? 78  ARG A NE    1 
ATOM   259  C  CZ    . ARG A 1 51  ? 85.109  34.450  55.305  1.00 70.71  ? 78  ARG A CZ    1 
ATOM   260  N  NH1   . ARG A 1 51  ? 85.924  33.487  55.704  1.00 69.58  ? 78  ARG A NH1   1 
ATOM   261  N  NH2   . ARG A 1 51  ? 84.778  34.530  54.019  1.00 74.73  ? 78  ARG A NH2   1 
ATOM   262  N  N     . HIS A 1 52  ? 79.977  34.854  61.157  1.00 51.29  ? 79  HIS A N     1 
ATOM   263  C  CA    . HIS A 1 52  ? 78.986  35.575  61.925  1.00 51.49  ? 79  HIS A CA    1 
ATOM   264  C  C     . HIS A 1 52  ? 79.181  35.082  63.355  1.00 53.31  ? 79  HIS A C     1 
ATOM   265  O  O     . HIS A 1 52  ? 79.255  33.859  63.570  1.00 60.30  ? 79  HIS A O     1 
ATOM   266  C  CB    . HIS A 1 52  ? 77.559  35.311  61.455  1.00 51.98  ? 79  HIS A CB    1 
ATOM   267  C  CG    . HIS A 1 52  ? 76.518  36.058  62.229  1.00 57.59  ? 79  HIS A CG    1 
ATOM   268  N  ND1   . HIS A 1 52  ? 75.917  35.542  63.357  1.00 60.95  ? 79  HIS A ND1   1 
ATOM   269  C  CD2   . HIS A 1 52  ? 75.966  37.280  62.035  1.00 49.53  ? 79  HIS A CD2   1 
ATOM   270  C  CE1   . HIS A 1 52  ? 75.043  36.414  63.827  1.00 57.64  ? 79  HIS A CE1   1 
ATOM   271  N  NE2   . HIS A 1 52  ? 75.054  37.478  63.044  1.00 58.33  ? 79  HIS A NE2   1 
ATOM   272  N  N     . PRO A 1 53  ? 79.273  35.985  64.331  1.00 54.47  ? 80  PRO A N     1 
ATOM   273  C  CA    . PRO A 1 53  ? 79.659  35.579  65.691  1.00 59.84  ? 80  PRO A CA    1 
ATOM   274  C  C     . PRO A 1 53  ? 78.716  34.528  66.258  1.00 59.32  ? 80  PRO A C     1 
ATOM   275  O  O     . PRO A 1 53  ? 77.493  34.659  66.185  1.00 67.08  ? 80  PRO A O     1 
ATOM   276  C  CB    . PRO A 1 53  ? 79.594  36.891  66.482  1.00 45.74  ? 80  PRO A CB    1 
ATOM   277  C  CG    . PRO A 1 53  ? 79.764  37.957  65.447  1.00 44.34  ? 80  PRO A CG    1 
ATOM   278  C  CD    . PRO A 1 53  ? 79.088  37.439  64.218  1.00 42.69  ? 80  PRO A CD    1 
ATOM   279  N  N     . ARG A 1 54  ? 79.306  33.468  66.816  1.00 56.99  ? 81  ARG A N     1 
ATOM   280  C  CA    . ARG A 1 54  ? 78.512  32.334  67.275  1.00 60.83  ? 81  ARG A CA    1 
ATOM   281  C  C     . ARG A 1 54  ? 77.647  32.711  68.470  1.00 55.02  ? 81  ARG A C     1 
ATOM   282  O  O     . ARG A 1 54  ? 76.532  32.198  68.621  1.00 59.70  ? 81  ARG A O     1 
ATOM   283  C  CB    . ARG A 1 54  ? 79.426  31.159  67.616  1.00 58.32  ? 81  ARG A CB    1 
ATOM   284  C  CG    . ARG A 1 54  ? 79.819  30.325  66.414  1.00 60.81  ? 81  ARG A CG    1 
ATOM   285  C  CD    . ARG A 1 54  ? 80.854  29.275  66.776  1.00 65.46  ? 81  ARG A CD    1 
ATOM   286  N  NE    . ARG A 1 54  ? 81.079  28.338  65.682  1.00 77.46  ? 81  ARG A NE    1 
ATOM   287  C  CZ    . ARG A 1 54  ? 82.084  27.474  65.629  1.00 77.60  ? 81  ARG A CZ    1 
ATOM   288  N  NH1   . ARG A 1 54  ? 82.993  27.411  66.588  1.00 75.62  ? 81  ARG A NH1   1 
ATOM   289  N  NH2   . ARG A 1 54  ? 82.181  26.655  64.585  1.00 82.52  ? 81  ARG A NH2   1 
ATOM   290  N  N     . GLU A 1 55  ? 78.144  33.591  69.340  1.00 56.84  ? 82  GLU A N     1 
ATOM   291  C  CA    . GLU A 1 55  ? 77.335  34.036  70.470  1.00 53.06  ? 82  GLU A CA    1 
ATOM   292  C  C     . GLU A 1 55  ? 76.158  34.894  70.021  1.00 52.26  ? 82  GLU A C     1 
ATOM   293  O  O     . GLU A 1 55  ? 75.221  35.105  70.800  1.00 61.01  ? 82  GLU A O     1 
ATOM   294  C  CB    . GLU A 1 55  ? 78.194  34.798  71.484  1.00 42.69  ? 82  GLU A CB    1 
ATOM   295  C  CG    . GLU A 1 55  ? 78.701  36.151  71.008  1.00 51.17  ? 82  GLU A CG    1 
ATOM   296  C  CD    . GLU A 1 55  ? 79.892  36.045  70.077  1.00 86.78  ? 82  GLU A CD    1 
ATOM   297  O  OE1   . GLU A 1 55  ? 80.270  34.911  69.712  1.00 88.79  ? 82  GLU A OE1   1 
ATOM   298  O  OE2   . GLU A 1 55  ? 80.456  37.098  69.710  1.00 89.66  ? 82  GLU A OE2   1 
ATOM   299  N  N     . ARG A 1 56  ? 76.191  35.394  68.786  1.00 48.78  ? 83  ARG A N     1 
ATOM   300  C  CA    . ARG A 1 56  ? 75.061  36.075  68.172  1.00 46.96  ? 83  ARG A CA    1 
ATOM   301  C  C     . ARG A 1 56  ? 74.272  35.151  67.252  1.00 56.51  ? 83  ARG A C     1 
ATOM   302  O  O     . ARG A 1 56  ? 73.474  35.625  66.435  1.00 45.83  ? 83  ARG A O     1 
ATOM   303  C  CB    . ARG A 1 56  ? 75.547  37.308  67.411  1.00 57.61  ? 83  ARG A CB    1 
ATOM   304  C  CG    . ARG A 1 56  ? 76.402  38.238  68.256  1.00 57.76  ? 83  ARG A CG    1 
ATOM   305  C  CD    . ARG A 1 56  ? 75.636  38.742  69.471  1.00 37.34  ? 83  ARG A CD    1 
ATOM   306  N  NE    . ARG A 1 56  ? 74.757  39.857  69.139  1.00 47.62  ? 83  ARG A NE    1 
ATOM   307  C  CZ    . ARG A 1 56  ? 74.004  40.507  70.017  1.00 49.75  ? 83  ARG A CZ    1 
ATOM   308  N  NH1   . ARG A 1 56  ? 73.985  40.169  71.296  1.00 49.54  ? 83  ARG A NH1   1 
ATOM   309  N  NH2   . ARG A 1 56  ? 73.253  41.523  69.601  1.00 57.04  ? 83  ARG A NH2   1 
ATOM   310  N  N     . THR A 1 57  ? 74.486  33.841  67.365  1.00 57.65  ? 84  THR A N     1 
ATOM   311  C  CA    . THR A 1 57  ? 73.813  32.843  66.547  1.00 45.27  ? 84  THR A CA    1 
ATOM   312  C  C     . THR A 1 57  ? 73.146  31.820  67.455  1.00 45.04  ? 84  THR A C     1 
ATOM   313  O  O     . THR A 1 57  ? 73.713  31.424  68.478  1.00 50.92  ? 84  THR A O     1 
ATOM   314  C  CB    . THR A 1 57  ? 74.799  32.139  65.599  1.00 50.15  ? 84  THR A CB    1 
ATOM   315  O  OG1   . THR A 1 57  ? 75.496  33.116  64.816  1.00 58.32  ? 84  THR A OG1   1 
ATOM   316  C  CG2   . THR A 1 57  ? 74.065  31.182  64.667  1.00 55.23  ? 84  THR A CG2   1 
ATOM   317  N  N     . ALA A 1 58  ? 71.938  31.405  67.085  1.00 51.42  ? 85  ALA A N     1 
ATOM   318  C  CA    . ALA A 1 58  ? 71.217  30.361  67.796  1.00 48.46  ? 85  ALA A CA    1 
ATOM   319  C  C     . ALA A 1 58  ? 70.768  29.301  66.802  1.00 44.58  ? 85  ALA A C     1 
ATOM   320  O  O     . ALA A 1 58  ? 70.595  29.573  65.612  1.00 44.04  ? 85  ALA A O     1 
ATOM   321  C  CB    . ALA A 1 58  ? 70.009  30.922  68.557  1.00 42.05  ? 85  ALA A CB    1 
ATOM   322  N  N     . LEU A 1 59  ? 70.574  28.084  67.305  1.00 41.66  ? 86  LEU A N     1 
ATOM   323  C  CA    . LEU A 1 59  ? 70.292  26.926  66.468  1.00 47.43  ? 86  LEU A CA    1 
ATOM   324  C  C     . LEU A 1 59  ? 68.927  26.343  66.804  1.00 48.39  ? 86  LEU A C     1 
ATOM   325  O  O     . LEU A 1 59  ? 68.565  26.215  67.978  1.00 57.20  ? 86  LEU A O     1 
ATOM   326  C  CB    . LEU A 1 59  ? 71.373  25.854  66.638  1.00 41.28  ? 86  LEU A CB    1 
ATOM   327  C  CG    . LEU A 1 59  ? 72.806  26.306  66.349  1.00 53.37  ? 86  LEU A CG    1 
ATOM   328  C  CD1   . LEU A 1 59  ? 73.783  25.174  66.610  1.00 46.05  ? 86  LEU A CD1   1 
ATOM   329  C  CD2   . LEU A 1 59  ? 72.933  26.807  64.919  1.00 47.49  ? 86  LEU A CD2   1 
ATOM   330  N  N     . TRP A 1 60  ? 68.179  25.989  65.761  1.00 46.95  ? 87  TRP A N     1 
ATOM   331  C  CA    . TRP A 1 60  ? 66.860  25.373  65.881  1.00 42.82  ? 87  TRP A CA    1 
ATOM   332  C  C     . TRP A 1 60  ? 66.820  24.209  64.901  1.00 51.55  ? 87  TRP A C     1 
ATOM   333  O  O     . TRP A 1 60  ? 66.776  24.421  63.685  1.00 50.50  ? 87  TRP A O     1 
ATOM   334  C  CB    . TRP A 1 60  ? 65.749  26.382  65.584  1.00 50.07  ? 87  TRP A CB    1 
ATOM   335  C  CG    . TRP A 1 60  ? 64.366  25.935  65.974  1.00 50.08  ? 87  TRP A CG    1 
ATOM   336  C  CD1   . TRP A 1 60  ? 63.691  26.261  67.117  1.00 46.42  ? 87  TRP A CD1   1 
ATOM   337  C  CD2   . TRP A 1 60  ? 63.484  25.095  65.216  1.00 47.48  ? 87  TRP A CD2   1 
ATOM   338  N  NE1   . TRP A 1 60  ? 62.449  25.673  67.118  1.00 43.43  ? 87  TRP A NE1   1 
ATOM   339  C  CE2   . TRP A 1 60  ? 62.297  24.951  65.963  1.00 46.85  ? 87  TRP A CE2   1 
ATOM   340  C  CE3   . TRP A 1 60  ? 63.585  24.448  63.981  1.00 43.92  ? 87  TRP A CE3   1 
ATOM   341  C  CZ2   . TRP A 1 60  ? 61.220  24.186  65.516  1.00 51.29  ? 87  TRP A CZ2   1 
ATOM   342  C  CZ3   . TRP A 1 60  ? 62.513  23.690  63.539  1.00 41.27  ? 87  TRP A CZ3   1 
ATOM   343  C  CH2   . TRP A 1 60  ? 61.347  23.566  64.304  1.00 42.33  ? 87  TRP A CH2   1 
ATOM   344  N  N     . VAL A 1 61  ? 66.844  22.986  65.423  1.00 53.20  ? 88  VAL A N     1 
ATOM   345  C  CA    . VAL A 1 61  ? 66.978  21.778  64.617  1.00 51.24  ? 88  VAL A CA    1 
ATOM   346  C  C     . VAL A 1 61  ? 65.806  20.853  64.907  1.00 51.90  ? 88  VAL A C     1 
ATOM   347  O  O     . VAL A 1 61  ? 65.533  20.531  66.069  1.00 58.45  ? 88  VAL A O     1 
ATOM   348  C  CB    . VAL A 1 61  ? 68.311  21.059  64.895  1.00 49.93  ? 88  VAL A CB    1 
ATOM   349  C  CG1   . VAL A 1 61  ? 68.446  19.846  63.996  1.00 41.67  ? 88  VAL A CG1   1 
ATOM   350  C  CG2   . VAL A 1 61  ? 69.478  22.012  64.702  1.00 48.79  ? 88  VAL A CG2   1 
ATOM   351  N  N     . ALA A 1 62  ? 65.129  20.415  63.848  1.00 47.99  ? 89  ALA A N     1 
ATOM   352  C  CA    . ALA A 1 62  ? 64.018  19.480  63.948  1.00 51.26  ? 89  ALA A CA    1 
ATOM   353  C  C     . ALA A 1 62  ? 64.240  18.348  62.958  1.00 59.40  ? 89  ALA A C     1 
ATOM   354  O  O     . ALA A 1 62  ? 64.451  18.597  61.767  1.00 58.57  ? 89  ALA A O     1 
ATOM   355  C  CB    . ALA A 1 62  ? 62.680  20.173  63.671  1.00 38.03  ? 89  ALA A CB    1 
ATOM   356  N  N     . THR A 1 63  ? 64.197  17.110  63.448  1.00 57.09  ? 90  THR A N     1 
ATOM   357  C  CA    . THR A 1 63  ? 64.357  15.934  62.605  1.00 49.90  ? 90  THR A CA    1 
ATOM   358  C  C     . THR A 1 63  ? 63.270  14.917  62.931  1.00 47.87  ? 90  THR A C     1 
ATOM   359  O  O     . THR A 1 63  ? 62.818  14.813  64.076  1.00 58.79  ? 90  THR A O     1 
ATOM   360  C  CB    . THR A 1 63  ? 65.755  15.302  62.769  1.00 46.97  ? 90  THR A CB    1 
ATOM   361  O  OG1   . THR A 1 63  ? 66.008  14.406  61.681  1.00 62.92  ? 90  THR A OG1   1 
ATOM   362  C  CG2   . THR A 1 63  ? 65.867  14.538  64.080  1.00 61.76  ? 90  THR A CG2   1 
ATOM   363  N  N     . ASP A 1 64  ? 62.840  14.185  61.904  1.00 48.61  ? 91  ASP A N     1 
ATOM   364  C  CA    . ASP A 1 64  ? 61.807  13.162  62.030  1.00 62.77  ? 91  ASP A CA    1 
ATOM   365  C  C     . ASP A 1 64  ? 61.681  12.433  60.700  1.00 51.48  ? 91  ASP A C     1 
ATOM   366  O  O     . ASP A 1 64  ? 62.168  12.905  59.668  1.00 49.45  ? 91  ASP A O     1 
ATOM   367  C  CB    . ASP A 1 64  ? 60.458  13.761  62.446  1.00 51.59  ? 91  ASP A CB    1 
ATOM   368  C  CG    . ASP A 1 64  ? 60.088  14.983  61.634  1.00 48.44  ? 91  ASP A CG    1 
ATOM   369  O  OD1   . ASP A 1 64  ? 59.591  14.822  60.500  1.00 55.98  ? 91  ASP A OD1   1 
ATOM   370  O  OD2   . ASP A 1 64  ? 60.300  16.113  62.125  1.00 54.34  ? 91  ASP A OD2   1 
ATOM   371  N  N     . HIS A 1 65  ? 61.020  11.274  60.742  1.00 56.81  ? 92  HIS A N     1 
ATOM   372  C  CA    . HIS A 1 65  ? 60.766  10.453  59.553  1.00 61.58  ? 92  HIS A CA    1 
ATOM   373  C  C     . HIS A 1 65  ? 62.066  10.085  58.839  1.00 58.68  ? 92  HIS A C     1 
ATOM   374  O  O     . HIS A 1 65  ? 62.192  10.209  57.619  1.00 60.97  ? 92  HIS A O     1 
ATOM   375  C  CB    . HIS A 1 65  ? 59.798  11.155  58.599  1.00 51.22  ? 92  HIS A CB    1 
ATOM   376  C  CG    . HIS A 1 65  ? 58.453  11.419  59.197  1.00 62.06  ? 92  HIS A CG    1 
ATOM   377  N  ND1   . HIS A 1 65  ? 58.137  12.605  59.823  1.00 51.69  ? 92  HIS A ND1   1 
ATOM   378  C  CD2   . HIS A 1 65  ? 57.349  10.641  59.282  1.00 65.56  ? 92  HIS A CD2   1 
ATOM   379  C  CE1   . HIS A 1 65  ? 56.891  12.550  60.259  1.00 48.98  ? 92  HIS A CE1   1 
ATOM   380  N  NE2   . HIS A 1 65  ? 56.390  11.369  59.944  1.00 55.45  ? 92  HIS A NE2   1 
ATOM   381  N  N     . ASN A 1 66  ? 63.039  9.619   59.616  1.00 61.82  ? 93  ASN A N     1 
ATOM   382  C  CA    . ASN A 1 66  ? 64.366  9.302   59.106  1.00 55.64  ? 93  ASN A CA    1 
ATOM   383  C  C     . ASN A 1 66  ? 64.502  7.800   58.895  1.00 65.11  ? 93  ASN A C     1 
ATOM   384  O  O     . ASN A 1 66  ? 64.253  7.013   59.814  1.00 72.74  ? 93  ASN A O     1 
ATOM   385  C  CB    . ASN A 1 66  ? 65.451  9.791   60.067  1.00 47.98  ? 93  ASN A CB    1 
ATOM   386  C  CG    . ASN A 1 66  ? 65.616  11.297  60.050  1.00 59.65  ? 93  ASN A CG    1 
ATOM   387  O  OD1   . ASN A 1 66  ? 65.617  11.922  58.989  1.00 66.70  ? 93  ASN A OD1   1 
ATOM   388  N  ND2   . ASN A 1 66  ? 65.763  11.890  61.230  1.00 59.10  ? 93  ASN A ND2   1 
ATOM   389  N  N     . MET A 1 67  ? 64.894  7.411   57.683  1.00 65.55  ? 94  MET A N     1 
ATOM   390  C  CA    . MET A 1 67  ? 65.272  6.035   57.394  1.00 64.30  ? 94  MET A CA    1 
ATOM   391  C  C     . MET A 1 67  ? 66.770  5.803   57.550  1.00 69.62  ? 94  MET A C     1 
ATOM   392  O  O     . MET A 1 67  ? 67.220  4.655   57.458  1.00 79.67  ? 94  MET A O     1 
ATOM   393  C  CB    . MET A 1 67  ? 64.827  5.654   55.975  1.00 53.57  ? 94  MET A CB    1 
ATOM   394  C  CG    . MET A 1 67  ? 64.658  4.158   55.737  1.00 89.45  ? 94  MET A CG    1 
ATOM   395  S  SD    . MET A 1 67  ? 63.313  3.432   56.696  1.00 93.64  ? 94  MET A SD    1 
ATOM   396  C  CE    . MET A 1 67  ? 61.917  4.373   56.084  1.00 72.66  ? 94  MET A CE    1 
ATOM   397  N  N     . ASP A 1 68  ? 67.544  6.859   57.790  1.00 70.90  ? 95  ASP A N     1 
ATOM   398  C  CA    . ASP A 1 68  ? 68.982  6.786   58.013  1.00 62.18  ? 95  ASP A CA    1 
ATOM   399  C  C     . ASP A 1 68  ? 69.303  7.292   59.422  1.00 59.86  ? 95  ASP A C     1 
ATOM   400  O  O     . ASP A 1 68  ? 68.408  7.534   60.238  1.00 74.11  ? 95  ASP A O     1 
ATOM   401  C  CB    . ASP A 1 68  ? 69.735  7.576   56.936  1.00 57.57  ? 95  ASP A CB    1 
ATOM   402  C  CG    . ASP A 1 68  ? 69.380  9.060   56.925  1.00 71.44  ? 95  ASP A CG    1 
ATOM   403  O  OD1   . ASP A 1 68  ? 68.509  9.488   57.715  1.00 72.96  ? 95  ASP A OD1   1 
ATOM   404  O  OD2   . ASP A 1 68  ? 69.980  9.805   56.117  1.00 68.62  ? 95  ASP A OD2   1 
ATOM   405  N  N     . ASN A 1 69  ? 70.595  7.465   59.700  1.00 61.31  ? 96  ASN A N     1 
ATOM   406  C  CA    . ASN A 1 69  ? 71.054  7.940   61.006  1.00 60.59  ? 96  ASN A CA    1 
ATOM   407  C  C     . ASN A 1 69  ? 71.165  9.458   61.069  1.00 60.51  ? 96  ASN A C     1 
ATOM   408  O  O     . ASN A 1 69  ? 72.099  9.995   61.672  1.00 68.89  ? 96  ASN A O     1 
ATOM   409  C  CB    . ASN A 1 69  ? 72.386  7.279   61.361  1.00 59.26  ? 96  ASN A CB    1 
ATOM   410  C  CG    . ASN A 1 69  ? 73.506  7.662   60.411  1.00 70.40  ? 96  ASN A CG    1 
ATOM   411  O  OD1   . ASN A 1 69  ? 73.265  8.053   59.270  1.00 64.56  ? 96  ASN A OD1   1 
ATOM   412  N  ND2   . ASN A 1 69  ? 74.744  7.546   60.881  1.00 62.83  ? 96  ASN A ND2   1 
ATOM   413  N  N     . THR A 1 70  ? 70.219  10.171  60.450  1.00 62.50  ? 97  THR A N     1 
ATOM   414  C  CA    . THR A 1 70  ? 70.211  11.629  60.527  1.00 49.44  ? 97  THR A CA    1 
ATOM   415  C  C     . THR A 1 70  ? 70.138  12.104  61.972  1.00 53.65  ? 97  THR A C     1 
ATOM   416  O  O     . THR A 1 70  ? 70.840  13.046  62.362  1.00 60.91  ? 97  THR A O     1 
ATOM   417  C  CB    . THR A 1 70  ? 69.035  12.193  59.724  1.00 53.96  ? 97  THR A CB    1 
ATOM   418  O  OG1   . THR A 1 70  ? 69.240  11.950  58.327  1.00 57.33  ? 97  THR A OG1   1 
ATOM   419  C  CG2   . THR A 1 70  ? 68.884  13.692  59.961  1.00 46.61  ? 97  THR A CG2   1 
ATOM   420  N  N     . SER A 1 71  ? 69.300  11.454  62.783  1.00 59.53  ? 98  SER A N     1 
ATOM   421  C  CA    . SER A 1 71  ? 69.127  11.870  64.170  1.00 49.87  ? 98  SER A CA    1 
ATOM   422  C  C     . SER A 1 71  ? 70.436  11.776  64.946  1.00 59.68  ? 98  SER A C     1 
ATOM   423  O  O     . SER A 1 71  ? 70.744  12.650  65.765  1.00 70.61  ? 98  SER A O     1 
ATOM   424  C  CB    . SER A 1 71  ? 68.045  11.020  64.834  1.00 62.86  ? 98  SER A CB    1 
ATOM   425  O  OG    . SER A 1 71  ? 67.620  11.594  66.057  1.00 88.16  ? 98  SER A OG    1 
ATOM   426  N  N     . THR A 1 72  ? 71.225  10.729  64.693  1.00 66.36  ? 99  THR A N     1 
ATOM   427  C  CA    . THR A 1 72  ? 72.466  10.543  65.439  1.00 58.99  ? 99  THR A CA    1 
ATOM   428  C  C     . THR A 1 72  ? 73.532  11.544  65.006  1.00 53.47  ? 99  THR A C     1 
ATOM   429  O  O     . THR A 1 72  ? 74.290  12.049  65.842  1.00 63.03  ? 99  THR A O     1 
ATOM   430  C  CB    . THR A 1 72  ? 72.971  9.111   65.265  1.00 65.09  ? 99  THR A CB    1 
ATOM   431  O  OG1   . THR A 1 72  ? 71.916  8.194   65.576  1.00 76.98  ? 99  THR A OG1   1 
ATOM   432  C  CG2   . THR A 1 72  ? 74.151  8.842   66.190  1.00 56.54  ? 99  THR A CG2   1 
ATOM   433  N  N     . VAL A 1 73  ? 73.607  11.842  63.707  1.00 51.62  ? 100 VAL A N     1 
ATOM   434  C  CA    . VAL A 1 73  ? 74.591  12.806  63.219  1.00 69.25  ? 100 VAL A CA    1 
ATOM   435  C  C     . VAL A 1 73  ? 74.309  14.189  63.793  1.00 65.14  ? 100 VAL A C     1 
ATOM   436  O  O     . VAL A 1 73  ? 75.216  14.881  64.271  1.00 65.80  ? 100 VAL A O     1 
ATOM   437  C  CB    . VAL A 1 73  ? 74.604  12.829  61.680  1.00 61.93  ? 100 VAL A CB    1 
ATOM   438  C  CG1   . VAL A 1 73  ? 75.587  13.870  61.169  1.00 62.06  ? 100 VAL A CG1   1 
ATOM   439  C  CG2   . VAL A 1 73  ? 74.946  11.453  61.131  1.00 56.72  ? 100 VAL A CG2   1 
ATOM   440  N  N     . LEU A 1 74  ? 73.044  14.614  63.748  1.00 62.10  ? 101 LEU A N     1 
ATOM   441  C  CA    . LEU A 1 74  ? 72.676  15.911  64.305  1.00 58.51  ? 101 LEU A CA    1 
ATOM   442  C  C     . LEU A 1 74  ? 72.976  15.980  65.796  1.00 62.05  ? 101 LEU A C     1 
ATOM   443  O  O     . LEU A 1 74  ? 73.500  16.987  66.286  1.00 69.48  ? 101 LEU A O     1 
ATOM   444  C  CB    . LEU A 1 74  ? 71.195  16.189  64.049  1.00 51.01  ? 101 LEU A CB    1 
ATOM   445  C  CG    . LEU A 1 74  ? 70.787  16.611  62.640  1.00 60.90  ? 101 LEU A CG    1 
ATOM   446  C  CD1   . LEU A 1 74  ? 69.277  16.588  62.512  1.00 50.85  ? 101 LEU A CD1   1 
ATOM   447  C  CD2   . LEU A 1 74  ? 71.328  17.997  62.335  1.00 38.78  ? 101 LEU A CD2   1 
ATOM   448  N  N     . ARG A 1 75  ? 72.653  14.916  66.534  1.00 57.57  ? 102 ARG A N     1 
ATOM   449  C  CA    . ARG A 1 75  ? 72.869  14.926  67.976  1.00 58.45  ? 102 ARG A CA    1 
ATOM   450  C  C     . ARG A 1 75  ? 74.354  14.979  68.313  1.00 58.52  ? 102 ARG A C     1 
ATOM   451  O  O     . ARG A 1 75  ? 74.756  15.671  69.254  1.00 69.21  ? 102 ARG A O     1 
ATOM   452  C  CB    . ARG A 1 75  ? 72.215  13.701  68.613  1.00 55.97  ? 102 ARG A CB    1 
ATOM   453  C  CG    . ARG A 1 75  ? 72.079  13.783  70.126  1.00 60.29  ? 102 ARG A CG    1 
ATOM   454  C  CD    . ARG A 1 75  ? 71.371  12.560  70.694  1.00 72.11  ? 102 ARG A CD    1 
ATOM   455  N  NE    . ARG A 1 75  ? 70.158  12.232  69.953  1.00 96.38  ? 102 ARG A NE    1 
ATOM   456  C  CZ    . ARG A 1 75  ? 70.040  11.202  69.124  1.00 98.86  ? 102 ARG A CZ    1 
ATOM   457  N  NH1   . ARG A 1 75  ? 71.039  10.355  68.925  1.00 89.09  ? 102 ARG A NH1   1 
ATOM   458  N  NH2   . ARG A 1 75  ? 68.892  11.016  68.480  1.00 91.14  ? 102 ARG A NH2   1 
ATOM   459  N  N     . GLU A 1 76  ? 75.184  14.259  67.556  1.00 61.34  ? 103 GLU A N     1 
ATOM   460  C  CA    . GLU A 1 76  ? 76.625  14.321  67.782  1.00 62.71  ? 103 GLU A CA    1 
ATOM   461  C  C     . GLU A 1 76  ? 77.155  15.727  67.538  1.00 69.78  ? 103 GLU A C     1 
ATOM   462  O  O     . GLU A 1 76  ? 77.985  16.231  68.306  1.00 76.23  ? 103 GLU A O     1 
ATOM   463  C  CB    . GLU A 1 76  ? 77.341  13.316  66.880  1.00 77.50  ? 103 GLU A CB    1 
ATOM   464  C  CG    . GLU A 1 76  ? 78.857  13.350  66.988  1.00 92.24  ? 103 GLU A CG    1 
ATOM   465  C  CD    . GLU A 1 76  ? 79.533  12.494  65.935  1.00 111.54 ? 103 GLU A CD    1 
ATOM   466  O  OE1   . GLU A 1 76  ? 78.857  12.119  64.953  1.00 113.20 ? 103 GLU A OE1   1 
ATOM   467  O  OE2   . GLU A 1 76  ? 80.737  12.195  66.089  1.00 103.27 ? 103 GLU A OE2   1 
ATOM   468  N  N     . TRP A 1 77  ? 76.680  16.378  66.476  1.00 62.30  ? 104 TRP A N     1 
ATOM   469  C  CA    . TRP A 1 77  ? 77.118  17.736  66.173  1.00 65.94  ? 104 TRP A CA    1 
ATOM   470  C  C     . TRP A 1 77  ? 76.628  18.724  67.224  1.00 55.97  ? 104 TRP A C     1 
ATOM   471  O  O     . TRP A 1 77  ? 77.394  19.578  67.683  1.00 60.62  ? 104 TRP A O     1 
ATOM   472  C  CB    . TRP A 1 77  ? 76.627  18.131  64.780  1.00 54.74  ? 104 TRP A CB    1 
ATOM   473  C  CG    . TRP A 1 77  ? 77.102  19.472  64.304  1.00 61.12  ? 104 TRP A CG    1 
ATOM   474  C  CD1   . TRP A 1 77  ? 78.363  19.799  63.895  1.00 68.05  ? 104 TRP A CD1   1 
ATOM   475  C  CD2   . TRP A 1 77  ? 76.314  20.661  64.161  1.00 51.39  ? 104 TRP A CD2   1 
ATOM   476  N  NE1   . TRP A 1 77  ? 78.412  21.120  63.519  1.00 64.29  ? 104 TRP A NE1   1 
ATOM   477  C  CE2   . TRP A 1 77  ? 77.167  21.672  63.672  1.00 52.92  ? 104 TRP A CE2   1 
ATOM   478  C  CE3   . TRP A 1 77  ? 74.972  20.970  64.404  1.00 55.63  ? 104 TRP A CE3   1 
ATOM   479  C  CZ2   . TRP A 1 77  ? 76.723  22.968  63.423  1.00 55.58  ? 104 TRP A CZ2   1 
ATOM   480  C  CZ3   . TRP A 1 77  ? 74.533  22.258  64.155  1.00 60.60  ? 104 TRP A CZ3   1 
ATOM   481  C  CH2   . TRP A 1 77  ? 75.406  23.240  63.670  1.00 56.45  ? 104 TRP A CH2   1 
ATOM   482  N  N     . LEU A 1 78  ? 75.358  18.616  67.627  1.00 55.43  ? 105 LEU A N     1 
ATOM   483  C  CA    . LEU A 1 78  ? 74.796  19.571  68.580  1.00 64.02  ? 105 LEU A CA    1 
ATOM   484  C  C     . LEU A 1 78  ? 75.486  19.486  69.935  1.00 66.05  ? 105 LEU A C     1 
ATOM   485  O  O     . LEU A 1 78  ? 75.768  20.516  70.560  1.00 61.48  ? 105 LEU A O     1 
ATOM   486  C  CB    . LEU A 1 78  ? 73.294  19.340  68.734  1.00 56.49  ? 105 LEU A CB    1 
ATOM   487  C  CG    . LEU A 1 78  ? 72.407  19.851  67.600  1.00 51.44  ? 105 LEU A CG    1 
ATOM   488  C  CD1   . LEU A 1 78  ? 70.950  19.590  67.925  1.00 50.90  ? 105 LEU A CD1   1 
ATOM   489  C  CD2   . LEU A 1 78  ? 72.648  21.331  67.361  1.00 49.15  ? 105 LEU A CD2   1 
ATOM   490  N  N     . VAL A 1 79  ? 75.756  18.268  70.414  1.00 61.86  ? 106 VAL A N     1 
ATOM   491  C  CA    . VAL A 1 79  ? 76.451  18.110  71.690  1.00 62.12  ? 106 VAL A CA    1 
ATOM   492  C  C     . VAL A 1 79  ? 77.825  18.764  71.636  1.00 61.11  ? 106 VAL A C     1 
ATOM   493  O  O     . VAL A 1 79  ? 78.296  19.325  72.633  1.00 71.29  ? 106 VAL A O     1 
ATOM   494  C  CB    . VAL A 1 79  ? 76.540  16.615  72.065  1.00 53.54  ? 106 VAL A CB    1 
ATOM   495  C  CG1   . VAL A 1 79  ? 77.463  16.403  73.259  1.00 56.49  ? 106 VAL A CG1   1 
ATOM   496  C  CG2   . VAL A 1 79  ? 75.156  16.060  72.369  1.00 53.72  ? 106 VAL A CG2   1 
ATOM   497  N  N     . ALA A 1 80  ? 78.474  18.735  70.473  1.00 64.23  ? 107 ALA A N     1 
ATOM   498  C  CA    . ALA A 1 80  ? 79.814  19.293  70.344  1.00 61.49  ? 107 ALA A CA    1 
ATOM   499  C  C     . ALA A 1 80  ? 79.819  20.801  70.127  1.00 67.65  ? 107 ALA A C     1 
ATOM   500  O  O     . ALA A 1 80  ? 80.831  21.447  70.421  1.00 80.69  ? 107 ALA A O     1 
ATOM   501  C  CB    . ALA A 1 80  ? 80.556  18.607  69.195  1.00 68.12  ? 107 ALA A CB    1 
ATOM   502  N  N     . VAL A 1 81  ? 78.725  21.378  69.630  1.00 53.86  ? 108 VAL A N     1 
ATOM   503  C  CA    . VAL A 1 81  ? 78.677  22.805  69.324  1.00 67.20  ? 108 VAL A CA    1 
ATOM   504  C  C     . VAL A 1 81  ? 77.788  23.592  70.274  1.00 60.96  ? 108 VAL A C     1 
ATOM   505  O  O     . VAL A 1 81  ? 77.758  24.829  70.177  1.00 66.29  ? 108 VAL A O     1 
ATOM   506  C  CB    . VAL A 1 81  ? 78.227  23.057  67.868  1.00 63.71  ? 108 VAL A CB    1 
ATOM   507  C  CG1   . VAL A 1 81  ? 79.094  22.275  66.898  1.00 54.21  ? 108 VAL A CG1   1 
ATOM   508  C  CG2   . VAL A 1 81  ? 76.756  22.703  67.697  1.00 52.58  ? 108 VAL A CG2   1 
ATOM   509  N  N     . LYS A 1 82  ? 77.069  22.929  71.183  1.00 65.12  ? 109 LYS A N     1 
ATOM   510  C  CA    . LYS A 1 82  ? 76.099  23.622  72.030  1.00 59.28  ? 109 LYS A CA    1 
ATOM   511  C  C     . LYS A 1 82  ? 76.743  24.771  72.800  1.00 67.27  ? 109 LYS A C     1 
ATOM   512  O  O     . LYS A 1 82  ? 76.220  25.891  72.826  1.00 67.26  ? 109 LYS A O     1 
ATOM   513  C  CB    . LYS A 1 82  ? 75.456  22.626  72.997  1.00 58.79  ? 109 LYS A CB    1 
ATOM   514  C  CG    . LYS A 1 82  ? 74.508  23.252  74.010  1.00 68.46  ? 109 LYS A CG    1 
ATOM   515  C  CD    . LYS A 1 82  ? 73.862  22.187  74.883  1.00 81.24  ? 109 LYS A CD    1 
ATOM   516  C  CE    . LYS A 1 82  ? 72.961  22.800  75.945  1.00 87.93  ? 109 LYS A CE    1 
ATOM   517  N  NZ    . LYS A 1 82  ? 71.835  23.573  75.349  1.00 81.27  ? 109 LYS A NZ    1 
ATOM   518  N  N     . SER A 1 83  ? 77.900  24.514  73.413  1.00 73.68  ? 110 SER A N     1 
ATOM   519  C  CA    . SER A 1 83  ? 78.518  25.456  74.341  1.00 64.34  ? 110 SER A CA    1 
ATOM   520  C  C     . SER A 1 83  ? 79.074  26.680  73.623  1.00 64.88  ? 110 SER A C     1 
ATOM   521  O  O     . SER A 1 83  ? 79.598  27.600  74.261  1.00 80.09  ? 110 SER A O     1 
ATOM   522  C  CB    . SER A 1 83  ? 79.635  24.774  75.133  1.00 59.17  ? 110 SER A CB    1 
ATOM   523  O  OG    . SER A 1 83  ? 80.707  24.403  74.283  1.00 73.23  ? 110 SER A OG    1 
ATOM   524  N  N     . LEU A 1 84  ? 78.964  26.703  72.298  1.00 57.64  ? 111 LEU A N     1 
ATOM   525  C  CA    . LEU A 1 84  ? 79.497  27.801  71.506  1.00 66.57  ? 111 LEU A CA    1 
ATOM   526  C  C     . LEU A 1 84  ? 78.424  28.769  71.026  1.00 64.38  ? 111 LEU A C     1 
ATOM   527  O  O     . LEU A 1 84  ? 78.759  29.875  70.589  1.00 65.70  ? 111 LEU A O     1 
ATOM   528  C  CB    . LEU A 1 84  ? 80.266  27.263  70.293  1.00 53.35  ? 111 LEU A CB    1 
ATOM   529  C  CG    . LEU A 1 84  ? 81.114  26.006  70.489  1.00 68.71  ? 111 LEU A CG    1 
ATOM   530  C  CD1   . LEU A 1 84  ? 81.776  25.629  69.176  1.00 72.14  ? 111 LEU A CD1   1 
ATOM   531  C  CD2   . LEU A 1 84  ? 82.155  26.206  71.581  1.00 76.72  ? 111 LEU A CD2   1 
ATOM   532  N  N     . TYR A 1 85  ? 77.154  28.388  71.094  1.00 61.84  ? 112 TYR A N     1 
ATOM   533  C  CA    . TYR A 1 85  ? 76.077  29.183  70.527  1.00 55.70  ? 112 TYR A CA    1 
ATOM   534  C  C     . TYR A 1 85  ? 75.168  29.732  71.620  1.00 60.59  ? 112 TYR A C     1 
ATOM   535  O  O     . TYR A 1 85  ? 75.162  29.256  72.759  1.00 56.75  ? 112 TYR A O     1 
ATOM   536  C  CB    . TYR A 1 85  ? 75.264  28.360  69.523  1.00 45.34  ? 112 TYR A CB    1 
ATOM   537  C  CG    . TYR A 1 85  ? 76.012  28.079  68.243  1.00 61.20  ? 112 TYR A CG    1 
ATOM   538  C  CD1   . TYR A 1 85  ? 76.946  27.057  68.173  1.00 59.68  ? 112 TYR A CD1   1 
ATOM   539  C  CD2   . TYR A 1 85  ? 75.792  28.843  67.107  1.00 50.20  ? 112 TYR A CD2   1 
ATOM   540  C  CE1   . TYR A 1 85  ? 77.639  26.800  67.007  1.00 59.88  ? 112 TYR A CE1   1 
ATOM   541  C  CE2   . TYR A 1 85  ? 76.480  28.594  65.938  1.00 60.75  ? 112 TYR A CE2   1 
ATOM   542  C  CZ    . TYR A 1 85  ? 77.401  27.572  65.892  1.00 49.30  ? 112 TYR A CZ    1 
ATOM   543  O  OH    . TYR A 1 85  ? 78.085  27.327  64.723  1.00 50.47  ? 112 TYR A OH    1 
ATOM   544  N  N     . HIS A 1 86  ? 74.397  30.757  71.246  1.00 54.73  ? 113 HIS A N     1 
ATOM   545  C  CA    . HIS A 1 86  ? 73.504  31.412  72.197  1.00 52.49  ? 113 HIS A CA    1 
ATOM   546  C  C     . HIS A 1 86  ? 72.509  30.423  72.792  1.00 49.74  ? 113 HIS A C     1 
ATOM   547  O  O     . HIS A 1 86  ? 72.287  30.401  74.009  1.00 50.11  ? 113 HIS A O     1 
ATOM   548  C  CB    . HIS A 1 86  ? 72.776  32.568  71.510  1.00 52.29  ? 113 HIS A CB    1 
ATOM   549  C  CG    . HIS A 1 86  ? 71.725  33.213  72.359  1.00 55.83  ? 113 HIS A CG    1 
ATOM   550  N  ND1   . HIS A 1 86  ? 72.019  34.144  73.332  1.00 47.81  ? 113 HIS A ND1   1 
ATOM   551  C  CD2   . HIS A 1 86  ? 70.379  33.064  72.375  1.00 46.29  ? 113 HIS A CD2   1 
ATOM   552  C  CE1   . HIS A 1 86  ? 70.900  34.540  73.913  1.00 46.39  ? 113 HIS A CE1   1 
ATOM   553  N  NE2   . HIS A 1 86  ? 69.891  33.899  73.351  1.00 59.21  ? 113 HIS A NE2   1 
ATOM   554  N  N     . SER A 1 87  ? 71.902  29.593  71.947  1.00 42.09  ? 114 SER A N     1 
ATOM   555  C  CA    . SER A 1 87  ? 70.960  28.586  72.412  1.00 47.90  ? 114 SER A CA    1 
ATOM   556  C  C     . SER A 1 87  ? 70.765  27.541  71.324  1.00 41.38  ? 114 SER A C     1 
ATOM   557  O  O     . SER A 1 87  ? 70.958  27.815  70.136  1.00 53.05  ? 114 SER A O     1 
ATOM   558  C  CB    . SER A 1 87  ? 69.612  29.206  72.796  1.00 44.80  ? 114 SER A CB    1 
ATOM   559  O  OG    . SER A 1 87  ? 68.953  29.726  71.656  1.00 67.68  ? 114 SER A OG    1 
ATOM   560  N  N     . VAL A 1 88  ? 70.379  26.341  71.751  1.00 48.21  ? 115 VAL A N     1 
ATOM   561  C  CA    . VAL A 1 88  ? 70.103  25.224  70.857  1.00 53.04  ? 115 VAL A CA    1 
ATOM   562  C  C     . VAL A 1 88  ? 68.734  24.660  71.207  1.00 46.32  ? 115 VAL A C     1 
ATOM   563  O  O     . VAL A 1 88  ? 68.459  24.370  72.378  1.00 53.06  ? 115 VAL A O     1 
ATOM   564  C  CB    . VAL A 1 88  ? 71.176  24.123  70.965  1.00 46.57  ? 115 VAL A CB    1 
ATOM   565  C  CG1   . VAL A 1 88  ? 70.794  22.924  70.109  1.00 56.24  ? 115 VAL A CG1   1 
ATOM   566  C  CG2   . VAL A 1 88  ? 72.540  24.663  70.565  1.00 51.46  ? 115 VAL A CG2   1 
ATOM   567  N  N     . GLU A 1 89  ? 67.877  24.512  70.200  1.00 47.74  ? 116 GLU A N     1 
ATOM   568  C  CA    . GLU A 1 89  ? 66.610  23.812  70.350  1.00 53.63  ? 116 GLU A CA    1 
ATOM   569  C  C     . GLU A 1 89  ? 66.638  22.571  69.472  1.00 60.38  ? 116 GLU A C     1 
ATOM   570  O  O     . GLU A 1 89  ? 67.021  22.643  68.299  1.00 57.44  ? 116 GLU A O     1 
ATOM   571  C  CB    . GLU A 1 89  ? 65.418  24.704  69.991  1.00 59.60  ? 116 GLU A CB    1 
ATOM   572  C  CG    . GLU A 1 89  ? 64.078  24.056  70.307  1.00 65.51  ? 116 GLU A CG    1 
ATOM   573  C  CD    . GLU A 1 89  ? 62.939  25.051  70.388  1.00 76.90  ? 116 GLU A CD    1 
ATOM   574  O  OE1   . GLU A 1 89  ? 63.200  26.270  70.296  1.00 74.96  ? 116 GLU A OE1   1 
ATOM   575  O  OE2   . GLU A 1 89  ? 61.780  24.609  70.549  1.00 76.85  ? 116 GLU A OE2   1 
ATOM   576  N  N     . TRP A 1 90  ? 66.227  21.441  70.043  1.00 50.87  ? 117 TRP A N     1 
ATOM   577  C  CA    . TRP A 1 90  ? 66.406  20.125  69.439  1.00 50.89  ? 117 TRP A CA    1 
ATOM   578  C  C     . TRP A 1 90  ? 65.087  19.374  69.547  1.00 60.78  ? 117 TRP A C     1 
ATOM   579  O  O     . TRP A 1 90  ? 64.638  19.060  70.653  1.00 71.78  ? 117 TRP A O     1 
ATOM   580  C  CB    . TRP A 1 90  ? 67.546  19.380  70.139  1.00 59.04  ? 117 TRP A CB    1 
ATOM   581  C  CG    . TRP A 1 90  ? 67.697  17.921  69.819  1.00 63.20  ? 117 TRP A CG    1 
ATOM   582  C  CD1   . TRP A 1 90  ? 67.680  16.889  70.710  1.00 47.55  ? 117 TRP A CD1   1 
ATOM   583  C  CD2   . TRP A 1 90  ? 67.918  17.333  68.530  1.00 58.96  ? 117 TRP A CD2   1 
ATOM   584  N  NE1   . TRP A 1 90  ? 67.868  15.695  70.058  1.00 69.38  ? 117 TRP A NE1   1 
ATOM   585  C  CE2   . TRP A 1 90  ? 68.015  15.940  68.718  1.00 72.81  ? 117 TRP A CE2   1 
ATOM   586  C  CE3   . TRP A 1 90  ? 68.035  17.848  67.236  1.00 65.43  ? 117 TRP A CE3   1 
ATOM   587  C  CZ2   . TRP A 1 90  ? 68.225  15.056  67.661  1.00 70.10  ? 117 TRP A CZ2   1 
ATOM   588  C  CZ3   . TRP A 1 90  ? 68.245  16.968  66.187  1.00 74.08  ? 117 TRP A CZ3   1 
ATOM   589  C  CH2   . TRP A 1 90  ? 68.337  15.588  66.407  1.00 67.94  ? 117 TRP A CH2   1 
ATOM   590  N  N     . ARG A 1 91  ? 64.459  19.102  68.399  1.00 56.52  ? 118 ARG A N     1 
ATOM   591  C  CA    . ARG A 1 91  ? 63.143  18.469  68.334  1.00 48.67  ? 118 ARG A CA    1 
ATOM   592  C  C     . ARG A 1 91  ? 63.244  17.205  67.488  1.00 65.23  ? 118 ARG A C     1 
ATOM   593  O  O     . ARG A 1 91  ? 62.899  17.211  66.296  1.00 60.60  ? 118 ARG A O     1 
ATOM   594  C  CB    . ARG A 1 91  ? 62.098  19.431  67.773  1.00 50.83  ? 118 ARG A CB    1 
ATOM   595  C  CG    . ARG A 1 91  ? 61.812  20.617  68.678  1.00 78.26  ? 118 ARG A CG    1 
ATOM   596  C  CD    . ARG A 1 91  ? 60.812  21.578  68.056  1.00 63.89  ? 118 ARG A CD    1 
ATOM   597  N  NE    . ARG A 1 91  ? 59.643  20.889  67.521  1.00 78.39  ? 118 ARG A NE    1 
ATOM   598  C  CZ    . ARG A 1 91  ? 58.462  21.460  67.325  1.00 87.98  ? 118 ARG A CZ    1 
ATOM   599  N  NH1   . ARG A 1 91  ? 58.242  22.723  67.654  1.00 64.59  ? 118 ARG A NH1   1 
ATOM   600  N  NH2   . ARG A 1 91  ? 57.476  20.743  66.792  1.00 66.72  ? 118 ARG A NH2   1 
ATOM   601  N  N     . PRO A 1 92  ? 63.716  16.106  68.065  1.00 64.71  ? 119 PRO A N     1 
ATOM   602  C  CA    . PRO A 1 92  ? 63.763  14.837  67.339  1.00 60.04  ? 119 PRO A CA    1 
ATOM   603  C  C     . PRO A 1 92  ? 62.459  14.059  67.486  1.00 59.43  ? 119 PRO A C     1 
ATOM   604  O  O     . PRO A 1 92  ? 61.621  14.345  68.344  1.00 72.21  ? 119 PRO A O     1 
ATOM   605  C  CB    . PRO A 1 92  ? 64.918  14.101  68.022  1.00 72.31  ? 119 PRO A CB    1 
ATOM   606  C  CG    . PRO A 1 92  ? 64.828  14.567  69.440  1.00 49.38  ? 119 PRO A CG    1 
ATOM   607  C  CD    . PRO A 1 92  ? 64.366  16.005  69.383  1.00 59.83  ? 119 PRO A CD    1 
ATOM   608  N  N     . ALA A 1 93  ? 62.305  13.054  66.618  1.00 66.42  ? 120 ALA A N     1 
ATOM   609  C  CA    . ALA A 1 93  ? 61.152  12.154  66.680  1.00 69.94  ? 120 ALA A CA    1 
ATOM   610  C  C     . ALA A 1 93  ? 61.531  10.902  65.891  1.00 62.05  ? 120 ALA A C     1 
ATOM   611  O  O     . ALA A 1 93  ? 61.539  10.929  64.658  1.00 64.55  ? 120 ALA A O     1 
ATOM   612  C  CB    . ALA A 1 93  ? 59.900  12.811  66.128  1.00 56.09  ? 120 ALA A CB    1 
ATOM   613  N  N     . GLU A 1 94  ? 61.835  9.817   66.607  1.00 67.39  ? 121 GLU A N     1 
ATOM   614  C  CA    . GLU A 1 94  ? 62.369  8.628   65.951  1.00 78.39  ? 121 GLU A CA    1 
ATOM   615  C  C     . GLU A 1 94  ? 61.284  7.834   65.234  1.00 70.67  ? 121 GLU A C     1 
ATOM   616  O  O     . GLU A 1 94  ? 61.530  7.285   64.155  1.00 69.54  ? 121 GLU A O     1 
ATOM   617  C  CB    . GLU A 1 94  ? 63.093  7.747   66.968  1.00 62.37  ? 121 GLU A CB    1 
ATOM   618  C  CG    . GLU A 1 94  ? 64.169  8.479   67.751  1.00 81.67  ? 121 GLU A CG    1 
ATOM   619  C  CD    . GLU A 1 94  ? 65.188  9.159   66.854  1.00 109.30 ? 121 GLU A CD    1 
ATOM   620  O  OE1   . GLU A 1 94  ? 65.622  8.536   65.861  1.00 113.54 ? 121 GLU A OE1   1 
ATOM   621  O  OE2   . GLU A 1 94  ? 65.550  10.321  67.139  1.00 91.69  ? 121 GLU A OE2   1 
ATOM   622  N  N     . GLU A 1 95  ? 60.086  7.754   65.809  1.00 67.30  ? 122 GLU A N     1 
ATOM   623  C  CA    . GLU A 1 95  ? 59.024  7.022   65.146  1.00 68.11  ? 122 GLU A CA    1 
ATOM   624  C  C     . GLU A 1 95  ? 57.846  7.938   64.837  1.00 70.18  ? 122 GLU A C     1 
ATOM   625  O  O     . GLU A 1 95  ? 57.524  8.825   65.635  1.00 78.07  ? 122 GLU A O     1 
ATOM   626  C  CB    . GLU A 1 95  ? 58.539  5.837   65.998  1.00 73.12  ? 122 GLU A CB    1 
ATOM   627  C  CG    . GLU A 1 95  ? 59.562  4.717   66.164  1.00 76.67  ? 122 GLU A CG    1 
ATOM   628  C  CD    . GLU A 1 95  ? 59.898  4.009   64.858  1.00 95.16  ? 122 GLU A CD    1 
ATOM   629  O  OE1   . GLU A 1 95  ? 59.187  4.218   63.851  1.00 101.42 ? 122 GLU A OE1   1 
ATOM   630  O  OE2   . GLU A 1 95  ? 60.879  3.237   64.838  1.00 97.00  ? 122 GLU A OE2   1 
ATOM   631  N  N     . PRO A 1 96  ? 57.183  7.748   63.689  1.00 71.10  ? 123 PRO A N     1 
ATOM   632  C  CA    . PRO A 1 96  ? 57.469  6.750   62.650  1.00 64.44  ? 123 PRO A CA    1 
ATOM   633  C  C     . PRO A 1 96  ? 58.623  7.186   61.756  1.00 66.14  ? 123 PRO A C     1 
ATOM   634  O  O     . PRO A 1 96  ? 59.072  8.327   61.828  1.00 75.07  ? 123 PRO A O     1 
ATOM   635  C  CB    . PRO A 1 96  ? 56.143  6.670   61.887  1.00 60.05  ? 123 PRO A CB    1 
ATOM   636  C  CG    . PRO A 1 96  ? 55.599  8.063   61.980  1.00 67.18  ? 123 PRO A CG    1 
ATOM   637  C  CD    . PRO A 1 96  ? 55.991  8.550   63.359  1.00 62.24  ? 123 PRO A CD    1 
ATOM   638  N  N     . ARG A 1 97  ? 59.130  6.298   60.906  1.00 66.13  ? 124 ARG A N     1 
ATOM   639  C  CA    . ARG A 1 97  ? 60.231  6.624   60.012  1.00 68.54  ? 124 ARG A CA    1 
ATOM   640  C  C     . ARG A 1 97  ? 59.769  6.921   58.593  1.00 64.44  ? 124 ARG A C     1 
ATOM   641  O  O     . ARG A 1 97  ? 60.601  7.225   57.733  1.00 70.21  ? 124 ARG A O     1 
ATOM   642  C  CB    . ARG A 1 97  ? 61.256  5.486   60.005  1.00 59.65  ? 124 ARG A CB    1 
ATOM   643  C  CG    . ARG A 1 97  ? 61.770  5.131   61.392  1.00 74.72  ? 124 ARG A CG    1 
ATOM   644  C  CD    . ARG A 1 97  ? 62.965  4.201   61.324  1.00 63.93  ? 124 ARG A CD    1 
ATOM   645  N  NE    . ARG A 1 97  ? 62.665  2.986   60.578  1.00 93.74  ? 124 ARG A NE    1 
ATOM   646  C  CZ    . ARG A 1 97  ? 63.558  2.052   60.282  1.00 111.54 ? 124 ARG A CZ    1 
ATOM   647  N  NH1   . ARG A 1 97  ? 64.823  2.161   60.658  1.00 108.30 ? 124 ARG A NH1   1 
ATOM   648  N  NH2   . ARG A 1 97  ? 63.175  0.983   59.589  1.00 98.78  ? 124 ARG A NH2   1 
ATOM   649  N  N     . SER A 1 98  ? 58.466  6.844   58.331  1.00 68.06  ? 125 SER A N     1 
ATOM   650  C  CA    . SER A 1 98  ? 57.901  7.216   57.044  1.00 58.13  ? 125 SER A CA    1 
ATOM   651  C  C     . SER A 1 98  ? 56.452  7.628   57.254  1.00 58.58  ? 125 SER A C     1 
ATOM   652  O  O     . SER A 1 98  ? 55.763  7.099   58.132  1.00 61.66  ? 125 SER A O     1 
ATOM   653  C  CB    . SER A 1 98  ? 58.001  6.071   56.027  1.00 56.54  ? 125 SER A CB    1 
ATOM   654  O  OG    . SER A 1 98  ? 57.528  4.852   56.570  1.00 78.60  ? 125 SER A OG    1 
ATOM   655  N  N     . TYR A 1 99  ? 56.001  8.586   56.451  1.00 61.24  ? 126 TYR A N     1 
ATOM   656  C  CA    . TYR A 1 99  ? 54.635  9.072   56.574  1.00 61.10  ? 126 TYR A CA    1 
ATOM   657  C  C     . TYR A 1 99  ? 53.646  7.989   56.146  1.00 62.44  ? 126 TYR A C     1 
ATOM   658  O  O     . TYR A 1 99  ? 53.912  7.242   55.199  1.00 73.32  ? 126 TYR A O     1 
ATOM   659  C  CB    . TYR A 1 99  ? 54.431  10.327  55.727  1.00 68.42  ? 126 TYR A CB    1 
ATOM   660  C  CG    . TYR A 1 99  ? 55.111  11.567  56.268  1.00 64.68  ? 126 TYR A CG    1 
ATOM   661  C  CD1   . TYR A 1 99  ? 56.433  11.856  55.946  1.00 51.37  ? 126 TYR A CD1   1 
ATOM   662  C  CD2   . TYR A 1 99  ? 54.429  12.455  57.093  1.00 50.75  ? 126 TYR A CD2   1 
ATOM   663  C  CE1   . TYR A 1 99  ? 57.057  12.989  56.433  1.00 51.91  ? 126 TYR A CE1   1 
ATOM   664  C  CE2   . TYR A 1 99  ? 55.045  13.591  57.586  1.00 48.69  ? 126 TYR A CE2   1 
ATOM   665  C  CZ    . TYR A 1 99  ? 56.357  13.853  57.252  1.00 53.93  ? 126 TYR A CZ    1 
ATOM   666  O  OH    . TYR A 1 99  ? 56.973  14.982  57.740  1.00 59.18  ? 126 TYR A OH    1 
ATOM   667  N  N     . PRO A 1 100 ? 52.497  7.878   56.821  1.00 71.39  ? 127 PRO A N     1 
ATOM   668  C  CA    . PRO A 1 100 ? 51.529  6.830   56.457  1.00 66.06  ? 127 PRO A CA    1 
ATOM   669  C  C     . PRO A 1 100 ? 50.888  7.023   55.092  1.00 66.20  ? 127 PRO A C     1 
ATOM   670  O  O     . PRO A 1 100 ? 50.372  6.050   54.531  1.00 82.17  ? 127 PRO A O     1 
ATOM   671  C  CB    . PRO A 1 100 ? 50.480  6.913   57.576  1.00 64.60  ? 127 PRO A CB    1 
ATOM   672  C  CG    . PRO A 1 100 ? 51.170  7.620   58.702  1.00 62.80  ? 127 PRO A CG    1 
ATOM   673  C  CD    . PRO A 1 100 ? 52.108  8.586   58.051  1.00 59.62  ? 127 PRO A CD    1 
ATOM   674  N  N     . ASP A 1 101 ? 50.899  8.237   54.539  1.00 69.96  ? 128 ASP A N     1 
ATOM   675  C  CA    . ASP A 1 101 ? 50.264  8.511   53.256  1.00 72.83  ? 128 ASP A CA    1 
ATOM   676  C  C     . ASP A 1 101 ? 51.279  8.738   52.140  1.00 68.17  ? 128 ASP A C     1 
ATOM   677  O  O     . ASP A 1 101 ? 50.925  9.276   51.086  1.00 67.68  ? 128 ASP A O     1 
ATOM   678  C  CB    . ASP A 1 101 ? 49.326  9.715   53.370  1.00 73.93  ? 128 ASP A CB    1 
ATOM   679  C  CG    . ASP A 1 101 ? 50.068  11.028  53.571  1.00 72.20  ? 128 ASP A CG    1 
ATOM   680  O  OD1   . ASP A 1 101 ? 51.216  11.002  54.062  1.00 71.08  ? 128 ASP A OD1   1 
ATOM   681  O  OD2   . ASP A 1 101 ? 49.498  12.090  53.239  1.00 76.60  ? 128 ASP A OD2   1 
ATOM   682  N  N     . GLU A 1 102 ? 52.530  8.337   52.344  1.00 65.49  ? 129 GLU A N     1 
ATOM   683  C  CA    . GLU A 1 102 ? 53.574  8.571   51.359  1.00 64.69  ? 129 GLU A CA    1 
ATOM   684  C  C     . GLU A 1 102 ? 53.693  7.393   50.399  1.00 68.15  ? 129 GLU A C     1 
ATOM   685  O  O     . GLU A 1 102 ? 53.369  6.249   50.736  1.00 61.35  ? 129 GLU A O     1 
ATOM   686  C  CB    . GLU A 1 102 ? 54.922  8.820   52.041  1.00 60.33  ? 129 GLU A CB    1 
ATOM   687  C  CG    . GLU A 1 102 ? 55.637  7.556   52.495  1.00 59.18  ? 129 GLU A CG    1 
ATOM   688  C  CD    . GLU A 1 102 ? 57.017  7.832   53.057  1.00 60.83  ? 129 GLU A CD    1 
ATOM   689  O  OE1   . GLU A 1 102 ? 57.163  8.801   53.833  1.00 62.68  ? 129 GLU A OE1   1 
ATOM   690  O  OE2   . GLU A 1 102 ? 57.958  7.085   52.716  1.00 64.88  ? 129 GLU A OE2   1 
ATOM   691  N  N     . GLU A 1 103 ? 54.154  7.692   49.187  1.00 70.41  ? 130 GLU A N     1 
ATOM   692  C  CA    . GLU A 1 103 ? 54.463  6.685   48.184  1.00 63.30  ? 130 GLU A CA    1 
ATOM   693  C  C     . GLU A 1 103 ? 55.958  6.418   48.084  1.00 59.09  ? 130 GLU A C     1 
ATOM   694  O  O     . GLU A 1 103 ? 56.371  5.533   47.331  1.00 70.38  ? 130 GLU A O     1 
ATOM   695  C  CB    . GLU A 1 103 ? 53.918  7.115   46.818  1.00 61.12  ? 130 GLU A CB    1 
ATOM   696  C  CG    . GLU A 1 103 ? 52.450  7.508   46.835  1.00 75.91  ? 130 GLU A CG    1 
ATOM   697  C  CD    . GLU A 1 103 ? 52.011  8.190   45.555  1.00 88.13  ? 130 GLU A CD    1 
ATOM   698  O  OE1   . GLU A 1 103 ? 52.830  8.274   44.615  1.00 72.96  ? 130 GLU A OE1   1 
ATOM   699  O  OE2   . GLU A 1 103 ? 50.847  8.643   45.492  1.00 88.42  ? 130 GLU A OE2   1 
ATOM   700  N  N     . GLY A 1 104 ? 56.769  7.167   48.823  1.00 57.21  ? 131 GLY A N     1 
ATOM   701  C  CA    . GLY A 1 104 ? 58.201  7.013   48.815  1.00 55.69  ? 131 GLY A CA    1 
ATOM   702  C  C     . GLY A 1 104 ? 58.845  8.063   49.694  1.00 56.01  ? 131 GLY A C     1 
ATOM   703  O  O     . GLY A 1 104 ? 58.189  9.004   50.153  1.00 59.74  ? 131 GLY A O     1 
ATOM   704  N  N     . PRO A 1 105 ? 60.147  7.920   49.956  1.00 61.53  ? 132 PRO A N     1 
ATOM   705  C  CA    . PRO A 1 105 ? 60.834  8.916   50.796  1.00 50.17  ? 132 PRO A CA    1 
ATOM   706  C  C     . PRO A 1 105 ? 60.982  10.274  50.126  1.00 63.33  ? 132 PRO A C     1 
ATOM   707  O  O     . PRO A 1 105 ? 61.110  11.285  50.829  1.00 48.92  ? 132 PRO A O     1 
ATOM   708  C  CB    . PRO A 1 105 ? 62.199  8.269   51.062  1.00 50.30  ? 132 PRO A CB    1 
ATOM   709  C  CG    . PRO A 1 105 ? 62.417  7.391   49.878  1.00 61.77  ? 132 PRO A CG    1 
ATOM   710  C  CD    . PRO A 1 105 ? 61.062  6.860   49.496  1.00 53.59  ? 132 PRO A CD    1 
ATOM   711  N  N     . LYS A 1 106 ? 60.961  10.335  48.795  1.00 56.17  ? 133 LYS A N     1 
ATOM   712  C  CA    . LYS A 1 106 ? 61.023  11.600  48.077  1.00 53.29  ? 133 LYS A CA    1 
ATOM   713  C  C     . LYS A 1 106 ? 59.652  12.073  47.615  1.00 54.97  ? 133 LYS A C     1 
ATOM   714  O  O     . LYS A 1 106 ? 59.564  13.042  46.856  1.00 64.23  ? 133 LYS A O     1 
ATOM   715  C  CB    . LYS A 1 106 ? 61.975  11.484  46.885  1.00 58.38  ? 133 LYS A CB    1 
ATOM   716  C  CG    . LYS A 1 106 ? 63.381  11.071  47.280  1.00 59.04  ? 133 LYS A CG    1 
ATOM   717  C  CD    . LYS A 1 106 ? 63.919  11.984  48.370  1.00 45.75  ? 133 LYS A CD    1 
ATOM   718  C  CE    . LYS A 1 106 ? 65.175  11.413  49.008  1.00 72.03  ? 133 LYS A CE    1 
ATOM   719  N  NZ    . LYS A 1 106 ? 65.650  12.239  50.156  1.00 69.22  ? 133 LYS A NZ    1 
ATOM   720  N  N     . HIS A 1 107 ? 58.585  11.415  48.058  1.00 62.19  ? 134 HIS A N     1 
ATOM   721  C  CA    . HIS A 1 107 ? 57.227  11.842  47.752  1.00 55.71  ? 134 HIS A CA    1 
ATOM   722  C  C     . HIS A 1 107 ? 56.768  12.861  48.785  1.00 55.77  ? 134 HIS A C     1 
ATOM   723  O  O     . HIS A 1 107 ? 56.927  12.647  49.992  1.00 57.91  ? 134 HIS A O     1 
ATOM   724  C  CB    . HIS A 1 107 ? 56.273  10.649  47.731  1.00 54.49  ? 134 HIS A CB    1 
ATOM   725  C  CG    . HIS A 1 107 ? 54.838  11.027  47.527  1.00 68.43  ? 134 HIS A CG    1 
ATOM   726  N  ND1   . HIS A 1 107 ? 53.810  10.465  48.254  1.00 63.95  ? 134 HIS A ND1   1 
ATOM   727  C  CD2   . HIS A 1 107 ? 54.259  11.907  46.675  1.00 57.37  ? 134 HIS A CD2   1 
ATOM   728  C  CE1   . HIS A 1 107 ? 52.660  10.983  47.861  1.00 61.22  ? 134 HIS A CE1   1 
ATOM   729  N  NE2   . HIS A 1 107 ? 52.905  11.861  46.904  1.00 56.20  ? 134 HIS A NE2   1 
ATOM   730  N  N     . TRP A 1 108 ? 56.194  13.965  48.311  1.00 59.31  ? 135 TRP A N     1 
ATOM   731  C  CA    . TRP A 1 108 ? 55.698  15.033  49.180  1.00 62.52  ? 135 TRP A CA    1 
ATOM   732  C  C     . TRP A 1 108 ? 54.178  14.924  49.250  1.00 62.80  ? 135 TRP A C     1 
ATOM   733  O  O     . TRP A 1 108 ? 53.456  15.500  48.436  1.00 69.62  ? 135 TRP A O     1 
ATOM   734  C  CB    . TRP A 1 108 ? 56.145  16.398  48.671  1.00 47.74  ? 135 TRP A CB    1 
ATOM   735  C  CG    . TRP A 1 108 ? 57.563  16.721  49.001  1.00 55.29  ? 135 TRP A CG    1 
ATOM   736  C  CD1   . TRP A 1 108 ? 58.674  16.330  48.316  1.00 57.91  ? 135 TRP A CD1   1 
ATOM   737  C  CD2   . TRP A 1 108 ? 58.028  17.507  50.105  1.00 61.19  ? 135 TRP A CD2   1 
ATOM   738  N  NE1   . TRP A 1 108 ? 59.804  16.823  48.925  1.00 66.86  ? 135 TRP A NE1   1 
ATOM   739  C  CE2   . TRP A 1 108 ? 59.433  17.549  50.026  1.00 51.53  ? 135 TRP A CE2   1 
ATOM   740  C  CE3   . TRP A 1 108 ? 57.390  18.179  51.152  1.00 57.05  ? 135 TRP A CE3   1 
ATOM   741  C  CZ2   . TRP A 1 108 ? 60.213  18.236  50.956  1.00 54.89  ? 135 TRP A CZ2   1 
ATOM   742  C  CZ3   . TRP A 1 108 ? 58.164  18.860  52.072  1.00 55.87  ? 135 TRP A CZ3   1 
ATOM   743  C  CH2   . TRP A 1 108 ? 59.561  18.883  51.969  1.00 49.17  ? 135 TRP A CH2   1 
ATOM   744  N  N     . SER A 1 109 ? 53.693  14.175  50.235  1.00 57.41  ? 136 SER A N     1 
ATOM   745  C  CA    . SER A 1 109 ? 52.266  14.055  50.480  1.00 63.59  ? 136 SER A CA    1 
ATOM   746  C  C     . SER A 1 109 ? 51.779  15.221  51.340  1.00 66.19  ? 136 SER A C     1 
ATOM   747  O  O     . SER A 1 109 ? 52.567  15.982  51.904  1.00 62.75  ? 136 SER A O     1 
ATOM   748  C  CB    . SER A 1 109 ? 51.944  12.722  51.153  1.00 62.09  ? 136 SER A CB    1 
ATOM   749  O  OG    . SER A 1 109 ? 52.426  12.696  52.487  1.00 63.25  ? 136 SER A OG    1 
ATOM   750  N  N     . ASP A 1 110 ? 50.453  15.351  51.438  1.00 61.15  ? 137 ASP A N     1 
ATOM   751  C  CA    . ASP A 1 110 ? 49.872  16.456  52.195  1.00 64.75  ? 137 ASP A CA    1 
ATOM   752  C  C     . ASP A 1 110 ? 50.290  16.410  53.659  1.00 68.37  ? 137 ASP A C     1 
ATOM   753  O  O     . ASP A 1 110 ? 50.476  17.458  54.290  1.00 60.97  ? 137 ASP A O     1 
ATOM   754  C  CB    . ASP A 1 110 ? 48.347  16.435  52.069  1.00 71.28  ? 137 ASP A CB    1 
ATOM   755  C  CG    . ASP A 1 110 ? 47.870  16.851  50.691  1.00 77.88  ? 137 ASP A CG    1 
ATOM   756  O  OD1   . ASP A 1 110 ? 48.709  17.308  49.885  1.00 75.69  ? 137 ASP A OD1   1 
ATOM   757  O  OD2   . ASP A 1 110 ? 46.660  16.722  50.413  1.00 85.20  ? 137 ASP A OD2   1 
ATOM   758  N  N     . SER A 1 111 ? 50.447  15.206  54.214  1.00 60.55  ? 138 SER A N     1 
ATOM   759  C  CA    . SER A 1 111 ? 50.919  15.084  55.590  1.00 54.87  ? 138 SER A CA    1 
ATOM   760  C  C     . SER A 1 111 ? 52.338  15.618  55.731  1.00 61.82  ? 138 SER A C     1 
ATOM   761  O  O     . SER A 1 111 ? 52.660  16.290  56.718  1.00 61.99  ? 138 SER A O     1 
ATOM   762  C  CB    . SER A 1 111 ? 50.846  13.626  56.045  1.00 54.10  ? 138 SER A CB    1 
ATOM   763  O  OG    . SER A 1 111 ? 49.516  13.142  55.994  1.00 74.27  ? 138 SER A OG    1 
ATOM   764  N  N     . ARG A 1 112 ? 53.199  15.334  54.750  1.00 55.74  ? 139 ARG A N     1 
ATOM   765  C  CA    . ARG A 1 112 ? 54.565  15.847  54.781  1.00 63.79  ? 139 ARG A CA    1 
ATOM   766  C  C     . ARG A 1 112 ? 54.582  17.363  54.621  1.00 59.69  ? 139 ARG A C     1 
ATOM   767  O  O     . ARG A 1 112 ? 55.293  18.066  55.350  1.00 57.01  ? 139 ARG A O     1 
ATOM   768  C  CB    . ARG A 1 112 ? 55.398  15.176  53.687  1.00 60.77  ? 139 ARG A CB    1 
ATOM   769  C  CG    . ARG A 1 112 ? 56.877  15.524  53.716  1.00 49.28  ? 139 ARG A CG    1 
ATOM   770  C  CD    . ARG A 1 112 ? 57.611  14.844  52.570  1.00 52.67  ? 139 ARG A CD    1 
ATOM   771  N  NE    . ARG A 1 112 ? 59.053  15.042  52.638  1.00 56.96  ? 139 ARG A NE    1 
ATOM   772  C  CZ    . ARG A 1 112 ? 59.919  14.573  51.750  1.00 59.65  ? 139 ARG A CZ    1 
ATOM   773  N  NH1   . ARG A 1 112 ? 59.524  13.861  50.707  1.00 48.40  ? 139 ARG A NH1   1 
ATOM   774  N  NH2   . ARG A 1 112 ? 61.215  14.826  51.911  1.00 50.74  ? 139 ARG A NH2   1 
ATOM   775  N  N     . TYR A 1 113 ? 53.798  17.883  53.673  1.00 54.63  ? 140 TYR A N     1 
ATOM   776  C  CA    . TYR A 1 113 ? 53.696  19.328  53.487  1.00 54.55  ? 140 TYR A CA    1 
ATOM   777  C  C     . TYR A 1 113 ? 53.212  20.012  54.759  1.00 56.49  ? 140 TYR A C     1 
ATOM   778  O  O     . TYR A 1 113 ? 53.788  21.015  55.196  1.00 55.34  ? 140 TYR A O     1 
ATOM   779  C  CB    . TYR A 1 113 ? 52.751  19.639  52.326  1.00 57.49  ? 140 TYR A CB    1 
ATOM   780  C  CG    . TYR A 1 113 ? 53.406  19.687  50.963  1.00 56.26  ? 140 TYR A CG    1 
ATOM   781  C  CD1   . TYR A 1 113 ? 54.623  20.329  50.774  1.00 55.70  ? 140 TYR A CD1   1 
ATOM   782  C  CD2   . TYR A 1 113 ? 52.800  19.096  49.863  1.00 56.76  ? 140 TYR A CD2   1 
ATOM   783  C  CE1   . TYR A 1 113 ? 55.217  20.379  49.525  1.00 60.08  ? 140 TYR A CE1   1 
ATOM   784  C  CE2   . TYR A 1 113 ? 53.384  19.141  48.614  1.00 55.29  ? 140 TYR A CE2   1 
ATOM   785  C  CZ    . TYR A 1 113 ? 54.591  19.782  48.449  1.00 60.33  ? 140 TYR A CZ    1 
ATOM   786  O  OH    . TYR A 1 113 ? 55.176  19.826  47.203  1.00 71.27  ? 140 TYR A OH    1 
ATOM   787  N  N     . GLU A 1 114 ? 52.151  19.478  55.370  1.00 57.72  ? 141 GLU A N     1 
ATOM   788  C  CA    . GLU A 1 114 ? 51.605  20.094  56.575  1.00 58.92  ? 141 GLU A CA    1 
ATOM   789  C  C     . GLU A 1 114 ? 52.621  20.086  57.710  1.00 58.65  ? 141 GLU A C     1 
ATOM   790  O  O     . GLU A 1 114 ? 52.766  21.081  58.430  1.00 50.50  ? 141 GLU A O     1 
ATOM   791  C  CB    . GLU A 1 114 ? 50.323  19.378  57.001  1.00 56.44  ? 141 GLU A CB    1 
ATOM   792  C  CG    . GLU A 1 114 ? 49.736  19.890  58.310  1.00 67.06  ? 141 GLU A CG    1 
ATOM   793  C  CD    . GLU A 1 114 ? 48.474  19.152  58.714  1.00 74.34  ? 141 GLU A CD    1 
ATOM   794  O  OE1   . GLU A 1 114 ? 48.050  18.240  57.972  1.00 101.65 ? 141 GLU A OE1   1 
ATOM   795  O  OE2   . GLU A 1 114 ? 47.906  19.484  59.775  1.00 98.24  ? 141 GLU A OE2   1 
ATOM   796  N  N     . HIS A 1 115 ? 53.341  18.976  57.880  1.00 48.77  ? 142 HIS A N     1 
ATOM   797  C  CA    . HIS A 1 115 ? 54.323  18.889  58.957  1.00 45.56  ? 142 HIS A CA    1 
ATOM   798  C  C     . HIS A 1 115 ? 55.477  19.856  58.726  1.00 55.02  ? 142 HIS A C     1 
ATOM   799  O  O     . HIS A 1 115 ? 55.908  20.557  59.650  1.00 54.39  ? 142 HIS A O     1 
ATOM   800  C  CB    . HIS A 1 115 ? 54.838  17.455  59.086  1.00 48.07  ? 142 HIS A CB    1 
ATOM   801  C  CG    . HIS A 1 115 ? 55.782  17.253  60.231  1.00 52.39  ? 142 HIS A CG    1 
ATOM   802  N  ND1   . HIS A 1 115 ? 55.429  17.504  61.539  1.00 50.75  ? 142 HIS A ND1   1 
ATOM   803  C  CD2   . HIS A 1 115 ? 57.067  16.826  60.264  1.00 48.06  ? 142 HIS A CD2   1 
ATOM   804  C  CE1   . HIS A 1 115 ? 56.455  17.241  62.329  1.00 53.71  ? 142 HIS A CE1   1 
ATOM   805  N  NE2   . HIS A 1 115 ? 57.461  16.828  61.579  1.00 62.45  ? 142 HIS A NE2   1 
ATOM   806  N  N     . VAL A 1 116 ? 55.992  19.907  57.495  1.00 53.19  ? 143 VAL A N     1 
ATOM   807  C  CA    . VAL A 1 116 ? 57.098  20.810  57.182  1.00 53.22  ? 143 VAL A CA    1 
ATOM   808  C  C     . VAL A 1 116 ? 56.678  22.257  57.403  1.00 54.08  ? 143 VAL A C     1 
ATOM   809  O  O     . VAL A 1 116 ? 57.416  23.052  57.998  1.00 50.95  ? 143 VAL A O     1 
ATOM   810  C  CB    . VAL A 1 116 ? 57.590  20.578  55.743  1.00 55.45  ? 143 VAL A CB    1 
ATOM   811  C  CG1   . VAL A 1 116 ? 58.498  21.714  55.304  1.00 40.79  ? 143 VAL A CG1   1 
ATOM   812  C  CG2   . VAL A 1 116 ? 58.319  19.253  55.647  1.00 39.61  ? 143 VAL A CG2   1 
ATOM   813  N  N     . MET A 1 117 ? 55.481  22.619  56.926  1.00 56.70  ? 144 MET A N     1 
ATOM   814  C  CA    . MET A 1 117 ? 54.962  23.964  57.156  1.00 45.60  ? 144 MET A CA    1 
ATOM   815  C  C     . MET A 1 117 ? 54.875  24.276  58.643  1.00 40.63  ? 144 MET A C     1 
ATOM   816  O  O     . MET A 1 117 ? 55.259  25.367  59.080  1.00 50.71  ? 144 MET A O     1 
ATOM   817  C  CB    . MET A 1 117 ? 53.588  24.127  56.504  1.00 43.31  ? 144 MET A CB    1 
ATOM   818  C  CG    . MET A 1 117 ? 53.619  24.261  54.994  1.00 55.70  ? 144 MET A CG    1 
ATOM   819  S  SD    . MET A 1 117 ? 52.012  24.720  54.314  1.00 56.96  ? 144 MET A SD    1 
ATOM   820  C  CE    . MET A 1 117 ? 51.539  23.205  53.484  1.00 50.96  ? 144 MET A CE    1 
ATOM   821  N  N     . LYS A 1 118 ? 54.375  23.326  59.439  1.00 52.25  ? 145 LYS A N     1 
ATOM   822  C  CA    . LYS A 1 118 ? 54.279  23.547  60.877  1.00 45.48  ? 145 LYS A CA    1 
ATOM   823  C  C     . LYS A 1 118 ? 55.651  23.678  61.526  1.00 46.98  ? 145 LYS A C     1 
ATOM   824  O  O     . LYS A 1 118 ? 55.807  24.434  62.492  1.00 42.99  ? 145 LYS A O     1 
ATOM   825  C  CB    . LYS A 1 118 ? 53.487  22.412  61.529  1.00 43.42  ? 145 LYS A CB    1 
ATOM   826  C  CG    . LYS A 1 118 ? 51.994  22.452  61.231  1.00 50.81  ? 145 LYS A CG    1 
ATOM   827  C  CD    . LYS A 1 118 ? 51.233  21.455  62.091  1.00 47.58  ? 145 LYS A CD    1 
ATOM   828  C  CE    . LYS A 1 118 ? 49.743  21.503  61.794  1.00 49.79  ? 145 LYS A CE    1 
ATOM   829  N  NZ    . LYS A 1 118 ? 48.976  20.536  62.626  1.00 68.35  ? 145 LYS A NZ    1 
ATOM   830  N  N     . LEU A 1 119 ? 56.655  22.968  61.012  1.00 44.02  ? 146 LEU A N     1 
ATOM   831  C  CA    . LEU A 1 119 ? 57.994  23.084  61.578  1.00 46.21  ? 146 LEU A CA    1 
ATOM   832  C  C     . LEU A 1 119 ? 58.573  24.471  61.332  1.00 51.86  ? 146 LEU A C     1 
ATOM   833  O  O     . LEU A 1 119 ? 59.150  25.082  62.238  1.00 49.90  ? 146 LEU A O     1 
ATOM   834  C  CB    . LEU A 1 119 ? 58.904  22.005  60.998  1.00 44.77  ? 146 LEU A CB    1 
ATOM   835  C  CG    . LEU A 1 119 ? 58.586  20.581  61.454  1.00 51.08  ? 146 LEU A CG    1 
ATOM   836  C  CD1   . LEU A 1 119 ? 59.497  19.581  60.765  1.00 51.33  ? 146 LEU A CD1   1 
ATOM   837  C  CD2   . LEU A 1 119 ? 58.704  20.469  62.964  1.00 47.27  ? 146 LEU A CD2   1 
ATOM   838  N  N     . ARG A 1 120 ? 58.427  24.989  60.109  1.00 44.42  ? 147 ARG A N     1 
ATOM   839  C  CA    . ARG A 1 120 ? 58.937  26.325  59.819  1.00 41.74  ? 147 ARG A CA    1 
ATOM   840  C  C     . ARG A 1 120 ? 58.179  27.389  60.604  1.00 41.40  ? 147 ARG A C     1 
ATOM   841  O  O     . ARG A 1 120 ? 58.770  28.381  61.045  1.00 52.76  ? 147 ARG A O     1 
ATOM   842  C  CB    . ARG A 1 120 ? 58.866  26.605  58.318  1.00 39.65  ? 147 ARG A CB    1 
ATOM   843  C  CG    . ARG A 1 120 ? 59.703  25.654  57.487  1.00 42.22  ? 147 ARG A CG    1 
ATOM   844  C  CD    . ARG A 1 120 ? 60.195  26.314  56.215  1.00 45.65  ? 147 ARG A CD    1 
ATOM   845  N  NE    . ARG A 1 120 ? 60.951  25.379  55.390  1.00 42.43  ? 147 ARG A NE    1 
ATOM   846  C  CZ    . ARG A 1 120 ? 60.443  24.705  54.368  1.00 47.65  ? 147 ARG A CZ    1 
ATOM   847  N  NH1   . ARG A 1 120 ? 59.185  24.864  53.991  1.00 55.44  ? 147 ARG A NH1   1 
ATOM   848  N  NH2   . ARG A 1 120 ? 61.218  23.849  53.707  1.00 44.45  ? 147 ARG A NH2   1 
ATOM   849  N  N     . GLN A 1 121 ? 56.870  27.202  60.789  1.00 47.62  ? 148 GLN A N     1 
ATOM   850  C  CA    . GLN A 1 121 ? 56.113  28.111  61.645  1.00 47.44  ? 148 GLN A CA    1 
ATOM   851  C  C     . GLN A 1 121 ? 56.597  28.029  63.086  1.00 48.69  ? 148 GLN A C     1 
ATOM   852  O  O     . GLN A 1 121 ? 56.705  29.051  63.774  1.00 48.53  ? 148 GLN A O     1 
ATOM   853  C  CB    . GLN A 1 121 ? 54.618  27.793  61.566  1.00 42.08  ? 148 GLN A CB    1 
ATOM   854  C  CG    . GLN A 1 121 ? 53.732  28.775  62.323  1.00 40.48  ? 148 GLN A CG    1 
ATOM   855  C  CD    . GLN A 1 121 ? 53.756  30.162  61.715  1.00 40.00  ? 148 GLN A CD    1 
ATOM   856  O  OE1   . GLN A 1 121 ? 53.939  30.318  60.507  1.00 43.49  ? 148 GLN A OE1   1 
ATOM   857  N  NE2   . GLN A 1 121 ? 53.578  31.179  62.549  1.00 40.38  ? 148 GLN A NE2   1 
ATOM   858  N  N     . ALA A 1 122 ? 56.890  26.815  63.559  1.00 44.57  ? 149 ALA A N     1 
ATOM   859  C  CA    . ALA A 1 122 ? 57.420  26.647  64.907  1.00 42.31  ? 149 ALA A CA    1 
ATOM   860  C  C     . ALA A 1 122 ? 58.771  27.334  65.050  1.00 45.67  ? 149 ALA A C     1 
ATOM   861  O  O     . ALA A 1 122 ? 59.029  28.027  66.041  1.00 45.14  ? 149 ALA A O     1 
ATOM   862  C  CB    . ALA A 1 122 ? 57.531  25.160  65.241  1.00 39.09  ? 149 ALA A CB    1 
ATOM   863  N  N     . ALA A 1 123 ? 59.648  27.155  64.059  1.00 42.80  ? 150 ALA A N     1 
ATOM   864  C  CA    . ALA A 1 123 ? 60.941  27.830  64.084  1.00 48.02  ? 150 ALA A CA    1 
ATOM   865  C  C     . ALA A 1 123 ? 60.773  29.345  64.059  1.00 49.48  ? 150 ALA A C     1 
ATOM   866  O  O     . ALA A 1 123 ? 61.507  30.070  64.742  1.00 47.34  ? 150 ALA A O     1 
ATOM   867  C  CB    . ALA A 1 123 ? 61.796  27.363  62.908  1.00 33.44  ? 150 ALA A CB    1 
ATOM   868  N  N     . LEU A 1 124 ? 59.810  29.843  63.280  1.00 44.06  ? 151 LEU A N     1 
ATOM   869  C  CA    . LEU A 1 124 ? 59.555  31.279  63.244  1.00 37.75  ? 151 LEU A CA    1 
ATOM   870  C  C     . LEU A 1 124 ? 59.068  31.780  64.598  1.00 43.46  ? 151 LEU A C     1 
ATOM   871  O  O     . LEU A 1 124 ? 59.524  32.818  65.091  1.00 48.01  ? 151 LEU A O     1 
ATOM   872  C  CB    . LEU A 1 124 ? 58.537  31.601  62.151  1.00 42.41  ? 151 LEU A CB    1 
ATOM   873  C  CG    . LEU A 1 124 ? 58.201  33.075  61.926  1.00 44.09  ? 151 LEU A CG    1 
ATOM   874  C  CD1   . LEU A 1 124 ? 59.430  33.844  61.472  1.00 33.80  ? 151 LEU A CD1   1 
ATOM   875  C  CD2   . LEU A 1 124 ? 57.085  33.200  60.909  1.00 35.84  ? 151 LEU A CD2   1 
ATOM   876  N  N     . LYS A 1 125 ? 58.138  31.047  65.216  1.00 40.94  ? 152 LYS A N     1 
ATOM   877  C  CA    . LYS A 1 125 ? 57.660  31.425  66.542  1.00 41.77  ? 152 LYS A CA    1 
ATOM   878  C  C     . LYS A 1 125 ? 58.793  31.407  67.558  1.00 39.70  ? 152 LYS A C     1 
ATOM   879  O  O     . LYS A 1 125 ? 58.867  32.278  68.433  1.00 38.99  ? 152 LYS A O     1 
ATOM   880  C  CB    . LYS A 1 125 ? 56.529  30.492  66.979  1.00 39.24  ? 152 LYS A CB    1 
ATOM   881  C  CG    . LYS A 1 125 ? 56.050  30.721  68.407  1.00 40.86  ? 152 LYS A CG    1 
ATOM   882  C  CD    . LYS A 1 125 ? 54.829  29.877  68.740  1.00 42.80  ? 152 LYS A CD    1 
ATOM   883  C  CE    . LYS A 1 125 ? 54.537  29.892  70.235  1.00 44.63  ? 152 LYS A CE    1 
ATOM   884  N  NZ    . LYS A 1 125 ? 54.327  31.268  70.763  1.00 51.30  ? 152 LYS A NZ    1 
ATOM   885  N  N     . SER A 1 126 ? 59.689  30.422  67.455  1.00 36.68  ? 153 SER A N     1 
ATOM   886  C  CA    . SER A 1 126 ? 60.863  30.392  68.323  1.00 42.01  ? 153 SER A CA    1 
ATOM   887  C  C     . SER A 1 126 ? 61.705  31.647  68.143  1.00 44.34  ? 153 SER A C     1 
ATOM   888  O  O     . SER A 1 126 ? 62.050  32.324  69.119  1.00 45.78  ? 153 SER A O     1 
ATOM   889  C  CB    . SER A 1 126 ? 61.697  29.142  68.038  1.00 41.36  ? 153 SER A CB    1 
ATOM   890  O  OG    . SER A 1 126 ? 61.060  27.975  68.526  1.00 55.43  ? 153 SER A OG    1 
ATOM   891  N  N     . ALA A 1 127 ? 62.040  31.975  66.892  1.00 41.69  ? 154 ALA A N     1 
ATOM   892  C  CA    . ALA A 1 127 ? 62.862  33.149  66.626  1.00 42.30  ? 154 ALA A CA    1 
ATOM   893  C  C     . ALA A 1 127 ? 62.220  34.415  67.182  1.00 40.09  ? 154 ALA A C     1 
ATOM   894  O  O     . ALA A 1 127 ? 62.905  35.263  67.765  1.00 41.45  ? 154 ALA A O     1 
ATOM   895  C  CB    . ALA A 1 127 ? 63.107  33.279  65.124  1.00 46.75  ? 154 ALA A CB    1 
ATOM   896  N  N     . ARG A 1 128 ? 60.903  34.554  67.021  1.00 42.34  ? 155 ARG A N     1 
ATOM   897  C  CA    . ARG A 1 128 ? 60.212  35.715  67.574  1.00 36.04  ? 155 ARG A CA    1 
ATOM   898  C  C     . ARG A 1 128 ? 60.251  35.705  69.096  1.00 42.71  ? 155 ARG A C     1 
ATOM   899  O  O     . ARG A 1 128 ? 60.533  36.732  69.725  1.00 44.17  ? 155 ARG A O     1 
ATOM   900  C  CB    . ARG A 1 128 ? 58.766  35.752  67.082  1.00 36.91  ? 155 ARG A CB    1 
ATOM   901  C  CG    . ARG A 1 128 ? 58.594  36.139  65.624  1.00 37.91  ? 155 ARG A CG    1 
ATOM   902  C  CD    . ARG A 1 128 ? 57.136  35.998  65.222  1.00 47.72  ? 155 ARG A CD    1 
ATOM   903  N  NE    . ARG A 1 128 ? 56.887  36.417  63.849  1.00 46.32  ? 155 ARG A NE    1 
ATOM   904  C  CZ    . ARG A 1 128 ? 55.938  35.903  63.079  1.00 51.45  ? 155 ARG A CZ    1 
ATOM   905  N  NH1   . ARG A 1 128 ? 55.163  34.917  63.503  1.00 40.35  ? 155 ARG A NH1   1 
ATOM   906  N  NH2   . ARG A 1 128 ? 55.768  36.384  61.851  1.00 39.84  ? 155 ARG A NH2   1 
ATOM   907  N  N     . ASP A 1 129 ? 59.969  34.549  69.707  1.00 38.50  ? 156 ASP A N     1 
ATOM   908  C  CA    . ASP A 1 129 ? 59.904  34.479  71.164  1.00 40.09  ? 156 ASP A CA    1 
ATOM   909  C  C     . ASP A 1 129 ? 61.259  34.746  71.810  1.00 39.06  ? 156 ASP A C     1 
ATOM   910  O  O     . ASP A 1 129 ? 61.317  35.271  72.928  1.00 41.62  ? 156 ASP A O     1 
ATOM   911  C  CB    . ASP A 1 129 ? 59.366  33.116  71.606  1.00 40.36  ? 156 ASP A CB    1 
ATOM   912  C  CG    . ASP A 1 129 ? 57.878  32.952  71.332  1.00 63.56  ? 156 ASP A CG    1 
ATOM   913  O  OD1   . ASP A 1 129 ? 57.184  33.977  71.150  1.00 61.02  ? 156 ASP A OD1   1 
ATOM   914  O  OD2   . ASP A 1 129 ? 57.400  31.795  71.311  1.00 50.27  ? 156 ASP A OD2   1 
ATOM   915  N  N     . MET A 1 130 ? 62.354  34.395  71.136  1.00 37.70  ? 157 MET A N     1 
ATOM   916  C  CA    . MET A 1 130 ? 63.690  34.611  71.676  1.00 39.57  ? 157 MET A CA    1 
ATOM   917  C  C     . MET A 1 130 ? 64.279  35.959  71.274  1.00 45.34  ? 157 MET A C     1 
ATOM   918  O  O     . MET A 1 130 ? 65.464  36.202  71.529  1.00 51.04  ? 157 MET A O     1 
ATOM   919  C  CB    . MET A 1 130 ? 64.629  33.481  71.241  1.00 39.28  ? 157 MET A CB    1 
ATOM   920  C  CG    . MET A 1 130 ? 65.011  33.501  69.772  1.00 41.63  ? 157 MET A CG    1 
ATOM   921  S  SD    . MET A 1 130 ? 66.087  32.120  69.355  1.00 53.58  ? 157 MET A SD    1 
ATOM   922  C  CE    . MET A 1 130 ? 67.331  32.292  70.629  1.00 59.73  ? 157 MET A CE    1 
ATOM   923  N  N     . TRP A 1 131 ? 63.482  36.827  70.646  1.00 43.81  ? 158 TRP A N     1 
ATOM   924  C  CA    . TRP A 1 131 ? 63.890  38.195  70.316  1.00 44.96  ? 158 TRP A CA    1 
ATOM   925  C  C     . TRP A 1 131 ? 65.089  38.219  69.370  1.00 47.55  ? 158 TRP A C     1 
ATOM   926  O  O     . TRP A 1 131 ? 65.998  39.040  69.511  1.00 44.53  ? 158 TRP A O     1 
ATOM   927  C  CB    . TRP A 1 131 ? 64.176  39.006  71.584  1.00 37.79  ? 158 TRP A CB    1 
ATOM   928  C  CG    . TRP A 1 131 ? 62.991  39.779  72.059  1.00 39.82  ? 158 TRP A CG    1 
ATOM   929  C  CD1   . TRP A 1 131 ? 61.804  39.938  71.408  1.00 39.10  ? 158 TRP A CD1   1 
ATOM   930  C  CD2   . TRP A 1 131 ? 62.876  40.511  73.285  1.00 45.27  ? 158 TRP A CD2   1 
ATOM   931  N  NE1   . TRP A 1 131 ? 60.955  40.720  72.153  1.00 45.32  ? 158 TRP A NE1   1 
ATOM   932  C  CE2   . TRP A 1 131 ? 61.589  41.084  73.310  1.00 41.63  ? 158 TRP A CE2   1 
ATOM   933  C  CE3   . TRP A 1 131 ? 63.735  40.735  74.364  1.00 41.57  ? 158 TRP A CE3   1 
ATOM   934  C  CZ2   . TRP A 1 131 ? 61.144  41.869  74.367  1.00 43.46  ? 158 TRP A CZ2   1 
ATOM   935  C  CZ3   . TRP A 1 131 ? 63.289  41.513  75.415  1.00 43.37  ? 158 TRP A CZ3   1 
ATOM   936  C  CH2   . TRP A 1 131 ? 62.005  42.069  75.409  1.00 45.42  ? 158 TRP A CH2   1 
ATOM   937  N  N     . ALA A 1 132 ? 65.088  37.319  68.392  1.00 43.56  ? 159 ALA A N     1 
ATOM   938  C  CA    . ALA A 1 132 ? 66.128  37.328  67.379  1.00 42.09  ? 159 ALA A CA    1 
ATOM   939  C  C     . ALA A 1 132 ? 65.879  38.452  66.377  1.00 49.34  ? 159 ALA A C     1 
ATOM   940  O  O     . ALA A 1 132 ? 64.761  38.942  66.214  1.00 42.20  ? 159 ALA A O     1 
ATOM   941  C  CB    . ALA A 1 132 ? 66.190  35.981  66.659  1.00 36.90  ? 159 ALA A CB    1 
ATOM   942  N  N     . ASP A 1 133 ? 66.951  38.870  65.706  1.00 45.30  ? 160 ASP A N     1 
ATOM   943  C  CA    . ASP A 1 133 ? 66.818  39.878  64.659  1.00 44.58  ? 160 ASP A CA    1 
ATOM   944  C  C     . ASP A 1 133 ? 66.446  39.241  63.328  1.00 44.01  ? 160 ASP A C     1 
ATOM   945  O  O     . ASP A 1 133 ? 65.630  39.789  62.577  1.00 49.38  ? 160 ASP A O     1 
ATOM   946  C  CB    . ASP A 1 133 ? 68.116  40.679  64.521  1.00 50.24  ? 160 ASP A CB    1 
ATOM   947  C  CG    . ASP A 1 133 ? 68.412  41.523  65.744  1.00 46.35  ? 160 ASP A CG    1 
ATOM   948  O  OD1   . ASP A 1 133 ? 67.465  42.108  66.307  1.00 53.86  ? 160 ASP A OD1   1 
ATOM   949  O  OD2   . ASP A 1 133 ? 69.594  41.599  66.138  1.00 47.42  ? 160 ASP A OD2   1 
ATOM   950  N  N     . TYR A 1 134 ? 67.034  38.088  63.025  1.00 45.73  ? 161 TYR A N     1 
ATOM   951  C  CA    . TYR A 1 134 ? 66.787  37.383  61.780  1.00 44.41  ? 161 TYR A CA    1 
ATOM   952  C  C     . TYR A 1 134 ? 66.612  35.901  62.069  1.00 41.48  ? 161 TYR A C     1 
ATOM   953  O  O     . TYR A 1 134 ? 67.156  35.374  63.040  1.00 42.04  ? 161 TYR A O     1 
ATOM   954  C  CB    . TYR A 1 134 ? 67.939  37.564  60.785  1.00 39.17  ? 161 TYR A CB    1 
ATOM   955  C  CG    . TYR A 1 134 ? 68.193  38.989  60.361  1.00 48.02  ? 161 TYR A CG    1 
ATOM   956  C  CD1   . TYR A 1 134 ? 68.977  39.839  61.132  1.00 48.14  ? 161 TYR A CD1   1 
ATOM   957  C  CD2   . TYR A 1 134 ? 67.665  39.480  59.175  1.00 39.16  ? 161 TYR A CD2   1 
ATOM   958  C  CE1   . TYR A 1 134 ? 69.215  41.139  60.742  1.00 48.92  ? 161 TYR A CE1   1 
ATOM   959  C  CE2   . TYR A 1 134 ? 67.898  40.779  58.776  1.00 50.23  ? 161 TYR A CE2   1 
ATOM   960  C  CZ    . TYR A 1 134 ? 68.674  41.604  59.563  1.00 48.03  ? 161 TYR A CZ    1 
ATOM   961  O  OH    . TYR A 1 134 ? 68.909  42.901  59.168  1.00 51.18  ? 161 TYR A OH    1 
ATOM   962  N  N     . ILE A 1 135 ? 65.843  35.234  61.215  1.00 41.94  ? 162 ILE A N     1 
ATOM   963  C  CA    . ILE A 1 135 ? 65.809  33.778  61.160  1.00 38.85  ? 162 ILE A CA    1 
ATOM   964  C  C     . ILE A 1 135 ? 66.305  33.354  59.784  1.00 50.09  ? 162 ILE A C     1 
ATOM   965  O  O     . ILE A 1 135 ? 65.865  33.894  58.761  1.00 41.60  ? 162 ILE A O     1 
ATOM   966  C  CB    . ILE A 1 135 ? 64.406  33.211  61.455  1.00 39.98  ? 162 ILE A CB    1 
ATOM   967  C  CG1   . ILE A 1 135 ? 64.419  31.685  61.329  1.00 33.61  ? 162 ILE A CG1   1 
ATOM   968  C  CG2   . ILE A 1 135 ? 63.354  33.828  60.548  1.00 41.14  ? 162 ILE A CG2   1 
ATOM   969  C  CD1   . ILE A 1 135 ? 63.173  31.008  61.859  1.00 37.63  ? 162 ILE A CD1   1 
ATOM   970  N  N     . LEU A 1 136 ? 67.246  32.417  59.766  1.00 48.60  ? 163 LEU A N     1 
ATOM   971  C  CA    . LEU A 1 136 ? 67.852  31.923  58.536  1.00 40.62  ? 163 LEU A CA    1 
ATOM   972  C  C     . LEU A 1 136 ? 67.429  30.473  58.349  1.00 47.64  ? 163 LEU A C     1 
ATOM   973  O  O     . LEU A 1 136 ? 67.810  29.603  59.139  1.00 47.40  ? 163 LEU A O     1 
ATOM   974  C  CB    . LEU A 1 136 ? 69.373  32.051  58.590  1.00 40.31  ? 163 LEU A CB    1 
ATOM   975  C  CG    . LEU A 1 136 ? 70.160  31.480  57.411  1.00 36.92  ? 163 LEU A CG    1 
ATOM   976  C  CD1   . LEU A 1 136 ? 69.917  32.294  56.150  1.00 33.12  ? 163 LEU A CD1   1 
ATOM   977  C  CD2   . LEU A 1 136 ? 71.641  31.424  57.740  1.00 42.08  ? 163 LEU A CD2   1 
ATOM   978  N  N     . PHE A 1 137 ? 66.628  30.220  57.319  1.00 42.14  ? 164 PHE A N     1 
ATOM   979  C  CA    . PHE A 1 137 ? 66.265  28.862  56.946  1.00 43.85  ? 164 PHE A CA    1 
ATOM   980  C  C     . PHE A 1 137 ? 67.301  28.324  55.972  1.00 43.09  ? 164 PHE A C     1 
ATOM   981  O  O     . PHE A 1 137 ? 67.612  28.972  54.968  1.00 44.42  ? 164 PHE A O     1 
ATOM   982  C  CB    . PHE A 1 137 ? 64.873  28.815  56.316  1.00 46.89  ? 164 PHE A CB    1 
ATOM   983  C  CG    . PHE A 1 137 ? 63.753  28.920  57.308  1.00 49.40  ? 164 PHE A CG    1 
ATOM   984  C  CD1   . PHE A 1 137 ? 63.268  27.792  57.946  1.00 42.69  ? 164 PHE A CD1   1 
ATOM   985  C  CD2   . PHE A 1 137 ? 63.179  30.146  57.598  1.00 44.64  ? 164 PHE A CD2   1 
ATOM   986  C  CE1   . PHE A 1 137 ? 62.232  27.887  58.858  1.00 36.68  ? 164 PHE A CE1   1 
ATOM   987  C  CE2   . PHE A 1 137 ? 62.143  30.247  58.508  1.00 37.67  ? 164 PHE A CE2   1 
ATOM   988  C  CZ    . PHE A 1 137 ? 61.670  29.117  59.138  1.00 37.51  ? 164 PHE A CZ    1 
ATOM   989  N  N     . VAL A 1 138 ? 67.851  27.155  56.286  1.00 44.33  ? 165 VAL A N     1 
ATOM   990  C  CA    . VAL A 1 138 ? 68.793  26.462  55.417  1.00 50.99  ? 165 VAL A CA    1 
ATOM   991  C  C     . VAL A 1 138 ? 68.339  25.016  55.312  1.00 56.14  ? 165 VAL A C     1 
ATOM   992  O  O     . VAL A 1 138 ? 68.200  24.331  56.333  1.00 52.34  ? 165 VAL A O     1 
ATOM   993  C  CB    . VAL A 1 138 ? 70.238  26.531  55.939  1.00 41.86  ? 165 VAL A CB    1 
ATOM   994  C  CG1   . VAL A 1 138 ? 71.197  25.971  54.901  1.00 32.07  ? 165 VAL A CG1   1 
ATOM   995  C  CG2   . VAL A 1 138 ? 70.615  27.955  56.309  1.00 41.09  ? 165 VAL A CG2   1 
ATOM   996  N  N     . ASP A 1 139 ? 68.101  24.554  54.091  1.00 45.41  ? 166 ASP A N     1 
ATOM   997  C  CA    . ASP A 1 139 ? 67.776  23.151  53.898  1.00 54.22  ? 166 ASP A CA    1 
ATOM   998  C  C     . ASP A 1 139 ? 69.007  22.285  54.137  1.00 51.00  ? 166 ASP A C     1 
ATOM   999  O  O     . ASP A 1 139 ? 70.141  22.685  53.859  1.00 48.66  ? 166 ASP A O     1 
ATOM   1000 C  CB    . ASP A 1 139 ? 67.218  22.918  52.497  1.00 49.61  ? 166 ASP A CB    1 
ATOM   1001 C  CG    . ASP A 1 139 ? 65.746  23.262  52.397  1.00 68.37  ? 166 ASP A CG    1 
ATOM   1002 O  OD1   . ASP A 1 139 ? 65.188  23.802  53.377  1.00 72.93  ? 166 ASP A OD1   1 
ATOM   1003 O  OD2   . ASP A 1 139 ? 65.144  22.981  51.343  1.00 69.23  ? 166 ASP A OD2   1 
ATOM   1004 N  N     . ALA A 1 140 ? 68.768  21.081  54.661  1.00 48.57  ? 167 ALA A N     1 
ATOM   1005 C  CA    . ALA A 1 140 ? 69.855  20.235  55.137  1.00 41.88  ? 167 ALA A CA    1 
ATOM   1006 C  C     . ALA A 1 140 ? 70.811  19.802  54.031  1.00 46.19  ? 167 ALA A C     1 
ATOM   1007 O  O     . ALA A 1 140 ? 71.936  19.393  54.337  1.00 54.85  ? 167 ALA A O     1 
ATOM   1008 C  CB    . ALA A 1 140 ? 69.283  19.007  55.841  1.00 49.40  ? 167 ALA A CB    1 
ATOM   1009 N  N     . ASP A 1 141 ? 70.402  19.872  52.765  1.00 42.40  ? 168 ASP A N     1 
ATOM   1010 C  CA    . ASP A 1 141 ? 71.297  19.559  51.659  1.00 40.73  ? 168 ASP A CA    1 
ATOM   1011 C  C     . ASP A 1 141 ? 71.787  20.803  50.930  1.00 48.44  ? 168 ASP A C     1 
ATOM   1012 O  O     . ASP A 1 141 ? 72.400  20.681  49.866  1.00 56.08  ? 168 ASP A O     1 
ATOM   1013 C  CB    . ASP A 1 141 ? 70.625  18.594  50.675  1.00 40.93  ? 168 ASP A CB    1 
ATOM   1014 C  CG    . ASP A 1 141 ? 69.375  19.169  50.034  1.00 51.22  ? 168 ASP A CG    1 
ATOM   1015 O  OD1   . ASP A 1 141 ? 68.974  20.301  50.374  1.00 52.93  ? 168 ASP A OD1   1 
ATOM   1016 O  OD2   . ASP A 1 141 ? 68.786  18.474  49.182  1.00 63.01  ? 168 ASP A OD2   1 
ATOM   1017 N  N     . ASN A 1 142 ? 71.533  21.990  51.473  1.00 48.30  ? 169 ASN A N     1 
ATOM   1018 C  CA    . ASN A 1 142 ? 72.045  23.227  50.900  1.00 44.34  ? 169 ASN A CA    1 
ATOM   1019 C  C     . ASN A 1 142 ? 73.404  23.537  51.514  1.00 52.37  ? 169 ASN A C     1 
ATOM   1020 O  O     . ASN A 1 142 ? 73.542  23.593  52.740  1.00 51.17  ? 169 ASN A O     1 
ATOM   1021 C  CB    . ASN A 1 142 ? 71.077  24.388  51.136  1.00 52.06  ? 169 ASN A CB    1 
ATOM   1022 C  CG    . ASN A 1 142 ? 69.791  24.262  50.329  1.00 54.37  ? 169 ASN A CG    1 
ATOM   1023 O  OD1   . ASN A 1 142 ? 68.911  25.119  50.411  1.00 47.73  ? 169 ASN A OD1   1 
ATOM   1024 N  ND2   . ASN A 1 142 ? 69.675  23.191  49.551  1.00 59.13  ? 169 ASN A ND2   1 
ATOM   1025 N  N     . LEU A 1 143 ? 74.405  23.723  50.657  1.00 45.79  ? 170 LEU A N     1 
ATOM   1026 C  CA    . LEU A 1 143 ? 75.788  23.926  51.074  1.00 49.14  ? 170 LEU A CA    1 
ATOM   1027 C  C     . LEU A 1 143 ? 76.143  25.398  50.902  1.00 44.50  ? 170 LEU A C     1 
ATOM   1028 O  O     . LEU A 1 143 ? 76.200  25.899  49.775  1.00 44.80  ? 170 LEU A O     1 
ATOM   1029 C  CB    . LEU A 1 143 ? 76.731  23.040  50.264  1.00 41.64  ? 170 LEU A CB    1 
ATOM   1030 C  CG    . LEU A 1 143 ? 78.218  23.301  50.479  1.00 49.94  ? 170 LEU A CG    1 
ATOM   1031 C  CD1   . LEU A 1 143 ? 78.570  23.098  51.936  1.00 54.68  ? 170 LEU A CD1   1 
ATOM   1032 C  CD2   . LEU A 1 143 ? 79.051  22.398  49.591  1.00 49.30  ? 170 LEU A CD2   1 
ATOM   1033 N  N     . ILE A 1 144 ? 76.392  26.084  52.015  1.00 46.62  ? 171 ILE A N     1 
ATOM   1034 C  CA    . ILE A 1 144 ? 76.714  27.507  51.986  1.00 47.58  ? 171 ILE A CA    1 
ATOM   1035 C  C     . ILE A 1 144 ? 78.226  27.677  52.059  1.00 53.18  ? 171 ILE A C     1 
ATOM   1036 O  O     . ILE A 1 144 ? 78.788  27.899  53.138  1.00 53.38  ? 171 ILE A O     1 
ATOM   1037 C  CB    . ILE A 1 144 ? 76.012  28.259  53.130  1.00 55.65  ? 171 ILE A CB    1 
ATOM   1038 C  CG1   . ILE A 1 144 ? 74.537  27.859  53.200  1.00 47.79  ? 171 ILE A CG1   1 
ATOM   1039 C  CG2   . ILE A 1 144 ? 76.136  29.754  52.935  1.00 50.70  ? 171 ILE A CG2   1 
ATOM   1040 C  CD1   . ILE A 1 144 ? 73.779  28.082  51.911  1.00 42.29  ? 171 ILE A CD1   1 
ATOM   1041 N  N     . LEU A 1 145 ? 78.891  27.575  50.904  1.00 54.58  ? 172 LEU A N     1 
ATOM   1042 C  CA    . LEU A 1 145 ? 80.349  27.628  50.871  1.00 45.38  ? 172 LEU A CA    1 
ATOM   1043 C  C     . LEU A 1 145 ? 80.875  28.979  51.338  1.00 50.32  ? 172 LEU A C     1 
ATOM   1044 O  O     . LEU A 1 145 ? 81.884  29.045  52.049  1.00 61.98  ? 172 LEU A O     1 
ATOM   1045 C  CB    . LEU A 1 145 ? 80.857  27.331  49.462  1.00 48.67  ? 172 LEU A CB    1 
ATOM   1046 C  CG    . LEU A 1 145 ? 81.222  25.889  49.120  1.00 60.64  ? 172 LEU A CG    1 
ATOM   1047 C  CD1   . LEU A 1 145 ? 82.022  25.860  47.830  1.00 48.23  ? 172 LEU A CD1   1 
ATOM   1048 C  CD2   . LEU A 1 145 ? 82.003  25.255  50.256  1.00 57.94  ? 172 LEU A CD2   1 
ATOM   1049 N  N     . ASN A 1 146 ? 80.215  30.066  50.938  1.00 46.09  ? 173 ASN A N     1 
ATOM   1050 C  CA    . ASN A 1 146 ? 80.673  31.412  51.259  1.00 50.62  ? 173 ASN A CA    1 
ATOM   1051 C  C     . ASN A 1 146 ? 80.400  31.723  52.725  1.00 55.08  ? 173 ASN A C     1 
ATOM   1052 O  O     . ASN A 1 146 ? 79.236  31.855  53.126  1.00 55.35  ? 173 ASN A O     1 
ATOM   1053 C  CB    . ASN A 1 146 ? 79.989  32.446  50.361  1.00 49.14  ? 173 ASN A CB    1 
ATOM   1054 C  CG    . ASN A 1 146 ? 80.620  33.825  50.467  1.00 57.90  ? 173 ASN A CG    1 
ATOM   1055 O  OD1   . ASN A 1 146 ? 81.421  34.091  51.364  1.00 65.54  ? 173 ASN A OD1   1 
ATOM   1056 N  ND2   . ASN A 1 146 ? 80.256  34.712  49.548  1.00 66.50  ? 173 ASN A ND2   1 
ATOM   1057 N  N     . PRO A 1 147 ? 81.440  31.864  53.551  1.00 54.96  ? 174 PRO A N     1 
ATOM   1058 C  CA    . PRO A 1 147 ? 81.205  32.139  54.978  1.00 67.68  ? 174 PRO A CA    1 
ATOM   1059 C  C     . PRO A 1 147 ? 80.576  33.495  55.234  1.00 60.71  ? 174 PRO A C     1 
ATOM   1060 O  O     . PRO A 1 147 ? 80.044  33.717  56.328  1.00 57.49  ? 174 PRO A O     1 
ATOM   1061 C  CB    . PRO A 1 147 ? 82.612  32.050  55.594  1.00 48.85  ? 174 PRO A CB    1 
ATOM   1062 C  CG    . PRO A 1 147 ? 83.466  31.383  54.552  1.00 47.29  ? 174 PRO A CG    1 
ATOM   1063 C  CD    . PRO A 1 147 ? 82.874  31.776  53.238  1.00 44.87  ? 174 PRO A CD    1 
ATOM   1064 N  N     . ASP A 1 148 ? 80.613  34.403  54.261  1.00 50.61  ? 175 ASP A N     1 
ATOM   1065 C  CA    . ASP A 1 148 ? 80.058  35.739  54.414  1.00 61.90  ? 175 ASP A CA    1 
ATOM   1066 C  C     . ASP A 1 148 ? 78.608  35.835  53.960  1.00 59.15  ? 175 ASP A C     1 
ATOM   1067 O  O     . ASP A 1 148 ? 78.047  36.936  53.968  1.00 57.05  ? 175 ASP A O     1 
ATOM   1068 C  CB    . ASP A 1 148 ? 80.905  36.751  53.635  1.00 51.69  ? 175 ASP A CB    1 
ATOM   1069 C  CG    . ASP A 1 148 ? 82.337  36.814  54.126  1.00 59.29  ? 175 ASP A CG    1 
ATOM   1070 O  OD1   . ASP A 1 148 ? 82.560  36.625  55.340  1.00 63.59  ? 175 ASP A OD1   1 
ATOM   1071 O  OD2   . ASP A 1 148 ? 83.242  37.053  53.296  1.00 72.96  ? 175 ASP A OD2   1 
ATOM   1072 N  N     . THR A 1 149 ? 77.989  34.715  53.580  1.00 50.17  ? 176 THR A N     1 
ATOM   1073 C  CA    . THR A 1 149 ? 76.642  34.758  53.019  1.00 54.27  ? 176 THR A CA    1 
ATOM   1074 C  C     . THR A 1 149 ? 75.652  35.392  53.992  1.00 45.61  ? 176 THR A C     1 
ATOM   1075 O  O     . THR A 1 149 ? 74.856  36.256  53.607  1.00 45.05  ? 176 THR A O     1 
ATOM   1076 C  CB    . THR A 1 149 ? 76.188  33.351  52.632  1.00 60.98  ? 176 THR A CB    1 
ATOM   1077 O  OG1   . THR A 1 149 ? 77.011  32.854  51.570  1.00 54.44  ? 176 THR A OG1   1 
ATOM   1078 C  CG2   . THR A 1 149 ? 74.736  33.365  52.175  1.00 47.13  ? 176 THR A CG2   1 
ATOM   1079 N  N     . LEU A 1 150 ? 75.690  34.979  55.261  1.00 42.22  ? 177 LEU A N     1 
ATOM   1080 C  CA    . LEU A 1 150 ? 74.761  35.532  56.243  1.00 45.34  ? 177 LEU A CA    1 
ATOM   1081 C  C     . LEU A 1 150 ? 74.975  37.030  56.412  1.00 55.11  ? 177 LEU A C     1 
ATOM   1082 O  O     . LEU A 1 150 ? 74.017  37.811  56.408  1.00 52.58  ? 177 LEU A O     1 
ATOM   1083 C  CB    . LEU A 1 150 ? 74.914  34.807  57.580  1.00 40.68  ? 177 LEU A CB    1 
ATOM   1084 C  CG    . LEU A 1 150 ? 74.042  35.326  58.722  1.00 41.31  ? 177 LEU A CG    1 
ATOM   1085 C  CD1   . LEU A 1 150 ? 72.576  35.343  58.317  1.00 42.46  ? 177 LEU A CD1   1 
ATOM   1086 C  CD2   . LEU A 1 150 ? 74.240  34.489  59.973  1.00 42.13  ? 177 LEU A CD2   1 
ATOM   1087 N  N     . SER A 1 151 ? 76.234  37.451  56.546  1.00 50.86  ? 178 SER A N     1 
ATOM   1088 C  CA    . SER A 1 151 ? 76.535  38.875  56.643  1.00 42.40  ? 178 SER A CA    1 
ATOM   1089 C  C     . SER A 1 151 ? 76.088  39.617  55.388  1.00 49.31  ? 178 SER A C     1 
ATOM   1090 O  O     . SER A 1 151 ? 75.467  40.683  55.471  1.00 48.90  ? 178 SER A O     1 
ATOM   1091 C  CB    . SER A 1 151 ? 78.031  39.078  56.882  1.00 41.91  ? 178 SER A CB    1 
ATOM   1092 O  OG    . SER A 1 151 ? 78.477  38.350  58.014  1.00 54.70  ? 178 SER A OG    1 
ATOM   1093 N  N     . LEU A 1 152 ? 76.395  39.062  54.212  1.00 40.52  ? 179 LEU A N     1 
ATOM   1094 C  CA    . LEU A 1 152 ? 76.004  39.702  52.958  1.00 38.88  ? 179 LEU A CA    1 
ATOM   1095 C  C     . LEU A 1 152 ? 74.490  39.850  52.857  1.00 54.09  ? 179 LEU A C     1 
ATOM   1096 O  O     . LEU A 1 152 ? 73.988  40.897  52.433  1.00 60.37  ? 179 LEU A O     1 
ATOM   1097 C  CB    . LEU A 1 152 ? 76.541  38.900  51.769  1.00 50.91  ? 179 LEU A CB    1 
ATOM   1098 C  CG    . LEU A 1 152 ? 78.049  38.898  51.508  1.00 52.94  ? 179 LEU A CG    1 
ATOM   1099 C  CD1   . LEU A 1 152 ? 78.410  37.867  50.445  1.00 56.82  ? 179 LEU A CD1   1 
ATOM   1100 C  CD2   . LEU A 1 152 ? 78.528  40.279  51.096  1.00 41.03  ? 179 LEU A CD2   1 
ATOM   1101 N  N     . LEU A 1 153 ? 73.746  38.807  53.237  1.00 42.09  ? 180 LEU A N     1 
ATOM   1102 C  CA    . LEU A 1 153 ? 72.290  38.869  53.160  1.00 39.84  ? 180 LEU A CA    1 
ATOM   1103 C  C     . LEU A 1 153 ? 71.727  39.908  54.121  1.00 52.96  ? 180 LEU A C     1 
ATOM   1104 O  O     . LEU A 1 153 ? 70.765  40.613  53.792  1.00 51.77  ? 180 LEU A O     1 
ATOM   1105 C  CB    . LEU A 1 153 ? 71.689  37.494  53.449  1.00 49.29  ? 180 LEU A CB    1 
ATOM   1106 C  CG    . LEU A 1 153 ? 71.907  36.395  52.409  1.00 46.63  ? 180 LEU A CG    1 
ATOM   1107 C  CD1   . LEU A 1 153 ? 71.509  35.052  52.991  1.00 33.16  ? 180 LEU A CD1   1 
ATOM   1108 C  CD2   . LEU A 1 153 ? 71.124  36.684  51.138  1.00 40.07  ? 180 LEU A CD2   1 
ATOM   1109 N  N     . ILE A 1 154 ? 72.308  40.015  55.318  1.00 46.17  ? 181 ILE A N     1 
ATOM   1110 C  CA    . ILE A 1 154 ? 71.852  41.019  56.275  1.00 46.93  ? 181 ILE A CA    1 
ATOM   1111 C  C     . ILE A 1 154 ? 72.095  42.420  55.732  1.00 46.86  ? 181 ILE A C     1 
ATOM   1112 O  O     . ILE A 1 154 ? 71.299  43.338  55.961  1.00 55.43  ? 181 ILE A O     1 
ATOM   1113 C  CB    . ILE A 1 154 ? 72.545  40.813  57.635  1.00 52.41  ? 181 ILE A CB    1 
ATOM   1114 C  CG1   . ILE A 1 154 ? 72.150  39.464  58.232  1.00 49.07  ? 181 ILE A CG1   1 
ATOM   1115 C  CG2   . ILE A 1 154 ? 72.184  41.928  58.604  1.00 45.08  ? 181 ILE A CG2   1 
ATOM   1116 C  CD1   . ILE A 1 154 ? 72.881  39.135  59.515  1.00 42.44  ? 181 ILE A CD1   1 
ATOM   1117 N  N     . ALA A 1 155 ? 73.186  42.604  54.987  1.00 48.36  ? 182 ALA A N     1 
ATOM   1118 C  CA    . ALA A 1 155 ? 73.537  43.938  54.514  1.00 50.21  ? 182 ALA A CA    1 
ATOM   1119 C  C     . ALA A 1 155 ? 72.537  44.463  53.494  1.00 49.22  ? 182 ALA A C     1 
ATOM   1120 O  O     . ALA A 1 155 ? 72.411  45.681  53.323  1.00 51.34  ? 182 ALA A O     1 
ATOM   1121 C  CB    . ALA A 1 155 ? 74.947  43.936  53.925  1.00 39.10  ? 182 ALA A CB    1 
ATOM   1122 N  N     . GLU A 1 156 ? 71.827  43.571  52.803  1.00 44.85  ? 183 GLU A N     1 
ATOM   1123 C  CA    . GLU A 1 156 ? 70.871  44.013  51.796  1.00 50.39  ? 183 GLU A CA    1 
ATOM   1124 C  C     . GLU A 1 156 ? 69.645  44.689  52.398  1.00 42.79  ? 183 GLU A C     1 
ATOM   1125 O  O     . GLU A 1 156 ? 68.908  45.358  51.665  1.00 57.36  ? 183 GLU A O     1 
ATOM   1126 C  CB    . GLU A 1 156 ? 70.446  42.831  50.922  1.00 58.96  ? 183 GLU A CB    1 
ATOM   1127 C  CG    . GLU A 1 156 ? 71.609  42.128  50.230  1.00 70.90  ? 183 GLU A CG    1 
ATOM   1128 C  CD    . GLU A 1 156 ? 72.416  43.050  49.324  1.00 77.98  ? 183 GLU A CD    1 
ATOM   1129 O  OE1   . GLU A 1 156 ? 71.847  44.027  48.788  1.00 60.89  ? 183 GLU A OE1   1 
ATOM   1130 O  OE2   . GLU A 1 156 ? 73.625  42.793  49.144  1.00 77.98  ? 183 GLU A OE2   1 
ATOM   1131 N  N     . ASN A 1 157 ? 69.419  44.536  53.701  1.00 43.19  ? 184 ASN A N     1 
ATOM   1132 C  CA    . ASN A 1 157 ? 68.338  45.211  54.418  1.00 50.08  ? 184 ASN A CA    1 
ATOM   1133 C  C     . ASN A 1 157 ? 66.984  44.976  53.749  1.00 55.59  ? 184 ASN A C     1 
ATOM   1134 O  O     . ASN A 1 157 ? 66.225  45.906  53.466  1.00 53.24  ? 184 ASN A O     1 
ATOM   1135 C  CB    . ASN A 1 157 ? 68.625  46.706  54.563  1.00 40.42  ? 184 ASN A CB    1 
ATOM   1136 C  CG    . ASN A 1 157 ? 67.666  47.388  55.519  1.00 49.42  ? 184 ASN A CG    1 
ATOM   1137 O  OD1   . ASN A 1 157 ? 67.036  46.737  56.352  1.00 56.03  ? 184 ASN A OD1   1 
ATOM   1138 N  ND2   . ASN A 1 157 ? 67.543  48.705  55.397  1.00 48.35  ? 184 ASN A ND2   1 
ATOM   1139 N  N     . LYS A 1 158 ? 66.686  43.709  53.493  1.00 50.37  ? 185 LYS A N     1 
ATOM   1140 C  CA    . LYS A 1 158 ? 65.384  43.293  53.000  1.00 54.47  ? 185 LYS A CA    1 
ATOM   1141 C  C     . LYS A 1 158 ? 64.656  42.524  54.093  1.00 50.42  ? 185 LYS A C     1 
ATOM   1142 O  O     . LYS A 1 158 ? 65.255  42.078  55.073  1.00 55.81  ? 185 LYS A O     1 
ATOM   1143 C  CB    . LYS A 1 158 ? 65.515  42.422  51.747  1.00 58.69  ? 185 LYS A CB    1 
ATOM   1144 C  CG    . LYS A 1 158 ? 66.273  43.075  50.600  1.00 47.42  ? 185 LYS A CG    1 
ATOM   1145 C  CD    . LYS A 1 158 ? 65.590  44.345  50.136  1.00 57.99  ? 185 LYS A CD    1 
ATOM   1146 C  CE    . LYS A 1 158 ? 66.159  44.816  48.807  1.00 51.66  ? 185 LYS A CE    1 
ATOM   1147 N  NZ    . LYS A 1 158 ? 65.398  45.973  48.262  1.00 72.10  ? 185 LYS A NZ    1 
ATOM   1148 N  N     . THR A 1 159 ? 63.343  42.380  53.922  1.00 47.78  ? 186 THR A N     1 
ATOM   1149 C  CA    . THR A 1 159 ? 62.575  41.615  54.898  1.00 56.10  ? 186 THR A CA    1 
ATOM   1150 C  C     . THR A 1 159 ? 62.658  40.121  54.611  1.00 47.95  ? 186 THR A C     1 
ATOM   1151 O  O     . THR A 1 159 ? 62.767  39.314  55.541  1.00 48.48  ? 186 THR A O     1 
ATOM   1152 C  CB    . THR A 1 159 ? 61.123  42.094  54.924  1.00 40.65  ? 186 THR A CB    1 
ATOM   1153 O  OG1   . THR A 1 159 ? 61.095  43.492  55.246  1.00 57.54  ? 186 THR A OG1   1 
ATOM   1154 C  CG2   . THR A 1 159 ? 60.324  41.332  55.966  1.00 44.71  ? 186 THR A CG2   1 
ATOM   1155 N  N     . VAL A 1 160 ? 62.604  39.738  53.337  1.00 48.13  ? 187 VAL A N     1 
ATOM   1156 C  CA    . VAL A 1 160 ? 62.806  38.357  52.912  1.00 40.20  ? 187 VAL A CA    1 
ATOM   1157 C  C     . VAL A 1 160 ? 63.760  38.371  51.729  1.00 52.11  ? 187 VAL A C     1 
ATOM   1158 O  O     . VAL A 1 160 ? 63.430  38.917  50.671  1.00 53.09  ? 187 VAL A O     1 
ATOM   1159 C  CB    . VAL A 1 160 ? 61.488  37.660  52.535  1.00 42.28  ? 187 VAL A CB    1 
ATOM   1160 C  CG1   . VAL A 1 160 ? 61.766  36.246  52.046  1.00 39.48  ? 187 VAL A CG1   1 
ATOM   1161 C  CG2   . VAL A 1 160 ? 60.533  37.643  53.715  1.00 55.56  ? 187 VAL A CG2   1 
ATOM   1162 N  N     . VAL A 1 161 ? 64.935  37.778  51.904  1.00 48.53  ? 188 VAL A N     1 
ATOM   1163 C  CA    . VAL A 1 161 ? 65.946  37.736  50.855  1.00 52.14  ? 188 VAL A CA    1 
ATOM   1164 C  C     . VAL A 1 161 ? 66.617  36.369  50.875  1.00 43.50  ? 188 VAL A C     1 
ATOM   1165 O  O     . VAL A 1 161 ? 66.871  35.800  51.942  1.00 44.74  ? 188 VAL A O     1 
ATOM   1166 C  CB    . VAL A 1 161 ? 66.982  38.870  51.017  1.00 51.32  ? 188 VAL A CB    1 
ATOM   1167 C  CG1   . VAL A 1 161 ? 67.741  38.736  52.330  1.00 40.52  ? 188 VAL A CG1   1 
ATOM   1168 C  CG2   . VAL A 1 161 ? 67.934  38.886  49.842  1.00 41.24  ? 188 VAL A CG2   1 
ATOM   1169 N  N     . ALA A 1 162 ? 66.887  35.837  49.685  1.00 51.83  ? 189 ALA A N     1 
ATOM   1170 C  CA    . ALA A 1 162 ? 67.528  34.551  49.519  1.00 41.05  ? 189 ALA A CA    1 
ATOM   1171 C  C     . ALA A 1 162 ? 68.799  34.692  48.693  1.00 43.75  ? 189 ALA A C     1 
ATOM   1172 O  O     . ALA A 1 162 ? 68.827  35.462  47.727  1.00 54.44  ? 189 ALA A O     1 
ATOM   1173 C  CB    . ALA A 1 162 ? 66.586  33.555  48.831  1.00 39.11  ? 189 ALA A CB    1 
ATOM   1174 N  N     . PRO A 1 163 ? 69.865  33.981  49.049  1.00 49.96  ? 190 PRO A N     1 
ATOM   1175 C  CA    . PRO A 1 163 ? 71.045  33.944  48.181  1.00 47.53  ? 190 PRO A CA    1 
ATOM   1176 C  C     . PRO A 1 163 ? 70.847  32.926  47.071  1.00 46.13  ? 190 PRO A C     1 
ATOM   1177 O  O     . PRO A 1 163 ? 70.343  31.824  47.296  1.00 55.08  ? 190 PRO A O     1 
ATOM   1178 C  CB    . PRO A 1 163 ? 72.166  33.519  49.135  1.00 42.65  ? 190 PRO A CB    1 
ATOM   1179 C  CG    . PRO A 1 163 ? 71.467  32.663  50.143  1.00 38.88  ? 190 PRO A CG    1 
ATOM   1180 C  CD    . PRO A 1 163 ? 70.067  33.217  50.292  1.00 43.46  ? 190 PRO A CD    1 
ATOM   1181 N  N     . MET A 1 164 ? 71.234  33.304  45.857  1.00 45.23  ? 191 MET A N     1 
ATOM   1182 C  CA    . MET A 1 164 ? 71.045  32.413  44.715  1.00 48.76  ? 191 MET A CA    1 
ATOM   1183 C  C     . MET A 1 164 ? 72.069  31.288  44.784  1.00 52.59  ? 191 MET A C     1 
ATOM   1184 O  O     . MET A 1 164 ? 73.275  31.526  44.660  1.00 53.27  ? 191 MET A O     1 
ATOM   1185 C  CB    . MET A 1 164 ? 71.162  33.171  43.397  1.00 48.31  ? 191 MET A CB    1 
ATOM   1186 C  CG    . MET A 1 164 ? 70.700  32.339  42.206  1.00 44.77  ? 191 MET A CG    1 
ATOM   1187 S  SD    . MET A 1 164 ? 71.212  32.983  40.605  1.00 65.41  ? 191 MET A SD    1 
ATOM   1188 C  CE    . MET A 1 164 ? 72.987  32.770  40.702  1.00 57.38  ? 191 MET A CE    1 
ATOM   1189 N  N     . LEU A 1 165 ? 71.592  30.064  44.991  1.00 50.62  ? 192 LEU A N     1 
ATOM   1190 C  CA    . LEU A 1 165 ? 72.465  28.906  45.087  1.00 52.92  ? 192 LEU A CA    1 
ATOM   1191 C  C     . LEU A 1 165 ? 72.622  28.247  43.724  1.00 54.30  ? 192 LEU A C     1 
ATOM   1192 O  O     . LEU A 1 165 ? 71.661  28.135  42.958  1.00 52.99  ? 192 LEU A O     1 
ATOM   1193 C  CB    . LEU A 1 165 ? 71.914  27.900  46.099  1.00 52.83  ? 192 LEU A CB    1 
ATOM   1194 C  CG    . LEU A 1 165 ? 71.764  28.440  47.520  1.00 53.50  ? 192 LEU A CG    1 
ATOM   1195 C  CD1   . LEU A 1 165 ? 71.228  27.367  48.450  1.00 51.24  ? 192 LEU A CD1   1 
ATOM   1196 C  CD2   . LEU A 1 165 ? 73.097  28.967  48.017  1.00 38.86  ? 192 LEU A CD2   1 
ATOM   1197 N  N     . ASP A 1 166 ? 73.844  27.815  43.427  1.00 54.11  ? 193 ASP A N     1 
ATOM   1198 C  CA    . ASP A 1 166 ? 74.131  27.164  42.160  1.00 55.15  ? 193 ASP A CA    1 
ATOM   1199 C  C     . ASP A 1 166 ? 73.750  25.690  42.208  1.00 59.14  ? 193 ASP A C     1 
ATOM   1200 O  O     . ASP A 1 166 ? 73.850  25.031  43.246  1.00 59.41  ? 193 ASP A O     1 
ATOM   1201 C  CB    . ASP A 1 166 ? 75.614  27.296  41.807  1.00 65.87  ? 193 ASP A CB    1 
ATOM   1202 C  CG    . ASP A 1 166 ? 76.035  28.733  41.572  1.00 77.46  ? 193 ASP A CG    1 
ATOM   1203 O  OD1   . ASP A 1 166 ? 75.189  29.538  41.131  1.00 76.60  ? 193 ASP A OD1   1 
ATOM   1204 O  OD2   . ASP A 1 166 ? 77.215  29.056  41.823  1.00 79.13  ? 193 ASP A OD2   1 
ATOM   1205 N  N     . SER A 1 167 ? 73.309  25.177  41.065  1.00 63.71  ? 194 SER A N     1 
ATOM   1206 C  CA    . SER A 1 167 ? 73.040  23.760  40.889  1.00 53.44  ? 194 SER A CA    1 
ATOM   1207 C  C     . SER A 1 167 ? 73.721  23.293  39.612  1.00 54.06  ? 194 SER A C     1 
ATOM   1208 O  O     . SER A 1 167 ? 74.277  24.088  38.850  1.00 63.01  ? 194 SER A O     1 
ATOM   1209 C  CB    . SER A 1 167 ? 71.534  23.465  40.832  1.00 58.94  ? 194 SER A CB    1 
ATOM   1210 O  OG    . SER A 1 167 ? 70.997  23.786  39.560  1.00 57.23  ? 194 SER A OG    1 
ATOM   1211 N  N     . ARG A 1 168 ? 73.674  21.981  39.380  1.00 67.04  ? 195 ARG A N     1 
ATOM   1212 C  CA    . ARG A 1 168 ? 74.254  21.423  38.164  1.00 61.26  ? 195 ARG A CA    1 
ATOM   1213 C  C     . ARG A 1 168 ? 73.461  21.800  36.920  1.00 55.82  ? 195 ARG A C     1 
ATOM   1214 O  O     . ARG A 1 168 ? 73.976  21.660  35.806  1.00 69.14  ? 195 ARG A O     1 
ATOM   1215 C  CB    . ARG A 1 168 ? 74.339  19.902  38.274  1.00 64.75  ? 195 ARG A CB    1 
ATOM   1216 C  CG    . ARG A 1 168 ? 72.983  19.247  38.450  1.00 54.50  ? 195 ARG A CG    1 
ATOM   1217 C  CD    . ARG A 1 168 ? 73.060  17.736  38.398  1.00 55.84  ? 195 ARG A CD    1 
ATOM   1218 N  NE    . ARG A 1 168 ? 71.733  17.152  38.540  1.00 64.93  ? 195 ARG A NE    1 
ATOM   1219 C  CZ    . ARG A 1 168 ? 70.873  16.998  37.542  1.00 63.47  ? 195 ARG A CZ    1 
ATOM   1220 N  NH1   . ARG A 1 168 ? 71.182  17.347  36.303  1.00 59.32  ? 195 ARG A NH1   1 
ATOM   1221 N  NH2   . ARG A 1 168 ? 69.673  16.483  37.794  1.00 57.27  ? 195 ARG A NH2   1 
ATOM   1222 N  N     . ALA A 1 169 ? 72.227  22.266  37.079  1.00 64.66  ? 196 ALA A N     1 
ATOM   1223 C  CA    . ALA A 1 169 ? 71.372  22.606  35.950  1.00 56.55  ? 196 ALA A CA    1 
ATOM   1224 C  C     . ALA A 1 169 ? 70.885  24.043  36.128  1.00 60.90  ? 196 ALA A C     1 
ATOM   1225 O  O     . ALA A 1 169 ? 71.418  24.820  36.932  1.00 64.42  ? 196 ALA A O     1 
ATOM   1226 C  CB    . ALA A 1 169 ? 70.220  21.601  35.834  1.00 57.02  ? 196 ALA A CB    1 
ATOM   1227 N  N     . ALA A 1 170 ? 69.849  24.414  35.371  1.00 56.78  ? 197 ALA A N     1 
ATOM   1228 C  CA    . ALA A 1 170 ? 69.262  25.744  35.481  1.00 61.57  ? 197 ALA A CA    1 
ATOM   1229 C  C     . ALA A 1 170 ? 68.473  25.938  36.769  1.00 68.03  ? 197 ALA A C     1 
ATOM   1230 O  O     . ALA A 1 170 ? 68.130  27.080  37.096  1.00 61.33  ? 197 ALA A O     1 
ATOM   1231 C  CB    . ALA A 1 170 ? 68.355  26.021  34.280  1.00 58.73  ? 197 ALA A CB    1 
ATOM   1232 N  N     . TYR A 1 171 ? 68.179  24.863  37.498  1.00 58.79  ? 198 TYR A N     1 
ATOM   1233 C  CA    . TYR A 1 171 ? 67.443  24.973  38.749  1.00 54.63  ? 198 TYR A CA    1 
ATOM   1234 C  C     . TYR A 1 171 ? 68.186  25.871  39.730  1.00 52.74  ? 198 TYR A C     1 
ATOM   1235 O  O     . TYR A 1 171 ? 69.419  25.908  39.763  1.00 57.17  ? 198 TYR A O     1 
ATOM   1236 C  CB    . TYR A 1 171 ? 67.233  23.585  39.365  1.00 49.30  ? 198 TYR A CB    1 
ATOM   1237 C  CG    . TYR A 1 171 ? 66.483  23.585  40.686  1.00 55.21  ? 198 TYR A CG    1 
ATOM   1238 C  CD1   . TYR A 1 171 ? 67.156  23.748  41.893  1.00 56.60  ? 198 TYR A CD1   1 
ATOM   1239 C  CD2   . TYR A 1 171 ? 65.105  23.403  40.727  1.00 47.41  ? 198 TYR A CD2   1 
ATOM   1240 C  CE1   . TYR A 1 171 ? 66.478  23.749  43.096  1.00 43.50  ? 198 TYR A CE1   1 
ATOM   1241 C  CE2   . TYR A 1 171 ? 64.421  23.398  41.929  1.00 55.50  ? 198 TYR A CE2   1 
ATOM   1242 C  CZ    . TYR A 1 171 ? 65.112  23.573  43.108  1.00 46.98  ? 198 TYR A CZ    1 
ATOM   1243 O  OH    . TYR A 1 171 ? 64.432  23.565  44.304  1.00 54.33  ? 198 TYR A OH    1 
ATOM   1244 N  N     . SER A 1 172 ? 67.417  26.604  40.531  1.00 51.40  ? 199 SER A N     1 
ATOM   1245 C  CA    . SER A 1 172 ? 67.953  27.401  41.627  1.00 50.99  ? 199 SER A CA    1 
ATOM   1246 C  C     . SER A 1 172 ? 66.821  27.640  42.618  1.00 53.03  ? 199 SER A C     1 
ATOM   1247 O  O     . SER A 1 172 ? 65.694  27.179  42.421  1.00 57.39  ? 199 SER A O     1 
ATOM   1248 C  CB    . SER A 1 172 ? 68.564  28.715  41.121  1.00 53.69  ? 199 SER A CB    1 
ATOM   1249 O  OG    . SER A 1 172 ? 69.346  29.334  42.131  1.00 52.22  ? 199 SER A OG    1 
ATOM   1250 N  N     . ASN A 1 173 ? 67.126  28.368  43.687  1.00 53.06  ? 200 ASN A N     1 
ATOM   1251 C  CA    . ASN A 1 173 ? 66.170  28.567  44.776  1.00 42.74  ? 200 ASN A CA    1 
ATOM   1252 C  C     . ASN A 1 173 ? 65.344  29.839  44.595  1.00 51.46  ? 200 ASN A C     1 
ATOM   1253 O  O     . ASN A 1 173 ? 65.209  30.643  45.515  1.00 57.35  ? 200 ASN A O     1 
ATOM   1254 C  CB    . ASN A 1 173 ? 66.905  28.576  46.112  1.00 48.86  ? 200 ASN A CB    1 
ATOM   1255 C  CG    . ASN A 1 173 ? 68.072  29.547  46.133  1.00 55.20  ? 200 ASN A CG    1 
ATOM   1256 O  OD1   . ASN A 1 173 ? 68.916  29.547  45.236  1.00 52.68  ? 200 ASN A OD1   1 
ATOM   1257 N  ND2   . ASN A 1 173 ? 68.121  30.385  47.161  1.00 51.22  ? 200 ASN A ND2   1 
ATOM   1258 N  N     . PHE A 1 174 ? 64.778  30.029  43.404  1.00 52.75  ? 201 PHE A N     1 
ATOM   1259 C  CA    . PHE A 1 174 ? 63.914  31.177  43.152  1.00 55.39  ? 201 PHE A CA    1 
ATOM   1260 C  C     . PHE A 1 174 ? 63.169  30.969  41.841  1.00 55.81  ? 201 PHE A C     1 
ATOM   1261 O  O     . PHE A 1 174 ? 63.566  30.155  41.003  1.00 55.18  ? 201 PHE A O     1 
ATOM   1262 C  CB    . PHE A 1 174 ? 64.707  32.490  43.108  1.00 57.69  ? 201 PHE A CB    1 
ATOM   1263 C  CG    . PHE A 1 174 ? 65.505  32.677  41.847  1.00 47.08  ? 201 PHE A CG    1 
ATOM   1264 C  CD1   . PHE A 1 174 ? 66.737  32.067  41.694  1.00 59.33  ? 201 PHE A CD1   1 
ATOM   1265 C  CD2   . PHE A 1 174 ? 65.021  33.468  40.819  1.00 51.72  ? 201 PHE A CD2   1 
ATOM   1266 C  CE1   . PHE A 1 174 ? 67.471  32.237  40.534  1.00 59.48  ? 201 PHE A CE1   1 
ATOM   1267 C  CE2   . PHE A 1 174 ? 65.751  33.639  39.660  1.00 55.71  ? 201 PHE A CE2   1 
ATOM   1268 C  CZ    . PHE A 1 174 ? 66.976  33.024  39.518  1.00 54.28  ? 201 PHE A CZ    1 
ATOM   1269 N  N     . TRP A 1 175 ? 62.077  31.716  41.685  1.00 55.57  ? 202 TRP A N     1 
ATOM   1270 C  CA    . TRP A 1 175 ? 61.347  31.835  40.430  1.00 58.77  ? 202 TRP A CA    1 
ATOM   1271 C  C     . TRP A 1 175 ? 61.314  33.298  40.020  1.00 53.54  ? 202 TRP A C     1 
ATOM   1272 O  O     . TRP A 1 175 ? 61.222  34.185  40.874  1.00 67.03  ? 202 TRP A O     1 
ATOM   1273 C  CB    . TRP A 1 175 ? 59.898  31.343  40.536  1.00 53.33  ? 202 TRP A CB    1 
ATOM   1274 C  CG    . TRP A 1 175 ? 59.692  29.966  41.071  1.00 61.98  ? 202 TRP A CG    1 
ATOM   1275 C  CD1   . TRP A 1 175 ? 60.646  29.034  41.359  1.00 60.31  ? 202 TRP A CD1   1 
ATOM   1276 C  CD2   . TRP A 1 175 ? 58.433  29.363  41.380  1.00 61.52  ? 202 TRP A CD2   1 
ATOM   1277 N  NE1   . TRP A 1 175 ? 60.055  27.887  41.832  1.00 52.83  ? 202 TRP A NE1   1 
ATOM   1278 C  CE2   . TRP A 1 175 ? 58.696  28.065  41.853  1.00 50.67  ? 202 TRP A CE2   1 
ATOM   1279 C  CE3   . TRP A 1 175 ? 57.107  29.798  41.301  1.00 65.72  ? 202 TRP A CE3   1 
ATOM   1280 C  CZ2   . TRP A 1 175 ? 57.682  27.196  42.247  1.00 53.20  ? 202 TRP A CZ2   1 
ATOM   1281 C  CZ3   . TRP A 1 175 ? 56.101  28.936  41.693  1.00 62.79  ? 202 TRP A CZ3   1 
ATOM   1282 C  CH2   . TRP A 1 175 ? 56.394  27.649  42.160  1.00 55.74  ? 202 TRP A CH2   1 
ATOM   1283 N  N     . CYS A 1 176 ? 61.368  33.553  38.717  1.00 61.19  ? 203 CYS A N     1 
ATOM   1284 C  CA    . CYS A 1 176 ? 61.177  34.904  38.211  1.00 70.61  ? 203 CYS A CA    1 
ATOM   1285 C  C     . CYS A 1 176 ? 59.728  35.201  37.845  1.00 79.05  ? 203 CYS A C     1 
ATOM   1286 O  O     . CYS A 1 176 ? 59.381  36.372  37.657  1.00 76.00  ? 203 CYS A O     1 
ATOM   1287 C  CB    . CYS A 1 176 ? 62.073  35.147  36.993  1.00 67.35  ? 203 CYS A CB    1 
ATOM   1288 S  SG    . CYS A 1 176 ? 63.780  35.580  37.398  1.00 93.23  ? 203 CYS A SG    1 
ATOM   1289 N  N     . GLY A 1 177 ? 58.882  34.185  37.748  1.00 76.52  ? 204 GLY A N     1 
ATOM   1290 C  CA    . GLY A 1 177 ? 57.488  34.394  37.398  1.00 76.91  ? 204 GLY A CA    1 
ATOM   1291 C  C     . GLY A 1 177 ? 56.594  33.392  38.090  1.00 73.63  ? 204 GLY A C     1 
ATOM   1292 O  O     . GLY A 1 177 ? 57.020  32.286  38.439  1.00 70.46  ? 204 GLY A O     1 
ATOM   1293 N  N     . MET A 1 178 ? 55.338  33.787  38.287  1.00 73.22  ? 205 MET A N     1 
ATOM   1294 C  CA    . MET A 1 178 ? 54.337  32.939  38.914  1.00 80.01  ? 205 MET A CA    1 
ATOM   1295 C  C     . MET A 1 178 ? 52.988  33.208  38.267  1.00 81.29  ? 205 MET A C     1 
ATOM   1296 O  O     . MET A 1 178 ? 52.615  34.364  38.055  1.00 88.71  ? 205 MET A O     1 
ATOM   1297 C  CB    . MET A 1 178 ? 54.254  33.187  40.426  1.00 72.42  ? 205 MET A CB    1 
ATOM   1298 C  CG    . MET A 1 178 ? 53.248  32.303  41.146  1.00 80.31  ? 205 MET A CG    1 
ATOM   1299 S  SD    . MET A 1 178 ? 53.131  32.668  42.907  1.00 84.85  ? 205 MET A SD    1 
ATOM   1300 C  CE    . MET A 1 178 ? 54.829  32.415  43.411  1.00 55.21  ? 205 MET A CE    1 
ATOM   1301 N  N     . THR A 1 179 ? 52.263  32.136  37.955  1.00 91.30  ? 206 THR A N     1 
ATOM   1302 C  CA    . THR A 1 179 ? 50.962  32.261  37.319  1.00 89.85  ? 206 THR A CA    1 
ATOM   1303 C  C     . THR A 1 179 ? 49.920  32.720  38.337  1.00 93.13  ? 206 THR A C     1 
ATOM   1304 O  O     . THR A 1 179 ? 50.199  32.880  39.529  1.00 84.96  ? 206 THR A O     1 
ATOM   1305 C  CB    . THR A 1 179 ? 50.544  30.937  36.683  1.00 82.32  ? 206 THR A CB    1 
ATOM   1306 O  OG1   . THR A 1 179 ? 50.033  30.060  37.694  1.00 95.37  ? 206 THR A OG1   1 
ATOM   1307 C  CG2   . THR A 1 179 ? 51.734  30.274  36.004  1.00 85.03  ? 206 THR A CG2   1 
ATOM   1308 N  N     . SER A 1 180 ? 48.693  32.929  37.857  1.00 108.55 ? 207 SER A N     1 
ATOM   1309 C  CA    . SER A 1 180 ? 47.591  33.315  38.728  1.00 104.42 ? 207 SER A CA    1 
ATOM   1310 C  C     . SER A 1 180 ? 47.148  32.190  39.653  1.00 99.85  ? 207 SER A C     1 
ATOM   1311 O  O     . SER A 1 180 ? 46.328  32.433  40.545  1.00 92.72  ? 207 SER A O     1 
ATOM   1312 C  CB    . SER A 1 180 ? 46.407  33.794  37.885  1.00 101.11 ? 207 SER A CB    1 
ATOM   1313 O  OG    . SER A 1 180 ? 46.070  32.839  36.892  1.00 100.75 ? 207 SER A OG    1 
ATOM   1314 N  N     . GLN A 1 181 ? 47.668  30.974  39.469  1.00 99.89  ? 208 GLN A N     1 
ATOM   1315 C  CA    . GLN A 1 181 ? 47.308  29.830  40.299  1.00 91.85  ? 208 GLN A CA    1 
ATOM   1316 C  C     . GLN A 1 181 ? 48.497  29.300  41.094  1.00 83.20  ? 208 GLN A C     1 
ATOM   1317 O  O     . GLN A 1 181 ? 48.448  28.176  41.603  1.00 94.85  ? 208 GLN A O     1 
ATOM   1318 C  CB    . GLN A 1 181 ? 46.702  28.722  39.437  1.00 100.98 ? 208 GLN A CB    1 
ATOM   1319 C  CG    . GLN A 1 181 ? 45.572  29.205  38.541  1.00 99.61  ? 208 GLN A CG    1 
ATOM   1320 C  CD    . GLN A 1 181 ? 44.867  28.077  37.814  1.00 118.99 ? 208 GLN A CD    1 
ATOM   1321 O  OE1   . GLN A 1 181 ? 45.277  26.920  37.890  1.00 130.19 ? 208 GLN A OE1   1 
ATOM   1322 N  NE2   . GLN A 1 181 ? 43.793  28.411  37.107  1.00 124.61 ? 208 GLN A NE2   1 
ATOM   1323 N  N     . GLY A 1 182 ? 49.565  30.086  41.210  1.00 81.36  ? 209 GLY A N     1 
ATOM   1324 C  CA    . GLY A 1 182 ? 50.720  29.692  41.991  1.00 74.43  ? 209 GLY A CA    1 
ATOM   1325 C  C     . GLY A 1 182 ? 51.710  28.800  41.280  1.00 78.60  ? 209 GLY A C     1 
ATOM   1326 O  O     . GLY A 1 182 ? 52.646  28.310  41.921  1.00 84.49  ? 209 GLY A O     1 
ATOM   1327 N  N     . TYR A 1 183 ? 51.542  28.573  39.982  1.00 90.25  ? 210 TYR A N     1 
ATOM   1328 C  CA    . TYR A 1 183 ? 52.444  27.696  39.252  1.00 86.80  ? 210 TYR A CA    1 
ATOM   1329 C  C     . TYR A 1 183 ? 53.675  28.462  38.787  1.00 74.84  ? 210 TYR A C     1 
ATOM   1330 O  O     . TYR A 1 183 ? 53.642  29.683  38.605  1.00 81.31  ? 210 TYR A O     1 
ATOM   1331 C  CB    . TYR A 1 183 ? 51.733  27.078  38.045  1.00 89.15  ? 210 TYR A CB    1 
ATOM   1332 C  CG    . TYR A 1 183 ? 50.425  26.391  38.375  1.00 99.81  ? 210 TYR A CG    1 
ATOM   1333 C  CD1   . TYR A 1 183 ? 50.254  25.710  39.576  1.00 106.91 ? 210 TYR A CD1   1 
ATOM   1334 C  CD2   . TYR A 1 183 ? 49.360  26.429  37.485  1.00 100.68 ? 210 TYR A CD2   1 
ATOM   1335 C  CE1   . TYR A 1 183 ? 49.056  25.084  39.878  1.00 114.25 ? 210 TYR A CE1   1 
ATOM   1336 C  CE2   . TYR A 1 183 ? 48.161  25.805  37.778  1.00 116.27 ? 210 TYR A CE2   1 
ATOM   1337 C  CZ    . TYR A 1 183 ? 48.014  25.135  38.975  1.00 122.05 ? 210 TYR A CZ    1 
ATOM   1338 O  OH    . TYR A 1 183 ? 46.821  24.514  39.269  1.00 111.68 ? 210 TYR A OH    1 
ATOM   1339 N  N     . TYR A 1 184 ? 54.772  27.729  38.601  1.00 63.58  ? 211 TYR A N     1 
ATOM   1340 C  CA    . TYR A 1 184 ? 55.994  28.340  38.099  1.00 73.44  ? 211 TYR A CA    1 
ATOM   1341 C  C     . TYR A 1 184 ? 55.783  28.868  36.687  1.00 84.15  ? 211 TYR A C     1 
ATOM   1342 O  O     . TYR A 1 184 ? 55.121  28.238  35.859  1.00 81.01  ? 211 TYR A O     1 
ATOM   1343 C  CB    . TYR A 1 184 ? 57.148  27.333  38.114  1.00 68.66  ? 211 TYR A CB    1 
ATOM   1344 C  CG    . TYR A 1 184 ? 58.396  27.827  37.408  1.00 77.19  ? 211 TYR A CG    1 
ATOM   1345 C  CD1   . TYR A 1 184 ? 59.298  28.668  38.048  1.00 77.49  ? 211 TYR A CD1   1 
ATOM   1346 C  CD2   . TYR A 1 184 ? 58.669  27.450  36.099  1.00 71.32  ? 211 TYR A CD2   1 
ATOM   1347 C  CE1   . TYR A 1 184 ? 60.438  29.122  37.403  1.00 83.48  ? 211 TYR A CE1   1 
ATOM   1348 C  CE2   . TYR A 1 184 ? 59.804  27.899  35.447  1.00 85.11  ? 211 TYR A CE2   1 
ATOM   1349 C  CZ    . TYR A 1 184 ? 60.686  28.734  36.103  1.00 90.46  ? 211 TYR A CZ    1 
ATOM   1350 O  OH    . TYR A 1 184 ? 61.819  29.184  35.460  1.00 86.43  ? 211 TYR A OH    1 
ATOM   1351 N  N     . LYS A 1 185 ? 56.350  30.040  36.422  1.00 81.35  ? 212 LYS A N     1 
ATOM   1352 C  CA    . LYS A 1 185 ? 56.281  30.688  35.121  1.00 80.07  ? 212 LYS A CA    1 
ATOM   1353 C  C     . LYS A 1 185 ? 57.674  31.178  34.760  1.00 80.74  ? 212 LYS A C     1 
ATOM   1354 O  O     . LYS A 1 185 ? 58.311  31.875  35.555  1.00 90.76  ? 212 LYS A O     1 
ATOM   1355 C  CB    . LYS A 1 185 ? 55.288  31.857  35.136  1.00 92.58  ? 212 LYS A CB    1 
ATOM   1356 C  CG    . LYS A 1 185 ? 55.208  32.639  33.833  1.00 85.92  ? 212 LYS A CG    1 
ATOM   1357 C  CD    . LYS A 1 185 ? 54.216  33.786  33.959  1.00 98.39  ? 212 LYS A CD    1 
ATOM   1358 C  CE    . LYS A 1 185 ? 54.128  34.602  32.678  1.00 114.36 ? 212 LYS A CE    1 
ATOM   1359 N  NZ    . LYS A 1 185 ? 53.140  35.712  32.797  1.00 100.31 ? 212 LYS A NZ    1 
ATOM   1360 N  N     . ARG A 1 186 ? 58.150  30.808  33.575  1.00 101.47 ? 213 ARG A N     1 
ATOM   1361 C  CA    . ARG A 1 186 ? 59.477  31.211  33.137  1.00 103.54 ? 213 ARG A CA    1 
ATOM   1362 C  C     . ARG A 1 186 ? 59.413  32.556  32.428  1.00 98.04  ? 213 ARG A C     1 
ATOM   1363 O  O     . ARG A 1 186 ? 58.516  32.806  31.618  1.00 94.94  ? 213 ARG A O     1 
ATOM   1364 C  CB    . ARG A 1 186 ? 60.100  30.165  32.212  1.00 107.62 ? 213 ARG A CB    1 
ATOM   1365 C  CG    . ARG A 1 186 ? 61.616  30.291  32.124  1.00 116.18 ? 213 ARG A CG    1 
ATOM   1366 C  CD    . ARG A 1 186 ? 62.244  29.223  31.245  1.00 145.30 ? 213 ARG A CD    1 
ATOM   1367 N  NE    . ARG A 1 186 ? 63.587  28.881  31.695  1.00 145.09 ? 213 ARG A NE    1 
ATOM   1368 C  CZ    . ARG A 1 186 ? 64.430  28.104  31.029  1.00 152.55 ? 213 ARG A CZ    1 
ATOM   1369 N  NH1   . ARG A 1 186 ? 64.097  27.550  29.875  1.00 134.85 ? 213 ARG A NH1   1 
ATOM   1370 N  NH2   . ARG A 1 186 ? 65.643  27.886  31.530  1.00 136.56 ? 213 ARG A NH2   1 
ATOM   1371 N  N     . THR A 1 187 ? 60.363  33.421  32.751  1.00 93.20  ? 214 THR A N     1 
ATOM   1372 C  CA    . THR A 1 187 ? 60.500  34.747  32.176  1.00 96.09  ? 214 THR A CA    1 
ATOM   1373 C  C     . THR A 1 187 ? 61.884  34.876  31.553  1.00 98.85  ? 214 THR A C     1 
ATOM   1374 O  O     . THR A 1 187 ? 62.797  34.108  31.883  1.00 89.92  ? 214 THR A O     1 
ATOM   1375 C  CB    . THR A 1 187 ? 60.309  35.841  33.238  1.00 96.19  ? 214 THR A CB    1 
ATOM   1376 O  OG1   . THR A 1 187 ? 61.506  35.972  34.015  1.00 90.09  ? 214 THR A OG1   1 
ATOM   1377 C  CG2   . THR A 1 187 ? 59.146  35.491  34.157  1.00 93.13  ? 214 THR A CG2   1 
ATOM   1378 N  N     . PRO A 1 188 ? 62.070  35.820  30.626  1.00 97.23  ? 215 PRO A N     1 
ATOM   1379 C  CA    . PRO A 1 188 ? 63.409  36.009  30.044  1.00 97.82  ? 215 PRO A CA    1 
ATOM   1380 C  C     . PRO A 1 188 ? 64.449  36.423  31.065  1.00 81.89  ? 215 PRO A C     1 
ATOM   1381 O  O     . PRO A 1 188 ? 65.642  36.179  30.854  1.00 84.34  ? 215 PRO A O     1 
ATOM   1382 C  CB    . PRO A 1 188 ? 63.182  37.102  28.989  1.00 87.04  ? 215 PRO A CB    1 
ATOM   1383 C  CG    . PRO A 1 188 ? 61.728  37.015  28.663  1.00 84.67  ? 215 PRO A CG    1 
ATOM   1384 C  CD    . PRO A 1 188 ? 61.054  36.640  29.945  1.00 95.05  ? 215 PRO A CD    1 
ATOM   1385 N  N     . ALA A 1 189 ? 64.032  37.026  32.180  1.00 71.30  ? 216 ALA A N     1 
ATOM   1386 C  CA    . ALA A 1 189 ? 64.989  37.506  33.170  1.00 84.88  ? 216 ALA A CA    1 
ATOM   1387 C  C     . ALA A 1 189 ? 65.667  36.375  33.930  1.00 85.95  ? 216 ALA A C     1 
ATOM   1388 O  O     . ALA A 1 189 ? 66.712  36.605  34.549  1.00 87.62  ? 216 ALA A O     1 
ATOM   1389 C  CB    . ALA A 1 189 ? 64.297  38.448  34.155  1.00 80.08  ? 216 ALA A CB    1 
ATOM   1390 N  N     . TYR A 1 190 ? 65.109  35.162  33.891  1.00 86.34  ? 217 TYR A N     1 
ATOM   1391 C  CA    . TYR A 1 190 ? 65.628  34.082  34.724  1.00 78.86  ? 217 TYR A CA    1 
ATOM   1392 C  C     . TYR A 1 190 ? 67.065  33.738  34.356  1.00 79.51  ? 217 TYR A C     1 
ATOM   1393 O  O     . TYR A 1 190 ? 67.940  33.665  35.227  1.00 73.69  ? 217 TYR A O     1 
ATOM   1394 C  CB    . TYR A 1 190 ? 64.737  32.844  34.610  1.00 72.00  ? 217 TYR A CB    1 
ATOM   1395 C  CG    . TYR A 1 190 ? 65.139  31.743  35.565  1.00 64.89  ? 217 TYR A CG    1 
ATOM   1396 C  CD1   . TYR A 1 190 ? 66.073  30.780  35.199  1.00 64.00  ? 217 TYR A CD1   1 
ATOM   1397 C  CD2   . TYR A 1 190 ? 64.598  31.677  36.841  1.00 60.16  ? 217 TYR A CD2   1 
ATOM   1398 C  CE1   . TYR A 1 190 ? 66.452  29.781  36.076  1.00 64.76  ? 217 TYR A CE1   1 
ATOM   1399 C  CE2   . TYR A 1 190 ? 64.969  30.682  37.724  1.00 65.32  ? 217 TYR A CE2   1 
ATOM   1400 C  CZ    . TYR A 1 190 ? 65.897  29.736  37.336  1.00 67.54  ? 217 TYR A CZ    1 
ATOM   1401 O  OH    . TYR A 1 190 ? 66.271  28.742  38.211  1.00 58.64  ? 217 TYR A OH    1 
ATOM   1402 N  N     . ILE A 1 191 ? 67.327  33.520  33.067  1.00 75.96  ? 218 ILE A N     1 
ATOM   1403 C  CA    . ILE A 1 191 ? 68.647  33.045  32.651  1.00 76.94  ? 218 ILE A CA    1 
ATOM   1404 C  C     . ILE A 1 191 ? 69.758  34.029  33.004  1.00 75.36  ? 218 ILE A C     1 
ATOM   1405 O  O     . ILE A 1 191 ? 70.766  33.600  33.589  1.00 81.44  ? 218 ILE A O     1 
ATOM   1406 C  CB    . ILE A 1 191 ? 68.629  32.679  31.154  1.00 82.40  ? 218 ILE A CB    1 
ATOM   1407 C  CG1   . ILE A 1 191 ? 67.573  31.606  30.889  1.00 80.71  ? 218 ILE A CG1   1 
ATOM   1408 C  CG2   . ILE A 1 191 ? 70.001  32.199  30.709  1.00 68.86  ? 218 ILE A CG2   1 
ATOM   1409 C  CD1   . ILE A 1 191 ? 67.789  30.339  31.685  1.00 89.93  ? 218 ILE A CD1   1 
ATOM   1410 N  N     . PRO A 1 192 ? 69.658  35.330  32.692  1.00 82.41  ? 219 PRO A N     1 
ATOM   1411 C  CA    . PRO A 1 192 ? 70.759  36.237  33.064  1.00 77.71  ? 219 PRO A CA    1 
ATOM   1412 C  C     . PRO A 1 192 ? 71.000  36.305  34.561  1.00 71.09  ? 219 PRO A C     1 
ATOM   1413 O  O     . PRO A 1 192 ? 72.154  36.413  34.994  1.00 73.08  ? 219 PRO A O     1 
ATOM   1414 C  CB    . PRO A 1 192 ? 70.305  37.590  32.497  1.00 71.30  ? 219 PRO A CB    1 
ATOM   1415 C  CG    . PRO A 1 192 ? 69.342  37.247  31.422  1.00 70.30  ? 219 PRO A CG    1 
ATOM   1416 C  CD    . PRO A 1 192 ? 68.622  36.037  31.917  1.00 75.73  ? 219 PRO A CD    1 
ATOM   1417 N  N     . ILE A 1 193 ? 69.938  36.244  35.366  1.00 69.18  ? 220 ILE A N     1 
ATOM   1418 C  CA    . ILE A 1 193 ? 70.111  36.168  36.812  1.00 66.93  ? 220 ILE A CA    1 
ATOM   1419 C  C     . ILE A 1 193 ? 70.783  34.857  37.198  1.00 62.53  ? 220 ILE A C     1 
ATOM   1420 O  O     . ILE A 1 193 ? 71.702  34.833  38.025  1.00 67.47  ? 220 ILE A O     1 
ATOM   1421 C  CB    . ILE A 1 193 ? 68.755  36.339  37.521  1.00 66.07  ? 220 ILE A CB    1 
ATOM   1422 C  CG1   . ILE A 1 193 ? 68.186  37.735  37.271  1.00 64.38  ? 220 ILE A CG1   1 
ATOM   1423 C  CG2   . ILE A 1 193 ? 68.896  36.074  39.008  1.00 63.41  ? 220 ILE A CG2   1 
ATOM   1424 C  CD1   . ILE A 1 193 ? 66.802  37.937  37.846  1.00 59.07  ? 220 ILE A CD1   1 
ATOM   1425 N  N     . ARG A 1 194 ? 70.343  33.750  36.597  1.00 64.47  ? 221 ARG A N     1 
ATOM   1426 C  CA    . ARG A 1 194 ? 70.871  32.438  36.957  1.00 65.14  ? 221 ARG A CA    1 
ATOM   1427 C  C     . ARG A 1 194 ? 72.349  32.315  36.606  1.00 63.90  ? 221 ARG A C     1 
ATOM   1428 O  O     . ARG A 1 194 ? 73.130  31.734  37.369  1.00 70.60  ? 221 ARG A O     1 
ATOM   1429 C  CB    . ARG A 1 194 ? 70.054  31.350  36.260  1.00 57.81  ? 221 ARG A CB    1 
ATOM   1430 C  CG    . ARG A 1 194 ? 70.556  29.940  36.480  1.00 61.26  ? 221 ARG A CG    1 
ATOM   1431 C  CD    . ARG A 1 194 ? 70.419  29.520  37.927  1.00 57.88  ? 221 ARG A CD    1 
ATOM   1432 N  NE    . ARG A 1 194 ? 70.972  28.189  38.136  1.00 66.11  ? 221 ARG A NE    1 
ATOM   1433 C  CZ    . ARG A 1 194 ? 72.241  27.946  38.427  1.00 68.12  ? 221 ARG A CZ    1 
ATOM   1434 N  NH1   . ARG A 1 194 ? 73.113  28.929  38.585  1.00 65.03  ? 221 ARG A NH1   1 
ATOM   1435 N  NH2   . ARG A 1 194 ? 72.646  26.687  38.562  1.00 63.76  ? 221 ARG A NH2   1 
ATOM   1436 N  N     . LYS A 1 195 ? 72.753  32.863  35.461  1.00 60.71  ? 222 LYS A N     1 
ATOM   1437 C  CA    . LYS A 1 195 ? 74.132  32.800  34.998  1.00 64.53  ? 222 LYS A CA    1 
ATOM   1438 C  C     . LYS A 1 195 ? 74.990  33.943  35.525  1.00 63.50  ? 222 LYS A C     1 
ATOM   1439 O  O     . LYS A 1 195 ? 76.143  34.080  35.101  1.00 71.55  ? 222 LYS A O     1 
ATOM   1440 C  CB    . LYS A 1 195 ? 74.176  32.794  33.468  1.00 80.17  ? 222 LYS A CB    1 
ATOM   1441 C  CG    . LYS A 1 195 ? 73.583  31.554  32.821  1.00 64.44  ? 222 LYS A CG    1 
ATOM   1442 C  CD    . LYS A 1 195 ? 73.689  31.638  31.306  1.00 96.82  ? 222 LYS A CD    1 
ATOM   1443 C  CE    . LYS A 1 195 ? 73.243  30.349  30.637  1.00 95.32  ? 222 LYS A CE    1 
ATOM   1444 N  NZ    . LYS A 1 195 ? 73.366  30.434  29.153  1.00 101.21 ? 222 LYS A NZ    1 
ATOM   1445 N  N     . ARG A 1 196 ? 74.453  34.763  36.430  1.00 68.13  ? 223 ARG A N     1 
ATOM   1446 C  CA    . ARG A 1 196 ? 75.160  35.925  36.975  1.00 63.22  ? 223 ARG A CA    1 
ATOM   1447 C  C     . ARG A 1 196 ? 75.607  36.877  35.869  1.00 73.26  ? 223 ARG A C     1 
ATOM   1448 O  O     . ARG A 1 196 ? 76.678  37.484  35.940  1.00 68.25  ? 223 ARG A O     1 
ATOM   1449 C  CB    . ARG A 1 196 ? 76.347  35.503  37.844  1.00 72.68  ? 223 ARG A CB    1 
ATOM   1450 C  CG    . ARG A 1 196 ? 75.947  34.893  39.175  1.00 68.04  ? 223 ARG A CG    1 
ATOM   1451 C  CD    . ARG A 1 196 ? 77.156  34.633  40.057  1.00 60.23  ? 223 ARG A CD    1 
ATOM   1452 N  NE    . ARG A 1 196 ? 76.781  33.919  41.271  1.00 80.63  ? 223 ARG A NE    1 
ATOM   1453 C  CZ    . ARG A 1 196 ? 76.804  32.600  41.402  1.00 81.20  ? 223 ARG A CZ    1 
ATOM   1454 N  NH1   . ARG A 1 196 ? 77.218  31.815  40.420  1.00 76.02  ? 223 ARG A NH1   1 
ATOM   1455 N  NH2   . ARG A 1 196 ? 76.401  32.054  42.546  1.00 88.44  ? 223 ARG A NH2   1 
ATOM   1456 N  N     . ASP A 1 197 ? 74.783  37.000  34.828  1.00 74.00  ? 224 ASP A N     1 
ATOM   1457 C  CA    . ASP A 1 197 ? 75.009  38.038  33.828  1.00 70.10  ? 224 ASP A CA    1 
ATOM   1458 C  C     . ASP A 1 197 ? 74.558  39.393  34.357  1.00 79.00  ? 224 ASP A C     1 
ATOM   1459 O  O     . ASP A 1 197 ? 75.270  40.393  34.216  1.00 84.43  ? 224 ASP A O     1 
ATOM   1460 C  CB    . ASP A 1 197 ? 74.285  37.686  32.527  1.00 75.45  ? 224 ASP A CB    1 
ATOM   1461 C  CG    . ASP A 1 197 ? 74.948  36.543  31.784  1.00 88.45  ? 224 ASP A CG    1 
ATOM   1462 O  OD1   . ASP A 1 197 ? 75.943  35.993  32.302  1.00 88.84  ? 224 ASP A OD1   1 
ATOM   1463 O  OD2   . ASP A 1 197 ? 74.477  36.198  30.679  1.00 91.77  ? 224 ASP A OD2   1 
ATOM   1464 N  N     . ARG A 1 198 ? 73.377  39.439  34.970  1.00 93.31  ? 225 ARG A N     1 
ATOM   1465 C  CA    . ARG A 1 198 ? 72.942  40.571  35.777  1.00 87.31  ? 225 ARG A CA    1 
ATOM   1466 C  C     . ARG A 1 198 ? 73.195  40.225  37.238  1.00 80.75  ? 225 ARG A C     1 
ATOM   1467 O  O     . ARG A 1 198 ? 72.692  39.210  37.734  1.00 79.38  ? 225 ARG A O     1 
ATOM   1468 C  CB    . ARG A 1 198 ? 71.461  40.880  35.552  1.00 91.68  ? 225 ARG A CB    1 
ATOM   1469 C  CG    . ARG A 1 198 ? 71.086  41.226  34.122  1.00 111.19 ? 225 ARG A CG    1 
ATOM   1470 C  CD    . ARG A 1 198 ? 69.581  41.106  33.906  1.00 123.24 ? 225 ARG A CD    1 
ATOM   1471 N  NE    . ARG A 1 198 ? 68.815  42.047  34.716  1.00 131.28 ? 225 ARG A NE    1 
ATOM   1472 C  CZ    . ARG A 1 198 ? 67.491  42.068  34.786  1.00 122.27 ? 225 ARG A CZ    1 
ATOM   1473 N  NH1   . ARG A 1 198 ? 66.749  41.201  34.116  1.00 115.48 ? 225 ARG A NH1   1 
ATOM   1474 N  NH2   . ARG A 1 198 ? 66.895  42.982  35.547  1.00 102.02 ? 225 ARG A NH2   1 
ATOM   1475 N  N     . ARG A 1 199 ? 73.978  41.056  37.920  1.00 78.43  ? 226 ARG A N     1 
ATOM   1476 C  CA    . ARG A 1 199 ? 74.298  40.854  39.327  1.00 78.49  ? 226 ARG A CA    1 
ATOM   1477 C  C     . ARG A 1 199 ? 73.586  41.904  40.166  1.00 60.67  ? 226 ARG A C     1 
ATOM   1478 O  O     . ARG A 1 199 ? 73.622  43.095  39.839  1.00 63.65  ? 226 ARG A O     1 
ATOM   1479 C  CB    . ARG A 1 199 ? 75.809  40.908  39.559  1.00 82.26  ? 226 ARG A CB    1 
ATOM   1480 C  CG    . ARG A 1 199 ? 76.562  39.750  38.928  1.00 65.11  ? 226 ARG A CG    1 
ATOM   1481 C  CD    . ARG A 1 199 ? 78.053  39.831  39.201  1.00 73.08  ? 226 ARG A CD    1 
ATOM   1482 N  NE    . ARG A 1 199 ? 78.777  38.728  38.580  1.00 90.85  ? 226 ARG A NE    1 
ATOM   1483 C  CZ    . ARG A 1 199 ? 79.122  37.610  39.206  1.00 97.62  ? 226 ARG A CZ    1 
ATOM   1484 N  NH1   . ARG A 1 199 ? 78.838  37.416  40.483  1.00 107.57 ? 226 ARG A NH1   1 
ATOM   1485 N  NH2   . ARG A 1 199 ? 79.774  36.665  38.533  1.00 89.41  ? 226 ARG A NH2   1 
ATOM   1486 N  N     . GLY A 1 200 ? 72.943  41.461  41.237  1.00 69.51  ? 227 GLY A N     1 
ATOM   1487 C  CA    . GLY A 1 200 ? 72.214  42.358  42.109  1.00 57.33  ? 227 GLY A CA    1 
ATOM   1488 C  C     . GLY A 1 200 ? 71.185  41.594  42.919  1.00 62.79  ? 227 GLY A C     1 
ATOM   1489 O  O     . GLY A 1 200 ? 71.177  40.365  42.949  1.00 60.37  ? 227 GLY A O     1 
ATOM   1490 N  N     . CYS A 1 201 ? 70.321  42.357  43.582  1.00 52.18  ? 228 CYS A N     1 
ATOM   1491 C  CA    . CYS A 1 201 ? 69.202  41.809  44.340  1.00 65.56  ? 228 CYS A CA    1 
ATOM   1492 C  C     . CYS A 1 201 ? 67.914  42.141  43.602  1.00 61.94  ? 228 CYS A C     1 
ATOM   1493 O  O     . CYS A 1 201 ? 67.570  43.318  43.443  1.00 56.28  ? 228 CYS A O     1 
ATOM   1494 C  CB    . CYS A 1 201 ? 69.169  42.364  45.763  1.00 52.66  ? 228 CYS A CB    1 
ATOM   1495 S  SG    . CYS A 1 201 ? 70.602  41.912  46.760  1.00 100.41 ? 228 CYS A SG    1 
ATOM   1496 N  N     . PHE A 1 202 ? 67.206  41.108  43.158  1.00 64.11  ? 229 PHE A N     1 
ATOM   1497 C  CA    . PHE A 1 202 ? 66.062  41.265  42.272  1.00 62.09  ? 229 PHE A CA    1 
ATOM   1498 C  C     . PHE A 1 202 ? 64.777  40.868  42.982  1.00 53.97  ? 229 PHE A C     1 
ATOM   1499 O  O     . PHE A 1 202 ? 64.730  39.852  43.682  1.00 56.28  ? 229 PHE A O     1 
ATOM   1500 C  CB    . PHE A 1 202 ? 66.240  40.422  41.006  1.00 53.27  ? 229 PHE A CB    1 
ATOM   1501 C  CG    . PHE A 1 202 ? 67.544  40.659  40.304  1.00 60.61  ? 229 PHE A CG    1 
ATOM   1502 C  CD1   . PHE A 1 202 ? 67.694  41.727  39.438  1.00 57.60  ? 229 PHE A CD1   1 
ATOM   1503 C  CD2   . PHE A 1 202 ? 68.622  39.818  40.515  1.00 56.77  ? 229 PHE A CD2   1 
ATOM   1504 C  CE1   . PHE A 1 202 ? 68.895  41.950  38.792  1.00 62.41  ? 229 PHE A CE1   1 
ATOM   1505 C  CE2   . PHE A 1 202 ? 69.826  40.035  39.873  1.00 65.67  ? 229 PHE A CE2   1 
ATOM   1506 C  CZ    . PHE A 1 202 ? 69.963  41.102  39.010  1.00 70.81  ? 229 PHE A CZ    1 
ATOM   1507 N  N     . ALA A 1 203 ? 63.739  41.678  42.797  1.00 48.93  ? 230 ALA A N     1 
ATOM   1508 C  CA    . ALA A 1 203 ? 62.419  41.346  43.315  1.00 64.31  ? 230 ALA A CA    1 
ATOM   1509 C  C     . ALA A 1 203 ? 61.835  40.184  42.519  1.00 62.10  ? 230 ALA A C     1 
ATOM   1510 O  O     . ALA A 1 203 ? 61.629  40.298  41.308  1.00 61.16  ? 230 ALA A O     1 
ATOM   1511 C  CB    . ALA A 1 203 ? 61.506  42.565  43.234  1.00 52.79  ? 230 ALA A CB    1 
ATOM   1512 N  N     . VAL A 1 204 ? 61.574  39.066  43.189  1.00 50.13  ? 231 VAL A N     1 
ATOM   1513 C  CA    . VAL A 1 204 ? 61.029  37.885  42.521  1.00 50.75  ? 231 VAL A CA    1 
ATOM   1514 C  C     . VAL A 1 204 ? 59.802  37.396  43.283  1.00 64.48  ? 231 VAL A C     1 
ATOM   1515 O  O     . VAL A 1 204 ? 59.686  37.658  44.485  1.00 65.81  ? 231 VAL A O     1 
ATOM   1516 C  CB    . VAL A 1 204 ? 62.094  36.781  42.402  1.00 45.92  ? 231 VAL A CB    1 
ATOM   1517 C  CG1   . VAL A 1 204 ? 63.222  37.221  41.484  1.00 51.53  ? 231 VAL A CG1   1 
ATOM   1518 C  CG2   . VAL A 1 204 ? 62.627  36.422  43.771  1.00 47.02  ? 231 VAL A CG2   1 
ATOM   1519 N  N     . PRO A 1 205 ? 58.866  36.692  42.640  1.00 52.99  ? 232 PRO A N     1 
ATOM   1520 C  CA    . PRO A 1 205 ? 57.676  36.219  43.355  1.00 47.43  ? 232 PRO A CA    1 
ATOM   1521 C  C     . PRO A 1 205 ? 57.896  34.963  44.180  1.00 50.97  ? 232 PRO A C     1 
ATOM   1522 O  O     . PRO A 1 205 ? 56.944  34.495  44.812  1.00 50.61  ? 232 PRO A O     1 
ATOM   1523 C  CB    . PRO A 1 205 ? 56.682  35.949  42.215  1.00 58.31  ? 232 PRO A CB    1 
ATOM   1524 C  CG    . PRO A 1 205 ? 57.543  35.550  41.078  1.00 56.85  ? 232 PRO A CG    1 
ATOM   1525 C  CD    . PRO A 1 205 ? 58.783  36.406  41.195  1.00 49.47  ? 232 PRO A CD    1 
ATOM   1526 N  N     . MET A 1 206 ? 59.101  34.396  44.196  1.00 55.10  ? 233 MET A N     1 
ATOM   1527 C  CA    . MET A 1 206 ? 59.313  33.126  44.879  1.00 52.88  ? 233 MET A CA    1 
ATOM   1528 C  C     . MET A 1 206 ? 60.784  32.963  45.225  1.00 51.98  ? 233 MET A C     1 
ATOM   1529 O  O     . MET A 1 206 ? 61.644  33.081  44.348  1.00 59.39  ? 233 MET A O     1 
ATOM   1530 C  CB    . MET A 1 206 ? 58.850  31.954  44.007  1.00 49.38  ? 233 MET A CB    1 
ATOM   1531 C  CG    . MET A 1 206 ? 59.232  30.590  44.558  1.00 50.49  ? 233 MET A CG    1 
ATOM   1532 S  SD    . MET A 1 206 ? 58.353  30.202  46.081  1.00 54.14  ? 233 MET A SD    1 
ATOM   1533 C  CE    . MET A 1 206 ? 56.703  29.928  45.442  1.00 58.93  ? 233 MET A CE    1 
ATOM   1534 N  N     . VAL A 1 207 ? 61.061  32.699  46.502  1.00 53.24  ? 234 VAL A N     1 
ATOM   1535 C  CA    . VAL A 1 207 ? 62.357  32.220  46.966  1.00 41.34  ? 234 VAL A CA    1 
ATOM   1536 C  C     . VAL A 1 207 ? 62.093  31.092  47.952  1.00 48.09  ? 234 VAL A C     1 
ATOM   1537 O  O     . VAL A 1 207 ? 61.041  31.046  48.596  1.00 52.85  ? 234 VAL A O     1 
ATOM   1538 C  CB    . VAL A 1 207 ? 63.205  33.325  47.627  1.00 44.17  ? 234 VAL A CB    1 
ATOM   1539 C  CG1   . VAL A 1 207 ? 63.573  34.398  46.619  1.00 46.45  ? 234 VAL A CG1   1 
ATOM   1540 C  CG2   . VAL A 1 207 ? 62.466  33.922  48.809  1.00 46.71  ? 234 VAL A CG2   1 
ATOM   1541 N  N     . HIS A 1 208 ? 63.051  30.176  48.067  1.00 46.30  ? 235 HIS A N     1 
ATOM   1542 C  CA    . HIS A 1 208 ? 62.878  29.013  48.929  1.00 43.24  ? 235 HIS A CA    1 
ATOM   1543 C  C     . HIS A 1 208 ? 64.242  28.408  49.243  1.00 45.97  ? 235 HIS A C     1 
ATOM   1544 O  O     . HIS A 1 208 ? 65.287  28.941  48.856  1.00 39.11  ? 235 HIS A O     1 
ATOM   1545 C  CB    . HIS A 1 208 ? 61.947  27.983  48.281  1.00 40.47  ? 235 HIS A CB    1 
ATOM   1546 C  CG    . HIS A 1 208 ? 62.468  27.424  46.993  1.00 52.26  ? 235 HIS A CG    1 
ATOM   1547 N  ND1   . HIS A 1 208 ? 63.411  26.420  46.944  1.00 44.66  ? 235 HIS A ND1   1 
ATOM   1548 C  CD2   . HIS A 1 208 ? 62.174  27.728  45.707  1.00 41.15  ? 235 HIS A CD2   1 
ATOM   1549 C  CE1   . HIS A 1 208 ? 63.677  26.131  45.683  1.00 55.25  ? 235 HIS A CE1   1 
ATOM   1550 N  NE2   . HIS A 1 208 ? 62.940  26.910  44.912  1.00 50.29  ? 235 HIS A NE2   1 
ATOM   1551 N  N     . SER A 1 209 ? 64.209  27.285  49.970  1.00 46.03  ? 236 SER A N     1 
ATOM   1552 C  CA    . SER A 1 209 ? 65.375  26.477  50.322  1.00 43.06  ? 236 SER A CA    1 
ATOM   1553 C  C     . SER A 1 209 ? 66.289  27.180  51.322  1.00 47.76  ? 236 SER A C     1 
ATOM   1554 O  O     . SER A 1 209 ? 66.497  26.677  52.432  1.00 52.30  ? 236 SER A O     1 
ATOM   1555 C  CB    . SER A 1 209 ? 66.154  26.075  49.066  1.00 44.70  ? 236 SER A CB    1 
ATOM   1556 O  OG    . SER A 1 209 ? 65.390  25.189  48.261  1.00 59.92  ? 236 SER A OG    1 
ATOM   1557 N  N     . THR A 1 210 ? 66.845  28.331  50.951  1.00 45.53  ? 237 THR A N     1 
ATOM   1558 C  CA    . THR A 1 210 ? 67.668  29.119  51.864  1.00 46.26  ? 237 THR A CA    1 
ATOM   1559 C  C     . THR A 1 210 ? 67.298  30.584  51.707  1.00 45.95  ? 237 THR A C     1 
ATOM   1560 O  O     . THR A 1 210 ? 67.470  31.155  50.627  1.00 44.72  ? 237 THR A O     1 
ATOM   1561 C  CB    . THR A 1 210 ? 69.165  28.912  51.601  1.00 45.63  ? 237 THR A CB    1 
ATOM   1562 O  OG1   . THR A 1 210 ? 69.538  27.576  51.962  1.00 45.47  ? 237 THR A OG1   1 
ATOM   1563 C  CG2   . THR A 1 210 ? 69.991  29.898  52.416  1.00 38.35  ? 237 THR A CG2   1 
ATOM   1564 N  N     . PHE A 1 211 ? 66.792  31.189  52.779  1.00 47.22  ? 238 PHE A N     1 
ATOM   1565 C  CA    . PHE A 1 211 ? 66.383  32.585  52.729  1.00 44.48  ? 238 PHE A CA    1 
ATOM   1566 C  C     . PHE A 1 211 ? 66.397  33.159  54.138  1.00 45.86  ? 238 PHE A C     1 
ATOM   1567 O  O     . PHE A 1 211 ? 66.369  32.426  55.130  1.00 41.13  ? 238 PHE A O     1 
ATOM   1568 C  CB    . PHE A 1 211 ? 65.001  32.743  52.084  1.00 48.05  ? 238 PHE A CB    1 
ATOM   1569 C  CG    . PHE A 1 211 ? 63.922  31.947  52.757  1.00 50.14  ? 238 PHE A CG    1 
ATOM   1570 C  CD1   . PHE A 1 211 ? 63.193  32.491  53.803  1.00 35.64  ? 238 PHE A CD1   1 
ATOM   1571 C  CD2   . PHE A 1 211 ? 63.635  30.656  52.342  1.00 46.15  ? 238 PHE A CD2   1 
ATOM   1572 C  CE1   . PHE A 1 211 ? 62.199  31.761  54.424  1.00 52.53  ? 238 PHE A CE1   1 
ATOM   1573 C  CE2   . PHE A 1 211 ? 62.642  29.917  52.958  1.00 44.19  ? 238 PHE A CE2   1 
ATOM   1574 C  CZ    . PHE A 1 211 ? 61.922  30.470  54.002  1.00 65.99  ? 238 PHE A CZ    1 
ATOM   1575 N  N     . LEU A 1 212 ? 66.430  34.489  54.205  1.00 46.17  ? 239 LEU A N     1 
ATOM   1576 C  CA    . LEU A 1 212 ? 66.593  35.229  55.449  1.00 41.84  ? 239 LEU A CA    1 
ATOM   1577 C  C     . LEU A 1 212 ? 65.383  36.123  55.681  1.00 49.29  ? 239 LEU A C     1 
ATOM   1578 O  O     . LEU A 1 212 ? 65.000  36.897  54.797  1.00 47.33  ? 239 LEU A O     1 
ATOM   1579 C  CB    . LEU A 1 212 ? 67.870  36.072  55.406  1.00 41.73  ? 239 LEU A CB    1 
ATOM   1580 C  CG    . LEU A 1 212 ? 68.261  36.840  56.664  1.00 45.78  ? 239 LEU A CG    1 
ATOM   1581 C  CD1   . LEU A 1 212 ? 68.753  35.877  57.726  1.00 42.85  ? 239 LEU A CD1   1 
ATOM   1582 C  CD2   . LEU A 1 212 ? 69.321  37.878  56.339  1.00 42.96  ? 239 LEU A CD2   1 
ATOM   1583 N  N     . ILE A 1 213 ? 64.790  36.026  56.869  1.00 38.66  ? 240 ILE A N     1 
ATOM   1584 C  CA    . ILE A 1 213 ? 63.658  36.860  57.261  1.00 44.16  ? 240 ILE A CA    1 
ATOM   1585 C  C     . ILE A 1 213 ? 64.138  37.878  58.287  1.00 44.47  ? 240 ILE A C     1 
ATOM   1586 O  O     . ILE A 1 213 ? 64.801  37.516  59.267  1.00 45.24  ? 240 ILE A O     1 
ATOM   1587 C  CB    . ILE A 1 213 ? 62.498  36.020  57.822  1.00 47.19  ? 240 ILE A CB    1 
ATOM   1588 C  CG1   . ILE A 1 213 ? 62.107  34.920  56.839  1.00 44.21  ? 240 ILE A CG1   1 
ATOM   1589 C  CG2   . ILE A 1 213 ? 61.297  36.905  58.119  1.00 38.76  ? 240 ILE A CG2   1 
ATOM   1590 C  CD1   . ILE A 1 213 ? 60.927  34.092  57.302  1.00 42.88  ? 240 ILE A CD1   1 
ATOM   1591 N  N     . ASP A 1 214 ? 63.799  39.148  58.061  1.00 49.05  ? 241 ASP A N     1 
ATOM   1592 C  CA    . ASP A 1 214 ? 64.179  40.242  58.955  1.00 38.18  ? 241 ASP A CA    1 
ATOM   1593 C  C     . ASP A 1 214 ? 63.071  40.421  59.986  1.00 44.51  ? 241 ASP A C     1 
ATOM   1594 O  O     . ASP A 1 214 ? 62.040  41.036  59.709  1.00 44.23  ? 241 ASP A O     1 
ATOM   1595 C  CB    . ASP A 1 214 ? 64.420  41.523  58.163  1.00 50.31  ? 241 ASP A CB    1 
ATOM   1596 C  CG    . ASP A 1 214 ? 65.104  42.608  58.983  1.00 58.40  ? 241 ASP A CG    1 
ATOM   1597 O  OD1   . ASP A 1 214 ? 64.975  42.603  60.225  1.00 54.95  ? 241 ASP A OD1   1 
ATOM   1598 O  OD2   . ASP A 1 214 ? 65.776  43.471  58.377  1.00 58.40  ? 241 ASP A OD2   1 
ATOM   1599 N  N     . LEU A 1 215 ? 63.290  39.893  61.188  1.00 44.35  ? 242 LEU A N     1 
ATOM   1600 C  CA    . LEU A 1 215 ? 62.293  39.971  62.246  1.00 46.41  ? 242 LEU A CA    1 
ATOM   1601 C  C     . LEU A 1 215 ? 62.272  41.320  62.951  1.00 45.26  ? 242 LEU A C     1 
ATOM   1602 O  O     . LEU A 1 215 ? 61.446  41.516  63.850  1.00 53.04  ? 242 LEU A O     1 
ATOM   1603 C  CB    . LEU A 1 215 ? 62.532  38.855  63.260  1.00 38.85  ? 242 LEU A CB    1 
ATOM   1604 C  CG    . LEU A 1 215 ? 62.470  37.475  62.612  1.00 38.07  ? 242 LEU A CG    1 
ATOM   1605 C  CD1   . LEU A 1 215 ? 62.877  36.414  63.601  1.00 41.13  ? 242 LEU A CD1   1 
ATOM   1606 C  CD2   . LEU A 1 215 ? 61.074  37.207  62.077  1.00 38.84  ? 242 LEU A CD2   1 
ATOM   1607 N  N     . ARG A 1 216 ? 63.159  42.245  62.580  1.00 44.25  ? 243 ARG A N     1 
ATOM   1608 C  CA    . ARG A 1 216 ? 63.065  43.607  63.089  1.00 45.93  ? 243 ARG A CA    1 
ATOM   1609 C  C     . ARG A 1 216 ? 61.983  44.399  62.371  1.00 50.44  ? 243 ARG A C     1 
ATOM   1610 O  O     . ARG A 1 216 ? 61.438  45.352  62.938  1.00 50.41  ? 243 ARG A O     1 
ATOM   1611 C  CB    . ARG A 1 216 ? 64.401  44.328  62.938  1.00 38.64  ? 243 ARG A CB    1 
ATOM   1612 C  CG    . ARG A 1 216 ? 65.602  43.560  63.444  1.00 52.55  ? 243 ARG A CG    1 
ATOM   1613 C  CD    . ARG A 1 216 ? 66.874  44.242  62.976  1.00 51.59  ? 243 ARG A CD    1 
ATOM   1614 N  NE    . ARG A 1 216 ? 66.886  44.395  61.525  1.00 51.26  ? 243 ARG A NE    1 
ATOM   1615 C  CZ    . ARG A 1 216 ? 67.405  45.435  60.887  1.00 55.75  ? 243 ARG A CZ    1 
ATOM   1616 N  NH1   . ARG A 1 216 ? 67.956  46.445  61.543  1.00 48.17  ? 243 ARG A NH1   1 
ATOM   1617 N  NH2   . ARG A 1 216 ? 67.354  45.473  59.558  1.00 44.38  ? 243 ARG A NH2   1 
ATOM   1618 N  N     . LYS A 1 217 ? 61.670  44.026  61.132  1.00 56.35  ? 244 LYS A N     1 
ATOM   1619 C  CA    . LYS A 1 217 ? 60.680  44.754  60.352  1.00 45.71  ? 244 LYS A CA    1 
ATOM   1620 C  C     . LYS A 1 217 ? 59.281  44.459  60.875  1.00 49.79  ? 244 LYS A C     1 
ATOM   1621 O  O     . LYS A 1 217 ? 58.947  43.307  61.168  1.00 52.96  ? 244 LYS A O     1 
ATOM   1622 C  CB    . LYS A 1 217 ? 60.781  44.373  58.875  1.00 49.53  ? 244 LYS A CB    1 
ATOM   1623 C  CG    . LYS A 1 217 ? 62.162  44.548  58.255  1.00 50.29  ? 244 LYS A CG    1 
ATOM   1624 C  CD    . LYS A 1 217 ? 62.646  45.986  58.344  1.00 44.58  ? 244 LYS A CD    1 
ATOM   1625 C  CE    . LYS A 1 217 ? 63.543  46.340  57.168  1.00 50.50  ? 244 LYS A CE    1 
ATOM   1626 N  NZ    . LYS A 1 217 ? 64.675  45.387  57.014  1.00 59.61  ? 244 LYS A NZ    1 
ATOM   1627 N  N     . ALA A 1 218 ? 58.461  45.506  60.985  1.00 47.44  ? 245 ALA A N     1 
ATOM   1628 C  CA    . ALA A 1 218 ? 57.101  45.332  61.486  1.00 43.02  ? 245 ALA A CA    1 
ATOM   1629 C  C     . ALA A 1 218 ? 56.296  44.396  60.593  1.00 51.92  ? 245 ALA A C     1 
ATOM   1630 O  O     . ALA A 1 218 ? 55.472  43.615  61.083  1.00 48.96  ? 245 ALA A O     1 
ATOM   1631 C  CB    . ALA A 1 218 ? 56.409  46.689  61.602  1.00 39.97  ? 245 ALA A CB    1 
ATOM   1632 N  N     . ALA A 1 219 ? 56.528  44.454  59.278  1.00 52.22  ? 246 ALA A N     1 
ATOM   1633 C  CA    . ALA A 1 219 ? 55.776  43.623  58.344  1.00 46.58  ? 246 ALA A CA    1 
ATOM   1634 C  C     . ALA A 1 219 ? 56.066  42.139  58.517  1.00 48.24  ? 246 ALA A C     1 
ATOM   1635 O  O     . ALA A 1 219 ? 55.235  41.313  58.129  1.00 50.53  ? 246 ALA A O     1 
ATOM   1636 C  CB    . ALA A 1 219 ? 56.073  44.041  56.903  1.00 44.12  ? 246 ALA A CB    1 
ATOM   1637 N  N     . SER A 1 220 ? 57.219  41.780  59.088  1.00 43.72  ? 247 SER A N     1 
ATOM   1638 C  CA    . SER A 1 220 ? 57.522  40.372  59.318  1.00 50.76  ? 247 SER A CA    1 
ATOM   1639 C  C     . SER A 1 220 ? 56.540  39.726  60.284  1.00 48.10  ? 247 SER A C     1 
ATOM   1640 O  O     . SER A 1 220 ? 56.401  38.498  60.282  1.00 47.95  ? 247 SER A O     1 
ATOM   1641 C  CB    . SER A 1 220 ? 58.945  40.213  59.852  1.00 38.45  ? 247 SER A CB    1 
ATOM   1642 O  OG    . SER A 1 220 ? 59.037  40.669  61.190  1.00 47.05  ? 247 SER A OG    1 
ATOM   1643 N  N     . ARG A 1 221 ? 55.858  40.525  61.109  1.00 46.93  ? 248 ARG A N     1 
ATOM   1644 C  CA    . ARG A 1 221 ? 54.870  39.973  62.028  1.00 46.75  ? 248 ARG A CA    1 
ATOM   1645 C  C     . ARG A 1 221 ? 53.720  39.304  61.286  1.00 55.15  ? 248 ARG A C     1 
ATOM   1646 O  O     . ARG A 1 221 ? 53.096  38.378  61.818  1.00 55.18  ? 248 ARG A O     1 
ATOM   1647 C  CB    . ARG A 1 221 ? 54.334  41.073  62.945  1.00 49.75  ? 248 ARG A CB    1 
ATOM   1648 C  CG    . ARG A 1 221 ? 55.374  41.674  63.874  1.00 45.62  ? 248 ARG A CG    1 
ATOM   1649 C  CD    . ARG A 1 221 ? 54.846  42.935  64.543  1.00 52.65  ? 248 ARG A CD    1 
ATOM   1650 N  NE    . ARG A 1 221 ? 53.590  42.704  65.248  1.00 77.26  ? 248 ARG A NE    1 
ATOM   1651 C  CZ    . ARG A 1 221 ? 52.825  43.666  65.747  1.00 78.17  ? 248 ARG A CZ    1 
ATOM   1652 N  NH1   . ARG A 1 221 ? 53.156  44.941  65.631  1.00 65.93  ? 248 ARG A NH1   1 
ATOM   1653 N  NH2   . ARG A 1 221 ? 51.699  43.340  66.374  1.00 90.26  ? 248 ARG A NH2   1 
ATOM   1654 N  N     . ASN A 1 222 ? 53.426  39.748  60.063  1.00 55.28  ? 249 ASN A N     1 
ATOM   1655 C  CA    . ASN A 1 222 ? 52.305  39.210  59.303  1.00 43.79  ? 249 ASN A CA    1 
ATOM   1656 C  C     . ASN A 1 222 ? 52.662  37.972  58.490  1.00 41.16  ? 249 ASN A C     1 
ATOM   1657 O  O     . ASN A 1 222 ? 51.770  37.380  57.873  1.00 53.91  ? 249 ASN A O     1 
ATOM   1658 C  CB    . ASN A 1 222 ? 51.741  40.284  58.367  1.00 49.67  ? 249 ASN A CB    1 
ATOM   1659 C  CG    . ASN A 1 222 ? 51.227  41.497  59.116  1.00 63.59  ? 249 ASN A CG    1 
ATOM   1660 O  OD1   . ASN A 1 222 ? 50.781  41.396  60.260  1.00 52.98  ? 249 ASN A OD1   1 
ATOM   1661 N  ND2   . ASN A 1 222 ? 51.286  42.656  58.472  1.00 58.50  ? 249 ASN A ND2   1 
ATOM   1662 N  N     . LEU A 1 223 ? 53.929  37.570  58.469  1.00 41.31  ? 250 LEU A N     1 
ATOM   1663 C  CA    . LEU A 1 223 ? 54.334  36.375  57.745  1.00 35.03  ? 250 LEU A CA    1 
ATOM   1664 C  C     . LEU A 1 223 ? 54.002  35.132  58.555  1.00 45.70  ? 250 LEU A C     1 
ATOM   1665 O  O     . LEU A 1 223 ? 54.128  35.121  59.783  1.00 44.02  ? 250 LEU A O     1 
ATOM   1666 C  CB    . LEU A 1 223 ? 55.833  36.410  57.445  1.00 40.99  ? 250 LEU A CB    1 
ATOM   1667 C  CG    . LEU A 1 223 ? 56.349  37.582  56.611  1.00 46.68  ? 250 LEU A CG    1 
ATOM   1668 C  CD1   . LEU A 1 223 ? 57.859  37.502  56.435  1.00 48.11  ? 250 LEU A CD1   1 
ATOM   1669 C  CD2   . LEU A 1 223 ? 55.652  37.615  55.265  1.00 52.72  ? 250 LEU A CD2   1 
ATOM   1670 N  N     . ALA A 1 224 ? 53.582  34.079  57.861  1.00 46.49  ? 251 ALA A N     1 
ATOM   1671 C  CA    . ALA A 1 224 ? 53.248  32.825  58.519  1.00 41.05  ? 251 ALA A CA    1 
ATOM   1672 C  C     . ALA A 1 224 ? 53.486  31.678  57.552  1.00 49.56  ? 251 ALA A C     1 
ATOM   1673 O  O     . ALA A 1 224 ? 53.060  31.742  56.395  1.00 47.52  ? 251 ALA A O     1 
ATOM   1674 C  CB    . ALA A 1 224 ? 51.794  32.821  59.001  1.00 37.12  ? 251 ALA A CB    1 
ATOM   1675 N  N     . PHE A 1 225 ? 54.179  30.642  58.027  1.00 42.51  ? 252 PHE A N     1 
ATOM   1676 C  CA    . PHE A 1 225 ? 54.330  29.429  57.235  1.00 46.71  ? 252 PHE A CA    1 
ATOM   1677 C  C     . PHE A 1 225 ? 53.107  28.530  57.344  1.00 47.01  ? 252 PHE A C     1 
ATOM   1678 O  O     . PHE A 1 225 ? 52.823  27.762  56.418  1.00 56.38  ? 252 PHE A O     1 
ATOM   1679 C  CB    . PHE A 1 225 ? 55.577  28.659  57.668  1.00 37.24  ? 252 PHE A CB    1 
ATOM   1680 C  CG    . PHE A 1 225 ? 56.863  29.344  57.318  1.00 48.47  ? 252 PHE A CG    1 
ATOM   1681 C  CD1   . PHE A 1 225 ? 57.451  29.147  56.082  1.00 46.72  ? 252 PHE A CD1   1 
ATOM   1682 C  CD2   . PHE A 1 225 ? 57.486  30.181  58.227  1.00 45.96  ? 252 PHE A CD2   1 
ATOM   1683 C  CE1   . PHE A 1 225 ? 58.636  29.773  55.757  1.00 44.90  ? 252 PHE A CE1   1 
ATOM   1684 C  CE2   . PHE A 1 225 ? 58.672  30.810  57.908  1.00 41.38  ? 252 PHE A CE2   1 
ATOM   1685 C  CZ    . PHE A 1 225 ? 59.247  30.607  56.671  1.00 44.01  ? 252 PHE A CZ    1 
ATOM   1686 N  N     . TYR A 1 226 ? 52.376  28.613  58.461  1.00 47.24  ? 253 TYR A N     1 
ATOM   1687 C  CA    . TYR A 1 226 ? 51.177  27.815  58.670  1.00 51.29  ? 253 TYR A CA    1 
ATOM   1688 C  C     . TYR A 1 226 ? 50.317  28.502  59.715  1.00 48.53  ? 253 TYR A C     1 
ATOM   1689 O  O     . TYR A 1 226 ? 50.868  29.068  60.670  1.00 60.79  ? 253 TYR A O     1 
ATOM   1690 C  CB    . TYR A 1 226 ? 51.525  26.392  59.122  1.00 47.80  ? 253 TYR A CB    1 
ATOM   1691 C  CG    . TYR A 1 226 ? 50.374  25.420  59.008  1.00 57.78  ? 253 TYR A CG    1 
ATOM   1692 C  CD1   . TYR A 1 226 ? 50.105  24.772  57.810  1.00 53.16  ? 253 TYR A CD1   1 
ATOM   1693 C  CD2   . TYR A 1 226 ? 49.551  25.156  60.096  1.00 64.69  ? 253 TYR A CD2   1 
ATOM   1694 C  CE1   . TYR A 1 226 ? 49.051  23.885  57.699  1.00 63.26  ? 253 TYR A CE1   1 
ATOM   1695 C  CE2   . TYR A 1 226 ? 48.494  24.274  59.995  1.00 49.16  ? 253 TYR A CE2   1 
ATOM   1696 C  CZ    . TYR A 1 226 ? 48.249  23.640  58.795  1.00 63.18  ? 253 TYR A CZ    1 
ATOM   1697 O  OH    . TYR A 1 226 ? 47.198  22.758  58.690  1.00 70.86  ? 253 TYR A OH    1 
ATOM   1698 N  N     . PRO A 1 227 ? 48.982  28.486  59.579  1.00 54.27  ? 254 PRO A N     1 
ATOM   1699 C  CA    . PRO A 1 227 ? 48.185  27.903  58.487  1.00 52.36  ? 254 PRO A CA    1 
ATOM   1700 C  C     . PRO A 1 227 ? 48.244  28.752  57.223  1.00 59.04  ? 254 PRO A C     1 
ATOM   1701 O  O     . PRO A 1 227 ? 48.757  29.867  57.258  1.00 64.66  ? 254 PRO A O     1 
ATOM   1702 C  CB    . PRO A 1 227 ? 46.772  27.854  59.087  1.00 47.00  ? 254 PRO A CB    1 
ATOM   1703 C  CG    . PRO A 1 227 ? 46.739  29.010  60.033  1.00 48.07  ? 254 PRO A CG    1 
ATOM   1704 C  CD    . PRO A 1 227 ? 48.121  29.051  60.635  1.00 58.90  ? 254 PRO A CD    1 
ATOM   1705 N  N     . PRO A 1 228 ? 47.755  28.247  56.089  1.00 62.24  ? 255 PRO A N     1 
ATOM   1706 C  CA    . PRO A 1 228 ? 47.670  29.091  54.893  1.00 58.41  ? 255 PRO A CA    1 
ATOM   1707 C  C     . PRO A 1 228 ? 46.816  30.320  55.158  1.00 54.31  ? 255 PRO A C     1 
ATOM   1708 O  O     . PRO A 1 228 ? 45.943  30.320  56.029  1.00 62.07  ? 255 PRO A O     1 
ATOM   1709 C  CB    . PRO A 1 228 ? 47.024  28.171  53.852  1.00 60.17  ? 255 PRO A CB    1 
ATOM   1710 C  CG    . PRO A 1 228 ? 47.363  26.796  54.308  1.00 47.30  ? 255 PRO A CG    1 
ATOM   1711 C  CD    . PRO A 1 228 ? 47.379  26.850  55.808  1.00 48.76  ? 255 PRO A CD    1 
ATOM   1712 N  N     . HIS A 1 229 ? 47.086  31.376  54.400  1.00 52.25  ? 256 HIS A N     1 
ATOM   1713 C  CA    . HIS A 1 229 ? 46.356  32.621  54.577  1.00 47.99  ? 256 HIS A CA    1 
ATOM   1714 C  C     . HIS A 1 229 ? 44.864  32.385  54.347  1.00 54.42  ? 256 HIS A C     1 
ATOM   1715 O  O     . HIS A 1 229 ? 44.490  31.542  53.522  1.00 67.90  ? 256 HIS A O     1 
ATOM   1716 C  CB    . HIS A 1 229 ? 46.883  33.688  53.617  1.00 56.68  ? 256 HIS A CB    1 
ATOM   1717 C  CG    . HIS A 1 229 ? 46.300  35.048  53.844  1.00 57.94  ? 256 HIS A CG    1 
ATOM   1718 N  ND1   . HIS A 1 229 ? 45.071  35.422  53.347  1.00 67.57  ? 256 HIS A ND1   1 
ATOM   1719 C  CD2   . HIS A 1 229 ? 46.775  36.121  54.520  1.00 58.87  ? 256 HIS A CD2   1 
ATOM   1720 C  CE1   . HIS A 1 229 ? 44.814  36.667  53.704  1.00 63.78  ? 256 HIS A CE1   1 
ATOM   1721 N  NE2   . HIS A 1 229 ? 45.832  37.115  54.416  1.00 60.62  ? 256 HIS A NE2   1 
ATOM   1722 N  N     . PRO A 1 230 ? 43.990  33.084  55.073  1.00 66.11  ? 257 PRO A N     1 
ATOM   1723 C  CA    . PRO A 1 230 ? 42.543  32.866  54.899  1.00 71.15  ? 257 PRO A CA    1 
ATOM   1724 C  C     . PRO A 1 230 ? 42.056  32.948  53.459  1.00 60.41  ? 257 PRO A C     1 
ATOM   1725 O  O     . PRO A 1 230 ? 41.055  32.303  53.122  1.00 65.27  ? 257 PRO A O     1 
ATOM   1726 C  CB    . PRO A 1 230 ? 41.931  33.974  55.764  1.00 60.80  ? 257 PRO A CB    1 
ATOM   1727 C  CG    . PRO A 1 230 ? 42.934  34.179  56.849  1.00 52.91  ? 257 PRO A CG    1 
ATOM   1728 C  CD    . PRO A 1 230 ? 44.286  33.949  56.229  1.00 62.10  ? 257 PRO A CD    1 
ATOM   1729 N  N     . ASP A 1 231 ? 42.727  33.712  52.598  1.00 65.34  ? 258 ASP A N     1 
ATOM   1730 C  CA    . ASP A 1 231 ? 42.327  33.855  51.204  1.00 69.46  ? 258 ASP A CA    1 
ATOM   1731 C  C     . ASP A 1 231 ? 43.105  32.938  50.267  1.00 68.85  ? 258 ASP A C     1 
ATOM   1732 O  O     . ASP A 1 231 ? 43.007  33.090  49.046  1.00 62.64  ? 258 ASP A O     1 
ATOM   1733 C  CB    . ASP A 1 231 ? 42.485  35.310  50.757  1.00 73.34  ? 258 ASP A CB    1 
ATOM   1734 C  CG    . ASP A 1 231 ? 41.615  36.262  51.552  1.00 78.50  ? 258 ASP A CG    1 
ATOM   1735 O  OD1   . ASP A 1 231 ? 40.645  35.794  52.185  1.00 84.55  ? 258 ASP A OD1   1 
ATOM   1736 O  OD2   . ASP A 1 231 ? 41.898  37.479  51.540  1.00 77.70  ? 258 ASP A OD2   1 
ATOM   1737 N  N     . TYR A 1 232 ? 43.869  31.993  50.808  1.00 68.04  ? 259 TYR A N     1 
ATOM   1738 C  CA    . TYR A 1 232 ? 44.678  31.108  49.980  1.00 67.12  ? 259 TYR A CA    1 
ATOM   1739 C  C     . TYR A 1 232 ? 43.795  30.084  49.274  1.00 75.03  ? 259 TYR A C     1 
ATOM   1740 O  O     . TYR A 1 232 ? 42.975  29.412  49.908  1.00 69.65  ? 259 TYR A O     1 
ATOM   1741 C  CB    . TYR A 1 232 ? 45.730  30.407  50.840  1.00 55.71  ? 259 TYR A CB    1 
ATOM   1742 C  CG    . TYR A 1 232 ? 46.737  29.590  50.062  1.00 56.50  ? 259 TYR A CG    1 
ATOM   1743 C  CD1   . TYR A 1 232 ? 47.876  30.180  49.531  1.00 60.79  ? 259 TYR A CD1   1 
ATOM   1744 C  CD2   . TYR A 1 232 ? 46.554  28.227  49.871  1.00 51.75  ? 259 TYR A CD2   1 
ATOM   1745 C  CE1   . TYR A 1 232 ? 48.801  29.437  48.823  1.00 65.44  ? 259 TYR A CE1   1 
ATOM   1746 C  CE2   . TYR A 1 232 ? 47.473  27.477  49.165  1.00 53.95  ? 259 TYR A CE2   1 
ATOM   1747 C  CZ    . TYR A 1 232 ? 48.595  28.086  48.645  1.00 63.43  ? 259 TYR A CZ    1 
ATOM   1748 O  OH    . TYR A 1 232 ? 49.513  27.343  47.940  1.00 66.48  ? 259 TYR A OH    1 
ATOM   1749 N  N     . THR A 1 233 ? 43.964  29.966  47.953  1.00 72.67  ? 260 THR A N     1 
ATOM   1750 C  CA    . THR A 1 233 ? 43.170  29.046  47.147  1.00 78.46  ? 260 THR A CA    1 
ATOM   1751 C  C     . THR A 1 233 ? 44.028  28.140  46.270  1.00 79.38  ? 260 THR A C     1 
ATOM   1752 O  O     . THR A 1 233 ? 43.487  27.460  45.390  1.00 83.25  ? 260 THR A O     1 
ATOM   1753 C  CB    . THR A 1 233 ? 42.178  29.815  46.262  1.00 74.71  ? 260 THR A CB    1 
ATOM   1754 O  OG1   . THR A 1 233 ? 42.896  30.693  45.385  1.00 87.95  ? 260 THR A OG1   1 
ATOM   1755 C  CG2   . THR A 1 233 ? 41.218  30.631  47.114  1.00 78.77  ? 260 THR A CG2   1 
ATOM   1756 N  N     . TRP A 1 234 ? 45.339  28.107  46.481  1.00 61.63  ? 261 TRP A N     1 
ATOM   1757 C  CA    . TRP A 1 234 ? 46.237  27.368  45.608  1.00 69.54  ? 261 TRP A CA    1 
ATOM   1758 C  C     . TRP A 1 234 ? 46.493  25.973  46.182  1.00 75.54  ? 261 TRP A C     1 
ATOM   1759 O  O     . TRP A 1 234 ? 45.818  25.526  47.112  1.00 70.03  ? 261 TRP A O     1 
ATOM   1760 C  CB    . TRP A 1 234 ? 47.519  28.168  45.400  1.00 62.40  ? 261 TRP A CB    1 
ATOM   1761 C  CG    . TRP A 1 234 ? 47.287  29.454  44.663  1.00 75.48  ? 261 TRP A CG    1 
ATOM   1762 C  CD1   . TRP A 1 234 ? 46.229  29.753  43.856  1.00 73.50  ? 261 TRP A CD1   1 
ATOM   1763 C  CD2   . TRP A 1 234 ? 48.124  30.618  44.674  1.00 81.25  ? 261 TRP A CD2   1 
ATOM   1764 N  NE1   . TRP A 1 234 ? 46.358  31.027  43.358  1.00 81.41  ? 261 TRP A NE1   1 
ATOM   1765 C  CE2   . TRP A 1 234 ? 47.513  31.579  43.846  1.00 80.70  ? 261 TRP A CE2   1 
ATOM   1766 C  CE3   . TRP A 1 234 ? 49.329  30.940  45.302  1.00 73.98  ? 261 TRP A CE3   1 
ATOM   1767 C  CZ2   . TRP A 1 234 ? 48.068  32.838  43.628  1.00 72.08  ? 261 TRP A CZ2   1 
ATOM   1768 C  CZ3   . TRP A 1 234 ? 49.880  32.188  45.084  1.00 74.88  ? 261 TRP A CZ3   1 
ATOM   1769 C  CH2   . TRP A 1 234 ? 49.248  33.122  44.255  1.00 70.86  ? 261 TRP A CH2   1 
ATOM   1770 N  N     . SER A 1 235 ? 47.470  25.265  45.621  1.00 66.80  ? 262 SER A N     1 
ATOM   1771 C  CA    . SER A 1 235 ? 47.757  23.905  46.058  1.00 58.75  ? 262 SER A CA    1 
ATOM   1772 C  C     . SER A 1 235 ? 48.382  23.903  47.447  1.00 66.54  ? 262 SER A C     1 
ATOM   1773 O  O     . SER A 1 235 ? 49.057  24.852  47.853  1.00 65.49  ? 262 SER A O     1 
ATOM   1774 C  CB    . SER A 1 235 ? 48.693  23.210  45.069  1.00 69.63  ? 262 SER A CB    1 
ATOM   1775 O  OG    . SER A 1 235 ? 48.121  23.166  43.775  1.00 106.40 ? 262 SER A OG    1 
ATOM   1776 N  N     . PHE A 1 236 ? 48.153  22.812  48.177  1.00 60.82  ? 263 PHE A N     1 
ATOM   1777 C  CA    . PHE A 1 236 ? 48.710  22.639  49.513  1.00 57.04  ? 263 PHE A CA    1 
ATOM   1778 C  C     . PHE A 1 236 ? 50.215  22.399  49.431  1.00 63.46  ? 263 PHE A C     1 
ATOM   1779 O  O     . PHE A 1 236 ? 50.698  21.311  49.759  1.00 77.62  ? 263 PHE A O     1 
ATOM   1780 C  CB    . PHE A 1 236 ? 48.004  21.479  50.227  1.00 63.95  ? 263 PHE A CB    1 
ATOM   1781 C  CG    . PHE A 1 236 ? 48.235  21.442  51.713  1.00 65.45  ? 263 PHE A CG    1 
ATOM   1782 C  CD1   . PHE A 1 236 ? 47.702  22.419  52.537  1.00 58.22  ? 263 PHE A CD1   1 
ATOM   1783 C  CD2   . PHE A 1 236 ? 48.963  20.413  52.287  1.00 63.41  ? 263 PHE A CD2   1 
ATOM   1784 C  CE1   . PHE A 1 236 ? 47.905  22.382  53.905  1.00 70.21  ? 263 PHE A CE1   1 
ATOM   1785 C  CE2   . PHE A 1 236 ? 49.171  20.369  53.655  1.00 67.61  ? 263 PHE A CE2   1 
ATOM   1786 C  CZ    . PHE A 1 236 ? 48.640  21.355  54.465  1.00 65.56  ? 263 PHE A CZ    1 
ATOM   1787 N  N     . ASP A 1 237 ? 50.957  23.410  48.984  1.00 71.89  ? 264 ASP A N     1 
ATOM   1788 C  CA    . ASP A 1 237 ? 52.401  23.347  48.803  1.00 72.16  ? 264 ASP A CA    1 
ATOM   1789 C  C     . ASP A 1 237 ? 53.070  24.313  49.772  1.00 64.95  ? 264 ASP A C     1 
ATOM   1790 O  O     . ASP A 1 237 ? 52.573  25.420  49.998  1.00 66.90  ? 264 ASP A O     1 
ATOM   1791 C  CB    . ASP A 1 237 ? 52.775  23.695  47.355  1.00 69.21  ? 264 ASP A CB    1 
ATOM   1792 C  CG    . ASP A 1 237 ? 54.230  23.407  47.032  1.00 78.46  ? 264 ASP A CG    1 
ATOM   1793 O  OD1   . ASP A 1 237 ? 54.998  23.046  47.947  1.00 96.53  ? 264 ASP A OD1   1 
ATOM   1794 O  OD2   . ASP A 1 237 ? 54.604  23.541  45.846  1.00 77.28  ? 264 ASP A OD2   1 
ATOM   1795 N  N     . ASP A 1 238 ? 54.205  23.897  50.339  1.00 57.90  ? 265 ASP A N     1 
ATOM   1796 C  CA    . ASP A 1 238 ? 54.786  24.657  51.443  1.00 50.55  ? 265 ASP A CA    1 
ATOM   1797 C  C     . ASP A 1 238 ? 55.378  25.983  50.973  1.00 59.14  ? 265 ASP A C     1 
ATOM   1798 O  O     . ASP A 1 238 ? 55.233  27.004  51.655  1.00 57.86  ? 265 ASP A O     1 
ATOM   1799 C  CB    . ASP A 1 238 ? 55.839  23.817  52.174  1.00 48.09  ? 265 ASP A CB    1 
ATOM   1800 C  CG    . ASP A 1 238 ? 56.960  23.346  51.265  1.00 63.06  ? 265 ASP A CG    1 
ATOM   1801 O  OD1   . ASP A 1 238 ? 56.817  23.434  50.027  1.00 68.37  ? 265 ASP A OD1   1 
ATOM   1802 O  OD2   . ASP A 1 238 ? 57.992  22.887  51.799  1.00 54.26  ? 265 ASP A OD2   1 
ATOM   1803 N  N     . ILE A 1 239 ? 56.041  25.996  49.815  1.00 59.04  ? 266 ILE A N     1 
ATOM   1804 C  CA    . ILE A 1 239 ? 56.683  27.229  49.365  1.00 53.68  ? 266 ILE A CA    1 
ATOM   1805 C  C     . ILE A 1 239 ? 55.672  28.193  48.756  1.00 51.19  ? 266 ILE A C     1 
ATOM   1806 O  O     . ILE A 1 239 ? 55.873  29.412  48.801  1.00 51.09  ? 266 ILE A O     1 
ATOM   1807 C  CB    . ILE A 1 239 ? 57.825  26.925  48.380  1.00 51.26  ? 266 ILE A CB    1 
ATOM   1808 C  CG1   . ILE A 1 239 ? 57.300  26.184  47.149  1.00 59.32  ? 266 ILE A CG1   1 
ATOM   1809 C  CG2   . ILE A 1 239 ? 58.918  26.128  49.066  1.00 43.72  ? 266 ILE A CG2   1 
ATOM   1810 C  CD1   . ILE A 1 239 ? 58.359  25.927  46.099  1.00 44.05  ? 266 ILE A CD1   1 
ATOM   1811 N  N     . ILE A 1 240 ? 54.580  27.683  48.183  1.00 59.90  ? 267 ILE A N     1 
ATOM   1812 C  CA    . ILE A 1 240 ? 53.566  28.570  47.622  1.00 57.60  ? 267 ILE A CA    1 
ATOM   1813 C  C     . ILE A 1 240 ? 52.784  29.252  48.736  1.00 54.78  ? 267 ILE A C     1 
ATOM   1814 O  O     . ILE A 1 240 ? 52.445  30.438  48.641  1.00 47.00  ? 267 ILE A O     1 
ATOM   1815 C  CB    . ILE A 1 240 ? 52.635  27.795  46.672  1.00 58.36  ? 267 ILE A CB    1 
ATOM   1816 C  CG1   . ILE A 1 240 ? 53.444  26.921  45.714  1.00 71.68  ? 267 ILE A CG1   1 
ATOM   1817 C  CG2   . ILE A 1 240 ? 51.780  28.755  45.882  1.00 66.65  ? 267 ILE A CG2   1 
ATOM   1818 C  CD1   . ILE A 1 240 ? 52.593  26.179  44.700  1.00 75.59  ? 267 ILE A CD1   1 
ATOM   1819 N  N     . VAL A 1 241 ? 52.484  28.514  49.808  1.00 54.38  ? 268 VAL A N     1 
ATOM   1820 C  CA    . VAL A 1 241 ? 51.773  29.091  50.947  1.00 49.78  ? 268 VAL A CA    1 
ATOM   1821 C  C     . VAL A 1 241 ? 52.553  30.268  51.517  1.00 56.91  ? 268 VAL A C     1 
ATOM   1822 O  O     . VAL A 1 241 ? 52.001  31.351  51.745  1.00 56.96  ? 268 VAL A O     1 
ATOM   1823 C  CB    . VAL A 1 241 ? 51.509  28.016  52.017  1.00 47.99  ? 268 VAL A CB    1 
ATOM   1824 C  CG1   . VAL A 1 241 ? 51.167  28.663  53.350  1.00 47.58  ? 268 VAL A CG1   1 
ATOM   1825 C  CG2   . VAL A 1 241 ? 50.380  27.099  51.577  1.00 45.72  ? 268 VAL A CG2   1 
ATOM   1826 N  N     . PHE A 1 242 ? 53.856  30.078  51.743  1.00 46.07  ? 269 PHE A N     1 
ATOM   1827 C  CA    . PHE A 1 242 ? 54.667  31.161  52.289  1.00 51.45  ? 269 PHE A CA    1 
ATOM   1828 C  C     . PHE A 1 242 ? 54.785  32.317  51.304  1.00 50.37  ? 269 PHE A C     1 
ATOM   1829 O  O     . PHE A 1 242 ? 54.761  33.486  51.707  1.00 51.46  ? 269 PHE A O     1 
ATOM   1830 C  CB    . PHE A 1 242 ? 56.050  30.645  52.678  1.00 44.12  ? 269 PHE A CB    1 
ATOM   1831 C  CG    . PHE A 1 242 ? 56.893  31.669  53.376  1.00 46.98  ? 269 PHE A CG    1 
ATOM   1832 C  CD1   . PHE A 1 242 ? 56.511  32.167  54.609  1.00 50.64  ? 269 PHE A CD1   1 
ATOM   1833 C  CD2   . PHE A 1 242 ? 58.058  32.142  52.798  1.00 49.41  ? 269 PHE A CD2   1 
ATOM   1834 C  CE1   . PHE A 1 242 ? 57.279  33.115  55.256  1.00 52.24  ? 269 PHE A CE1   1 
ATOM   1835 C  CE2   . PHE A 1 242 ? 58.831  33.090  53.439  1.00 42.00  ? 269 PHE A CE2   1 
ATOM   1836 C  CZ    . PHE A 1 242 ? 58.441  33.578  54.670  1.00 39.72  ? 269 PHE A CZ    1 
ATOM   1837 N  N     . ALA A 1 243 ? 54.917  32.013  50.011  1.00 47.84  ? 270 ALA A N     1 
ATOM   1838 C  CA    . ALA A 1 243 ? 54.972  33.072  49.009  1.00 44.87  ? 270 ALA A CA    1 
ATOM   1839 C  C     . ALA A 1 243 ? 53.695  33.898  49.012  1.00 47.42  ? 270 ALA A C     1 
ATOM   1840 O  O     . ALA A 1 243 ? 53.742  35.132  48.944  1.00 62.47  ? 270 ALA A O     1 
ATOM   1841 C  CB    . ALA A 1 243 ? 55.217  32.474  47.625  1.00 41.22  ? 270 ALA A CB    1 
ATOM   1842 N  N     . PHE A 1 244 ? 52.541  33.234  49.095  1.00 45.09  ? 271 PHE A N     1 
ATOM   1843 C  CA    . PHE A 1 244 ? 51.279  33.954  49.193  1.00 51.09  ? 271 PHE A CA    1 
ATOM   1844 C  C     . PHE A 1 244 ? 51.194  34.746  50.488  1.00 54.52  ? 271 PHE A C     1 
ATOM   1845 O  O     . PHE A 1 244 ? 50.535  35.790  50.535  1.00 56.14  ? 271 PHE A O     1 
ATOM   1846 C  CB    . PHE A 1 244 ? 50.112  32.971  49.085  1.00 51.42  ? 271 PHE A CB    1 
ATOM   1847 C  CG    . PHE A 1 244 ? 48.764  33.629  49.014  1.00 56.92  ? 271 PHE A CG    1 
ATOM   1848 C  CD1   . PHE A 1 244 ? 48.294  34.143  47.817  1.00 54.75  ? 271 PHE A CD1   1 
ATOM   1849 C  CD2   . PHE A 1 244 ? 47.960  33.721  50.139  1.00 56.16  ? 271 PHE A CD2   1 
ATOM   1850 C  CE1   . PHE A 1 244 ? 47.053  34.746  47.745  1.00 58.18  ? 271 PHE A CE1   1 
ATOM   1851 C  CE2   . PHE A 1 244 ? 46.716  34.322  50.072  1.00 58.91  ? 271 PHE A CE2   1 
ATOM   1852 C  CZ    . PHE A 1 244 ? 46.263  34.835  48.873  1.00 62.68  ? 271 PHE A CZ    1 
ATOM   1853 N  N     . SER A 1 245 ? 51.857  34.271  51.546  1.00 54.21  ? 272 SER A N     1 
ATOM   1854 C  CA    . SER A 1 245 ? 51.848  34.995  52.813  1.00 54.90  ? 272 SER A CA    1 
ATOM   1855 C  C     . SER A 1 245 ? 52.613  36.307  52.705  1.00 54.26  ? 272 SER A C     1 
ATOM   1856 O  O     . SER A 1 245 ? 52.177  37.332  53.244  1.00 56.58  ? 272 SER A O     1 
ATOM   1857 C  CB    . SER A 1 245 ? 52.433  34.122  53.922  1.00 51.17  ? 272 SER A CB    1 
ATOM   1858 O  OG    . SER A 1 245 ? 52.397  34.799  55.164  1.00 41.36  ? 272 SER A OG    1 
ATOM   1859 N  N     . CYS A 1 246 ? 53.759  36.296  52.018  1.00 53.52  ? 273 CYS A N     1 
ATOM   1860 C  CA    . CYS A 1 246 ? 54.483  37.541  51.781  1.00 51.86  ? 273 CYS A CA    1 
ATOM   1861 C  C     . CYS A 1 246 ? 53.676  38.478  50.895  1.00 50.20  ? 273 CYS A C     1 
ATOM   1862 O  O     . CYS A 1 246 ? 53.730  39.702  51.058  1.00 62.28  ? 273 CYS A O     1 
ATOM   1863 C  CB    . CYS A 1 246 ? 55.845  37.250  51.151  1.00 47.78  ? 273 CYS A CB    1 
ATOM   1864 S  SG    . CYS A 1 246 ? 56.926  36.188  52.133  1.00 49.22  ? 273 CYS A SG    1 
ATOM   1865 N  N     . LYS A 1 247 ? 52.917  37.917  49.950  1.00 55.34  ? 274 LYS A N     1 
ATOM   1866 C  CA    . LYS A 1 247 ? 52.074  38.734  49.084  1.00 51.03  ? 274 LYS A CA    1 
ATOM   1867 C  C     . LYS A 1 247 ? 51.028  39.491  49.894  1.00 58.38  ? 274 LYS A C     1 
ATOM   1868 O  O     . LYS A 1 247 ? 50.836  40.698  49.710  1.00 67.45  ? 274 LYS A O     1 
ATOM   1869 C  CB    . LYS A 1 247 ? 51.409  37.852  48.025  1.00 48.70  ? 274 LYS A CB    1 
ATOM   1870 C  CG    . LYS A 1 247 ? 50.570  38.612  47.013  1.00 62.74  ? 274 LYS A CG    1 
ATOM   1871 C  CD    . LYS A 1 247 ? 51.410  39.619  46.247  1.00 82.44  ? 274 LYS A CD    1 
ATOM   1872 C  CE    . LYS A 1 247 ? 50.543  40.500  45.360  1.00 90.00  ? 274 LYS A CE    1 
ATOM   1873 N  NZ    . LYS A 1 247 ? 51.331  41.591  44.722  1.00 94.75  ? 274 LYS A NZ    1 
ATOM   1874 N  N     . GLN A 1 248 ? 50.344  38.794  50.806  1.00 51.67  ? 275 GLN A N     1 
ATOM   1875 C  CA    . GLN A 1 248 ? 49.330  39.447  51.627  1.00 45.33  ? 275 GLN A CA    1 
ATOM   1876 C  C     . GLN A 1 248 ? 49.951  40.420  52.619  1.00 53.52  ? 275 GLN A C     1 
ATOM   1877 O  O     . GLN A 1 248 ? 49.321  41.420  52.980  1.00 60.29  ? 275 GLN A O     1 
ATOM   1878 C  CB    . GLN A 1 248 ? 48.493  38.404  52.367  1.00 57.30  ? 275 GLN A CB    1 
ATOM   1879 C  CG    . GLN A 1 248 ? 47.846  37.378  51.457  1.00 60.69  ? 275 GLN A CG    1 
ATOM   1880 C  CD    . GLN A 1 248 ? 47.133  38.013  50.283  1.00 59.20  ? 275 GLN A CD    1 
ATOM   1881 O  OE1   . GLN A 1 248 ? 46.152  38.736  50.454  1.00 53.27  ? 275 GLN A OE1   1 
ATOM   1882 N  NE2   . GLN A 1 248 ? 47.628  37.749  49.078  1.00 70.05  ? 275 GLN A NE2   1 
ATOM   1883 N  N     . ALA A 1 249 ? 51.173  40.148  53.070  1.00 59.26  ? 276 ALA A N     1 
ATOM   1884 C  CA    . ALA A 1 249 ? 51.875  41.059  53.965  1.00 51.22  ? 276 ALA A CA    1 
ATOM   1885 C  C     . ALA A 1 249 ? 52.504  42.233  53.231  1.00 53.60  ? 276 ALA A C     1 
ATOM   1886 O  O     . ALA A 1 249 ? 53.077  43.113  53.884  1.00 64.22  ? 276 ALA A O     1 
ATOM   1887 C  CB    . ALA A 1 249 ? 52.954  40.303  54.744  1.00 46.40  ? 276 ALA A CB    1 
ATOM   1888 N  N     . GLU A 1 250 ? 52.397  42.271  51.900  1.00 60.06  ? 277 GLU A N     1 
ATOM   1889 C  CA    . GLU A 1 250 ? 53.065  43.276  51.072  1.00 57.86  ? 277 GLU A CA    1 
ATOM   1890 C  C     . GLU A 1 250 ? 54.572  43.259  51.309  1.00 50.22  ? 277 GLU A C     1 
ATOM   1891 O  O     . GLU A 1 250 ? 55.232  44.299  51.333  1.00 55.82  ? 277 GLU A O     1 
ATOM   1892 C  CB    . GLU A 1 250 ? 52.481  44.671  51.305  1.00 57.51  ? 277 GLU A CB    1 
ATOM   1893 C  CG    . GLU A 1 250 ? 51.011  44.789  50.926  1.00 78.02  ? 277 GLU A CG    1 
ATOM   1894 C  CD    . GLU A 1 250 ? 50.461  46.187  51.135  1.00 90.51  ? 277 GLU A CD    1 
ATOM   1895 O  OE1   . GLU A 1 250 ? 51.252  47.096  51.464  1.00 95.69  ? 277 GLU A OE1   1 
ATOM   1896 O  OE2   . GLU A 1 250 ? 49.237  46.377  50.971  1.00 95.81  ? 277 GLU A OE2   1 
ATOM   1897 N  N     . VAL A 1 251 ? 55.118  42.060  51.489  1.00 46.86  ? 278 VAL A N     1 
ATOM   1898 C  CA    . VAL A 1 251 ? 56.547  41.846  51.674  1.00 48.17  ? 278 VAL A CA    1 
ATOM   1899 C  C     . VAL A 1 251 ? 57.105  41.285  50.375  1.00 57.49  ? 278 VAL A C     1 
ATOM   1900 O  O     . VAL A 1 251 ? 56.642  40.246  49.887  1.00 60.22  ? 278 VAL A O     1 
ATOM   1901 C  CB    . VAL A 1 251 ? 56.835  40.902  52.850  1.00 47.87  ? 278 VAL A CB    1 
ATOM   1902 C  CG1   . VAL A 1 251 ? 58.297  40.492  52.849  1.00 42.99  ? 278 VAL A CG1   1 
ATOM   1903 C  CG2   . VAL A 1 251 ? 56.470  41.571  54.163  1.00 45.33  ? 278 VAL A CG2   1 
ATOM   1904 N  N     . GLN A 1 252 ? 58.101  41.966  49.820  1.00 55.57  ? 279 GLN A N     1 
ATOM   1905 C  CA    . GLN A 1 252 ? 58.684  41.584  48.542  1.00 45.72  ? 279 GLN A CA    1 
ATOM   1906 C  C     . GLN A 1 252 ? 59.817  40.591  48.771  1.00 47.56  ? 279 GLN A C     1 
ATOM   1907 O  O     . GLN A 1 252 ? 60.783  40.895  49.479  1.00 57.17  ? 279 GLN A O     1 
ATOM   1908 C  CB    . GLN A 1 252 ? 59.192  42.815  47.794  1.00 46.17  ? 279 GLN A CB    1 
ATOM   1909 C  CG    . GLN A 1 252 ? 59.849  42.491  46.467  1.00 53.69  ? 279 GLN A CG    1 
ATOM   1910 C  CD    . GLN A 1 252 ? 58.921  41.745  45.531  1.00 54.37  ? 279 GLN A CD    1 
ATOM   1911 O  OE1   . GLN A 1 252 ? 57.820  42.207  45.234  1.00 59.19  ? 279 GLN A OE1   1 
ATOM   1912 N  NE2   . GLN A 1 252 ? 59.361  40.582  45.063  1.00 62.26  ? 279 GLN A NE2   1 
ATOM   1913 N  N     . MET A 1 253 ? 59.694  39.409  48.173  1.00 51.56  ? 280 MET A N     1 
ATOM   1914 C  CA    . MET A 1 253 ? 60.782  38.445  48.203  1.00 59.51  ? 280 MET A CA    1 
ATOM   1915 C  C     . MET A 1 253 ? 61.882  38.863  47.235  1.00 51.83  ? 280 MET A C     1 
ATOM   1916 O  O     . MET A 1 253 ? 61.613  39.297  46.112  1.00 46.70  ? 280 MET A O     1 
ATOM   1917 C  CB    . MET A 1 253 ? 60.266  37.051  47.851  1.00 41.35  ? 280 MET A CB    1 
ATOM   1918 C  CG    . MET A 1 253 ? 59.675  36.294  49.033  1.00 65.63  ? 280 MET A CG    1 
ATOM   1919 S  SD    . MET A 1 253 ? 58.787  34.802  48.555  1.00 58.51  ? 280 MET A SD    1 
ATOM   1920 C  CE    . MET A 1 253 ? 57.332  35.533  47.814  1.00 76.72  ? 280 MET A CE    1 
ATOM   1921 N  N     . TYR A 1 254 ? 63.128  38.742  47.681  1.00 46.27  ? 281 TYR A N     1 
ATOM   1922 C  CA    . TYR A 1 254 ? 64.282  39.094  46.869  1.00 46.53  ? 281 TYR A CA    1 
ATOM   1923 C  C     . TYR A 1 254 ? 65.236  37.915  46.764  1.00 49.59  ? 281 TYR A C     1 
ATOM   1924 O  O     . TYR A 1 254 ? 65.341  37.090  47.677  1.00 41.32  ? 281 TYR A O     1 
ATOM   1925 C  CB    . TYR A 1 254 ? 65.045  40.293  47.449  1.00 45.38  ? 281 TYR A CB    1 
ATOM   1926 C  CG    . TYR A 1 254 ? 64.313  41.607  47.359  1.00 52.95  ? 281 TYR A CG    1 
ATOM   1927 C  CD1   . TYR A 1 254 ? 64.441  42.419  46.244  1.00 54.32  ? 281 TYR A CD1   1 
ATOM   1928 C  CD2   . TYR A 1 254 ? 63.500  42.039  48.397  1.00 60.63  ? 281 TYR A CD2   1 
ATOM   1929 C  CE1   . TYR A 1 254 ? 63.775  43.622  46.161  1.00 48.25  ? 281 TYR A CE1   1 
ATOM   1930 C  CE2   . TYR A 1 254 ? 62.829  43.240  48.322  1.00 55.97  ? 281 TYR A CE2   1 
ATOM   1931 C  CZ    . TYR A 1 254 ? 62.971  44.027  47.203  1.00 57.05  ? 281 TYR A CZ    1 
ATOM   1932 O  OH    . TYR A 1 254 ? 62.306  45.226  47.128  1.00 73.79  ? 281 TYR A OH    1 
ATOM   1933 N  N     . VAL A 1 255 ? 65.935  37.847  45.637  1.00 52.41  ? 282 VAL A N     1 
ATOM   1934 C  CA    . VAL A 1 255 ? 67.077  36.961  45.466  1.00 46.84  ? 282 VAL A CA    1 
ATOM   1935 C  C     . VAL A 1 255 ? 68.271  37.817  45.070  1.00 56.99  ? 282 VAL A C     1 
ATOM   1936 O  O     . VAL A 1 255 ? 68.146  38.730  44.246  1.00 54.88  ? 282 VAL A O     1 
ATOM   1937 C  CB    . VAL A 1 255 ? 66.806  35.854  44.422  1.00 54.65  ? 282 VAL A CB    1 
ATOM   1938 C  CG1   . VAL A 1 255 ? 66.493  36.448  43.053  1.00 43.24  ? 282 VAL A CG1   1 
ATOM   1939 C  CG2   . VAL A 1 255 ? 67.987  34.897  44.341  1.00 51.39  ? 282 VAL A CG2   1 
ATOM   1940 N  N     . CYS A 1 256 ? 69.417  37.553  45.690  1.00 50.78  ? 283 CYS A N     1 
ATOM   1941 C  CA    . CYS A 1 256 ? 70.652  38.258  45.380  1.00 58.01  ? 283 CYS A CA    1 
ATOM   1942 C  C     . CYS A 1 256 ? 71.639  37.279  44.764  1.00 60.77  ? 283 CYS A C     1 
ATOM   1943 O  O     . CYS A 1 256 ? 71.803  36.160  45.263  1.00 63.52  ? 283 CYS A O     1 
ATOM   1944 C  CB    . CYS A 1 256 ? 71.256  38.907  46.628  1.00 46.38  ? 283 CYS A CB    1 
ATOM   1945 S  SG    . CYS A 1 256 ? 70.168  40.069  47.502  1.00 112.11 ? 283 CYS A SG    1 
ATOM   1946 N  N     . ASN A 1 257 ? 72.282  37.698  43.674  1.00 63.56  ? 284 ASN A N     1 
ATOM   1947 C  CA    . ASN A 1 257 ? 73.264  36.878  42.975  1.00 55.86  ? 284 ASN A CA    1 
ATOM   1948 C  C     . ASN A 1 257 ? 74.568  37.641  42.774  1.00 62.03  ? 284 ASN A C     1 
ATOM   1949 O  O     . ASN A 1 257 ? 75.279  37.419  41.789  1.00 61.64  ? 284 ASN A O     1 
ATOM   1950 C  CB    . ASN A 1 257 ? 72.711  36.392  41.633  1.00 51.16  ? 284 ASN A CB    1 
ATOM   1951 C  CG    . ASN A 1 257 ? 72.474  37.525  40.650  1.00 66.72  ? 284 ASN A CG    1 
ATOM   1952 O  OD1   . ASN A 1 257 ? 72.471  38.698  41.024  1.00 69.11  ? 284 ASN A OD1   1 
ATOM   1953 N  ND2   . ASN A 1 257 ? 72.268  37.177  39.385  1.00 63.08  ? 284 ASN A ND2   1 
ATOM   1954 N  N     . LYS A 1 258 ? 74.896  38.541  43.703  1.00 50.14  ? 285 LYS A N     1 
ATOM   1955 C  CA    . LYS A 1 258 ? 76.057  39.406  43.533  1.00 62.08  ? 285 LYS A CA    1 
ATOM   1956 C  C     . LYS A 1 258 ? 77.374  38.640  43.555  1.00 71.75  ? 285 LYS A C     1 
ATOM   1957 O  O     . LYS A 1 258 ? 78.365  39.124  43.000  1.00 76.43  ? 285 LYS A O     1 
ATOM   1958 C  CB    . LYS A 1 258 ? 76.049  40.490  44.611  1.00 54.90  ? 285 LYS A CB    1 
ATOM   1959 C  CG    . LYS A 1 258 ? 74.893  41.467  44.449  1.00 52.79  ? 285 LYS A CG    1 
ATOM   1960 C  CD    . LYS A 1 258 ? 74.843  42.501  45.554  1.00 53.48  ? 285 LYS A CD    1 
ATOM   1961 C  CE    . LYS A 1 258 ? 73.628  43.402  45.381  1.00 59.58  ? 285 LYS A CE    1 
ATOM   1962 N  NZ    . LYS A 1 258 ? 73.525  44.437  46.449  1.00 75.49  ? 285 LYS A NZ    1 
ATOM   1963 N  N     . GLU A 1 259 ? 77.407  37.458  44.166  1.00 74.42  ? 286 GLU A N     1 
ATOM   1964 C  CA    . GLU A 1 259 ? 78.584  36.602  44.128  1.00 72.23  ? 286 GLU A CA    1 
ATOM   1965 C  C     . GLU A 1 259 ? 78.144  35.167  44.375  1.00 65.25  ? 286 GLU A C     1 
ATOM   1966 O  O     . GLU A 1 259 ? 76.955  34.882  44.549  1.00 54.00  ? 286 GLU A O     1 
ATOM   1967 C  CB    . GLU A 1 259 ? 79.635  37.054  45.145  1.00 59.40  ? 286 GLU A CB    1 
ATOM   1968 C  CG    . GLU A 1 259 ? 79.071  37.476  46.485  1.00 62.33  ? 286 GLU A CG    1 
ATOM   1969 C  CD    . GLU A 1 259 ? 80.125  38.089  47.385  1.00 83.78  ? 286 GLU A CD    1 
ATOM   1970 O  OE1   . GLU A 1 259 ? 81.167  37.437  47.607  1.00 71.71  ? 286 GLU A OE1   1 
ATOM   1971 O  OE2   . GLU A 1 259 ? 79.914  39.224  47.864  1.00 85.54  ? 286 GLU A OE2   1 
ATOM   1972 N  N     . GLU A 1 260 ? 79.111  34.255  44.373  1.00 63.63  ? 287 GLU A N     1 
ATOM   1973 C  CA    . GLU A 1 260 ? 78.809  32.871  44.705  1.00 48.82  ? 287 GLU A CA    1 
ATOM   1974 C  C     . GLU A 1 260 ? 78.545  32.747  46.199  1.00 69.49  ? 287 GLU A C     1 
ATOM   1975 O  O     . GLU A 1 260 ? 79.336  33.221  47.021  1.00 58.24  ? 287 GLU A O     1 
ATOM   1976 C  CB    . GLU A 1 260 ? 79.952  31.946  44.293  1.00 50.76  ? 287 GLU A CB    1 
ATOM   1977 C  CG    . GLU A 1 260 ? 79.613  31.034  43.123  1.00 95.33  ? 287 GLU A CG    1 
ATOM   1978 C  CD    . GLU A 1 260 ? 80.582  29.878  42.980  1.00 94.16  ? 287 GLU A CD    1 
ATOM   1979 O  OE1   . GLU A 1 260 ? 81.506  29.771  43.815  1.00 85.55  ? 287 GLU A OE1   1 
ATOM   1980 O  OE2   . GLU A 1 260 ? 80.417  29.076  42.036  1.00 91.09  ? 287 GLU A OE2   1 
ATOM   1981 N  N     . TYR A 1 261 ? 77.425  32.122  46.549  1.00 57.01  ? 288 TYR A N     1 
ATOM   1982 C  CA    . TYR A 1 261 ? 77.080  31.863  47.941  1.00 50.84  ? 288 TYR A CA    1 
ATOM   1983 C  C     . TYR A 1 261 ? 77.155  30.392  48.304  1.00 54.85  ? 288 TYR A C     1 
ATOM   1984 O  O     . TYR A 1 261 ? 77.698  30.047  49.355  1.00 68.62  ? 288 TYR A O     1 
ATOM   1985 C  CB    . TYR A 1 261 ? 75.673  32.390  48.248  1.00 51.84  ? 288 TYR A CB    1 
ATOM   1986 C  CG    . TYR A 1 261 ? 75.491  33.856  47.929  1.00 52.25  ? 288 TYR A CG    1 
ATOM   1987 C  CD1   . TYR A 1 261 ? 76.143  34.834  48.669  1.00 54.80  ? 288 TYR A CD1   1 
ATOM   1988 C  CD2   . TYR A 1 261 ? 74.667  34.262  46.888  1.00 48.02  ? 288 TYR A CD2   1 
ATOM   1989 C  CE1   . TYR A 1 261 ? 75.980  36.177  48.378  1.00 57.55  ? 288 TYR A CE1   1 
ATOM   1990 C  CE2   . TYR A 1 261 ? 74.497  35.600  46.592  1.00 56.83  ? 288 TYR A CE2   1 
ATOM   1991 C  CZ    . TYR A 1 261 ? 75.155  36.554  47.339  1.00 63.60  ? 288 TYR A CZ    1 
ATOM   1992 O  OH    . TYR A 1 261 ? 74.986  37.889  47.043  1.00 66.86  ? 288 TYR A OH    1 
ATOM   1993 N  N     . GLY A 1 262 ? 76.640  29.514  47.453  1.00 42.96  ? 289 GLY A N     1 
ATOM   1994 C  CA    . GLY A 1 262 ? 76.685  28.100  47.757  1.00 51.15  ? 289 GLY A CA    1 
ATOM   1995 C  C     . GLY A 1 262 ? 76.059  27.278  46.654  1.00 50.73  ? 289 GLY A C     1 
ATOM   1996 O  O     . GLY A 1 262 ? 75.733  27.785  45.579  1.00 47.46  ? 289 GLY A O     1 
ATOM   1997 N  N     . PHE A 1 263 ? 75.897  25.987  46.946  1.00 49.08  ? 290 PHE A N     1 
ATOM   1998 C  CA    . PHE A 1 263 ? 75.428  25.004  45.983  1.00 56.86  ? 290 PHE A CA    1 
ATOM   1999 C  C     . PHE A 1 263 ? 74.306  24.183  46.599  1.00 46.86  ? 290 PHE A C     1 
ATOM   2000 O  O     . PHE A 1 263 ? 74.242  24.008  47.818  1.00 43.36  ? 290 PHE A O     1 
ATOM   2001 C  CB    . PHE A 1 263 ? 76.562  24.072  45.533  1.00 42.77  ? 290 PHE A CB    1 
ATOM   2002 C  CG    . PHE A 1 263 ? 77.714  24.782  44.884  1.00 46.28  ? 290 PHE A CG    1 
ATOM   2003 C  CD1   . PHE A 1 263 ? 78.640  25.477  45.647  1.00 55.24  ? 290 PHE A CD1   1 
ATOM   2004 C  CD2   . PHE A 1 263 ? 77.879  24.741  43.512  1.00 56.79  ? 290 PHE A CD2   1 
ATOM   2005 C  CE1   . PHE A 1 263 ? 79.703  26.129  45.051  1.00 59.48  ? 290 PHE A CE1   1 
ATOM   2006 C  CE2   . PHE A 1 263 ? 78.938  25.385  42.909  1.00 65.34  ? 290 PHE A CE2   1 
ATOM   2007 C  CZ    . PHE A 1 263 ? 79.853  26.082  43.678  1.00 77.78  ? 290 PHE A CZ    1 
ATOM   2008 N  N     . LEU A 1 264 ? 73.415  23.684  45.746  1.00 47.47  ? 291 LEU A N     1 
ATOM   2009 C  CA    . LEU A 1 264 ? 72.306  22.855  46.196  1.00 55.94  ? 291 LEU A CA    1 
ATOM   2010 C  C     . LEU A 1 264 ? 72.008  21.808  45.134  1.00 48.48  ? 291 LEU A C     1 
ATOM   2011 O  O     . LEU A 1 264 ? 72.202  22.066  43.940  1.00 63.87  ? 291 LEU A O     1 
ATOM   2012 C  CB    . LEU A 1 264 ? 71.047  23.690  46.487  1.00 45.73  ? 291 LEU A CB    1 
ATOM   2013 C  CG    . LEU A 1 264 ? 70.080  24.049  45.353  1.00 48.64  ? 291 LEU A CG    1 
ATOM   2014 C  CD1   . LEU A 1 264 ? 68.834  24.711  45.920  1.00 52.03  ? 291 LEU A CD1   1 
ATOM   2015 C  CD2   . LEU A 1 264 ? 70.730  24.943  44.305  1.00 58.29  ? 291 LEU A CD2   1 
ATOM   2016 N  N     . PRO A 1 265 ? 71.552  20.621  45.530  1.00 52.65  ? 292 PRO A N     1 
ATOM   2017 C  CA    . PRO A 1 265 ? 71.224  19.589  44.544  1.00 46.75  ? 292 PRO A CA    1 
ATOM   2018 C  C     . PRO A 1 265 ? 69.852  19.808  43.928  1.00 53.82  ? 292 PRO A C     1 
ATOM   2019 O  O     . PRO A 1 265 ? 68.943  20.371  44.542  1.00 52.45  ? 292 PRO A O     1 
ATOM   2020 C  CB    . PRO A 1 265 ? 71.256  18.298  45.369  1.00 44.34  ? 292 PRO A CB    1 
ATOM   2021 C  CG    . PRO A 1 265 ? 70.833  18.736  46.728  1.00 44.59  ? 292 PRO A CG    1 
ATOM   2022 C  CD    . PRO A 1 265 ? 71.380  20.136  46.912  1.00 54.93  ? 292 PRO A CD    1 
ATOM   2023 N  N     . VAL A 1 266 ? 69.715  19.355  42.690  1.00 52.92  ? 293 VAL A N     1 
ATOM   2024 C  CA    . VAL A 1 266 ? 68.421  19.455  42.007  1.00 48.23  ? 293 VAL A CA    1 
ATOM   2025 C  C     . VAL A 1 266 ? 67.449  18.461  42.636  1.00 48.63  ? 293 VAL A C     1 
ATOM   2026 O  O     . VAL A 1 266 ? 67.786  17.271  42.769  1.00 61.52  ? 293 VAL A O     1 
ATOM   2027 C  CB    . VAL A 1 266 ? 68.589  19.193  40.511  1.00 43.18  ? 293 VAL A CB    1 
ATOM   2028 C  CG1   . VAL A 1 266 ? 67.238  19.203  39.819  1.00 43.92  ? 293 VAL A CG1   1 
ATOM   2029 C  CG2   . VAL A 1 266 ? 69.517  20.233  39.895  1.00 58.10  ? 293 VAL A CG2   1 
ATOM   2030 N  N     . PRO A 1 267 ? 66.255  18.892  43.045  1.00 63.88  ? 294 PRO A N     1 
ATOM   2031 C  CA    . PRO A 1 267 ? 65.315  17.966  43.689  1.00 60.59  ? 294 PRO A CA    1 
ATOM   2032 C  C     . PRO A 1 267 ? 64.922  16.824  42.763  1.00 53.49  ? 294 PRO A C     1 
ATOM   2033 O  O     . PRO A 1 267 ? 64.887  16.965  41.540  1.00 54.39  ? 294 PRO A O     1 
ATOM   2034 C  CB    . PRO A 1 267 ? 64.110  18.857  44.019  1.00 43.37  ? 294 PRO A CB    1 
ATOM   2035 C  CG    . PRO A 1 267 ? 64.667  20.244  44.064  1.00 51.73  ? 294 PRO A CG    1 
ATOM   2036 C  CD    . PRO A 1 267 ? 65.746  20.272  43.025  1.00 49.64  ? 294 PRO A CD    1 
ATOM   2037 N  N     . LEU A 1 268 ? 64.621  15.681  43.368  1.00 59.92  ? 295 LEU A N     1 
ATOM   2038 C  CA    . LEU A 1 268 ? 64.316  14.463  42.635  1.00 46.70  ? 295 LEU A CA    1 
ATOM   2039 C  C     . LEU A 1 268 ? 62.809  14.236  42.551  1.00 59.78  ? 295 LEU A C     1 
ATOM   2040 O  O     . LEU A 1 268 ? 62.009  14.935  43.178  1.00 60.60  ? 295 LEU A O     1 
ATOM   2041 C  CB    . LEU A 1 268 ? 65.001  13.265  43.295  1.00 54.74  ? 295 LEU A CB    1 
ATOM   2042 C  CG    . LEU A 1 268 ? 66.527  13.319  43.310  1.00 53.07  ? 295 LEU A CG    1 
ATOM   2043 C  CD1   . LEU A 1 268 ? 67.082  12.200  44.167  1.00 54.68  ? 295 LEU A CD1   1 
ATOM   2044 C  CD2   . LEU A 1 268 ? 67.079  13.240  41.895  1.00 53.93  ? 295 LEU A CD2   1 
ATOM   2045 N  N     . ARG A 1 269 ? 62.428  13.235  41.761  1.00 65.65  ? 296 ARG A N     1 
ATOM   2046 C  CA    . ARG A 1 269 ? 61.024  12.927  41.545  1.00 52.32  ? 296 ARG A CA    1 
ATOM   2047 C  C     . ARG A 1 269 ? 60.423  12.242  42.769  1.00 60.37  ? 296 ARG A C     1 
ATOM   2048 O  O     . ARG A 1 269 ? 61.125  11.817  43.691  1.00 62.55  ? 296 ARG A O     1 
ATOM   2049 C  CB    . ARG A 1 269 ? 60.847  12.038  40.316  1.00 70.04  ? 296 ARG A CB    1 
ATOM   2050 C  CG    . ARG A 1 269 ? 61.168  12.706  38.995  1.00 73.90  ? 296 ARG A CG    1 
ATOM   2051 C  CD    . ARG A 1 269 ? 60.896  11.747  37.852  1.00 99.43  ? 296 ARG A CD    1 
ATOM   2052 N  NE    . ARG A 1 269 ? 61.286  12.289  36.558  1.00 126.39 ? 296 ARG A NE    1 
ATOM   2053 C  CZ    . ARG A 1 269 ? 61.276  11.597  35.427  1.00 128.63 ? 296 ARG A CZ    1 
ATOM   2054 N  NH1   . ARG A 1 269 ? 60.898  10.329  35.397  1.00 113.09 ? 296 ARG A NH1   1 
ATOM   2055 N  NH2   . ARG A 1 269 ? 61.659  12.189  34.300  1.00 130.14 ? 296 ARG A NH2   1 
ATOM   2056 N  N     . ALA A 1 270 ? 59.091  12.132  42.757  1.00 56.82  ? 297 ALA A N     1 
ATOM   2057 C  CA    . ALA A 1 270 ? 58.382  11.511  43.871  1.00 56.53  ? 297 ALA A CA    1 
ATOM   2058 C  C     . ALA A 1 270 ? 58.812  10.062  44.066  1.00 66.44  ? 297 ALA A C     1 
ATOM   2059 O  O     . ALA A 1 270 ? 58.945  9.593   45.202  1.00 66.27  ? 297 ALA A O     1 
ATOM   2060 C  CB    . ALA A 1 270 ? 56.874  11.597  43.641  1.00 57.18  ? 297 ALA A CB    1 
ATOM   2061 N  N     . HIS A 1 271 ? 59.039  9.339   42.969  1.00 58.54  ? 298 HIS A N     1 
ATOM   2062 C  CA    . HIS A 1 271 ? 59.410  7.933   43.025  1.00 60.60  ? 298 HIS A CA    1 
ATOM   2063 C  C     . HIS A 1 271 ? 60.917  7.722   42.954  1.00 63.55  ? 298 HIS A C     1 
ATOM   2064 O  O     . HIS A 1 271 ? 61.369  6.641   42.562  1.00 65.52  ? 298 HIS A O     1 
ATOM   2065 C  CB    . HIS A 1 271 ? 58.710  7.160   41.909  1.00 82.37  ? 298 HIS A CB    1 
ATOM   2066 C  CG    . HIS A 1 271 ? 57.229  7.065   42.091  1.00 75.70  ? 298 HIS A CG    1 
ATOM   2067 N  ND1   . HIS A 1 271 ? 56.374  6.715   41.070  1.00 68.64  ? 298 HIS A ND1   1 
ATOM   2068 C  CD2   . HIS A 1 271 ? 56.451  7.274   43.179  1.00 68.13  ? 298 HIS A CD2   1 
ATOM   2069 C  CE1   . HIS A 1 271 ? 55.132  6.713   41.518  1.00 87.74  ? 298 HIS A CE1   1 
ATOM   2070 N  NE2   . HIS A 1 271 ? 55.151  7.049   42.796  1.00 78.13  ? 298 HIS A NE2   1 
ATOM   2071 N  N     . SER A 1 272 ? 61.705  8.725   43.330  1.00 58.61  ? 299 SER A N     1 
ATOM   2072 C  CA    . SER A 1 272 ? 63.148  8.562   43.388  1.00 55.61  ? 299 SER A CA    1 
ATOM   2073 C  C     . SER A 1 272 ? 63.533  7.817   44.664  1.00 56.41  ? 299 SER A C     1 
ATOM   2074 O  O     . SER A 1 272 ? 62.684  7.438   45.475  1.00 63.60  ? 299 SER A O     1 
ATOM   2075 C  CB    . SER A 1 272 ? 63.840  9.919   43.306  1.00 65.34  ? 299 SER A CB    1 
ATOM   2076 O  OG    . SER A 1 272 ? 63.473  10.599  42.120  1.00 78.10  ? 299 SER A OG    1 
ATOM   2077 N  N     . THR A 1 273 ? 64.832  7.605   44.849  1.00 55.61  ? 300 THR A N     1 
ATOM   2078 C  CA    . THR A 1 273 ? 65.337  6.788   45.942  1.00 63.02  ? 300 THR A CA    1 
ATOM   2079 C  C     . THR A 1 273 ? 66.294  7.584   46.818  1.00 59.05  ? 300 THR A C     1 
ATOM   2080 O  O     . THR A 1 273 ? 66.798  8.642   46.432  1.00 60.92  ? 300 THR A O     1 
ATOM   2081 C  CB    . THR A 1 273 ? 66.052  5.529   45.422  1.00 58.81  ? 300 THR A CB    1 
ATOM   2082 O  OG1   . THR A 1 273 ? 67.341  5.884   44.906  1.00 66.42  ? 300 THR A OG1   1 
ATOM   2083 C  CG2   . THR A 1 273 ? 65.242  4.869   44.321  1.00 60.85  ? 300 THR A CG2   1 
ATOM   2084 N  N     . LEU A 1 274 ? 66.533  7.051   48.019  1.00 50.95  ? 301 LEU A N     1 
ATOM   2085 C  CA    . LEU A 1 274 ? 67.497  7.656   48.931  1.00 51.20  ? 301 LEU A CA    1 
ATOM   2086 C  C     . LEU A 1 274 ? 68.914  7.574   48.382  1.00 48.38  ? 301 LEU A C     1 
ATOM   2087 O  O     . LEU A 1 274 ? 69.731  8.462   48.648  1.00 59.75  ? 301 LEU A O     1 
ATOM   2088 C  CB    . LEU A 1 274 ? 67.411  6.983   50.301  1.00 50.64  ? 301 LEU A CB    1 
ATOM   2089 C  CG    . LEU A 1 274 ? 66.075  7.156   51.028  1.00 70.87  ? 301 LEU A CG    1 
ATOM   2090 C  CD1   . LEU A 1 274 ? 66.004  6.251   52.245  1.00 53.58  ? 301 LEU A CD1   1 
ATOM   2091 C  CD2   . LEU A 1 274 ? 65.871  8.613   51.423  1.00 59.75  ? 301 LEU A CD2   1 
ATOM   2092 N  N     . GLN A 1 275 ? 69.224  6.522   47.620  1.00 49.71  ? 302 GLN A N     1 
ATOM   2093 C  CA    . GLN A 1 275 ? 70.537  6.438   46.989  1.00 51.45  ? 302 GLN A CA    1 
ATOM   2094 C  C     . GLN A 1 275 ? 70.682  7.485   45.893  1.00 60.03  ? 302 GLN A C     1 
ATOM   2095 O  O     . GLN A 1 275 ? 71.762  8.060   45.717  1.00 67.90  ? 302 GLN A O     1 
ATOM   2096 C  CB    . GLN A 1 275 ? 70.768  5.036   46.428  1.00 53.22  ? 302 GLN A CB    1 
ATOM   2097 C  CG    . GLN A 1 275 ? 72.146  4.833   45.827  1.00 68.73  ? 302 GLN A CG    1 
ATOM   2098 C  CD    . GLN A 1 275 ? 72.272  3.515   45.094  1.00 78.93  ? 302 GLN A CD    1 
ATOM   2099 O  OE1   . GLN A 1 275 ? 71.322  2.733   45.022  1.00 77.81  ? 302 GLN A OE1   1 
ATOM   2100 N  NE2   . GLN A 1 275 ? 73.450  3.262   44.540  1.00 76.23  ? 302 GLN A NE2   1 
ATOM   2101 N  N     . ASP A 1 276 ? 69.602  7.744   45.148  1.00 59.66  ? 303 ASP A N     1 
ATOM   2102 C  CA    . ASP A 1 276 ? 69.619  8.825   44.167  1.00 53.28  ? 303 ASP A CA    1 
ATOM   2103 C  C     . ASP A 1 276 ? 69.933  10.159  44.832  1.00 62.06  ? 303 ASP A C     1 
ATOM   2104 O  O     . ASP A 1 276 ? 70.730  10.948  44.312  1.00 59.29  ? 303 ASP A O     1 
ATOM   2105 C  CB    . ASP A 1 276 ? 68.278  8.902   43.437  1.00 57.60  ? 303 ASP A CB    1 
ATOM   2106 C  CG    . ASP A 1 276 ? 68.082  7.767   42.457  1.00 74.62  ? 303 ASP A CG    1 
ATOM   2107 O  OD1   . ASP A 1 276 ? 69.011  7.503   41.664  1.00 82.98  ? 303 ASP A OD1   1 
ATOM   2108 O  OD2   . ASP A 1 276 ? 66.998  7.141   42.481  1.00 69.65  ? 303 ASP A OD2   1 
ATOM   2109 N  N     . GLU A 1 277 ? 69.324  10.420  45.991  1.00 57.08  ? 304 GLU A N     1 
ATOM   2110 C  CA    . GLU A 1 277 ? 69.594  11.659  46.714  1.00 50.76  ? 304 GLU A CA    1 
ATOM   2111 C  C     . GLU A 1 277 ? 71.043  11.717  47.180  1.00 50.79  ? 304 GLU A C     1 
ATOM   2112 O  O     . GLU A 1 277 ? 71.723  12.736  47.008  1.00 54.65  ? 304 GLU A O     1 
ATOM   2113 C  CB    . GLU A 1 277 ? 68.641  11.785  47.902  1.00 51.37  ? 304 GLU A CB    1 
ATOM   2114 C  CG    . GLU A 1 277 ? 68.692  13.134  48.594  1.00 55.92  ? 304 GLU A CG    1 
ATOM   2115 C  CD    . GLU A 1 277 ? 68.004  14.222  47.792  1.00 72.31  ? 304 GLU A CD    1 
ATOM   2116 O  OE1   . GLU A 1 277 ? 66.964  13.931  47.165  1.00 69.94  ? 304 GLU A OE1   1 
ATOM   2117 O  OE2   . GLU A 1 277 ? 68.501  15.368  47.787  1.00 79.21  ? 304 GLU A OE2   1 
ATOM   2118 N  N     . ALA A 1 278 ? 71.535  10.623  47.766  1.00 51.00  ? 305 ALA A N     1 
ATOM   2119 C  CA    . ALA A 1 278 ? 72.892  10.611  48.303  1.00 57.41  ? 305 ALA A CA    1 
ATOM   2120 C  C     . ALA A 1 278 ? 73.921  10.843  47.205  1.00 58.00  ? 305 ALA A C     1 
ATOM   2121 O  O     . ALA A 1 278 ? 74.846  11.648  47.365  1.00 58.24  ? 305 ALA A O     1 
ATOM   2122 C  CB    . ALA A 1 278 ? 73.161  9.289   49.020  1.00 44.52  ? 305 ALA A CB    1 
ATOM   2123 N  N     . GLU A 1 279 ? 73.776  10.141  46.078  1.00 57.12  ? 306 GLU A N     1 
ATOM   2124 C  CA    . GLU A 1 279 ? 74.704  10.331  44.970  1.00 61.61  ? 306 GLU A CA    1 
ATOM   2125 C  C     . GLU A 1 279 ? 74.536  11.699  44.322  1.00 45.96  ? 306 GLU A C     1 
ATOM   2126 O  O     . GLU A 1 279 ? 75.511  12.262  43.810  1.00 52.57  ? 306 GLU A O     1 
ATOM   2127 C  CB    . GLU A 1 279 ? 74.521  9.222   43.936  1.00 50.54  ? 306 GLU A CB    1 
ATOM   2128 C  CG    . GLU A 1 279 ? 74.975  7.853   44.417  1.00 58.59  ? 306 GLU A CG    1 
ATOM   2129 C  CD    . GLU A 1 279 ? 74.658  6.752   43.426  1.00 70.46  ? 306 GLU A CD    1 
ATOM   2130 O  OE1   . GLU A 1 279 ? 73.950  7.030   42.437  1.00 65.73  ? 306 GLU A OE1   1 
ATOM   2131 O  OE2   . GLU A 1 279 ? 75.116  5.609   43.638  1.00 68.07  ? 306 GLU A OE2   1 
ATOM   2132 N  N     . SER A 1 280 ? 73.320  12.249  44.336  1.00 49.86  ? 307 SER A N     1 
ATOM   2133 C  CA    . SER A 1 280 ? 73.109  13.584  43.784  1.00 49.98  ? 307 SER A CA    1 
ATOM   2134 C  C     . SER A 1 280 ? 73.852  14.640  44.592  1.00 50.84  ? 307 SER A C     1 
ATOM   2135 O  O     . SER A 1 280 ? 74.482  15.538  44.021  1.00 55.37  ? 307 SER A O     1 
ATOM   2136 C  CB    . SER A 1 280 ? 71.617  13.907  43.733  1.00 48.40  ? 307 SER A CB    1 
ATOM   2137 O  OG    . SER A 1 280 ? 71.401  15.225  43.262  1.00 63.96  ? 307 SER A OG    1 
ATOM   2138 N  N     . PHE A 1 281 ? 73.796  14.553  45.924  1.00 53.21  ? 308 PHE A N     1 
ATOM   2139 C  CA    . PHE A 1 281 ? 74.544  15.503  46.741  1.00 51.23  ? 308 PHE A CA    1 
ATOM   2140 C  C     . PHE A 1 281 ? 76.043  15.293  46.592  1.00 48.70  ? 308 PHE A C     1 
ATOM   2141 O  O     . PHE A 1 281 ? 76.818  16.253  46.659  1.00 52.86  ? 308 PHE A O     1 
ATOM   2142 C  CB    . PHE A 1 281 ? 74.143  15.396  48.211  1.00 47.81  ? 308 PHE A CB    1 
ATOM   2143 C  CG    . PHE A 1 281 ? 74.918  16.317  49.111  1.00 50.17  ? 308 PHE A CG    1 
ATOM   2144 C  CD1   . PHE A 1 281 ? 74.532  17.638  49.268  1.00 39.73  ? 308 PHE A CD1   1 
ATOM   2145 C  CD2   . PHE A 1 281 ? 76.046  15.867  49.785  1.00 47.46  ? 308 PHE A CD2   1 
ATOM   2146 C  CE1   . PHE A 1 281 ? 75.248  18.490  50.087  1.00 40.30  ? 308 PHE A CE1   1 
ATOM   2147 C  CE2   . PHE A 1 281 ? 76.766  16.716  50.601  1.00 49.21  ? 308 PHE A CE2   1 
ATOM   2148 C  CZ    . PHE A 1 281 ? 76.366  18.028  50.754  1.00 48.46  ? 308 PHE A CZ    1 
ATOM   2149 N  N     . MET A 1 282 ? 76.472  14.043  46.411  1.00 55.57  ? 309 MET A N     1 
ATOM   2150 C  CA    . MET A 1 282 ? 77.878  13.788  46.122  1.00 61.87  ? 309 MET A CA    1 
ATOM   2151 C  C     . MET A 1 282 ? 78.313  14.522  44.860  1.00 52.68  ? 309 MET A C     1 
ATOM   2152 O  O     . MET A 1 282 ? 79.430  15.047  44.787  1.00 47.31  ? 309 MET A O     1 
ATOM   2153 C  CB    . MET A 1 282 ? 78.121  12.287  45.982  1.00 44.20  ? 309 MET A CB    1 
ATOM   2154 C  CG    . MET A 1 282 ? 79.555  11.925  45.660  1.00 44.60  ? 309 MET A CG    1 
ATOM   2155 S  SD    . MET A 1 282 ? 79.672  10.725  44.325  1.00 71.67  ? 309 MET A SD    1 
ATOM   2156 C  CE    . MET A 1 282 ? 78.930  11.642  42.980  1.00 57.76  ? 309 MET A CE    1 
ATOM   2157 N  N     . HIS A 1 283 ? 77.430  14.584  43.860  1.00 44.01  ? 310 HIS A N     1 
ATOM   2158 C  CA    . HIS A 1 283 ? 77.738  15.328  42.646  1.00 59.02  ? 310 HIS A CA    1 
ATOM   2159 C  C     . HIS A 1 283 ? 77.892  16.815  42.928  1.00 53.66  ? 310 HIS A C     1 
ATOM   2160 O  O     . HIS A 1 283 ? 78.664  17.497  42.244  1.00 54.32  ? 310 HIS A O     1 
ATOM   2161 C  CB    . HIS A 1 283 ? 76.653  15.098  41.596  1.00 50.28  ? 310 HIS A CB    1 
ATOM   2162 C  CG    . HIS A 1 283 ? 76.974  15.692  40.262  1.00 45.64  ? 310 HIS A CG    1 
ATOM   2163 N  ND1   . HIS A 1 283 ? 76.410  16.866  39.812  1.00 53.70  ? 310 HIS A ND1   1 
ATOM   2164 C  CD2   . HIS A 1 283 ? 77.814  15.280  39.285  1.00 49.88  ? 310 HIS A CD2   1 
ATOM   2165 C  CE1   . HIS A 1 283 ? 76.880  17.145  38.610  1.00 51.65  ? 310 HIS A CE1   1 
ATOM   2166 N  NE2   . HIS A 1 283 ? 77.735  16.198  38.267  1.00 66.37  ? 310 HIS A NE2   1 
ATOM   2167 N  N     . VAL A 1 284 ? 77.164  17.338  43.917  1.00 52.51  ? 311 VAL A N     1 
ATOM   2168 C  CA    . VAL A 1 284 ? 77.371  18.722  44.336  1.00 51.85  ? 311 VAL A CA    1 
ATOM   2169 C  C     . VAL A 1 284 ? 78.803  18.914  44.816  1.00 50.55  ? 311 VAL A C     1 
ATOM   2170 O  O     . VAL A 1 284 ? 79.472  19.893  44.464  1.00 54.36  ? 311 VAL A O     1 
ATOM   2171 C  CB    . VAL A 1 284 ? 76.355  19.114  45.425  1.00 52.09  ? 311 VAL A CB    1 
ATOM   2172 C  CG1   . VAL A 1 284 ? 76.670  20.496  45.973  1.00 38.37  ? 311 VAL A CG1   1 
ATOM   2173 C  CG2   . VAL A 1 284 ? 74.939  19.061  44.879  1.00 38.87  ? 311 VAL A CG2   1 
ATOM   2174 N  N     . GLN A 1 285 ? 79.295  17.972  45.624  1.00 46.90  ? 312 GLN A N     1 
ATOM   2175 C  CA    . GLN A 1 285 ? 80.669  18.049  46.105  1.00 53.04  ? 312 GLN A CA    1 
ATOM   2176 C  C     . GLN A 1 285 ? 81.659  17.934  44.954  1.00 59.20  ? 312 GLN A C     1 
ATOM   2177 O  O     . GLN A 1 285 ? 82.690  18.617  44.941  1.00 61.16  ? 312 GLN A O     1 
ATOM   2178 C  CB    . GLN A 1 285 ? 80.916  16.956  47.144  1.00 53.93  ? 312 GLN A CB    1 
ATOM   2179 C  CG    . GLN A 1 285 ? 79.765  16.766  48.123  1.00 58.85  ? 312 GLN A CG    1 
ATOM   2180 C  CD    . GLN A 1 285 ? 80.120  15.833  49.263  1.00 55.77  ? 312 GLN A CD    1 
ATOM   2181 O  OE1   . GLN A 1 285 ? 79.643  14.699  49.326  1.00 58.95  ? 312 GLN A OE1   1 
ATOM   2182 N  NE2   . GLN A 1 285 ? 80.960  16.308  50.175  1.00 41.91  ? 312 GLN A NE2   1 
ATOM   2183 N  N     . LEU A 1 286 ? 81.363  17.069  43.979  1.00 61.56  ? 313 LEU A N     1 
ATOM   2184 C  CA    . LEU A 1 286 ? 82.173  17.013  42.766  1.00 54.85  ? 313 LEU A CA    1 
ATOM   2185 C  C     . LEU A 1 286 ? 82.162  18.350  42.039  1.00 54.87  ? 313 LEU A C     1 
ATOM   2186 O  O     . LEU A 1 286 ? 83.211  18.832  41.595  1.00 65.87  ? 313 LEU A O     1 
ATOM   2187 C  CB    . LEU A 1 286 ? 81.668  15.908  41.839  1.00 53.33  ? 313 LEU A CB    1 
ATOM   2188 C  CG    . LEU A 1 286 ? 81.856  14.453  42.264  1.00 50.93  ? 313 LEU A CG    1 
ATOM   2189 C  CD1   . LEU A 1 286 ? 81.444  13.524  41.134  1.00 57.10  ? 313 LEU A CD1   1 
ATOM   2190 C  CD2   . LEU A 1 286 ? 83.292  14.200  42.666  1.00 45.47  ? 313 LEU A CD2   1 
ATOM   2191 N  N     . GLU A 1 287 ? 80.983  18.967  41.911  1.00 51.50  ? 314 GLU A N     1 
ATOM   2192 C  CA    . GLU A 1 287 ? 80.884  20.244  41.211  1.00 66.54  ? 314 GLU A CA    1 
ATOM   2193 C  C     . GLU A 1 287 ? 81.615  21.355  41.954  1.00 60.71  ? 314 GLU A C     1 
ATOM   2194 O  O     . GLU A 1 287 ? 82.139  22.279  41.323  1.00 59.52  ? 314 GLU A O     1 
ATOM   2195 C  CB    . GLU A 1 287 ? 79.416  20.613  41.003  1.00 48.50  ? 314 GLU A CB    1 
ATOM   2196 C  CG    . GLU A 1 287 ? 78.710  19.743  39.977  1.00 53.80  ? 314 GLU A CG    1 
ATOM   2197 C  CD    . GLU A 1 287 ? 79.309  19.878  38.590  1.00 81.68  ? 314 GLU A CD    1 
ATOM   2198 O  OE1   . GLU A 1 287 ? 79.119  20.942  37.963  1.00 69.29  ? 314 GLU A OE1   1 
ATOM   2199 O  OE2   . GLU A 1 287 ? 79.979  18.927  38.130  1.00 83.17  ? 314 GLU A OE2   1 
ATOM   2200 N  N     . VAL A 1 288 ? 81.656  21.289  43.286  1.00 57.57  ? 315 VAL A N     1 
ATOM   2201 C  CA    . VAL A 1 288 ? 82.428  22.263  44.053  1.00 55.90  ? 315 VAL A CA    1 
ATOM   2202 C  C     . VAL A 1 288 ? 83.912  22.121  43.740  1.00 68.09  ? 315 VAL A C     1 
ATOM   2203 O  O     . VAL A 1 288 ? 84.610  23.110  43.488  1.00 67.32  ? 315 VAL A O     1 
ATOM   2204 C  CB    . VAL A 1 288 ? 82.153  22.103  45.559  1.00 57.76  ? 315 VAL A CB    1 
ATOM   2205 C  CG1   . VAL A 1 288 ? 83.259  22.757  46.371  1.00 62.33  ? 315 VAL A CG1   1 
ATOM   2206 C  CG2   . VAL A 1 288 ? 80.805  22.701  45.918  1.00 44.15  ? 315 VAL A CG2   1 
ATOM   2207 N  N     . MET A 1 289 ? 84.413  20.886  43.736  1.00 59.81  ? 316 MET A N     1 
ATOM   2208 C  CA    . MET A 1 289 ? 85.834  20.642  43.517  1.00 68.93  ? 316 MET A CA    1 
ATOM   2209 C  C     . MET A 1 289 ? 86.276  20.899  42.083  1.00 63.71  ? 316 MET A C     1 
ATOM   2210 O  O     . MET A 1 289 ? 87.450  20.670  41.776  1.00 62.17  ? 316 MET A O     1 
ATOM   2211 C  CB    . MET A 1 289 ? 86.188  19.207  43.912  1.00 55.62  ? 316 MET A CB    1 
ATOM   2212 C  CG    . MET A 1 289 ? 85.938  18.893  45.374  1.00 72.54  ? 316 MET A CG    1 
ATOM   2213 S  SD    . MET A 1 289 ? 86.442  17.219  45.797  1.00 76.41  ? 316 MET A SD    1 
ATOM   2214 C  CE    . MET A 1 289 ? 85.707  16.307  44.444  1.00 82.16  ? 316 MET A CE    1 
ATOM   2215 N  N     . VAL A 1 290 ? 85.387  21.362  41.203  1.00 62.46  ? 317 VAL A N     1 
ATOM   2216 C  CA    . VAL A 1 290 ? 85.798  21.688  39.840  1.00 56.93  ? 317 VAL A CA    1 
ATOM   2217 C  C     . VAL A 1 290 ? 86.661  22.944  39.832  1.00 68.02  ? 317 VAL A C     1 
ATOM   2218 O  O     . VAL A 1 290 ? 87.763  22.957  39.270  1.00 81.61  ? 317 VAL A O     1 
ATOM   2219 C  CB    . VAL A 1 290 ? 84.566  21.842  38.929  1.00 62.66  ? 317 VAL A CB    1 
ATOM   2220 C  CG1   . VAL A 1 290 ? 84.983  22.316  37.542  1.00 67.26  ? 317 VAL A CG1   1 
ATOM   2221 C  CG2   . VAL A 1 290 ? 83.802  20.528  38.839  1.00 62.64  ? 317 VAL A CG2   1 
ATOM   2222 N  N     . LYS A 1 291 ? 86.177  24.018  40.462  1.00 74.18  ? 318 LYS A N     1 
ATOM   2223 C  CA    . LYS A 1 291 ? 86.892  25.289  40.480  1.00 68.71  ? 318 LYS A CA    1 
ATOM   2224 C  C     . LYS A 1 291 ? 87.081  25.836  41.891  1.00 68.21  ? 318 LYS A C     1 
ATOM   2225 O  O     . LYS A 1 291 ? 87.422  27.013  42.046  1.00 82.02  ? 318 LYS A O     1 
ATOM   2226 C  CB    . LYS A 1 291 ? 86.167  26.320  39.609  1.00 66.39  ? 318 LYS A CB    1 
ATOM   2227 C  CG    . LYS A 1 291 ? 85.968  25.876  38.165  1.00 82.02  ? 318 LYS A CG    1 
ATOM   2228 C  CD    . LYS A 1 291 ? 85.164  26.892  37.371  1.00 97.29  ? 318 LYS A CD    1 
ATOM   2229 C  CE    . LYS A 1 291 ? 84.835  26.370  35.982  1.00 97.43  ? 318 LYS A CE    1 
ATOM   2230 N  NZ    . LYS A 1 291 ? 86.065  26.038  35.212  1.00 90.16  ? 318 LYS A NZ    1 
ATOM   2231 N  N     . HIS A 1 292 ? 86.870  25.024  42.915  1.00 63.77  ? 319 HIS A N     1 
ATOM   2232 C  CA    . HIS A 1 292 ? 87.091  25.406  44.300  1.00 62.98  ? 319 HIS A CA    1 
ATOM   2233 C  C     . HIS A 1 292 ? 87.824  24.272  44.999  1.00 69.19  ? 319 HIS A C     1 
ATOM   2234 O  O     . HIS A 1 292 ? 87.816  23.133  44.520  1.00 63.03  ? 319 HIS A O     1 
ATOM   2235 C  CB    . HIS A 1 292 ? 85.777  25.694  45.043  1.00 68.21  ? 319 HIS A CB    1 
ATOM   2236 C  CG    . HIS A 1 292 ? 84.799  26.517  44.263  1.00 68.01  ? 319 HIS A CG    1 
ATOM   2237 N  ND1   . HIS A 1 292 ? 83.997  25.983  43.278  1.00 87.96  ? 319 HIS A ND1   1 
ATOM   2238 C  CD2   . HIS A 1 292 ? 84.480  27.831  44.336  1.00 66.93  ? 319 HIS A CD2   1 
ATOM   2239 C  CE1   . HIS A 1 292 ? 83.233  26.934  42.771  1.00 84.46  ? 319 HIS A CE1   1 
ATOM   2240 N  NE2   . HIS A 1 292 ? 83.507  28.065  43.395  1.00 80.23  ? 319 HIS A NE2   1 
ATOM   2241 N  N     . PRO A 1 293 ? 88.472  24.552  46.126  1.00 63.76  ? 320 PRO A N     1 
ATOM   2242 C  CA    . PRO A 1 293 ? 88.974  23.470  46.980  1.00 63.33  ? 320 PRO A CA    1 
ATOM   2243 C  C     . PRO A 1 293 ? 87.822  22.630  47.497  1.00 64.96  ? 320 PRO A C     1 
ATOM   2244 O  O     . PRO A 1 293 ? 86.664  23.074  47.474  1.00 71.05  ? 320 PRO A O     1 
ATOM   2245 C  CB    . PRO A 1 293 ? 89.678  24.219  48.123  1.00 59.13  ? 320 PRO A CB    1 
ATOM   2246 C  CG    . PRO A 1 293 ? 90.018  25.549  47.548  1.00 60.92  ? 320 PRO A CG    1 
ATOM   2247 C  CD    . PRO A 1 293 ? 88.897  25.876  46.609  1.00 60.07  ? 320 PRO A CD    1 
ATOM   2248 N  N     . PRO A 1 294 ? 88.086  21.409  47.960  1.00 66.16  ? 321 PRO A N     1 
ATOM   2249 C  CA    . PRO A 1 294 ? 86.990  20.566  48.453  1.00 71.50  ? 321 PRO A CA    1 
ATOM   2250 C  C     . PRO A 1 294 ? 86.334  21.170  49.686  1.00 71.95  ? 321 PRO A C     1 
ATOM   2251 O  O     . PRO A 1 294 ? 87.003  21.731  50.557  1.00 76.10  ? 321 PRO A O     1 
ATOM   2252 C  CB    . PRO A 1 294 ? 87.680  19.235  48.773  1.00 57.96  ? 321 PRO A CB    1 
ATOM   2253 C  CG    . PRO A 1 294 ? 89.115  19.594  48.983  1.00 74.14  ? 321 PRO A CG    1 
ATOM   2254 C  CD    . PRO A 1 294 ? 89.387  20.723  48.037  1.00 60.89  ? 321 PRO A CD    1 
ATOM   2255 N  N     . ALA A 1 295 ? 85.008  21.060  49.745  1.00 60.53  ? 322 ALA A N     1 
ATOM   2256 C  CA    . ALA A 1 295 ? 84.252  21.537  50.898  1.00 52.87  ? 322 ALA A CA    1 
ATOM   2257 C  C     . ALA A 1 295 ? 84.476  20.587  52.068  1.00 67.76  ? 322 ALA A C     1 
ATOM   2258 O  O     . ALA A 1 295 ? 84.002  19.447  52.051  1.00 54.51  ? 322 ALA A O     1 
ATOM   2259 C  CB    . ALA A 1 295 ? 82.771  21.643  50.549  1.00 43.46  ? 322 ALA A CB    1 
ATOM   2260 N  N     . GLU A 1 296 ? 85.201  21.049  53.082  1.00 53.00  ? 323 GLU A N     1 
ATOM   2261 C  CA    . GLU A 1 296 ? 85.563  20.191  54.197  1.00 61.23  ? 323 GLU A CA    1 
ATOM   2262 C  C     . GLU A 1 296 ? 84.359  19.947  55.108  1.00 60.76  ? 323 GLU A C     1 
ATOM   2263 O  O     . GLU A 1 296 ? 83.453  20.782  55.193  1.00 53.89  ? 323 GLU A O     1 
ATOM   2264 C  CB    . GLU A 1 296 ? 86.699  20.816  55.001  1.00 59.03  ? 323 GLU A CB    1 
ATOM   2265 C  CG    . GLU A 1 296 ? 87.957  21.097  54.185  1.00 77.29  ? 323 GLU A CG    1 
ATOM   2266 C  CD    . GLU A 1 296 ? 88.606  19.835  53.643  1.00 96.38  ? 323 GLU A CD    1 
ATOM   2267 O  OE1   . GLU A 1 296 ? 88.379  18.746  54.215  1.00 97.21  ? 323 GLU A OE1   1 
ATOM   2268 O  OE2   . GLU A 1 296 ? 89.350  19.935  52.644  1.00 90.42  ? 323 GLU A OE2   1 
ATOM   2269 N  N     . PRO A 1 297 ? 84.318  18.809  55.789  1.00 71.94  ? 324 PRO A N     1 
ATOM   2270 C  CA    . PRO A 1 297 ? 83.213  18.525  56.710  1.00 66.30  ? 324 PRO A CA    1 
ATOM   2271 C  C     . PRO A 1 297 ? 83.450  19.183  58.066  1.00 66.12  ? 324 PRO A C     1 
ATOM   2272 O  O     . PRO A 1 297 ? 84.483  19.802  58.307  1.00 67.32  ? 324 PRO A O     1 
ATOM   2273 C  CB    . PRO A 1 297 ? 83.238  16.998  56.812  1.00 65.04  ? 324 PRO A CB    1 
ATOM   2274 C  CG    . PRO A 1 297 ? 84.687  16.672  56.674  1.00 50.48  ? 324 PRO A CG    1 
ATOM   2275 C  CD    . PRO A 1 297 ? 85.245  17.668  55.686  1.00 49.90  ? 324 PRO A CD    1 
ATOM   2276 N  N     . SER A 1 298 ? 82.466  19.041  58.951  1.00 68.71  ? 325 SER A N     1 
ATOM   2277 C  CA    . SER A 1 298 ? 82.620  19.539  60.310  1.00 58.29  ? 325 SER A CA    1 
ATOM   2278 C  C     . SER A 1 298 ? 83.687  18.736  61.043  1.00 63.38  ? 325 SER A C     1 
ATOM   2279 O  O     . SER A 1 298 ? 83.830  17.530  60.830  1.00 72.87  ? 325 SER A O     1 
ATOM   2280 C  CB    . SER A 1 298 ? 81.287  19.455  61.057  1.00 65.19  ? 325 SER A CB    1 
ATOM   2281 O  OG    . SER A 1 298 ? 81.458  19.713  62.443  1.00 62.96  ? 325 SER A OG    1 
ATOM   2282 N  N     . ARG A 1 299 ? 84.444  19.410  61.908  1.00 68.62  ? 326 ARG A N     1 
ATOM   2283 C  CA    . ARG A 1 299 ? 85.451  18.730  62.712  1.00 74.93  ? 326 ARG A CA    1 
ATOM   2284 C  C     . ARG A 1 299 ? 84.850  17.957  63.877  1.00 75.50  ? 326 ARG A C     1 
ATOM   2285 O  O     . ARG A 1 299 ? 85.596  17.316  64.625  1.00 83.99  ? 326 ARG A O     1 
ATOM   2286 C  CB    . ARG A 1 299 ? 86.482  19.735  63.233  1.00 84.96  ? 326 ARG A CB    1 
ATOM   2287 C  CG    . ARG A 1 299 ? 85.915  20.798  64.153  1.00 80.42  ? 326 ARG A CG    1 
ATOM   2288 C  CD    . ARG A 1 299 ? 86.977  21.823  64.515  1.00 91.71  ? 326 ARG A CD    1 
ATOM   2289 N  NE    . ARG A 1 299 ? 86.563  22.676  65.622  1.00 111.46 ? 326 ARG A NE    1 
ATOM   2290 C  CZ    . ARG A 1 299 ? 86.844  22.435  66.896  1.00 119.16 ? 326 ARG A CZ    1 
ATOM   2291 N  NH1   . ARG A 1 299 ? 87.538  21.369  67.262  1.00 113.38 ? 326 ARG A NH1   1 
ATOM   2292 N  NH2   . ARG A 1 299 ? 86.417  23.284  67.827  1.00 124.68 ? 326 ARG A NH2   1 
ATOM   2293 N  N     . PHE A 1 300 ? 83.529  18.003  64.049  1.00 71.44  ? 327 PHE A N     1 
ATOM   2294 C  CA    . PHE A 1 300 ? 82.844  17.230  65.072  1.00 77.14  ? 327 PHE A CA    1 
ATOM   2295 C  C     . PHE A 1 300 ? 82.076  16.045  64.508  1.00 73.99  ? 327 PHE A C     1 
ATOM   2296 O  O     . PHE A 1 300 ? 81.587  15.219  65.286  1.00 84.13  ? 327 PHE A O     1 
ATOM   2297 C  CB    . PHE A 1 300 ? 81.881  18.129  65.860  1.00 72.59  ? 327 PHE A CB    1 
ATOM   2298 C  CG    . PHE A 1 300 ? 82.447  19.481  66.183  1.00 84.40  ? 327 PHE A CG    1 
ATOM   2299 C  CD1   . PHE A 1 300 ? 83.375  19.635  67.200  1.00 76.45  ? 327 PHE A CD1   1 
ATOM   2300 C  CD2   . PHE A 1 300 ? 82.050  20.600  65.468  1.00 82.59  ? 327 PHE A CD2   1 
ATOM   2301 C  CE1   . PHE A 1 300 ? 83.898  20.880  67.498  1.00 72.11  ? 327 PHE A CE1   1 
ATOM   2302 C  CE2   . PHE A 1 300 ? 82.568  21.849  65.760  1.00 87.96  ? 327 PHE A CE2   1 
ATOM   2303 C  CZ    . PHE A 1 300 ? 83.493  21.989  66.777  1.00 88.85  ? 327 PHE A CZ    1 
ATOM   2304 N  N     . ILE A 1 301 ? 81.951  15.945  63.187  1.00 68.03  ? 328 ILE A N     1 
ATOM   2305 C  CA    . ILE A 1 301 ? 81.297  14.824  62.525  1.00 65.58  ? 328 ILE A CA    1 
ATOM   2306 C  C     . ILE A 1 301 ? 82.303  14.171  61.590  1.00 84.91  ? 328 ILE A C     1 
ATOM   2307 O  O     . ILE A 1 301 ? 83.123  14.857  60.969  1.00 90.72  ? 328 ILE A O     1 
ATOM   2308 C  CB    . ILE A 1 301 ? 80.048  15.267  61.734  1.00 77.01  ? 328 ILE A CB    1 
ATOM   2309 C  CG1   . ILE A 1 301 ? 79.192  16.230  62.554  1.00 77.90  ? 328 ILE A CG1   1 
ATOM   2310 C  CG2   . ILE A 1 301 ? 79.227  14.059  61.310  1.00 92.51  ? 328 ILE A CG2   1 
ATOM   2311 C  CD1   . ILE A 1 301 ? 78.089  16.885  61.746  1.00 63.23  ? 328 ILE A CD1   1 
ATOM   2312 N  N     . SER A 1 302 ? 82.239  12.848  61.489  1.00 93.30  ? 329 SER A N     1 
ATOM   2313 C  CA    . SER A 1 302 ? 83.036  12.093  60.533  1.00 91.11  ? 329 SER A CA    1 
ATOM   2314 C  C     . SER A 1 302 ? 82.109  11.459  59.507  1.00 100.77 ? 329 SER A C     1 
ATOM   2315 O  O     . SER A 1 302 ? 81.108  10.834  59.871  1.00 101.16 ? 329 SER A O     1 
ATOM   2316 C  CB    . SER A 1 302 ? 83.870  11.017  61.232  1.00 97.28  ? 329 SER A CB    1 
ATOM   2317 O  OG    . SER A 1 302 ? 83.043  10.121  61.954  1.00 105.51 ? 329 SER A OG    1 
ATOM   2318 N  N     . ALA A 1 303 ? 82.436  11.635  58.230  1.00 102.38 ? 330 ALA A N     1 
ATOM   2319 C  CA    . ALA A 1 303 ? 81.707  10.957  57.175  1.00 98.98  ? 330 ALA A CA    1 
ATOM   2320 C  C     . ALA A 1 303 ? 82.089  9.476   57.153  1.00 106.98 ? 330 ALA A C     1 
ATOM   2321 O  O     . ALA A 1 303 ? 83.183  9.104   57.585  1.00 96.06  ? 330 ALA A O     1 
ATOM   2322 C  CB    . ALA A 1 303 ? 82.006  11.600  55.823  1.00 84.76  ? 330 ALA A CB    1 
ATOM   2323 N  N     . PRO A 1 304 ? 81.201  8.607   56.674  1.00 113.40 ? 331 PRO A N     1 
ATOM   2324 C  CA    . PRO A 1 304 ? 81.524  7.177   56.650  1.00 118.87 ? 331 PRO A CA    1 
ATOM   2325 C  C     . PRO A 1 304 ? 82.564  6.851   55.590  1.00 112.69 ? 331 PRO A C     1 
ATOM   2326 O  O     . PRO A 1 304 ? 82.636  7.487   54.535  1.00 105.85 ? 331 PRO A O     1 
ATOM   2327 C  CB    . PRO A 1 304 ? 80.178  6.517   56.333  1.00 118.64 ? 331 PRO A CB    1 
ATOM   2328 C  CG    . PRO A 1 304 ? 79.437  7.552   55.565  1.00 117.87 ? 331 PRO A CG    1 
ATOM   2329 C  CD    . PRO A 1 304 ? 79.844  8.873   56.163  1.00 113.19 ? 331 PRO A CD    1 
ATOM   2330 N  N     . THR A 1 305 ? 83.381  5.846   55.893  1.00 112.50 ? 332 THR A N     1 
ATOM   2331 C  CA    . THR A 1 305 ? 84.421  5.416   54.969  1.00 114.33 ? 332 THR A CA    1 
ATOM   2332 C  C     . THR A 1 305 ? 83.801  4.878   53.683  1.00 108.94 ? 332 THR A C     1 
ATOM   2333 O  O     . THR A 1 305 ? 82.711  4.300   53.685  1.00 109.13 ? 332 THR A O     1 
ATOM   2334 C  CB    . THR A 1 305 ? 85.302  4.347   55.623  1.00 121.27 ? 332 THR A CB    1 
ATOM   2335 O  OG1   . THR A 1 305 ? 85.728  4.805   56.912  1.00 124.59 ? 332 THR A OG1   1 
ATOM   2336 C  CG2   . THR A 1 305 ? 86.534  4.061   54.772  1.00 121.25 ? 332 THR A CG2   1 
ATOM   2337 N  N     . LYS A 1 306 ? 84.503  5.085   52.573  1.00 96.08  ? 333 LYS A N     1 
ATOM   2338 C  CA    . LYS A 1 306 ? 84.046  4.664   51.257  1.00 97.51  ? 333 LYS A CA    1 
ATOM   2339 C  C     . LYS A 1 306 ? 84.926  3.534   50.739  1.00 91.25  ? 333 LYS A C     1 
ATOM   2340 O  O     . LYS A 1 306 ? 86.139  3.525   50.970  1.00 89.34  ? 333 LYS A O     1 
ATOM   2341 C  CB    . LYS A 1 306 ? 84.061  5.840   50.280  1.00 95.08  ? 333 LYS A CB    1 
ATOM   2342 C  CG    . LYS A 1 306 ? 83.861  7.185   50.957  1.00 84.70  ? 333 LYS A CG    1 
ATOM   2343 C  CD    . LYS A 1 306 ? 83.462  8.271   49.972  1.00 83.32  ? 333 LYS A CD    1 
ATOM   2344 C  CE    . LYS A 1 306 ? 82.029  8.085   49.499  1.00 87.82  ? 333 LYS A CE    1 
ATOM   2345 N  NZ    . LYS A 1 306 ? 81.515  9.286   48.783  1.00 79.02  ? 333 LYS A NZ    1 
ATOM   2346 N  N     . THR A 1 307 ? 84.311  2.585   50.035  1.00 89.07  ? 334 THR A N     1 
ATOM   2347 C  CA    . THR A 1 307 ? 85.022  1.423   49.508  1.00 95.85  ? 334 THR A CA    1 
ATOM   2348 C  C     . THR A 1 307 ? 85.170  1.553   47.999  1.00 82.46  ? 334 THR A C     1 
ATOM   2349 O  O     . THR A 1 307 ? 84.180  1.385   47.267  1.00 76.45  ? 334 THR A O     1 
ATOM   2350 C  CB    . THR A 1 307 ? 84.289  0.127   49.863  1.00 96.39  ? 334 THR A CB    1 
ATOM   2351 O  OG1   . THR A 1 307 ? 82.969  0.151   49.306  1.00 114.22 ? 334 THR A OG1   1 
ATOM   2352 C  CG2   . THR A 1 307 ? 84.194  -0.034  51.375  1.00 91.00  ? 334 THR A CG2   1 
ATOM   2353 N  N     . PRO A 1 308 ? 86.360  1.855   47.487  1.00 80.72  ? 335 PRO A N     1 
ATOM   2354 C  CA    . PRO A 1 308 ? 86.526  2.021   46.040  1.00 77.49  ? 335 PRO A CA    1 
ATOM   2355 C  C     . PRO A 1 308 ? 86.547  0.687   45.314  1.00 75.44  ? 335 PRO A C     1 
ATOM   2356 O  O     . PRO A 1 308 ? 86.913  -0.351  45.869  1.00 83.71  ? 335 PRO A O     1 
ATOM   2357 C  CB    . PRO A 1 308 ? 87.882  2.731   45.916  1.00 89.66  ? 335 PRO A CB    1 
ATOM   2358 C  CG    . PRO A 1 308 ? 88.251  3.165   47.313  1.00 89.48  ? 335 PRO A CG    1 
ATOM   2359 C  CD    . PRO A 1 308 ? 87.588  2.189   48.225  1.00 84.06  ? 335 PRO A CD    1 
ATOM   2360 N  N     . ASP A 1 309 ? 86.148  0.728   44.046  1.00 83.79  ? 336 ASP A N     1 
ATOM   2361 C  CA    . ASP A 1 309 ? 86.161  -0.460  43.199  1.00 78.53  ? 336 ASP A CA    1 
ATOM   2362 C  C     . ASP A 1 309 ? 86.577  -0.038  41.792  1.00 81.39  ? 336 ASP A C     1 
ATOM   2363 O  O     . ASP A 1 309 ? 86.950  1.114   41.550  1.00 76.80  ? 336 ASP A O     1 
ATOM   2364 C  CB    . ASP A 1 309 ? 84.801  -1.180  43.243  1.00 60.89  ? 336 ASP A CB    1 
ATOM   2365 C  CG    . ASP A 1 309 ? 83.692  -0.420  42.525  1.00 82.02  ? 336 ASP A CG    1 
ATOM   2366 O  OD1   . ASP A 1 309 ? 83.920  0.711   42.053  1.00 97.56  ? 336 ASP A OD1   1 
ATOM   2367 O  OD2   . ASP A 1 309 ? 82.571  -0.971  42.438  1.00 82.19  ? 336 ASP A OD2   1 
ATOM   2368 N  N     . LYS A 1 310 ? 86.509  -0.984  40.856  1.00 81.54  ? 337 LYS A N     1 
ATOM   2369 C  CA    . LYS A 1 310 ? 86.854  -0.749  39.459  1.00 84.29  ? 337 LYS A CA    1 
ATOM   2370 C  C     . LYS A 1 310 ? 85.631  -0.711  38.549  1.00 76.44  ? 337 LYS A C     1 
ATOM   2371 O  O     . LYS A 1 310 ? 85.786  -0.678  37.324  1.00 75.38  ? 337 LYS A O     1 
ATOM   2372 C  CB    . LYS A 1 310 ? 87.834  -1.816  38.967  1.00 81.50  ? 337 LYS A CB    1 
ATOM   2373 C  CG    . LYS A 1 310 ? 89.177  -1.819  39.683  1.00 77.31  ? 337 LYS A CG    1 
ATOM   2374 C  CD    . LYS A 1 310 ? 90.026  -0.630  39.271  1.00 86.31  ? 337 LYS A CD    1 
ATOM   2375 C  CE    . LYS A 1 310 ? 91.360  -0.623  39.999  1.00 91.65  ? 337 LYS A CE    1 
ATOM   2376 N  NZ    . LYS A 1 310 ? 92.151  -1.856  39.739  1.00 90.03  ? 337 LYS A NZ    1 
ATOM   2377 N  N     . MET A 1 311 ? 84.423  -0.724  39.119  1.00 80.91  ? 338 MET A N     1 
ATOM   2378 C  CA    . MET A 1 311 ? 83.167  -0.649  38.366  1.00 71.72  ? 338 MET A CA    1 
ATOM   2379 C  C     . MET A 1 311 ? 82.991  -1.828  37.413  1.00 75.59  ? 338 MET A C     1 
ATOM   2380 O  O     . MET A 1 311 ? 82.311  -1.715  36.390  1.00 84.65  ? 338 MET A O     1 
ATOM   2381 C  CB    . MET A 1 311 ? 83.054  0.668   37.593  1.00 68.97  ? 338 MET A CB    1 
ATOM   2382 C  CG    . MET A 1 311 ? 82.995  1.905   38.463  1.00 74.05  ? 338 MET A CG    1 
ATOM   2383 S  SD    . MET A 1 311 ? 83.015  3.398   37.459  1.00 69.12  ? 338 MET A SD    1 
ATOM   2384 C  CE    . MET A 1 311 ? 84.636  3.261   36.714  1.00 80.48  ? 338 MET A CE    1 
ATOM   2385 N  N     . GLY A 1 312 ? 83.592  -2.972  37.742  1.00 76.01  ? 339 GLY A N     1 
ATOM   2386 C  CA    . GLY A 1 312 ? 83.522  -4.143  36.899  1.00 63.70  ? 339 GLY A CA    1 
ATOM   2387 C  C     . GLY A 1 312 ? 84.529  -4.185  35.771  1.00 63.94  ? 339 GLY A C     1 
ATOM   2388 O  O     . GLY A 1 312 ? 84.722  -5.251  35.173  1.00 86.72  ? 339 GLY A O     1 
ATOM   2389 N  N     . PHE A 1 313 ? 85.171  -3.064  35.453  1.00 74.89  ? 340 PHE A N     1 
ATOM   2390 C  CA    . PHE A 1 313 ? 86.218  -3.063  34.446  1.00 76.60  ? 340 PHE A CA    1 
ATOM   2391 C  C     . PHE A 1 313 ? 87.415  -3.878  34.927  1.00 88.21  ? 340 PHE A C     1 
ATOM   2392 O  O     . PHE A 1 313 ? 87.623  -4.085  36.126  1.00 95.93  ? 340 PHE A O     1 
ATOM   2393 C  CB    . PHE A 1 313 ? 86.664  -1.637  34.127  1.00 60.77  ? 340 PHE A CB    1 
ATOM   2394 C  CG    . PHE A 1 313 ? 85.601  -0.794  33.486  1.00 68.10  ? 340 PHE A CG    1 
ATOM   2395 C  CD1   . PHE A 1 313 ? 85.349  -0.888  32.128  1.00 70.75  ? 340 PHE A CD1   1 
ATOM   2396 C  CD2   . PHE A 1 313 ? 84.862  0.104   34.237  1.00 71.19  ? 340 PHE A CD2   1 
ATOM   2397 C  CE1   . PHE A 1 313 ? 84.374  -0.110  31.534  1.00 66.31  ? 340 PHE A CE1   1 
ATOM   2398 C  CE2   . PHE A 1 313 ? 83.887  0.886   33.648  1.00 75.67  ? 340 PHE A CE2   1 
ATOM   2399 C  CZ    . PHE A 1 313 ? 83.643  0.779   32.294  1.00 58.74  ? 340 PHE A CZ    1 
ATOM   2400 N  N     . ASP A 1 314 ? 88.212  -4.348  33.965  1.00 74.47  ? 341 ASP A N     1 
ATOM   2401 C  CA    . ASP A 1 314 ? 89.421  -5.083  34.317  1.00 79.11  ? 341 ASP A CA    1 
ATOM   2402 C  C     . ASP A 1 314 ? 90.488  -4.157  34.884  1.00 83.02  ? 341 ASP A C     1 
ATOM   2403 O  O     . ASP A 1 314 ? 91.318  -4.592  35.692  1.00 91.68  ? 341 ASP A O     1 
ATOM   2404 C  CB    . ASP A 1 314 ? 89.950  -5.835  33.097  1.00 89.16  ? 341 ASP A CB    1 
ATOM   2405 C  CG    . ASP A 1 314 ? 88.954  -6.844  32.561  1.00 88.21  ? 341 ASP A CG    1 
ATOM   2406 O  OD1   . ASP A 1 314 ? 87.846  -6.948  33.129  1.00 94.62  ? 341 ASP A OD1   1 
ATOM   2407 O  OD2   . ASP A 1 314 ? 89.278  -7.535  31.575  1.00 106.16 ? 341 ASP A OD2   1 
ATOM   2408 N  N     . GLU A 1 315 ? 90.478  -2.887  34.483  1.00 83.59  ? 342 GLU A N     1 
ATOM   2409 C  CA    . GLU A 1 315 ? 91.401  -1.896  35.017  1.00 88.10  ? 342 GLU A CA    1 
ATOM   2410 C  C     . GLU A 1 315 ? 90.878  -0.507  34.678  1.00 82.97  ? 342 GLU A C     1 
ATOM   2411 O  O     . GLU A 1 315 ? 90.217  -0.310  33.655  1.00 84.08  ? 342 GLU A O     1 
ATOM   2412 C  CB    . GLU A 1 315 ? 92.822  -2.085  34.467  1.00 89.52  ? 342 GLU A CB    1 
ATOM   2413 C  CG    . GLU A 1 315 ? 93.862  -1.153  35.083  1.00 92.56  ? 342 GLU A CG    1 
ATOM   2414 C  CD    . GLU A 1 315 ? 94.058  -1.388  36.568  1.00 98.94  ? 342 GLU A CD    1 
ATOM   2415 O  OE1   . GLU A 1 315 ? 94.870  -2.266  36.932  1.00 103.35 ? 342 GLU A OE1   1 
ATOM   2416 O  OE2   . GLU A 1 315 ? 93.394  -0.699  37.372  1.00 96.60  ? 342 GLU A OE2   1 
ATOM   2417 N  N     . VAL A 1 316 ? 91.172  0.447   35.558  1.00 72.55  ? 343 VAL A N     1 
ATOM   2418 C  CA    . VAL A 1 316 ? 90.827  1.850   35.364  1.00 76.40  ? 343 VAL A CA    1 
ATOM   2419 C  C     . VAL A 1 316 ? 92.126  2.643   35.399  1.00 78.83  ? 343 VAL A C     1 
ATOM   2420 O  O     . VAL A 1 316 ? 92.788  2.716   36.442  1.00 89.89  ? 343 VAL A O     1 
ATOM   2421 C  CB    . VAL A 1 316 ? 89.841  2.355   36.427  1.00 70.16  ? 343 VAL A CB    1 
ATOM   2422 C  CG1   . VAL A 1 316 ? 89.458  3.804   36.153  1.00 65.60  ? 343 VAL A CG1   1 
ATOM   2423 C  CG2   . VAL A 1 316 ? 88.605  1.469   36.470  1.00 79.65  ? 343 VAL A CG2   1 
ATOM   2424 N  N     . PHE A 1 317 ? 92.492  3.235   34.264  1.00 73.16  ? 344 PHE A N     1 
ATOM   2425 C  CA    . PHE A 1 317 ? 93.726  3.995   34.135  1.00 84.70  ? 344 PHE A CA    1 
ATOM   2426 C  C     . PHE A 1 317 ? 93.452  5.488   34.269  1.00 76.62  ? 344 PHE A C     1 
ATOM   2427 O  O     . PHE A 1 317 ? 92.372  5.975   33.928  1.00 78.97  ? 344 PHE A O     1 
ATOM   2428 C  CB    . PHE A 1 317 ? 94.404  3.721   32.790  1.00 79.05  ? 344 PHE A CB    1 
ATOM   2429 C  CG    . PHE A 1 317 ? 94.804  2.288   32.588  1.00 74.90  ? 344 PHE A CG    1 
ATOM   2430 C  CD1   . PHE A 1 317 ? 96.039  1.832   33.022  1.00 84.91  ? 344 PHE A CD1   1 
ATOM   2431 C  CD2   . PHE A 1 317 ? 93.951  1.400   31.955  1.00 80.51  ? 344 PHE A CD2   1 
ATOM   2432 C  CE1   . PHE A 1 317 ? 96.412  0.512   32.834  1.00 88.04  ? 344 PHE A CE1   1 
ATOM   2433 C  CE2   . PHE A 1 317 ? 94.318  0.078   31.762  1.00 94.79  ? 344 PHE A CE2   1 
ATOM   2434 C  CZ    . PHE A 1 317 ? 95.552  -0.365  32.201  1.00 94.77  ? 344 PHE A CZ    1 
ATOM   2435 N  N     . MET A 1 318 ? 94.456  6.211   34.763  1.00 85.38  ? 345 MET A N     1 
ATOM   2436 C  CA    . MET A 1 318 ? 94.382  7.661   34.925  1.00 85.31  ? 345 MET A CA    1 
ATOM   2437 C  C     . MET A 1 318 ? 95.725  8.239   34.502  1.00 84.31  ? 345 MET A C     1 
ATOM   2438 O  O     . MET A 1 318 ? 96.735  8.035   35.185  1.00 88.67  ? 345 MET A O     1 
ATOM   2439 C  CB    . MET A 1 318 ? 94.043  8.042   36.368  1.00 96.77  ? 345 MET A CB    1 
ATOM   2440 C  CG    . MET A 1 318 ? 92.946  9.091   36.497  1.00 87.77  ? 345 MET A CG    1 
ATOM   2441 S  SD    . MET A 1 318 ? 93.518  10.775  36.208  1.00 105.54 ? 345 MET A SD    1 
ATOM   2442 C  CE    . MET A 1 318 ? 94.628  10.998  37.595  1.00 96.59  ? 345 MET A CE    1 
ATOM   2443 N  N     . ILE A 1 319 ? 95.738  8.940   33.372  1.00 84.94  ? 346 ILE A N     1 
ATOM   2444 C  CA    . ILE A 1 319 ? 96.950  9.550   32.838  1.00 87.08  ? 346 ILE A CA    1 
ATOM   2445 C  C     . ILE A 1 319 ? 97.135  10.911  33.495  1.00 89.70  ? 346 ILE A C     1 
ATOM   2446 O  O     . ILE A 1 319 ? 96.278  11.792  33.369  1.00 88.55  ? 346 ILE A O     1 
ATOM   2447 C  CB    . ILE A 1 319 ? 96.875  9.685   31.310  1.00 76.35  ? 346 ILE A CB    1 
ATOM   2448 C  CG1   . ILE A 1 319 ? 96.552  8.337   30.667  1.00 84.26  ? 346 ILE A CG1   1 
ATOM   2449 C  CG2   . ILE A 1 319 ? 98.176  10.240  30.762  1.00 72.47  ? 346 ILE A CG2   1 
ATOM   2450 C  CD1   . ILE A 1 319 ? 96.462  8.393   29.160  1.00 79.49  ? 346 ILE A CD1   1 
ATOM   2451 N  N     . ASN A 1 320 ? 98.257  11.089  34.188  1.00 88.25  ? 347 ASN A N     1 
ATOM   2452 C  CA    . ASN A 1 320 ? 98.537  12.336  34.885  1.00 88.20  ? 347 ASN A CA    1 
ATOM   2453 C  C     . ASN A 1 320 ? 100.027 12.632  34.834  1.00 97.16  ? 347 ASN A C     1 
ATOM   2454 O  O     . ASN A 1 320 ? 100.845 11.786  35.210  1.00 92.86  ? 347 ASN A O     1 
ATOM   2455 C  CB    . ASN A 1 320 ? 98.065  12.277  36.340  1.00 85.05  ? 347 ASN A CB    1 
ATOM   2456 C  CG    . ASN A 1 320 ? 98.535  13.465  37.150  1.00 93.45  ? 347 ASN A CG    1 
ATOM   2457 O  OD1   . ASN A 1 320 ? 99.351  13.326  38.059  1.00 97.26  ? 347 ASN A OD1   1 
ATOM   2458 N  ND2   . ASN A 1 320 ? 98.030  14.647  36.814  1.00 92.60  ? 347 ASN A ND2   1 
ATOM   2459 N  N     . LEU A 1 321 ? 100.370 13.830  34.369  1.00 101.71 ? 348 LEU A N     1 
ATOM   2460 C  CA    . LEU A 1 321 ? 101.750 14.289  34.414  1.00 98.30  ? 348 LEU A CA    1 
ATOM   2461 C  C     . LEU A 1 321 ? 102.202 14.443  35.860  1.00 100.37 ? 348 LEU A C     1 
ATOM   2462 O  O     . LEU A 1 321 ? 101.456 14.931  36.713  1.00 94.34  ? 348 LEU A O     1 
ATOM   2463 C  CB    . LEU A 1 321 ? 101.892 15.617  33.674  1.00 104.18 ? 348 LEU A CB    1 
ATOM   2464 C  CG    . LEU A 1 321 ? 101.598 15.596  32.172  1.00 107.55 ? 348 LEU A CG    1 
ATOM   2465 C  CD1   . LEU A 1 321 ? 101.217 16.981  31.684  1.00 117.72 ? 348 LEU A CD1   1 
ATOM   2466 C  CD2   . LEU A 1 321 ? 102.795 15.068  31.394  1.00 109.14 ? 348 LEU A CD2   1 
ATOM   2467 N  N     . ARG A 1 322 ? 103.440 14.023  36.132  1.00 105.53 ? 349 ARG A N     1 
ATOM   2468 C  CA    . ARG A 1 322 ? 103.952 14.058  37.499  1.00 111.47 ? 349 ARG A CA    1 
ATOM   2469 C  C     . ARG A 1 322 ? 104.024 15.478  38.046  1.00 116.94 ? 349 ARG A C     1 
ATOM   2470 O  O     . ARG A 1 322 ? 103.955 15.673  39.265  1.00 119.88 ? 349 ARG A O     1 
ATOM   2471 C  CB    . ARG A 1 322 ? 105.327 13.390  37.557  1.00 118.65 ? 349 ARG A CB    1 
ATOM   2472 C  CG    . ARG A 1 322 ? 105.873 13.182  38.959  1.00 124.59 ? 349 ARG A CG    1 
ATOM   2473 C  CD    . ARG A 1 322 ? 107.326 12.756  38.895  1.00 136.66 ? 349 ARG A CD    1 
ATOM   2474 N  NE    . ARG A 1 322 ? 108.116 13.702  38.115  1.00 151.84 ? 349 ARG A NE    1 
ATOM   2475 C  CZ    . ARG A 1 322 ? 108.966 14.579  38.633  1.00 158.89 ? 349 ARG A CZ    1 
ATOM   2476 N  NH1   . ARG A 1 322 ? 109.200 14.630  39.934  1.00 159.52 ? 349 ARG A NH1   1 
ATOM   2477 N  NH2   . ARG A 1 322 ? 109.600 15.423  37.824  1.00 139.09 ? 349 ARG A NH2   1 
ATOM   2478 N  N     . ARG A 1 323 ? 104.143 16.479  37.171  1.00 112.11 ? 350 ARG A N     1 
ATOM   2479 C  CA    . ARG A 1 323 ? 104.226 17.862  37.624  1.00 111.10 ? 350 ARG A CA    1 
ATOM   2480 C  C     . ARG A 1 323 ? 102.861 18.478  37.909  1.00 112.43 ? 350 ARG A C     1 
ATOM   2481 O  O     . ARG A 1 323 ? 102.792 19.499  38.602  1.00 118.18 ? 350 ARG A O     1 
ATOM   2482 C  CB    . ARG A 1 323 ? 104.966 18.718  36.593  1.00 107.85 ? 350 ARG A CB    1 
ATOM   2483 C  CG    . ARG A 1 323 ? 104.244 18.888  35.266  1.00 123.55 ? 350 ARG A CG    1 
ATOM   2484 C  CD    . ARG A 1 323 ? 105.014 19.835  34.356  1.00 120.56 ? 350 ARG A CD    1 
ATOM   2485 N  NE    . ARG A 1 323 ? 104.290 20.154  33.132  1.00 124.40 ? 350 ARG A NE    1 
ATOM   2486 C  CZ    . ARG A 1 323 ? 104.443 19.512  31.982  1.00 122.82 ? 350 ARG A CZ    1 
ATOM   2487 N  NH1   . ARG A 1 323 ? 105.281 18.495  31.865  1.00 115.04 ? 350 ARG A NH1   1 
ATOM   2488 N  NH2   . ARG A 1 323 ? 103.741 19.901  30.922  1.00 127.60 ? 350 ARG A NH2   1 
ATOM   2489 N  N     . ARG A 1 324 ? 101.779 17.892  37.396  1.00 107.72 ? 351 ARG A N     1 
ATOM   2490 C  CA    . ARG A 1 324 ? 100.432 18.422  37.615  1.00 102.47 ? 351 ARG A CA    1 
ATOM   2491 C  C     . ARG A 1 324 ? 99.840  17.798  38.879  1.00 101.31 ? 351 ARG A C     1 
ATOM   2492 O  O     . ARG A 1 324 ? 98.981  16.916  38.843  1.00 99.48  ? 351 ARG A O     1 
ATOM   2493 C  CB    . ARG A 1 324 ? 99.556  18.167  36.395  1.00 107.71 ? 351 ARG A CB    1 
ATOM   2494 C  CG    . ARG A 1 324 ? 100.084 18.797  35.119  1.00 105.69 ? 351 ARG A CG    1 
ATOM   2495 C  CD    . ARG A 1 324 ? 100.162 20.310  35.243  1.00 112.67 ? 351 ARG A CD    1 
ATOM   2496 N  NE    . ARG A 1 324 ? 100.966 20.904  34.183  1.00 131.56 ? 351 ARG A NE    1 
ATOM   2497 C  CZ    . ARG A 1 324 ? 101.200 22.204  34.061  1.00 137.41 ? 351 ARG A CZ    1 
ATOM   2498 N  NH1   . ARG A 1 324 ? 100.704 23.079  34.921  1.00 129.64 ? 351 ARG A NH1   1 
ATOM   2499 N  NH2   . ARG A 1 324 ? 101.948 22.637  33.050  1.00 122.06 ? 351 ARG A NH2   1 
ATOM   2500 N  N     . GLN A 1 325 ? 100.332 18.284  40.022  1.00 101.32 ? 352 GLN A N     1 
ATOM   2501 C  CA    . GLN A 1 325 ? 99.881  17.754  41.305  1.00 105.86 ? 352 GLN A CA    1 
ATOM   2502 C  C     . GLN A 1 325 ? 98.442  18.156  41.601  1.00 96.03  ? 352 GLN A C     1 
ATOM   2503 O  O     . GLN A 1 325 ? 97.669  17.359  42.146  1.00 90.94  ? 352 GLN A O     1 
ATOM   2504 C  CB    . GLN A 1 325 ? 100.805 18.227  42.427  1.00 105.91 ? 352 GLN A CB    1 
ATOM   2505 C  CG    . GLN A 1 325 ? 102.251 17.791  42.277  1.00 129.21 ? 352 GLN A CG    1 
ATOM   2506 C  CD    . GLN A 1 325 ? 103.079 18.113  43.503  1.00 143.99 ? 352 GLN A CD    1 
ATOM   2507 O  OE1   . GLN A 1 325 ? 102.551 18.563  44.520  1.00 129.11 ? 352 GLN A OE1   1 
ATOM   2508 N  NE2   . GLN A 1 325 ? 104.384 17.883  43.416  1.00 146.05 ? 352 GLN A NE2   1 
ATOM   2509 N  N     . ASP A 1 326 ? 98.065  19.389  41.252  1.00 96.41  ? 353 ASP A N     1 
ATOM   2510 C  CA    . ASP A 1 326 ? 96.710  19.861  41.528  1.00 95.17  ? 353 ASP A CA    1 
ATOM   2511 C  C     . ASP A 1 326 ? 95.669  18.999  40.825  1.00 86.43  ? 353 ASP A C     1 
ATOM   2512 O  O     . ASP A 1 326 ? 94.636  18.656  41.412  1.00 82.48  ? 353 ASP A O     1 
ATOM   2513 C  CB    . ASP A 1 326 ? 96.572  21.324  41.106  1.00 84.45  ? 353 ASP A CB    1 
ATOM   2514 C  CG    . ASP A 1 326 ? 97.077  21.572  39.697  1.00 115.68 ? 353 ASP A CG    1 
ATOM   2515 O  OD1   . ASP A 1 326 ? 97.653  20.641  39.093  1.00 107.43 ? 353 ASP A OD1   1 
ATOM   2516 O  OD2   . ASP A 1 326 ? 96.896  22.700  39.191  1.00 118.99 ? 353 ASP A OD2   1 
ATOM   2517 N  N     . ARG A 1 327 ? 95.928  18.637  39.568  1.00 89.24  ? 354 ARG A N     1 
ATOM   2518 C  CA    . ARG A 1 327 ? 94.998  17.788  38.830  1.00 85.57  ? 354 ARG A CA    1 
ATOM   2519 C  C     . ARG A 1 327 ? 94.890  16.408  39.466  1.00 89.17  ? 354 ARG A C     1 
ATOM   2520 O  O     . ARG A 1 327 ? 93.788  15.874  39.630  1.00 81.00  ? 354 ARG A O     1 
ATOM   2521 C  CB    . ARG A 1 327 ? 95.442  17.667  37.373  1.00 84.95  ? 354 ARG A CB    1 
ATOM   2522 C  CG    . ARG A 1 327 ? 95.272  18.924  36.548  1.00 70.92  ? 354 ARG A CG    1 
ATOM   2523 C  CD    . ARG A 1 327 ? 95.561  18.621  35.090  1.00 82.29  ? 354 ARG A CD    1 
ATOM   2524 N  NE    . ARG A 1 327 ? 95.224  19.728  34.206  1.00 84.38  ? 354 ARG A NE    1 
ATOM   2525 C  CZ    . ARG A 1 327 ? 95.237  19.654  32.883  1.00 90.75  ? 354 ARG A CZ    1 
ATOM   2526 N  NH1   . ARG A 1 327 ? 95.567  18.536  32.256  1.00 86.69  ? 354 ARG A NH1   1 
ATOM   2527 N  NH2   . ARG A 1 327 ? 94.906  20.727  32.169  1.00 101.93 ? 354 ARG A NH2   1 
ATOM   2528 N  N     . ARG A 1 328 ? 96.032  15.815  39.826  1.00 85.39  ? 355 ARG A N     1 
ATOM   2529 C  CA    . ARG A 1 328 ? 96.032  14.476  40.408  1.00 84.06  ? 355 ARG A CA    1 
ATOM   2530 C  C     . ARG A 1 328 ? 95.192  14.428  41.677  1.00 81.37  ? 355 ARG A C     1 
ATOM   2531 O  O     . ARG A 1 328 ? 94.337  13.550  41.837  1.00 75.72  ? 355 ARG A O     1 
ATOM   2532 C  CB    . ARG A 1 328 ? 97.464  14.030  40.700  1.00 86.47  ? 355 ARG A CB    1 
ATOM   2533 C  CG    . ARG A 1 328 ? 97.557  12.679  41.388  1.00 91.23  ? 355 ARG A CG    1 
ATOM   2534 C  CD    . ARG A 1 328 ? 98.960  12.406  41.908  1.00 93.36  ? 355 ARG A CD    1 
ATOM   2535 N  NE    . ARG A 1 328 ? 99.975  12.564  40.874  1.00 114.96 ? 355 ARG A NE    1 
ATOM   2536 C  CZ    . ARG A 1 328 ? 100.863 13.549  40.837  1.00 107.02 ? 355 ARG A CZ    1 
ATOM   2537 N  NH1   . ARG A 1 328 ? 100.906 14.477  41.779  1.00 97.63  ? 355 ARG A NH1   1 
ATOM   2538 N  NH2   . ARG A 1 328 ? 101.732 13.601  39.833  1.00 109.79 ? 355 ARG A NH2   1 
ATOM   2539 N  N     . GLU A 1 329 ? 95.419  15.375  42.589  1.00 85.02  ? 356 GLU A N     1 
ATOM   2540 C  CA    . GLU A 1 329 ? 94.678  15.387  43.846  1.00 79.80  ? 356 GLU A CA    1 
ATOM   2541 C  C     . GLU A 1 329 ? 93.187  15.587  43.607  1.00 80.53  ? 356 GLU A C     1 
ATOM   2542 O  O     . GLU A 1 329 ? 92.356  14.922  44.237  1.00 77.15  ? 356 GLU A O     1 
ATOM   2543 C  CB    . GLU A 1 329 ? 95.225  16.479  44.764  1.00 91.96  ? 356 GLU A CB    1 
ATOM   2544 C  CG    . GLU A 1 329 ? 96.719  16.384  45.018  1.00 106.40 ? 356 GLU A CG    1 
ATOM   2545 C  CD    . GLU A 1 329 ? 97.270  17.625  45.690  1.00 123.84 ? 356 GLU A CD    1 
ATOM   2546 O  OE1   . GLU A 1 329 ? 96.466  18.404  46.246  1.00 109.21 ? 356 GLU A OE1   1 
ATOM   2547 O  OE2   . GLU A 1 329 ? 98.504  17.824  45.656  1.00 125.00 ? 356 GLU A OE2   1 
ATOM   2548 N  N     . ARG A 1 330 ? 92.828  16.500  42.699  1.00 70.39  ? 357 ARG A N     1 
ATOM   2549 C  CA    . ARG A 1 330 ? 91.418  16.720  42.397  1.00 63.96  ? 357 ARG A CA    1 
ATOM   2550 C  C     . ARG A 1 330 ? 90.775  15.462  41.828  1.00 74.23  ? 357 ARG A C     1 
ATOM   2551 O  O     . ARG A 1 330 ? 89.656  15.099  42.210  1.00 78.67  ? 357 ARG A O     1 
ATOM   2552 C  CB    . ARG A 1 330 ? 91.263  17.885  41.422  1.00 64.92  ? 357 ARG A CB    1 
ATOM   2553 C  CG    . ARG A 1 330 ? 89.840  18.405  41.312  1.00 63.88  ? 357 ARG A CG    1 
ATOM   2554 C  CD    . ARG A 1 330 ? 89.616  19.153  40.011  1.00 53.15  ? 357 ARG A CD    1 
ATOM   2555 N  NE    . ARG A 1 330 ? 89.254  18.251  38.925  1.00 69.23  ? 357 ARG A NE    1 
ATOM   2556 C  CZ    . ARG A 1 330 ? 88.018  17.836  38.681  1.00 68.40  ? 357 ARG A CZ    1 
ATOM   2557 N  NH1   . ARG A 1 330 ? 87.000  18.220  39.432  1.00 66.94  ? 357 ARG A NH1   1 
ATOM   2558 N  NH2   . ARG A 1 330 ? 87.800  17.012  37.660  1.00 81.29  ? 357 ARG A NH2   1 
ATOM   2559 N  N     . MET A 1 331 ? 91.472  14.780  40.917  1.00 74.05  ? 358 MET A N     1 
ATOM   2560 C  CA    . MET A 1 331 ? 90.938  13.548  40.347  1.00 70.24  ? 358 MET A CA    1 
ATOM   2561 C  C     . MET A 1 331 ? 90.849  12.445  41.394  1.00 71.14  ? 358 MET A C     1 
ATOM   2562 O  O     . MET A 1 331 ? 89.835  11.742  41.475  1.00 79.84  ? 358 MET A O     1 
ATOM   2563 C  CB    . MET A 1 331 ? 91.802  13.101  39.168  1.00 72.55  ? 358 MET A CB    1 
ATOM   2564 C  CG    . MET A 1 331 ? 91.715  14.015  37.955  1.00 89.42  ? 358 MET A CG    1 
ATOM   2565 S  SD    . MET A 1 331 ? 90.062  14.039  37.243  1.00 79.45  ? 358 MET A SD    1 
ATOM   2566 C  CE    . MET A 1 331 ? 89.792  12.287  36.989  1.00 71.30  ? 358 MET A CE    1 
ATOM   2567 N  N     . LEU A 1 332 ? 91.897  12.279  42.205  1.00 68.94  ? 359 LEU A N     1 
ATOM   2568 C  CA    . LEU A 1 332 ? 91.876  11.244  43.235  1.00 69.83  ? 359 LEU A CA    1 
ATOM   2569 C  C     . LEU A 1 332 ? 90.768  11.498  44.249  1.00 70.73  ? 359 LEU A C     1 
ATOM   2570 O  O     . LEU A 1 332 ? 90.145  10.552  44.748  1.00 72.18  ? 359 LEU A O     1 
ATOM   2571 C  CB    . LEU A 1 332 ? 93.234  11.163  43.932  1.00 67.79  ? 359 LEU A CB    1 
ATOM   2572 C  CG    . LEU A 1 332 ? 94.412  10.667  43.091  1.00 67.95  ? 359 LEU A CG    1 
ATOM   2573 C  CD1   . LEU A 1 332 ? 95.686  10.613  43.922  1.00 67.17  ? 359 LEU A CD1   1 
ATOM   2574 C  CD2   . LEU A 1 332 ? 94.110  9.310   42.472  1.00 65.97  ? 359 LEU A CD2   1 
ATOM   2575 N  N     . ARG A 1 333 ? 90.511  12.768  44.571  1.00 61.45  ? 360 ARG A N     1 
ATOM   2576 C  CA    . ARG A 1 333 ? 89.392  13.094  45.450  1.00 61.81  ? 360 ARG A CA    1 
ATOM   2577 C  C     . ARG A 1 333 ? 88.062  12.771  44.782  1.00 63.40  ? 360 ARG A C     1 
ATOM   2578 O  O     . ARG A 1 333 ? 87.166  12.190  45.405  1.00 71.18  ? 360 ARG A O     1 
ATOM   2579 C  CB    . ARG A 1 333 ? 89.446  14.568  45.848  1.00 72.29  ? 360 ARG A CB    1 
ATOM   2580 C  CG    . ARG A 1 333 ? 90.546  14.916  46.829  1.00 78.75  ? 360 ARG A CG    1 
ATOM   2581 C  CD    . ARG A 1 333 ? 90.580  16.412  47.090  1.00 89.07  ? 360 ARG A CD    1 
ATOM   2582 N  NE    . ARG A 1 333 ? 91.457  16.750  48.203  1.00 113.23 ? 360 ARG A NE    1 
ATOM   2583 C  CZ    . ARG A 1 333 ? 91.093  16.705  49.478  1.00 123.52 ? 360 ARG A CZ    1 
ATOM   2584 N  NH1   . ARG A 1 333 ? 89.876  16.329  49.838  1.00 112.26 ? 360 ARG A NH1   1 
ATOM   2585 N  NH2   . ARG A 1 333 ? 91.973  17.044  50.416  1.00 121.93 ? 360 ARG A NH2   1 
ATOM   2586 N  N     . ALA A 1 334 ? 87.919  13.144  43.508  1.00 67.17  ? 361 ALA A N     1 
ATOM   2587 C  CA    . ALA A 1 334 ? 86.670  12.895  42.796  1.00 73.26  ? 361 ALA A CA    1 
ATOM   2588 C  C     . ALA A 1 334 ? 86.402  11.402  42.652  1.00 68.79  ? 361 ALA A C     1 
ATOM   2589 O  O     . ALA A 1 334 ? 85.257  10.953  42.778  1.00 66.48  ? 361 ALA A O     1 
ATOM   2590 C  CB    . ALA A 1 334 ? 86.708  13.568  41.425  1.00 65.41  ? 361 ALA A CB    1 
ATOM   2591 N  N     . LEU A 1 335 ? 87.447  10.617  42.390  1.00 64.21  ? 362 LEU A N     1 
ATOM   2592 C  CA    . LEU A 1 335 ? 87.269  9.177   42.254  1.00 69.13  ? 362 LEU A CA    1 
ATOM   2593 C  C     . LEU A 1 335 ? 86.929  8.533   43.592  1.00 63.90  ? 362 LEU A C     1 
ATOM   2594 O  O     . LEU A 1 335 ? 86.087  7.630   43.656  1.00 60.32  ? 362 LEU A O     1 
ATOM   2595 C  CB    . LEU A 1 335 ? 88.528  8.553   41.652  1.00 56.91  ? 362 LEU A CB    1 
ATOM   2596 C  CG    . LEU A 1 335 ? 88.809  8.966   40.206  1.00 68.10  ? 362 LEU A CG    1 
ATOM   2597 C  CD1   . LEU A 1 335 ? 90.124  8.387   39.714  1.00 67.76  ? 362 LEU A CD1   1 
ATOM   2598 C  CD2   . LEU A 1 335 ? 87.663  8.538   39.306  1.00 65.86  ? 362 LEU A CD2   1 
ATOM   2599 N  N     . GLN A 1 336 ? 87.567  8.988   44.674  1.00 62.87  ? 363 GLN A N     1 
ATOM   2600 C  CA    . GLN A 1 336 ? 87.262  8.445   45.995  1.00 58.04  ? 363 GLN A CA    1 
ATOM   2601 C  C     . GLN A 1 336 ? 85.839  8.786   46.419  1.00 64.20  ? 363 GLN A C     1 
ATOM   2602 O  O     . GLN A 1 336 ? 85.152  7.961   47.034  1.00 69.47  ? 363 GLN A O     1 
ATOM   2603 C  CB    . GLN A 1 336 ? 88.274  8.960   47.021  1.00 62.00  ? 363 GLN A CB    1 
ATOM   2604 C  CG    . GLN A 1 336 ? 87.867  8.751   48.479  1.00 86.99  ? 363 GLN A CG    1 
ATOM   2605 C  CD    . GLN A 1 336 ? 87.822  7.285   48.889  1.00 103.64 ? 363 GLN A CD    1 
ATOM   2606 O  OE1   . GLN A 1 336 ? 88.238  6.401   48.140  1.00 105.94 ? 363 GLN A OE1   1 
ATOM   2607 N  NE2   . GLN A 1 336 ? 87.318  7.025   50.092  1.00 97.14  ? 363 GLN A NE2   1 
ATOM   2608 N  N     . ALA A 1 337 ? 85.377  9.997   46.097  1.00 66.62  ? 364 ALA A N     1 
ATOM   2609 C  CA    . ALA A 1 337 ? 84.002  10.370  46.409  1.00 54.29  ? 364 ALA A CA    1 
ATOM   2610 C  C     . ALA A 1 337 ? 82.999  9.479   45.687  1.00 63.81  ? 364 ALA A C     1 
ATOM   2611 O  O     . ALA A 1 337 ? 81.929  9.184   46.230  1.00 56.40  ? 364 ALA A O     1 
ATOM   2612 C  CB    . ALA A 1 337 ? 83.765  11.835  46.047  1.00 53.15  ? 364 ALA A CB    1 
ATOM   2613 N  N     . GLN A 1 338 ? 83.326  9.030   44.477  1.00 63.49  ? 365 GLN A N     1 
ATOM   2614 C  CA    . GLN A 1 338 ? 82.458  8.151   43.708  1.00 60.04  ? 365 GLN A CA    1 
ATOM   2615 C  C     . GLN A 1 338 ? 82.765  6.677   43.934  1.00 69.49  ? 365 GLN A C     1 
ATOM   2616 O  O     . GLN A 1 338 ? 82.217  5.831   43.220  1.00 68.54  ? 365 GLN A O     1 
ATOM   2617 C  CB    . GLN A 1 338 ? 82.562  8.484   42.217  1.00 55.35  ? 365 GLN A CB    1 
ATOM   2618 C  CG    . GLN A 1 338 ? 82.142  9.902   41.871  1.00 55.93  ? 365 GLN A CG    1 
ATOM   2619 C  CD    . GLN A 1 338 ? 82.394  10.245  40.419  1.00 55.34  ? 365 GLN A CD    1 
ATOM   2620 O  OE1   . GLN A 1 338 ? 81.504  10.128  39.578  1.00 60.92  ? 365 GLN A OE1   1 
ATOM   2621 N  NE2   . GLN A 1 338 ? 83.611  10.680  40.117  1.00 58.59  ? 365 GLN A NE2   1 
ATOM   2622 N  N     . GLU A 1 339 ? 83.615  6.358   44.915  1.00 69.77  ? 366 GLU A N     1 
ATOM   2623 C  CA    . GLU A 1 339 ? 83.998  4.980   45.234  1.00 71.48  ? 366 GLU A CA    1 
ATOM   2624 C  C     . GLU A 1 339 ? 84.551  4.259   44.005  1.00 59.08  ? 366 GLU A C     1 
ATOM   2625 O  O     . GLU A 1 339 ? 84.128  3.155   43.656  1.00 67.91  ? 366 GLU A O     1 
ATOM   2626 C  CB    . GLU A 1 339 ? 82.829  4.206   45.849  1.00 77.52  ? 366 GLU A CB    1 
ATOM   2627 C  CG    . GLU A 1 339 ? 82.413  4.704   47.223  1.00 79.16  ? 366 GLU A CG    1 
ATOM   2628 C  CD    . GLU A 1 339 ? 81.541  3.708   47.963  1.00 100.00 ? 366 GLU A CD    1 
ATOM   2629 O  OE1   . GLU A 1 339 ? 81.051  2.756   47.319  1.00 110.10 ? 366 GLU A OE1   1 
ATOM   2630 O  OE2   . GLU A 1 339 ? 81.353  3.872   49.187  1.00 97.61  ? 366 GLU A OE2   1 
ATOM   2631 N  N     . ILE A 1 340 ? 85.508  4.902   43.343  1.00 64.57  ? 367 ILE A N     1 
ATOM   2632 C  CA    . ILE A 1 340 ? 86.141  4.374   42.141  1.00 69.94  ? 367 ILE A CA    1 
ATOM   2633 C  C     . ILE A 1 340 ? 87.644  4.352   42.365  1.00 78.64  ? 367 ILE A C     1 
ATOM   2634 O  O     . ILE A 1 340 ? 88.230  5.361   42.775  1.00 76.17  ? 367 ILE A O     1 
ATOM   2635 C  CB    . ILE A 1 340 ? 85.792  5.210   40.895  1.00 63.18  ? 367 ILE A CB    1 
ATOM   2636 C  CG1   . ILE A 1 340 ? 84.279  5.248   40.684  1.00 67.96  ? 367 ILE A CG1   1 
ATOM   2637 C  CG2   . ILE A 1 340 ? 86.486  4.648   39.667  1.00 72.90  ? 367 ILE A CG2   1 
ATOM   2638 C  CD1   . ILE A 1 340 ? 83.843  6.179   39.577  1.00 60.79  ? 367 ILE A CD1   1 
ATOM   2639 N  N     . GLU A 1 341 ? 88.262  3.207   42.100  1.00 84.78  ? 368 GLU A N     1 
ATOM   2640 C  CA    . GLU A 1 341 ? 89.699  3.026   42.242  1.00 77.98  ? 368 GLU A CA    1 
ATOM   2641 C  C     . GLU A 1 341 ? 90.353  3.044   40.867  1.00 76.26  ? 368 GLU A C     1 
ATOM   2642 O  O     . GLU A 1 341 ? 89.813  2.491   39.905  1.00 76.61  ? 368 GLU A O     1 
ATOM   2643 C  CB    . GLU A 1 341 ? 90.009  1.711   42.960  1.00 80.31  ? 368 GLU A CB    1 
ATOM   2644 C  CG    . GLU A 1 341 ? 91.475  1.495   43.287  1.00 96.04  ? 368 GLU A CG    1 
ATOM   2645 C  CD    . GLU A 1 341 ? 91.702  0.247   44.117  1.00 109.71 ? 368 GLU A CD    1 
ATOM   2646 O  OE1   . GLU A 1 341 ? 90.710  -0.447  44.428  1.00 109.85 ? 368 GLU A OE1   1 
ATOM   2647 O  OE2   . GLU A 1 341 ? 92.869  -0.040  44.460  1.00 119.29 ? 368 GLU A OE2   1 
ATOM   2648 N  N     . CYS A 1 342 ? 91.516  3.684   40.777  1.00 81.89  ? 369 CYS A N     1 
ATOM   2649 C  CA    . CYS A 1 342 ? 92.210  3.840   39.510  1.00 80.98  ? 369 CYS A CA    1 
ATOM   2650 C  C     . CYS A 1 342 ? 93.664  3.418   39.656  1.00 82.04  ? 369 CYS A C     1 
ATOM   2651 O  O     . CYS A 1 342 ? 94.195  3.301   40.764  1.00 79.47  ? 369 CYS A O     1 
ATOM   2652 C  CB    . CYS A 1 342 ? 92.146  5.288   39.007  1.00 67.41  ? 369 CYS A CB    1 
ATOM   2653 S  SG    . CYS A 1 342 ? 93.391  6.374   39.733  1.00 87.98  ? 369 CYS A SG    1 
ATOM   2654 N  N     . ARG A 1 343 ? 94.301  3.188   38.511  1.00 86.47  ? 370 ARG A N     1 
ATOM   2655 C  CA    . ARG A 1 343 ? 95.736  2.940   38.427  1.00 78.33  ? 370 ARG A CA    1 
ATOM   2656 C  C     . ARG A 1 343 ? 96.383  4.190   37.843  1.00 78.61  ? 370 ARG A C     1 
ATOM   2657 O  O     . ARG A 1 343 ? 96.211  4.490   36.657  1.00 80.54  ? 370 ARG A O     1 
ATOM   2658 C  CB    . ARG A 1 343 ? 96.045  1.710   37.576  1.00 84.18  ? 370 ARG A CB    1 
ATOM   2659 C  CG    . ARG A 1 343 ? 97.533  1.443   37.433  1.00 99.02  ? 370 ARG A CG    1 
ATOM   2660 C  CD    . ARG A 1 343 ? 97.822  0.042   36.919  1.00 101.52 ? 370 ARG A CD    1 
ATOM   2661 N  NE    . ARG A 1 343 ? 99.254  -0.219  36.854  1.00 107.46 ? 370 ARG A NE    1 
ATOM   2662 C  CZ    . ARG A 1 343 ? 99.793  -1.399  36.579  1.00 123.37 ? 370 ARG A CZ    1 
ATOM   2663 N  NH1   . ARG A 1 343 ? 99.043  -2.457  36.314  1.00 118.33 ? 370 ARG A NH1   1 
ATOM   2664 N  NH2   . ARG A 1 343 ? 101.117 -1.522  36.572  1.00 133.60 ? 370 ARG A NH2   1 
ATOM   2665 N  N     . LEU A 1 344 ? 97.118  4.915   38.677  1.00 79.43  ? 371 LEU A N     1 
ATOM   2666 C  CA    . LEU A 1 344 ? 97.725  6.182   38.280  1.00 85.72  ? 371 LEU A CA    1 
ATOM   2667 C  C     . LEU A 1 344 ? 98.921  5.907   37.380  1.00 85.74  ? 371 LEU A C     1 
ATOM   2668 O  O     . LEU A 1 344 ? 99.985  5.494   37.844  1.00 89.94  ? 371 LEU A O     1 
ATOM   2669 C  CB    . LEU A 1 344 ? 98.135  6.977   39.513  1.00 91.50  ? 371 LEU A CB    1 
ATOM   2670 C  CG    . LEU A 1 344 ? 98.771  8.341   39.244  1.00 102.44 ? 371 LEU A CG    1 
ATOM   2671 C  CD1   . LEU A 1 344 ? 97.803  9.246   38.495  1.00 103.69 ? 371 LEU A CD1   1 
ATOM   2672 C  CD2   . LEU A 1 344 ? 99.224  8.987   40.544  1.00 110.13 ? 371 LEU A CD2   1 
ATOM   2673 N  N     . VAL A 1 345 ? 98.749  6.135   36.083  1.00 92.00  ? 372 VAL A N     1 
ATOM   2674 C  CA    . VAL A 1 345 ? 99.825  5.987   35.110  1.00 95.90  ? 372 VAL A CA    1 
ATOM   2675 C  C     . VAL A 1 345 ? 100.570 7.309   35.004  1.00 106.63 ? 372 VAL A C     1 
ATOM   2676 O  O     . VAL A 1 345 ? 99.961  8.354   34.745  1.00 103.23 ? 372 VAL A O     1 
ATOM   2677 C  CB    . VAL A 1 345 ? 99.273  5.554   33.742  1.00 79.21  ? 372 VAL A CB    1 
ATOM   2678 C  CG1   . VAL A 1 345 ? 100.394 5.475   32.720  1.00 80.47  ? 372 VAL A CG1   1 
ATOM   2679 C  CG2   . VAL A 1 345 ? 98.554  4.222   33.859  1.00 84.13  ? 372 VAL A CG2   1 
ATOM   2680 N  N     . GLU A 1 346 ? 101.884 7.269   35.216  1.00 122.03 ? 373 GLU A N     1 
ATOM   2681 C  CA    . GLU A 1 346 ? 102.703 8.464   35.064  1.00 117.40 ? 373 GLU A CA    1 
ATOM   2682 C  C     . GLU A 1 346 ? 102.839 8.803   33.585  1.00 105.06 ? 373 GLU A C     1 
ATOM   2683 O  O     . GLU A 1 346 ? 103.392 8.017   32.807  1.00 100.77 ? 373 GLU A O     1 
ATOM   2684 C  CB    . GLU A 1 346 ? 104.077 8.261   35.698  1.00 124.62 ? 373 GLU A CB    1 
ATOM   2685 C  CG    . GLU A 1 346 ? 104.939 9.516   35.679  1.00 132.78 ? 373 GLU A CG    1 
ATOM   2686 C  CD    . GLU A 1 346 ? 106.310 9.298   36.285  1.00 136.88 ? 373 GLU A CD    1 
ATOM   2687 O  OE1   . GLU A 1 346 ? 106.586 8.171   36.747  1.00 138.73 ? 373 GLU A OE1   1 
ATOM   2688 O  OE2   . GLU A 1 346 ? 107.114 10.254  36.298  1.00 132.42 ? 373 GLU A OE2   1 
ATOM   2689 N  N     . ALA A 1 347 ? 102.340 9.974   33.201  1.00 101.87 ? 374 ALA A N     1 
ATOM   2690 C  CA    . ALA A 1 347 ? 102.305 10.359  31.800  1.00 101.94 ? 374 ALA A CA    1 
ATOM   2691 C  C     . ALA A 1 347 ? 103.714 10.573  31.257  1.00 106.00 ? 374 ALA A C     1 
ATOM   2692 O  O     . ALA A 1 347 ? 104.670 10.817  31.998  1.00 118.45 ? 374 ALA A O     1 
ATOM   2693 C  CB    . ALA A 1 347 ? 101.477 11.629  31.616  1.00 102.91 ? 374 ALA A CB    1 
ATOM   2694 N  N     . VAL A 1 348 ? 103.831 10.474  29.936  1.00 99.07  ? 375 VAL A N     1 
ATOM   2695 C  CA    . VAL A 1 348 ? 105.087 10.731  29.241  1.00 107.08 ? 375 VAL A CA    1 
ATOM   2696 C  C     . VAL A 1 348 ? 105.136 12.219  28.915  1.00 112.00 ? 375 VAL A C     1 
ATOM   2697 O  O     . VAL A 1 348 ? 104.331 12.717  28.125  1.00 117.04 ? 375 VAL A O     1 
ATOM   2698 C  CB    . VAL A 1 348 ? 105.214 9.879   27.972  1.00 108.56 ? 375 VAL A CB    1 
ATOM   2699 C  CG1   . VAL A 1 348 ? 106.553 10.129  27.299  1.00 96.27  ? 375 VAL A CG1   1 
ATOM   2700 C  CG2   . VAL A 1 348 ? 105.040 8.403   28.301  1.00 100.89 ? 375 VAL A CG2   1 
ATOM   2701 N  N     . ASP A 1 349 ? 106.077 12.933  29.529  1.00 108.69 ? 376 ASP A N     1 
ATOM   2702 C  CA    . ASP A 1 349 ? 106.237 14.362  29.282  1.00 117.52 ? 376 ASP A CA    1 
ATOM   2703 C  C     . ASP A 1 349 ? 106.913 14.551  27.929  1.00 125.95 ? 376 ASP A C     1 
ATOM   2704 O  O     . ASP A 1 349 ? 108.109 14.282  27.782  1.00 126.77 ? 376 ASP A O     1 
ATOM   2705 C  CB    . ASP A 1 349 ? 107.045 15.016  30.398  1.00 116.23 ? 376 ASP A CB    1 
ATOM   2706 C  CG    . ASP A 1 349 ? 107.058 16.530  30.300  1.00 133.92 ? 376 ASP A CG    1 
ATOM   2707 O  OD1   . ASP A 1 349 ? 106.261 17.085  29.513  1.00 135.24 ? 376 ASP A OD1   1 
ATOM   2708 O  OD2   . ASP A 1 349 ? 107.864 17.167  31.009  1.00 145.04 ? 376 ASP A OD2   1 
ATOM   2709 N  N     . GLY A 1 350 ? 106.147 15.015  26.940  1.00 127.73 ? 377 GLY A N     1 
ATOM   2710 C  CA    . GLY A 1 350 ? 106.698 15.190  25.608  1.00 130.66 ? 377 GLY A CA    1 
ATOM   2711 C  C     . GLY A 1 350 ? 107.732 16.294  25.522  1.00 139.28 ? 377 GLY A C     1 
ATOM   2712 O  O     . GLY A 1 350 ? 108.641 16.232  24.688  1.00 144.40 ? 377 GLY A O     1 
ATOM   2713 N  N     . LYS A 1 351 ? 107.611 17.319  26.370  1.00 129.99 ? 378 LYS A N     1 
ATOM   2714 C  CA    . LYS A 1 351 ? 108.602 18.389  26.377  1.00 136.72 ? 378 LYS A CA    1 
ATOM   2715 C  C     . LYS A 1 351 ? 109.938 17.910  26.933  1.00 140.89 ? 378 LYS A C     1 
ATOM   2716 O  O     . LYS A 1 351 ? 110.994 18.399  26.514  1.00 133.67 ? 378 LYS A O     1 
ATOM   2717 C  CB    . LYS A 1 351 ? 108.083 19.581  27.183  1.00 135.48 ? 378 LYS A CB    1 
ATOM   2718 C  CG    . LYS A 1 351 ? 109.005 20.791  27.177  1.00 144.68 ? 378 LYS A CG    1 
ATOM   2719 C  CD    . LYS A 1 351 ? 108.419 21.942  27.978  1.00 137.36 ? 378 LYS A CD    1 
ATOM   2720 C  CE    . LYS A 1 351 ? 109.358 23.138  27.990  1.00 135.20 ? 378 LYS A CE    1 
ATOM   2721 N  NZ    . LYS A 1 351 ? 108.798 24.278  28.766  1.00 129.95 ? 378 LYS A NZ    1 
ATOM   2722 N  N     . ALA A 1 352 ? 109.913 16.951  27.862  1.00 139.89 ? 379 ALA A N     1 
ATOM   2723 C  CA    . ALA A 1 352 ? 111.151 16.469  28.465  1.00 132.21 ? 379 ALA A CA    1 
ATOM   2724 C  C     . ALA A 1 352 ? 111.981 15.655  27.482  1.00 123.69 ? 379 ALA A C     1 
ATOM   2725 O  O     . ALA A 1 352 ? 113.205 15.573  27.629  1.00 128.42 ? 379 ALA A O     1 
ATOM   2726 C  CB    . ALA A 1 352 ? 110.841 15.637  29.709  1.00 120.84 ? 379 ALA A CB    1 
ATOM   2727 N  N     . MET A 1 353 ? 111.344 15.052  26.484  1.00 136.59 ? 380 MET A N     1 
ATOM   2728 C  CA    . MET A 1 353 ? 112.065 14.222  25.530  1.00 144.62 ? 380 MET A CA    1 
ATOM   2729 C  C     . MET A 1 353 ? 112.932 15.078  24.617  1.00 137.42 ? 380 MET A C     1 
ATOM   2730 O  O     . MET A 1 353 ? 112.493 16.113  24.107  1.00 129.55 ? 380 MET A O     1 
ATOM   2731 C  CB    . MET A 1 353 ? 111.088 13.403  24.688  1.00 142.74 ? 380 MET A CB    1 
ATOM   2732 C  CG    . MET A 1 353 ? 110.186 12.478  25.480  1.00 134.31 ? 380 MET A CG    1 
ATOM   2733 S  SD    . MET A 1 353 ? 109.014 11.605  24.424  1.00 146.22 ? 380 MET A SD    1 
ATOM   2734 C  CE    . MET A 1 353 ? 110.123 10.781  23.283  1.00 138.07 ? 380 MET A CE    1 
ATOM   2735 N  N     . ASN A 1 354 ? 114.168 14.641  24.409  1.00 130.86 ? 381 ASN A N     1 
ATOM   2736 C  CA    . ASN A 1 354 ? 115.017 15.248  23.398  1.00 142.03 ? 381 ASN A CA    1 
ATOM   2737 C  C     . ASN A 1 354 ? 114.821 14.533  22.065  1.00 143.76 ? 381 ASN A C     1 
ATOM   2738 O  O     . ASN A 1 354 ? 114.233 13.451  21.994  1.00 146.56 ? 381 ASN A O     1 
ATOM   2739 C  CB    . ASN A 1 354 ? 116.492 15.214  23.812  1.00 136.37 ? 381 ASN A CB    1 
ATOM   2740 C  CG    . ASN A 1 354 ? 116.970 13.823  24.177  1.00 143.93 ? 381 ASN A CG    1 
ATOM   2741 O  OD1   . ASN A 1 354 ? 117.082 12.946  23.320  1.00 143.26 ? 381 ASN A OD1   1 
ATOM   2742 N  ND2   . ASN A 1 354 ? 117.277 13.620  25.452  1.00 144.51 ? 381 ASN A ND2   1 
ATOM   2743 N  N     . THR A 1 355 ? 115.318 15.167  20.998  1.00 133.28 ? 382 THR A N     1 
ATOM   2744 C  CA    . THR A 1 355 ? 115.112 14.640  19.651  1.00 144.20 ? 382 THR A CA    1 
ATOM   2745 C  C     . THR A 1 355 ? 115.676 13.231  19.510  1.00 148.53 ? 382 THR A C     1 
ATOM   2746 O  O     . THR A 1 355 ? 115.092 12.388  18.816  1.00 146.82 ? 382 THR A O     1 
ATOM   2747 C  CB    . THR A 1 355 ? 115.745 15.573  18.619  1.00 151.00 ? 382 THR A CB    1 
ATOM   2748 O  OG1   . THR A 1 355 ? 115.243 16.901  18.803  1.00 152.95 ? 382 THR A OG1   1 
ATOM   2749 C  CG2   . THR A 1 355 ? 115.406 15.110  17.209  1.00 145.00 ? 382 THR A CG2   1 
ATOM   2750 N  N     . SER A 1 356 ? 116.800 12.951  20.179  1.00 144.79 ? 383 SER A N     1 
ATOM   2751 C  CA    . SER A 1 356 ? 117.403 11.623  20.105  1.00 142.99 ? 383 SER A CA    1 
ATOM   2752 C  C     . SER A 1 356 ? 116.504 10.566  20.736  1.00 134.64 ? 383 SER A C     1 
ATOM   2753 O  O     . SER A 1 356 ? 116.373 9.460   20.200  1.00 131.62 ? 383 SER A O     1 
ATOM   2754 C  CB    . SER A 1 356 ? 118.778 11.628  20.775  1.00 145.34 ? 383 SER A CB    1 
ATOM   2755 O  OG    . SER A 1 356 ? 119.614 12.619  20.203  1.00 141.37 ? 383 SER A OG    1 
ATOM   2756 N  N     . GLN A 1 357 ? 115.873 10.887  21.870  1.00 137.53 ? 384 GLN A N     1 
ATOM   2757 C  CA    . GLN A 1 357 ? 114.950 9.941   22.493  1.00 135.02 ? 384 GLN A CA    1 
ATOM   2758 C  C     . GLN A 1 357 ? 113.725 9.694   21.621  1.00 130.56 ? 384 GLN A C     1 
ATOM   2759 O  O     . GLN A 1 357 ? 113.185 8.582   21.614  1.00 119.19 ? 384 GLN A O     1 
ATOM   2760 C  CB    . GLN A 1 357 ? 114.524 10.451  23.870  1.00 125.48 ? 384 GLN A CB    1 
ATOM   2761 C  CG    . GLN A 1 357 ? 115.649 10.471  24.895  1.00 119.89 ? 384 GLN A CG    1 
ATOM   2762 C  CD    . GLN A 1 357 ? 115.228 11.085  26.213  1.00 125.92 ? 384 GLN A CD    1 
ATOM   2763 O  OE1   . GLN A 1 357 ? 114.105 11.573  26.357  1.00 128.21 ? 384 GLN A OE1   1 
ATOM   2764 N  NE2   . GLN A 1 357 ? 116.129 11.065  27.184  1.00 116.10 ? 384 GLN A NE2   1 
ATOM   2765 N  N     . VAL A 1 358 ? 113.281 10.709  20.875  1.00 129.13 ? 385 VAL A N     1 
ATOM   2766 C  CA    . VAL A 1 358 ? 112.197 10.509  19.914  1.00 123.46 ? 385 VAL A CA    1 
ATOM   2767 C  C     . VAL A 1 358 ? 112.637 9.540   18.826  1.00 133.72 ? 385 VAL A C     1 
ATOM   2768 O  O     . VAL A 1 358 ? 111.905 8.613   18.457  1.00 131.34 ? 385 VAL A O     1 
ATOM   2769 C  CB    . VAL A 1 358 ? 111.746 11.855  19.318  1.00 133.70 ? 385 VAL A CB    1 
ATOM   2770 C  CG1   . VAL A 1 358 ? 110.616 11.647  18.317  1.00 131.77 ? 385 VAL A CG1   1 
ATOM   2771 C  CG2   . VAL A 1 358 ? 111.319 12.811  20.420  1.00 136.48 ? 385 VAL A CG2   1 
ATOM   2772 N  N     . GLU A 1 359 ? 113.852 9.738   18.302  1.00 144.91 ? 386 GLU A N     1 
ATOM   2773 C  CA    . GLU A 1 359 ? 114.390 8.829   17.295  1.00 136.93 ? 386 GLU A CA    1 
ATOM   2774 C  C     . GLU A 1 359 ? 114.651 7.442   17.867  1.00 131.42 ? 386 GLU A C     1 
ATOM   2775 O  O     . GLU A 1 359 ? 114.511 6.444   17.151  1.00 127.36 ? 386 GLU A O     1 
ATOM   2776 C  CB    . GLU A 1 359 ? 115.676 9.407   16.707  1.00 145.94 ? 386 GLU A CB    1 
ATOM   2777 C  CG    . GLU A 1 359 ? 115.500 10.771  16.057  1.00 147.39 ? 386 GLU A CG    1 
ATOM   2778 C  CD    . GLU A 1 359 ? 116.818 11.481  15.835  1.00 153.33 ? 386 GLU A CD    1 
ATOM   2779 O  OE1   . GLU A 1 359 ? 117.863 10.947  16.261  1.00 156.05 ? 386 GLU A OE1   1 
ATOM   2780 O  OE2   . GLU A 1 359 ? 116.805 12.577  15.237  1.00 158.31 ? 386 GLU A OE2   1 
ATOM   2781 N  N     . ALA A 1 360 ? 115.026 7.358   19.148  1.00 132.52 ? 387 ALA A N     1 
ATOM   2782 C  CA    . ALA A 1 360 ? 115.218 6.057   19.781  1.00 128.42 ? 387 ALA A CA    1 
ATOM   2783 C  C     . ALA A 1 360 ? 113.927 5.253   19.778  1.00 126.37 ? 387 ALA A C     1 
ATOM   2784 O  O     . ALA A 1 360 ? 113.950 4.027   19.619  1.00 125.00 ? 387 ALA A O     1 
ATOM   2785 C  CB    . ALA A 1 360 ? 115.733 6.236   21.210  1.00 128.43 ? 387 ALA A CB    1 
ATOM   2786 N  N     . LEU A 1 361 ? 112.792 5.926   19.950  1.00 117.82 ? 388 LEU A N     1 
ATOM   2787 C  CA    . LEU A 1 361 ? 111.486 5.291   19.879  1.00 118.63 ? 388 LEU A CA    1 
ATOM   2788 C  C     . LEU A 1 361 ? 110.959 5.185   18.453  1.00 121.91 ? 388 LEU A C     1 
ATOM   2789 O  O     . LEU A 1 361 ? 109.869 4.640   18.252  1.00 121.27 ? 388 LEU A O     1 
ATOM   2790 C  CB    . LEU A 1 361 ? 110.482 6.054   20.748  1.00 120.00 ? 388 LEU A CB    1 
ATOM   2791 C  CG    . LEU A 1 361 ? 110.897 6.269   22.207  1.00 121.65 ? 388 LEU A CG    1 
ATOM   2792 C  CD1   . LEU A 1 361 ? 109.817 7.016   22.972  1.00 105.20 ? 388 LEU A CD1   1 
ATOM   2793 C  CD2   . LEU A 1 361 ? 111.220 4.942   22.878  1.00 109.87 ? 388 LEU A CD2   1 
ATOM   2794 N  N     . GLY A 1 362 ? 111.701 5.687   17.467  1.00 127.06 ? 389 GLY A N     1 
ATOM   2795 C  CA    . GLY A 1 362 ? 111.304 5.589   16.075  1.00 121.45 ? 389 GLY A CA    1 
ATOM   2796 C  C     . GLY A 1 362 ? 109.973 6.244   15.774  1.00 127.83 ? 389 GLY A C     1 
ATOM   2797 O  O     . GLY A 1 362 ? 109.094 5.632   15.158  1.00 128.36 ? 389 GLY A O     1 
ATOM   2798 N  N     . ILE A 1 363 ? 109.812 7.491   16.202  1.00 126.53 ? 390 ILE A N     1 
ATOM   2799 C  CA    . ILE A 1 363 ? 108.560 8.223   16.054  1.00 127.24 ? 390 ILE A CA    1 
ATOM   2800 C  C     . ILE A 1 363 ? 108.703 9.190   14.889  1.00 127.78 ? 390 ILE A C     1 
ATOM   2801 O  O     . ILE A 1 363 ? 109.612 10.028  14.873  1.00 127.38 ? 390 ILE A O     1 
ATOM   2802 C  CB    . ILE A 1 363 ? 108.193 8.966   17.347  1.00 128.51 ? 390 ILE A CB    1 
ATOM   2803 C  CG1   . ILE A 1 363 ? 108.122 7.983   18.517  1.00 121.71 ? 390 ILE A CG1   1 
ATOM   2804 C  CG2   . ILE A 1 363 ? 106.873 9.700   17.178  1.00 125.52 ? 390 ILE A CG2   1 
ATOM   2805 C  CD1   . ILE A 1 363 ? 108.111 8.648   19.870  1.00 115.31 ? 390 ILE A CD1   1 
ATOM   2806 N  N     . GLN A 1 364 ? 107.807 9.074   13.913  1.00 130.57 ? 391 GLN A N     1 
ATOM   2807 C  CA    . GLN A 1 364 ? 107.790 9.959   12.757  1.00 131.53 ? 391 GLN A CA    1 
ATOM   2808 C  C     . GLN A 1 364 ? 106.385 10.504  12.571  1.00 127.46 ? 391 GLN A C     1 
ATOM   2809 O  O     . GLN A 1 364 ? 105.410 9.746   12.601  1.00 130.71 ? 391 GLN A O     1 
ATOM   2810 C  CB    . GLN A 1 364 ? 108.243 9.238   11.485  1.00 133.99 ? 391 GLN A CB    1 
ATOM   2811 C  CG    . GLN A 1 364 ? 108.243 10.126  10.248  1.00 130.17 ? 391 GLN A CG    1 
ATOM   2812 C  CD    . GLN A 1 364 ? 108.510 9.353   8.972   1.00 139.42 ? 391 GLN A CD    1 
ATOM   2813 O  OE1   . GLN A 1 364 ? 108.722 8.141   9.000   1.00 150.72 ? 391 GLN A OE1   1 
ATOM   2814 N  NE2   . GLN A 1 364 ? 108.499 10.052  7.843   1.00 132.81 ? 391 GLN A NE2   1 
ATOM   2815 N  N     . MET A 1 365 ? 106.291 11.814  12.378  1.00 126.84 ? 392 MET A N     1 
ATOM   2816 C  CA    . MET A 1 365 ? 105.011 12.462  12.149  1.00 122.50 ? 392 MET A CA    1 
ATOM   2817 C  C     . MET A 1 365 ? 104.422 12.008  10.820  1.00 124.89 ? 392 MET A C     1 
ATOM   2818 O  O     . MET A 1 365 ? 105.146 11.740  9.858   1.00 137.38 ? 392 MET A O     1 
ATOM   2819 C  CB    . MET A 1 365 ? 105.193 13.976  12.166  1.00 120.54 ? 392 MET A CB    1 
ATOM   2820 C  CG    . MET A 1 365 ? 103.949 14.797  11.936  1.00 121.51 ? 392 MET A CG    1 
ATOM   2821 S  SD    . MET A 1 365 ? 104.327 16.555  12.041  1.00 143.67 ? 392 MET A SD    1 
ATOM   2822 C  CE    . MET A 1 365 ? 102.778 17.254  11.505  1.00 120.17 ? 392 MET A CE    1 
ATOM   2823 N  N     . LEU A 1 366 ? 103.095 11.903  10.782  1.00 122.02 ? 393 LEU A N     1 
ATOM   2824 C  CA    . LEU A 1 366 ? 102.407 11.583  9.539   1.00 123.82 ? 393 LEU A CA    1 
ATOM   2825 C  C     . LEU A 1 366 ? 102.716 12.660  8.504   1.00 128.08 ? 393 LEU A C     1 
ATOM   2826 O  O     . LEU A 1 366 ? 102.513 13.851  8.778   1.00 121.42 ? 393 LEU A O     1 
ATOM   2827 C  CB    . LEU A 1 366 ? 100.899 11.474  9.765   1.00 120.10 ? 393 LEU A CB    1 
ATOM   2828 C  CG    . LEU A 1 366 ? 100.050 11.041  8.562   1.00 123.88 ? 393 LEU A CG    1 
ATOM   2829 C  CD1   . LEU A 1 366 ? 98.901  10.152  9.002   1.00 121.51 ? 393 LEU A CD1   1 
ATOM   2830 C  CD2   . LEU A 1 366 ? 99.518  12.241  7.792   1.00 127.89 ? 393 LEU A CD2   1 
ATOM   2831 N  N     . PRO A 1 367 ? 103.217 12.294  7.325   1.00 127.91 ? 394 PRO A N     1 
ATOM   2832 C  CA    . PRO A 1 367 ? 103.655 13.309  6.356   1.00 129.65 ? 394 PRO A CA    1 
ATOM   2833 C  C     . PRO A 1 367 ? 102.527 14.210  5.880   1.00 128.00 ? 394 PRO A C     1 
ATOM   2834 O  O     . PRO A 1 367 ? 101.593 13.758  5.210   1.00 122.72 ? 394 PRO A O     1 
ATOM   2835 C  CB    . PRO A 1 367 ? 104.222 12.470  5.202   1.00 119.94 ? 394 PRO A CB    1 
ATOM   2836 C  CG    . PRO A 1 367 ? 104.513 11.127  5.807   1.00 117.29 ? 394 PRO A CG    1 
ATOM   2837 C  CD    . PRO A 1 367 ? 103.475 10.924  6.857   1.00 116.90 ? 394 PRO A CD    1 
ATOM   2838 N  N     . GLY A 1 368 ? 102.605 15.491  6.236   1.00 121.46 ? 395 GLY A N     1 
ATOM   2839 C  CA    . GLY A 1 368 ? 101.666 16.492  5.769   1.00 118.72 ? 395 GLY A CA    1 
ATOM   2840 C  C     . GLY A 1 368 ? 100.647 16.955  6.787   1.00 128.37 ? 395 GLY A C     1 
ATOM   2841 O  O     . GLY A 1 368 ? 99.833  17.827  6.459   1.00 129.67 ? 395 GLY A O     1 
ATOM   2842 N  N     . TYR A 1 369 ? 100.655 16.416  8.004   1.00 123.09 ? 396 TYR A N     1 
ATOM   2843 C  CA    . TYR A 1 369 ? 99.656  16.816  8.985   1.00 118.04 ? 396 TYR A CA    1 
ATOM   2844 C  C     . TYR A 1 369 ? 99.846  18.269  9.398   1.00 125.26 ? 396 TYR A C     1 
ATOM   2845 O  O     . TYR A 1 369 ? 100.970 18.764  9.501   1.00 126.49 ? 396 TYR A O     1 
ATOM   2846 C  CB    . TYR A 1 369 ? 99.708  15.925  10.225  1.00 120.58 ? 396 TYR A CB    1 
ATOM   2847 C  CG    . TYR A 1 369 ? 98.858  16.468  11.357  1.00 120.38 ? 396 TYR A CG    1 
ATOM   2848 C  CD1   . TYR A 1 369 ? 97.473  16.400  11.302  1.00 121.38 ? 396 TYR A CD1   1 
ATOM   2849 C  CD2   . TYR A 1 369 ? 99.439  17.076  12.465  1.00 117.00 ? 396 TYR A CD2   1 
ATOM   2850 C  CE1   . TYR A 1 369 ? 96.690  16.904  12.320  1.00 120.88 ? 396 TYR A CE1   1 
ATOM   2851 C  CE2   . TYR A 1 369 ? 98.663  17.585  13.489  1.00 119.62 ? 396 TYR A CE2   1 
ATOM   2852 C  CZ    . TYR A 1 369 ? 97.289  17.495  13.411  1.00 120.83 ? 396 TYR A CZ    1 
ATOM   2853 O  OH    . TYR A 1 369 ? 96.508  17.998  14.424  1.00 116.25 ? 396 TYR A OH    1 
ATOM   2854 N  N     . ARG A 1 370 ? 98.727  18.952  9.626   1.00 132.53 ? 397 ARG A N     1 
ATOM   2855 C  CA    . ARG A 1 370 ? 98.716  20.284  10.205  1.00 130.44 ? 397 ARG A CA    1 
ATOM   2856 C  C     . ARG A 1 370 ? 97.490  20.401  11.096  1.00 127.80 ? 397 ARG A C     1 
ATOM   2857 O  O     . ARG A 1 370 ? 96.470  19.749  10.856  1.00 124.80 ? 397 ARG A O     1 
ATOM   2858 C  CB    . ARG A 1 370 ? 98.715  21.379  9.127   1.00 128.19 ? 397 ARG A CB    1 
ATOM   2859 C  CG    . ARG A 1 370 ? 100.050 21.525  8.417   1.00 123.57 ? 397 ARG A CG    1 
ATOM   2860 C  CD    . ARG A 1 370 ? 99.959  22.379  7.170   1.00 141.11 ? 397 ARG A CD    1 
ATOM   2861 N  NE    . ARG A 1 370 ? 101.197 22.313  6.403   1.00 146.28 ? 397 ARG A NE    1 
ATOM   2862 C  CZ    . ARG A 1 370 ? 101.408 22.948  5.258   1.00 143.46 ? 397 ARG A CZ    1 
ATOM   2863 N  NH1   . ARG A 1 370 ? 100.483 23.723  4.717   1.00 147.17 ? 397 ARG A NH1   1 
ATOM   2864 N  NH2   . ARG A 1 370 ? 102.576 22.798  4.639   1.00 133.30 ? 397 ARG A NH2   1 
ATOM   2865 N  N     . ASP A 1 371 ? 97.608  21.215  12.138  1.00 133.76 ? 398 ASP A N     1 
ATOM   2866 C  CA    . ASP A 1 371 ? 96.506  21.387  13.074  1.00 131.44 ? 398 ASP A CA    1 
ATOM   2867 C  C     . ASP A 1 371 ? 95.273  21.899  12.335  1.00 134.44 ? 398 ASP A C     1 
ATOM   2868 O  O     . ASP A 1 371 ? 95.379  22.847  11.545  1.00 135.70 ? 398 ASP A O     1 
ATOM   2869 C  CB    . ASP A 1 371 ? 96.898  22.357  14.188  1.00 136.01 ? 398 ASP A CB    1 
ATOM   2870 C  CG    . ASP A 1 371 ? 95.737  22.693  15.102  1.00 141.91 ? 398 ASP A CG    1 
ATOM   2871 O  OD1   . ASP A 1 371 ? 95.188  21.767  15.736  1.00 145.15 ? 398 ASP A OD1   1 
ATOM   2872 O  OD2   . ASP A 1 371 ? 95.375  23.884  15.191  1.00 145.54 ? 398 ASP A OD2   1 
ATOM   2873 N  N     . PRO A 1 372 ? 94.099  21.298  12.545  1.00 141.40 ? 399 PRO A N     1 
ATOM   2874 C  CA    . PRO A 1 372 ? 92.895  21.763  11.835  1.00 131.41 ? 399 PRO A CA    1 
ATOM   2875 C  C     . PRO A 1 372 ? 92.482  23.187  12.177  1.00 132.16 ? 399 PRO A C     1 
ATOM   2876 O  O     . PRO A 1 372 ? 91.610  23.734  11.488  1.00 118.35 ? 399 PRO A O     1 
ATOM   2877 C  CB    . PRO A 1 372 ? 91.819  20.757  12.269  1.00 118.62 ? 399 PRO A CB    1 
ATOM   2878 C  CG    . PRO A 1 372 ? 92.581  19.543  12.696  1.00 124.78 ? 399 PRO A CG    1 
ATOM   2879 C  CD    . PRO A 1 372 ? 93.851  20.060  13.304  1.00 135.56 ? 399 PRO A CD    1 
ATOM   2880 N  N     . TYR A 1 373 ? 93.073  23.806  13.200  1.00 142.05 ? 400 TYR A N     1 
ATOM   2881 C  CA    . TYR A 1 373 ? 92.665  25.131  13.649  1.00 141.29 ? 400 TYR A CA    1 
ATOM   2882 C  C     . TYR A 1 373 ? 93.701  26.201  13.325  1.00 142.86 ? 400 TYR A C     1 
ATOM   2883 O  O     . TYR A 1 373 ? 93.404  27.132  12.569  1.00 145.53 ? 400 TYR A O     1 
ATOM   2884 C  CB    . TYR A 1 373 ? 92.363  25.100  15.154  1.00 145.29 ? 400 TYR A CB    1 
ATOM   2885 C  CG    . TYR A 1 373 ? 91.396  24.005  15.547  1.00 145.39 ? 400 TYR A CG    1 
ATOM   2886 C  CD1   . TYR A 1 373 ? 90.078  24.023  15.105  1.00 129.48 ? 400 TYR A CD1   1 
ATOM   2887 C  CD2   . TYR A 1 373 ? 91.801  22.953  16.358  1.00 155.25 ? 400 TYR A CD2   1 
ATOM   2888 C  CE1   . TYR A 1 373 ? 89.191  23.022  15.460  1.00 132.26 ? 400 TYR A CE1   1 
ATOM   2889 C  CE2   . TYR A 1 373 ? 90.922  21.949  16.719  1.00 156.13 ? 400 TYR A CE2   1 
ATOM   2890 C  CZ    . TYR A 1 373 ? 89.619  21.988  16.268  1.00 153.62 ? 400 TYR A CZ    1 
ATOM   2891 O  OH    . TYR A 1 373 ? 88.745  20.988  16.628  1.00 154.59 ? 400 TYR A OH    1 
ATOM   2892 N  N     . HIS A 1 374 ? 94.915  26.103  13.873  1.00 149.68 ? 401 HIS A N     1 
ATOM   2893 C  CA    . HIS A 1 374 ? 95.965  27.077  13.594  1.00 145.21 ? 401 HIS A CA    1 
ATOM   2894 C  C     . HIS A 1 374 ? 97.053  26.550  12.665  1.00 142.47 ? 401 HIS A C     1 
ATOM   2895 O  O     . HIS A 1 374 ? 97.952  27.312  12.297  1.00 143.28 ? 401 HIS A O     1 
ATOM   2896 C  CB    . HIS A 1 374 ? 96.596  27.586  14.899  1.00 145.20 ? 401 HIS A CB    1 
ATOM   2897 C  CG    . HIS A 1 374 ? 96.908  26.511  15.894  1.00 150.64 ? 401 HIS A CG    1 
ATOM   2898 N  ND1   . HIS A 1 374 ? 97.821  25.507  15.650  1.00 145.85 ? 401 HIS A ND1   1 
ATOM   2899 C  CD2   . HIS A 1 374 ? 96.438  26.294  17.146  1.00 152.59 ? 401 HIS A CD2   1 
ATOM   2900 C  CE1   . HIS A 1 374 ? 97.895  24.714  16.704  1.00 148.51 ? 401 HIS A CE1   1 
ATOM   2901 N  NE2   . HIS A 1 374 ? 97.065  25.169  17.626  1.00 153.23 ? 401 HIS A NE2   1 
ATOM   2902 N  N     . GLY A 1 375 ? 97.001  25.276  12.275  1.00 144.22 ? 402 GLY A N     1 
ATOM   2903 C  CA    . GLY A 1 375 ? 97.875  24.750  11.245  1.00 136.80 ? 402 GLY A CA    1 
ATOM   2904 C  C     . GLY A 1 375 ? 99.240  24.283  11.701  1.00 133.59 ? 402 GLY A C     1 
ATOM   2905 O  O     . GLY A 1 375 ? 100.047 23.874  10.855  1.00 138.21 ? 402 GLY A O     1 
ATOM   2906 N  N     . ARG A 1 376 ? 99.527  24.320  12.998  1.00 131.98 ? 403 ARG A N     1 
ATOM   2907 C  CA    . ARG A 1 376 ? 100.842 23.931  13.477  1.00 127.58 ? 403 ARG A CA    1 
ATOM   2908 C  C     . ARG A 1 376 ? 101.021 22.415  13.394  1.00 128.04 ? 403 ARG A C     1 
ATOM   2909 O  O     . ARG A 1 376 ? 100.050 21.658  13.474  1.00 124.02 ? 403 ARG A O     1 
ATOM   2910 C  CB    . ARG A 1 376 ? 101.044 24.395  14.916  1.00 131.92 ? 403 ARG A CB    1 
ATOM   2911 C  CG    . ARG A 1 376 ? 101.020 25.902  15.093  1.00 135.47 ? 403 ARG A CG    1 
ATOM   2912 C  CD    . ARG A 1 376 ? 101.061 26.275  16.563  1.00 139.34 ? 403 ARG A CD    1 
ATOM   2913 N  NE    . ARG A 1 376 ? 100.875 27.706  16.770  1.00 147.45 ? 403 ARG A NE    1 
ATOM   2914 C  CZ    . ARG A 1 376 ? 100.778 28.282  17.960  1.00 144.69 ? 403 ARG A CZ    1 
ATOM   2915 N  NH1   . ARG A 1 376 ? 100.842 27.576  19.077  1.00 143.68 ? 403 ARG A NH1   1 
ATOM   2916 N  NH2   . ARG A 1 376 ? 100.611 29.600  18.031  1.00 141.64 ? 403 ARG A NH2   1 
ATOM   2917 N  N     . PRO A 1 377 ? 102.257 21.946  13.222  1.00 124.43 ? 404 PRO A N     1 
ATOM   2918 C  CA    . PRO A 1 377 ? 102.500 20.498  13.197  1.00 117.70 ? 404 PRO A CA    1 
ATOM   2919 C  C     . PRO A 1 377 ? 102.309 19.853  14.561  1.00 110.98 ? 404 PRO A C     1 
ATOM   2920 O  O     . PRO A 1 377 ? 101.937 20.527  15.526  1.00 117.29 ? 404 PRO A O     1 
ATOM   2921 C  CB    . PRO A 1 377 ? 103.959 20.393  12.729  1.00 118.15 ? 404 PRO A CB    1 
ATOM   2922 C  CG    . PRO A 1 377 ? 104.267 21.717  12.098  1.00 114.87 ? 404 PRO A CG    1 
ATOM   2923 C  CD    . PRO A 1 377 ? 103.458 22.715  12.859  1.00 119.29 ? 404 PRO A CD    1 
ATOM   2924 N  N     . LEU A 1 378 ? 102.564 18.549  14.648  1.00 120.16 ? 405 LEU A N     1 
ATOM   2925 C  CA    . LEU A 1 378 ? 102.446 17.842  15.916  1.00 126.11 ? 405 LEU A CA    1 
ATOM   2926 C  C     . LEU A 1 378 ? 103.380 18.448  16.955  1.00 127.96 ? 405 LEU A C     1 
ATOM   2927 O  O     . LEU A 1 378 ? 104.547 18.733  16.674  1.00 124.96 ? 405 LEU A O     1 
ATOM   2928 C  CB    . LEU A 1 378 ? 102.771 16.361  15.729  1.00 124.51 ? 405 LEU A CB    1 
ATOM   2929 C  CG    . LEU A 1 378 ? 102.637 15.453  16.953  1.00 120.12 ? 405 LEU A CG    1 
ATOM   2930 C  CD1   . LEU A 1 378 ? 101.198 14.987  17.129  1.00 120.14 ? 405 LEU A CD1   1 
ATOM   2931 C  CD2   . LEU A 1 378 ? 103.585 14.268  16.855  1.00 119.52 ? 405 LEU A CD2   1 
ATOM   2932 N  N     . THR A 1 379 ? 102.860 18.643  18.161  1.00 122.71 ? 406 THR A N     1 
ATOM   2933 C  CA    . THR A 1 379 ? 103.637 19.216  19.249  1.00 122.09 ? 406 THR A CA    1 
ATOM   2934 C  C     . THR A 1 379 ? 104.269 18.113  20.090  1.00 122.35 ? 406 THR A C     1 
ATOM   2935 O  O     . THR A 1 379 ? 103.878 16.945  20.021  1.00 117.34 ? 406 THR A O     1 
ATOM   2936 C  CB    . THR A 1 379 ? 102.768 20.115  20.134  1.00 115.61 ? 406 THR A CB    1 
ATOM   2937 O  OG1   . THR A 1 379 ? 102.047 19.313  21.076  1.00 115.36 ? 406 THR A OG1   1 
ATOM   2938 C  CG2   . THR A 1 379 ? 101.779 20.898  19.283  1.00 100.94 ? 406 THR A CG2   1 
ATOM   2939 N  N     . LYS A 1 380 ? 105.277 18.502  20.876  1.00 121.33 ? 407 LYS A N     1 
ATOM   2940 C  CA    . LYS A 1 380 ? 105.917 17.551  21.779  1.00 115.30 ? 407 LYS A CA    1 
ATOM   2941 C  C     . LYS A 1 380 ? 104.925 17.013  22.800  1.00 114.71 ? 407 LYS A C     1 
ATOM   2942 O  O     . LYS A 1 380 ? 104.928 15.815  23.107  1.00 116.37 ? 407 LYS A O     1 
ATOM   2943 C  CB    . LYS A 1 380 ? 107.108 18.206  22.479  1.00 117.69 ? 407 LYS A CB    1 
ATOM   2944 C  CG    . LYS A 1 380 ? 108.315 18.417  21.580  1.00 130.76 ? 407 LYS A CG    1 
ATOM   2945 C  CD    . LYS A 1 380 ? 109.503 18.945  22.367  1.00 132.06 ? 407 LYS A CD    1 
ATOM   2946 C  CE    . LYS A 1 380 ? 110.685 19.235  21.455  1.00 139.74 ? 407 LYS A CE    1 
ATOM   2947 N  NZ    . LYS A 1 380 ? 111.844 19.810  22.196  1.00 138.99 ? 407 LYS A NZ    1 
ATOM   2948 N  N     . GLY A 1 381 ? 104.057 17.879  23.326  1.00 111.37 ? 408 GLY A N     1 
ATOM   2949 C  CA    . GLY A 1 381 ? 103.068 17.423  24.293  1.00 117.49 ? 408 GLY A CA    1 
ATOM   2950 C  C     . GLY A 1 381 ? 102.086 16.433  23.698  1.00 114.67 ? 408 GLY A C     1 
ATOM   2951 O  O     . GLY A 1 381 ? 101.783 15.400  24.301  1.00 113.11 ? 408 GLY A O     1 
ATOM   2952 N  N     . GLU A 1 382 ? 101.574 16.735  22.500  1.00 108.83 ? 409 GLU A N     1 
ATOM   2953 C  CA    . GLU A 1 382 ? 100.701 15.793  21.804  1.00 105.63 ? 409 GLU A CA    1 
ATOM   2954 C  C     . GLU A 1 382 ? 101.407 14.465  21.569  1.00 110.36 ? 409 GLU A C     1 
ATOM   2955 O  O     . GLU A 1 382 ? 100.781 13.400  21.626  1.00 105.49 ? 409 GLU A O     1 
ATOM   2956 C  CB    . GLU A 1 382 ? 100.236 16.386  20.474  1.00 108.83 ? 409 GLU A CB    1 
ATOM   2957 C  CG    . GLU A 1 382 ? 99.387  17.639  20.601  1.00 114.02 ? 409 GLU A CG    1 
ATOM   2958 C  CD    . GLU A 1 382 ? 99.130  18.300  19.262  1.00 117.41 ? 409 GLU A CD    1 
ATOM   2959 O  OE1   . GLU A 1 382 ? 99.758  17.886  18.264  1.00 118.21 ? 409 GLU A OE1   1 
ATOM   2960 O  OE2   . GLU A 1 382 ? 98.301  19.232  19.206  1.00 117.25 ? 409 GLU A OE2   1 
ATOM   2961 N  N     . LEU A 1 383 ? 102.714 14.513  21.302  1.00 114.65 ? 410 LEU A N     1 
ATOM   2962 C  CA    . LEU A 1 383 ? 103.498 13.291  21.162  1.00 101.91 ? 410 LEU A CA    1 
ATOM   2963 C  C     . LEU A 1 383 ? 103.478 12.480  22.452  1.00 101.97 ? 410 LEU A C     1 
ATOM   2964 O  O     . LEU A 1 383 ? 103.196 11.276  22.438  1.00 105.67 ? 410 LEU A O     1 
ATOM   2965 C  CB    . LEU A 1 383 ? 104.931 13.642  20.757  1.00 111.20 ? 410 LEU A CB    1 
ATOM   2966 C  CG    . LEU A 1 383 ? 106.049 12.645  21.062  1.00 114.14 ? 410 LEU A CG    1 
ATOM   2967 C  CD1   . LEU A 1 383 ? 105.848 11.354  20.299  1.00 117.09 ? 410 LEU A CD1   1 
ATOM   2968 C  CD2   . LEU A 1 383 ? 107.403 13.256  20.734  1.00 113.67 ? 410 LEU A CD2   1 
ATOM   2969 N  N     . GLY A 1 384 ? 103.769 13.128  23.582  1.00 101.13 ? 411 GLY A N     1 
ATOM   2970 C  CA    . GLY A 1 384 ? 103.741 12.425  24.854  1.00 104.27 ? 411 GLY A CA    1 
ATOM   2971 C  C     . GLY A 1 384 ? 102.354 11.935  25.221  1.00 110.31 ? 411 GLY A C     1 
ATOM   2972 O  O     . GLY A 1 384 ? 102.198 10.843  25.776  1.00 110.12 ? 411 GLY A O     1 
ATOM   2973 N  N     . CYS A 1 385 ? 101.328 12.736  24.920  1.00 111.17 ? 412 CYS A N     1 
ATOM   2974 C  CA    . CYS A 1 385 ? 99.953  12.306  25.155  1.00 108.40 ? 412 CYS A CA    1 
ATOM   2975 C  C     . CYS A 1 385 ? 99.644  11.034  24.376  1.00 103.30 ? 412 CYS A C     1 
ATOM   2976 O  O     . CYS A 1 385 ? 99.056  10.089  24.914  1.00 98.38  ? 412 CYS A O     1 
ATOM   2977 C  CB    . CYS A 1 385 ? 98.983  13.426  24.774  1.00 101.77 ? 412 CYS A CB    1 
ATOM   2978 S  SG    . CYS A 1 385 ? 97.233  13.006  24.961  1.00 96.43  ? 412 CYS A SG    1 
ATOM   2979 N  N     . PHE A 1 386 ? 100.048 10.991  23.105  1.00 105.69 ? 413 PHE A N     1 
ATOM   2980 C  CA    . PHE A 1 386 ? 99.873  9.779   22.312  1.00 108.55 ? 413 PHE A CA    1 
ATOM   2981 C  C     . PHE A 1 386 ? 100.656 8.616   22.909  1.00 106.87 ? 413 PHE A C     1 
ATOM   2982 O  O     . PHE A 1 386 ? 100.175 7.477   22.925  1.00 104.60 ? 413 PHE A O     1 
ATOM   2983 C  CB    . PHE A 1 386 ? 100.309 10.036  20.868  1.00 107.88 ? 413 PHE A CB    1 
ATOM   2984 C  CG    . PHE A 1 386 ? 99.858  8.981   19.896  1.00 108.54 ? 413 PHE A CG    1 
ATOM   2985 C  CD1   . PHE A 1 386 ? 100.532 7.774   19.795  1.00 105.41 ? 413 PHE A CD1   1 
ATOM   2986 C  CD2   . PHE A 1 386 ? 98.767  9.203   19.074  1.00 112.99 ? 413 PHE A CD2   1 
ATOM   2987 C  CE1   . PHE A 1 386 ? 100.119 6.806   18.902  1.00 107.54 ? 413 PHE A CE1   1 
ATOM   2988 C  CE2   . PHE A 1 386 ? 98.349  8.240   18.177  1.00 105.69 ? 413 PHE A CE2   1 
ATOM   2989 C  CZ    . PHE A 1 386 ? 99.025  7.041   18.091  1.00 108.96 ? 413 PHE A CZ    1 
ATOM   2990 N  N     . LEU A 1 387 ? 101.865 8.886   23.409  1.00 104.24 ? 414 LEU A N     1 
ATOM   2991 C  CA    . LEU A 1 387 ? 102.698 7.817   23.950  1.00 100.88 ? 414 LEU A CA    1 
ATOM   2992 C  C     . LEU A 1 387 ? 102.100 7.232   25.223  1.00 96.93  ? 414 LEU A C     1 
ATOM   2993 O  O     . LEU A 1 387 ? 102.162 6.016   25.439  1.00 97.74  ? 414 LEU A O     1 
ATOM   2994 C  CB    . LEU A 1 387 ? 104.112 8.335   24.209  1.00 100.02 ? 414 LEU A CB    1 
ATOM   2995 C  CG    . LEU A 1 387 ? 104.947 8.646   22.963  1.00 104.94 ? 414 LEU A CG    1 
ATOM   2996 C  CD1   . LEU A 1 387 ? 106.283 9.259   23.348  1.00 108.40 ? 414 LEU A CD1   1 
ATOM   2997 C  CD2   . LEU A 1 387 ? 105.148 7.392   22.126  1.00 101.45 ? 414 LEU A CD2   1 
ATOM   2998 N  N     . SER A 1 388 ? 101.518 8.078   26.076  1.00 98.09  ? 415 SER A N     1 
ATOM   2999 C  CA    . SER A 1 388 ? 100.909 7.584   27.308  1.00 100.81 ? 415 SER A CA    1 
ATOM   3000 C  C     . SER A 1 388 ? 99.725  6.672   27.006  1.00 96.34  ? 415 SER A C     1 
ATOM   3001 O  O     . SER A 1 388 ? 99.601  5.585   27.584  1.00 103.35 ? 415 SER A O     1 
ATOM   3002 C  CB    . SER A 1 388 ? 100.479 8.757   28.189  1.00 97.30  ? 415 SER A CB    1 
ATOM   3003 O  OG    . SER A 1 388 ? 101.601 9.518   28.605  1.00 104.39 ? 415 SER A OG    1 
ATOM   3004 N  N     . HIS A 1 389 ? 98.841  7.100   26.100  1.00 89.71  ? 416 HIS A N     1 
ATOM   3005 C  CA    . HIS A 1 389 ? 97.757  6.228   25.659  1.00 92.60  ? 416 HIS A CA    1 
ATOM   3006 C  C     . HIS A 1 389 ? 98.301  4.968   24.997  1.00 101.21 ? 416 HIS A C     1 
ATOM   3007 O  O     . HIS A 1 389 ? 97.819  3.861   25.261  1.00 96.94  ? 416 HIS A O     1 
ATOM   3008 C  CB    . HIS A 1 389 ? 96.830  6.978   24.700  1.00 81.11  ? 416 HIS A CB    1 
ATOM   3009 C  CG    . HIS A 1 389 ? 96.006  8.043   25.355  1.00 88.44  ? 416 HIS A CG    1 
ATOM   3010 N  ND1   . HIS A 1 389 ? 94.776  7.789   25.920  1.00 87.83  ? 416 HIS A ND1   1 
ATOM   3011 C  CD2   . HIS A 1 389 ? 96.231  9.367   25.524  1.00 95.25  ? 416 HIS A CD2   1 
ATOM   3012 C  CE1   . HIS A 1 389 ? 94.280  8.909   26.416  1.00 83.59  ? 416 HIS A CE1   1 
ATOM   3013 N  NE2   . HIS A 1 389 ? 95.144  9.882   26.189  1.00 96.22  ? 416 HIS A NE2   1 
ATOM   3014 N  N     . TYR A 1 390 ? 99.307  5.120   24.132  1.00 97.35  ? 417 TYR A N     1 
ATOM   3015 C  CA    . TYR A 1 390 ? 99.918  3.966   23.481  1.00 95.10  ? 417 TYR A CA    1 
ATOM   3016 C  C     . TYR A 1 390 ? 100.451 2.973   24.506  1.00 99.67  ? 417 TYR A C     1 
ATOM   3017 O  O     . TYR A 1 390 ? 100.251 1.761   24.366  1.00 95.93  ? 417 TYR A O     1 
ATOM   3018 C  CB    . TYR A 1 390 ? 101.035 4.435   22.545  1.00 107.16 ? 417 TYR A CB    1 
ATOM   3019 C  CG    . TYR A 1 390 ? 101.749 3.336   21.792  1.00 114.02 ? 417 TYR A CG    1 
ATOM   3020 C  CD1   . TYR A 1 390 ? 101.241 2.841   20.597  1.00 123.23 ? 417 TYR A CD1   1 
ATOM   3021 C  CD2   . TYR A 1 390 ? 102.945 2.810   22.262  1.00 119.96 ? 417 TYR A CD2   1 
ATOM   3022 C  CE1   . TYR A 1 390 ? 101.899 1.843   19.900  1.00 126.21 ? 417 TYR A CE1   1 
ATOM   3023 C  CE2   . TYR A 1 390 ? 103.608 1.812   21.572  1.00 121.46 ? 417 TYR A CE2   1 
ATOM   3024 C  CZ    . TYR A 1 390 ? 103.079 1.331   20.393  1.00 125.44 ? 417 TYR A CZ    1 
ATOM   3025 O  OH    . TYR A 1 390 ? 103.734 0.338   19.702  1.00 119.84 ? 417 TYR A OH    1 
ATOM   3026 N  N     . ASN A 1 391 ? 101.120 3.468   25.551  1.00 98.05  ? 418 ASN A N     1 
ATOM   3027 C  CA    . ASN A 1 391 ? 101.656 2.576   26.575  1.00 98.04  ? 418 ASN A CA    1 
ATOM   3028 C  C     . ASN A 1 391 ? 100.543 1.843   27.310  1.00 97.74  ? 418 ASN A C     1 
ATOM   3029 O  O     . ASN A 1 391 ? 100.701 0.674   27.683  1.00 108.85 ? 418 ASN A O     1 
ATOM   3030 C  CB    . ASN A 1 391 ? 102.525 3.360   27.559  1.00 101.07 ? 418 ASN A CB    1 
ATOM   3031 C  CG    . ASN A 1 391 ? 103.778 3.913   26.913  1.00 107.05 ? 418 ASN A CG    1 
ATOM   3032 O  OD1   . ASN A 1 391 ? 104.240 3.400   25.893  1.00 98.23  ? 418 ASN A OD1   1 
ATOM   3033 N  ND2   . ASN A 1 391 ? 104.335 4.963   27.504  1.00 110.51 ? 418 ASN A ND2   1 
ATOM   3034 N  N     . ILE A 1 392 ? 99.409  2.512   27.533  1.00 89.51  ? 419 ILE A N     1 
ATOM   3035 C  CA    . ILE A 1 392 ? 98.270  1.844   28.154  1.00 95.44  ? 419 ILE A CA    1 
ATOM   3036 C  C     . ILE A 1 392 ? 97.713  0.770   27.226  1.00 90.39  ? 419 ILE A C     1 
ATOM   3037 O  O     . ILE A 1 392 ? 97.307  -0.310  27.675  1.00 91.81  ? 419 ILE A O     1 
ATOM   3038 C  CB    . ILE A 1 392 ? 97.194  2.873   28.547  1.00 94.03  ? 419 ILE A CB    1 
ATOM   3039 C  CG1   . ILE A 1 392 ? 97.740  3.836   29.603  1.00 90.13  ? 419 ILE A CG1   1 
ATOM   3040 C  CG2   . ILE A 1 392 ? 95.940  2.179   29.058  1.00 84.71  ? 419 ILE A CG2   1 
ATOM   3041 C  CD1   . ILE A 1 392 ? 96.704  4.784   30.157  1.00 94.30  ? 419 ILE A CD1   1 
ATOM   3042 N  N     . TRP A 1 393 ? 97.694  1.043   25.918  1.00 93.13  ? 420 TRP A N     1 
ATOM   3043 C  CA    . TRP A 1 393 ? 97.253  0.038   24.955  1.00 93.36  ? 420 TRP A CA    1 
ATOM   3044 C  C     . TRP A 1 393 ? 98.131  -1.206  25.021  1.00 105.05 ? 420 TRP A C     1 
ATOM   3045 O  O     . TRP A 1 393 ? 97.629  -2.334  24.951  1.00 102.55 ? 420 TRP A O     1 
ATOM   3046 C  CB    . TRP A 1 393 ? 97.261  0.620   23.541  1.00 91.92  ? 420 TRP A CB    1 
ATOM   3047 C  CG    . TRP A 1 393 ? 96.443  1.866   23.380  1.00 90.00  ? 420 TRP A CG    1 
ATOM   3048 C  CD1   . TRP A 1 393 ? 95.453  2.313   24.207  1.00 80.46  ? 420 TRP A CD1   1 
ATOM   3049 C  CD2   . TRP A 1 393 ? 96.554  2.832   22.328  1.00 100.59 ? 420 TRP A CD2   1 
ATOM   3050 N  NE1   . TRP A 1 393 ? 94.939  3.496   23.733  1.00 76.78  ? 420 TRP A NE1   1 
ATOM   3051 C  CE2   . TRP A 1 393 ? 95.598  3.837   22.580  1.00 90.93  ? 420 TRP A CE2   1 
ATOM   3052 C  CE3   . TRP A 1 393 ? 97.368  2.944   21.194  1.00 90.19  ? 420 TRP A CE3   1 
ATOM   3053 C  CZ2   . TRP A 1 393 ? 95.434  4.940   21.741  1.00 83.54  ? 420 TRP A CZ2   1 
ATOM   3054 C  CZ3   . TRP A 1 393 ? 97.203  4.040   20.364  1.00 89.52  ? 420 TRP A CZ3   1 
ATOM   3055 C  CH2   . TRP A 1 393 ? 96.243  5.022   20.642  1.00 94.25  ? 420 TRP A CH2   1 
ATOM   3056 N  N     . LYS A 1 394 ? 99.447  -1.018  25.154  1.00 102.60 ? 421 LYS A N     1 
ATOM   3057 C  CA    . LYS A 1 394 ? 100.348 -2.157  25.298  1.00 98.65  ? 421 LYS A CA    1 
ATOM   3058 C  C     . LYS A 1 394 ? 100.045 -2.936  26.570  1.00 103.37 ? 421 LYS A C     1 
ATOM   3059 O  O     . LYS A 1 394 ? 100.018 -4.172  26.561  1.00 108.59 ? 421 LYS A O     1 
ATOM   3060 C  CB    . LYS A 1 394 ? 101.801 -1.680  25.308  1.00 108.38 ? 421 LYS A CB    1 
ATOM   3061 C  CG    . LYS A 1 394 ? 102.154 -0.712  24.197  1.00 118.46 ? 421 LYS A CG    1 
ATOM   3062 C  CD    . LYS A 1 394 ? 103.388 0.100   24.561  1.00 115.60 ? 421 LYS A CD    1 
ATOM   3063 C  CE    . LYS A 1 394 ? 104.656 -0.726  24.455  1.00 110.93 ? 421 LYS A CE    1 
ATOM   3064 N  NZ    . LYS A 1 394 ? 104.957 -1.089  23.044  1.00 127.35 ? 421 LYS A NZ    1 
ATOM   3065 N  N     . GLU A 1 395 ? 99.815  -2.227  27.677  1.00 100.75 ? 422 GLU A N     1 
ATOM   3066 C  CA    . GLU A 1 395 ? 99.551  -2.894  28.946  1.00 99.89  ? 422 GLU A CA    1 
ATOM   3067 C  C     . GLU A 1 395 ? 98.227  -3.650  28.922  1.00 96.84  ? 422 GLU A C     1 
ATOM   3068 O  O     . GLU A 1 395 ? 98.092  -4.679  29.594  1.00 99.10  ? 422 GLU A O     1 
ATOM   3069 C  CB    . GLU A 1 395 ? 99.570  -1.873  30.085  1.00 99.56  ? 422 GLU A CB    1 
ATOM   3070 C  CG    . GLU A 1 395 ? 99.406  -2.476  31.468  1.00 95.07  ? 422 GLU A CG    1 
ATOM   3071 C  CD    . GLU A 1 395 ? 99.451  -1.435  32.567  1.00 104.66 ? 422 GLU A CD    1 
ATOM   3072 O  OE1   . GLU A 1 395 ? 99.990  -0.333  32.325  1.00 106.78 ? 422 GLU A OE1   1 
ATOM   3073 O  OE2   . GLU A 1 395 ? 98.943  -1.718  33.673  1.00 98.31  ? 422 GLU A OE2   1 
ATOM   3074 N  N     . VAL A 1 396 ? 97.246  -3.162  28.159  1.00 92.98  ? 423 VAL A N     1 
ATOM   3075 C  CA    . VAL A 1 396 ? 95.986  -3.888  28.015  1.00 98.28  ? 423 VAL A CA    1 
ATOM   3076 C  C     . VAL A 1 396 ? 96.224  -5.231  27.336  1.00 103.02 ? 423 VAL A C     1 
ATOM   3077 O  O     . VAL A 1 396 ? 95.696  -6.265  27.766  1.00 105.99 ? 423 VAL A O     1 
ATOM   3078 C  CB    . VAL A 1 396 ? 94.959  -3.035  27.246  1.00 91.63  ? 423 VAL A CB    1 
ATOM   3079 C  CG1   . VAL A 1 396 ? 93.769  -3.883  26.821  1.00 99.26  ? 423 VAL A CG1   1 
ATOM   3080 C  CG2   . VAL A 1 396 ? 94.497  -1.863  28.098  1.00 93.65  ? 423 VAL A CG2   1 
ATOM   3081 N  N     . VAL A 1 397 ? 97.033  -5.241  26.275  1.00 102.04 ? 424 VAL A N     1 
ATOM   3082 C  CA    . VAL A 1 397 ? 97.336  -6.490  25.584  1.00 105.76 ? 424 VAL A CA    1 
ATOM   3083 C  C     . VAL A 1 397 ? 98.257  -7.361  26.430  1.00 98.48  ? 424 VAL A C     1 
ATOM   3084 O  O     . VAL A 1 397 ? 98.094  -8.586  26.488  1.00 99.46  ? 424 VAL A O     1 
ATOM   3085 C  CB    . VAL A 1 397 ? 97.940  -6.198  24.198  1.00 99.72  ? 424 VAL A CB    1 
ATOM   3086 C  CG1   . VAL A 1 397 ? 98.296  -7.494  23.485  1.00 96.53  ? 424 VAL A CG1   1 
ATOM   3087 C  CG2   . VAL A 1 397 ? 96.971  -5.378  23.362  1.00 97.45  ? 424 VAL A CG2   1 
ATOM   3088 N  N     . ASP A 1 398 ? 99.233  -6.747  27.104  1.00 103.12 ? 425 ASP A N     1 
ATOM   3089 C  CA    . ASP A 1 398 ? 100.179 -7.516  27.908  1.00 99.63  ? 425 ASP A CA    1 
ATOM   3090 C  C     . ASP A 1 398 ? 99.474  -8.218  29.063  1.00 99.38  ? 425 ASP A C     1 
ATOM   3091 O  O     . ASP A 1 398 ? 99.708  -9.405  29.319  1.00 101.50 ? 425 ASP A O     1 
ATOM   3092 C  CB    . ASP A 1 398 ? 101.289 -6.601  28.429  1.00 103.22 ? 425 ASP A CB    1 
ATOM   3093 C  CG    . ASP A 1 398 ? 102.430 -7.372  29.067  1.00 127.21 ? 425 ASP A CG    1 
ATOM   3094 O  OD1   . ASP A 1 398 ? 102.533 -8.594  28.829  1.00 146.79 ? 425 ASP A OD1   1 
ATOM   3095 O  OD2   . ASP A 1 398 ? 103.222 -6.756  29.810  1.00 137.95 ? 425 ASP A OD2   1 
ATOM   3096 N  N     . ARG A 1 399 ? 98.605  -7.499  29.772  1.00 99.35  ? 426 ARG A N     1 
ATOM   3097 C  CA    . ARG A 1 399 ? 97.855  -8.075  30.882  1.00 98.24  ? 426 ARG A CA    1 
ATOM   3098 C  C     . ARG A 1 399 ? 96.587  -8.792  30.438  1.00 100.67 ? 426 ARG A C     1 
ATOM   3099 O  O     . ARG A 1 399 ? 95.917  -9.403  31.278  1.00 99.87  ? 426 ARG A O     1 
ATOM   3100 C  CB    . ARG A 1 399 ? 97.496  -6.986  31.897  1.00 94.24  ? 426 ARG A CB    1 
ATOM   3101 C  CG    . ARG A 1 399 ? 98.675  -6.464  32.701  1.00 87.71  ? 426 ARG A CG    1 
ATOM   3102 C  CD    . ARG A 1 399 ? 98.273  -5.251  33.522  1.00 95.13  ? 426 ARG A CD    1 
ATOM   3103 N  NE    . ARG A 1 399 ? 97.210  -5.553  34.473  1.00 95.38  ? 426 ARG A NE    1 
ATOM   3104 C  CZ    . ARG A 1 399 ? 96.451  -4.639  35.062  1.00 107.35 ? 426 ARG A CZ    1 
ATOM   3105 N  NH1   . ARG A 1 399 ? 96.594  -3.350  34.801  1.00 99.92  ? 426 ARG A NH1   1 
ATOM   3106 N  NH2   . ARG A 1 399 ? 95.521  -5.028  35.929  1.00 110.32 ? 426 ARG A NH2   1 
ATOM   3107 N  N     . GLY A 1 400 ? 96.243  -8.737  29.155  1.00 96.83  ? 427 GLY A N     1 
ATOM   3108 C  CA    . GLY A 1 400 ? 95.041  -9.407  28.681  1.00 92.98  ? 427 GLY A CA    1 
ATOM   3109 C  C     . GLY A 1 400 ? 93.765  -8.820  29.242  1.00 102.17 ? 427 GLY A C     1 
ATOM   3110 O  O     . GLY A 1 400 ? 92.825  -9.562  29.554  1.00 103.90 ? 427 GLY A O     1 
ATOM   3111 N  N     . LEU A 1 401 ? 93.712  -7.499  29.381  1.00 93.83  ? 428 LEU A N     1 
ATOM   3112 C  CA    . LEU A 1 401 ? 92.549  -6.830  29.947  1.00 94.73  ? 428 LEU A CA    1 
ATOM   3113 C  C     . LEU A 1 401 ? 91.438  -6.772  28.906  1.00 95.99  ? 428 LEU A C     1 
ATOM   3114 O  O     . LEU A 1 401 ? 91.604  -6.159  27.846  1.00 95.41  ? 428 LEU A O     1 
ATOM   3115 C  CB    . LEU A 1 401 ? 92.930  -5.430  30.417  1.00 93.01  ? 428 LEU A CB    1 
ATOM   3116 C  CG    . LEU A 1 401 ? 94.161  -5.371  31.325  1.00 98.64  ? 428 LEU A CG    1 
ATOM   3117 C  CD1   . LEU A 1 401 ? 94.512  -3.934  31.671  1.00 96.54  ? 428 LEU A CD1   1 
ATOM   3118 C  CD2   . LEU A 1 401 ? 93.931  -6.189  32.585  1.00 90.05  ? 428 LEU A CD2   1 
ATOM   3119 N  N     . GLN A 1 402 ? 90.306  -7.413  29.209  1.00 94.48  ? 429 GLN A N     1 
ATOM   3120 C  CA    . GLN A 1 402 ? 89.194  -7.445  28.263  1.00 85.98  ? 429 GLN A CA    1 
ATOM   3121 C  C     . GLN A 1 402 ? 88.591  -6.058  28.077  1.00 87.30  ? 429 GLN A C     1 
ATOM   3122 O  O     . GLN A 1 402 ? 88.489  -5.559  26.951  1.00 92.72  ? 429 GLN A O     1 
ATOM   3123 C  CB    . GLN A 1 402 ? 88.132  -8.442  28.730  1.00 88.14  ? 429 GLN A CB    1 
ATOM   3124 C  CG    . GLN A 1 402 ? 88.592  -9.891  28.730  1.00 80.61  ? 429 GLN A CG    1 
ATOM   3125 C  CD    . GLN A 1 402 ? 88.953  -10.392 27.343  1.00 111.72 ? 429 GLN A CD    1 
ATOM   3126 O  OE1   . GLN A 1 402 ? 88.485  -9.862  26.334  1.00 98.38  ? 429 GLN A OE1   1 
ATOM   3127 N  NE2   . GLN A 1 402 ? 89.794  -11.419 27.286  1.00 120.77 ? 429 GLN A NE2   1 
ATOM   3128 N  N     . LYS A 1 403 ? 88.181  -5.418  29.171  1.00 88.87  ? 430 LYS A N     1 
ATOM   3129 C  CA    . LYS A 1 403 ? 87.640  -4.067  29.122  1.00 80.66  ? 430 LYS A CA    1 
ATOM   3130 C  C     . LYS A 1 403 ? 88.370  -3.192  30.129  1.00 81.57  ? 430 LYS A C     1 
ATOM   3131 O  O     . LYS A 1 403 ? 88.479  -3.549  31.306  1.00 69.27  ? 430 LYS A O     1 
ATOM   3132 C  CB    . LYS A 1 403 ? 86.130  -4.052  29.393  1.00 67.63  ? 430 LYS A CB    1 
ATOM   3133 C  CG    . LYS A 1 403 ? 85.693  -4.822  30.626  1.00 76.53  ? 430 LYS A CG    1 
ATOM   3134 C  CD    . LYS A 1 403 ? 84.224  -4.569  30.924  1.00 82.71  ? 430 LYS A CD    1 
ATOM   3135 C  CE    . LYS A 1 403 ? 83.752  -5.376  32.121  1.00 94.57  ? 430 LYS A CE    1 
ATOM   3136 N  NZ    . LYS A 1 403 ? 82.371  -5.003  32.540  1.00 98.42  ? 430 LYS A NZ    1 
ATOM   3137 N  N     . SER A 1 404 ? 88.866  -2.050  29.661  1.00 82.74  ? 431 SER A N     1 
ATOM   3138 C  CA    . SER A 1 404 ? 89.586  -1.102  30.497  1.00 65.37  ? 431 SER A CA    1 
ATOM   3139 C  C     . SER A 1 404 ? 89.084  0.304   30.211  1.00 71.43  ? 431 SER A C     1 
ATOM   3140 O  O     . SER A 1 404 ? 88.774  0.640   29.064  1.00 75.00  ? 431 SER A O     1 
ATOM   3141 C  CB    . SER A 1 404 ? 91.097  -1.177  30.255  1.00 70.81  ? 431 SER A CB    1 
ATOM   3142 O  OG    . SER A 1 404 ? 91.555  -2.515  30.316  1.00 83.30  ? 431 SER A OG    1 
ATOM   3143 N  N     . LEU A 1 405 ? 89.002  1.118   31.259  1.00 72.57  ? 432 LEU A N     1 
ATOM   3144 C  CA    . LEU A 1 405 ? 88.558  2.502   31.162  1.00 64.64  ? 432 LEU A CA    1 
ATOM   3145 C  C     . LEU A 1 405 ? 89.742  3.428   31.409  1.00 68.76  ? 432 LEU A C     1 
ATOM   3146 O  O     . LEU A 1 405 ? 90.473  3.260   32.390  1.00 69.23  ? 432 LEU A O     1 
ATOM   3147 C  CB    . LEU A 1 405 ? 87.436  2.782   32.164  1.00 67.46  ? 432 LEU A CB    1 
ATOM   3148 C  CG    . LEU A 1 405 ? 87.078  4.236   32.463  1.00 65.09  ? 432 LEU A CG    1 
ATOM   3149 C  CD1   . LEU A 1 405 ? 86.452  4.904   31.253  1.00 63.20  ? 432 LEU A CD1   1 
ATOM   3150 C  CD2   . LEU A 1 405 ? 86.138  4.279   33.645  1.00 61.19  ? 432 LEU A CD2   1 
ATOM   3151 N  N     . VAL A 1 406 ? 89.929  4.398   30.518  1.00 67.89  ? 433 VAL A N     1 
ATOM   3152 C  CA    . VAL A 1 406 ? 91.066  5.310   30.562  1.00 73.12  ? 433 VAL A CA    1 
ATOM   3153 C  C     . VAL A 1 406 ? 90.559  6.712   30.869  1.00 63.74  ? 433 VAL A C     1 
ATOM   3154 O  O     . VAL A 1 406 ? 89.616  7.195   30.231  1.00 62.65  ? 433 VAL A O     1 
ATOM   3155 C  CB    . VAL A 1 406 ? 91.858  5.284   29.242  1.00 72.04  ? 433 VAL A CB    1 
ATOM   3156 C  CG1   . VAL A 1 406 ? 93.095  6.170   29.340  1.00 69.98  ? 433 VAL A CG1   1 
ATOM   3157 C  CG2   . VAL A 1 406 ? 92.247  3.859   28.892  1.00 66.15  ? 433 VAL A CG2   1 
ATOM   3158 N  N     . PHE A 1 407 ? 91.194  7.363   31.840  1.00 68.53  ? 434 PHE A N     1 
ATOM   3159 C  CA    . PHE A 1 407 ? 90.848  8.711   32.260  1.00 68.73  ? 434 PHE A CA    1 
ATOM   3160 C  C     . PHE A 1 407 ? 92.007  9.658   31.985  1.00 72.35  ? 434 PHE A C     1 
ATOM   3161 O  O     . PHE A 1 407 ? 93.175  9.261   32.013  1.00 73.24  ? 434 PHE A O     1 
ATOM   3162 C  CB    . PHE A 1 407 ? 90.516  8.767   33.759  1.00 71.42  ? 434 PHE A CB    1 
ATOM   3163 C  CG    . PHE A 1 407 ? 89.131  8.305   34.101  1.00 70.69  ? 434 PHE A CG    1 
ATOM   3164 C  CD1   . PHE A 1 407 ? 88.098  8.419   33.188  1.00 75.09  ? 434 PHE A CD1   1 
ATOM   3165 C  CD2   . PHE A 1 407 ? 88.860  7.768   35.350  1.00 75.79  ? 434 PHE A CD2   1 
ATOM   3166 C  CE1   . PHE A 1 407 ? 86.823  7.997   33.511  1.00 82.20  ? 434 PHE A CE1   1 
ATOM   3167 C  CE2   . PHE A 1 407 ? 87.585  7.346   35.678  1.00 71.07  ? 434 PHE A CE2   1 
ATOM   3168 C  CZ    . PHE A 1 407 ? 86.565  7.466   34.758  1.00 80.68  ? 434 PHE A CZ    1 
ATOM   3169 N  N     . GLU A 1 408 ? 91.670  10.916  31.723  1.00 70.82  ? 435 GLU A N     1 
ATOM   3170 C  CA    . GLU A 1 408 ? 92.632  12.002  31.769  1.00 77.55  ? 435 GLU A CA    1 
ATOM   3171 C  C     . GLU A 1 408 ? 92.479  12.728  33.106  1.00 78.22  ? 435 GLU A C     1 
ATOM   3172 O  O     . GLU A 1 408 ? 91.629  12.387  33.931  1.00 83.77  ? 435 GLU A O     1 
ATOM   3173 C  CB    . GLU A 1 408 ? 92.455  12.935  30.567  1.00 77.62  ? 435 GLU A CB    1 
ATOM   3174 C  CG    . GLU A 1 408 ? 92.963  12.330  29.257  1.00 88.58  ? 435 GLU A CG    1 
ATOM   3175 C  CD    . GLU A 1 408 ? 92.943  13.309  28.096  1.00 95.36  ? 435 GLU A CD    1 
ATOM   3176 O  OE1   . GLU A 1 408 ? 92.402  14.422  28.262  1.00 101.83 ? 435 GLU A OE1   1 
ATOM   3177 O  OE2   . GLU A 1 408 ? 93.468  12.962  27.015  1.00 84.33  ? 435 GLU A OE2   1 
ATOM   3178 N  N     . ASP A 1 409 ? 93.320  13.737  33.329  1.00 79.88  ? 436 ASP A N     1 
ATOM   3179 C  CA    . ASP A 1 409 ? 93.462  14.346  34.647  1.00 86.66  ? 436 ASP A CA    1 
ATOM   3180 C  C     . ASP A 1 409 ? 92.733  15.683  34.779  1.00 86.04  ? 436 ASP A C     1 
ATOM   3181 O  O     . ASP A 1 409 ? 93.043  16.457  35.689  1.00 94.25  ? 436 ASP A O     1 
ATOM   3182 C  CB    . ASP A 1 409 ? 94.947  14.511  34.990  1.00 75.79  ? 436 ASP A CB    1 
ATOM   3183 C  CG    . ASP A 1 409 ? 95.713  15.299  33.938  1.00 86.80  ? 436 ASP A CG    1 
ATOM   3184 O  OD1   . ASP A 1 409 ? 95.102  15.714  32.931  1.00 92.27  ? 436 ASP A OD1   1 
ATOM   3185 O  OD2   . ASP A 1 409 ? 96.933  15.503  34.124  1.00 101.91 ? 436 ASP A OD2   1 
ATOM   3186 N  N     . ASP A 1 410 ? 91.763  15.964  33.916  1.00 83.28  ? 437 ASP A N     1 
ATOM   3187 C  CA    . ASP A 1 410 ? 91.085  17.259  33.947  1.00 83.32  ? 437 ASP A CA    1 
ATOM   3188 C  C     . ASP A 1 410 ? 89.656  17.123  33.421  1.00 84.53  ? 437 ASP A C     1 
ATOM   3189 O  O     . ASP A 1 410 ? 89.257  17.735  32.435  1.00 91.54  ? 437 ASP A O     1 
ATOM   3190 C  CB    . ASP A 1 410 ? 91.877  18.295  33.150  1.00 88.23  ? 437 ASP A CB    1 
ATOM   3191 C  CG    . ASP A 1 410 ? 92.053  17.902  31.693  1.00 103.09 ? 437 ASP A CG    1 
ATOM   3192 O  OD1   . ASP A 1 410 ? 91.787  16.730  31.350  1.00 98.37  ? 437 ASP A OD1   1 
ATOM   3193 O  OD2   . ASP A 1 410 ? 92.449  18.775  30.891  1.00 119.76 ? 437 ASP A OD2   1 
ATOM   3194 N  N     . LEU A 1 411 ? 88.834  16.322  34.092  1.00 69.40  ? 438 LEU A N     1 
ATOM   3195 C  CA    . LEU A 1 411 ? 87.498  16.037  33.596  1.00 80.94  ? 438 LEU A CA    1 
ATOM   3196 C  C     . LEU A 1 411 ? 86.462  16.168  34.706  1.00 79.75  ? 438 LEU A C     1 
ATOM   3197 O  O     . LEU A 1 411 ? 86.729  15.877  35.876  1.00 83.51  ? 438 LEU A O     1 
ATOM   3198 C  CB    . LEU A 1 411 ? 87.439  14.640  32.958  1.00 77.04  ? 438 LEU A CB    1 
ATOM   3199 C  CG    . LEU A 1 411 ? 88.102  13.471  33.686  1.00 66.01  ? 438 LEU A CG    1 
ATOM   3200 C  CD1   . LEU A 1 411 ? 87.122  12.822  34.635  1.00 91.83  ? 438 LEU A CD1   1 
ATOM   3201 C  CD2   . LEU A 1 411 ? 88.636  12.456  32.691  1.00 63.23  ? 438 LEU A CD2   1 
ATOM   3202 N  N     . ARG A 1 412 ? 85.275  16.622  34.314  1.00 63.55  ? 439 ARG A N     1 
ATOM   3203 C  CA    . ARG A 1 412 ? 84.151  16.848  35.213  1.00 60.39  ? 439 ARG A CA    1 
ATOM   3204 C  C     . ARG A 1 412 ? 83.167  15.694  35.089  1.00 58.41  ? 439 ARG A C     1 
ATOM   3205 O  O     . ARG A 1 412 ? 82.710  15.380  33.986  1.00 65.55  ? 439 ARG A O     1 
ATOM   3206 C  CB    . ARG A 1 412 ? 83.461  18.171  34.880  1.00 58.51  ? 439 ARG A CB    1 
ATOM   3207 C  CG    . ARG A 1 412 ? 82.057  18.316  35.432  1.00 75.07  ? 439 ARG A CG    1 
ATOM   3208 C  CD    . ARG A 1 412 ? 81.327  19.454  34.734  1.00 74.53  ? 439 ARG A CD    1 
ATOM   3209 N  NE    . ARG A 1 412 ? 81.905  20.754  35.045  1.00 82.82  ? 439 ARG A NE    1 
ATOM   3210 C  CZ    . ARG A 1 412 ? 81.213  21.799  35.479  1.00 88.97  ? 439 ARG A CZ    1 
ATOM   3211 N  NH1   . ARG A 1 412 ? 79.900  21.745  35.630  1.00 63.96  ? 439 ARG A NH1   1 
ATOM   3212 N  NH2   . ARG A 1 412 ? 81.855  22.929  35.761  1.00 102.68 ? 439 ARG A NH2   1 
ATOM   3213 N  N     . PHE A 1 413 ? 82.841  15.069  36.216  1.00 65.30  ? 440 PHE A N     1 
ATOM   3214 C  CA    . PHE A 1 413 ? 81.988  13.889  36.207  1.00 47.01  ? 440 PHE A CA    1 
ATOM   3215 C  C     . PHE A 1 413 ? 80.517  14.282  36.194  1.00 48.02  ? 440 PHE A C     1 
ATOM   3216 O  O     . PHE A 1 413 ? 80.093  15.166  36.944  1.00 50.43  ? 440 PHE A O     1 
ATOM   3217 C  CB    . PHE A 1 413 ? 82.278  13.015  37.424  1.00 46.65  ? 440 PHE A CB    1 
ATOM   3218 C  CG    . PHE A 1 413 ? 83.591  12.296  37.359  1.00 67.85  ? 440 PHE A CG    1 
ATOM   3219 C  CD1   . PHE A 1 413 ? 83.681  11.053  36.756  1.00 61.86  ? 440 PHE A CD1   1 
ATOM   3220 C  CD2   . PHE A 1 413 ? 84.730  12.852  37.917  1.00 63.92  ? 440 PHE A CD2   1 
ATOM   3221 C  CE1   . PHE A 1 413 ? 84.884  10.379  36.704  1.00 72.32  ? 440 PHE A CE1   1 
ATOM   3222 C  CE2   . PHE A 1 413 ? 85.937  12.184  37.869  1.00 59.29  ? 440 PHE A CE2   1 
ATOM   3223 C  CZ    . PHE A 1 413 ? 86.013  10.944  37.263  1.00 76.63  ? 440 PHE A CZ    1 
ATOM   3224 N  N     . GLU A 1 414 ? 79.739  13.620  35.343  1.00 45.96  ? 441 GLU A N     1 
ATOM   3225 C  CA    . GLU A 1 414 ? 78.299  13.803  35.354  1.00 51.26  ? 441 GLU A CA    1 
ATOM   3226 C  C     . GLU A 1 414 ? 77.686  13.136  36.584  1.00 58.15  ? 441 GLU A C     1 
ATOM   3227 O  O     . GLU A 1 414 ? 78.314  12.323  37.268  1.00 57.51  ? 441 GLU A O     1 
ATOM   3228 C  CB    . GLU A 1 414 ? 77.673  13.234  34.080  1.00 52.32  ? 441 GLU A CB    1 
ATOM   3229 C  CG    . GLU A 1 414 ? 77.620  14.213  32.919  1.00 67.80  ? 441 GLU A CG    1 
ATOM   3230 C  CD    . GLU A 1 414 ? 76.580  15.298  33.121  1.00 76.15  ? 441 GLU A CD    1 
ATOM   3231 O  OE1   . GLU A 1 414 ? 75.680  15.112  33.970  1.00 85.15  ? 441 GLU A OE1   1 
ATOM   3232 O  OE2   . GLU A 1 414 ? 76.661  16.338  32.432  1.00 66.29  ? 441 GLU A OE2   1 
ATOM   3233 N  N     . ILE A 1 415 ? 76.432  13.493  36.859  1.00 49.99  ? 442 ILE A N     1 
ATOM   3234 C  CA    . ILE A 1 415 ? 75.717  12.907  37.984  1.00 54.81  ? 442 ILE A CA    1 
ATOM   3235 C  C     . ILE A 1 415 ? 75.422  11.441  37.693  1.00 55.82  ? 442 ILE A C     1 
ATOM   3236 O  O     . ILE A 1 415 ? 75.178  11.049  36.541  1.00 53.45  ? 442 ILE A O     1 
ATOM   3237 C  CB    . ILE A 1 415 ? 74.434  13.707  38.273  1.00 53.10  ? 442 ILE A CB    1 
ATOM   3238 C  CG1   . ILE A 1 415 ? 73.786  13.251  39.582  1.00 54.07  ? 442 ILE A CG1   1 
ATOM   3239 C  CG2   . ILE A 1 415 ? 73.456  13.604  37.109  1.00 44.02  ? 442 ILE A CG2   1 
ATOM   3240 C  CD1   . ILE A 1 415 ? 72.607  14.101  40.004  1.00 43.61  ? 442 ILE A CD1   1 
ATOM   3241 N  N     . PHE A 1 416 ? 75.473  10.614  38.740  1.00 55.07  ? 443 PHE A N     1 
ATOM   3242 C  CA    . PHE A 1 416 ? 75.208  9.177   38.638  1.00 55.48  ? 443 PHE A CA    1 
ATOM   3243 C  C     . PHE A 1 416 ? 76.174  8.491   37.676  1.00 60.22  ? 443 PHE A C     1 
ATOM   3244 O  O     . PHE A 1 416 ? 75.810  7.523   37.005  1.00 59.96  ? 443 PHE A O     1 
ATOM   3245 C  CB    . PHE A 1 416 ? 73.759  8.909   38.221  1.00 50.27  ? 443 PHE A CB    1 
ATOM   3246 C  CG    . PHE A 1 416 ? 72.746  9.659   39.035  1.00 61.98  ? 443 PHE A CG    1 
ATOM   3247 C  CD1   . PHE A 1 416 ? 72.834  9.691   40.418  1.00 54.56  ? 443 PHE A CD1   1 
ATOM   3248 C  CD2   . PHE A 1 416 ? 71.715  10.347  38.417  1.00 55.50  ? 443 PHE A CD2   1 
ATOM   3249 C  CE1   . PHE A 1 416 ? 71.904  10.385  41.170  1.00 58.79  ? 443 PHE A CE1   1 
ATOM   3250 C  CE2   . PHE A 1 416 ? 70.783  11.046  39.162  1.00 48.21  ? 443 PHE A CE2   1 
ATOM   3251 C  CZ    . PHE A 1 416 ? 70.875  11.064  40.541  1.00 53.27  ? 443 PHE A CZ    1 
ATOM   3252 N  N     . PHE A 1 417 ? 77.415  8.983   37.618  1.00 57.12  ? 444 PHE A N     1 
ATOM   3253 C  CA    . PHE A 1 417 ? 78.374  8.496   36.630  1.00 51.86  ? 444 PHE A CA    1 
ATOM   3254 C  C     . PHE A 1 417 ? 78.631  7.002   36.790  1.00 54.94  ? 444 PHE A C     1 
ATOM   3255 O  O     . PHE A 1 417 ? 78.563  6.242   35.817  1.00 57.38  ? 444 PHE A O     1 
ATOM   3256 C  CB    . PHE A 1 417 ? 79.683  9.282   36.743  1.00 57.00  ? 444 PHE A CB    1 
ATOM   3257 C  CG    . PHE A 1 417 ? 80.838  8.650   36.013  1.00 59.06  ? 444 PHE A CG    1 
ATOM   3258 C  CD1   . PHE A 1 417 ? 80.980  8.811   34.645  1.00 51.99  ? 444 PHE A CD1   1 
ATOM   3259 C  CD2   . PHE A 1 417 ? 81.787  7.905   36.697  1.00 60.50  ? 444 PHE A CD2   1 
ATOM   3260 C  CE1   . PHE A 1 417 ? 82.043  8.234   33.971  1.00 58.19  ? 444 PHE A CE1   1 
ATOM   3261 C  CE2   . PHE A 1 417 ? 82.849  7.326   36.030  1.00 58.87  ? 444 PHE A CE2   1 
ATOM   3262 C  CZ    . PHE A 1 417 ? 82.978  7.492   34.665  1.00 62.10  ? 444 PHE A CZ    1 
ATOM   3263 N  N     . LYS A 1 418 ? 78.931  6.565   38.015  1.00 58.45  ? 445 LYS A N     1 
ATOM   3264 C  CA    . LYS A 1 418 ? 79.317  5.176   38.238  1.00 47.08  ? 445 LYS A CA    1 
ATOM   3265 C  C     . LYS A 1 418 ? 78.202  4.220   37.832  1.00 52.23  ? 445 LYS A C     1 
ATOM   3266 O  O     . LYS A 1 418 ? 78.433  3.261   37.087  1.00 61.89  ? 445 LYS A O     1 
ATOM   3267 C  CB    . LYS A 1 418 ? 79.703  4.971   39.703  1.00 49.64  ? 445 LYS A CB    1 
ATOM   3268 C  CG    . LYS A 1 418 ? 80.144  3.558   40.035  1.00 48.53  ? 445 LYS A CG    1 
ATOM   3269 C  CD    . LYS A 1 418 ? 80.725  3.480   41.434  1.00 56.61  ? 445 LYS A CD    1 
ATOM   3270 C  CE    . LYS A 1 418 ? 81.102  2.057   41.799  1.00 57.31  ? 445 LYS A CE    1 
ATOM   3271 N  NZ    . LYS A 1 418 ? 81.751  1.993   43.140  1.00 66.20  ? 445 LYS A NZ    1 
ATOM   3272 N  N     . ARG A 1 419 ? 76.979  4.473   38.303  1.00 58.92  ? 446 ARG A N     1 
ATOM   3273 C  CA    . ARG A 1 419 ? 75.866  3.594   37.959  1.00 57.78  ? 446 ARG A CA    1 
ATOM   3274 C  C     . ARG A 1 419 ? 75.551  3.649   36.469  1.00 60.56  ? 446 ARG A C     1 
ATOM   3275 O  O     . ARG A 1 419 ? 75.237  2.622   35.858  1.00 61.15  ? 446 ARG A O     1 
ATOM   3276 C  CB    . ARG A 1 419 ? 74.628  3.958   38.777  1.00 60.22  ? 446 ARG A CB    1 
ATOM   3277 C  CG    . ARG A 1 419 ? 74.701  3.548   40.235  1.00 73.32  ? 446 ARG A CG    1 
ATOM   3278 C  CD    . ARG A 1 419 ? 73.326  3.584   40.873  1.00 74.30  ? 446 ARG A CD    1 
ATOM   3279 N  NE    . ARG A 1 419 ? 72.888  4.937   41.176  1.00 60.28  ? 446 ARG A NE    1 
ATOM   3280 C  CZ    . ARG A 1 419 ? 71.638  5.271   41.458  1.00 72.13  ? 446 ARG A CZ    1 
ATOM   3281 N  NH1   . ARG A 1 419 ? 70.674  4.367   41.492  1.00 84.95  ? 446 ARG A NH1   1 
ATOM   3282 N  NH2   . ARG A 1 419 ? 71.347  6.546   41.699  1.00 82.28  ? 446 ARG A NH2   1 
ATOM   3283 N  N     . ARG A 1 420 ? 75.636  4.837   35.864  1.00 54.68  ? 447 ARG A N     1 
ATOM   3284 C  CA    . ARG A 1 420 ? 75.286  4.965   34.452  1.00 58.76  ? 447 ARG A CA    1 
ATOM   3285 C  C     . ARG A 1 420 ? 76.312  4.279   33.557  1.00 58.79  ? 447 ARG A C     1 
ATOM   3286 O  O     . ARG A 1 420 ? 75.945  3.661   32.552  1.00 61.75  ? 447 ARG A O     1 
ATOM   3287 C  CB    . ARG A 1 420 ? 75.134  6.439   34.075  1.00 58.74  ? 447 ARG A CB    1 
ATOM   3288 C  CG    . ARG A 1 420 ? 73.849  7.068   34.592  1.00 51.82  ? 447 ARG A CG    1 
ATOM   3289 C  CD    . ARG A 1 420 ? 73.925  8.586   34.595  1.00 56.03  ? 447 ARG A CD    1 
ATOM   3290 N  NE    . ARG A 1 420 ? 73.851  9.152   33.254  1.00 65.97  ? 447 ARG A NE    1 
ATOM   3291 C  CZ    . ARG A 1 420 ? 73.934  10.448  32.985  1.00 67.14  ? 447 ARG A CZ    1 
ATOM   3292 N  NH1   . ARG A 1 420 ? 74.108  11.344  33.944  1.00 48.95  ? 447 ARG A NH1   1 
ATOM   3293 N  NH2   . ARG A 1 420 ? 73.846  10.855  31.722  1.00 51.19  ? 447 ARG A NH2   1 
ATOM   3294 N  N     . LEU A 1 421 ? 77.598  4.364   33.906  1.00 55.32  ? 448 LEU A N     1 
ATOM   3295 C  CA    . LEU A 1 421 ? 78.615  3.687   33.105  1.00 49.64  ? 448 LEU A CA    1 
ATOM   3296 C  C     . LEU A 1 421 ? 78.561  2.179   33.309  1.00 62.11  ? 448 LEU A C     1 
ATOM   3297 O  O     . LEU A 1 421 ? 78.761  1.412   32.360  1.00 60.83  ? 448 LEU A O     1 
ATOM   3298 C  CB    . LEU A 1 421 ? 80.007  4.225   33.439  1.00 52.80  ? 448 LEU A CB    1 
ATOM   3299 C  CG    . LEU A 1 421 ? 81.158  3.598   32.645  1.00 61.50  ? 448 LEU A CG    1 
ATOM   3300 C  CD1   . LEU A 1 421 ? 80.901  3.701   31.149  1.00 51.92  ? 448 LEU A CD1   1 
ATOM   3301 C  CD2   . LEU A 1 421 ? 82.484  4.247   33.006  1.00 67.76  ? 448 LEU A CD2   1 
ATOM   3302 N  N     . MET A 1 422 ? 78.289  1.732   34.539  1.00 60.58  ? 449 MET A N     1 
ATOM   3303 C  CA    . MET A 1 422 ? 78.171  0.299   34.789  1.00 58.55  ? 449 MET A CA    1 
ATOM   3304 C  C     . MET A 1 422 ? 76.956  -0.282  34.079  1.00 55.56  ? 449 MET A C     1 
ATOM   3305 O  O     . MET A 1 422 ? 77.023  -1.387  33.529  1.00 60.47  ? 449 MET A O     1 
ATOM   3306 C  CB    . MET A 1 422 ? 78.098  0.023   36.291  1.00 54.26  ? 449 MET A CB    1 
ATOM   3307 C  CG    . MET A 1 422 ? 79.403  0.260   37.029  1.00 63.94  ? 449 MET A CG    1 
ATOM   3308 S  SD    . MET A 1 422 ? 79.325  -0.208  38.769  1.00 70.75  ? 449 MET A SD    1 
ATOM   3309 C  CE    . MET A 1 422 ? 79.309  -1.995  38.645  1.00 75.79  ? 449 MET A CE    1 
ATOM   3310 N  N     . ASN A 1 423 ? 75.839  0.448   34.076  1.00 53.17  ? 450 ASN A N     1 
ATOM   3311 C  CA    . ASN A 1 423 ? 74.648  -0.036  33.386  1.00 58.13  ? 450 ASN A CA    1 
ATOM   3312 C  C     . ASN A 1 423 ? 74.883  -0.143  31.886  1.00 65.96  ? 450 ASN A C     1 
ATOM   3313 O  O     . ASN A 1 423 ? 74.387  -1.072  31.239  1.00 72.55  ? 450 ASN A O     1 
ATOM   3314 C  CB    . ASN A 1 423 ? 73.457  0.878   33.677  1.00 51.24  ? 450 ASN A CB    1 
ATOM   3315 C  CG    . ASN A 1 423 ? 72.945  0.736   35.096  1.00 64.97  ? 450 ASN A CG    1 
ATOM   3316 O  OD1   . ASN A 1 423 ? 73.294  -0.210  35.804  1.00 68.50  ? 450 ASN A OD1   1 
ATOM   3317 N  ND2   . ASN A 1 423 ? 72.104  1.673   35.517  1.00 58.89  ? 450 ASN A ND2   1 
ATOM   3318 N  N     . LEU A 1 424 ? 75.639  0.798   31.313  1.00 63.43  ? 451 LEU A N     1 
ATOM   3319 C  CA    . LEU A 1 424 ? 75.911  0.752   29.880  1.00 63.37  ? 451 LEU A CA    1 
ATOM   3320 C  C     . LEU A 1 424 ? 76.731  -0.479  29.517  1.00 66.34  ? 451 LEU A C     1 
ATOM   3321 O  O     . LEU A 1 424 ? 76.399  -1.206  28.574  1.00 69.71  ? 451 LEU A O     1 
ATOM   3322 C  CB    . LEU A 1 424 ? 76.633  2.020   29.433  1.00 54.84  ? 451 LEU A CB    1 
ATOM   3323 C  CG    . LEU A 1 424 ? 77.072  1.959   27.969  1.00 68.56  ? 451 LEU A CG    1 
ATOM   3324 C  CD1   . LEU A 1 424 ? 75.866  2.031   27.045  1.00 57.25  ? 451 LEU A CD1   1 
ATOM   3325 C  CD2   . LEU A 1 424 ? 78.068  3.054   27.650  1.00 63.20  ? 451 LEU A CD2   1 
ATOM   3326 N  N     . MET A 1 425 ? 77.818  -0.721  30.256  1.00 58.52  ? 452 MET A N     1 
ATOM   3327 C  CA    . MET A 1 425 ? 78.639  -1.900  30.003  1.00 58.40  ? 452 MET A CA    1 
ATOM   3328 C  C     . MET A 1 425 ? 77.833  -3.178  30.183  1.00 69.54  ? 452 MET A C     1 
ATOM   3329 O  O     . MET A 1 425 ? 78.002  -4.142  29.427  1.00 79.52  ? 452 MET A O     1 
ATOM   3330 C  CB    . MET A 1 425 ? 79.856  -1.899  30.928  1.00 63.04  ? 452 MET A CB    1 
ATOM   3331 C  CG    . MET A 1 425 ? 80.769  -0.695  30.756  1.00 67.21  ? 452 MET A CG    1 
ATOM   3332 S  SD    . MET A 1 425 ? 81.312  -0.475  29.048  1.00 78.32  ? 452 MET A SD    1 
ATOM   3333 C  CE    . MET A 1 425 ? 82.117  -2.044  28.736  1.00 65.68  ? 452 MET A CE    1 
ATOM   3334 N  N     . ARG A 1 426 ? 76.946  -3.202  31.180  1.00 68.93  ? 453 ARG A N     1 
ATOM   3335 C  CA    . ARG A 1 426 ? 76.092  -4.366  31.387  1.00 64.80  ? 453 ARG A CA    1 
ATOM   3336 C  C     . ARG A 1 426 ? 75.181  -4.597  30.188  1.00 72.20  ? 453 ARG A C     1 
ATOM   3337 O  O     . ARG A 1 426 ? 74.964  -5.743  29.777  1.00 76.14  ? 453 ARG A O     1 
ATOM   3338 C  CB    . ARG A 1 426 ? 75.272  -4.188  32.664  1.00 74.28  ? 453 ARG A CB    1 
ATOM   3339 C  CG    . ARG A 1 426 ? 74.424  -5.391  33.043  1.00 86.01  ? 453 ARG A CG    1 
ATOM   3340 C  CD    . ARG A 1 426 ? 75.288  -6.596  33.366  1.00 94.80  ? 453 ARG A CD    1 
ATOM   3341 N  NE    . ARG A 1 426 ? 74.505  -7.690  33.927  1.00 98.36  ? 453 ARG A NE    1 
ATOM   3342 C  CZ    . ARG A 1 426 ? 74.273  -7.854  35.222  1.00 95.18  ? 453 ARG A CZ    1 
ATOM   3343 N  NH1   . ARG A 1 426 ? 74.756  -7.014  36.123  1.00 104.28 ? 453 ARG A NH1   1 
ATOM   3344 N  NH2   . ARG A 1 426 ? 73.537  -8.887  35.623  1.00 98.99  ? 453 ARG A NH2   1 
ATOM   3345 N  N     . ASP A 1 427 ? 74.639  -3.521  29.611  1.00 73.41  ? 454 ASP A N     1 
ATOM   3346 C  CA    . ASP A 1 427 ? 73.797  -3.667  28.427  1.00 72.99  ? 454 ASP A CA    1 
ATOM   3347 C  C     . ASP A 1 427 ? 74.619  -4.057  27.205  1.00 82.81  ? 454 ASP A C     1 
ATOM   3348 O  O     . ASP A 1 427 ? 74.141  -4.802  26.341  1.00 75.09  ? 454 ASP A O     1 
ATOM   3349 C  CB    . ASP A 1 427 ? 73.026  -2.374  28.160  1.00 69.23  ? 454 ASP A CB    1 
ATOM   3350 C  CG    . ASP A 1 427 ? 71.798  -2.233  29.038  1.00 93.12  ? 454 ASP A CG    1 
ATOM   3351 O  OD1   . ASP A 1 427 ? 71.655  -3.022  29.996  1.00 99.22  ? 454 ASP A OD1   1 
ATOM   3352 O  OD2   . ASP A 1 427 ? 70.971  -1.336  28.764  1.00 88.88  ? 454 ASP A OD2   1 
ATOM   3353 N  N     . VAL A 1 428 ? 75.856  -3.563  27.114  1.00 80.38  ? 455 VAL A N     1 
ATOM   3354 C  CA    . VAL A 1 428 ? 76.715  -3.905  25.982  1.00 72.83  ? 455 VAL A CA    1 
ATOM   3355 C  C     . VAL A 1 428 ? 77.040  -5.394  25.991  1.00 74.90  ? 455 VAL A C     1 
ATOM   3356 O  O     . VAL A 1 428 ? 76.912  -6.083  24.971  1.00 90.60  ? 455 VAL A O     1 
ATOM   3357 C  CB    . VAL A 1 428 ? 77.993  -3.046  25.997  1.00 73.15  ? 455 VAL A CB    1 
ATOM   3358 C  CG1   . VAL A 1 428 ? 79.065  -3.675  25.125  1.00 64.15  ? 455 VAL A CG1   1 
ATOM   3359 C  CG2   . VAL A 1 428 ? 77.685  -1.636  25.521  1.00 60.65  ? 455 VAL A CG2   1 
ATOM   3360 N  N     . GLU A 1 429 ? 77.455  -5.916  27.149  1.00 68.84  ? 456 GLU A N     1 
ATOM   3361 C  CA    . GLU A 1 429 ? 77.828  -7.324  27.225  1.00 76.62  ? 456 GLU A CA    1 
ATOM   3362 C  C     . GLU A 1 429 ? 76.616  -8.238  27.100  1.00 74.65  ? 456 GLU A C     1 
ATOM   3363 O  O     . GLU A 1 429 ? 76.747  -9.377  26.637  1.00 95.13  ? 456 GLU A O     1 
ATOM   3364 C  CB    . GLU A 1 429 ? 78.578  -7.601  28.528  1.00 83.97  ? 456 GLU A CB    1 
ATOM   3365 C  CG    . GLU A 1 429 ? 77.736  -7.466  29.787  1.00 106.29 ? 456 GLU A CG    1 
ATOM   3366 C  CD    . GLU A 1 429 ? 78.579  -7.449  31.048  1.00 113.56 ? 456 GLU A CD    1 
ATOM   3367 O  OE1   . GLU A 1 429 ? 79.798  -7.198  30.943  1.00 118.02 ? 456 GLU A OE1   1 
ATOM   3368 O  OE2   . GLU A 1 429 ? 78.026  -7.686  32.143  1.00 109.38 ? 456 GLU A OE2   1 
ATOM   3369 N  N     . ARG A 1 430 ? 75.435  -7.762  27.498  1.00 87.03  ? 457 ARG A N     1 
ATOM   3370 C  CA    . ARG A 1 430 ? 74.235  -8.587  27.401  1.00 83.64  ? 457 ARG A CA    1 
ATOM   3371 C  C     . ARG A 1 430 ? 73.786  -8.755  25.955  1.00 83.72  ? 457 ARG A C     1 
ATOM   3372 O  O     . ARG A 1 430 ? 73.172  -9.772  25.611  1.00 90.04  ? 457 ARG A O     1 
ATOM   3373 C  CB    . ARG A 1 430 ? 73.117  -7.977  28.245  1.00 78.63  ? 457 ARG A CB    1 
ATOM   3374 C  CG    . ARG A 1 430 ? 71.930  -8.889  28.501  1.00 69.07  ? 457 ARG A CG    1 
ATOM   3375 C  CD    . ARG A 1 430 ? 71.404  -8.660  29.907  1.00 71.64  ? 457 ARG A CD    1 
ATOM   3376 N  NE    . ARG A 1 430 ? 71.411  -7.244  30.252  1.00 84.76  ? 457 ARG A NE    1 
ATOM   3377 C  CZ    . ARG A 1 430 ? 71.389  -6.771  31.491  1.00 75.08  ? 457 ARG A CZ    1 
ATOM   3378 N  NH1   . ARG A 1 430 ? 71.371  -7.578  32.539  1.00 90.42  ? 457 ARG A NH1   1 
ATOM   3379 N  NH2   . ARG A 1 430 ? 71.391  -5.455  31.683  1.00 65.62  ? 457 ARG A NH2   1 
ATOM   3380 N  N     . GLU A 1 431 ? 74.085  -7.782  25.098  1.00 90.05  ? 458 GLU A N     1 
ATOM   3381 C  CA    . GLU A 1 431 ? 73.710  -7.839  23.692  1.00 97.61  ? 458 GLU A CA    1 
ATOM   3382 C  C     . GLU A 1 431 ? 74.811  -8.403  22.804  1.00 97.96  ? 458 GLU A C     1 
ATOM   3383 O  O     . GLU A 1 431 ? 74.594  -8.553  21.597  1.00 89.96  ? 458 GLU A O     1 
ATOM   3384 C  CB    . GLU A 1 431 ? 73.316  -6.445  23.197  1.00 97.50  ? 458 GLU A CB    1 
ATOM   3385 C  CG    . GLU A 1 431 ? 72.113  -5.859  23.917  1.00 117.62 ? 458 GLU A CG    1 
ATOM   3386 C  CD    . GLU A 1 431 ? 70.828  -6.603  23.610  1.00 123.73 ? 458 GLU A CD    1 
ATOM   3387 O  OE1   . GLU A 1 431 ? 70.742  -7.223  22.528  1.00 107.90 ? 458 GLU A OE1   1 
ATOM   3388 O  OE2   . GLU A 1 431 ? 69.903  -6.565  24.451  1.00 129.82 ? 458 GLU A OE2   1 
ATOM   3389 N  N     . GLY A 1 432 ? 75.976  -8.715  23.366  1.00 98.26  ? 459 GLY A N     1 
ATOM   3390 C  CA    . GLY A 1 432 ? 77.061  -9.270  22.576  1.00 98.26  ? 459 GLY A CA    1 
ATOM   3391 C  C     . GLY A 1 432 ? 77.593  -8.340  21.511  1.00 88.33  ? 459 GLY A C     1 
ATOM   3392 O  O     . GLY A 1 432 ? 77.989  -8.802  20.435  1.00 86.09  ? 459 GLY A O     1 
ATOM   3393 N  N     . LEU A 1 433 ? 77.611  -7.038  21.777  1.00 86.58  ? 460 LEU A N     1 
ATOM   3394 C  CA    . LEU A 1 433 ? 78.096  -6.078  20.795  1.00 79.35  ? 460 LEU A CA    1 
ATOM   3395 C  C     . LEU A 1 433 ? 79.597  -6.236  20.592  1.00 88.58  ? 460 LEU A C     1 
ATOM   3396 O  O     . LEU A 1 433 ? 80.364  -6.289  21.558  1.00 89.39  ? 460 LEU A O     1 
ATOM   3397 C  CB    . LEU A 1 433 ? 77.773  -4.653  21.243  1.00 80.65  ? 460 LEU A CB    1 
ATOM   3398 C  CG    . LEU A 1 433 ? 78.365  -3.530  20.388  1.00 86.08  ? 460 LEU A CG    1 
ATOM   3399 C  CD1   . LEU A 1 433 ? 77.840  -3.602  18.962  1.00 95.95  ? 460 LEU A CD1   1 
ATOM   3400 C  CD2   . LEU A 1 433 ? 78.071  -2.173  21.004  1.00 78.78  ? 460 LEU A CD2   1 
ATOM   3401 N  N     . ASP A 1 434 ? 80.014  -6.311  19.331  1.00 92.12  ? 461 ASP A N     1 
ATOM   3402 C  CA    . ASP A 1 434 ? 81.433  -6.345  18.985  1.00 82.36  ? 461 ASP A CA    1 
ATOM   3403 C  C     . ASP A 1 434 ? 81.953  -4.914  19.016  1.00 87.80  ? 461 ASP A C     1 
ATOM   3404 O  O     . ASP A 1 434 ? 81.830  -4.175  18.038  1.00 100.72 ? 461 ASP A O     1 
ATOM   3405 C  CB    . ASP A 1 434 ? 81.635  -6.984  17.616  1.00 92.16  ? 461 ASP A CB    1 
ATOM   3406 C  CG    . ASP A 1 434 ? 83.094  -7.043  17.205  1.00 109.20 ? 461 ASP A CG    1 
ATOM   3407 O  OD1   . ASP A 1 434 ? 83.973  -6.836  18.070  1.00 108.23 ? 461 ASP A OD1   1 
ATOM   3408 O  OD2   . ASP A 1 434 ? 83.362  -7.294  16.011  1.00 118.03 ? 461 ASP A OD2   1 
ATOM   3409 N  N     . TRP A 1 435 ? 82.536  -4.517  20.144  1.00 88.70  ? 462 TRP A N     1 
ATOM   3410 C  CA    . TRP A 1 435 ? 83.001  -3.152  20.345  1.00 88.23  ? 462 TRP A CA    1 
ATOM   3411 C  C     . TRP A 1 435 ? 84.506  -3.134  20.577  1.00 82.83  ? 462 TRP A C     1 
ATOM   3412 O  O     . TRP A 1 435 ? 85.063  -4.047  21.197  1.00 75.11  ? 462 TRP A O     1 
ATOM   3413 C  CB    . TRP A 1 435 ? 82.279  -2.489  21.528  1.00 86.22  ? 462 TRP A CB    1 
ATOM   3414 C  CG    . TRP A 1 435 ? 82.648  -3.060  22.864  1.00 78.86  ? 462 TRP A CG    1 
ATOM   3415 C  CD1   . TRP A 1 435 ? 82.069  -4.124  23.492  1.00 68.27  ? 462 TRP A CD1   1 
ATOM   3416 C  CD2   . TRP A 1 435 ? 83.681  -2.592  23.737  1.00 80.96  ? 462 TRP A CD2   1 
ATOM   3417 N  NE1   . TRP A 1 435 ? 82.680  -4.348  24.703  1.00 73.16  ? 462 TRP A NE1   1 
ATOM   3418 C  CE2   . TRP A 1 435 ? 83.674  -3.421  24.876  1.00 69.76  ? 462 TRP A CE2   1 
ATOM   3419 C  CE3   . TRP A 1 435 ? 84.614  -1.553  23.665  1.00 86.21  ? 462 TRP A CE3   1 
ATOM   3420 C  CZ2   . TRP A 1 435 ? 84.562  -3.243  25.934  1.00 67.19  ? 462 TRP A CZ2   1 
ATOM   3421 C  CZ3   . TRP A 1 435 ? 85.493  -1.377  24.717  1.00 81.04  ? 462 TRP A CZ3   1 
ATOM   3422 C  CH2   . TRP A 1 435 ? 85.463  -2.219  25.834  1.00 78.42  ? 462 TRP A CH2   1 
ATOM   3423 N  N     . ASP A 1 436 ? 85.155  -2.089  20.068  1.00 84.77  ? 463 ASP A N     1 
ATOM   3424 C  CA    . ASP A 1 436 ? 86.573  -1.831  20.293  1.00 85.85  ? 463 ASP A CA    1 
ATOM   3425 C  C     . ASP A 1 436 ? 86.824  -0.599  21.146  1.00 83.79  ? 463 ASP A C     1 
ATOM   3426 O  O     . ASP A 1 436 ? 87.731  -0.604  21.981  1.00 79.00  ? 463 ASP A O     1 
ATOM   3427 C  CB    . ASP A 1 436 ? 87.300  -1.664  18.954  1.00 92.41  ? 463 ASP A CB    1 
ATOM   3428 C  CG    . ASP A 1 436 ? 87.283  -2.926  18.118  1.00 108.53 ? 463 ASP A CG    1 
ATOM   3429 O  OD1   . ASP A 1 436 ? 87.307  -4.029  18.703  1.00 104.70 ? 463 ASP A OD1   1 
ATOM   3430 O  OD2   . ASP A 1 436 ? 87.246  -2.815  16.874  1.00 108.25 ? 463 ASP A OD2   1 
ATOM   3431 N  N     . LEU A 1 437 ? 86.029  0.452   20.959  1.00 81.30  ? 464 LEU A N     1 
ATOM   3432 C  CA    . LEU A 1 437 ? 86.228  1.727   21.632  1.00 75.34  ? 464 LEU A CA    1 
ATOM   3433 C  C     . LEU A 1 437 ? 84.872  2.315   21.986  1.00 72.74  ? 464 LEU A C     1 
ATOM   3434 O  O     . LEU A 1 437 ? 83.959  2.311   21.155  1.00 67.24  ? 464 LEU A O     1 
ATOM   3435 C  CB    . LEU A 1 437 ? 87.012  2.694   20.737  1.00 76.41  ? 464 LEU A CB    1 
ATOM   3436 C  CG    . LEU A 1 437 ? 87.178  4.132   21.224  1.00 78.25  ? 464 LEU A CG    1 
ATOM   3437 C  CD1   . LEU A 1 437 ? 88.095  4.175   22.428  1.00 73.83  ? 464 LEU A CD1   1 
ATOM   3438 C  CD2   . LEU A 1 437 ? 87.707  5.020   20.108  1.00 78.26  ? 464 LEU A CD2   1 
ATOM   3439 N  N     . ILE A 1 438 ? 84.735  2.814   23.212  1.00 70.30  ? 465 ILE A N     1 
ATOM   3440 C  CA    . ILE A 1 438 ? 83.503  3.450   23.667  1.00 66.29  ? 465 ILE A CA    1 
ATOM   3441 C  C     . ILE A 1 438 ? 83.875  4.790   24.285  1.00 60.04  ? 465 ILE A C     1 
ATOM   3442 O  O     . ILE A 1 438 ? 84.475  4.833   25.366  1.00 67.43  ? 465 ILE A O     1 
ATOM   3443 C  CB    . ILE A 1 438 ? 82.729  2.583   24.669  1.00 67.60  ? 465 ILE A CB    1 
ATOM   3444 C  CG1   . ILE A 1 438 ? 82.393  1.223   24.056  1.00 63.83  ? 465 ILE A CG1   1 
ATOM   3445 C  CG2   . ILE A 1 438 ? 81.452  3.283   25.099  1.00 64.90  ? 465 ILE A CG2   1 
ATOM   3446 C  CD1   . ILE A 1 438 ? 81.598  0.320   24.974  1.00 70.92  ? 465 ILE A CD1   1 
ATOM   3447 N  N     . TYR A 1 439 ? 83.526  5.880   23.604  1.00 60.06  ? 466 TYR A N     1 
ATOM   3448 C  CA    . TYR A 1 439 ? 83.769  7.211   24.143  1.00 60.55  ? 466 TYR A CA    1 
ATOM   3449 C  C     . TYR A 1 439 ? 82.904  7.449   25.373  1.00 66.28  ? 466 TYR A C     1 
ATOM   3450 O  O     . TYR A 1 439 ? 81.692  7.219   25.345  1.00 60.88  ? 466 TYR A O     1 
ATOM   3451 C  CB    . TYR A 1 439 ? 83.465  8.282   23.095  1.00 66.55  ? 466 TYR A CB    1 
ATOM   3452 C  CG    . TYR A 1 439 ? 84.518  8.463   22.027  1.00 81.06  ? 466 TYR A CG    1 
ATOM   3453 C  CD1   . TYR A 1 439 ? 85.724  9.092   22.311  1.00 74.60  ? 466 TYR A CD1   1 
ATOM   3454 C  CD2   . TYR A 1 439 ? 84.294  8.033   20.727  1.00 71.90  ? 466 TYR A CD2   1 
ATOM   3455 C  CE1   . TYR A 1 439 ? 86.684  9.270   21.334  1.00 70.15  ? 466 TYR A CE1   1 
ATOM   3456 C  CE2   . TYR A 1 439 ? 85.248  8.207   19.742  1.00 72.88  ? 466 TYR A CE2   1 
ATOM   3457 C  CZ    . TYR A 1 439 ? 86.441  8.827   20.052  1.00 78.77  ? 466 TYR A CZ    1 
ATOM   3458 O  OH    . TYR A 1 439 ? 87.394  9.003   19.075  1.00 94.87  ? 466 TYR A OH    1 
ATOM   3459 N  N     . VAL A 1 440 ? 83.526  7.913   26.452  1.00 61.23  ? 467 VAL A N     1 
ATOM   3460 C  CA    . VAL A 1 440 ? 82.801  8.411   27.612  1.00 63.28  ? 467 VAL A CA    1 
ATOM   3461 C  C     . VAL A 1 440 ? 82.788  9.934   27.641  1.00 64.66  ? 467 VAL A C     1 
ATOM   3462 O  O     . VAL A 1 440 ? 81.785  10.545  28.010  1.00 72.93  ? 467 VAL A O     1 
ATOM   3463 C  CB    . VAL A 1 440 ? 83.401  7.831   28.911  1.00 68.60  ? 467 VAL A CB    1 
ATOM   3464 C  CG1   . VAL A 1 440 ? 82.663  8.366   30.130  1.00 70.68  ? 467 VAL A CG1   1 
ATOM   3465 C  CG2   . VAL A 1 440 ? 83.349  6.312   28.881  1.00 58.41  ? 467 VAL A CG2   1 
ATOM   3466 N  N     . GLY A 1 441 ? 83.895  10.554  27.239  1.00 72.77  ? 468 GLY A N     1 
ATOM   3467 C  CA    . GLY A 1 441 ? 83.970  11.990  27.067  1.00 69.38  ? 468 GLY A CA    1 
ATOM   3468 C  C     . GLY A 1 441 ? 84.657  12.346  25.765  1.00 84.41  ? 468 GLY A C     1 
ATOM   3469 O  O     . GLY A 1 441 ? 85.790  11.920  25.520  1.00 93.87  ? 468 GLY A O     1 
ATOM   3470 N  N     . ARG A 1 442 ? 83.982  13.117  24.916  1.00 78.98  ? 469 ARG A N     1 
ATOM   3471 C  CA    . ARG A 1 442 ? 84.505  13.454  23.600  1.00 72.49  ? 469 ARG A CA    1 
ATOM   3472 C  C     . ARG A 1 442 ? 83.903  14.779  23.153  1.00 70.90  ? 469 ARG A C     1 
ATOM   3473 O  O     . ARG A 1 442 ? 83.056  15.362  23.836  1.00 73.85  ? 469 ARG A O     1 
ATOM   3474 C  CB    . ARG A 1 442 ? 84.192  12.352  22.584  1.00 76.71  ? 469 ARG A CB    1 
ATOM   3475 C  CG    . ARG A 1 442 ? 82.702  12.096  22.436  1.00 74.59  ? 469 ARG A CG    1 
ATOM   3476 C  CD    . ARG A 1 442 ? 82.351  11.442  21.113  1.00 63.18  ? 469 ARG A CD    1 
ATOM   3477 N  NE    . ARG A 1 442 ? 80.907  11.399  20.918  1.00 73.22  ? 469 ARG A NE    1 
ATOM   3478 C  CZ    . ARG A 1 442 ? 80.309  11.074  19.780  1.00 76.45  ? 469 ARG A CZ    1 
ATOM   3479 N  NH1   . ARG A 1 442 ? 81.004  10.750  18.702  1.00 89.82  ? 469 ARG A NH1   1 
ATOM   3480 N  NH2   . ARG A 1 442 ? 78.980  11.077  19.721  1.00 73.54  ? 469 ARG A NH2   1 
ATOM   3481 N  N     . LYS A 1 443 ? 84.346  15.252  21.989  1.00 85.45  ? 470 LYS A N     1 
ATOM   3482 C  CA    . LYS A 1 443 ? 83.744  16.399  21.316  1.00 71.60  ? 470 LYS A CA    1 
ATOM   3483 C  C     . LYS A 1 443 ? 83.088  15.893  20.037  1.00 79.48  ? 470 LYS A C     1 
ATOM   3484 O  O     . LYS A 1 443 ? 83.778  15.552  19.071  1.00 94.77  ? 470 LYS A O     1 
ATOM   3485 C  CB    . LYS A 1 443 ? 84.777  17.482  21.012  1.00 74.42  ? 470 LYS A CB    1 
ATOM   3486 C  CG    . LYS A 1 443 ? 84.166  18.778  20.503  1.00 70.24  ? 470 LYS A CG    1 
ATOM   3487 C  CD    . LYS A 1 443 ? 85.141  19.938  20.621  1.00 88.63  ? 470 LYS A CD    1 
ATOM   3488 C  CE    . LYS A 1 443 ? 84.561  21.214  20.028  1.00 79.14  ? 470 LYS A CE    1 
ATOM   3489 N  NZ    . LYS A 1 443 ? 84.345  21.093  18.560  1.00 89.72  ? 470 LYS A NZ    1 
ATOM   3490 N  N     . ARG A 1 444 ? 81.760  15.839  20.036  1.00 84.15  ? 471 ARG A N     1 
ATOM   3491 C  CA    . ARG A 1 444 ? 81.030  15.345  18.877  1.00 73.79  ? 471 ARG A CA    1 
ATOM   3492 C  C     . ARG A 1 444 ? 81.040  16.386  17.762  1.00 78.88  ? 471 ARG A C     1 
ATOM   3493 O  O     . ARG A 1 444 ? 80.665  17.543  17.976  1.00 83.49  ? 471 ARG A O     1 
ATOM   3494 C  CB    . ARG A 1 444 ? 79.598  14.998  19.279  1.00 63.84  ? 471 ARG A CB    1 
ATOM   3495 C  CG    . ARG A 1 444 ? 78.663  14.743  18.121  1.00 81.36  ? 471 ARG A CG    1 
ATOM   3496 C  CD    . ARG A 1 444 ? 77.239  14.574  18.618  1.00 67.02  ? 471 ARG A CD    1 
ATOM   3497 N  NE    . ARG A 1 444 ? 76.278  14.561  17.523  1.00 84.08  ? 471 ARG A NE    1 
ATOM   3498 C  CZ    . ARG A 1 444 ? 74.964  14.485  17.680  1.00 91.18  ? 471 ARG A CZ    1 
ATOM   3499 N  NH1   . ARG A 1 444 ? 74.415  14.403  18.881  1.00 78.37  ? 471 ARG A NH1   1 
ATOM   3500 N  NH2   . ARG A 1 444 ? 74.180  14.495  16.605  1.00 98.08  ? 471 ARG A NH2   1 
ATOM   3501 N  N     . MET A 1 445 ? 81.475  15.977  16.571  1.00 77.43  ? 472 MET A N     1 
ATOM   3502 C  CA    . MET A 1 445 ? 81.580  16.889  15.438  1.00 73.29  ? 472 MET A CA    1 
ATOM   3503 C  C     . MET A 1 445 ? 80.415  16.783  14.465  1.00 81.98  ? 472 MET A C     1 
ATOM   3504 O  O     . MET A 1 445 ? 80.032  17.795  13.868  1.00 98.12  ? 472 MET A O     1 
ATOM   3505 C  CB    . MET A 1 445 ? 82.892  16.651  14.681  1.00 87.50  ? 472 MET A CB    1 
ATOM   3506 C  CG    . MET A 1 445 ? 84.134  16.821  15.542  1.00 98.31  ? 472 MET A CG    1 
ATOM   3507 S  SD    . MET A 1 445 ? 84.248  18.454  16.300  1.00 103.56 ? 472 MET A SD    1 
ATOM   3508 C  CE    . MET A 1 445 ? 84.594  19.473  14.869  1.00 84.37  ? 472 MET A CE    1 
ATOM   3509 N  N     . GLN A 1 446 ? 79.849  15.593  14.280  1.00 75.09  ? 473 GLN A N     1 
ATOM   3510 C  CA    . GLN A 1 446 ? 78.630  15.435  13.488  1.00 78.37  ? 473 GLN A CA    1 
ATOM   3511 C  C     . GLN A 1 446 ? 77.461  15.925  14.334  1.00 86.07  ? 473 GLN A C     1 
ATOM   3512 O  O     . GLN A 1 446 ? 76.962  15.211  15.208  1.00 79.81  ? 473 GLN A O     1 
ATOM   3513 C  CB    . GLN A 1 446 ? 78.454  13.984  13.047  1.00 84.58  ? 473 GLN A CB    1 
ATOM   3514 C  CG    . GLN A 1 446 ? 77.048  13.603  12.575  1.00 77.03  ? 473 GLN A CG    1 
ATOM   3515 C  CD    . GLN A 1 446 ? 76.414  14.636  11.664  1.00 95.47  ? 473 GLN A CD    1 
ATOM   3516 O  OE1   . GLN A 1 446 ? 75.306  15.101  11.926  1.00 108.45 ? 473 GLN A OE1   1 
ATOM   3517 N  NE2   . GLN A 1 446 ? 77.108  14.995  10.589  1.00 118.57 ? 473 GLN A NE2   1 
ATOM   3518 N  N     . VAL A 1 447 ? 77.027  17.157  14.079  1.00 89.07  ? 474 VAL A N     1 
ATOM   3519 C  CA    . VAL A 1 447 ? 75.967  17.787  14.858  1.00 89.91  ? 474 VAL A CA    1 
ATOM   3520 C  C     . VAL A 1 447 ? 74.752  18.163  14.026  1.00 82.90  ? 474 VAL A C     1 
ATOM   3521 O  O     . VAL A 1 447 ? 73.742  18.592  14.603  1.00 81.51  ? 474 VAL A O     1 
ATOM   3522 C  CB    . VAL A 1 447 ? 76.486  19.032  15.613  1.00 72.10  ? 474 VAL A CB    1 
ATOM   3523 C  CG1   . VAL A 1 447 ? 77.548  18.637  16.629  1.00 76.57  ? 474 VAL A CG1   1 
ATOM   3524 C  CG2   . VAL A 1 447 ? 77.035  20.056  14.630  1.00 85.61  ? 474 VAL A CG2   1 
ATOM   3525 N  N     . GLU A 1 448 ? 74.804  18.028  12.698  1.00 77.40  ? 475 GLU A N     1 
ATOM   3526 C  CA    . GLU A 1 448 ? 73.646  18.392  11.888  1.00 91.71  ? 475 GLU A CA    1 
ATOM   3527 C  C     . GLU A 1 448 ? 72.501  17.403  12.068  1.00 90.22  ? 475 GLU A C     1 
ATOM   3528 O  O     . GLU A 1 448 ? 71.333  17.792  11.974  1.00 88.86  ? 475 GLU A O     1 
ATOM   3529 C  CB    . GLU A 1 448 ? 74.034  18.496  10.408  1.00 92.28  ? 475 GLU A CB    1 
ATOM   3530 C  CG    . GLU A 1 448 ? 74.484  17.188  9.776   1.00 114.58 ? 475 GLU A CG    1 
ATOM   3531 C  CD    . GLU A 1 448 ? 74.993  17.358  8.358   1.00 129.10 ? 475 GLU A CD    1 
ATOM   3532 O  OE1   . GLU A 1 448 ? 74.360  18.106  7.582   1.00 102.57 ? 475 GLU A OE1   1 
ATOM   3533 O  OE2   . GLU A 1 448 ? 76.030  16.744  8.023   1.00 128.06 ? 475 GLU A OE2   1 
ATOM   3534 N  N     . HIS A 1 449 ? 72.807  16.141  12.337  1.00 96.57  ? 476 HIS A N     1 
ATOM   3535 C  CA    . HIS A 1 449 ? 71.805  15.106  12.532  1.00 91.01  ? 476 HIS A CA    1 
ATOM   3536 C  C     . HIS A 1 449 ? 72.289  14.156  13.614  1.00 91.64  ? 476 HIS A C     1 
ATOM   3537 O  O     . HIS A 1 449 ? 73.495  14.049  13.861  1.00 90.07  ? 476 HIS A O     1 
ATOM   3538 C  CB    . HIS A 1 449 ? 71.521  14.333  11.233  1.00 95.88  ? 476 HIS A CB    1 
ATOM   3539 C  CG    . HIS A 1 449 ? 72.679  13.523  10.737  1.00 99.44  ? 476 HIS A CG    1 
ATOM   3540 N  ND1   . HIS A 1 449 ? 73.002  12.286  11.254  1.00 103.11 ? 476 HIS A ND1   1 
ATOM   3541 C  CD2   . HIS A 1 449 ? 73.584  13.769  9.760   1.00 98.92  ? 476 HIS A CD2   1 
ATOM   3542 C  CE1   . HIS A 1 449 ? 74.060  11.809  10.623  1.00 110.49 ? 476 HIS A CE1   1 
ATOM   3543 N  NE2   . HIS A 1 449 ? 74.432  12.689  9.712   1.00 110.92 ? 476 HIS A NE2   1 
ATOM   3544 N  N     . PRO A 1 450 ? 71.372  13.461  14.287  1.00 93.58  ? 477 PRO A N     1 
ATOM   3545 C  CA    . PRO A 1 450 ? 71.791  12.526  15.339  1.00 74.30  ? 477 PRO A CA    1 
ATOM   3546 C  C     . PRO A 1 450 ? 72.617  11.380  14.775  1.00 77.86  ? 477 PRO A C     1 
ATOM   3547 O  O     . PRO A 1 450 ? 72.458  10.978  13.620  1.00 93.30  ? 477 PRO A O     1 
ATOM   3548 C  CB    . PRO A 1 450 ? 70.462  12.024  15.918  1.00 68.37  ? 477 PRO A CB    1 
ATOM   3549 C  CG    . PRO A 1 450 ? 69.458  12.274  14.843  1.00 79.65  ? 477 PRO A CG    1 
ATOM   3550 C  CD    . PRO A 1 450 ? 69.904  13.534  14.173  1.00 80.28  ? 477 PRO A CD    1 
ATOM   3551 N  N     . GLU A 1 451 ? 73.512  10.862  15.608  1.00 80.77  ? 478 GLU A N     1 
ATOM   3552 C  CA    . GLU A 1 451 ? 74.350  9.747   15.212  1.00 85.29  ? 478 GLU A CA    1 
ATOM   3553 C  C     . GLU A 1 451 ? 73.564  8.442   15.299  1.00 84.01  ? 478 GLU A C     1 
ATOM   3554 O  O     . GLU A 1 451 ? 72.550  8.344   15.994  1.00 80.78  ? 478 GLU A O     1 
ATOM   3555 C  CB    . GLU A 1 451 ? 75.607  9.683   16.082  1.00 91.35  ? 478 GLU A CB    1 
ATOM   3556 C  CG    . GLU A 1 451 ? 76.441  10.959  16.031  1.00 88.82  ? 478 GLU A CG    1 
ATOM   3557 C  CD    . GLU A 1 451 ? 77.768  10.831  16.755  1.00 88.14  ? 478 GLU A CD    1 
ATOM   3558 O  OE1   . GLU A 1 451 ? 77.993  9.793   17.409  1.00 106.61 ? 478 GLU A OE1   1 
ATOM   3559 O  OE2   . GLU A 1 451 ? 78.588  11.770  16.666  1.00 92.64  ? 478 GLU A OE2   1 
ATOM   3560 N  N     . LYS A 1 452 ? 74.049  7.432   14.576  1.00 88.66  ? 479 LYS A N     1 
ATOM   3561 C  CA    . LYS A 1 452 ? 73.307  6.186   14.416  1.00 81.26  ? 479 LYS A CA    1 
ATOM   3562 C  C     . LYS A 1 452 ? 73.209  5.445   15.745  1.00 87.73  ? 479 LYS A C     1 
ATOM   3563 O  O     . LYS A 1 452 ? 74.226  5.163   16.387  1.00 84.93  ? 479 LYS A O     1 
ATOM   3564 C  CB    . LYS A 1 452 ? 73.969  5.306   13.361  1.00 82.86  ? 479 LYS A CB    1 
ATOM   3565 C  CG    . LYS A 1 452 ? 73.225  4.005   13.110  1.00 85.56  ? 479 LYS A CG    1 
ATOM   3566 C  CD    . LYS A 1 452 ? 73.800  3.240   11.932  1.00 89.63  ? 479 LYS A CD    1 
ATOM   3567 C  CE    . LYS A 1 452 ? 73.041  1.943   11.695  1.00 85.61  ? 479 LYS A CE    1 
ATOM   3568 N  NZ    . LYS A 1 452 ? 73.600  1.172   10.549  1.00 94.08  ? 479 LYS A NZ    1 
ATOM   3569 N  N     . ALA A 1 453 ? 71.985  5.122   16.151  1.00 85.95  ? 480 ALA A N     1 
ATOM   3570 C  CA    . ALA A 1 453 ? 71.773  4.434   17.415  1.00 72.86  ? 480 ALA A CA    1 
ATOM   3571 C  C     . ALA A 1 453 ? 72.131  2.957   17.292  1.00 89.61  ? 480 ALA A C     1 
ATOM   3572 O  O     . ALA A 1 453 ? 72.017  2.350   16.225  1.00 94.01  ? 480 ALA A O     1 
ATOM   3573 C  CB    . ALA A 1 453 ? 70.319  4.582   17.866  1.00 66.34  ? 480 ALA A CB    1 
ATOM   3574 N  N     . VAL A 1 454 ? 72.570  2.384   18.407  1.00 82.53  ? 481 VAL A N     1 
ATOM   3575 C  CA    . VAL A 1 454 ? 72.913  0.968   18.480  1.00 82.37  ? 481 VAL A CA    1 
ATOM   3576 C  C     . VAL A 1 454 ? 71.657  0.203   18.884  1.00 84.89  ? 481 VAL A C     1 
ATOM   3577 O  O     . VAL A 1 454 ? 71.105  0.473   19.963  1.00 87.68  ? 481 VAL A O     1 
ATOM   3578 C  CB    . VAL A 1 454 ? 74.053  0.713   19.473  1.00 83.19  ? 481 VAL A CB    1 
ATOM   3579 C  CG1   . VAL A 1 454 ? 74.307  -0.780  19.611  1.00 73.55  ? 481 VAL A CG1   1 
ATOM   3580 C  CG2   . VAL A 1 454 ? 75.312  1.430   19.021  1.00 76.22  ? 481 VAL A CG2   1 
ATOM   3581 N  N     . PRO A 1 455 ? 71.173  -0.731  18.067  1.00 90.05  ? 482 PRO A N     1 
ATOM   3582 C  CA    . PRO A 1 455 ? 69.947  -1.454  18.420  1.00 91.37  ? 482 PRO A CA    1 
ATOM   3583 C  C     . PRO A 1 455 ? 70.119  -2.261  19.698  1.00 95.91  ? 482 PRO A C     1 
ATOM   3584 O  O     . PRO A 1 455 ? 71.149  -2.903  19.917  1.00 90.86  ? 482 PRO A O     1 
ATOM   3585 C  CB    . PRO A 1 455 ? 69.710  -2.365  17.209  1.00 94.59  ? 482 PRO A CB    1 
ATOM   3586 C  CG    . PRO A 1 455 ? 70.453  -1.712  16.088  1.00 86.23  ? 482 PRO A CG    1 
ATOM   3587 C  CD    . PRO A 1 455 ? 71.657  -1.084  16.721  1.00 91.11  ? 482 PRO A CD    1 
ATOM   3588 N  N     . ARG A 1 456 ? 69.095  -2.203  20.551  1.00 90.81  ? 483 ARG A N     1 
ATOM   3589 C  CA    . ARG A 1 456 ? 68.969  -2.978  21.784  1.00 86.14  ? 483 ARG A CA    1 
ATOM   3590 C  C     . ARG A 1 456 ? 69.950  -2.555  22.871  1.00 80.58  ? 483 ARG A C     1 
ATOM   3591 O  O     . ARG A 1 456 ? 70.081  -3.260  23.880  1.00 88.84  ? 483 ARG A O     1 
ATOM   3592 C  CB    . ARG A 1 456 ? 69.121  -4.481  21.519  1.00 93.52  ? 483 ARG A CB    1 
ATOM   3593 C  CG    . ARG A 1 456 ? 68.073  -5.053  20.581  1.00 95.26  ? 483 ARG A CG    1 
ATOM   3594 C  CD    . ARG A 1 456 ? 68.452  -6.449  20.111  1.00 91.70  ? 483 ARG A CD    1 
ATOM   3595 N  NE    . ARG A 1 456 ? 69.356  -6.419  18.967  1.00 103.25 ? 483 ARG A NE    1 
ATOM   3596 C  CZ    . ARG A 1 456 ? 70.678  -6.502  19.046  1.00 112.96 ? 483 ARG A CZ    1 
ATOM   3597 N  NH1   . ARG A 1 456 ? 71.297  -6.618  20.210  1.00 108.97 ? 483 ARG A NH1   1 
ATOM   3598 N  NH2   . ARG A 1 456 ? 71.397  -6.471  17.927  1.00 103.07 ? 483 ARG A NH2   1 
ATOM   3599 N  N     . VAL A 1 457 ? 70.643  -1.430  22.705  1.00 76.61  ? 484 VAL A N     1 
ATOM   3600 C  CA    . VAL A 1 457 ? 71.561  -0.901  23.714  1.00 81.56  ? 484 VAL A CA    1 
ATOM   3601 C  C     . VAL A 1 457 ? 71.227  0.576   23.889  1.00 78.26  ? 484 VAL A C     1 
ATOM   3602 O  O     . VAL A 1 457 ? 71.581  1.403   23.041  1.00 78.44  ? 484 VAL A O     1 
ATOM   3603 C  CB    . VAL A 1 457 ? 73.034  -1.089  23.333  1.00 81.45  ? 484 VAL A CB    1 
ATOM   3604 C  CG1   . VAL A 1 457 ? 73.938  -0.547  24.430  1.00 69.87  ? 484 VAL A CG1   1 
ATOM   3605 C  CG2   . VAL A 1 457 ? 73.339  -2.553  23.070  1.00 70.42  ? 484 VAL A CG2   1 
ATOM   3606 N  N     . ARG A 1 458 ? 70.557  0.914   24.987  1.00 71.71  ? 485 ARG A N     1 
ATOM   3607 C  CA    . ARG A 1 458 ? 70.179  2.296   25.238  1.00 73.16  ? 485 ARG A CA    1 
ATOM   3608 C  C     . ARG A 1 458 ? 71.402  3.144   25.566  1.00 68.53  ? 485 ARG A C     1 
ATOM   3609 O  O     . ARG A 1 458 ? 72.410  2.651   26.080  1.00 71.30  ? 485 ARG A O     1 
ATOM   3610 C  CB    . ARG A 1 458 ? 69.169  2.377   26.382  1.00 85.30  ? 485 ARG A CB    1 
ATOM   3611 C  CG    . ARG A 1 458 ? 67.754  1.992   25.986  1.00 95.88  ? 485 ARG A CG    1 
ATOM   3612 C  CD    . ARG A 1 458 ? 66.865  1.785   27.204  1.00 87.60  ? 485 ARG A CD    1 
ATOM   3613 N  NE    . ARG A 1 458 ? 67.225  0.580   27.942  1.00 104.90 ? 485 ARG A NE    1 
ATOM   3614 C  CZ    . ARG A 1 458 ? 67.968  0.564   29.040  1.00 112.50 ? 485 ARG A CZ    1 
ATOM   3615 N  NH1   . ARG A 1 458 ? 68.437  1.681   29.575  1.00 115.87 ? 485 ARG A NH1   1 
ATOM   3616 N  NH2   . ARG A 1 458 ? 68.248  -0.601  29.618  1.00 114.31 ? 485 ARG A NH2   1 
ATOM   3617 N  N     . ASN A 1 459 ? 71.301  4.436   25.247  1.00 68.93  ? 486 ASN A N     1 
ATOM   3618 C  CA    . ASN A 1 459 ? 72.330  5.428   25.563  1.00 72.13  ? 486 ASN A CA    1 
ATOM   3619 C  C     . ASN A 1 459 ? 73.661  5.119   24.881  1.00 69.84  ? 486 ASN A C     1 
ATOM   3620 O  O     . ASN A 1 459 ? 74.728  5.470   25.390  1.00 67.21  ? 486 ASN A O     1 
ATOM   3621 C  CB    . ASN A 1 459 ? 72.526  5.563   27.077  1.00 78.28  ? 486 ASN A CB    1 
ATOM   3622 C  CG    . ASN A 1 459 ? 71.261  6.001   27.790  1.00 70.02  ? 486 ASN A CG    1 
ATOM   3623 O  OD1   . ASN A 1 459 ? 70.418  6.688   27.214  1.00 76.49  ? 486 ASN A OD1   1 
ATOM   3624 N  ND2   . ASN A 1 459 ? 71.123  5.606   29.049  1.00 75.07  ? 486 ASN A ND2   1 
ATOM   3625 N  N     . LEU A 1 460 ? 73.614  4.467   23.721  1.00 65.21  ? 487 LEU A N     1 
ATOM   3626 C  CA    . LEU A 1 460 ? 74.819  4.159   22.966  1.00 68.21  ? 487 LEU A CA    1 
ATOM   3627 C  C     . LEU A 1 460 ? 74.578  4.457   21.495  1.00 77.00  ? 487 LEU A C     1 
ATOM   3628 O  O     . LEU A 1 460 ? 73.525  4.116   20.948  1.00 75.74  ? 487 LEU A O     1 
ATOM   3629 C  CB    . LEU A 1 460 ? 75.240  2.694   23.145  1.00 65.73  ? 487 LEU A CB    1 
ATOM   3630 C  CG    . LEU A 1 460 ? 76.625  2.319   22.616  1.00 66.81  ? 487 LEU A CG    1 
ATOM   3631 C  CD1   . LEU A 1 460 ? 77.709  3.051   23.391  1.00 62.84  ? 487 LEU A CD1   1 
ATOM   3632 C  CD2   . LEU A 1 460 ? 76.834  0.819   22.689  1.00 77.31  ? 487 LEU A CD2   1 
ATOM   3633 N  N     . VAL A 1 461 ? 75.558  5.101   20.860  1.00 71.62  ? 488 VAL A N     1 
ATOM   3634 C  CA    . VAL A 1 461 ? 75.476  5.469   19.455  1.00 74.46  ? 488 VAL A CA    1 
ATOM   3635 C  C     . VAL A 1 461 ? 76.757  5.040   18.754  1.00 75.31  ? 488 VAL A C     1 
ATOM   3636 O  O     . VAL A 1 461 ? 77.783  4.779   19.385  1.00 76.93  ? 488 VAL A O     1 
ATOM   3637 C  CB    . VAL A 1 461 ? 75.246  6.983   19.261  1.00 77.37  ? 488 VAL A CB    1 
ATOM   3638 C  CG1   . VAL A 1 461 ? 73.832  7.365   19.664  1.00 73.13  ? 488 VAL A CG1   1 
ATOM   3639 C  CG2   . VAL A 1 461 ? 76.266  7.776   20.065  1.00 62.44  ? 488 VAL A CG2   1 
ATOM   3640 N  N     . GLU A 1 462 ? 76.684  4.972   17.427  1.00 78.48  ? 489 GLU A N     1 
ATOM   3641 C  CA    . GLU A 1 462 ? 77.870  4.742   16.612  1.00 75.36  ? 489 GLU A CA    1 
ATOM   3642 C  C     . GLU A 1 462 ? 78.624  6.057   16.463  1.00 87.65  ? 489 GLU A C     1 
ATOM   3643 O  O     . GLU A 1 462 ? 78.071  7.044   15.962  1.00 84.81  ? 489 GLU A O     1 
ATOM   3644 C  CB    . GLU A 1 462 ? 77.487  4.170   15.249  1.00 75.21  ? 489 GLU A CB    1 
ATOM   3645 C  CG    . GLU A 1 462 ? 76.781  2.825   15.320  1.00 87.32  ? 489 GLU A CG    1 
ATOM   3646 C  CD    . GLU A 1 462 ? 76.554  2.211   13.953  1.00 91.19  ? 489 GLU A CD    1 
ATOM   3647 O  OE1   . GLU A 1 462 ? 77.189  2.669   12.980  1.00 100.90 ? 489 GLU A OE1   1 
ATOM   3648 O  OE2   . GLU A 1 462 ? 75.738  1.270   13.853  1.00 97.50  ? 489 GLU A OE2   1 
ATOM   3649 N  N     . ALA A 1 463 ? 79.880  6.073   16.902  1.00 82.53  ? 490 ALA A N     1 
ATOM   3650 C  CA    . ALA A 1 463 ? 80.646  7.311   16.963  1.00 89.04  ? 490 ALA A CA    1 
ATOM   3651 C  C     . ALA A 1 463 ? 80.991  7.802   15.562  1.00 96.80  ? 490 ALA A C     1 
ATOM   3652 O  O     . ALA A 1 463 ? 81.616  7.082   14.775  1.00 88.07  ? 490 ALA A O     1 
ATOM   3653 C  CB    . ALA A 1 463 ? 81.915  7.101   17.785  1.00 81.31  ? 490 ALA A CB    1 
ATOM   3654 N  N     . ASP A 1 464 ? 80.581  9.028   15.249  1.00 83.69  ? 491 ASP A N     1 
ATOM   3655 C  CA    . ASP A 1 464 ? 81.011  9.700   14.033  1.00 96.18  ? 491 ASP A CA    1 
ATOM   3656 C  C     . ASP A 1 464 ? 82.325  10.426  14.326  1.00 94.03  ? 491 ASP A C     1 
ATOM   3657 O  O     . ASP A 1 464 ? 83.050  10.059  15.255  1.00 92.57  ? 491 ASP A O     1 
ATOM   3658 C  CB    . ASP A 1 464 ? 79.902  10.629  13.527  1.00 97.93  ? 491 ASP A CB    1 
ATOM   3659 C  CG    . ASP A 1 464 ? 78.728  9.868   12.939  1.00 108.23 ? 491 ASP A CG    1 
ATOM   3660 O  OD1   . ASP A 1 464 ? 78.778  8.619   12.925  1.00 114.77 ? 491 ASP A OD1   1 
ATOM   3661 O  OD2   . ASP A 1 464 ? 77.759  10.514  12.487  1.00 92.77  ? 491 ASP A OD2   1 
ATOM   3662 N  N     . TYR A 1 465 ? 82.653  11.456  13.549  1.00 91.53  ? 492 TYR A N     1 
ATOM   3663 C  CA    . TYR A 1 465 ? 83.887  12.194  13.785  1.00 92.69  ? 492 TYR A CA    1 
ATOM   3664 C  C     . TYR A 1 465 ? 83.872  12.813  15.176  1.00 93.55  ? 492 TYR A C     1 
ATOM   3665 O  O     . TYR A 1 465 ? 82.956  13.565  15.523  1.00 87.18  ? 492 TYR A O     1 
ATOM   3666 C  CB    . TYR A 1 465 ? 84.074  13.277  12.724  1.00 83.78  ? 492 TYR A CB    1 
ATOM   3667 C  CG    . TYR A 1 465 ? 85.439  13.933  12.769  1.00 99.52  ? 492 TYR A CG    1 
ATOM   3668 C  CD1   . TYR A 1 465 ? 86.568  13.209  13.138  1.00 100.44 ? 492 TYR A CD1   1 
ATOM   3669 C  CD2   . TYR A 1 465 ? 85.597  15.277  12.459  1.00 100.23 ? 492 TYR A CD2   1 
ATOM   3670 C  CE1   . TYR A 1 465 ? 87.815  13.804  13.185  1.00 107.80 ? 492 TYR A CE1   1 
ATOM   3671 C  CE2   . TYR A 1 465 ? 86.839  15.880  12.505  1.00 99.14  ? 492 TYR A CE2   1 
ATOM   3672 C  CZ    . TYR A 1 465 ? 87.944  15.139  12.868  1.00 110.92 ? 492 TYR A CZ    1 
ATOM   3673 O  OH    . TYR A 1 465 ? 89.184  15.733  12.915  1.00 111.03 ? 492 TYR A OH    1 
ATOM   3674 N  N     . SER A 1 466 ? 84.880  12.480  15.976  1.00 97.05  ? 493 SER A N     1 
ATOM   3675 C  CA    . SER A 1 466 ? 85.014  12.973  17.338  1.00 91.38  ? 493 SER A CA    1 
ATOM   3676 C  C     . SER A 1 466 ? 86.403  13.571  17.508  1.00 93.33  ? 493 SER A C     1 
ATOM   3677 O  O     . SER A 1 466 ? 87.288  13.379  16.670  1.00 102.83 ? 493 SER A O     1 
ATOM   3678 C  CB    . SER A 1 466 ? 84.771  11.854  18.358  1.00 89.51  ? 493 SER A CB    1 
ATOM   3679 O  OG    . SER A 1 466 ? 83.560  11.176  18.071  1.00 85.37  ? 493 SER A OG    1 
ATOM   3680 N  N     . TYR A 1 467 ? 86.604  14.296  18.604  1.00 96.03  ? 494 TYR A N     1 
ATOM   3681 C  CA    . TYR A 1 467 ? 87.823  15.083  18.738  1.00 105.53 ? 494 TYR A CA    1 
ATOM   3682 C  C     . TYR A 1 467 ? 88.174  15.324  20.206  1.00 109.08 ? 494 TYR A C     1 
ATOM   3683 O  O     . TYR A 1 467 ? 88.347  16.455  20.648  1.00 131.94 ? 494 TYR A O     1 
ATOM   3684 C  CB    . TYR A 1 467 ? 87.664  16.401  17.982  1.00 112.26 ? 494 TYR A CB    1 
ATOM   3685 C  CG    . TYR A 1 467 ? 88.961  17.012  17.510  1.00 128.43 ? 494 TYR A CG    1 
ATOM   3686 C  CD1   . TYR A 1 467 ? 89.676  17.888  18.317  1.00 138.42 ? 494 TYR A CD1   1 
ATOM   3687 C  CD2   . TYR A 1 467 ? 89.469  16.716  16.253  1.00 128.19 ? 494 TYR A CD2   1 
ATOM   3688 C  CE1   . TYR A 1 467 ? 90.863  18.449  17.888  1.00 146.79 ? 494 TYR A CE1   1 
ATOM   3689 C  CE2   . TYR A 1 467 ? 90.654  17.273  15.812  1.00 138.35 ? 494 TYR A CE2   1 
ATOM   3690 C  CZ    . TYR A 1 467 ? 91.348  18.138  16.634  1.00 150.49 ? 494 TYR A CZ    1 
ATOM   3691 O  OH    . TYR A 1 467 ? 92.529  18.693  16.197  1.00 155.86 ? 494 TYR A OH    1 
ATOM   3692 N  N     . TRP A 1 468 ? 88.294  14.252  20.988  1.00 79.03  ? 495 TRP A N     1 
ATOM   3693 C  CA    . TRP A 1 468 ? 88.794  14.338  22.358  1.00 96.13  ? 495 TRP A CA    1 
ATOM   3694 C  C     . TRP A 1 468 ? 89.138  12.940  22.849  1.00 95.64  ? 495 TRP A C     1 
ATOM   3695 O  O     . TRP A 1 468 ? 88.657  11.937  22.312  1.00 93.60  ? 495 TRP A O     1 
ATOM   3696 C  CB    . TRP A 1 468 ? 87.785  14.999  23.308  1.00 98.45  ? 495 TRP A CB    1 
ATOM   3697 C  CG    . TRP A 1 468 ? 88.037  16.464  23.511  1.00 92.39  ? 495 TRP A CG    1 
ATOM   3698 C  CD1   . TRP A 1 468 ? 89.217  17.125  23.322  1.00 91.36  ? 495 TRP A CD1   1 
ATOM   3699 C  CD2   . TRP A 1 468 ? 87.085  17.455  23.917  1.00 91.73  ? 495 TRP A CD2   1 
ATOM   3700 N  NE1   . TRP A 1 468 ? 89.060  18.462  23.590  1.00 96.72  ? 495 TRP A NE1   1 
ATOM   3701 C  CE2   . TRP A 1 468 ? 87.761  18.691  23.959  1.00 98.90  ? 495 TRP A CE2   1 
ATOM   3702 C  CE3   . TRP A 1 468 ? 85.729  17.417  24.258  1.00 87.47  ? 495 TRP A CE3   1 
ATOM   3703 C  CZ2   . TRP A 1 468 ? 87.128  19.877  24.326  1.00 85.75  ? 495 TRP A CZ2   1 
ATOM   3704 C  CZ3   . TRP A 1 468 ? 85.101  18.596  24.618  1.00 83.05  ? 495 TRP A CZ3   1 
ATOM   3705 C  CH2   . TRP A 1 468 ? 85.801  19.809  24.649  1.00 87.21  ? 495 TRP A CH2   1 
ATOM   3706 N  N     . THR A 1 469 ? 89.980  12.891  23.879  1.00 90.26  ? 496 THR A N     1 
ATOM   3707 C  CA    . THR A 1 469 ? 90.387  11.651  24.533  1.00 86.73  ? 496 THR A CA    1 
ATOM   3708 C  C     . THR A 1 469 ? 90.304  11.792  26.046  1.00 83.19  ? 496 THR A C     1 
ATOM   3709 O  O     . THR A 1 469 ? 91.140  11.259  26.782  1.00 80.19  ? 496 THR A O     1 
ATOM   3710 C  CB    . THR A 1 469 ? 91.797  11.240  24.114  1.00 77.48  ? 496 THR A CB    1 
ATOM   3711 O  OG1   . THR A 1 469 ? 92.690  12.350  24.278  1.00 90.19  ? 496 THR A OG1   1 
ATOM   3712 C  CG2   . THR A 1 469 ? 91.817  10.778  22.664  1.00 88.90  ? 496 THR A CG2   1 
ATOM   3713 N  N     . LEU A 1 470 ? 89.294  12.519  26.531  1.00 80.19  ? 497 LEU A N     1 
ATOM   3714 C  CA    . LEU A 1 470 ? 89.122  12.696  27.972  1.00 70.92  ? 497 LEU A CA    1 
ATOM   3715 C  C     . LEU A 1 470 ? 88.929  11.358  28.671  1.00 75.50  ? 497 LEU A C     1 
ATOM   3716 O  O     . LEU A 1 470 ? 89.658  11.021  29.612  1.00 77.70  ? 497 LEU A O     1 
ATOM   3717 C  CB    . LEU A 1 470 ? 87.928  13.607  28.254  1.00 67.01  ? 497 LEU A CB    1 
ATOM   3718 C  CG    . LEU A 1 470 ? 87.865  14.974  27.582  1.00 76.85  ? 497 LEU A CG    1 
ATOM   3719 C  CD1   . LEU A 1 470 ? 86.470  15.535  27.753  1.00 75.58  ? 497 LEU A CD1   1 
ATOM   3720 C  CD2   . LEU A 1 470 ? 88.901  15.912  28.175  1.00 89.22  ? 497 LEU A CD2   1 
ATOM   3721 N  N     . ALA A 1 471 ? 87.942  10.584  28.228  1.00 66.31  ? 498 ALA A N     1 
ATOM   3722 C  CA    . ALA A 1 471 ? 87.626  9.307   28.846  1.00 71.15  ? 498 ALA A CA    1 
ATOM   3723 C  C     . ALA A 1 471 ? 87.059  8.374   27.790  1.00 73.54  ? 498 ALA A C     1 
ATOM   3724 O  O     . ALA A 1 471 ? 86.283  8.799   26.931  1.00 67.77  ? 498 ALA A O     1 
ATOM   3725 C  CB    . ALA A 1 471 ? 86.629  9.473   29.996  1.00 61.16  ? 498 ALA A CB    1 
ATOM   3726 N  N     . TYR A 1 472 ? 87.454  7.105   27.858  1.00 67.52  ? 499 TYR A N     1 
ATOM   3727 C  CA    . TYR A 1 472 ? 86.945  6.109   26.928  1.00 59.42  ? 499 TYR A CA    1 
ATOM   3728 C  C     . TYR A 1 472 ? 87.163  4.722   27.510  1.00 72.05  ? 499 TYR A C     1 
ATOM   3729 O  O     . TYR A 1 472 ? 88.010  4.518   28.383  1.00 67.70  ? 499 TYR A O     1 
ATOM   3730 C  CB    . TYR A 1 472 ? 87.611  6.224   25.550  1.00 61.70  ? 499 TYR A CB    1 
ATOM   3731 C  CG    . TYR A 1 472 ? 89.107  5.977   25.544  1.00 63.73  ? 499 TYR A CG    1 
ATOM   3732 C  CD1   . TYR A 1 472 ? 89.620  4.687   25.468  1.00 68.15  ? 499 TYR A CD1   1 
ATOM   3733 C  CD2   . TYR A 1 472 ? 90.005  7.034   25.595  1.00 76.20  ? 499 TYR A CD2   1 
ATOM   3734 C  CE1   . TYR A 1 472 ? 90.982  4.457   25.454  1.00 76.08  ? 499 TYR A CE1   1 
ATOM   3735 C  CE2   . TYR A 1 472 ? 91.372  6.812   25.582  1.00 76.20  ? 499 TYR A CE2   1 
ATOM   3736 C  CZ    . TYR A 1 472 ? 91.852  5.522   25.511  1.00 79.88  ? 499 TYR A CZ    1 
ATOM   3737 O  OH    . TYR A 1 472 ? 93.208  5.294   25.497  1.00 76.20  ? 499 TYR A OH    1 
ATOM   3738 N  N     . VAL A 1 473 ? 86.384  3.770   27.006  1.00 70.69  ? 500 VAL A N     1 
ATOM   3739 C  CA    . VAL A 1 473 ? 86.556  2.355   27.306  1.00 62.24  ? 500 VAL A CA    1 
ATOM   3740 C  C     . VAL A 1 473 ? 87.152  1.692   26.074  1.00 77.88  ? 500 VAL A C     1 
ATOM   3741 O  O     . VAL A 1 473 ? 86.793  2.034   24.941  1.00 73.75  ? 500 VAL A O     1 
ATOM   3742 C  CB    . VAL A 1 473 ? 85.223  1.693   27.705  1.00 67.11  ? 500 VAL A CB    1 
ATOM   3743 C  CG1   . VAL A 1 473 ? 85.459  0.276   28.196  1.00 68.52  ? 500 VAL A CG1   1 
ATOM   3744 C  CG2   . VAL A 1 473 ? 84.525  2.517   28.773  1.00 58.62  ? 500 VAL A CG2   1 
ATOM   3745 N  N     . ILE A 1 474 ? 88.075  0.759   26.291  1.00 79.64  ? 501 ILE A N     1 
ATOM   3746 C  CA    . ILE A 1 474 ? 88.785  0.107   25.197  1.00 76.21  ? 501 ILE A CA    1 
ATOM   3747 C  C     . ILE A 1 474 ? 88.810  -1.394  25.452  1.00 77.86  ? 501 ILE A C     1 
ATOM   3748 O  O     . ILE A 1 474 ? 89.025  -1.843  26.583  1.00 84.93  ? 501 ILE A O     1 
ATOM   3749 C  CB    . ILE A 1 474 ? 90.209  0.684   25.025  1.00 75.31  ? 501 ILE A CB    1 
ATOM   3750 C  CG1   . ILE A 1 474 ? 90.883  0.110   23.779  1.00 76.29  ? 501 ILE A CG1   1 
ATOM   3751 C  CG2   . ILE A 1 474 ? 91.058  0.441   26.270  1.00 70.57  ? 501 ILE A CG2   1 
ATOM   3752 C  CD1   . ILE A 1 474 ? 92.215  0.758   23.467  1.00 79.33  ? 501 ILE A CD1   1 
ATOM   3753 N  N     . SER A 1 475 ? 88.564  -2.166  24.401  1.00 81.02  ? 502 SER A N     1 
ATOM   3754 C  CA    . SER A 1 475 ? 88.563  -3.615  24.502  1.00 84.70  ? 502 SER A CA    1 
ATOM   3755 C  C     . SER A 1 475 ? 89.946  -4.170  24.183  1.00 92.87  ? 502 SER A C     1 
ATOM   3756 O  O     . SER A 1 475 ? 90.810  -3.482  23.635  1.00 93.98  ? 502 SER A O     1 
ATOM   3757 C  CB    . SER A 1 475 ? 87.524  -4.230  23.561  1.00 74.02  ? 502 SER A CB    1 
ATOM   3758 O  OG    . SER A 1 475 ? 87.924  -4.110  22.208  1.00 83.40  ? 502 SER A OG    1 
ATOM   3759 N  N     . LEU A 1 476 ? 90.151  -5.437  24.550  1.00 79.33  ? 503 LEU A N     1 
ATOM   3760 C  CA    . LEU A 1 476 ? 91.401  -6.103  24.206  1.00 87.12  ? 503 LEU A CA    1 
ATOM   3761 C  C     . LEU A 1 476 ? 91.576  -6.186  22.696  1.00 94.56  ? 503 LEU A C     1 
ATOM   3762 O  O     . LEU A 1 476 ? 92.679  -5.977  22.176  1.00 94.51  ? 503 LEU A O     1 
ATOM   3763 C  CB    . LEU A 1 476 ? 91.441  -7.497  24.831  1.00 100.23 ? 503 LEU A CB    1 
ATOM   3764 C  CG    . LEU A 1 476 ? 92.763  -8.248  24.665  1.00 96.24  ? 503 LEU A CG    1 
ATOM   3765 C  CD1   . LEU A 1 476 ? 93.905  -7.415  25.214  1.00 103.75 ? 503 LEU A CD1   1 
ATOM   3766 C  CD2   . LEU A 1 476 ? 92.708  -9.603  25.351  1.00 87.48  ? 503 LEU A CD2   1 
ATOM   3767 N  N     . GLN A 1 477 ? 90.492  -6.483  21.975  1.00 91.53  ? 504 GLN A N     1 
ATOM   3768 C  CA    . GLN A 1 477 ? 90.540  -6.483  20.517  1.00 103.16 ? 504 GLN A CA    1 
ATOM   3769 C  C     . GLN A 1 477 ? 90.889  -5.099  19.982  1.00 101.95 ? 504 GLN A C     1 
ATOM   3770 O  O     . GLN A 1 477 ? 91.737  -4.958  19.092  1.00 104.77 ? 504 GLN A O     1 
ATOM   3771 C  CB    . GLN A 1 477 ? 89.199  -6.955  19.955  1.00 98.50  ? 504 GLN A CB    1 
ATOM   3772 C  CG    . GLN A 1 477 ? 89.070  -6.830  18.447  1.00 116.86 ? 504 GLN A CG    1 
ATOM   3773 C  CD    . GLN A 1 477 ? 87.650  -7.060  17.970  1.00 119.08 ? 504 GLN A CD    1 
ATOM   3774 O  OE1   . GLN A 1 477 ? 86.724  -7.152  18.775  1.00 112.93 ? 504 GLN A OE1   1 
ATOM   3775 N  NE2   . GLN A 1 477 ? 87.471  -7.155  16.658  1.00 128.51 ? 504 GLN A NE2   1 
ATOM   3776 N  N     . GLY A 1 478 ? 90.242  -4.062  20.518  1.00 97.89  ? 505 GLY A N     1 
ATOM   3777 C  CA    . GLY A 1 478 ? 90.506  -2.713  20.046  1.00 101.95 ? 505 GLY A CA    1 
ATOM   3778 C  C     . GLY A 1 478 ? 91.922  -2.255  20.336  1.00 104.05 ? 505 GLY A C     1 
ATOM   3779 O  O     . GLY A 1 478 ? 92.522  -1.523  19.545  1.00 106.05 ? 505 GLY A O     1 
ATOM   3780 N  N     . ALA A 1 479 ? 92.475  -2.678  21.476  1.00 92.66  ? 506 ALA A N     1 
ATOM   3781 C  CA    . ALA A 1 479 ? 93.858  -2.341  21.790  1.00 98.55  ? 506 ALA A CA    1 
ATOM   3782 C  C     . ALA A 1 479 ? 94.817  -2.974  20.789  1.00 103.51 ? 506 ALA A C     1 
ATOM   3783 O  O     . ALA A 1 479 ? 95.805  -2.351  20.384  1.00 100.13 ? 506 ALA A O     1 
ATOM   3784 C  CB    . ALA A 1 479 ? 94.195  -2.780  23.214  1.00 91.30  ? 506 ALA A CB    1 
ATOM   3785 N  N     . ARG A 1 480 ? 94.536  -4.212  20.374  1.00 98.63  ? 507 ARG A N     1 
ATOM   3786 C  CA    . ARG A 1 480 ? 95.366  -4.859  19.364  1.00 97.91  ? 507 ARG A CA    1 
ATOM   3787 C  C     . ARG A 1 480 ? 95.276  -4.136  18.027  1.00 104.94 ? 507 ARG A C     1 
ATOM   3788 O  O     . ARG A 1 480 ? 96.285  -3.986  17.329  1.00 100.45 ? 507 ARG A O     1 
ATOM   3789 C  CB    . ARG A 1 480 ? 94.955  -6.322  19.198  1.00 93.86  ? 507 ARG A CB    1 
ATOM   3790 C  CG    . ARG A 1 480 ? 95.228  -7.211  20.399  1.00 101.63 ? 507 ARG A CG    1 
ATOM   3791 C  CD    . ARG A 1 480 ? 95.006  -8.669  20.026  1.00 105.81 ? 507 ARG A CD    1 
ATOM   3792 N  NE    . ARG A 1 480 ? 95.242  -9.580  21.139  1.00 114.86 ? 507 ARG A NE    1 
ATOM   3793 C  CZ    . ARG A 1 480 ? 94.286  -10.100 21.895  1.00 116.83 ? 507 ARG A CZ    1 
ATOM   3794 N  NH1   . ARG A 1 480 ? 93.011  -9.811  21.694  1.00 111.61 ? 507 ARG A NH1   1 
ATOM   3795 N  NH2   . ARG A 1 480 ? 94.617  -10.937 22.875  1.00 112.54 ? 507 ARG A NH2   1 
ATOM   3796 N  N     . LYS A 1 481 ? 94.075  -3.684  17.653  1.00 101.31 ? 508 LYS A N     1 
ATOM   3797 C  CA    . LYS A 1 481 ? 93.898  -3.023  16.363  1.00 92.25  ? 508 LYS A CA    1 
ATOM   3798 C  C     . LYS A 1 481 ? 94.729  -1.750  16.272  1.00 101.10 ? 508 LYS A C     1 
ATOM   3799 O  O     . LYS A 1 481 ? 95.319  -1.459  15.224  1.00 100.17 ? 508 LYS A O     1 
ATOM   3800 C  CB    . LYS A 1 481 ? 92.421  -2.710  16.126  1.00 89.78  ? 508 LYS A CB    1 
ATOM   3801 C  CG    . LYS A 1 481 ? 91.535  -3.933  15.985  1.00 90.09  ? 508 LYS A CG    1 
ATOM   3802 C  CD    . LYS A 1 481 ? 90.139  -3.541  15.533  1.00 99.56  ? 508 LYS A CD    1 
ATOM   3803 C  CE    . LYS A 1 481 ? 89.298  -4.764  15.210  1.00 98.56  ? 508 LYS A CE    1 
ATOM   3804 N  NZ    . LYS A 1 481 ? 87.973  -4.382  14.648  1.00 107.13 ? 508 LYS A NZ    1 
ATOM   3805 N  N     . LEU A 1 482 ? 94.785  -0.976  17.357  1.00 104.59 ? 509 LEU A N     1 
ATOM   3806 C  CA    . LEU A 1 482 ? 95.576  0.250   17.349  1.00 105.04 ? 509 LEU A CA    1 
ATOM   3807 C  C     . LEU A 1 482 ? 97.061  -0.062  17.216  1.00 104.09 ? 509 LEU A C     1 
ATOM   3808 O  O     . LEU A 1 482 ? 97.762  0.529   16.385  1.00 105.83 ? 509 LEU A O     1 
ATOM   3809 C  CB    . LEU A 1 482 ? 95.300  1.060   18.615  1.00 92.35  ? 509 LEU A CB    1 
ATOM   3810 C  CG    . LEU A 1 482 ? 93.834  1.431   18.845  1.00 102.11 ? 509 LEU A CG    1 
ATOM   3811 C  CD1   . LEU A 1 482 ? 93.700  2.371   20.028  1.00 93.55  ? 509 LEU A CD1   1 
ATOM   3812 C  CD2   . LEU A 1 482 ? 93.229  2.048   17.593  1.00 105.21 ? 509 LEU A CD2   1 
ATOM   3813 N  N     . LEU A 1 483 ? 97.558  -1.001  18.028  1.00 98.66  ? 510 LEU A N     1 
ATOM   3814 C  CA    . LEU A 1 483 ? 98.955  -1.408  17.925  1.00 102.23 ? 510 LEU A CA    1 
ATOM   3815 C  C     . LEU A 1 483 ? 99.258  -2.034  16.570  1.00 106.11 ? 510 LEU A C     1 
ATOM   3816 O  O     . LEU A 1 483 ? 100.385 -1.922  16.073  1.00 105.10 ? 510 LEU A O     1 
ATOM   3817 C  CB    . LEU A 1 483 ? 99.298  -2.387  19.048  1.00 97.92  ? 510 LEU A CB    1 
ATOM   3818 C  CG    . LEU A 1 483 ? 98.995  -1.941  20.479  1.00 99.24  ? 510 LEU A CG    1 
ATOM   3819 C  CD1   . LEU A 1 483 ? 99.122  -3.114  21.436  1.00 102.35 ? 510 LEU A CD1   1 
ATOM   3820 C  CD2   . LEU A 1 483 ? 99.915  -0.812  20.901  1.00 94.79  ? 510 LEU A CD2   1 
ATOM   3821 N  N     . ALA A 1 484 ? 98.269  -2.694  15.960  1.00 111.13 ? 511 ALA A N     1 
ATOM   3822 C  CA    . ALA A 1 484 ? 98.480  -3.302  14.650  1.00 113.00 ? 511 ALA A CA    1 
ATOM   3823 C  C     . ALA A 1 484 ? 98.715  -2.245  13.579  1.00 108.11 ? 511 ALA A C     1 
ATOM   3824 O  O     . ALA A 1 484 ? 99.510  -2.456  12.657  1.00 120.67 ? 511 ALA A O     1 
ATOM   3825 C  CB    . ALA A 1 484 ? 97.287  -4.183  14.279  1.00 104.19 ? 511 ALA A CB    1 
ATOM   3826 N  N     . ALA A 1 485 ? 98.038  -1.100  13.686  1.00 121.44 ? 512 ALA A N     1 
ATOM   3827 C  CA    . ALA A 1 485 ? 98.228  -0.032  12.713  1.00 120.45 ? 512 ALA A CA    1 
ATOM   3828 C  C     . ALA A 1 485 ? 99.633  0.551   12.763  1.00 122.47 ? 512 ALA A C     1 
ATOM   3829 O  O     . ALA A 1 485 ? 100.062 1.180   11.789  1.00 129.43 ? 512 ALA A O     1 
ATOM   3830 C  CB    . ALA A 1 485 ? 97.195  1.075   12.936  1.00 123.65 ? 512 ALA A CB    1 
ATOM   3831 N  N     . GLU A 1 486 ? 100.358 0.348   13.870  1.00 125.00 ? 513 GLU A N     1 
ATOM   3832 C  CA    . GLU A 1 486 ? 101.709 0.860   14.072  1.00 130.01 ? 513 GLU A CA    1 
ATOM   3833 C  C     . GLU A 1 486 ? 101.751 2.354   13.779  1.00 128.62 ? 513 GLU A C     1 
ATOM   3834 O  O     . GLU A 1 486 ? 102.380 2.783   12.803  1.00 123.09 ? 513 GLU A O     1 
ATOM   3835 C  CB    . GLU A 1 486 ? 102.708 0.100   13.197  1.00 127.75 ? 513 GLU A CB    1 
ATOM   3836 C  CG    . GLU A 1 486 ? 102.828 -1.373  13.560  1.00 119.55 ? 513 GLU A CG    1 
ATOM   3837 C  CD    . GLU A 1 486 ? 103.480 -2.197  12.469  1.00 136.97 ? 513 GLU A CD    1 
ATOM   3838 O  OE1   . GLU A 1 486 ? 104.115 -1.607  11.570  1.00 151.93 ? 513 GLU A OE1   1 
ATOM   3839 O  OE2   . GLU A 1 486 ? 103.349 -3.439  12.508  1.00 153.96 ? 513 GLU A OE2   1 
ATOM   3840 N  N     . PRO A 1 487 ? 101.096 3.177   14.602  1.00 128.46 ? 514 PRO A N     1 
ATOM   3841 C  CA    . PRO A 1 487 ? 100.959 4.602   14.282  1.00 124.59 ? 514 PRO A CA    1 
ATOM   3842 C  C     . PRO A 1 487 ? 102.192 5.438   14.581  1.00 127.24 ? 514 PRO A C     1 
ATOM   3843 O  O     . PRO A 1 487 ? 102.186 6.636   14.279  1.00 136.77 ? 514 PRO A O     1 
ATOM   3844 C  CB    . PRO A 1 487 ? 99.785  5.028   15.173  1.00 126.46 ? 514 PRO A CB    1 
ATOM   3845 C  CG    . PRO A 1 487 ? 99.915  4.151   16.373  1.00 120.98 ? 514 PRO A CG    1 
ATOM   3846 C  CD    . PRO A 1 487 ? 100.447 2.830   15.879  1.00 118.37 ? 514 PRO A CD    1 
ATOM   3847 N  N     . LEU A 1 488 ? 103.246 4.853   15.153  1.00 120.45 ? 515 LEU A N     1 
ATOM   3848 C  CA    . LEU A 1 488 ? 104.405 5.650   15.543  1.00 121.94 ? 515 LEU A CA    1 
ATOM   3849 C  C     . LEU A 1 488 ? 105.155 6.198   14.333  1.00 127.93 ? 515 LEU A C     1 
ATOM   3850 O  O     . LEU A 1 488 ? 105.728 7.291   14.407  1.00 132.51 ? 515 LEU A O     1 
ATOM   3851 C  CB    . LEU A 1 488 ? 105.335 4.815   16.421  1.00 121.19 ? 515 LEU A CB    1 
ATOM   3852 C  CG    . LEU A 1 488 ? 104.646 4.123   17.598  1.00 115.83 ? 515 LEU A CG    1 
ATOM   3853 C  CD1   . LEU A 1 488 ? 105.653 3.343   18.425  1.00 113.36 ? 515 LEU A CD1   1 
ATOM   3854 C  CD2   . LEU A 1 488 ? 103.905 5.134   18.459  1.00 107.30 ? 515 LEU A CD2   1 
ATOM   3855 N  N     . SER A 1 489 ? 105.162 5.462   13.218  1.00 124.56 ? 516 SER A N     1 
ATOM   3856 C  CA    . SER A 1 489 ? 105.815 5.928   12.000  1.00 135.06 ? 516 SER A CA    1 
ATOM   3857 C  C     . SER A 1 489 ? 105.012 6.997   11.271  1.00 136.18 ? 516 SER A C     1 
ATOM   3858 O  O     . SER A 1 489 ? 105.565 7.690   10.410  1.00 131.81 ? 516 SER A O     1 
ATOM   3859 C  CB    . SER A 1 489 ? 106.068 4.748   11.057  1.00 131.27 ? 516 SER A CB    1 
ATOM   3860 O  OG    . SER A 1 489 ? 104.866 4.052   10.771  1.00 132.54 ? 516 SER A OG    1 
ATOM   3861 N  N     . LYS A 1 490 ? 103.733 7.146   11.598  1.00 126.64 ? 517 LYS A N     1 
ATOM   3862 C  CA    . LYS A 1 490 ? 102.840 8.100   10.947  1.00 127.36 ? 517 LYS A CA    1 
ATOM   3863 C  C     . LYS A 1 490 ? 101.960 8.768   11.999  1.00 119.30 ? 517 LYS A C     1 
ATOM   3864 O  O     . LYS A 1 490 ? 100.732 8.781   11.905  1.00 110.07 ? 517 LYS A O     1 
ATOM   3865 C  CB    . LYS A 1 490 ? 102.004 7.397   9.880   1.00 125.61 ? 517 LYS A CB    1 
ATOM   3866 C  CG    . LYS A 1 490 ? 101.499 6.032   10.328  1.00 121.58 ? 517 LYS A CG    1 
ATOM   3867 C  CD    . LYS A 1 490 ? 100.781 5.282   9.220   1.00 115.81 ? 517 LYS A CD    1 
ATOM   3868 C  CE    . LYS A 1 490 ? 100.441 3.864   9.658   1.00 114.48 ? 517 LYS A CE    1 
ATOM   3869 N  NZ    . LYS A 1 490 ? 99.659  3.129   8.627   1.00 123.29 ? 517 LYS A NZ    1 
ATOM   3870 N  N     . MET A 1 491 ? 102.597 9.345   13.017  1.00 125.46 ? 518 MET A N     1 
ATOM   3871 C  CA    . MET A 1 491 ? 101.886 9.738   14.226  1.00 134.55 ? 518 MET A CA    1 
ATOM   3872 C  C     . MET A 1 491 ? 101.005 10.959  13.996  1.00 127.63 ? 518 MET A C     1 
ATOM   3873 O  O     . MET A 1 491 ? 101.438 11.959  13.416  1.00 131.94 ? 518 MET A O     1 
ATOM   3874 C  CB    . MET A 1 491 ? 102.874 10.014  15.358  1.00 135.51 ? 518 MET A CB    1 
ATOM   3875 C  CG    . MET A 1 491 ? 102.217 10.548  16.622  1.00 124.55 ? 518 MET A CG    1 
ATOM   3876 S  SD    . MET A 1 491 ? 103.323 10.583  18.042  1.00 118.69 ? 518 MET A SD    1 
ATOM   3877 C  CE    . MET A 1 491 ? 103.552 8.832   18.336  1.00 127.99 ? 518 MET A CE    1 
ATOM   3878 N  N     . LEU A 1 492 ? 99.764  10.869  14.468  1.00 115.07 ? 519 LEU A N     1 
ATOM   3879 C  CA    . LEU A 1 492 ? 98.802  11.961  14.488  1.00 112.58 ? 519 LEU A CA    1 
ATOM   3880 C  C     . LEU A 1 492 ? 98.428  12.259  15.934  1.00 114.16 ? 519 LEU A C     1 
ATOM   3881 O  O     . LEU A 1 492 ? 98.764  11.475  16.831  1.00 113.69 ? 519 LEU A O     1 
ATOM   3882 C  CB    . LEU A 1 492 ? 97.554  11.600  13.681  1.00 112.39 ? 519 LEU A CB    1 
ATOM   3883 C  CG    . LEU A 1 492 ? 97.658  11.670  12.161  1.00 121.21 ? 519 LEU A CG    1 
ATOM   3884 C  CD1   . LEU A 1 492 ? 96.298  11.424  11.530  1.00 120.06 ? 519 LEU A CD1   1 
ATOM   3885 C  CD2   . LEU A 1 492 ? 98.207  13.017  11.746  1.00 132.10 ? 519 LEU A CD2   1 
ATOM   3886 N  N     . PRO A 1 493 ? 97.760  13.378  16.210  1.00 113.51 ? 520 PRO A N     1 
ATOM   3887 C  CA    . PRO A 1 493 ? 97.136  13.541  17.527  1.00 105.29 ? 520 PRO A CA    1 
ATOM   3888 C  C     . PRO A 1 493 ? 96.163  12.401  17.787  1.00 103.07 ? 520 PRO A C     1 
ATOM   3889 O  O     . PRO A 1 493 ? 95.411  11.992  16.900  1.00 108.76 ? 520 PRO A O     1 
ATOM   3890 C  CB    . PRO A 1 493 ? 96.421  14.891  17.414  1.00 96.57  ? 520 PRO A CB    1 
ATOM   3891 C  CG    . PRO A 1 493 ? 97.214  15.636  16.399  1.00 104.31 ? 520 PRO A CG    1 
ATOM   3892 C  CD    . PRO A 1 493 ? 97.677  14.608  15.404  1.00 110.63 ? 520 PRO A CD    1 
ATOM   3893 N  N     . VAL A 1 494 ? 96.197  11.876  19.015  1.00 95.83  ? 521 VAL A N     1 
ATOM   3894 C  CA    . VAL A 1 494 ? 95.460  10.652  19.322  1.00 104.24 ? 521 VAL A CA    1 
ATOM   3895 C  C     . VAL A 1 494 ? 93.967  10.842  19.076  1.00 108.98 ? 521 VAL A C     1 
ATOM   3896 O  O     . VAL A 1 494 ? 93.282  9.928   18.600  1.00 102.87 ? 521 VAL A O     1 
ATOM   3897 C  CB    . VAL A 1 494 ? 95.755  10.197  20.765  1.00 108.10 ? 521 VAL A CB    1 
ATOM   3898 C  CG1   . VAL A 1 494 ? 95.405  11.291  21.764  1.00 94.08  ? 521 VAL A CG1   1 
ATOM   3899 C  CG2   . VAL A 1 494 ? 95.013  8.904   21.083  1.00 94.74  ? 521 VAL A CG2   1 
ATOM   3900 N  N     . ASP A 1 495 ? 93.442  12.036  19.367  1.00 100.64 ? 522 ASP A N     1 
ATOM   3901 C  CA    . ASP A 1 495 ? 92.030  12.301  19.117  1.00 97.63  ? 522 ASP A CA    1 
ATOM   3902 C  C     . ASP A 1 495 ? 91.702  12.389  17.633  1.00 104.96 ? 522 ASP A C     1 
ATOM   3903 O  O     . ASP A 1 495 ? 90.518  12.430  17.281  1.00 110.91 ? 522 ASP A O     1 
ATOM   3904 C  CB    . ASP A 1 495 ? 91.594  13.586  19.824  1.00 109.77 ? 522 ASP A CB    1 
ATOM   3905 C  CG    . ASP A 1 495 ? 92.360  14.804  19.349  1.00 118.67 ? 522 ASP A CG    1 
ATOM   3906 O  OD1   . ASP A 1 495 ? 93.361  14.641  18.621  1.00 121.21 ? 522 ASP A OD1   1 
ATOM   3907 O  OD2   . ASP A 1 495 ? 91.957  15.931  19.706  1.00 125.27 ? 522 ASP A OD2   1 
ATOM   3908 N  N     . GLU A 1 496 ? 92.713  12.442  16.764  1.00 103.36 ? 523 GLU A N     1 
ATOM   3909 C  CA    . GLU A 1 496 ? 92.518  12.297  15.328  1.00 109.90 ? 523 GLU A CA    1 
ATOM   3910 C  C     . GLU A 1 496 ? 92.920  10.922  14.818  1.00 110.02 ? 523 GLU A C     1 
ATOM   3911 O  O     . GLU A 1 496 ? 92.417  10.493  13.774  1.00 107.72 ? 523 GLU A O     1 
ATOM   3912 C  CB    . GLU A 1 496 ? 93.316  13.360  14.563  1.00 106.42 ? 523 GLU A CB    1 
ATOM   3913 C  CG    . GLU A 1 496 ? 92.932  14.791  14.890  1.00 122.00 ? 523 GLU A CG    1 
ATOM   3914 C  CD    . GLU A 1 496 ? 93.655  15.797  14.017  1.00 113.84 ? 523 GLU A CD    1 
ATOM   3915 O  OE1   . GLU A 1 496 ? 93.984  15.453  12.862  1.00 126.31 ? 523 GLU A OE1   1 
ATOM   3916 O  OE2   . GLU A 1 496 ? 93.900  16.928  14.485  1.00 118.50 ? 523 GLU A OE2   1 
ATOM   3917 N  N     . PHE A 1 497 ? 93.811  10.228  15.529  1.00 111.45 ? 524 PHE A N     1 
ATOM   3918 C  CA    . PHE A 1 497 ? 94.200  8.881   15.127  1.00 94.88  ? 524 PHE A CA    1 
ATOM   3919 C  C     . PHE A 1 497 ? 93.036  7.909   15.261  1.00 92.12  ? 524 PHE A C     1 
ATOM   3920 O  O     . PHE A 1 497 ? 92.854  7.029   14.411  1.00 96.71  ? 524 PHE A O     1 
ATOM   3921 C  CB    . PHE A 1 497 ? 95.394  8.416   15.960  1.00 93.92  ? 524 PHE A CB    1 
ATOM   3922 C  CG    . PHE A 1 497 ? 95.631  6.934   15.911  1.00 99.74  ? 524 PHE A CG    1 
ATOM   3923 C  CD1   . PHE A 1 497 ? 96.044  6.322   14.739  1.00 99.26  ? 524 PHE A CD1   1 
ATOM   3924 C  CD2   . PHE A 1 497 ? 95.451  6.155   17.042  1.00 96.39  ? 524 PHE A CD2   1 
ATOM   3925 C  CE1   . PHE A 1 497 ? 96.265  4.958   14.694  1.00 99.39  ? 524 PHE A CE1   1 
ATOM   3926 C  CE2   . PHE A 1 497 ? 95.671  4.792   17.004  1.00 100.17 ? 524 PHE A CE2   1 
ATOM   3927 C  CZ    . PHE A 1 497 ? 96.079  4.192   15.828  1.00 96.93  ? 524 PHE A CZ    1 
ATOM   3928 N  N     . LEU A 1 498 ? 92.237  8.053   16.317  1.00 93.26  ? 525 LEU A N     1 
ATOM   3929 C  CA    . LEU A 1 498 ? 91.079  7.177   16.486  1.00 98.22  ? 525 LEU A CA    1 
ATOM   3930 C  C     . LEU A 1 498 ? 90.052  7.353   15.374  1.00 94.21  ? 525 LEU A C     1 
ATOM   3931 O  O     . LEU A 1 498 ? 89.675  6.343   14.755  1.00 92.00  ? 525 LEU A O     1 
ATOM   3932 C  CB    . LEU A 1 498 ? 90.463  7.392   17.875  1.00 89.40  ? 525 LEU A CB    1 
ATOM   3933 C  CG    . LEU A 1 498 ? 91.420  7.363   19.069  1.00 84.42  ? 525 LEU A CG    1 
ATOM   3934 C  CD1   . LEU A 1 498 ? 90.662  7.594   20.368  1.00 82.18  ? 525 LEU A CD1   1 
ATOM   3935 C  CD2   . LEU A 1 498 ? 92.202  6.058   19.120  1.00 82.32  ? 525 LEU A CD2   1 
ATOM   3936 N  N     . PRO A 1 499 ? 89.572  8.564   15.051  1.00 93.38  ? 526 PRO A N     1 
ATOM   3937 C  CA    . PRO A 1 499 ? 88.612  8.692   13.940  1.00 96.57  ? 526 PRO A CA    1 
ATOM   3938 C  C     . PRO A 1 499 ? 89.140  8.186   12.613  1.00 100.03 ? 526 PRO A C     1 
ATOM   3939 O  O     . PRO A 1 499 ? 88.339  7.814   11.745  1.00 97.54  ? 526 PRO A O     1 
ATOM   3940 C  CB    . PRO A 1 499 ? 88.327  10.200  13.892  1.00 96.73  ? 526 PRO A CB    1 
ATOM   3941 C  CG    . PRO A 1 499 ? 88.609  10.671  15.265  1.00 88.64  ? 526 PRO A CG    1 
ATOM   3942 C  CD    . PRO A 1 499 ? 89.783  9.861   15.719  1.00 87.99  ? 526 PRO A CD    1 
ATOM   3943 N  N     . VAL A 1 500 ? 90.459  8.167   12.420  1.00 95.19  ? 527 VAL A N     1 
ATOM   3944 C  CA    . VAL A 1 500 ? 91.018  7.472   11.267  1.00 97.70  ? 527 VAL A CA    1 
ATOM   3945 C  C     . VAL A 1 500 ? 90.745  5.978   11.376  1.00 94.66  ? 527 VAL A C     1 
ATOM   3946 O  O     . VAL A 1 500 ? 90.343  5.332   10.403  1.00 94.28  ? 527 VAL A O     1 
ATOM   3947 C  CB    . VAL A 1 500 ? 92.525  7.763   11.138  1.00 103.34 ? 527 VAL A CB    1 
ATOM   3948 C  CG1   . VAL A 1 500 ? 93.140  6.897   10.053  1.00 100.05 ? 527 VAL A CG1   1 
ATOM   3949 C  CG2   . VAL A 1 500 ? 92.762  9.235   10.841  1.00 102.97 ? 527 VAL A CG2   1 
ATOM   3950 N  N     . MET A 1 501 ? 90.923  5.412   12.573  1.00 94.10  ? 528 MET A N     1 
ATOM   3951 C  CA    . MET A 1 501 ? 90.850  3.963   12.722  1.00 95.42  ? 528 MET A CA    1 
ATOM   3952 C  C     . MET A 1 501 ? 89.425  3.431   12.610  1.00 92.27  ? 528 MET A C     1 
ATOM   3953 O  O     . MET A 1 501 ? 89.241  2.270   12.228  1.00 93.29  ? 528 MET A O     1 
ATOM   3954 C  CB    . MET A 1 501 ? 91.484  3.536   14.047  1.00 91.84  ? 528 MET A CB    1 
ATOM   3955 C  CG    . MET A 1 501 ? 92.997  3.717   14.077  1.00 91.24  ? 528 MET A CG    1 
ATOM   3956 S  SD    . MET A 1 501 ? 93.803  3.064   12.599  1.00 113.13 ? 528 MET A SD    1 
ATOM   3957 C  CE    . MET A 1 501 ? 93.428  1.319   12.749  1.00 94.34  ? 528 MET A CE    1 
ATOM   3958 N  N     . PHE A 1 502 ? 88.408  4.237   12.928  1.00 86.17  ? 529 PHE A N     1 
ATOM   3959 C  CA    . PHE A 1 502 ? 87.044  3.863   12.575  1.00 90.89  ? 529 PHE A CA    1 
ATOM   3960 C  C     . PHE A 1 502 ? 86.517  4.654   11.380  1.00 93.74  ? 529 PHE A C     1 
ATOM   3961 O  O     . PHE A 1 502 ? 85.299  4.773   11.208  1.00 92.27  ? 529 PHE A O     1 
ATOM   3962 C  CB    . PHE A 1 502 ? 86.095  3.966   13.777  1.00 87.61  ? 529 PHE A CB    1 
ATOM   3963 C  CG    . PHE A 1 502 ? 86.090  5.295   14.484  1.00 96.47  ? 529 PHE A CG    1 
ATOM   3964 C  CD1   . PHE A 1 502 ? 86.929  5.521   15.561  1.00 92.54  ? 529 PHE A CD1   1 
ATOM   3965 C  CD2   . PHE A 1 502 ? 85.192  6.288   14.124  1.00 100.29 ? 529 PHE A CD2   1 
ATOM   3966 C  CE1   . PHE A 1 502 ? 86.902  6.724   16.243  1.00 90.56  ? 529 PHE A CE1   1 
ATOM   3967 C  CE2   . PHE A 1 502 ? 85.163  7.499   14.798  1.00 94.33  ? 529 PHE A CE2   1 
ATOM   3968 C  CZ    . PHE A 1 502 ? 86.017  7.716   15.862  1.00 87.51  ? 529 PHE A CZ    1 
ATOM   3969 N  N     . ASP A 1 503 ? 87.422  5.191   10.556  1.00 92.56  ? 530 ASP A N     1 
ATOM   3970 C  CA    . ASP A 1 503 ? 87.119  5.636   9.192   1.00 96.40  ? 530 ASP A CA    1 
ATOM   3971 C  C     . ASP A 1 503 ? 86.076  6.754   9.171   1.00 103.30 ? 530 ASP A C     1 
ATOM   3972 O  O     . ASP A 1 503 ? 85.115  6.729   8.400   1.00 92.54  ? 530 ASP A O     1 
ATOM   3973 C  CB    . ASP A 1 503 ? 86.677  4.456   8.323   1.00 95.98  ? 530 ASP A CB    1 
ATOM   3974 C  CG    . ASP A 1 503 ? 86.907  4.700   6.842   1.00 110.02 ? 530 ASP A CG    1 
ATOM   3975 O  OD1   . ASP A 1 503 ? 87.500  5.742   6.490   1.00 119.17 ? 530 ASP A OD1   1 
ATOM   3976 O  OD2   . ASP A 1 503 ? 86.497  3.847   6.029   1.00 114.66 ? 530 ASP A OD2   1 
ATOM   3977 N  N     . LYS A 1 504 ? 86.283  7.756   10.022  1.00 92.74  ? 531 LYS A N     1 
ATOM   3978 C  CA    . LYS A 1 504 ? 85.410  8.917   10.065  1.00 86.83  ? 531 LYS A CA    1 
ATOM   3979 C  C     . LYS A 1 504 ? 86.162  10.228  9.899   1.00 97.70  ? 531 LYS A C     1 
ATOM   3980 O  O     . LYS A 1 504 ? 85.524  11.285  9.822   1.00 94.98  ? 531 LYS A O     1 
ATOM   3981 C  CB    . LYS A 1 504 ? 84.614  8.943   11.376  1.00 97.76  ? 531 LYS A CB    1 
ATOM   3982 C  CG    . LYS A 1 504 ? 83.565  7.848   11.497  1.00 96.59  ? 531 LYS A CG    1 
ATOM   3983 C  CD    . LYS A 1 504 ? 82.497  7.967   10.423  1.00 93.08  ? 531 LYS A CD    1 
ATOM   3984 C  CE    . LYS A 1 504 ? 81.320  7.052   10.715  1.00 97.67  ? 531 LYS A CE    1 
ATOM   3985 N  NZ    . LYS A 1 504 ? 80.203  7.267   9.757   1.00 111.53 ? 531 LYS A NZ    1 
ATOM   3986 N  N     . HIS A 1 505 ? 87.490  10.194  9.838   1.00 100.67 ? 532 HIS A N     1 
ATOM   3987 C  CA    . HIS A 1 505 ? 88.256  11.424  9.736   1.00 97.74  ? 532 HIS A CA    1 
ATOM   3988 C  C     . HIS A 1 505 ? 87.995  12.092  8.388   1.00 97.45  ? 532 HIS A C     1 
ATOM   3989 O  O     . HIS A 1 505 ? 87.940  11.414  7.357   1.00 103.50 ? 532 HIS A O     1 
ATOM   3990 C  CB    . HIS A 1 505 ? 89.747  11.148  9.909   1.00 93.90  ? 532 HIS A CB    1 
ATOM   3991 C  CG    . HIS A 1 505 ? 90.541  12.360  10.284  1.00 99.74  ? 532 HIS A CG    1 
ATOM   3992 N  ND1   . HIS A 1 505 ? 90.988  13.272  9.353   1.00 108.52 ? 532 HIS A ND1   1 
ATOM   3993 C  CD2   . HIS A 1 505 ? 90.956  12.816  11.489  1.00 101.43 ? 532 HIS A CD2   1 
ATOM   3994 C  CE1   . HIS A 1 505 ? 91.647  14.237  9.969   1.00 117.05 ? 532 HIS A CE1   1 
ATOM   3995 N  NE2   . HIS A 1 505 ? 91.645  13.984  11.265  1.00 114.89 ? 532 HIS A NE2   1 
ATOM   3996 N  N     . PRO A 1 506 ? 87.818  13.414  8.363   1.00 102.72 ? 533 PRO A N     1 
ATOM   3997 C  CA    . PRO A 1 506 ? 87.465  14.077  7.099   1.00 106.69 ? 533 PRO A CA    1 
ATOM   3998 C  C     . PRO A 1 506 ? 88.599  14.109  6.091   1.00 101.43 ? 533 PRO A C     1 
ATOM   3999 O  O     . PRO A 1 506 ? 88.334  14.084  4.884   1.00 107.96 ? 533 PRO A O     1 
ATOM   4000 C  CB    . PRO A 1 506 ? 87.065  15.489  7.547   1.00 98.68  ? 533 PRO A CB    1 
ATOM   4001 C  CG    . PRO A 1 506 ? 87.806  15.696  8.826   1.00 101.82 ? 533 PRO A CG    1 
ATOM   4002 C  CD    . PRO A 1 506 ? 87.852  14.354  9.496   1.00 97.92  ? 533 PRO A CD    1 
ATOM   4003 N  N     . VAL A 1 507 ? 89.850  14.166  6.540   1.00 102.00 ? 534 VAL A N     1 
ATOM   4004 C  CA    . VAL A 1 507 ? 90.988  14.213  5.627   1.00 113.73 ? 534 VAL A CA    1 
ATOM   4005 C  C     . VAL A 1 507 ? 91.214  12.809  5.073   1.00 115.00 ? 534 VAL A C     1 
ATOM   4006 O  O     . VAL A 1 507 ? 91.622  11.902  5.802   1.00 118.65 ? 534 VAL A O     1 
ATOM   4007 C  CB    . VAL A 1 507 ? 92.247  14.745  6.318   1.00 113.84 ? 534 VAL A CB    1 
ATOM   4008 C  CG1   . VAL A 1 507 ? 93.419  14.753  5.347   1.00 113.32 ? 534 VAL A CG1   1 
ATOM   4009 C  CG2   . VAL A 1 507 ? 91.999  16.138  6.874   1.00 105.62 ? 534 VAL A CG2   1 
ATOM   4010 N  N     . SER A 1 508 ? 90.946  12.629  3.778   1.00 111.69 ? 535 SER A N     1 
ATOM   4011 C  CA    . SER A 1 508 ? 91.193  11.336  3.150   1.00 128.37 ? 535 SER A CA    1 
ATOM   4012 C  C     . SER A 1 508 ? 92.682  11.033  3.058   1.00 132.24 ? 535 SER A C     1 
ATOM   4013 O  O     . SER A 1 508 ? 93.074  9.860   3.035   1.00 129.43 ? 535 SER A O     1 
ATOM   4014 C  CB    . SER A 1 508 ? 90.558  11.293  1.759   1.00 120.34 ? 535 SER A CB    1 
ATOM   4015 O  OG    . SER A 1 508 ? 89.149  11.415  1.834   1.00 132.63 ? 535 SER A OG    1 
ATOM   4016 N  N     . GLU A 1 509 ? 93.522  12.070  3.008   1.00 131.53 ? 536 GLU A N     1 
ATOM   4017 C  CA    . GLU A 1 509 ? 94.962  11.854  2.907   1.00 125.70 ? 536 GLU A CA    1 
ATOM   4018 C  C     . GLU A 1 509 ? 95.512  11.186  4.161   1.00 133.30 ? 536 GLU A C     1 
ATOM   4019 O  O     . GLU A 1 509 ? 96.418  10.349  4.080   1.00 132.62 ? 536 GLU A O     1 
ATOM   4020 C  CB    . GLU A 1 509 ? 95.675  13.181  2.648   1.00 122.91 ? 536 GLU A CB    1 
ATOM   4021 C  CG    . GLU A 1 509 ? 95.264  13.872  1.356   1.00 129.11 ? 536 GLU A CG    1 
ATOM   4022 C  CD    . GLU A 1 509 ? 95.769  13.154  0.115   1.00 158.17 ? 536 GLU A CD    1 
ATOM   4023 O  OE1   . GLU A 1 509 ? 96.636  12.264  0.247   1.00 159.04 ? 536 GLU A OE1   1 
ATOM   4024 O  OE2   . GLU A 1 509 ? 95.301  13.482  -0.995  1.00 149.46 ? 536 GLU A OE2   1 
ATOM   4025 N  N     . TYR A 1 510 ? 94.976  11.543  5.331   1.00 132.33 ? 537 TYR A N     1 
ATOM   4026 C  CA    . TYR A 1 510 ? 95.428  10.919  6.571   1.00 125.28 ? 537 TYR A CA    1 
ATOM   4027 C  C     . TYR A 1 510 ? 95.020  9.453   6.621   1.00 117.62 ? 537 TYR A C     1 
ATOM   4028 O  O     . TYR A 1 510 ? 95.840  8.578   6.920   1.00 116.18 ? 537 TYR A O     1 
ATOM   4029 C  CB    . TYR A 1 510 ? 94.866  11.669  7.780   1.00 116.00 ? 537 TYR A CB    1 
ATOM   4030 C  CG    . TYR A 1 510 ? 95.310  13.112  7.903   1.00 122.59 ? 537 TYR A CG    1 
ATOM   4031 C  CD1   . TYR A 1 510 ? 96.354  13.615  7.137   1.00 128.19 ? 537 TYR A CD1   1 
ATOM   4032 C  CD2   . TYR A 1 510 ? 94.685  13.969  8.798   1.00 122.07 ? 537 TYR A CD2   1 
ATOM   4033 C  CE1   . TYR A 1 510 ? 96.756  14.934  7.254   1.00 120.87 ? 537 TYR A CE1   1 
ATOM   4034 C  CE2   . TYR A 1 510 ? 95.078  15.285  8.922   1.00 127.90 ? 537 TYR A CE2   1 
ATOM   4035 C  CZ    . TYR A 1 510 ? 96.113  15.763  8.150   1.00 131.94 ? 537 TYR A CZ    1 
ATOM   4036 O  OH    . TYR A 1 510 ? 96.503  17.076  8.277   1.00 141.68 ? 537 TYR A OH    1 
ATOM   4037 N  N     . LYS A 1 511 ? 93.750  9.167   6.323   1.00 117.55 ? 538 LYS A N     1 
ATOM   4038 C  CA    . LYS A 1 511 ? 93.263  7.793   6.338   1.00 120.90 ? 538 LYS A CA    1 
ATOM   4039 C  C     . LYS A 1 511 ? 93.956  6.920   5.299   1.00 118.75 ? 538 LYS A C     1 
ATOM   4040 O  O     . LYS A 1 511 ? 93.957  5.692   5.441   1.00 130.60 ? 538 LYS A O     1 
ATOM   4041 C  CB    . LYS A 1 511 ? 91.749  7.773   6.112   1.00 112.45 ? 538 LYS A CB    1 
ATOM   4042 C  CG    . LYS A 1 511 ? 90.959  8.608   7.108   1.00 112.75 ? 538 LYS A CG    1 
ATOM   4043 C  CD    . LYS A 1 511 ? 89.472  8.579   6.797   1.00 116.63 ? 538 LYS A CD    1 
ATOM   4044 C  CE    . LYS A 1 511 ? 89.187  9.152   5.418   1.00 117.11 ? 538 LYS A CE    1 
ATOM   4045 N  NZ    . LYS A 1 511 ? 87.726  9.266   5.159   1.00 120.29 ? 538 LYS A NZ    1 
ATOM   4046 N  N     . ALA A 1 512 ? 94.548  7.521   4.263   1.00 133.34 ? 539 ALA A N     1 
ATOM   4047 C  CA    . ALA A 1 512 ? 95.228  6.733   3.240   1.00 119.29 ? 539 ALA A CA    1 
ATOM   4048 C  C     . ALA A 1 512 ? 96.513  6.105   3.767   1.00 124.77 ? 539 ALA A C     1 
ATOM   4049 O  O     . ALA A 1 512 ? 96.915  5.035   3.295   1.00 133.45 ? 539 ALA A O     1 
ATOM   4050 C  CB    . ALA A 1 512 ? 95.525  7.600   2.018   1.00 123.42 ? 539 ALA A CB    1 
ATOM   4051 N  N     . HIS A 1 513 ? 97.171  6.750   4.734   1.00 126.69 ? 540 HIS A N     1 
ATOM   4052 C  CA    . HIS A 1 513 ? 98.380  6.181   5.319   1.00 121.82 ? 540 HIS A CA    1 
ATOM   4053 C  C     . HIS A 1 513 ? 98.091  4.946   6.161   1.00 120.05 ? 540 HIS A C     1 
ATOM   4054 O  O     . HIS A 1 513 ? 99.016  4.184   6.460   1.00 124.69 ? 540 HIS A O     1 
ATOM   4055 C  CB    . HIS A 1 513 ? 99.101  7.225   6.177   1.00 119.22 ? 540 HIS A CB    1 
ATOM   4056 C  CG    . HIS A 1 513 ? 99.639  8.385   5.399   1.00 134.53 ? 540 HIS A CG    1 
ATOM   4057 N  ND1   . HIS A 1 513 ? 98.913  9.535   5.177   1.00 146.44 ? 540 HIS A ND1   1 
ATOM   4058 C  CD2   . HIS A 1 513 ? 100.837 8.575   4.796   1.00 127.13 ? 540 HIS A CD2   1 
ATOM   4059 C  CE1   . HIS A 1 513 ? 99.638  10.382  4.469   1.00 138.81 ? 540 HIS A CE1   1 
ATOM   4060 N  NE2   . HIS A 1 513 ? 100.810 9.824   4.224   1.00 128.80 ? 540 HIS A NE2   1 
ATOM   4061 N  N     . PHE A 1 514 ? 96.835  4.731   6.545   1.00 120.14 ? 541 PHE A N     1 
ATOM   4062 C  CA    . PHE A 1 514 ? 96.435  3.615   7.396   1.00 120.03 ? 541 PHE A CA    1 
ATOM   4063 C  C     . PHE A 1 514 ? 95.613  2.645   6.557   1.00 119.51 ? 541 PHE A C     1 
ATOM   4064 O  O     . PHE A 1 514 ? 94.463  2.936   6.209   1.00 128.51 ? 541 PHE A O     1 
ATOM   4065 C  CB    . PHE A 1 514 ? 95.654  4.116   8.609   1.00 111.11 ? 541 PHE A CB    1 
ATOM   4066 C  CG    . PHE A 1 514 ? 96.459  5.001   9.521   1.00 110.87 ? 541 PHE A CG    1 
ATOM   4067 C  CD1   . PHE A 1 514 ? 96.628  6.346   9.233   1.00 112.13 ? 541 PHE A CD1   1 
ATOM   4068 C  CD2   . PHE A 1 514 ? 97.052  4.487   10.661  1.00 116.44 ? 541 PHE A CD2   1 
ATOM   4069 C  CE1   . PHE A 1 514 ? 97.371  7.160   10.066  1.00 112.20 ? 541 PHE A CE1   1 
ATOM   4070 C  CE2   . PHE A 1 514 ? 97.795  5.297   11.499  1.00 121.37 ? 541 PHE A CE2   1 
ATOM   4071 C  CZ    . PHE A 1 514 ? 97.956  6.635   11.200  1.00 111.22 ? 541 PHE A CZ    1 
ATOM   4072 N  N     . SER A 1 515 ? 96.205  1.490   6.242   1.00 122.77 ? 542 SER A N     1 
ATOM   4073 C  CA    . SER A 1 515 ? 95.593  0.568   5.289   1.00 125.22 ? 542 SER A CA    1 
ATOM   4074 C  C     . SER A 1 515 ? 94.303  -0.037  5.832   1.00 129.58 ? 542 SER A C     1 
ATOM   4075 O  O     . SER A 1 515 ? 93.314  -0.158  5.099   1.00 135.95 ? 542 SER A O     1 
ATOM   4076 C  CB    . SER A 1 515 ? 96.588  -0.532  4.919   1.00 121.81 ? 542 SER A CB    1 
ATOM   4077 O  OG    . SER A 1 515 ? 97.067  -1.199  6.074   1.00 120.49 ? 542 SER A OG    1 
ATOM   4078 N  N     . LEU A 1 516 ? 94.288  -0.426  7.104   1.00 117.69 ? 543 LEU A N     1 
ATOM   4079 C  CA    . LEU A 1 516 ? 93.140  -1.092  7.708   1.00 114.99 ? 543 LEU A CA    1 
ATOM   4080 C  C     . LEU A 1 516 ? 92.531  -0.180  8.763   1.00 114.78 ? 543 LEU A C     1 
ATOM   4081 O  O     . LEU A 1 516 ? 93.193  0.168   9.745   1.00 122.55 ? 543 LEU A O     1 
ATOM   4082 C  CB    . LEU A 1 516 ? 93.544  -2.432  8.322   1.00 116.10 ? 543 LEU A CB    1 
ATOM   4083 C  CG    . LEU A 1 516 ? 92.420  -3.239  8.973   1.00 118.11 ? 543 LEU A CG    1 
ATOM   4084 C  CD1   . LEU A 1 516 ? 91.249  -3.396  8.015   1.00 116.33 ? 543 LEU A CD1   1 
ATOM   4085 C  CD2   . LEU A 1 516 ? 92.934  -4.597  9.418   1.00 108.92 ? 543 LEU A CD2   1 
ATOM   4086 N  N     . ARG A 1 517 ? 91.270  0.200   8.560   1.00 111.04 ? 544 ARG A N     1 
ATOM   4087 C  CA    . ARG A 1 517 ? 90.551  1.093   9.465   1.00 107.23 ? 544 ARG A CA    1 
ATOM   4088 C  C     . ARG A 1 517 ? 89.232  0.425   9.860   1.00 106.27 ? 544 ARG A C     1 
ATOM   4089 O  O     . ARG A 1 517 ? 88.147  0.868   9.482   1.00 103.46 ? 544 ARG A O     1 
ATOM   4090 C  CB    . ARG A 1 517 ? 90.338  2.464   8.812   1.00 101.89 ? 544 ARG A CB    1 
ATOM   4091 C  CG    . ARG A 1 517 ? 91.618  3.075   8.251   1.00 104.86 ? 544 ARG A CG    1 
ATOM   4092 C  CD    . ARG A 1 517 ? 91.389  4.458   7.663   1.00 105.80 ? 544 ARG A CD    1 
ATOM   4093 N  NE    . ARG A 1 517 ? 90.340  4.463   6.651   1.00 113.44 ? 544 ARG A NE    1 
ATOM   4094 C  CZ    . ARG A 1 517 ? 90.540  4.210   5.365   1.00 115.51 ? 544 ARG A CZ    1 
ATOM   4095 N  NH1   . ARG A 1 517 ? 91.742  3.913   4.898   1.00 112.93 ? 544 ARG A NH1   1 
ATOM   4096 N  NH2   . ARG A 1 517 ? 89.509  4.256   4.527   1.00 114.49 ? 544 ARG A NH2   1 
ATOM   4097 N  N     . ASN A 1 518 ? 89.340  -0.649  10.641  1.00 102.07 ? 545 ASN A N     1 
ATOM   4098 C  CA    . ASN A 1 518 ? 88.206  -1.494  10.994  1.00 104.94 ? 545 ASN A CA    1 
ATOM   4099 C  C     . ASN A 1 518 ? 87.819  -1.377  12.467  1.00 100.11 ? 545 ASN A C     1 
ATOM   4100 O  O     . ASN A 1 518 ? 87.220  -2.303  13.023  1.00 93.75  ? 545 ASN A O     1 
ATOM   4101 C  CB    . ASN A 1 518 ? 88.515  -2.952  10.653  1.00 106.19 ? 545 ASN A CB    1 
ATOM   4102 C  CG    . ASN A 1 518 ? 89.692  -3.495  11.443  1.00 111.45 ? 545 ASN A CG    1 
ATOM   4103 O  OD1   . ASN A 1 518 ? 90.516  -2.734  11.952  1.00 100.89 ? 545 ASN A OD1   1 
ATOM   4104 N  ND2   . ASN A 1 518 ? 89.777  -4.817  11.548  1.00 111.67 ? 545 ASN A ND2   1 
ATOM   4105 N  N     . LEU A 1 519 ? 88.150  -0.261  13.109  1.00 97.95  ? 546 LEU A N     1 
ATOM   4106 C  CA    . LEU A 1 519 ? 87.869  -0.101  14.530  1.00 98.77  ? 546 LEU A CA    1 
ATOM   4107 C  C     . LEU A 1 519 ? 86.376  0.108   14.754  1.00 95.25  ? 546 LEU A C     1 
ATOM   4108 O  O     . LEU A 1 519 ? 85.730  0.878   14.038  1.00 106.04 ? 546 LEU A O     1 
ATOM   4109 C  CB    . LEU A 1 519 ? 88.663  1.077   15.094  1.00 89.52  ? 546 LEU A CB    1 
ATOM   4110 C  CG    . LEU A 1 519 ? 88.772  1.223   16.611  1.00 86.31  ? 546 LEU A CG    1 
ATOM   4111 C  CD1   . LEU A 1 519 ? 89.781  0.236   17.174  1.00 87.08  ? 546 LEU A CD1   1 
ATOM   4112 C  CD2   . LEU A 1 519 ? 89.151  2.649   16.979  1.00 84.86  ? 546 LEU A CD2   1 
ATOM   4113 N  N     . HIS A 1 520 ? 85.825  -0.587  15.747  1.00 88.60  ? 547 HIS A N     1 
ATOM   4114 C  CA    . HIS A 1 520 ? 84.419  -0.452  16.121  1.00 101.16 ? 547 HIS A CA    1 
ATOM   4115 C  C     . HIS A 1 520 ? 84.349  0.499   17.311  1.00 95.41  ? 547 HIS A C     1 
ATOM   4116 O  O     . HIS A 1 520 ? 84.625  0.108   18.448  1.00 80.18  ? 547 HIS A O     1 
ATOM   4117 C  CB    . HIS A 1 520 ? 83.806  -1.809  16.452  1.00 94.89  ? 547 HIS A CB    1 
ATOM   4118 C  CG    . HIS A 1 520 ? 84.009  -2.843  15.389  1.00 101.62 ? 547 HIS A CG    1 
ATOM   4119 N  ND1   . HIS A 1 520 ? 83.411  -2.766  14.150  1.00 104.66 ? 547 HIS A ND1   1 
ATOM   4120 C  CD2   . HIS A 1 520 ? 84.737  -3.985  15.385  1.00 114.37 ? 547 HIS A CD2   1 
ATOM   4121 C  CE1   . HIS A 1 520 ? 83.766  -3.812  13.426  1.00 99.12  ? 547 HIS A CE1   1 
ATOM   4122 N  NE2   . HIS A 1 520 ? 84.570  -4.568  14.153  1.00 109.66 ? 547 HIS A NE2   1 
ATOM   4123 N  N     . ALA A 1 521 ? 83.976  1.749   17.051  1.00 79.95  ? 548 ALA A N     1 
ATOM   4124 C  CA    . ALA A 1 521 ? 83.981  2.790   18.069  1.00 88.09  ? 548 ALA A CA    1 
ATOM   4125 C  C     . ALA A 1 521 ? 82.574  3.327   18.283  1.00 88.48  ? 548 ALA A C     1 
ATOM   4126 O  O     . ALA A 1 521 ? 81.866  3.633   17.318  1.00 76.93  ? 548 ALA A O     1 
ATOM   4127 C  CB    . ALA A 1 521 ? 84.925  3.928   17.690  1.00 86.92  ? 548 ALA A CB    1 
ATOM   4128 N  N     . PHE A 1 522 ? 82.187  3.455   19.549  1.00 76.52  ? 549 PHE A N     1 
ATOM   4129 C  CA    . PHE A 1 522 ? 80.881  3.954   19.945  1.00 76.48  ? 549 PHE A CA    1 
ATOM   4130 C  C     . PHE A 1 522 ? 81.067  5.070   20.964  1.00 75.01  ? 549 PHE A C     1 
ATOM   4131 O  O     . PHE A 1 522 ? 82.179  5.349   21.418  1.00 75.49  ? 549 PHE A O     1 
ATOM   4132 C  CB    . PHE A 1 522 ? 80.010  2.831   20.526  1.00 71.62  ? 549 PHE A CB    1 
ATOM   4133 C  CG    . PHE A 1 522 ? 79.902  1.624   19.637  1.00 84.09  ? 549 PHE A CG    1 
ATOM   4134 C  CD1   . PHE A 1 522 ? 80.863  0.626   19.681  1.00 88.17  ? 549 PHE A CD1   1 
ATOM   4135 C  CD2   . PHE A 1 522 ? 78.838  1.485   18.761  1.00 81.63  ? 549 PHE A CD2   1 
ATOM   4136 C  CE1   . PHE A 1 522 ? 80.768  -0.485  18.864  1.00 88.11  ? 549 PHE A CE1   1 
ATOM   4137 C  CE2   . PHE A 1 522 ? 78.736  0.375   17.943  1.00 81.01  ? 549 PHE A CE2   1 
ATOM   4138 C  CZ    . PHE A 1 522 ? 79.702  -0.611  17.995  1.00 83.26  ? 549 PHE A CZ    1 
ATOM   4139 N  N     . SER A 1 523 ? 79.960  5.715   21.324  1.00 68.52  ? 550 SER A N     1 
ATOM   4140 C  CA    . SER A 1 523 ? 79.987  6.784   22.310  1.00 66.56  ? 550 SER A CA    1 
ATOM   4141 C  C     . SER A 1 523 ? 78.755  6.694   23.196  1.00 75.03  ? 550 SER A C     1 
ATOM   4142 O  O     . SER A 1 523 ? 77.676  6.298   22.749  1.00 74.68  ? 550 SER A O     1 
ATOM   4143 C  CB    . SER A 1 523 ? 80.044  8.169   21.653  1.00 74.77  ? 550 SER A CB    1 
ATOM   4144 O  OG    . SER A 1 523 ? 80.067  9.193   22.632  1.00 74.63  ? 550 SER A OG    1 
ATOM   4145 N  N     . VAL A 1 524 ? 78.932  7.064   24.464  1.00 64.26  ? 551 VAL A N     1 
ATOM   4146 C  CA    . VAL A 1 524 ? 77.799  7.180   25.370  1.00 72.16  ? 551 VAL A CA    1 
ATOM   4147 C  C     . VAL A 1 524 ? 76.936  8.355   24.933  1.00 74.68  ? 551 VAL A C     1 
ATOM   4148 O  O     . VAL A 1 524 ? 77.446  9.390   24.481  1.00 85.17  ? 551 VAL A O     1 
ATOM   4149 C  CB    . VAL A 1 524 ? 78.278  7.349   26.822  1.00 71.82  ? 551 VAL A CB    1 
ATOM   4150 C  CG1   . VAL A 1 524 ? 77.108  7.228   27.785  1.00 75.74  ? 551 VAL A CG1   1 
ATOM   4151 C  CG2   . VAL A 1 524 ? 79.345  6.326   27.154  1.00 71.59  ? 551 VAL A CG2   1 
ATOM   4152 N  N     . GLU A 1 525 ? 75.621  8.199   25.052  1.00 75.84  ? 552 GLU A N     1 
ATOM   4153 C  CA    . GLU A 1 525 ? 74.709  9.269   24.672  1.00 71.98  ? 552 GLU A CA    1 
ATOM   4154 C  C     . GLU A 1 525 ? 73.593  9.407   25.700  1.00 62.86  ? 552 GLU A C     1 
ATOM   4155 O  O     . GLU A 1 525 ? 72.738  8.520   25.811  1.00 69.90  ? 552 GLU A O     1 
ATOM   4156 C  CB    . GLU A 1 525 ? 74.127  9.014   23.282  1.00 75.07  ? 552 GLU A CB    1 
ATOM   4157 C  CG    . GLU A 1 525 ? 73.078  10.030  22.862  1.00 76.42  ? 552 GLU A CG    1 
ATOM   4158 C  CD    . GLU A 1 525 ? 73.595  11.457  22.896  1.00 91.28  ? 552 GLU A CD    1 
ATOM   4159 O  OE1   . GLU A 1 525 ? 74.776  11.674  22.550  1.00 93.34  ? 552 GLU A OE1   1 
ATOM   4160 O  OE2   . GLU A 1 525 ? 72.819  12.361  23.273  1.00 81.27  ? 552 GLU A OE2   1 
ATOM   4161 N  N     . PRO A 1 526 ? 73.556  10.502  26.466  1.00 71.94  ? 553 PRO A N     1 
ATOM   4162 C  CA    . PRO A 1 526 ? 74.476  11.649  26.445  1.00 68.65  ? 553 PRO A CA    1 
ATOM   4163 C  C     . PRO A 1 526 ? 75.823  11.326  27.082  1.00 65.70  ? 553 PRO A C     1 
ATOM   4164 O  O     . PRO A 1 526 ? 76.006  10.254  27.651  1.00 72.59  ? 553 PRO A O     1 
ATOM   4165 C  CB    . PRO A 1 526 ? 73.705  12.715  27.234  1.00 57.08  ? 553 PRO A CB    1 
ATOM   4166 C  CG    . PRO A 1 526 ? 72.886  11.922  28.207  1.00 55.97  ? 553 PRO A CG    1 
ATOM   4167 C  CD    . PRO A 1 526 ? 72.473  10.688  27.448  1.00 67.69  ? 553 PRO A CD    1 
ATOM   4168 N  N     . LEU A 1 527 ? 76.784  12.242  26.997  1.00 65.15  ? 554 LEU A N     1 
ATOM   4169 C  CA    . LEU A 1 527 ? 78.111  11.989  27.536  1.00 68.42  ? 554 LEU A CA    1 
ATOM   4170 C  C     . LEU A 1 527 ? 78.093  12.002  29.060  1.00 68.01  ? 554 LEU A C     1 
ATOM   4171 O  O     . LEU A 1 527 ? 77.252  12.645  29.694  1.00 60.21  ? 554 LEU A O     1 
ATOM   4172 C  CB    . LEU A 1 527 ? 79.105  13.026  27.012  1.00 66.87  ? 554 LEU A CB    1 
ATOM   4173 C  CG    . LEU A 1 527 ? 79.452  12.932  25.525  1.00 72.38  ? 554 LEU A CG    1 
ATOM   4174 C  CD1   . LEU A 1 527 ? 80.161  14.192  25.055  1.00 64.80  ? 554 LEU A CD1   1 
ATOM   4175 C  CD2   . LEU A 1 527 ? 80.311  11.705  25.262  1.00 67.55  ? 554 LEU A CD2   1 
ATOM   4176 N  N     . LEU A 1 528 ? 79.038  11.273  29.649  1.00 67.11  ? 555 LEU A N     1 
ATOM   4177 C  CA    . LEU A 1 528 ? 79.156  11.179  31.096  1.00 65.82  ? 555 LEU A CA    1 
ATOM   4178 C  C     . LEU A 1 528 ? 80.309  11.999  31.655  1.00 66.18  ? 555 LEU A C     1 
ATOM   4179 O  O     . LEU A 1 528 ? 80.404  12.148  32.877  1.00 60.24  ? 555 LEU A O     1 
ATOM   4180 C  CB    . LEU A 1 528 ? 79.326  9.717   31.520  1.00 53.88  ? 555 LEU A CB    1 
ATOM   4181 C  CG    . LEU A 1 528 ? 78.237  8.748   31.061  1.00 66.94  ? 555 LEU A CG    1 
ATOM   4182 C  CD1   . LEU A 1 528 ? 78.496  7.360   31.620  1.00 62.25  ? 555 LEU A CD1   1 
ATOM   4183 C  CD2   . LEU A 1 528 ? 76.865  9.251   31.474  1.00 63.93  ? 555 LEU A CD2   1 
ATOM   4184 N  N     . ILE A 1 529 ? 81.178  12.533  30.800  1.00 63.66  ? 556 ILE A N     1 
ATOM   4185 C  CA    . ILE A 1 529 ? 82.364  13.255  31.241  1.00 59.74  ? 556 ILE A CA    1 
ATOM   4186 C  C     . ILE A 1 529 ? 82.619  14.420  30.295  1.00 61.11  ? 556 ILE A C     1 
ATOM   4187 O  O     . ILE A 1 529 ? 82.552  14.267  29.071  1.00 76.07  ? 556 ILE A O     1 
ATOM   4188 C  CB    . ILE A 1 529 ? 83.586  12.318  31.321  1.00 63.78  ? 556 ILE A CB    1 
ATOM   4189 C  CG1   . ILE A 1 529 ? 83.590  11.581  32.660  1.00 70.40  ? 556 ILE A CG1   1 
ATOM   4190 C  CG2   . ILE A 1 529 ? 84.879  13.082  31.106  1.00 59.02  ? 556 ILE A CG2   1 
ATOM   4191 C  CD1   . ILE A 1 529 ? 84.742  10.636  32.832  1.00 80.32  ? 556 ILE A CD1   1 
ATOM   4192 N  N     . TYR A 1 530 ? 82.901  15.582  30.868  1.00 56.71  ? 557 TYR A N     1 
ATOM   4193 C  CA    . TYR A 1 530 ? 83.210  16.808  30.151  1.00 58.35  ? 557 TYR A CA    1 
ATOM   4194 C  C     . TYR A 1 530 ? 84.499  17.396  30.700  1.00 67.06  ? 557 TYR A C     1 
ATOM   4195 O  O     . TYR A 1 530 ? 84.930  17.040  31.802  1.00 69.12  ? 557 TYR A O     1 
ATOM   4196 C  CB    . TYR A 1 530 ? 82.067  17.826  30.288  1.00 57.56  ? 557 TYR A CB    1 
ATOM   4197 C  CG    . TYR A 1 530 ? 80.788  17.401  29.608  1.00 57.62  ? 557 TYR A CG    1 
ATOM   4198 C  CD1   . TYR A 1 530 ? 80.544  17.729  28.281  1.00 59.03  ? 557 TYR A CD1   1 
ATOM   4199 C  CD2   . TYR A 1 530 ? 79.826  16.671  30.291  1.00 67.15  ? 557 TYR A CD2   1 
ATOM   4200 C  CE1   . TYR A 1 530 ? 79.375  17.342  27.653  1.00 66.35  ? 557 TYR A CE1   1 
ATOM   4201 C  CE2   . TYR A 1 530 ? 78.654  16.280  29.672  1.00 72.34  ? 557 TYR A CE2   1 
ATOM   4202 C  CZ    . TYR A 1 530 ? 78.434  16.618  28.353  1.00 79.28  ? 557 TYR A CZ    1 
ATOM   4203 O  OH    . TYR A 1 530 ? 77.268  16.231  27.731  1.00 84.03  ? 557 TYR A OH    1 
ATOM   4204 N  N     . PRO A 1 531 ? 85.149  18.289  29.955  1.00 81.52  ? 558 PRO A N     1 
ATOM   4205 C  CA    . PRO A 1 531 ? 86.334  18.961  30.497  1.00 78.79  ? 558 PRO A CA    1 
ATOM   4206 C  C     . PRO A 1 531 ? 85.962  19.889  31.641  1.00 71.22  ? 558 PRO A C     1 
ATOM   4207 O  O     . PRO A 1 531 ? 84.869  20.459  31.682  1.00 70.57  ? 558 PRO A O     1 
ATOM   4208 C  CB    . PRO A 1 531 ? 86.881  19.751  29.301  1.00 79.34  ? 558 PRO A CB    1 
ATOM   4209 C  CG    . PRO A 1 531 ? 86.252  19.132  28.101  1.00 75.04  ? 558 PRO A CG    1 
ATOM   4210 C  CD    . PRO A 1 531 ? 84.910  18.657  28.549  1.00 67.56  ? 558 PRO A CD    1 
ATOM   4211 N  N     . THR A 1 532 ? 86.892  20.034  32.586  1.00 74.73  ? 559 THR A N     1 
ATOM   4212 C  CA    . THR A 1 532 ? 86.692  20.983  33.676  1.00 72.98  ? 559 THR A CA    1 
ATOM   4213 C  C     . THR A 1 532 ? 86.774  22.415  33.164  1.00 75.79  ? 559 THR A C     1 
ATOM   4214 O  O     . THR A 1 532 ? 85.847  23.213  33.351  1.00 77.74  ? 559 THR A O     1 
ATOM   4215 C  CB    . THR A 1 532 ? 87.723  20.746  34.781  1.00 70.34  ? 559 THR A CB    1 
ATOM   4216 O  OG1   . THR A 1 532 ? 89.043  20.814  34.228  1.00 74.61  ? 559 THR A OG1   1 
ATOM   4217 C  CG2   . THR A 1 532 ? 87.513  19.384  35.417  1.00 76.13  ? 559 THR A CG2   1 
ATOM   4218 N  N     . HIS A 1 533 ? 87.878  22.753  32.506  1.00 82.65  ? 560 HIS A N     1 
ATOM   4219 C  CA    . HIS A 1 533 ? 88.085  24.068  31.925  1.00 92.42  ? 560 HIS A CA    1 
ATOM   4220 C  C     . HIS A 1 533 ? 88.096  23.962  30.407  1.00 97.17  ? 560 HIS A C     1 
ATOM   4221 O  O     . HIS A 1 533 ? 88.709  23.050  29.843  1.00 92.77  ? 560 HIS A O     1 
ATOM   4222 C  CB    . HIS A 1 533 ? 89.401  24.686  32.406  1.00 83.46  ? 560 HIS A CB    1 
ATOM   4223 C  CG    . HIS A 1 533 ? 89.505  24.810  33.894  1.00 85.48  ? 560 HIS A CG    1 
ATOM   4224 N  ND1   . HIS A 1 533 ? 89.633  23.719  34.726  1.00 91.71  ? 560 HIS A ND1   1 
ATOM   4225 C  CD2   . HIS A 1 533 ? 89.504  25.899  34.699  1.00 86.06  ? 560 HIS A CD2   1 
ATOM   4226 C  CE1   . HIS A 1 533 ? 89.705  24.130  35.980  1.00 93.92  ? 560 HIS A CE1   1 
ATOM   4227 N  NE2   . HIS A 1 533 ? 89.630  25.449  35.991  1.00 84.56  ? 560 HIS A NE2   1 
ATOM   4228 N  N     . TYR A 1 534 ? 87.411  24.891  29.753  1.00 107.84 ? 561 TYR A N     1 
ATOM   4229 C  CA    . TYR A 1 534 ? 87.479  25.039  28.308  1.00 114.65 ? 561 TYR A CA    1 
ATOM   4230 C  C     . TYR A 1 534 ? 88.498  26.114  27.948  1.00 114.06 ? 561 TYR A C     1 
ATOM   4231 O  O     . TYR A 1 534 ? 88.971  26.870  28.801  1.00 117.49 ? 561 TYR A O     1 
ATOM   4232 C  CB    . TYR A 1 534 ? 86.100  25.381  27.733  1.00 111.58 ? 561 TYR A CB    1 
ATOM   4233 C  CG    . TYR A 1 534 ? 85.125  24.225  27.755  1.00 113.67 ? 561 TYR A CG    1 
ATOM   4234 C  CD1   . TYR A 1 534 ? 84.396  23.927  28.900  1.00 109.42 ? 561 TYR A CD1   1 
ATOM   4235 C  CD2   . TYR A 1 534 ? 84.934  23.430  26.631  1.00 103.97 ? 561 TYR A CD2   1 
ATOM   4236 C  CE1   . TYR A 1 534 ? 83.504  22.871  28.925  1.00 98.22  ? 561 TYR A CE1   1 
ATOM   4237 C  CE2   . TYR A 1 534 ? 84.044  22.373  26.647  1.00 102.14 ? 561 TYR A CE2   1 
ATOM   4238 C  CZ    . TYR A 1 534 ? 83.333  22.098  27.795  1.00 95.05  ? 561 TYR A CZ    1 
ATOM   4239 O  OH    . TYR A 1 534 ? 82.447  21.046  27.811  1.00 88.72  ? 561 TYR A OH    1 
ATOM   4240 N  N     . THR A 1 535 ? 88.845  26.169  26.664  1.00 113.47 ? 562 THR A N     1 
ATOM   4241 C  CA    . THR A 1 535 ? 89.803  27.162  26.195  1.00 115.10 ? 562 THR A CA    1 
ATOM   4242 C  C     . THR A 1 535 ? 89.275  28.568  26.452  1.00 107.12 ? 562 THR A C     1 
ATOM   4243 O  O     . THR A 1 535 ? 88.156  28.909  26.055  1.00 113.58 ? 562 THR A O     1 
ATOM   4244 C  CB    . THR A 1 535 ? 90.088  26.967  24.706  1.00 111.44 ? 562 THR A CB    1 
ATOM   4245 O  OG1   . THR A 1 535 ? 90.505  25.616  24.472  1.00 112.86 ? 562 THR A OG1   1 
ATOM   4246 C  CG2   . THR A 1 535 ? 91.190  27.914  24.247  1.00 94.42  ? 562 THR A CG2   1 
ATOM   4247 N  N     . GLY A 1 536 ? 90.084  29.381  27.131  1.00 103.11 ? 563 GLY A N     1 
ATOM   4248 C  CA    . GLY A 1 536 ? 89.699  30.716  27.522  1.00 104.79 ? 563 GLY A CA    1 
ATOM   4249 C  C     . GLY A 1 536 ? 89.210  30.835  28.951  1.00 111.31 ? 563 GLY A C     1 
ATOM   4250 O  O     . GLY A 1 536 ? 89.183  31.947  29.492  1.00 112.76 ? 563 GLY A O     1 
ATOM   4251 N  N     . ASP A 1 537 ? 88.817  29.726  29.570  1.00 134.45 ? 564 ASP A N     1 
ATOM   4252 C  CA    . ASP A 1 537 ? 88.397  29.753  30.962  1.00 133.66 ? 564 ASP A CA    1 
ATOM   4253 C  C     . ASP A 1 537 ? 89.592  30.014  31.871  1.00 126.90 ? 564 ASP A C     1 
ATOM   4254 O  O     . ASP A 1 537 ? 90.737  29.699  31.536  1.00 124.20 ? 564 ASP A O     1 
ATOM   4255 C  CB    . ASP A 1 537 ? 87.722  28.435  31.349  1.00 126.65 ? 564 ASP A CB    1 
ATOM   4256 C  CG    . ASP A 1 537 ? 86.503  28.129  30.500  1.00 128.97 ? 564 ASP A CG    1 
ATOM   4257 O  OD1   . ASP A 1 537 ? 86.267  28.852  29.506  1.00 138.15 ? 564 ASP A OD1   1 
ATOM   4258 O  OD2   . ASP A 1 537 ? 85.777  27.167  30.827  1.00 120.99 ? 564 ASP A OD2   1 
ATOM   4259 N  N     . ASP A 1 538 ? 89.314  30.600  33.032  1.00 116.74 ? 565 ASP A N     1 
ATOM   4260 C  CA    . ASP A 1 538 ? 90.366  30.913  33.991  1.00 111.83 ? 565 ASP A CA    1 
ATOM   4261 C  C     . ASP A 1 538 ? 90.938  29.623  34.568  1.00 105.35 ? 565 ASP A C     1 
ATOM   4262 O  O     . ASP A 1 538 ? 90.200  28.805  35.128  1.00 105.53 ? 565 ASP A O     1 
ATOM   4263 C  CB    . ASP A 1 538 ? 89.816  31.807  35.099  1.00 110.97 ? 565 ASP A CB    1 
ATOM   4264 C  CG    . ASP A 1 538 ? 90.902  32.342  36.012  1.00 120.92 ? 565 ASP A CG    1 
ATOM   4265 O  OD1   . ASP A 1 538 ? 92.096  32.182  35.683  1.00 132.89 ? 565 ASP A OD1   1 
ATOM   4266 O  OD2   . ASP A 1 538 ? 90.560  32.924  37.063  1.00 118.82 ? 565 ASP A OD2   1 
ATOM   4267 N  N     . GLY A 1 539 ? 92.250  29.441  34.433  1.00 92.90  ? 566 GLY A N     1 
ATOM   4268 C  CA    . GLY A 1 539 ? 92.914  28.246  34.906  1.00 88.16  ? 566 GLY A CA    1 
ATOM   4269 C  C     . GLY A 1 539 ? 93.062  27.146  33.878  1.00 93.18  ? 566 GLY A C     1 
ATOM   4270 O  O     . GLY A 1 539 ? 93.543  26.059  34.224  1.00 108.76 ? 566 GLY A O     1 
ATOM   4271 N  N     . TYR A 1 540 ? 92.667  27.391  32.631  1.00 100.00 ? 567 TYR A N     1 
ATOM   4272 C  CA    . TYR A 1 540 ? 92.779  26.383  31.585  1.00 108.62 ? 567 TYR A CA    1 
ATOM   4273 C  C     . TYR A 1 540 ? 94.243  26.076  31.298  1.00 110.34 ? 567 TYR A C     1 
ATOM   4274 O  O     . TYR A 1 540 ? 95.061  26.986  31.136  1.00 103.17 ? 567 TYR A O     1 
ATOM   4275 C  CB    . TYR A 1 540 ? 92.073  26.869  30.321  1.00 110.85 ? 567 TYR A CB    1 
ATOM   4276 C  CG    . TYR A 1 540 ? 92.268  25.994  29.102  1.00 112.96 ? 567 TYR A CG    1 
ATOM   4277 C  CD1   . TYR A 1 540 ? 91.536  24.826  28.935  1.00 115.34 ? 567 TYR A CD1   1 
ATOM   4278 C  CD2   . TYR A 1 540 ? 93.170  26.352  28.108  1.00 113.76 ? 567 TYR A CD2   1 
ATOM   4279 C  CE1   . TYR A 1 540 ? 91.706  24.031  27.816  1.00 122.18 ? 567 TYR A CE1   1 
ATOM   4280 C  CE2   . TYR A 1 540 ? 93.346  25.565  26.987  1.00 118.47 ? 567 TYR A CE2   1 
ATOM   4281 C  CZ    . TYR A 1 540 ? 92.612  24.406  26.846  1.00 129.24 ? 567 TYR A CZ    1 
ATOM   4282 O  OH    . TYR A 1 540 ? 92.784  23.618  25.731  1.00 113.10 ? 567 TYR A OH    1 
ATOM   4283 N  N     . VAL A 1 541 ? 94.571  24.787  31.245  1.00 119.57 ? 568 VAL A N     1 
ATOM   4284 C  CA    . VAL A 1 541 ? 95.929  24.320  30.997  1.00 119.34 ? 568 VAL A CA    1 
ATOM   4285 C  C     . VAL A 1 541 ? 95.880  23.240  29.927  1.00 122.91 ? 568 VAL A C     1 
ATOM   4286 O  O     . VAL A 1 541 ? 95.133  22.264  30.060  1.00 125.61 ? 568 VAL A O     1 
ATOM   4287 C  CB    . VAL A 1 541 ? 96.595  23.783  32.279  1.00 119.35 ? 568 VAL A CB    1 
ATOM   4288 C  CG1   . VAL A 1 541 ? 97.895  23.077  31.939  1.00 113.94 ? 568 VAL A CG1   1 
ATOM   4289 C  CG2   . VAL A 1 541 ? 96.845  24.914  33.259  1.00 106.84 ? 568 VAL A CG2   1 
ATOM   4290 N  N     . SER A 1 542 ? 96.678  23.417  28.872  1.00 149.22 ? 569 SER A N     1 
ATOM   4291 C  CA    . SER A 1 542 ? 96.772  22.471  27.760  1.00 151.31 ? 569 SER A CA    1 
ATOM   4292 C  C     . SER A 1 542 ? 98.251  22.190  27.512  1.00 158.15 ? 569 SER A C     1 
ATOM   4293 O  O     . SER A 1 542 ? 98.876  22.830  26.664  1.00 174.84 ? 569 SER A O     1 
ATOM   4294 C  CB    . SER A 1 542 ? 96.084  23.016  26.515  1.00 166.41 ? 569 SER A CB    1 
ATOM   4295 O  OG    . SER A 1 542 ? 96.197  22.102  25.438  1.00 168.86 ? 569 SER A OG    1 
ATOM   4296 N  N     . ASP A 1 543 ? 98.804  21.244  28.273  1.00 127.23 ? 570 ASP A N     1 
ATOM   4297 C  CA    . ASP A 1 543 ? 100.251 20.918  28.143  1.00 123.39 ? 570 ASP A CA    1 
ATOM   4298 C  C     . ASP A 1 543 ? 100.501 20.306  26.762  1.00 129.58 ? 570 ASP A C     1 
ATOM   4299 O  O     . ASP A 1 543 ? 101.675 20.263  26.340  1.00 135.64 ? 570 ASP A O     1 
ATOM   4300 C  CB    . ASP A 1 543 ? 100.716 20.059  29.306  1.00 121.79 ? 570 ASP A CB    1 
ATOM   4301 C  CG    . ASP A 1 543 ? 100.826 20.796  30.632  1.00 127.74 ? 570 ASP A CG    1 
ATOM   4302 O  OD1   . ASP A 1 543 ? 100.602 22.023  30.636  1.00 135.63 ? 570 ASP A OD1   1 
ATOM   4303 O  OD2   . ASP A 1 543 ? 101.135 20.140  31.646  1.00 124.08 ? 570 ASP A OD2   1 
ATOM   4304 N  N     . THR A 1 544 ? 99.443  19.849  26.088  1.00 130.05 ? 571 THR A N     1 
ATOM   4305 C  CA    . THR A 1 544 ? 99.604  19.334  24.712  1.00 132.96 ? 571 THR A CA    1 
ATOM   4306 C  C     . THR A 1 544 ? 99.883  20.503  23.794  1.00 136.39 ? 571 THR A C     1 
ATOM   4307 O  O     . THR A 1 544 ? 100.827 20.407  22.982  1.00 142.64 ? 571 THR A O     1 
ATOM   4308 C  CB    . THR A 1 544 ? 98.354  18.566  24.290  1.00 123.45 ? 571 THR A CB    1 
ATOM   4309 O  OG1   . THR A 1 544 ? 97.275  19.460  24.541  1.00 134.33 ? 571 THR A OG1   1 
ATOM   4310 C  CG2   . THR A 1 544 ? 98.175  17.279  25.074  1.00 116.15 ? 571 THR A CG2   1 
ATOM   4311 N  N     . GLU A 1 545 ? 99.099  21.577  23.923  1.00 158.52 ? 572 GLU A N     1 
ATOM   4312 C  CA    . GLU A 1 545 ? 99.302  22.798  23.099  1.00 153.52 ? 572 GLU A CA    1 
ATOM   4313 C  C     . GLU A 1 545 ? 100.213 23.772  23.861  1.00 157.07 ? 572 GLU A C     1 
ATOM   4314 O  O     . GLU A 1 545 ? 99.705  24.804  24.349  1.00 157.67 ? 572 GLU A O     1 
ATOM   4315 C  CB    . GLU A 1 545 ? 97.966  23.452  22.743  1.00 155.57 ? 572 GLU A CB    1 
ATOM   4316 C  CG    . GLU A 1 545 ? 98.089  24.516  21.655  1.00 164.09 ? 572 GLU A CG    1 
ATOM   4317 C  CD    . GLU A 1 545 ? 98.789  24.040  20.395  1.00 167.15 ? 572 GLU A CD    1 
ATOM   4318 O  OE1   . GLU A 1 545 ? 98.297  23.074  19.774  1.00 162.76 ? 572 GLU A OE1   1 
ATOM   4319 O  OE2   . GLU A 1 545 ? 99.825  24.636  20.033  1.00 161.80 ? 572 GLU A OE2   1 
ATOM   4320 N  N     . THR A 1 546 ? 101.503 23.446  23.967  1.00 169.50 ? 573 THR A N     1 
ATOM   4321 C  CA    . THR A 1 546 ? 102.467 24.356  24.624  1.00 169.20 ? 573 THR A CA    1 
ATOM   4322 C  C     . THR A 1 546 ? 103.311 25.006  23.551  1.00 170.10 ? 573 THR A C     1 
ATOM   4323 O  O     . THR A 1 546 ? 104.468 25.375  23.852  1.00 168.31 ? 573 THR A O     1 
ATOM   4324 C  CB    . THR A 1 546 ? 103.311 23.588  25.640  1.00 163.18 ? 573 THR A CB    1 
ATOM   4325 O  OG1   . THR A 1 546 ? 103.487 22.289  25.084  1.00 162.51 ? 573 THR A OG1   1 
ATOM   4326 C  CG2   . THR A 1 546 ? 102.628 23.474  26.990  1.00 153.82 ? 573 THR A CG2   1 
ATOM   4327 N  N     . SER A 1 547 ? 102.765 25.135  22.338  1.00 166.41 ? 574 SER A N     1 
ATOM   4328 C  CA    . SER A 1 547 ? 103.486 25.805  21.224  1.00 173.15 ? 574 SER A CA    1 
ATOM   4329 C  C     . SER A 1 547 ? 104.937 25.310  21.151  1.00 181.14 ? 574 SER A C     1 
ATOM   4330 O  O     . SER A 1 547 ? 105.853 26.161  21.193  1.00 178.49 ? 574 SER A O     1 
ATOM   4331 C  CB    . SER A 1 547 ? 103.424 27.307  21.360  1.00 168.84 ? 574 SER A CB    1 
ATOM   4332 O  OG    . SER A 1 547 ? 104.121 27.748  22.517  1.00 167.27 ? 574 SER A OG    1 
ATOM   4333 N  N     . VAL A 1 548 ? 105.131 23.988  21.044  1.00 172.01 ? 575 VAL A N     1 
ATOM   4334 C  CA    . VAL A 1 548 ? 106.502 23.393  20.953  1.00 166.37 ? 575 VAL A CA    1 
ATOM   4335 C  C     . VAL A 1 548 ? 106.462 22.212  19.970  1.00 154.46 ? 575 VAL A C     1 
ATOM   4336 O  O     . VAL A 1 548 ? 106.002 21.126  20.380  1.00 142.04 ? 575 VAL A O     1 
ATOM   4337 C  CB    . VAL A 1 548 ? 107.016 22.947  22.334  1.00 154.60 ? 575 VAL A CB    1 
ATOM   4338 C  CG1   . VAL A 1 548 ? 106.041 21.997  23.020  1.00 143.94 ? 575 VAL A CG1   1 
ATOM   4339 C  CG2   . VAL A 1 548 ? 108.405 22.326  22.249  1.00 133.95 ? 575 VAL A CG2   1 
ATOM   4340 N  N     . VAL A 1 549 ? 106.946 22.410  18.739  1.00 156.72 ? 576 VAL A N     1 
ATOM   4341 C  CA    . VAL A 1 549 ? 106.884 21.344  17.690  1.00 154.56 ? 576 VAL A CA    1 
ATOM   4342 C  C     . VAL A 1 549 ? 107.671 20.110  18.160  1.00 152.76 ? 576 VAL A C     1 
ATOM   4343 O  O     . VAL A 1 549 ? 108.685 20.287  18.865  1.00 154.78 ? 576 VAL A O     1 
ATOM   4344 C  CB    . VAL A 1 549 ? 107.415 21.867  16.341  1.00 155.58 ? 576 VAL A CB    1 
ATOM   4345 C  CG1   . VAL A 1 549 ? 107.277 20.831  15.232  1.00 158.04 ? 576 VAL A CG1   1 
ATOM   4346 C  CG2   . VAL A 1 549 ? 106.734 23.169  15.938  1.00 153.22 ? 576 VAL A CG2   1 
ATOM   4347 N  N     . TRP A 1 550 ? 107.218 18.914  17.776  1.00 148.34 ? 577 TRP A N     1 
ATOM   4348 C  CA    . TRP A 1 550 ? 107.886 17.659  18.201  1.00 148.38 ? 577 TRP A CA    1 
ATOM   4349 C  C     . TRP A 1 550 ? 109.272 17.553  17.565  1.00 155.12 ? 577 TRP A C     1 
ATOM   4350 O  O     . TRP A 1 550 ? 110.205 17.097  18.260  1.00 153.62 ? 577 TRP A O     1 
ATOM   4351 C  CB    . TRP A 1 550 ? 107.021 16.456  17.804  1.00 150.93 ? 577 TRP A CB    1 
ATOM   4352 C  CG    . TRP A 1 550 ? 107.099 16.124  16.337  1.00 157.97 ? 577 TRP A CG    1 
ATOM   4353 C  CD1   . TRP A 1 550 ? 106.359 16.669  15.329  1.00 161.68 ? 577 TRP A CD1   1 
ATOM   4354 C  CD2   . TRP A 1 550 ? 107.985 15.170  15.712  1.00 162.60 ? 577 TRP A CD2   1 
ATOM   4355 N  NE1   . TRP A 1 550 ? 106.719 16.125  14.126  1.00 168.32 ? 577 TRP A NE1   1 
ATOM   4356 C  CE2   . TRP A 1 550 ? 107.712 15.203  14.328  1.00 168.87 ? 577 TRP A CE2   1 
ATOM   4357 C  CE3   . TRP A 1 550 ? 108.973 14.299  16.184  1.00 162.44 ? 577 TRP A CE3   1 
ATOM   4358 C  CZ2   . TRP A 1 550 ? 108.393 14.398  13.418  1.00 174.68 ? 577 TRP A CZ2   1 
ATOM   4359 C  CZ3   . TRP A 1 550 ? 109.644 13.504  15.282  1.00 168.25 ? 577 TRP A CZ3   1 
ATOM   4360 C  CH2   . TRP A 1 550 ? 109.356 13.554  13.920  1.00 174.16 ? 577 TRP A CH2   1 
ATOM   4361 N  N     . ASN A 1 551 ? 109.410 17.957  16.298  1.00 158.17 ? 578 ASN A N     1 
ATOM   4362 C  CA    . ASN A 1 551 ? 110.702 17.776  15.577  1.00 161.85 ? 578 ASN A CA    1 
ATOM   4363 C  C     . ASN A 1 551 ? 111.857 18.280  16.445  1.00 159.90 ? 578 ASN A C     1 
ATOM   4364 O  O     . ASN A 1 551 ? 112.793 17.492  16.700  1.00 160.80 ? 578 ASN A O     1 
ATOM   4365 C  CB    . ASN A 1 551 ? 110.675 18.453  14.211  1.00 167.53 ? 578 ASN A CB    1 
ATOM   4366 C  CG    . ASN A 1 551 ? 111.750 17.916  13.298  1.00 175.02 ? 578 ASN A CG    1 
ATOM   4367 O  OD1   . ASN A 1 551 ? 111.795 16.710  13.033  1.00 179.77 ? 578 ASN A OD1   1 
ATOM   4368 N  ND2   . ASN A 1 551 ? 112.624 18.786  12.813  1.00 180.13 ? 578 ASN A ND2   1 
ATOM   4369 N  N     . ASN A 1 552 ? 111.793 19.542  16.874  1.00 161.62 ? 579 ASN A N     1 
ATOM   4370 C  CA    . ASN A 1 552 ? 112.886 20.137  17.689  1.00 161.23 ? 579 ASN A CA    1 
ATOM   4371 C  C     . ASN A 1 552 ? 112.324 21.284  18.531  1.00 163.00 ? 579 ASN A C     1 
ATOM   4372 O  O     . ASN A 1 552 ? 111.139 21.633  18.343  1.00 161.97 ? 579 ASN A O     1 
ATOM   4373 C  CB    . ASN A 1 552 ? 114.044 20.601  16.813  1.00 171.67 ? 579 ASN A CB    1 
ATOM   4374 C  CG    . ASN A 1 552 ? 113.589 21.497  15.686  1.00 179.01 ? 579 ASN A CG    1 
ATOM   4375 O  OD1   . ASN A 1 552 ? 113.035 22.576  15.927  1.00 176.12 ? 579 ASN A OD1   1 
ATOM   4376 N  ND2   . ASN A 1 552 ? 113.820 21.077  14.451  1.00 182.39 ? 579 ASN A ND2   1 
ATOM   4377 N  N     . GLU A 1 553 ? 113.147 21.849  19.416  1.00 169.91 ? 580 GLU A N     1 
ATOM   4378 C  CA    . GLU A 1 553 ? 112.710 22.994  20.255  1.00 162.47 ? 580 GLU A CA    1 
ATOM   4379 C  C     . GLU A 1 553 ? 111.793 23.909  19.427  1.00 151.80 ? 580 GLU A C     1 
ATOM   4380 O  O     . GLU A 1 553 ? 112.307 24.510  18.459  1.00 157.23 ? 580 GLU A O     1 
ATOM   4381 C  CB    . GLU A 1 553 ? 113.942 23.739  20.768  1.00 155.25 ? 580 GLU A CB    1 
ATOM   4382 C  CG    . GLU A 1 553 ? 114.972 22.817  21.411  1.00 146.67 ? 580 GLU A CG    1 
ATOM   4383 C  CD    . GLU A 1 553 ? 114.423 21.981  22.553  1.00 153.82 ? 580 GLU A CD    1 
ATOM   4384 O  OE1   . GLU A 1 553 ? 113.953 22.572  23.547  1.00 147.95 ? 580 GLU A OE1   1 
ATOM   4385 O  OE2   . GLU A 1 553 ? 114.463 20.737  22.445  1.00 152.06 ? 580 GLU A OE2   1 
ATOM   4386 N  N     . ARG B 1 15  ? 63.664  48.023  40.754  1.00 69.11  ? 42  ARG B N     1 
ATOM   4387 C  CA    . ARG B 1 15  ? 62.368  48.016  41.422  1.00 78.85  ? 42  ARG B CA    1 
ATOM   4388 C  C     . ARG B 1 15  ? 62.483  48.467  42.873  1.00 72.61  ? 42  ARG B C     1 
ATOM   4389 O  O     . ARG B 1 15  ? 62.864  47.682  43.743  1.00 85.09  ? 42  ARG B O     1 
ATOM   4390 C  CB    . ARG B 1 15  ? 61.737  46.621  41.363  1.00 78.99  ? 42  ARG B CB    1 
ATOM   4391 C  CG    . ARG B 1 15  ? 60.921  46.353  40.110  1.00 104.52 ? 42  ARG B CG    1 
ATOM   4392 C  CD    . ARG B 1 15  ? 59.681  47.230  40.067  1.00 100.97 ? 42  ARG B CD    1 
ATOM   4393 N  NE    . ARG B 1 15  ? 58.943  47.204  41.324  1.00 107.28 ? 42  ARG B NE    1 
ATOM   4394 C  CZ    . ARG B 1 15  ? 57.724  47.703  41.482  1.00 114.60 ? 42  ARG B CZ    1 
ATOM   4395 N  NH1   . ARG B 1 15  ? 57.062  48.239  40.468  1.00 86.24  ? 42  ARG B NH1   1 
ATOM   4396 N  NH2   . ARG B 1 15  ? 57.155  47.662  42.684  1.00 83.00  ? 42  ARG B NH2   1 
ATOM   4397 N  N     . TRP B 1 16  ? 62.154  49.731  43.132  1.00 59.55  ? 43  TRP B N     1 
ATOM   4398 C  CA    . TRP B 1 16  ? 62.128  50.219  44.504  1.00 59.53  ? 43  TRP B CA    1 
ATOM   4399 C  C     . TRP B 1 16  ? 60.930  49.638  45.242  1.00 60.56  ? 43  TRP B C     1 
ATOM   4400 O  O     . TRP B 1 16  ? 59.813  49.613  44.717  1.00 62.90  ? 43  TRP B O     1 
ATOM   4401 C  CB    . TRP B 1 16  ? 62.069  51.745  44.549  1.00 55.53  ? 43  TRP B CB    1 
ATOM   4402 C  CG    . TRP B 1 16  ? 61.842  52.255  45.947  1.00 58.93  ? 43  TRP B CG    1 
ATOM   4403 C  CD1   . TRP B 1 16  ? 62.756  52.293  46.961  1.00 60.52  ? 43  TRP B CD1   1 
ATOM   4404 C  CD2   . TRP B 1 16  ? 60.620  52.779  46.491  1.00 59.12  ? 43  TRP B CD2   1 
ATOM   4405 N  NE1   . TRP B 1 16  ? 62.184  52.813  48.098  1.00 58.89  ? 43  TRP B NE1   1 
ATOM   4406 C  CE2   . TRP B 1 16  ? 60.874  53.121  47.837  1.00 55.94  ? 43  TRP B CE2   1 
ATOM   4407 C  CE3   . TRP B 1 16  ? 59.340  52.998  45.972  1.00 61.96  ? 43  TRP B CE3   1 
ATOM   4408 C  CZ2   . TRP B 1 16  ? 59.897  53.669  48.668  1.00 50.92  ? 43  TRP B CZ2   1 
ATOM   4409 C  CZ3   . TRP B 1 16  ? 58.369  53.542  46.800  1.00 55.63  ? 43  TRP B CZ3   1 
ATOM   4410 C  CH2   . TRP B 1 16  ? 58.653  53.871  48.133  1.00 62.47  ? 43  TRP B CH2   1 
ATOM   4411 N  N     . SER B 1 17  ? 61.169  49.159  46.457  1.00 53.04  ? 44  SER B N     1 
ATOM   4412 C  CA    . SER B 1 17  ? 60.089  48.703  47.317  1.00 51.69  ? 44  SER B CA    1 
ATOM   4413 C  C     . SER B 1 17  ? 60.398  49.149  48.739  1.00 51.42  ? 44  SER B C     1 
ATOM   4414 O  O     . SER B 1 17  ? 61.475  48.843  49.272  1.00 62.62  ? 44  SER B O     1 
ATOM   4415 C  CB    . SER B 1 17  ? 59.912  47.187  47.245  1.00 59.40  ? 44  SER B CB    1 
ATOM   4416 O  OG    . SER B 1 17  ? 58.771  46.772  47.973  1.00 80.12  ? 44  SER B OG    1 
ATOM   4417 N  N     . PRO B 1 18  ? 59.492  49.884  49.378  1.00 52.45  ? 45  PRO B N     1 
ATOM   4418 C  CA    . PRO B 1 18  ? 59.772  50.384  50.725  1.00 52.66  ? 45  PRO B CA    1 
ATOM   4419 C  C     . PRO B 1 18  ? 59.781  49.260  51.745  1.00 53.65  ? 45  PRO B C     1 
ATOM   4420 O  O     . PRO B 1 18  ? 59.043  48.278  51.633  1.00 60.25  ? 45  PRO B O     1 
ATOM   4421 C  CB    . PRO B 1 18  ? 58.620  51.361  50.986  1.00 47.80  ? 45  PRO B CB    1 
ATOM   4422 C  CG    . PRO B 1 18  ? 57.505  50.832  50.146  1.00 49.29  ? 45  PRO B CG    1 
ATOM   4423 C  CD    . PRO B 1 18  ? 58.155  50.282  48.905  1.00 54.31  ? 45  PRO B CD    1 
ATOM   4424 N  N     . GLU B 1 19  ? 60.645  49.411  52.744  1.00 49.74  ? 46  GLU B N     1 
ATOM   4425 C  CA    . GLU B 1 19  ? 60.682  48.498  53.875  1.00 46.03  ? 46  GLU B CA    1 
ATOM   4426 C  C     . GLU B 1 19  ? 59.802  49.045  54.990  1.00 50.11  ? 46  GLU B C     1 
ATOM   4427 O  O     . GLU B 1 19  ? 59.729  50.260  55.196  1.00 57.96  ? 46  GLU B O     1 
ATOM   4428 C  CB    . GLU B 1 19  ? 62.114  48.309  54.376  1.00 42.25  ? 46  GLU B CB    1 
ATOM   4429 C  CG    . GLU B 1 19  ? 63.028  47.578  53.400  1.00 62.11  ? 46  GLU B CG    1 
ATOM   4430 C  CD    . GLU B 1 19  ? 62.683  46.106  53.260  1.00 67.73  ? 46  GLU B CD    1 
ATOM   4431 O  OE1   . GLU B 1 19  ? 62.418  45.458  54.294  1.00 59.73  ? 46  GLU B OE1   1 
ATOM   4432 O  OE2   . GLU B 1 19  ? 62.676  45.598  52.117  1.00 74.77  ? 46  GLU B OE2   1 
ATOM   4433 N  N     . SER B 1 20  ? 59.124  48.146  55.698  1.00 54.36  ? 47  SER B N     1 
ATOM   4434 C  CA    . SER B 1 20  ? 58.276  48.552  56.804  1.00 41.00  ? 47  SER B CA    1 
ATOM   4435 C  C     . SER B 1 20  ? 59.136  49.089  57.946  1.00 46.45  ? 47  SER B C     1 
ATOM   4436 O  O     . SER B 1 20  ? 60.349  48.865  57.977  1.00 49.62  ? 47  SER B O     1 
ATOM   4437 C  CB    . SER B 1 20  ? 57.426  47.376  57.280  1.00 40.88  ? 47  SER B CB    1 
ATOM   4438 O  OG    . SER B 1 20  ? 58.233  46.384  57.887  1.00 46.99  ? 47  SER B OG    1 
ATOM   4439 N  N     . PRO B 1 21  ? 58.535  49.817  58.890  1.00 38.99  ? 48  PRO B N     1 
ATOM   4440 C  CA    . PRO B 1 21  ? 59.318  50.371  60.000  1.00 41.29  ? 48  PRO B CA    1 
ATOM   4441 C  C     . PRO B 1 21  ? 59.955  49.284  60.851  1.00 41.02  ? 48  PRO B C     1 
ATOM   4442 O  O     . PRO B 1 21  ? 59.497  48.141  60.899  1.00 49.04  ? 48  PRO B O     1 
ATOM   4443 C  CB    . PRO B 1 21  ? 58.283  51.163  60.807  1.00 37.60  ? 48  PRO B CB    1 
ATOM   4444 C  CG    . PRO B 1 21  ? 57.210  51.479  59.838  1.00 38.95  ? 48  PRO B CG    1 
ATOM   4445 C  CD    . PRO B 1 21  ? 57.146  50.311  58.903  1.00 47.77  ? 48  PRO B CD    1 
ATOM   4446 N  N     . LEU B 1 22  ? 61.036  49.660  61.527  1.00 47.49  ? 49  LEU B N     1 
ATOM   4447 C  CA    . LEU B 1 22  ? 61.635  48.773  62.512  1.00 38.17  ? 49  LEU B CA    1 
ATOM   4448 C  C     . LEU B 1 22  ? 60.800  48.774  63.785  1.00 38.49  ? 49  LEU B C     1 
ATOM   4449 O  O     . LEU B 1 22  ? 60.221  49.795  64.167  1.00 42.25  ? 49  LEU B O     1 
ATOM   4450 C  CB    . LEU B 1 22  ? 63.066  49.210  62.833  1.00 34.54  ? 49  LEU B CB    1 
ATOM   4451 C  CG    . LEU B 1 22  ? 64.111  49.158  61.722  1.00 52.12  ? 49  LEU B CG    1 
ATOM   4452 C  CD1   . LEU B 1 22  ? 65.468  49.557  62.277  1.00 34.80  ? 49  LEU B CD1   1 
ATOM   4453 C  CD2   . LEU B 1 22  ? 64.168  47.772  61.116  1.00 45.65  ? 49  LEU B CD2   1 
ATOM   4454 N  N     . GLN B 1 23  ? 60.726  47.620  64.437  1.00 43.95  ? 50  GLN B N     1 
ATOM   4455 C  CA    . GLN B 1 23  ? 60.093  47.571  65.741  1.00 46.02  ? 50  GLN B CA    1 
ATOM   4456 C  C     . GLN B 1 23  ? 60.976  48.270  66.771  1.00 52.96  ? 50  GLN B C     1 
ATOM   4457 O  O     . GLN B 1 23  ? 62.193  48.391  66.604  1.00 39.73  ? 50  GLN B O     1 
ATOM   4458 C  CB    . GLN B 1 23  ? 59.821  46.125  66.157  1.00 42.26  ? 50  GLN B CB    1 
ATOM   4459 C  CG    . GLN B 1 23  ? 58.899  45.375  65.209  1.00 45.73  ? 50  GLN B CG    1 
ATOM   4460 C  CD    . GLN B 1 23  ? 58.503  44.010  65.734  1.00 54.38  ? 50  GLN B CD    1 
ATOM   4461 O  OE1   . GLN B 1 23  ? 57.893  43.893  66.797  1.00 57.73  ? 50  GLN B OE1   1 
ATOM   4462 N  NE2   . GLN B 1 23  ? 58.853  42.966  64.991  1.00 52.43  ? 50  GLN B NE2   1 
ATOM   4463 N  N     . ALA B 1 24  ? 60.341  48.744  67.846  1.00 46.18  ? 51  ALA B N     1 
ATOM   4464 C  CA    . ALA B 1 24  ? 61.058  49.459  68.888  1.00 45.17  ? 51  ALA B CA    1 
ATOM   4465 C  C     . ALA B 1 24  ? 62.116  48.557  69.525  1.00 40.87  ? 51  ALA B C     1 
ATOM   4466 O  O     . ALA B 1 24  ? 62.025  47.329  69.450  1.00 42.53  ? 51  ALA B O     1 
ATOM   4467 C  CB    . ALA B 1 24  ? 60.080  49.965  69.947  1.00 39.22  ? 51  ALA B CB    1 
ATOM   4468 N  N     . PRO B 1 25  ? 63.142  49.146  70.145  1.00 49.46  ? 52  PRO B N     1 
ATOM   4469 C  CA    . PRO B 1 25  ? 64.145  48.326  70.836  1.00 36.63  ? 52  PRO B CA    1 
ATOM   4470 C  C     . PRO B 1 25  ? 63.513  47.482  71.934  1.00 45.97  ? 52  PRO B C     1 
ATOM   4471 O  O     . PRO B 1 25  ? 62.472  47.830  72.497  1.00 50.48  ? 52  PRO B O     1 
ATOM   4472 C  CB    . PRO B 1 25  ? 65.114  49.362  71.417  1.00 42.91  ? 52  PRO B CB    1 
ATOM   4473 C  CG    . PRO B 1 25  ? 64.948  50.559  70.555  1.00 36.54  ? 52  PRO B CG    1 
ATOM   4474 C  CD    . PRO B 1 25  ? 63.504  50.574  70.148  1.00 35.94  ? 52  PRO B CD    1 
ATOM   4475 N  N     . ARG B 1 26  ? 64.161  46.359  72.233  1.00 41.99  ? 53  ARG B N     1 
ATOM   4476 C  CA    . ARG B 1 26  ? 63.668  45.412  73.225  1.00 46.23  ? 53  ARG B CA    1 
ATOM   4477 C  C     . ARG B 1 26  ? 64.316  45.710  74.572  1.00 42.34  ? 53  ARG B C     1 
ATOM   4478 O  O     . ARG B 1 26  ? 65.539  45.606  74.716  1.00 38.43  ? 53  ARG B O     1 
ATOM   4479 C  CB    . ARG B 1 26  ? 63.958  43.979  72.783  1.00 44.91  ? 53  ARG B CB    1 
ATOM   4480 C  CG    . ARG B 1 26  ? 63.167  43.545  71.559  1.00 46.95  ? 53  ARG B CG    1 
ATOM   4481 C  CD    . ARG B 1 26  ? 63.994  42.658  70.642  1.00 45.82  ? 53  ARG B CD    1 
ATOM   4482 N  NE    . ARG B 1 26  ? 64.973  43.423  69.882  1.00 52.59  ? 53  ARG B NE    1 
ATOM   4483 C  CZ    . ARG B 1 26  ? 65.722  42.927  68.907  1.00 44.56  ? 53  ARG B CZ    1 
ATOM   4484 N  NH1   . ARG B 1 26  ? 65.625  41.662  68.535  1.00 56.59  ? 53  ARG B NH1   1 
ATOM   4485 N  NH2   . ARG B 1 26  ? 66.588  43.723  68.287  1.00 60.59  ? 53  ARG B NH2   1 
ATOM   4486 N  N     . VAL B 1 27  ? 63.496  46.072  75.554  1.00 44.71  ? 54  VAL B N     1 
ATOM   4487 C  CA    . VAL B 1 27  ? 63.965  46.554  76.847  1.00 44.04  ? 54  VAL B CA    1 
ATOM   4488 C  C     . VAL B 1 27  ? 63.409  45.656  77.942  1.00 43.39  ? 54  VAL B C     1 
ATOM   4489 O  O     . VAL B 1 27  ? 62.206  45.369  77.966  1.00 41.49  ? 54  VAL B O     1 
ATOM   4490 C  CB    . VAL B 1 27  ? 63.544  48.014  77.086  1.00 38.81  ? 54  VAL B CB    1 
ATOM   4491 C  CG1   . VAL B 1 27  ? 64.085  48.505  78.413  1.00 45.89  ? 54  VAL B CG1   1 
ATOM   4492 C  CG2   . VAL B 1 27  ? 64.019  48.896  75.944  1.00 44.38  ? 54  VAL B CG2   1 
ATOM   4493 N  N     . LEU B 1 28  ? 64.282  45.224  78.849  1.00 43.64  ? 55  LEU B N     1 
ATOM   4494 C  CA    . LEU B 1 28  ? 63.881  44.518  80.058  1.00 39.95  ? 55  LEU B CA    1 
ATOM   4495 C  C     . LEU B 1 28  ? 63.897  45.502  81.220  1.00 41.57  ? 55  LEU B C     1 
ATOM   4496 O  O     . LEU B 1 28  ? 64.920  46.146  81.476  1.00 39.67  ? 55  LEU B O     1 
ATOM   4497 C  CB    . LEU B 1 28  ? 64.813  43.342  80.348  1.00 36.68  ? 55  LEU B CB    1 
ATOM   4498 C  CG    . LEU B 1 28  ? 64.597  42.670  81.709  1.00 45.35  ? 55  LEU B CG    1 
ATOM   4499 C  CD1   . LEU B 1 28  ? 63.305  41.872  81.727  1.00 43.82  ? 55  LEU B CD1   1 
ATOM   4500 C  CD2   . LEU B 1 28  ? 65.773  41.788  82.093  1.00 34.77  ? 55  LEU B CD2   1 
ATOM   4501 N  N     . ILE B 1 29  ? 62.769  45.617  81.916  1.00 37.12  ? 56  ILE B N     1 
ATOM   4502 C  CA    . ILE B 1 29  ? 62.665  46.462  83.100  1.00 37.62  ? 56  ILE B CA    1 
ATOM   4503 C  C     . ILE B 1 29  ? 62.902  45.579  84.320  1.00 43.33  ? 56  ILE B C     1 
ATOM   4504 O  O     . ILE B 1 29  ? 62.098  44.693  84.626  1.00 47.84  ? 56  ILE B O     1 
ATOM   4505 C  CB    . ILE B 1 29  ? 61.305  47.163  83.174  1.00 43.17  ? 56  ILE B CB    1 
ATOM   4506 C  CG1   . ILE B 1 29  ? 61.088  48.040  81.941  1.00 35.33  ? 56  ILE B CG1   1 
ATOM   4507 C  CG2   . ILE B 1 29  ? 61.213  47.999  84.435  1.00 35.56  ? 56  ILE B CG2   1 
ATOM   4508 C  CD1   . ILE B 1 29  ? 59.760  48.756  81.933  1.00 32.68  ? 56  ILE B CD1   1 
ATOM   4509 N  N     . ALA B 1 30  ? 64.014  45.817  85.013  1.00 40.06  ? 57  ALA B N     1 
ATOM   4510 C  CA    . ALA B 1 30  ? 64.402  45.040  86.183  1.00 48.67  ? 57  ALA B CA    1 
ATOM   4511 C  C     . ALA B 1 30  ? 64.005  45.800  87.441  1.00 50.98  ? 57  ALA B C     1 
ATOM   4512 O  O     . ALA B 1 30  ? 64.435  46.940  87.646  1.00 44.94  ? 57  ALA B O     1 
ATOM   4513 C  CB    . ALA B 1 30  ? 65.904  44.758  86.173  1.00 37.10  ? 57  ALA B CB    1 
ATOM   4514 N  N     . LEU B 1 31  ? 63.191  45.168  88.282  1.00 41.88  ? 58  LEU B N     1 
ATOM   4515 C  CA    . LEU B 1 31  ? 62.660  45.791  89.490  1.00 51.40  ? 58  LEU B CA    1 
ATOM   4516 C  C     . LEU B 1 31  ? 63.012  44.938  90.703  1.00 45.62  ? 58  LEU B C     1 
ATOM   4517 O  O     . LEU B 1 31  ? 62.528  43.807  90.837  1.00 39.43  ? 58  LEU B O     1 
ATOM   4518 C  CB    . LEU B 1 31  ? 61.148  45.983  89.382  1.00 55.19  ? 58  LEU B CB    1 
ATOM   4519 C  CG    . LEU B 1 31  ? 60.448  46.413  90.673  1.00 70.24  ? 58  LEU B CG    1 
ATOM   4520 C  CD1   . LEU B 1 31  ? 61.034  47.711  91.207  1.00 59.98  ? 58  LEU B CD1   1 
ATOM   4521 C  CD2   . LEU B 1 31  ? 58.954  46.552  90.447  1.00 61.54  ? 58  LEU B CD2   1 
ATOM   4522 N  N     . LEU B 1 32  ? 63.849  45.482  91.585  1.00 57.76  ? 59  LEU B N     1 
ATOM   4523 C  CA    . LEU B 1 32  ? 64.099  44.903  92.900  1.00 49.73  ? 59  LEU B CA    1 
ATOM   4524 C  C     . LEU B 1 32  ? 63.217  45.630  93.906  1.00 39.98  ? 59  LEU B C     1 
ATOM   4525 O  O     . LEU B 1 32  ? 63.277  46.860  94.012  1.00 60.49  ? 59  LEU B O     1 
ATOM   4526 C  CB    . LEU B 1 32  ? 65.569  45.030  93.302  1.00 45.54  ? 59  LEU B CB    1 
ATOM   4527 C  CG    . LEU B 1 32  ? 66.695  44.628  92.349  1.00 55.35  ? 59  LEU B CG    1 
ATOM   4528 C  CD1   . LEU B 1 32  ? 68.002  44.532  93.121  1.00 51.97  ? 59  LEU B CD1   1 
ATOM   4529 C  CD2   . LEU B 1 32  ? 66.389  43.322  91.656  1.00 57.84  ? 59  LEU B CD2   1 
ATOM   4530 N  N     . ALA B 1 33  ? 62.402  44.879  94.641  1.00 40.11  ? 60  ALA B N     1 
ATOM   4531 C  CA    . ALA B 1 33  ? 61.464  45.461  95.594  1.00 46.19  ? 60  ALA B CA    1 
ATOM   4532 C  C     . ALA B 1 33  ? 61.637  44.806  96.956  1.00 51.26  ? 60  ALA B C     1 
ATOM   4533 O  O     . ALA B 1 33  ? 61.487  43.586  97.086  1.00 47.04  ? 60  ALA B O     1 
ATOM   4534 C  CB    . ALA B 1 33  ? 60.020  45.311  95.106  1.00 40.03  ? 60  ALA B CB    1 
ATOM   4535 N  N     . ARG B 1 34  ? 61.953  45.616  97.966  1.00 43.47  ? 61  ARG B N     1 
ATOM   4536 C  CA    . ARG B 1 34  ? 61.936  45.187  99.359  1.00 54.26  ? 61  ARG B CA    1 
ATOM   4537 C  C     . ARG B 1 34  ? 61.321  46.294  100.197 1.00 53.79  ? 61  ARG B C     1 
ATOM   4538 O  O     . ARG B 1 34  ? 61.796  47.433  100.157 1.00 48.19  ? 61  ARG B O     1 
ATOM   4539 C  CB    . ARG B 1 34  ? 63.337  44.866  99.889  1.00 40.18  ? 61  ARG B CB    1 
ATOM   4540 C  CG    . ARG B 1 34  ? 63.317  44.451  101.351 1.00 48.22  ? 61  ARG B CG    1 
ATOM   4541 C  CD    . ARG B 1 34  ? 64.668  44.583  102.025 1.00 44.53  ? 61  ARG B CD    1 
ATOM   4542 N  NE    . ARG B 1 34  ? 64.573  44.268  103.447 1.00 50.07  ? 61  ARG B NE    1 
ATOM   4543 C  CZ    . ARG B 1 34  ? 65.571  44.386  104.313 1.00 53.14  ? 61  ARG B CZ    1 
ATOM   4544 N  NH1   . ARG B 1 34  ? 66.763  44.824  103.941 1.00 50.00  ? 61  ARG B NH1   1 
ATOM   4545 N  NH2   . ARG B 1 34  ? 65.367  44.058  105.585 1.00 50.34  ? 61  ARG B NH2   1 
ATOM   4546 N  N     . ASN B 1 35  ? 60.278  45.956  100.957 1.00 47.62  ? 62  ASN B N     1 
ATOM   4547 C  CA    . ASN B 1 35  ? 59.583  46.916  101.817 1.00 41.40  ? 62  ASN B CA    1 
ATOM   4548 C  C     . ASN B 1 35  ? 59.171  48.152  101.021 1.00 46.85  ? 62  ASN B C     1 
ATOM   4549 O  O     . ASN B 1 35  ? 59.480  49.291  101.381 1.00 48.96  ? 62  ASN B O     1 
ATOM   4550 C  CB    . ASN B 1 35  ? 60.448  47.295  103.022 1.00 44.08  ? 62  ASN B CB    1 
ATOM   4551 C  CG    . ASN B 1 35  ? 60.634  46.145  103.987 1.00 45.88  ? 62  ASN B CG    1 
ATOM   4552 O  OD1   . ASN B 1 35  ? 59.685  45.428  104.305 1.00 49.50  ? 62  ASN B OD1   1 
ATOM   4553 N  ND2   . ASN B 1 35  ? 61.865  45.953  104.450 1.00 59.51  ? 62  ASN B ND2   1 
ATOM   4554 N  N     . ALA B 1 36  ? 58.472  47.910  99.910  1.00 56.10  ? 63  ALA B N     1 
ATOM   4555 C  CA    . ALA B 1 36  ? 58.133  48.962  98.961  1.00 47.26  ? 63  ALA B CA    1 
ATOM   4556 C  C     . ALA B 1 36  ? 56.638  49.085  98.708  1.00 48.87  ? 63  ALA B C     1 
ATOM   4557 O  O     . ALA B 1 36  ? 56.239  49.832  97.807  1.00 55.85  ? 63  ALA B O     1 
ATOM   4558 C  CB    . ALA B 1 36  ? 58.857  48.725  97.632  1.00 37.23  ? 63  ALA B CB    1 
ATOM   4559 N  N     . ALA B 1 37  ? 55.802  48.386  99.481  1.00 57.73  ? 64  ALA B N     1 
ATOM   4560 C  CA    . ALA B 1 37  ? 54.360  48.415  99.246  1.00 51.52  ? 64  ALA B CA    1 
ATOM   4561 C  C     . ALA B 1 37  ? 53.807  49.832  99.275  1.00 49.35  ? 64  ALA B C     1 
ATOM   4562 O  O     . ALA B 1 37  ? 52.824  50.132  98.587  1.00 58.23  ? 64  ALA B O     1 
ATOM   4563 C  CB    . ALA B 1 37  ? 53.640  47.553  100.284 1.00 42.60  ? 64  ALA B CB    1 
ATOM   4564 N  N     . HIS B 1 38  ? 54.423  50.718  100.061 1.00 51.49  ? 65  HIS B N     1 
ATOM   4565 C  CA    . HIS B 1 38  ? 53.949  52.094  100.143 1.00 45.09  ? 65  HIS B CA    1 
ATOM   4566 C  C     . HIS B 1 38  ? 54.105  52.825  98.815  1.00 55.15  ? 65  HIS B C     1 
ATOM   4567 O  O     . HIS B 1 38  ? 53.333  53.744  98.519  1.00 54.00  ? 65  HIS B O     1 
ATOM   4568 C  CB    . HIS B 1 38  ? 54.700  52.838  101.247 1.00 41.98  ? 65  HIS B CB    1 
ATOM   4569 C  CG    . HIS B 1 38  ? 56.175  52.938  101.010 1.00 49.95  ? 65  HIS B CG    1 
ATOM   4570 N  ND1   . HIS B 1 38  ? 57.047  51.909  101.298 1.00 58.87  ? 65  HIS B ND1   1 
ATOM   4571 C  CD2   . HIS B 1 38  ? 56.932  53.943  100.509 1.00 57.76  ? 65  HIS B CD2   1 
ATOM   4572 C  CE1   . HIS B 1 38  ? 58.277  52.277  100.984 1.00 55.22  ? 65  HIS B CE1   1 
ATOM   4573 N  NE2   . HIS B 1 38  ? 58.235  53.507  100.504 1.00 58.21  ? 65  HIS B NE2   1 
ATOM   4574 N  N     . ALA B 1 39  ? 55.082  52.430  98.001  1.00 48.94  ? 66  ALA B N     1 
ATOM   4575 C  CA    . ALA B 1 39  ? 55.407  53.155  96.779  1.00 52.92  ? 66  ALA B CA    1 
ATOM   4576 C  C     . ALA B 1 39  ? 54.907  52.479  95.510  1.00 54.00  ? 66  ALA B C     1 
ATOM   4577 O  O     . ALA B 1 39  ? 54.687  53.167  94.509  1.00 49.50  ? 66  ALA B O     1 
ATOM   4578 C  CB    . ALA B 1 39  ? 56.923  53.353  96.673  1.00 56.13  ? 66  ALA B CB    1 
ATOM   4579 N  N     . LEU B 1 40  ? 54.714  51.160  95.530  1.00 53.10  ? 67  LEU B N     1 
ATOM   4580 C  CA    . LEU B 1 40  ? 54.365  50.413  94.320  1.00 53.81  ? 67  LEU B CA    1 
ATOM   4581 C  C     . LEU B 1 40  ? 53.123  50.924  93.596  1.00 50.99  ? 67  LEU B C     1 
ATOM   4582 O  O     . LEU B 1 40  ? 53.173  51.040  92.362  1.00 49.43  ? 67  LEU B O     1 
ATOM   4583 C  CB    . LEU B 1 40  ? 54.212  48.926  94.670  1.00 42.30  ? 67  LEU B CB    1 
ATOM   4584 C  CG    . LEU B 1 40  ? 55.477  48.224  95.162  1.00 51.71  ? 67  LEU B CG    1 
ATOM   4585 C  CD1   . LEU B 1 40  ? 55.173  46.784  95.541  1.00 55.94  ? 67  LEU B CD1   1 
ATOM   4586 C  CD2   . LEU B 1 40  ? 56.576  48.289  94.111  1.00 40.82  ? 67  LEU B CD2   1 
ATOM   4587 N  N     . PRO B 1 41  ? 51.995  51.230  94.263  1.00 59.67  ? 68  PRO B N     1 
ATOM   4588 C  CA    . PRO B 1 41  ? 50.813  51.683  93.502  1.00 53.59  ? 68  PRO B CA    1 
ATOM   4589 C  C     . PRO B 1 41  ? 51.094  52.861  92.589  1.00 55.50  ? 68  PRO B C     1 
ATOM   4590 O  O     . PRO B 1 41  ? 50.527  52.946  91.493  1.00 59.65  ? 68  PRO B O     1 
ATOM   4591 C  CB    . PRO B 1 41  ? 49.812  52.058  94.603  1.00 47.43  ? 68  PRO B CB    1 
ATOM   4592 C  CG    . PRO B 1 41  ? 50.206  51.235  95.761  1.00 44.54  ? 68  PRO B CG    1 
ATOM   4593 C  CD    . PRO B 1 41  ? 51.700  51.130  95.706  1.00 42.49  ? 68  PRO B CD    1 
ATOM   4594 N  N     . THR B 1 42  ? 51.962  53.774  93.016  1.00 51.98  ? 69  THR B N     1 
ATOM   4595 C  CA    . THR B 1 42  ? 52.361  54.912  92.201  1.00 52.28  ? 69  THR B CA    1 
ATOM   4596 C  C     . THR B 1 42  ? 53.533  54.576  91.287  1.00 50.65  ? 69  THR B C     1 
ATOM   4597 O  O     . THR B 1 42  ? 53.534  54.959  90.111  1.00 53.00  ? 69  THR B O     1 
ATOM   4598 C  CB    . THR B 1 42  ? 52.724  56.096  93.102  1.00 38.16  ? 69  THR B CB    1 
ATOM   4599 O  OG1   . THR B 1 42  ? 51.620  56.395  93.966  1.00 53.15  ? 69  THR B OG1   1 
ATOM   4600 C  CG2   . THR B 1 42  ? 53.036  57.322  92.274  1.00 65.67  ? 69  THR B CG2   1 
ATOM   4601 N  N     . THR B 1 43  ? 54.527  53.851  91.808  1.00 52.77  ? 70  THR B N     1 
ATOM   4602 C  CA    . THR B 1 43  ? 55.701  53.501  91.015  1.00 55.52  ? 70  THR B CA    1 
ATOM   4603 C  C     . THR B 1 43  ? 55.345  52.534  89.892  1.00 54.91  ? 70  THR B C     1 
ATOM   4604 O  O     . THR B 1 43  ? 55.775  52.712  88.745  1.00 39.60  ? 70  THR B O     1 
ATOM   4605 C  CB    . THR B 1 43  ? 56.782  52.903  91.917  1.00 44.19  ? 70  THR B CB    1 
ATOM   4606 O  OG1   . THR B 1 43  ? 57.299  53.921  92.781  1.00 55.38  ? 70  THR B OG1   1 
ATOM   4607 C  CG2   . THR B 1 43  ? 57.922  52.331  91.085  1.00 63.81  ? 70  THR B CG2   1 
ATOM   4608 N  N     . LEU B 1 44  ? 54.557  51.499  90.200  1.00 46.35  ? 71  LEU B N     1 
ATOM   4609 C  CA    . LEU B 1 44  ? 54.177  50.540  89.166  1.00 54.52  ? 71  LEU B CA    1 
ATOM   4610 C  C     . LEU B 1 44  ? 53.208  51.153  88.165  1.00 46.02  ? 71  LEU B C     1 
ATOM   4611 O  O     . LEU B 1 44  ? 53.260  50.831  86.974  1.00 47.60  ? 71  LEU B O     1 
ATOM   4612 C  CB    . LEU B 1 44  ? 53.576  49.284  89.796  1.00 39.01  ? 71  LEU B CB    1 
ATOM   4613 C  CG    . LEU B 1 44  ? 54.595  48.455  90.579  1.00 48.25  ? 71  LEU B CG    1 
ATOM   4614 C  CD1   . LEU B 1 44  ? 53.964  47.194  91.136  1.00 51.76  ? 71  LEU B CD1   1 
ATOM   4615 C  CD2   . LEU B 1 44  ? 55.779  48.124  89.688  1.00 43.61  ? 71  LEU B CD2   1 
ATOM   4616 N  N     . GLY B 1 45  ? 52.322  52.037  88.627  1.00 48.66  ? 72  GLY B N     1 
ATOM   4617 C  CA    . GLY B 1 45  ? 51.448  52.741  87.703  1.00 48.96  ? 72  GLY B CA    1 
ATOM   4618 C  C     . GLY B 1 45  ? 52.222  53.560  86.690  1.00 53.40  ? 72  GLY B C     1 
ATOM   4619 O  O     . GLY B 1 45  ? 51.850  53.629  85.516  1.00 55.40  ? 72  GLY B O     1 
ATOM   4620 N  N     . ALA B 1 46  ? 53.321  54.177  87.128  1.00 52.97  ? 73  ALA B N     1 
ATOM   4621 C  CA    . ALA B 1 46  ? 54.161  54.936  86.209  1.00 52.93  ? 73  ALA B CA    1 
ATOM   4622 C  C     . ALA B 1 46  ? 54.810  54.024  85.176  1.00 49.50  ? 73  ALA B C     1 
ATOM   4623 O  O     . ALA B 1 46  ? 54.945  54.398  84.005  1.00 60.55  ? 73  ALA B O     1 
ATOM   4624 C  CB    . ALA B 1 46  ? 55.230  55.710  86.983  1.00 37.95  ? 73  ALA B CB    1 
ATOM   4625 N  N     . LEU B 1 47  ? 55.209  52.819  85.592  1.00 46.25  ? 74  LEU B N     1 
ATOM   4626 C  CA    . LEU B 1 47  ? 55.856  51.894  84.669  1.00 50.26  ? 74  LEU B CA    1 
ATOM   4627 C  C     . LEU B 1 47  ? 54.877  51.384  83.618  1.00 53.58  ? 74  LEU B C     1 
ATOM   4628 O  O     . LEU B 1 47  ? 55.245  51.232  82.448  1.00 51.76  ? 74  LEU B O     1 
ATOM   4629 C  CB    . LEU B 1 47  ? 56.479  50.730  85.439  1.00 50.52  ? 74  LEU B CB    1 
ATOM   4630 C  CG    . LEU B 1 47  ? 57.652  51.081  86.357  1.00 55.06  ? 74  LEU B CG    1 
ATOM   4631 C  CD1   . LEU B 1 47  ? 58.219  49.828  87.000  1.00 52.10  ? 74  LEU B CD1   1 
ATOM   4632 C  CD2   . LEU B 1 47  ? 58.731  51.822  85.587  1.00 41.28  ? 74  LEU B CD2   1 
ATOM   4633 N  N     . GLU B 1 48  ? 53.630  51.111  84.016  1.00 49.09  ? 75  GLU B N     1 
ATOM   4634 C  CA    . GLU B 1 48  ? 52.604  50.720  83.053  1.00 50.11  ? 75  GLU B CA    1 
ATOM   4635 C  C     . GLU B 1 48  ? 52.501  51.736  81.925  1.00 54.60  ? 75  GLU B C     1 
ATOM   4636 O  O     . GLU B 1 48  ? 52.510  51.380  80.741  1.00 60.88  ? 75  GLU B O     1 
ATOM   4637 C  CB    . GLU B 1 48  ? 51.244  50.591  83.742  1.00 55.46  ? 75  GLU B CB    1 
ATOM   4638 C  CG    . GLU B 1 48  ? 51.174  49.634  84.905  1.00 64.57  ? 75  GLU B CG    1 
ATOM   4639 C  CD    . GLU B 1 48  ? 49.855  49.752  85.645  1.00 70.12  ? 75  GLU B CD    1 
ATOM   4640 O  OE1   . GLU B 1 48  ? 49.032  50.613  85.259  1.00 49.78  ? 75  GLU B OE1   1 
ATOM   4641 O  OE2   . GLU B 1 48  ? 49.639  48.988  86.608  1.00 72.05  ? 75  GLU B OE2   1 
ATOM   4642 N  N     . ARG B 1 49  ? 52.411  53.013  82.282  1.00 52.88  ? 76  ARG B N     1 
ATOM   4643 C  CA    . ARG B 1 49  ? 52.119  54.082  81.341  1.00 43.28  ? 76  ARG B CA    1 
ATOM   4644 C  C     . ARG B 1 49  ? 53.350  54.582  80.597  1.00 50.41  ? 76  ARG B C     1 
ATOM   4645 O  O     . ARG B 1 49  ? 53.264  55.614  79.923  1.00 61.09  ? 76  ARG B O     1 
ATOM   4646 C  CB    . ARG B 1 49  ? 51.440  55.241  82.076  1.00 48.12  ? 76  ARG B CB    1 
ATOM   4647 C  CG    . ARG B 1 49  ? 50.136  54.845  82.761  1.00 47.00  ? 76  ARG B CG    1 
ATOM   4648 C  CD    . ARG B 1 49  ? 49.455  56.038  83.412  1.00 42.76  ? 76  ARG B CD    1 
ATOM   4649 N  NE    . ARG B 1 49  ? 50.176  56.510  84.588  1.00 54.72  ? 76  ARG B NE    1 
ATOM   4650 C  CZ    . ARG B 1 49  ? 49.898  56.143  85.832  1.00 60.52  ? 76  ARG B CZ    1 
ATOM   4651 N  NH1   . ARG B 1 49  ? 48.915  55.298  86.100  1.00 38.25  ? 76  ARG B NH1   1 
ATOM   4652 N  NH2   . ARG B 1 49  ? 50.624  56.636  86.831  1.00 55.79  ? 76  ARG B NH2   1 
ATOM   4653 N  N     . LEU B 1 50  ? 54.483  53.890  80.703  1.00 49.29  ? 77  LEU B N     1 
ATOM   4654 C  CA    . LEU B 1 50  ? 55.638  54.229  79.881  1.00 36.30  ? 77  LEU B CA    1 
ATOM   4655 C  C     . LEU B 1 50  ? 55.286  54.080  78.408  1.00 54.24  ? 77  LEU B C     1 
ATOM   4656 O  O     . LEU B 1 50  ? 54.772  53.042  77.980  1.00 55.28  ? 77  LEU B O     1 
ATOM   4657 C  CB    . LEU B 1 50  ? 56.826  53.333  80.228  1.00 45.70  ? 77  LEU B CB    1 
ATOM   4658 C  CG    . LEU B 1 50  ? 57.610  53.622  81.506  1.00 46.94  ? 77  LEU B CG    1 
ATOM   4659 C  CD1   . LEU B 1 50  ? 58.717  52.596  81.676  1.00 37.83  ? 77  LEU B CD1   1 
ATOM   4660 C  CD2   . LEU B 1 50  ? 58.184  55.025  81.473  1.00 36.35  ? 77  LEU B CD2   1 
ATOM   4661 N  N     . ARG B 1 51  ? 55.558  55.126  77.628  1.00 54.45  ? 78  ARG B N     1 
ATOM   4662 C  CA    . ARG B 1 51  ? 55.262  55.099  76.197  1.00 49.99  ? 78  ARG B CA    1 
ATOM   4663 C  C     . ARG B 1 51  ? 56.394  54.364  75.486  1.00 55.78  ? 78  ARG B C     1 
ATOM   4664 O  O     . ARG B 1 51  ? 57.335  54.954  74.948  1.00 47.46  ? 78  ARG B O     1 
ATOM   4665 C  CB    . ARG B 1 51  ? 55.051  56.507  75.655  1.00 46.48  ? 78  ARG B CB    1 
ATOM   4666 C  CG    . ARG B 1 51  ? 53.603  56.963  75.756  1.00 59.60  ? 78  ARG B CG    1 
ATOM   4667 C  CD    . ARG B 1 51  ? 53.370  58.264  75.018  1.00 53.14  ? 78  ARG B CD    1 
ATOM   4668 N  NE    . ARG B 1 51  ? 54.039  59.379  75.673  1.00 59.40  ? 78  ARG B NE    1 
ATOM   4669 C  CZ    . ARG B 1 51  ? 53.476  60.148  76.594  1.00 53.18  ? 78  ARG B CZ    1 
ATOM   4670 N  NH1   . ARG B 1 51  ? 52.230  59.949  76.990  1.00 46.04  ? 78  ARG B NH1   1 
ATOM   4671 N  NH2   . ARG B 1 51  ? 54.180  61.141  77.128  1.00 52.57  ? 78  ARG B NH2   1 
ATOM   4672 N  N     . HIS B 1 52  ? 56.290  53.040  75.506  1.00 49.40  ? 79  HIS B N     1 
ATOM   4673 C  CA    . HIS B 1 52  ? 57.167  52.109  74.816  1.00 42.37  ? 79  HIS B CA    1 
ATOM   4674 C  C     . HIS B 1 52  ? 56.375  50.824  74.616  1.00 45.51  ? 79  HIS B C     1 
ATOM   4675 O  O     . HIS B 1 52  ? 55.700  50.369  75.549  1.00 42.16  ? 79  HIS B O     1 
ATOM   4676 C  CB    . HIS B 1 52  ? 58.447  51.865  75.614  1.00 36.64  ? 79  HIS B CB    1 
ATOM   4677 C  CG    . HIS B 1 52  ? 59.437  50.980  74.922  1.00 44.51  ? 79  HIS B CG    1 
ATOM   4678 N  ND1   . HIS B 1 52  ? 59.481  49.616  75.117  1.00 57.72  ? 79  HIS B ND1   1 
ATOM   4679 C  CD2   . HIS B 1 52  ? 60.430  51.266  74.045  1.00 45.58  ? 79  HIS B CD2   1 
ATOM   4680 C  CE1   . HIS B 1 52  ? 60.453  49.099  74.386  1.00 51.83  ? 79  HIS B CE1   1 
ATOM   4681 N  NE2   . HIS B 1 52  ? 61.044  50.079  73.726  1.00 43.82  ? 79  HIS B NE2   1 
ATOM   4682 N  N     . PRO B 1 53  ? 56.405  50.233  73.423  1.00 47.57  ? 80  PRO B N     1 
ATOM   4683 C  CA    . PRO B 1 53  ? 55.563  49.061  73.148  1.00 40.36  ? 80  PRO B CA    1 
ATOM   4684 C  C     . PRO B 1 53  ? 55.788  47.945  74.155  1.00 54.22  ? 80  PRO B C     1 
ATOM   4685 O  O     . PRO B 1 53  ? 56.921  47.541  74.423  1.00 56.03  ? 80  PRO B O     1 
ATOM   4686 C  CB    . PRO B 1 53  ? 55.996  48.647  71.738  1.00 46.42  ? 80  PRO B CB    1 
ATOM   4687 C  CG    . PRO B 1 53  ? 56.474  49.919  71.122  1.00 39.61  ? 80  PRO B CG    1 
ATOM   4688 C  CD    . PRO B 1 53  ? 57.145  50.675  72.228  1.00 40.04  ? 80  PRO B CD    1 
ATOM   4689 N  N     . ARG B 1 54  ? 54.686  47.453  74.723  1.00 48.95  ? 81  ARG B N     1 
ATOM   4690 C  CA    . ARG B 1 54  ? 54.774  46.438  75.767  1.00 47.01  ? 81  ARG B CA    1 
ATOM   4691 C  C     . ARG B 1 54  ? 55.177  45.081  75.207  1.00 44.55  ? 81  ARG B C     1 
ATOM   4692 O  O     . ARG B 1 54  ? 55.771  44.269  75.927  1.00 49.98  ? 81  ARG B O     1 
ATOM   4693 C  CB    . ARG B 1 54  ? 53.443  46.344  76.510  1.00 54.58  ? 81  ARG B CB    1 
ATOM   4694 C  CG    . ARG B 1 54  ? 53.182  47.507  77.455  1.00 55.81  ? 81  ARG B CG    1 
ATOM   4695 C  CD    . ARG B 1 54  ? 51.713  47.600  77.826  1.00 59.09  ? 81  ARG B CD    1 
ATOM   4696 N  NE    . ARG B 1 54  ? 51.498  48.417  79.011  1.00 81.98  ? 81  ARG B NE    1 
ATOM   4697 C  CZ    . ARG B 1 54  ? 50.312  48.834  79.430  1.00 87.49  ? 81  ARG B CZ    1 
ATOM   4698 N  NH1   . ARG B 1 54  ? 49.200  48.510  78.791  1.00 76.14  ? 81  ARG B NH1   1 
ATOM   4699 N  NH2   . ARG B 1 54  ? 50.241  49.608  80.510  1.00 79.37  ? 81  ARG B NH2   1 
ATOM   4700 N  N     . GLU B 1 55  ? 54.873  44.815  73.936  1.00 50.11  ? 82  GLU B N     1 
ATOM   4701 C  CA    . GLU B 1 55  ? 55.365  43.599  73.299  1.00 44.53  ? 82  GLU B CA    1 
ATOM   4702 C  C     . GLU B 1 55  ? 56.877  43.625  73.115  1.00 51.10  ? 82  GLU B C     1 
ATOM   4703 O  O     . GLU B 1 55  ? 57.487  42.564  72.946  1.00 49.01  ? 82  GLU B O     1 
ATOM   4704 C  CB    . GLU B 1 55  ? 54.676  43.384  71.947  1.00 49.18  ? 82  GLU B CB    1 
ATOM   4705 C  CG    . GLU B 1 55  ? 54.832  44.533  70.960  1.00 58.29  ? 82  GLU B CG    1 
ATOM   4706 C  CD    . GLU B 1 55  ? 53.838  45.658  71.198  1.00 81.72  ? 82  GLU B CD    1 
ATOM   4707 O  OE1   . GLU B 1 55  ? 53.043  45.561  72.159  1.00 85.27  ? 82  GLU B OE1   1 
ATOM   4708 O  OE2   . GLU B 1 55  ? 53.850  46.636  70.421  1.00 88.25  ? 82  GLU B OE2   1 
ATOM   4709 N  N     . ARG B 1 56  ? 57.491  44.809  73.144  1.00 52.38  ? 83  ARG B N     1 
ATOM   4710 C  CA    . ARG B 1 56  ? 58.939  44.957  73.121  1.00 43.91  ? 83  ARG B CA    1 
ATOM   4711 C  C     . ARG B 1 56  ? 59.505  45.214  74.511  1.00 44.63  ? 83  ARG B C     1 
ATOM   4712 O  O     . ARG B 1 56  ? 60.632  45.703  74.640  1.00 49.68  ? 83  ARG B O     1 
ATOM   4713 C  CB    . ARG B 1 56  ? 59.340  46.083  72.169  1.00 51.69  ? 83  ARG B CB    1 
ATOM   4714 C  CG    . ARG B 1 56  ? 58.667  46.000  70.810  1.00 52.26  ? 83  ARG B CG    1 
ATOM   4715 C  CD    . ARG B 1 56  ? 59.145  44.792  70.022  1.00 33.18  ? 83  ARG B CD    1 
ATOM   4716 N  NE    . ARG B 1 56  ? 60.449  45.020  69.416  1.00 53.49  ? 83  ARG B NE    1 
ATOM   4717 C  CZ    . ARG B 1 56  ? 61.105  44.126  68.688  1.00 60.85  ? 83  ARG B CZ    1 
ATOM   4718 N  NH1   . ARG B 1 56  ? 60.605  42.923  68.455  1.00 52.56  ? 83  ARG B NH1   1 
ATOM   4719 N  NH2   . ARG B 1 56  ? 62.292  44.447  68.180  1.00 52.43  ? 83  ARG B NH2   1 
ATOM   4720 N  N     . THR B 1 57  ? 58.736  44.906  75.552  1.00 44.83  ? 84  THR B N     1 
ATOM   4721 C  CA    . THR B 1 57  ? 59.138  45.121  76.933  1.00 46.57  ? 84  THR B CA    1 
ATOM   4722 C  C     . THR B 1 57  ? 58.968  43.829  77.717  1.00 40.29  ? 84  THR B C     1 
ATOM   4723 O  O     . THR B 1 57  ? 57.994  43.095  77.521  1.00 42.74  ? 84  THR B O     1 
ATOM   4724 C  CB    . THR B 1 57  ? 58.312  46.236  77.590  1.00 39.19  ? 84  THR B CB    1 
ATOM   4725 O  OG1   . THR B 1 57  ? 58.312  47.393  76.746  1.00 55.82  ? 84  THR B OG1   1 
ATOM   4726 C  CG2   . THR B 1 57  ? 58.899  46.614  78.948  1.00 32.27  ? 84  THR B CG2   1 
ATOM   4727 N  N     . ALA B 1 58  ? 59.924  43.552  78.601  1.00 39.87  ? 85  ALA B N     1 
ATOM   4728 C  CA    . ALA B 1 58  ? 59.868  42.396  79.481  1.00 52.57  ? 85  ALA B CA    1 
ATOM   4729 C  C     . ALA B 1 58  ? 60.057  42.852  80.920  1.00 48.47  ? 85  ALA B C     1 
ATOM   4730 O  O     . ALA B 1 58  ? 60.675  43.887  81.182  1.00 47.68  ? 85  ALA B O     1 
ATOM   4731 C  CB    . ALA B 1 58  ? 60.930  41.351  79.114  1.00 34.37  ? 85  ALA B CB    1 
ATOM   4732 N  N     . LEU B 1 59  ? 59.522  42.068  81.851  1.00 46.46  ? 86  LEU B N     1 
ATOM   4733 C  CA    . LEU B 1 59  ? 59.516  42.416  83.265  1.00 44.01  ? 86  LEU B CA    1 
ATOM   4734 C  C     . LEU B 1 59  ? 60.307  41.384  84.053  1.00 45.53  ? 86  LEU B C     1 
ATOM   4735 O  O     . LEU B 1 59  ? 60.088  40.178  83.903  1.00 57.38  ? 86  LEU B O     1 
ATOM   4736 C  CB    . LEU B 1 59  ? 58.087  42.508  83.804  1.00 32.87  ? 86  LEU B CB    1 
ATOM   4737 C  CG    . LEU B 1 59  ? 57.224  43.614  83.202  1.00 51.90  ? 86  LEU B CG    1 
ATOM   4738 C  CD1   . LEU B 1 59  ? 55.847  43.621  83.840  1.00 43.53  ? 86  LEU B CD1   1 
ATOM   4739 C  CD2   . LEU B 1 59  ? 57.901  44.962  83.369  1.00 39.98  ? 86  LEU B CD2   1 
ATOM   4740 N  N     . TRP B 1 60  ? 61.221  41.865  84.892  1.00 46.39  ? 87  TRP B N     1 
ATOM   4741 C  CA    . TRP B 1 60  ? 62.026  41.030  85.779  1.00 46.16  ? 87  TRP B CA    1 
ATOM   4742 C  C     . TRP B 1 60  ? 61.871  41.593  87.185  1.00 45.63  ? 87  TRP B C     1 
ATOM   4743 O  O     . TRP B 1 60  ? 62.296  42.721  87.456  1.00 52.44  ? 87  TRP B O     1 
ATOM   4744 C  CB    . TRP B 1 60  ? 63.489  41.023  85.340  1.00 36.78  ? 87  TRP B CB    1 
ATOM   4745 C  CG    . TRP B 1 60  ? 64.339  39.991  86.003  1.00 58.74  ? 87  TRP B CG    1 
ATOM   4746 C  CD1   . TRP B 1 60  ? 64.676  38.766  85.505  1.00 45.56  ? 87  TRP B CD1   1 
ATOM   4747 C  CD2   . TRP B 1 60  ? 64.981  40.095  87.281  1.00 56.75  ? 87  TRP B CD2   1 
ATOM   4748 N  NE1   . TRP B 1 60  ? 65.482  38.099  86.394  1.00 51.89  ? 87  TRP B NE1   1 
ATOM   4749 C  CE2   . TRP B 1 60  ? 65.685  38.892  87.492  1.00 41.14  ? 87  TRP B CE2   1 
ATOM   4750 C  CE3   . TRP B 1 60  ? 65.026  41.086  88.266  1.00 43.53  ? 87  TRP B CE3   1 
ATOM   4751 C  CZ2   . TRP B 1 60  ? 66.426  38.654  88.648  1.00 44.11  ? 87  TRP B CZ2   1 
ATOM   4752 C  CZ3   . TRP B 1 60  ? 65.763  40.845  89.414  1.00 52.73  ? 87  TRP B CZ3   1 
ATOM   4753 C  CH2   . TRP B 1 60  ? 66.452  39.640  89.596  1.00 44.82  ? 87  TRP B CH2   1 
ATOM   4754 N  N     . VAL B 1 61  ? 61.250  40.821  88.074  1.00 49.09  ? 88  VAL B N     1 
ATOM   4755 C  CA    . VAL B 1 61  ? 60.875  41.286  89.404  1.00 47.18  ? 88  VAL B CA    1 
ATOM   4756 C  C     . VAL B 1 61  ? 61.398  40.304  90.443  1.00 38.74  ? 88  VAL B C     1 
ATOM   4757 O  O     . VAL B 1 61  ? 61.153  39.096  90.343  1.00 53.86  ? 88  VAL B O     1 
ATOM   4758 C  CB    . VAL B 1 61  ? 59.348  41.440  89.539  1.00 50.24  ? 88  VAL B CB    1 
ATOM   4759 C  CG1   . VAL B 1 61  ? 58.996  42.009  90.900  1.00 41.68  ? 88  VAL B CG1   1 
ATOM   4760 C  CG2   . VAL B 1 61  ? 58.794  42.314  88.423  1.00 41.11  ? 88  VAL B CG2   1 
ATOM   4761 N  N     . ALA B 1 62  ? 62.098  40.825  91.447  1.00 40.02  ? 89  ALA B N     1 
ATOM   4762 C  CA    . ALA B 1 62  ? 62.600  40.027  92.557  1.00 45.05  ? 89  ALA B CA    1 
ATOM   4763 C  C     . ALA B 1 62  ? 62.282  40.737  93.863  1.00 53.75  ? 89  ALA B C     1 
ATOM   4764 O  O     . ALA B 1 62  ? 62.587  41.923  94.016  1.00 50.24  ? 89  ALA B O     1 
ATOM   4765 C  CB    . ALA B 1 62  ? 64.108  39.790  92.437  1.00 38.10  ? 89  ALA B CB    1 
ATOM   4766 N  N     . THR B 1 63  ? 61.670  40.012  94.798  1.00 47.21  ? 90  THR B N     1 
ATOM   4767 C  CA    . THR B 1 63  ? 61.314  40.562  96.097  1.00 52.27  ? 90  THR B CA    1 
ATOM   4768 C  C     . THR B 1 63  ? 61.665  39.555  97.187  1.00 50.20  ? 90  THR B C     1 
ATOM   4769 O  O     . THR B 1 63  ? 61.585  38.340  96.981  1.00 58.39  ? 90  THR B O     1 
ATOM   4770 C  CB    . THR B 1 63  ? 59.823  40.935  96.163  1.00 46.26  ? 90  THR B CB    1 
ATOM   4771 O  OG1   . THR B 1 63  ? 59.562  41.674  97.361  1.00 59.17  ? 90  THR B OG1   1 
ATOM   4772 C  CG2   . THR B 1 63  ? 58.945  39.693  96.138  1.00 47.73  ? 90  THR B CG2   1 
ATOM   4773 N  N     . ASP B 1 64  ? 62.065  40.075  98.346  1.00 42.37  ? 91  ASP B N     1 
ATOM   4774 C  CA    . ASP B 1 64  ? 62.508  39.244  99.460  1.00 58.60  ? 91  ASP B CA    1 
ATOM   4775 C  C     . ASP B 1 64  ? 62.744  40.135  100.672 1.00 41.37  ? 91  ASP B C     1 
ATOM   4776 O  O     . ASP B 1 64  ? 62.845  41.360  100.550 1.00 46.63  ? 91  ASP B O     1 
ATOM   4777 C  CB    . ASP B 1 64  ? 63.783  38.467  99.111  1.00 46.80  ? 91  ASP B CB    1 
ATOM   4778 C  CG    . ASP B 1 64  ? 64.846  39.351  98.491  1.00 54.70  ? 91  ASP B CG    1 
ATOM   4779 O  OD1   . ASP B 1 64  ? 65.516  40.093  99.241  1.00 49.27  ? 91  ASP B OD1   1 
ATOM   4780 O  OD2   . ASP B 1 64  ? 65.000  39.318  97.251  1.00 49.41  ? 91  ASP B OD2   1 
ATOM   4781 N  N     . HIS B 1 65  ? 62.834  39.498  101.844 1.00 45.77  ? 92  HIS B N     1 
ATOM   4782 C  CA    . HIS B 1 65  ? 63.108  40.181  103.114 1.00 53.42  ? 92  HIS B CA    1 
ATOM   4783 C  C     . HIS B 1 65  ? 62.090  41.288  103.383 1.00 55.38  ? 92  HIS B C     1 
ATOM   4784 O  O     . HIS B 1 65  ? 62.443  42.424  103.710 1.00 60.18  ? 92  HIS B O     1 
ATOM   4785 C  CB    . HIS B 1 65  ? 64.535  40.736  103.146 1.00 49.16  ? 92  HIS B CB    1 
ATOM   4786 C  CG    . HIS B 1 65  ? 65.598  39.689  103.043 1.00 59.11  ? 92  HIS B CG    1 
ATOM   4787 N  ND1   . HIS B 1 65  ? 66.096  39.249  101.835 1.00 50.12  ? 92  HIS B ND1   1 
ATOM   4788 C  CD2   . HIS B 1 65  ? 66.264  38.997  103.998 1.00 56.55  ? 92  HIS B CD2   1 
ATOM   4789 C  CE1   . HIS B 1 65  ? 67.021  38.331  102.051 1.00 47.08  ? 92  HIS B CE1   1 
ATOM   4790 N  NE2   . HIS B 1 65  ? 67.143  38.160  103.355 1.00 50.35  ? 92  HIS B NE2   1 
ATOM   4791 N  N     . ASN B 1 66  ? 60.813  40.946  103.254 1.00 50.39  ? 93  ASN B N     1 
ATOM   4792 C  CA    . ASN B 1 66  ? 59.732  41.917  103.345 1.00 58.41  ? 93  ASN B CA    1 
ATOM   4793 C  C     . ASN B 1 66  ? 59.065  41.850  104.712 1.00 58.74  ? 93  ASN B C     1 
ATOM   4794 O  O     . ASN B 1 66  ? 58.698  40.767  105.178 1.00 54.93  ? 93  ASN B O     1 
ATOM   4795 C  CB    . ASN B 1 66  ? 58.693  41.682  102.248 1.00 56.19  ? 93  ASN B CB    1 
ATOM   4796 C  CG    . ASN B 1 66  ? 59.197  42.074  100.875 1.00 48.15  ? 93  ASN B CG    1 
ATOM   4797 O  OD1   . ASN B 1 66  ? 59.498  43.241  100.624 1.00 52.56  ? 93  ASN B OD1   1 
ATOM   4798 N  ND2   . ASN B 1 66  ? 59.281  41.102  99.974  1.00 52.36  ? 93  ASN B ND2   1 
ATOM   4799 N  N     . MET B 1 67  ? 58.916  43.013  105.349 1.00 57.56  ? 94  MET B N     1 
ATOM   4800 C  CA    . MET B 1 67  ? 58.099  43.145  106.547 1.00 54.63  ? 94  MET B CA    1 
ATOM   4801 C  C     . MET B 1 67  ? 56.673  43.575  106.237 1.00 52.42  ? 94  MET B C     1 
ATOM   4802 O  O     . MET B 1 67  ? 55.790  43.399  107.084 1.00 61.20  ? 94  MET B O     1 
ATOM   4803 C  CB    . MET B 1 67  ? 58.734  44.146  107.519 1.00 45.27  ? 94  MET B CB    1 
ATOM   4804 C  CG    . MET B 1 67  ? 59.927  43.594  108.275 1.00 46.24  ? 94  MET B CG    1 
ATOM   4805 S  SD    . MET B 1 67  ? 59.429  42.339  109.468 1.00 72.46  ? 94  MET B SD    1 
ATOM   4806 C  CE    . MET B 1 67  ? 61.022  41.670  109.938 1.00 76.09  ? 94  MET B CE    1 
ATOM   4807 N  N     . ASP B 1 68  ? 56.434  44.128  105.050 1.00 58.57  ? 95  ASP B N     1 
ATOM   4808 C  CA    . ASP B 1 68  ? 55.115  44.526  104.592 1.00 48.98  ? 95  ASP B CA    1 
ATOM   4809 C  C     . ASP B 1 68  ? 54.614  43.536  103.541 1.00 57.21  ? 95  ASP B C     1 
ATOM   4810 O  O     . ASP B 1 68  ? 55.213  42.477  103.314 1.00 64.92  ? 95  ASP B O     1 
ATOM   4811 C  CB    . ASP B 1 68  ? 55.150  45.962  104.054 1.00 45.36  ? 95  ASP B CB    1 
ATOM   4812 C  CG    . ASP B 1 68  ? 56.098  46.130  102.873 1.00 62.78  ? 95  ASP B CG    1 
ATOM   4813 O  OD1   . ASP B 1 68  ? 56.757  45.146  102.475 1.00 56.16  ? 95  ASP B OD1   1 
ATOM   4814 O  OD2   . ASP B 1 68  ? 56.183  47.258  102.341 1.00 62.67  ? 95  ASP B OD2   1 
ATOM   4815 N  N     . ASN B 1 69  ? 53.512  43.891  102.887 1.00 57.43  ? 96  ASN B N     1 
ATOM   4816 C  CA    . ASN B 1 69  ? 52.888  43.024  101.887 1.00 60.27  ? 96  ASN B CA    1 
ATOM   4817 C  C     . ASN B 1 69  ? 53.380  43.354  100.482 1.00 57.89  ? 96  ASN B C     1 
ATOM   4818 O  O     . ASN B 1 69  ? 52.602  43.467  99.537  1.00 55.08  ? 96  ASN B O     1 
ATOM   4819 C  CB    . ASN B 1 69  ? 51.372  43.133  101.979 1.00 49.56  ? 96  ASN B CB    1 
ATOM   4820 C  CG    . ASN B 1 69  ? 50.877  44.542  101.731 1.00 66.27  ? 96  ASN B CG    1 
ATOM   4821 O  OD1   . ASN B 1 69  ? 51.567  45.519  102.021 1.00 75.00  ? 96  ASN B OD1   1 
ATOM   4822 N  ND2   . ASN B 1 69  ? 49.669  44.653  101.192 1.00 69.31  ? 96  ASN B ND2   1 
ATOM   4823 N  N     . THR B 1 70  ? 54.699  43.502  100.344 1.00 59.40  ? 97  THR B N     1 
ATOM   4824 C  CA    . THR B 1 70  ? 55.270  43.875  99.054  1.00 53.55  ? 97  THR B CA    1 
ATOM   4825 C  C     . THR B 1 70  ? 55.007  42.801  98.004  1.00 47.95  ? 97  THR B C     1 
ATOM   4826 O  O     . THR B 1 70  ? 54.536  43.099  96.900  1.00 51.74  ? 97  THR B O     1 
ATOM   4827 C  CB    . THR B 1 70  ? 56.770  44.131  99.195  1.00 54.66  ? 97  THR B CB    1 
ATOM   4828 O  OG1   . THR B 1 70  ? 56.988  45.360  99.901  1.00 52.50  ? 97  THR B OG1   1 
ATOM   4829 C  CG2   . THR B 1 70  ? 57.425  44.216  97.827  1.00 49.53  ? 97  THR B CG2   1 
ATOM   4830 N  N     . SER B 1 71  ? 55.288  41.539  98.342  1.00 44.64  ? 98  SER B N     1 
ATOM   4831 C  CA    . SER B 1 71  ? 55.131  40.460  97.371  1.00 61.00  ? 98  SER B CA    1 
ATOM   4832 C  C     . SER B 1 71  ? 53.673  40.283  96.964  1.00 54.03  ? 98  SER B C     1 
ATOM   4833 O  O     . SER B 1 71  ? 53.380  39.972  95.804  1.00 56.55  ? 98  SER B O     1 
ATOM   4834 C  CB    . SER B 1 71  ? 55.696  39.156  97.937  1.00 38.89  ? 98  SER B CB    1 
ATOM   4835 O  OG    . SER B 1 71  ? 55.038  38.787  99.136  1.00 78.40  ? 98  SER B OG    1 
ATOM   4836 N  N     . THR B 1 72  ? 52.744  40.480  97.904  1.00 50.01  ? 99  THR B N     1 
ATOM   4837 C  CA    . THR B 1 72  ? 51.325  40.395  97.572  1.00 55.53  ? 99  THR B CA    1 
ATOM   4838 C  C     . THR B 1 72  ? 50.936  41.467  96.562  1.00 56.03  ? 99  THR B C     1 
ATOM   4839 O  O     . THR B 1 72  ? 50.293  41.178  95.546  1.00 54.14  ? 99  THR B O     1 
ATOM   4840 C  CB    . THR B 1 72  ? 50.478  40.521  98.839  1.00 59.17  ? 99  THR B CB    1 
ATOM   4841 O  OG1   . THR B 1 72  ? 50.795  39.452  99.738  1.00 66.41  ? 99  THR B OG1   1 
ATOM   4842 C  CG2   . THR B 1 72  ? 48.998  40.468  98.495  1.00 44.22  ? 99  THR B CG2   1 
ATOM   4843 N  N     . VAL B 1 73  ? 51.324  42.717  96.827  1.00 53.00  ? 100 VAL B N     1 
ATOM   4844 C  CA    . VAL B 1 73  ? 51.010  43.813  95.913  1.00 55.48  ? 100 VAL B CA    1 
ATOM   4845 C  C     . VAL B 1 73  ? 51.622  43.552  94.542  1.00 52.32  ? 100 VAL B C     1 
ATOM   4846 O  O     . VAL B 1 73  ? 50.975  43.744  93.505  1.00 56.32  ? 100 VAL B O     1 
ATOM   4847 C  CB    . VAL B 1 73  ? 51.492  45.153  96.498  1.00 47.79  ? 100 VAL B CB    1 
ATOM   4848 C  CG1   . VAL B 1 73  ? 51.304  46.278  95.490  1.00 45.28  ? 100 VAL B CG1   1 
ATOM   4849 C  CG2   . VAL B 1 73  ? 50.754  45.463  97.791  1.00 39.07  ? 100 VAL B CG2   1 
ATOM   4850 N  N     . LEU B 1 74  ? 52.879  43.100  94.521  1.00 54.20  ? 101 LEU B N     1 
ATOM   4851 C  CA    . LEU B 1 74  ? 53.565  42.853  93.256  1.00 49.78  ? 101 LEU B CA    1 
ATOM   4852 C  C     . LEU B 1 74  ? 52.876  41.755  92.455  1.00 56.84  ? 101 LEU B C     1 
ATOM   4853 O  O     . LEU B 1 74  ? 52.629  41.910  91.254  1.00 57.23  ? 101 LEU B O     1 
ATOM   4854 C  CB    . LEU B 1 74  ? 55.026  42.489  93.515  1.00 49.44  ? 101 LEU B CB    1 
ATOM   4855 C  CG    . LEU B 1 74  ? 56.013  43.641  93.689  1.00 50.31  ? 101 LEU B CG    1 
ATOM   4856 C  CD1   . LEU B 1 74  ? 57.339  43.103  94.184  1.00 50.96  ? 101 LEU B CD1   1 
ATOM   4857 C  CD2   . LEU B 1 74  ? 56.193  44.383  92.376  1.00 44.47  ? 101 LEU B CD2   1 
ATOM   4858 N  N     . ARG B 1 75  ? 52.555  40.632  93.106  1.00 59.88  ? 102 ARG B N     1 
ATOM   4859 C  CA    . ARG B 1 75  ? 51.984  39.506  92.375  1.00 52.17  ? 102 ARG B CA    1 
ATOM   4860 C  C     . ARG B 1 75  ? 50.624  39.863  91.787  1.00 52.12  ? 102 ARG B C     1 
ATOM   4861 O  O     . ARG B 1 75  ? 50.283  39.419  90.686  1.00 68.13  ? 102 ARG B O     1 
ATOM   4862 C  CB    . ARG B 1 75  ? 51.888  38.272  93.277  1.00 41.28  ? 102 ARG B CB    1 
ATOM   4863 C  CG    . ARG B 1 75  ? 50.542  38.058  93.948  1.00 80.54  ? 102 ARG B CG    1 
ATOM   4864 C  CD    . ARG B 1 75  ? 50.313  36.589  94.255  1.00 101.14 ? 102 ARG B CD    1 
ATOM   4865 N  NE    . ARG B 1 75  ? 50.428  35.766  93.057  1.00 92.03  ? 102 ARG B NE    1 
ATOM   4866 C  CZ    . ARG B 1 75  ? 50.252  34.452  93.030  1.00 104.24 ? 102 ARG B CZ    1 
ATOM   4867 N  NH1   . ARG B 1 75  ? 49.943  33.773  94.123  1.00 117.44 ? 102 ARG B NH1   1 
ATOM   4868 N  NH2   . ARG B 1 75  ? 50.390  33.802  91.877  1.00 84.50  ? 102 ARG B NH2   1 
ATOM   4869 N  N     . GLU B 1 76  ? 49.843  40.689  92.487  1.00 46.95  ? 103 GLU B N     1 
ATOM   4870 C  CA    . GLU B 1 76  ? 48.556  41.107  91.942  1.00 53.72  ? 103 GLU B CA    1 
ATOM   4871 C  C     . GLU B 1 76  ? 48.745  42.003  90.728  1.00 62.40  ? 103 GLU B C     1 
ATOM   4872 O  O     . GLU B 1 76  ? 47.970  41.932  89.767  1.00 61.24  ? 103 GLU B O     1 
ATOM   4873 C  CB    . GLU B 1 76  ? 47.733  41.818  93.015  1.00 48.20  ? 103 GLU B CB    1 
ATOM   4874 C  CG    . GLU B 1 76  ? 47.241  40.897  94.119  1.00 81.18  ? 103 GLU B CG    1 
ATOM   4875 C  CD    . GLU B 1 76  ? 46.482  41.634  95.204  1.00 96.93  ? 103 GLU B CD    1 
ATOM   4876 O  OE1   . GLU B 1 76  ? 46.193  42.837  95.018  1.00 85.52  ? 103 GLU B OE1   1 
ATOM   4877 O  OE2   . GLU B 1 76  ? 46.179  41.009  96.243  1.00 91.04  ? 103 GLU B OE2   1 
ATOM   4878 N  N     . TRP B 1 77  ? 49.776  42.848  90.751  1.00 56.74  ? 104 TRP B N     1 
ATOM   4879 C  CA    . TRP B 1 77  ? 50.065  43.691  89.597  1.00 56.05  ? 104 TRP B CA    1 
ATOM   4880 C  C     . TRP B 1 77  ? 50.561  42.862  88.421  1.00 58.45  ? 104 TRP B C     1 
ATOM   4881 O  O     . TRP B 1 77  ? 50.133  43.073  87.281  1.00 57.03  ? 104 TRP B O     1 
ATOM   4882 C  CB    . TRP B 1 77  ? 51.097  44.748  89.974  1.00 49.66  ? 104 TRP B CB    1 
ATOM   4883 C  CG    . TRP B 1 77  ? 51.442  45.679  88.860  1.00 52.45  ? 104 TRP B CG    1 
ATOM   4884 C  CD1   . TRP B 1 77  ? 50.673  46.695  88.374  1.00 42.04  ? 104 TRP B CD1   1 
ATOM   4885 C  CD2   . TRP B 1 77  ? 52.654  45.692  88.099  1.00 45.54  ? 104 TRP B CD2   1 
ATOM   4886 N  NE1   . TRP B 1 77  ? 51.328  47.338  87.352  1.00 48.44  ? 104 TRP B NE1   1 
ATOM   4887 C  CE2   . TRP B 1 77  ? 52.548  46.741  87.164  1.00 59.33  ? 104 TRP B CE2   1 
ATOM   4888 C  CE3   . TRP B 1 77  ? 53.817  44.918  88.116  1.00 38.52  ? 104 TRP B CE3   1 
ATOM   4889 C  CZ2   . TRP B 1 77  ? 53.560  47.035  86.254  1.00 43.10  ? 104 TRP B CZ2   1 
ATOM   4890 C  CZ3   . TRP B 1 77  ? 54.822  45.212  87.213  1.00 44.25  ? 104 TRP B CZ3   1 
ATOM   4891 C  CH2   . TRP B 1 77  ? 54.687  46.261  86.294  1.00 47.27  ? 104 TRP B CH2   1 
ATOM   4892 N  N     . LEU B 1 78  ? 51.465  41.916  88.678  1.00 55.32  ? 105 LEU B N     1 
ATOM   4893 C  CA    . LEU B 1 78  ? 51.981  41.076  87.604  1.00 52.94  ? 105 LEU B CA    1 
ATOM   4894 C  C     . LEU B 1 78  ? 50.884  40.201  87.013  1.00 54.94  ? 105 LEU B C     1 
ATOM   4895 O  O     . LEU B 1 78  ? 50.842  39.985  85.797  1.00 59.16  ? 105 LEU B O     1 
ATOM   4896 C  CB    . LEU B 1 78  ? 53.137  40.222  88.120  1.00 45.56  ? 105 LEU B CB    1 
ATOM   4897 C  CG    . LEU B 1 78  ? 54.436  40.989  88.349  1.00 44.87  ? 105 LEU B CG    1 
ATOM   4898 C  CD1   . LEU B 1 78  ? 55.430  40.127  89.094  1.00 45.35  ? 105 LEU B CD1   1 
ATOM   4899 C  CD2   . LEU B 1 78  ? 55.015  41.447  87.021  1.00 35.12  ? 105 LEU B CD2   1 
ATOM   4900 N  N     . VAL B 1 79  ? 49.983  39.693  87.859  1.00 47.96  ? 106 VAL B N     1 
ATOM   4901 C  CA    . VAL B 1 79  ? 48.845  38.923  87.363  1.00 56.92  ? 106 VAL B CA    1 
ATOM   4902 C  C     . VAL B 1 79  ? 48.027  39.755  86.385  1.00 53.00  ? 106 VAL B C     1 
ATOM   4903 O  O     . VAL B 1 79  ? 47.516  39.243  85.381  1.00 56.36  ? 106 VAL B O     1 
ATOM   4904 C  CB    . VAL B 1 79  ? 47.988  38.423  88.544  1.00 54.10  ? 106 VAL B CB    1 
ATOM   4905 C  CG1   . VAL B 1 79  ? 46.577  38.087  88.087  1.00 51.77  ? 106 VAL B CG1   1 
ATOM   4906 C  CG2   . VAL B 1 79  ? 48.635  37.207  89.190  1.00 49.30  ? 106 VAL B CG2   1 
ATOM   4907 N  N     . ALA B 1 80  ? 47.921  41.057  86.641  1.00 52.19  ? 107 ALA B N     1 
ATOM   4908 C  CA    . ALA B 1 80  ? 47.075  41.935  85.847  1.00 47.66  ? 107 ALA B CA    1 
ATOM   4909 C  C     . ALA B 1 80  ? 47.753  42.479  84.595  1.00 46.01  ? 107 ALA B C     1 
ATOM   4910 O  O     . ALA B 1 80  ? 47.059  43.013  83.723  1.00 58.95  ? 107 ALA B O     1 
ATOM   4911 C  CB    . ALA B 1 80  ? 46.588  43.106  86.704  1.00 45.45  ? 107 ALA B CB    1 
ATOM   4912 N  N     . VAL B 1 81  ? 49.076  42.369  84.474  1.00 42.43  ? 108 VAL B N     1 
ATOM   4913 C  CA    . VAL B 1 81  ? 49.793  42.914  83.327  1.00 54.55  ? 108 VAL B CA    1 
ATOM   4914 C  C     . VAL B 1 81  ? 50.620  41.871  82.593  1.00 57.55  ? 108 VAL B C     1 
ATOM   4915 O  O     . VAL B 1 81  ? 51.280  42.208  81.610  1.00 66.21  ? 108 VAL B O     1 
ATOM   4916 C  CB    . VAL B 1 81  ? 50.687  44.104  83.734  1.00 59.57  ? 108 VAL B CB    1 
ATOM   4917 C  CG1   . VAL B 1 81  ? 49.873  45.161  84.465  1.00 49.33  ? 108 VAL B CG1   1 
ATOM   4918 C  CG2   . VAL B 1 81  ? 51.852  43.627  84.591  1.00 55.92  ? 108 VAL B CG2   1 
ATOM   4919 N  N     . LYS B 1 82  ? 50.597  40.611  83.033  1.00 54.71  ? 109 LYS B N     1 
ATOM   4920 C  CA    . LYS B 1 82  ? 51.482  39.603  82.453  1.00 57.15  ? 109 LYS B CA    1 
ATOM   4921 C  C     . LYS B 1 82  ? 51.215  39.414  80.965  1.00 62.18  ? 109 LYS B C     1 
ATOM   4922 O  O     . LYS B 1 82  ? 52.154  39.288  80.169  1.00 66.18  ? 109 LYS B O     1 
ATOM   4923 C  CB    . LYS B 1 82  ? 51.320  38.275  83.199  1.00 56.01  ? 109 LYS B CB    1 
ATOM   4924 C  CG    . LYS B 1 82  ? 52.561  37.383  83.205  1.00 65.51  ? 109 LYS B CG    1 
ATOM   4925 C  CD    . LYS B 1 82  ? 52.698  36.568  81.925  1.00 89.65  ? 109 LYS B CD    1 
ATOM   4926 C  CE    . LYS B 1 82  ? 53.870  35.601  82.007  1.00 88.30  ? 109 LYS B CE    1 
ATOM   4927 N  NZ    . LYS B 1 82  ? 53.718  34.621  83.118  1.00 78.40  ? 109 LYS B NZ    1 
ATOM   4928 N  N     . SER B 1 83  ? 49.939  39.402  80.570  1.00 61.97  ? 110 SER B N     1 
ATOM   4929 C  CA    . SER B 1 83  ? 49.582  39.105  79.188  1.00 59.08  ? 110 SER B CA    1 
ATOM   4930 C  C     . SER B 1 83  ? 50.032  40.186  78.215  1.00 51.63  ? 110 SER B C     1 
ATOM   4931 O  O     . SER B 1 83  ? 50.145  39.914  77.016  1.00 65.30  ? 110 SER B O     1 
ATOM   4932 C  CB    . SER B 1 83  ? 48.069  38.910  79.071  1.00 58.86  ? 110 SER B CB    1 
ATOM   4933 O  OG    . SER B 1 83  ? 47.382  40.119  79.346  1.00 72.73  ? 110 SER B OG    1 
ATOM   4934 N  N     . LEU B 1 84  ? 50.299  41.396  78.698  1.00 59.15  ? 111 LEU B N     1 
ATOM   4935 C  CA    . LEU B 1 84  ? 50.643  42.510  77.827  1.00 58.08  ? 111 LEU B CA    1 
ATOM   4936 C  C     . LEU B 1 84  ? 52.121  42.562  77.465  1.00 56.33  ? 111 LEU B C     1 
ATOM   4937 O  O     . LEU B 1 84  ? 52.494  43.326  76.570  1.00 55.75  ? 111 LEU B O     1 
ATOM   4938 C  CB    . LEU B 1 84  ? 50.239  43.831  78.488  1.00 63.35  ? 111 LEU B CB    1 
ATOM   4939 C  CG    . LEU B 1 84  ? 48.832  43.865  79.084  1.00 69.91  ? 111 LEU B CG    1 
ATOM   4940 C  CD1   . LEU B 1 84  ? 48.626  45.137  79.887  1.00 60.11  ? 111 LEU B CD1   1 
ATOM   4941 C  CD2   . LEU B 1 84  ? 47.785  43.743  77.989  1.00 72.03  ? 111 LEU B CD2   1 
ATOM   4942 N  N     . TYR B 1 85  ? 52.966  41.776  78.122  1.00 58.29  ? 112 TYR B N     1 
ATOM   4943 C  CA    . TYR B 1 85  ? 54.407  41.898  77.974  1.00 48.44  ? 112 TYR B CA    1 
ATOM   4944 C  C     . TYR B 1 85  ? 55.002  40.675  77.291  1.00 45.82  ? 112 TYR B C     1 
ATOM   4945 O  O     . TYR B 1 85  ? 54.419  39.587  77.281  1.00 53.98  ? 112 TYR B O     1 
ATOM   4946 C  CB    . TYR B 1 85  ? 55.076  42.114  79.335  1.00 45.07  ? 112 TYR B CB    1 
ATOM   4947 C  CG    . TYR B 1 85  ? 54.824  43.491  79.897  1.00 53.06  ? 112 TYR B CG    1 
ATOM   4948 C  CD1   . TYR B 1 85  ? 55.667  44.551  79.592  1.00 59.47  ? 112 TYR B CD1   1 
ATOM   4949 C  CD2   . TYR B 1 85  ? 53.731  43.738  80.714  1.00 49.91  ? 112 TYR B CD2   1 
ATOM   4950 C  CE1   . TYR B 1 85  ? 55.434  45.815  80.094  1.00 53.10  ? 112 TYR B CE1   1 
ATOM   4951 C  CE2   . TYR B 1 85  ? 53.489  44.997  81.222  1.00 54.15  ? 112 TYR B CE2   1 
ATOM   4952 C  CZ    . TYR B 1 85  ? 54.343  46.032  80.908  1.00 50.94  ? 112 TYR B CZ    1 
ATOM   4953 O  OH    . TYR B 1 85  ? 54.103  47.288  81.413  1.00 38.07  ? 112 TYR B OH    1 
ATOM   4954 N  N     . HIS B 1 86  ? 56.188  40.883  76.714  1.00 49.28  ? 113 HIS B N     1 
ATOM   4955 C  CA    . HIS B 1 86  ? 56.899  39.810  76.024  1.00 49.70  ? 113 HIS B CA    1 
ATOM   4956 C  C     . HIS B 1 86  ? 57.145  38.625  76.948  1.00 42.55  ? 113 HIS B C     1 
ATOM   4957 O  O     . HIS B 1 86  ? 56.987  37.468  76.543  1.00 46.96  ? 113 HIS B O     1 
ATOM   4958 C  CB    . HIS B 1 86  ? 58.219  40.348  75.468  1.00 47.30  ? 113 HIS B CB    1 
ATOM   4959 C  CG    . HIS B 1 86  ? 59.087  39.307  74.835  1.00 44.12  ? 113 HIS B CG    1 
ATOM   4960 N  ND1   . HIS B 1 86  ? 58.846  38.801  73.576  1.00 55.23  ? 113 HIS B ND1   1 
ATOM   4961 C  CD2   . HIS B 1 86  ? 60.206  38.689  75.282  1.00 47.72  ? 113 HIS B CD2   1 
ATOM   4962 C  CE1   . HIS B 1 86  ? 59.775  37.910  73.278  1.00 44.48  ? 113 HIS B CE1   1 
ATOM   4963 N  NE2   . HIS B 1 86  ? 60.612  37.823  74.296  1.00 38.08  ? 113 HIS B NE2   1 
ATOM   4964 N  N     . SER B 1 87  ? 57.525  38.895  78.193  1.00 43.09  ? 114 SER B N     1 
ATOM   4965 C  CA    . SER B 1 87  ? 57.734  37.855  79.190  1.00 57.92  ? 114 SER B CA    1 
ATOM   4966 C  C     . SER B 1 87  ? 57.791  38.510  80.561  1.00 48.10  ? 114 SER B C     1 
ATOM   4967 O  O     . SER B 1 87  ? 58.016  39.717  80.683  1.00 48.59  ? 114 SER B O     1 
ATOM   4968 C  CB    . SER B 1 87  ? 59.015  37.060  78.926  1.00 45.37  ? 114 SER B CB    1 
ATOM   4969 O  OG    . SER B 1 87  ? 60.156  37.845  79.211  1.00 52.03  ? 114 SER B OG    1 
ATOM   4970 N  N     . VAL B 1 88  ? 57.589  37.693  81.590  1.00 42.54  ? 115 VAL B N     1 
ATOM   4971 C  CA    . VAL B 1 88  ? 57.621  38.141  82.977  1.00 55.38  ? 115 VAL B CA    1 
ATOM   4972 C  C     . VAL B 1 88  ? 58.361  37.099  83.803  1.00 53.31  ? 115 VAL B C     1 
ATOM   4973 O  O     . VAL B 1 88  ? 58.048  35.906  83.730  1.00 58.34  ? 115 VAL B O     1 
ATOM   4974 C  CB    . VAL B 1 88  ? 56.205  38.367  83.542  1.00 43.29  ? 115 VAL B CB    1 
ATOM   4975 C  CG1   . VAL B 1 88  ? 56.255  38.534  85.050  1.00 43.04  ? 115 VAL B CG1   1 
ATOM   4976 C  CG2   . VAL B 1 88  ? 55.560  39.581  82.894  1.00 42.65  ? 115 VAL B CG2   1 
ATOM   4977 N  N     . GLU B 1 89  ? 59.342  37.546  84.581  1.00 46.75  ? 116 GLU B N     1 
ATOM   4978 C  CA    . GLU B 1 89  ? 60.055  36.693  85.519  1.00 57.93  ? 116 GLU B CA    1 
ATOM   4979 C  C     . GLU B 1 89  ? 59.741  37.129  86.945  1.00 58.06  ? 116 GLU B C     1 
ATOM   4980 O  O     . GLU B 1 89  ? 59.737  38.325  87.253  1.00 52.66  ? 116 GLU B O     1 
ATOM   4981 C  CB    . GLU B 1 89  ? 61.566  36.733  85.272  1.00 52.25  ? 116 GLU B CB    1 
ATOM   4982 C  CG    . GLU B 1 89  ? 62.363  35.874  86.241  1.00 76.90  ? 116 GLU B CG    1 
ATOM   4983 C  CD    . GLU B 1 89  ? 63.578  35.235  85.601  1.00 83.47  ? 116 GLU B CD    1 
ATOM   4984 O  OE1   . GLU B 1 89  ? 63.829  35.498  84.405  1.00 65.35  ? 116 GLU B OE1   1 
ATOM   4985 O  OE2   . GLU B 1 89  ? 64.277  34.465  86.297  1.00 75.90  ? 116 GLU B OE2   1 
ATOM   4986 N  N     . TRP B 1 90  ? 59.485  36.150  87.810  1.00 47.40  ? 117 TRP B N     1 
ATOM   4987 C  CA    . TRP B 1 90  ? 58.989  36.387  89.160  1.00 47.37  ? 117 TRP B CA    1 
ATOM   4988 C  C     . TRP B 1 90  ? 59.816  35.562  90.134  1.00 57.48  ? 117 TRP B C     1 
ATOM   4989 O  O     . TRP B 1 90  ? 59.824  34.329  90.053  1.00 52.44  ? 117 TRP B O     1 
ATOM   4990 C  CB    . TRP B 1 90  ? 57.502  36.028  89.247  1.00 44.12  ? 117 TRP B CB    1 
ATOM   4991 C  CG    . TRP B 1 90  ? 56.876  36.126  90.608  1.00 59.45  ? 117 TRP B CG    1 
ATOM   4992 C  CD1   . TRP B 1 90  ? 56.156  35.157  91.242  1.00 46.31  ? 117 TRP B CD1   1 
ATOM   4993 C  CD2   . TRP B 1 90  ? 56.895  37.254  91.493  1.00 53.68  ? 117 TRP B CD2   1 
ATOM   4994 N  NE1   . TRP B 1 90  ? 55.727  35.608  92.466  1.00 51.55  ? 117 TRP B NE1   1 
ATOM   4995 C  CE2   . TRP B 1 90  ? 56.169  36.892  92.645  1.00 54.10  ? 117 TRP B CE2   1 
ATOM   4996 C  CE3   . TRP B 1 90  ? 57.459  38.532  91.427  1.00 54.61  ? 117 TRP B CE3   1 
ATOM   4997 C  CZ2   . TRP B 1 90  ? 55.991  37.760  93.720  1.00 56.51  ? 117 TRP B CZ2   1 
ATOM   4998 C  CZ3   . TRP B 1 90  ? 57.279  39.393  92.495  1.00 69.75  ? 117 TRP B CZ3   1 
ATOM   4999 C  CH2   . TRP B 1 90  ? 56.552  39.002  93.626  1.00 54.85  ? 117 TRP B CH2   1 
ATOM   5000 N  N     . ARG B 1 91  ? 60.513  36.241  91.049  1.00 55.00  ? 118 ARG B N     1 
ATOM   5001 C  CA    . ARG B 1 91  ? 61.438  35.599  91.984  1.00 53.92  ? 118 ARG B CA    1 
ATOM   5002 C  C     . ARG B 1 91  ? 61.168  36.100  93.398  1.00 56.68  ? 118 ARG B C     1 
ATOM   5003 O  O     . ARG B 1 91  ? 61.870  36.988  93.901  1.00 54.98  ? 118 ARG B O     1 
ATOM   5004 C  CB    . ARG B 1 91  ? 62.890  35.857  91.578  1.00 46.10  ? 118 ARG B CB    1 
ATOM   5005 C  CG    . ARG B 1 91  ? 63.239  35.326  90.195  1.00 86.40  ? 118 ARG B CG    1 
ATOM   5006 C  CD    . ARG B 1 91  ? 64.673  35.639  89.816  1.00 68.63  ? 118 ARG B CD    1 
ATOM   5007 N  NE    . ARG B 1 91  ? 65.600  35.321  90.894  1.00 77.09  ? 118 ARG B NE    1 
ATOM   5008 C  CZ    . ARG B 1 91  ? 66.899  35.114  90.725  1.00 80.29  ? 118 ARG B CZ    1 
ATOM   5009 N  NH1   . ARG B 1 91  ? 67.454  35.147  89.524  1.00 69.55  ? 118 ARG B NH1   1 
ATOM   5010 N  NH2   . ARG B 1 91  ? 67.659  34.860  91.787  1.00 61.01  ? 118 ARG B NH2   1 
ATOM   5011 N  N     . PRO B 1 92  ? 60.157  35.553  94.068  1.00 59.01  ? 119 PRO B N     1 
ATOM   5012 C  CA    . PRO B 1 92  ? 59.895  35.921  95.460  1.00 57.24  ? 119 PRO B CA    1 
ATOM   5013 C  C     . PRO B 1 92  ? 60.558  34.967  96.445  1.00 52.88  ? 119 PRO B C     1 
ATOM   5014 O  O     . PRO B 1 92  ? 60.951  33.848  96.112  1.00 59.19  ? 119 PRO B O     1 
ATOM   5015 C  CB    . PRO B 1 92  ? 58.368  35.816  95.551  1.00 51.64  ? 119 PRO B CB    1 
ATOM   5016 C  CG    . PRO B 1 92  ? 58.053  34.673  94.636  1.00 55.59  ? 119 PRO B CG    1 
ATOM   5017 C  CD    . PRO B 1 92  ? 59.079  34.712  93.517  1.00 50.14  ? 119 PRO B CD    1 
ATOM   5018 N  N     . ALA B 1 93  ? 60.672  35.440  97.688  1.00 57.66  ? 120 ALA B N     1 
ATOM   5019 C  CA    . ALA B 1 93  ? 61.216  34.625  98.774  1.00 59.88  ? 120 ALA B CA    1 
ATOM   5020 C  C     . ALA B 1 93  ? 60.659  35.190  100.081 1.00 56.39  ? 120 ALA B C     1 
ATOM   5021 O  O     . ALA B 1 93  ? 61.128  36.227  100.557 1.00 60.64  ? 120 ALA B O     1 
ATOM   5022 C  CB    . ALA B 1 93  ? 62.736  34.626  98.764  1.00 51.24  ? 120 ALA B CB    1 
ATOM   5023 N  N     . GLU B 1 94  ? 59.667  34.500  100.647 1.00 68.62  ? 121 GLU B N     1 
ATOM   5024 C  CA    . GLU B 1 94  ? 58.959  35.032  101.808 1.00 67.53  ? 121 GLU B CA    1 
ATOM   5025 C  C     . GLU B 1 94  ? 59.861  35.082  103.037 1.00 54.89  ? 121 GLU B C     1 
ATOM   5026 O  O     . GLU B 1 94  ? 59.998  36.133  103.674 1.00 75.50  ? 121 GLU B O     1 
ATOM   5027 C  CB    . GLU B 1 94  ? 57.707  34.198  102.083 1.00 51.46  ? 121 GLU B CB    1 
ATOM   5028 C  CG    . GLU B 1 94  ? 56.773  34.096  100.886 1.00 73.62  ? 121 GLU B CG    1 
ATOM   5029 C  CD    . GLU B 1 94  ? 56.396  35.455  100.322 1.00 93.27  ? 121 GLU B CD    1 
ATOM   5030 O  OE1   . GLU B 1 94  ? 55.936  36.318  101.101 1.00 94.14  ? 121 GLU B OE1   1 
ATOM   5031 O  OE2   . GLU B 1 94  ? 56.569  35.663  99.100  1.00 82.86  ? 121 GLU B OE2   1 
ATOM   5032 N  N     . GLU B 1 95  ? 60.482  33.959  103.386 1.00 59.17  ? 122 GLU B N     1 
ATOM   5033 C  CA    . GLU B 1 95  ? 61.349  33.916  104.551 1.00 58.38  ? 122 GLU B CA    1 
ATOM   5034 C  C     . GLU B 1 95  ? 62.816  33.866  104.130 1.00 58.41  ? 122 GLU B C     1 
ATOM   5035 O  O     . GLU B 1 95  ? 63.150  33.281  103.095 1.00 63.32  ? 122 GLU B O     1 
ATOM   5036 C  CB    . GLU B 1 95  ? 61.029  32.701  105.432 1.00 60.64  ? 122 GLU B CB    1 
ATOM   5037 C  CG    . GLU B 1 95  ? 59.678  32.779  106.136 1.00 72.51  ? 122 GLU B CG    1 
ATOM   5038 C  CD    . GLU B 1 95  ? 59.619  33.885  107.178 1.00 89.42  ? 122 GLU B CD    1 
ATOM   5039 O  OE1   . GLU B 1 95  ? 60.659  34.165  107.812 1.00 93.54  ? 122 GLU B OE1   1 
ATOM   5040 O  OE2   . GLU B 1 95  ? 58.534  34.477  107.362 1.00 101.01 ? 122 GLU B OE2   1 
ATOM   5041 N  N     . PRO B 1 96  ? 63.720  34.484  104.904 1.00 65.70  ? 123 PRO B N     1 
ATOM   5042 C  CA    . PRO B 1 96  ? 63.480  35.256  106.130 1.00 53.41  ? 123 PRO B CA    1 
ATOM   5043 C  C     . PRO B 1 96  ? 63.019  36.673  105.814 1.00 60.80  ? 123 PRO B C     1 
ATOM   5044 O  O     . PRO B 1 96  ? 63.228  37.163  104.707 1.00 65.95  ? 123 PRO B O     1 
ATOM   5045 C  CB    . PRO B 1 96  ? 64.851  35.233  106.812 1.00 55.94  ? 123 PRO B CB    1 
ATOM   5046 C  CG    . PRO B 1 96  ? 65.810  35.259  105.659 1.00 51.52  ? 123 PRO B CG    1 
ATOM   5047 C  CD    . PRO B 1 96  ? 65.157  34.417  104.582 1.00 50.32  ? 123 PRO B CD    1 
ATOM   5048 N  N     . ARG B 1 97  ? 62.388  37.360  106.762 1.00 56.96  ? 124 ARG B N     1 
ATOM   5049 C  CA    . ARG B 1 97  ? 61.906  38.714  106.532 1.00 66.57  ? 124 ARG B CA    1 
ATOM   5050 C  C     . ARG B 1 97  ? 62.941  39.779  106.865 1.00 52.19  ? 124 ARG B C     1 
ATOM   5051 O  O     . ARG B 1 97  ? 62.671  40.967  106.664 1.00 64.92  ? 124 ARG B O     1 
ATOM   5052 C  CB    . ARG B 1 97  ? 60.625  38.961  107.335 1.00 52.26  ? 124 ARG B CB    1 
ATOM   5053 C  CG    . ARG B 1 97  ? 59.489  38.020  106.971 1.00 70.47  ? 124 ARG B CG    1 
ATOM   5054 C  CD    . ARG B 1 97  ? 58.157  38.556  107.455 1.00 73.59  ? 124 ARG B CD    1 
ATOM   5055 N  NE    . ARG B 1 97  ? 58.105  38.657  108.908 1.00 84.56  ? 124 ARG B NE    1 
ATOM   5056 C  CZ    . ARG B 1 97  ? 57.220  39.385  109.575 1.00 98.42  ? 124 ARG B CZ    1 
ATOM   5057 N  NH1   . ARG B 1 97  ? 56.309  40.112  108.947 1.00 81.23  ? 124 ARG B NH1   1 
ATOM   5058 N  NH2   . ARG B 1 97  ? 57.253  39.388  110.904 1.00 82.30  ? 124 ARG B NH2   1 
ATOM   5059 N  N     . SER B 1 98  ? 64.114  39.389  107.357 1.00 55.93  ? 125 SER B N     1 
ATOM   5060 C  CA    . SER B 1 98  ? 65.172  40.340  107.664 1.00 62.33  ? 125 SER B CA    1 
ATOM   5061 C  C     . SER B 1 98  ? 66.508  39.612  107.638 1.00 62.79  ? 125 SER B C     1 
ATOM   5062 O  O     . SER B 1 98  ? 66.580  38.411  107.911 1.00 54.83  ? 125 SER B O     1 
ATOM   5063 C  CB    . SER B 1 98  ? 64.941  41.021  109.020 1.00 54.36  ? 125 SER B CB    1 
ATOM   5064 O  OG    . SER B 1 98  ? 64.422  40.112  109.976 1.00 77.76  ? 125 SER B OG    1 
ATOM   5065 N  N     . TYR B 1 99  ? 67.561  40.352  107.297 1.00 56.31  ? 126 TYR B N     1 
ATOM   5066 C  CA    . TYR B 1 99  ? 68.880  39.751  107.176 1.00 56.63  ? 126 TYR B CA    1 
ATOM   5067 C  C     . TYR B 1 99  ? 69.441  39.408  108.556 1.00 65.09  ? 126 TYR B C     1 
ATOM   5068 O  O     . TYR B 1 99  ? 69.275  40.181  109.505 1.00 72.71  ? 126 TYR B O     1 
ATOM   5069 C  CB    . TYR B 1 99  ? 69.832  40.693  106.442 1.00 53.26  ? 126 TYR B CB    1 
ATOM   5070 C  CG    . TYR B 1 99  ? 69.567  40.785  104.958 1.00 62.53  ? 126 TYR B CG    1 
ATOM   5071 C  CD1   . TYR B 1 99  ? 70.149  39.886  104.074 1.00 63.63  ? 126 TYR B CD1   1 
ATOM   5072 C  CD2   . TYR B 1 99  ? 68.730  41.765  104.441 1.00 51.34  ? 126 TYR B CD2   1 
ATOM   5073 C  CE1   . TYR B 1 99  ? 69.908  39.963  102.715 1.00 51.51  ? 126 TYR B CE1   1 
ATOM   5074 C  CE2   . TYR B 1 99  ? 68.483  41.850  103.082 1.00 49.82  ? 126 TYR B CE2   1 
ATOM   5075 C  CZ    . TYR B 1 99  ? 69.076  40.946  102.225 1.00 48.50  ? 126 TYR B CZ    1 
ATOM   5076 O  OH    . TYR B 1 99  ? 68.839  41.019  100.874 1.00 51.11  ? 126 TYR B OH    1 
ATOM   5077 N  N     . PRO B 1 100 ? 70.115  38.262  108.697 1.00 65.11  ? 127 PRO B N     1 
ATOM   5078 C  CA    . PRO B 1 100 ? 70.644  37.873  110.016 1.00 58.61  ? 127 PRO B CA    1 
ATOM   5079 C  C     . PRO B 1 100 ? 71.727  38.801  110.537 1.00 66.15  ? 127 PRO B C     1 
ATOM   5080 O  O     . PRO B 1 100 ? 72.083  38.702  111.718 1.00 66.25  ? 127 PRO B O     1 
ATOM   5081 C  CB    . PRO B 1 100 ? 71.199  36.460  109.777 1.00 60.87  ? 127 PRO B CB    1 
ATOM   5082 C  CG    . PRO B 1 100 ? 70.612  36.014  108.467 1.00 68.32  ? 127 PRO B CG    1 
ATOM   5083 C  CD    . PRO B 1 100 ? 70.411  37.257  107.665 1.00 52.15  ? 127 PRO B CD    1 
ATOM   5084 N  N     . ASP B 1 101 ? 72.261  39.688  109.698 1.00 66.11  ? 128 ASP B N     1 
ATOM   5085 C  CA    . ASP B 1 101 ? 73.291  40.639  110.095 1.00 63.49  ? 128 ASP B CA    1 
ATOM   5086 C  C     . ASP B 1 101 ? 72.805  42.081  110.040 1.00 66.61  ? 128 ASP B C     1 
ATOM   5087 O  O     . ASP B 1 101 ? 73.620  43.004  110.147 1.00 65.41  ? 128 ASP B O     1 
ATOM   5088 C  CB    . ASP B 1 101 ? 74.533  40.471  109.214 1.00 60.68  ? 128 ASP B CB    1 
ATOM   5089 C  CG    . ASP B 1 101 ? 74.271  40.813  107.756 1.00 67.90  ? 128 ASP B CG    1 
ATOM   5090 O  OD1   . ASP B 1 101 ? 73.092  40.797  107.337 1.00 63.04  ? 128 ASP B OD1   1 
ATOM   5091 O  OD2   . ASP B 1 101 ? 75.246  41.096  107.025 1.00 65.81  ? 128 ASP B OD2   1 
ATOM   5092 N  N     . GLU B 1 102 ? 71.504  42.300  109.872 1.00 69.39  ? 129 GLU B N     1 
ATOM   5093 C  CA    . GLU B 1 102 ? 70.965  43.648  109.769 1.00 67.53  ? 129 GLU B CA    1 
ATOM   5094 C  C     . GLU B 1 102 ? 70.666  44.210  111.154 1.00 63.13  ? 129 GLU B C     1 
ATOM   5095 O  O     . GLU B 1 102 ? 70.254  43.479  112.063 1.00 64.78  ? 129 GLU B O     1 
ATOM   5096 C  CB    . GLU B 1 102 ? 69.699  43.666  108.902 1.00 63.60  ? 129 GLU B CB    1 
ATOM   5097 C  CG    . GLU B 1 102 ? 68.381  43.645  109.672 1.00 57.75  ? 129 GLU B CG    1 
ATOM   5098 C  CD    . GLU B 1 102 ? 67.170  43.754  108.764 1.00 74.67  ? 129 GLU B CD    1 
ATOM   5099 O  OE1   . GLU B 1 102 ? 67.274  43.349  107.586 1.00 62.35  ? 129 GLU B OE1   1 
ATOM   5100 O  OE2   . GLU B 1 102 ? 66.117  44.248  109.227 1.00 67.96  ? 129 GLU B OE2   1 
ATOM   5101 N  N     . GLU B 1 103 ? 70.916  45.510  111.315 1.00 64.48  ? 130 GLU B N     1 
ATOM   5102 C  CA    . GLU B 1 103 ? 70.483  46.239  112.498 1.00 58.03  ? 130 GLU B CA    1 
ATOM   5103 C  C     . GLU B 1 103 ? 69.059  46.752  112.367 1.00 69.36  ? 130 GLU B C     1 
ATOM   5104 O  O     . GLU B 1 103 ? 68.407  47.016  113.385 1.00 74.78  ? 130 GLU B O     1 
ATOM   5105 C  CB    . GLU B 1 103 ? 71.415  47.424  112.764 1.00 66.58  ? 130 GLU B CB    1 
ATOM   5106 C  CG    . GLU B 1 103 ? 72.883  47.056  112.898 1.00 78.50  ? 130 GLU B CG    1 
ATOM   5107 C  CD    . GLU B 1 103 ? 73.786  48.275  112.943 1.00 80.96  ? 130 GLU B CD    1 
ATOM   5108 O  OE1   . GLU B 1 103 ? 73.260  49.408  112.948 1.00 89.20  ? 130 GLU B OE1   1 
ATOM   5109 O  OE2   . GLU B 1 103 ? 75.022  48.100  112.970 1.00 70.67  ? 130 GLU B OE2   1 
ATOM   5110 N  N     . GLY B 1 104 ? 68.569  46.896  111.138 1.00 63.99  ? 131 GLY B N     1 
ATOM   5111 C  CA    . GLY B 1 104 ? 67.228  47.356  110.875 1.00 54.49  ? 131 GLY B CA    1 
ATOM   5112 C  C     . GLY B 1 104 ? 66.908  47.257  109.398 1.00 59.85  ? 131 GLY B C     1 
ATOM   5113 O  O     . GLY B 1 104 ? 67.782  46.977  108.572 1.00 66.09  ? 131 GLY B O     1 
ATOM   5114 N  N     . PRO B 1 105 ? 65.643  47.486  109.034 1.00 59.01  ? 132 PRO B N     1 
ATOM   5115 C  CA    . PRO B 1 105 ? 65.252  47.341  107.622 1.00 50.96  ? 132 PRO B CA    1 
ATOM   5116 C  C     . PRO B 1 105 ? 65.885  48.367  106.699 1.00 55.63  ? 132 PRO B C     1 
ATOM   5117 O  O     . PRO B 1 105 ? 65.945  48.127  105.487 1.00 56.16  ? 132 PRO B O     1 
ATOM   5118 C  CB    . PRO B 1 105 ? 63.726  47.492  107.663 1.00 50.59  ? 132 PRO B CB    1 
ATOM   5119 C  CG    . PRO B 1 105 ? 63.462  48.283  108.903 1.00 62.32  ? 132 PRO B CG    1 
ATOM   5120 C  CD    . PRO B 1 105 ? 64.505  47.854  109.892 1.00 48.14  ? 132 PRO B CD    1 
ATOM   5121 N  N     . LYS B 1 106 ? 66.355  49.497  107.220 1.00 53.48  ? 133 LYS B N     1 
ATOM   5122 C  CA    . LYS B 1 106 ? 67.053  50.488  106.414 1.00 59.91  ? 133 LYS B CA    1 
ATOM   5123 C  C     . LYS B 1 106 ? 68.565  50.395  106.548 1.00 59.47  ? 133 LYS B C     1 
ATOM   5124 O  O     . LYS B 1 106 ? 69.278  51.221  105.973 1.00 69.16  ? 133 LYS B O     1 
ATOM   5125 C  CB    . LYS B 1 106 ? 66.579  51.898  106.778 1.00 52.69  ? 133 LYS B CB    1 
ATOM   5126 C  CG    . LYS B 1 106 ? 65.113  52.133  106.464 1.00 59.29  ? 133 LYS B CG    1 
ATOM   5127 C  CD    . LYS B 1 106 ? 64.794  51.700  105.042 1.00 55.63  ? 133 LYS B CD    1 
ATOM   5128 C  CE    . LYS B 1 106 ? 63.297  51.597  104.814 1.00 64.00  ? 133 LYS B CE    1 
ATOM   5129 N  NZ    . LYS B 1 106 ? 62.979  51.079  103.455 1.00 64.88  ? 133 LYS B NZ    1 
ATOM   5130 N  N     . HIS B 1 107 ? 69.070  49.413  107.285 1.00 57.12  ? 134 HIS B N     1 
ATOM   5131 C  CA    . HIS B 1 107 ? 70.506  49.209  107.395 1.00 59.51  ? 134 HIS B CA    1 
ATOM   5132 C  C     . HIS B 1 107 ? 71.004  48.375  106.219 1.00 61.62  ? 134 HIS B C     1 
ATOM   5133 O  O     . HIS B 1 107 ? 70.450  47.312  105.919 1.00 56.50  ? 134 HIS B O     1 
ATOM   5134 C  CB    . HIS B 1 107 ? 70.844  48.524  108.717 1.00 61.67  ? 134 HIS B CB    1 
ATOM   5135 C  CG    . HIS B 1 107 ? 72.283  48.133  108.845 1.00 69.97  ? 134 HIS B CG    1 
ATOM   5136 N  ND1   . HIS B 1 107 ? 72.683  46.971  109.467 1.00 64.79  ? 134 HIS B ND1   1 
ATOM   5137 C  CD2   . HIS B 1 107 ? 73.416  48.750  108.435 1.00 52.16  ? 134 HIS B CD2   1 
ATOM   5138 C  CE1   . HIS B 1 107 ? 74.001  46.887  109.432 1.00 62.05  ? 134 HIS B CE1   1 
ATOM   5139 N  NE2   . HIS B 1 107 ? 74.470  47.954  108.812 1.00 51.90  ? 134 HIS B NE2   1 
ATOM   5140 N  N     . TRP B 1 108 ? 72.047  48.863  105.550 1.00 53.71  ? 135 TRP B N     1 
ATOM   5141 C  CA    . TRP B 1 108 ? 72.654  48.148  104.427 1.00 55.66  ? 135 TRP B CA    1 
ATOM   5142 C  C     . TRP B 1 108 ? 73.816  47.323  104.960 1.00 64.64  ? 135 TRP B C     1 
ATOM   5143 O  O     . TRP B 1 108 ? 74.949  47.793  105.067 1.00 58.03  ? 135 TRP B O     1 
ATOM   5144 C  CB    . TRP B 1 108 ? 73.095  49.119  103.338 1.00 49.93  ? 135 TRP B CB    1 
ATOM   5145 C  CG    . TRP B 1 108 ? 71.966  49.558  102.465 1.00 48.21  ? 135 TRP B CG    1 
ATOM   5146 C  CD1   . TRP B 1 108 ? 71.167  50.647  102.645 1.00 49.02  ? 135 TRP B CD1   1 
ATOM   5147 C  CD2   . TRP B 1 108 ? 71.497  48.906  101.279 1.00 47.12  ? 135 TRP B CD2   1 
ATOM   5148 N  NE1   . TRP B 1 108 ? 70.232  50.719  101.641 1.00 57.98  ? 135 TRP B NE1   1 
ATOM   5149 C  CE2   . TRP B 1 108 ? 70.413  49.662  100.789 1.00 53.66  ? 135 TRP B CE2   1 
ATOM   5150 C  CE3   . TRP B 1 108 ? 71.892  47.761  100.580 1.00 46.72  ? 135 TRP B CE3   1 
ATOM   5151 C  CZ2   . TRP B 1 108 ? 69.719  49.309  99.633  1.00 52.52  ? 135 TRP B CZ2   1 
ATOM   5152 C  CZ3   . TRP B 1 108 ? 71.200  47.412  99.435  1.00 53.69  ? 135 TRP B CZ3   1 
ATOM   5153 C  CH2   . TRP B 1 108 ? 70.126  48.183  98.973  1.00 53.22  ? 135 TRP B CH2   1 
ATOM   5154 N  N     . SER B 1 109 ? 73.524  46.072  105.306 1.00 56.73  ? 136 SER B N     1 
ATOM   5155 C  CA    . SER B 1 109 ? 74.554  45.149  105.746 1.00 50.19  ? 136 SER B CA    1 
ATOM   5156 C  C     . SER B 1 109 ? 75.277  44.550  104.541 1.00 64.50  ? 136 SER B C     1 
ATOM   5157 O  O     . SER B 1 109 ? 74.833  44.661  103.394 1.00 54.70  ? 136 SER B O     1 
ATOM   5158 C  CB    . SER B 1 109 ? 73.949  44.042  106.606 1.00 61.98  ? 136 SER B CB    1 
ATOM   5159 O  OG    . SER B 1 109 ? 73.161  43.162  105.823 1.00 62.21  ? 136 SER B OG    1 
ATOM   5160 N  N     . ASP B 1 110 ? 76.411  43.902  104.814 1.00 50.12  ? 137 ASP B N     1 
ATOM   5161 C  CA    . ASP B 1 110 ? 77.176  43.291  103.733 1.00 69.55  ? 137 ASP B CA    1 
ATOM   5162 C  C     . ASP B 1 110 ? 76.415  42.141  103.085 1.00 63.06  ? 137 ASP B C     1 
ATOM   5163 O  O     . ASP B 1 110 ? 76.544  41.922  101.874 1.00 53.29  ? 137 ASP B O     1 
ATOM   5164 C  CB    . ASP B 1 110 ? 78.533  42.817  104.250 1.00 55.23  ? 137 ASP B CB    1 
ATOM   5165 C  CG    . ASP B 1 110 ? 79.483  43.967  104.527 1.00 82.31  ? 137 ASP B CG    1 
ATOM   5166 O  OD1   . ASP B 1 110 ? 79.091  45.133  104.294 1.00 74.66  ? 137 ASP B OD1   1 
ATOM   5167 O  OD2   . ASP B 1 110 ? 80.620  43.703  104.976 1.00 77.88  ? 137 ASP B OD2   1 
ATOM   5168 N  N     . SER B 1 111 ? 75.615  41.406  103.864 1.00 56.84  ? 138 SER B N     1 
ATOM   5169 C  CA    . SER B 1 111 ? 74.784  40.359  103.276 1.00 59.06  ? 138 SER B CA    1 
ATOM   5170 C  C     . SER B 1 111 ? 73.687  40.948  102.399 1.00 63.54  ? 138 SER B C     1 
ATOM   5171 O  O     . SER B 1 111 ? 73.318  40.347  101.384 1.00 66.12  ? 138 SER B O     1 
ATOM   5172 C  CB    . SER B 1 111 ? 74.177  39.483  104.373 1.00 47.96  ? 138 SER B CB    1 
ATOM   5173 O  OG    . SER B 1 111 ? 75.189  38.823  105.111 1.00 72.58  ? 138 SER B OG    1 
ATOM   5174 N  N     . ARG B 1 112 ? 73.163  42.119  102.768 1.00 56.45  ? 139 ARG B N     1 
ATOM   5175 C  CA    . ARG B 1 112 ? 72.194  42.801  101.915 1.00 54.36  ? 139 ARG B CA    1 
ATOM   5176 C  C     . ARG B 1 112 ? 72.861  43.346  100.660 1.00 51.85  ? 139 ARG B C     1 
ATOM   5177 O  O     . ARG B 1 112 ? 72.311  43.230  99.559  1.00 49.06  ? 139 ARG B O     1 
ATOM   5178 C  CB    . ARG B 1 112 ? 71.516  43.928  102.693 1.00 54.54  ? 139 ARG B CB    1 
ATOM   5179 C  CG    . ARG B 1 112 ? 70.417  44.654  101.933 1.00 41.55  ? 139 ARG B CG    1 
ATOM   5180 C  CD    . ARG B 1 112 ? 69.922  45.845  102.734 1.00 51.84  ? 139 ARG B CD    1 
ATOM   5181 N  NE    . ARG B 1 112 ? 68.703  46.421  102.184 1.00 43.42  ? 139 ARG B NE    1 
ATOM   5182 C  CZ    . ARG B 1 112 ? 68.105  47.502  102.666 1.00 50.82  ? 139 ARG B CZ    1 
ATOM   5183 N  NH1   . ARG B 1 112 ? 68.588  48.148  103.714 1.00 55.54  ? 139 ARG B NH1   1 
ATOM   5184 N  NH2   . ARG B 1 112 ? 66.999  47.948  102.078 1.00 49.55  ? 139 ARG B NH2   1 
ATOM   5185 N  N     . TYR B 1 113 ? 74.045  43.947  100.808 1.00 58.47  ? 140 TYR B N     1 
ATOM   5186 C  CA    . TYR B 1 113 ? 74.814  44.391  99.649  1.00 51.50  ? 140 TYR B CA    1 
ATOM   5187 C  C     . TYR B 1 113 ? 75.080  43.235  98.694  1.00 53.61  ? 140 TYR B C     1 
ATOM   5188 O  O     . TYR B 1 113 ? 74.898  43.364  97.478  1.00 57.17  ? 140 TYR B O     1 
ATOM   5189 C  CB    . TYR B 1 113 ? 76.134  45.015  100.105 1.00 54.17  ? 140 TYR B CB    1 
ATOM   5190 C  CG    . TYR B 1 113 ? 76.068  46.489  100.430 1.00 56.87  ? 140 TYR B CG    1 
ATOM   5191 C  CD1   . TYR B 1 113 ? 75.471  47.389  99.558  1.00 49.37  ? 140 TYR B CD1   1 
ATOM   5192 C  CD2   . TYR B 1 113 ? 76.614  46.981  101.609 1.00 56.15  ? 140 TYR B CD2   1 
ATOM   5193 C  CE1   . TYR B 1 113 ? 75.416  48.738  99.854  1.00 45.73  ? 140 TYR B CE1   1 
ATOM   5194 C  CE2   . TYR B 1 113 ? 76.565  48.326  101.913 1.00 53.06  ? 140 TYR B CE2   1 
ATOM   5195 C  CZ    . TYR B 1 113 ? 75.966  49.200  101.034 1.00 59.11  ? 140 TYR B CZ    1 
ATOM   5196 O  OH    . TYR B 1 113 ? 75.919  50.539  101.342 1.00 63.01  ? 140 TYR B OH    1 
ATOM   5197 N  N     . GLU B 1 114 ? 75.515  42.092  99.231  1.00 47.44  ? 141 GLU B N     1 
ATOM   5198 C  CA    . GLU B 1 114 ? 75.835  40.944  98.387  1.00 52.30  ? 141 GLU B CA    1 
ATOM   5199 C  C     . GLU B 1 114 ? 74.604  40.441  97.645  1.00 54.15  ? 141 GLU B C     1 
ATOM   5200 O  O     . GLU B 1 114 ? 74.658  40.169  96.440  1.00 65.64  ? 141 GLU B O     1 
ATOM   5201 C  CB    . GLU B 1 114 ? 76.441  39.821  99.229  1.00 55.60  ? 141 GLU B CB    1 
ATOM   5202 C  CG    . GLU B 1 114 ? 76.576  38.502  98.478  1.00 67.41  ? 141 GLU B CG    1 
ATOM   5203 C  CD    . GLU B 1 114 ? 77.148  37.394  99.336  1.00 63.34  ? 141 GLU B CD    1 
ATOM   5204 O  OE1   . GLU B 1 114 ? 77.441  37.656  100.520 1.00 68.91  ? 141 GLU B OE1   1 
ATOM   5205 O  OE2   . GLU B 1 114 ? 77.305  36.264  98.827  1.00 81.85  ? 141 GLU B OE2   1 
ATOM   5206 N  N     . HIS B 1 115 ? 73.482  40.300  98.354  1.00 49.48  ? 142 HIS B N     1 
ATOM   5207 C  CA    . HIS B 1 115 ? 72.273  39.776  97.727  1.00 44.30  ? 142 HIS B CA    1 
ATOM   5208 C  C     . HIS B 1 115 ? 71.765  40.711  96.637  1.00 47.59  ? 142 HIS B C     1 
ATOM   5209 O  O     . HIS B 1 115 ? 71.355  40.259  95.562  1.00 47.66  ? 142 HIS B O     1 
ATOM   5210 C  CB    . HIS B 1 115 ? 71.190  39.546  98.781  1.00 40.49  ? 142 HIS B CB    1 
ATOM   5211 C  CG    . HIS B 1 115 ? 69.939  38.932  98.236  1.00 47.71  ? 142 HIS B CG    1 
ATOM   5212 N  ND1   . HIS B 1 115 ? 69.920  37.691  97.639  1.00 49.63  ? 142 HIS B ND1   1 
ATOM   5213 C  CD2   . HIS B 1 115 ? 68.665  39.390  98.194  1.00 43.39  ? 142 HIS B CD2   1 
ATOM   5214 C  CE1   . HIS B 1 115 ? 68.688  37.408  97.255  1.00 52.67  ? 142 HIS B CE1   1 
ATOM   5215 N  NE2   . HIS B 1 115 ? 67.908  38.423  97.579  1.00 51.39  ? 142 HIS B NE2   1 
ATOM   5216 N  N     . VAL B 1 116 ? 71.788  42.020  96.894  1.00 45.41  ? 143 VAL B N     1 
ATOM   5217 C  CA    . VAL B 1 116 ? 71.287  42.973  95.910  1.00 48.35  ? 143 VAL B CA    1 
ATOM   5218 C  C     . VAL B 1 116 ? 72.185  42.993  94.680  1.00 52.29  ? 143 VAL B C     1 
ATOM   5219 O  O     . VAL B 1 116 ? 71.703  43.083  93.544  1.00 53.44  ? 143 VAL B O     1 
ATOM   5220 C  CB    . VAL B 1 116 ? 71.150  44.369  96.546  1.00 45.69  ? 143 VAL B CB    1 
ATOM   5221 C  CG1   . VAL B 1 116 ? 70.917  45.427  95.482  1.00 43.26  ? 143 VAL B CG1   1 
ATOM   5222 C  CG2   . VAL B 1 116 ? 70.013  44.377  97.549  1.00 42.40  ? 143 VAL B CG2   1 
ATOM   5223 N  N     . MET B 1 117 ? 73.501  42.901  94.884  1.00 48.48  ? 144 MET B N     1 
ATOM   5224 C  CA    . MET B 1 117 ? 74.422  42.827  93.754  1.00 44.76  ? 144 MET B CA    1 
ATOM   5225 C  C     . MET B 1 117 ? 74.155  41.585  92.913  1.00 47.15  ? 144 MET B C     1 
ATOM   5226 O  O     . MET B 1 117 ? 74.068  41.662  91.681  1.00 48.71  ? 144 MET B O     1 
ATOM   5227 C  CB    . MET B 1 117 ? 75.869  42.845  94.251  1.00 41.35  ? 144 MET B CB    1 
ATOM   5228 C  CG    . MET B 1 117 ? 76.432  44.241  94.463  1.00 45.51  ? 144 MET B CG    1 
ATOM   5229 S  SD    . MET B 1 117 ? 78.163  44.263  94.975  1.00 59.18  ? 144 MET B SD    1 
ATOM   5230 C  CE    . MET B 1 117 ? 78.010  43.990  96.736  1.00 57.78  ? 144 MET B CE    1 
ATOM   5231 N  N     . LYS B 1 118 ? 74.016  40.428  93.567  1.00 42.48  ? 145 LYS B N     1 
ATOM   5232 C  CA    . LYS B 1 118 ? 73.712  39.197  92.844  1.00 44.13  ? 145 LYS B CA    1 
ATOM   5233 C  C     . LYS B 1 118 ? 72.378  39.297  92.116  1.00 52.79  ? 145 LYS B C     1 
ATOM   5234 O  O     . LYS B 1 118 ? 72.227  38.771  91.006  1.00 51.75  ? 145 LYS B O     1 
ATOM   5235 C  CB    . LYS B 1 118 ? 73.705  38.010  93.805  1.00 39.54  ? 145 LYS B CB    1 
ATOM   5236 C  CG    . LYS B 1 118 ? 75.065  37.650  94.380  1.00 40.17  ? 145 LYS B CG    1 
ATOM   5237 C  CD    . LYS B 1 118 ? 74.967  36.404  95.244  1.00 49.93  ? 145 LYS B CD    1 
ATOM   5238 C  CE    . LYS B 1 118 ? 76.328  35.938  95.724  1.00 46.66  ? 145 LYS B CE    1 
ATOM   5239 N  NZ    . LYS B 1 118 ? 76.209  34.740  96.600  1.00 67.06  ? 145 LYS B NZ    1 
ATOM   5240 N  N     . LEU B 1 119 ? 71.397  39.966  92.727  1.00 45.03  ? 146 LEU B N     1 
ATOM   5241 C  CA    . LEU B 1 119 ? 70.102  40.137  92.076  1.00 47.21  ? 146 LEU B CA    1 
ATOM   5242 C  C     . LEU B 1 119 ? 70.235  40.955  90.798  1.00 44.05  ? 146 LEU B C     1 
ATOM   5243 O  O     . LEU B 1 119 ? 69.721  40.567  89.742  1.00 49.15  ? 146 LEU B O     1 
ATOM   5244 C  CB    . LEU B 1 119 ? 69.112  40.790  93.040  1.00 48.18  ? 146 LEU B CB    1 
ATOM   5245 C  CG    . LEU B 1 119 ? 68.499  39.866  94.091  1.00 50.31  ? 146 LEU B CG    1 
ATOM   5246 C  CD1   . LEU B 1 119 ? 67.554  40.639  94.992  1.00 54.08  ? 146 LEU B CD1   1 
ATOM   5247 C  CD2   . LEU B 1 119 ? 67.778  38.708  93.422  1.00 43.20  ? 146 LEU B CD2   1 
ATOM   5248 N  N     . ARG B 1 120 ? 70.931  42.093  90.873  1.00 44.33  ? 147 ARG B N     1 
ATOM   5249 C  CA    . ARG B 1 120 ? 71.135  42.912  89.682  1.00 49.43  ? 147 ARG B CA    1 
ATOM   5250 C  C     . ARG B 1 120 ? 71.950  42.166  88.634  1.00 46.85  ? 147 ARG B C     1 
ATOM   5251 O  O     . ARG B 1 120 ? 71.714  42.317  87.430  1.00 47.34  ? 147 ARG B O     1 
ATOM   5252 C  CB    . ARG B 1 120 ? 71.814  44.227  90.057  1.00 46.30  ? 147 ARG B CB    1 
ATOM   5253 C  CG    . ARG B 1 120 ? 70.965  45.121  90.938  1.00 42.05  ? 147 ARG B CG    1 
ATOM   5254 C  CD    . ARG B 1 120 ? 71.319  46.581  90.745  1.00 50.60  ? 147 ARG B CD    1 
ATOM   5255 N  NE    . ARG B 1 120 ? 70.550  47.434  91.642  1.00 52.90  ? 147 ARG B NE    1 
ATOM   5256 C  CZ    . ARG B 1 120 ? 71.003  47.904  92.795  1.00 49.64  ? 147 ARG B CZ    1 
ATOM   5257 N  NH1   . ARG B 1 120 ? 72.237  47.658  93.204  1.00 57.64  ? 147 ARG B NH1   1 
ATOM   5258 N  NH2   . ARG B 1 120 ? 70.198  48.640  93.556  1.00 34.35  ? 147 ARG B NH2   1 
ATOM   5259 N  N     . GLN B 1 121 ? 72.915  41.357  89.073  1.00 46.73  ? 148 GLN B N     1 
ATOM   5260 C  CA    . GLN B 1 121 ? 73.644  40.511  88.135  1.00 41.63  ? 148 GLN B CA    1 
ATOM   5261 C  C     . GLN B 1 121 ? 72.719  39.485  87.496  1.00 48.90  ? 148 GLN B C     1 
ATOM   5262 O  O     . GLN B 1 121 ? 72.819  39.210  86.294  1.00 45.34  ? 148 GLN B O     1 
ATOM   5263 C  CB    . GLN B 1 121 ? 74.805  39.816  88.845  1.00 42.49  ? 148 GLN B CB    1 
ATOM   5264 C  CG    . GLN B 1 121 ? 75.707  39.016  87.918  1.00 47.29  ? 148 GLN B CG    1 
ATOM   5265 C  CD    . GLN B 1 121 ? 76.457  39.894  86.936  1.00 44.82  ? 148 GLN B CD    1 
ATOM   5266 O  OE1   . GLN B 1 121 ? 76.659  41.085  87.178  1.00 50.62  ? 148 GLN B OE1   1 
ATOM   5267 N  NE2   . GLN B 1 121 ? 76.872  39.312  85.817  1.00 38.28  ? 148 GLN B NE2   1 
ATOM   5268 N  N     . ALA B 1 122 ? 71.810  38.907  88.285  1.00 47.26  ? 149 ALA B N     1 
ATOM   5269 C  CA    . ALA B 1 122 ? 70.869  37.932  87.743  1.00 46.25  ? 149 ALA B CA    1 
ATOM   5270 C  C     . ALA B 1 122 ? 69.959  38.566  86.700  1.00 40.14  ? 149 ALA B C     1 
ATOM   5271 O  O     . ALA B 1 122 ? 69.688  37.964  85.654  1.00 48.85  ? 149 ALA B O     1 
ATOM   5272 C  CB    . ALA B 1 122 ? 70.044  37.316  88.872  1.00 35.57  ? 149 ALA B CB    1 
ATOM   5273 N  N     . ALA B 1 123 ? 69.475  39.782  86.969  1.00 36.47  ? 150 ALA B N     1 
ATOM   5274 C  CA    . ALA B 1 123 ? 68.668  40.491  85.983  1.00 48.61  ? 150 ALA B CA    1 
ATOM   5275 C  C     . ALA B 1 123 ? 69.489  40.834  84.746  1.00 52.50  ? 150 ALA B C     1 
ATOM   5276 O  O     . ALA B 1 123 ? 68.984  40.769  83.618  1.00 44.07  ? 150 ALA B O     1 
ATOM   5277 C  CB    . ALA B 1 123 ? 68.076  41.752  86.605  1.00 33.61  ? 150 ALA B CB    1 
ATOM   5278 N  N     . LEU B 1 124 ? 70.759  41.197  84.936  1.00 49.52  ? 151 LEU B N     1 
ATOM   5279 C  CA    . LEU B 1 124 ? 71.631  41.480  83.801  1.00 45.97  ? 151 LEU B CA    1 
ATOM   5280 C  C     . LEU B 1 124 ? 71.862  40.228  82.966  1.00 39.18  ? 151 LEU B C     1 
ATOM   5281 O  O     . LEU B 1 124 ? 71.793  40.268  81.733  1.00 37.10  ? 151 LEU B O     1 
ATOM   5282 C  CB    . LEU B 1 124 ? 72.960  42.055  84.294  1.00 45.31  ? 151 LEU B CB    1 
ATOM   5283 C  CG    . LEU B 1 124 ? 74.051  42.277  83.246  1.00 47.51  ? 151 LEU B CG    1 
ATOM   5284 C  CD1   . LEU B 1 124 ? 73.552  43.175  82.126  1.00 37.63  ? 151 LEU B CD1   1 
ATOM   5285 C  CD2   . LEU B 1 124 ? 75.291  42.871  83.892  1.00 47.30  ? 151 LEU B CD2   1 
ATOM   5286 N  N     . LYS B 1 125 ? 72.142  39.101  83.626  1.00 45.45  ? 152 LYS B N     1 
ATOM   5287 C  CA    . LYS B 1 125 ? 72.281  37.842  82.901  1.00 51.60  ? 152 LYS B CA    1 
ATOM   5288 C  C     . LYS B 1 125 ? 70.977  37.460  82.214  1.00 42.80  ? 152 LYS B C     1 
ATOM   5289 O  O     . LYS B 1 125 ? 70.985  37.000  81.066  1.00 46.26  ? 152 LYS B O     1 
ATOM   5290 C  CB    . LYS B 1 125 ? 72.732  36.730  83.850  1.00 43.01  ? 152 LYS B CB    1 
ATOM   5291 C  CG    . LYS B 1 125 ? 72.681  35.338  83.230  1.00 40.29  ? 152 LYS B CG    1 
ATOM   5292 C  CD    . LYS B 1 125 ? 73.136  34.262  84.204  1.00 47.84  ? 152 LYS B CD    1 
ATOM   5293 C  CE    . LYS B 1 125 ? 72.837  32.871  83.666  1.00 36.66  ? 152 LYS B CE    1 
ATOM   5294 N  NZ    . LYS B 1 125 ? 73.496  32.616  82.355  1.00 72.21  ? 152 LYS B NZ    1 
ATOM   5295 N  N     . SER B 1 126 ? 69.846  37.654  82.896  1.00 42.69  ? 153 SER B N     1 
ATOM   5296 C  CA    . SER B 1 126 ? 68.557  37.324  82.298  1.00 43.92  ? 153 SER B CA    1 
ATOM   5297 C  C     . SER B 1 126 ? 68.305  38.150  81.044  1.00 47.84  ? 153 SER B C     1 
ATOM   5298 O  O     . SER B 1 126 ? 67.775  37.639  80.049  1.00 45.78  ? 153 SER B O     1 
ATOM   5299 C  CB    . SER B 1 126 ? 67.438  37.541  83.316  1.00 40.58  ? 153 SER B CB    1 
ATOM   5300 O  OG    . SER B 1 126 ? 66.229  36.941  82.882  1.00 73.01  ? 153 SER B OG    1 
ATOM   5301 N  N     . ALA B 1 127 ? 68.684  39.430  81.072  1.00 40.99  ? 154 ALA B N     1 
ATOM   5302 C  CA    . ALA B 1 127 ? 68.501  40.285  79.905  1.00 40.64  ? 154 ALA B CA    1 
ATOM   5303 C  C     . ALA B 1 127 ? 69.366  39.825  78.738  1.00 44.62  ? 154 ALA B C     1 
ATOM   5304 O  O     . ALA B 1 127 ? 68.905  39.800  77.591  1.00 48.55  ? 154 ALA B O     1 
ATOM   5305 C  CB    . ALA B 1 127 ? 68.815  41.735  80.268  1.00 32.86  ? 154 ALA B CB    1 
ATOM   5306 N  N     . ARG B 1 128 ? 70.622  39.456  79.009  1.00 51.45  ? 155 ARG B N     1 
ATOM   5307 C  CA    . ARG B 1 128 ? 71.490  38.951  77.949  1.00 40.16  ? 155 ARG B CA    1 
ATOM   5308 C  C     . ARG B 1 128 ? 70.955  37.646  77.374  1.00 52.44  ? 155 ARG B C     1 
ATOM   5309 O  O     . ARG B 1 128 ? 71.020  37.419  76.160  1.00 47.46  ? 155 ARG B O     1 
ATOM   5310 C  CB    . ARG B 1 128 ? 72.911  38.743  78.477  1.00 45.05  ? 155 ARG B CB    1 
ATOM   5311 C  CG    . ARG B 1 128 ? 73.623  39.998  78.957  1.00 38.35  ? 155 ARG B CG    1 
ATOM   5312 C  CD    . ARG B 1 128 ? 75.106  39.708  79.167  1.00 39.57  ? 155 ARG B CD    1 
ATOM   5313 N  NE    . ARG B 1 128 ? 75.871  40.891  79.546  1.00 40.31  ? 155 ARG B NE    1 
ATOM   5314 C  CZ    . ARG B 1 128 ? 76.553  41.013  80.676  1.00 48.78  ? 155 ARG B CZ    1 
ATOM   5315 N  NH1   . ARG B 1 128 ? 76.591  40.037  81.570  1.00 39.18  ? 155 ARG B NH1   1 
ATOM   5316 N  NH2   . ARG B 1 128 ? 77.223  42.138  80.911  1.00 42.42  ? 155 ARG B NH2   1 
ATOM   5317 N  N     . ASP B 1 129 ? 70.423  36.775  78.234  1.00 45.72  ? 156 ASP B N     1 
ATOM   5318 C  CA    . ASP B 1 129 ? 69.974  35.461  77.787  1.00 50.69  ? 156 ASP B CA    1 
ATOM   5319 C  C     . ASP B 1 129 ? 68.727  35.547  76.915  1.00 44.75  ? 156 ASP B C     1 
ATOM   5320 O  O     . ASP B 1 129 ? 68.517  34.684  76.054  1.00 59.05  ? 156 ASP B O     1 
ATOM   5321 C  CB    . ASP B 1 129 ? 69.725  34.558  78.997  1.00 58.43  ? 156 ASP B CB    1 
ATOM   5322 C  CG    . ASP B 1 129 ? 71.008  34.174  79.713  1.00 69.54  ? 156 ASP B CG    1 
ATOM   5323 O  OD1   . ASP B 1 129 ? 72.099  34.453  79.167  1.00 63.76  ? 156 ASP B OD1   1 
ATOM   5324 O  OD2   . ASP B 1 129 ? 70.925  33.593  80.819  1.00 58.08  ? 156 ASP B OD2   1 
ATOM   5325 N  N     . MET B 1 130 ? 67.891  36.566  77.113  1.00 46.24  ? 157 MET B N     1 
ATOM   5326 C  CA    . MET B 1 130 ? 66.693  36.748  76.303  1.00 53.97  ? 157 MET B CA    1 
ATOM   5327 C  C     . MET B 1 130 ? 66.926  37.658  75.108  1.00 51.67  ? 157 MET B C     1 
ATOM   5328 O  O     . MET B 1 130 ? 65.977  37.932  74.364  1.00 47.08  ? 157 MET B O     1 
ATOM   5329 C  CB    . MET B 1 130 ? 65.549  37.299  77.160  1.00 46.27  ? 157 MET B CB    1 
ATOM   5330 C  CG    . MET B 1 130 ? 65.679  38.770  77.513  1.00 51.01  ? 157 MET B CG    1 
ATOM   5331 S  SD    . MET B 1 130 ? 64.389  39.288  78.655  1.00 62.23  ? 157 MET B SD    1 
ATOM   5332 C  CE    . MET B 1 130 ? 62.995  38.401  77.974  1.00 52.72  ? 157 MET B CE    1 
ATOM   5333 N  N     . TRP B 1 131 ? 68.158  38.135  74.920  1.00 40.13  ? 158 TRP B N     1 
ATOM   5334 C  CA    . TRP B 1 131 ? 68.550  38.916  73.746  1.00 50.40  ? 158 TRP B CA    1 
ATOM   5335 C  C     . TRP B 1 131 ? 67.866  40.281  73.717  1.00 51.34  ? 158 TRP B C     1 
ATOM   5336 O  O     . TRP B 1 131 ? 67.500  40.786  72.657  1.00 47.92  ? 158 TRP B O     1 
ATOM   5337 C  CB    . TRP B 1 131 ? 68.281  38.143  72.453  1.00 40.81  ? 158 TRP B CB    1 
ATOM   5338 C  CG    . TRP B 1 131 ? 69.498  37.469  71.911  1.00 45.99  ? 158 TRP B CG    1 
ATOM   5339 C  CD1   . TRP B 1 131 ? 70.786  37.641  72.330  1.00 43.95  ? 158 TRP B CD1   1 
ATOM   5340 C  CD2   . TRP B 1 131 ? 69.549  36.519  70.841  1.00 47.13  ? 158 TRP B CD2   1 
ATOM   5341 N  NE1   . TRP B 1 131 ? 71.635  36.857  71.589  1.00 41.36  ? 158 TRP B NE1   1 
ATOM   5342 C  CE2   . TRP B 1 131 ? 70.900  36.157  70.668  1.00 49.82  ? 158 TRP B CE2   1 
ATOM   5343 C  CE3   . TRP B 1 131 ? 68.584  35.938  70.014  1.00 39.26  ? 158 TRP B CE3   1 
ATOM   5344 C  CZ2   . TRP B 1 131 ? 71.309  35.243  69.700  1.00 47.26  ? 158 TRP B CZ2   1 
ATOM   5345 C  CZ3   . TRP B 1 131 ? 68.993  35.031  69.057  1.00 52.98  ? 158 TRP B CZ3   1 
ATOM   5346 C  CH2   . TRP B 1 131 ? 70.342  34.692  68.908  1.00 49.83  ? 158 TRP B CH2   1 
ATOM   5347 N  N     . ALA B 1 132 ? 67.699  40.882  74.890  1.00 46.41  ? 159 ALA B N     1 
ATOM   5348 C  CA    . ALA B 1 132 ? 67.164  42.230  74.951  1.00 51.84  ? 159 ALA B CA    1 
ATOM   5349 C  C     . ALA B 1 132 ? 68.189  43.230  74.422  1.00 49.75  ? 159 ALA B C     1 
ATOM   5350 O  O     . ALA B 1 132 ? 69.398  42.978  74.408  1.00 43.88  ? 159 ALA B O     1 
ATOM   5351 C  CB    . ALA B 1 132 ? 66.763  42.583  76.383  1.00 30.58  ? 159 ALA B CB    1 
ATOM   5352 N  N     . ASP B 1 133 ? 67.685  44.370  73.952  1.00 44.83  ? 160 ASP B N     1 
ATOM   5353 C  CA    . ASP B 1 133 ? 68.563  45.459  73.542  1.00 48.37  ? 160 ASP B CA    1 
ATOM   5354 C  C     . ASP B 1 133 ? 69.044  46.254  74.745  1.00 45.20  ? 160 ASP B C     1 
ATOM   5355 O  O     . ASP B 1 133 ? 70.217  46.638  74.815  1.00 43.66  ? 160 ASP B O     1 
ATOM   5356 C  CB    . ASP B 1 133 ? 67.841  46.388  72.564  1.00 47.76  ? 160 ASP B CB    1 
ATOM   5357 C  CG    . ASP B 1 133 ? 67.582  45.739  71.219  1.00 42.92  ? 160 ASP B CG    1 
ATOM   5358 O  OD1   . ASP B 1 133 ? 68.514  45.126  70.656  1.00 54.32  ? 160 ASP B OD1   1 
ATOM   5359 O  OD2   . ASP B 1 133 ? 66.442  45.847  70.720  1.00 57.36  ? 160 ASP B OD2   1 
ATOM   5360 N  N     . TYR B 1 134 ? 68.151  46.501  75.698  1.00 41.02  ? 161 TYR B N     1 
ATOM   5361 C  CA    . TYR B 1 134 ? 68.439  47.323  76.860  1.00 44.51  ? 161 TYR B CA    1 
ATOM   5362 C  C     . TYR B 1 134 ? 67.922  46.636  78.112  1.00 40.62  ? 161 TYR B C     1 
ATOM   5363 O  O     . TYR B 1 134 ? 66.981  45.841  78.061  1.00 42.39  ? 161 TYR B O     1 
ATOM   5364 C  CB    . TYR B 1 134 ? 67.790  48.707  76.750  1.00 35.87  ? 161 TYR B CB    1 
ATOM   5365 C  CG    . TYR B 1 134 ? 68.290  49.563  75.609  1.00 47.46  ? 161 TYR B CG    1 
ATOM   5366 C  CD1   . TYR B 1 134 ? 67.728  49.466  74.342  1.00 40.08  ? 161 TYR B CD1   1 
ATOM   5367 C  CD2   . TYR B 1 134 ? 69.311  50.484  75.804  1.00 48.26  ? 161 TYR B CD2   1 
ATOM   5368 C  CE1   . TYR B 1 134 ? 68.179  50.254  73.300  1.00 45.07  ? 161 TYR B CE1   1 
ATOM   5369 C  CE2   . TYR B 1 134 ? 69.767  51.275  74.769  1.00 50.56  ? 161 TYR B CE2   1 
ATOM   5370 C  CZ    . TYR B 1 134 ? 69.198  51.156  73.519  1.00 46.85  ? 161 TYR B CZ    1 
ATOM   5371 O  OH    . TYR B 1 134 ? 69.650  51.944  72.486  1.00 47.72  ? 161 TYR B OH    1 
ATOM   5372 N  N     . ILE B 1 135 ? 68.543  46.954  79.242  1.00 36.32  ? 162 ILE B N     1 
ATOM   5373 C  CA    . ILE B 1 135 ? 68.006  46.620  80.553  1.00 35.32  ? 162 ILE B CA    1 
ATOM   5374 C  C     . ILE B 1 135 ? 67.872  47.920  81.333  1.00 35.15  ? 162 ILE B C     1 
ATOM   5375 O  O     . ILE B 1 135 ? 68.846  48.671  81.478  1.00 42.78  ? 162 ILE B O     1 
ATOM   5376 C  CB    . ILE B 1 135 ? 68.876  45.595  81.302  1.00 44.32  ? 162 ILE B CB    1 
ATOM   5377 C  CG1   . ILE B 1 135 ? 68.340  45.380  82.720  1.00 33.46  ? 162 ILE B CG1   1 
ATOM   5378 C  CG2   . ILE B 1 135 ? 70.342  46.010  81.312  1.00 32.47  ? 162 ILE B CG2   1 
ATOM   5379 C  CD1   . ILE B 1 135 ? 68.902  44.154  83.409  1.00 42.78  ? 162 ILE B CD1   1 
ATOM   5380 N  N     . LEU B 1 136 ? 66.659  48.204  81.796  1.00 44.09  ? 163 LEU B N     1 
ATOM   5381 C  CA    . LEU B 1 136 ? 66.362  49.405  82.565  1.00 40.30  ? 163 LEU B CA    1 
ATOM   5382 C  C     . LEU B 1 136 ? 66.148  49.015  84.018  1.00 44.98  ? 163 LEU B C     1 
ATOM   5383 O  O     . LEU B 1 136 ? 65.208  48.278  84.332  1.00 39.84  ? 163 LEU B O     1 
ATOM   5384 C  CB    . LEU B 1 136 ? 65.123  50.116  82.023  1.00 38.28  ? 163 LEU B CB    1 
ATOM   5385 C  CG    . LEU B 1 136 ? 64.629  51.302  82.852  1.00 34.93  ? 163 LEU B CG    1 
ATOM   5386 C  CD1   . LEU B 1 136 ? 65.494  52.529  82.606  1.00 39.04  ? 163 LEU B CD1   1 
ATOM   5387 C  CD2   . LEU B 1 136 ? 63.169  51.592  82.544  1.00 33.40  ? 163 LEU B CD2   1 
ATOM   5388 N  N     . PHE B 1 137 ? 67.012  49.510  84.898  1.00 44.31  ? 164 PHE B N     1 
ATOM   5389 C  CA    . PHE B 1 137 ? 66.836  49.323  86.330  1.00 42.19  ? 164 PHE B CA    1 
ATOM   5390 C  C     . PHE B 1 137 ? 66.018  50.476  86.891  1.00 42.29  ? 164 PHE B C     1 
ATOM   5391 O  O     . PHE B 1 137 ? 66.291  51.642  86.592  1.00 43.52  ? 164 PHE B O     1 
ATOM   5392 C  CB    . PHE B 1 137 ? 68.188  49.234  87.039  1.00 47.25  ? 164 PHE B CB    1 
ATOM   5393 C  CG    . PHE B 1 137 ? 68.874  47.911  86.865  1.00 43.66  ? 164 PHE B CG    1 
ATOM   5394 C  CD1   . PHE B 1 137 ? 68.593  46.857  87.716  1.00 36.53  ? 164 PHE B CD1   1 
ATOM   5395 C  CD2   . PHE B 1 137 ? 69.795  47.720  85.849  1.00 39.88  ? 164 PHE B CD2   1 
ATOM   5396 C  CE1   . PHE B 1 137 ? 69.218  45.637  87.560  1.00 36.25  ? 164 PHE B CE1   1 
ATOM   5397 C  CE2   . PHE B 1 137 ? 70.423  46.502  85.686  1.00 45.74  ? 164 PHE B CE2   1 
ATOM   5398 C  CZ    . PHE B 1 137 ? 70.135  45.459  86.543  1.00 42.45  ? 164 PHE B CZ    1 
ATOM   5399 N  N     . VAL B 1 138 ? 65.001  50.147  87.683  1.00 41.77  ? 165 VAL B N     1 
ATOM   5400 C  CA    . VAL B 1 138 ? 64.189  51.137  88.378  1.00 43.96  ? 165 VAL B CA    1 
ATOM   5401 C  C     . VAL B 1 138 ? 64.058  50.684  89.822  1.00 45.93  ? 165 VAL B C     1 
ATOM   5402 O  O     . VAL B 1 138 ? 63.564  49.581  90.085  1.00 55.47  ? 165 VAL B O     1 
ATOM   5403 C  CB    . VAL B 1 138 ? 62.798  51.308  87.741  1.00 41.30  ? 165 VAL B CB    1 
ATOM   5404 C  CG1   . VAL B 1 138 ? 62.032  52.421  88.435  1.00 39.47  ? 165 VAL B CG1   1 
ATOM   5405 C  CG2   . VAL B 1 138 ? 62.914  51.585  86.253  1.00 43.49  ? 165 VAL B CG2   1 
ATOM   5406 N  N     . ASP B 1 139 ? 64.510  51.517  90.755  1.00 48.25  ? 166 ASP B N     1 
ATOM   5407 C  CA    . ASP B 1 139 ? 64.267  51.228  92.158  1.00 48.51  ? 166 ASP B CA    1 
ATOM   5408 C  C     . ASP B 1 139 ? 62.779  51.361  92.458  1.00 51.45  ? 166 ASP B C     1 
ATOM   5409 O  O     . ASP B 1 139 ? 62.075  52.187  91.871  1.00 54.30  ? 166 ASP B O     1 
ATOM   5410 C  CB    . ASP B 1 139 ? 65.080  52.158  93.057  1.00 58.63  ? 166 ASP B CB    1 
ATOM   5411 C  CG    . ASP B 1 139 ? 66.548  51.780  93.111  1.00 69.26  ? 166 ASP B CG    1 
ATOM   5412 O  OD1   . ASP B 1 139 ? 67.009  51.032  92.221  1.00 73.63  ? 166 ASP B OD1   1 
ATOM   5413 O  OD2   . ASP B 1 139 ? 67.236  52.223  94.054  1.00 68.52  ? 166 ASP B OD2   1 
ATOM   5414 N  N     . ALA B 1 140 ? 62.302  50.525  93.381  1.00 55.56  ? 167 ALA B N     1 
ATOM   5415 C  CA    . ALA B 1 140 ? 60.870  50.441  93.646  1.00 54.44  ? 167 ALA B CA    1 
ATOM   5416 C  C     . ALA B 1 140 ? 60.292  51.742  94.185  1.00 51.06  ? 167 ALA B C     1 
ATOM   5417 O  O     . ALA B 1 140 ? 59.071  51.930  94.136  1.00 59.88  ? 167 ALA B O     1 
ATOM   5418 C  CB    . ALA B 1 140 ? 60.587  49.296  94.617  1.00 43.10  ? 167 ALA B CB    1 
ATOM   5419 N  N     . ASP B 1 141 ? 61.128  52.640  94.694  1.00 54.68  ? 168 ASP B N     1 
ATOM   5420 C  CA    . ASP B 1 141 ? 60.668  53.934  95.173  1.00 50.52  ? 168 ASP B CA    1 
ATOM   5421 C  C     . ASP B 1 141 ? 60.880  55.052  94.162  1.00 56.01  ? 168 ASP B C     1 
ATOM   5422 O  O     . ASP B 1 141 ? 60.523  56.199  94.447  1.00 55.66  ? 168 ASP B O     1 
ATOM   5423 C  CB    . ASP B 1 141 ? 61.368  54.293  96.489  1.00 38.75  ? 168 ASP B CB    1 
ATOM   5424 C  CG    . ASP B 1 141 ? 62.882  54.243  96.381  1.00 63.42  ? 168 ASP B CG    1 
ATOM   5425 O  OD1   . ASP B 1 141 ? 63.400  53.888  95.302  1.00 74.90  ? 168 ASP B OD1   1 
ATOM   5426 O  OD2   . ASP B 1 141 ? 63.552  54.556  97.385  1.00 52.65  ? 168 ASP B OD2   1 
ATOM   5427 N  N     . ASN B 1 142 ? 61.457  54.754  93.001  1.00 51.49  ? 169 ASN B N     1 
ATOM   5428 C  CA    . ASN B 1 142 ? 61.675  55.774  91.985  1.00 52.59  ? 169 ASN B CA    1 
ATOM   5429 C  C     . ASN B 1 142 ? 60.421  55.932  91.134  1.00 50.61  ? 169 ASN B C     1 
ATOM   5430 O  O     . ASN B 1 142 ? 59.906  54.956  90.579  1.00 51.86  ? 169 ASN B O     1 
ATOM   5431 C  CB    . ASN B 1 142 ? 62.873  55.418  91.104  1.00 60.08  ? 169 ASN B CB    1 
ATOM   5432 C  CG    . ASN B 1 142 ? 64.189  55.454  91.855  1.00 54.88  ? 169 ASN B CG    1 
ATOM   5433 O  OD1   . ASN B 1 142 ? 65.225  55.059  91.324  1.00 52.65  ? 169 ASN B OD1   1 
ATOM   5434 N  ND2   . ASN B 1 142 ? 64.153  55.918  93.099  1.00 58.03  ? 169 ASN B ND2   1 
ATOM   5435 N  N     . LEU B 1 143 ? 59.932  57.164  91.035  1.00 46.14  ? 170 LEU B N     1 
ATOM   5436 C  CA    . LEU B 1 143 ? 58.705  57.477  90.311  1.00 48.33  ? 170 LEU B CA    1 
ATOM   5437 C  C     . LEU B 1 143 ? 59.076  58.095  88.969  1.00 45.76  ? 170 LEU B C     1 
ATOM   5438 O  O     . LEU B 1 143 ? 59.600  59.210  88.918  1.00 52.06  ? 170 LEU B O     1 
ATOM   5439 C  CB    . LEU B 1 143 ? 57.829  58.425  91.128  1.00 38.85  ? 170 LEU B CB    1 
ATOM   5440 C  CG    . LEU B 1 143 ? 56.583  58.969  90.435  1.00 51.63  ? 170 LEU B CG    1 
ATOM   5441 C  CD1   . LEU B 1 143 ? 55.698  57.824  89.985  1.00 66.35  ? 170 LEU B CD1   1 
ATOM   5442 C  CD2   . LEU B 1 143 ? 55.830  59.901  91.364  1.00 52.43  ? 170 LEU B CD2   1 
ATOM   5443 N  N     . ILE B 1 144 ? 58.799  57.377  87.882  1.00 45.80  ? 171 ILE B N     1 
ATOM   5444 C  CA    . ILE B 1 144 ? 59.124  57.852  86.536  1.00 52.16  ? 171 ILE B CA    1 
ATOM   5445 C  C     . ILE B 1 144 ? 57.874  58.553  86.014  1.00 40.03  ? 171 ILE B C     1 
ATOM   5446 O  O     . ILE B 1 144 ? 57.046  57.964  85.319  1.00 50.81  ? 171 ILE B O     1 
ATOM   5447 C  CB    . ILE B 1 144 ? 59.579  56.718  85.625  1.00 50.26  ? 171 ILE B CB    1 
ATOM   5448 C  CG1   . ILE B 1 144 ? 60.602  55.841  86.348  1.00 51.60  ? 171 ILE B CG1   1 
ATOM   5449 C  CG2   . ILE B 1 144 ? 60.169  57.277  84.348  1.00 43.04  ? 171 ILE B CG2   1 
ATOM   5450 C  CD1   . ILE B 1 144 ? 61.858  56.581  86.778  1.00 46.97  ? 171 ILE B CD1   1 
ATOM   5451 N  N     . LEU B 1 145 ? 57.738  59.835  86.359  1.00 47.49  ? 172 LEU B N     1 
ATOM   5452 C  CA    . LEU B 1 145 ? 56.544  60.584  85.975  1.00 52.30  ? 172 LEU B CA    1 
ATOM   5453 C  C     . LEU B 1 145 ? 56.480  60.806  84.470  1.00 47.21  ? 172 LEU B C     1 
ATOM   5454 O  O     . LEU B 1 145 ? 55.399  60.729  83.875  1.00 56.25  ? 172 LEU B O     1 
ATOM   5455 C  CB    . LEU B 1 145 ? 56.498  61.923  86.705  1.00 59.17  ? 172 LEU B CB    1 
ATOM   5456 C  CG    . LEU B 1 145 ? 55.611  61.990  87.945  1.00 69.36  ? 172 LEU B CG    1 
ATOM   5457 C  CD1   . LEU B 1 145 ? 55.317  63.440  88.260  1.00 57.40  ? 172 LEU B CD1   1 
ATOM   5458 C  CD2   . LEU B 1 145 ? 54.323  61.204  87.740  1.00 75.02  ? 172 LEU B CD2   1 
ATOM   5459 N  N     . ASN B 1 146 ? 57.618  61.096  83.839  1.00 51.20  ? 173 ASN B N     1 
ATOM   5460 C  CA    . ASN B 1 146 ? 57.672  61.326  82.398  1.00 55.88  ? 173 ASN B CA    1 
ATOM   5461 C  C     . ASN B 1 146 ? 57.557  59.993  81.671  1.00 51.65  ? 173 ASN B C     1 
ATOM   5462 O  O     . ASN B 1 146 ? 58.461  59.155  81.768  1.00 45.85  ? 173 ASN B O     1 
ATOM   5463 C  CB    . ASN B 1 146 ? 58.969  62.044  82.012  1.00 56.89  ? 173 ASN B CB    1 
ATOM   5464 C  CG    . ASN B 1 146 ? 59.001  62.473  80.547  1.00 49.48  ? 173 ASN B CG    1 
ATOM   5465 O  OD1   . ASN B 1 146 ? 58.224  61.989  79.721  1.00 57.44  ? 173 ASN B OD1   1 
ATOM   5466 N  ND2   . ASN B 1 146 ? 59.914  63.381  80.221  1.00 56.93  ? 173 ASN B ND2   1 
ATOM   5467 N  N     . PRO B 1 147 ? 56.470  59.757  80.931  1.00 48.74  ? 174 PRO B N     1 
ATOM   5468 C  CA    . PRO B 1 147 ? 56.325  58.474  80.231  1.00 50.78  ? 174 PRO B CA    1 
ATOM   5469 C  C     . PRO B 1 147 ? 57.280  58.307  79.064  1.00 58.99  ? 174 PRO B C     1 
ATOM   5470 O  O     . PRO B 1 147 ? 57.397  57.190  78.542  1.00 51.89  ? 174 PRO B O     1 
ATOM   5471 C  CB    . PRO B 1 147 ? 54.866  58.496  79.752  1.00 48.14  ? 174 PRO B CB    1 
ATOM   5472 C  CG    . PRO B 1 147 ? 54.209  59.617  80.513  1.00 39.42  ? 174 PRO B CG    1 
ATOM   5473 C  CD    . PRO B 1 147 ? 55.293  60.617  80.741  1.00 47.33  ? 174 PRO B CD    1 
ATOM   5474 N  N     . ASP B 1 148 ? 57.961  59.366  78.636  1.00 49.14  ? 175 ASP B N     1 
ATOM   5475 C  CA    . ASP B 1 148 ? 58.914  59.281  77.538  1.00 56.00  ? 175 ASP B CA    1 
ATOM   5476 C  C     . ASP B 1 148 ? 60.340  59.049  78.011  1.00 55.08  ? 175 ASP B C     1 
ATOM   5477 O  O     . ASP B 1 148 ? 61.255  59.039  77.182  1.00 56.21  ? 175 ASP B O     1 
ATOM   5478 C  CB    . ASP B 1 148 ? 58.864  60.558  76.694  1.00 48.15  ? 175 ASP B CB    1 
ATOM   5479 C  CG    . ASP B 1 148 ? 57.521  60.764  76.027  1.00 63.84  ? 175 ASP B CG    1 
ATOM   5480 O  OD1   . ASP B 1 148 ? 56.896  59.762  75.617  1.00 72.88  ? 175 ASP B OD1   1 
ATOM   5481 O  OD2   . ASP B 1 148 ? 57.090  61.931  75.917  1.00 73.48  ? 175 ASP B OD2   1 
ATOM   5482 N  N     . THR B 1 149 ? 60.544  58.851  79.316  1.00 48.80  ? 176 THR B N     1 
ATOM   5483 C  CA    . THR B 1 149 ? 61.896  58.740  79.857  1.00 49.94  ? 176 THR B CA    1 
ATOM   5484 C  C     . THR B 1 149 ? 62.671  57.609  79.195  1.00 45.65  ? 176 THR B C     1 
ATOM   5485 O  O     . THR B 1 149 ? 63.846  57.773  78.847  1.00 48.73  ? 176 THR B O     1 
ATOM   5486 C  CB    . THR B 1 149 ? 61.838  58.530  81.370  1.00 50.19  ? 176 THR B CB    1 
ATOM   5487 O  OG1   . THR B 1 149 ? 61.009  59.536  81.964  1.00 52.97  ? 176 THR B OG1   1 
ATOM   5488 C  CG2   . THR B 1 149 ? 63.232  58.610  81.975  1.00 46.39  ? 176 THR B CG2   1 
ATOM   5489 N  N     . LEU B 1 150 ? 62.031  56.453  79.010  1.00 44.74  ? 177 LEU B N     1 
ATOM   5490 C  CA    . LEU B 1 150 ? 62.712  55.324  78.385  1.00 41.30  ? 177 LEU B CA    1 
ATOM   5491 C  C     . LEU B 1 150 ? 63.123  55.650  76.956  1.00 54.92  ? 177 LEU B C     1 
ATOM   5492 O  O     . LEU B 1 150 ? 64.244  55.337  76.538  1.00 48.28  ? 177 LEU B O     1 
ATOM   5493 C  CB    . LEU B 1 150 ? 61.811  54.089  78.421  1.00 36.44  ? 177 LEU B CB    1 
ATOM   5494 C  CG    . LEU B 1 150 ? 62.352  52.801  77.799  1.00 41.78  ? 177 LEU B CG    1 
ATOM   5495 C  CD1   . LEU B 1 150 ? 63.643  52.355  78.468  1.00 45.63  ? 177 LEU B CD1   1 
ATOM   5496 C  CD2   . LEU B 1 150 ? 61.304  51.708  77.879  1.00 36.89  ? 177 LEU B CD2   1 
ATOM   5497 N  N     . SER B 1 151 ? 62.232  56.291  76.194  1.00 53.05  ? 178 SER B N     1 
ATOM   5498 C  CA    . SER B 1 151 ? 62.558  56.642  74.816  1.00 43.09  ? 178 SER B CA    1 
ATOM   5499 C  C     . SER B 1 151 ? 63.683  57.667  74.758  1.00 50.38  ? 178 SER B C     1 
ATOM   5500 O  O     . SER B 1 151 ? 64.586  57.563  73.919  1.00 44.02  ? 178 SER B O     1 
ATOM   5501 C  CB    . SER B 1 151 ? 61.316  57.173  74.103  1.00 41.08  ? 178 SER B CB    1 
ATOM   5502 O  OG    . SER B 1 151 ? 60.298  56.190  74.049  1.00 53.06  ? 178 SER B OG    1 
ATOM   5503 N  N     . LEU B 1 152 ? 63.648  58.662  75.646  1.00 45.70  ? 179 LEU B N     1 
ATOM   5504 C  CA    . LEU B 1 152 ? 64.675  59.697  75.638  1.00 48.25  ? 179 LEU B CA    1 
ATOM   5505 C  C     . LEU B 1 152 ? 66.039  59.136  76.028  1.00 49.44  ? 179 LEU B C     1 
ATOM   5506 O  O     . LEU B 1 152 ? 67.065  59.556  75.483  1.00 58.04  ? 179 LEU B O     1 
ATOM   5507 C  CB    . LEU B 1 152 ? 64.270  60.837  76.570  1.00 44.79  ? 179 LEU B CB    1 
ATOM   5508 C  CG    . LEU B 1 152 ? 62.935  61.507  76.239  1.00 54.48  ? 179 LEU B CG    1 
ATOM   5509 C  CD1   . LEU B 1 152 ? 62.520  62.448  77.353  1.00 36.98  ? 179 LEU B CD1   1 
ATOM   5510 C  CD2   . LEU B 1 152 ? 63.009  62.243  74.910  1.00 34.31  ? 179 LEU B CD2   1 
ATOM   5511 N  N     . LEU B 1 153 ? 66.074  58.184  76.963  1.00 49.14  ? 180 LEU B N     1 
ATOM   5512 C  CA    . LEU B 1 153 ? 67.345  57.574  77.341  1.00 43.72  ? 180 LEU B CA    1 
ATOM   5513 C  C     . LEU B 1 153 ? 67.908  56.729  76.207  1.00 52.44  ? 180 LEU B C     1 
ATOM   5514 O  O     . LEU B 1 153 ? 69.122  56.730  75.968  1.00 53.35  ? 180 LEU B O     1 
ATOM   5515 C  CB    . LEU B 1 153 ? 67.172  56.729  78.603  1.00 45.91  ? 180 LEU B CB    1 
ATOM   5516 C  CG    . LEU B 1 153 ? 66.828  57.490  79.884  1.00 45.11  ? 180 LEU B CG    1 
ATOM   5517 C  CD1   . LEU B 1 153 ? 66.585  56.523  81.029  1.00 38.77  ? 180 LEU B CD1   1 
ATOM   5518 C  CD2   . LEU B 1 153 ? 67.931  58.475  80.233  1.00 47.84  ? 180 LEU B CD2   1 
ATOM   5519 N  N     . ILE B 1 154 ? 67.042  55.997  75.503  1.00 57.43  ? 181 ILE B N     1 
ATOM   5520 C  CA    . ILE B 1 154 ? 67.486  55.233  74.340  1.00 46.13  ? 181 ILE B CA    1 
ATOM   5521 C  C     . ILE B 1 154 ? 68.024  56.170  73.267  1.00 39.13  ? 181 ILE B C     1 
ATOM   5522 O  O     . ILE B 1 154 ? 69.001  55.855  72.577  1.00 51.36  ? 181 ILE B O     1 
ATOM   5523 C  CB    . ILE B 1 154 ? 66.335  54.359  73.806  1.00 48.79  ? 181 ILE B CB    1 
ATOM   5524 C  CG1   . ILE B 1 154 ? 65.988  53.256  74.806  1.00 42.56  ? 181 ILE B CG1   1 
ATOM   5525 C  CG2   . ILE B 1 154 ? 66.691  53.752  72.457  1.00 35.74  ? 181 ILE B CG2   1 
ATOM   5526 C  CD1   . ILE B 1 154 ? 64.869  52.350  74.340  1.00 42.58  ? 181 ILE B CD1   1 
ATOM   5527 N  N     . ALA B 1 155 ? 67.410  57.346  73.125  1.00 50.33  ? 182 ALA B N     1 
ATOM   5528 C  CA    . ALA B 1 155 ? 67.799  58.279  72.075  1.00 53.97  ? 182 ALA B CA    1 
ATOM   5529 C  C     . ALA B 1 155 ? 69.196  58.851  72.278  1.00 48.78  ? 182 ALA B C     1 
ATOM   5530 O  O     . ALA B 1 155 ? 69.799  59.330  71.311  1.00 57.34  ? 182 ALA B O     1 
ATOM   5531 C  CB    . ALA B 1 155 ? 66.784  59.419  71.983  1.00 39.79  ? 182 ALA B CB    1 
ATOM   5532 N  N     . GLU B 1 156 ? 69.724  58.819  73.502  1.00 41.15  ? 183 GLU B N     1 
ATOM   5533 C  CA    . GLU B 1 156 ? 71.045  59.379  73.756  1.00 48.58  ? 183 GLU B CA    1 
ATOM   5534 C  C     . GLU B 1 156 ? 72.175  58.482  73.270  1.00 43.86  ? 183 GLU B C     1 
ATOM   5535 O  O     . GLU B 1 156 ? 73.318  58.947  73.190  1.00 49.99  ? 183 GLU B O     1 
ATOM   5536 C  CB    . GLU B 1 156 ? 71.217  59.670  75.249  1.00 52.55  ? 183 GLU B CB    1 
ATOM   5537 C  CG    . GLU B 1 156 ? 70.196  60.654  75.807  1.00 68.13  ? 183 GLU B CG    1 
ATOM   5538 C  CD    . GLU B 1 156 ? 70.240  62.013  75.122  1.00 69.48  ? 183 GLU B CD    1 
ATOM   5539 O  OE1   . GLU B 1 156 ? 71.308  62.389  74.590  1.00 55.49  ? 183 GLU B OE1   1 
ATOM   5540 O  OE2   . GLU B 1 156 ? 69.204  62.713  75.122  1.00 72.58  ? 183 GLU B OE2   1 
ATOM   5541 N  N     . ASN B 1 157 ? 71.879  57.222  72.951  1.00 51.87  ? 184 ASN B N     1 
ATOM   5542 C  CA    . ASN B 1 157 ? 72.850  56.289  72.378  1.00 52.43  ? 184 ASN B CA    1 
ATOM   5543 C  C     . ASN B 1 157 ? 74.092  56.160  73.257  1.00 55.10  ? 184 ASN B C     1 
ATOM   5544 O  O     . ASN B 1 157 ? 75.226  56.125  72.773  1.00 54.60  ? 184 ASN B O     1 
ATOM   5545 C  CB    . ASN B 1 157 ? 73.225  56.694  70.952  1.00 38.42  ? 184 ASN B CB    1 
ATOM   5546 C  CG    . ASN B 1 157 ? 73.872  55.561  70.178  1.00 53.15  ? 184 ASN B CG    1 
ATOM   5547 O  OD1   . ASN B 1 157 ? 73.613  54.387  70.441  1.00 57.79  ? 184 ASN B OD1   1 
ATOM   5548 N  ND2   . ASN B 1 157 ? 74.726  55.909  69.223  1.00 57.50  ? 184 ASN B ND2   1 
ATOM   5549 N  N     . LYS B 1 158 ? 73.877  56.095  74.565  1.00 50.99  ? 185 LYS B N     1 
ATOM   5550 C  CA    . LYS B 1 158 ? 74.937  55.799  75.514  1.00 48.73  ? 185 LYS B CA    1 
ATOM   5551 C  C     . LYS B 1 158 ? 74.884  54.324  75.893  1.00 49.76  ? 185 LYS B C     1 
ATOM   5552 O  O     . LYS B 1 158 ? 73.901  53.624  75.637  1.00 58.88  ? 185 LYS B O     1 
ATOM   5553 C  CB    . LYS B 1 158 ? 74.813  56.683  76.758  1.00 50.16  ? 185 LYS B CB    1 
ATOM   5554 C  CG    . LYS B 1 158 ? 74.734  58.172  76.460  1.00 53.81  ? 185 LYS B CG    1 
ATOM   5555 C  CD    . LYS B 1 158 ? 75.925  58.640  75.641  1.00 53.24  ? 185 LYS B CD    1 
ATOM   5556 C  CE    . LYS B 1 158 ? 75.837  60.128  75.352  1.00 48.64  ? 185 LYS B CE    1 
ATOM   5557 N  NZ    . LYS B 1 158 ? 76.979  60.594  74.520  1.00 70.22  ? 185 LYS B NZ    1 
ATOM   5558 N  N     . THR B 1 159 ? 75.967  53.846  76.503  1.00 48.73  ? 186 THR B N     1 
ATOM   5559 C  CA    . THR B 1 159 ? 75.976  52.473  76.991  1.00 47.11  ? 186 THR B CA    1 
ATOM   5560 C  C     . THR B 1 159 ? 75.368  52.369  78.383  1.00 45.04  ? 186 THR B C     1 
ATOM   5561 O  O     . THR B 1 159 ? 74.609  51.435  78.658  1.00 53.23  ? 186 THR B O     1 
ATOM   5562 C  CB    . THR B 1 159 ? 77.401  51.914  76.992  1.00 44.81  ? 186 THR B CB    1 
ATOM   5563 O  OG1   . THR B 1 159 ? 77.980  52.073  75.691  1.00 55.26  ? 186 THR B OG1   1 
ATOM   5564 C  CG2   . THR B 1 159 ? 77.394  50.433  77.348  1.00 43.19  ? 186 THR B CG2   1 
ATOM   5565 N  N     . VAL B 1 160 ? 75.685  53.313  79.267  1.00 45.99  ? 187 VAL B N     1 
ATOM   5566 C  CA    . VAL B 1 160 ? 75.079  53.404  80.592  1.00 49.30  ? 187 VAL B CA    1 
ATOM   5567 C  C     . VAL B 1 160 ? 74.681  54.857  80.808  1.00 48.56  ? 187 VAL B C     1 
ATOM   5568 O  O     . VAL B 1 160 ? 75.547  55.723  80.974  1.00 50.84  ? 187 VAL B O     1 
ATOM   5569 C  CB    . VAL B 1 160 ? 76.020  52.929  81.709  1.00 55.05  ? 187 VAL B CB    1 
ATOM   5570 C  CG1   . VAL B 1 160 ? 75.355  53.106  83.067  1.00 41.13  ? 187 VAL B CG1   1 
ATOM   5571 C  CG2   . VAL B 1 160 ? 76.418  51.477  81.495  1.00 45.20  ? 187 VAL B CG2   1 
ATOM   5572 N  N     . VAL B 1 161 ? 73.381  55.127  80.805  1.00 47.75  ? 188 VAL B N     1 
ATOM   5573 C  CA    . VAL B 1 161 ? 72.858  56.470  81.015  1.00 47.33  ? 188 VAL B CA    1 
ATOM   5574 C  C     . VAL B 1 161 ? 71.736  56.402  82.042  1.00 47.56  ? 188 VAL B C     1 
ATOM   5575 O  O     . VAL B 1 161 ? 70.949  55.449  82.059  1.00 43.62  ? 188 VAL B O     1 
ATOM   5576 C  CB    . VAL B 1 161 ? 72.368  57.107  79.696  1.00 40.30  ? 188 VAL B CB    1 
ATOM   5577 C  CG1   . VAL B 1 161 ? 71.233  56.297  79.084  1.00 40.26  ? 188 VAL B CG1   1 
ATOM   5578 C  CG2   . VAL B 1 161 ? 71.945  58.543  79.921  1.00 36.28  ? 188 VAL B CG2   1 
ATOM   5579 N  N     . ALA B 1 162 ? 71.679  57.407  82.914  1.00 39.95  ? 189 ALA B N     1 
ATOM   5580 C  CA    . ALA B 1 162 ? 70.646  57.506  83.925  1.00 42.53  ? 189 ALA B CA    1 
ATOM   5581 C  C     . ALA B 1 162 ? 69.902  58.829  83.795  1.00 46.26  ? 189 ALA B C     1 
ATOM   5582 O  O     . ALA B 1 162 ? 70.496  59.850  83.434  1.00 45.39  ? 189 ALA B O     1 
ATOM   5583 C  CB    . ALA B 1 162 ? 71.231  57.395  85.338  1.00 37.69  ? 189 ALA B CB    1 
ATOM   5584 N  N     . PRO B 1 163 ? 68.598  58.840  84.068  1.00 40.39  ? 190 PRO B N     1 
ATOM   5585 C  CA    . PRO B 1 163 ? 67.860  60.108  84.090  1.00 47.26  ? 190 PRO B CA    1 
ATOM   5586 C  C     . PRO B 1 163 ? 67.999  60.757  85.462  1.00 50.85  ? 190 PRO B C     1 
ATOM   5587 O  O     . PRO B 1 163 ? 67.830  60.104  86.499  1.00 50.76  ? 190 PRO B O     1 
ATOM   5588 C  CB    . PRO B 1 163 ? 66.414  59.679  83.821  1.00 49.62  ? 190 PRO B CB    1 
ATOM   5589 C  CG    . PRO B 1 163 ? 66.336  58.307  84.392  1.00 44.00  ? 190 PRO B CG    1 
ATOM   5590 C  CD    . PRO B 1 163 ? 67.706  57.679  84.241  1.00 39.64  ? 190 PRO B CD    1 
ATOM   5591 N  N     . MET B 1 164 ? 68.323  62.049  85.469  1.00 50.22  ? 191 MET B N     1 
ATOM   5592 C  CA    . MET B 1 164 ? 68.458  62.770  86.729  1.00 51.40  ? 191 MET B CA    1 
ATOM   5593 C  C     . MET B 1 164 ? 67.087  62.905  87.373  1.00 57.02  ? 191 MET B C     1 
ATOM   5594 O  O     . MET B 1 164 ? 66.250  63.690  86.917  1.00 54.64  ? 191 MET B O     1 
ATOM   5595 C  CB    . MET B 1 164 ? 69.085  64.142  86.513  1.00 46.98  ? 191 MET B CB    1 
ATOM   5596 C  CG    . MET B 1 164 ? 69.368  64.850  87.823  1.00 48.83  ? 191 MET B CG    1 
ATOM   5597 S  SD    . MET B 1 164 ? 69.860  66.574  87.680  1.00 68.65  ? 191 MET B SD    1 
ATOM   5598 C  CE    . MET B 1 164 ? 68.291  67.351  87.308  1.00 64.45  ? 191 MET B CE    1 
ATOM   5599 N  N     . LEU B 1 165 ? 66.848  62.129  88.421  1.00 56.84  ? 192 LEU B N     1 
ATOM   5600 C  CA    . LEU B 1 165 ? 65.606  62.210  89.169  1.00 45.92  ? 192 LEU B CA    1 
ATOM   5601 C  C     . LEU B 1 165 ? 65.717  63.289  90.237  1.00 49.52  ? 192 LEU B C     1 
ATOM   5602 O  O     . LEU B 1 165 ? 66.791  63.530  90.795  1.00 58.23  ? 192 LEU B O     1 
ATOM   5603 C  CB    . LEU B 1 165 ? 65.274  60.860  89.807  1.00 47.51  ? 192 LEU B CB    1 
ATOM   5604 C  CG    . LEU B 1 165 ? 65.200  59.697  88.812  1.00 49.67  ? 192 LEU B CG    1 
ATOM   5605 C  CD1   . LEU B 1 165 ? 64.897  58.387  89.522  1.00 57.15  ? 192 LEU B CD1   1 
ATOM   5606 C  CD2   . LEU B 1 165 ? 64.161  59.982  87.740  1.00 43.65  ? 192 LEU B CD2   1 
ATOM   5607 N  N     . ASP B 1 166 ? 64.596  63.943  90.509  1.00 58.69  ? 193 ASP B N     1 
ATOM   5608 C  CA    . ASP B 1 166 ? 64.558  65.060  91.440  1.00 55.80  ? 193 ASP B CA    1 
ATOM   5609 C  C     . ASP B 1 166 ? 64.220  64.584  92.846  1.00 58.40  ? 193 ASP B C     1 
ATOM   5610 O  O     . ASP B 1 166 ? 63.515  63.589  93.037  1.00 60.79  ? 193 ASP B O     1 
ATOM   5611 C  CB    . ASP B 1 166 ? 63.534  66.101  90.985  1.00 59.69  ? 193 ASP B CB    1 
ATOM   5612 C  CG    . ASP B 1 166 ? 63.859  66.678  89.621  1.00 87.61  ? 193 ASP B CG    1 
ATOM   5613 O  OD1   . ASP B 1 166 ? 64.989  66.458  89.139  1.00 95.77  ? 193 ASP B OD1   1 
ATOM   5614 O  OD2   . ASP B 1 166 ? 62.985  67.343  89.029  1.00 94.06  ? 193 ASP B OD2   1 
ATOM   5615 N  N     . SER B 1 167 ? 64.730  65.315  93.835  1.00 57.69  ? 194 SER B N     1 
ATOM   5616 C  CA    . SER B 1 167 ? 64.461  65.027  95.234  1.00 56.61  ? 194 SER B CA    1 
ATOM   5617 C  C     . SER B 1 167 ? 64.155  66.330  95.957  1.00 58.23  ? 194 SER B C     1 
ATOM   5618 O  O     . SER B 1 167 ? 64.261  67.422  95.393  1.00 58.99  ? 194 SER B O     1 
ATOM   5619 C  CB    . SER B 1 167 ? 65.640  64.310  95.906  1.00 57.64  ? 194 SER B CB    1 
ATOM   5620 O  OG    . SER B 1 167 ? 66.696  65.213  96.187  1.00 55.01  ? 194 SER B OG    1 
ATOM   5621 N  N     . ARG B 1 168 ? 63.771  66.204  97.228  1.00 66.10  ? 195 ARG B N     1 
ATOM   5622 C  CA    . ARG B 1 168 ? 63.530  67.369  98.068  1.00 62.05  ? 195 ARG B CA    1 
ATOM   5623 C  C     . ARG B 1 168 ? 64.805  68.129  98.400  1.00 61.46  ? 195 ARG B C     1 
ATOM   5624 O  O     . ARG B 1 168 ? 64.722  69.243  98.930  1.00 67.38  ? 195 ARG B O     1 
ATOM   5625 C  CB    . ARG B 1 168 ? 62.849  66.947  99.371  1.00 50.61  ? 195 ARG B CB    1 
ATOM   5626 C  CG    . ARG B 1 168 ? 63.725  66.067  100.252 1.00 57.30  ? 195 ARG B CG    1 
ATOM   5627 C  CD    . ARG B 1 168 ? 63.037  65.714  101.558 1.00 53.81  ? 195 ARG B CD    1 
ATOM   5628 N  NE    . ARG B 1 168 ? 63.716  64.619  102.240 1.00 65.30  ? 195 ARG B NE    1 
ATOM   5629 C  CZ    . ARG B 1 168 ? 64.674  64.774  103.143 1.00 53.56  ? 195 ARG B CZ    1 
ATOM   5630 N  NH1   . ARG B 1 168 ? 65.088  65.975  103.512 1.00 56.47  ? 195 ARG B NH1   1 
ATOM   5631 N  NH2   . ARG B 1 168 ? 65.229  63.697  103.691 1.00 64.66  ? 195 ARG B NH2   1 
ATOM   5632 N  N     . ALA B 1 169 ? 65.972  67.560  98.113  1.00 55.63  ? 196 ALA B N     1 
ATOM   5633 C  CA    . ALA B 1 169 ? 67.242  68.154  98.504  1.00 50.31  ? 196 ALA B CA    1 
ATOM   5634 C  C     . ALA B 1 169 ? 68.207  68.047  97.329  1.00 55.21  ? 196 ALA B C     1 
ATOM   5635 O  O     . ALA B 1 169 ? 67.816  67.718  96.204  1.00 57.67  ? 196 ALA B O     1 
ATOM   5636 C  CB    . ALA B 1 169 ? 67.788  67.475  99.767  1.00 47.83  ? 196 ALA B CB    1 
ATOM   5637 N  N     . ALA B 1 170 ? 69.485  68.324  97.598  1.00 55.18  ? 197 ALA B N     1 
ATOM   5638 C  CA    . ALA B 1 170 ? 70.509  68.231  96.565  1.00 51.01  ? 197 ALA B CA    1 
ATOM   5639 C  C     . ALA B 1 170 ? 70.763  66.796  96.126  1.00 61.56  ? 197 ALA B C     1 
ATOM   5640 O  O     . ALA B 1 170 ? 71.365  66.583  95.067  1.00 67.01  ? 197 ALA B O     1 
ATOM   5641 C  CB    . ALA B 1 170 ? 71.813  68.861  97.058  1.00 54.50  ? 197 ALA B CB    1 
ATOM   5642 N  N     . TYR B 1 171 ? 70.324  65.813  96.911  1.00 64.11  ? 198 TYR B N     1 
ATOM   5643 C  CA    . TYR B 1 171 ? 70.531  64.418  96.551  1.00 55.26  ? 198 TYR B CA    1 
ATOM   5644 C  C     . TYR B 1 171 ? 69.881  64.101  95.212  1.00 57.53  ? 198 TYR B C     1 
ATOM   5645 O  O     . TYR B 1 171 ? 68.790  64.584  94.899  1.00 62.66  ? 198 TYR B O     1 
ATOM   5646 C  CB    . TYR B 1 171 ? 69.963  63.498  97.636  1.00 43.50  ? 198 TYR B CB    1 
ATOM   5647 C  CG    . TYR B 1 171 ? 69.932  62.033  97.247  1.00 51.48  ? 198 TYR B CG    1 
ATOM   5648 C  CD1   . TYR B 1 171 ? 71.019  61.204  97.491  1.00 42.24  ? 198 TYR B CD1   1 
ATOM   5649 C  CD2   . TYR B 1 171 ? 68.811  61.479  96.641  1.00 63.64  ? 198 TYR B CD2   1 
ATOM   5650 C  CE1   . TYR B 1 171 ? 70.991  59.868  97.137  1.00 50.51  ? 198 TYR B CE1   1 
ATOM   5651 C  CE2   . TYR B 1 171 ? 68.776  60.149  96.281  1.00 59.41  ? 198 TYR B CE2   1 
ATOM   5652 C  CZ    . TYR B 1 171 ? 69.868  59.347  96.532  1.00 50.63  ? 198 TYR B CZ    1 
ATOM   5653 O  OH    . TYR B 1 171 ? 69.834  58.017  96.180  1.00 59.37  ? 198 TYR B OH    1 
ATOM   5654 N  N     . SER B 1 172 ? 70.564  63.280  94.423  1.00 51.96  ? 199 SER B N     1 
ATOM   5655 C  CA    . SER B 1 172 ? 70.035  62.762  93.172  1.00 53.49  ? 199 SER B CA    1 
ATOM   5656 C  C     . SER B 1 172 ? 70.743  61.447  92.880  1.00 58.98  ? 199 SER B C     1 
ATOM   5657 O  O     . SER B 1 172 ? 71.626  61.015  93.627  1.00 60.98  ? 199 SER B O     1 
ATOM   5658 C  CB    . SER B 1 172 ? 70.209  63.770  92.031  1.00 48.38  ? 199 SER B CB    1 
ATOM   5659 O  OG    . SER B 1 172 ? 69.562  63.320  90.854  1.00 53.81  ? 199 SER B OG    1 
ATOM   5660 N  N     . ASN B 1 173 ? 70.353  60.807  91.783  1.00 50.13  ? 200 ASN B N     1 
ATOM   5661 C  CA    . ASN B 1 173 ? 70.908  59.505  91.421  1.00 43.20  ? 200 ASN B CA    1 
ATOM   5662 C  C     . ASN B 1 173 ? 72.247  59.604  90.695  1.00 55.32  ? 200 ASN B C     1 
ATOM   5663 O  O     . ASN B 1 173 ? 72.526  58.804  89.801  1.00 53.82  ? 200 ASN B O     1 
ATOM   5664 C  CB    . ASN B 1 173 ? 69.888  58.739  90.580  1.00 48.95  ? 200 ASN B CB    1 
ATOM   5665 C  CG    . ASN B 1 173 ? 69.341  59.563  89.424  1.00 57.67  ? 200 ASN B CG    1 
ATOM   5666 O  OD1   . ASN B 1 173 ? 68.897  60.697  89.607  1.00 55.37  ? 200 ASN B OD1   1 
ATOM   5667 N  ND2   . ASN B 1 173 ? 69.378  58.994  88.224  1.00 50.60  ? 200 ASN B ND2   1 
ATOM   5668 N  N     . PHE B 1 174 ? 73.093  60.568  91.054  1.00 52.09  ? 201 PHE B N     1 
ATOM   5669 C  CA    . PHE B 1 174 ? 74.374  60.709  90.376  1.00 62.19  ? 201 PHE B CA    1 
ATOM   5670 C  C     . PHE B 1 174 ? 75.347  61.478  91.257  1.00 55.42  ? 201 PHE B C     1 
ATOM   5671 O  O     . PHE B 1 174 ? 74.951  62.352  92.031  1.00 53.84  ? 201 PHE B O     1 
ATOM   5672 C  CB    . PHE B 1 174 ? 74.218  61.412  89.023  1.00 60.86  ? 201 PHE B CB    1 
ATOM   5673 C  CG    . PHE B 1 174 ? 74.096  62.909  89.120  1.00 57.13  ? 201 PHE B CG    1 
ATOM   5674 C  CD1   . PHE B 1 174 ? 72.885  63.500  89.434  1.00 52.76  ? 201 PHE B CD1   1 
ATOM   5675 C  CD2   . PHE B 1 174 ? 75.193  63.723  88.885  1.00 55.53  ? 201 PHE B CD2   1 
ATOM   5676 C  CE1   . PHE B 1 174 ? 72.771  64.875  89.521  1.00 62.29  ? 201 PHE B CE1   1 
ATOM   5677 C  CE2   . PHE B 1 174 ? 75.083  65.098  88.972  1.00 55.40  ? 201 PHE B CE2   1 
ATOM   5678 C  CZ    . PHE B 1 174 ? 73.871  65.674  89.289  1.00 54.94  ? 201 PHE B CZ    1 
ATOM   5679 N  N     . TRP B 1 175 ? 76.624  61.133  91.124  1.00 55.58  ? 202 TRP B N     1 
ATOM   5680 C  CA    . TRP B 1 175 ? 77.727  61.885  91.700  1.00 53.09  ? 202 TRP B CA    1 
ATOM   5681 C  C     . TRP B 1 175 ? 78.485  62.587  90.584  1.00 64.10  ? 202 TRP B C     1 
ATOM   5682 O  O     . TRP B 1 175 ? 78.575  62.081  89.462  1.00 66.49  ? 202 TRP B O     1 
ATOM   5683 C  CB    . TRP B 1 175 ? 78.708  60.986  92.459  1.00 61.10  ? 202 TRP B CB    1 
ATOM   5684 C  CG    . TRP B 1 175 ? 78.112  60.103  93.512  1.00 63.63  ? 202 TRP B CG    1 
ATOM   5685 C  CD1   . TRP B 1 175 ? 76.815  60.080  93.941  1.00 62.13  ? 202 TRP B CD1   1 
ATOM   5686 C  CD2   . TRP B 1 175 ? 78.806  59.112  94.278  1.00 66.52  ? 202 TRP B CD2   1 
ATOM   5687 N  NE1   . TRP B 1 175 ? 76.660  59.132  94.926  1.00 71.60  ? 202 TRP B NE1   1 
ATOM   5688 C  CE2   . TRP B 1 175 ? 77.869  58.524  95.150  1.00 59.98  ? 202 TRP B CE2   1 
ATOM   5689 C  CE3   . TRP B 1 175 ? 80.130  58.664  94.308  1.00 67.91  ? 202 TRP B CE3   1 
ATOM   5690 C  CZ2   . TRP B 1 175 ? 78.214  57.511  96.042  1.00 51.87  ? 202 TRP B CZ2   1 
ATOM   5691 C  CZ3   . TRP B 1 175 ? 80.471  57.660  95.194  1.00 59.45  ? 202 TRP B CZ3   1 
ATOM   5692 C  CH2   . TRP B 1 175 ? 79.518  57.095  96.050  1.00 68.90  ? 202 TRP B CH2   1 
ATOM   5693 N  N     . CYS B 1 176 ? 79.045  63.751  90.900  1.00 71.73  ? 203 CYS B N     1 
ATOM   5694 C  CA    . CYS B 1 176 ? 79.888  64.446  89.936  1.00 80.52  ? 203 CYS B CA    1 
ATOM   5695 C  C     . CYS B 1 176 ? 81.369  64.156  90.134  1.00 84.12  ? 203 CYS B C     1 
ATOM   5696 O  O     . CYS B 1 176 ? 82.144  64.267  89.178  1.00 70.36  ? 203 CYS B O     1 
ATOM   5697 C  CB    . CYS B 1 176 ? 79.645  65.953  90.007  1.00 67.21  ? 203 CYS B CB    1 
ATOM   5698 S  SG    . CYS B 1 176 ? 78.655  66.593  88.641  1.00 79.67  ? 203 CYS B SG    1 
ATOM   5699 N  N     . GLY B 1 177 ? 81.778  63.787  91.347  1.00 81.43  ? 204 GLY B N     1 
ATOM   5700 C  CA    . GLY B 1 177 ? 83.163  63.458  91.609  1.00 66.53  ? 204 GLY B CA    1 
ATOM   5701 C  C     . GLY B 1 177 ? 83.274  62.224  92.482  1.00 78.11  ? 204 GLY B C     1 
ATOM   5702 O  O     . GLY B 1 177 ? 82.335  61.843  93.184  1.00 82.05  ? 204 GLY B O     1 
ATOM   5703 N  N     . MET B 1 178 ? 84.448  61.598  92.418  1.00 81.49  ? 205 MET B N     1 
ATOM   5704 C  CA    . MET B 1 178 ? 84.763  60.425  93.220  1.00 78.97  ? 205 MET B CA    1 
ATOM   5705 C  C     . MET B 1 178 ? 86.205  60.532  93.696  1.00 84.27  ? 205 MET B C     1 
ATOM   5706 O  O     . MET B 1 178 ? 87.070  61.030  92.969  1.00 97.27  ? 205 MET B O     1 
ATOM   5707 C  CB    . MET B 1 178 ? 84.549  59.126  92.428  1.00 65.87  ? 205 MET B CB    1 
ATOM   5708 C  CG    . MET B 1 178 ? 84.439  57.879  93.294  1.00 79.94  ? 205 MET B CG    1 
ATOM   5709 S  SD    . MET B 1 178 ? 84.252  56.356  92.343  1.00 83.76  ? 205 MET B SD    1 
ATOM   5710 C  CE    . MET B 1 178 ? 82.629  56.590  91.625  1.00 52.43  ? 205 MET B CE    1 
ATOM   5711 N  N     . THR B 1 179 ? 86.459  60.053  94.915  1.00 94.21  ? 206 THR B N     1 
ATOM   5712 C  CA    . THR B 1 179 ? 87.689  60.343  95.641  1.00 98.12  ? 206 THR B CA    1 
ATOM   5713 C  C     . THR B 1 179 ? 88.800  59.328  95.395  1.00 106.61 ? 206 THR B C     1 
ATOM   5714 O  O     . THR B 1 179 ? 89.709  59.218  96.227  1.00 112.44 ? 206 THR B O     1 
ATOM   5715 C  CB    . THR B 1 179 ? 87.408  60.417  97.142  1.00 98.31  ? 206 THR B CB    1 
ATOM   5716 O  OG1   . THR B 1 179 ? 87.024  59.120  97.615  1.00 97.34  ? 206 THR B OG1   1 
ATOM   5717 C  CG2   . THR B 1 179 ? 86.296  61.409  97.431  1.00 104.93 ? 206 THR B CG2   1 
ATOM   5718 N  N     . SER B 1 180 ? 88.741  58.578  94.292  1.00 94.89  ? 207 SER B N     1 
ATOM   5719 C  CA    . SER B 1 180 ? 89.756  57.580  93.956  1.00 102.98 ? 207 SER B CA    1 
ATOM   5720 C  C     . SER B 1 180 ? 89.851  56.487  95.018  1.00 103.60 ? 207 SER B C     1 
ATOM   5721 O  O     . SER B 1 180 ? 90.722  55.614  94.944  1.00 84.82  ? 207 SER B O     1 
ATOM   5722 C  CB    . SER B 1 180 ? 91.125  58.241  93.744  1.00 108.16 ? 207 SER B CB    1 
ATOM   5723 O  OG    . SER B 1 180 ? 91.679  58.703  94.965  1.00 123.84 ? 207 SER B OG    1 
ATOM   5724 N  N     . GLN B 1 181 ? 88.963  56.531  96.012  1.00 104.11 ? 208 GLN B N     1 
ATOM   5725 C  CA    . GLN B 1 181 ? 88.768  55.432  96.948  1.00 90.13  ? 208 GLN B CA    1 
ATOM   5726 C  C     . GLN B 1 181 ? 87.312  54.989  96.986  1.00 89.31  ? 208 GLN B C     1 
ATOM   5727 O  O     . GLN B 1 181 ? 86.941  54.172  97.838  1.00 91.19  ? 208 GLN B O     1 
ATOM   5728 C  CB    . GLN B 1 181 ? 89.242  55.820  98.352  1.00 86.84  ? 208 GLN B CB    1 
ATOM   5729 C  CG    . GLN B 1 181 ? 90.722  56.160  98.447  1.00 103.45 ? 208 GLN B CG    1 
ATOM   5730 C  CD    . GLN B 1 181 ? 91.184  56.349  99.881  1.00 102.94 ? 208 GLN B CD    1 
ATOM   5731 O  OE1   . GLN B 1 181 ? 90.517  55.916  100.820 1.00 97.68  ? 208 GLN B OE1   1 
ATOM   5732 N  NE2   . GLN B 1 181 ? 92.329  56.999  100.056 1.00 111.85 ? 208 GLN B NE2   1 
ATOM   5733 N  N     . GLY B 1 182 ? 86.479  55.515  96.088  1.00 84.49  ? 209 GLY B N     1 
ATOM   5734 C  CA    . GLY B 1 182 ? 85.079  55.159  96.014  1.00 85.98  ? 209 GLY B CA    1 
ATOM   5735 C  C     . GLY B 1 182 ? 84.131  56.092  96.735  1.00 81.66  ? 209 GLY B C     1 
ATOM   5736 O  O     . GLY B 1 182 ? 82.913  55.914  96.621  1.00 82.53  ? 209 GLY B O     1 
ATOM   5737 N  N     . TYR B 1 183 ? 84.642  57.078  97.463  1.00 88.41  ? 210 TYR B N     1 
ATOM   5738 C  CA    . TYR B 1 183 ? 83.803  57.952  98.269  1.00 81.65  ? 210 TYR B CA    1 
ATOM   5739 C  C     . TYR B 1 183 ? 83.255  59.102  97.432  1.00 83.21  ? 210 TYR B C     1 
ATOM   5740 O  O     . TYR B 1 183 ? 83.861  59.522  96.441  1.00 74.83  ? 210 TYR B O     1 
ATOM   5741 C  CB    . TYR B 1 183 ? 84.590  58.503  99.461  1.00 90.24  ? 210 TYR B CB    1 
ATOM   5742 C  CG    . TYR B 1 183 ? 85.310  57.442  100.268 1.00 99.76  ? 210 TYR B CG    1 
ATOM   5743 C  CD1   . TYR B 1 183 ? 84.670  56.263  100.632 1.00 101.04 ? 210 TYR B CD1   1 
ATOM   5744 C  CD2   . TYR B 1 183 ? 86.634  57.615  100.657 1.00 104.96 ? 210 TYR B CD2   1 
ATOM   5745 C  CE1   . TYR B 1 183 ? 85.324  55.291  101.368 1.00 96.09  ? 210 TYR B CE1   1 
ATOM   5746 C  CE2   . TYR B 1 183 ? 87.297  56.647  101.391 1.00 106.24 ? 210 TYR B CE2   1 
ATOM   5747 C  CZ    . TYR B 1 183 ? 86.636  55.487  101.744 1.00 108.42 ? 210 TYR B CZ    1 
ATOM   5748 O  OH    . TYR B 1 183 ? 87.289  54.521  102.475 1.00 99.30  ? 210 TYR B OH    1 
ATOM   5749 N  N     . TYR B 1 184 ? 82.092  59.606  97.843  1.00 75.84  ? 211 TYR B N     1 
ATOM   5750 C  CA    . TYR B 1 184 ? 81.477  60.734  97.157  1.00 78.30  ? 211 TYR B CA    1 
ATOM   5751 C  C     . TYR B 1 184 ? 82.340  61.983  97.301  1.00 84.72  ? 211 TYR B C     1 
ATOM   5752 O  O     . TYR B 1 184 ? 82.998  62.201  98.322  1.00 72.39  ? 211 TYR B O     1 
ATOM   5753 C  CB    . TYR B 1 184 ? 80.073  60.996  97.707  1.00 67.63  ? 211 TYR B CB    1 
ATOM   5754 C  CG    . TYR B 1 184 ? 79.418  62.246  97.157  1.00 74.86  ? 211 TYR B CG    1 
ATOM   5755 C  CD1   . TYR B 1 184 ? 78.714  62.217  95.961  1.00 79.68  ? 211 TYR B CD1   1 
ATOM   5756 C  CD2   . TYR B 1 184 ? 79.506  63.455  97.836  1.00 68.90  ? 211 TYR B CD2   1 
ATOM   5757 C  CE1   . TYR B 1 184 ? 78.117  63.357  95.453  1.00 71.52  ? 211 TYR B CE1   1 
ATOM   5758 C  CE2   . TYR B 1 184 ? 78.914  64.599  97.337  1.00 70.84  ? 211 TYR B CE2   1 
ATOM   5759 C  CZ    . TYR B 1 184 ? 78.221  64.545  96.147  1.00 94.69  ? 211 TYR B CZ    1 
ATOM   5760 O  OH    . TYR B 1 184 ? 77.631  65.687  95.655  1.00 102.69 ? 211 TYR B OH    1 
ATOM   5761 N  N     . LYS B 1 185 ? 82.325  62.813  96.261  1.00 81.78  ? 212 LYS B N     1 
ATOM   5762 C  CA    . LYS B 1 185 ? 83.120  64.033  96.219  1.00 82.20  ? 212 LYS B CA    1 
ATOM   5763 C  C     . LYS B 1 185 ? 82.315  65.122  95.529  1.00 90.01  ? 212 LYS B C     1 
ATOM   5764 O  O     . LYS B 1 185 ? 81.706  64.877  94.483  1.00 86.74  ? 212 LYS B O     1 
ATOM   5765 C  CB    . LYS B 1 185 ? 84.443  63.797  95.484  1.00 86.01  ? 212 LYS B CB    1 
ATOM   5766 C  CG    . LYS B 1 185 ? 85.379  64.991  95.454  1.00 94.58  ? 212 LYS B CG    1 
ATOM   5767 C  CD    . LYS B 1 185 ? 86.651  64.644  94.700  1.00 95.39  ? 212 LYS B CD    1 
ATOM   5768 C  CE    . LYS B 1 185 ? 87.606  65.820  94.644  1.00 103.23 ? 212 LYS B CE    1 
ATOM   5769 N  NZ    . LYS B 1 185 ? 88.848  65.476  93.899  1.00 103.69 ? 212 LYS B NZ    1 
ATOM   5770 N  N     . ARG B 1 186 ? 82.313  66.316  96.113  1.00 104.12 ? 213 ARG B N     1 
ATOM   5771 C  CA    . ARG B 1 186 ? 81.554  67.438  95.579  1.00 109.94 ? 213 ARG B CA    1 
ATOM   5772 C  C     . ARG B 1 186 ? 82.420  68.241  94.618  1.00 106.33 ? 213 ARG B C     1 
ATOM   5773 O  O     . ARG B 1 186 ? 83.547  68.618  94.953  1.00 110.28 ? 213 ARG B O     1 
ATOM   5774 C  CB    . ARG B 1 186 ? 81.046  68.330  96.712  1.00 116.48 ? 213 ARG B CB    1 
ATOM   5775 C  CG    . ARG B 1 186 ? 80.082  69.424  96.272  1.00 123.73 ? 213 ARG B CG    1 
ATOM   5776 C  CD    . ARG B 1 186 ? 78.955  69.581  97.281  1.00 127.41 ? 213 ARG B CD    1 
ATOM   5777 N  NE    . ARG B 1 186 ? 78.046  68.442  97.255  1.00 135.31 ? 213 ARG B NE    1 
ATOM   5778 C  CZ    . ARG B 1 186 ? 76.769  68.508  96.901  1.00 130.97 ? 213 ARG B CZ    1 
ATOM   5779 N  NH1   . ARG B 1 186 ? 76.200  69.659  96.580  1.00 115.63 ? 213 ARG B NH1   1 
ATOM   5780 N  NH2   . ARG B 1 186 ? 76.044  67.394  96.876  1.00 117.50 ? 213 ARG B NH2   1 
ATOM   5781 N  N     . THR B 1 187 ? 81.894  68.490  93.426  1.00 74.64  ? 214 THR B N     1 
ATOM   5782 C  CA    . THR B 1 187 ? 82.541  69.288  92.399  1.00 84.87  ? 214 THR B CA    1 
ATOM   5783 C  C     . THR B 1 187 ? 81.682  70.508  92.091  1.00 94.52  ? 214 THR B C     1 
ATOM   5784 O  O     . THR B 1 187 ? 80.486  70.528  92.405  1.00 76.59  ? 214 THR B O     1 
ATOM   5785 C  CB    . THR B 1 187 ? 82.757  68.470  91.116  1.00 93.05  ? 214 THR B CB    1 
ATOM   5786 O  OG1   . THR B 1 187 ? 81.529  68.405  90.382  1.00 93.42  ? 214 THR B OG1   1 
ATOM   5787 C  CG2   . THR B 1 187 ? 83.220  67.064  91.454  1.00 94.83  ? 214 THR B CG2   1 
ATOM   5788 N  N     . PRO B 1 188 ? 82.260  71.553  91.486  1.00 99.08  ? 215 PRO B N     1 
ATOM   5789 C  CA    . PRO B 1 188 ? 81.460  72.751  91.183  1.00 94.59  ? 215 PRO B CA    1 
ATOM   5790 C  C     . PRO B 1 188 ? 80.363  72.516  90.160  1.00 84.46  ? 215 PRO B C     1 
ATOM   5791 O  O     . PRO B 1 188 ? 79.449  73.344  90.064  1.00 94.91  ? 215 PRO B O     1 
ATOM   5792 C  CB    . PRO B 1 188 ? 82.502  73.751  90.657  1.00 91.43  ? 215 PRO B CB    1 
ATOM   5793 C  CG    . PRO B 1 188 ? 83.813  73.248  91.156  1.00 95.15  ? 215 PRO B CG    1 
ATOM   5794 C  CD    . PRO B 1 188 ? 83.687  71.758  91.182  1.00 98.24  ? 215 PRO B CD    1 
ATOM   5795 N  N     . ALA B 1 189 ? 80.419  71.425  89.397  1.00 66.67  ? 216 ALA B N     1 
ATOM   5796 C  CA    . ALA B 1 189 ? 79.431  71.176  88.356  1.00 74.63  ? 216 ALA B CA    1 
ATOM   5797 C  C     . ALA B 1 189 ? 78.173  70.487  88.869  1.00 78.08  ? 216 ALA B C     1 
ATOM   5798 O  O     . ALA B 1 189 ? 77.197  70.389  88.118  1.00 80.87  ? 216 ALA B O     1 
ATOM   5799 C  CB    . ALA B 1 189 ? 80.047  70.334  87.234  1.00 66.41  ? 216 ALA B CB    1 
ATOM   5800 N  N     . TYR B 1 190 ? 78.163  70.018  90.119  1.00 61.73  ? 217 TYR B N     1 
ATOM   5801 C  CA    . TYR B 1 190 ? 77.007  69.275  90.612  1.00 66.04  ? 217 TYR B CA    1 
ATOM   5802 C  C     . TYR B 1 190 ? 75.774  70.166  90.702  1.00 72.37  ? 217 TYR B C     1 
ATOM   5803 O  O     . TYR B 1 190 ? 74.711  69.826  90.168  1.00 76.59  ? 217 TYR B O     1 
ATOM   5804 C  CB    . TYR B 1 190 ? 77.310  68.649  91.974  1.00 67.22  ? 217 TYR B CB    1 
ATOM   5805 C  CG    . TYR B 1 190 ? 76.200  67.739  92.449  1.00 61.93  ? 217 TYR B CG    1 
ATOM   5806 C  CD1   . TYR B 1 190 ? 76.152  66.410  92.051  1.00 69.73  ? 217 TYR B CD1   1 
ATOM   5807 C  CD2   . TYR B 1 190 ? 75.190  68.211  93.276  1.00 62.53  ? 217 TYR B CD2   1 
ATOM   5808 C  CE1   . TYR B 1 190 ? 75.134  65.574  92.471  1.00 69.96  ? 217 TYR B CE1   1 
ATOM   5809 C  CE2   . TYR B 1 190 ? 74.168  67.383  93.701  1.00 65.07  ? 217 TYR B CE2   1 
ATOM   5810 C  CZ    . TYR B 1 190 ? 74.145  66.066  93.295  1.00 66.75  ? 217 TYR B CZ    1 
ATOM   5811 O  OH    . TYR B 1 190 ? 73.131  65.237  93.716  1.00 68.30  ? 217 TYR B OH    1 
ATOM   5812 N  N     . ILE B 1 191 ? 75.891  71.305  91.388  1.00 68.59  ? 218 ILE B N     1 
ATOM   5813 C  CA    . ILE B 1 191 ? 74.731  72.182  91.571  1.00 67.63  ? 218 ILE B CA    1 
ATOM   5814 C  C     . ILE B 1 191 ? 74.152  72.656  90.241  1.00 73.29  ? 218 ILE B C     1 
ATOM   5815 O  O     . ILE B 1 191 ? 72.921  72.624  90.084  1.00 68.08  ? 218 ILE B O     1 
ATOM   5816 C  CB    . ILE B 1 191 ? 75.089  73.345  92.511  1.00 69.09  ? 218 ILE B CB    1 
ATOM   5817 C  CG1   . ILE B 1 191 ? 75.695  72.816  93.813  1.00 73.47  ? 218 ILE B CG1   1 
ATOM   5818 C  CG2   . ILE B 1 191 ? 73.857  74.191  92.807  1.00 68.69  ? 218 ILE B CG2   1 
ATOM   5819 C  CD1   . ILE B 1 191 ? 74.743  71.975  94.636  1.00 69.19  ? 218 ILE B CD1   1 
ATOM   5820 N  N     . PRO B 1 192 ? 74.950  73.109  89.260  1.00 73.50  ? 219 PRO B N     1 
ATOM   5821 C  CA    . PRO B 1 192 ? 74.344  73.509  87.976  1.00 75.57  ? 219 PRO B CA    1 
ATOM   5822 C  C     . PRO B 1 192 ? 73.602  72.385  87.273  1.00 71.13  ? 219 PRO B C     1 
ATOM   5823 O  O     . PRO B 1 192 ? 72.544  72.629  86.678  1.00 69.32  ? 219 PRO B O     1 
ATOM   5824 C  CB    . PRO B 1 192 ? 75.551  73.995  87.161  1.00 73.91  ? 219 PRO B CB    1 
ATOM   5825 C  CG    . PRO B 1 192 ? 76.531  74.438  88.181  1.00 74.74  ? 219 PRO B CG    1 
ATOM   5826 C  CD    . PRO B 1 192 ? 76.380  73.467  89.311  1.00 67.91  ? 219 PRO B CD    1 
ATOM   5827 N  N     . ILE B 1 193 ? 74.126  71.158  87.317  1.00 67.15  ? 220 ILE B N     1 
ATOM   5828 C  CA    . ILE B 1 193 ? 73.409  70.029  86.731  1.00 67.26  ? 220 ILE B CA    1 
ATOM   5829 C  C     . ILE B 1 193 ? 72.165  69.705  87.549  1.00 64.61  ? 220 ILE B C     1 
ATOM   5830 O  O     . ILE B 1 193 ? 71.082  69.480  86.997  1.00 73.29  ? 220 ILE B O     1 
ATOM   5831 C  CB    . ILE B 1 193 ? 74.337  68.807  86.607  1.00 63.42  ? 220 ILE B CB    1 
ATOM   5832 C  CG1   . ILE B 1 193 ? 75.513  69.111  85.678  1.00 71.67  ? 220 ILE B CG1   1 
ATOM   5833 C  CG2   . ILE B 1 193 ? 73.565  67.598  86.106  1.00 52.47  ? 220 ILE B CG2   1 
ATOM   5834 C  CD1   . ILE B 1 193 ? 76.495  67.967  85.555  1.00 67.55  ? 220 ILE B CD1   1 
ATOM   5835 N  N     . ARG B 1 194 ? 72.301  69.683  88.877  1.00 67.09  ? 221 ARG B N     1 
ATOM   5836 C  CA    . ARG B 1 194 ? 71.174  69.360  89.746  1.00 68.76  ? 221 ARG B CA    1 
ATOM   5837 C  C     . ARG B 1 194 ? 70.036  70.365  89.602  1.00 64.41  ? 221 ARG B C     1 
ATOM   5838 O  O     . ARG B 1 194 ? 68.863  69.987  89.686  1.00 66.67  ? 221 ARG B O     1 
ATOM   5839 C  CB    . ARG B 1 194 ? 71.649  69.293  91.199  1.00 55.10  ? 221 ARG B CB    1 
ATOM   5840 C  CG    . ARG B 1 194 ? 70.553  69.041  92.217  1.00 64.22  ? 221 ARG B CG    1 
ATOM   5841 C  CD    . ARG B 1 194 ? 69.963  67.651  92.076  1.00 60.32  ? 221 ARG B CD    1 
ATOM   5842 N  NE    . ARG B 1 194 ? 68.862  67.449  93.008  1.00 53.63  ? 221 ARG B NE    1 
ATOM   5843 C  CZ    . ARG B 1 194 ? 67.597  67.742  92.742  1.00 63.08  ? 221 ARG B CZ    1 
ATOM   5844 N  NH1   . ARG B 1 194 ? 67.231  68.225  91.566  1.00 63.43  ? 221 ARG B NH1   1 
ATOM   5845 N  NH2   . ARG B 1 194 ? 66.675  67.545  93.680  1.00 56.10  ? 221 ARG B NH2   1 
ATOM   5846 N  N     . LYS B 1 195 ? 70.357  71.637  89.373  1.00 62.99  ? 222 LYS B N     1 
ATOM   5847 C  CA    . LYS B 1 195 ? 69.354  72.685  89.229  1.00 69.22  ? 222 LYS B CA    1 
ATOM   5848 C  C     . LYS B 1 195 ? 68.860  72.853  87.799  1.00 60.87  ? 222 LYS B C     1 
ATOM   5849 O  O     . LYS B 1 195 ? 68.003  73.710  87.557  1.00 75.13  ? 222 LYS B O     1 
ATOM   5850 C  CB    . LYS B 1 195 ? 69.909  74.026  89.721  1.00 79.28  ? 222 LYS B CB    1 
ATOM   5851 C  CG    . LYS B 1 195 ? 69.932  74.197  91.227  1.00 78.54  ? 222 LYS B CG    1 
ATOM   5852 C  CD    . LYS B 1 195 ? 70.356  75.610  91.595  1.00 91.79  ? 222 LYS B CD    1 
ATOM   5853 C  CE    . LYS B 1 195 ? 70.316  75.832  93.096  1.00 96.18  ? 222 LYS B CE    1 
ATOM   5854 N  NZ    . LYS B 1 195 ? 70.780  77.200  93.455  1.00 111.47 ? 222 LYS B NZ    1 
ATOM   5855 N  N     . ARG B 1 196 ? 69.381  72.068  86.854  1.00 65.00  ? 223 ARG B N     1 
ATOM   5856 C  CA    . ARG B 1 196 ? 69.072  72.214  85.430  1.00 69.17  ? 223 ARG B CA    1 
ATOM   5857 C  C     . ARG B 1 196 ? 69.445  73.599  84.906  1.00 76.10  ? 223 ARG B C     1 
ATOM   5858 O  O     . ARG B 1 196 ? 68.825  74.107  83.967  1.00 80.01  ? 223 ARG B O     1 
ATOM   5859 C  CB    . ARG B 1 196 ? 67.601  71.907  85.132  1.00 61.23  ? 223 ARG B CB    1 
ATOM   5860 C  CG    . ARG B 1 196 ? 67.223  70.447  85.310  1.00 56.24  ? 223 ARG B CG    1 
ATOM   5861 C  CD    . ARG B 1 196 ? 65.789  70.187  84.879  1.00 58.40  ? 223 ARG B CD    1 
ATOM   5862 N  NE    . ARG B 1 196 ? 65.394  68.805  85.126  1.00 82.69  ? 223 ARG B NE    1 
ATOM   5863 C  CZ    . ARG B 1 196 ? 64.685  68.402  86.172  1.00 77.56  ? 223 ARG B CZ    1 
ATOM   5864 N  NH1   . ARG B 1 196 ? 64.247  69.257  87.082  1.00 76.41  ? 223 ARG B NH1   1 
ATOM   5865 N  NH2   . ARG B 1 196 ? 64.407  67.108  86.307  1.00 78.98  ? 223 ARG B NH2   1 
ATOM   5866 N  N     . ASP B 1 197 ? 70.456  74.227  85.512  1.00 71.02  ? 224 ASP B N     1 
ATOM   5867 C  CA    . ASP B 1 197 ? 71.029  75.430  84.919  1.00 64.11  ? 224 ASP B CA    1 
ATOM   5868 C  C     . ASP B 1 197 ? 71.851  75.079  83.686  1.00 75.30  ? 224 ASP B C     1 
ATOM   5869 O  O     . ASP B 1 197 ? 71.895  75.847  82.717  1.00 83.12  ? 224 ASP B O     1 
ATOM   5870 C  CB    . ASP B 1 197 ? 71.879  76.174  85.949  1.00 80.25  ? 224 ASP B CB    1 
ATOM   5871 C  CG    . ASP B 1 197 ? 71.040  76.891  86.991  1.00 90.09  ? 224 ASP B CG    1 
ATOM   5872 O  OD1   . ASP B 1 197 ? 69.800  76.926  86.836  1.00 90.33  ? 224 ASP B OD1   1 
ATOM   5873 O  OD2   . ASP B 1 197 ? 71.619  77.420  87.964  1.00 73.80  ? 224 ASP B OD2   1 
ATOM   5874 N  N     . ARG B 1 198 ? 72.513  73.925  83.713  1.00 72.44  ? 225 ARG B N     1 
ATOM   5875 C  CA    . ARG B 1 198 ? 73.142  73.321  82.547  1.00 63.27  ? 225 ARG B CA    1 
ATOM   5876 C  C     . ARG B 1 198 ? 72.342  72.078  82.181  1.00 67.00  ? 225 ARG B C     1 
ATOM   5877 O  O     . ARG B 1 198 ? 72.194  71.169  83.006  1.00 76.07  ? 225 ARG B O     1 
ATOM   5878 C  CB    . ARG B 1 198 ? 74.599  72.952  82.826  1.00 57.26  ? 225 ARG B CB    1 
ATOM   5879 C  CG    . ARG B 1 198 ? 75.527  74.123  83.093  1.00 79.87  ? 225 ARG B CG    1 
ATOM   5880 C  CD    . ARG B 1 198 ? 76.848  73.633  83.674  1.00 107.25 ? 225 ARG B CD    1 
ATOM   5881 N  NE    . ARG B 1 198 ? 77.486  72.626  82.833  1.00 106.93 ? 225 ARG B NE    1 
ATOM   5882 C  CZ    . ARG B 1 198 ? 78.553  71.921  83.185  1.00 96.28  ? 225 ARG B CZ    1 
ATOM   5883 N  NH1   . ARG B 1 198 ? 79.125  72.077  84.368  1.00 91.28  ? 225 ARG B NH1   1 
ATOM   5884 N  NH2   . ARG B 1 198 ? 79.058  71.036  82.329  1.00 80.03  ? 225 ARG B NH2   1 
ATOM   5885 N  N     . ARG B 1 199 ? 71.823  72.043  80.958  1.00 51.62  ? 226 ARG B N     1 
ATOM   5886 C  CA    . ARG B 1 199 ? 71.069  70.902  80.466  1.00 63.97  ? 226 ARG B CA    1 
ATOM   5887 C  C     . ARG B 1 199 ? 71.906  70.112  79.469  1.00 62.19  ? 226 ARG B C     1 
ATOM   5888 O  O     . ARG B 1 199 ? 72.779  70.662  78.791  1.00 59.12  ? 226 ARG B O     1 
ATOM   5889 C  CB    . ARG B 1 199 ? 69.752  71.346  79.820  1.00 66.89  ? 226 ARG B CB    1 
ATOM   5890 C  CG    . ARG B 1 199 ? 68.758  71.951  80.804  1.00 59.98  ? 226 ARG B CG    1 
ATOM   5891 C  CD    . ARG B 1 199 ? 67.431  72.295  80.138  1.00 81.01  ? 226 ARG B CD    1 
ATOM   5892 N  NE    . ARG B 1 199 ? 66.477  72.853  81.090  1.00 106.75 ? 226 ARG B NE    1 
ATOM   5893 C  CZ    . ARG B 1 199 ? 65.541  72.151  81.716  1.00 116.51 ? 226 ARG B CZ    1 
ATOM   5894 N  NH1   . ARG B 1 199 ? 65.399  70.850  81.513  1.00 107.62 ? 226 ARG B NH1   1 
ATOM   5895 N  NH2   . ARG B 1 199 ? 64.724  72.769  82.564  1.00 106.24 ? 226 ARG B NH2   1 
ATOM   5896 N  N     . GLY B 1 200 ? 71.635  68.816  79.388  1.00 63.69  ? 227 GLY B N     1 
ATOM   5897 C  CA    . GLY B 1 200 ? 72.335  67.925  78.493  1.00 61.33  ? 227 GLY B CA    1 
ATOM   5898 C  C     . GLY B 1 200 ? 72.621  66.607  79.175  1.00 60.40  ? 227 GLY B C     1 
ATOM   5899 O  O     . GLY B 1 200 ? 72.054  66.286  80.217  1.00 59.75  ? 227 GLY B O     1 
ATOM   5900 N  N     . CYS B 1 201 ? 73.513  65.831  78.566  1.00 60.45  ? 228 CYS B N     1 
ATOM   5901 C  CA    . CYS B 1 201 ? 73.962  64.553  79.106  1.00 58.82  ? 228 CYS B CA    1 
ATOM   5902 C  C     . CYS B 1 201 ? 75.433  64.671  79.475  1.00 51.77  ? 228 CYS B C     1 
ATOM   5903 O  O     . CYS B 1 201 ? 76.275  64.913  78.604  1.00 64.42  ? 228 CYS B O     1 
ATOM   5904 C  CB    . CYS B 1 201 ? 73.751  63.424  78.100  1.00 47.28  ? 228 CYS B CB    1 
ATOM   5905 S  SG    . CYS B 1 201 ? 72.028  63.109  77.692  1.00 101.49 ? 228 CYS B SG    1 
ATOM   5906 N  N     . PHE B 1 202 ? 75.739  64.490  80.755  1.00 55.70  ? 229 PHE B N     1 
ATOM   5907 C  CA    . PHE B 1 202 ? 77.060  64.773  81.292  1.00 65.00  ? 229 PHE B CA    1 
ATOM   5908 C  C     . PHE B 1 202 ? 77.761  63.489  81.708  1.00 59.60  ? 229 PHE B C     1 
ATOM   5909 O  O     . PHE B 1 202 ? 77.148  62.594  82.301  1.00 60.07  ? 229 PHE B O     1 
ATOM   5910 C  CB    . PHE B 1 202 ? 76.967  65.725  82.486  1.00 53.56  ? 229 PHE B CB    1 
ATOM   5911 C  CG    . PHE B 1 202 ? 76.211  66.987  82.189  1.00 57.26  ? 229 PHE B CG    1 
ATOM   5912 C  CD1   . PHE B 1 202 ? 76.859  68.084  81.652  1.00 60.35  ? 229 PHE B CD1   1 
ATOM   5913 C  CD2   . PHE B 1 202 ? 74.851  67.073  82.437  1.00 60.00  ? 229 PHE B CD2   1 
ATOM   5914 C  CE1   . PHE B 1 202 ? 76.168  69.246  81.372  1.00 67.22  ? 229 PHE B CE1   1 
ATOM   5915 C  CE2   . PHE B 1 202 ? 74.152  68.231  82.159  1.00 65.86  ? 229 PHE B CE2   1 
ATOM   5916 C  CZ    . PHE B 1 202 ? 74.812  69.319  81.626  1.00 69.52  ? 229 PHE B CZ    1 
ATOM   5917 N  N     . ALA B 1 203 ? 79.051  63.407  81.390  1.00 67.50  ? 230 ALA B N     1 
ATOM   5918 C  CA    . ALA B 1 203 ? 79.870  62.287  81.833  1.00 65.57  ? 230 ALA B CA    1 
ATOM   5919 C  C     . ALA B 1 203 ? 80.119  62.407  83.329  1.00 62.42  ? 230 ALA B C     1 
ATOM   5920 O  O     . ALA B 1 203 ? 80.602  63.439  83.804  1.00 61.28  ? 230 ALA B O     1 
ATOM   5921 C  CB    . ALA B 1 203 ? 81.189  62.253  81.065  1.00 53.77  ? 230 ALA B CB    1 
ATOM   5922 N  N     . VAL B 1 204 ? 79.777  61.360  84.074  1.00 59.42  ? 231 VAL B N     1 
ATOM   5923 C  CA    . VAL B 1 204 ? 79.906  61.378  85.529  1.00 56.08  ? 231 VAL B CA    1 
ATOM   5924 C  C     . VAL B 1 204 ? 80.492  60.061  85.994  1.00 57.88  ? 231 VAL B C     1 
ATOM   5925 O  O     . VAL B 1 204 ? 80.351  59.019  85.335  1.00 56.62  ? 231 VAL B O     1 
ATOM   5926 C  CB    . VAL B 1 204 ? 78.546  61.619  86.219  1.00 54.61  ? 231 VAL B CB    1 
ATOM   5927 C  CG1   . VAL B 1 204 ? 78.123  63.066  86.063  1.00 50.59  ? 231 VAL B CG1   1 
ATOM   5928 C  CG2   . VAL B 1 204 ? 77.504  60.684  85.641  1.00 49.95  ? 231 VAL B CG2   1 
ATOM   5929 N  N     . PRO B 1 205 ? 81.165  60.078  87.150  1.00 57.21  ? 232 PRO B N     1 
ATOM   5930 C  CA    . PRO B 1 205 ? 81.760  58.842  87.671  1.00 57.14  ? 232 PRO B CA    1 
ATOM   5931 C  C     . PRO B 1 205 ? 80.775  57.921  88.371  1.00 54.46  ? 232 PRO B C     1 
ATOM   5932 O  O     . PRO B 1 205 ? 81.165  56.808  88.749  1.00 59.21  ? 232 PRO B O     1 
ATOM   5933 C  CB    . PRO B 1 205 ? 82.815  59.360  88.651  1.00 57.53  ? 232 PRO B CB    1 
ATOM   5934 C  CG    . PRO B 1 205 ? 82.235  60.638  89.148  1.00 65.42  ? 232 PRO B CG    1 
ATOM   5935 C  CD    . PRO B 1 205 ? 81.529  61.255  87.970  1.00 62.03  ? 232 PRO B CD    1 
ATOM   5936 N  N     . MET B 1 206 ? 79.521  58.334  88.557  1.00 53.63  ? 233 MET B N     1 
ATOM   5937 C  CA    . MET B 1 206 ? 78.573  57.528  89.315  1.00 50.48  ? 233 MET B CA    1 
ATOM   5938 C  C     . MET B 1 206 ? 77.145  57.899  88.942  1.00 64.99  ? 233 MET B C     1 
ATOM   5939 O  O     . MET B 1 206 ? 76.765  59.070  89.019  1.00 63.12  ? 233 MET B O     1 
ATOM   5940 C  CB    . MET B 1 206 ? 78.777  57.714  90.822  1.00 57.57  ? 233 MET B CB    1 
ATOM   5941 C  CG    . MET B 1 206 ? 77.669  57.106  91.674  1.00 63.46  ? 233 MET B CG    1 
ATOM   5942 S  SD    . MET B 1 206 ? 77.711  55.307  91.682  1.00 62.16  ? 233 MET B SD    1 
ATOM   5943 C  CE    . MET B 1 206 ? 79.209  55.017  92.621  1.00 60.34  ? 233 MET B CE    1 
ATOM   5944 N  N     . VAL B 1 207 ? 76.365  56.895  88.543  1.00 55.45  ? 234 VAL B N     1 
ATOM   5945 C  CA    . VAL B 1 207 ? 74.913  56.986  88.453  1.00 57.04  ? 234 VAL B CA    1 
ATOM   5946 C  C     . VAL B 1 207 ? 74.336  55.714  89.054  1.00 56.27  ? 234 VAL B C     1 
ATOM   5947 O  O     . VAL B 1 207 ? 74.957  54.649  89.004  1.00 53.03  ? 234 VAL B O     1 
ATOM   5948 C  CB    . VAL B 1 207 ? 74.412  57.177  87.007  1.00 46.58  ? 234 VAL B CB    1 
ATOM   5949 C  CG1   . VAL B 1 207 ? 74.761  58.560  86.502  1.00 47.39  ? 234 VAL B CG1   1 
ATOM   5950 C  CG2   . VAL B 1 207 ? 74.991  56.111  86.107  1.00 50.41  ? 234 VAL B CG2   1 
ATOM   5951 N  N     . HIS B 1 208 ? 73.145  55.828  89.630  1.00 55.62  ? 235 HIS B N     1 
ATOM   5952 C  CA    . HIS B 1 208 ? 72.538  54.700  90.323  1.00 50.27  ? 235 HIS B CA    1 
ATOM   5953 C  C     . HIS B 1 208 ? 71.022  54.860  90.302  1.00 44.14  ? 235 HIS B C     1 
ATOM   5954 O  O     . HIS B 1 208 ? 70.478  55.693  89.571  1.00 49.39  ? 235 HIS B O     1 
ATOM   5955 C  CB    . HIS B 1 208 ? 73.094  54.589  91.747  1.00 45.39  ? 235 HIS B CB    1 
ATOM   5956 C  CG    . HIS B 1 208 ? 72.859  55.807  92.584  1.00 50.75  ? 235 HIS B CG    1 
ATOM   5957 N  ND1   . HIS B 1 208 ? 71.698  56.006  93.301  1.00 50.37  ? 235 HIS B ND1   1 
ATOM   5958 C  CD2   . HIS B 1 208 ? 73.639  56.889  92.822  1.00 41.91  ? 235 HIS B CD2   1 
ATOM   5959 C  CE1   . HIS B 1 208 ? 71.774  57.156  93.946  1.00 57.45  ? 235 HIS B CE1   1 
ATOM   5960 N  NE2   . HIS B 1 208 ? 72.941  57.712  93.671  1.00 40.93  ? 235 HIS B NE2   1 
ATOM   5961 N  N     . SER B 1 209 ? 70.345  54.040  91.108  1.00 49.50  ? 236 SER B N     1 
ATOM   5962 C  CA    . SER B 1 209 ? 68.892  54.043  91.266  1.00 54.20  ? 236 SER B CA    1 
ATOM   5963 C  C     . SER B 1 209 ? 68.183  53.621  89.985  1.00 47.81  ? 236 SER B C     1 
ATOM   5964 O  O     . SER B 1 209 ? 67.841  52.446  89.822  1.00 59.71  ? 236 SER B O     1 
ATOM   5965 C  CB    . SER B 1 209 ? 68.396  55.419  91.724  1.00 46.85  ? 236 SER B CB    1 
ATOM   5966 O  OG    . SER B 1 209 ? 68.983  55.774  92.963  1.00 64.55  ? 236 SER B OG    1 
ATOM   5967 N  N     . THR B 1 210 ? 67.949  54.561  89.076  1.00 53.54  ? 237 THR B N     1 
ATOM   5968 C  CA    . THR B 1 210 ? 67.336  54.273  87.786  1.00 44.79  ? 237 THR B CA    1 
ATOM   5969 C  C     . THR B 1 210 ? 68.340  54.587  86.687  1.00 51.38  ? 237 THR B C     1 
ATOM   5970 O  O     . THR B 1 210 ? 68.773  55.735  86.551  1.00 50.92  ? 237 THR B O     1 
ATOM   5971 C  CB    . THR B 1 210 ? 66.054  55.078  87.585  1.00 49.67  ? 237 THR B CB    1 
ATOM   5972 O  OG1   . THR B 1 210 ? 65.061  54.632  88.514  1.00 53.94  ? 237 THR B OG1   1 
ATOM   5973 C  CG2   . THR B 1 210 ? 65.533  54.887  86.169  1.00 47.80  ? 237 THR B CG2   1 
ATOM   5974 N  N     . PHE B 1 211 ? 68.714  53.570  85.914  1.00 49.15  ? 238 PHE B N     1 
ATOM   5975 C  CA    . PHE B 1 211 ? 69.660  53.758  84.823  1.00 48.32  ? 238 PHE B CA    1 
ATOM   5976 C  C     . PHE B 1 211 ? 69.390  52.731  83.732  1.00 49.36  ? 238 PHE B C     1 
ATOM   5977 O  O     . PHE B 1 211 ? 68.731  51.711  83.954  1.00 40.18  ? 238 PHE B O     1 
ATOM   5978 C  CB    . PHE B 1 211 ? 71.117  53.672  85.309  1.00 41.41  ? 238 PHE B CB    1 
ATOM   5979 C  CG    . PHE B 1 211 ? 71.442  52.414  86.070  1.00 57.45  ? 238 PHE B CG    1 
ATOM   5980 C  CD1   . PHE B 1 211 ? 71.182  52.321  87.428  1.00 53.32  ? 238 PHE B CD1   1 
ATOM   5981 C  CD2   . PHE B 1 211 ? 72.031  51.334  85.432  1.00 49.46  ? 238 PHE B CD2   1 
ATOM   5982 C  CE1   . PHE B 1 211 ? 71.486  51.171  88.131  1.00 60.29  ? 238 PHE B CE1   1 
ATOM   5983 C  CE2   . PHE B 1 211 ? 72.340  50.181  86.130  1.00 56.93  ? 238 PHE B CE2   1 
ATOM   5984 C  CZ    . PHE B 1 211 ? 72.066  50.099  87.481  1.00 62.54  ? 238 PHE B CZ    1 
ATOM   5985 N  N     . LEU B 1 212 ? 69.913  53.017  82.542  1.00 44.39  ? 239 LEU B N     1 
ATOM   5986 C  CA    . LEU B 1 212 ? 69.668  52.219  81.346  1.00 41.94  ? 239 LEU B CA    1 
ATOM   5987 C  C     . LEU B 1 212 ? 70.996  51.724  80.788  1.00 42.39  ? 239 LEU B C     1 
ATOM   5988 O  O     . LEU B 1 212 ? 71.898  52.525  80.520  1.00 46.69  ? 239 LEU B O     1 
ATOM   5989 C  CB    . LEU B 1 212 ? 68.923  53.036  80.290  1.00 44.89  ? 239 LEU B CB    1 
ATOM   5990 C  CG    . LEU B 1 212 ? 68.648  52.336  78.959  1.00 42.42  ? 239 LEU B CG    1 
ATOM   5991 C  CD1   . LEU B 1 212 ? 67.424  51.442  79.071  1.00 43.63  ? 239 LEU B CD1   1 
ATOM   5992 C  CD2   . LEU B 1 212 ? 68.485  53.346  77.838  1.00 38.26  ? 239 LEU B CD2   1 
ATOM   5993 N  N     . ILE B 1 213 ? 71.111  50.410  80.610  1.00 35.73  ? 240 ILE B N     1 
ATOM   5994 C  CA    . ILE B 1 213 ? 72.297  49.786  80.033  1.00 38.62  ? 240 ILE B CA    1 
ATOM   5995 C  C     . ILE B 1 213 ? 71.968  49.359  78.611  1.00 49.36  ? 240 ILE B C     1 
ATOM   5996 O  O     . ILE B 1 213 ? 70.927  48.738  78.367  1.00 43.95  ? 240 ILE B O     1 
ATOM   5997 C  CB    . ILE B 1 213 ? 72.780  48.587  80.869  1.00 44.73  ? 240 ILE B CB    1 
ATOM   5998 C  CG1   . ILE B 1 213 ? 72.995  48.996  82.329  1.00 32.69  ? 240 ILE B CG1   1 
ATOM   5999 C  CG2   . ILE B 1 213 ? 74.059  48.009  80.279  1.00 32.57  ? 240 ILE B CG2   1 
ATOM   6000 C  CD1   . ILE B 1 213 ? 73.562  47.883  83.205  1.00 43.17  ? 240 ILE B CD1   1 
ATOM   6001 N  N     . ASP B 1 214 ? 72.856  49.691  77.677  1.00 49.42  ? 241 ASP B N     1 
ATOM   6002 C  CA    . ASP B 1 214 ? 72.686  49.345  76.268  1.00 50.77  ? 241 ASP B CA    1 
ATOM   6003 C  C     . ASP B 1 214 ? 73.409  48.029  76.010  1.00 47.55  ? 241 ASP B C     1 
ATOM   6004 O  O     . ASP B 1 214 ? 74.632  47.995  75.847  1.00 49.76  ? 241 ASP B O     1 
ATOM   6005 C  CB    . ASP B 1 214 ? 73.215  50.462  75.374  1.00 52.99  ? 241 ASP B CB    1 
ATOM   6006 C  CG    . ASP B 1 214 ? 72.899  50.238  73.907  1.00 58.91  ? 241 ASP B CG    1 
ATOM   6007 O  OD1   . ASP B 1 214 ? 72.333  49.178  73.566  1.00 59.84  ? 241 ASP B OD1   1 
ATOM   6008 O  OD2   . ASP B 1 214 ? 73.212  51.129  73.092  1.00 61.14  ? 241 ASP B OD2   1 
ATOM   6009 N  N     . LEU B 1 215 ? 72.646  46.940  75.961  1.00 40.17  ? 242 LEU B N     1 
ATOM   6010 C  CA    . LEU B 1 215 ? 73.206  45.620  75.715  1.00 45.02  ? 242 LEU B CA    1 
ATOM   6011 C  C     . LEU B 1 215 ? 73.528  45.376  74.248  1.00 47.49  ? 242 LEU B C     1 
ATOM   6012 O  O     . LEU B 1 215 ? 74.016  44.292  73.913  1.00 52.97  ? 242 LEU B O     1 
ATOM   6013 C  CB    . LEU B 1 215 ? 72.245  44.546  76.225  1.00 41.04  ? 242 LEU B CB    1 
ATOM   6014 C  CG    . LEU B 1 215 ? 71.902  44.689  77.709  1.00 43.57  ? 242 LEU B CG    1 
ATOM   6015 C  CD1   . LEU B 1 215 ? 70.888  43.645  78.114  1.00 39.85  ? 242 LEU B CD1   1 
ATOM   6016 C  CD2   . LEU B 1 215 ? 73.160  44.581  78.557  1.00 42.34  ? 242 LEU B CD2   1 
ATOM   6017 N  N     . ARG B 1 216 ? 73.261  46.343  73.370  1.00 50.57  ? 243 ARG B N     1 
ATOM   6018 C  CA    . ARG B 1 216 ? 73.750  46.254  72.001  1.00 38.23  ? 243 ARG B CA    1 
ATOM   6019 C  C     . ARG B 1 216 ? 75.236  46.568  71.921  1.00 51.94  ? 243 ARG B C     1 
ATOM   6020 O  O     . ARG B 1 216 ? 75.942  46.004  71.077  1.00 49.36  ? 243 ARG B O     1 
ATOM   6021 C  CB    . ARG B 1 216 ? 72.972  47.208  71.093  1.00 41.18  ? 243 ARG B CB    1 
ATOM   6022 C  CG    . ARG B 1 216 ? 71.465  47.040  71.155  1.00 44.09  ? 243 ARG B CG    1 
ATOM   6023 C  CD    . ARG B 1 216 ? 70.743  48.155  70.408  1.00 42.55  ? 243 ARG B CD    1 
ATOM   6024 N  NE    . ARG B 1 216 ? 71.204  49.480  70.810  1.00 46.01  ? 243 ARG B NE    1 
ATOM   6025 C  CZ    . ARG B 1 216 ? 71.725  50.376  69.983  1.00 59.12  ? 243 ARG B CZ    1 
ATOM   6026 N  NH1   . ARG B 1 216 ? 71.826  50.142  68.686  1.00 56.18  ? 243 ARG B NH1   1 
ATOM   6027 N  NH2   . ARG B 1 216 ? 72.148  51.539  70.471  1.00 39.02  ? 243 ARG B NH2   1 
ATOM   6028 N  N     . LYS B 1 217 ? 75.722  47.453  72.788  1.00 48.97  ? 244 LYS B N     1 
ATOM   6029 C  CA    . LYS B 1 217 ? 77.118  47.857  72.750  1.00 42.27  ? 244 LYS B CA    1 
ATOM   6030 C  C     . LYS B 1 217 ? 78.025  46.692  73.127  1.00 44.96  ? 244 LYS B C     1 
ATOM   6031 O  O     . LYS B 1 217 ? 77.706  45.896  74.015  1.00 55.02  ? 244 LYS B O     1 
ATOM   6032 C  CB    . LYS B 1 217 ? 77.352  49.036  73.693  1.00 52.26  ? 244 LYS B CB    1 
ATOM   6033 C  CG    . LYS B 1 217 ? 76.541  50.282  73.362  1.00 52.82  ? 244 LYS B CG    1 
ATOM   6034 C  CD    . LYS B 1 217 ? 76.705  50.686  71.905  1.00 48.40  ? 244 LYS B CD    1 
ATOM   6035 C  CE    . LYS B 1 217 ? 76.616  52.193  71.736  1.00 57.07  ? 244 LYS B CE    1 
ATOM   6036 N  NZ    . LYS B 1 217 ? 75.382  52.756  72.345  1.00 52.03  ? 244 LYS B NZ    1 
ATOM   6037 N  N     . ALA B 1 218 ? 79.166  46.597  72.440  1.00 52.38  ? 245 ALA B N     1 
ATOM   6038 C  CA    . ALA B 1 218 ? 80.101  45.507  72.698  1.00 43.90  ? 245 ALA B CA    1 
ATOM   6039 C  C     . ALA B 1 218 ? 80.697  45.602  74.097  1.00 43.89  ? 245 ALA B C     1 
ATOM   6040 O  O     . ALA B 1 218 ? 80.935  44.578  74.747  1.00 55.96  ? 245 ALA B O     1 
ATOM   6041 C  CB    . ALA B 1 218 ? 81.209  45.509  71.646  1.00 37.22  ? 245 ALA B CB    1 
ATOM   6042 N  N     . ALA B 1 219 ? 80.941  46.822  74.581  1.00 45.58  ? 246 ALA B N     1 
ATOM   6043 C  CA    . ALA B 1 219 ? 81.546  46.994  75.895  1.00 50.31  ? 246 ALA B CA    1 
ATOM   6044 C  C     . ALA B 1 219 ? 80.612  46.587  77.027  1.00 53.07  ? 246 ALA B C     1 
ATOM   6045 O  O     . ALA B 1 219 ? 81.087  46.335  78.138  1.00 46.58  ? 246 ALA B O     1 
ATOM   6046 C  CB    . ALA B 1 219 ? 81.995  48.445  76.083  1.00 42.80  ? 246 ALA B CB    1 
ATOM   6047 N  N     . SER B 1 220 ? 79.302  46.513  76.775  1.00 48.21  ? 247 SER B N     1 
ATOM   6048 C  CA    . SER B 1 220 ? 78.368  46.087  77.810  1.00 48.13  ? 247 SER B CA    1 
ATOM   6049 C  C     . SER B 1 220 ? 78.584  44.641  78.234  1.00 54.19  ? 247 SER B C     1 
ATOM   6050 O  O     . SER B 1 220 ? 78.211  44.278  79.354  1.00 48.38  ? 247 SER B O     1 
ATOM   6051 C  CB    . SER B 1 220 ? 76.930  46.269  77.326  1.00 44.02  ? 247 SER B CB    1 
ATOM   6052 O  OG    . SER B 1 220 ? 76.641  45.405  76.244  1.00 47.16  ? 247 SER B OG    1 
ATOM   6053 N  N     . ARG B 1 221 ? 79.185  43.813  77.376  1.00 47.12  ? 248 ARG B N     1 
ATOM   6054 C  CA    . ARG B 1 221 ? 79.451  42.426  77.742  1.00 52.19  ? 248 ARG B CA    1 
ATOM   6055 C  C     . ARG B 1 221 ? 80.400  42.314  78.926  1.00 51.85  ? 248 ARG B C     1 
ATOM   6056 O  O     . ARG B 1 221 ? 80.415  41.277  79.597  1.00 48.03  ? 248 ARG B O     1 
ATOM   6057 C  CB    . ARG B 1 221 ? 80.029  41.661  76.548  1.00 47.76  ? 248 ARG B CB    1 
ATOM   6058 C  CG    . ARG B 1 221 ? 79.149  41.673  75.311  1.00 51.62  ? 248 ARG B CG    1 
ATOM   6059 C  CD    . ARG B 1 221 ? 79.707  40.777  74.214  1.00 54.55  ? 248 ARG B CD    1 
ATOM   6060 N  NE    . ARG B 1 221 ? 79.716  39.373  74.607  1.00 73.71  ? 248 ARG B NE    1 
ATOM   6061 C  CZ    . ARG B 1 221 ? 78.690  38.545  74.457  1.00 79.46  ? 248 ARG B CZ    1 
ATOM   6062 N  NH1   . ARG B 1 221 ? 77.546  38.948  73.924  1.00 57.12  ? 248 ARG B NH1   1 
ATOM   6063 N  NH2   . ARG B 1 221 ? 78.812  37.282  74.857  1.00 66.74  ? 248 ARG B NH2   1 
ATOM   6064 N  N     . ASN B 1 222 ? 81.188  43.353  79.199  1.00 49.37  ? 249 ASN B N     1 
ATOM   6065 C  CA    . ASN B 1 222 ? 82.161  43.331  80.282  1.00 41.82  ? 249 ASN B CA    1 
ATOM   6066 C  C     . ASN B 1 222 ? 81.637  43.937  81.577  1.00 47.72  ? 249 ASN B C     1 
ATOM   6067 O  O     . ASN B 1 222 ? 82.339  43.886  82.593  1.00 46.01  ? 249 ASN B O     1 
ATOM   6068 C  CB    . ASN B 1 222 ? 83.436  44.067  79.856  1.00 52.39  ? 249 ASN B CB    1 
ATOM   6069 C  CG    . ASN B 1 222 ? 84.118  43.410  78.674  1.00 57.70  ? 249 ASN B CG    1 
ATOM   6070 O  OD1   . ASN B 1 222 ? 84.213  42.184  78.601  1.00 55.74  ? 249 ASN B OD1   1 
ATOM   6071 N  ND2   . ASN B 1 222 ? 84.595  44.222  77.739  1.00 60.44  ? 249 ASN B ND2   1 
ATOM   6072 N  N     . LEU B 1 223 ? 80.439  44.512  81.566  1.00 44.67  ? 250 LEU B N     1 
ATOM   6073 C  CA    . LEU B 1 223 ? 79.855  45.049  82.786  1.00 50.57  ? 250 LEU B CA    1 
ATOM   6074 C  C     . LEU B 1 223 ? 79.364  43.917  83.680  1.00 47.42  ? 250 LEU B C     1 
ATOM   6075 O  O     . LEU B 1 223 ? 78.891  42.881  83.207  1.00 43.38  ? 250 LEU B O     1 
ATOM   6076 C  CB    . LEU B 1 223 ? 78.700  45.992  82.454  1.00 41.66  ? 250 LEU B CB    1 
ATOM   6077 C  CG    . LEU B 1 223 ? 79.024  47.146  81.505  1.00 54.75  ? 250 LEU B CG    1 
ATOM   6078 C  CD1   . LEU B 1 223 ? 77.757  47.887  81.109  1.00 41.82  ? 250 LEU B CD1   1 
ATOM   6079 C  CD2   . LEU B 1 223 ? 80.020  48.093  82.150  1.00 46.42  ? 250 LEU B CD2   1 
ATOM   6080 N  N     . ALA B 1 224 ? 79.480  44.123  84.989  1.00 41.11  ? 251 ALA B N     1 
ATOM   6081 C  CA    . ALA B 1 224 ? 79.055  43.118  85.953  1.00 42.75  ? 251 ALA B CA    1 
ATOM   6082 C  C     . ALA B 1 224 ? 78.707  43.793  87.269  1.00 44.82  ? 251 ALA B C     1 
ATOM   6083 O  O     . ALA B 1 224 ? 79.466  44.635  87.760  1.00 50.76  ? 251 ALA B O     1 
ATOM   6084 C  CB    . ALA B 1 224 ? 80.145  42.065  86.174  1.00 38.01  ? 251 ALA B CB    1 
ATOM   6085 N  N     . PHE B 1 225 ? 77.554  43.428  87.830  1.00 44.85  ? 252 PHE B N     1 
ATOM   6086 C  CA    . PHE B 1 225 ? 77.207  43.879  89.171  1.00 37.63  ? 252 PHE B CA    1 
ATOM   6087 C  C     . PHE B 1 225 ? 77.856  43.015  90.241  1.00 41.41  ? 252 PHE B C     1 
ATOM   6088 O  O     . PHE B 1 225 ? 78.078  43.486  91.362  1.00 51.89  ? 252 PHE B O     1 
ATOM   6089 C  CB    . PHE B 1 225 ? 75.689  43.876  89.360  1.00 41.27  ? 252 PHE B CB    1 
ATOM   6090 C  CG    . PHE B 1 225 ? 74.965  44.852  88.481  1.00 54.75  ? 252 PHE B CG    1 
ATOM   6091 C  CD1   . PHE B 1 225 ? 74.747  46.151  88.903  1.00 41.12  ? 252 PHE B CD1   1 
ATOM   6092 C  CD2   . PHE B 1 225 ? 74.497  44.468  87.236  1.00 41.76  ? 252 PHE B CD2   1 
ATOM   6093 C  CE1   . PHE B 1 225 ? 74.079  47.051  88.100  1.00 46.40  ? 252 PHE B CE1   1 
ATOM   6094 C  CE2   . PHE B 1 225 ? 73.828  45.365  86.429  1.00 49.15  ? 252 PHE B CE2   1 
ATOM   6095 C  CZ    . PHE B 1 225 ? 73.619  46.658  86.862  1.00 48.42  ? 252 PHE B CZ    1 
ATOM   6096 N  N     . TYR B 1 226 ? 78.164  41.757  89.915  1.00 46.02  ? 253 TYR B N     1 
ATOM   6097 C  CA    . TYR B 1 226 ? 78.743  40.830  90.874  1.00 43.62  ? 253 TYR B CA    1 
ATOM   6098 C  C     . TYR B 1 226 ? 79.442  39.719  90.113  1.00 54.76  ? 253 TYR B C     1 
ATOM   6099 O  O     . TYR B 1 226 ? 78.951  39.315  89.050  1.00 55.34  ? 253 TYR B O     1 
ATOM   6100 C  CB    . TYR B 1 226 ? 77.670  40.245  91.798  1.00 42.59  ? 253 TYR B CB    1 
ATOM   6101 C  CG    . TYR B 1 226 ? 78.236  39.611  93.041  1.00 49.14  ? 253 TYR B CG    1 
ATOM   6102 C  CD1   . TYR B 1 226 ? 78.593  40.390  94.134  1.00 53.26  ? 253 TYR B CD1   1 
ATOM   6103 C  CD2   . TYR B 1 226 ? 78.428  38.238  93.120  1.00 48.28  ? 253 TYR B CD2   1 
ATOM   6104 C  CE1   . TYR B 1 226 ? 79.119  39.818  95.279  1.00 56.53  ? 253 TYR B CE1   1 
ATOM   6105 C  CE2   . TYR B 1 226 ? 78.955  37.657  94.258  1.00 54.96  ? 253 TYR B CE2   1 
ATOM   6106 C  CZ    . TYR B 1 226 ? 79.297  38.450  95.335  1.00 58.90  ? 253 TYR B CZ    1 
ATOM   6107 O  OH    . TYR B 1 226 ? 79.820  37.873  96.471  1.00 69.92  ? 253 TYR B OH    1 
ATOM   6108 N  N     . PRO B 1 227 ? 80.583  39.214  90.602  1.00 57.54  ? 254 PRO B N     1 
ATOM   6109 C  CA    . PRO B 1 227 ? 81.329  39.660  91.787  1.00 57.65  ? 254 PRO B CA    1 
ATOM   6110 C  C     . PRO B 1 227 ? 82.091  40.941  91.482  1.00 59.13  ? 254 PRO B C     1 
ATOM   6111 O  O     . PRO B 1 227 ? 82.090  41.385  90.336  1.00 53.61  ? 254 PRO B O     1 
ATOM   6112 C  CB    . PRO B 1 227 ? 82.253  38.469  92.069  1.00 44.44  ? 254 PRO B CB    1 
ATOM   6113 C  CG    . PRO B 1 227 ? 82.532  37.907  90.712  1.00 49.25  ? 254 PRO B CG    1 
ATOM   6114 C  CD    . PRO B 1 227 ? 81.231  38.055  89.959  1.00 57.03  ? 254 PRO B CD    1 
ATOM   6115 N  N     . PRO B 1 228 ? 82.724  41.578  92.466  1.00 58.51  ? 255 PRO B N     1 
ATOM   6116 C  CA    . PRO B 1 228 ? 83.564  42.739  92.156  1.00 61.15  ? 255 PRO B CA    1 
ATOM   6117 C  C     . PRO B 1 228 ? 84.655  42.380  91.158  1.00 58.98  ? 255 PRO B C     1 
ATOM   6118 O  O     . PRO B 1 228 ? 85.109  41.237  91.084  1.00 65.13  ? 255 PRO B O     1 
ATOM   6119 C  CB    . PRO B 1 228 ? 84.152  43.124  93.518  1.00 54.55  ? 255 PRO B CB    1 
ATOM   6120 C  CG    . PRO B 1 228 ? 83.136  42.651  94.502  1.00 50.86  ? 255 PRO B CG    1 
ATOM   6121 C  CD    . PRO B 1 228 ? 82.568  41.384  93.920  1.00 53.54  ? 255 PRO B CD    1 
ATOM   6122 N  N     . HIS B 1 229 ? 85.057  43.377  90.372  1.00 53.81  ? 256 HIS B N     1 
ATOM   6123 C  CA    . HIS B 1 229 ? 86.124  43.193  89.402  1.00 49.85  ? 256 HIS B CA    1 
ATOM   6124 C  C     . HIS B 1 229 ? 87.398  42.714  90.104  1.00 56.83  ? 256 HIS B C     1 
ATOM   6125 O  O     . HIS B 1 229 ? 87.638  43.053  91.266  1.00 56.36  ? 256 HIS B O     1 
ATOM   6126 C  CB    . HIS B 1 229 ? 86.381  44.504  88.658  1.00 52.39  ? 256 HIS B CB    1 
ATOM   6127 C  CG    . HIS B 1 229 ? 87.329  44.375  87.507  1.00 56.57  ? 256 HIS B CG    1 
ATOM   6128 N  ND1   . HIS B 1 229 ? 88.697  44.451  87.659  1.00 64.72  ? 256 HIS B ND1   1 
ATOM   6129 C  CD2   . HIS B 1 229 ? 87.108  44.175  86.187  1.00 46.89  ? 256 HIS B CD2   1 
ATOM   6130 C  CE1   . HIS B 1 229 ? 89.277  44.302  86.482  1.00 55.53  ? 256 HIS B CE1   1 
ATOM   6131 N  NE2   . HIS B 1 229 ? 88.335  44.134  85.572  1.00 54.99  ? 256 HIS B NE2   1 
ATOM   6132 N  N     . PRO B 1 230 ? 88.223  41.896  89.426  1.00 59.55  ? 257 PRO B N     1 
ATOM   6133 C  CA    . PRO B 1 230 ? 89.458  41.392  90.050  1.00 54.94  ? 257 PRO B CA    1 
ATOM   6134 C  C     . PRO B 1 230 ? 90.377  42.477  90.597  1.00 57.36  ? 257 PRO B C     1 
ATOM   6135 O  O     . PRO B 1 230 ? 91.161  42.224  91.519  1.00 70.69  ? 257 PRO B O     1 
ATOM   6136 C  CB    . PRO B 1 230 ? 90.127  40.626  88.905  1.00 51.64  ? 257 PRO B CB    1 
ATOM   6137 C  CG    . PRO B 1 230 ? 88.983  40.137  88.088  1.00 49.70  ? 257 PRO B CG    1 
ATOM   6138 C  CD    . PRO B 1 230 ? 87.933  41.213  88.152  1.00 47.97  ? 257 PRO B CD    1 
ATOM   6139 N  N     . ASP B 1 231 ? 90.286  43.683  90.043  1.00 58.35  ? 258 ASP B N     1 
ATOM   6140 C  CA    . ASP B 1 231 ? 91.093  44.815  90.477  1.00 61.11  ? 258 ASP B CA    1 
ATOM   6141 C  C     . ASP B 1 231 ? 90.383  45.703  91.490  1.00 63.87  ? 258 ASP B C     1 
ATOM   6142 O  O     . ASP B 1 231 ? 90.940  46.732  91.889  1.00 64.35  ? 258 ASP B O     1 
ATOM   6143 C  CB    . ASP B 1 231 ? 91.513  45.649  89.266  1.00 55.69  ? 258 ASP B CB    1 
ATOM   6144 C  CG    . ASP B 1 231 ? 92.442  44.898  88.348  1.00 62.18  ? 258 ASP B CG    1 
ATOM   6145 O  OD1   . ASP B 1 231 ? 93.232  44.081  88.865  1.00 72.49  ? 258 ASP B OD1   1 
ATOM   6146 O  OD2   . ASP B 1 231 ? 92.384  45.114  87.119  1.00 78.88  ? 258 ASP B OD2   1 
ATOM   6147 N  N     . TYR B 1 232 ? 89.173  45.337  91.909  1.00 64.30  ? 259 TYR B N     1 
ATOM   6148 C  CA    . TYR B 1 232 ? 88.428  46.151  92.860  1.00 57.86  ? 259 TYR B CA    1 
ATOM   6149 C  C     . TYR B 1 232 ? 89.098  46.109  94.229  1.00 67.72  ? 259 TYR B C     1 
ATOM   6150 O  O     . TYR B 1 232 ? 89.424  45.035  94.740  1.00 64.55  ? 259 TYR B O     1 
ATOM   6151 C  CB    . TYR B 1 232 ? 86.984  45.659  92.957  1.00 53.01  ? 259 TYR B CB    1 
ATOM   6152 C  CG    . TYR B 1 232 ? 86.071  46.552  93.772  1.00 64.68  ? 259 TYR B CG    1 
ATOM   6153 C  CD1   . TYR B 1 232 ? 85.581  47.742  93.247  1.00 69.24  ? 259 TYR B CD1   1 
ATOM   6154 C  CD2   . TYR B 1 232 ? 85.684  46.197  95.057  1.00 58.09  ? 259 TYR B CD2   1 
ATOM   6155 C  CE1   . TYR B 1 232 ? 84.742  48.559  93.984  1.00 74.09  ? 259 TYR B CE1   1 
ATOM   6156 C  CE2   . TYR B 1 232 ? 84.844  47.007  95.801  1.00 63.24  ? 259 TYR B CE2   1 
ATOM   6157 C  CZ    . TYR B 1 232 ? 84.376  48.187  95.258  1.00 67.36  ? 259 TYR B CZ    1 
ATOM   6158 O  OH    . TYR B 1 232 ? 83.541  49.000  95.991  1.00 65.97  ? 259 TYR B OH    1 
ATOM   6159 N  N     . THR B 1 233 ? 89.311  47.290  94.821  1.00 65.54  ? 260 THR B N     1 
ATOM   6160 C  CA    . THR B 1 233 ? 89.961  47.389  96.123  1.00 68.33  ? 260 THR B CA    1 
ATOM   6161 C  C     . THR B 1 233 ? 89.230  48.353  97.054  1.00 67.03  ? 260 THR B C     1 
ATOM   6162 O  O     . THR B 1 233 ? 89.835  48.859  98.006  1.00 67.36  ? 260 THR B O     1 
ATOM   6163 C  CB    . THR B 1 233 ? 91.424  47.827  95.981  1.00 63.73  ? 260 THR B CB    1 
ATOM   6164 O  OG1   . THR B 1 233 ? 91.497  49.016  95.186  1.00 78.77  ? 260 THR B OG1   1 
ATOM   6165 C  CG2   . THR B 1 233 ? 92.254  46.729  95.329  1.00 63.99  ? 260 THR B CG2   1 
ATOM   6166 N  N     . TRP B 1 234 ? 87.953  48.618  96.804  1.00 68.23  ? 261 TRP B N     1 
ATOM   6167 C  CA    . TRP B 1 234 ? 87.173  49.575  97.567  1.00 57.98  ? 261 TRP B CA    1 
ATOM   6168 C  C     . TRP B 1 234 ? 86.188  48.848  98.478  1.00 67.54  ? 261 TRP B C     1 
ATOM   6169 O  O     . TRP B 1 234 ? 86.258  47.628  98.663  1.00 78.53  ? 261 TRP B O     1 
ATOM   6170 C  CB    . TRP B 1 234 ? 86.468  50.542  96.614  1.00 57.73  ? 261 TRP B CB    1 
ATOM   6171 C  CG    . TRP B 1 234 ? 87.413  51.411  95.839  1.00 78.69  ? 261 TRP B CG    1 
ATOM   6172 C  CD1   . TRP B 1 234 ? 88.710  51.695  96.154  1.00 86.14  ? 261 TRP B CD1   1 
ATOM   6173 C  CD2   . TRP B 1 234 ? 87.138  52.100  94.612  1.00 73.82  ? 261 TRP B CD2   1 
ATOM   6174 N  NE1   . TRP B 1 234 ? 89.258  52.523  95.203  1.00 88.00  ? 261 TRP B NE1   1 
ATOM   6175 C  CE2   . TRP B 1 234 ? 88.313  52.786  94.246  1.00 76.81  ? 261 TRP B CE2   1 
ATOM   6176 C  CE3   . TRP B 1 234 ? 86.014  52.205  93.790  1.00 75.81  ? 261 TRP B CE3   1 
ATOM   6177 C  CZ2   . TRP B 1 234 ? 88.393  53.565  93.094  1.00 79.03  ? 261 TRP B CZ2   1 
ATOM   6178 C  CZ3   . TRP B 1 234 ? 86.094  52.980  92.649  1.00 72.54  ? 261 TRP B CZ3   1 
ATOM   6179 C  CH2   . TRP B 1 234 ? 87.276  53.649  92.311  1.00 81.17  ? 261 TRP B CH2   1 
ATOM   6180 N  N     . SER B 1 235 ? 85.257  49.607  99.051  1.00 68.10  ? 262 SER B N     1 
ATOM   6181 C  CA    . SER B 1 235 ? 84.323  49.049  100.021 1.00 58.71  ? 262 SER B CA    1 
ATOM   6182 C  C     . SER B 1 235 ? 83.282  48.174  99.337  1.00 62.93  ? 262 SER B C     1 
ATOM   6183 O  O     . SER B 1 235 ? 82.971  48.344  98.155  1.00 70.35  ? 262 SER B O     1 
ATOM   6184 C  CB    . SER B 1 235 ? 83.627  50.169  100.798 1.00 54.71  ? 262 SER B CB    1 
ATOM   6185 O  OG    . SER B 1 235 ? 84.568  50.933  101.528 1.00 96.29  ? 262 SER B OG    1 
ATOM   6186 N  N     . PHE B 1 236 ? 82.736  47.231  100.102 1.00 69.73  ? 263 PHE B N     1 
ATOM   6187 C  CA    . PHE B 1 236 ? 81.707  46.324  99.612  1.00 69.79  ? 263 PHE B CA    1 
ATOM   6188 C  C     . PHE B 1 236 ? 80.383  47.073  99.459  1.00 70.32  ? 263 PHE B C     1 
ATOM   6189 O  O     . PHE B 1 236 ? 79.412  46.803  100.183 1.00 76.54  ? 263 PHE B O     1 
ATOM   6190 C  CB    . PHE B 1 236 ? 81.549  45.140  100.575 1.00 63.94  ? 263 PHE B CB    1 
ATOM   6191 C  CG    . PHE B 1 236 ? 80.859  43.950  99.971  1.00 56.71  ? 263 PHE B CG    1 
ATOM   6192 C  CD1   . PHE B 1 236 ? 81.500  43.172  99.025  1.00 48.96  ? 263 PHE B CD1   1 
ATOM   6193 C  CD2   . PHE B 1 236 ? 79.578  43.591  100.369 1.00 63.01  ? 263 PHE B CD2   1 
ATOM   6194 C  CE1   . PHE B 1 236 ? 80.884  42.068  98.471  1.00 57.23  ? 263 PHE B CE1   1 
ATOM   6195 C  CE2   . PHE B 1 236 ? 78.949  42.477  99.815  1.00 71.34  ? 263 PHE B CE2   1 
ATOM   6196 C  CZ    . PHE B 1 236 ? 79.610  41.716  98.864  1.00 60.87  ? 263 PHE B CZ    1 
ATOM   6197 N  N     . ASP B 1 237 ? 80.334  48.015  98.518  1.00 69.84  ? 264 ASP B N     1 
ATOM   6198 C  CA    . ASP B 1 237 ? 79.156  48.825  98.236  1.00 66.42  ? 264 ASP B CA    1 
ATOM   6199 C  C     . ASP B 1 237 ? 78.697  48.543  96.811  1.00 63.16  ? 264 ASP B C     1 
ATOM   6200 O  O     . ASP B 1 237 ? 79.514  48.491  95.886  1.00 70.77  ? 264 ASP B O     1 
ATOM   6201 C  CB    . ASP B 1 237 ? 79.463  50.324  98.420  1.00 66.05  ? 264 ASP B CB    1 
ATOM   6202 C  CG    . ASP B 1 237 ? 78.206  51.195  98.408  1.00 79.49  ? 264 ASP B CG    1 
ATOM   6203 O  OD1   . ASP B 1 237 ? 77.109  50.690  98.091  1.00 92.42  ? 264 ASP B OD1   1 
ATOM   6204 O  OD2   . ASP B 1 237 ? 78.319  52.402  98.728  1.00 83.95  ? 264 ASP B OD2   1 
ATOM   6205 N  N     . ASP B 1 238 ? 77.383  48.388  96.628  1.00 57.70  ? 265 ASP B N     1 
ATOM   6206 C  CA    . ASP B 1 238 ? 76.872  47.874  95.358  1.00 54.27  ? 265 ASP B CA    1 
ATOM   6207 C  C     . ASP B 1 238 ? 77.047  48.879  94.224  1.00 57.90  ? 265 ASP B C     1 
ATOM   6208 O  O     . ASP B 1 238 ? 77.459  48.507  93.118  1.00 57.52  ? 265 ASP B O     1 
ATOM   6209 C  CB    . ASP B 1 238 ? 75.405  47.468  95.505  1.00 45.55  ? 265 ASP B CB    1 
ATOM   6210 C  CG    . ASP B 1 238 ? 74.519  48.615  95.934  1.00 59.78  ? 265 ASP B CG    1 
ATOM   6211 O  OD1   . ASP B 1 238 ? 75.041  49.596  96.502  1.00 57.47  ? 265 ASP B OD1   1 
ATOM   6212 O  OD2   . ASP B 1 238 ? 73.293  48.533  95.703  1.00 63.29  ? 265 ASP B OD2   1 
ATOM   6213 N  N     . ILE B 1 239 ? 76.743  50.155  94.471  1.00 58.07  ? 266 ILE B N     1 
ATOM   6214 C  CA    . ILE B 1 239 ? 76.841  51.145  93.402  1.00 44.95  ? 266 ILE B CA    1 
ATOM   6215 C  C     . ILE B 1 239 ? 78.296  51.461  93.081  1.00 54.28  ? 266 ILE B C     1 
ATOM   6216 O  O     . ILE B 1 239 ? 78.621  51.823  91.944  1.00 62.98  ? 266 ILE B O     1 
ATOM   6217 C  CB    . ILE B 1 239 ? 76.058  52.421  93.765  1.00 55.92  ? 266 ILE B CB    1 
ATOM   6218 C  CG1   . ILE B 1 239 ? 76.672  53.112  94.982  1.00 60.24  ? 266 ILE B CG1   1 
ATOM   6219 C  CG2   . ILE B 1 239 ? 74.601  52.093  94.027  1.00 44.21  ? 266 ILE B CG2   1 
ATOM   6220 C  CD1   . ILE B 1 239 ? 76.125  54.497  95.223  1.00 51.11  ? 266 ILE B CD1   1 
ATOM   6221 N  N     . ILE B 1 240 ? 79.191  51.339  94.064  1.00 63.40  ? 267 ILE B N     1 
ATOM   6222 C  CA    . ILE B 1 240 ? 80.611  51.544  93.799  1.00 52.05  ? 267 ILE B CA    1 
ATOM   6223 C  C     . ILE B 1 240 ? 81.161  50.402  92.955  1.00 55.37  ? 267 ILE B C     1 
ATOM   6224 O  O     . ILE B 1 240 ? 81.949  50.620  92.028  1.00 61.65  ? 267 ILE B O     1 
ATOM   6225 C  CB    . ILE B 1 240 ? 81.385  51.692  95.121  1.00 58.79  ? 267 ILE B CB    1 
ATOM   6226 C  CG1   . ILE B 1 240 ? 80.764  52.785  95.993  1.00 70.01  ? 267 ILE B CG1   1 
ATOM   6227 C  CG2   . ILE B 1 240 ? 82.837  52.008  94.848  1.00 73.33  ? 267 ILE B CG2   1 
ATOM   6228 C  CD1   . ILE B 1 240 ? 81.525  53.043  97.281  1.00 79.30  ? 267 ILE B CD1   1 
ATOM   6229 N  N     . VAL B 1 241 ? 80.749  49.168  93.259  1.00 60.14  ? 268 VAL B N     1 
ATOM   6230 C  CA    . VAL B 1 241 ? 81.234  48.007  92.516  1.00 55.85  ? 268 VAL B CA    1 
ATOM   6231 C  C     . VAL B 1 241 ? 80.848  48.117  91.046  1.00 57.31  ? 268 VAL B C     1 
ATOM   6232 O  O     . VAL B 1 241 ? 81.668  47.880  90.151  1.00 61.35  ? 268 VAL B O     1 
ATOM   6233 C  CB    . VAL B 1 241 ? 80.701  46.707  93.145  1.00 51.32  ? 268 VAL B CB    1 
ATOM   6234 C  CG1   . VAL B 1 241 ? 80.761  45.564  92.147  1.00 43.23  ? 268 VAL B CG1   1 
ATOM   6235 C  CG2   . VAL B 1 241 ? 81.498  46.358  94.391  1.00 54.81  ? 268 VAL B CG2   1 
ATOM   6236 N  N     . PHE B 1 242 ? 79.594  48.483  90.773  1.00 57.57  ? 269 PHE B N     1 
ATOM   6237 C  CA    . PHE B 1 242 ? 79.164  48.608  89.385  1.00 54.63  ? 269 PHE B CA    1 
ATOM   6238 C  C     . PHE B 1 242 ? 79.835  49.793  88.703  1.00 56.86  ? 269 PHE B C     1 
ATOM   6239 O  O     . PHE B 1 242 ? 80.202  49.710  87.526  1.00 53.96  ? 269 PHE B O     1 
ATOM   6240 C  CB    . PHE B 1 242 ? 77.645  48.739  89.297  1.00 44.81  ? 269 PHE B CB    1 
ATOM   6241 C  CG    . PHE B 1 242 ? 77.141  48.878  87.891  1.00 49.62  ? 269 PHE B CG    1 
ATOM   6242 C  CD1   . PHE B 1 242 ? 77.319  47.852  86.978  1.00 52.30  ? 269 PHE B CD1   1 
ATOM   6243 C  CD2   . PHE B 1 242 ? 76.502  50.034  87.476  1.00 47.71  ? 269 PHE B CD2   1 
ATOM   6244 C  CE1   . PHE B 1 242 ? 76.868  47.973  85.681  1.00 54.51  ? 269 PHE B CE1   1 
ATOM   6245 C  CE2   . PHE B 1 242 ? 76.045  50.161  86.178  1.00 48.69  ? 269 PHE B CE2   1 
ATOM   6246 C  CZ    . PHE B 1 242 ? 76.230  49.129  85.280  1.00 47.23  ? 269 PHE B CZ    1 
ATOM   6247 N  N     . ALA B 1 243 ? 79.992  50.907  89.420  1.00 51.39  ? 270 ALA B N     1 
ATOM   6248 C  CA    . ALA B 1 243 ? 80.695  52.054  88.854  1.00 55.95  ? 270 ALA B CA    1 
ATOM   6249 C  C     . ALA B 1 243 ? 82.114  51.678  88.451  1.00 58.73  ? 270 ALA B C     1 
ATOM   6250 O  O     . ALA B 1 243 ? 82.583  52.054  87.371  1.00 60.40  ? 270 ALA B O     1 
ATOM   6251 C  CB    . ALA B 1 243 ? 80.711  53.209  89.855  1.00 51.28  ? 270 ALA B CB    1 
ATOM   6252 N  N     . PHE B 1 244 ? 82.806  50.925  89.309  1.00 57.65  ? 271 PHE B N     1 
ATOM   6253 C  CA    . PHE B 1 244 ? 84.153  50.465  88.991  1.00 54.86  ? 271 PHE B CA    1 
ATOM   6254 C  C     . PHE B 1 244 ? 84.153  49.500  87.814  1.00 59.89  ? 271 PHE B C     1 
ATOM   6255 O  O     . PHE B 1 244 ? 85.102  49.496  87.020  1.00 59.31  ? 271 PHE B O     1 
ATOM   6256 C  CB    . PHE B 1 244 ? 84.776  49.808  90.224  1.00 49.03  ? 271 PHE B CB    1 
ATOM   6257 C  CG    . PHE B 1 244 ? 86.213  49.413  90.046  1.00 57.67  ? 271 PHE B CG    1 
ATOM   6258 C  CD1   . PHE B 1 244 ? 87.226  50.334  90.242  1.00 62.30  ? 271 PHE B CD1   1 
ATOM   6259 C  CD2   . PHE B 1 244 ? 86.551  48.116  89.697  1.00 57.23  ? 271 PHE B CD2   1 
ATOM   6260 C  CE1   . PHE B 1 244 ? 88.548  49.973  90.084  1.00 61.75  ? 271 PHE B CE1   1 
ATOM   6261 C  CE2   . PHE B 1 244 ? 87.872  47.750  89.538  1.00 52.32  ? 271 PHE B CE2   1 
ATOM   6262 C  CZ    . PHE B 1 244 ? 88.871  48.680  89.732  1.00 58.46  ? 271 PHE B CZ    1 
ATOM   6263 N  N     . SER B 1 245 ? 83.105  48.682  87.684  1.00 58.87  ? 272 SER B N     1 
ATOM   6264 C  CA    . SER B 1 245 ? 83.000  47.788  86.536  1.00 48.18  ? 272 SER B CA    1 
ATOM   6265 C  C     . SER B 1 245 ? 82.916  48.562  85.228  1.00 50.87  ? 272 SER B C     1 
ATOM   6266 O  O     . SER B 1 245 ? 83.418  48.098  84.199  1.00 59.80  ? 272 SER B O     1 
ATOM   6267 C  CB    . SER B 1 245 ? 81.779  46.881  86.690  1.00 48.40  ? 272 SER B CB    1 
ATOM   6268 O  OG    . SER B 1 245 ? 81.762  45.869  85.700  1.00 42.28  ? 272 SER B OG    1 
ATOM   6269 N  N     . CYS B 1 246 ? 82.295  49.744  85.245  1.00 51.93  ? 273 CYS B N     1 
ATOM   6270 C  CA    . CYS B 1 246 ? 82.194  50.538  84.026  1.00 46.40  ? 273 CYS B CA    1 
ATOM   6271 C  C     . CYS B 1 246 ? 83.540  51.141  83.647  1.00 58.56  ? 273 CYS B C     1 
ATOM   6272 O  O     . CYS B 1 246 ? 83.872  51.227  82.459  1.00 63.45  ? 273 CYS B O     1 
ATOM   6273 C  CB    . CYS B 1 246 ? 81.142  51.633  84.199  1.00 43.89  ? 273 CYS B CB    1 
ATOM   6274 S  SG    . CYS B 1 246 ? 79.473  51.022  84.539  1.00 50.16  ? 273 CYS B SG    1 
ATOM   6275 N  N     . LYS B 1 247 ? 84.326  51.568  84.639  1.00 48.67  ? 274 LYS B N     1 
ATOM   6276 C  CA    . LYS B 1 247 ? 85.637  52.142  84.350  1.00 57.76  ? 274 LYS B CA    1 
ATOM   6277 C  C     . LYS B 1 247 ? 86.561  51.114  83.711  1.00 51.72  ? 274 LYS B C     1 
ATOM   6278 O  O     . LYS B 1 247 ? 87.274  51.423  82.749  1.00 57.00  ? 274 LYS B O     1 
ATOM   6279 C  CB    . LYS B 1 247 ? 86.261  52.701  85.629  1.00 53.31  ? 274 LYS B CB    1 
ATOM   6280 C  CG    . LYS B 1 247 ? 85.550  53.928  86.166  1.00 88.17  ? 274 LYS B CG    1 
ATOM   6281 C  CD    . LYS B 1 247 ? 85.897  54.182  87.622  1.00 100.59 ? 274 LYS B CD    1 
ATOM   6282 C  CE    . LYS B 1 247 ? 84.975  55.229  88.227  1.00 100.49 ? 274 LYS B CE    1 
ATOM   6283 N  NZ    . LYS B 1 247 ? 85.169  55.360  89.697  1.00 104.16 ? 274 LYS B NZ    1 
ATOM   6284 N  N     . GLN B 1 248 ? 86.556  49.883  84.227  1.00 50.51  ? 275 GLN B N     1 
ATOM   6285 C  CA    . GLN B 1 248 ? 87.418  48.844  83.674  1.00 44.85  ? 275 GLN B CA    1 
ATOM   6286 C  C     . GLN B 1 248 ? 86.967  48.415  82.283  1.00 44.91  ? 275 GLN B C     1 
ATOM   6287 O  O     . GLN B 1 248 ? 87.802  48.046  81.449  1.00 63.41  ? 275 GLN B O     1 
ATOM   6288 C  CB    . GLN B 1 248 ? 87.460  47.644  84.620  1.00 55.53  ? 275 GLN B CB    1 
ATOM   6289 C  CG    . GLN B 1 248 ? 87.915  48.000  86.025  1.00 54.07  ? 275 GLN B CG    1 
ATOM   6290 C  CD    . GLN B 1 248 ? 89.261  48.698  86.040  1.00 64.33  ? 275 GLN B CD    1 
ATOM   6291 O  OE1   . GLN B 1 248 ? 90.296  48.082  85.784  1.00 66.92  ? 275 GLN B OE1   1 
ATOM   6292 N  NE2   . GLN B 1 248 ? 89.253  49.993  86.336  1.00 64.71  ? 275 GLN B NE2   1 
ATOM   6293 N  N     . ALA B 1 249 ? 85.664  48.454  82.012  1.00 52.28  ? 276 ALA B N     1 
ATOM   6294 C  CA    . ALA B 1 249 ? 85.160  48.208  80.668  1.00 51.87  ? 276 ALA B CA    1 
ATOM   6295 C  C     . ALA B 1 249 ? 85.272  49.430  79.767  1.00 58.36  ? 276 ALA B C     1 
ATOM   6296 O  O     . ALA B 1 249 ? 84.857  49.361  78.605  1.00 54.60  ? 276 ALA B O     1 
ATOM   6297 C  CB    . ALA B 1 249 ? 83.702  47.745  80.728  1.00 43.20  ? 276 ALA B CB    1 
ATOM   6298 N  N     . GLU B 1 250 ? 85.824  50.535  80.276  1.00 62.98  ? 277 GLU B N     1 
ATOM   6299 C  CA    . GLU B 1 250 ? 85.903  51.800  79.544  1.00 61.87  ? 277 GLU B CA    1 
ATOM   6300 C  C     . GLU B 1 250 ? 84.525  52.244  79.062  1.00 57.80  ? 277 GLU B C     1 
ATOM   6301 O  O     . GLU B 1 250 ? 84.370  52.773  77.959  1.00 64.98  ? 277 GLU B O     1 
ATOM   6302 C  CB    . GLU B 1 250 ? 86.898  51.710  78.386  1.00 62.29  ? 277 GLU B CB    1 
ATOM   6303 C  CG    . GLU B 1 250 ? 88.343  51.629  78.848  1.00 74.36  ? 277 GLU B CG    1 
ATOM   6304 C  CD    . GLU B 1 250 ? 89.308  51.368  77.712  1.00 109.46 ? 277 GLU B CD    1 
ATOM   6305 O  OE1   . GLU B 1 250 ? 88.855  51.275  76.552  1.00 120.23 ? 277 GLU B OE1   1 
ATOM   6306 O  OE2   . GLU B 1 250 ? 90.522  51.253  77.981  1.00 120.83 ? 277 GLU B OE2   1 
ATOM   6307 N  N     . VAL B 1 251 ? 83.516  52.024  79.899  1.00 55.61  ? 278 VAL B N     1 
ATOM   6308 C  CA    . VAL B 1 251 ? 82.152  52.475  79.646  1.00 48.21  ? 278 VAL B CA    1 
ATOM   6309 C  C     . VAL B 1 251 ? 81.916  53.735  80.466  1.00 65.50  ? 278 VAL B C     1 
ATOM   6310 O  O     . VAL B 1 251 ? 81.979  53.702  81.701  1.00 58.88  ? 278 VAL B O     1 
ATOM   6311 C  CB    . VAL B 1 251 ? 81.125  51.389  80.002  1.00 49.99  ? 278 VAL B CB    1 
ATOM   6312 C  CG1   . VAL B 1 251 ? 79.713  51.910  79.809  1.00 46.62  ? 278 VAL B CG1   1 
ATOM   6313 C  CG2   . VAL B 1 251 ? 81.358  50.144  79.167  1.00 47.81  ? 278 VAL B CG2   1 
ATOM   6314 N  N     . GLN B 1 252 ? 81.643  54.845  79.788  1.00 63.38  ? 279 GLN B N     1 
ATOM   6315 C  CA    . GLN B 1 252 ? 81.395  56.101  80.478  1.00 49.63  ? 279 GLN B CA    1 
ATOM   6316 C  C     . GLN B 1 252 ? 79.949  56.162  80.950  1.00 57.14  ? 279 GLN B C     1 
ATOM   6317 O  O     . GLN B 1 252 ? 79.021  55.966  80.160  1.00 63.63  ? 279 GLN B O     1 
ATOM   6318 C  CB    . GLN B 1 252 ? 81.701  57.286  79.565  1.00 46.72  ? 279 GLN B CB    1 
ATOM   6319 C  CG    . GLN B 1 252 ? 81.408  58.635  80.198  1.00 60.59  ? 279 GLN B CG    1 
ATOM   6320 C  CD    . GLN B 1 252 ? 82.117  58.817  81.526  1.00 70.81  ? 279 GLN B CD    1 
ATOM   6321 O  OE1   . GLN B 1 252 ? 83.343  58.729  81.604  1.00 57.73  ? 279 GLN B OE1   1 
ATOM   6322 N  NE2   . GLN B 1 252 ? 81.347  59.065  82.581  1.00 55.78  ? 279 GLN B NE2   1 
ATOM   6323 N  N     . MET B 1 253 ? 79.761  56.423  82.240  1.00 53.01  ? 280 MET B N     1 
ATOM   6324 C  CA    . MET B 1 253 ? 78.428  56.648  82.775  1.00 54.01  ? 280 MET B CA    1 
ATOM   6325 C  C     . MET B 1 253 ? 77.988  58.076  82.489  1.00 50.27  ? 280 MET B C     1 
ATOM   6326 O  O     . MET B 1 253 ? 78.785  59.015  82.565  1.00 56.89  ? 280 MET B O     1 
ATOM   6327 C  CB    . MET B 1 253 ? 78.398  56.373  84.278  1.00 49.97  ? 280 MET B CB    1 
ATOM   6328 C  CG    . MET B 1 253 ? 78.144  54.915  84.632  1.00 64.74  ? 280 MET B CG    1 
ATOM   6329 S  SD    . MET B 1 253 ? 78.329  54.575  86.391  1.00 60.94  ? 280 MET B SD    1 
ATOM   6330 C  CE    . MET B 1 253 ? 80.098  54.779  86.562  1.00 85.58  ? 280 MET B CE    1 
ATOM   6331 N  N     . TYR B 1 254 ? 76.713  58.235  82.143  1.00 46.99  ? 281 TYR B N     1 
ATOM   6332 C  CA    . TYR B 1 254 ? 76.152  59.534  81.807  1.00 57.48  ? 281 TYR B CA    1 
ATOM   6333 C  C     . TYR B 1 254 ? 74.887  59.784  82.614  1.00 52.05  ? 281 TYR B C     1 
ATOM   6334 O  O     . TYR B 1 254 ? 74.152  58.854  82.958  1.00 49.42  ? 281 TYR B O     1 
ATOM   6335 C  CB    . TYR B 1 254 ? 75.822  59.648  80.310  1.00 47.32  ? 281 TYR B CB    1 
ATOM   6336 C  CG    . TYR B 1 254 ? 77.028  59.713  79.399  1.00 48.15  ? 281 TYR B CG    1 
ATOM   6337 C  CD1   . TYR B 1 254 ? 77.650  60.924  79.120  1.00 55.92  ? 281 TYR B CD1   1 
ATOM   6338 C  CD2   . TYR B 1 254 ? 77.535  58.563  78.806  1.00 58.99  ? 281 TYR B CD2   1 
ATOM   6339 C  CE1   . TYR B 1 254 ? 78.748  60.987  78.283  1.00 58.63  ? 281 TYR B CE1   1 
ATOM   6340 C  CE2   . TYR B 1 254 ? 78.632  58.616  77.966  1.00 61.32  ? 281 TYR B CE2   1 
ATOM   6341 C  CZ    . TYR B 1 254 ? 79.235  59.830  77.709  1.00 68.05  ? 281 TYR B CZ    1 
ATOM   6342 O  OH    . TYR B 1 254 ? 80.328  59.883  76.874  1.00 78.70  ? 281 TYR B OH    1 
ATOM   6343 N  N     . VAL B 1 255 ? 74.641  61.057  82.911  1.00 55.94  ? 282 VAL B N     1 
ATOM   6344 C  CA    . VAL B 1 255 ? 73.380  61.514  83.480  1.00 53.41  ? 282 VAL B CA    1 
ATOM   6345 C  C     . VAL B 1 255 ? 72.838  62.613  82.576  1.00 56.00  ? 282 VAL B C     1 
ATOM   6346 O  O     . VAL B 1 255 ? 73.588  63.496  82.144  1.00 45.82  ? 282 VAL B O     1 
ATOM   6347 C  CB    . VAL B 1 255 ? 73.547  62.009  84.931  1.00 61.47  ? 282 VAL B CB    1 
ATOM   6348 C  CG1   . VAL B 1 255 ? 74.592  63.115  85.018  1.00 48.23  ? 282 VAL B CG1   1 
ATOM   6349 C  CG2   . VAL B 1 255 ? 72.213  62.481  85.489  1.00 48.35  ? 282 VAL B CG2   1 
ATOM   6350 N  N     . CYS B 1 256 ? 71.548  62.541  82.263  1.00 60.40  ? 283 CYS B N     1 
ATOM   6351 C  CA    . CYS B 1 256 ? 70.899  63.518  81.401  1.00 59.40  ? 283 CYS B CA    1 
ATOM   6352 C  C     . CYS B 1 256 ? 69.842  64.260  82.202  1.00 57.94  ? 283 CYS B C     1 
ATOM   6353 O  O     . CYS B 1 256 ? 69.065  63.639  82.934  1.00 55.30  ? 283 CYS B O     1 
ATOM   6354 C  CB    . CYS B 1 256 ? 70.260  62.854  80.177  1.00 42.03  ? 283 CYS B CB    1 
ATOM   6355 S  SG    . CYS B 1 256 ? 71.378  61.860  79.157  1.00 117.87 ? 283 CYS B SG    1 
ATOM   6356 N  N     . ASN B 1 257 ? 69.818  65.586  82.065  1.00 57.10  ? 284 ASN B N     1 
ATOM   6357 C  CA    . ASN B 1 257 ? 68.814  66.417  82.720  1.00 52.40  ? 284 ASN B CA    1 
ATOM   6358 C  C     . ASN B 1 257 ? 68.100  67.323  81.723  1.00 60.06  ? 284 ASN B C     1 
ATOM   6359 O  O     . ASN B 1 257 ? 67.599  68.383  82.110  1.00 58.19  ? 284 ASN B O     1 
ATOM   6360 C  CB    . ASN B 1 257 ? 69.446  67.253  83.834  1.00 47.81  ? 284 ASN B CB    1 
ATOM   6361 C  CG    . ASN B 1 257 ? 70.470  68.244  83.311  1.00 61.95  ? 284 ASN B CG    1 
ATOM   6362 O  OD1   . ASN B 1 257 ? 70.933  68.138  82.175  1.00 58.05  ? 284 ASN B OD1   1 
ATOM   6363 N  ND2   . ASN B 1 257 ? 70.834  69.212  84.145  1.00 69.44  ? 284 ASN B ND2   1 
ATOM   6364 N  N     . LYS B 1 258 ? 68.039  66.918  80.449  1.00 61.78  ? 285 LYS B N     1 
ATOM   6365 C  CA    . LYS B 1 258 ? 67.485  67.784  79.411  1.00 61.21  ? 285 LYS B CA    1 
ATOM   6366 C  C     . LYS B 1 258 ? 66.038  68.159  79.701  1.00 66.26  ? 285 LYS B C     1 
ATOM   6367 O  O     . LYS B 1 258 ? 65.562  69.203  79.237  1.00 78.46  ? 285 LYS B O     1 
ATOM   6368 C  CB    . LYS B 1 258 ? 67.596  67.112  78.041  1.00 49.74  ? 285 LYS B CB    1 
ATOM   6369 C  CG    . LYS B 1 258 ? 69.015  66.931  77.543  1.00 41.37  ? 285 LYS B CG    1 
ATOM   6370 C  CD    . LYS B 1 258 ? 69.031  66.248  76.182  1.00 38.55  ? 285 LYS B CD    1 
ATOM   6371 C  CE    . LYS B 1 258 ? 70.447  65.998  75.689  1.00 58.30  ? 285 LYS B CE    1 
ATOM   6372 N  NZ    . LYS B 1 258 ? 70.446  65.309  74.370  1.00 58.92  ? 285 LYS B NZ    1 
ATOM   6373 N  N     . GLU B 1 259 ? 65.325  67.328  80.453  1.00 65.41  ? 286 GLU B N     1 
ATOM   6374 C  CA    . GLU B 1 259 ? 63.978  67.650  80.893  1.00 70.95  ? 286 GLU B CA    1 
ATOM   6375 C  C     . GLU B 1 259 ? 63.693  66.860  82.162  1.00 59.34  ? 286 GLU B C     1 
ATOM   6376 O  O     . GLU B 1 259 ? 64.530  66.091  82.641  1.00 57.73  ? 286 GLU B O     1 
ATOM   6377 C  CB    . GLU B 1 259 ? 62.946  67.366  79.795  1.00 68.18  ? 286 GLU B CB    1 
ATOM   6378 C  CG    . GLU B 1 259 ? 63.134  66.043  79.072  1.00 67.97  ? 286 GLU B CG    1 
ATOM   6379 C  CD    . GLU B 1 259 ? 62.183  65.888  77.898  1.00 86.18  ? 286 GLU B CD    1 
ATOM   6380 O  OE1   . GLU B 1 259 ? 60.956  66.003  78.107  1.00 86.58  ? 286 GLU B OE1   1 
ATOM   6381 O  OE2   . GLU B 1 259 ? 62.660  65.669  76.763  1.00 78.06  ? 286 GLU B OE2   1 
ATOM   6382 N  N     . GLU B 1 260 ? 62.503  67.065  82.715  1.00 61.32  ? 287 GLU B N     1 
ATOM   6383 C  CA    . GLU B 1 260 ? 62.111  66.374  83.933  1.00 51.03  ? 287 GLU B CA    1 
ATOM   6384 C  C     . GLU B 1 260 ? 61.716  64.941  83.610  1.00 59.96  ? 287 GLU B C     1 
ATOM   6385 O  O     . GLU B 1 260 ? 60.994  64.686  82.643  1.00 60.28  ? 287 GLU B O     1 
ATOM   6386 C  CB    . GLU B 1 260 ? 60.951  67.104  84.607  1.00 44.92  ? 287 GLU B CB    1 
ATOM   6387 C  CG    . GLU B 1 260 ? 60.773  66.757  86.067  1.00 72.51  ? 287 GLU B CG    1 
ATOM   6388 C  CD    . GLU B 1 260 ? 59.615  67.496  86.699  1.00 83.07  ? 287 GLU B CD    1 
ATOM   6389 O  OE1   . GLU B 1 260 ? 58.470  67.303  86.241  1.00 89.42  ? 287 GLU B OE1   1 
ATOM   6390 O  OE2   . GLU B 1 260 ? 59.849  68.276  87.648  1.00 85.73  ? 287 GLU B OE2   1 
ATOM   6391 N  N     . TYR B 1 261 ? 62.204  64.005  84.416  1.00 56.82  ? 288 TYR B N     1 
ATOM   6392 C  CA    . TYR B 1 261 ? 61.912  62.591  84.219  1.00 46.45  ? 288 TYR B CA    1 
ATOM   6393 C  C     . TYR B 1 261 ? 61.149  61.972  85.375  1.00 51.36  ? 288 TYR B C     1 
ATOM   6394 O  O     . TYR B 1 261 ? 60.197  61.223  85.145  1.00 48.18  ? 288 TYR B O     1 
ATOM   6395 C  CB    . TYR B 1 261 ? 63.211  61.806  83.990  1.00 44.81  ? 288 TYR B CB    1 
ATOM   6396 C  CG    . TYR B 1 261 ? 64.075  62.367  82.887  1.00 54.08  ? 288 TYR B CG    1 
ATOM   6397 C  CD1   . TYR B 1 261 ? 63.674  62.297  81.560  1.00 51.33  ? 288 TYR B CD1   1 
ATOM   6398 C  CD2   . TYR B 1 261 ? 65.295  62.962  83.173  1.00 51.73  ? 288 TYR B CD2   1 
ATOM   6399 C  CE1   . TYR B 1 261 ? 64.466  62.811  80.549  1.00 56.39  ? 288 TYR B CE1   1 
ATOM   6400 C  CE2   . TYR B 1 261 ? 66.092  63.475  82.171  1.00 44.86  ? 288 TYR B CE2   1 
ATOM   6401 C  CZ    . TYR B 1 261 ? 65.675  63.400  80.862  1.00 63.51  ? 288 TYR B CZ    1 
ATOM   6402 O  OH    . TYR B 1 261 ? 66.472  63.915  79.864  1.00 71.55  ? 288 TYR B OH    1 
ATOM   6403 N  N     . GLY B 1 262 ? 61.534  62.262  86.611  1.00 49.49  ? 289 GLY B N     1 
ATOM   6404 C  CA    . GLY B 1 262 ? 60.830  61.686  87.738  1.00 47.02  ? 289 GLY B CA    1 
ATOM   6405 C  C     . GLY B 1 262 ? 61.413  62.145  89.055  1.00 56.51  ? 289 GLY B C     1 
ATOM   6406 O  O     . GLY B 1 262 ? 62.243  63.056  89.112  1.00 59.26  ? 289 GLY B O     1 
ATOM   6407 N  N     . PHE B 1 263 ? 60.958  61.488  90.120  1.00 52.46  ? 290 PHE B N     1 
ATOM   6408 C  CA    . PHE B 1 263 ? 61.298  61.856  91.484  1.00 49.66  ? 290 PHE B CA    1 
ATOM   6409 C  C     . PHE B 1 263 ? 61.685  60.609  92.264  1.00 49.56  ? 290 PHE B C     1 
ATOM   6410 O  O     . PHE B 1 263 ? 61.348  59.484  91.887  1.00 53.27  ? 290 PHE B O     1 
ATOM   6411 C  CB    . PHE B 1 263 ? 60.128  62.562  92.186  1.00 49.93  ? 290 PHE B CB    1 
ATOM   6412 C  CG    . PHE B 1 263 ? 59.661  63.807  91.489  1.00 57.48  ? 290 PHE B CG    1 
ATOM   6413 C  CD1   . PHE B 1 263 ? 58.834  63.731  90.380  1.00 53.87  ? 290 PHE B CD1   1 
ATOM   6414 C  CD2   . PHE B 1 263 ? 60.040  65.055  91.950  1.00 57.25  ? 290 PHE B CD2   1 
ATOM   6415 C  CE1   . PHE B 1 263 ? 58.403  64.876  89.737  1.00 63.54  ? 290 PHE B CE1   1 
ATOM   6416 C  CE2   . PHE B 1 263 ? 59.611  66.202  91.314  1.00 70.39  ? 290 PHE B CE2   1 
ATOM   6417 C  CZ    . PHE B 1 263 ? 58.791  66.112  90.206  1.00 69.82  ? 290 PHE B CZ    1 
ATOM   6418 N  N     . LEU B 1 264 ? 62.395  60.823  93.368  1.00 57.93  ? 291 LEU B N     1 
ATOM   6419 C  CA    . LEU B 1 264 ? 62.821  59.736  94.237  1.00 52.42  ? 291 LEU B CA    1 
ATOM   6420 C  C     . LEU B 1 264 ? 62.996  60.276  95.647  1.00 45.55  ? 291 LEU B C     1 
ATOM   6421 O  O     . LEU B 1 264 ? 63.370  61.443  95.819  1.00 51.95  ? 291 LEU B O     1 
ATOM   6422 C  CB    . LEU B 1 264 ? 64.130  59.093  93.746  1.00 55.00  ? 291 LEU B CB    1 
ATOM   6423 C  CG    . LEU B 1 264 ? 65.483  59.737  94.061  1.00 48.45  ? 291 LEU B CG    1 
ATOM   6424 C  CD1   . LEU B 1 264 ? 66.609  58.841  93.571  1.00 46.75  ? 291 LEU B CD1   1 
ATOM   6425 C  CD2   . LEU B 1 264 ? 65.610  61.124  93.455  1.00 51.35  ? 291 LEU B CD2   1 
ATOM   6426 N  N     . PRO B 1 265 ? 62.720  59.471  96.668  1.00 58.40  ? 292 PRO B N     1 
ATOM   6427 C  CA    . PRO B 1 265 ? 62.957  59.924  98.041  1.00 48.92  ? 292 PRO B CA    1 
ATOM   6428 C  C     . PRO B 1 265 ? 64.441  59.941  98.369  1.00 50.58  ? 292 PRO B C     1 
ATOM   6429 O  O     . PRO B 1 265 ? 65.266  59.308  97.705  1.00 51.10  ? 292 PRO B O     1 
ATOM   6430 C  CB    . PRO B 1 265 ? 62.210  58.890  98.888  1.00 48.43  ? 292 PRO B CB    1 
ATOM   6431 C  CG    . PRO B 1 265 ? 62.227  57.656  98.052  1.00 46.44  ? 292 PRO B CG    1 
ATOM   6432 C  CD    . PRO B 1 265 ? 62.130  58.122  96.623  1.00 54.85  ? 292 PRO B CD    1 
ATOM   6433 N  N     . VAL B 1 266 ? 64.776  60.692  99.413  1.00 52.41  ? 293 VAL B N     1 
ATOM   6434 C  CA    . VAL B 1 266 ? 66.152  60.760  99.896  1.00 57.40  ? 293 VAL B CA    1 
ATOM   6435 C  C     . VAL B 1 266 ? 66.385  59.579  100.831 1.00 51.52  ? 293 VAL B C     1 
ATOM   6436 O  O     . VAL B 1 266 ? 65.589  59.359  101.757 1.00 50.04  ? 293 VAL B O     1 
ATOM   6437 C  CB    . VAL B 1 266 ? 66.437  62.101  100.589 1.00 54.65  ? 293 VAL B CB    1 
ATOM   6438 C  CG1   . VAL B 1 266 ? 67.846  62.117  101.155 1.00 44.46  ? 293 VAL B CG1   1 
ATOM   6439 C  CG2   . VAL B 1 266 ? 66.242  63.247  99.608  1.00 59.44  ? 293 VAL B CG2   1 
ATOM   6440 N  N     . PRO B 1 267 ? 67.443  58.793  100.619 1.00 59.67  ? 294 PRO B N     1 
ATOM   6441 C  CA    . PRO B 1 267 ? 67.656  57.595  101.441 1.00 54.59  ? 294 PRO B CA    1 
ATOM   6442 C  C     . PRO B 1 267 ? 67.744  57.927  102.922 1.00 60.50  ? 294 PRO B C     1 
ATOM   6443 O  O     . PRO B 1 267 ? 68.304  58.951  103.321 1.00 60.11  ? 294 PRO B O     1 
ATOM   6444 C  CB    . PRO B 1 267 ? 68.982  57.037  100.913 1.00 44.79  ? 294 PRO B CB    1 
ATOM   6445 C  CG    . PRO B 1 267 ? 69.066  57.542  99.517  1.00 50.17  ? 294 PRO B CG    1 
ATOM   6446 C  CD    . PRO B 1 267 ? 68.447  58.909  99.549  1.00 48.13  ? 294 PRO B CD    1 
ATOM   6447 N  N     . LEU B 1 268 ? 67.181  57.040  103.734 1.00 59.12  ? 295 LEU B N     1 
ATOM   6448 C  CA    . LEU B 1 268 ? 67.147  57.222  105.172 1.00 56.89  ? 295 LEU B CA    1 
ATOM   6449 C  C     . LEU B 1 268 ? 68.424  56.686  105.810 1.00 58.28  ? 295 LEU B C     1 
ATOM   6450 O  O     . LEU B 1 268 ? 69.344  56.217  105.137 1.00 59.60  ? 295 LEU B O     1 
ATOM   6451 C  CB    . LEU B 1 268 ? 65.917  56.539  105.758 1.00 59.41  ? 295 LEU B CB    1 
ATOM   6452 C  CG    . LEU B 1 268 ? 64.575  57.131  105.342 1.00 55.90  ? 295 LEU B CG    1 
ATOM   6453 C  CD1   . LEU B 1 268 ? 63.467  56.234  105.830 1.00 64.97  ? 295 LEU B CD1   1 
ATOM   6454 C  CD2   . LEU B 1 268 ? 64.413  58.537  105.899 1.00 55.36  ? 295 LEU B CD2   1 
ATOM   6455 N  N     . ARG B 1 269 ? 68.476  56.754  107.134 1.00 63.21  ? 296 ARG B N     1 
ATOM   6456 C  CA    . ARG B 1 269 ? 69.612  56.262  107.893 1.00 64.78  ? 296 ARG B CA    1 
ATOM   6457 C  C     . ARG B 1 269 ? 69.377  54.815  108.320 1.00 63.81  ? 296 ARG B C     1 
ATOM   6458 O  O     . ARG B 1 269 ? 68.264  54.287  108.242 1.00 73.40  ? 296 ARG B O     1 
ATOM   6459 C  CB    . ARG B 1 269 ? 69.860  57.162  109.102 1.00 81.53  ? 296 ARG B CB    1 
ATOM   6460 C  CG    . ARG B 1 269 ? 69.947  58.636  108.736 1.00 75.52  ? 296 ARG B CG    1 
ATOM   6461 C  CD    . ARG B 1 269 ? 70.199  59.512  109.949 1.00 104.94 ? 296 ARG B CD    1 
ATOM   6462 N  NE    . ARG B 1 269 ? 70.491  60.888  109.563 1.00 123.71 ? 296 ARG B NE    1 
ATOM   6463 C  CZ    . ARG B 1 269 ? 70.816  61.851  110.415 1.00 129.59 ? 296 ARG B CZ    1 
ATOM   6464 N  NH1   . ARG B 1 269 ? 70.893  61.627  111.717 1.00 125.53 ? 296 ARG B NH1   1 
ATOM   6465 N  NH2   . ARG B 1 269 ? 71.072  63.071  109.948 1.00 119.33 ? 296 ARG B NH2   1 
ATOM   6466 N  N     . ALA B 1 270 ? 70.454  54.171  108.777 1.00 56.31  ? 297 ALA B N     1 
ATOM   6467 C  CA    . ALA B 1 270 ? 70.388  52.748  109.092 1.00 69.56  ? 297 ALA B CA    1 
ATOM   6468 C  C     . ALA B 1 270 ? 69.379  52.449  110.195 1.00 68.19  ? 297 ALA B C     1 
ATOM   6469 O  O     . ALA B 1 270 ? 68.731  51.395  110.172 1.00 52.82  ? 297 ALA B O     1 
ATOM   6470 C  CB    . ALA B 1 270 ? 71.776  52.241  109.484 1.00 54.38  ? 297 ALA B CB    1 
ATOM   6471 N  N     . HIS B 1 271 ? 69.224  53.355  111.160 1.00 71.73  ? 298 HIS B N     1 
ATOM   6472 C  CA    . HIS B 1 271 ? 68.310  53.161  112.276 1.00 55.74  ? 298 HIS B CA    1 
ATOM   6473 C  C     . HIS B 1 271 ? 66.951  53.813  112.041 1.00 63.02  ? 298 HIS B C     1 
ATOM   6474 O  O     . HIS B 1 271 ? 66.219  54.073  113.002 1.00 69.48  ? 298 HIS B O     1 
ATOM   6475 C  CB    . HIS B 1 271 ? 68.943  53.681  113.567 1.00 78.77  ? 298 HIS B CB    1 
ATOM   6476 C  CG    . HIS B 1 271 ? 70.072  52.831  114.059 1.00 92.38  ? 298 HIS B CG    1 
ATOM   6477 N  ND1   . HIS B 1 271 ? 70.990  53.269  114.988 1.00 87.08  ? 298 HIS B ND1   1 
ATOM   6478 C  CD2   . HIS B 1 271 ? 70.432  51.565  113.745 1.00 57.73  ? 298 HIS B CD2   1 
ATOM   6479 C  CE1   . HIS B 1 271 ? 71.864  52.309  115.230 1.00 92.10  ? 298 HIS B CE1   1 
ATOM   6480 N  NE2   . HIS B 1 271 ? 71.549  51.264  114.487 1.00 80.10  ? 298 HIS B NE2   1 
ATOM   6481 N  N     . SER B 1 272 ? 66.599  54.077  110.784 1.00 55.18  ? 299 SER B N     1 
ATOM   6482 C  CA    . SER B 1 272 ? 65.281  54.593  110.456 1.00 57.57  ? 299 SER B CA    1 
ATOM   6483 C  C     . SER B 1 272 ? 64.262  53.456  110.419 1.00 64.24  ? 299 SER B C     1 
ATOM   6484 O  O     . SER B 1 272 ? 64.607  52.271  110.407 1.00 68.90  ? 299 SER B O     1 
ATOM   6485 C  CB    . SER B 1 272 ? 65.311  55.325  109.117 1.00 61.25  ? 299 SER B CB    1 
ATOM   6486 O  OG    . SER B 1 272 ? 66.316  56.323  109.112 1.00 69.37  ? 299 SER B OG    1 
ATOM   6487 N  N     . THR B 1 273 ? 62.989  53.830  110.401 1.00 61.98  ? 300 THR B N     1 
ATOM   6488 C  CA    . THR B 1 273 ? 61.886  52.883  110.450 1.00 61.49  ? 300 THR B CA    1 
ATOM   6489 C  C     . THR B 1 273 ? 61.205  52.789  109.090 1.00 57.33  ? 300 THR B C     1 
ATOM   6490 O  O     . THR B 1 273 ? 61.449  53.591  108.185 1.00 70.47  ? 300 THR B O     1 
ATOM   6491 C  CB    . THR B 1 273 ? 60.867  53.286  111.521 1.00 50.21  ? 300 THR B CB    1 
ATOM   6492 O  OG1   . THR B 1 273 ? 60.111  54.414  111.063 1.00 58.23  ? 300 THR B OG1   1 
ATOM   6493 C  CG2   . THR B 1 273 ? 61.579  53.652  112.814 1.00 52.14  ? 300 THR B CG2   1 
ATOM   6494 N  N     . LEU B 1 274 ? 60.346  51.777  108.954 1.00 55.33  ? 301 LEU B N     1 
ATOM   6495 C  CA    . LEU B 1 274 ? 59.543  51.656  107.742 1.00 49.52  ? 301 LEU B CA    1 
ATOM   6496 C  C     . LEU B 1 274 ? 58.574  52.822  107.614 1.00 58.06  ? 301 LEU B C     1 
ATOM   6497 O  O     . LEU B 1 274 ? 58.335  53.323  106.508 1.00 53.40  ? 301 LEU B O     1 
ATOM   6498 C  CB    . LEU B 1 274 ? 58.791  50.325  107.738 1.00 45.01  ? 301 LEU B CB    1 
ATOM   6499 C  CG    . LEU B 1 274 ? 59.650  49.065  107.614 1.00 64.36  ? 301 LEU B CG    1 
ATOM   6500 C  CD1   . LEU B 1 274 ? 58.770  47.838  107.455 1.00 62.84  ? 301 LEU B CD1   1 
ATOM   6501 C  CD2   . LEU B 1 274 ? 60.617  49.190  106.449 1.00 57.44  ? 301 LEU B CD2   1 
ATOM   6502 N  N     . GLN B 1 275 ? 58.009  53.271  108.739 1.00 60.96  ? 302 GLN B N     1 
ATOM   6503 C  CA    . GLN B 1 275 ? 57.134  54.439  108.719 1.00 55.73  ? 302 GLN B CA    1 
ATOM   6504 C  C     . GLN B 1 275 ? 57.876  55.674  108.227 1.00 66.85  ? 302 GLN B C     1 
ATOM   6505 O  O     . GLN B 1 275 ? 57.309  56.500  107.501 1.00 64.40  ? 302 GLN B O     1 
ATOM   6506 C  CB    . GLN B 1 275 ? 56.553  54.683  110.110 1.00 48.91  ? 302 GLN B CB    1 
ATOM   6507 C  CG    . GLN B 1 275 ? 55.673  55.917  110.205 1.00 53.93  ? 302 GLN B CG    1 
ATOM   6508 C  CD    . GLN B 1 275 ? 55.348  56.292  111.635 1.00 62.53  ? 302 GLN B CD    1 
ATOM   6509 O  OE1   . GLN B 1 275 ? 55.741  55.601  112.576 1.00 79.99  ? 302 GLN B OE1   1 
ATOM   6510 N  NE2   . GLN B 1 275 ? 54.631  57.396  111.808 1.00 73.84  ? 302 GLN B NE2   1 
ATOM   6511 N  N     . ASP B 1 276 ? 59.145  55.821  108.619 1.00 58.72  ? 303 ASP B N     1 
ATOM   6512 C  CA    . ASP B 1 276 ? 59.969  56.899  108.082 1.00 59.15  ? 303 ASP B CA    1 
ATOM   6513 C  C     . ASP B 1 276 ? 60.021  56.836  106.560 1.00 58.36  ? 303 ASP B C     1 
ATOM   6514 O  O     . ASP B 1 276 ? 59.877  57.856  105.877 1.00 61.95  ? 303 ASP B O     1 
ATOM   6515 C  CB    . ASP B 1 276 ? 61.381  56.828  108.668 1.00 59.21  ? 303 ASP B CB    1 
ATOM   6516 C  CG    . ASP B 1 276 ? 61.418  57.124  110.153 1.00 62.76  ? 303 ASP B CG    1 
ATOM   6517 O  OD1   . ASP B 1 276 ? 60.353  57.423  110.733 1.00 87.66  ? 303 ASP B OD1   1 
ATOM   6518 O  OD2   . ASP B 1 276 ? 62.518  57.058  110.742 1.00 65.56  ? 303 ASP B OD2   1 
ATOM   6519 N  N     . GLU B 1 277 ? 60.215  55.633  106.011 1.00 66.36  ? 304 GLU B N     1 
ATOM   6520 C  CA    . GLU B 1 277 ? 60.256  55.477  104.561 1.00 55.19  ? 304 GLU B CA    1 
ATOM   6521 C  C     . GLU B 1 277 ? 58.897  55.759  103.935 1.00 50.03  ? 304 GLU B C     1 
ATOM   6522 O  O     . GLU B 1 277 ? 58.814  56.412  102.888 1.00 56.57  ? 304 GLU B O     1 
ATOM   6523 C  CB    . GLU B 1 277 ? 60.730  54.071  104.200 1.00 55.62  ? 304 GLU B CB    1 
ATOM   6524 C  CG    . GLU B 1 277 ? 60.895  53.845  102.708 1.00 67.13  ? 304 GLU B CG    1 
ATOM   6525 C  CD    . GLU B 1 277 ? 62.025  54.664  102.119 1.00 69.77  ? 304 GLU B CD    1 
ATOM   6526 O  OE1   . GLU B 1 277 ? 63.146  54.607  102.666 1.00 71.62  ? 304 GLU B OE1   1 
ATOM   6527 O  OE2   . GLU B 1 277 ? 61.792  55.370  101.114 1.00 68.45  ? 304 GLU B OE2   1 
ATOM   6528 N  N     . ALA B 1 278 ? 57.822  55.276  104.562 1.00 58.39  ? 305 ALA B N     1 
ATOM   6529 C  CA    . ALA B 1 278 ? 56.484  55.499  104.024 1.00 52.07  ? 305 ALA B CA    1 
ATOM   6530 C  C     . ALA B 1 278 ? 56.167  56.987  103.939 1.00 61.23  ? 305 ALA B C     1 
ATOM   6531 O  O     . ALA B 1 278 ? 55.688  57.475  102.909 1.00 48.74  ? 305 ALA B O     1 
ATOM   6532 C  CB    . ALA B 1 278 ? 55.450  54.771  104.882 1.00 43.24  ? 305 ALA B CB    1 
ATOM   6533 N  N     . GLU B 1 279 ? 56.433  57.727  105.018 1.00 52.90  ? 306 GLU B N     1 
ATOM   6534 C  CA    . GLU B 1 279 ? 56.201  59.166  104.990 1.00 55.99  ? 306 GLU B CA    1 
ATOM   6535 C  C     . GLU B 1 279 ? 57.170  59.874  104.052 1.00 57.05  ? 306 GLU B C     1 
ATOM   6536 O  O     . GLU B 1 279 ? 56.823  60.909  103.474 1.00 59.41  ? 306 GLU B O     1 
ATOM   6537 C  CB    . GLU B 1 279 ? 56.302  59.743  106.401 1.00 46.77  ? 306 GLU B CB    1 
ATOM   6538 C  CG    . GLU B 1 279 ? 55.147  59.343  107.309 1.00 52.28  ? 306 GLU B CG    1 
ATOM   6539 C  CD    . GLU B 1 279 ? 55.299  59.868  108.723 1.00 64.78  ? 306 GLU B CD    1 
ATOM   6540 O  OE1   . GLU B 1 279 ? 56.091  60.813  108.930 1.00 77.98  ? 306 GLU B OE1   1 
ATOM   6541 O  OE2   . GLU B 1 279 ? 54.627  59.331  109.629 1.00 72.67  ? 306 GLU B OE2   1 
ATOM   6542 N  N     . SER B 1 280 ? 58.378  59.331  103.881 1.00 57.09  ? 307 SER B N     1 
ATOM   6543 C  CA    . SER B 1 280 ? 59.341  59.945  102.972 1.00 47.39  ? 307 SER B CA    1 
ATOM   6544 C  C     . SER B 1 280 ? 58.833  59.910  101.536 1.00 57.21  ? 307 SER B C     1 
ATOM   6545 O  O     . SER B 1 280 ? 58.901  60.915  100.818 1.00 47.91  ? 307 SER B O     1 
ATOM   6546 C  CB    . SER B 1 280 ? 60.696  59.246  103.085 1.00 53.06  ? 307 SER B CB    1 
ATOM   6547 O  OG    . SER B 1 280 ? 61.680  59.929  102.327 1.00 62.44  ? 307 SER B OG    1 
ATOM   6548 N  N     . PHE B 1 281 ? 58.309  58.760  101.099 1.00 53.05  ? 308 PHE B N     1 
ATOM   6549 C  CA    . PHE B 1 281 ? 57.757  58.688  99.750  1.00 59.60  ? 308 PHE B CA    1 
ATOM   6550 C  C     . PHE B 1 281 ? 56.469  59.489  99.628  1.00 50.11  ? 308 PHE B C     1 
ATOM   6551 O  O     . PHE B 1 281 ? 56.168  60.012  98.548  1.00 55.37  ? 308 PHE B O     1 
ATOM   6552 C  CB    . PHE B 1 281 ? 57.505  57.238  99.337  1.00 52.06  ? 308 PHE B CB    1 
ATOM   6553 C  CG    . PHE B 1 281 ? 56.978  57.100  97.935  1.00 58.30  ? 308 PHE B CG    1 
ATOM   6554 C  CD1   . PHE B 1 281 ? 57.845  57.102  96.855  1.00 48.07  ? 308 PHE B CD1   1 
ATOM   6555 C  CD2   . PHE B 1 281 ? 55.616  56.992  97.695  1.00 46.53  ? 308 PHE B CD2   1 
ATOM   6556 C  CE1   . PHE B 1 281 ? 57.368  56.988  95.563  1.00 46.48  ? 308 PHE B CE1   1 
ATOM   6557 C  CE2   . PHE B 1 281 ? 55.131  56.879  96.405  1.00 44.17  ? 308 PHE B CE2   1 
ATOM   6558 C  CZ    . PHE B 1 281 ? 56.009  56.876  95.338  1.00 57.62  ? 308 PHE B CZ    1 
ATOM   6559 N  N     . MET B 1 282 ? 55.688  59.578  100.706 1.00 49.46  ? 309 MET B N     1 
ATOM   6560 C  CA    . MET B 1 282 ? 54.514  60.443  100.686 1.00 49.74  ? 309 MET B CA    1 
ATOM   6561 C  C     . MET B 1 282 ? 54.913  61.889  100.427 1.00 57.14  ? 309 MET B C     1 
ATOM   6562 O  O     . MET B 1 282 ? 54.221  62.614  99.702  1.00 59.94  ? 309 MET B O     1 
ATOM   6563 C  CB    . MET B 1 282 ? 53.744  60.315  102.001 1.00 43.46  ? 309 MET B CB    1 
ATOM   6564 C  CG    . MET B 1 282 ? 52.555  61.260  102.142 1.00 55.17  ? 309 MET B CG    1 
ATOM   6565 S  SD    . MET B 1 282 ? 52.985  62.827  102.927 1.00 65.22  ? 309 MET B SD    1 
ATOM   6566 C  CE    . MET B 1 282 ? 53.840  62.239  104.387 1.00 69.35  ? 309 MET B CE    1 
ATOM   6567 N  N     . HIS B 1 283 ? 56.035  62.324  101.008 1.00 52.84  ? 310 HIS B N     1 
ATOM   6568 C  CA    . HIS B 1 283 ? 56.530  63.668  100.738 1.00 52.61  ? 310 HIS B CA    1 
ATOM   6569 C  C     . HIS B 1 283 ? 56.962  63.820  99.287  1.00 56.17  ? 310 HIS B C     1 
ATOM   6570 O  O     . HIS B 1 283 ? 56.896  64.922  98.732  1.00 55.31  ? 310 HIS B O     1 
ATOM   6571 C  CB    . HIS B 1 283 ? 57.691  64.002  101.674 1.00 48.91  ? 310 HIS B CB    1 
ATOM   6572 C  CG    . HIS B 1 283 ? 58.179  65.411  101.549 1.00 48.51  ? 310 HIS B CG    1 
ATOM   6573 N  ND1   . HIS B 1 283 ? 59.314  65.747  100.843 1.00 56.23  ? 310 HIS B ND1   1 
ATOM   6574 C  CD2   . HIS B 1 283 ? 57.682  66.572  102.036 1.00 55.27  ? 310 HIS B CD2   1 
ATOM   6575 C  CE1   . HIS B 1 283 ? 59.498  67.054  100.904 1.00 57.21  ? 310 HIS B CE1   1 
ATOM   6576 N  NE2   . HIS B 1 283 ? 58.521  67.578  101.622 1.00 60.80  ? 310 HIS B NE2   1 
ATOM   6577 N  N     . VAL B 1 284 ? 57.411  62.731  98.660  1.00 51.97  ? 311 VAL B N     1 
ATOM   6578 C  CA    . VAL B 1 284 ? 57.709  62.772  97.232  1.00 49.53  ? 311 VAL B CA    1 
ATOM   6579 C  C     . VAL B 1 284 ? 56.447  63.087  96.441  1.00 53.37  ? 311 VAL B C     1 
ATOM   6580 O  O     . VAL B 1 284 ? 56.468  63.889  95.500  1.00 46.40  ? 311 VAL B O     1 
ATOM   6581 C  CB    . VAL B 1 284 ? 58.344  61.445  96.779  1.00 54.64  ? 311 VAL B CB    1 
ATOM   6582 C  CG1   . VAL B 1 284 ? 58.652  61.481  95.294  1.00 49.46  ? 311 VAL B CG1   1 
ATOM   6583 C  CG2   . VAL B 1 284 ? 59.598  61.159  97.583  1.00 62.06  ? 311 VAL B CG2   1 
ATOM   6584 N  N     . GLN B 1 285 ? 55.327  62.463  96.813  1.00 48.84  ? 312 GLN B N     1 
ATOM   6585 C  CA    . GLN B 1 285 ? 54.059  62.761  96.156  1.00 47.33  ? 312 GLN B CA    1 
ATOM   6586 C  C     . GLN B 1 285 ? 53.658  64.214  96.373  1.00 56.22  ? 312 GLN B C     1 
ATOM   6587 O  O     . GLN B 1 285 ? 53.129  64.862  95.462  1.00 62.53  ? 312 GLN B O     1 
ATOM   6588 C  CB    . GLN B 1 285 ? 52.973  61.815  96.669  1.00 42.59  ? 312 GLN B CB    1 
ATOM   6589 C  CG    . GLN B 1 285 ? 53.273  60.346  96.414  1.00 48.16  ? 312 GLN B CG    1 
ATOM   6590 C  CD    . GLN B 1 285 ? 52.353  59.417  97.183  1.00 56.56  ? 312 GLN B CD    1 
ATOM   6591 O  OE1   . GLN B 1 285 ? 52.197  59.544  98.397  1.00 65.54  ? 312 GLN B OE1   1 
ATOM   6592 N  NE2   . GLN B 1 285 ? 51.740  58.473  96.477  1.00 46.87  ? 312 GLN B NE2   1 
ATOM   6593 N  N     . LEU B 1 286 ? 53.903  64.742  97.575  1.00 53.17  ? 313 LEU B N     1 
ATOM   6594 C  CA    . LEU B 1 286 ? 53.639  66.153  97.838  1.00 54.58  ? 313 LEU B CA    1 
ATOM   6595 C  C     . LEU B 1 286 ? 54.467  67.043  96.920  1.00 52.54  ? 313 LEU B C     1 
ATOM   6596 O  O     . LEU B 1 286 ? 53.956  68.012  96.347  1.00 55.70  ? 313 LEU B O     1 
ATOM   6597 C  CB    . LEU B 1 286 ? 53.932  66.478  99.304  1.00 48.69  ? 313 LEU B CB    1 
ATOM   6598 C  CG    . LEU B 1 286 ? 53.045  65.857  100.385 1.00 53.59  ? 313 LEU B CG    1 
ATOM   6599 C  CD1   . LEU B 1 286 ? 53.500  66.317  101.761 1.00 47.75  ? 313 LEU B CD1   1 
ATOM   6600 C  CD2   . LEU B 1 286 ? 51.590  66.217  100.160 1.00 50.98  ? 313 LEU B CD2   1 
ATOM   6601 N  N     . GLU B 1 287 ? 55.756  66.726  96.770  1.00 50.93  ? 314 GLU B N     1 
ATOM   6602 C  CA    . GLU B 1 287 ? 56.620  67.517  95.899  1.00 56.17  ? 314 GLU B CA    1 
ATOM   6603 C  C     . GLU B 1 287 ? 56.128  67.484  94.458  1.00 60.97  ? 314 GLU B C     1 
ATOM   6604 O  O     . GLU B 1 287 ? 56.202  68.492  93.745  1.00 65.67  ? 314 GLU B O     1 
ATOM   6605 C  CB    . GLU B 1 287 ? 58.058  67.009  95.992  1.00 50.76  ? 314 GLU B CB    1 
ATOM   6606 C  CG    . GLU B 1 287 ? 58.689  67.210  97.358  1.00 53.38  ? 314 GLU B CG    1 
ATOM   6607 C  CD    . GLU B 1 287 ? 58.750  68.671  97.758  1.00 63.75  ? 314 GLU B CD    1 
ATOM   6608 O  OE1   . GLU B 1 287 ? 59.530  69.425  97.138  1.00 68.55  ? 314 GLU B OE1   1 
ATOM   6609 O  OE2   . GLU B 1 287 ? 58.011  69.069  98.684  1.00 80.60  ? 314 GLU B OE2   1 
ATOM   6610 N  N     . VAL B 1 288 ? 55.624  66.332  94.014  1.00 60.12  ? 315 VAL B N     1 
ATOM   6611 C  CA    . VAL B 1 288 ? 55.049  66.231  92.676  1.00 47.12  ? 315 VAL B CA    1 
ATOM   6612 C  C     . VAL B 1 288 ? 53.874  67.188  92.533  1.00 59.04  ? 315 VAL B C     1 
ATOM   6613 O  O     . VAL B 1 288 ? 53.753  67.911  91.536  1.00 61.97  ? 315 VAL B O     1 
ATOM   6614 C  CB    . VAL B 1 288 ? 54.627  64.781  92.382  1.00 52.30  ? 315 VAL B CB    1 
ATOM   6615 C  CG1   . VAL B 1 288 ? 53.708  64.730  91.174  1.00 53.26  ? 315 VAL B CG1   1 
ATOM   6616 C  CG2   . VAL B 1 288 ? 55.846  63.902  92.169  1.00 40.35  ? 315 VAL B CG2   1 
ATOM   6617 N  N     . MET B 1 289 ? 52.994  67.215  93.536  1.00 56.06  ? 316 MET B N     1 
ATOM   6618 C  CA    . MET B 1 289 ? 51.771  68.003  93.452  1.00 55.29  ? 316 MET B CA    1 
ATOM   6619 C  C     . MET B 1 289 ? 52.011  69.504  93.563  1.00 55.66  ? 316 MET B C     1 
ATOM   6620 O  O     . MET B 1 289 ? 51.054  70.271  93.416  1.00 53.61  ? 316 MET B O     1 
ATOM   6621 C  CB    . MET B 1 289 ? 50.785  67.552  94.532  1.00 45.62  ? 316 MET B CB    1 
ATOM   6622 C  CG    . MET B 1 289 ? 50.309  66.118  94.370  1.00 54.73  ? 316 MET B CG    1 
ATOM   6623 S  SD    . MET B 1 289 ? 48.973  65.696  95.499  1.00 75.66  ? 316 MET B SD    1 
ATOM   6624 C  CE    . MET B 1 289 ? 49.790  65.929  97.072  1.00 71.05  ? 316 MET B CE    1 
ATOM   6625 N  N     . VAL B 1 290 ? 53.249  69.944  93.807  1.00 61.47  ? 317 VAL B N     1 
ATOM   6626 C  CA    . VAL B 1 290 ? 53.530  71.378  93.846  1.00 62.02  ? 317 VAL B CA    1 
ATOM   6627 C  C     . VAL B 1 290 ? 53.281  72.001  92.477  1.00 62.45  ? 317 VAL B C     1 
ATOM   6628 O  O     . VAL B 1 290 ? 52.552  72.992  92.348  1.00 81.10  ? 317 VAL B O     1 
ATOM   6629 C  CB    . VAL B 1 290 ? 54.969  71.634  94.331  1.00 69.82  ? 317 VAL B CB    1 
ATOM   6630 C  CG1   . VAL B 1 290 ? 55.329  73.107  94.197  1.00 60.71  ? 317 VAL B CG1   1 
ATOM   6631 C  CG2   . VAL B 1 290 ? 55.129  71.176  95.772  1.00 70.21  ? 317 VAL B CG2   1 
ATOM   6632 N  N     . LYS B 1 291 ? 53.866  71.415  91.432  1.00 68.16  ? 318 LYS B N     1 
ATOM   6633 C  CA    . LYS B 1 291 ? 53.768  71.950  90.082  1.00 66.44  ? 318 LYS B CA    1 
ATOM   6634 C  C     . LYS B 1 291 ? 53.119  70.991  89.092  1.00 58.18  ? 318 LYS B C     1 
ATOM   6635 O  O     . LYS B 1 291 ? 52.906  71.371  87.935  1.00 65.25  ? 318 LYS B O     1 
ATOM   6636 C  CB    . LYS B 1 291 ? 55.158  72.355  89.574  1.00 77.83  ? 318 LYS B CB    1 
ATOM   6637 C  CG    . LYS B 1 291 ? 55.782  73.510  90.344  1.00 91.29  ? 318 LYS B CG    1 
ATOM   6638 C  CD    . LYS B 1 291 ? 57.184  73.831  89.844  1.00 102.96 ? 318 LYS B CD    1 
ATOM   6639 C  CE    . LYS B 1 291 ? 57.811  74.965  90.640  1.00 104.22 ? 318 LYS B CE    1 
ATOM   6640 N  NZ    . LYS B 1 291 ? 59.209  75.239  90.209  1.00 90.07  ? 318 LYS B NZ    1 
ATOM   6641 N  N     . HIS B 1 292 ? 52.796  69.768  89.503  1.00 56.16  ? 319 HIS B N     1 
ATOM   6642 C  CA    . HIS B 1 292 ? 52.156  68.811  88.610  1.00 58.01  ? 319 HIS B CA    1 
ATOM   6643 C  C     . HIS B 1 292 ? 50.834  68.346  89.209  1.00 57.64  ? 319 HIS B C     1 
ATOM   6644 O  O     . HIS B 1 292 ? 50.570  68.591  90.393  1.00 59.04  ? 319 HIS B O     1 
ATOM   6645 C  CB    . HIS B 1 292 ? 53.065  67.605  88.359  1.00 53.90  ? 319 HIS B CB    1 
ATOM   6646 C  CG    . HIS B 1 292 ? 54.475  67.967  88.010  1.00 63.79  ? 319 HIS B CG    1 
ATOM   6647 N  ND1   . HIS B 1 292 ? 55.412  68.310  88.961  1.00 75.28  ? 319 HIS B ND1   1 
ATOM   6648 C  CD2   . HIS B 1 292 ? 55.109  68.030  86.816  1.00 54.57  ? 319 HIS B CD2   1 
ATOM   6649 C  CE1   . HIS B 1 292 ? 56.562  68.574  88.367  1.00 63.73  ? 319 HIS B CE1   1 
ATOM   6650 N  NE2   . HIS B 1 292 ? 56.405  68.412  87.065  1.00 64.31  ? 319 HIS B NE2   1 
ATOM   6651 N  N     . PRO B 1 293 ? 49.976  67.692  88.432  1.00 51.69  ? 320 PRO B N     1 
ATOM   6652 C  CA    . PRO B 1 293 ? 48.854  66.960  89.022  1.00 45.60  ? 320 PRO B CA    1 
ATOM   6653 C  C     . PRO B 1 293 ? 49.365  65.805  89.862  1.00 53.75  ? 320 PRO B C     1 
ATOM   6654 O  O     . PRO B 1 293 ? 50.521  65.383  89.707  1.00 59.00  ? 320 PRO B O     1 
ATOM   6655 C  CB    . PRO B 1 293 ? 48.074  66.457  87.796  1.00 43.07  ? 320 PRO B CB    1 
ATOM   6656 C  CG    . PRO B 1 293 ? 48.455  67.382  86.704  1.00 46.79  ? 320 PRO B CG    1 
ATOM   6657 C  CD    . PRO B 1 293 ? 49.885  67.746  86.963  1.00 46.42  ? 320 PRO B CD    1 
ATOM   6658 N  N     . PRO B 1 294 ? 48.546  65.269  90.765  1.00 61.20  ? 321 PRO B N     1 
ATOM   6659 C  CA    . PRO B 1 294 ? 49.004  64.143  91.586  1.00 50.12  ? 321 PRO B CA    1 
ATOM   6660 C  C     . PRO B 1 294 ? 49.331  62.931  90.727  1.00 53.37  ? 321 PRO B C     1 
ATOM   6661 O  O     . PRO B 1 294 ? 48.617  62.610  89.775  1.00 48.85  ? 321 PRO B O     1 
ATOM   6662 C  CB    . PRO B 1 294 ? 47.814  63.874  92.515  1.00 42.47  ? 321 PRO B CB    1 
ATOM   6663 C  CG    . PRO B 1 294 ? 46.637  64.468  91.815  1.00 50.46  ? 321 PRO B CG    1 
ATOM   6664 C  CD    . PRO B 1 294 ? 47.170  65.671  91.100  1.00 60.42  ? 321 PRO B CD    1 
ATOM   6665 N  N     . ALA B 1 295 ? 50.433  62.266  91.068  1.00 49.60  ? 322 ALA B N     1 
ATOM   6666 C  CA    . ALA B 1 295 ? 50.858  61.074  90.346  1.00 40.48  ? 322 ALA B CA    1 
ATOM   6667 C  C     . ALA B 1 295 ? 49.833  59.965  90.548  1.00 43.75  ? 322 ALA B C     1 
ATOM   6668 O  O     . ALA B 1 295 ? 49.617  59.504  91.674  1.00 50.61  ? 322 ALA B O     1 
ATOM   6669 C  CB    . ALA B 1 295 ? 52.242  60.634  90.819  1.00 46.82  ? 322 ALA B CB    1 
ATOM   6670 N  N     . GLU B 1 296 ? 49.208  59.536  89.458  1.00 46.19  ? 323 GLU B N     1 
ATOM   6671 C  CA    . GLU B 1 296 ? 48.095  58.608  89.527  1.00 53.73  ? 323 GLU B CA    1 
ATOM   6672 C  C     . GLU B 1 296 ? 48.576  57.188  89.815  1.00 60.46  ? 323 GLU B C     1 
ATOM   6673 O  O     . GLU B 1 296 ? 49.669  56.795  89.399  1.00 50.19  ? 323 GLU B O     1 
ATOM   6674 C  CB    . GLU B 1 296 ? 47.308  58.631  88.222  1.00 52.07  ? 323 GLU B CB    1 
ATOM   6675 C  CG    . GLU B 1 296 ? 46.614  59.955  87.958  1.00 83.08  ? 323 GLU B CG    1 
ATOM   6676 C  CD    . GLU B 1 296 ? 45.641  60.329  89.059  1.00 91.37  ? 323 GLU B CD    1 
ATOM   6677 O  OE1   . GLU B 1 296 ? 44.777  59.491  89.401  1.00 94.10  ? 323 GLU B OE1   1 
ATOM   6678 O  OE2   . GLU B 1 296 ? 45.745  61.458  89.586  1.00 83.53  ? 323 GLU B OE2   1 
ATOM   6679 N  N     . PRO B 1 297 ? 47.777  56.403  90.523  1.00 55.39  ? 324 PRO B N     1 
ATOM   6680 C  CA    . PRO B 1 297 ? 48.156  55.024  90.834  1.00 48.14  ? 324 PRO B CA    1 
ATOM   6681 C  C     . PRO B 1 297 ? 47.893  54.106  89.646  1.00 55.97  ? 324 PRO B C     1 
ATOM   6682 O  O     . PRO B 1 297 ? 47.436  54.524  88.582  1.00 59.79  ? 324 PRO B O     1 
ATOM   6683 C  CB    . PRO B 1 297 ? 47.254  54.679  92.017  1.00 46.54  ? 324 PRO B CB    1 
ATOM   6684 C  CG    . PRO B 1 297 ? 46.030  55.489  91.777  1.00 45.07  ? 324 PRO B CG    1 
ATOM   6685 C  CD    . PRO B 1 297 ? 46.503  56.778  91.159  1.00 49.22  ? 324 PRO B CD    1 
ATOM   6686 N  N     . SER B 1 298 ? 48.191  52.829  89.852  1.00 54.39  ? 325 SER B N     1 
ATOM   6687 C  CA    . SER B 1 298 ? 47.935  51.826  88.834  1.00 57.55  ? 325 SER B CA    1 
ATOM   6688 C  C     . SER B 1 298 ? 46.441  51.553  88.713  1.00 58.05  ? 325 SER B C     1 
ATOM   6689 O  O     . SER B 1 298 ? 45.674  51.709  89.668  1.00 66.04  ? 325 SER B O     1 
ATOM   6690 C  CB    . SER B 1 298 ? 48.674  50.532  89.170  1.00 51.16  ? 325 SER B CB    1 
ATOM   6691 O  OG    . SER B 1 298 ? 48.128  49.442  88.454  1.00 61.89  ? 325 SER B OG    1 
ATOM   6692 N  N     . ARG B 1 299 ? 46.032  51.146  87.512  1.00 59.77  ? 326 ARG B N     1 
ATOM   6693 C  CA    . ARG B 1 299 ? 44.654  50.730  87.286  1.00 62.50  ? 326 ARG B CA    1 
ATOM   6694 C  C     . ARG B 1 299 ? 44.308  49.460  88.054  1.00 62.69  ? 326 ARG B C     1 
ATOM   6695 O  O     . ARG B 1 299 ? 43.125  49.192  88.290  1.00 73.22  ? 326 ARG B O     1 
ATOM   6696 C  CB    . ARG B 1 299 ? 44.419  50.525  85.789  1.00 63.34  ? 326 ARG B CB    1 
ATOM   6697 C  CG    . ARG B 1 299 ? 42.988  50.203  85.398  1.00 74.26  ? 326 ARG B CG    1 
ATOM   6698 C  CD    . ARG B 1 299 ? 42.921  49.765  83.949  1.00 88.35  ? 326 ARG B CD    1 
ATOM   6699 N  NE    . ARG B 1 299 ? 43.621  50.703  83.082  1.00 103.36 ? 326 ARG B NE    1 
ATOM   6700 C  CZ    . ARG B 1 299 ? 43.883  50.488  81.800  1.00 103.51 ? 326 ARG B CZ    1 
ATOM   6701 N  NH1   . ARG B 1 299 ? 43.510  49.372  81.196  1.00 101.15 ? 326 ARG B NH1   1 
ATOM   6702 N  NH2   . ARG B 1 299 ? 44.541  51.415  81.109  1.00 87.42  ? 326 ARG B NH2   1 
ATOM   6703 N  N     . PHE B 1 300 ? 45.315  48.686  88.465  1.00 67.75  ? 327 PHE B N     1 
ATOM   6704 C  CA    . PHE B 1 300 ? 45.102  47.401  89.112  1.00 71.93  ? 327 PHE B CA    1 
ATOM   6705 C  C     . PHE B 1 300 ? 45.529  47.370  90.572  1.00 66.28  ? 327 PHE B C     1 
ATOM   6706 O  O     . PHE B 1 300 ? 45.099  46.473  91.302  1.00 66.57  ? 327 PHE B O     1 
ATOM   6707 C  CB    . PHE B 1 300 ? 45.850  46.304  88.343  1.00 56.09  ? 327 PHE B CB    1 
ATOM   6708 C  CG    . PHE B 1 300 ? 45.873  46.522  86.853  1.00 62.38  ? 327 PHE B CG    1 
ATOM   6709 C  CD1   . PHE B 1 300 ? 44.817  46.106  86.060  1.00 55.14  ? 327 PHE B CD1   1 
ATOM   6710 C  CD2   . PHE B 1 300 ? 46.947  47.155  86.249  1.00 66.68  ? 327 PHE B CD2   1 
ATOM   6711 C  CE1   . PHE B 1 300 ? 44.835  46.312  84.691  1.00 62.59  ? 327 PHE B CE1   1 
ATOM   6712 C  CE2   . PHE B 1 300 ? 46.971  47.365  84.882  1.00 63.34  ? 327 PHE B CE2   1 
ATOM   6713 C  CZ    . PHE B 1 300 ? 45.914  46.942  84.102  1.00 61.07  ? 327 PHE B CZ    1 
ATOM   6714 N  N     . ILE B 1 301 ? 46.355  48.315  91.014  1.00 63.10  ? 328 ILE B N     1 
ATOM   6715 C  CA    . ILE B 1 301 ? 46.772  48.425  92.406  1.00 58.90  ? 328 ILE B CA    1 
ATOM   6716 C  C     . ILE B 1 301 ? 46.118  49.661  93.004  1.00 64.99  ? 328 ILE B C     1 
ATOM   6717 O  O     . ILE B 1 301 ? 46.157  50.743  92.405  1.00 65.44  ? 328 ILE B O     1 
ATOM   6718 C  CB    . ILE B 1 301 ? 48.300  48.519  92.544  1.00 56.07  ? 328 ILE B CB    1 
ATOM   6719 C  CG1   . ILE B 1 301 ? 48.987  47.337  91.883  1.00 61.45  ? 328 ILE B CG1   1 
ATOM   6720 C  CG2   . ILE B 1 301 ? 48.695  48.559  94.007  1.00 80.13  ? 328 ILE B CG2   1 
ATOM   6721 C  CD1   . ILE B 1 301 ? 50.475  47.383  92.071  1.00 68.81  ? 328 ILE B CD1   1 
ATOM   6722 N  N     . SER B 1 302 ? 45.540  49.506  94.190  1.00 75.48  ? 329 SER B N     1 
ATOM   6723 C  CA    . SER B 1 302 ? 44.980  50.615  94.946  1.00 73.23  ? 329 SER B CA    1 
ATOM   6724 C  C     . SER B 1 302 ? 45.781  50.812  96.225  1.00 74.46  ? 329 SER B C     1 
ATOM   6725 O  O     . SER B 1 302 ? 46.133  49.842  96.903  1.00 81.58  ? 329 SER B O     1 
ATOM   6726 C  CB    . SER B 1 302 ? 43.508  50.370  95.283  1.00 76.99  ? 329 SER B CB    1 
ATOM   6727 O  OG    . SER B 1 302 ? 42.748  50.149  94.108  1.00 91.27  ? 329 SER B OG    1 
ATOM   6728 N  N     . ALA B 1 303 ? 46.077  52.067  96.540  1.00 84.42  ? 330 ALA B N     1 
ATOM   6729 C  CA    . ALA B 1 303 ? 46.761  52.376  97.783  1.00 87.31  ? 330 ALA B CA    1 
ATOM   6730 C  C     . ALA B 1 303 ? 45.783  52.307  98.955  1.00 79.73  ? 330 ALA B C     1 
ATOM   6731 O  O     . ALA B 1 303 ? 44.590  52.578  98.792  1.00 70.84  ? 330 ALA B O     1 
ATOM   6732 C  CB    . ALA B 1 303 ? 47.393  53.762  97.714  1.00 76.31  ? 330 ALA B CB    1 
ATOM   6733 N  N     . PRO B 1 304 ? 46.260  51.936  100.143 1.00 95.39  ? 331 PRO B N     1 
ATOM   6734 C  CA    . PRO B 1 304 ? 45.358  51.839  101.297 1.00 89.61  ? 331 PRO B CA    1 
ATOM   6735 C  C     . PRO B 1 304 ? 44.734  53.185  101.637 1.00 87.18  ? 331 PRO B C     1 
ATOM   6736 O  O     . PRO B 1 304 ? 45.362  54.237  101.503 1.00 79.56  ? 331 PRO B O     1 
ATOM   6737 C  CB    . PRO B 1 304 ? 46.271  51.338  102.423 1.00 74.37  ? 331 PRO B CB    1 
ATOM   6738 C  CG    . PRO B 1 304 ? 47.658  51.669  101.974 1.00 79.21  ? 331 PRO B CG    1 
ATOM   6739 C  CD    . PRO B 1 304 ? 47.635  51.533  100.484 1.00 87.03  ? 331 PRO B CD    1 
ATOM   6740 N  N     . THR B 1 305 ? 43.478  53.137  102.074 1.00 99.54  ? 332 THR B N     1 
ATOM   6741 C  CA    . THR B 1 305 ? 42.757  54.348  102.437 1.00 93.68  ? 332 THR B CA    1 
ATOM   6742 C  C     . THR B 1 305 ? 43.371  54.981  103.679 1.00 88.56  ? 332 THR B C     1 
ATOM   6743 O  O     . THR B 1 305 ? 43.754  54.289  104.626 1.00 92.96  ? 332 THR B O     1 
ATOM   6744 C  CB    . THR B 1 305 ? 41.280  54.033  102.686 1.00 99.86  ? 332 THR B CB    1 
ATOM   6745 O  OG1   . THR B 1 305 ? 40.716  53.423  101.519 1.00 90.46  ? 332 THR B OG1   1 
ATOM   6746 C  CG2   . THR B 1 305 ? 40.501  55.301  103.015 1.00 89.99  ? 332 THR B CG2   1 
ATOM   6747 N  N     . LYS B 1 306 ? 43.476  56.305  103.666 1.00 84.53  ? 333 LYS B N     1 
ATOM   6748 C  CA    . LYS B 1 306 ? 43.944  57.064  104.814 1.00 91.69  ? 333 LYS B CA    1 
ATOM   6749 C  C     . LYS B 1 306 ? 42.770  57.723  105.528 1.00 76.40  ? 333 LYS B C     1 
ATOM   6750 O  O     . LYS B 1 306 ? 41.687  57.898  104.965 1.00 88.56  ? 333 LYS B O     1 
ATOM   6751 C  CB    . LYS B 1 306 ? 44.970  58.115  104.384 1.00 90.02  ? 333 LYS B CB    1 
ATOM   6752 C  CG    . LYS B 1 306 ? 44.730  58.687  102.999 1.00 71.22  ? 333 LYS B CG    1 
ATOM   6753 C  CD    . LYS B 1 306 ? 45.987  59.348  102.459 1.00 73.88  ? 333 LYS B CD    1 
ATOM   6754 C  CE    . LYS B 1 306 ? 47.170  58.393  102.494 1.00 67.02  ? 333 LYS B CE    1 
ATOM   6755 N  NZ    . LYS B 1 306 ? 48.414  59.013  101.957 1.00 66.60  ? 333 LYS B NZ    1 
ATOM   6756 N  N     . THR B 1 307 ? 42.996  58.077  106.791 1.00 78.49  ? 334 THR B N     1 
ATOM   6757 C  CA    . THR B 1 307 ? 41.975  58.698  107.630 1.00 93.32  ? 334 THR B CA    1 
ATOM   6758 C  C     . THR B 1 307 ? 42.588  59.915  108.311 1.00 75.86  ? 334 THR B C     1 
ATOM   6759 O  O     . THR B 1 307 ? 43.534  59.762  109.111 1.00 81.61  ? 334 THR B O     1 
ATOM   6760 C  CB    . THR B 1 307 ? 41.431  57.707  108.661 1.00 89.62  ? 334 THR B CB    1 
ATOM   6761 O  OG1   . THR B 1 307 ? 42.523  57.081  109.348 1.00 101.09 ? 334 THR B OG1   1 
ATOM   6762 C  CG2   . THR B 1 307 ? 40.589  56.638  107.980 1.00 77.81  ? 334 THR B CG2   1 
ATOM   6763 N  N     . PRO B 1 308 ? 42.101  61.122  108.043 1.00 80.15  ? 335 PRO B N     1 
ATOM   6764 C  CA    . PRO B 1 308 ? 42.745  62.321  108.585 1.00 74.55  ? 335 PRO B CA    1 
ATOM   6765 C  C     . PRO B 1 308 ? 42.295  62.638  110.004 1.00 75.81  ? 335 PRO B C     1 
ATOM   6766 O  O     . PRO B 1 308 ? 41.229  62.224  110.461 1.00 73.82  ? 335 PRO B O     1 
ATOM   6767 C  CB    . PRO B 1 308 ? 42.296  63.418  107.615 1.00 72.68  ? 335 PRO B CB    1 
ATOM   6768 C  CG    . PRO B 1 308 ? 40.944  62.960  107.164 1.00 61.24  ? 335 PRO B CG    1 
ATOM   6769 C  CD    . PRO B 1 308 ? 41.000  61.451  107.119 1.00 73.47  ? 335 PRO B CD    1 
ATOM   6770 N  N     . ASP B 1 309 ? 43.140  63.401  110.700 1.00 77.20  ? 336 ASP B N     1 
ATOM   6771 C  CA    . ASP B 1 309 ? 42.801  63.913  112.024 1.00 68.82  ? 336 ASP B CA    1 
ATOM   6772 C  C     . ASP B 1 309 ? 43.132  65.396  112.133 1.00 76.34  ? 336 ASP B C     1 
ATOM   6773 O  O     . ASP B 1 309 ? 43.497  66.024  111.135 1.00 72.61  ? 336 ASP B O     1 
ATOM   6774 C  CB    . ASP B 1 309 ? 43.533  63.117  113.109 1.00 66.23  ? 336 ASP B CB    1 
ATOM   6775 C  CG    . ASP B 1 309 ? 45.038  63.218  113.002 1.00 80.27  ? 336 ASP B CG    1 
ATOM   6776 O  OD1   . ASP B 1 309 ? 45.543  63.853  112.055 1.00 95.47  ? 336 ASP B OD1   1 
ATOM   6777 O  OD2   . ASP B 1 309 ? 45.725  62.653  113.881 1.00 88.68  ? 336 ASP B OD2   1 
ATOM   6778 N  N     . LYS B 1 310 ? 43.008  65.969  113.328 1.00 82.18  ? 337 LYS B N     1 
ATOM   6779 C  CA    . LYS B 1 310 ? 43.341  67.368  113.550 1.00 68.65  ? 337 LYS B CA    1 
ATOM   6780 C  C     . LYS B 1 310 ? 44.701  67.551  114.217 1.00 72.17  ? 337 LYS B C     1 
ATOM   6781 O  O     . LYS B 1 310 ? 44.986  68.643  114.718 1.00 73.01  ? 337 LYS B O     1 
ATOM   6782 C  CB    . LYS B 1 310 ? 42.252  68.038  114.394 1.00 69.61  ? 337 LYS B CB    1 
ATOM   6783 C  CG    . LYS B 1 310 ? 40.919  68.203  113.680 1.00 63.57  ? 337 LYS B CG    1 
ATOM   6784 C  CD    . LYS B 1 310 ? 41.007  69.244  112.575 1.00 84.69  ? 337 LYS B CD    1 
ATOM   6785 C  CE    . LYS B 1 310 ? 39.685  69.382  111.832 1.00 85.30  ? 337 LYS B CE    1 
ATOM   6786 N  NZ    . LYS B 1 310 ? 38.589  69.858  112.721 1.00 74.17  ? 337 LYS B NZ    1 
ATOM   6787 N  N     . MET B 1 311 ? 45.546  66.515  114.222 1.00 73.58  ? 338 MET B N     1 
ATOM   6788 C  CA    . MET B 1 311 ? 46.880  66.536  114.822 1.00 76.67  ? 338 MET B CA    1 
ATOM   6789 C  C     . MET B 1 311 ? 46.866  66.926  116.295 1.00 76.71  ? 338 MET B C     1 
ATOM   6790 O  O     . MET B 1 311 ? 47.859  67.458  116.805 1.00 78.55  ? 338 MET B O     1 
ATOM   6791 C  CB    . MET B 1 311 ? 47.826  67.473  114.058 1.00 77.21  ? 338 MET B CB    1 
ATOM   6792 C  CG    . MET B 1 311 ? 48.235  66.960  112.696 1.00 72.94  ? 338 MET B CG    1 
ATOM   6793 S  SD    . MET B 1 311 ? 49.299  68.126  111.834 1.00 80.19  ? 338 MET B SD    1 
ATOM   6794 C  CE    . MET B 1 311 ? 48.172  69.498  111.612 1.00 77.87  ? 338 MET B CE    1 
ATOM   6795 N  N     . GLY B 1 312 ? 45.772  66.670  117.006 1.00 70.84  ? 339 GLY B N     1 
ATOM   6796 C  CA    . GLY B 1 312 ? 45.667  67.068  118.392 1.00 58.10  ? 339 GLY B CA    1 
ATOM   6797 C  C     . GLY B 1 312 ? 45.288  68.514  118.619 1.00 74.97  ? 339 GLY B C     1 
ATOM   6798 O  O     . GLY B 1 312 ? 44.956  68.875  119.754 1.00 94.93  ? 339 GLY B O     1 
ATOM   6799 N  N     . PHE B 1 313 ? 45.331  69.355  117.590 1.00 67.86  ? 340 PHE B N     1 
ATOM   6800 C  CA    . PHE B 1 313 ? 44.884  70.731  117.730 1.00 78.94  ? 340 PHE B CA    1 
ATOM   6801 C  C     . PHE B 1 313 ? 43.374  70.782  117.935 1.00 72.99  ? 340 PHE B C     1 
ATOM   6802 O  O     . PHE B 1 313 ? 42.634  69.878  117.538 1.00 76.56  ? 340 PHE B O     1 
ATOM   6803 C  CB    . PHE B 1 313 ? 45.261  71.556  116.500 1.00 66.35  ? 340 PHE B CB    1 
ATOM   6804 C  CG    . PHE B 1 313 ? 46.737  71.766  116.337 1.00 71.95  ? 340 PHE B CG    1 
ATOM   6805 C  CD1   . PHE B 1 313 ? 47.385  72.776  117.029 1.00 71.28  ? 340 PHE B CD1   1 
ATOM   6806 C  CD2   . PHE B 1 313 ? 47.475  70.965  115.483 1.00 73.76  ? 340 PHE B CD2   1 
ATOM   6807 C  CE1   . PHE B 1 313 ? 48.744  72.976  116.879 1.00 71.71  ? 340 PHE B CE1   1 
ATOM   6808 C  CE2   . PHE B 1 313 ? 48.833  71.160  115.327 1.00 70.60  ? 340 PHE B CE2   1 
ATOM   6809 C  CZ    . PHE B 1 313 ? 49.469  72.167  116.026 1.00 69.87  ? 340 PHE B CZ    1 
ATOM   6810 N  N     . ASP B 1 314 ? 42.917  71.865  118.567 1.00 59.17  ? 341 ASP B N     1 
ATOM   6811 C  CA    . ASP B 1 314 ? 41.481  72.058  118.728 1.00 80.42  ? 341 ASP B CA    1 
ATOM   6812 C  C     . ASP B 1 314 ? 40.808  72.333  117.391 1.00 79.34  ? 341 ASP B C     1 
ATOM   6813 O  O     . ASP B 1 314 ? 39.632  72.000  117.210 1.00 86.44  ? 341 ASP B O     1 
ATOM   6814 C  CB    . ASP B 1 314 ? 41.208  73.193  119.713 1.00 78.50  ? 341 ASP B CB    1 
ATOM   6815 C  CG    . ASP B 1 314 ? 41.820  72.939  121.080 1.00 77.09  ? 341 ASP B CG    1 
ATOM   6816 O  OD1   . ASP B 1 314 ? 42.636  72.004  121.207 1.00 86.11  ? 341 ASP B OD1   1 
ATOM   6817 O  OD2   . ASP B 1 314 ? 41.481  73.673  122.030 1.00 110.14 ? 341 ASP B OD2   1 
ATOM   6818 N  N     . GLU B 1 315 ? 41.536  72.923  116.445 1.00 78.75  ? 342 GLU B N     1 
ATOM   6819 C  CA    . GLU B 1 315 ? 41.010  73.175  115.112 1.00 77.70  ? 342 GLU B CA    1 
ATOM   6820 C  C     . GLU B 1 315 ? 42.174  73.453  114.171 1.00 73.13  ? 342 GLU B C     1 
ATOM   6821 O  O     . GLU B 1 315 ? 43.226  73.939  114.593 1.00 70.82  ? 342 GLU B O     1 
ATOM   6822 C  CB    . GLU B 1 315 ? 40.018  74.348  115.114 1.00 65.07  ? 342 GLU B CB    1 
ATOM   6823 C  CG    . GLU B 1 315 ? 39.403  74.686  113.756 1.00 78.42  ? 342 GLU B CG    1 
ATOM   6824 C  CD    . GLU B 1 315 ? 38.593  73.547  113.160 1.00 83.14  ? 342 GLU B CD    1 
ATOM   6825 O  OE1   . GLU B 1 315 ? 39.197  72.576  112.653 1.00 78.09  ? 342 GLU B OE1   1 
ATOM   6826 O  OE2   . GLU B 1 315 ? 37.346  73.625  113.195 1.00 80.32  ? 342 GLU B OE2   1 
ATOM   6827 N  N     . VAL B 1 316 ? 41.977  73.119  112.896 1.00 76.55  ? 343 VAL B N     1 
ATOM   6828 C  CA    . VAL B 1 316 ? 42.939  73.395  111.834 1.00 72.30  ? 343 VAL B CA    1 
ATOM   6829 C  C     . VAL B 1 316 ? 42.217  74.207  110.766 1.00 72.97  ? 343 VAL B C     1 
ATOM   6830 O  O     . VAL B 1 316 ? 41.315  73.694  110.091 1.00 70.59  ? 343 VAL B O     1 
ATOM   6831 C  CB    . VAL B 1 316 ? 43.535  72.110  111.244 1.00 73.56  ? 343 VAL B CB    1 
ATOM   6832 C  CG1   . VAL B 1 316 ? 44.431  72.437  110.057 1.00 62.97  ? 343 VAL B CG1   1 
ATOM   6833 C  CG2   . VAL B 1 316 ? 44.316  71.352  112.306 1.00 55.14  ? 343 VAL B CG2   1 
ATOM   6834 N  N     . PHE B 1 317 ? 42.602  75.471  110.618 1.00 75.07  ? 344 PHE B N     1 
ATOM   6835 C  CA    . PHE B 1 317 ? 42.013  76.359  109.627 1.00 61.67  ? 344 PHE B CA    1 
ATOM   6836 C  C     . PHE B 1 317 ? 42.855  76.376  108.357 1.00 59.47  ? 344 PHE B C     1 
ATOM   6837 O  O     . PHE B 1 317 ? 44.059  76.114  108.383 1.00 64.90  ? 344 PHE B O     1 
ATOM   6838 C  CB    . PHE B 1 317 ? 41.886  77.786  110.166 1.00 62.40  ? 344 PHE B CB    1 
ATOM   6839 C  CG    . PHE B 1 317 ? 40.991  77.912  111.363 1.00 70.22  ? 344 PHE B CG    1 
ATOM   6840 C  CD1   . PHE B 1 317 ? 39.623  78.062  111.211 1.00 69.04  ? 344 PHE B CD1   1 
ATOM   6841 C  CD2   . PHE B 1 317 ? 41.519  77.896  112.642 1.00 79.01  ? 344 PHE B CD2   1 
ATOM   6842 C  CE1   . PHE B 1 317 ? 38.797  78.185  112.313 1.00 70.51  ? 344 PHE B CE1   1 
ATOM   6843 C  CE2   . PHE B 1 317 ? 40.700  78.019  113.750 1.00 81.15  ? 344 PHE B CE2   1 
ATOM   6844 C  CZ    . PHE B 1 317 ? 39.336  78.164  113.585 1.00 77.99  ? 344 PHE B CZ    1 
ATOM   6845 N  N     . MET B 1 318 ? 42.203  76.696  107.240 1.00 66.14  ? 345 MET B N     1 
ATOM   6846 C  CA    . MET B 1 318 ? 42.881  76.898  105.963 1.00 58.70  ? 345 MET B CA    1 
ATOM   6847 C  C     . MET B 1 318 ? 42.172  78.026  105.233 1.00 61.89  ? 345 MET B C     1 
ATOM   6848 O  O     . MET B 1 318 ? 40.993  77.898  104.890 1.00 60.95  ? 345 MET B O     1 
ATOM   6849 C  CB    . MET B 1 318 ? 42.891  75.619  105.119 1.00 67.42  ? 345 MET B CB    1 
ATOM   6850 C  CG    . MET B 1 318 ? 44.115  75.484  104.218 1.00 64.45  ? 345 MET B CG    1 
ATOM   6851 S  SD    . MET B 1 318 ? 43.744  75.633  102.462 1.00 80.75  ? 345 MET B SD    1 
ATOM   6852 C  CE    . MET B 1 318 ? 42.654  74.233  102.226 1.00 59.20  ? 345 MET B CE    1 
ATOM   6853 N  N     . ILE B 1 319 ? 42.883  79.126  105.011 1.00 56.77  ? 346 ILE B N     1 
ATOM   6854 C  CA    . ILE B 1 319 ? 42.318  80.303  104.364 1.00 56.59  ? 346 ILE B CA    1 
ATOM   6855 C  C     . ILE B 1 319 ? 42.456  80.152  102.857 1.00 55.68  ? 346 ILE B C     1 
ATOM   6856 O  O     . ILE B 1 319 ? 43.551  79.888  102.346 1.00 57.24  ? 346 ILE B O     1 
ATOM   6857 C  CB    . ILE B 1 319 ? 43.013  81.583  104.853 1.00 60.25  ? 346 ILE B CB    1 
ATOM   6858 C  CG1   . ILE B 1 319 ? 43.072  81.611  106.379 1.00 60.85  ? 346 ILE B CG1   1 
ATOM   6859 C  CG2   . ILE B 1 319 ? 42.278  82.809  104.345 1.00 59.02  ? 346 ILE B CG2   1 
ATOM   6860 C  CD1   . ILE B 1 319 ? 43.768  82.828  106.934 1.00 55.75  ? 346 ILE B CD1   1 
ATOM   6861 N  N     . ASN B 1 320 ? 41.346  80.320  102.142 1.00 57.85  ? 347 ASN B N     1 
ATOM   6862 C  CA    . ASN B 1 320 ? 41.351  80.233  100.690 1.00 52.69  ? 347 ASN B CA    1 
ATOM   6863 C  C     . ASN B 1 320 ? 40.257  81.125  100.125 1.00 54.22  ? 347 ASN B C     1 
ATOM   6864 O  O     . ASN B 1 320 ? 39.126  81.123  100.620 1.00 55.42  ? 347 ASN B O     1 
ATOM   6865 C  CB    . ASN B 1 320 ? 41.149  78.793  100.213 1.00 52.15  ? 347 ASN B CB    1 
ATOM   6866 C  CG    . ASN B 1 320 ? 40.996  78.697  98.710  1.00 53.82  ? 347 ASN B CG    1 
ATOM   6867 O  OD1   . ASN B 1 320 ? 39.904  78.442  98.204  1.00 57.85  ? 347 ASN B OD1   1 
ATOM   6868 N  ND2   . ASN B 1 320 ? 42.090  78.911  97.985  1.00 57.38  ? 347 ASN B ND2   1 
ATOM   6869 N  N     . LEU B 1 321 ? 40.607  81.889  99.094  1.00 54.33  ? 348 LEU B N     1 
ATOM   6870 C  CA    . LEU B 1 321 ? 39.621  82.647  98.339  1.00 55.88  ? 348 LEU B CA    1 
ATOM   6871 C  C     . LEU B 1 321 ? 38.976  81.729  97.310  1.00 64.27  ? 348 LEU B C     1 
ATOM   6872 O  O     . LEU B 1 321 ? 39.660  80.935  96.656  1.00 61.90  ? 348 LEU B O     1 
ATOM   6873 C  CB    . LEU B 1 321 ? 40.279  83.846  97.655  1.00 60.29  ? 348 LEU B CB    1 
ATOM   6874 C  CG    . LEU B 1 321 ? 39.524  85.179  97.656  1.00 73.49  ? 348 LEU B CG    1 
ATOM   6875 C  CD1   . LEU B 1 321 ? 40.425  86.299  97.161  1.00 74.13  ? 348 LEU B CD1   1 
ATOM   6876 C  CD2   . LEU B 1 321 ? 38.260  85.100  96.812  1.00 82.54  ? 348 LEU B CD2   1 
ATOM   6877 N  N     . ARG B 1 322 ? 37.649  81.834  97.173  1.00 59.17  ? 349 ARG B N     1 
ATOM   6878 C  CA    . ARG B 1 322 ? 36.913  80.857  96.374  1.00 72.34  ? 349 ARG B CA    1 
ATOM   6879 C  C     . ARG B 1 322 ? 37.345  80.876  94.912  1.00 62.48  ? 349 ARG B C     1 
ATOM   6880 O  O     . ARG B 1 322 ? 37.310  79.836  94.242  1.00 72.41  ? 349 ARG B O     1 
ATOM   6881 C  CB    . ARG B 1 322 ? 35.407  81.096  96.493  1.00 65.71  ? 349 ARG B CB    1 
ATOM   6882 C  CG    . ARG B 1 322 ? 34.571  79.960  95.913  1.00 89.04  ? 349 ARG B CG    1 
ATOM   6883 C  CD    . ARG B 1 322 ? 33.121  79.991  96.380  1.00 99.58  ? 349 ARG B CD    1 
ATOM   6884 N  NE    . ARG B 1 322 ? 32.403  81.175  95.925  1.00 117.61 ? 349 ARG B NE    1 
ATOM   6885 C  CZ    . ARG B 1 322 ? 31.883  82.095  96.727  1.00 119.48 ? 349 ARG B CZ    1 
ATOM   6886 N  NH1   . ARG B 1 322 ? 31.963  81.990  98.044  1.00 112.22 ? 349 ARG B NH1   1 
ATOM   6887 N  NH2   . ARG B 1 322 ? 31.259  83.143  96.195  1.00 110.84 ? 349 ARG B NH2   1 
ATOM   6888 N  N     . ARG B 1 323 ? 37.782  82.033  94.404  1.00 68.69  ? 350 ARG B N     1 
ATOM   6889 C  CA    . ARG B 1 323 ? 38.234  82.096  93.018  1.00 71.37  ? 350 ARG B CA    1 
ATOM   6890 C  C     . ARG B 1 323 ? 39.522  81.312  92.794  1.00 63.92  ? 350 ARG B C     1 
ATOM   6891 O  O     . ARG B 1 323 ? 39.842  80.981  91.648  1.00 68.50  ? 350 ARG B O     1 
ATOM   6892 C  CB    . ARG B 1 323 ? 38.428  83.548  92.577  1.00 59.27  ? 350 ARG B CB    1 
ATOM   6893 C  CG    . ARG B 1 323 ? 39.633  84.249  93.177  1.00 70.33  ? 350 ARG B CG    1 
ATOM   6894 C  CD    . ARG B 1 323 ? 39.928  85.545  92.429  1.00 59.25  ? 350 ARG B CD    1 
ATOM   6895 N  NE    . ARG B 1 323 ? 41.139  86.193  92.914  1.00 80.23  ? 350 ARG B NE    1 
ATOM   6896 C  CZ    . ARG B 1 323 ? 41.155  87.270  93.686  1.00 82.00  ? 350 ARG B CZ    1 
ATOM   6897 N  NH1   . ARG B 1 323 ? 40.038  87.887  94.038  1.00 77.34  ? 350 ARG B NH1   1 
ATOM   6898 N  NH2   . ARG B 1 323 ? 42.321  87.740  94.119  1.00 88.11  ? 350 ARG B NH2   1 
ATOM   6899 N  N     . ARG B 1 324 ? 40.259  80.998  93.857  1.00 61.31  ? 351 ARG B N     1 
ATOM   6900 C  CA    . ARG B 1 324 ? 41.502  80.234  93.740  1.00 64.55  ? 351 ARG B CA    1 
ATOM   6901 C  C     . ARG B 1 324 ? 41.199  78.746  93.926  1.00 60.42  ? 351 ARG B C     1 
ATOM   6902 O  O     . ARG B 1 324 ? 41.528  78.122  94.937  1.00 60.56  ? 351 ARG B O     1 
ATOM   6903 C  CB    . ARG B 1 324 ? 42.530  80.733  94.747  1.00 70.04  ? 351 ARG B CB    1 
ATOM   6904 C  CG    . ARG B 1 324 ? 42.948  82.183  94.553  1.00 62.89  ? 351 ARG B CG    1 
ATOM   6905 C  CD    . ARG B 1 324 ? 44.067  82.560  95.513  1.00 81.17  ? 351 ARG B CD    1 
ATOM   6906 N  NE    . ARG B 1 324 ? 44.719  83.810  95.145  1.00 77.49  ? 351 ARG B NE    1 
ATOM   6907 C  CZ    . ARG B 1 324 ? 44.535  84.966  95.767  1.00 79.60  ? 351 ARG B CZ    1 
ATOM   6908 N  NH1   . ARG B 1 324 ? 43.737  85.067  96.819  1.00 99.49  ? 351 ARG B NH1   1 
ATOM   6909 N  NH2   . ARG B 1 324 ? 45.170  86.049  95.326  1.00 70.45  ? 351 ARG B NH2   1 
ATOM   6910 N  N     . GLN B 1 325 ? 40.549  78.178  92.907  1.00 72.91  ? 352 GLN B N     1 
ATOM   6911 C  CA    . GLN B 1 325 ? 40.118  76.786  92.991  1.00 61.89  ? 352 GLN B CA    1 
ATOM   6912 C  C     . GLN B 1 325 ? 41.307  75.836  92.965  1.00 61.51  ? 352 GLN B C     1 
ATOM   6913 O  O     . GLN B 1 325 ? 41.311  74.819  93.670  1.00 67.96  ? 352 GLN B O     1 
ATOM   6914 C  CB    . GLN B 1 325 ? 39.146  76.468  91.854  1.00 66.69  ? 352 GLN B CB    1 
ATOM   6915 C  CG    . GLN B 1 325 ? 38.640  75.035  91.850  1.00 79.10  ? 352 GLN B CG    1 
ATOM   6916 C  CD    . GLN B 1 325 ? 37.704  74.753  90.692  1.00 102.41 ? 352 GLN B CD    1 
ATOM   6917 O  OE1   . GLN B 1 325 ? 37.457  75.620  89.854  1.00 106.77 ? 352 GLN B OE1   1 
ATOM   6918 N  NE2   . GLN B 1 325 ? 37.177  73.535  90.640  1.00 102.96 ? 352 GLN B NE2   1 
ATOM   6919 N  N     . ASP B 1 326 ? 42.330  76.155  92.167  1.00 60.51  ? 353 ASP B N     1 
ATOM   6920 C  CA    . ASP B 1 326 ? 43.489  75.274  92.053  1.00 60.27  ? 353 ASP B CA    1 
ATOM   6921 C  C     . ASP B 1 326 ? 44.230  75.160  93.379  1.00 65.78  ? 353 ASP B C     1 
ATOM   6922 O  O     . ASP B 1 326 ? 44.558  74.055  93.827  1.00 58.64  ? 353 ASP B O     1 
ATOM   6923 C  CB    . ASP B 1 326 ? 44.427  75.773  90.957  1.00 55.75  ? 353 ASP B CB    1 
ATOM   6924 C  CG    . ASP B 1 326 ? 43.971  75.366  89.575  1.00 87.56  ? 353 ASP B CG    1 
ATOM   6925 O  OD1   . ASP B 1 326 ? 42.905  74.721  89.464  1.00 82.47  ? 353 ASP B OD1   1 
ATOM   6926 O  OD2   . ASP B 1 326 ? 44.682  75.689  88.598  1.00 104.32 ? 353 ASP B OD2   1 
ATOM   6927 N  N     . ARG B 1 327 ? 44.511  76.300  94.021  1.00 60.13  ? 354 ARG B N     1 
ATOM   6928 C  CA    . ARG B 1 327 ? 45.151  76.273  95.334  1.00 59.12  ? 354 ARG B CA    1 
ATOM   6929 C  C     . ARG B 1 327 ? 44.341  75.449  96.325  1.00 60.24  ? 354 ARG B C     1 
ATOM   6930 O  O     . ARG B 1 327 ? 44.907  74.686  97.116  1.00 57.55  ? 354 ARG B O     1 
ATOM   6931 C  CB    . ARG B 1 327 ? 45.337  77.694  95.863  1.00 55.43  ? 354 ARG B CB    1 
ATOM   6932 C  CG    . ARG B 1 327 ? 46.318  78.541  95.083  1.00 50.82  ? 354 ARG B CG    1 
ATOM   6933 C  CD    . ARG B 1 327 ? 46.523  79.873  95.779  1.00 58.78  ? 354 ARG B CD    1 
ATOM   6934 N  NE    . ARG B 1 327 ? 47.348  80.785  94.998  1.00 90.36  ? 354 ARG B NE    1 
ATOM   6935 C  CZ    . ARG B 1 327 ? 47.675  82.012  95.380  1.00 83.62  ? 354 ARG B CZ    1 
ATOM   6936 N  NH1   . ARG B 1 327 ? 47.273  82.504  96.540  1.00 79.87  ? 354 ARG B NH1   1 
ATOM   6937 N  NH2   . ARG B 1 327 ? 48.423  82.763  94.577  1.00 86.65  ? 354 ARG B NH2   1 
ATOM   6938 N  N     . ARG B 1 328 ? 43.014  75.585  96.290  1.00 56.73  ? 355 ARG B N     1 
ATOM   6939 C  CA    . ARG B 1 328 ? 42.159  74.836  97.205  1.00 55.34  ? 355 ARG B CA    1 
ATOM   6940 C  C     . ARG B 1 328 ? 42.298  73.335  96.981  1.00 58.81  ? 355 ARG B C     1 
ATOM   6941 O  O     . ARG B 1 328 ? 42.520  72.571  97.927  1.00 48.45  ? 355 ARG B O     1 
ATOM   6942 C  CB    . ARG B 1 328 ? 40.706  75.281  97.038  1.00 51.11  ? 355 ARG B CB    1 
ATOM   6943 C  CG    . ARG B 1 328 ? 39.733  74.634  98.006  1.00 51.97  ? 355 ARG B CG    1 
ATOM   6944 C  CD    . ARG B 1 328 ? 38.360  75.286  97.929  1.00 53.81  ? 355 ARG B CD    1 
ATOM   6945 N  NE    . ARG B 1 328 ? 37.785  75.229  96.590  1.00 60.88  ? 355 ARG B NE    1 
ATOM   6946 C  CZ    . ARG B 1 328 ? 37.653  76.273  95.782  1.00 62.73  ? 355 ARG B CZ    1 
ATOM   6947 N  NH1   . ARG B 1 328 ? 38.046  77.484  96.145  1.00 55.53  ? 355 ARG B NH1   1 
ATOM   6948 N  NH2   . ARG B 1 328 ? 37.108  76.100  94.581  1.00 61.57  ? 355 ARG B NH2   1 
ATOM   6949 N  N     . GLU B 1 329 ? 42.188  72.895  95.724  1.00 53.29  ? 356 GLU B N     1 
ATOM   6950 C  CA    . GLU B 1 329 ? 42.286  71.469  95.427  1.00 53.43  ? 356 GLU B CA    1 
ATOM   6951 C  C     . GLU B 1 329 ? 43.670  70.926  95.760  1.00 56.04  ? 356 GLU B C     1 
ATOM   6952 O  O     . GLU B 1 329 ? 43.798  69.820  96.298  1.00 58.12  ? 356 GLU B O     1 
ATOM   6953 C  CB    . GLU B 1 329 ? 41.956  71.215  93.957  1.00 65.27  ? 356 GLU B CB    1 
ATOM   6954 C  CG    . GLU B 1 329 ? 40.558  71.643  93.542  1.00 77.57  ? 356 GLU B CG    1 
ATOM   6955 C  CD    . GLU B 1 329 ? 40.325  71.488  92.051  1.00 98.29  ? 356 GLU B CD    1 
ATOM   6956 O  OE1   . GLU B 1 329 ? 41.228  70.970  91.358  1.00 103.52 ? 356 GLU B OE1   1 
ATOM   6957 O  OE2   . GLU B 1 329 ? 39.242  71.885  91.573  1.00 88.70  ? 356 GLU B OE2   1 
ATOM   6958 N  N     . ARG B 1 330 ? 44.720  71.689  95.448  1.00 52.74  ? 357 ARG B N     1 
ATOM   6959 C  CA    . ARG B 1 330 ? 46.075  71.222  95.723  1.00 45.90  ? 357 ARG B CA    1 
ATOM   6960 C  C     . ARG B 1 330 ? 46.323  71.092  97.220  1.00 57.47  ? 357 ARG B C     1 
ATOM   6961 O  O     . ARG B 1 330 ? 46.944  70.120  97.668  1.00 59.58  ? 357 ARG B O     1 
ATOM   6962 C  CB    . ARG B 1 330 ? 47.098  72.167  95.096  1.00 48.94  ? 357 ARG B CB    1 
ATOM   6963 C  CG    . ARG B 1 330 ? 48.520  71.627  95.107  1.00 50.30  ? 357 ARG B CG    1 
ATOM   6964 C  CD    . ARG B 1 330 ? 49.539  72.718  94.820  1.00 59.36  ? 357 ARG B CD    1 
ATOM   6965 N  NE    . ARG B 1 330 ? 49.791  73.547  95.993  1.00 77.92  ? 357 ARG B NE    1 
ATOM   6966 C  CZ    . ARG B 1 330 ? 50.773  73.337  96.859  1.00 71.24  ? 357 ARG B CZ    1 
ATOM   6967 N  NH1   . ARG B 1 330 ? 51.627  72.338  96.709  1.00 71.52  ? 357 ARG B NH1   1 
ATOM   6968 N  NH2   . ARG B 1 330 ? 50.900  74.150  97.904  1.00 68.63  ? 357 ARG B NH2   1 
ATOM   6969 N  N     . MET B 1 331 ? 45.846  72.058  98.010  1.00 58.13  ? 358 MET B N     1 
ATOM   6970 C  CA    . MET B 1 331 ? 46.043  72.000  99.455  1.00 49.57  ? 358 MET B CA    1 
ATOM   6971 C  C     . MET B 1 331 ? 45.298  70.818  100.063 1.00 57.78  ? 358 MET B C     1 
ATOM   6972 O  O     . MET B 1 331 ? 45.847  70.085  100.894 1.00 57.68  ? 358 MET B O     1 
ATOM   6973 C  CB    . MET B 1 331 ? 45.593  73.311  100.101 1.00 61.48  ? 358 MET B CB    1 
ATOM   6974 C  CG    . MET B 1 331 ? 46.497  74.495  99.804  1.00 64.26  ? 358 MET B CG    1 
ATOM   6975 S  SD    . MET B 1 331 ? 48.135  74.313  100.527 1.00 66.93  ? 358 MET B SD    1 
ATOM   6976 C  CE    . MET B 1 331 ? 47.704  74.119  102.253 1.00 56.89  ? 358 MET B CE    1 
ATOM   6977 N  N     . LEU B 1 332 ? 44.042  70.617  99.657  1.00 49.38  ? 359 LEU B N     1 
ATOM   6978 C  CA    . LEU B 1 332 ? 43.269  69.499  100.186 1.00 55.22  ? 359 LEU B CA    1 
ATOM   6979 C  C     . LEU B 1 332 ? 43.908  68.165  99.819  1.00 59.35  ? 359 LEU B C     1 
ATOM   6980 O  O     . LEU B 1 332 ? 43.924  67.232  100.632 1.00 57.48  ? 359 LEU B O     1 
ATOM   6981 C  CB    . LEU B 1 332 ? 41.830  69.573  99.679  1.00 49.31  ? 359 LEU B CB    1 
ATOM   6982 C  CG    . LEU B 1 332 ? 41.058  70.831  100.084 1.00 56.59  ? 359 LEU B CG    1 
ATOM   6983 C  CD1   . LEU B 1 332 ? 39.694  70.870  99.414  1.00 51.30  ? 359 LEU B CD1   1 
ATOM   6984 C  CD2   . LEU B 1 332 ? 40.923  70.924  101.597 1.00 50.55  ? 359 LEU B CD2   1 
ATOM   6985 N  N     . ARG B 1 333 ? 44.442  68.055  98.599  1.00 46.05  ? 360 ARG B N     1 
ATOM   6986 C  CA    . ARG B 1 333 ? 45.211  66.868  98.237  1.00 48.60  ? 360 ARG B CA    1 
ATOM   6987 C  C     . ARG B 1 333 ? 46.429  66.712  99.137  1.00 57.41  ? 360 ARG B C     1 
ATOM   6988 O  O     . ARG B 1 333 ? 46.744  65.602  99.583  1.00 58.70  ? 360 ARG B O     1 
ATOM   6989 C  CB    . ARG B 1 333 ? 45.644  66.936  96.772  1.00 45.52  ? 360 ARG B CB    1 
ATOM   6990 C  CG    . ARG B 1 333 ? 44.515  66.805  95.765  1.00 45.48  ? 360 ARG B CG    1 
ATOM   6991 C  CD    . ARG B 1 333 ? 45.054  66.605  94.354  1.00 56.20  ? 360 ARG B CD    1 
ATOM   6992 N  NE    . ARG B 1 333 ? 44.247  67.298  93.357  1.00 73.87  ? 360 ARG B NE    1 
ATOM   6993 C  CZ    . ARG B 1 333 ? 44.626  68.399  92.721  1.00 81.90  ? 360 ARG B CZ    1 
ATOM   6994 N  NH1   . ARG B 1 333 ? 45.817  68.941  92.924  1.00 55.18  ? 360 ARG B NH1   1 
ATOM   6995 N  NH2   . ARG B 1 333 ? 43.790  68.969  91.856  1.00 83.80  ? 360 ARG B NH2   1 
ATOM   6996 N  N     . ALA B 1 334 ? 47.121  67.818  99.419  1.00 54.24  ? 361 ALA B N     1 
ATOM   6997 C  CA    . ALA B 1 334 ? 48.292  67.762  100.287 1.00 51.29  ? 361 ALA B CA    1 
ATOM   6998 C  C     . ALA B 1 334 ? 47.911  67.376  101.709 1.00 53.63  ? 361 ALA B C     1 
ATOM   6999 O  O     . ALA B 1 334 ? 48.588  66.553  102.335 1.00 53.43  ? 361 ALA B O     1 
ATOM   7000 C  CB    . ALA B 1 334 ? 49.018  69.106  100.273 1.00 44.74  ? 361 ALA B CB    1 
ATOM   7001 N  N     . LEU B 1 335 ? 46.829  67.952  102.236 1.00 53.28  ? 362 LEU B N     1 
ATOM   7002 C  CA    . LEU B 1 335 ? 46.418  67.636  103.601 1.00 52.00  ? 362 LEU B CA    1 
ATOM   7003 C  C     . LEU B 1 335 ? 45.921  66.200  103.709 1.00 58.92  ? 362 LEU B C     1 
ATOM   7004 O  O     . LEU B 1 335 ? 46.236  65.501  104.679 1.00 59.29  ? 362 LEU B O     1 
ATOM   7005 C  CB    . LEU B 1 335 ? 45.341  68.617  104.063 1.00 48.65  ? 362 LEU B CB    1 
ATOM   7006 C  CG    . LEU B 1 335 ? 45.786  70.077  104.146 1.00 65.28  ? 362 LEU B CG    1 
ATOM   7007 C  CD1   . LEU B 1 335 ? 44.625  70.979  104.532 1.00 61.24  ? 362 LEU B CD1   1 
ATOM   7008 C  CD2   . LEU B 1 335 ? 46.928  70.220  105.134 1.00 52.08  ? 362 LEU B CD2   1 
ATOM   7009 N  N     . GLN B 1 336 ? 45.144  65.744  102.723 1.00 59.46  ? 363 GLN B N     1 
ATOM   7010 C  CA    . GLN B 1 336 ? 44.643  64.373  102.745 1.00 60.37  ? 363 GLN B CA    1 
ATOM   7011 C  C     . GLN B 1 336 ? 45.786  63.367  102.734 1.00 57.02  ? 363 GLN B C     1 
ATOM   7012 O  O     . GLN B 1 336 ? 45.748  62.366  103.459 1.00 66.30  ? 363 GLN B O     1 
ATOM   7013 C  CB    . GLN B 1 336 ? 43.713  64.135  101.556 1.00 50.37  ? 363 GLN B CB    1 
ATOM   7014 C  CG    . GLN B 1 336 ? 43.082  62.752  101.533 1.00 66.06  ? 363 GLN B CG    1 
ATOM   7015 C  CD    . GLN B 1 336 ? 42.535  62.384  100.167 1.00 97.30  ? 363 GLN B CD    1 
ATOM   7016 O  OE1   . GLN B 1 336 ? 42.756  63.095  99.186  1.00 93.72  ? 363 GLN B OE1   1 
ATOM   7017 N  NE2   . GLN B 1 336 ? 41.820  61.267  100.097 1.00 101.26 ? 363 GLN B NE2   1 
ATOM   7018 N  N     . ALA B 1 337 ? 46.813  63.616  101.917 1.00 53.99  ? 364 ALA B N     1 
ATOM   7019 C  CA    . ALA B 1 337 ? 47.947  62.701  101.847 1.00 47.27  ? 364 ALA B CA    1 
ATOM   7020 C  C     . ALA B 1 337 ? 48.657  62.595  103.191 1.00 65.92  ? 364 ALA B C     1 
ATOM   7021 O  O     . ALA B 1 337 ? 49.114  61.512  103.576 1.00 66.11  ? 364 ALA B O     1 
ATOM   7022 C  CB    . ALA B 1 337 ? 48.923  63.157  100.764 1.00 44.19  ? 364 ALA B CB    1 
ATOM   7023 N  N     . GLN B 1 338 ? 48.758  63.707  103.916 1.00 49.77  ? 365 GLN B N     1 
ATOM   7024 C  CA    . GLN B 1 338 ? 49.390  63.728  105.227 1.00 51.51  ? 365 GLN B CA    1 
ATOM   7025 C  C     . GLN B 1 338 ? 48.426  63.365  106.346 1.00 55.53  ? 365 GLN B C     1 
ATOM   7026 O  O     . GLN B 1 338 ? 48.790  63.483  107.521 1.00 60.44  ? 365 GLN B O     1 
ATOM   7027 C  CB    . GLN B 1 338 ? 50.005  65.105  105.492 1.00 54.43  ? 365 GLN B CB    1 
ATOM   7028 C  CG    . GLN B 1 338 ? 51.061  65.509  104.475 1.00 70.09  ? 365 GLN B CG    1 
ATOM   7029 C  CD    . GLN B 1 338 ? 51.572  66.920  104.685 1.00 63.63  ? 365 GLN B CD    1 
ATOM   7030 O  OE1   . GLN B 1 338 ? 52.667  67.124  105.210 1.00 67.90  ? 365 GLN B OE1   1 
ATOM   7031 N  NE2   . GLN B 1 338 ? 50.780  67.904  104.272 1.00 52.52  ? 365 GLN B NE2   1 
ATOM   7032 N  N     . GLU B 1 339 ? 47.214  62.920  106.004 1.00 59.80  ? 366 GLU B N     1 
ATOM   7033 C  CA    . GLU B 1 339 ? 46.192  62.559  106.987 1.00 66.88  ? 366 GLU B CA    1 
ATOM   7034 C  C     . GLU B 1 339 ? 45.884  63.730  107.916 1.00 63.76  ? 366 GLU B C     1 
ATOM   7035 O  O     . GLU B 1 339 ? 45.781  63.574  109.134 1.00 56.74  ? 366 GLU B O     1 
ATOM   7036 C  CB    . GLU B 1 339 ? 46.601  61.318  107.783 1.00 65.91  ? 366 GLU B CB    1 
ATOM   7037 C  CG    . GLU B 1 339 ? 46.810  60.087  106.917 1.00 72.13  ? 366 GLU B CG    1 
ATOM   7038 C  CD    . GLU B 1 339 ? 46.979  58.819  107.727 1.00 90.62  ? 366 GLU B CD    1 
ATOM   7039 O  OE1   . GLU B 1 339 ? 47.532  58.893  108.845 1.00 97.25  ? 366 GLU B OE1   1 
ATOM   7040 O  OE2   . GLU B 1 339 ? 46.551  57.748  107.247 1.00 96.73  ? 366 GLU B OE2   1 
ATOM   7041 N  N     . ILE B 1 340 ? 45.739  64.916  107.331 1.00 67.13  ? 367 ILE B N     1 
ATOM   7042 C  CA    . ILE B 1 340 ? 45.421  66.135  108.061 1.00 69.53  ? 367 ILE B CA    1 
ATOM   7043 C  C     . ILE B 1 340 ? 44.082  66.652  107.557 1.00 62.31  ? 367 ILE B C     1 
ATOM   7044 O  O     . ILE B 1 340 ? 43.887  66.807  106.345 1.00 64.22  ? 367 ILE B O     1 
ATOM   7045 C  CB    . ILE B 1 340 ? 46.518  67.203  107.895 1.00 64.26  ? 367 ILE B CB    1 
ATOM   7046 C  CG1   . ILE B 1 340 ? 47.862  66.672  108.399 1.00 54.70  ? 367 ILE B CG1   1 
ATOM   7047 C  CG2   . ILE B 1 340 ? 46.136  68.477  108.630 1.00 59.67  ? 367 ILE B CG2   1 
ATOM   7048 C  CD1   . ILE B 1 340 ? 49.023  67.610  108.147 1.00 50.58  ? 367 ILE B CD1   1 
ATOM   7049 N  N     . GLU B 1 341 ? 43.161  66.902  108.481 1.00 59.41  ? 368 GLU B N     1 
ATOM   7050 C  CA    . GLU B 1 341 ? 41.855  67.464  108.178 1.00 66.72  ? 368 GLU B CA    1 
ATOM   7051 C  C     . GLU B 1 341 ? 41.816  68.921  108.623 1.00 72.58  ? 368 GLU B C     1 
ATOM   7052 O  O     . GLU B 1 341 ? 42.429  69.293  109.627 1.00 77.60  ? 368 GLU B O     1 
ATOM   7053 C  CB    . GLU B 1 341 ? 40.747  66.664  108.871 1.00 65.91  ? 368 GLU B CB    1 
ATOM   7054 C  CG    . GLU B 1 341 ? 39.334  67.085  108.511 1.00 88.24  ? 368 GLU B CG    1 
ATOM   7055 C  CD    . GLU B 1 341 ? 38.288  66.325  109.299 1.00 96.18  ? 368 GLU B CD    1 
ATOM   7056 O  OE1   . GLU B 1 341 ? 38.670  65.585  110.231 1.00 81.15  ? 368 GLU B OE1   1 
ATOM   7057 O  OE2   . GLU B 1 341 ? 37.086  66.468  108.987 1.00 106.56 ? 368 GLU B OE2   1 
ATOM   7058 N  N     . CYS B 1 342 ? 41.096  69.750  107.869 1.00 58.40  ? 369 CYS B N     1 
ATOM   7059 C  CA    . CYS B 1 342 ? 41.073  71.180  108.140 1.00 69.60  ? 369 CYS B CA    1 
ATOM   7060 C  C     . CYS B 1 342 ? 39.668  71.733  107.953 1.00 69.25  ? 369 CYS B C     1 
ATOM   7061 O  O     . CYS B 1 342 ? 38.815  71.127  107.299 1.00 76.32  ? 369 CYS B O     1 
ATOM   7062 C  CB    . CYS B 1 342 ? 42.045  71.944  107.232 1.00 64.74  ? 369 CYS B CB    1 
ATOM   7063 S  SG    . CYS B 1 342 ? 41.415  72.246  105.564 1.00 77.48  ? 369 CYS B SG    1 
ATOM   7064 N  N     . ARG B 1 343 ? 39.440  72.906  108.537 1.00 65.34  ? 370 ARG B N     1 
ATOM   7065 C  CA    . ARG B 1 343 ? 38.232  73.683  108.300 1.00 64.15  ? 370 ARG B CA    1 
ATOM   7066 C  C     . ARG B 1 343 ? 38.563  74.779  107.294 1.00 71.12  ? 370 ARG B C     1 
ATOM   7067 O  O     . ARG B 1 343 ? 39.407  75.640  107.564 1.00 73.50  ? 370 ARG B O     1 
ATOM   7068 C  CB    . ARG B 1 343 ? 37.691  74.283  109.598 1.00 59.14  ? 370 ARG B CB    1 
ATOM   7069 C  CG    . ARG B 1 343 ? 36.350  74.982  109.437 1.00 62.15  ? 370 ARG B CG    1 
ATOM   7070 C  CD    . ARG B 1 343 ? 35.902  75.648  110.727 1.00 67.29  ? 370 ARG B CD    1 
ATOM   7071 N  NE    . ARG B 1 343 ? 34.669  76.406  110.539 1.00 85.19  ? 370 ARG B NE    1 
ATOM   7072 C  CZ    . ARG B 1 343 ? 34.620  77.669  110.136 1.00 95.71  ? 370 ARG B CZ    1 
ATOM   7073 N  NH1   . ARG B 1 343 ? 35.721  78.357  109.881 1.00 91.48  ? 370 ARG B NH1   1 
ATOM   7074 N  NH2   . ARG B 1 343 ? 33.436  78.255  109.983 1.00 90.59  ? 370 ARG B NH2   1 
ATOM   7075 N  N     . LEU B 1 344 ? 37.912  74.734  106.137 1.00 65.33  ? 371 LEU B N     1 
ATOM   7076 C  CA    . LEU B 1 344 ? 38.146  75.716  105.086 1.00 64.39  ? 371 LEU B CA    1 
ATOM   7077 C  C     . LEU B 1 344 ? 37.445  77.022  105.441 1.00 63.82  ? 371 LEU B C     1 
ATOM   7078 O  O     . LEU B 1 344 ? 36.230  77.043  105.663 1.00 67.89  ? 371 LEU B O     1 
ATOM   7079 C  CB    . LEU B 1 344 ? 37.649  75.179  103.745 1.00 60.22  ? 371 LEU B CB    1 
ATOM   7080 C  CG    . LEU B 1 344 ? 37.782  76.090  102.525 1.00 76.55  ? 371 LEU B CG    1 
ATOM   7081 C  CD1   . LEU B 1 344 ? 39.243  76.295  102.160 1.00 77.39  ? 371 LEU B CD1   1 
ATOM   7082 C  CD2   . LEU B 1 344 ? 37.007  75.513  101.353 1.00 89.30  ? 371 LEU B CD2   1 
ATOM   7083 N  N     . VAL B 1 345 ? 38.208  78.109  105.498 1.00 63.15  ? 372 VAL B N     1 
ATOM   7084 C  CA    . VAL B 1 345 ? 37.678  79.439  105.779 1.00 65.55  ? 372 VAL B CA    1 
ATOM   7085 C  C     . VAL B 1 345 ? 37.772  80.255  104.499 1.00 70.24  ? 372 VAL B C     1 
ATOM   7086 O  O     . VAL B 1 345 ? 38.863  80.419  103.938 1.00 65.34  ? 372 VAL B O     1 
ATOM   7087 C  CB    . VAL B 1 345 ? 38.435  80.126  106.925 1.00 58.99  ? 372 VAL B CB    1 
ATOM   7088 C  CG1   . VAL B 1 345 ? 37.823  81.483  107.226 1.00 58.07  ? 372 VAL B CG1   1 
ATOM   7089 C  CG2   . VAL B 1 345 ? 38.433  79.248  108.161 1.00 63.20  ? 372 VAL B CG2   1 
ATOM   7090 N  N     . GLU B 1 346 ? 36.634  80.766  104.035 1.00 66.40  ? 373 GLU B N     1 
ATOM   7091 C  CA    . GLU B 1 346 ? 36.617  81.556  102.811 1.00 66.99  ? 373 GLU B CA    1 
ATOM   7092 C  C     . GLU B 1 346 ? 37.232  82.924  103.068 1.00 60.80  ? 373 GLU B C     1 
ATOM   7093 O  O     . GLU B 1 346 ? 36.769  83.669  103.939 1.00 65.66  ? 373 GLU B O     1 
ATOM   7094 C  CB    . GLU B 1 346 ? 35.193  81.691  102.281 1.00 68.22  ? 373 GLU B CB    1 
ATOM   7095 C  CG    . GLU B 1 346 ? 34.687  80.444  101.573 1.00 88.58  ? 373 GLU B CG    1 
ATOM   7096 C  CD    . GLU B 1 346 ? 33.538  80.733  100.629 1.00 110.33 ? 373 GLU B CD    1 
ATOM   7097 O  OE1   . GLU B 1 346 ? 33.034  81.876  100.639 1.00 117.14 ? 373 GLU B OE1   1 
ATOM   7098 O  OE2   . GLU B 1 346 ? 33.143  79.818  99.874  1.00 108.54 ? 373 GLU B OE2   1 
ATOM   7099 N  N     . ALA B 1 347 ? 38.274  83.251  102.309 1.00 67.46  ? 374 ALA B N     1 
ATOM   7100 C  CA    . ALA B 1 347 ? 39.003  84.491  102.518 1.00 59.97  ? 374 ALA B CA    1 
ATOM   7101 C  C     . ALA B 1 347 ? 38.157  85.698  102.132 1.00 62.52  ? 374 ALA B C     1 
ATOM   7102 O  O     . ALA B 1 347 ? 37.304  85.633  101.243 1.00 72.81  ? 374 ALA B O     1 
ATOM   7103 C  CB    . ALA B 1 347 ? 40.301  84.489  101.708 1.00 58.56  ? 374 ALA B CB    1 
ATOM   7104 N  N     . VAL B 1 348 ? 38.403  86.808  102.819 1.00 62.47  ? 375 VAL B N     1 
ATOM   7105 C  CA    . VAL B 1 348 ? 37.768  88.077  102.485 1.00 74.20  ? 375 VAL B CA    1 
ATOM   7106 C  C     . VAL B 1 348 ? 38.452  88.646  101.249 1.00 70.65  ? 375 VAL B C     1 
ATOM   7107 O  O     . VAL B 1 348 ? 39.675  88.827  101.232 1.00 72.57  ? 375 VAL B O     1 
ATOM   7108 C  CB    . VAL B 1 348 ? 37.847  89.060  103.661 1.00 76.10  ? 375 VAL B CB    1 
ATOM   7109 C  CG1   . VAL B 1 348 ? 37.261  90.407  103.267 1.00 76.27  ? 375 VAL B CG1   1 
ATOM   7110 C  CG2   . VAL B 1 348 ? 37.133  88.492  104.879 1.00 69.79  ? 375 VAL B CG2   1 
ATOM   7111 N  N     . ASP B 1 349 ? 37.668  88.923  100.211 1.00 71.60  ? 376 ASP B N     1 
ATOM   7112 C  CA    . ASP B 1 349 ? 38.193  89.530  98.992  1.00 89.93  ? 376 ASP B CA    1 
ATOM   7113 C  C     . ASP B 1 349 ? 38.179  91.040  99.188  1.00 94.41  ? 376 ASP B C     1 
ATOM   7114 O  O     . ASP B 1 349 ? 37.144  91.689  99.026  1.00 82.84  ? 376 ASP B O     1 
ATOM   7115 C  CB    . ASP B 1 349 ? 37.377  89.108  97.777  1.00 80.56  ? 376 ASP B CB    1 
ATOM   7116 C  CG    . ASP B 1 349 ? 38.124  89.318  96.474  1.00 93.36  ? 376 ASP B CG    1 
ATOM   7117 O  OD1   . ASP B 1 349 ? 39.203  89.945  96.501  1.00 100.27 ? 376 ASP B OD1   1 
ATOM   7118 O  OD2   . ASP B 1 349 ? 37.639  88.845  95.425  1.00 93.34  ? 376 ASP B OD2   1 
ATOM   7119 N  N     . GLY B 1 350 ? 39.337  91.599  99.548  1.00 112.90 ? 377 GLY B N     1 
ATOM   7120 C  CA    . GLY B 1 350 ? 39.413  93.022  99.826  1.00 117.12 ? 377 GLY B CA    1 
ATOM   7121 C  C     . GLY B 1 350 ? 39.158  93.893  98.613  1.00 117.87 ? 377 GLY B C     1 
ATOM   7122 O  O     . GLY B 1 350 ? 38.677  95.024  98.749  1.00 123.39 ? 377 GLY B O     1 
ATOM   7123 N  N     . LYS B 1 351 ? 39.473  93.390  97.418  1.00 99.70  ? 378 LYS B N     1 
ATOM   7124 C  CA    . LYS B 1 351 ? 39.190  94.147  96.204  1.00 103.89 ? 378 LYS B CA    1 
ATOM   7125 C  C     . LYS B 1 351 ? 37.691  94.310  95.981  1.00 103.08 ? 378 LYS B C     1 
ATOM   7126 O  O     . LYS B 1 351 ? 37.251  95.347  95.472  1.00 101.60 ? 378 LYS B O     1 
ATOM   7127 C  CB    . LYS B 1 351 ? 39.831  93.466  94.991  1.00 109.79 ? 378 LYS B CB    1 
ATOM   7128 C  CG    . LYS B 1 351 ? 41.329  93.722  94.812  1.00 108.38 ? 378 LYS B CG    1 
ATOM   7129 C  CD    . LYS B 1 351 ? 42.165  92.971  95.836  1.00 119.00 ? 378 LYS B CD    1 
ATOM   7130 C  CE    . LYS B 1 351 ? 43.651  93.093  95.541  1.00 113.63 ? 378 LYS B CE    1 
ATOM   7131 N  NZ    . LYS B 1 351 ? 44.040  92.344  94.313  1.00 85.97  ? 378 LYS B NZ    1 
ATOM   7132 N  N     . ALA B 1 352 ? 36.894  93.310  96.362  1.00 98.21  ? 379 ALA B N     1 
ATOM   7133 C  CA    . ALA B 1 352 ? 35.446  93.393  96.218  1.00 95.49  ? 379 ALA B CA    1 
ATOM   7134 C  C     . ALA B 1 352 ? 34.801  94.312  97.244  1.00 101.56 ? 379 ALA B C     1 
ATOM   7135 O  O     . ALA B 1 352 ? 33.611  94.615  97.112  1.00 111.65 ? 379 ALA B O     1 
ATOM   7136 C  CB    . ALA B 1 352 ? 34.826  91.998  96.321  1.00 95.08  ? 379 ALA B CB    1 
ATOM   7137 N  N     . MET B 1 353 ? 35.544  94.761  98.253  1.00 107.67 ? 380 MET B N     1 
ATOM   7138 C  CA    . MET B 1 353 ? 34.983  95.612  99.293  1.00 111.62 ? 380 MET B CA    1 
ATOM   7139 C  C     . MET B 1 353 ? 34.916  97.059  98.826  1.00 120.83 ? 380 MET B C     1 
ATOM   7140 O  O     . MET B 1 353 ? 35.926  97.634  98.409  1.00 114.94 ? 380 MET B O     1 
ATOM   7141 C  CB    . MET B 1 353 ? 35.818  95.522  100.570 1.00 109.78 ? 380 MET B CB    1 
ATOM   7142 C  CG    . MET B 1 353 ? 35.836  94.148  101.214 1.00 105.77 ? 380 MET B CG    1 
ATOM   7143 S  SD    . MET B 1 353 ? 36.674  94.160  102.810 1.00 109.70 ? 380 MET B SD    1 
ATOM   7144 C  CE    . MET B 1 353 ? 35.681  95.354  103.702 1.00 95.69  ? 380 MET B CE    1 
ATOM   7145 N  N     . ASN B 1 354 ? 33.723  97.643  98.892  1.00 126.72 ? 381 ASN B N     1 
ATOM   7146 C  CA    . ASN B 1 354 ? 33.581  99.061  98.614  1.00 136.47 ? 381 ASN B CA    1 
ATOM   7147 C  C     . ASN B 1 354 ? 33.960  99.875  99.851  1.00 140.89 ? 381 ASN B C     1 
ATOM   7148 O  O     . ASN B 1 354 ? 34.095  99.348  100.959 1.00 133.42 ? 381 ASN B O     1 
ATOM   7149 C  CB    . ASN B 1 354 ? 32.157  99.383  98.147  1.00 136.57 ? 381 ASN B CB    1 
ATOM   7150 C  CG    . ASN B 1 354 ? 31.092  99.017  99.175  1.00 136.05 ? 381 ASN B CG    1 
ATOM   7151 O  OD1   . ASN B 1 354 ? 31.213  99.328  100.359 1.00 143.70 ? 381 ASN B OD1   1 
ATOM   7152 N  ND2   . ASN B 1 354 ? 30.032  98.361  98.715  1.00 125.70 ? 381 ASN B ND2   1 
ATOM   7153 N  N     . THR B 1 355 ? 34.135  101.184 99.648  1.00 125.82 ? 382 THR B N     1 
ATOM   7154 C  CA    . THR B 1 355 ? 34.523  102.054 100.753 1.00 121.81 ? 382 THR B CA    1 
ATOM   7155 C  C     . THR B 1 355 ? 33.466  102.080 101.849 1.00 124.05 ? 382 THR B C     1 
ATOM   7156 O  O     . THR B 1 355 ? 33.797  102.278 103.023 1.00 120.97 ? 382 THR B O     1 
ATOM   7157 C  CB    . THR B 1 355 ? 34.789  103.467 100.237 1.00 114.35 ? 382 THR B CB    1 
ATOM   7158 O  OG1   . THR B 1 355 ? 33.623  103.956 99.564  1.00 125.43 ? 382 THR B OG1   1 
ATOM   7159 C  CG2   . THR B 1 355 ? 35.964  103.467 99.269  1.00 114.24 ? 382 THR B CG2   1 
ATOM   7160 N  N     . SER B 1 356 ? 32.196  101.875 101.491 1.00 124.05 ? 383 SER B N     1 
ATOM   7161 C  CA    . SER B 1 356 ? 31.135  101.861 102.494 1.00 117.44 ? 383 SER B CA    1 
ATOM   7162 C  C     . SER B 1 356 ? 31.297  100.680 103.446 1.00 117.88 ? 383 SER B C     1 
ATOM   7163 O  O     . SER B 1 356 ? 31.192  100.833 104.668 1.00 117.99 ? 383 SER B O     1 
ATOM   7164 C  CB    . SER B 1 356 ? 29.767  101.821 101.811 1.00 119.54 ? 383 SER B CB    1 
ATOM   7165 O  OG    . SER B 1 356 ? 29.619  102.894 100.898 1.00 137.98 ? 383 SER B OG    1 
ATOM   7166 N  N     . GLN B 1 357 ? 31.555  99.489  102.899 1.00 122.94 ? 384 GLN B N     1 
ATOM   7167 C  CA    . GLN B 1 357 ? 31.775  98.317  103.741 1.00 111.70 ? 384 GLN B CA    1 
ATOM   7168 C  C     . GLN B 1 357 ? 33.031  98.464  104.590 1.00 108.88 ? 384 GLN B C     1 
ATOM   7169 O  O     . GLN B 1 357 ? 33.076  97.969  105.723 1.00 105.93 ? 384 GLN B O     1 
ATOM   7170 C  CB    . GLN B 1 357 ? 31.865  97.060  102.877 1.00 122.29 ? 384 GLN B CB    1 
ATOM   7171 C  CG    . GLN B 1 357 ? 30.615  96.769  102.066 1.00 124.12 ? 384 GLN B CG    1 
ATOM   7172 C  CD    . GLN B 1 357 ? 30.900  95.906  100.853 1.00 133.58 ? 384 GLN B CD    1 
ATOM   7173 O  OE1   . GLN B 1 357 ? 32.047  95.544  100.591 1.00 126.32 ? 384 GLN B OE1   1 
ATOM   7174 N  NE2   . GLN B 1 357 ? 29.857  95.577  100.102 1.00 129.61 ? 384 GLN B NE2   1 
ATOM   7175 N  N     . VAL B 1 358 ? 34.059  99.133  104.060 1.00 112.71 ? 385 VAL B N     1 
ATOM   7176 C  CA    . VAL B 1 358 ? 35.267  99.387  104.840 1.00 111.99 ? 385 VAL B CA    1 
ATOM   7177 C  C     . VAL B 1 358 ? 34.955  100.298 106.021 1.00 113.58 ? 385 VAL B C     1 
ATOM   7178 O  O     . VAL B 1 358 ? 35.397  100.051 107.150 1.00 111.75 ? 385 VAL B O     1 
ATOM   7179 C  CB    . VAL B 1 358 ? 36.369  99.977  103.939 1.00 104.42 ? 385 VAL B CB    1 
ATOM   7180 C  CG1   . VAL B 1 358 ? 37.609  100.306 104.753 1.00 100.65 ? 385 VAL B CG1   1 
ATOM   7181 C  CG2   . VAL B 1 358 ? 36.710  99.011  102.811 1.00 100.03 ? 385 VAL B CG2   1 
ATOM   7182 N  N     . GLU B 1 359 ? 34.178  101.359 105.783 1.00 106.80 ? 386 GLU B N     1 
ATOM   7183 C  CA    . GLU B 1 359 ? 33.802  102.262 106.865 1.00 106.82 ? 386 GLU B CA    1 
ATOM   7184 C  C     . GLU B 1 359 ? 32.840  101.601 107.844 1.00 112.55 ? 386 GLU B C     1 
ATOM   7185 O  O     . GLU B 1 359 ? 32.864  101.916 109.039 1.00 110.45 ? 386 GLU B O     1 
ATOM   7186 C  CB    . GLU B 1 359 ? 33.178  103.534 106.294 1.00 117.27 ? 386 GLU B CB    1 
ATOM   7187 C  CG    . GLU B 1 359 ? 34.108  104.331 105.396 1.00 123.71 ? 386 GLU B CG    1 
ATOM   7188 C  CD    . GLU B 1 359 ? 33.367  105.356 104.561 1.00 142.16 ? 386 GLU B CD    1 
ATOM   7189 O  OE1   . GLU B 1 359 ? 32.161  105.565 104.808 1.00 135.06 ? 386 GLU B OE1   1 
ATOM   7190 O  OE2   . GLU B 1 359 ? 33.989  105.947 103.653 1.00 152.30 ? 386 GLU B OE2   1 
ATOM   7191 N  N     . ALA B 1 360 ? 31.990  100.691 107.359 1.00 118.72 ? 387 ALA B N     1 
ATOM   7192 C  CA    . ALA B 1 360 ? 31.051  100.004 108.240 1.00 114.85 ? 387 ALA B CA    1 
ATOM   7193 C  C     . ALA B 1 360 ? 31.773  99.171  109.291 1.00 117.81 ? 387 ALA B C     1 
ATOM   7194 O  O     . ALA B 1 360 ? 31.253  98.979  110.396 1.00 115.33 ? 387 ALA B O     1 
ATOM   7195 C  CB    . ALA B 1 360 ? 30.110  99.122  107.420 1.00 107.18 ? 387 ALA B CB    1 
ATOM   7196 N  N     . LEU B 1 361 ? 32.962  98.670  108.969 1.00 115.64 ? 388 LEU B N     1 
ATOM   7197 C  CA    . LEU B 1 361 ? 33.780  97.931  109.919 1.00 112.71 ? 388 LEU B CA    1 
ATOM   7198 C  C     . LEU B 1 361 ? 34.737  98.829  110.693 1.00 110.52 ? 388 LEU B C     1 
ATOM   7199 O  O     . LEU B 1 361 ? 35.521  98.323  111.501 1.00 100.17 ? 388 LEU B O     1 
ATOM   7200 C  CB    . LEU B 1 361 ? 34.569  96.840  109.193 1.00 107.08 ? 388 LEU B CB    1 
ATOM   7201 C  CG    . LEU B 1 361 ? 33.720  95.901  108.329 1.00 106.54 ? 388 LEU B CG    1 
ATOM   7202 C  CD1   . LEU B 1 361 ? 34.596  94.900  107.598 1.00 82.29  ? 388 LEU B CD1   1 
ATOM   7203 C  CD2   . LEU B 1 361 ? 32.676  95.191  109.177 1.00 93.62  ? 388 LEU B CD2   1 
ATOM   7204 N  N     . GLY B 1 362 ? 34.689  100.139 110.469 1.00 99.03  ? 389 GLY B N     1 
ATOM   7205 C  CA    . GLY B 1 362 ? 35.568  101.061 111.171 1.00 99.44  ? 389 GLY B CA    1 
ATOM   7206 C  C     . GLY B 1 362 ? 37.035  100.849 110.871 1.00 102.82 ? 389 GLY B C     1 
ATOM   7207 O  O     . GLY B 1 362 ? 37.871  100.912 111.782 1.00 102.32 ? 389 GLY B O     1 
ATOM   7208 N  N     . ILE B 1 363 ? 37.370  100.604 109.611 1.00 100.37 ? 390 ILE B N     1 
ATOM   7209 C  CA    . ILE B 1 363 ? 38.734  100.278 109.211 1.00 98.38  ? 390 ILE B CA    1 
ATOM   7210 C  C     . ILE B 1 363 ? 39.455  101.554 108.802 1.00 97.43  ? 390 ILE B C     1 
ATOM   7211 O  O     . ILE B 1 363 ? 38.957  102.326 107.975 1.00 102.74 ? 390 ILE B O     1 
ATOM   7212 C  CB    . ILE B 1 363 ? 38.741  99.250  108.066 1.00 97.43  ? 390 ILE B CB    1 
ATOM   7213 C  CG1   . ILE B 1 363 ? 38.082  97.945  108.518 1.00 104.77 ? 390 ILE B CG1   1 
ATOM   7214 C  CG2   . ILE B 1 363 ? 40.158  98.995  107.587 1.00 86.45  ? 390 ILE B CG2   1 
ATOM   7215 C  CD1   . ILE B 1 363 ? 37.923  96.933  107.409 1.00 92.03  ? 390 ILE B CD1   1 
ATOM   7216 N  N     . GLN B 1 364 ? 40.626  101.781 109.392 1.00 94.40  ? 391 GLN B N     1 
ATOM   7217 C  CA    . GLN B 1 364 ? 41.468  102.922 109.063 1.00 96.05  ? 391 GLN B CA    1 
ATOM   7218 C  C     . GLN B 1 364 ? 42.915  102.458 109.041 1.00 99.77  ? 391 GLN B C     1 
ATOM   7219 O  O     . GLN B 1 364 ? 43.357  101.763 109.960 1.00 101.68 ? 391 GLN B O     1 
ATOM   7220 C  CB    . GLN B 1 364 ? 41.290  104.061 110.074 1.00 102.64 ? 391 GLN B CB    1 
ATOM   7221 C  CG    . GLN B 1 364 ? 39.861  104.566 110.206 1.00 105.61 ? 391 GLN B CG    1 
ATOM   7222 C  CD    . GLN B 1 364 ? 39.693  105.576 111.325 1.00 124.88 ? 391 GLN B CD    1 
ATOM   7223 O  OE1   . GLN B 1 364 ? 40.669  106.011 111.937 1.00 125.36 ? 391 GLN B OE1   1 
ATOM   7224 N  NE2   . GLN B 1 364 ? 38.449  105.953 111.599 1.00 115.53 ? 391 GLN B NE2   1 
ATOM   7225 N  N     . MET B 1 365 ? 43.644  102.833 107.993 1.00 97.38  ? 392 MET B N     1 
ATOM   7226 C  CA    . MET B 1 365 ? 45.047  102.456 107.888 1.00 92.04  ? 392 MET B CA    1 
ATOM   7227 C  C     . MET B 1 365 ? 45.849  103.106 109.009 1.00 108.27 ? 392 MET B C     1 
ATOM   7228 O  O     . MET B 1 365 ? 45.520  104.198 109.482 1.00 103.76 ? 392 MET B O     1 
ATOM   7229 C  CB    . MET B 1 365 ? 45.611  102.874 106.527 1.00 92.57  ? 392 MET B CB    1 
ATOM   7230 C  CG    . MET B 1 365 ? 47.015  102.361 106.245 1.00 98.35  ? 392 MET B CG    1 
ATOM   7231 S  SD    . MET B 1 365 ? 47.790  103.132 104.811 1.00 100.51 ? 392 MET B SD    1 
ATOM   7232 C  CE    . MET B 1 365 ? 48.058  104.798 105.413 1.00 107.70 ? 392 MET B CE    1 
ATOM   7233 N  N     . LEU B 1 366 ? 46.896  102.413 109.447 1.00 97.16  ? 393 LEU B N     1 
ATOM   7234 C  CA    . LEU B 1 366 ? 47.802  102.985 110.431 1.00 102.93 ? 393 LEU B CA    1 
ATOM   7235 C  C     . LEU B 1 366 ? 48.389  104.278 109.876 1.00 108.28 ? 393 LEU B C     1 
ATOM   7236 O  O     . LEU B 1 366 ? 48.946  104.274 108.769 1.00 112.22 ? 393 LEU B O     1 
ATOM   7237 C  CB    . LEU B 1 366 ? 48.917  102.000 110.785 1.00 97.66  ? 393 LEU B CB    1 
ATOM   7238 C  CG    . LEU B 1 366 ? 49.923  102.460 111.844 1.00 103.58 ? 393 LEU B CG    1 
ATOM   7239 C  CD1   . LEU B 1 366 ? 50.331  101.302 112.732 1.00 92.94  ? 393 LEU B CD1   1 
ATOM   7240 C  CD2   . LEU B 1 366 ? 51.153  103.086 111.204 1.00 116.03 ? 393 LEU B CD2   1 
ATOM   7241 N  N     . PRO B 1 367 ? 48.269  105.396 110.589 1.00 116.07 ? 394 PRO B N     1 
ATOM   7242 C  CA    . PRO B 1 367 ? 48.704  106.688 110.035 1.00 110.27 ? 394 PRO B CA    1 
ATOM   7243 C  C     . PRO B 1 367 ? 50.193  106.696 109.726 1.00 109.99 ? 394 PRO B C     1 
ATOM   7244 O  O     . PRO B 1 367 ? 51.032  106.493 110.607 1.00 118.57 ? 394 PRO B O     1 
ATOM   7245 C  CB    . PRO B 1 367 ? 48.349  107.684 111.145 1.00 107.53 ? 394 PRO B CB    1 
ATOM   7246 C  CG    . PRO B 1 367 ? 47.281  107.001 111.941 1.00 105.34 ? 394 PRO B CG    1 
ATOM   7247 C  CD    . PRO B 1 367 ? 47.612  105.544 111.898 1.00 111.97 ? 394 PRO B CD    1 
ATOM   7248 N  N     . GLY B 1 368 ? 50.515  106.924 108.456 1.00 106.08 ? 395 GLY B N     1 
ATOM   7249 C  CA    . GLY B 1 368 ? 51.888  107.016 108.014 1.00 111.67 ? 395 GLY B CA    1 
ATOM   7250 C  C     . GLY B 1 368 ? 52.512  105.726 107.535 1.00 122.52 ? 395 GLY B C     1 
ATOM   7251 O  O     . GLY B 1 368 ? 53.733  105.688 107.339 1.00 116.99 ? 395 GLY B O     1 
ATOM   7252 N  N     . TYR B 1 369 ? 51.726  104.670 107.338 1.00 112.68 ? 396 TYR B N     1 
ATOM   7253 C  CA    . TYR B 1 369 ? 52.296  103.406 106.894 1.00 107.85 ? 396 TYR B CA    1 
ATOM   7254 C  C     . TYR B 1 369 ? 52.781  103.503 105.454 1.00 114.34 ? 396 TYR B C     1 
ATOM   7255 O  O     . TYR B 1 369 ? 52.130  104.107 104.598 1.00 117.96 ? 396 TYR B O     1 
ATOM   7256 C  CB    . TYR B 1 369 ? 51.279  102.274 107.012 1.00 108.66 ? 396 TYR B CB    1 
ATOM   7257 C  CG    . TYR B 1 369 ? 51.733  101.021 106.291 1.00 109.66 ? 396 TYR B CG    1 
ATOM   7258 C  CD1   . TYR B 1 369 ? 52.765  100.241 106.797 1.00 110.61 ? 396 TYR B CD1   1 
ATOM   7259 C  CD2   . TYR B 1 369 ? 51.145  100.631 105.094 1.00 110.21 ? 396 TYR B CD2   1 
ATOM   7260 C  CE1   . TYR B 1 369 ? 53.189  99.104  106.142 1.00 100.81 ? 396 TYR B CE1   1 
ATOM   7261 C  CE2   . TYR B 1 369 ? 51.565  99.495  104.431 1.00 111.27 ? 396 TYR B CE2   1 
ATOM   7262 C  CZ    . TYR B 1 369 ? 52.587  98.736  104.961 1.00 102.34 ? 396 TYR B CZ    1 
ATOM   7263 O  OH    . TYR B 1 369 ? 53.015  97.602  104.311 1.00 95.65  ? 396 TYR B OH    1 
ATOM   7264 N  N     . ARG B 1 370 ? 53.933  102.890 105.190 1.00 113.85 ? 397 ARG B N     1 
ATOM   7265 C  CA    . ARG B 1 370 ? 54.495  102.821 103.850 1.00 117.67 ? 397 ARG B CA    1 
ATOM   7266 C  C     . ARG B 1 370 ? 55.080  101.435 103.620 1.00 120.72 ? 397 ARG B C     1 
ATOM   7267 O  O     . ARG B 1 370 ? 55.635  100.828 104.540 1.00 110.40 ? 397 ARG B O     1 
ATOM   7268 C  CB    . ARG B 1 370 ? 55.573  103.893 103.635 1.00 124.22 ? 397 ARG B CB    1 
ATOM   7269 C  CG    . ARG B 1 370 ? 55.016  105.295 103.447 1.00 114.80 ? 397 ARG B CG    1 
ATOM   7270 C  CD    . ARG B 1 370 ? 56.113  106.283 103.085 1.00 127.73 ? 397 ARG B CD    1 
ATOM   7271 N  NE    . ARG B 1 370 ? 55.574  107.564 102.647 1.00 149.89 ? 397 ARG B NE    1 
ATOM   7272 C  CZ    . ARG B 1 370 ? 56.313  108.595 102.258 1.00 154.72 ? 397 ARG B CZ    1 
ATOM   7273 N  NH1   . ARG B 1 370 ? 57.634  108.529 102.237 1.00 156.98 ? 397 ARG B NH1   1 
ATOM   7274 N  NH2   . ARG B 1 370 ? 55.711  109.720 101.882 1.00 158.17 ? 397 ARG B NH2   1 
ATOM   7275 N  N     . ASP B 1 371 ? 54.927  100.940 102.394 1.00 135.32 ? 398 ASP B N     1 
ATOM   7276 C  CA    . ASP B 1 371 ? 55.506  99.664  101.998 1.00 124.57 ? 398 ASP B CA    1 
ATOM   7277 C  C     . ASP B 1 371 ? 57.004  99.665  102.299 1.00 129.01 ? 398 ASP B C     1 
ATOM   7278 O  O     . ASP B 1 371 ? 57.719  100.574 101.855 1.00 140.18 ? 398 ASP B O     1 
ATOM   7279 C  CB    . ASP B 1 371 ? 55.256  99.431  100.505 1.00 128.71 ? 398 ASP B CB    1 
ATOM   7280 C  CG    . ASP B 1 371 ? 55.788  98.094  100.001 1.00 141.85 ? 398 ASP B CG    1 
ATOM   7281 O  OD1   . ASP B 1 371 ? 56.404  97.335  100.777 1.00 140.60 ? 398 ASP B OD1   1 
ATOM   7282 O  OD2   . ASP B 1 371 ? 55.580  97.801  98.804  1.00 141.91 ? 398 ASP B OD2   1 
ATOM   7283 N  N     . PRO B 1 372 ? 57.513  98.684  103.051 1.00 115.62 ? 399 PRO B N     1 
ATOM   7284 C  CA    . PRO B 1 372 ? 58.959  98.648  103.333 1.00 118.46 ? 399 PRO B CA    1 
ATOM   7285 C  C     . PRO B 1 372 ? 59.835  98.562  102.089 1.00 122.41 ? 399 PRO B C     1 
ATOM   7286 O  O     . PRO B 1 372 ? 61.060  98.677  102.218 1.00 112.72 ? 399 PRO B O     1 
ATOM   7287 C  CB    . PRO B 1 372 ? 59.117  97.394  104.204 1.00 113.07 ? 399 PRO B CB    1 
ATOM   7288 C  CG    . PRO B 1 372 ? 57.780  97.194  104.826 1.00 122.24 ? 399 PRO B CG    1 
ATOM   7289 C  CD    . PRO B 1 372 ? 56.774  97.661  103.813 1.00 117.38 ? 399 PRO B CD    1 
ATOM   7290 N  N     . TYR B 1 373 ? 59.259  98.379  100.901 1.00 131.58 ? 400 TYR B N     1 
ATOM   7291 C  CA    . TYR B 1 373 ? 60.053  98.227  99.688  1.00 123.92 ? 400 TYR B CA    1 
ATOM   7292 C  C     . TYR B 1 373 ? 59.636  99.228  98.619  1.00 127.76 ? 400 TYR B C     1 
ATOM   7293 O  O     . TYR B 1 373 ? 60.436  99.579  97.745  1.00 132.22 ? 400 TYR B O     1 
ATOM   7294 C  CB    . TYR B 1 373 ? 59.933  96.797  99.157  1.00 127.36 ? 400 TYR B CB    1 
ATOM   7295 C  CG    . TYR B 1 373 ? 60.443  95.753  100.124 1.00 129.09 ? 400 TYR B CG    1 
ATOM   7296 C  CD1   . TYR B 1 373 ? 61.778  95.371  100.121 1.00 130.71 ? 400 TYR B CD1   1 
ATOM   7297 C  CD2   . TYR B 1 373 ? 59.594  95.155  101.046 1.00 128.20 ? 400 TYR B CD2   1 
ATOM   7298 C  CE1   . TYR B 1 373 ? 62.252  94.421  101.004 1.00 129.56 ? 400 TYR B CE1   1 
ATOM   7299 C  CE2   . TYR B 1 373 ? 60.059  94.203  101.934 1.00 139.24 ? 400 TYR B CE2   1 
ATOM   7300 C  CZ    . TYR B 1 373 ? 61.389  93.840  101.908 1.00 139.10 ? 400 TYR B CZ    1 
ATOM   7301 O  OH    . TYR B 1 373 ? 61.860  92.893  102.788 1.00 145.10 ? 400 TYR B OH    1 
ATOM   7302 N  N     . HIS B 1 374 ? 58.390  99.701  98.680  1.00 138.57 ? 401 HIS B N     1 
ATOM   7303 C  CA    . HIS B 1 374 ? 57.887  100.648 97.697  1.00 142.72 ? 401 HIS B CA    1 
ATOM   7304 C  C     . HIS B 1 374 ? 57.179  101.853 98.303  1.00 145.63 ? 401 HIS B C     1 
ATOM   7305 O  O     . HIS B 1 374 ? 56.674  102.691 97.549  1.00 146.11 ? 401 HIS B O     1 
ATOM   7306 C  CB    . HIS B 1 374 ? 56.940  99.943  96.713  1.00 144.64 ? 401 HIS B CB    1 
ATOM   7307 C  CG    . HIS B 1 374 ? 57.577  98.807  95.974  1.00 144.04 ? 401 HIS B CG    1 
ATOM   7308 N  ND1   . HIS B 1 374 ? 58.276  98.981  94.798  1.00 139.62 ? 401 HIS B ND1   1 
ATOM   7309 C  CD2   . HIS B 1 374 ? 57.628  97.482  96.249  1.00 144.29 ? 401 HIS B CD2   1 
ATOM   7310 C  CE1   . HIS B 1 374 ? 58.726  97.812  94.378  1.00 143.48 ? 401 HIS B CE1   1 
ATOM   7311 N  NE2   . HIS B 1 374 ? 58.347  96.886  95.241  1.00 146.67 ? 401 HIS B NE2   1 
ATOM   7312 N  N     . GLY B 1 375 ? 57.125  101.968 99.629  1.00 137.90 ? 402 GLY B N     1 
ATOM   7313 C  CA    . GLY B 1 375 ? 56.538  103.135 100.264 1.00 130.09 ? 402 GLY B CA    1 
ATOM   7314 C  C     . GLY B 1 375 ? 55.080  103.377 99.946  1.00 123.33 ? 402 GLY B C     1 
ATOM   7315 O  O     . GLY B 1 375 ? 54.591  104.494 100.136 1.00 131.37 ? 402 GLY B O     1 
ATOM   7316 N  N     . ARG B 1 376 ? 54.366  102.358 99.466  1.00 129.32 ? 403 ARG B N     1 
ATOM   7317 C  CA    . ARG B 1 376 ? 52.978  102.456 99.046  1.00 124.43 ? 403 ARG B CA    1 
ATOM   7318 C  C     . ARG B 1 376 ? 52.035  102.234 100.225 1.00 117.56 ? 403 ARG B C     1 
ATOM   7319 O  O     . ARG B 1 376 ? 52.382  101.539 101.185 1.00 112.33 ? 403 ARG B O     1 
ATOM   7320 C  CB    . ARG B 1 376 ? 52.686  101.430 97.955  1.00 127.59 ? 403 ARG B CB    1 
ATOM   7321 C  CG    . ARG B 1 376 ? 53.493  101.641 96.688  1.00 132.56 ? 403 ARG B CG    1 
ATOM   7322 C  CD    . ARG B 1 376 ? 53.177  100.591 95.634  1.00 145.32 ? 403 ARG B CD    1 
ATOM   7323 N  NE    . ARG B 1 376 ? 51.743  100.422 95.437  1.00 146.44 ? 403 ARG B NE    1 
ATOM   7324 C  CZ    . ARG B 1 376 ? 51.072  99.318  95.734  1.00 137.97 ? 403 ARG B CZ    1 
ATOM   7325 N  NH1   . ARG B 1 376 ? 51.682  98.246  96.214  1.00 125.75 ? 403 ARG B NH1   1 
ATOM   7326 N  NH2   . ARG B 1 376 ? 49.757  99.286  95.539  1.00 143.01 ? 403 ARG B NH2   1 
ATOM   7327 N  N     . PRO B 1 377 ? 50.837  102.820 100.180 1.00 114.10 ? 404 PRO B N     1 
ATOM   7328 C  CA    . PRO B 1 377 ? 49.877  102.615 101.273 1.00 110.18 ? 404 PRO B CA    1 
ATOM   7329 C  C     . PRO B 1 377 ? 49.367  101.184 101.332 1.00 110.35 ? 404 PRO B C     1 
ATOM   7330 O  O     . PRO B 1 377 ? 49.728  100.349 100.497 1.00 107.57 ? 404 PRO B O     1 
ATOM   7331 C  CB    . PRO B 1 377 ? 48.746  103.601 100.946 1.00 107.99 ? 404 PRO B CB    1 
ATOM   7332 C  CG    . PRO B 1 377 ? 49.341  104.573 99.973  1.00 108.76 ? 404 PRO B CG    1 
ATOM   7333 C  CD    . PRO B 1 377 ? 50.357  103.805 99.198  1.00 110.60 ? 404 PRO B CD    1 
ATOM   7334 N  N     . LEU B 1 378 ? 48.527  100.891 102.321 1.00 107.17 ? 405 LEU B N     1 
ATOM   7335 C  CA    . LEU B 1 378 ? 47.968  99.553  102.456 1.00 107.49 ? 405 LEU B CA    1 
ATOM   7336 C  C     . LEU B 1 378 ? 46.976  99.282  101.332 1.00 96.39  ? 405 LEU B C     1 
ATOM   7337 O  O     . LEU B 1 378 ? 46.118  100.116 101.029 1.00 94.27  ? 405 LEU B O     1 
ATOM   7338 C  CB    . LEU B 1 378 ? 47.291  99.398  103.816 1.00 98.42  ? 405 LEU B CB    1 
ATOM   7339 C  CG    . LEU B 1 378 ? 46.664  98.036  104.105 1.00 97.67  ? 405 LEU B CG    1 
ATOM   7340 C  CD1   . LEU B 1 378 ? 47.273  97.421  105.351 1.00 94.38  ? 405 LEU B CD1   1 
ATOM   7341 C  CD2   . LEU B 1 378 ? 45.157  98.165  104.249 1.00 89.33  ? 405 LEU B CD2   1 
ATOM   7342 N  N     . THR B 1 379 ? 47.096  98.112  100.713 1.00 89.82  ? 406 THR B N     1 
ATOM   7343 C  CA    . THR B 1 379 ? 46.265  97.752  99.575  1.00 96.38  ? 406 THR B CA    1 
ATOM   7344 C  C     . THR B 1 379 ? 44.995  97.038  100.031 1.00 98.65  ? 406 THR B C     1 
ATOM   7345 O  O     . THR B 1 379 ? 44.892  96.557  101.163 1.00 100.97 ? 406 THR B O     1 
ATOM   7346 C  CB    . THR B 1 379 ? 47.037  96.859  98.602  1.00 93.77  ? 406 THR B CB    1 
ATOM   7347 O  OG1   . THR B 1 379 ? 46.900  95.487  98.997  1.00 82.41  ? 406 THR B OG1   1 
ATOM   7348 C  CG2   . THR B 1 379 ? 48.514  97.229  98.601  1.00 83.90  ? 406 THR B CG2   1 
ATOM   7349 N  N     . LYS B 1 380 ? 44.019  96.973  99.119  1.00 97.99  ? 407 LYS B N     1 
ATOM   7350 C  CA    . LYS B 1 380 ? 42.792  96.231  99.395  1.00 95.34  ? 407 LYS B CA    1 
ATOM   7351 C  C     . LYS B 1 380 ? 43.072  94.748  99.608  1.00 89.79  ? 407 LYS B C     1 
ATOM   7352 O  O     . LYS B 1 380 ? 42.377  94.092  100.393 1.00 92.69  ? 407 LYS B O     1 
ATOM   7353 C  CB    . LYS B 1 380 ? 41.791  96.423  98.253  1.00 103.33 ? 407 LYS B CB    1 
ATOM   7354 C  CG    . LYS B 1 380 ? 41.320  97.857  98.046  1.00 82.98  ? 407 LYS B CG    1 
ATOM   7355 C  CD    . LYS B 1 380 ? 40.372  98.308  99.145  1.00 102.72 ? 407 LYS B CD    1 
ATOM   7356 C  CE    . LYS B 1 380 ? 39.856  99.714  98.875  1.00 131.62 ? 407 LYS B CE    1 
ATOM   7357 N  NZ    . LYS B 1 380 ? 39.018  100.232 99.993  1.00 128.17 ? 407 LYS B NZ    1 
ATOM   7358 N  N     . GLY B 1 381 ? 44.079  94.204  98.923  1.00 83.68  ? 408 GLY B N     1 
ATOM   7359 C  CA    . GLY B 1 381 ? 44.425  92.804  99.117  1.00 84.13  ? 408 GLY B CA    1 
ATOM   7360 C  C     . GLY B 1 381 ? 44.953  92.523  100.511 1.00 91.85  ? 408 GLY B C     1 
ATOM   7361 O  O     . GLY B 1 381 ? 44.547  91.553  101.160 1.00 83.20  ? 408 GLY B O     1 
ATOM   7362 N  N     . GLU B 1 382 ? 45.870  93.370  100.992 1.00 81.17  ? 409 GLU B N     1 
ATOM   7363 C  CA    . GLU B 1 382 ? 46.358  93.233  102.361 1.00 73.81  ? 409 GLU B CA    1 
ATOM   7364 C  C     . GLU B 1 382 ? 45.233  93.420  103.368 1.00 91.31  ? 409 GLU B C     1 
ATOM   7365 O  O     . GLU B 1 382 ? 45.255  92.814  104.446 1.00 74.88  ? 409 GLU B O     1 
ATOM   7366 C  CB    . GLU B 1 382 ? 47.476  94.240  102.626 1.00 84.61  ? 409 GLU B CB    1 
ATOM   7367 C  CG    . GLU B 1 382 ? 48.709  94.050  101.761 1.00 73.59  ? 409 GLU B CG    1 
ATOM   7368 C  CD    . GLU B 1 382 ? 49.694  95.200  101.885 1.00 101.44 ? 409 GLU B CD    1 
ATOM   7369 O  OE1   . GLU B 1 382 ? 49.323  96.254  102.446 1.00 107.05 ? 409 GLU B OE1   1 
ATOM   7370 O  OE2   . GLU B 1 382 ? 50.842  95.048  101.417 1.00 98.02  ? 409 GLU B OE2   1 
ATOM   7371 N  N     . LEU B 1 383 ? 44.245  94.253  103.035 1.00 82.39  ? 410 LEU B N     1 
ATOM   7372 C  CA    . LEU B 1 383 ? 43.092  94.434  103.912 1.00 77.77  ? 410 LEU B CA    1 
ATOM   7373 C  C     . LEU B 1 383 ? 42.297  93.141  104.043 1.00 81.03  ? 410 LEU B C     1 
ATOM   7374 O  O     . LEU B 1 383 ? 42.000  92.692  105.156 1.00 76.34  ? 410 LEU B O     1 
ATOM   7375 C  CB    . LEU B 1 383 ? 42.204  95.561  103.382 1.00 83.95  ? 410 LEU B CB    1 
ATOM   7376 C  CG    . LEU B 1 383 ? 40.830  95.702  104.038 1.00 90.95  ? 410 LEU B CG    1 
ATOM   7377 C  CD1   . LEU B 1 383 ? 40.973  96.123  105.490 1.00 86.29  ? 410 LEU B CD1   1 
ATOM   7378 C  CD2   . LEU B 1 383 ? 39.964  96.687  103.266 1.00 87.11  ? 410 LEU B CD2   1 
ATOM   7379 N  N     . GLY B 1 384 ? 41.945  92.529  102.909 1.00 76.84  ? 411 GLY B N     1 
ATOM   7380 C  CA    . GLY B 1 384 ? 41.170  91.299  102.949 1.00 77.04  ? 411 GLY B CA    1 
ATOM   7381 C  C     . GLY B 1 384 ? 41.914  90.161  103.620 1.00 75.27  ? 411 GLY B C     1 
ATOM   7382 O  O     . GLY B 1 384 ? 41.325  89.377  104.369 1.00 71.73  ? 411 GLY B O     1 
ATOM   7383 N  N     . CYS B 1 385 ? 43.222  90.060  103.366 1.00 75.45  ? 412 CYS B N     1 
ATOM   7384 C  CA    . CYS B 1 385 ? 44.024  89.036  104.024 1.00 79.78  ? 412 CYS B CA    1 
ATOM   7385 C  C     . CYS B 1 385 ? 44.015  89.229  105.535 1.00 71.37  ? 412 CYS B C     1 
ATOM   7386 O  O     . CYS B 1 385 ? 43.873  88.261  106.292 1.00 73.58  ? 412 CYS B O     1 
ATOM   7387 C  CB    . CYS B 1 385 ? 45.452  89.062  103.479 1.00 74.82  ? 412 CYS B CB    1 
ATOM   7388 S  SG    . CYS B 1 385 ? 46.413  87.560  103.796 1.00 95.87  ? 412 CYS B SG    1 
ATOM   7389 N  N     . PHE B 1 386 ? 44.138  90.478  105.991 1.00 73.13  ? 413 PHE B N     1 
ATOM   7390 C  CA    . PHE B 1 386 ? 44.058  90.765  107.419 1.00 73.90  ? 413 PHE B CA    1 
ATOM   7391 C  C     . PHE B 1 386 ? 42.699  90.365  107.981 1.00 70.78  ? 413 PHE B C     1 
ATOM   7392 O  O     . PHE B 1 386 ? 42.615  89.689  109.013 1.00 74.45  ? 413 PHE B O     1 
ATOM   7393 C  CB    . PHE B 1 386 ? 44.324  92.251  107.666 1.00 81.83  ? 413 PHE B CB    1 
ATOM   7394 C  CG    . PHE B 1 386 ? 44.554  92.596  109.109 1.00 74.15  ? 413 PHE B CG    1 
ATOM   7395 C  CD1   . PHE B 1 386 ? 43.488  92.810  109.968 1.00 71.41  ? 413 PHE B CD1   1 
ATOM   7396 C  CD2   . PHE B 1 386 ? 45.841  92.715  109.604 1.00 82.02  ? 413 PHE B CD2   1 
ATOM   7397 C  CE1   . PHE B 1 386 ? 43.704  93.127  111.292 1.00 84.58  ? 413 PHE B CE1   1 
ATOM   7398 C  CE2   . PHE B 1 386 ? 46.062  93.032  110.926 1.00 78.29  ? 413 PHE B CE2   1 
ATOM   7399 C  CZ    . PHE B 1 386 ? 44.994  93.237  111.769 1.00 82.91  ? 413 PHE B CZ    1 
ATOM   7400 N  N     . LEU B 1 387 ? 41.620  90.778  107.311 1.00 76.21  ? 414 LEU B N     1 
ATOM   7401 C  CA    . LEU B 1 387 ? 40.280  90.447  107.784 1.00 72.39  ? 414 LEU B CA    1 
ATOM   7402 C  C     . LEU B 1 387 ? 40.055  88.943  107.827 1.00 70.98  ? 414 LEU B C     1 
ATOM   7403 O  O     . LEU B 1 387 ? 39.301  88.455  108.676 1.00 65.29  ? 414 LEU B O     1 
ATOM   7404 C  CB    . LEU B 1 387 ? 39.230  91.117  106.897 1.00 71.61  ? 414 LEU B CB    1 
ATOM   7405 C  CG    . LEU B 1 387 ? 39.224  92.647  106.921 1.00 82.36  ? 414 LEU B CG    1 
ATOM   7406 C  CD1   . LEU B 1 387 ? 38.174  93.196  105.971 1.00 80.88  ? 414 LEU B CD1   1 
ATOM   7407 C  CD2   . LEU B 1 387 ? 38.995  93.163  108.335 1.00 76.68  ? 414 LEU B CD2   1 
ATOM   7408 N  N     . SER B 1 388 ? 40.698  88.194  106.929 1.00 70.97  ? 415 SER B N     1 
ATOM   7409 C  CA    . SER B 1 388 ? 40.586  86.740  106.963 1.00 65.47  ? 415 SER B CA    1 
ATOM   7410 C  C     . SER B 1 388 ? 41.193  86.178  108.242 1.00 61.31  ? 415 SER B C     1 
ATOM   7411 O  O     . SER B 1 388 ? 40.574  85.359  108.931 1.00 65.04  ? 415 SER B O     1 
ATOM   7412 C  CB    . SER B 1 388 ? 41.257  86.137  105.729 1.00 63.24  ? 415 SER B CB    1 
ATOM   7413 O  OG    . SER B 1 388 ? 40.708  86.681  104.542 1.00 72.24  ? 415 SER B OG    1 
ATOM   7414 N  N     . HIS B 1 389 ? 42.408  86.617  108.580 1.00 62.45  ? 416 HIS B N     1 
ATOM   7415 C  CA    . HIS B 1 389 ? 43.018  86.203  109.840 1.00 68.07  ? 416 HIS B CA    1 
ATOM   7416 C  C     . HIS B 1 389 ? 42.244  86.754  111.031 1.00 68.69  ? 416 HIS B C     1 
ATOM   7417 O  O     . HIS B 1 389 ? 42.128  86.088  112.066 1.00 63.94  ? 416 HIS B O     1 
ATOM   7418 C  CB    . HIS B 1 389 ? 44.479  86.656  109.891 1.00 71.51  ? 416 HIS B CB    1 
ATOM   7419 C  CG    . HIS B 1 389 ? 45.367  85.968  108.899 1.00 71.10  ? 416 HIS B CG    1 
ATOM   7420 N  ND1   . HIS B 1 389 ? 46.254  84.976  109.258 1.00 59.61  ? 416 HIS B ND1   1 
ATOM   7421 C  CD2   . HIS B 1 389 ? 45.510  86.135  107.563 1.00 70.59  ? 416 HIS B CD2   1 
ATOM   7422 C  CE1   . HIS B 1 389 ? 46.902  84.559  108.185 1.00 69.19  ? 416 HIS B CE1   1 
ATOM   7423 N  NE2   . HIS B 1 389 ? 46.470  85.246  107.144 1.00 70.46  ? 416 HIS B NE2   1 
ATOM   7424 N  N     . TYR B 1 390 ? 41.705  87.970  110.899 1.00 69.61  ? 417 TYR B N     1 
ATOM   7425 C  CA    . TYR B 1 390 ? 40.922  88.566  111.976 1.00 76.66  ? 417 TYR B CA    1 
ATOM   7426 C  C     . TYR B 1 390 ? 39.679  87.737  112.281 1.00 71.05  ? 417 TYR B C     1 
ATOM   7427 O  O     . TYR B 1 390 ? 39.341  87.520  113.451 1.00 67.00  ? 417 TYR B O     1 
ATOM   7428 C  CB    . TYR B 1 390 ? 40.544  90.002  111.604 1.00 72.80  ? 417 TYR B CB    1 
ATOM   7429 C  CG    . TYR B 1 390 ? 39.567  90.667  112.548 1.00 71.49  ? 417 TYR B CG    1 
ATOM   7430 C  CD1   . TYR B 1 390 ? 39.998  91.233  113.741 1.00 78.94  ? 417 TYR B CD1   1 
ATOM   7431 C  CD2   . TYR B 1 390 ? 38.215  90.742  112.238 1.00 71.05  ? 417 TYR B CD2   1 
ATOM   7432 C  CE1   . TYR B 1 390 ? 39.106  91.847  114.603 1.00 76.62  ? 417 TYR B CE1   1 
ATOM   7433 C  CE2   . TYR B 1 390 ? 37.317  91.352  113.093 1.00 73.46  ? 417 TYR B CE2   1 
ATOM   7434 C  CZ    . TYR B 1 390 ? 37.767  91.903  114.275 1.00 87.03  ? 417 TYR B CZ    1 
ATOM   7435 O  OH    . TYR B 1 390 ? 36.874  92.511  115.127 1.00 97.90  ? 417 TYR B OH    1 
ATOM   7436 N  N     . ASN B 1 391 ? 38.989  87.261  111.240 1.00 71.37  ? 418 ASN B N     1 
ATOM   7437 C  CA    . ASN B 1 391 ? 37.801  86.441  111.454 1.00 70.60  ? 418 ASN B CA    1 
ATOM   7438 C  C     . ASN B 1 391 ? 38.147  85.118  112.122 1.00 70.53  ? 418 ASN B C     1 
ATOM   7439 O  O     . ASN B 1 391 ? 37.347  84.591  112.904 1.00 70.41  ? 418 ASN B O     1 
ATOM   7440 C  CB    . ASN B 1 391 ? 37.080  86.194  110.128 1.00 64.50  ? 418 ASN B CB    1 
ATOM   7441 C  CG    . ASN B 1 391 ? 36.569  87.474  109.495 1.00 75.32  ? 418 ASN B CG    1 
ATOM   7442 O  OD1   . ASN B 1 391 ? 36.431  88.498  110.163 1.00 82.22  ? 418 ASN B OD1   1 
ATOM   7443 N  ND2   . ASN B 1 391 ? 36.283  87.420  108.198 1.00 77.34  ? 418 ASN B ND2   1 
ATOM   7444 N  N     . ILE B 1 392 ? 39.328  84.566  111.832 1.00 68.08  ? 419 ILE B N     1 
ATOM   7445 C  CA    . ILE B 1 392 ? 39.743  83.332  112.491 1.00 62.23  ? 419 ILE B CA    1 
ATOM   7446 C  C     . ILE B 1 392 ? 40.026  83.586  113.965 1.00 62.90  ? 419 ILE B C     1 
ATOM   7447 O  O     . ILE B 1 392 ? 39.609  82.808  114.832 1.00 72.55  ? 419 ILE B O     1 
ATOM   7448 C  CB    . ILE B 1 392 ? 40.958  82.718  111.773 1.00 66.56  ? 419 ILE B CB    1 
ATOM   7449 C  CG1   . ILE B 1 392 ? 40.577  82.313  110.350 1.00 62.20  ? 419 ILE B CG1   1 
ATOM   7450 C  CG2   . ILE B 1 392 ? 41.485  81.519  112.544 1.00 63.42  ? 419 ILE B CG2   1 
ATOM   7451 C  CD1   . ILE B 1 392 ? 41.630  81.488  109.655 1.00 59.39  ? 419 ILE B CD1   1 
ATOM   7452 N  N     . TRP B 1 393 ? 40.736  84.677  114.275 1.00 63.92  ? 420 TRP B N     1 
ATOM   7453 C  CA    . TRP B 1 393 ? 40.937  85.055  115.671 1.00 65.62  ? 420 TRP B CA    1 
ATOM   7454 C  C     . TRP B 1 393 ? 39.603  85.226  116.383 1.00 74.05  ? 420 TRP B C     1 
ATOM   7455 O  O     . TRP B 1 393 ? 39.441  84.799  117.533 1.00 72.86  ? 420 TRP B O     1 
ATOM   7456 C  CB    . TRP B 1 393 ? 41.744  86.350  115.768 1.00 73.72  ? 420 TRP B CB    1 
ATOM   7457 C  CG    . TRP B 1 393 ? 43.005  86.381  114.961 1.00 75.97  ? 420 TRP B CG    1 
ATOM   7458 C  CD1   . TRP B 1 393 ? 43.738  85.314  114.530 1.00 68.16  ? 420 TRP B CD1   1 
ATOM   7459 C  CD2   . TRP B 1 393 ? 43.678  87.551  114.481 1.00 81.30  ? 420 TRP B CD2   1 
ATOM   7460 N  NE1   . TRP B 1 393 ? 44.828  85.748  113.813 1.00 70.82  ? 420 TRP B NE1   1 
ATOM   7461 C  CE2   . TRP B 1 393 ? 44.814  87.118  113.769 1.00 76.46  ? 420 TRP B CE2   1 
ATOM   7462 C  CE3   . TRP B 1 393 ? 43.430  88.924  114.587 1.00 71.90  ? 420 TRP B CE3   1 
ATOM   7463 C  CZ2   . TRP B 1 393 ? 45.701  88.008  113.165 1.00 69.97  ? 420 TRP B CZ2   1 
ATOM   7464 C  CZ3   . TRP B 1 393 ? 44.311  89.807  113.986 1.00 73.92  ? 420 TRP B CZ3   1 
ATOM   7465 C  CH2   . TRP B 1 393 ? 45.432  89.345  113.284 1.00 80.24  ? 420 TRP B CH2   1 
ATOM   7466 N  N     . LYS B 1 394 ? 38.636  85.854  115.710 1.00 75.13  ? 421 LYS B N     1 
ATOM   7467 C  CA    . LYS B 1 394 ? 37.301  85.993  116.279 1.00 69.18  ? 421 LYS B CA    1 
ATOM   7468 C  C     . LYS B 1 394 ? 36.657  84.632  116.513 1.00 68.57  ? 421 LYS B C     1 
ATOM   7469 O  O     . LYS B 1 394 ? 36.041  84.401  117.559 1.00 78.18  ? 421 LYS B O     1 
ATOM   7470 C  CB    . LYS B 1 394 ? 36.430  86.850  115.362 1.00 69.78  ? 421 LYS B CB    1 
ATOM   7471 C  CG    . LYS B 1 394 ? 36.166  88.251  115.881 1.00 72.11  ? 421 LYS B CG    1 
ATOM   7472 C  CD    . LYS B 1 394 ? 35.215  88.999  114.963 1.00 87.62  ? 421 LYS B CD    1 
ATOM   7473 C  CE    . LYS B 1 394 ? 34.585  90.185  115.671 1.00 98.22  ? 421 LYS B CE    1 
ATOM   7474 N  NZ    . LYS B 1 394 ? 33.628  90.911  114.790 1.00 110.93 ? 421 LYS B NZ    1 
ATOM   7475 N  N     . GLU B 1 395 ? 36.797  83.712  115.555 1.00 75.08  ? 422 GLU B N     1 
ATOM   7476 C  CA    . GLU B 1 395 ? 36.207  82.387  115.720 1.00 70.99  ? 422 GLU B CA    1 
ATOM   7477 C  C     . GLU B 1 395 ? 36.913  81.597  116.815 1.00 75.93  ? 422 GLU B C     1 
ATOM   7478 O  O     . GLU B 1 395 ? 36.271  80.825  117.538 1.00 73.21  ? 422 GLU B O     1 
ATOM   7479 C  CB    . GLU B 1 395 ? 36.242  81.618  114.399 1.00 64.20  ? 422 GLU B CB    1 
ATOM   7480 C  CG    . GLU B 1 395 ? 35.656  80.216  114.505 1.00 76.62  ? 422 GLU B CG    1 
ATOM   7481 C  CD    . GLU B 1 395 ? 35.500  79.530  113.165 1.00 81.39  ? 422 GLU B CD    1 
ATOM   7482 O  OE1   . GLU B 1 395 ? 35.686  80.200  112.128 1.00 90.23  ? 422 GLU B OE1   1 
ATOM   7483 O  OE2   . GLU B 1 395 ? 35.190  78.319  113.153 1.00 72.90  ? 422 GLU B OE2   1 
ATOM   7484 N  N     . VAL B 1 396 ? 38.230  81.774  116.951 1.00 73.01  ? 423 VAL B N     1 
ATOM   7485 C  CA    . VAL B 1 396 ? 38.966  81.099  118.018 1.00 75.05  ? 423 VAL B CA    1 
ATOM   7486 C  C     . VAL B 1 396 ? 38.418  81.504  119.381 1.00 81.60  ? 423 VAL B C     1 
ATOM   7487 O  O     . VAL B 1 396 ? 38.239  80.663  120.271 1.00 86.84  ? 423 VAL B O     1 
ATOM   7488 C  CB    . VAL B 1 396 ? 40.473  81.396  117.900 1.00 71.32  ? 423 VAL B CB    1 
ATOM   7489 C  CG1   . VAL B 1 396 ? 41.199  81.004  119.178 1.00 81.51  ? 423 VAL B CG1   1 
ATOM   7490 C  CG2   . VAL B 1 396 ? 41.069  80.660  116.710 1.00 63.07  ? 423 VAL B CG2   1 
ATOM   7491 N  N     . VAL B 1 397 ? 38.124  82.792  119.560 1.00 81.62  ? 424 VAL B N     1 
ATOM   7492 C  CA    . VAL B 1 397 ? 37.645  83.274  120.851 1.00 76.47  ? 424 VAL B CA    1 
ATOM   7493 C  C     . VAL B 1 397 ? 36.186  82.885  121.082 1.00 79.95  ? 424 VAL B C     1 
ATOM   7494 O  O     . VAL B 1 397 ? 35.782  82.628  122.223 1.00 84.28  ? 424 VAL B O     1 
ATOM   7495 C  CB    . VAL B 1 397 ? 37.857  84.795  120.951 1.00 76.33  ? 424 VAL B CB    1 
ATOM   7496 C  CG1   . VAL B 1 397 ? 37.258  85.346  122.235 1.00 76.50  ? 424 VAL B CG1   1 
ATOM   7497 C  CG2   . VAL B 1 397 ? 39.340  85.122  120.880 1.00 75.05  ? 424 VAL B CG2   1 
ATOM   7498 N  N     . ASP B 1 398 ? 35.379  82.817  120.020 1.00 74.71  ? 425 ASP B N     1 
ATOM   7499 C  CA    . ASP B 1 398 ? 33.977  82.443  120.185 1.00 83.07  ? 425 ASP B CA    1 
ATOM   7500 C  C     . ASP B 1 398 ? 33.834  80.978  120.582 1.00 88.06  ? 425 ASP B C     1 
ATOM   7501 O  O     . ASP B 1 398 ? 33.054  80.648  121.483 1.00 87.02  ? 425 ASP B O     1 
ATOM   7502 C  CB    . ASP B 1 398 ? 33.201  82.729  118.899 1.00 82.46  ? 425 ASP B CB    1 
ATOM   7503 C  CG    . ASP B 1 398 ? 33.152  84.207  118.566 1.00 106.27 ? 425 ASP B CG    1 
ATOM   7504 O  OD1   . ASP B 1 398 ? 33.696  85.012  119.350 1.00 111.14 ? 425 ASP B OD1   1 
ATOM   7505 O  OD2   . ASP B 1 398 ? 32.572  84.565  117.519 1.00 114.74 ? 425 ASP B OD2   1 
ATOM   7506 N  N     . ARG B 1 399 ? 34.578  80.088  119.925 1.00 81.08  ? 426 ARG B N     1 
ATOM   7507 C  CA    . ARG B 1 399 ? 34.512  78.664  120.228 1.00 77.29  ? 426 ARG B CA    1 
ATOM   7508 C  C     . ARG B 1 399 ? 35.416  78.257  121.384 1.00 87.01  ? 426 ARG B C     1 
ATOM   7509 O  O     . ARG B 1 399 ? 35.334  77.109  121.836 1.00 91.65  ? 426 ARG B O     1 
ATOM   7510 C  CB    . ARG B 1 399 ? 34.872  77.846  118.986 1.00 75.87  ? 426 ARG B CB    1 
ATOM   7511 C  CG    . ARG B 1 399 ? 33.855  77.952  117.861 1.00 75.53  ? 426 ARG B CG    1 
ATOM   7512 C  CD    . ARG B 1 399 ? 34.442  77.494  116.536 1.00 74.06  ? 426 ARG B CD    1 
ATOM   7513 N  NE    . ARG B 1 399 ? 34.920  76.118  116.581 1.00 71.54  ? 426 ARG B NE    1 
ATOM   7514 C  CZ    . ARG B 1 399 ? 35.557  75.517  115.586 1.00 81.08  ? 426 ARG B CZ    1 
ATOM   7515 N  NH1   . ARG B 1 399 ? 35.815  76.145  114.450 1.00 88.43  ? 426 ARG B NH1   1 
ATOM   7516 N  NH2   . ARG B 1 399 ? 35.949  74.254  115.735 1.00 86.92  ? 426 ARG B NH2   1 
ATOM   7517 N  N     . GLY B 1 400 ? 36.265  79.157  121.872 1.00 75.46  ? 427 GLY B N     1 
ATOM   7518 C  CA    . GLY B 1 400 ? 37.149  78.825  122.974 1.00 77.76  ? 427 GLY B CA    1 
ATOM   7519 C  C     . GLY B 1 400 ? 38.235  77.834  122.623 1.00 91.99  ? 427 GLY B C     1 
ATOM   7520 O  O     . GLY B 1 400 ? 38.658  77.056  123.484 1.00 97.86  ? 427 GLY B O     1 
ATOM   7521 N  N     . LEU B 1 401 ? 38.698  77.841  121.376 1.00 88.56  ? 428 LEU B N     1 
ATOM   7522 C  CA    . LEU B 1 401 ? 39.738  76.918  120.940 1.00 82.66  ? 428 LEU B CA    1 
ATOM   7523 C  C     . LEU B 1 401 ? 41.055  77.259  121.626 1.00 87.14  ? 428 LEU B C     1 
ATOM   7524 O  O     . LEU B 1 401 ? 41.590  78.358  121.444 1.00 97.15  ? 428 LEU B O     1 
ATOM   7525 C  CB    . LEU B 1 401 ? 39.888  76.985  119.424 1.00 80.24  ? 428 LEU B CB    1 
ATOM   7526 C  CG    . LEU B 1 401 ? 38.583  77.002  118.627 1.00 77.17  ? 428 LEU B CG    1 
ATOM   7527 C  CD1   . LEU B 1 401 ? 38.859  77.301  117.163 1.00 78.75  ? 428 LEU B CD1   1 
ATOM   7528 C  CD2   . LEU B 1 401 ? 37.843  75.683  118.778 1.00 70.82  ? 428 LEU B CD2   1 
ATOM   7529 N  N     . GLN B 1 402 ? 41.581  76.316  122.409 1.00 77.48  ? 429 GLN B N     1 
ATOM   7530 C  CA    . GLN B 1 402 ? 42.799  76.580  123.169 1.00 87.64  ? 429 GLN B CA    1 
ATOM   7531 C  C     . GLN B 1 402 ? 44.011  76.688  122.252 1.00 89.11  ? 429 GLN B C     1 
ATOM   7532 O  O     . GLN B 1 402 ? 44.825  77.608  122.392 1.00 89.91  ? 429 GLN B O     1 
ATOM   7533 C  CB    . GLN B 1 402 ? 43.011  75.489  124.220 1.00 93.10  ? 429 GLN B CB    1 
ATOM   7534 C  CG    . GLN B 1 402 ? 41.804  75.239  125.116 1.00 100.05 ? 429 GLN B CG    1 
ATOM   7535 C  CD    . GLN B 1 402 ? 41.359  76.478  125.876 1.00 113.79 ? 429 GLN B CD    1 
ATOM   7536 O  OE1   . GLN B 1 402 ? 42.154  77.379  126.146 1.00 114.00 ? 429 GLN B OE1   1 
ATOM   7537 N  NE2   . GLN B 1 402 ? 40.077  76.526  126.224 1.00 111.93 ? 429 GLN B NE2   1 
ATOM   7538 N  N     . LYS B 1 403 ? 44.156  75.757  121.312 1.00 87.24  ? 430 LYS B N     1 
ATOM   7539 C  CA    . LYS B 1 403 ? 45.251  75.781  120.351 1.00 84.12  ? 430 LYS B CA    1 
ATOM   7540 C  C     . LYS B 1 403 ? 44.707  75.495  118.960 1.00 78.37  ? 430 LYS B C     1 
ATOM   7541 O  O     . LYS B 1 403 ? 44.034  74.481  118.748 1.00 80.91  ? 430 LYS B O     1 
ATOM   7542 C  CB    . LYS B 1 403 ? 46.344  74.768  120.721 1.00 81.10  ? 430 LYS B CB    1 
ATOM   7543 C  CG    . LYS B 1 403 ? 45.828  73.400  121.131 1.00 78.86  ? 430 LYS B CG    1 
ATOM   7544 C  CD    . LYS B 1 403 ? 46.967  72.404  121.267 1.00 86.92  ? 430 LYS B CD    1 
ATOM   7545 C  CE    . LYS B 1 403 ? 46.451  71.030  121.653 1.00 93.09  ? 430 LYS B CE    1 
ATOM   7546 N  NZ    . LYS B 1 403 ? 47.515  69.993  121.560 1.00 90.95  ? 430 LYS B NZ    1 
ATOM   7547 N  N     . SER B 1 404 ? 44.995  76.390  118.018 1.00 78.70  ? 431 SER B N     1 
ATOM   7548 C  CA    . SER B 1 404 ? 44.542  76.255  116.643 1.00 66.31  ? 431 SER B CA    1 
ATOM   7549 C  C     . SER B 1 404 ? 45.719  76.438  115.696 1.00 62.34  ? 431 SER B C     1 
ATOM   7550 O  O     . SER B 1 404 ? 46.637  77.217  115.964 1.00 66.98  ? 431 SER B O     1 
ATOM   7551 C  CB    . SER B 1 404 ? 43.446  77.275  116.306 1.00 67.20  ? 431 SER B CB    1 
ATOM   7552 O  OG    . SER B 1 404 ? 42.336  77.143  117.178 1.00 83.79  ? 431 SER B OG    1 
ATOM   7553 N  N     . LEU B 1 405 ? 45.683  75.710  114.584 1.00 68.49  ? 432 LEU B N     1 
ATOM   7554 C  CA    . LEU B 1 405 ? 46.672  75.834  113.522 1.00 63.61  ? 432 LEU B CA    1 
ATOM   7555 C  C     . LEU B 1 405 ? 46.028  76.525  112.329 1.00 59.58  ? 432 LEU B C     1 
ATOM   7556 O  O     . LEU B 1 405 ? 44.913  76.170  111.933 1.00 56.15  ? 432 LEU B O     1 
ATOM   7557 C  CB    . LEU B 1 405 ? 47.222  74.466  113.116 1.00 61.03  ? 432 LEU B CB    1 
ATOM   7558 C  CG    . LEU B 1 405 ? 48.221  74.463  111.958 1.00 65.32  ? 432 LEU B CG    1 
ATOM   7559 C  CD1   . LEU B 1 405 ? 49.391  75.389  112.247 1.00 63.87  ? 432 LEU B CD1   1 
ATOM   7560 C  CD2   . LEU B 1 405 ? 48.708  73.054  111.697 1.00 63.05  ? 432 LEU B CD2   1 
ATOM   7561 N  N     . VAL B 1 406 ? 46.727  77.505  111.762 1.00 59.91  ? 433 VAL B N     1 
ATOM   7562 C  CA    . VAL B 1 406 ? 46.187  78.355  110.705 1.00 63.44  ? 433 VAL B CA    1 
ATOM   7563 C  C     . VAL B 1 406 ? 47.052  78.194  109.462 1.00 70.25  ? 433 VAL B C     1 
ATOM   7564 O  O     . VAL B 1 406 ? 48.271  78.400  109.516 1.00 63.11  ? 433 VAL B O     1 
ATOM   7565 C  CB    . VAL B 1 406 ? 46.119  79.826  111.144 1.00 61.55  ? 433 VAL B CB    1 
ATOM   7566 C  CG1   . VAL B 1 406 ? 45.590  80.692  110.016 1.00 61.02  ? 433 VAL B CG1   1 
ATOM   7567 C  CG2   . VAL B 1 406 ? 45.248  79.968  112.386 1.00 57.04  ? 433 VAL B CG2   1 
ATOM   7568 N  N     . PHE B 1 407 ? 46.422  77.835  108.345 1.00 64.32  ? 434 PHE B N     1 
ATOM   7569 C  CA    . PHE B 1 407 ? 47.098  77.639  107.071 1.00 60.08  ? 434 PHE B CA    1 
ATOM   7570 C  C     . PHE B 1 407 ? 46.653  78.683  106.055 1.00 58.22  ? 434 PHE B C     1 
ATOM   7571 O  O     . PHE B 1 407 ? 45.513  79.156  106.082 1.00 58.90  ? 434 PHE B O     1 
ATOM   7572 C  CB    . PHE B 1 407 ? 46.805  76.250  106.491 1.00 63.60  ? 434 PHE B CB    1 
ATOM   7573 C  CG    . PHE B 1 407 ? 47.609  75.142  107.102 1.00 62.91  ? 434 PHE B CG    1 
ATOM   7574 C  CD1   . PHE B 1 407 ? 48.930  75.335  107.462 1.00 71.19  ? 434 PHE B CD1   1 
ATOM   7575 C  CD2   . PHE B 1 407 ? 47.038  73.894  107.304 1.00 63.22  ? 434 PHE B CD2   1 
ATOM   7576 C  CE1   . PHE B 1 407 ? 49.663  74.304  108.022 1.00 71.30  ? 434 PHE B CE1   1 
ATOM   7577 C  CE2   . PHE B 1 407 ? 47.767  72.861  107.861 1.00 58.61  ? 434 PHE B CE2   1 
ATOM   7578 C  CZ    . PHE B 1 407 ? 49.081  73.065  108.219 1.00 57.05  ? 434 PHE B CZ    1 
ATOM   7579 N  N     . GLU B 1 408 ? 47.562  79.030  105.151 1.00 62.77  ? 435 GLU B N     1 
ATOM   7580 C  CA    . GLU B 1 408 ? 47.209  79.688  103.906 1.00 54.56  ? 435 GLU B CA    1 
ATOM   7581 C  C     . GLU B 1 408 ? 47.209  78.629  102.802 1.00 55.59  ? 435 GLU B C     1 
ATOM   7582 O  O     . GLU B 1 408 ? 47.398  77.438  103.062 1.00 71.41  ? 435 GLU B O     1 
ATOM   7583 C  CB    . GLU B 1 408 ? 48.157  80.858  103.636 1.00 67.26  ? 435 GLU B CB    1 
ATOM   7584 C  CG    . GLU B 1 408 ? 47.929  82.043  104.573 1.00 67.93  ? 435 GLU B CG    1 
ATOM   7585 C  CD    . GLU B 1 408 ? 48.863  83.211  104.302 1.00 76.46  ? 435 GLU B CD    1 
ATOM   7586 O  OE1   . GLU B 1 408 ? 49.861  83.024  103.577 1.00 91.33  ? 435 GLU B OE1   1 
ATOM   7587 O  OE2   . GLU B 1 408 ? 48.598  84.319  104.818 1.00 72.27  ? 435 GLU B OE2   1 
ATOM   7588 N  N     . ASP B 1 409 ? 47.000  79.046  101.554 1.00 58.88  ? 436 ASP B N     1 
ATOM   7589 C  CA    . ASP B 1 409 ? 46.662  78.101  100.496 1.00 55.14  ? 436 ASP B CA    1 
ATOM   7590 C  C     . ASP B 1 409 ? 47.746  77.934  99.434  1.00 55.76  ? 436 ASP B C     1 
ATOM   7591 O  O     . ASP B 1 409 ? 47.458  77.399  98.359  1.00 57.52  ? 436 ASP B O     1 
ATOM   7592 C  CB    . ASP B 1 409 ? 45.346  78.510  99.830  1.00 56.69  ? 436 ASP B CB    1 
ATOM   7593 C  CG    . ASP B 1 409 ? 45.430  79.862  99.145  1.00 63.30  ? 436 ASP B CG    1 
ATOM   7594 O  OD1   . ASP B 1 409 ? 46.440  80.574  99.333  1.00 74.76  ? 436 ASP B OD1   1 
ATOM   7595 O  OD2   . ASP B 1 409 ? 44.483  80.214  98.412  1.00 67.42  ? 436 ASP B OD2   1 
ATOM   7596 N  N     . ASP B 1 410 ? 48.990  78.357  99.702  1.00 58.47  ? 437 ASP B N     1 
ATOM   7597 C  CA    . ASP B 1 410 ? 50.074  78.273  98.712  1.00 73.05  ? 437 ASP B CA    1 
ATOM   7598 C  C     . ASP B 1 410 ? 51.401  78.002  99.429  1.00 60.00  ? 437 ASP B C     1 
ATOM   7599 O  O     . ASP B 1 410 ? 52.330  78.803  99.418  1.00 73.10  ? 437 ASP B O     1 
ATOM   7600 C  CB    . ASP B 1 410 ? 50.147  79.543  97.858  1.00 86.53  ? 437 ASP B CB    1 
ATOM   7601 C  CG    . ASP B 1 410 ? 50.139  80.813  98.694  1.00 118.62 ? 437 ASP B CG    1 
ATOM   7602 O  OD1   . ASP B 1 410 ? 50.005  80.709  99.933  1.00 104.11 ? 437 ASP B OD1   1 
ATOM   7603 O  OD2   . ASP B 1 410 ? 50.269  81.913  98.113  1.00 128.89 ? 437 ASP B OD2   1 
ATOM   7604 N  N     . LEU B 1 411 ? 51.502  76.830  100.048 1.00 58.41  ? 438 LEU B N     1 
ATOM   7605 C  CA    . LEU B 1 411 ? 52.670  76.490  100.843 1.00 70.64  ? 438 LEU B CA    1 
ATOM   7606 C  C     . LEU B 1 411 ? 53.091  75.052  100.576 1.00 59.76  ? 438 LEU B C     1 
ATOM   7607 O  O     . LEU B 1 411 ? 52.275  74.201  100.214 1.00 69.66  ? 438 LEU B O     1 
ATOM   7608 C  CB    . LEU B 1 411 ? 52.398  76.709  102.337 1.00 73.28  ? 438 LEU B CB    1 
ATOM   7609 C  CG    . LEU B 1 411 ? 51.020  76.295  102.855 1.00 65.14  ? 438 LEU B CG    1 
ATOM   7610 C  CD1   . LEU B 1 411 ? 51.048  74.864  103.347 1.00 87.69  ? 438 LEU B CD1   1 
ATOM   7611 C  CD2   . LEU B 1 411 ? 50.541  77.237  103.951 1.00 68.45  ? 438 LEU B CD2   1 
ATOM   7612 N  N     . ARG B 1 412 ? 54.384  74.799  100.755 1.00 64.95  ? 439 ARG B N     1 
ATOM   7613 C  CA    . ARG B 1 412 ? 54.996  73.496  100.539 1.00 58.12  ? 439 ARG B CA    1 
ATOM   7614 C  C     . ARG B 1 412 ? 55.377  72.896  101.886 1.00 62.93  ? 439 ARG B C     1 
ATOM   7615 O  O     . ARG B 1 412 ? 56.013  73.565  102.710 1.00 70.97  ? 439 ARG B O     1 
ATOM   7616 C  CB    . ARG B 1 412 ? 56.230  73.622  99.642  1.00 56.76  ? 439 ARG B CB    1 
ATOM   7617 C  CG    . ARG B 1 412 ? 57.015  72.332  99.475  1.00 86.60  ? 439 ARG B CG    1 
ATOM   7618 C  CD    . ARG B 1 412 ? 58.317  72.558  98.717  1.00 69.12  ? 439 ARG B CD    1 
ATOM   7619 N  NE    . ARG B 1 412 ? 58.086  73.054  97.367  1.00 79.19  ? 439 ARG B NE    1 
ATOM   7620 C  CZ    . ARG B 1 412 ? 59.037  73.233  96.460  1.00 95.87  ? 439 ARG B CZ    1 
ATOM   7621 N  NH1   . ARG B 1 412 ? 60.306  72.971  96.727  1.00 87.72  ? 439 ARG B NH1   1 
ATOM   7622 N  NH2   . ARG B 1 412 ? 58.705  73.683  95.253  1.00 104.00 ? 439 ARG B NH2   1 
ATOM   7623 N  N     . PHE B 1 413 ? 54.994  71.639  102.101 1.00 66.68  ? 440 PHE B N     1 
ATOM   7624 C  CA    . PHE B 1 413 ? 55.204  70.970  103.378 1.00 57.05  ? 440 PHE B CA    1 
ATOM   7625 C  C     . PHE B 1 413 ? 56.561  70.278  103.421 1.00 58.42  ? 440 PHE B C     1 
ATOM   7626 O  O     . PHE B 1 413 ? 57.002  69.679  102.435 1.00 60.62  ? 440 PHE B O     1 
ATOM   7627 C  CB    . PHE B 1 413 ? 54.100  69.944  103.634 1.00 49.17  ? 440 PHE B CB    1 
ATOM   7628 C  CG    . PHE B 1 413 ? 52.747  70.549  103.875 1.00 55.78  ? 440 PHE B CG    1 
ATOM   7629 C  CD1   . PHE B 1 413 ? 51.897  70.821  102.817 1.00 48.06  ? 440 PHE B CD1   1 
ATOM   7630 C  CD2   . PHE B 1 413 ? 52.320  70.829  105.162 1.00 59.50  ? 440 PHE B CD2   1 
ATOM   7631 C  CE1   . PHE B 1 413 ? 50.648  71.369  103.037 1.00 49.35  ? 440 PHE B CE1   1 
ATOM   7632 C  CE2   . PHE B 1 413 ? 51.070  71.378  105.388 1.00 62.36  ? 440 PHE B CE2   1 
ATOM   7633 C  CZ    . PHE B 1 413 ? 50.233  71.646  104.325 1.00 61.21  ? 440 PHE B CZ    1 
ATOM   7634 N  N     . GLU B 1 414 ? 57.214  70.361  104.578 1.00 55.36  ? 441 GLU B N     1 
ATOM   7635 C  CA    . GLU B 1 414 ? 58.460  69.651  104.807 1.00 57.38  ? 441 GLU B CA    1 
ATOM   7636 C  C     . GLU B 1 414 ? 58.191  68.173  105.074 1.00 61.86  ? 441 GLU B C     1 
ATOM   7637 O  O     . GLU B 1 414 ? 57.067  67.760  105.373 1.00 60.08  ? 441 GLU B O     1 
ATOM   7638 C  CB    . GLU B 1 414 ? 59.222  70.265  105.982 1.00 57.70  ? 441 GLU B CB    1 
ATOM   7639 C  CG    . GLU B 1 414 ? 60.029  71.506  105.631 1.00 73.97  ? 441 GLU B CG    1 
ATOM   7640 C  CD    . GLU B 1 414 ? 61.337  71.175  104.933 1.00 89.47  ? 441 GLU B CD    1 
ATOM   7641 O  OE1   . GLU B 1 414 ? 61.863  70.062  105.145 1.00 86.03  ? 441 GLU B OE1   1 
ATOM   7642 O  OE2   . GLU B 1 414 ? 61.838  72.028  104.169 1.00 81.64  ? 441 GLU B OE2   1 
ATOM   7643 N  N     . ILE B 1 415 ? 59.251  67.371  104.960 1.00 55.83  ? 442 ILE B N     1 
ATOM   7644 C  CA    . ILE B 1 415 ? 59.131  65.948  105.242 1.00 53.51  ? 442 ILE B CA    1 
ATOM   7645 C  C     . ILE B 1 415 ? 58.829  65.749  106.722 1.00 64.98  ? 442 ILE B C     1 
ATOM   7646 O  O     . ILE B 1 415 ? 59.291  66.512  107.580 1.00 64.17  ? 442 ILE B O     1 
ATOM   7647 C  CB    . ILE B 1 415 ? 60.409  65.209  104.808 1.00 54.74  ? 442 ILE B CB    1 
ATOM   7648 C  CG1   . ILE B 1 415 ? 60.233  63.694  104.931 1.00 54.77  ? 442 ILE B CG1   1 
ATOM   7649 C  CG2   . ILE B 1 415 ? 61.609  65.692  105.608 1.00 56.43  ? 442 ILE B CG2   1 
ATOM   7650 C  CD1   . ILE B 1 415 ? 61.358  62.894  104.312 1.00 55.84  ? 442 ILE B CD1   1 
ATOM   7651 N  N     . PHE B 1 416 ? 58.020  64.729  107.020 1.00 54.28  ? 443 PHE B N     1 
ATOM   7652 C  CA    . PHE B 1 416 ? 57.630  64.399  108.392 1.00 54.64  ? 443 PHE B CA    1 
ATOM   7653 C  C     . PHE B 1 416 ? 56.938  65.570  109.081 1.00 61.89  ? 443 PHE B C     1 
ATOM   7654 O  O     . PHE B 1 416 ? 57.083  65.755  110.290 1.00 66.63  ? 443 PHE B O     1 
ATOM   7655 C  CB    . PHE B 1 416 ? 58.833  63.941  109.225 1.00 56.57  ? 443 PHE B CB    1 
ATOM   7656 C  CG    . PHE B 1 416 ? 59.658  62.873  108.572 1.00 61.17  ? 443 PHE B CG    1 
ATOM   7657 C  CD1   . PHE B 1 416 ? 59.057  61.802  107.932 1.00 59.52  ? 443 PHE B CD1   1 
ATOM   7658 C  CD2   . PHE B 1 416 ? 61.041  62.945  108.593 1.00 58.57  ? 443 PHE B CD2   1 
ATOM   7659 C  CE1   . PHE B 1 416 ? 59.821  60.819  107.327 1.00 57.59  ? 443 PHE B CE1   1 
ATOM   7660 C  CE2   . PHE B 1 416 ? 61.809  61.970  107.991 1.00 59.27  ? 443 PHE B CE2   1 
ATOM   7661 C  CZ    . PHE B 1 416 ? 61.199  60.905  107.357 1.00 58.49  ? 443 PHE B CZ    1 
ATOM   7662 N  N     . PHE B 1 417 ? 56.184  66.366  108.319 1.00 57.87  ? 444 PHE B N     1 
ATOM   7663 C  CA    . PHE B 1 417 ? 55.573  67.571  108.876 1.00 53.00  ? 444 PHE B CA    1 
ATOM   7664 C  C     . PHE B 1 417 ? 54.689  67.244  110.073 1.00 53.51  ? 444 PHE B C     1 
ATOM   7665 O  O     . PHE B 1 417 ? 54.815  67.859  111.139 1.00 62.61  ? 444 PHE B O     1 
ATOM   7666 C  CB    . PHE B 1 417 ? 54.762  68.299  107.803 1.00 55.99  ? 444 PHE B CB    1 
ATOM   7667 C  CG    . PHE B 1 417 ? 53.891  69.398  108.348 1.00 57.48  ? 444 PHE B CG    1 
ATOM   7668 C  CD1   . PHE B 1 417 ? 54.407  70.666  108.568 1.00 53.62  ? 444 PHE B CD1   1 
ATOM   7669 C  CD2   . PHE B 1 417 ? 52.556  69.163  108.643 1.00 51.11  ? 444 PHE B CD2   1 
ATOM   7670 C  CE1   . PHE B 1 417 ? 53.610  71.679  109.071 1.00 57.05  ? 444 PHE B CE1   1 
ATOM   7671 C  CE2   . PHE B 1 417 ? 51.756  70.171  109.149 1.00 51.25  ? 444 PHE B CE2   1 
ATOM   7672 C  CZ    . PHE B 1 417 ? 52.283  71.431  109.361 1.00 54.29  ? 444 PHE B CZ    1 
ATOM   7673 N  N     . LYS B 1 418 ? 53.789  66.273  109.914 1.00 52.98  ? 445 LYS B N     1 
ATOM   7674 C  CA    . LYS B 1 418 ? 52.793  66.003  110.946 1.00 53.57  ? 445 LYS B CA    1 
ATOM   7675 C  C     . LYS B 1 418 ? 53.446  65.550  112.246 1.00 65.88  ? 445 LYS B C     1 
ATOM   7676 O  O     . LYS B 1 418 ? 53.130  66.066  113.324 1.00 66.55  ? 445 LYS B O     1 
ATOM   7677 C  CB    . LYS B 1 418 ? 51.799  64.957  110.446 1.00 52.98  ? 445 LYS B CB    1 
ATOM   7678 C  CG    . LYS B 1 418 ? 50.745  64.577  111.469 1.00 55.37  ? 445 LYS B CG    1 
ATOM   7679 C  CD    . LYS B 1 418 ? 49.728  63.613  110.883 1.00 53.45  ? 445 LYS B CD    1 
ATOM   7680 C  CE    . LYS B 1 418 ? 48.708  63.194  111.927 1.00 58.04  ? 445 LYS B CE    1 
ATOM   7681 N  NZ    . LYS B 1 418 ? 47.653  62.320  111.348 1.00 70.36  ? 445 LYS B NZ    1 
ATOM   7682 N  N     . ARG B 1 419 ? 54.360  64.580  112.167 1.00 62.23  ? 446 ARG B N     1 
ATOM   7683 C  CA    . ARG B 1 419 ? 55.022  64.099  113.376 1.00 58.86  ? 446 ARG B CA    1 
ATOM   7684 C  C     . ARG B 1 419 ? 55.903  65.177  113.995 1.00 61.11  ? 446 ARG B C     1 
ATOM   7685 O  O     . ARG B 1 419 ? 55.973  65.296  115.223 1.00 69.02  ? 446 ARG B O     1 
ATOM   7686 C  CB    . ARG B 1 419 ? 55.847  62.848  113.069 1.00 58.80  ? 446 ARG B CB    1 
ATOM   7687 C  CG    . ARG B 1 419 ? 55.098  61.539  113.263 1.00 59.27  ? 446 ARG B CG    1 
ATOM   7688 C  CD    . ARG B 1 419 ? 56.061  60.363  113.284 1.00 65.60  ? 446 ARG B CD    1 
ATOM   7689 N  NE    . ARG B 1 419 ? 56.829  60.269  112.048 1.00 62.96  ? 446 ARG B NE    1 
ATOM   7690 C  CZ    . ARG B 1 419 ? 57.848  59.443  111.858 1.00 70.48  ? 446 ARG B CZ    1 
ATOM   7691 N  NH1   . ARG B 1 419 ? 58.259  58.620  112.808 1.00 76.70  ? 446 ARG B NH1   1 
ATOM   7692 N  NH2   . ARG B 1 419 ? 58.474  59.447  110.684 1.00 72.23  ? 446 ARG B NH2   1 
ATOM   7693 N  N     . ARG B 1 420 ? 56.581  65.974  113.166 1.00 61.45  ? 447 ARG B N     1 
ATOM   7694 C  CA    . ARG B 1 420 ? 57.498  66.977  113.700 1.00 67.07  ? 447 ARG B CA    1 
ATOM   7695 C  C     . ARG B 1 420 ? 56.750  68.086  114.431 1.00 72.54  ? 447 ARG B C     1 
ATOM   7696 O  O     . ARG B 1 420 ? 57.223  68.587  115.458 1.00 71.01  ? 447 ARG B O     1 
ATOM   7697 C  CB    . ARG B 1 420 ? 58.368  67.548  112.578 1.00 58.94  ? 447 ARG B CB    1 
ATOM   7698 C  CG    . ARG B 1 420 ? 59.484  66.607  112.141 1.00 59.65  ? 447 ARG B CG    1 
ATOM   7699 C  CD    . ARG B 1 420 ? 60.062  66.982  110.784 1.00 58.77  ? 447 ARG B CD    1 
ATOM   7700 N  NE    . ARG B 1 420 ? 60.850  68.208  110.831 1.00 66.27  ? 447 ARG B NE    1 
ATOM   7701 C  CZ    . ARG B 1 420 ? 61.578  68.667  109.822 1.00 73.17  ? 447 ARG B CZ    1 
ATOM   7702 N  NH1   . ARG B 1 420 ? 61.647  68.022  108.668 1.00 66.46  ? 447 ARG B NH1   1 
ATOM   7703 N  NH2   . ARG B 1 420 ? 62.257  69.801  109.974 1.00 78.23  ? 447 ARG B NH2   1 
ATOM   7704 N  N     . LEU B 1 421 ? 55.576  68.478  113.929 1.00 69.60  ? 448 LEU B N     1 
ATOM   7705 C  CA    . LEU B 1 421 ? 54.813  69.526  114.599 1.00 67.15  ? 448 LEU B CA    1 
ATOM   7706 C  C     . LEU B 1 421 ? 54.146  69.003  115.865 1.00 69.83  ? 448 LEU B C     1 
ATOM   7707 O  O     . LEU B 1 421 ? 54.138  69.688  116.895 1.00 71.13  ? 448 LEU B O     1 
ATOM   7708 C  CB    . LEU B 1 421 ? 53.773  70.115  113.647 1.00 68.48  ? 448 LEU B CB    1 
ATOM   7709 C  CG    . LEU B 1 421 ? 52.948  71.282  114.197 1.00 71.83  ? 448 LEU B CG    1 
ATOM   7710 C  CD1   . LEU B 1 421 ? 53.857  72.419  114.632 1.00 58.18  ? 448 LEU B CD1   1 
ATOM   7711 C  CD2   . LEU B 1 421 ? 51.946  71.763  113.162 1.00 63.74  ? 448 LEU B CD2   1 
ATOM   7712 N  N     . MET B 1 422 ? 53.585  67.790  115.812 1.00 68.16  ? 449 MET B N     1 
ATOM   7713 C  CA    . MET B 1 422 ? 52.909  67.240  116.983 1.00 71.31  ? 449 MET B CA    1 
ATOM   7714 C  C     . MET B 1 422 ? 53.876  67.007  118.136 1.00 76.75  ? 449 MET B C     1 
ATOM   7715 O  O     . MET B 1 422 ? 53.490  67.138  119.304 1.00 86.13  ? 449 MET B O     1 
ATOM   7716 C  CB    . MET B 1 422 ? 52.193  65.936  116.622 1.00 61.70  ? 449 MET B CB    1 
ATOM   7717 C  CG    . MET B 1 422 ? 50.965  66.118  115.740 1.00 73.03  ? 449 MET B CG    1 
ATOM   7718 S  SD    . MET B 1 422 ? 50.073  64.579  115.431 1.00 79.64  ? 449 MET B SD    1 
ATOM   7719 C  CE    . MET B 1 422 ? 49.222  64.340  116.989 1.00 77.02  ? 449 MET B CE    1 
ATOM   7720 N  N     . ASN B 1 423 ? 55.131  66.665  117.835 1.00 69.03  ? 450 ASN B N     1 
ATOM   7721 C  CA    . ASN B 1 423 ? 56.105  66.452  118.901 1.00 77.09  ? 450 ASN B CA    1 
ATOM   7722 C  C     . ASN B 1 423 ? 56.508  67.769  119.551 1.00 80.43  ? 450 ASN B C     1 
ATOM   7723 O  O     . ASN B 1 423 ? 56.749  67.820  120.764 1.00 95.16  ? 450 ASN B O     1 
ATOM   7724 C  CB    . ASN B 1 423 ? 57.332  65.721  118.360 1.00 68.24  ? 450 ASN B CB    1 
ATOM   7725 C  CG    . ASN B 1 423 ? 57.006  64.327  117.867 1.00 78.56  ? 450 ASN B CG    1 
ATOM   7726 O  OD1   . ASN B 1 423 ? 55.971  63.759  118.217 1.00 82.94  ? 450 ASN B OD1   1 
ATOM   7727 N  ND2   . ASN B 1 423 ? 57.889  63.766  117.048 1.00 73.33  ? 450 ASN B ND2   1 
ATOM   7728 N  N     . LEU B 1 424 ? 56.588  68.843  118.763 1.00 77.77  ? 451 LEU B N     1 
ATOM   7729 C  CA    . LEU B 1 424 ? 56.906  70.150  119.327 1.00 80.11  ? 451 LEU B CA    1 
ATOM   7730 C  C     . LEU B 1 424 ? 55.810  70.615  120.277 1.00 83.07  ? 451 LEU B C     1 
ATOM   7731 O  O     . LEU B 1 424 ? 56.089  71.071  121.392 1.00 89.61  ? 451 LEU B O     1 
ATOM   7732 C  CB    . LEU B 1 424 ? 57.118  71.170  118.209 1.00 72.44  ? 451 LEU B CB    1 
ATOM   7733 C  CG    . LEU B 1 424 ? 57.314  72.613  118.681 1.00 70.99  ? 451 LEU B CG    1 
ATOM   7734 C  CD1   . LEU B 1 424 ? 58.525  72.723  119.589 1.00 69.15  ? 451 LEU B CD1   1 
ATOM   7735 C  CD2   . LEU B 1 424 ? 57.443  73.561  117.506 1.00 84.92  ? 451 LEU B CD2   1 
ATOM   7736 N  N     . MET B 1 425 ? 54.549  70.502  119.850 1.00 76.91  ? 452 MET B N     1 
ATOM   7737 C  CA    . MET B 1 425 ? 53.437  70.903  120.707 1.00 77.93  ? 452 MET B CA    1 
ATOM   7738 C  C     . MET B 1 425 ? 53.412  70.089  121.993 1.00 86.79  ? 452 MET B C     1 
ATOM   7739 O  O     . MET B 1 425 ? 53.107  70.622  123.067 1.00 92.36  ? 452 MET B O     1 
ATOM   7740 C  CB    . MET B 1 425 ? 52.115  70.755  119.955 1.00 71.29  ? 452 MET B CB    1 
ATOM   7741 C  CG    . MET B 1 425 ? 52.043  71.580  118.684 1.00 85.78  ? 452 MET B CG    1 
ATOM   7742 S  SD    . MET B 1 425 ? 52.378  73.327  118.982 1.00 80.11  ? 452 MET B SD    1 
ATOM   7743 C  CE    . MET B 1 425 ? 50.994  73.764  120.032 1.00 77.06  ? 452 MET B CE    1 
ATOM   7744 N  N     . ARG B 1 426 ? 53.738  68.798  121.904 1.00 87.24  ? 453 ARG B N     1 
ATOM   7745 C  CA    . ARG B 1 426 ? 53.789  67.959  123.097 1.00 87.54  ? 453 ARG B CA    1 
ATOM   7746 C  C     . ARG B 1 426 ? 54.873  68.443  124.053 1.00 87.90  ? 453 ARG B C     1 
ATOM   7747 O  O     . ARG B 1 426 ? 54.654  68.527  125.267 1.00 94.77  ? 453 ARG B O     1 
ATOM   7748 C  CB    . ARG B 1 426 ? 54.024  66.502  122.697 1.00 79.04  ? 453 ARG B CB    1 
ATOM   7749 C  CG    . ARG B 1 426 ? 53.396  65.488  123.638 1.00 92.62  ? 453 ARG B CG    1 
ATOM   7750 C  CD    . ARG B 1 426 ? 53.454  64.081  123.058 1.00 103.21 ? 453 ARG B CD    1 
ATOM   7751 N  NE    . ARG B 1 426 ? 52.798  63.979  121.759 1.00 106.92 ? 453 ARG B NE    1 
ATOM   7752 C  CZ    . ARG B 1 426 ? 53.432  63.793  120.609 1.00 102.17 ? 453 ARG B CZ    1 
ATOM   7753 N  NH1   . ARG B 1 426 ? 54.748  63.668  120.557 1.00 90.92  ? 453 ARG B NH1   1 
ATOM   7754 N  NH2   . ARG B 1 426 ? 52.728  63.726  119.482 1.00 82.92  ? 453 ARG B NH2   1 
ATOM   7755 N  N     . ASP B 1 427 ? 56.048  68.787  123.515 1.00 85.29  ? 454 ASP B N     1 
ATOM   7756 C  CA    . ASP B 1 427 ? 57.118  69.329  124.349 1.00 89.03  ? 454 ASP B CA    1 
ATOM   7757 C  C     . ASP B 1 427 ? 56.713  70.661  124.966 1.00 88.17  ? 454 ASP B C     1 
ATOM   7758 O  O     . ASP B 1 427 ? 56.989  70.915  126.144 1.00 94.06  ? 454 ASP B O     1 
ATOM   7759 C  CB    . ASP B 1 427 ? 58.398  69.493  123.530 1.00 89.99  ? 454 ASP B CB    1 
ATOM   7760 C  CG    . ASP B 1 427 ? 58.969  68.170  123.066 1.00 105.87 ? 454 ASP B CG    1 
ATOM   7761 O  OD1   . ASP B 1 427 ? 58.332  67.124  123.319 1.00 112.50 ? 454 ASP B OD1   1 
ATOM   7762 O  OD2   . ASP B 1 427 ? 60.056  68.179  122.449 1.00 109.23 ? 454 ASP B OD2   1 
ATOM   7763 N  N     . VAL B 1 428 ? 56.050  71.520  124.187 1.00 87.35  ? 455 VAL B N     1 
ATOM   7764 C  CA    . VAL B 1 428 ? 55.607  72.814  124.702 1.00 88.90  ? 455 VAL B CA    1 
ATOM   7765 C  C     . VAL B 1 428 ? 54.681  72.622  125.896 1.00 93.18  ? 455 VAL B C     1 
ATOM   7766 O  O     . VAL B 1 428 ? 54.841  73.264  126.942 1.00 108.21 ? 455 VAL B O     1 
ATOM   7767 C  CB    . VAL B 1 428 ? 54.927  73.631  123.589 1.00 85.62  ? 455 VAL B CB    1 
ATOM   7768 C  CG1   . VAL B 1 428 ? 54.231  74.846  124.178 1.00 85.02  ? 455 VAL B CG1   1 
ATOM   7769 C  CG2   . VAL B 1 428 ? 55.946  74.056  122.549 1.00 76.04  ? 455 VAL B CG2   1 
ATOM   7770 N  N     . GLU B 1 429 ? 53.701  71.726  125.760 1.00 88.79  ? 456 GLU B N     1 
ATOM   7771 C  CA    . GLU B 1 429 ? 52.781  71.464  126.862 1.00 87.02  ? 456 GLU B CA    1 
ATOM   7772 C  C     . GLU B 1 429 ? 53.509  70.857  128.055 1.00 106.19 ? 456 GLU B C     1 
ATOM   7773 O  O     . GLU B 1 429 ? 53.246  71.228  129.206 1.00 103.42 ? 456 GLU B O     1 
ATOM   7774 C  CB    . GLU B 1 429 ? 51.655  70.544  126.394 1.00 84.63  ? 456 GLU B CB    1 
ATOM   7775 C  CG    . GLU B 1 429 ? 50.660  70.173  127.484 1.00 117.58 ? 456 GLU B CG    1 
ATOM   7776 C  CD    . GLU B 1 429 ? 49.546  69.280  126.975 1.00 128.88 ? 456 GLU B CD    1 
ATOM   7777 O  OE1   . GLU B 1 429 ? 49.541  68.971  125.765 1.00 117.52 ? 456 GLU B OE1   1 
ATOM   7778 O  OE2   . GLU B 1 429 ? 48.677  68.888  127.783 1.00 130.39 ? 456 GLU B OE2   1 
ATOM   7779 N  N     . ARG B 1 430 ? 54.435  69.930  127.797 1.00 106.22 ? 457 ARG B N     1 
ATOM   7780 C  CA    . ARG B 1 430 ? 55.182  69.300  128.881 1.00 103.66 ? 457 ARG B CA    1 
ATOM   7781 C  C     . ARG B 1 430 ? 55.933  70.336  129.707 1.00 106.15 ? 457 ARG B C     1 
ATOM   7782 O  O     . ARG B 1 430 ? 56.017  70.220  130.934 1.00 116.33 ? 457 ARG B O     1 
ATOM   7783 C  CB    . ARG B 1 430 ? 56.152  68.267  128.312 1.00 98.65  ? 457 ARG B CB    1 
ATOM   7784 C  CG    . ARG B 1 430 ? 56.666  67.262  129.325 1.00 114.67 ? 457 ARG B CG    1 
ATOM   7785 C  CD    . ARG B 1 430 ? 55.832  65.997  129.293 1.00 106.38 ? 457 ARG B CD    1 
ATOM   7786 N  NE    . ARG B 1 430 ? 55.771  65.433  127.950 1.00 121.14 ? 457 ARG B NE    1 
ATOM   7787 C  CZ    . ARG B 1 430 ? 55.084  64.348  127.624 1.00 113.97 ? 457 ARG B CZ    1 
ATOM   7788 N  NH1   . ARG B 1 430 ? 54.387  63.676  128.525 1.00 117.81 ? 457 ARG B NH1   1 
ATOM   7789 N  NH2   . ARG B 1 430 ? 55.095  63.927  126.362 1.00 87.50  ? 457 ARG B NH2   1 
ATOM   7790 N  N     . GLU B 1 431 ? 56.474  71.362  129.052 1.00 106.94 ? 458 GLU B N     1 
ATOM   7791 C  CA    . GLU B 1 431 ? 57.210  72.421  129.728 1.00 113.44 ? 458 GLU B CA    1 
ATOM   7792 C  C     . GLU B 1 431 ? 56.315  73.555  130.206 1.00 115.57 ? 458 GLU B C     1 
ATOM   7793 O  O     . GLU B 1 431 ? 56.807  74.465  130.882 1.00 109.21 ? 458 GLU B O     1 
ATOM   7794 C  CB    . GLU B 1 431 ? 58.302  72.976  128.810 1.00 102.18 ? 458 GLU B CB    1 
ATOM   7795 C  CG    . GLU B 1 431 ? 59.182  71.907  128.174 1.00 134.81 ? 458 GLU B CG    1 
ATOM   7796 C  CD    . GLU B 1 431 ? 59.916  71.051  129.193 1.00 137.48 ? 458 GLU B CD    1 
ATOM   7797 O  OE1   . GLU B 1 431 ? 60.152  71.532  130.322 1.00 140.55 ? 458 GLU B OE1   1 
ATOM   7798 O  OE2   . GLU B 1 431 ? 60.266  69.896  128.859 1.00 132.92 ? 458 GLU B OE2   1 
ATOM   7799 N  N     . GLY B 1 432 ? 55.024  73.521  129.880 1.00 106.95 ? 459 GLY B N     1 
ATOM   7800 C  CA    . GLY B 1 432 ? 54.105  74.556  130.326 1.00 96.03  ? 459 GLY B CA    1 
ATOM   7801 C  C     . GLY B 1 432 ? 54.448  75.941  129.830 1.00 99.28  ? 459 GLY B C     1 
ATOM   7802 O  O     . GLY B 1 432 ? 54.184  76.926  130.528 1.00 97.92  ? 459 GLY B O     1 
ATOM   7803 N  N     . LEU B 1 433 ? 55.036  76.043  128.641 1.00 98.41  ? 460 LEU B N     1 
ATOM   7804 C  CA    . LEU B 1 433 ? 55.437  77.336  128.106 1.00 95.28  ? 460 LEU B CA    1 
ATOM   7805 C  C     . LEU B 1 433 ? 54.223  78.231  127.893 1.00 98.70  ? 460 LEU B C     1 
ATOM   7806 O  O     . LEU B 1 433 ? 53.201  77.800  127.352 1.00 100.56 ? 460 LEU B O     1 
ATOM   7807 C  CB    . LEU B 1 433 ? 56.189  77.145  126.790 1.00 99.95  ? 460 LEU B CB    1 
ATOM   7808 C  CG    . LEU B 1 433 ? 56.675  78.398  126.060 1.00 98.07  ? 460 LEU B CG    1 
ATOM   7809 C  CD1   . LEU B 1 433 ? 57.705  79.143  126.892 1.00 87.91  ? 460 LEU B CD1   1 
ATOM   7810 C  CD2   . LEU B 1 433 ? 57.245  78.031  124.699 1.00 87.12  ? 460 LEU B CD2   1 
ATOM   7811 N  N     . ASP B 1 434 ? 54.333  79.481  128.330 1.00 94.94  ? 461 ASP B N     1 
ATOM   7812 C  CA    . ASP B 1 434 ? 53.301  80.480  128.071 1.00 94.85  ? 461 ASP B CA    1 
ATOM   7813 C  C     . ASP B 1 434 ? 53.540  81.051  126.679 1.00 105.30 ? 461 ASP B C     1 
ATOM   7814 O  O     . ASP B 1 434 ? 54.524  81.765  126.452 1.00 114.90 ? 461 ASP B O     1 
ATOM   7815 C  CB    . ASP B 1 434 ? 53.332  81.576  129.133 1.00 98.82  ? 461 ASP B CB    1 
ATOM   7816 C  CG    . ASP B 1 434 ? 52.255  82.625  128.925 1.00 108.57 ? 461 ASP B CG    1 
ATOM   7817 O  OD1   . ASP B 1 434 ? 51.344  82.404  128.096 1.00 116.46 ? 461 ASP B OD1   1 
ATOM   7818 O  OD2   . ASP B 1 434 ? 52.323  83.677  129.592 1.00 106.43 ? 461 ASP B OD2   1 
ATOM   7819 N  N     . TRP B 1 435 ? 52.649  80.733  125.743 1.00 96.58  ? 462 TRP B N     1 
ATOM   7820 C  CA    . TRP B 1 435 ? 52.839  81.107  124.351 1.00 96.77  ? 462 TRP B CA    1 
ATOM   7821 C  C     . TRP B 1 435 ? 51.533  81.626  123.771 1.00 85.33  ? 462 TRP B C     1 
ATOM   7822 O  O     . TRP B 1 435 ? 50.445  81.193  124.158 1.00 85.54  ? 462 TRP B O     1 
ATOM   7823 C  CB    . TRP B 1 435 ? 53.344  79.922  123.517 1.00 83.21  ? 462 TRP B CB    1 
ATOM   7824 C  CG    . TRP B 1 435 ? 52.338  78.824  123.380 1.00 83.01  ? 462 TRP B CG    1 
ATOM   7825 C  CD1   . TRP B 1 435 ? 52.146  77.775  124.231 1.00 75.43  ? 462 TRP B CD1   1 
ATOM   7826 C  CD2   . TRP B 1 435 ? 51.378  78.669  122.328 1.00 77.20  ? 462 TRP B CD2   1 
ATOM   7827 N  NE1   . TRP B 1 435 ? 51.126  76.975  123.773 1.00 72.26  ? 462 TRP B NE1   1 
ATOM   7828 C  CE2   . TRP B 1 435 ? 50.638  77.503  122.606 1.00 70.12  ? 462 TRP B CE2   1 
ATOM   7829 C  CE3   . TRP B 1 435 ? 51.073  79.404  121.178 1.00 76.42  ? 462 TRP B CE3   1 
ATOM   7830 C  CZ2   . TRP B 1 435 ? 49.613  77.055  121.777 1.00 71.45  ? 462 TRP B CZ2   1 
ATOM   7831 C  CZ3   . TRP B 1 435 ? 50.056  78.958  120.356 1.00 76.48  ? 462 TRP B CZ3   1 
ATOM   7832 C  CH2   . TRP B 1 435 ? 49.337  77.795  120.660 1.00 88.88  ? 462 TRP B CH2   1 
ATOM   7833 N  N     . ASP B 1 436 ? 51.658  82.561  122.829 1.00 80.87  ? 463 ASP B N     1 
ATOM   7834 C  CA    . ASP B 1 436 ? 50.523  83.088  122.085 1.00 80.39  ? 463 ASP B CA    1 
ATOM   7835 C  C     . ASP B 1 436 ? 50.569  82.757  120.604 1.00 76.88  ? 463 ASP B C     1 
ATOM   7836 O  O     . ASP B 1 436 ? 49.516  82.544  119.998 1.00 73.54  ? 463 ASP B O     1 
ATOM   7837 C  CB    . ASP B 1 436 ? 50.444  84.612  122.238 1.00 85.75  ? 463 ASP B CB    1 
ATOM   7838 C  CG    . ASP B 1 436 ? 50.319  85.047  123.680 1.00 98.90  ? 463 ASP B CG    1 
ATOM   7839 O  OD1   . ASP B 1 436 ? 49.746  84.283  124.484 1.00 106.28 ? 463 ASP B OD1   1 
ATOM   7840 O  OD2   . ASP B 1 436 ? 50.794  86.155  124.008 1.00 91.73  ? 463 ASP B OD2   1 
ATOM   7841 N  N     . LEU B 1 437 ? 51.761  82.702  120.015 1.00 73.84  ? 464 LEU B N     1 
ATOM   7842 C  CA    . LEU B 1 437 ? 51.920  82.529  118.578 1.00 73.55  ? 464 LEU B CA    1 
ATOM   7843 C  C     . LEU B 1 437 ? 53.161  81.693  118.309 1.00 76.59  ? 464 LEU B C     1 
ATOM   7844 O  O     . LEU B 1 437 ? 54.229  81.970  118.864 1.00 80.85  ? 464 LEU B O     1 
ATOM   7845 C  CB    . LEU B 1 437 ? 52.037  83.886  117.876 1.00 68.16  ? 464 LEU B CB    1 
ATOM   7846 C  CG    . LEU B 1 437 ? 52.266  83.878  116.367 1.00 84.05  ? 464 LEU B CG    1 
ATOM   7847 C  CD1   . LEU B 1 437 ? 51.058  83.293  115.675 1.00 64.40  ? 464 LEU B CD1   1 
ATOM   7848 C  CD2   . LEU B 1 437 ? 52.546  85.285  115.861 1.00 95.90  ? 464 LEU B CD2   1 
ATOM   7849 N  N     . ILE B 1 438 ? 53.023  80.682  117.456 1.00 71.84  ? 465 ILE B N     1 
ATOM   7850 C  CA    . ILE B 1 438 ? 54.133  79.818  117.072 1.00 76.60  ? 465 ILE B CA    1 
ATOM   7851 C  C     . ILE B 1 438 ? 54.181  79.769  115.553 1.00 72.04  ? 465 ILE B C     1 
ATOM   7852 O  O     . ILE B 1 438 ? 53.276  79.218  114.917 1.00 68.80  ? 465 ILE B O     1 
ATOM   7853 C  CB    . ILE B 1 438 ? 54.006  78.407  117.658 1.00 74.60  ? 465 ILE B CB    1 
ATOM   7854 C  CG1   . ILE B 1 438 ? 53.980  78.471  119.185 1.00 69.84  ? 465 ILE B CG1   1 
ATOM   7855 C  CG2   . ILE B 1 438 ? 55.162  77.537  117.192 1.00 68.40  ? 465 ILE B CG2   1 
ATOM   7856 C  CD1   . ILE B 1 438 ? 53.909  77.120  119.854 1.00 74.00  ? 465 ILE B CD1   1 
ATOM   7857 N  N     . TYR B 1 439 ? 55.236  80.335  114.973 1.00 72.33  ? 466 TYR B N     1 
ATOM   7858 C  CA    . TYR B 1 439 ? 55.403  80.324  113.524 1.00 69.56  ? 466 TYR B CA    1 
ATOM   7859 C  C     . TYR B 1 439 ? 55.799  78.931  113.052 1.00 73.49  ? 466 TYR B C     1 
ATOM   7860 O  O     . TYR B 1 439 ? 56.858  78.422  113.432 1.00 76.63  ? 466 TYR B O     1 
ATOM   7861 C  CB    . TYR B 1 439 ? 56.471  81.331  113.102 1.00 70.75  ? 466 TYR B CB    1 
ATOM   7862 C  CG    . TYR B 1 439 ? 56.042  82.779  113.095 1.00 84.79  ? 466 TYR B CG    1 
ATOM   7863 C  CD1   . TYR B 1 439 ? 55.339  83.310  112.023 1.00 82.92  ? 466 TYR B CD1   1 
ATOM   7864 C  CD2   . TYR B 1 439 ? 56.369  83.624  114.146 1.00 81.09  ? 466 TYR B CD2   1 
ATOM   7865 C  CE1   . TYR B 1 439 ? 54.957  84.639  112.005 1.00 75.90  ? 466 TYR B CE1   1 
ATOM   7866 C  CE2   . TYR B 1 439 ? 55.991  84.954  114.137 1.00 78.11  ? 466 TYR B CE2   1 
ATOM   7867 C  CZ    . TYR B 1 439 ? 55.286  85.455  113.064 1.00 73.61  ? 466 TYR B CZ    1 
ATOM   7868 O  OH    . TYR B 1 439 ? 54.910  86.779  113.054 1.00 87.03  ? 466 TYR B OH    1 
ATOM   7869 N  N     . VAL B 1 440 ? 54.957  78.319  112.220 1.00 69.03  ? 467 VAL B N     1 
ATOM   7870 C  CA    . VAL B 1 440 ? 55.356  77.111  111.508 1.00 68.24  ? 467 VAL B CA    1 
ATOM   7871 C  C     . VAL B 1 440 ? 55.996  77.440  110.163 1.00 68.78  ? 467 VAL B C     1 
ATOM   7872 O  O     . VAL B 1 440 ? 56.796  76.644  109.652 1.00 68.41  ? 467 VAL B O     1 
ATOM   7873 C  CB    . VAL B 1 440 ? 54.155  76.168  111.315 1.00 67.20  ? 467 VAL B CB    1 
ATOM   7874 C  CG1   . VAL B 1 440 ? 54.625  74.783  110.893 1.00 66.87  ? 467 VAL B CG1   1 
ATOM   7875 C  CG2   . VAL B 1 440 ? 53.339  76.086  112.594 1.00 64.08  ? 467 VAL B CG2   1 
ATOM   7876 N  N     . GLY B 1 441 ? 55.675  78.594  109.584 1.00 69.06  ? 468 GLY B N     1 
ATOM   7877 C  CA    . GLY B 1 441 ? 56.325  79.078  108.383 1.00 64.20  ? 468 GLY B CA    1 
ATOM   7878 C  C     . GLY B 1 441 ? 56.349  80.593  108.348 1.00 83.49  ? 468 GLY B C     1 
ATOM   7879 O  O     . GLY B 1 441 ? 55.333  81.236  108.633 1.00 83.82  ? 468 GLY B O     1 
ATOM   7880 N  N     . ARG B 1 442 ? 57.490  81.179  108.003 1.00 82.56  ? 469 ARG B N     1 
ATOM   7881 C  CA    . ARG B 1 442 ? 57.663  82.627  108.063 1.00 78.32  ? 469 ARG B CA    1 
ATOM   7882 C  C     . ARG B 1 442 ? 58.917  82.994  107.277 1.00 85.92  ? 469 ARG B C     1 
ATOM   7883 O  O     . ARG B 1 442 ? 59.580  82.137  106.684 1.00 84.93  ? 469 ARG B O     1 
ATOM   7884 C  CB    . ARG B 1 442 ? 57.756  83.114  109.508 1.00 85.02  ? 469 ARG B CB    1 
ATOM   7885 C  CG    . ARG B 1 442 ? 58.784  82.359  110.335 1.00 86.55  ? 469 ARG B CG    1 
ATOM   7886 C  CD    . ARG B 1 442 ? 59.637  83.307  111.155 1.00 79.71  ? 469 ARG B CD    1 
ATOM   7887 N  NE    . ARG B 1 442 ? 60.728  82.612  111.824 1.00 84.18  ? 469 ARG B NE    1 
ATOM   7888 C  CZ    . ARG B 1 442 ? 61.673  83.212  112.536 1.00 95.08  ? 469 ARG B CZ    1 
ATOM   7889 N  NH1   . ARG B 1 442 ? 61.687  84.524  112.700 1.00 93.32  ? 469 ARG B NH1   1 
ATOM   7890 N  NH2   . ARG B 1 442 ? 62.629  82.475  113.095 1.00 97.45  ? 469 ARG B NH2   1 
ATOM   7891 N  N     . LYS B 1 443 ? 59.242  84.286  107.286 1.00 89.94  ? 470 LYS B N     1 
ATOM   7892 C  CA    . LYS B 1 443 ? 60.453  84.817  106.662 1.00 84.56  ? 470 LYS B CA    1 
ATOM   7893 C  C     . LYS B 1 443 ? 61.276  85.482  107.758 1.00 90.22  ? 470 LYS B C     1 
ATOM   7894 O  O     . LYS B 1 443 ? 60.982  86.611  108.162 1.00 93.58  ? 470 LYS B O     1 
ATOM   7895 C  CB    . LYS B 1 443 ? 60.121  85.801  105.547 1.00 90.16  ? 470 LYS B CB    1 
ATOM   7896 C  CG    . LYS B 1 443 ? 61.332  86.256  104.748 1.00 89.59  ? 470 LYS B CG    1 
ATOM   7897 C  CD    . LYS B 1 443 ? 60.947  87.279  103.689 1.00 100.84 ? 470 LYS B CD    1 
ATOM   7898 C  CE    . LYS B 1 443 ? 62.154  87.702  102.863 1.00 99.51  ? 470 LYS B CE    1 
ATOM   7899 N  NZ    . LYS B 1 443 ? 61.798  88.740  101.854 1.00 108.56 ? 470 LYS B NZ    1 
ATOM   7900 N  N     . ARG B 1 444 ? 62.299  84.781  108.238 1.00 95.97  ? 471 ARG B N     1 
ATOM   7901 C  CA    . ARG B 1 444 ? 63.167  85.321  109.275 1.00 94.20  ? 471 ARG B CA    1 
ATOM   7902 C  C     . ARG B 1 444 ? 63.953  86.505  108.726 1.00 88.64  ? 471 ARG B C     1 
ATOM   7903 O  O     . ARG B 1 444 ? 64.717  86.361  107.766 1.00 97.61  ? 471 ARG B O     1 
ATOM   7904 C  CB    . ARG B 1 444 ? 64.110  84.234  109.784 1.00 83.41  ? 471 ARG B CB    1 
ATOM   7905 C  CG    . ARG B 1 444 ? 65.096  84.704  110.834 1.00 102.89 ? 471 ARG B CG    1 
ATOM   7906 C  CD    . ARG B 1 444 ? 65.982  83.560  111.304 1.00 108.21 ? 471 ARG B CD    1 
ATOM   7907 N  NE    . ARG B 1 444 ? 67.020  84.010  112.223 1.00 121.52 ? 471 ARG B NE    1 
ATOM   7908 C  CZ    . ARG B 1 444 ? 67.876  83.206  112.840 1.00 122.99 ? 471 ARG B CZ    1 
ATOM   7909 N  NH1   . ARG B 1 444 ? 67.840  81.896  112.666 1.00 115.85 ? 471 ARG B NH1   1 
ATOM   7910 N  NH2   . ARG B 1 444 ? 68.788  83.731  113.653 1.00 135.24 ? 471 ARG B NH2   1 
ATOM   7911 N  N     . MET B 1 445 ? 63.755  87.678  109.327 1.00 92.06  ? 472 MET B N     1 
ATOM   7912 C  CA    . MET B 1 445 ? 64.443  88.888  108.900 1.00 95.51  ? 472 MET B CA    1 
ATOM   7913 C  C     . MET B 1 445 ? 65.678  89.203  109.732 1.00 113.02 ? 472 MET B C     1 
ATOM   7914 O  O     . MET B 1 445 ? 66.545  89.950  109.265 1.00 115.41 ? 472 MET B O     1 
ATOM   7915 C  CB    . MET B 1 445 ? 63.487  90.086  108.945 1.00 102.95 ? 472 MET B CB    1 
ATOM   7916 C  CG    . MET B 1 445 ? 62.190  89.871  108.179 1.00 108.64 ? 472 MET B CG    1 
ATOM   7917 S  SD    . MET B 1 445 ? 62.437  89.621  106.409 1.00 121.91 ? 472 MET B SD    1 
ATOM   7918 C  CE    . MET B 1 445 ? 62.837  91.282  105.876 1.00 95.01  ? 472 MET B CE    1 
ATOM   7919 N  N     . GLN B 1 446 ? 65.780  88.659  110.942 1.00 108.91 ? 473 GLN B N     1 
ATOM   7920 C  CA    . GLN B 1 446 ? 66.938  88.862  111.810 1.00 119.87 ? 473 GLN B CA    1 
ATOM   7921 C  C     . GLN B 1 446 ? 67.775  87.588  111.762 1.00 124.15 ? 473 GLN B C     1 
ATOM   7922 O  O     . GLN B 1 446 ? 67.476  86.610  112.451 1.00 123.81 ? 473 GLN B O     1 
ATOM   7923 C  CB    . GLN B 1 446 ? 66.496  89.203  113.230 1.00 124.94 ? 473 GLN B CB    1 
ATOM   7924 C  CG    . GLN B 1 446 ? 67.607  89.723  114.136 1.00 122.76 ? 473 GLN B CG    1 
ATOM   7925 C  CD    . GLN B 1 446 ? 68.517  88.624  114.646 1.00 137.04 ? 473 GLN B CD    1 
ATOM   7926 O  OE1   . GLN B 1 446 ? 69.724  88.641  114.407 1.00 141.94 ? 473 GLN B OE1   1 
ATOM   7927 N  NE2   . GLN B 1 446 ? 67.941  87.660  115.356 1.00 138.91 ? 473 GLN B NE2   1 
ATOM   7928 N  N     . VAL B 1 447 ? 68.828  87.603  110.944 1.00 131.03 ? 474 VAL B N     1 
ATOM   7929 C  CA    . VAL B 1 447 ? 69.692  86.446  110.750 1.00 133.95 ? 474 VAL B CA    1 
ATOM   7930 C  C     . VAL B 1 447 ? 71.146  86.734  111.088 1.00 137.79 ? 474 VAL B C     1 
ATOM   7931 O  O     . VAL B 1 447 ? 71.997  85.860  110.896 1.00 137.58 ? 474 VAL B O     1 
ATOM   7932 C  CB    . VAL B 1 447 ? 69.584  85.900  109.311 1.00 122.54 ? 474 VAL B CB    1 
ATOM   7933 C  CG1   . VAL B 1 447 ? 68.146  85.525  108.987 1.00 114.09 ? 474 VAL B CG1   1 
ATOM   7934 C  CG2   . VAL B 1 447 ? 70.116  86.920  108.315 1.00 120.20 ? 474 VAL B CG2   1 
ATOM   7935 N  N     . GLU B 1 448 ? 71.460  87.932  111.586 1.00 148.66 ? 475 GLU B N     1 
ATOM   7936 C  CA    . GLU B 1 448 ? 72.851  88.269  111.875 1.00 151.17 ? 475 GLU B CA    1 
ATOM   7937 C  C     . GLU B 1 448 ? 73.341  87.565  113.134 1.00 142.36 ? 475 GLU B C     1 
ATOM   7938 O  O     . GLU B 1 448 ? 74.494  87.124  113.196 1.00 138.39 ? 475 GLU B O     1 
ATOM   7939 C  CB    . GLU B 1 448 ? 73.009  89.785  112.001 1.00 150.95 ? 475 GLU B CB    1 
ATOM   7940 C  CG    . GLU B 1 448 ? 72.962  90.536  110.671 1.00 157.12 ? 475 GLU B CG    1 
ATOM   7941 C  CD    . GLU B 1 448 ? 71.600  90.479  109.999 1.00 163.35 ? 475 GLU B CD    1 
ATOM   7942 O  OE1   . GLU B 1 448 ? 70.595  90.227  110.698 1.00 157.68 ? 475 GLU B OE1   1 
ATOM   7943 O  OE2   . GLU B 1 448 ? 71.535  90.681  108.767 1.00 163.86 ? 475 GLU B OE2   1 
ATOM   7944 N  N     . HIS B 1 449 ? 72.486  87.453  114.144 1.00 145.37 ? 476 HIS B N     1 
ATOM   7945 C  CA    . HIS B 1 449 ? 72.776  86.672  115.334 1.00 144.17 ? 476 HIS B CA    1 
ATOM   7946 C  C     . HIS B 1 449 ? 71.638  85.693  115.581 1.00 139.80 ? 476 HIS B C     1 
ATOM   7947 O  O     . HIS B 1 449 ? 70.483  85.983  115.250 1.00 137.37 ? 476 HIS B O     1 
ATOM   7948 C  CB    . HIS B 1 449 ? 72.979  87.571  116.566 1.00 134.54 ? 476 HIS B CB    1 
ATOM   7949 C  CG    . HIS B 1 449 ? 71.811  88.454  116.876 1.00 139.75 ? 476 HIS B CG    1 
ATOM   7950 N  ND1   . HIS B 1 449 ? 70.708  88.013  117.575 1.00 143.01 ? 476 HIS B ND1   1 
ATOM   7951 C  CD2   . HIS B 1 449 ? 71.579  89.758  116.592 1.00 140.11 ? 476 HIS B CD2   1 
ATOM   7952 C  CE1   . HIS B 1 449 ? 69.845  89.004  117.704 1.00 141.10 ? 476 HIS B CE1   1 
ATOM   7953 N  NE2   . HIS B 1 449 ? 70.348  90.074  117.115 1.00 137.93 ? 476 HIS B NE2   1 
ATOM   7954 N  N     . PRO B 1 450 ? 71.934  84.521  116.143 1.00 133.07 ? 477 PRO B N     1 
ATOM   7955 C  CA    . PRO B 1 450 ? 70.891  83.500  116.304 1.00 121.79 ? 477 PRO B CA    1 
ATOM   7956 C  C     . PRO B 1 450 ? 69.793  83.945  117.257 1.00 127.43 ? 477 PRO B C     1 
ATOM   7957 O  O     . PRO B 1 450 ? 70.048  84.600  118.271 1.00 133.60 ? 477 PRO B O     1 
ATOM   7958 C  CB    . PRO B 1 450 ? 71.656  82.293  116.862 1.00 106.59 ? 477 PRO B CB    1 
ATOM   7959 C  CG    . PRO B 1 450 ? 72.883  82.875  117.483 1.00 111.92 ? 477 PRO B CG    1 
ATOM   7960 C  CD    . PRO B 1 450 ? 73.244  84.052  116.629 1.00 121.17 ? 477 PRO B CD    1 
ATOM   7961 N  N     . GLU B 1 451 ? 68.560  83.582  116.914 1.00 133.30 ? 478 GLU B N     1 
ATOM   7962 C  CA    . GLU B 1 451 ? 67.423  83.880  117.772 1.00 132.20 ? 478 GLU B CA    1 
ATOM   7963 C  C     . GLU B 1 451 ? 67.495  83.054  119.052 1.00 122.51 ? 478 GLU B C     1 
ATOM   7964 O  O     . GLU B 1 451 ? 67.962  81.911  119.057 1.00 128.33 ? 478 GLU B O     1 
ATOM   7965 C  CB    . GLU B 1 451 ? 66.113  83.611  117.029 1.00 131.68 ? 478 GLU B CB    1 
ATOM   7966 C  CG    . GLU B 1 451 ? 65.963  84.425  115.746 1.00 131.65 ? 478 GLU B CG    1 
ATOM   7967 C  CD    . GLU B 1 451 ? 64.668  84.138  115.008 1.00 124.84 ? 478 GLU B CD    1 
ATOM   7968 O  OE1   . GLU B 1 451 ? 64.009  83.126  115.328 1.00 120.26 ? 478 GLU B OE1   1 
ATOM   7969 O  OE2   . GLU B 1 451 ? 64.307  84.927  114.108 1.00 117.23 ? 478 GLU B OE2   1 
ATOM   7970 N  N     . LYS B 1 452 ? 67.028  83.651  120.146 1.00 117.36 ? 479 LYS B N     1 
ATOM   7971 C  CA    . LYS B 1 452 ? 67.191  83.057  121.468 1.00 112.21 ? 479 LYS B CA    1 
ATOM   7972 C  C     . LYS B 1 452 ? 66.410  81.753  121.568 1.00 111.74 ? 479 LYS B C     1 
ATOM   7973 O  O     . LYS B 1 452 ? 65.194  81.728  121.349 1.00 117.72 ? 479 LYS B O     1 
ATOM   7974 C  CB    . LYS B 1 452 ? 66.736  84.039  122.543 1.00 113.89 ? 479 LYS B CB    1 
ATOM   7975 C  CG    . LYS B 1 452 ? 67.014  83.583  123.966 1.00 113.14 ? 479 LYS B CG    1 
ATOM   7976 C  CD    . LYS B 1 452 ? 66.738  84.703  124.957 1.00 113.74 ? 479 LYS B CD    1 
ATOM   7977 C  CE    . LYS B 1 452 ? 67.029  84.267  126.383 1.00 117.87 ? 479 LYS B CE    1 
ATOM   7978 N  NZ    . LYS B 1 452 ? 66.844  85.382  127.350 1.00 118.08 ? 479 LYS B NZ    1 
ATOM   7979 N  N     . ALA B 1 453 ? 67.112  80.673  121.903 1.00 112.69 ? 480 ALA B N     1 
ATOM   7980 C  CA    . ALA B 1 453 ? 66.476  79.370  122.019 1.00 101.67 ? 480 ALA B CA    1 
ATOM   7981 C  C     . ALA B 1 453 ? 65.584  79.317  123.251 1.00 109.35 ? 480 ALA B C     1 
ATOM   7982 O  O     . ALA B 1 453 ? 65.843  79.969  124.266 1.00 108.84 ? 480 ALA B O     1 
ATOM   7983 C  CB    . ALA B 1 453 ? 67.529  78.264  122.092 1.00 93.11  ? 480 ALA B CB    1 
ATOM   7984 N  N     . VAL B 1 454 ? 64.523  78.528  123.152 1.00 98.87  ? 481 VAL B N     1 
ATOM   7985 C  CA    . VAL B 1 454 ? 63.580  78.343  124.252 1.00 104.25 ? 481 VAL B CA    1 
ATOM   7986 C  C     . VAL B 1 454 ? 64.066  77.164  125.085 1.00 109.37 ? 481 VAL B C     1 
ATOM   7987 O  O     . VAL B 1 454 ? 64.072  76.028  124.585 1.00 108.12 ? 481 VAL B O     1 
ATOM   7988 C  CB    . VAL B 1 454 ? 62.158  78.108  123.732 1.00 97.26  ? 481 VAL B CB    1 
ATOM   7989 C  CG1   . VAL B 1 454 ? 61.213  77.860  124.896 1.00 95.40  ? 481 VAL B CG1   1 
ATOM   7990 C  CG2   . VAL B 1 454 ? 61.703  79.305  122.921 1.00 93.13  ? 481 VAL B CG2   1 
ATOM   7991 N  N     . PRO B 1 455 ? 64.476  77.376  126.336 1.00 106.98 ? 482 PRO B N     1 
ATOM   7992 C  CA    . PRO B 1 455 ? 64.995  76.263  127.143 1.00 110.13 ? 482 PRO B CA    1 
ATOM   7993 C  C     . PRO B 1 455 ? 63.921  75.218  127.425 1.00 114.28 ? 482 PRO B C     1 
ATOM   7994 O  O     . PRO B 1 455 ? 62.740  75.532  127.592 1.00 118.32 ? 482 PRO B O     1 
ATOM   7995 C  CB    . PRO B 1 455 ? 65.469  76.949  128.437 1.00 103.33 ? 482 PRO B CB    1 
ATOM   7996 C  CG    . PRO B 1 455 ? 65.556  78.397  128.110 1.00 109.75 ? 482 PRO B CG    1 
ATOM   7997 C  CD    . PRO B 1 455 ? 64.523  78.656  127.065 1.00 100.39 ? 482 PRO B CD    1 
ATOM   7998 N  N     . ARG B 1 456 ? 64.360  73.961  127.464 1.00 111.62 ? 483 ARG B N     1 
ATOM   7999 C  CA    . ARG B 1 456 ? 63.639  72.708  127.674 1.00 109.50 ? 483 ARG B CA    1 
ATOM   8000 C  C     . ARG B 1 456 ? 62.660  72.376  126.540 1.00 108.65 ? 483 ARG B C     1 
ATOM   8001 O  O     . ARG B 1 456 ? 62.047  71.310  126.570 1.00 98.08  ? 483 ARG B O     1 
ATOM   8002 C  CB    . ARG B 1 456 ? 62.893  72.655  129.020 1.00 114.43 ? 483 ARG B CB    1 
ATOM   8003 C  CG    . ARG B 1 456 ? 63.775  72.681  130.259 1.00 103.26 ? 483 ARG B CG    1 
ATOM   8004 C  CD    . ARG B 1 456 ? 62.970  73.103  131.493 1.00 117.43 ? 483 ARG B CD    1 
ATOM   8005 N  NE    . ARG B 1 456 ? 62.384  74.431  131.348 1.00 138.79 ? 483 ARG B NE    1 
ATOM   8006 C  CZ    . ARG B 1 456 ? 63.043  75.568  131.534 1.00 137.03 ? 483 ARG B CZ    1 
ATOM   8007 N  NH1   . ARG B 1 456 ? 64.320  75.576  131.880 1.00 120.12 ? 483 ARG B NH1   1 
ATOM   8008 N  NH2   . ARG B 1 456 ? 62.409  76.725  131.358 1.00 139.53 ? 483 ARG B NH2   1 
ATOM   8009 N  N     . VAL B 1 457 ? 62.483  73.242  125.550 1.00 109.69 ? 484 VAL B N     1 
ATOM   8010 C  CA    . VAL B 1 457 ? 61.626  72.958  124.401 1.00 98.10  ? 484 VAL B CA    1 
ATOM   8011 C  C     . VAL B 1 457 ? 62.529  72.847  123.182 1.00 99.60  ? 484 VAL B C     1 
ATOM   8012 O  O     . VAL B 1 457 ? 63.181  73.822  122.790 1.00 96.87  ? 484 VAL B O     1 
ATOM   8013 C  CB    . VAL B 1 457 ? 60.544  74.031  124.190 1.00 108.55 ? 484 VAL B CB    1 
ATOM   8014 C  CG1   . VAL B 1 457 ? 59.598  73.629  123.060 1.00 101.42 ? 484 VAL B CG1   1 
ATOM   8015 C  CG2   . VAL B 1 457 ? 59.771  74.258  125.482 1.00 89.44  ? 484 VAL B CG2   1 
ATOM   8016 N  N     . ARG B 1 458 ? 62.572  71.662  122.583 1.00 92.32  ? 485 ARG B N     1 
ATOM   8017 C  CA    . ARG B 1 458 ? 63.461  71.417  121.458 1.00 83.28  ? 485 ARG B CA    1 
ATOM   8018 C  C     . ARG B 1 458 ? 62.864  71.978  120.173 1.00 87.84  ? 485 ARG B C     1 
ATOM   8019 O  O     . ARG B 1 458 ? 61.645  72.001  119.990 1.00 86.17  ? 485 ARG B O     1 
ATOM   8020 C  CB    . ARG B 1 458 ? 63.718  69.920  121.308 1.00 91.28  ? 485 ARG B CB    1 
ATOM   8021 C  CG    . ARG B 1 458 ? 64.988  69.553  120.560 1.00 102.92 ? 485 ARG B CG    1 
ATOM   8022 C  CD    . ARG B 1 458 ? 65.276  68.081  120.776 1.00 115.34 ? 485 ARG B CD    1 
ATOM   8023 N  NE    . ARG B 1 458 ? 64.990  67.697  122.154 1.00 125.84 ? 485 ARG B NE    1 
ATOM   8024 C  CZ    . ARG B 1 458 ? 65.052  66.458  122.620 1.00 130.70 ? 485 ARG B CZ    1 
ATOM   8025 N  NH1   . ARG B 1 458 ? 65.401  65.444  121.845 1.00 129.14 ? 485 ARG B NH1   1 
ATOM   8026 N  NH2   . ARG B 1 458 ? 64.755  66.229  123.897 1.00 118.10 ? 485 ARG B NH2   1 
ATOM   8027 N  N     . ASN B 1 459 ? 63.743  72.448  119.287 1.00 84.73  ? 486 ASN B N     1 
ATOM   8028 C  CA    . ASN B 1 459 ? 63.374  72.937  117.961 1.00 84.80  ? 486 ASN B CA    1 
ATOM   8029 C  C     . ASN B 1 459 ? 62.467  74.165  118.018 1.00 89.82  ? 486 ASN B C     1 
ATOM   8030 O  O     . ASN B 1 459 ? 61.714  74.429  117.073 1.00 85.38  ? 486 ASN B O     1 
ATOM   8031 C  CB    . ASN B 1 459 ? 62.712  71.832  117.129 1.00 80.14  ? 486 ASN B CB    1 
ATOM   8032 C  CG    . ASN B 1 459 ? 63.633  70.651  116.890 1.00 84.03  ? 486 ASN B CG    1 
ATOM   8033 O  OD1   . ASN B 1 459 ? 64.726  70.802  116.344 1.00 80.46  ? 486 ASN B OD1   1 
ATOM   8034 N  ND2   . ASN B 1 459 ? 63.201  69.467  117.313 1.00 83.03  ? 486 ASN B ND2   1 
ATOM   8035 N  N     . LEU B 1 460 ? 62.523  74.927  119.107 1.00 94.79  ? 487 LEU B N     1 
ATOM   8036 C  CA    . LEU B 1 460 ? 61.723  76.132  119.264 1.00 88.39  ? 487 LEU B CA    1 
ATOM   8037 C  C     . LEU B 1 460 ? 62.619  77.278  119.705 1.00 84.25  ? 487 LEU B C     1 
ATOM   8038 O  O     . LEU B 1 460 ? 63.516  77.092  120.534 1.00 91.89  ? 487 LEU B O     1 
ATOM   8039 C  CB    . LEU B 1 460 ? 60.593  75.927  120.279 1.00 87.56  ? 487 LEU B CB    1 
ATOM   8040 C  CG    . LEU B 1 460 ? 59.513  77.010  120.302 1.00 97.07  ? 487 LEU B CG    1 
ATOM   8041 C  CD1   . LEU B 1 460 ? 58.754  77.038  118.983 1.00 79.49  ? 487 LEU B CD1   1 
ATOM   8042 C  CD2   . LEU B 1 460 ? 58.560  76.798  121.468 1.00 94.09  ? 487 LEU B CD2   1 
ATOM   8043 N  N     . VAL B 1 461 ? 62.380  78.464  119.140 1.00 87.58  ? 488 VAL B N     1 
ATOM   8044 C  CA    . VAL B 1 461 ? 63.159  79.655  119.450 1.00 96.03  ? 488 VAL B CA    1 
ATOM   8045 C  C     . VAL B 1 461 ? 62.213  80.836  119.614 1.00 93.22  ? 488 VAL B C     1 
ATOM   8046 O  O     . VAL B 1 461 ? 61.055  80.798  119.195 1.00 94.58  ? 488 VAL B O     1 
ATOM   8047 C  CB    . VAL B 1 461 ? 64.213  79.978  118.366 1.00 90.05  ? 488 VAL B CB    1 
ATOM   8048 C  CG1   . VAL B 1 461 ? 65.202  78.831  118.211 1.00 88.12  ? 488 VAL B CG1   1 
ATOM   8049 C  CG2   . VAL B 1 461 ? 63.531  80.292  117.043 1.00 76.79  ? 488 VAL B CG2   1 
ATOM   8050 N  N     . GLU B 1 462 ? 62.726  81.896  120.233 1.00 99.88  ? 489 GLU B N     1 
ATOM   8051 C  CA    . GLU B 1 462 ? 61.963  83.129  120.356 1.00 99.13  ? 489 GLU B CA    1 
ATOM   8052 C  C     . GLU B 1 462 ? 61.879  83.828  119.005 1.00 100.49 ? 489 GLU B C     1 
ATOM   8053 O  O     . GLU B 1 462 ? 62.872  83.934  118.280 1.00 107.16 ? 489 GLU B O     1 
ATOM   8054 C  CB    . GLU B 1 462 ? 62.603  84.054  121.390 1.00 113.70 ? 489 GLU B CB    1 
ATOM   8055 C  CG    . GLU B 1 462 ? 62.739  83.437  122.771 1.00 123.32 ? 489 GLU B CG    1 
ATOM   8056 C  CD    . GLU B 1 462 ? 63.354  84.390  123.777 1.00 129.37 ? 489 GLU B CD    1 
ATOM   8057 O  OE1   . GLU B 1 462 ? 63.651  85.544  123.401 1.00 136.57 ? 489 GLU B OE1   1 
ATOM   8058 O  OE2   . GLU B 1 462 ? 63.540  83.985  124.944 1.00 128.33 ? 489 GLU B OE2   1 
ATOM   8059 N  N     . ALA B 1 463 ? 60.685  84.308  118.669 1.00 108.63 ? 490 ALA B N     1 
ATOM   8060 C  CA    . ALA B 1 463 ? 60.438  84.884  117.353 1.00 107.96 ? 490 ALA B CA    1 
ATOM   8061 C  C     . ALA B 1 463 ? 60.919  86.329  117.309 1.00 110.61 ? 490 ALA B C     1 
ATOM   8062 O  O     . ALA B 1 463 ? 60.446  87.171  118.080 1.00 101.94 ? 490 ALA B O     1 
ATOM   8063 C  CB    . ALA B 1 463 ? 58.952  84.805  117.008 1.00 96.01  ? 490 ALA B CB    1 
ATOM   8064 N  N     . ASP B 1 464 ? 61.858  86.612  116.411 1.00 109.31 ? 491 ASP B N     1 
ATOM   8065 C  CA    . ASP B 1 464 ? 62.270  87.979  116.130 1.00 115.37 ? 491 ASP B CA    1 
ATOM   8066 C  C     . ASP B 1 464 ? 61.453  88.492  114.941 1.00 102.32 ? 491 ASP B C     1 
ATOM   8067 O  O     . ASP B 1 464 ? 60.418  87.918  114.593 1.00 101.82 ? 491 ASP B O     1 
ATOM   8068 C  CB    . ASP B 1 464 ? 63.782  88.035  115.902 1.00 123.51 ? 491 ASP B CB    1 
ATOM   8069 C  CG    . ASP B 1 464 ? 64.572  87.747  117.168 1.00 121.54 ? 491 ASP B CG    1 
ATOM   8070 O  OD1   . ASP B 1 464 ? 63.951  87.386  118.189 1.00 115.55 ? 491 ASP B OD1   1 
ATOM   8071 O  OD2   . ASP B 1 464 ? 65.813  87.887  117.141 1.00 122.53 ? 491 ASP B OD2   1 
ATOM   8072 N  N     . TYR B 1 465 ? 61.903  89.571  114.302 1.00 94.42  ? 492 TYR B N     1 
ATOM   8073 C  CA    . TYR B 1 465 ? 61.127  90.185  113.229 1.00 100.56 ? 492 TYR B CA    1 
ATOM   8074 C  C     . TYR B 1 465 ? 60.936  89.211  112.070 1.00 97.65  ? 492 TYR B C     1 
ATOM   8075 O  O     . TYR B 1 465 ? 61.904  88.661  111.537 1.00 96.10  ? 492 TYR B O     1 
ATOM   8076 C  CB    . TYR B 1 465 ? 61.817  91.465  112.750 1.00 96.72  ? 492 TYR B CB    1 
ATOM   8077 C  CG    . TYR B 1 465 ? 60.986  92.283  111.787 1.00 103.48 ? 492 TYR B CG    1 
ATOM   8078 C  CD1   . TYR B 1 465 ? 59.693  92.668  112.113 1.00 99.16  ? 492 TYR B CD1   1 
ATOM   8079 C  CD2   . TYR B 1 465 ? 61.498  92.682  110.559 1.00 110.57 ? 492 TYR B CD2   1 
ATOM   8080 C  CE1   . TYR B 1 465 ? 58.927  93.415  111.238 1.00 103.26 ? 492 TYR B CE1   1 
ATOM   8081 C  CE2   . TYR B 1 465 ? 60.739  93.433  109.677 1.00 113.22 ? 492 TYR B CE2   1 
ATOM   8082 C  CZ    . TYR B 1 465 ? 59.454  93.796  110.023 1.00 106.90 ? 492 TYR B CZ    1 
ATOM   8083 O  OH    . TYR B 1 465 ? 58.693  94.543  109.152 1.00 101.00 ? 492 TYR B OH    1 
ATOM   8084 N  N     . SER B 1 466 ? 59.676  88.996  111.693 1.00 100.81 ? 493 SER B N     1 
ATOM   8085 C  CA    . SER B 1 466 ? 59.303  88.068  110.636 1.00 95.91  ? 493 SER B CA    1 
ATOM   8086 C  C     . SER B 1 466 ? 58.384  88.778  109.651 1.00 102.25 ? 493 SER B C     1 
ATOM   8087 O  O     . SER B 1 466 ? 57.800  89.819  109.959 1.00 100.73 ? 493 SER B O     1 
ATOM   8088 C  CB    . SER B 1 466 ? 58.622  86.816  111.208 1.00 91.95  ? 493 SER B CB    1 
ATOM   8089 O  OG    . SER B 1 466 ? 59.388  86.268  112.267 1.00 79.07  ? 493 SER B OG    1 
ATOM   8090 N  N     . TYR B 1 467 ? 58.249  88.204  108.451 1.00 107.08 ? 494 TYR B N     1 
ATOM   8091 C  CA    . TYR B 1 467 ? 57.632  88.932  107.348 1.00 114.66 ? 494 TYR B CA    1 
ATOM   8092 C  C     . TYR B 1 467 ? 56.539  88.154  106.615 1.00 110.19 ? 494 TYR B C     1 
ATOM   8093 O  O     . TYR B 1 467 ? 56.002  88.662  105.626 1.00 130.57 ? 494 TYR B O     1 
ATOM   8094 C  CB    . TYR B 1 467 ? 58.704  89.391  106.353 1.00 116.98 ? 494 TYR B CB    1 
ATOM   8095 C  CG    . TYR B 1 467 ? 58.327  90.646  105.593 1.00 121.57 ? 494 TYR B CG    1 
ATOM   8096 C  CD1   . TYR B 1 467 ? 58.411  91.895  106.195 1.00 120.79 ? 494 TYR B CD1   1 
ATOM   8097 C  CD2   . TYR B 1 467 ? 57.894  90.583  104.273 1.00 131.78 ? 494 TYR B CD2   1 
ATOM   8098 C  CE1   . TYR B 1 467 ? 58.065  93.045  105.509 1.00 137.00 ? 494 TYR B CE1   1 
ATOM   8099 C  CE2   . TYR B 1 467 ? 57.546  91.726  103.579 1.00 144.80 ? 494 TYR B CE2   1 
ATOM   8100 C  CZ    . TYR B 1 467 ? 57.634  92.955  104.202 1.00 153.84 ? 494 TYR B CZ    1 
ATOM   8101 O  OH    . TYR B 1 467 ? 57.290  94.100  103.518 1.00 161.67 ? 494 TYR B OH    1 
ATOM   8102 N  N     . TRP B 1 468 ? 56.184  86.950  107.057 1.00 77.14  ? 495 TRP B N     1 
ATOM   8103 C  CA    . TRP B 1 468 ? 55.128  86.190  106.398 1.00 81.54  ? 495 TRP B CA    1 
ATOM   8104 C  C     . TRP B 1 468 ? 54.135  85.664  107.427 1.00 78.42  ? 495 TRP B C     1 
ATOM   8105 O  O     . TRP B 1 468 ? 54.381  85.680  108.636 1.00 97.93  ? 495 TRP B O     1 
ATOM   8106 C  CB    . TRP B 1 468 ? 55.694  85.030  105.569 1.00 91.05  ? 495 TRP B CB    1 
ATOM   8107 C  CG    . TRP B 1 468 ? 56.421  85.459  104.326 1.00 84.87  ? 495 TRP B CG    1 
ATOM   8108 C  CD1   . TRP B 1 468 ? 56.213  86.597  103.600 1.00 78.31  ? 495 TRP B CD1   1 
ATOM   8109 C  CD2   . TRP B 1 468 ? 57.476  84.751  103.667 1.00 92.76  ? 495 TRP B CD2   1 
ATOM   8110 N  NE1   . TRP B 1 468 ? 57.075  86.641  102.530 1.00 84.75  ? 495 TRP B NE1   1 
ATOM   8111 C  CE2   . TRP B 1 468 ? 57.861  85.518  102.549 1.00 90.14  ? 495 TRP B CE2   1 
ATOM   8112 C  CE3   . TRP B 1 468 ? 58.133  83.542  103.915 1.00 84.34  ? 495 TRP B CE3   1 
ATOM   8113 C  CZ2   . TRP B 1 468 ? 58.873  85.114  101.681 1.00 87.48  ? 495 TRP B CZ2   1 
ATOM   8114 C  CZ3   . TRP B 1 468 ? 59.139  83.145  103.054 1.00 78.98  ? 495 TRP B CZ3   1 
ATOM   8115 C  CH2   . TRP B 1 468 ? 59.498  83.927  101.950 1.00 92.83  ? 495 TRP B CH2   1 
ATOM   8116 N  N     . THR B 1 469 ? 52.995  85.197  106.922 1.00 78.60  ? 496 THR B N     1 
ATOM   8117 C  CA    . THR B 1 469 ? 51.949  84.557  107.713 1.00 82.73  ? 496 THR B CA    1 
ATOM   8118 C  C     . THR B 1 469 ? 51.489  83.269  107.043 1.00 76.70  ? 496 THR B C     1 
ATOM   8119 O  O     . THR B 1 469 ? 50.291  82.981  106.967 1.00 73.42  ? 496 THR B O     1 
ATOM   8120 C  CB    . THR B 1 469 ? 50.763  85.496  107.931 1.00 70.23  ? 496 THR B CB    1 
ATOM   8121 O  OG1   . THR B 1 469 ? 50.327  86.029  106.673 1.00 78.12  ? 496 THR B OG1   1 
ATOM   8122 C  CG2   . THR B 1 469 ? 51.147  86.637  108.861 1.00 72.40  ? 496 THR B CG2   1 
ATOM   8123 N  N     . LEU B 1 470 ? 52.441  82.470  106.552 1.00 73.25  ? 497 LEU B N     1 
ATOM   8124 C  CA    . LEU B 1 470 ? 52.099  81.252  105.820 1.00 73.53  ? 497 LEU B CA    1 
ATOM   8125 C  C     . LEU B 1 470 ? 51.342  80.269  106.703 1.00 70.74  ? 497 LEU B C     1 
ATOM   8126 O  O     . LEU B 1 470 ? 50.266  79.784  106.333 1.00 60.57  ? 497 LEU B O     1 
ATOM   8127 C  CB    . LEU B 1 470 ? 53.364  80.599  105.266 1.00 57.92  ? 497 LEU B CB    1 
ATOM   8128 C  CG    . LEU B 1 470 ? 54.260  81.460  104.379 1.00 88.41  ? 497 LEU B CG    1 
ATOM   8129 C  CD1   . LEU B 1 470 ? 55.606  80.785  104.214 1.00 84.60  ? 497 LEU B CD1   1 
ATOM   8130 C  CD2   . LEU B 1 470 ? 53.606  81.704  103.027 1.00 82.69  ? 497 LEU B CD2   1 
ATOM   8131 N  N     . ALA B 1 471 ? 51.894  79.958  107.873 1.00 65.18  ? 498 ALA B N     1 
ATOM   8132 C  CA    . ALA B 1 471 ? 51.285  79.002  108.787 1.00 63.53  ? 498 ALA B CA    1 
ATOM   8133 C  C     . ALA B 1 471 ? 51.733  79.325  110.202 1.00 62.08  ? 498 ALA B C     1 
ATOM   8134 O  O     . ALA B 1 471 ? 52.922  79.560  110.438 1.00 75.26  ? 498 ALA B O     1 
ATOM   8135 C  CB    . ALA B 1 471 ? 51.666  77.563  108.424 1.00 67.02  ? 498 ALA B CB    1 
ATOM   8136 N  N     . TYR B 1 472 ? 50.787  79.341  111.137 1.00 58.25  ? 499 TYR B N     1 
ATOM   8137 C  CA    . TYR B 1 472 ? 51.109  79.652  112.521 1.00 64.51  ? 499 TYR B CA    1 
ATOM   8138 C  C     . TYR B 1 472 ? 50.117  78.962  113.443 1.00 68.45  ? 499 TYR B C     1 
ATOM   8139 O  O     . TYR B 1 472 ? 48.977  78.683  113.060 1.00 65.74  ? 499 TYR B O     1 
ATOM   8140 C  CB    . TYR B 1 472 ? 51.108  81.166  112.774 1.00 59.51  ? 499 TYR B CB    1 
ATOM   8141 C  CG    . TYR B 1 472 ? 49.792  81.866  112.490 1.00 63.44  ? 499 TYR B CG    1 
ATOM   8142 C  CD1   . TYR B 1 472 ? 48.796  81.941  113.459 1.00 64.48  ? 499 TYR B CD1   1 
ATOM   8143 C  CD2   . TYR B 1 472 ? 49.554  82.468  111.261 1.00 65.72  ? 499 TYR B CD2   1 
ATOM   8144 C  CE1   . TYR B 1 472 ? 47.600  82.585  113.207 1.00 70.75  ? 499 TYR B CE1   1 
ATOM   8145 C  CE2   . TYR B 1 472 ? 48.358  83.116  111.000 1.00 66.36  ? 499 TYR B CE2   1 
ATOM   8146 C  CZ    . TYR B 1 472 ? 47.386  83.170  111.977 1.00 71.74  ? 499 TYR B CZ    1 
ATOM   8147 O  OH    . TYR B 1 472 ? 46.197  83.812  111.722 1.00 69.70  ? 499 TYR B OH    1 
ATOM   8148 N  N     . VAL B 1 473 ? 50.570  78.686  114.663 1.00 72.03  ? 500 VAL B N     1 
ATOM   8149 C  CA    . VAL B 1 473 ? 49.723  78.167  115.728 1.00 59.88  ? 500 VAL B CA    1 
ATOM   8150 C  C     . VAL B 1 473 ? 49.393  79.319  116.664 1.00 65.63  ? 500 VAL B C     1 
ATOM   8151 O  O     . VAL B 1 473 ? 50.291  80.053  117.096 1.00 69.12  ? 500 VAL B O     1 
ATOM   8152 C  CB    . VAL B 1 473 ? 50.414  77.022  116.487 1.00 63.34  ? 500 VAL B CB    1 
ATOM   8153 C  CG1   . VAL B 1 473 ? 49.454  76.398  117.485 1.00 75.31  ? 500 VAL B CG1   1 
ATOM   8154 C  CG2   . VAL B 1 473 ? 50.937  75.978  115.517 1.00 69.72  ? 500 VAL B CG2   1 
ATOM   8155 N  N     . ILE B 1 474 ? 48.110  79.486  116.974 1.00 67.71  ? 501 ILE B N     1 
ATOM   8156 C  CA    . ILE B 1 474 ? 47.646  80.565  117.835 1.00 72.42  ? 501 ILE B CA    1 
ATOM   8157 C  C     . ILE B 1 474 ? 46.904  79.963  119.021 1.00 73.13  ? 501 ILE B C     1 
ATOM   8158 O  O     . ILE B 1 474 ? 46.156  78.990  118.875 1.00 71.27  ? 501 ILE B O     1 
ATOM   8159 C  CB    . ILE B 1 474 ? 46.756  81.567  117.065 1.00 63.24  ? 501 ILE B CB    1 
ATOM   8160 C  CG1   . ILE B 1 474 ? 46.415  82.776  117.940 1.00 69.02  ? 501 ILE B CG1   1 
ATOM   8161 C  CG2   . ILE B 1 474 ? 45.493  80.895  116.540 1.00 65.63  ? 501 ILE B CG2   1 
ATOM   8162 C  CD1   . ILE B 1 474 ? 45.735  83.903  117.188 1.00 82.76  ? 501 ILE B CD1   1 
ATOM   8163 N  N     . SER B 1 475 ? 47.137  80.528  120.200 1.00 71.31  ? 502 SER B N     1 
ATOM   8164 C  CA    . SER B 1 475 ? 46.443  80.104  121.404 1.00 74.71  ? 502 SER B CA    1 
ATOM   8165 C  C     . SER B 1 475 ? 45.216  80.977  121.639 1.00 82.06  ? 502 SER B C     1 
ATOM   8166 O  O     . SER B 1 475 ? 45.084  82.070  121.083 1.00 86.43  ? 502 SER B O     1 
ATOM   8167 C  CB    . SER B 1 475 ? 47.369  80.165  122.619 1.00 75.06  ? 502 SER B CB    1 
ATOM   8168 O  OG    . SER B 1 475 ? 47.629  81.506  122.997 1.00 85.48  ? 502 SER B OG    1 
ATOM   8169 N  N     . LEU B 1 476 ? 44.304  80.470  122.474 1.00 77.56  ? 503 LEU B N     1 
ATOM   8170 C  CA    . LEU B 1 476 ? 43.135  81.260  122.846 1.00 78.35  ? 503 LEU B CA    1 
ATOM   8171 C  C     . LEU B 1 476 ? 43.552  82.569  123.499 1.00 83.37  ? 503 LEU B C     1 
ATOM   8172 O  O     . LEU B 1 476 ? 42.935  83.615  123.266 1.00 94.61  ? 503 LEU B O     1 
ATOM   8173 C  CB    . LEU B 1 476 ? 42.231  80.458  123.780 1.00 89.78  ? 503 LEU B CB    1 
ATOM   8174 C  CG    . LEU B 1 476 ? 40.939  81.161  124.201 1.00 87.61  ? 503 LEU B CG    1 
ATOM   8175 C  CD1   . LEU B 1 476 ? 40.076  81.468  122.986 1.00 81.29  ? 503 LEU B CD1   1 
ATOM   8176 C  CD2   . LEU B 1 476 ? 40.174  80.324  125.212 1.00 77.55  ? 503 LEU B CD2   1 
ATOM   8177 N  N     . GLN B 1 477 ? 44.604  82.529  124.318 1.00 80.28  ? 504 GLN B N     1 
ATOM   8178 C  CA    . GLN B 1 477 ? 45.154  83.755  124.885 1.00 79.01  ? 504 GLN B CA    1 
ATOM   8179 C  C     . GLN B 1 477 ? 45.663  84.683  123.789 1.00 92.26  ? 504 GLN B C     1 
ATOM   8180 O  O     . GLN B 1 477 ? 45.411  85.893  123.814 1.00 90.31  ? 504 GLN B O     1 
ATOM   8181 C  CB    . GLN B 1 477 ? 46.271  83.412  125.870 1.00 86.41  ? 504 GLN B CB    1 
ATOM   8182 C  CG    . GLN B 1 477 ? 47.040  84.612  126.393 1.00 96.51  ? 504 GLN B CG    1 
ATOM   8183 C  CD    . GLN B 1 477 ? 48.192  84.212  127.295 1.00 111.36 ? 504 GLN B CD    1 
ATOM   8184 O  OE1   . GLN B 1 477 ? 48.460  83.027  127.491 1.00 120.10 ? 504 GLN B OE1   1 
ATOM   8185 N  NE2   . GLN B 1 477 ? 48.880  85.203  127.850 1.00 118.42 ? 504 GLN B NE2   1 
ATOM   8186 N  N     . GLY B 1 478 ? 46.377  84.126  122.807 1.00 83.02  ? 505 GLY B N     1 
ATOM   8187 C  CA    . GLY B 1 478 ? 46.921  84.950  121.740 1.00 74.58  ? 505 GLY B CA    1 
ATOM   8188 C  C     . GLY B 1 478 ? 45.846  85.594  120.887 1.00 83.86  ? 505 GLY B C     1 
ATOM   8189 O  O     . GLY B 1 478 ? 45.974  86.751  120.478 1.00 86.91  ? 505 GLY B O     1 
ATOM   8190 N  N     . ALA B 1 479 ? 44.770  84.855  120.608 1.00 80.95  ? 506 ALA B N     1 
ATOM   8191 C  CA    . ALA B 1 479 ? 43.672  85.419  119.832 1.00 80.04  ? 506 ALA B CA    1 
ATOM   8192 C  C     . ALA B 1 479 ? 43.006  86.568  120.576 1.00 83.85  ? 506 ALA B C     1 
ATOM   8193 O  O     . ALA B 1 479 ? 42.582  87.553  119.960 1.00 89.23  ? 506 ALA B O     1 
ATOM   8194 C  CB    . ALA B 1 479 ? 42.654  84.331  119.494 1.00 86.54  ? 506 ALA B CB    1 
ATOM   8195 N  N     . ARG B 1 480 ? 42.913  86.467  121.905 1.00 87.05  ? 507 ARG B N     1 
ATOM   8196 C  CA    . ARG B 1 480 ? 42.323  87.550  122.686 1.00 89.55  ? 507 ARG B CA    1 
ATOM   8197 C  C     . ARG B 1 480 ? 43.176  88.810  122.615 1.00 89.46  ? 507 ARG B C     1 
ATOM   8198 O  O     . ARG B 1 480 ? 42.645  89.922  122.498 1.00 87.24  ? 507 ARG B O     1 
ATOM   8199 C  CB    . ARG B 1 480 ? 42.138  87.117  124.140 1.00 80.82  ? 507 ARG B CB    1 
ATOM   8200 C  CG    . ARG B 1 480 ? 41.070  86.058  124.355 1.00 87.11  ? 507 ARG B CG    1 
ATOM   8201 C  CD    . ARG B 1 480 ? 40.573  86.070  125.795 1.00 96.42  ? 507 ARG B CD    1 
ATOM   8202 N  NE    . ARG B 1 480 ? 39.513  85.096  126.024 1.00 101.60 ? 507 ARG B NE    1 
ATOM   8203 C  CZ    . ARG B 1 480 ? 39.685  83.930  126.633 1.00 105.15 ? 507 ARG B CZ    1 
ATOM   8204 N  NH1   . ARG B 1 480 ? 40.868  83.559  127.097 1.00 85.93  ? 507 ARG B NH1   1 
ATOM   8205 N  NH2   . ARG B 1 480 ? 38.643  83.118  126.787 1.00 96.43  ? 507 ARG B NH2   1 
ATOM   8206 N  N     . LYS B 1 481 ? 44.501  88.658  122.685 1.00 82.45  ? 508 LYS B N     1 
ATOM   8207 C  CA    . LYS B 1 481 ? 45.388  89.818  122.676 1.00 80.22  ? 508 LYS B CA    1 
ATOM   8208 C  C     . LYS B 1 481 ? 45.290  90.577  121.359 1.00 86.74  ? 508 LYS B C     1 
ATOM   8209 O  O     . LYS B 1 481 ? 45.197  91.810  121.345 1.00 97.26  ? 508 LYS B O     1 
ATOM   8210 C  CB    . LYS B 1 481 ? 46.831  89.382  122.932 1.00 86.31  ? 508 LYS B CB    1 
ATOM   8211 C  CG    . LYS B 1 481 ? 47.081  88.803  124.312 1.00 81.30  ? 508 LYS B CG    1 
ATOM   8212 C  CD    . LYS B 1 481 ? 48.570  88.607  124.545 1.00 81.89  ? 508 LYS B CD    1 
ATOM   8213 C  CE    . LYS B 1 481 ? 48.850  88.075  125.939 1.00 86.82  ? 508 LYS B CE    1 
ATOM   8214 N  NZ    . LYS B 1 481 ? 50.312  88.008  126.213 1.00 88.29  ? 508 LYS B NZ    1 
ATOM   8215 N  N     . LEU B 1 482 ? 45.318  89.854  120.237 1.00 86.72  ? 509 LEU B N     1 
ATOM   8216 C  CA    . LEU B 1 482 ? 45.257  90.509  118.935 1.00 79.68  ? 509 LEU B CA    1 
ATOM   8217 C  C     . LEU B 1 482 ? 43.944  91.261  118.757 1.00 86.06  ? 509 LEU B C     1 
ATOM   8218 O  O     . LEU B 1 482 ? 43.930  92.393  118.257 1.00 91.33  ? 509 LEU B O     1 
ATOM   8219 C  CB    . LEU B 1 482 ? 45.444  89.478  117.822 1.00 82.21  ? 509 LEU B CB    1 
ATOM   8220 C  CG    . LEU B 1 482 ? 46.727  88.645  117.881 1.00 71.69  ? 509 LEU B CG    1 
ATOM   8221 C  CD1   . LEU B 1 482 ? 46.793  87.684  116.705 1.00 69.30  ? 509 LEU B CD1   1 
ATOM   8222 C  CD2   . LEU B 1 482 ? 47.957  89.541  117.919 1.00 73.24  ? 509 LEU B CD2   1 
ATOM   8223 N  N     . LEU B 1 483 ? 42.829  90.651  119.166 1.00 86.54  ? 510 LEU B N     1 
ATOM   8224 C  CA    . LEU B 1 483 ? 41.541  91.330  119.077 1.00 77.03  ? 510 LEU B CA    1 
ATOM   8225 C  C     . LEU B 1 483 ? 41.500  92.557  119.979 1.00 90.97  ? 510 LEU B C     1 
ATOM   8226 O  O     . LEU B 1 483 ? 40.927  93.589  119.609 1.00 90.64  ? 510 LEU B O     1 
ATOM   8227 C  CB    . LEU B 1 483 ? 40.412  90.364  119.438 1.00 78.45  ? 510 LEU B CB    1 
ATOM   8228 C  CG    . LEU B 1 483 ? 40.206  89.152  118.532 1.00 76.75  ? 510 LEU B CG    1 
ATOM   8229 C  CD1   . LEU B 1 483 ? 39.074  88.294  119.063 1.00 74.55  ? 510 LEU B CD1   1 
ATOM   8230 C  CD2   . LEU B 1 483 ? 39.924  89.588  117.108 1.00 76.99  ? 510 LEU B CD2   1 
ATOM   8231 N  N     . ALA B 1 484 ? 42.110  92.467  121.165 1.00 93.63  ? 511 ALA B N     1 
ATOM   8232 C  CA    . ALA B 1 484 ? 42.103  93.582  122.106 1.00 88.78  ? 511 ALA B CA    1 
ATOM   8233 C  C     . ALA B 1 484 ? 42.873  94.791  121.594 1.00 88.92  ? 511 ALA B C     1 
ATOM   8234 O  O     . ALA B 1 484 ? 42.618  95.909  122.054 1.00 93.66  ? 511 ALA B O     1 
ATOM   8235 C  CB    . ALA B 1 484 ? 42.673  93.137  123.453 1.00 85.60  ? 511 ALA B CB    1 
ATOM   8236 N  N     . ALA B 1 485 ? 43.804  94.599  120.658 1.00 91.31  ? 512 ALA B N     1 
ATOM   8237 C  CA    . ALA B 1 485 ? 44.567  95.715  120.115 1.00 97.97  ? 512 ALA B CA    1 
ATOM   8238 C  C     . ALA B 1 485 ? 43.730  96.638  119.242 1.00 97.27  ? 512 ALA B C     1 
ATOM   8239 O  O     . ALA B 1 485 ? 44.178  97.752  118.950 1.00 89.12  ? 512 ALA B O     1 
ATOM   8240 C  CB    . ALA B 1 485 ? 45.757  95.193  119.307 1.00 89.01  ? 512 ALA B CB    1 
ATOM   8241 N  N     . GLU B 1 486 ? 42.536  96.212  118.838 1.00 96.51  ? 513 GLU B N     1 
ATOM   8242 C  CA    . GLU B 1 486 ? 41.716  96.933  117.870 1.00 98.06  ? 513 GLU B CA    1 
ATOM   8243 C  C     . GLU B 1 486 ? 42.543  97.309  116.639 1.00 94.94  ? 513 GLU B C     1 
ATOM   8244 O  O     . GLU B 1 486 ? 42.741  98.499  116.355 1.00 104.38 ? 513 GLU B O     1 
ATOM   8245 C  CB    . GLU B 1 486 ? 41.081  98.165  118.499 1.00 90.68  ? 513 GLU B CB    1 
ATOM   8246 C  CG    . GLU B 1 486 ? 39.969  98.791  117.665 1.00 115.76 ? 513 GLU B CG    1 
ATOM   8247 C  CD    . GLU B 1 486 ? 39.482  100.105 118.240 1.00 133.93 ? 513 GLU B CD    1 
ATOM   8248 O  OE1   . GLU B 1 486 ? 39.850  100.424 119.391 1.00 120.33 ? 513 GLU B OE1   1 
ATOM   8249 O  OE2   . GLU B 1 486 ? 38.735  100.821 117.540 1.00 149.21 ? 513 GLU B OE2   1 
ATOM   8250 N  N     . PRO B 1 487 ? 43.056  96.327  115.895 1.00 88.41  ? 514 PRO B N     1 
ATOM   8251 C  CA    . PRO B 1 487 ? 43.917  96.651  114.750 1.00 89.78  ? 514 PRO B CA    1 
ATOM   8252 C  C     . PRO B 1 487 ? 43.164  97.220  113.561 1.00 91.10  ? 514 PRO B C     1 
ATOM   8253 O  O     . PRO B 1 487 ? 43.806  97.717  112.628 1.00 103.67 ? 514 PRO B O     1 
ATOM   8254 C  CB    . PRO B 1 487 ? 44.556  95.303  114.408 1.00 90.34  ? 514 PRO B CB    1 
ATOM   8255 C  CG    . PRO B 1 487 ? 43.526  94.306  114.813 1.00 77.13  ? 514 PRO B CG    1 
ATOM   8256 C  CD    . PRO B 1 487 ? 42.855  94.873  116.037 1.00 82.70  ? 514 PRO B CD    1 
ATOM   8257 N  N     . LEU B 1 488 ? 41.830  97.171  113.562 1.00 84.99  ? 515 LEU B N     1 
ATOM   8258 C  CA    . LEU B 1 488 ? 41.077  97.680  112.421 1.00 89.82  ? 515 LEU B CA    1 
ATOM   8259 C  C     . LEU B 1 488 ? 41.182  99.197  112.322 1.00 99.66  ? 515 LEU B C     1 
ATOM   8260 O  O     . LEU B 1 488 ? 41.252  99.747  111.217 1.00 105.61 ? 515 LEU B O     1 
ATOM   8261 C  CB    . LEU B 1 488 ? 39.617  97.241  112.520 1.00 92.83  ? 515 LEU B CB    1 
ATOM   8262 C  CG    . LEU B 1 488 ? 39.378  95.740  112.702 1.00 83.85  ? 515 LEU B CG    1 
ATOM   8263 C  CD1   . LEU B 1 488 ? 37.904  95.411  112.529 1.00 79.13  ? 515 LEU B CD1   1 
ATOM   8264 C  CD2   . LEU B 1 488 ? 40.233  94.920  111.746 1.00 76.76  ? 515 LEU B CD2   1 
ATOM   8265 N  N     . SER B 1 489 ? 41.197  99.889  113.464 1.00 100.21 ? 516 SER B N     1 
ATOM   8266 C  CA    . SER B 1 489 ? 41.375  101.336 113.455 1.00 99.58  ? 516 SER B CA    1 
ATOM   8267 C  C     . SER B 1 489 ? 42.783  101.742 113.039 1.00 96.90  ? 516 SER B C     1 
ATOM   8268 O  O     . SER B 1 489 ? 42.983  102.878 112.599 1.00 97.09  ? 516 SER B O     1 
ATOM   8269 C  CB    . SER B 1 489 ? 41.055  101.912 114.834 1.00 93.01  ? 516 SER B CB    1 
ATOM   8270 O  OG    . SER B 1 489 ? 41.902  101.359 115.827 1.00 107.30 ? 516 SER B OG    1 
ATOM   8271 N  N     . LYS B 1 490 ? 43.755  100.847 113.174 1.00 95.45  ? 517 LYS B N     1 
ATOM   8272 C  CA    . LYS B 1 490 ? 45.146  101.087 112.808 1.00 95.75  ? 517 LYS B CA    1 
ATOM   8273 C  C     . LYS B 1 490 ? 45.628  99.995  111.866 1.00 93.14  ? 517 LYS B C     1 
ATOM   8274 O  O     . LYS B 1 490 ? 46.625  99.313  112.119 1.00 91.80  ? 517 LYS B O     1 
ATOM   8275 C  CB    . LYS B 1 490 ? 46.014  101.167 114.061 1.00 102.70 ? 517 LYS B CB    1 
ATOM   8276 C  CG    . LYS B 1 490 ? 45.279  100.739 115.325 1.00 98.46  ? 517 LYS B CG    1 
ATOM   8277 C  CD    . LYS B 1 490 ? 46.117  100.956 116.574 1.00 93.39  ? 517 LYS B CD    1 
ATOM   8278 C  CE    . LYS B 1 490 ? 45.350  100.543 117.820 1.00 92.41  ? 517 LYS B CE    1 
ATOM   8279 N  NZ    . LYS B 1 490 ? 46.184  100.619 119.052 1.00 114.55 ? 517 LYS B NZ    1 
ATOM   8280 N  N     . MET B 1 491 ? 44.896  99.821  110.761 1.00 95.90  ? 518 MET B N     1 
ATOM   8281 C  CA    . MET B 1 491 ? 45.130  98.716  109.842 1.00 88.84  ? 518 MET B CA    1 
ATOM   8282 C  C     . MET B 1 491 ? 46.567  98.717  109.335 1.00 88.19  ? 518 MET B C     1 
ATOM   8283 O  O     . MET B 1 491 ? 47.082  99.737  108.873 1.00 97.52  ? 518 MET B O     1 
ATOM   8284 C  CB    . MET B 1 491 ? 44.148  98.804  108.674 1.00 99.08  ? 518 MET B CB    1 
ATOM   8285 C  CG    . MET B 1 491 ? 44.259  97.669  107.670 1.00 95.81  ? 518 MET B CG    1 
ATOM   8286 S  SD    . MET B 1 491 ? 43.840  96.049  108.342 1.00 101.40 ? 518 MET B SD    1 
ATOM   8287 C  CE    . MET B 1 491 ? 42.195  96.352  108.973 1.00 96.03  ? 518 MET B CE    1 
ATOM   8288 N  N     . LEU B 1 492 ? 47.212  97.558  109.445 1.00 84.02  ? 519 LEU B N     1 
ATOM   8289 C  CA    . LEU B 1 492 ? 48.601  97.327  109.105 1.00 84.71  ? 519 LEU B CA    1 
ATOM   8290 C  C     . LEU B 1 492 ? 48.654  95.906  108.567 1.00 84.76  ? 519 LEU B C     1 
ATOM   8291 O  O     . LEU B 1 492 ? 47.878  95.056  109.028 1.00 85.38  ? 519 LEU B O     1 
ATOM   8292 C  CB    . LEU B 1 492 ? 49.514  97.473  110.326 1.00 90.59  ? 519 LEU B CB    1 
ATOM   8293 C  CG    . LEU B 1 492 ? 51.030  97.551  110.160 1.00 90.99  ? 519 LEU B CG    1 
ATOM   8294 C  CD1   . LEU B 1 492 ? 51.439  98.927  109.673 1.00 101.06 ? 519 LEU B CD1   1 
ATOM   8295 C  CD2   . LEU B 1 492 ? 51.728  97.210  111.465 1.00 90.71  ? 519 LEU B CD2   1 
ATOM   8296 N  N     . PRO B 1 493 ? 49.518  95.620  107.593 1.00 94.09  ? 520 PRO B N     1 
ATOM   8297 C  CA    . PRO B 1 493 ? 49.598  94.253  107.062 1.00 87.17  ? 520 PRO B CA    1 
ATOM   8298 C  C     . PRO B 1 493 ? 49.800  93.240  108.179 1.00 81.67  ? 520 PRO B C     1 
ATOM   8299 O  O     . PRO B 1 493 ? 50.585  93.458  109.105 1.00 85.82  ? 520 PRO B O     1 
ATOM   8300 C  CB    . PRO B 1 493 ? 50.805  94.312  106.123 1.00 83.64  ? 520 PRO B CB    1 
ATOM   8301 C  CG    . PRO B 1 493 ? 50.840  95.733  105.684 1.00 91.97  ? 520 PRO B CG    1 
ATOM   8302 C  CD    . PRO B 1 493 ? 50.401  96.547  106.861 1.00 92.53  ? 520 PRO B CD    1 
ATOM   8303 N  N     . VAL B 1 494 ? 49.064  92.130  108.091 1.00 70.35  ? 521 VAL B N     1 
ATOM   8304 C  CA    . VAL B 1 494 ? 49.019  91.170  109.191 1.00 69.09  ? 521 VAL B CA    1 
ATOM   8305 C  C     . VAL B 1 494 ? 50.411  90.632  109.496 1.00 83.03  ? 521 VAL B C     1 
ATOM   8306 O  O     . VAL B 1 494 ? 50.773  90.429  110.663 1.00 92.04  ? 521 VAL B O     1 
ATOM   8307 C  CB    . VAL B 1 494 ? 48.022  90.039  108.869 1.00 79.66  ? 521 VAL B CB    1 
ATOM   8308 C  CG1   . VAL B 1 494 ? 48.349  89.396  107.529 1.00 80.21  ? 521 VAL B CG1   1 
ATOM   8309 C  CG2   . VAL B 1 494 ? 48.016  89.006  109.981 1.00 77.06  ? 521 VAL B CG2   1 
ATOM   8310 N  N     . ASP B 1 495 ? 51.223  90.415  108.460 1.00 83.86  ? 522 ASP B N     1 
ATOM   8311 C  CA    . ASP B 1 495 ? 52.596  89.972  108.663 1.00 89.99  ? 522 ASP B CA    1 
ATOM   8312 C  C     . ASP B 1 495 ? 53.473  91.049  109.292 1.00 96.65  ? 522 ASP B C     1 
ATOM   8313 O  O     . ASP B 1 495 ? 54.610  90.749  109.671 1.00 106.26 ? 522 ASP B O     1 
ATOM   8314 C  CB    . ASP B 1 495 ? 53.203  89.511  107.336 1.00 86.41  ? 522 ASP B CB    1 
ATOM   8315 C  CG    . ASP B 1 495 ? 53.244  90.616  106.301 1.00 105.42 ? 522 ASP B CG    1 
ATOM   8316 O  OD1   . ASP B 1 495 ? 52.454  91.573  106.425 1.00 123.80 ? 522 ASP B OD1   1 
ATOM   8317 O  OD2   . ASP B 1 495 ? 54.063  90.531  105.364 1.00 117.44 ? 522 ASP B OD2   1 
ATOM   8318 N  N     . GLU B 1 496 ? 52.984  92.286  109.393 1.00 98.70  ? 523 GLU B N     1 
ATOM   8319 C  CA    . GLU B 1 496 ? 53.639  93.332  110.170 1.00 96.96  ? 523 GLU B CA    1 
ATOM   8320 C  C     . GLU B 1 496 ? 52.930  93.625  111.482 1.00 92.78  ? 523 GLU B C     1 
ATOM   8321 O  O     . GLU B 1 496 ? 53.575  94.070  112.437 1.00 86.23  ? 523 GLU B O     1 
ATOM   8322 C  CB    . GLU B 1 496 ? 53.733  94.633  109.363 1.00 98.69  ? 523 GLU B CB    1 
ATOM   8323 C  CG    . GLU B 1 496 ? 54.626  94.558  108.139 1.00 101.07 ? 523 GLU B CG    1 
ATOM   8324 C  CD    . GLU B 1 496 ? 54.777  95.899  107.449 1.00 98.19  ? 523 GLU B CD    1 
ATOM   8325 O  OE1   . GLU B 1 496 ? 54.587  96.939  108.113 1.00 116.84 ? 523 GLU B OE1   1 
ATOM   8326 O  OE2   . GLU B 1 496 ? 55.082  95.913  106.239 1.00 99.20  ? 523 GLU B OE2   1 
ATOM   8327 N  N     . PHE B 1 497 ? 51.618  93.383  111.548 1.00 87.22  ? 524 PHE B N     1 
ATOM   8328 C  CA    . PHE B 1 497 ? 50.878  93.604  112.785 1.00 80.82  ? 524 PHE B CA    1 
ATOM   8329 C  C     . PHE B 1 497 ? 51.345  92.662  113.887 1.00 84.84  ? 524 PHE B C     1 
ATOM   8330 O  O     . PHE B 1 497 ? 51.449  93.065  115.051 1.00 89.40  ? 524 PHE B O     1 
ATOM   8331 C  CB    . PHE B 1 497 ? 49.379  93.439  112.536 1.00 75.05  ? 524 PHE B CB    1 
ATOM   8332 C  CG    . PHE B 1 497 ? 48.566  93.297  113.791 1.00 76.91  ? 524 PHE B CG    1 
ATOM   8333 C  CD1   . PHE B 1 497 ? 48.446  94.354  114.679 1.00 81.45  ? 524 PHE B CD1   1 
ATOM   8334 C  CD2   . PHE B 1 497 ? 47.915  92.109  114.079 1.00 81.35  ? 524 PHE B CD2   1 
ATOM   8335 C  CE1   . PHE B 1 497 ? 47.698  94.226  115.833 1.00 78.45  ? 524 PHE B CE1   1 
ATOM   8336 C  CE2   . PHE B 1 497 ? 47.164  91.975  115.231 1.00 74.94  ? 524 PHE B CE2   1 
ATOM   8337 C  CZ    . PHE B 1 497 ? 47.056  93.036  116.109 1.00 82.54  ? 524 PHE B CZ    1 
ATOM   8338 N  N     . LEU B 1 498 ? 51.627  91.405  113.546 1.00 82.80  ? 525 LEU B N     1 
ATOM   8339 C  CA    . LEU B 1 498 ? 52.132  90.475  114.554 1.00 87.97  ? 525 LEU B CA    1 
ATOM   8340 C  C     . LEU B 1 498 ? 53.504  90.883  115.076 1.00 91.66  ? 525 LEU B C     1 
ATOM   8341 O  O     . LEU B 1 498 ? 53.675  90.936  116.306 1.00 88.54  ? 525 LEU B O     1 
ATOM   8342 C  CB    . LEU B 1 498 ? 52.131  89.046  113.997 1.00 73.12  ? 525 LEU B CB    1 
ATOM   8343 C  CG    . LEU B 1 498 ? 50.796  88.526  113.460 1.00 75.09  ? 525 LEU B CG    1 
ATOM   8344 C  CD1   . LEU B 1 498 ? 50.908  87.064  113.051 1.00 71.52  ? 525 LEU B CD1   1 
ATOM   8345 C  CD2   . LEU B 1 498 ? 49.689  88.720  114.484 1.00 70.35  ? 525 LEU B CD2   1 
ATOM   8346 N  N     . PRO B 1 499 ? 54.506  91.190  114.238 1.00 90.71  ? 526 PRO B N     1 
ATOM   8347 C  CA    . PRO B 1 499 ? 55.784  91.674  114.791 1.00 94.22  ? 526 PRO B CA    1 
ATOM   8348 C  C     . PRO B 1 499 ? 55.652  92.936  115.621 1.00 96.72  ? 526 PRO B C     1 
ATOM   8349 O  O     . PRO B 1 499 ? 56.467  93.158  116.526 1.00 93.97  ? 526 PRO B O     1 
ATOM   8350 C  CB    . PRO B 1 499 ? 56.639  91.905  113.539 1.00 93.36  ? 526 PRO B CB    1 
ATOM   8351 C  CG    . PRO B 1 499 ? 56.094  90.961  112.546 1.00 91.06  ? 526 PRO B CG    1 
ATOM   8352 C  CD    . PRO B 1 499 ? 54.613  90.954  112.786 1.00 91.08  ? 526 PRO B CD    1 
ATOM   8353 N  N     . VAL B 1 500 ? 54.656  93.778  115.340 1.00 88.38  ? 527 VAL B N     1 
ATOM   8354 C  CA    . VAL B 1 500 ? 54.382  94.904  116.224 1.00 94.58  ? 527 VAL B CA    1 
ATOM   8355 C  C     . VAL B 1 500 ? 53.901  94.405  117.580 1.00 93.85  ? 527 VAL B C     1 
ATOM   8356 O  O     . VAL B 1 500 ? 54.305  94.925  118.627 1.00 86.72  ? 527 VAL B O     1 
ATOM   8357 C  CB    . VAL B 1 500 ? 53.364  95.862  115.575 1.00 96.91  ? 527 VAL B CB    1 
ATOM   8358 C  CG1   . VAL B 1 500 ? 52.853  96.868  116.595 1.00 90.02  ? 527 VAL B CG1   1 
ATOM   8359 C  CG2   . VAL B 1 500 ? 53.992  96.585  114.393 1.00 94.99  ? 527 VAL B CG2   1 
ATOM   8360 N  N     . MET B 1 501 ? 53.060  93.367  117.586 1.00 93.30  ? 528 MET B N     1 
ATOM   8361 C  CA    . MET B 1 501 ? 52.452  92.912  118.832 1.00 88.94  ? 528 MET B CA    1 
ATOM   8362 C  C     . MET B 1 501 ? 53.430  92.172  119.738 1.00 97.60  ? 528 MET B C     1 
ATOM   8363 O  O     . MET B 1 501 ? 53.243  92.182  120.959 1.00 98.18  ? 528 MET B O     1 
ATOM   8364 C  CB    . MET B 1 501 ? 51.235  92.035  118.536 1.00 85.87  ? 528 MET B CB    1 
ATOM   8365 C  CG    . MET B 1 501 ? 50.025  92.828  118.063 1.00 87.43  ? 528 MET B CG    1 
ATOM   8366 S  SD    . MET B 1 501 ? 49.592  94.177  119.180 1.00 91.92  ? 528 MET B SD    1 
ATOM   8367 C  CE    . MET B 1 501 ? 48.968  93.270  120.593 1.00 82.87  ? 528 MET B CE    1 
ATOM   8368 N  N     . PHE B 1 502 ? 54.466  91.528  119.194 1.00 101.92 ? 529 PHE B N     1 
ATOM   8369 C  CA    . PHE B 1 502 ? 55.546  91.041  120.045 1.00 104.38 ? 529 PHE B CA    1 
ATOM   8370 C  C     . PHE B 1 502 ? 56.774  91.946  119.990 1.00 106.60 ? 529 PHE B C     1 
ATOM   8371 O  O     . PHE B 1 502 ? 57.885  91.497  120.294 1.00 109.58 ? 529 PHE B O     1 
ATOM   8372 C  CB    . PHE B 1 502 ? 55.907  89.580  119.735 1.00 102.47 ? 529 PHE B CB    1 
ATOM   8373 C  CG    . PHE B 1 502 ? 56.299  89.298  118.307 1.00 104.80 ? 529 PHE B CG    1 
ATOM   8374 C  CD1   . PHE B 1 502 ? 57.605  89.473  117.879 1.00 104.35 ? 529 PHE B CD1   1 
ATOM   8375 C  CD2   . PHE B 1 502 ? 55.376  88.777  117.417 1.00 103.23 ? 529 PHE B CD2   1 
ATOM   8376 C  CE1   . PHE B 1 502 ? 57.970  89.181  116.574 1.00 102.72 ? 529 PHE B CE1   1 
ATOM   8377 C  CE2   . PHE B 1 502 ? 55.733  88.478  116.114 1.00 91.52  ? 529 PHE B CE2   1 
ATOM   8378 C  CZ    . PHE B 1 502 ? 57.033  88.679  115.692 1.00 93.60  ? 529 PHE B CZ    1 
ATOM   8379 N  N     . ASP B 1 503 ? 56.581  93.215  119.615 1.00 104.70 ? 530 ASP B N     1 
ATOM   8380 C  CA    . ASP B 1 503 ? 57.535  94.299  119.866 1.00 105.82 ? 530 ASP B CA    1 
ATOM   8381 C  C     . ASP B 1 503 ? 58.912  94.011  119.267 1.00 106.59 ? 530 ASP B C     1 
ATOM   8382 O  O     . ASP B 1 503 ? 59.948  94.193  119.911 1.00 106.99 ? 530 ASP B O     1 
ATOM   8383 C  CB    . ASP B 1 503 ? 57.640  94.590  121.366 1.00 109.41 ? 530 ASP B CB    1 
ATOM   8384 C  CG    . ASP B 1 503 ? 58.220  95.963  121.655 1.00 106.37 ? 530 ASP B CG    1 
ATOM   8385 O  OD1   . ASP B 1 503 ? 58.463  96.726  120.695 1.00 123.54 ? 530 ASP B OD1   1 
ATOM   8386 O  OD2   . ASP B 1 503 ? 58.435  96.281  122.843 1.00 117.93 ? 530 ASP B OD2   1 
ATOM   8387 N  N     . LYS B 1 504 ? 58.919  93.565  118.013 1.00 107.50 ? 531 LYS B N     1 
ATOM   8388 C  CA    . LYS B 1 504 ? 60.151  93.383  117.263 1.00 89.12  ? 531 LYS B CA    1 
ATOM   8389 C  C     . LYS B 1 504 ? 60.142  94.137  115.942 1.00 99.08  ? 531 LYS B C     1 
ATOM   8390 O  O     . LYS B 1 504 ? 61.120  94.051  115.188 1.00 102.66 ? 531 LYS B O     1 
ATOM   8391 C  CB    . LYS B 1 504 ? 60.413  91.891  117.007 1.00 98.33  ? 531 LYS B CB    1 
ATOM   8392 C  CG    . LYS B 1 504 ? 60.661  91.063  118.264 1.00 108.77 ? 531 LYS B CG    1 
ATOM   8393 C  CD    . LYS B 1 504 ? 61.980  91.414  118.935 1.00 100.69 ? 531 LYS B CD    1 
ATOM   8394 C  CE    . LYS B 1 504 ? 62.299  90.435  120.056 1.00 93.48  ? 531 LYS B CE    1 
ATOM   8395 N  NZ    . LYS B 1 504 ? 62.415  89.040  119.546 1.00 109.70 ? 531 LYS B NZ    1 
ATOM   8396 N  N     . HIS B 1 505 ? 59.072  94.869  115.642 1.00 99.49  ? 532 HIS B N     1 
ATOM   8397 C  CA    . HIS B 1 505 ? 59.017  95.646  114.415 1.00 101.81 ? 532 HIS B CA    1 
ATOM   8398 C  C     . HIS B 1 505 ? 60.050  96.769  114.465 1.00 104.12 ? 532 HIS B C     1 
ATOM   8399 O  O     . HIS B 1 505 ? 60.224  97.408  115.507 1.00 98.49  ? 532 HIS B O     1 
ATOM   8400 C  CB    . HIS B 1 505 ? 57.618  96.229  114.213 1.00 98.33  ? 532 HIS B CB    1 
ATOM   8401 C  CG    . HIS B 1 505 ? 57.325  96.629  112.800 1.00 100.15 ? 532 HIS B CG    1 
ATOM   8402 N  ND1   . HIS B 1 505 ? 57.718  97.839  112.271 1.00 102.76 ? 532 HIS B ND1   1 
ATOM   8403 C  CD2   . HIS B 1 505 ? 56.672  95.980  111.807 1.00 91.12  ? 532 HIS B CD2   1 
ATOM   8404 C  CE1   . HIS B 1 505 ? 57.325  97.916  111.012 1.00 107.02 ? 532 HIS B CE1   1 
ATOM   8405 N  NE2   . HIS B 1 505 ? 56.687  96.801  110.706 1.00 100.65 ? 532 HIS B NE2   1 
ATOM   8406 N  N     . PRO B 1 506 ? 60.756  97.029  113.362 1.00 111.73 ? 533 PRO B N     1 
ATOM   8407 C  CA    . PRO B 1 506 ? 61.797  98.069  113.405 1.00 110.49 ? 533 PRO B CA    1 
ATOM   8408 C  C     . PRO B 1 506 ? 61.241  99.473  113.568 1.00 106.60 ? 533 PRO B C     1 
ATOM   8409 O  O     . PRO B 1 506 ? 61.778  100.255 114.363 1.00 119.95 ? 533 PRO B O     1 
ATOM   8410 C  CB    . PRO B 1 506 ? 62.521  97.890  112.062 1.00 107.38 ? 533 PRO B CB    1 
ATOM   8411 C  CG    . PRO B 1 506 ? 61.502  97.260  111.170 1.00 97.80  ? 533 PRO B CG    1 
ATOM   8412 C  CD    . PRO B 1 506 ? 60.691  96.359  112.052 1.00 98.22  ? 533 PRO B CD    1 
ATOM   8413 N  N     . VAL B 1 507 ? 60.179  99.815  112.840 1.00 103.32 ? 534 VAL B N     1 
ATOM   8414 C  CA    . VAL B 1 507 ? 59.608  101.156 112.896 1.00 105.89 ? 534 VAL B CA    1 
ATOM   8415 C  C     . VAL B 1 507 ? 58.956  101.375 114.254 1.00 118.08 ? 534 VAL B C     1 
ATOM   8416 O  O     . VAL B 1 507 ? 57.841  100.902 114.504 1.00 110.30 ? 534 VAL B O     1 
ATOM   8417 C  CB    . VAL B 1 507 ? 58.598  101.382 111.758 1.00 104.17 ? 534 VAL B CB    1 
ATOM   8418 C  CG1   . VAL B 1 507 ? 58.106  102.822 111.770 1.00 118.97 ? 534 VAL B CG1   1 
ATOM   8419 C  CG2   . VAL B 1 507 ? 59.222  101.038 110.415 1.00 107.00 ? 534 VAL B CG2   1 
ATOM   8420 N  N     . SER B 1 508 ? 59.649  102.095 115.141 1.00 123.62 ? 535 SER B N     1 
ATOM   8421 C  CA    . SER B 1 508 ? 59.098  102.389 116.458 1.00 127.04 ? 535 SER B CA    1 
ATOM   8422 C  C     . SER B 1 508 ? 57.870  103.286 116.380 1.00 123.53 ? 535 SER B C     1 
ATOM   8423 O  O     . SER B 1 508 ? 57.049  103.275 117.305 1.00 121.88 ? 535 SER B O     1 
ATOM   8424 C  CB    . SER B 1 508 ? 60.164  103.037 117.344 1.00 128.55 ? 535 SER B CB    1 
ATOM   8425 O  OG    . SER B 1 508 ? 61.273  102.173 117.527 1.00 139.92 ? 535 SER B OG    1 
ATOM   8426 N  N     . GLU B 1 509 ? 57.725  104.061 115.302 1.00 122.68 ? 536 GLU B N     1 
ATOM   8427 C  CA    . GLU B 1 509 ? 56.539  104.897 115.150 1.00 123.54 ? 536 GLU B CA    1 
ATOM   8428 C  C     . GLU B 1 509 ? 55.290  104.048 114.946 1.00 117.95 ? 536 GLU B C     1 
ATOM   8429 O  O     . GLU B 1 509 ? 54.208  104.400 115.432 1.00 123.07 ? 536 GLU B O     1 
ATOM   8430 C  CB    . GLU B 1 509 ? 56.723  105.870 113.987 1.00 132.45 ? 536 GLU B CB    1 
ATOM   8431 C  CG    . GLU B 1 509 ? 55.528  106.782 113.758 1.00 139.20 ? 536 GLU B CG    1 
ATOM   8432 C  CD    . GLU B 1 509 ? 55.793  107.844 112.713 1.00 153.28 ? 536 GLU B CD    1 
ATOM   8433 O  OE1   . GLU B 1 509 ? 56.803  107.728 111.987 1.00 165.46 ? 536 GLU B OE1   1 
ATOM   8434 O  OE2   . GLU B 1 509 ? 54.992  108.798 112.621 1.00 154.91 ? 536 GLU B OE2   1 
ATOM   8435 N  N     . TYR B 1 510 ? 55.415  102.930 114.227 1.00 120.26 ? 537 TYR B N     1 
ATOM   8436 C  CA    . TYR B 1 510 ? 54.279  102.029 114.061 1.00 114.92 ? 537 TYR B CA    1 
ATOM   8437 C  C     . TYR B 1 510 ? 53.857  101.437 115.399 1.00 111.59 ? 537 TYR B C     1 
ATOM   8438 O  O     . TYR B 1 510 ? 52.671  101.441 115.749 1.00 115.21 ? 537 TYR B O     1 
ATOM   8439 C  CB    . TYR B 1 510 ? 54.622  100.913 113.070 1.00 114.43 ? 537 TYR B CB    1 
ATOM   8440 C  CG    . TYR B 1 510 ? 54.801  101.358 111.633 1.00 117.23 ? 537 TYR B CG    1 
ATOM   8441 C  CD1   . TYR B 1 510 ? 54.590  102.678 111.256 1.00 112.32 ? 537 TYR B CD1   1 
ATOM   8442 C  CD2   . TYR B 1 510 ? 55.171  100.448 110.651 1.00 103.57 ? 537 TYR B CD2   1 
ATOM   8443 C  CE1   . TYR B 1 510 ? 54.753  103.080 109.943 1.00 116.00 ? 537 TYR B CE1   1 
ATOM   8444 C  CE2   . TYR B 1 510 ? 55.336  100.840 109.338 1.00 100.16 ? 537 TYR B CE2   1 
ATOM   8445 C  CZ    . TYR B 1 510 ? 55.125  102.156 108.988 1.00 109.68 ? 537 TYR B CZ    1 
ATOM   8446 O  OH    . TYR B 1 510 ? 55.288  102.550 107.681 1.00 108.63 ? 537 TYR B OH    1 
ATOM   8447 N  N     . LYS B 1 511 ? 54.824  100.926 116.167 1.00 110.52 ? 538 LYS B N     1 
ATOM   8448 C  CA    . LYS B 1 511 ? 54.522  100.352 117.473 1.00 108.85 ? 538 LYS B CA    1 
ATOM   8449 C  C     . LYS B 1 511 ? 54.007  101.394 118.456 1.00 107.66 ? 538 LYS B C     1 
ATOM   8450 O  O     . LYS B 1 511 ? 53.377  101.029 119.454 1.00 106.93 ? 538 LYS B O     1 
ATOM   8451 C  CB    . LYS B 1 511 ? 55.764  99.666  118.045 1.00 103.66 ? 538 LYS B CB    1 
ATOM   8452 C  CG    . LYS B 1 511 ? 56.284  98.516  117.198 1.00 115.03 ? 538 LYS B CG    1 
ATOM   8453 C  CD    . LYS B 1 511 ? 57.555  97.921  117.783 1.00 111.30 ? 538 LYS B CD    1 
ATOM   8454 C  CE    . LYS B 1 511 ? 58.664  98.957  117.862 1.00 102.33 ? 538 LYS B CE    1 
ATOM   8455 N  NZ    . LYS B 1 511 ? 59.964  98.345  118.254 1.00 103.44 ? 538 LYS B NZ    1 
ATOM   8456 N  N     . ALA B 1 512 ? 54.261  102.680 118.198 1.00 112.35 ? 539 ALA B N     1 
ATOM   8457 C  CA    . ALA B 1 512 ? 53.761  103.725 119.085 1.00 112.38 ? 539 ALA B CA    1 
ATOM   8458 C  C     . ALA B 1 512 ? 52.240  103.810 119.055 1.00 113.94 ? 539 ALA B C     1 
ATOM   8459 O  O     . ALA B 1 512 ? 51.624  104.198 120.054 1.00 106.49 ? 539 ALA B O     1 
ATOM   8460 C  CB    . ALA B 1 512 ? 54.378  105.073 118.709 1.00 109.86 ? 539 ALA B CB    1 
ATOM   8461 N  N     . HIS B 1 513 ? 51.619  103.452 117.929 1.00 117.19 ? 540 HIS B N     1 
ATOM   8462 C  CA    . HIS B 1 513 ? 50.164  103.457 117.838 1.00 111.09 ? 540 HIS B CA    1 
ATOM   8463 C  C     . HIS B 1 513 ? 49.520  102.322 118.624 1.00 105.86 ? 540 HIS B C     1 
ATOM   8464 O  O     . HIS B 1 513 ? 48.308  102.366 118.859 1.00 102.68 ? 540 HIS B O     1 
ATOM   8465 C  CB    . HIS B 1 513 ? 49.725  103.381 116.373 1.00 116.65 ? 540 HIS B CB    1 
ATOM   8466 C  CG    . HIS B 1 513 ? 50.166  104.550 115.546 1.00 118.68 ? 540 HIS B CG    1 
ATOM   8467 N  ND1   . HIS B 1 513 ? 51.333  104.546 114.813 1.00 127.41 ? 540 HIS B ND1   1 
ATOM   8468 C  CD2   . HIS B 1 513 ? 49.595  105.760 115.337 1.00 104.91 ? 540 HIS B CD2   1 
ATOM   8469 C  CE1   . HIS B 1 513 ? 51.462  105.702 114.187 1.00 125.18 ? 540 HIS B CE1   1 
ATOM   8470 N  NE2   . HIS B 1 513 ? 50.421  106.457 114.489 1.00 108.00 ? 540 HIS B NE2   1 
ATOM   8471 N  N     . PHE B 1 514 ? 50.291  101.317 119.032 1.00 104.10 ? 541 PHE B N     1 
ATOM   8472 C  CA    . PHE B 1 514 ? 49.784  100.173 119.784 1.00 105.67 ? 541 PHE B CA    1 
ATOM   8473 C  C     . PHE B 1 514 ? 50.374  100.227 121.188 1.00 114.19 ? 541 PHE B C     1 
ATOM   8474 O  O     . PHE B 1 514 ? 51.581  100.036 121.366 1.00 115.50 ? 541 PHE B O     1 
ATOM   8475 C  CB    . PHE B 1 514 ? 50.137  98.862  119.086 1.00 91.96  ? 541 PHE B CB    1 
ATOM   8476 C  CG    . PHE B 1 514 ? 49.524  98.717  117.722 1.00 89.89  ? 541 PHE B CG    1 
ATOM   8477 C  CD1   . PHE B 1 514 ? 50.125  99.287  116.613 1.00 92.77  ? 541 PHE B CD1   1 
ATOM   8478 C  CD2   . PHE B 1 514 ? 48.348  98.006  117.549 1.00 98.16  ? 541 PHE B CD2   1 
ATOM   8479 C  CE1   . PHE B 1 514 ? 49.564  99.155  115.358 1.00 96.45  ? 541 PHE B CE1   1 
ATOM   8480 C  CE2   . PHE B 1 514 ? 47.781  97.869  116.294 1.00 90.31  ? 541 PHE B CE2   1 
ATOM   8481 C  CZ    . PHE B 1 514 ? 48.390  98.446  115.198 1.00 92.06  ? 541 PHE B CZ    1 
ATOM   8482 N  N     . SER B 1 515 ? 49.520  100.479 122.182 1.00 127.91 ? 542 SER B N     1 
ATOM   8483 C  CA    . SER B 1 515 ? 49.998  100.655 123.550 1.00 137.71 ? 542 SER B CA    1 
ATOM   8484 C  C     . SER B 1 515 ? 50.560  99.354  124.113 1.00 132.14 ? 542 SER B C     1 
ATOM   8485 O  O     . SER B 1 515 ? 51.746  99.271  124.454 1.00 132.09 ? 542 SER B O     1 
ATOM   8486 C  CB    . SER B 1 515 ? 48.867  101.186 124.434 1.00 122.17 ? 542 SER B CB    1 
ATOM   8487 O  OG    . SER B 1 515 ? 47.717  100.364 124.339 1.00 130.15 ? 542 SER B OG    1 
ATOM   8488 N  N     . LEU B 1 516 ? 49.725  98.324  124.215 1.00 115.15 ? 543 LEU B N     1 
ATOM   8489 C  CA    . LEU B 1 516 ? 50.110  97.059  124.826 1.00 105.34 ? 543 LEU B CA    1 
ATOM   8490 C  C     . LEU B 1 516 ? 50.572  96.092  123.742 1.00 107.66 ? 543 LEU B C     1 
ATOM   8491 O  O     . LEU B 1 516 ? 49.798  95.743  122.844 1.00 111.25 ? 543 LEU B O     1 
ATOM   8492 C  CB    . LEU B 1 516 ? 48.947  96.467  125.622 1.00 95.82  ? 543 LEU B CB    1 
ATOM   8493 C  CG    . LEU B 1 516 ? 49.219  95.168  126.381 1.00 104.61 ? 543 LEU B CG    1 
ATOM   8494 C  CD1   . LEU B 1 516 ? 50.508  95.269  127.180 1.00 100.65 ? 543 LEU B CD1   1 
ATOM   8495 C  CD2   . LEU B 1 516 ? 48.050  94.838  127.295 1.00 95.59  ? 543 LEU B CD2   1 
ATOM   8496 N  N     . ARG B 1 517 ? 51.834  95.663  123.831 1.00 104.47 ? 544 ARG B N     1 
ATOM   8497 C  CA    . ARG B 1 517 ? 52.438  94.742  122.868 1.00 100.34 ? 544 ARG B CA    1 
ATOM   8498 C  C     . ARG B 1 517 ? 53.066  93.580  123.647 1.00 99.32  ? 544 ARG B C     1 
ATOM   8499 O  O     . ARG B 1 517 ? 54.289  93.453  123.730 1.00 91.16  ? 544 ARG B O     1 
ATOM   8500 C  CB    . ARG B 1 517 ? 53.471  95.459  121.992 1.00 91.33  ? 544 ARG B CB    1 
ATOM   8501 C  CG    . ARG B 1 517 ? 52.967  96.758  121.374 1.00 108.47 ? 544 ARG B CG    1 
ATOM   8502 C  CD    . ARG B 1 517 ? 54.016  97.418  120.489 1.00 102.59 ? 544 ARG B CD    1 
ATOM   8503 N  NE    . ARG B 1 517 ? 55.227  97.769  121.221 1.00 104.23 ? 544 ARG B NE    1 
ATOM   8504 C  CZ    . ARG B 1 517 ? 55.401  98.910  121.873 1.00 107.80 ? 544 ARG B CZ    1 
ATOM   8505 N  NH1   . ARG B 1 517 ? 54.452  99.830  121.921 1.00 100.98 ? 544 ARG B NH1   1 
ATOM   8506 N  NH2   . ARG B 1 517 ? 56.557  99.135  122.491 1.00 104.24 ? 544 ARG B NH2   1 
ATOM   8507 N  N     . ASN B 1 518 ? 52.215  92.725  124.211 1.00 100.55 ? 545 ASN B N     1 
ATOM   8508 C  CA    . ASN B 1 518 ? 52.637  91.648  125.102 1.00 97.92  ? 545 ASN B CA    1 
ATOM   8509 C  C     . ASN B 1 518 ? 52.413  90.270  124.482 1.00 93.77  ? 545 ASN B C     1 
ATOM   8510 O  O     . ASN B 1 518 ? 51.949  89.341  125.147 1.00 99.93  ? 545 ASN B O     1 
ATOM   8511 C  CB    . ASN B 1 518 ? 51.910  91.753  126.441 1.00 94.39  ? 545 ASN B CB    1 
ATOM   8512 C  CG    . ASN B 1 518 ? 50.403  91.662  126.293 1.00 107.60 ? 545 ASN B CG    1 
ATOM   8513 O  OD1   . ASN B 1 518 ? 49.864  91.831  125.197 1.00 108.95 ? 545 ASN B OD1   1 
ATOM   8514 N  ND2   . ASN B 1 518 ? 49.714  91.396  127.395 1.00 99.49  ? 545 ASN B ND2   1 
ATOM   8515 N  N     . LEU B 1 519 ? 52.750  90.119  123.204 1.00 99.07  ? 546 LEU B N     1 
ATOM   8516 C  CA    . LEU B 1 519 ? 52.543  88.865  122.494 1.00 89.15  ? 546 LEU B CA    1 
ATOM   8517 C  C     . LEU B 1 519 ? 53.726  87.931  122.723 1.00 96.26  ? 546 LEU B C     1 
ATOM   8518 O  O     . LEU B 1 519 ? 54.878  88.307  122.486 1.00 87.57  ? 546 LEU B O     1 
ATOM   8519 C  CB    . LEU B 1 519 ? 52.354  89.122  120.999 1.00 92.21  ? 546 LEU B CB    1 
ATOM   8520 C  CG    . LEU B 1 519 ? 51.760  88.000  120.147 1.00 85.28  ? 546 LEU B CG    1 
ATOM   8521 C  CD1   . LEU B 1 519 ? 50.303  87.775  120.511 1.00 81.75  ? 546 LEU B CD1   1 
ATOM   8522 C  CD2   . LEU B 1 519 ? 51.899  88.318  118.666 1.00 90.36  ? 546 LEU B CD2   1 
ATOM   8523 N  N     . HIS B 1 520 ? 53.438  86.716  123.185 1.00 109.76 ? 547 HIS B N     1 
ATOM   8524 C  CA    . HIS B 1 520 ? 54.458  85.679  123.339 1.00 103.92 ? 547 HIS B CA    1 
ATOM   8525 C  C     . HIS B 1 520 ? 54.565  84.941  122.011 1.00 100.60 ? 547 HIS B C     1 
ATOM   8526 O  O     . HIS B 1 520 ? 53.736  84.084  121.694 1.00 100.59 ? 547 HIS B O     1 
ATOM   8527 C  CB    . HIS B 1 520 ? 54.106  84.724  124.475 1.00 111.33 ? 547 HIS B CB    1 
ATOM   8528 C  CG    . HIS B 1 520 ? 53.822  85.405  125.777 1.00 116.72 ? 547 HIS B CG    1 
ATOM   8529 N  ND1   . HIS B 1 520 ? 52.551  85.506  126.300 1.00 123.36 ? 547 HIS B ND1   1 
ATOM   8530 C  CD2   . HIS B 1 520 ? 54.644  86.011  126.666 1.00 115.18 ? 547 HIS B CD2   1 
ATOM   8531 C  CE1   . HIS B 1 520 ? 52.602  86.147  127.454 1.00 126.66 ? 547 HIS B CE1   1 
ATOM   8532 N  NE2   . HIS B 1 520 ? 53.860  86.465  127.699 1.00 124.14 ? 547 HIS B NE2   1 
ATOM   8533 N  N     . ALA B 1 521 ? 55.585  85.273  121.228 1.00 96.33  ? 548 ALA B N     1 
ATOM   8534 C  CA    . ALA B 1 521 ? 55.761  84.708  119.899 1.00 86.25  ? 548 ALA B CA    1 
ATOM   8535 C  C     . ALA B 1 521 ? 56.989  83.811  119.858 1.00 90.21  ? 548 ALA B C     1 
ATOM   8536 O  O     . ALA B 1 521 ? 58.026  84.127  120.450 1.00 94.40  ? 548 ALA B O     1 
ATOM   8537 C  CB    . ALA B 1 521 ? 55.892  85.805  118.845 1.00 88.35  ? 548 ALA B CB    1 
ATOM   8538 N  N     . PHE B 1 522 ? 56.859  82.691  119.153 1.00 88.36  ? 549 PHE B N     1 
ATOM   8539 C  CA    . PHE B 1 522 ? 57.959  81.768  118.937 1.00 87.83  ? 549 PHE B CA    1 
ATOM   8540 C  C     . PHE B 1 522 ? 57.884  81.258  117.506 1.00 86.29  ? 549 PHE B C     1 
ATOM   8541 O  O     . PHE B 1 522 ? 56.866  81.403  116.826 1.00 84.27  ? 549 PHE B O     1 
ATOM   8542 C  CB    . PHE B 1 522 ? 57.924  80.599  119.932 1.00 85.99  ? 549 PHE B CB    1 
ATOM   8543 C  CG    . PHE B 1 522 ? 57.823  81.031  121.368 1.00 86.13  ? 549 PHE B CG    1 
ATOM   8544 C  CD1   . PHE B 1 522 ? 58.952  81.411  122.074 1.00 87.87  ? 549 PHE B CD1   1 
ATOM   8545 C  CD2   . PHE B 1 522 ? 56.597  81.058  122.012 1.00 86.95  ? 549 PHE B CD2   1 
ATOM   8546 C  CE1   . PHE B 1 522 ? 58.859  81.810  123.395 1.00 86.44  ? 549 PHE B CE1   1 
ATOM   8547 C  CE2   . PHE B 1 522 ? 56.498  81.456  123.333 1.00 93.87  ? 549 PHE B CE2   1 
ATOM   8548 C  CZ    . PHE B 1 522 ? 57.629  81.831  124.024 1.00 82.22  ? 549 PHE B CZ    1 
ATOM   8549 N  N     . SER B 1 523 ? 58.981  80.666  117.049 1.00 91.16  ? 550 SER B N     1 
ATOM   8550 C  CA    . SER B 1 523 ? 59.050  80.086  115.717 1.00 81.41  ? 550 SER B CA    1 
ATOM   8551 C  C     . SER B 1 523 ? 59.614  78.679  115.809 1.00 84.89  ? 550 SER B C     1 
ATOM   8552 O  O     . SER B 1 523 ? 60.529  78.417  116.596 1.00 79.74  ? 550 SER B O     1 
ATOM   8553 C  CB    . SER B 1 523 ? 59.917  80.933  114.775 1.00 79.51  ? 550 SER B CB    1 
ATOM   8554 O  OG    . SER B 1 523 ? 60.099  80.282  113.529 1.00 74.89  ? 550 SER B OG    1 
ATOM   8555 N  N     . VAL B 1 524 ? 59.052  77.771  115.011 1.00 81.24  ? 551 VAL B N     1 
ATOM   8556 C  CA    . VAL B 1 524 ? 59.623  76.439  114.889 1.00 79.29  ? 551 VAL B CA    1 
ATOM   8557 C  C     . VAL B 1 524 ? 60.986  76.547  114.222 1.00 80.29  ? 551 VAL B C     1 
ATOM   8558 O  O     . VAL B 1 524 ? 61.188  77.356  113.305 1.00 80.71  ? 551 VAL B O     1 
ATOM   8559 C  CB    . VAL B 1 524 ? 58.685  75.517  114.091 1.00 87.34  ? 551 VAL B CB    1 
ATOM   8560 C  CG1   . VAL B 1 524 ? 59.193  74.085  114.120 1.00 87.62  ? 551 VAL B CG1   1 
ATOM   8561 C  CG2   . VAL B 1 524 ? 57.270  75.595  114.637 1.00 84.30  ? 551 VAL B CG2   1 
ATOM   8562 N  N     . GLU B 1 525 ? 61.937  75.744  114.688 1.00 92.98  ? 552 GLU B N     1 
ATOM   8563 C  CA    . GLU B 1 525 ? 63.272  75.779  114.108 1.00 94.24  ? 552 GLU B CA    1 
ATOM   8564 C  C     . GLU B 1 525 ? 63.789  74.365  113.867 1.00 93.57  ? 552 GLU B C     1 
ATOM   8565 O  O     . GLU B 1 525 ? 63.976  73.598  114.820 1.00 88.93  ? 552 GLU B O     1 
ATOM   8566 C  CB    . GLU B 1 525 ? 64.229  76.559  115.010 1.00 82.79  ? 552 GLU B CB    1 
ATOM   8567 C  CG    . GLU B 1 525 ? 65.656  76.625  114.486 1.00 93.88  ? 552 GLU B CG    1 
ATOM   8568 C  CD    . GLU B 1 525 ? 65.760  77.281  113.118 1.00 107.66 ? 552 GLU B CD    1 
ATOM   8569 O  OE1   . GLU B 1 525 ? 64.873  78.087  112.762 1.00 106.36 ? 552 GLU B OE1   1 
ATOM   8570 O  OE2   . GLU B 1 525 ? 66.736  76.985  112.395 1.00 111.90 ? 552 GLU B OE2   1 
ATOM   8571 N  N     . PRO B 1 526 ? 64.039  73.984  112.608 1.00 86.65  ? 553 PRO B N     1 
ATOM   8572 C  CA    . PRO B 1 526 ? 63.892  74.786  111.387 1.00 79.55  ? 553 PRO B CA    1 
ATOM   8573 C  C     . PRO B 1 526 ? 62.435  74.903  110.954 1.00 77.19  ? 553 PRO B C     1 
ATOM   8574 O  O     . PRO B 1 526 ? 61.568  74.223  111.497 1.00 73.77  ? 553 PRO B O     1 
ATOM   8575 C  CB    . PRO B 1 526 ? 64.733  74.007  110.372 1.00 72.15  ? 553 PRO B CB    1 
ATOM   8576 C  CG    . PRO B 1 526 ? 64.560  72.576  110.798 1.00 73.20  ? 553 PRO B CG    1 
ATOM   8577 C  CD    . PRO B 1 526 ? 64.506  72.617  112.310 1.00 88.87  ? 553 PRO B CD    1 
ATOM   8578 N  N     . LEU B 1 527 ? 62.142  75.763  109.982 1.00 66.04  ? 554 LEU B N     1 
ATOM   8579 C  CA    . LEU B 1 527 ? 60.767  75.958  109.548 1.00 65.12  ? 554 LEU B CA    1 
ATOM   8580 C  C     . LEU B 1 527 ? 60.219  74.687  108.913 1.00 66.08  ? 554 LEU B C     1 
ATOM   8581 O  O     . LEU B 1 527 ? 60.916  73.989  108.172 1.00 76.58  ? 554 LEU B O     1 
ATOM   8582 C  CB    . LEU B 1 527 ? 60.687  77.121  108.559 1.00 62.32  ? 554 LEU B CB    1 
ATOM   8583 C  CG    . LEU B 1 527 ? 61.021  78.495  109.138 1.00 77.36  ? 554 LEU B CG    1 
ATOM   8584 C  CD1   . LEU B 1 527 ? 61.100  79.545  108.041 1.00 83.28  ? 554 LEU B CD1   1 
ATOM   8585 C  CD2   . LEU B 1 527 ? 59.997  78.892  110.193 1.00 78.36  ? 554 LEU B CD2   1 
ATOM   8586 N  N     . LEU B 1 528 ? 58.958  74.387  109.216 1.00 59.86  ? 555 LEU B N     1 
ATOM   8587 C  CA    . LEU B 1 528 ? 58.288  73.212  108.679 1.00 64.28  ? 555 LEU B CA    1 
ATOM   8588 C  C     . LEU B 1 528 ? 57.466  73.513  107.434 1.00 66.75  ? 555 LEU B C     1 
ATOM   8589 O  O     . LEU B 1 528 ? 57.023  72.576  106.763 1.00 63.07  ? 555 LEU B O     1 
ATOM   8590 C  CB    . LEU B 1 528 ? 57.381  72.584  109.744 1.00 60.98  ? 555 LEU B CB    1 
ATOM   8591 C  CG    . LEU B 1 528 ? 58.078  72.136  111.030 1.00 65.73  ? 555 LEU B CG    1 
ATOM   8592 C  CD1   . LEU B 1 528 ? 57.083  71.500  111.987 1.00 62.67  ? 555 LEU B CD1   1 
ATOM   8593 C  CD2   . LEU B 1 528 ? 59.219  71.180  110.714 1.00 59.50  ? 555 LEU B CD2   1 
ATOM   8594 N  N     . ILE B 1 529 ? 57.254  74.785  107.110 1.00 63.97  ? 556 ILE B N     1 
ATOM   8595 C  CA    . ILE B 1 529 ? 56.453  75.178  105.958 1.00 63.37  ? 556 ILE B CA    1 
ATOM   8596 C  C     . ILE B 1 529 ? 57.142  76.330  105.241 1.00 66.01  ? 556 ILE B C     1 
ATOM   8597 O  O     . ILE B 1 529 ? 57.612  77.280  105.875 1.00 64.69  ? 556 ILE B O     1 
ATOM   8598 C  CB    . ILE B 1 529 ? 55.017  75.559  106.375 1.00 61.04  ? 556 ILE B CB    1 
ATOM   8599 C  CG1   . ILE B 1 529 ? 54.192  74.292  106.598 1.00 67.73  ? 556 ILE B CG1   1 
ATOM   8600 C  CG2   . ILE B 1 529 ? 54.368  76.471  105.337 1.00 57.60  ? 556 ILE B CG2   1 
ATOM   8601 C  CD1   . ILE B 1 529 ? 52.714  74.527  106.582 1.00 71.15  ? 556 ILE B CD1   1 
ATOM   8602 N  N     . TYR B 1 530 ? 57.201  76.241  103.921 1.00 60.26  ? 557 TYR B N     1 
ATOM   8603 C  CA    . TYR B 1 530 ? 57.810  77.239  103.058 1.00 68.52  ? 557 TYR B CA    1 
ATOM   8604 C  C     . TYR B 1 530 ? 56.832  77.591  101.950 1.00 70.43  ? 557 TYR B C     1 
ATOM   8605 O  O     . TYR B 1 530 ? 55.892  76.835  101.684 1.00 59.07  ? 557 TYR B O     1 
ATOM   8606 C  CB    . TYR B 1 530 ? 59.122  76.717  102.452 1.00 64.38  ? 557 TYR B CB    1 
ATOM   8607 C  CG    . TYR B 1 530 ? 60.218  76.480  103.463 1.00 67.32  ? 557 TYR B CG    1 
ATOM   8608 C  CD1   . TYR B 1 530 ? 60.330  75.264  104.122 1.00 73.85  ? 557 TYR B CD1   1 
ATOM   8609 C  CD2   . TYR B 1 530 ? 61.144  77.472  103.755 1.00 81.84  ? 557 TYR B CD2   1 
ATOM   8610 C  CE1   . TYR B 1 530 ? 61.332  75.043  105.048 1.00 86.84  ? 557 TYR B CE1   1 
ATOM   8611 C  CE2   . TYR B 1 530 ? 62.150  77.261  104.679 1.00 75.14  ? 557 TYR B CE2   1 
ATOM   8612 C  CZ    . TYR B 1 530 ? 62.240  76.045  105.322 1.00 83.90  ? 557 TYR B CZ    1 
ATOM   8613 O  OH    . TYR B 1 530 ? 63.240  75.828  106.244 1.00 90.48  ? 557 TYR B OH    1 
ATOM   8614 N  N     . PRO B 1 531 ? 57.014  78.732  101.287 1.00 77.13  ? 558 PRO B N     1 
ATOM   8615 C  CA    . PRO B 1 531 ? 56.135  79.066  100.160 1.00 71.11  ? 558 PRO B CA    1 
ATOM   8616 C  C     . PRO B 1 531 ? 56.464  78.221  98.936  1.00 82.15  ? 558 PRO B C     1 
ATOM   8617 O  O     . PRO B 1 531 ? 57.539  77.630  98.823  1.00 84.51  ? 558 PRO B O     1 
ATOM   8618 C  CB    . PRO B 1 531 ? 56.418  80.552  99.904  1.00 69.48  ? 558 PRO B CB    1 
ATOM   8619 C  CG    . PRO B 1 531 ? 57.228  81.021  101.066 1.00 87.55  ? 558 PRO B CG    1 
ATOM   8620 C  CD    . PRO B 1 531 ? 57.941  79.831  101.602 1.00 77.65  ? 558 PRO B CD    1 
ATOM   8621 N  N     . THR B 1 532 ? 55.508  78.174  98.004  1.00 78.68  ? 559 THR B N     1 
ATOM   8622 C  CA    . THR B 1 532 ? 55.628  77.297  96.840  1.00 83.11  ? 559 THR B CA    1 
ATOM   8623 C  C     . THR B 1 532 ? 56.508  77.921  95.759  1.00 105.04 ? 559 THR B C     1 
ATOM   8624 O  O     . THR B 1 532 ? 57.574  77.393  95.425  1.00 94.65  ? 559 THR B O     1 
ATOM   8625 C  CB    . THR B 1 532 ? 54.242  76.971  96.272  1.00 66.58  ? 559 THR B CB    1 
ATOM   8626 O  OG1   . THR B 1 532 ? 53.470  78.174  96.159  1.00 93.46  ? 559 THR B OG1   1 
ATOM   8627 C  CG2   . THR B 1 532 ? 53.522  75.988  97.175  1.00 66.21  ? 559 THR B CG2   1 
ATOM   8628 N  N     . HIS B 1 533 ? 56.066  79.069  95.242  1.00 122.02 ? 560 HIS B N     1 
ATOM   8629 C  CA    . HIS B 1 533 ? 56.844  79.776  94.190  1.00 130.74 ? 560 HIS B CA    1 
ATOM   8630 C  C     . HIS B 1 533 ? 58.058  80.442  94.841  1.00 121.84 ? 560 HIS B C     1 
ATOM   8631 O  O     . HIS B 1 533 ? 59.007  80.832  94.128  1.00 137.00 ? 560 HIS B O     1 
ATOM   8632 C  CB    . HIS B 1 533 ? 55.949  80.788  93.469  1.00 127.63 ? 560 HIS B CB    1 
ATOM   8633 C  CG    . HIS B 1 533 ? 54.642  80.218  93.030  1.00 134.55 ? 560 HIS B CG    1 
ATOM   8634 N  ND1   . HIS B 1 533 ? 53.483  80.962  92.976  1.00 141.40 ? 560 HIS B ND1   1 
ATOM   8635 C  CD2   . HIS B 1 533 ? 54.306  78.983  92.638  1.00 122.55 ? 560 HIS B CD2   1 
ATOM   8636 C  CE1   . HIS B 1 533 ? 52.489  80.192  92.558  1.00 131.03 ? 560 HIS B CE1   1 
ATOM   8637 N  NE2   . HIS B 1 533 ? 52.967  78.986  92.347  1.00 126.01 ? 560 HIS B NE2   1 
ATOM   8638 N  N     . TYR B 1 534 ? 58.012  80.571  96.170  1.00 127.51 ? 561 TYR B N     1 
ATOM   8639 C  CA    . TYR B 1 534 ? 59.120  81.183  96.953  1.00 135.27 ? 561 TYR B CA    1 
ATOM   8640 C  C     . TYR B 1 534 ? 59.493  82.524  96.320  1.00 140.42 ? 561 TYR B C     1 
ATOM   8641 O  O     . TYR B 1 534 ? 60.697  82.780  96.094  1.00 129.17 ? 561 TYR B O     1 
ATOM   8642 C  CB    . TYR B 1 534 ? 60.315  80.227  97.023  1.00 139.60 ? 561 TYR B CB    1 
ATOM   8643 C  CG    . TYR B 1 534 ? 61.013  80.204  98.376  1.00 151.41 ? 561 TYR B CG    1 
ATOM   8644 C  CD1   . TYR B 1 534 ? 62.009  81.121  98.687  1.00 152.90 ? 561 TYR B CD1   1 
ATOM   8645 C  CD2   . TYR B 1 534 ? 60.679  79.259  99.338  1.00 163.63 ? 561 TYR B CD2   1 
ATOM   8646 C  CE1   . TYR B 1 534 ? 62.645  81.105  99.917  1.00 161.51 ? 561 TYR B CE1   1 
ATOM   8647 C  CE2   . TYR B 1 534 ? 61.310  79.231  100.570 1.00 174.57 ? 561 TYR B CE2   1 
ATOM   8648 C  CZ    . TYR B 1 534 ? 62.295  80.156  100.861 1.00 173.36 ? 561 TYR B CZ    1 
ATOM   8649 O  OH    . TYR B 1 534 ? 62.920  80.133  102.073 1.00 184.54 ? 561 TYR B OH    1 
ATOM   8650 N  N     . THR B 1 535 ? 58.489  83.360  96.036  1.00 148.48 ? 562 THR B N     1 
ATOM   8651 C  CA    . THR B 1 535 ? 58.743  84.681  95.422  1.00 145.31 ? 562 THR B CA    1 
ATOM   8652 C  C     . THR B 1 535 ? 59.661  85.479  96.323  1.00 143.12 ? 562 THR B C     1 
ATOM   8653 O  O     . THR B 1 535 ? 59.440  86.706  96.417  1.00 136.47 ? 562 THR B O     1 
ATOM   8654 C  CB    . THR B 1 535 ? 57.413  85.395  95.192  1.00 142.34 ? 562 THR B CB    1 
ATOM   8655 O  OG1   . THR B 1 535 ? 56.856  85.570  96.490  1.00 145.41 ? 562 THR B OG1   1 
ATOM   8656 C  CG2   . THR B 1 535 ? 56.464  84.588  94.325  1.00 132.38 ? 562 THR B CG2   1 
HETATM 8657 N  N1    . GDU C 2 .   ? 62.398  17.903  55.729  1.00 40.08  ? 701 GDU A N1    1 
HETATM 8658 C  C2    . GDU C 2 .   ? 62.231  17.504  57.159  1.00 46.23  ? 701 GDU A C2    1 
HETATM 8659 N  N3    . GDU C 2 .   ? 61.153  16.545  57.550  1.00 37.04  ? 701 GDU A N3    1 
HETATM 8660 C  C4    . GDU C 2 .   ? 60.257  16.011  56.526  1.00 55.49  ? 701 GDU A C4    1 
HETATM 8661 C  C5    . GDU C 2 .   ? 60.436  16.430  55.114  1.00 43.68  ? 701 GDU A C5    1 
HETATM 8662 C  C6    . GDU C 2 .   ? 61.506  17.382  54.723  1.00 28.17  ? 701 GDU A C6    1 
HETATM 8663 O  O2    . GDU C 2 .   ? 62.966  17.944  57.988  1.00 55.34  ? 701 GDU A O2    1 
HETATM 8664 O  O4    . GDU C 2 .   ? 59.394  15.244  56.826  1.00 54.16  ? 701 GDU A O4    1 
HETATM 8665 C  C1D   . GDU C 2 .   ? 63.444  18.866  55.401  1.00 54.92  ? 701 GDU A C1D   1 
HETATM 8666 C  C2D   . GDU C 2 .   ? 64.654  18.279  54.614  1.00 44.49  ? 701 GDU A C2D   1 
HETATM 8667 O  O2D   . GDU C 2 .   ? 65.613  17.785  55.436  1.00 52.44  ? 701 GDU A O2D   1 
HETATM 8668 C  C3D   . GDU C 2 .   ? 65.187  19.501  53.881  1.00 49.13  ? 701 GDU A C3D   1 
HETATM 8669 C  C4D   . GDU C 2 .   ? 64.114  20.248  53.613  1.00 42.08  ? 701 GDU A C4D   1 
HETATM 8670 O  O4D   . GDU C 2 .   ? 62.951  19.801  54.628  1.00 55.57  ? 701 GDU A O4D   1 
HETATM 8671 O  O3D   . GDU C 2 .   ? 66.089  20.276  54.772  1.00 55.03  ? 701 GDU A O3D   1 
HETATM 8672 C  C5D   . GDU C 2 .   ? 63.627  20.010  52.201  1.00 57.73  ? 701 GDU A C5D   1 
HETATM 8673 O  O5D   . GDU C 2 .   ? 63.563  18.583  51.928  1.00 78.76  ? 701 GDU A O5D   1 
HETATM 8674 P  PA    . GDU C 2 .   ? 64.350  18.129  50.557  1.00 58.89  ? 701 GDU A PA    1 
HETATM 8675 O  O1A   . GDU C 2 .   ? 65.825  18.277  50.753  1.00 56.00  ? 701 GDU A O1A   1 
HETATM 8676 O  O2A   . GDU C 2 .   ? 64.016  16.706  50.203  1.00 62.81  ? 701 GDU A O2A   1 
HETATM 8677 O  O3A   . GDU C 2 .   ? 63.792  19.216  49.449  1.00 56.53  ? 701 GDU A O3A   1 
HETATM 8678 P  PB    . GDU C 2 .   ? 63.894  19.199  47.808  1.00 46.75  ? 701 GDU A PB    1 
HETATM 8679 O  O1B   . GDU C 2 .   ? 65.342  19.063  47.353  1.00 48.20  ? 701 GDU A O1B   1 
HETATM 8680 O  O2B   . GDU C 2 .   ? 63.070  18.049  47.220  1.00 56.69  ? 701 GDU A O2B   1 
HETATM 8681 O  O3B   . GDU C 2 .   ? 63.246  20.662  47.330  1.00 67.19  ? 701 GDU A O3B   1 
HETATM 8682 C  "C1'" . GDU C 2 .   ? 62.549  21.369  48.273  1.00 40.42  ? 701 GDU A "C1'" 1 
HETATM 8683 C  "C2'" . GDU C 2 .   ? 61.174  20.723  48.489  1.00 48.50  ? 701 GDU A "C2'" 1 
HETATM 8684 C  "C3'" . GDU C 2 .   ? 60.070  21.723  48.515  1.00 43.46  ? 701 GDU A "C3'" 1 
HETATM 8685 C  "C4'" . GDU C 2 .   ? 60.420  22.894  49.369  1.00 67.99  ? 701 GDU A "C4'" 1 
HETATM 8686 C  "C5'" . GDU C 2 .   ? 61.682  23.611  48.848  1.00 55.65  ? 701 GDU A "C5'" 1 
HETATM 8687 C  "C6'" . GDU C 2 .   ? 62.593  23.896  49.985  1.00 50.68  ? 701 GDU A "C6'" 1 
HETATM 8688 O  "O2'" . GDU C 2 .   ? 60.914  19.796  47.424  1.00 99.69  ? 701 GDU A "O2'" 1 
HETATM 8689 O  "O3'" . GDU C 2 .   ? 58.844  21.104  49.033  1.00 46.95  ? 701 GDU A "O3'" 1 
HETATM 8690 O  "O4'" . GDU C 2 .   ? 60.634  22.459  50.713  1.00 33.19  ? 701 GDU A "O4'" 1 
HETATM 8691 O  "O5'" . GDU C 2 .   ? 62.428  22.807  47.858  1.00 47.76  ? 701 GDU A "O5'" 1 
HETATM 8692 O  "O6'" . GDU C 2 .   ? 61.961  24.751  50.921  1.00 80.90  ? 701 GDU A "O6'" 1 
HETATM 8693 N  N1    . UDP D 3 .   ? 99.775  14.319  28.727  1.00 117.02 ? 702 UDP A N1    1 
HETATM 8694 C  C2    . UDP D 3 .   ? 100.743 13.414  28.335  1.00 114.82 ? 702 UDP A C2    1 
HETATM 8695 N  N3    . UDP D 3 .   ? 101.869 13.973  27.781  1.00 121.00 ? 702 UDP A N3    1 
HETATM 8696 C  C4    . UDP D 3 .   ? 102.116 15.318  27.585  1.00 120.71 ? 702 UDP A C4    1 
HETATM 8697 C  C5    . UDP D 3 .   ? 101.066 16.189  28.018  1.00 117.87 ? 702 UDP A C5    1 
HETATM 8698 C  C6    . UDP D 3 .   ? 99.952  15.674  28.563  1.00 116.48 ? 702 UDP A C6    1 
HETATM 8699 O  O2    . UDP D 3 .   ? 100.616 12.205  28.465  1.00 114.40 ? 702 UDP A O2    1 
HETATM 8700 O  O4    . UDP D 3 .   ? 103.186 15.676  27.070  1.00 120.55 ? 702 UDP A O4    1 
HETATM 8701 C  "C1'" . UDP D 3 .   ? 98.545  13.784  29.329  1.00 111.87 ? 702 UDP A "C1'" 1 
HETATM 8702 C  "C2'" . UDP D 3 .   ? 97.961  14.688  30.419  1.00 98.92  ? 702 UDP A "C2'" 1 
HETATM 8703 O  "O2'" . UDP D 3 .   ? 98.424  14.291  31.705  1.00 89.59  ? 702 UDP A "O2'" 1 
HETATM 8704 C  "C3'" . UDP D 3 .   ? 96.464  14.439  30.247  1.00 105.73 ? 702 UDP A "C3'" 1 
HETATM 8705 C  "C4'" . UDP D 3 .   ? 96.335  14.306  28.735  1.00 105.74 ? 702 UDP A "C4'" 1 
HETATM 8706 O  "O4'" . UDP D 3 .   ? 97.563  13.674  28.311  1.00 112.32 ? 702 UDP A "O4'" 1 
HETATM 8707 O  "O3'" . UDP D 3 .   ? 96.054  13.243  30.901  1.00 94.92  ? 702 UDP A "O3'" 1 
HETATM 8708 C  "C5'" . UDP D 3 .   ? 96.152  15.602  27.984  1.00 105.69 ? 702 UDP A "C5'" 1 
HETATM 8709 O  "O5'" . UDP D 3 .   ? 95.603  16.605  28.866  1.00 124.79 ? 702 UDP A "O5'" 1 
HETATM 8710 P  PA    . UDP D 3 .   ? 95.875  18.146  28.629  1.00 114.52 ? 702 UDP A PA    1 
HETATM 8711 O  O1A   . UDP D 3 .   ? 94.760  18.887  29.265  1.00 99.00  ? 702 UDP A O1A   1 
HETATM 8712 O  O2A   . UDP D 3 .   ? 97.289  18.527  29.060  1.00 93.57  ? 702 UDP A O2A   1 
HETATM 8713 O  O3A   . UDP D 3 .   ? 95.826  18.324  27.046  1.00 121.17 ? 702 UDP A O3A   1 
HETATM 8714 P  PB    . UDP D 3 .   ? 94.552  18.703  26.182  1.00 116.95 ? 702 UDP A PB    1 
HETATM 8715 O  O1B   . UDP D 3 .   ? 94.563  20.232  26.202  1.00 122.57 ? 702 UDP A O1B   1 
HETATM 8716 O  O2B   . UDP D 3 .   ? 93.390  18.178  27.024  1.00 129.82 ? 702 UDP A O2B   1 
HETATM 8717 O  O3B   . UDP D 3 .   ? 94.608  18.114  24.810  1.00 115.88 ? 702 UDP A O3B   1 
HETATM 8718 MN MN    . MN  E 4 .   ? 92.265  18.403  28.772  1.00 92.52  ? 703 MN  A MN    1 
HETATM 8719 O  O1    . MES F 5 .   ? 58.907  4.037   44.543  1.00 69.83  ? 704 MES A O1    1 
HETATM 8720 C  C2    . MES F 5 .   ? 59.033  4.604   45.853  1.00 59.97  ? 704 MES A C2    1 
HETATM 8721 C  C3    . MES F 5 .   ? 60.156  3.989   46.683  1.00 55.51  ? 704 MES A C3    1 
HETATM 8722 N  N4    . MES F 5 .   ? 61.352  3.956   45.858  1.00 63.62  ? 704 MES A N4    1 
HETATM 8723 C  C5    . MES F 5 .   ? 61.263  3.288   44.569  1.00 62.55  ? 704 MES A C5    1 
HETATM 8724 C  C6    . MES F 5 .   ? 60.125  3.937   43.787  1.00 60.28  ? 704 MES A C6    1 
HETATM 8725 C  C7    . MES F 5 .   ? 62.657  3.942   46.515  1.00 65.17  ? 704 MES A C7    1 
HETATM 8726 C  C8    . MES F 5 .   ? 62.442  3.888   48.024  1.00 58.65  ? 704 MES A C8    1 
HETATM 8727 S  S     . MES F 5 .   ? 63.895  3.758   48.809  1.00 83.93  ? 704 MES A S     1 
HETATM 8728 O  O1S   . MES F 5 .   ? 64.799  4.863   48.428  1.00 68.21  ? 704 MES A O1S   1 
HETATM 8729 O  O2S   . MES F 5 .   ? 64.527  2.469   48.433  1.00 85.82  ? 704 MES A O2S   1 
HETATM 8730 O  O3S   . MES F 5 .   ? 63.671  3.797   50.274  1.00 74.66  ? 704 MES A O3S   1 
HETATM 8731 O  O1    . MES G 5 .   ? 65.294  10.230  40.073  1.00 104.03 ? 705 MES A O1    1 
HETATM 8732 C  C2    . MES G 5 .   ? 65.145  8.863   39.687  1.00 99.86  ? 705 MES A C2    1 
HETATM 8733 C  C3    . MES G 5 .   ? 66.504  8.218   39.416  1.00 109.74 ? 705 MES A C3    1 
HETATM 8734 N  N4    . MES G 5 .   ? 67.305  9.083   38.555  1.00 101.02 ? 705 MES A N4    1 
HETATM 8735 C  C5    . MES G 5 .   ? 67.322  10.526  38.760  1.00 85.36  ? 705 MES A C5    1 
HETATM 8736 C  C6    . MES G 5 .   ? 65.901  11.004  39.031  1.00 102.67 ? 705 MES A C6    1 
HETATM 8737 C  C7    . MES G 5 .   ? 68.503  8.526   37.929  1.00 107.42 ? 705 MES A C7    1 
HETATM 8738 C  C8    . MES G 5 .   ? 68.447  7.004   38.043  1.00 106.51 ? 705 MES A C8    1 
HETATM 8739 S  S     . MES G 5 .   ? 69.936  6.380   37.689  1.00 229.36 ? 705 MES A S     1 
HETATM 8740 O  O1S   . MES G 5 .   ? 70.431  6.946   36.410  1.00 129.03 ? 705 MES A O1S   1 
HETATM 8741 O  O2S   . MES G 5 .   ? 69.859  4.902   37.563  1.00 109.20 ? 705 MES A O2S   1 
HETATM 8742 O  O3S   . MES G 5 .   ? 70.868  6.704   38.794  1.00 107.54 ? 705 MES A O3S   1 
HETATM 8743 CL CL    . CL  H 6 .   ? 71.167  18.506  72.651  1.00 89.39  ? 706 CL  A CL    1 
HETATM 8744 CL CL    . CL  I 6 .   ? 73.333  26.798  33.862  1.00 93.02  ? 707 CL  A CL    1 
HETATM 8745 CL CL    . CL  J 6 .   ? 60.781  24.267  39.474  1.00 74.17  ? 708 CL  A CL    1 
HETATM 8746 CA CA    . CA  K 7 .   ? 66.886  19.541  48.827  1.00 49.68  ? 709 CA  A CA    1 
HETATM 8747 N  N1    . GDU L 2 .   ? 66.168  45.994  97.512  1.00 42.88  ? 701 GDU B N1    1 
HETATM 8748 C  C2    . GDU L 2 .   ? 65.657  44.599  97.336  1.00 42.48  ? 701 GDU B C2    1 
HETATM 8749 N  N3    . GDU L 2 .   ? 66.007  43.542  98.328  1.00 39.26  ? 701 GDU B N3    1 
HETATM 8750 C  C4    . GDU L 2 .   ? 66.857  43.882  99.464  1.00 45.60  ? 701 GDU B C4    1 
HETATM 8751 C  C5    . GDU L 2 .   ? 67.358  45.268  99.616  1.00 55.14  ? 701 GDU B C5    1 
HETATM 8752 C  C6    . GDU L 2 .   ? 67.014  46.321  98.631  1.00 33.66  ? 701 GDU B C6    1 
HETATM 8753 O  O2    . GDU L 2 .   ? 64.963  44.320  96.410  1.00 50.66  ? 701 GDU B O2    1 
HETATM 8754 O  O4    . GDU L 2 .   ? 67.141  43.049  100.263 1.00 52.86  ? 701 GDU B O4    1 
HETATM 8755 C  C1D   . GDU L 2 .   ? 65.828  47.000  96.510  1.00 47.77  ? 701 GDU B C1D   1 
HETATM 8756 C  C2D   . GDU L 2 .   ? 64.875  48.120  97.025  1.00 47.89  ? 701 GDU B C2D   1 
HETATM 8757 O  O2D   . GDU L 2 .   ? 63.578  47.758  96.852  1.00 47.06  ? 701 GDU B O2D   1 
HETATM 8758 C  C3D   . GDU L 2 .   ? 65.201  49.276  96.097  1.00 55.31  ? 701 GDU B C3D   1 
HETATM 8759 C  C4D   . GDU L 2 .   ? 66.517  49.182  95.920  1.00 44.19  ? 701 GDU B C4D   1 
HETATM 8760 O  O4D   . GDU L 2 .   ? 66.907  47.633  96.114  1.00 54.42  ? 701 GDU B O4D   1 
HETATM 8761 O  O3D   . GDU L 2 .   ? 64.514  49.118  94.788  1.00 48.95  ? 701 GDU B O3D   1 
HETATM 8762 C  C5D   . GDU L 2 .   ? 67.213  50.017  96.970  1.00 45.55  ? 701 GDU B C5D   1 
HETATM 8763 O  O5D   . GDU L 2 .   ? 66.368  51.155  97.287  1.00 65.05  ? 701 GDU B O5D   1 
HETATM 8764 P  PA    . GDU L 2 .   ? 66.157  51.520  98.881  1.00 48.46  ? 701 GDU B PA    1 
HETATM 8765 O  O1A   . GDU L 2 .   ? 65.121  52.599  99.013  1.00 71.54  ? 701 GDU B O1A   1 
HETATM 8766 O  O2A   . GDU L 2 .   ? 65.682  50.302  99.635  1.00 49.99  ? 701 GDU B O2A   1 
HETATM 8767 O  O3A   . GDU L 2 .   ? 67.618  52.035  99.472  1.00 46.25  ? 701 GDU B O3A   1 
HETATM 8768 P  PB    . GDU L 2 .   ? 68.210  53.567  99.272  1.00 58.48  ? 701 GDU B PB    1 
HETATM 8769 O  O1B   . GDU L 2 .   ? 69.215  53.860  100.387 1.00 70.98  ? 701 GDU B O1B   1 
HETATM 8770 O  O2B   . GDU L 2 .   ? 67.056  54.568  99.396  1.00 63.49  ? 701 GDU B O2B   1 
HETATM 8771 O  O3B   . GDU L 2 .   ? 68.926  53.791  97.777  1.00 54.11  ? 701 GDU B O3B   1 
HETATM 8772 C  "C1'" . GDU L 2 .   ? 69.747  52.863  97.203  1.00 62.98  ? 701 GDU B "C1'" 1 
HETATM 8773 C  "C2'" . GDU L 2 .   ? 70.922  52.527  98.127  1.00 51.26  ? 701 GDU B "C2'" 1 
HETATM 8774 C  "C3'" . GDU L 2 .   ? 72.073  51.879  97.429  1.00 59.79  ? 701 GDU B "C3'" 1 
HETATM 8775 C  "C4'" . GDU L 2 .   ? 71.756  51.383  96.052  1.00 65.29  ? 701 GDU B "C4'" 1 
HETATM 8776 C  "C5'" . GDU L 2 .   ? 71.126  52.482  95.166  1.00 50.08  ? 701 GDU B "C5'" 1 
HETATM 8777 C  "C6'" . GDU L 2 .   ? 70.346  51.853  94.067  1.00 69.49  ? 701 GDU B "C6'" 1 
HETATM 8778 O  "O2'" . GDU L 2 .   ? 71.394  53.752  98.708  1.00 89.36  ? 701 GDU B "O2'" 1 
HETATM 8779 O  "O3'" . GDU L 2 .   ? 72.570  50.751  98.227  1.00 50.02  ? 701 GDU B "O3'" 1 
HETATM 8780 O  "O4'" . GDU L 2 .   ? 70.906  50.227  96.119  1.00 38.59  ? 701 GDU B "O4'" 1 
HETATM 8781 O  "O5'" . GDU L 2 .   ? 70.243  53.415  95.896  1.00 47.01  ? 701 GDU B "O5'" 1 
HETATM 8782 O  "O6'" . GDU L 2 .   ? 71.214  51.459  93.015  1.00 75.33  ? 701 GDU B "O6'" 1 
HETATM 8783 CL CL    . CL  M 6 .   ? 72.746  52.784  118.300 1.00 74.15  ? 702 CL  B CL    1 
HETATM 8784 CL CL    . CL  N 6 .   ? 71.477  56.739  115.465 1.00 72.35  ? 703 CL  B CL    1 
HETATM 8785 CL CL    . CL  O 6 .   ? 72.882  55.949  118.189 1.00 118.79 ? 704 CL  B CL    1 
HETATM 8786 NA NA    . NA  P 8 .   ? 71.368  54.610  116.564 1.00 46.50  ? 705 NA  B NA    1 
HETATM 8787 CA CA    . CA  Q 7 .   ? 65.768  54.331  97.517  1.00 62.41  ? 706 CA  B CA    1 
HETATM 8788 O  O     . HOH R 9 .   ? 62.880  14.919  49.534  1.00 55.42  ? 801 HOH A O     1 
HETATM 8789 O  O     . HOH R 9 .   ? 60.508  19.022  45.318  1.00 56.64  ? 802 HOH A O     1 
HETATM 8790 O  O     . HOH R 9 .   ? 78.541  40.924  47.183  1.00 62.74  ? 803 HOH A O     1 
HETATM 8791 O  O     . HOH R 9 .   ? 80.370  28.391  55.679  1.00 51.37  ? 804 HOH A O     1 
HETATM 8792 O  O     . HOH R 9 .   ? 61.331  16.944  59.839  1.00 39.22  ? 805 HOH A O     1 
HETATM 8793 O  O     . HOH R 9 .   ? 60.273  8.402   46.705  1.00 49.04  ? 806 HOH A O     1 
HETATM 8794 O  O     . HOH R 9 .   ? 81.654  21.937  54.219  1.00 50.28  ? 807 HOH A O     1 
HETATM 8795 O  O     . HOH R 9 .   ? 61.610  26.943  51.731  1.00 49.12  ? 808 HOH A O     1 
HETATM 8796 O  O     . HOH R 9 .   ? 60.046  6.341   53.547  1.00 66.86  ? 809 HOH A O     1 
HETATM 8797 O  O     . HOH R 9 .   ? 81.617  11.230  63.518  1.00 64.62  ? 810 HOH A O     1 
HETATM 8798 O  O     . HOH R 9 .   ? 76.663  11.205  40.786  1.00 53.54  ? 811 HOH A O     1 
HETATM 8799 O  O     . HOH R 9 .   ? 83.927  24.304  41.386  1.00 75.06  ? 812 HOH A O     1 
HETATM 8800 O  O     . HOH R 9 .   ? 67.942  43.253  56.945  1.00 48.80  ? 813 HOH A O     1 
HETATM 8801 O  O     . HOH R 9 .   ? 77.570  39.018  60.210  1.00 52.81  ? 814 HOH A O     1 
HETATM 8802 O  O     . HOH R 9 .   ? 85.008  16.976  40.197  1.00 65.01  ? 815 HOH A O     1 
HETATM 8803 O  O     . HOH R 9 .   ? 67.761  28.210  70.043  1.00 42.64  ? 816 HOH A O     1 
HETATM 8804 O  O     . HOH R 9 .   ? 67.168  17.364  47.009  1.00 64.38  ? 817 HOH A O     1 
HETATM 8805 O  O     . HOH R 9 .   ? 63.238  26.766  42.047  1.00 47.87  ? 818 HOH A O     1 
HETATM 8806 O  O     . HOH R 9 .   ? 63.400  24.753  55.464  1.00 56.20  ? 819 HOH A O     1 
HETATM 8807 O  O     . HOH R 9 .   ? 77.694  31.869  63.440  1.00 55.29  ? 820 HOH A O     1 
HETATM 8808 O  O     . HOH R 9 .   ? 77.974  35.726  57.315  1.00 50.83  ? 821 HOH A O     1 
HETATM 8809 O  O     . HOH R 9 .   ? 75.360  24.593  54.288  1.00 44.10  ? 822 HOH A O     1 
HETATM 8810 O  O     . HOH R 9 .   ? 62.453  41.845  66.217  1.00 61.91  ? 823 HOH A O     1 
HETATM 8811 O  O     . HOH R 9 .   ? 61.353  42.364  51.539  1.00 58.28  ? 824 HOH A O     1 
HETATM 8812 O  O     . HOH R 9 .   ? 66.365  39.733  55.221  1.00 53.66  ? 825 HOH A O     1 
HETATM 8813 O  O     . HOH R 9 .   ? 79.011  11.367  39.594  1.00 56.88  ? 826 HOH A O     1 
HETATM 8814 O  O     . HOH R 9 .   ? 70.652  15.726  49.223  1.00 60.90  ? 827 HOH A O     1 
HETATM 8815 O  O     . HOH R 9 .   ? 75.835  30.726  44.990  1.00 59.23  ? 828 HOH A O     1 
HETATM 8816 O  O     . HOH R 9 .   ? 68.055  41.720  54.535  1.00 41.20  ? 829 HOH A O     1 
HETATM 8817 O  O     . HOH R 9 .   ? 59.450  10.685  62.964  1.00 60.64  ? 830 HOH A O     1 
HETATM 8818 O  O     . HOH R 9 .   ? 83.878  19.455  47.958  1.00 65.73  ? 831 HOH A O     1 
HETATM 8819 O  O     . HOH R 9 .   ? 60.808  16.998  64.668  1.00 56.58  ? 832 HOH A O     1 
HETATM 8820 O  O     . HOH R 9 .   ? 53.041  34.092  61.990  1.00 39.37  ? 833 HOH A O     1 
HETATM 8821 O  O     . HOH R 9 .   ? 54.656  27.533  54.465  1.00 45.04  ? 834 HOH A O     1 
HETATM 8822 O  O     . HOH R 9 .   ? 74.603  33.737  43.630  1.00 57.39  ? 835 HOH A O     1 
HETATM 8823 O  O     . HOH R 9 .   ? 81.300  30.402  62.929  1.00 67.50  ? 836 HOH A O     1 
HETATM 8824 O  O     . HOH R 9 .   ? 67.833  21.190  46.898  1.00 71.91  ? 837 HOH A O     1 
HETATM 8825 O  O     . HOH R 9 .   ? 63.304  12.052  52.300  1.00 59.03  ? 838 HOH A O     1 
HETATM 8826 O  O     . HOH R 9 .   ? 49.518  31.748  53.163  1.00 55.90  ? 839 HOH A O     1 
HETATM 8827 O  O     . HOH R 9 .   ? 75.163  40.891  74.994  1.00 44.55  ? 840 HOH A O     1 
HETATM 8828 O  O     . HOH R 9 .   ? 78.660  15.575  53.674  1.00 60.62  ? 841 HOH A O     1 
HETATM 8829 O  O     . HOH R 9 .   ? 50.307  31.487  55.624  1.00 50.57  ? 842 HOH A O     1 
HETATM 8830 O  O     . HOH R 9 .   ? 58.858  29.985  49.952  1.00 44.01  ? 843 HOH A O     1 
HETATM 8831 O  O     . HOH R 9 .   ? 48.822  25.904  43.272  1.00 72.84  ? 844 HOH A O     1 
HETATM 8832 O  O     . HOH R 9 .   ? 91.479  18.649  37.284  1.00 56.31  ? 845 HOH A O     1 
HETATM 8833 O  O     . HOH R 9 .   ? 77.720  29.356  62.821  1.00 56.22  ? 846 HOH A O     1 
HETATM 8834 O  O     . HOH R 9 .   ? 64.128  14.761  52.802  1.00 52.15  ? 847 HOH A O     1 
HETATM 8835 O  O     . HOH R 9 .   ? 66.128  22.023  48.871  1.00 66.99  ? 848 HOH A O     1 
HETATM 8836 O  O     . HOH R 9 .   ? 57.543  27.219  53.287  1.00 53.33  ? 849 HOH A O     1 
HETATM 8837 O  O     . HOH R 9 .   ? 65.382  24.078  56.850  1.00 63.65  ? 850 HOH A O     1 
HETATM 8838 O  O     . HOH R 9 .   ? 82.497  27.256  54.236  1.00 61.01  ? 851 HOH A O     1 
HETATM 8839 O  O     . HOH R 9 .   ? 56.950  45.326  53.437  1.00 50.89  ? 852 HOH A O     1 
HETATM 8840 O  O     . HOH R 9 .   ? 60.899  9.894   69.366  1.00 68.56  ? 853 HOH A O     1 
HETATM 8841 O  O     . HOH R 9 .   ? 57.992  39.193  63.500  1.00 47.53  ? 854 HOH A O     1 
HETATM 8842 O  O     . HOH R 9 .   ? 78.204  12.291  50.229  1.00 50.14  ? 855 HOH A O     1 
HETATM 8843 O  O     . HOH R 9 .   ? 56.036  14.767  45.469  1.00 53.23  ? 856 HOH A O     1 
HETATM 8844 O  O     . HOH R 9 .   ? 85.531  23.984  53.320  1.00 52.29  ? 857 HOH A O     1 
HETATM 8845 O  O     . HOH R 9 .   ? 72.468  7.583   30.813  1.00 53.29  ? 858 HOH A O     1 
HETATM 8846 O  O     . HOH R 9 .   ? 49.559  34.179  56.141  1.00 51.30  ? 859 HOH A O     1 
HETATM 8847 O  O     . HOH R 9 .   ? 67.909  3.651   48.134  1.00 48.74  ? 860 HOH A O     1 
HETATM 8848 O  O     . HOH R 9 .   ? 61.796  39.424  67.579  1.00 60.45  ? 861 HOH A O     1 
HETATM 8849 O  O     . HOH R 9 .   ? 61.845  0.993   50.178  1.00 48.94  ? 862 HOH A O     1 
HETATM 8850 O  O     . HOH R 9 .   ? 57.772  18.494  45.141  1.00 48.93  ? 863 HOH A O     1 
HETATM 8851 O  O     . HOH R 9 .   ? 59.339  28.192  52.176  1.00 47.14  ? 864 HOH A O     1 
HETATM 8852 O  O     . HOH R 9 .   ? 64.318  33.934  75.453  1.00 59.49  ? 865 HOH A O     1 
HETATM 8853 O  O     . HOH R 9 .   ? 76.256  41.353  60.029  1.00 56.72  ? 866 HOH A O     1 
HETATM 8854 O  O     . HOH S 9 .   ? 60.542  54.943  99.405  1.00 67.63  ? 801 HOH B O     1 
HETATM 8855 O  O     . HOH S 9 .   ? 67.764  49.043  91.376  1.00 46.19  ? 802 HOH B O     1 
HETATM 8856 O  O     . HOH S 9 .   ? 42.853  48.630  79.106  1.00 72.80  ? 803 HOH B O     1 
HETATM 8857 O  O     . HOH S 9 .   ? 51.964  57.247  89.263  1.00 43.69  ? 804 HOH B O     1 
HETATM 8858 O  O     . HOH S 9 .   ? 53.883  58.959  84.360  1.00 54.14  ? 805 HOH B O     1 
HETATM 8859 O  O     . HOH S 9 .   ? 64.184  55.406  99.526  1.00 65.90  ? 806 HOH B O     1 
HETATM 8860 O  O     . HOH S 9 .   ? 73.065  50.954  106.218 1.00 51.44  ? 807 HOH B O     1 
HETATM 8861 O  O     . HOH S 9 .   ? 66.503  50.444  109.951 1.00 49.50  ? 808 HOH B O     1 
HETATM 8862 O  O     . HOH S 9 .   ? 83.657  45.372  90.164  1.00 55.83  ? 809 HOH B O     1 
HETATM 8863 O  O     . HOH S 9 .   ? 43.203  75.686  86.645  1.00 64.68  ? 810 HOH B O     1 
HETATM 8864 O  O     . HOH S 9 .   ? 79.173  37.424  87.489  1.00 55.46  ? 811 HOH B O     1 
HETATM 8865 O  O     . HOH S 9 .   ? 64.432  37.461  95.709  1.00 55.15  ? 812 HOH B O     1 
HETATM 8866 O  O     . HOH S 9 .   ? 64.775  41.882  96.879  1.00 38.20  ? 813 HOH B O     1 
HETATM 8867 O  O     . HOH S 9 .   ? 63.856  64.370  86.648  1.00 54.84  ? 814 HOH B O     1 
HETATM 8868 O  O     . HOH S 9 .   ? 65.640  54.552  102.436 1.00 60.94  ? 815 HOH B O     1 
HETATM 8869 O  O     . HOH S 9 .   ? 55.418  49.304  80.704  1.00 46.16  ? 816 HOH B O     1 
HETATM 8870 O  O     . HOH S 9 .   ? 91.792  61.007  95.985  1.00 62.82  ? 817 HOH B O     1 
HETATM 8871 O  O     . HOH S 9 .   ? 63.865  48.115  104.056 1.00 51.45  ? 818 HOH B O     1 
HETATM 8872 O  O     . HOH S 9 .   ? 64.114  48.141  100.888 1.00 46.29  ? 819 HOH B O     1 
HETATM 8873 O  O     . HOH S 9 .   ? 78.503  40.377  83.568  1.00 45.17  ? 820 HOH B O     1 
HETATM 8874 O  O     . HOH S 9 .   ? 85.237  46.717  77.585  1.00 53.17  ? 821 HOH B O     1 
HETATM 8875 O  O     . HOH S 9 .   ? 55.226  56.839  83.179  1.00 53.23  ? 822 HOH B O     1 
HETATM 8876 O  O     . HOH S 9 .   ? 71.166  55.202  75.505  1.00 47.91  ? 823 HOH B O     1 
HETATM 8877 O  O     . HOH S 9 .   ? 77.965  55.054  77.686  1.00 59.52  ? 824 HOH B O     1 
HETATM 8878 O  O     . HOH S 9 .   ? 81.806  43.719  89.174  1.00 51.19  ? 825 HOH B O     1 
HETATM 8879 O  O     . HOH S 9 .   ? 65.197  47.547  90.376  1.00 53.16  ? 826 HOH B O     1 
HETATM 8880 O  O     . HOH S 9 .   ? 71.997  53.227  77.408  1.00 46.38  ? 827 HOH B O     1 
HETATM 8881 O  O     . HOH S 9 .   ? 71.497  53.560  73.438  1.00 53.90  ? 828 HOH B O     1 
HETATM 8882 O  O     . HOH S 9 .   ? 63.308  36.908  102.047 1.00 51.59  ? 829 HOH B O     1 
HETATM 8883 O  O     . HOH S 9 .   ? 58.995  32.309  99.310  1.00 65.94  ? 830 HOH B O     1 
HETATM 8884 O  O     . HOH S 9 .   ? 63.580  36.704  74.467  1.00 39.93  ? 831 HOH B O     1 
HETATM 8885 O  O     . HOH S 9 .   ? 58.163  54.716  88.530  1.00 48.14  ? 832 HOH B O     1 
HETATM 8886 O  O     . HOH S 9 .   ? 57.672  48.329  67.978  1.00 47.53  ? 833 HOH B O     1 
HETATM 8887 O  O     . HOH S 9 .   ? 59.011  45.460  55.283  1.00 42.37  ? 834 HOH B O     1 
HETATM 8888 O  O     . HOH S 9 .   ? 76.117  42.944  77.309  1.00 45.09  ? 835 HOH B O     1 
HETATM 8889 O  O     . HOH S 9 .   ? 48.734  69.134  92.481  1.00 52.01  ? 836 HOH B O     1 
HETATM 8890 O  O     . HOH S 9 .   ? 66.332  65.887  84.757  1.00 49.43  ? 837 HOH B O     1 
HETATM 8891 O  O     . HOH S 9 .   ? 73.901  60.068  94.866  1.00 53.60  ? 838 HOH B O     1 
HETATM 8892 O  O     . HOH S 9 .   ? 75.954  52.324  90.175  1.00 43.61  ? 839 HOH B O     1 
HETATM 8893 O  O     . HOH S 9 .   ? 62.669  63.616  97.456  1.00 58.55  ? 840 HOH B O     1 
HETATM 8894 O  O     . HOH S 9 .   ? 63.338  57.593  101.941 1.00 55.72  ? 841 HOH B O     1 
HETATM 8895 O  O     . HOH S 9 .   ? 65.456  56.609  96.867  1.00 62.81  ? 842 HOH B O     1 
HETATM 8896 O  O     . HOH S 9 .   ? 53.677  64.373  107.813 1.00 55.38  ? 843 HOH B O     1 
HETATM 8897 O  O     . HOH S 9 .   ? 74.543  48.450  91.712  1.00 61.24  ? 844 HOH B O     1 
HETATM 8898 O  O     . HOH S 9 .   ? 66.486  50.758  102.381 1.00 56.85  ? 845 HOH B O     1 
HETATM 8899 O  O     . HOH S 9 .   ? 46.134  48.295  80.576  1.00 58.18  ? 846 HOH B O     1 
HETATM 8900 O  O     . HOH S 9 .   ? 55.648  33.702  85.120  1.00 63.56  ? 847 HOH B O     1 
HETATM 8901 O  O     . HOH S 9 .   ? 73.821  36.410  90.260  1.00 40.03  ? 848 HOH B O     1 
HETATM 8902 O  O     . HOH S 9 .   ? 83.407  40.261  87.954  1.00 47.64  ? 849 HOH B O     1 
HETATM 8903 O  O     . HOH S 9 .   ? 76.595  38.396  76.660  1.00 52.62  ? 850 HOH B O     1 
HETATM 8904 O  O     . HOH S 9 .   ? 78.843  38.802  79.090  1.00 53.79  ? 851 HOH B O     1 
HETATM 8905 O  O     . HOH S 9 .   ? 44.753  47.243  95.955  1.00 63.24  ? 852 HOH B O     1 
HETATM 8906 O  O     . HOH S 9 .   ? 43.215  65.264  116.335 1.00 56.94  ? 853 HOH B O     1 
HETATM 8907 O  O     . HOH S 9 .   ? 75.779  37.145  81.548  1.00 54.86  ? 854 HOH B O     1 
HETATM 8908 O  O     . HOH S 9 .   ? 73.191  35.271  75.928  1.00 67.21  ? 855 HOH B O     1 
HETATM 8909 O  O     . HOH S 9 .   ? 47.492  53.298  84.097  1.00 63.80  ? 856 HOH B O     1 
HETATM 8910 O  O     . HOH S 9 .   ? 58.664  39.944  66.173  1.00 47.53  ? 857 HOH B O     1 
HETATM 8911 O  O     . HOH S 9 .   ? 47.739  51.333  81.687  1.00 60.67  ? 858 HOH B O     1 
HETATM 8912 O  O     . HOH S 9 .   ? 73.151  39.467  74.705  1.00 47.53  ? 859 HOH B O     1 
HETATM 8913 O  O     . HOH S 9 .   ? 44.347  79.031  91.929  1.00 49.04  ? 860 HOH B O     1 
HETATM 8914 O  O     . HOH S 9 .   ? 62.157  49.839  111.632 1.00 65.13  ? 861 HOH B O     1 
HETATM 8915 O  O     . HOH S 9 .   ? 61.875  60.812  111.735 1.00 54.31  ? 862 HOH B O     1 
HETATM 8916 O  O     . HOH S 9 .   ? 73.323  35.416  87.728  1.00 41.77  ? 863 HOH B O     1 
HETATM 8917 O  O     . HOH S 9 .   ? 65.594  33.045  78.005  1.00 52.74  ? 864 HOH B O     1 
HETATM 8918 O  O     . HOH S 9 .   ? 41.656  78.780  88.738  1.00 64.73  ? 865 HOH B O     1 
HETATM 8919 O  O     . HOH S 9 .   ? 75.231  36.195  76.651  1.00 55.72  ? 866 HOH B O     1 
HETATM 8920 O  O     . HOH S 9 .   ? 77.436  35.568  87.881  1.00 56.18  ? 867 HOH B O     1 
HETATM 8921 O  O     . HOH S 9 .   ? 48.408  60.982  95.924  1.00 48.90  ? 868 HOH B O     1 
HETATM 8922 O  O     . HOH S 9 .   ? 60.784  62.345  113.178 1.00 55.16  ? 869 HOH B O     1 
HETATM 8923 O  O     . HOH S 9 .   ? 53.144  35.172  87.613  1.00 63.64  ? 870 HOH B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 17  ? 1.4446 1.3175 1.3374 -0.2437 0.0132  -0.4123 44  SER A N   
2    C CA  . SER A 17  ? 1.5043 1.4078 1.3743 -0.2134 0.0024  -0.3998 44  SER A CA  
3    C C   . SER A 17  ? 1.5858 1.4687 1.4411 -0.1990 0.0143  -0.3641 44  SER A C   
4    O O   . SER A 17  ? 1.5821 1.4204 1.4145 -0.1887 0.0213  -0.3514 44  SER A O   
5    C CB  . SER A 17  ? 1.5569 1.4475 1.3972 -0.1979 -0.0061 -0.4140 44  SER A CB  
6    O OG  . SER A 17  ? 1.6492 1.5773 1.4685 -0.1733 -0.0178 -0.4074 44  SER A OG  
7    N N   . PRO A 18  ? 1.3893 1.3058 1.2600 -0.1977 0.0157  -0.3496 45  PRO A N   
8    C CA  . PRO A 18  ? 1.1355 1.0302 0.9952 -0.1889 0.0283  -0.3178 45  PRO A CA  
9    C C   . PRO A 18  ? 1.1273 1.0338 0.9615 -0.1586 0.0220  -0.3002 45  PRO A C   
10   O O   . PRO A 18  ? 1.1934 1.1418 1.0246 -0.1449 0.0084  -0.3067 45  PRO A O   
11   C CB  . PRO A 18  ? 0.8809 0.8093 0.7720 -0.2030 0.0339  -0.3150 45  PRO A CB  
12   C CG  . PRO A 18  ? 1.1446 1.1318 1.0577 -0.2019 0.0161  -0.3387 45  PRO A CG  
13   C CD  . PRO A 18  ? 1.2297 1.2045 1.1331 -0.2061 0.0062  -0.3639 45  PRO A CD  
14   N N   . GLU A 19  ? 0.9135 0.7809 0.7283 -0.1485 0.0316  -0.2776 46  GLU A N   
15   C CA  . GLU A 19  ? 0.8176 0.6940 0.6124 -0.1228 0.0293  -0.2583 46  GLU A CA  
16   C C   . GLU A 19  ? 0.7870 0.6918 0.5931 -0.1194 0.0316  -0.2408 46  GLU A C   
17   O O   . GLU A 19  ? 1.0022 0.8974 0.8227 -0.1348 0.0417  -0.2339 46  GLU A O   
18   C CB  . GLU A 19  ? 0.8221 0.6492 0.5979 -0.1135 0.0374  -0.2431 46  GLU A CB  
19   C CG  . GLU A 19  ? 1.0153 0.8170 0.7798 -0.1099 0.0350  -0.2601 46  GLU A CG  
20   C CD  . GLU A 19  ? 1.1249 0.9578 0.8745 -0.0929 0.0268  -0.2705 46  GLU A CD  
21   O OE1 . GLU A 19  ? 0.9670 0.8206 0.7059 -0.0761 0.0262  -0.2542 46  GLU A OE1 
22   O OE2 . GLU A 19  ? 0.9283 0.7625 0.6742 -0.0970 0.0216  -0.2951 46  GLU A OE2 
23   N N   . SER A 20  ? 0.8513 0.7890 0.6491 -0.0996 0.0232  -0.2338 47  SER A N   
24   C CA  . SER A 20  ? 0.7396 0.7041 0.5484 -0.0934 0.0242  -0.2182 47  SER A CA  
25   C C   . SER A 20  ? 0.7258 0.6568 0.5256 -0.0905 0.0377  -0.1939 47  SER A C   
26   O O   . SER A 20  ? 0.8128 0.7044 0.5949 -0.0872 0.0425  -0.1871 47  SER A O   
27   C CB  . SER A 20  ? 0.7283 0.7267 0.5246 -0.0711 0.0115  -0.2143 47  SER A CB  
28   O OG  . SER A 20  ? 0.8404 0.8160 0.6069 -0.0548 0.0142  -0.2027 47  SER A OG  
29   N N   . PRO A 21  ? 0.7436 0.6899 0.5564 -0.0914 0.0430  -0.1819 48  PRO A N   
30   C CA  . PRO A 21  ? 0.6954 0.6120 0.4958 -0.0870 0.0538  -0.1591 48  PRO A CA  
31   C C   . PRO A 21  ? 0.7486 0.6579 0.5271 -0.0640 0.0500  -0.1451 48  PRO A C   
32   O O   . PRO A 21  ? 0.8267 0.7607 0.5992 -0.0500 0.0408  -0.1488 48  PRO A O   
33   C CB  . PRO A 21  ? 0.6783 0.6233 0.4986 -0.0901 0.0588  -0.1538 48  PRO A CB  
34   C CG  . PRO A 21  ? 0.6873 0.6657 0.5364 -0.1052 0.0551  -0.1758 48  PRO A CG  
35   C CD  . PRO A 21  ? 0.6988 0.6886 0.5415 -0.0988 0.0403  -0.1913 48  PRO A CD  
36   N N   . LEU A 22  ? 0.8364 0.7103 0.6019 -0.0609 0.0573  -0.1291 49  LEU A N   
37   C CA  . LEU A 22  ? 0.6665 0.5350 0.4169 -0.0411 0.0559  -0.1156 49  LEU A CA  
38   C C   . LEU A 22  ? 0.6432 0.5376 0.3977 -0.0307 0.0561  -0.1027 49  LEU A C   
39   O O   . LEU A 22  ? 0.7201 0.6227 0.4867 -0.0388 0.0609  -0.0994 49  LEU A O   
40   C CB  . LEU A 22  ? 0.6730 0.4975 0.4125 -0.0407 0.0608  -0.1042 49  LEU A CB  
41   C CG  . LEU A 22  ? 0.8608 0.6524 0.5956 -0.0464 0.0596  -0.1147 49  LEU A CG  
42   C CD1 . LEU A 22  ? 0.7057 0.4559 0.4312 -0.0421 0.0610  -0.1013 49  LEU A CD1 
43   C CD2 . LEU A 22  ? 0.8672 0.6730 0.5987 -0.0358 0.0548  -0.1279 49  LEU A CD2 
44   N N   . GLN A 23  ? 0.7189 0.6250 0.4629 -0.0132 0.0524  -0.0962 50  GLN A N   
45   C CA  . GLN A 23  ? 0.6612 0.5823 0.4066 -0.0020 0.0533  -0.0817 50  GLN A CA  
46   C C   . GLN A 23  ? 0.6071 0.5003 0.3498 -0.0028 0.0616  -0.0668 50  GLN A C   
47   O O   . GLN A 23  ? 0.8230 0.6852 0.5586 -0.0066 0.0642  -0.0654 50  GLN A O   
48   C CB  . GLN A 23  ? 0.6451 0.5781 0.3755 0.0154  0.0491  -0.0765 50  GLN A CB  
49   C CG  . GLN A 23  ? 0.7209 0.6796 0.4459 0.0182  0.0387  -0.0902 50  GLN A CG  
50   C CD  . GLN A 23  ? 0.7956 0.7634 0.4993 0.0352  0.0355  -0.0815 50  GLN A CD  
51   O OE1 . GLN A 23  ? 0.7546 0.7291 0.4577 0.0452  0.0356  -0.0671 50  GLN A OE1 
52   N NE2 . GLN A 23  ? 0.7749 0.7404 0.4589 0.0379  0.0339  -0.0906 50  GLN A NE2 
53   N N   . ALA A 24  ? 0.7226 0.6266 0.4712 0.0016  0.0644  -0.0566 51  ALA A N   
54   C CA  . ALA A 24  ? 0.5874 0.4667 0.3311 0.0011  0.0710  -0.0435 51  ALA A CA  
55   C C   . ALA A 24  ? 0.7633 0.6260 0.4959 0.0134  0.0704  -0.0346 51  ALA A C   
56   O O   . ALA A 24  ? 0.6611 0.5366 0.3894 0.0238  0.0676  -0.0356 51  ALA A O   
57   C CB  . ALA A 24  ? 0.6875 0.5838 0.4407 0.0043  0.0746  -0.0370 51  ALA A CB  
58   N N   . PRO A 25  ? 0.7991 0.6333 0.5264 0.0117  0.0729  -0.0266 52  PRO A N   
59   C CA  . PRO A 25  ? 0.7608 0.5829 0.4846 0.0227  0.0722  -0.0202 52  PRO A CA  
60   C C   . PRO A 25  ? 0.7061 0.5453 0.4313 0.0345  0.0747  -0.0112 52  PRO A C   
61   O O   . PRO A 25  ? 0.6911 0.5437 0.4195 0.0354  0.0762  -0.0068 52  PRO A O   
62   C CB  . PRO A 25  ? 0.7147 0.5052 0.4341 0.0180  0.0715  -0.0138 52  PRO A CB  
63   C CG  . PRO A 25  ? 0.8383 0.6264 0.5542 0.0057  0.0749  -0.0131 52  PRO A CG  
64   C CD  . PRO A 25  ? 0.6101 0.4201 0.3329 -0.0011 0.0757  -0.0245 52  PRO A CD  
65   N N   . ARG A 26  ? 0.7437 0.5811 0.4675 0.0434  0.0763  -0.0092 53  ARG A N   
66   C CA  . ARG A 26  ? 0.7451 0.5940 0.4672 0.0536  0.0803  -0.0001 53  ARG A CA  
67   C C   . ARG A 26  ? 0.7697 0.6039 0.4978 0.0552  0.0829  0.0097  53  ARG A C   
68   O O   . ARG A 26  ? 0.8003 0.6175 0.5338 0.0542  0.0819  0.0088  53  ARG A O   
69   C CB  . ARG A 26  ? 0.6506 0.5038 0.3668 0.0598  0.0841  -0.0037 53  ARG A CB  
70   C CG  . ARG A 26  ? 0.7013 0.5680 0.4080 0.0583  0.0806  -0.0153 53  ARG A CG  
71   C CD  . ARG A 26  ? 0.6702 0.5305 0.3745 0.0592  0.0845  -0.0257 53  ARG A CD  
72   N NE  . ARG A 26  ? 0.8316 0.6763 0.5449 0.0519  0.0803  -0.0361 53  ARG A NE  
73   C CZ  . ARG A 26  ? 0.7391 0.5809 0.4504 0.0503  0.0800  -0.0505 53  ARG A CZ  
74   N NH1 . ARG A 26  ? 0.8020 0.6572 0.5006 0.0547  0.0843  -0.0576 53  ARG A NH1 
75   N NH2 . ARG A 26  ? 0.9553 0.7776 0.6748 0.0440  0.0755  -0.0581 53  ARG A NH2 
76   N N   . VAL A 27  ? 0.8306 0.6714 0.5593 0.0585  0.0848  0.0179  54  VAL A N   
77   C CA  . VAL A 27  ? 0.7693 0.5965 0.5029 0.0589  0.0867  0.0254  54  VAL A CA  
78   C C   . VAL A 27  ? 0.7307 0.5634 0.4650 0.0678  0.0921  0.0345  54  VAL A C   
79   O O   . VAL A 27  ? 0.7468 0.5935 0.4762 0.0735  0.0924  0.0377  54  VAL A O   
80   C CB  . VAL A 27  ? 0.6345 0.4587 0.3675 0.0525  0.0858  0.0251  54  VAL A CB  
81   C CG1 . VAL A 27  ? 0.6699 0.4785 0.4043 0.0527  0.0873  0.0312  54  VAL A CG1 
82   C CG2 . VAL A 27  ? 0.7497 0.5641 0.4781 0.0416  0.0824  0.0176  54  VAL A CG2 
83   N N   . LEU A 28  ? 0.7577 0.5781 0.4988 0.0690  0.0955  0.0386  55  LEU A N   
84   C CA  . LEU A 28  ? 0.7572 0.5764 0.5002 0.0747  0.1021  0.0478  55  LEU A CA  
85   C C   . LEU A 28  ? 0.7308 0.5382 0.4800 0.0727  0.1010  0.0507  55  LEU A C   
86   O O   . LEU A 28  ? 0.7227 0.5177 0.4780 0.0678  0.0974  0.0471  55  LEU A O   
87   C CB  . LEU A 28  ? 0.6617 0.4771 0.4112 0.0755  0.1091  0.0483  55  LEU A CB  
88   C CG  . LEU A 28  ? 0.7625 0.5716 0.5154 0.0784  0.1180  0.0580  55  LEU A CG  
89   C CD1 . LEU A 28  ? 0.7280 0.5427 0.4627 0.0851  0.1227  0.0670  55  LEU A CD1 
90   C CD2 . LEU A 28  ? 0.7192 0.5241 0.4880 0.0754  0.1255  0.0553  55  LEU A CD2 
91   N N   . ILE A 29  ? 0.6652 0.4760 0.4123 0.0775  0.1031  0.0562  56  ILE A N   
92   C CA  . ILE A 29  ? 0.7133 0.5128 0.4654 0.0764  0.1039  0.0576  56  ILE A CA  
93   C C   . ILE A 29  ? 0.7447 0.5334 0.5033 0.0795  0.1101  0.0646  56  ILE A C   
94   O O   . ILE A 29  ? 0.8355 0.6261 0.5904 0.0864  0.1152  0.0727  56  ILE A O   
95   C CB  . ILE A 29  ? 0.8393 0.6484 0.5904 0.0805  0.1039  0.0575  56  ILE A CB  
96   C CG1 . ILE A 29  ? 0.7872 0.6098 0.5353 0.0753  0.0998  0.0495  56  ILE A CG1 
97   C CG2 . ILE A 29  ? 0.7294 0.5260 0.4845 0.0787  0.1063  0.0562  56  ILE A CG2 
98   C CD1 . ILE A 29  ? 0.6421 0.4791 0.3962 0.0782  0.1005  0.0463  56  ILE A CD1 
99   N N   . ALA A 30  ? 0.7463 0.5223 0.5139 0.0740  0.1090  0.0613  57  ALA A N   
100  C CA  . ALA A 30  ? 0.6898 0.4558 0.4687 0.0739  0.1153  0.0653  57  ALA A CA  
101  C C   . ALA A 30  ? 0.7413 0.4948 0.5225 0.0739  0.1156  0.0656  57  ALA A C   
102  O O   . ALA A 30  ? 0.7616 0.5087 0.5410 0.0693  0.1092  0.0586  57  ALA A O   
103  C CB  . ALA A 30  ? 0.6273 0.3908 0.4208 0.0681  0.1124  0.0588  57  ALA A CB  
104  N N   . LEU A 31  ? 0.8108 0.5579 0.5934 0.0790  0.1234  0.0736  58  LEU A N   
105  C CA  . LEU A 31  ? 0.7652 0.4994 0.5503 0.0810  0.1249  0.0734  58  LEU A CA  
106  C C   . LEU A 31  ? 0.8122 0.5300 0.6089 0.0788  0.1326  0.0776  58  LEU A C   
107  O O   . LEU A 31  ? 0.8080 0.5207 0.6016 0.0834  0.1407  0.0884  58  LEU A O   
108  C CB  . LEU A 31  ? 0.6566 0.3967 0.4341 0.0914  0.1258  0.0783  58  LEU A CB  
109  C CG  . LEU A 31  ? 0.9566 0.6833 0.7392 0.0962  0.1287  0.0775  58  LEU A CG  
110  C CD1 . LEU A 31  ? 0.9329 0.6578 0.7157 0.0897  0.1257  0.0647  58  LEU A CD1 
111  C CD2 . LEU A 31  ? 0.9159 0.6497 0.6957 0.1097  0.1285  0.0838  58  LEU A CD2 
112  N N   . LEU A 32  ? 0.7591 0.4672 0.5674 0.0710  0.1297  0.0691  59  LEU A N   
113  C CA  . LEU A 32  ? 0.8345 0.5258 0.6571 0.0671  0.1367  0.0701  59  LEU A CA  
114  C C   . LEU A 32  ? 0.8451 0.5211 0.6645 0.0710  0.1375  0.0683  59  LEU A C   
115  O O   . LEU A 32  ? 0.8287 0.5049 0.6423 0.0698  0.1304  0.0586  59  LEU A O   
116  C CB  . LEU A 32  ? 0.7979 0.4889 0.6389 0.0567  0.1311  0.0592  59  LEU A CB  
117  C CG  . LEU A 32  ? 0.7912 0.4986 0.6398 0.0535  0.1254  0.0549  59  LEU A CG  
118  C CD1 . LEU A 32  ? 0.8536 0.5597 0.7281 0.0450  0.1198  0.0440  59  LEU A CD1 
119  C CD2 . LEU A 32  ? 0.8747 0.5922 0.7216 0.0562  0.1365  0.0640  59  LEU A CD2 
120  N N   . ALA A 33  ? 0.7150 0.3756 0.5365 0.0757  0.1469  0.0775  60  ALA A N   
121  C CA  . ALA A 33  ? 0.7460 0.3910 0.5662 0.0822  0.1485  0.0759  60  ALA A CA  
122  C C   . ALA A 33  ? 0.8430 0.4621 0.6762 0.0775  0.1568  0.0775  60  ALA A C   
123  O O   . ALA A 33  ? 0.8369 0.4446 0.6700 0.0783  0.1661  0.0905  60  ALA A O   
124  C CB  . ALA A 33  ? 0.9115 0.5610 0.7203 0.0970  0.1494  0.0863  60  ALA A CB  
125  N N   . ARG A 34  ? 0.8449 0.4525 0.6866 0.0715  0.1540  0.0639  61  ARG A N   
126  C CA  . ARG A 34  ? 0.8825 0.4629 0.7373 0.0672  0.1614  0.0624  61  ARG A CA  
127  C C   . ARG A 34  ? 0.8601 0.4274 0.7118 0.0731  0.1596  0.0520  61  ARG A C   
128  O O   . ARG A 34  ? 0.8983 0.4738 0.7446 0.0693  0.1517  0.0373  61  ARG A O   
129  C CB  . ARG A 34  ? 0.7661 0.3451 0.6403 0.0512  0.1597  0.0520  61  ARG A CB  
130  C CG  . ARG A 34  ? 0.7936 0.3440 0.6839 0.0445  0.1677  0.0484  61  ARG A CG  
131  C CD  . ARG A 34  ? 0.7295 0.2817 0.6430 0.0285  0.1626  0.0327  61  ARG A CD  
132  N NE  . ARG A 34  ? 0.8636 0.3874 0.7938 0.0209  0.1710  0.0281  61  ARG A NE  
133  C CZ  . ARG A 34  ? 0.8444 0.3649 0.7979 0.0067  0.1666  0.0117  61  ARG A CZ  
134  N NH1 . ARG A 34  ? 0.9177 0.4614 0.8809 0.0000  0.1519  -0.0013 61  ARG A NH1 
135  N NH2 . ARG A 34  ? 0.8366 0.3286 0.8049 -0.0004 0.1757  0.0077  61  ARG A NH2 
136  N N   . ASN A 35  ? 0.8632 0.4082 0.7164 0.0824  0.1673  0.0593  62  ASN A N   
137  C CA  . ASN A 35  ? 0.8911 0.4214 0.7453 0.0897  0.1679  0.0484  62  ASN A CA  
138  C C   . ASN A 35  ? 0.9574 0.5118 0.8006 0.0965  0.1620  0.0395  62  ASN A C   
139  O O   . ASN A 35  ? 0.8533 0.4083 0.6928 0.0916  0.1597  0.0222  62  ASN A O   
140  C CB  . ASN A 35  ? 0.8452 0.3564 0.7103 0.0766  0.1681  0.0317  62  ASN A CB  
141  C CG  . ASN A 35  ? 0.9001 0.3852 0.7805 0.0686  0.1766  0.0389  62  ASN A CG  
142  O OD1 . ASN A 35  ? 0.9750 0.4394 0.8551 0.0772  0.1851  0.0540  62  ASN A OD1 
143  N ND2 . ASN A 35  ? 1.0096 0.4946 0.9037 0.0518  0.1741  0.0280  62  ASN A ND2 
144  N N   . ALA A 36  ? 0.8673 0.4414 0.7039 0.1069  0.1602  0.0510  63  ALA A N   
145  C CA  . ALA A 36  ? 0.8877 0.4881 0.7167 0.1113  0.1561  0.0435  63  ALA A CA  
146  C C   . ALA A 36  ? 0.8914 0.4982 0.7256 0.1297  0.1575  0.0475  63  ALA A C   
147  O O   . ALA A 36  ? 0.9263 0.5587 0.7587 0.1335  0.1552  0.0421  63  ALA A O   
148  C CB  . ALA A 36  ? 0.8065 0.4313 0.6261 0.1049  0.1501  0.0491  63  ALA A CB  
149  N N   . ALA A 37  ? 0.9779 0.5612 0.8199 0.1412  0.1608  0.0564  64  ALA A N   
150  C CA  . ALA A 37  ? 0.9889 0.5781 0.8379 0.1617  0.1586  0.0616  64  ALA A CA  
151  C C   . ALA A 37  ? 0.8983 0.5034 0.7588 0.1675  0.1608  0.0421  64  ALA A C   
152  O O   . ALA A 37  ? 0.9614 0.5886 0.8312 0.1815  0.1572  0.0416  64  ALA A O   
153  C CB  . ALA A 37  ? 0.8935 0.4465 0.7468 0.1730  0.1612  0.0742  64  ALA A CB  
154  N N   . HIS A 38  ? 0.8765 0.4715 0.7367 0.1564  0.1669  0.0246  65  HIS A N   
155  C CA  . HIS A 38  ? 0.7538 0.3631 0.6209 0.1591  0.1725  0.0043  65  HIS A CA  
156  C C   . HIS A 38  ? 0.8521 0.4975 0.7116 0.1525  0.1709  -0.0003 65  HIS A C   
157  O O   . HIS A 38  ? 0.8692 0.5354 0.7394 0.1583  0.1761  -0.0129 65  HIS A O   
158  C CB  . HIS A 38  ? 0.8056 0.3931 0.6660 0.1466  0.1789  -0.0133 65  HIS A CB  
159  C CG  . HIS A 38  ? 0.8328 0.4193 0.6730 0.1260  0.1746  -0.0141 65  HIS A CG  
160  N ND1 . HIS A 38  ? 1.0133 0.5828 0.8518 0.1181  0.1698  -0.0030 65  HIS A ND1 
161  C CD2 . HIS A 38  ? 0.9316 0.5313 0.7530 0.1124  0.1737  -0.0247 65  HIS A CD2 
162  C CE1 . HIS A 38  ? 1.0072 0.5822 0.8309 0.1021  0.1644  -0.0080 65  HIS A CE1 
163  N NE2 . HIS A 38  ? 1.0129 0.6038 0.8233 0.0988  0.1657  -0.0199 65  HIS A NE2 
164  N N   . ALA A 39  ? 0.9267 0.5797 0.7702 0.1400  0.1649  0.0089  66  ALA A N   
165  C CA  . ALA A 39  ? 0.8697 0.5503 0.7028 0.1307  0.1635  0.0047  66  ALA A CA  
166  C C   . ALA A 39  ? 0.9007 0.6051 0.7374 0.1375  0.1562  0.0180  66  ALA A C   
167  O O   . ALA A 39  ? 0.8140 0.5452 0.6523 0.1354  0.1567  0.0120  66  ALA A O   
168  C CB  . ALA A 39  ? 0.7358 0.4069 0.5469 0.1117  0.1604  0.0026  66  ALA A CB  
169  N N   . LEU A 40  ? 0.8283 0.5228 0.6649 0.1441  0.1504  0.0351  67  LEU A N   
170  C CA  . LEU A 40  ? 0.8444 0.5588 0.6783 0.1493  0.1426  0.0475  67  LEU A CA  
171  C C   . LEU A 40  ? 0.7958 0.5395 0.6447 0.1617  0.1396  0.0424  67  LEU A C   
172  O O   . LEU A 40  ? 0.7805 0.5494 0.6260 0.1572  0.1352  0.0421  67  LEU A O   
173  C CB  . LEU A 40  ? 0.8265 0.5205 0.6555 0.1568  0.1396  0.0663  67  LEU A CB  
174  C CG  . LEU A 40  ? 0.9063 0.5797 0.7244 0.1427  0.1425  0.0723  67  LEU A CG  
175  C CD1 . LEU A 40  ? 0.8750 0.5268 0.6881 0.1496  0.1434  0.0907  67  LEU A CD1 
176  C CD2 . LEU A 40  ? 0.6970 0.3893 0.5049 0.1297  0.1390  0.0708  67  LEU A CD2 
177  N N   . PRO A 41  ? 0.9047 0.6480 0.7734 0.1776  0.1411  0.0371  68  PRO A N   
178  C CA  . PRO A 41  ? 0.8850 0.6621 0.7746 0.1897  0.1367  0.0300  68  PRO A CA  
179  C C   . PRO A 41  ? 0.8716 0.6780 0.7641 0.1752  0.1428  0.0141  68  PRO A C   
180  O O   . PRO A 41  ? 0.9585 0.7954 0.8597 0.1771  0.1367  0.0128  68  PRO A O   
181  C CB  . PRO A 41  ? 0.6876 0.4553 0.6009 0.2068  0.1403  0.0220  68  PRO A CB  
182  C CG  . PRO A 41  ? 0.7091 0.4348 0.6097 0.2095  0.1406  0.0350  68  PRO A CG  
183  C CD  . PRO A 41  ? 0.8370 0.5494 0.7132 0.1868  0.1453  0.0373  68  PRO A CD  
184  N N   . THR A 42  ? 0.7798 0.5756 0.6627 0.1600  0.1546  0.0021  69  THR A N   
185  C CA  . THR A 42  ? 0.8065 0.6231 0.6847 0.1438  0.1621  -0.0108 69  THR A CA  
186  C C   . THR A 42  ? 0.8557 0.6692 0.7082 0.1281  0.1565  -0.0016 69  THR A C   
187  O O   . THR A 42  ? 0.8439 0.6803 0.6966 0.1204  0.1559  -0.0049 69  THR A O   
188  C CB  . THR A 42  ? 0.7758 0.5790 0.6477 0.1341  0.1769  -0.0272 69  THR A CB  
189  O OG1 . THR A 42  ? 0.8814 0.6917 0.7819 0.1495  0.1837  -0.0390 69  THR A OG1 
190  C CG2 . THR A 42  ? 0.8959 0.7133 0.7544 0.1151  0.1863  -0.0381 69  THR A CG2 
191  N N   . THR A 43  ? 0.8918 0.6778 0.7253 0.1233  0.1524  0.0088  70  THR A N   
192  C CA  . THR A 43  ? 0.7420 0.5245 0.5550 0.1102  0.1467  0.0160  70  THR A CA  
193  C C   . THR A 43  ? 0.7857 0.5876 0.6030 0.1163  0.1376  0.0261  70  THR A C   
194  O O   . THR A 43  ? 0.7297 0.5461 0.5405 0.1070  0.1355  0.0242  70  THR A O   
195  C CB  . THR A 43  ? 0.7539 0.5069 0.5541 0.1056  0.1441  0.0229  70  THR A CB  
196  O OG1 . THR A 43  ? 0.9023 0.6387 0.6911 0.0953  0.1498  0.0115  70  THR A OG1 
197  C CG2 . THR A 43  ? 1.1092 0.8621 0.8967 0.0974  0.1365  0.0319  70  THR A CG2 
198  N N   . LEU A 44  ? 0.7786 0.5782 0.6041 0.1316  0.1321  0.0370  71  LEU A N   
199  C CA  . LEU A 44  ? 0.8374 0.6543 0.6624 0.1385  0.1226  0.0459  71  LEU A CA  
200  C C   . LEU A 44  ? 0.9115 0.7623 0.7541 0.1425  0.1200  0.0356  71  LEU A C   
201  O O   . LEU A 44  ? 0.7542 0.6239 0.5940 0.1403  0.1131  0.0368  71  LEU A O   
202  C CB  . LEU A 44  ? 0.7887 0.5910 0.6126 0.1543  0.1174  0.0609  71  LEU A CB  
203  C CG  . LEU A 44  ? 0.8282 0.5987 0.6380 0.1486  0.1216  0.0710  71  LEU A CG  
204  C CD1 . LEU A 44  ? 0.7556 0.5070 0.5623 0.1630  0.1193  0.0864  71  LEU A CD1 
205  C CD2 . LEU A 44  ? 0.8281 0.6012 0.6230 0.1354  0.1204  0.0742  71  LEU A CD2 
206  N N   . GLY A 45  ? 0.7925 0.6526 0.6558 0.1479  0.1262  0.0235  72  GLY A N   
207  C CA  . GLY A 45  ? 0.8014 0.6975 0.6879 0.1494  0.1261  0.0104  72  GLY A CA  
208  C C   . GLY A 45  ? 0.8484 0.7556 0.7259 0.1283  0.1325  0.0014  72  GLY A C   
209  O O   . GLY A 45  ? 0.7875 0.7227 0.6763 0.1255  0.1283  -0.0042 72  GLY A O   
210  N N   . ALA A 46  ? 0.8228 0.7061 0.6787 0.1129  0.1417  0.0001  73  ALA A N   
211  C CA  . ALA A 46  ? 0.7608 0.6461 0.6015 0.0929  0.1467  -0.0054 73  ALA A CA  
212  C C   . ALA A 46  ? 0.7798 0.6651 0.6071 0.0893  0.1355  0.0046  73  ALA A C   
213  O O   . ALA A 46  ? 0.8702 0.7718 0.6989 0.0796  0.1352  -0.0008 73  ALA A O   
214  C CB  . ALA A 46  ? 0.6306 0.4861 0.4465 0.0796  0.1556  -0.0078 73  ALA A CB  
215  N N   . LEU A 47  ? 0.7800 0.6469 0.5955 0.0962  0.1278  0.0179  74  LEU A N   
216  C CA  . LEU A 47  ? 0.8107 0.6764 0.6130 0.0927  0.1194  0.0258  74  LEU A CA  
217  C C   . LEU A 47  ? 0.8139 0.7080 0.6283 0.1003  0.1111  0.0249  74  LEU A C   
218  O O   . LEU A 47  ? 0.7356 0.6387 0.5444 0.0918  0.1075  0.0222  74  LEU A O   
219  C CB  . LEU A 47  ? 0.7664 0.6090 0.5574 0.0983  0.1160  0.0385  74  LEU A CB  
220  C CG  . LEU A 47  ? 0.8636 0.6788 0.6434 0.0899  0.1204  0.0389  74  LEU A CG  
221  C CD1 . LEU A 47  ? 0.7727 0.5710 0.5487 0.0948  0.1179  0.0500  74  LEU A CD1 
222  C CD2 . LEU A 47  ? 0.7160 0.5250 0.4813 0.0744  0.1199  0.0339  74  LEU A CD2 
223  N N   . GLU A 48  ? 0.7940 0.7011 0.6246 0.1170  0.1065  0.0265  75  GLU A N   
224  C CA  . GLU A 48  ? 0.8181 0.7523 0.6588 0.1263  0.0949  0.0255  75  GLU A CA  
225  C C   . GLU A 48  ? 0.8786 0.8436 0.7395 0.1170  0.0967  0.0090  75  GLU A C   
226  O O   . GLU A 48  ? 0.9433 0.9314 0.8104 0.1190  0.0864  0.0054  75  GLU A O   
227  C CB  . GLU A 48  ? 0.6688 0.6068 0.5216 0.1482  0.0872  0.0317  75  GLU A CB  
228  C CG  . GLU A 48  ? 0.8971 0.8511 0.7808 0.1549  0.0920  0.0194  75  GLU A CG  
229  C CD  . GLU A 48  ? 0.9879 0.9388 0.8828 0.1788  0.0831  0.0269  75  GLU A CD  
230  O OE1 . GLU A 48  ? 0.8131 0.7360 0.6856 0.1863  0.0791  0.0438  75  GLU A OE1 
231  O OE2 . GLU A 48  ? 0.9230 0.8985 0.8498 0.1899  0.0803  0.0157  75  GLU A OE2 
232  N N   . ARG A 49  ? 0.7643 0.7294 0.6343 0.1056  0.1102  -0.0018 76  ARG A N   
233  C CA  . ARG A 49  ? 0.7569 0.7491 0.6465 0.0933  0.1164  -0.0181 76  ARG A CA  
234  C C   . ARG A 49  ? 0.7724 0.7496 0.6405 0.0706  0.1239  -0.0201 76  ARG A C   
235  O O   . ARG A 49  ? 0.6501 0.6410 0.5291 0.0558  0.1339  -0.0329 76  ARG A O   
236  C CB  . ARG A 49  ? 0.6091 0.6129 0.5234 0.0947  0.1294  -0.0305 76  ARG A CB  
237  C CG  . ARG A 49  ? 0.7601 0.7836 0.7038 0.1187  0.1205  -0.0318 76  ARG A CG  
238  C CD  . ARG A 49  ? 0.6630 0.7045 0.6386 0.1198  0.1346  -0.0487 76  ARG A CD  
239  N NE  . ARG A 49  ? 0.9223 0.9324 0.8805 0.1156  0.1491  -0.0473 76  ARG A NE  
240  C CZ  . ARG A 49  ? 0.9386 0.9324 0.8999 0.1325  0.1474  -0.0421 76  ARG A CZ  
241  N NH1 . ARG A 49  ? 0.8456 0.8482 0.8244 0.1556  0.1319  -0.0356 76  ARG A NH1 
242  N NH2 . ARG A 49  ? 0.8854 0.8509 0.8297 0.1259  0.1607  -0.0435 76  ARG A NH2 
243  N N   . LEU A 50  ? 0.8111 0.7597 0.6503 0.0675  0.1197  -0.0082 77  LEU A N   
244  C CA  . LEU A 50  ? 0.7833 0.7153 0.6023 0.0490  0.1232  -0.0091 77  LEU A CA  
245  C C   . LEU A 50  ? 0.6287 0.5840 0.4585 0.0421  0.1182  -0.0175 77  LEU A C   
246  O O   . LEU A 50  ? 0.8228 0.7981 0.6627 0.0535  0.1063  -0.0170 77  LEU A O   
247  C CB  . LEU A 50  ? 0.7520 0.6542 0.5457 0.0507  0.1169  0.0037  77  LEU A CB  
248  C CG  . LEU A 50  ? 0.8013 0.6736 0.5789 0.0493  0.1220  0.0095  77  LEU A CG  
249  C CD1 . LEU A 50  ? 0.6312 0.4820 0.3930 0.0518  0.1143  0.0197  77  LEU A CD1 
250  C CD2 . LEU A 50  ? 0.6919 0.5497 0.4559 0.0321  0.1320  0.0029  77  LEU A CD2 
251  N N   . ARG A 51  ? 0.7536 0.7039 0.5788 0.0225  0.1274  -0.0253 78  ARG A N   
252  C CA  . ARG A 51  ? 0.7846 0.7530 0.6200 0.0122  0.1241  -0.0348 78  ARG A CA  
253  C C   . ARG A 51  ? 0.8742 0.8190 0.6851 0.0092  0.1154  -0.0275 78  ARG A C   
254  O O   . ARG A 51  ? 0.8891 0.8114 0.6838 -0.0066 0.1200  -0.0284 78  ARG A O   
255  C CB  . ARG A 51  ? 0.7029 0.6749 0.5456 -0.0089 0.1402  -0.0468 78  ARG A CB  
256  C CG  . ARG A 51  ? 0.6526 0.6638 0.5336 -0.0062 0.1475  -0.0608 78  ARG A CG  
257  C CD  . ARG A 51  ? 0.7787 0.7982 0.6707 -0.0303 0.1655  -0.0750 78  ARG A CD  
258  N NE  . ARG A 51  ? 0.8775 0.8644 0.7421 -0.0439 0.1838  -0.0714 78  ARG A NE  
259  C CZ  . ARG A 51  ? 0.9395 0.9336 0.8136 -0.0425 0.1982  -0.0772 78  ARG A CZ  
260  N NH1 . ARG A 51  ? 0.8989 0.9316 0.8134 -0.0269 0.1964  -0.0868 78  ARG A NH1 
261  N NH2 . ARG A 51  ? 1.0127 0.9730 0.8538 -0.0564 0.2141  -0.0738 78  ARG A NH2 
262  N N   . HIS A 52  ? 0.7309 0.6794 0.5387 0.0254  0.1032  -0.0202 79  HIS A N   
263  C CA  . HIS A 52  ? 0.7442 0.6776 0.5344 0.0261  0.0952  -0.0155 79  HIS A CA  
264  C C   . HIS A 52  ? 0.7573 0.7143 0.5540 0.0419  0.0836  -0.0147 79  HIS A C   
265  O O   . HIS A 52  ? 0.8419 0.8058 0.6433 0.0566  0.0813  -0.0078 79  HIS A O   
266  C CB  . HIS A 52  ? 0.7687 0.6686 0.5377 0.0289  0.0964  -0.0034 79  HIS A CB  
267  C CG  . HIS A 52  ? 0.8485 0.7353 0.6046 0.0302  0.0898  -0.0009 79  HIS A CG  
268  N ND1 . HIS A 52  ? 0.8901 0.7829 0.6431 0.0435  0.0841  0.0046  79  HIS A ND1 
269  C CD2 . HIS A 52  ? 0.7565 0.6233 0.5020 0.0200  0.0889  -0.0037 79  HIS A CD2 
270  C CE1 . HIS A 52  ? 0.8556 0.7358 0.5988 0.0412  0.0815  0.0034  79  HIS A CE1 
271  N NE2 . HIS A 52  ? 0.8707 0.7350 0.6108 0.0280  0.0832  -0.0018 79  HIS A NE2 
272  N N   . PRO A 53  ? 0.7694 0.7363 0.5639 0.0395  0.0758  -0.0216 80  PRO A N   
273  C CA  . PRO A 53  ? 0.8286 0.8195 0.6254 0.0535  0.0632  -0.0226 80  PRO A CA  
274  C C   . PRO A 53  ? 0.8326 0.8099 0.6115 0.0696  0.0609  -0.0071 80  PRO A C   
275  O O   . PRO A 53  ? 0.9449 0.8970 0.7067 0.0681  0.0658  0.0004  80  PRO A O   
276  C CB  . PRO A 53  ? 0.6514 0.6451 0.4412 0.0450  0.0575  -0.0330 80  PRO A CB  
277  C CG  . PRO A 53  ? 0.6359 0.6170 0.4318 0.0251  0.0669  -0.0409 80  PRO A CG  
278  C CD  . PRO A 53  ? 0.6265 0.5810 0.4145 0.0235  0.0775  -0.0296 80  PRO A CD  
279  N N   . ARG A 54  ? 0.7956 0.7894 0.5803 0.0850  0.0535  -0.0027 81  ARG A N   
280  C CA  . ARG A 54  ? 0.8555 0.8328 0.6229 0.0992  0.0532  0.0135  81  ARG A CA  
281  C C   . ARG A 54  ? 0.7940 0.7622 0.5344 0.1019  0.0499  0.0178  81  ARG A C   
282  O O   . ARG A 54  ? 0.8662 0.8122 0.5900 0.1053  0.0567  0.0296  81  ARG A O   
283  C CB  . ARG A 54  ? 0.8146 0.8082 0.5929 0.1161  0.0445  0.0176  81  ARG A CB  
284  C CG  . ARG A 54  ? 0.8397 0.8313 0.6395 0.1175  0.0525  0.0181  81  ARG A CG  
285  C CD  . ARG A 54  ? 0.8866 0.8973 0.7034 0.1357  0.0420  0.0191  81  ARG A CD  
286  N NE  . ARG A 54  ? 1.0346 1.0389 0.8696 0.1390  0.0514  0.0200  81  ARG A NE  
287  C CZ  . ARG A 54  ? 1.0223 1.0442 0.8820 0.1533  0.0454  0.0167  81  ARG A CZ  
288  N NH1 . ARG A 54  ? 0.9848 1.0332 0.8554 0.1665  0.0279  0.0129  81  ARG A NH1 
289  N NH2 . ARG A 54  ? 1.0826 1.0955 0.9571 0.1552  0.0563  0.0159  81  ARG A NH2 
290  N N   . GLU A 55  ? 0.8125 0.7983 0.5488 0.0996  0.0405  0.0069  82  GLU A N   
291  C CA  . GLU A 55  ? 0.7768 0.7539 0.4853 0.1009  0.0393  0.0083  82  GLU A CA  
292  C C   . GLU A 55  ? 0.7752 0.7308 0.4796 0.0889  0.0511  0.0058  82  GLU A C   
293  O O   . GLU A 55  ? 0.8965 0.8410 0.5806 0.0903  0.0548  0.0079  82  GLU A O   
294  C CB  . GLU A 55  ? 0.6386 0.6399 0.3433 0.1010  0.0251  -0.0054 82  GLU A CB  
295  C CG  . GLU A 55  ? 0.7360 0.7480 0.4603 0.0845  0.0251  -0.0239 82  GLU A CG  
296  C CD  . GLU A 55  ? 1.1690 1.2010 0.9272 0.0799  0.0237  -0.0311 82  GLU A CD  
297  O OE1 . GLU A 55  ? 1.1893 1.2264 0.9578 0.0904  0.0230  -0.0223 82  GLU A OE1 
298  O OE2 . GLU A 55  ? 1.1965 1.2383 0.9717 0.0651  0.0246  -0.0463 82  GLU A OE2 
299  N N   . ARG A 56  ? 0.7274 0.6761 0.4497 0.0775  0.0569  0.0011  83  ARG A N   
300  C CA  . ARG A 56  ? 0.7131 0.6380 0.4331 0.0686  0.0654  0.0008  83  ARG A CA  
301  C C   . ARG A 56  ? 0.8395 0.7455 0.5623 0.0711  0.0733  0.0131  83  ARG A C   
302  O O   . ARG A 56  ? 0.7097 0.5968 0.4349 0.0640  0.0778  0.0127  83  ARG A O   
303  C CB  . ARG A 56  ? 0.8447 0.7681 0.5763 0.0539  0.0654  -0.0114 83  ARG A CB  
304  C CG  . ARG A 56  ? 0.8396 0.7824 0.5727 0.0492  0.0575  -0.0260 83  ARG A CG  
305  C CD  . ARG A 56  ? 0.5883 0.5273 0.3029 0.0532  0.0555  -0.0300 83  ARG A CD  
306  N NE  . ARG A 56  ? 0.7264 0.6430 0.4399 0.0445  0.0605  -0.0359 83  ARG A NE  
307  C CZ  . ARG A 56  ? 0.7593 0.6697 0.4611 0.0460  0.0613  -0.0428 83  ARG A CZ  
308  N NH1 . ARG A 56  ? 0.7579 0.6816 0.4429 0.0544  0.0588  -0.0441 83  ARG A NH1 
309  N NH2 . ARG A 56  ? 0.8577 0.7465 0.5631 0.0395  0.0647  -0.0487 83  ARG A NH2 
310  N N   . THR A 57  ? 0.8529 0.7625 0.5752 0.0816  0.0735  0.0234  84  THR A N   
311  C CA  . THR A 57  ? 0.7006 0.5929 0.4265 0.0840  0.0805  0.0338  84  THR A CA  
312  C C   . THR A 57  ? 0.7044 0.5899 0.4171 0.0945  0.0835  0.0459  84  THR A C   
313  O O   . THR A 57  ? 0.7789 0.6753 0.4804 0.1036  0.0780  0.0494  84  THR A O   
314  C CB  . THR A 57  ? 0.7555 0.6540 0.4959 0.0851  0.0804  0.0340  84  THR A CB  
315  O OG1 . THR A 57  ? 0.8537 0.7585 0.6038 0.0732  0.0803  0.0227  84  THR A OG1 
316  C CG2 . THR A 57  ? 0.8257 0.7040 0.5686 0.0861  0.0874  0.0423  84  THR A CG2 
317  N N   . ALA A 58  ? 0.7912 0.6579 0.5046 0.0928  0.0919  0.0520  85  ALA A N   
318  C CA  . ALA A 58  ? 0.7607 0.6170 0.4634 0.0997  0.0985  0.0639  85  ALA A CA  
319  C C   . ALA A 58  ? 0.7130 0.5534 0.4275 0.0996  0.1040  0.0708  85  ALA A C   
320  O O   . ALA A 58  ? 0.7036 0.5385 0.4314 0.0928  0.1037  0.0653  85  ALA A O   
321  C CB  . ALA A 58  ? 0.6842 0.5351 0.3785 0.0960  0.1062  0.0620  85  ALA A CB  
322  N N   . LEU A 59  ? 0.6819 0.5122 0.3887 0.1068  0.1089  0.0830  86  LEU A N   
323  C CA  . LEU A 59  ? 0.7568 0.5710 0.4744 0.1077  0.1137  0.0893  86  LEU A CA  
324  C C   . LEU A 59  ? 0.7750 0.5722 0.4912 0.1041  0.1256  0.0962  86  LEU A C   
325  O O   . LEU A 59  ? 0.8933 0.6878 0.5922 0.1063  0.1317  0.1031  86  LEU A O   
326  C CB  . LEU A 59  ? 0.6802 0.4940 0.3944 0.1197  0.1092  0.0972  86  LEU A CB  
327  C CG  . LEU A 59  ? 0.8235 0.6588 0.5457 0.1238  0.0984  0.0887  86  LEU A CG  
328  C CD1 . LEU A 59  ? 0.7303 0.5659 0.4534 0.1385  0.0928  0.0961  86  LEU A CD1 
329  C CD2 . LEU A 59  ? 0.7424 0.5800 0.4819 0.1140  0.0996  0.0773  86  LEU A CD2 
330  N N   . TRP A 60  ? 0.7547 0.5406 0.4885 0.0977  0.1294  0.0934  87  TRP A N   
331  C CA  . TRP A 60  ? 0.7045 0.4764 0.4459 0.0923  0.1409  0.0973  87  TRP A CA  
332  C C   . TRP A 60  ? 0.8164 0.5722 0.5700 0.0920  0.1421  0.0998  87  TRP A C   
333  O O   . TRP A 60  ? 0.7988 0.5543 0.5658 0.0876  0.1362  0.0908  87  TRP A O   
334  C CB  . TRP A 60  ? 0.7892 0.5672 0.5460 0.0835  0.1419  0.0861  87  TRP A CB  
335  C CG  . TRP A 60  ? 0.7876 0.5587 0.5564 0.0775  0.1552  0.0873  87  TRP A CG  
336  C CD1 . TRP A 60  ? 0.7416 0.5176 0.5046 0.0754  0.1667  0.0877  87  TRP A CD1 
337  C CD2 . TRP A 60  ? 0.7513 0.5107 0.5419 0.0714  0.1597  0.0861  87  TRP A CD2 
338  N NE1 . TRP A 60  ? 0.6993 0.4689 0.4818 0.0678  0.1797  0.0870  87  TRP A NE1 
339  C CE2 . TRP A 60  ? 0.7398 0.4996 0.5409 0.0652  0.1746  0.0859  87  TRP A CE2 
340  C CE3 . TRP A 60  ? 0.7057 0.4548 0.5082 0.0699  0.1532  0.0838  87  TRP A CE3 
341  C CZ2 . TRP A 60  ? 0.7899 0.5419 0.6169 0.0570  0.1825  0.0831  87  TRP A CZ2 
342  C CZ3 . TRP A 60  ? 0.6679 0.4075 0.4926 0.0625  0.1593  0.0811  87  TRP A CZ3 
343  C CH2 . TRP A 60  ? 0.6759 0.4178 0.5147 0.0559  0.1734  0.0807  87  TRP A CH2 
344  N N   . VAL A 61  ? 0.8452 0.5849 0.5913 0.0965  0.1496  0.1120  88  VAL A N   
345  C CA  . VAL A 61  ? 0.8231 0.5449 0.5789 0.0980  0.1509  0.1145  88  VAL A CA  
346  C C   . VAL A 61  ? 0.8360 0.5377 0.5982 0.0910  0.1648  0.1209  88  VAL A C   
347  O O   . VAL A 61  ? 0.9271 0.6205 0.6733 0.0919  0.1746  0.1325  88  VAL A O   
348  C CB  . VAL A 61  ? 0.8120 0.5295 0.5556 0.1118  0.1456  0.1229  88  VAL A CB  
349  C CG1 . VAL A 61  ? 0.7098 0.4078 0.4657 0.1138  0.1475  0.1230  88  VAL A CG1 
350  C CG2 . VAL A 61  ? 0.7901 0.5318 0.5319 0.1171  0.1335  0.1149  88  VAL A CG2 
351  N N   . ALA A 62  ? 0.7821 0.4751 0.5661 0.0831  0.1659  0.1129  89  ALA A N   
352  C CA  . ALA A 62  ? 0.8253 0.5000 0.6224 0.0742  0.1789  0.1160  89  ALA A CA  
353  C C   . ALA A 62  ? 0.9316 0.5864 0.7390 0.0746  0.1773  0.1139  89  ALA A C   
354  O O   . ALA A 62  ? 0.9158 0.5764 0.7332 0.0735  0.1670  0.1015  89  ALA A O   
355  C CB  . ALA A 62  ? 0.6455 0.3330 0.4666 0.0618  0.1814  0.1038  89  ALA A CB  
356  N N   . THR A 63  ? 0.9127 0.5415 0.7148 0.0759  0.1879  0.1260  90  THR A N   
357  C CA  . THR A 63  ? 0.8259 0.4316 0.6385 0.0763  0.1882  0.1236  90  THR A CA  
358  C C   . THR A 63  ? 0.8048 0.3856 0.6285 0.0647  0.2042  0.1289  90  THR A C   
359  O O   . THR A 63  ? 0.9494 0.5229 0.7616 0.0613  0.2172  0.1415  90  THR A O   
360  C CB  . THR A 63  ? 0.7984 0.3923 0.5939 0.0933  0.1829  0.1329  90  THR A CB  
361  O OG1 . THR A 63  ? 1.0014 0.5786 0.8104 0.0944  0.1809  0.1245  90  THR A OG1 
362  C CG2 . THR A 63  ? 1.0007 0.5710 0.7747 0.0996  0.1922  0.1539  90  THR A CG2 
363  N N   . ASP A 64  ? 0.8114 0.3787 0.6568 0.0573  0.2040  0.1180  91  ASP A N   
364  C CA  . ASP A 64  ? 0.9933 0.5363 0.8553 0.0439  0.2189  0.1196  91  ASP A CA  
365  C C   . ASP A 64  ? 0.8476 0.3779 0.7303 0.0392  0.2130  0.1042  91  ASP A C   
366  O O   . ASP A 64  ? 0.8168 0.3612 0.7010 0.0438  0.1981  0.0909  91  ASP A O   
367  C CB  . ASP A 64  ? 0.8393 0.4000 0.7207 0.0283  0.2284  0.1142  91  ASP A CB  
368  C CG  . ASP A 64  ? 0.7822 0.3768 0.6814 0.0258  0.2132  0.0958  91  ASP A CG  
369  O OD1 . ASP A 64  ? 0.8694 0.4656 0.7921 0.0187  0.2046  0.0796  91  ASP A OD1 
370  O OD2 . ASP A 64  ? 0.8533 0.4707 0.7408 0.0312  0.2089  0.0975  91  ASP A OD2 
371  N N   . HIS A 65  ? 0.9201 0.4216 0.8167 0.0288  0.2257  0.1058  92  HIS A N   
372  C CA  . HIS A 65  ? 0.9789 0.4645 0.8964 0.0220  0.2218  0.0898  92  HIS A CA  
373  C C   . HIS A 65  ? 0.9508 0.4256 0.8531 0.0379  0.2113  0.0871  92  HIS A C   
374  O O   . HIS A 65  ? 0.9748 0.4571 0.8848 0.0370  0.1998  0.0687  92  HIS A O   
375  C CB  . HIS A 65  ? 0.8297 0.3420 0.7744 0.0093  0.2112  0.0676  92  HIS A CB  
376  C CG  . HIS A 65  ? 0.9543 0.4795 0.9241 -0.0065 0.2220  0.0659  92  HIS A CG  
377  N ND1 . HIS A 65  ? 0.8133 0.3686 0.7822 -0.0059 0.2215  0.0684  92  HIS A ND1 
378  C CD2 . HIS A 65  ? 0.9929 0.5058 0.9923 -0.0241 0.2352  0.0606  92  HIS A CD2 
379  C CE1 . HIS A 65  ? 0.7668 0.3296 0.7648 -0.0215 0.2343  0.0639  92  HIS A CE1 
380  N NE2 . HIS A 65  ? 0.8503 0.3886 0.8681 -0.0335 0.2431  0.0593  92  HIS A NE2 
381  N N   . ASN A 66  ? 1.0040 0.4608 0.8842 0.0530  0.2154  0.1050  93  ASN A N   
382  C CA  . ASN A 66  ? 0.9313 0.3819 0.8008 0.0706  0.2066  0.1028  93  ASN A CA  
383  C C   . ASN A 66  ? 1.0636 0.4710 0.9392 0.0729  0.2139  0.1041  93  ASN A C   
384  O O   . ASN A 66  ? 1.1678 0.5568 1.0392 0.0709  0.2219  0.1192  93  ASN A O   
385  C CB  . ASN A 66  ? 0.8387 0.3004 0.6840 0.0888  0.2024  0.1195  93  ASN A CB  
386  C CG  . ASN A 66  ? 0.9744 0.4782 0.8139 0.0889  0.1928  0.1142  93  ASN A CG  
387  O OD1 . ASN A 66  ? 1.0542 0.5778 0.9023 0.0845  0.1843  0.0967  93  ASN A OD1 
388  N ND2 . ASN A 66  ? 0.9696 0.4845 0.7916 0.0939  0.1940  0.1293  93  ASN A ND2 
389  N N   . MET A 67  ? 1.0675 0.4704 0.9529 0.0752  0.2078  0.0854  94  MET A N   
390  C CA  . MET A 67  ? 1.0594 0.4318 0.9517 0.0802  0.2101  0.0826  94  MET A CA  
391  C C   . MET A 67  ? 1.1306 0.5029 1.0117 0.1042  0.2037  0.0882  94  MET A C   
392  O O   . MET A 67  ? 1.2632 0.6134 1.1504 0.1116  0.2034  0.0876  94  MET A O   
393  C CB  . MET A 67  ? 0.9206 0.2844 0.8303 0.0689  0.2084  0.0567  94  MET A CB  
394  C CG  . MET A 67  ? 1.3805 0.7143 1.3040 0.0649  0.2120  0.0517  94  MET A CG  
395  S SD  . MET A 67  ? 1.4355 0.7514 1.3711 0.0452  0.2239  0.0650  94  MET A SD  
396  C CE  . MET A 67  ? 1.1564 0.4931 1.1112 0.0222  0.2243  0.0480  94  MET A CE  
397  N N   . ASP A 68  ? 1.1432 0.5398 1.0108 0.1167  0.1982  0.0928  95  ASP A N   
398  C CA  . ASP A 68  ? 1.0329 0.4355 0.8944 0.1402  0.1915  0.0972  95  ASP A CA  
399  C C   . ASP A 68  ? 1.0057 0.4199 0.8487 0.1497  0.1876  0.1203  95  ASP A C   
400  O O   . ASP A 68  ? 1.1896 0.6033 1.0230 0.1377  0.1924  0.1330  95  ASP A O   
401  C CB  . ASP A 68  ? 0.9619 0.3977 0.8280 0.1435  0.1848  0.0763  95  ASP A CB  
402  C CG  . ASP A 68  ? 1.1273 0.6023 0.9850 0.1324  0.1794  0.0741  95  ASP A CG  
403  O OD1 . ASP A 68  ? 1.1476 0.6254 0.9992 0.1228  0.1813  0.0865  95  ASP A OD1 
404  O OD2 . ASP A 68  ? 1.0828 0.5846 0.9400 0.1329  0.1745  0.0593  95  ASP A OD2 
405  N N   . ASN A 69  ? 1.0216 0.4477 0.8603 0.1715  0.1791  0.1241  96  ASN A N   
406  C CA  . ASN A 69  ? 1.0148 0.4530 0.8342 0.1829  0.1720  0.1440  96  ASN A CA  
407  C C   . ASN A 69  ? 1.0007 0.4840 0.8144 0.1778  0.1663  0.1389  96  ASN A C   
408  O O   . ASN A 69  ? 1.1017 0.6076 0.9082 0.1920  0.1562  0.1442  96  ASN A O   
409  C CB  . ASN A 69  ? 0.9981 0.4326 0.8208 0.2080  0.1610  0.1488  96  ASN A CB  
410  C CG  . ASN A 69  ? 1.1241 0.5844 0.9663 0.2209  0.1563  0.1289  96  ASN A CG  
411  O OD1 . ASN A 69  ? 1.0408 0.5173 0.8950 0.2073  0.1613  0.1082  96  ASN A OD1 
412  N ND2 . ASN A 69  ? 1.0230 0.4941 0.8700 0.2447  0.1448  0.1328  96  ASN A ND2 
413  N N   . THR A 70  ? 1.0193 0.5177 0.8378 0.1573  0.1709  0.1273  97  THR A N   
414  C CA  . THR A 70  ? 0.8426 0.3807 0.6554 0.1510  0.1652  0.1227  97  THR A CA  
415  C C   . THR A 70  ? 0.9010 0.4445 0.6929 0.1549  0.1636  0.1419  97  THR A C   
416  O O   . THR A 70  ? 0.9854 0.5587 0.7702 0.1616  0.1548  0.1418  97  THR A O   
417  C CB  . THR A 70  ? 0.8946 0.4404 0.7153 0.1296  0.1691  0.1097  97  THR A CB  
418  O OG1 . THR A 70  ? 0.9333 0.4783 0.7666 0.1264  0.1680  0.0900  97  THR A OG1 
419  C CG2 . THR A 70  ? 0.7924 0.3728 0.6056 0.1233  0.1636  0.1077  97  THR A CG2 
420  N N   . SER A 71  ? 0.9892 0.5031 0.7698 0.1497  0.1731  0.1578  98  SER A N   
421  C CA  . SER A 71  ? 0.8749 0.3903 0.6297 0.1514  0.1741  0.1758  98  SER A CA  
422  C C   . SER A 71  ? 1.0036 0.5219 0.7419 0.1743  0.1611  0.1872  98  SER A C   
423  O O   . SER A 71  ? 1.1404 0.6811 0.8613 0.1782  0.1543  0.1924  98  SER A O   
424  C CB  . SER A 71  ? 1.0535 0.5353 0.7996 0.1399  0.1888  0.1893  98  SER A CB  
425  O OG  . SER A 71  ? 1.3786 0.8695 1.1014 0.1349  0.1926  0.2009  98  SER A OG  
426  N N   . THR A 72  ? 1.0931 0.5897 0.8384 0.1903  0.1563  0.1895  99  THR A N   
427  C CA  . THR A 72  ? 1.0027 0.5019 0.7366 0.2142  0.1411  0.1997  99  THR A CA  
428  C C   . THR A 72  ? 0.9114 0.4583 0.6618 0.2221  0.1281  0.1830  99  THR A C   
429  O O   . THR A 72  ? 1.0302 0.5965 0.7681 0.2346  0.1150  0.1892  99  THR A O   
430  C CB  . THR A 72  ? 1.0851 0.5569 0.8310 0.2260  0.1370  0.2016  99  THR A CB  
431  O OG1 . THR A 72  ? 1.2488 0.6887 0.9874 0.2101  0.1481  0.2102  99  THR A OG1 
432  C CG2 . THR A 72  ? 0.9798 0.4540 0.7144 0.2502  0.1183  0.2132  99  THR A CG2 
433  N N   . VAL A 73  ? 0.8727 0.4387 0.6498 0.2137  0.1317  0.1613  100 VAL A N   
434  C CA  . VAL A 73  ? 1.0761 0.6859 0.8690 0.2175  0.1229  0.1445  100 VAL A CA  
435  C C   . VAL A 73  ? 1.0193 0.6583 0.7975 0.2069  0.1199  0.1453  100 VAL A C   
436  O O   . VAL A 73  ? 1.0180 0.6861 0.7959 0.2160  0.1083  0.1433  100 VAL A O   
437  C CB  . VAL A 73  ? 0.9728 0.5907 0.7895 0.2077  0.1303  0.1222  100 VAL A CB  
438  C CG1 . VAL A 73  ? 0.9556 0.6166 0.7860 0.2083  0.1248  0.1055  100 VAL A CG1 
439  C CG2 . VAL A 73  ? 0.9112 0.5003 0.7434 0.2192  0.1336  0.1189  100 VAL A CG2 
440  N N   . LEU A 74  ? 0.9861 0.6184 0.7549 0.1878  0.1299  0.1465  101 LEU A N   
441  C CA  . LEU A 74  ? 0.9369 0.5935 0.6928 0.1781  0.1281  0.1464  101 LEU A CA  
442  C C   . LEU A 74  ? 0.9908 0.6462 0.7205 0.1891  0.1210  0.1632  101 LEU A C   
443  O O   . LEU A 74  ? 1.0774 0.7616 0.8009 0.1913  0.1119  0.1597  101 LEU A O   
444  C CB  . LEU A 74  ? 0.8456 0.4925 0.6002 0.1580  0.1401  0.1448  101 LEU A CB  
445  C CG  . LEU A 74  ? 0.9613 0.6174 0.7352 0.1445  0.1428  0.1264  101 LEU A CG  
446  C CD1 . LEU A 74  ? 0.8377 0.4802 0.6142 0.1280  0.1526  0.1265  101 LEU A CD1 
447  C CD2 . LEU A 74  ? 0.6693 0.3595 0.4449 0.1413  0.1353  0.1147  101 LEU A CD2 
448  N N   . ARG A 75  ? 0.9519 0.5717 0.6636 0.1956  0.1250  0.1816  102 ARG A N   
449  C CA  . ARG A 75  ? 0.9767 0.5893 0.6547 0.2056  0.1184  0.1995  102 ARG A CA  
450  C C   . ARG A 75  ? 0.9703 0.6024 0.6506 0.2275  0.0977  0.1987  102 ARG A C   
451  O O   . ARG A 75  ? 1.1066 0.7565 0.7667 0.2329  0.0868  0.2025  102 ARG A O   
452  C CB  . ARG A 75  ? 0.9693 0.5332 0.6242 0.2069  0.1284  0.2208  102 ARG A CB  
453  C CG  . ARG A 75  ? 1.0385 0.5969 0.6552 0.2076  0.1252  0.2360  102 ARG A CG  
454  C CD  . ARG A 75  ? 1.2046 0.7265 0.8087 0.1997  0.1348  0.2488  102 ARG A CD  
455  N NE  . ARG A 75  ? 1.5096 1.0184 1.1340 0.1796  0.1551  0.2425  102 ARG A NE  
456  C CZ  . ARG A 75  ? 1.5410 1.0275 1.1878 0.1786  0.1596  0.2398  102 ARG A CZ  
457  N NH1 . ARG A 75  ? 1.4196 0.8927 1.0726 0.1967  0.1468  0.2429  102 ARG A NH1 
458  N NH2 . ARG A 75  ? 1.4399 0.9178 1.1054 0.1592  0.1767  0.2325  102 ARG A NH2 
459  N N   . GLU A 76  ? 0.9977 0.6285 0.7046 0.2405  0.0918  0.1918  103 GLU A N   
460  C CA  . GLU A 76  ? 1.0028 0.6581 0.7218 0.2617  0.0720  0.1871  103 GLU A CA  
461  C C   . GLU A 76  ? 1.0706 0.7758 0.8049 0.2544  0.0661  0.1685  103 GLU A C   
462  O O   . GLU A 76  ? 1.1461 0.8753 0.8750 0.2655  0.0496  0.1684  103 GLU A O   
463  C CB  . GLU A 76  ? 1.1821 0.8290 0.9335 0.2753  0.0705  0.1791  103 GLU A CB  
464  C CG  . GLU A 76  ? 1.3508 1.0282 1.1257 0.2978  0.0509  0.1703  103 GLU A CG  
465  C CD  . GLU A 76  ? 1.5832 1.2583 1.3965 0.3089  0.0531  0.1568  103 GLU A CD  
466  O OE1 . GLU A 76  ? 1.6074 1.2643 1.4295 0.2955  0.0703  0.1499  103 GLU A OE1 
467  O OE2 . GLU A 76  ? 1.4651 1.1576 1.3011 0.3314  0.0373  0.1516  103 GLU A OE2 
468  N N   . TRP A 77  ? 0.9653 0.6845 0.7173 0.2354  0.0786  0.1526  104 TRP A N   
469  C CA  . TRP A 77  ? 0.9935 0.7540 0.7579 0.2261  0.0752  0.1357  104 TRP A CA  
470  C C   . TRP A 77  ? 0.8737 0.6429 0.6101 0.2185  0.0721  0.1419  104 TRP A C   
471  O O   . TRP A 77  ? 0.9217 0.7217 0.6598 0.2217  0.0602  0.1348  104 TRP A O   
472  C CB  . TRP A 77  ? 0.8443 0.6089 0.6267 0.2078  0.0890  0.1201  104 TRP A CB  
473  C CG  . TRP A 77  ? 0.9090 0.7097 0.7035 0.1970  0.0874  0.1032  104 TRP A CG  
474  C CD1 . TRP A 77  ? 0.9783 0.8099 0.7975 0.2024  0.0817  0.0886  104 TRP A CD1 
475  C CD2 . TRP A 77  ? 0.7869 0.5947 0.5710 0.1783  0.0927  0.0986  104 TRP A CD2 
476  N NE1 . TRP A 77  ? 0.9221 0.7769 0.7438 0.1866  0.0842  0.0764  104 TRP A NE1 
477  C CE2 . TRP A 77  ? 0.7907 0.6299 0.5902 0.1727  0.0898  0.0828  104 TRP A CE2 
478  C CE3 . TRP A 77  ? 0.8524 0.6430 0.6182 0.1660  0.0999  0.1056  104 TRP A CE3 
479  C CZ2 . TRP A 77  ? 0.8232 0.6723 0.6164 0.1559  0.0928  0.0755  104 TRP A CZ2 
480  C CZ3 . TRP A 77  ? 0.9118 0.7158 0.6751 0.1511  0.1017  0.0970  104 TRP A CZ3 
481  C CH2 . TRP A 77  ? 0.8465 0.6771 0.6215 0.1465  0.0976  0.0830  104 TRP A CH2 
482  N N   . LEU A 78  ? 0.8834 0.6267 0.5958 0.2078  0.0836  0.1536  105 LEU A N   
483  C CA  . LEU A 78  ? 0.9983 0.7493 0.6849 0.1994  0.0840  0.1571  105 LEU A CA  
484  C C   . LEU A 78  ? 1.0323 0.7854 0.6917 0.2153  0.0688  0.1685  105 LEU A C   
485  O O   . LEU A 78  ? 0.9698 0.7472 0.6188 0.2133  0.0606  0.1623  105 LEU A O   
486  C CB  . LEU A 78  ? 0.9174 0.6407 0.5883 0.1854  0.1017  0.1662  105 LEU A CB  
487  C CG  . LEU A 78  ? 0.8446 0.5723 0.5376 0.1672  0.1135  0.1528  105 LEU A CG  
488  C CD1 . LEU A 78  ? 0.8492 0.5538 0.5310 0.1548  0.1295  0.1609  105 LEU A CD1 
489  C CD2 . LEU A 78  ? 0.8021 0.5624 0.5030 0.1592  0.1082  0.1372  105 LEU A CD2 
490  N N   . VAL A 79  ? 0.9930 0.7185 0.6387 0.2314  0.0635  0.1850  106 VAL A N   
491  C CA  . VAL A 79  ? 1.0070 0.7308 0.6226 0.2488  0.0455  0.1973  106 VAL A CA  
492  C C   . VAL A 79  ? 0.9719 0.7387 0.6115 0.2599  0.0244  0.1814  106 VAL A C   
493  O O   . VAL A 79  ? 1.1025 0.8852 0.7208 0.2664  0.0089  0.1822  106 VAL A O   
494  C CB  . VAL A 79  ? 0.9182 0.5996 0.5165 0.2656  0.0424  0.2185  106 VAL A CB  
495  C CG1 . VAL A 79  ? 0.9656 0.6459 0.5350 0.2878  0.0179  0.2305  106 VAL A CG1 
496  C CG2 . VAL A 79  ? 0.9445 0.5831 0.5134 0.2520  0.0644  0.2352  106 VAL A CG2 
497  N N   . ALA A 80  ? 0.9895 0.7771 0.6740 0.2607  0.0245  0.1651  107 ALA A N   
498  C CA  . ALA A 80  ? 0.9304 0.7610 0.6450 0.2698  0.0073  0.1480  107 ALA A CA  
499  C C   . ALA A 80  ? 0.9936 0.8592 0.7177 0.2514  0.0104  0.1299  107 ALA A C   
500  O O   . ALA A 80  ? 1.1418 1.0430 0.8811 0.2567  -0.0052 0.1174  107 ALA A O   
501  C CB  . ALA A 80  ? 0.9969 0.8353 0.7560 0.2780  0.0090  0.1368  107 ALA A CB  
502  N N   . VAL A 81  ? 0.8243 0.6802 0.5418 0.2304  0.0290  0.1274  108 VAL A N   
503  C CA  . VAL A 81  ? 0.9812 0.8642 0.7079 0.2129  0.0326  0.1108  108 VAL A CA  
504  C C   . VAL A 81  ? 0.9160 0.7923 0.6080 0.2033  0.0354  0.1160  108 VAL A C   
505  O O   . VAL A 81  ? 0.9751 0.8716 0.6721 0.1903  0.0365  0.1024  108 VAL A O   
506  C CB  . VAL A 81  ? 0.9299 0.8110 0.6800 0.1966  0.0495  0.1000  108 VAL A CB  
507  C CG1 . VAL A 81  ? 0.7966 0.6839 0.5793 0.2051  0.0496  0.0927  108 VAL A CG1 
508  C CG2 . VAL A 81  ? 0.8063 0.6534 0.5379 0.1866  0.0650  0.1110  108 VAL A CG2 
509  N N   . LYS A 82  ? 0.9902 0.8374 0.6468 0.2087  0.0380  0.1344  109 LYS A N   
510  C CA  . LYS A 82  ? 0.9298 0.7689 0.5538 0.1980  0.0456  0.1380  109 LYS A CA  
511  C C   . LYS A 82  ? 1.0241 0.8925 0.6392 0.1979  0.0315  0.1263  109 LYS A C   
512  O O   . LYS A 82  ? 1.0214 0.8995 0.6348 0.1835  0.0384  0.1154  109 LYS A O   
513  C CB  . LYS A 82  ? 0.9488 0.7522 0.5329 0.2052  0.0504  0.1604  109 LYS A CB  
514  C CG  . LYS A 82  ? 1.0863 0.8815 0.6333 0.1952  0.0601  0.1640  109 LYS A CG  
515  C CD  . LYS A 82  ? 1.2748 1.0310 0.7808 0.1999  0.0689  0.1871  109 LYS A CD  
516  C CE  . LYS A 82  ? 1.3750 1.1241 0.8418 0.1896  0.0812  0.1893  109 LYS A CE  
517  N NZ  . LYS A 82  ? 1.2804 1.0372 0.7703 0.1702  0.1012  0.1761  109 LYS A NZ  
518  N N   . SER A 83  ? 1.1014 0.9845 0.7135 0.2144  0.0102  0.1269  110 SER A N   
519  C CA  . SER A 83  ? 0.9792 0.8878 0.5775 0.2160  -0.0063 0.1168  110 SER A CA  
520  C C   . SER A 83  ? 0.9618 0.9058 0.5975 0.2033  -0.0077 0.0928  110 SER A C   
521  O O   . SER A 83  ? 1.1481 1.1158 0.7793 0.2013  -0.0203 0.0803  110 SER A O   
522  C CB  . SER A 83  ? 0.9148 0.8304 0.5031 0.2387  -0.0320 0.1234  110 SER A CB  
523  O OG  . SER A 83  ? 1.0696 1.0076 0.7053 0.2478  -0.0415 0.1142  110 SER A OG  
524  N N   . LEU A 84  ? 0.8580 0.8036 0.5284 0.1938  0.0053  0.0861  111 LEU A N   
525  C CA  . LEU A 84  ? 0.9508 0.9242 0.6542 0.1803  0.0065  0.0653  111 LEU A CA  
526  C C   . LEU A 84  ? 0.9283 0.8904 0.6273 0.1605  0.0234  0.0600  111 LEU A C   
527  O O   . LEU A 84  ? 0.9333 0.9132 0.6499 0.1479  0.0239  0.0439  111 LEU A O   
528  C CB  . LEU A 84  ? 0.7663 0.7507 0.5102 0.1828  0.0089  0.0591  111 LEU A CB  
529  C CG  . LEU A 84  ? 0.9562 0.9437 0.7107 0.2048  -0.0039 0.0665  111 LEU A CG  
530  C CD1 . LEU A 84  ? 0.9815 0.9810 0.7785 0.2040  0.0033  0.0562  111 LEU A CD1 
531  C CD2 . LEU A 84  ? 1.0492 1.0639 0.8021 0.2183  -0.0286 0.0613  111 LEU A CD2 
532  N N   . TYR A 85  ? 0.9130 0.8457 0.5910 0.1575  0.0368  0.0725  112 TYR A N   
533  C CA  . TYR A 85  ? 0.8383 0.7599 0.5180 0.1412  0.0515  0.0675  112 TYR A CA  
534  C C   . TYR A 85  ? 0.9134 0.8261 0.5627 0.1378  0.0556  0.0694  112 TYR A C   
535  O O   . TYR A 85  ? 0.8763 0.7836 0.4965 0.1473  0.0510  0.0788  112 TYR A O   
536  C CB  . TYR A 85  ? 0.7117 0.6100 0.4010 0.1384  0.0650  0.0761  112 TYR A CB  
537  C CG  . TYR A 85  ? 0.9003 0.8061 0.6191 0.1374  0.0649  0.0698  112 TYR A CG  
538  C CD1 . TYR A 85  ? 0.8754 0.7871 0.6052 0.1510  0.0581  0.0737  112 TYR A CD1 
539  C CD2 . TYR A 85  ? 0.7559 0.6616 0.4899 0.1232  0.0719  0.0595  112 TYR A CD2 
540  C CE1 . TYR A 85  ? 0.8660 0.7859 0.6235 0.1497  0.0606  0.0656  112 TYR A CE1 
541  C CE2 . TYR A 85  ? 0.8805 0.7916 0.6362 0.1208  0.0742  0.0532  112 TYR A CE2 
542  C CZ  . TYR A 85  ? 0.7283 0.6479 0.4969 0.1337  0.0698  0.0553  112 TYR A CZ  
543  O OH  . TYR A 85  ? 0.7334 0.6595 0.5245 0.1309  0.0747  0.0469  112 TYR A OH  
544  N N   . HIS A 86  ? 0.8381 0.7480 0.4934 0.1243  0.0644  0.0598  113 HIS A N   
545  C CA  . HIS A 86  ? 0.8195 0.7233 0.4516 0.1202  0.0705  0.0574  113 HIS A CA  
546  C C   . HIS A 86  ? 0.7994 0.6813 0.4092 0.1246  0.0824  0.0733  113 HIS A C   
547  O O   . HIS A 86  ? 0.8159 0.6942 0.3937 0.1282  0.0837  0.0771  113 HIS A O   
548  C CB  . HIS A 86  ? 0.8124 0.7134 0.4610 0.1069  0.0780  0.0451  113 HIS A CB  
549  C CG  . HIS A 86  ? 0.8650 0.7594 0.4969 0.1031  0.0869  0.0406  113 HIS A CG  
550  N ND1 . HIS A 86  ? 0.7652 0.6706 0.3806 0.1020  0.0815  0.0290  113 HIS A ND1 
551  C CD2 . HIS A 86  ? 0.7493 0.6285 0.3809 0.0998  0.1016  0.0440  113 HIS A CD2 
552  C CE1 . HIS A 86  ? 0.7540 0.6505 0.3582 0.0987  0.0937  0.0255  113 HIS A CE1 
553  N NE2 . HIS A 86  ? 0.9174 0.7992 0.5331 0.0973  0.1063  0.0344  113 HIS A NE2 
554  N N   . SER A 87  ? 0.7030 0.5689 0.3275 0.1233  0.0921  0.0821  114 SER A N   
555  C CA  . SER A 87  ? 0.7895 0.6332 0.3973 0.1251  0.1054  0.0969  114 SER A CA  
556  C C   . SER A 87  ? 0.7045 0.5341 0.3338 0.1255  0.1100  0.1048  114 SER A C   
557  O O   . SER A 87  ? 0.8412 0.6767 0.4976 0.1210  0.1070  0.0966  114 SER A O   
558  C CB  . SER A 87  ? 0.7535 0.5914 0.3572 0.1152  0.1210  0.0915  114 SER A CB  
559  O OG  . SER A 87  ? 1.0323 0.8709 0.6685 0.1063  0.1252  0.0819  114 SER A OG  
560  N N   . VAL A 88  ? 0.8032 0.6116 0.4171 0.1302  0.1179  0.1208  115 VAL A N   
561  C CA  . VAL A 88  ? 0.8643 0.6551 0.4957 0.1304  0.1237  0.1285  115 VAL A CA  
562  C C   . VAL A 88  ? 0.7887 0.5580 0.4132 0.1227  0.1429  0.1368  115 VAL A C   
563  O O   . VAL A 88  ? 0.8883 0.6463 0.4814 0.1244  0.1503  0.1472  115 VAL A O   
564  C CB  . VAL A 88  ? 0.7876 0.5705 0.4114 0.1451  0.1134  0.1402  115 VAL A CB  
565  C CG1 . VAL A 88  ? 0.9121 0.6726 0.5523 0.1448  0.1214  0.1475  115 VAL A CG1 
566  C CG2 . VAL A 88  ? 0.8358 0.6448 0.4747 0.1519  0.0960  0.1293  115 VAL A CG2 
567  N N   . GLU A 89  ? 0.7990 0.5628 0.4518 0.1134  0.1511  0.1315  116 GLU A N   
568  C CA  . GLU A 89  ? 0.8789 0.6239 0.5350 0.1050  0.1694  0.1377  116 GLU A CA  
569  C C   . GLU A 89  ? 0.9655 0.6913 0.6372 0.1061  0.1705  0.1444  116 GLU A C   
570  O O   . GLU A 89  ? 0.9187 0.6508 0.6130 0.1066  0.1612  0.1358  116 GLU A O   
571  C CB  . GLU A 89  ? 0.9427 0.6990 0.6230 0.0929  0.1776  0.1233  116 GLU A CB  
572  C CG  . GLU A 89  ? 1.0197 0.7620 0.7072 0.0830  0.1984  0.1272  116 GLU A CG  
573  C CD  . GLU A 89  ? 1.1520 0.9100 0.8600 0.0737  0.2071  0.1123  116 GLU A CD  
574  O OE1 . GLU A 89  ? 1.1202 0.8963 0.8316 0.0758  0.1967  0.1003  116 GLU A OE1 
575  O OE2 . GLU A 89  ? 1.1483 0.9004 0.8714 0.0642  0.2247  0.1117  116 GLU A OE2 
576  N N   . TRP A 90  ? 0.8585 0.5585 0.5157 0.1058  0.1830  0.1593  117 TRP A N   
577  C CA  . TRP A 90  ? 0.8640 0.5401 0.5295 0.1090  0.1838  0.1678  117 TRP A CA  
578  C C   . TRP A 90  ? 0.9939 0.6484 0.6672 0.0958  0.2045  0.1726  117 TRP A C   
579  O O   . TRP A 90  ? 1.1469 0.7861 0.7944 0.0926  0.2188  0.1848  117 TRP A O   
580  C CB  . TRP A 90  ? 0.9821 0.6432 0.6180 0.1253  0.1748  0.1839  117 TRP A CB  
581  C CG  . TRP A 90  ? 1.0448 0.6738 0.6826 0.1305  0.1776  0.1959  117 TRP A CG  
582  C CD1 . TRP A 90  ? 0.8654 0.4642 0.4770 0.1347  0.1830  0.2139  117 TRP A CD1 
583  C CD2 . TRP A 90  ? 0.9825 0.6069 0.6508 0.1314  0.1735  0.1880  117 TRP A CD2 
584  N NE1 . TRP A 90  ? 1.1448 0.7200 0.7713 0.1386  0.1825  0.2179  117 TRP A NE1 
585  C CE2 . TRP A 90  ? 1.1733 0.7611 0.8321 0.1376  0.1783  0.2033  117 TRP A CE2 
586  C CE3 . TRP A 90  ? 1.0473 0.6921 0.7466 0.1273  0.1668  0.1697  117 TRP A CE3 
587  C CZ2 . TRP A 90  ? 1.1358 0.7090 0.8185 0.1400  0.1768  0.1987  117 TRP A CZ2 
588  C CZ3 . TRP A 90  ? 1.1549 0.7858 0.8741 0.1291  0.1656  0.1655  117 TRP A CZ3 
589  C CH2 . TRP A 90  ? 1.0908 0.6873 0.8033 0.1356  0.1707  0.1789  117 TRP A CH2 
590  N N   . ARG A 91  ? 0.9286 0.5821 0.6368 0.0871  0.2066  0.1622  118 ARG A N   
591  C CA  . ARG A 91  ? 0.8281 0.4668 0.5544 0.0723  0.2252  0.1620  118 ARG A CA  
592  C C   . ARG A 91  ? 1.0414 0.6551 0.7820 0.0723  0.2249  0.1649  118 ARG A C   
593  O O   . ARG A 91  ? 0.9702 0.5905 0.7419 0.0666  0.2193  0.1505  118 ARG A O   
594  C CB  . ARG A 91  ? 0.8358 0.4998 0.5956 0.0606  0.2267  0.1428  118 ARG A CB  
595  C CG  . ARG A 91  ? 1.1798 0.8652 0.9286 0.0595  0.2308  0.1385  118 ARG A CG  
596  C CD  . ARG A 91  ? 0.9776 0.6868 0.7633 0.0508  0.2294  0.1188  118 ARG A CD  
597  N NE  . ARG A 91  ? 1.1517 0.8546 0.9721 0.0382  0.2402  0.1128  118 ARG A NE  
598  C CZ  . ARG A 91  ? 1.2555 0.9766 1.1108 0.0290  0.2453  0.0974  118 ARG A CZ  
599  N NH1 . ARG A 91  ? 0.9503 0.6943 0.8093 0.0312  0.2422  0.0873  118 ARG A NH1 
600  N NH2 . ARG A 91  ? 0.9761 0.6928 0.8661 0.0175  0.2530  0.0909  118 ARG A NH2 
601  N N   . PRO A 92  ? 1.0532 0.6356 0.7698 0.0790  0.2297  0.1829  119 PRO A N   
602  C CA  . PRO A 92  ? 0.9991 0.5530 0.7293 0.0789  0.2313  0.1855  119 PRO A CA  
603  C C   . PRO A 92  ? 0.9942 0.5258 0.7382 0.0608  0.2532  0.1879  119 PRO A C   
604  O O   . PRO A 92  ? 1.1575 0.6916 0.8947 0.0498  0.2698  0.1916  119 PRO A O   
605  C CB  . PRO A 92  ? 1.1721 0.7049 0.8706 0.0963  0.2236  0.2030  119 PRO A CB  
606  C CG  . PRO A 92  ? 0.8893 0.4301 0.5568 0.0961  0.2273  0.2122  119 PRO A CG  
607  C CD  . PRO A 92  ? 1.0101 0.5804 0.6829 0.0897  0.2305  0.2016  119 PRO A CD  
608  N N   . ALA A 93  ? 1.0828 0.5928 0.8481 0.0569  0.2543  0.1841  120 ALA A N   
609  C CA  . ALA A 93  ? 1.1289 0.6166 0.9119 0.0387  0.2738  0.1845  120 ALA A CA  
610  C C   . ALA A 93  ? 1.0336 0.4956 0.8285 0.0420  0.2677  0.1825  120 ALA A C   
611  O O   . ALA A 93  ? 1.0562 0.5205 0.8759 0.0410  0.2601  0.1678  120 ALA A O   
612  C CB  . ALA A 93  ? 0.9313 0.4459 0.7539 0.0211  0.2798  0.1647  120 ALA A CB  
613  N N   . GLU A 94  ? 1.1160 0.5529 0.8918 0.0457  0.2704  0.1963  121 GLU A N   
614  C CA  . GLU A 94  ? 1.2612 0.6726 1.0448 0.0521  0.2632  0.1954  121 GLU A CA  
615  C C   . GLU A 94  ? 1.1575 0.5529 0.9746 0.0325  0.2755  0.1839  121 GLU A C   
616  O O   . GLU A 94  ? 1.1401 0.5257 0.9765 0.0345  0.2679  0.1723  121 GLU A O   
617  C CB  . GLU A 94  ? 1.0772 0.4641 0.8287 0.0639  0.2599  0.2149  121 GLU A CB  
618  C CG  . GLU A 94  ? 1.3270 0.7298 1.0464 0.0830  0.2458  0.2253  121 GLU A CG  
619  C CD  . GLU A 94  ? 1.6662 1.0911 1.3955 0.0988  0.2283  0.2147  121 GLU A CD  
620  O OE1 . GLU A 94  ? 1.7170 1.1315 1.4654 0.1045  0.2221  0.2061  121 GLU A OE1 
621  O OE2 . GLU A 94  ? 1.4379 0.8903 1.1557 0.1050  0.2218  0.2139  121 GLU A OE2 
622  N N   . GLU A 95  ? 1.1127 0.5061 0.9384 0.0130  0.2949  0.1852  122 GLU A N   
623  C CA  . GLU A 95  ? 1.1147 0.4962 0.9770 -0.0070 0.3063  0.1723  122 GLU A CA  
624  C C   . GLU A 95  ? 1.1210 0.5292 1.0165 -0.0248 0.3163  0.1569  122 GLU A C   
625  O O   . GLU A 95  ? 1.2176 0.6452 1.1033 -0.0272 0.3249  0.1619  122 GLU A O   
626  C CB  . GLU A 95  ? 1.1915 0.5426 1.0442 -0.0178 0.3226  0.1849  122 GLU A CB  
627  C CG  . GLU A 95  ? 1.2558 0.5736 1.0836 -0.0024 0.3125  0.1984  122 GLU A CG  
628  C CD  . GLU A 95  ? 1.4857 0.7912 1.3387 0.0010  0.3012  0.1840  122 GLU A CD  
629  O OE1 . GLU A 95  ? 1.5488 0.8671 1.4377 -0.0121 0.3026  0.1635  122 GLU A OE1 
630  O OE2 . GLU A 95  ? 1.5219 0.8046 1.3590 0.0170  0.2903  0.1920  122 GLU A OE2 
631  N N   . PRO A 96  ? 1.1182 0.5285 1.0548 -0.0372 0.3144  0.1366  123 PRO A N   
632  C CA  . PRO A 96  ? 1.0362 0.4257 0.9866 -0.0360 0.3042  0.1264  123 PRO A CA  
633  C C   . PRO A 96  ? 1.0599 0.4550 0.9982 -0.0162 0.2823  0.1206  123 PRO A C   
634  O O   . PRO A 96  ? 1.1704 0.5870 1.0951 -0.0058 0.2745  0.1226  123 PRO A O   
635  C CB  . PRO A 96  ? 0.9611 0.3593 0.9614 -0.0593 0.3105  0.1039  123 PRO A CB  
636  C CG  . PRO A 96  ? 1.0339 0.4700 1.0485 -0.0629 0.3096  0.0961  123 PRO A CG  
637  C CD  . PRO A 96  ? 0.9842 0.4201 0.9607 -0.0549 0.3219  0.1196  123 PRO A CD  
638  N N   . ARG A 97  ? 1.0646 0.4407 1.0072 -0.0110 0.2730  0.1126  124 ARG A N   
639  C CA  . ARG A 97  ? 1.0969 0.4781 1.0293 0.0067  0.2550  0.1048  124 ARG A CA  
640  C C   . ARG A 97  ? 1.0328 0.4241 0.9915 -0.0020 0.2450  0.0782  124 ARG A C   
641  O O   . ARG A 97  ? 1.1053 0.5072 1.0550 0.0102  0.2295  0.0680  124 ARG A O   
642  C CB  . ARG A 97  ? 0.9978 0.3534 0.9153 0.0211  0.2504  0.1118  124 ARG A CB  
643  C CG  . ARG A 97  ? 1.2021 0.5459 1.0908 0.0313  0.2555  0.1374  124 ARG A CG  
644  C CD  . ARG A 97  ? 1.0771 0.3990 0.9529 0.0502  0.2462  0.1433  124 ARG A CD  
645  N NE  . ARG A 97  ? 1.4569 0.7520 1.3530 0.0423  0.2485  0.1318  124 ARG A NE  
646  C CZ  . ARG A 97  ? 1.6906 0.9635 1.5839 0.0564  0.2413  0.1316  124 ARG A CZ  
647  N NH1 . ARG A 97  ? 1.6551 0.9305 1.5293 0.0796  0.2309  0.1420  124 ARG A NH1 
648  N NH2 . ARG A 97  ? 1.5307 0.7791 1.4432 0.0471  0.2440  0.1193  124 ARG A NH2 
649  N N   . SER A 98  ? 1.0654 0.4639 1.0568 -0.0231 0.2501  0.0646  125 SER A N   
650  C CA  . SER A 98  ? 0.9237 0.3450 0.9400 -0.0315 0.2337  0.0375  125 SER A CA  
651  C C   . SER A 98  ? 0.9096 0.3548 0.9615 -0.0511 0.2386  0.0281  125 SER A C   
652  O O   . SER A 98  ? 0.9486 0.3801 1.0142 -0.0641 0.2596  0.0373  125 SER A O   
653  C CB  . SER A 98  ? 0.9104 0.3013 0.9366 -0.0354 0.2307  0.0220  125 SER A CB  
654  O OG  . SER A 98  ? 1.1955 0.5564 1.2345 -0.0467 0.2475  0.0289  125 SER A OG  
655  N N   . TYR A 99  ? 0.9265 0.4069 0.9933 -0.0530 0.2194  0.0096  126 TYR A N   
656  C CA  . TYR A 99  ? 0.9021 0.4109 1.0086 -0.0689 0.2204  -0.0025 126 TYR A CA  
657  C C   . TYR A 99  ? 0.9110 0.4042 1.0574 -0.0894 0.2271  -0.0187 126 TYR A C   
658  O O   . TYR A 99  ? 1.0562 0.5281 1.2014 -0.0902 0.2181  -0.0310 126 TYR A O   
659  C CB  . TYR A 99  ? 0.9808 0.5267 1.0922 -0.0635 0.1943  -0.0185 126 TYR A CB  
660  C CG  . TYR A 99  ? 0.9362 0.5029 1.0183 -0.0479 0.1897  -0.0048 126 TYR A CG  
661  C CD1 . TYR A 99  ? 0.7836 0.3432 0.8250 -0.0312 0.1803  0.0029  126 TYR A CD1 
662  C CD2 . TYR A 99  ? 0.7453 0.3398 0.8432 -0.0507 0.1956  -0.0017 126 TYR A CD2 
663  C CE1 . TYR A 99  ? 0.7922 0.3709 0.8094 -0.0187 0.1762  0.0138  126 TYR A CE1 
664  C CE2 . TYR A 99  ? 0.7221 0.3340 0.7936 -0.0372 0.1912  0.0091  126 TYR A CE2 
665  C CZ  . TYR A 99  ? 0.8047 0.4082 0.8361 -0.0217 0.1810  0.0170  126 TYR A CZ  
666  O OH  . TYR A 99  ? 0.8734 0.4942 0.8810 -0.0100 0.1768  0.0262  126 TYR A OH  
667  N N   . PRO A 100 ? 1.0083 0.5122 1.1920 -0.1071 0.2439  -0.0209 127 PRO A N   
668  C CA  . PRO A 100 ? 0.9311 0.4210 1.1577 -0.1292 0.2520  -0.0376 127 PRO A CA  
669  C C   . PRO A 100 ? 0.9148 0.4272 1.1735 -0.1350 0.2246  -0.0688 127 PRO A C   
670  O O   . PRO A 100 ? 1.1134 0.6087 1.3998 -0.1503 0.2255  -0.0852 127 PRO A O   
671  C CB  . PRO A 100 ? 0.8970 0.4015 1.1562 -0.1463 0.2778  -0.0328 127 PRO A CB  
672  C CG  . PRO A 100 ? 0.8869 0.3943 1.1050 -0.1317 0.2890  -0.0066 127 PRO A CG  
673  C CD  . PRO A 100 ? 0.8515 0.3760 1.0378 -0.1088 0.2608  -0.0073 127 PRO A CD  
674  N N   . ASP A 101 ? 0.9522 0.4997 1.2064 -0.1235 0.1993  -0.0775 128 ASP A N   
675  C CA  . ASP A 101 ? 0.9732 0.5414 1.2525 -0.1274 0.1698  -0.1059 128 ASP A CA  
676  C C   . ASP A 101 ? 0.9332 0.4897 1.1671 -0.1116 0.1456  -0.1097 128 ASP A C   
677  O O   . ASP A 101 ? 0.9194 0.4939 1.1583 -0.1101 0.1172  -0.1292 128 ASP A O   
678  C CB  . ASP A 101 ? 0.9602 0.5756 1.2731 -0.1278 0.1570  -0.1157 128 ASP A CB  
679  C CG  . ASP A 101 ? 0.9461 0.5775 1.2198 -0.1071 0.1463  -0.1014 128 ASP A CG  
680  O OD1 . ASP A 101 ? 0.9544 0.5649 1.1816 -0.0952 0.1578  -0.0795 128 ASP A OD1 
681  O OD2 . ASP A 101 ? 0.9849 0.6493 1.2761 -0.1025 0.1255  -0.1126 128 ASP A OD2 
682  N N   . GLU A 102 ? 0.9242 0.4507 1.1135 -0.0996 0.1561  -0.0921 129 GLU A N   
683  C CA  . GLU A 102 ? 0.9316 0.4485 1.0777 -0.0850 0.1380  -0.0955 129 GLU A CA  
684  C C   . GLU A 102 ? 0.9857 0.4720 1.1317 -0.0918 0.1345  -0.1128 129 GLU A C   
685  O O   . GLU A 102 ? 0.9004 0.3618 1.0689 -0.1038 0.1520  -0.1139 129 GLU A O   
686  C CB  . GLU A 102 ? 0.8947 0.4005 0.9972 -0.0671 0.1498  -0.0704 129 GLU A CB  
687  C CG  . GLU A 102 ? 0.8974 0.3631 0.9882 -0.0652 0.1707  -0.0584 129 GLU A CG  
688  C CD  . GLU A 102 ? 0.9343 0.3927 0.9843 -0.0453 0.1772  -0.0365 129 GLU A CD  
689  O OE1 . GLU A 102 ? 0.9534 0.4345 0.9935 -0.0382 0.1787  -0.0219 129 GLU A OE1 
690  O OE2 . GLU A 102 ? 1.0012 0.4324 1.0315 -0.0364 0.1802  -0.0357 129 GLU A OE2 
691  N N   . GLU A 103 ? 1.0237 0.5096 1.1419 -0.0847 0.1126  -0.1270 130 GLU A N   
692  C CA  . GLU A 103 ? 0.9469 0.4032 1.0548 -0.0882 0.1084  -0.1448 130 GLU A CA  
693  C C   . GLU A 103 ? 0.9166 0.3488 0.9799 -0.0718 0.1176  -0.1337 130 GLU A C   
694  O O   . GLU A 103 ? 1.0722 0.4771 1.1247 -0.0725 0.1180  -0.1476 130 GLU A O   
695  C CB  . GLU A 103 ? 0.9158 0.3859 1.0205 -0.0928 0.0777  -0.1713 130 GLU A CB  
696  C CG  . GLU A 103 ? 1.0771 0.5772 1.2297 -0.1062 0.0633  -0.1847 130 GLU A CG  
697  C CD  . GLU A 103 ? 1.2305 0.7464 1.3717 -0.1057 0.0278  -0.2065 130 GLU A CD  
698  O OE1 . GLU A 103 ? 1.0600 0.5597 1.1523 -0.0975 0.0169  -0.2117 130 GLU A OE1 
699  O OE2 . GLU A 103 ? 1.2117 0.7558 1.3922 -0.1133 0.0109  -0.2186 130 GLU A OE2 
700  N N   . GLY A 104 ? 0.8968 0.3401 0.9368 -0.0572 0.1247  -0.1110 131 GLY A N   
701  C CA  . GLY A 104 ? 0.8949 0.3221 0.8989 -0.0407 0.1329  -0.1007 131 GLY A CA  
702  C C   . GLY A 104 ? 0.8978 0.3467 0.8838 -0.0274 0.1368  -0.0777 131 GLY A C   
703  O O   . GLY A 104 ? 0.9324 0.4083 0.9291 -0.0306 0.1311  -0.0718 131 GLY A O   
704  N N   . PRO A 105 ? 0.9795 0.4179 0.9403 -0.0119 0.1462  -0.0657 132 PRO A N   
705  C CA  . PRO A 105 ? 0.8341 0.2940 0.7780 0.0006  0.1488  -0.0453 132 PRO A CA  
706  C C   . PRO A 105 ? 0.9987 0.4860 0.9217 0.0029  0.1319  -0.0512 132 PRO A C   
707  O O   . PRO A 105 ? 0.8108 0.3201 0.7279 0.0081  0.1311  -0.0373 132 PRO A O   
708  C CB  . PRO A 105 ? 0.8477 0.2885 0.7749 0.0164  0.1604  -0.0361 132 PRO A CB  
709  C CG  . PRO A 105 ? 1.0016 0.4196 0.9260 0.0141  0.1584  -0.0576 132 PRO A CG  
710  C CD  . PRO A 105 ? 0.8926 0.3010 0.8425 -0.0045 0.1541  -0.0721 132 PRO A CD  
711  N N   . LYS A 106 ? 0.9139 0.3976 0.8225 -0.0013 0.1186  -0.0712 133 LYS A N   
712  C CA  . LYS A 106 ? 0.8793 0.3824 0.7632 -0.0006 0.1018  -0.0761 133 LYS A CA  
713  C C   . LYS A 106 ? 0.8913 0.4060 0.7912 -0.0123 0.0826  -0.0879 133 LYS A C   
714  O O   . LYS A 106 ? 1.0128 0.5374 0.8903 -0.0124 0.0649  -0.0938 133 LYS A O   
715  C CB  . LYS A 106 ? 0.9594 0.4502 0.8086 0.0031  0.0994  -0.0895 133 LYS A CB  
716  C CG  . LYS A 106 ? 0.9734 0.4576 0.8123 0.0162  0.1172  -0.0807 133 LYS A CG  
717  C CD  . LYS A 106 ? 0.7984 0.3045 0.6355 0.0256  0.1221  -0.0592 133 LYS A CD  
718  C CE  . LYS A 106 ? 1.1328 0.6337 0.9702 0.0397  0.1380  -0.0493 133 LYS A CE  
719  N NZ  . LYS A 106 ? 1.0902 0.6126 0.9272 0.0485  0.1411  -0.0292 133 LYS A NZ  
720  N N   . HIS A 107 ? 0.9703 0.4834 0.9092 -0.0223 0.0855  -0.0914 134 HIS A N   
721  C CA  . HIS A 107 ? 0.8742 0.4037 0.8390 -0.0328 0.0674  -0.1036 134 HIS A CA  
722  C C   . HIS A 107 ? 0.8602 0.4168 0.8421 -0.0301 0.0687  -0.0889 134 HIS A C   
723  O O   . HIS A 107 ? 0.8826 0.4406 0.8773 -0.0280 0.0888  -0.0725 134 HIS A O   
724  C CB  . HIS A 107 ? 0.8493 0.3670 0.8539 -0.0469 0.0717  -0.1173 134 HIS A CB  
725  C CG  . HIS A 107 ? 1.0063 0.5458 1.0479 -0.0579 0.0539  -0.1313 134 HIS A CG  
726  N ND1 . HIS A 107 ? 0.9304 0.4766 1.0227 -0.0703 0.0648  -0.1337 134 HIS A ND1 
727  C CD2 . HIS A 107 ? 0.8623 0.4184 0.8991 -0.0579 0.0257  -0.1442 134 HIS A CD2 
728  C CE1 . HIS A 107 ? 0.8776 0.4480 1.0003 -0.0773 0.0440  -0.1493 134 HIS A CE1 
729  N NE2 . HIS A 107 ? 0.8234 0.3993 0.9125 -0.0688 0.0184  -0.1555 134 HIS A NE2 
730  N N   . TRP A 108 ? 0.8991 0.4750 0.8793 -0.0296 0.0467  -0.0952 135 TRP A N   
731  C CA  . TRP A 108 ? 0.9252 0.5273 0.9229 -0.0262 0.0455  -0.0848 135 TRP A CA  
732  C C   . TRP A 108 ? 0.9057 0.5252 0.9552 -0.0371 0.0367  -0.0988 135 TRP A C   
733  O O   . TRP A 108 ? 0.9861 0.6165 1.0425 -0.0381 0.0106  -0.1133 135 TRP A O   
734  C CB  . TRP A 108 ? 0.7473 0.3572 0.7093 -0.0168 0.0277  -0.0812 135 TRP A CB  
735  C CG  . TRP A 108 ? 0.8581 0.4612 0.7815 -0.0069 0.0412  -0.0650 135 TRP A CG  
736  C CD1 . TRP A 108 ? 0.9097 0.4938 0.7966 -0.0038 0.0453  -0.0662 135 TRP A CD1 
737  C CD2 . TRP A 108 ? 0.9292 0.5464 0.8494 0.0007  0.0525  -0.0474 135 TRP A CD2 
738  N NE1 . TRP A 108 ? 1.0291 0.6170 0.8943 0.0054  0.0579  -0.0505 135 TRP A NE1 
739  C CE2 . TRP A 108 ? 0.8223 0.4296 0.7058 0.0081  0.0615  -0.0387 135 TRP A CE2 
740  C CE3 . TRP A 108 ? 0.8612 0.4994 0.8070 0.0017  0.0562  -0.0400 135 TRP A CE3 
741  C CZ2 . TRP A 108 ? 0.8649 0.4832 0.7374 0.0162  0.0718  -0.0229 135 TRP A CZ2 
742  C CZ3 . TRP A 108 ? 0.8488 0.4952 0.7790 0.0098  0.0673  -0.0241 135 TRP A CZ3 
743  C CH2 . TRP A 108 ? 0.7792 0.4157 0.6733 0.0169  0.0739  -0.0157 135 TRP A CH2 
744  N N   . SER A 109 ? 0.8246 0.4460 0.9108 -0.0453 0.0586  -0.0947 136 SER A N   
745  C CA  . SER A 109 ? 0.8772 0.5191 1.0198 -0.0573 0.0562  -0.1080 136 SER A CA  
746  C C   . SER A 109 ? 0.8938 0.5659 1.0552 -0.0521 0.0572  -0.1007 136 SER A C   
747  O O   . SER A 109 ? 0.8599 0.5337 0.9905 -0.0408 0.0636  -0.0836 136 SER A O   
748  C CB  . SER A 109 ? 0.8530 0.4807 1.0255 -0.0709 0.0826  -0.1070 136 SER A CB  
749  O OG  . SER A 109 ? 0.8718 0.4957 1.0358 -0.0674 0.1102  -0.0841 136 SER A OG  
750  N N   . ASP A 110 ? 0.8034 0.5008 1.0191 -0.0609 0.0509  -0.1159 137 ASP A N   
751  C CA  . ASP A 110 ? 0.8307 0.5587 1.0709 -0.0558 0.0513  -0.1133 137 ASP A CA  
752  C C   . ASP A 110 ? 0.8790 0.6060 1.1127 -0.0556 0.0852  -0.0926 137 ASP A C   
753  O O   . ASP A 110 ? 0.7838 0.5254 1.0074 -0.0458 0.0871  -0.0832 137 ASP A O   
754  C CB  . ASP A 110 ? 0.8808 0.6381 1.1893 -0.0662 0.0415  -0.1360 137 ASP A CB  
755  C CG  . ASP A 110 ? 0.9609 0.7247 1.2735 -0.0619 0.0007  -0.1559 137 ASP A CG  
756  O OD1 . ASP A 110 ? 0.9576 0.7028 1.2157 -0.0507 -0.0183 -0.1501 137 ASP A OD1 
757  O OD2 . ASP A 110 ? 1.0266 0.8142 1.3965 -0.0700 -0.0124 -0.1776 137 ASP A OD2 
758  N N   . SER A 111 ? 0.7856 0.4928 1.0223 -0.0662 0.1114  -0.0854 138 SER A N   
759  C CA  . SER A 111 ? 0.7212 0.4214 0.9422 -0.0654 0.1422  -0.0638 138 SER A CA  
760  C C   . SER A 111 ? 0.8333 0.5201 0.9955 -0.0486 0.1399  -0.0449 138 SER A C   
761  O O   . SER A 111 ? 0.8375 0.5331 0.9849 -0.0418 0.1516  -0.0310 138 SER A O   
762  C CB  . SER A 111 ? 0.7172 0.3911 0.9473 -0.0795 0.1682  -0.0585 138 SER A CB  
763  O OG  . SER A 111 ? 0.9482 0.6365 1.2371 -0.0977 0.1735  -0.0769 138 SER A OG  
764  N N   . ARG A 112 ? 0.7741 0.4406 0.9034 -0.0424 0.1255  -0.0458 139 ARG A N   
765  C CA  . ARG A 112 ? 0.8960 0.5530 0.9747 -0.0275 0.1229  -0.0308 139 ARG A CA  
766  C C   . ARG A 112 ? 0.8398 0.5193 0.9087 -0.0179 0.1051  -0.0321 139 ARG A C   
767  O O   . ARG A 112 ? 0.8124 0.4966 0.8571 -0.0088 0.1118  -0.0181 139 ARG A O   
768  C CB  . ARG A 112 ? 0.8753 0.5076 0.9261 -0.0247 0.1135  -0.0352 139 ARG A CB  
769  C CG  . ARG A 112 ? 0.7485 0.3714 0.7525 -0.0108 0.1145  -0.0214 139 ARG A CG  
770  C CD  . ARG A 112 ? 0.8065 0.4071 0.7877 -0.0091 0.1071  -0.0295 139 ARG A CD  
771  N NE  . ARG A 112 ? 0.8757 0.4693 0.8192 0.0033  0.1115  -0.0180 139 ARG A NE  
772  C CZ  . ARG A 112 ? 0.9231 0.5000 0.8433 0.0071  0.1088  -0.0240 139 ARG A CZ  
773  N NH1 . ARG A 112 ? 0.7838 0.3461 0.7090 -0.0004 0.1011  -0.0411 139 ARG A NH1 
774  N NH2 . ARG A 112 ? 0.8197 0.3958 0.7125 0.0183  0.1141  -0.0145 139 ARG A NH2 
775  N N   . TYR A 113 ? 0.7655 0.4573 0.8528 -0.0196 0.0810  -0.0493 140 TYR A N   
776  C CA  . TYR A 113 ? 0.7611 0.4701 0.8413 -0.0104 0.0624  -0.0509 140 TYR A CA  
777  C C   . TYR A 113 ? 0.7704 0.5020 0.8739 -0.0089 0.0767  -0.0452 140 TYR A C   
778  O O   . TYR A 113 ? 0.7620 0.4988 0.8418 0.0007  0.0763  -0.0356 140 TYR A O   
779  C CB  . TYR A 113 ? 0.7887 0.5057 0.8900 -0.0124 0.0329  -0.0707 140 TYR A CB  
780  C CG  . TYR A 113 ? 0.7942 0.4904 0.8531 -0.0087 0.0111  -0.0748 140 TYR A CG  
781  C CD1 . TYR A 113 ? 0.8085 0.4918 0.8161 0.0003  0.0102  -0.0622 140 TYR A CD1 
782  C CD2 . TYR A 113 ? 0.7991 0.4886 0.8688 -0.0153 -0.0077 -0.0925 140 TYR A CD2 
783  C CE1 . TYR A 113 ? 0.8844 0.5477 0.8508 0.0020  -0.0063 -0.0664 140 TYR A CE1 
784  C CE2 . TYR A 113 ? 0.8023 0.4709 0.8277 -0.0127 -0.0262 -0.0969 140 TYR A CE2 
785  C CZ  . TYR A 113 ? 0.8880 0.5431 0.8610 -0.0044 -0.0242 -0.0834 140 TYR A CZ  
786  O OH  . TYR A 113 ? 1.0494 0.6827 0.9757 -0.0035 -0.0393 -0.0882 140 TYR A OH  
787  N N   . GLU A 114 ? 0.7660 0.5110 0.9162 -0.0195 0.0910  -0.0523 141 GLU A N   
788  C CA  . GLU A 114 ? 0.7658 0.5332 0.9397 -0.0195 0.1074  -0.0496 141 GLU A CA  
789  C C   . GLU A 114 ? 0.7788 0.5353 0.9142 -0.0150 0.1306  -0.0282 141 GLU A C   
790  O O   . GLU A 114 ? 0.6741 0.4438 0.8009 -0.0077 0.1341  -0.0230 141 GLU A O   
791  C CB  . GLU A 114 ? 0.7104 0.4928 0.9414 -0.0346 0.1230  -0.0618 141 GLU A CB  
792  C CG  . GLU A 114 ? 0.8293 0.6342 1.0846 -0.0369 0.1459  -0.0601 141 GLU A CG  
793  C CD  . GLU A 114 ? 0.8967 0.7172 1.2107 -0.0543 0.1650  -0.0733 141 GLU A CD  
794  O OE1 . GLU A 114 ? 1.2370 1.0507 1.5746 -0.0647 0.1588  -0.0841 141 GLU A OE1 
795  O OE2 . GLU A 114 ? 1.1853 1.0250 1.5222 -0.0585 0.1874  -0.0742 141 GLU A OE2 
796  N N   . HIS A 115 ? 0.6699 0.4014 0.7818 -0.0183 0.1451  -0.0163 142 HIS A N   
797  C CA  . HIS A 115 ? 0.6454 0.3653 0.7202 -0.0125 0.1641  0.0042  142 HIS A CA  
798  C C   . HIS A 115 ? 0.7787 0.4986 0.8131 0.0018  0.1495  0.0114  142 HIS A C   
799  O O   . HIS A 115 ? 0.7742 0.5019 0.7905 0.0082  0.1572  0.0210  142 HIS A O   
800  C CB  . HIS A 115 ? 0.6919 0.3821 0.7523 -0.0172 0.1791  0.0148  142 HIS A CB  
801  C CG  . HIS A 115 ? 0.7635 0.4400 0.7869 -0.0105 0.1966  0.0363  142 HIS A CG  
802  N ND1 . HIS A 115 ? 0.7402 0.4246 0.7633 -0.0133 0.2165  0.0450  142 HIS A ND1 
803  C CD2 . HIS A 115 ? 0.7282 0.3840 0.7138 -0.0004 0.1961  0.0499  142 HIS A CD2 
804  C CE1 . HIS A 115 ? 0.7968 0.4643 0.7797 -0.0050 0.2255  0.0641  142 HIS A CE1 
805  N NE2 . HIS A 115 ? 0.9196 0.5709 0.8822 0.0035  0.2127  0.0672  142 HIS A NE2 
806  N N   . VAL A 116 ? 0.7639 0.4744 0.7827 0.0058  0.1293  0.0058  143 VAL A N   
807  C CA  . VAL A 116 ? 0.7769 0.4865 0.7586 0.0169  0.1172  0.0114  143 VAL A CA  
808  C C   . VAL A 116 ? 0.7788 0.5087 0.7672 0.0214  0.1073  0.0071  143 VAL A C   
809  O O   . VAL A 116 ? 0.7454 0.4798 0.7105 0.0285  0.1099  0.0157  143 VAL A O   
810  C CB  . VAL A 116 ? 0.8161 0.5108 0.7800 0.0178  0.0997  0.0042  143 VAL A CB  
811  C CG1 . VAL A 116 ? 0.6411 0.3369 0.5717 0.0262  0.0867  0.0071  143 VAL A CG1 
812  C CG2 . VAL A 116 ? 0.6269 0.3000 0.5780 0.0168  0.1113  0.0098  143 VAL A CG2 
813  N N   . MET A 117 ? 0.7963 0.5389 0.8192 0.0177  0.0946  -0.0076 144 MET A N   
814  C CA  . MET A 117 ? 0.6455 0.4063 0.6809 0.0232  0.0847  -0.0132 144 MET A CA  
815  C C   . MET A 117 ? 0.5758 0.3504 0.6174 0.0239  0.1070  -0.0066 144 MET A C   
816  O O   . MET A 117 ? 0.7065 0.4875 0.7326 0.0313  0.1045  -0.0035 144 MET A O   
817  C CB  . MET A 117 ? 0.5971 0.3715 0.6771 0.0200  0.0681  -0.0314 144 MET A CB  
818  C CG  . MET A 117 ? 0.7626 0.5242 0.8295 0.0222  0.0391  -0.0392 144 MET A CG  
819  S SD  . MET A 117 ? 0.7547 0.5354 0.8741 0.0225  0.0130  -0.0609 144 MET A SD  
820  C CE  . MET A 117 ? 0.6750 0.4479 0.8135 0.0101  0.0100  -0.0721 144 MET A CE  
821  N N   . LYS A 118 ? 0.7157 0.4926 0.7772 0.0152  0.1297  -0.0045 145 LYS A N   
822  C CA  . LYS A 118 ? 0.6268 0.4137 0.6877 0.0145  0.1530  0.0022  145 LYS A CA  
823  C C   . LYS A 118 ? 0.6662 0.4411 0.6776 0.0220  0.1596  0.0195  145 LYS A C   
824  O O   . LYS A 118 ? 0.6161 0.4009 0.6163 0.0260  0.1681  0.0228  145 LYS A O   
825  C CB  . LYS A 118 ? 0.5921 0.3786 0.6792 0.0016  0.1777  0.0023  145 LYS A CB  
826  C CG  . LYS A 118 ? 0.6587 0.4668 0.8050 -0.0068 0.1760  -0.0176 145 LYS A CG  
827  C CD  . LYS A 118 ? 0.6090 0.4181 0.7806 -0.0220 0.2065  -0.0170 145 LYS A CD  
828  C CE  . LYS A 118 ? 0.6060 0.4418 0.8442 -0.0313 0.2054  -0.0396 145 LYS A CE  
829  N NZ  . LYS A 118 ? 0.8316 0.6685 1.0969 -0.0490 0.2386  -0.0401 145 LYS A NZ  
830  N N   . LEU A 119 ? 0.6447 0.3997 0.6281 0.0243  0.1553  0.0287  146 LEU A N   
831  C CA  . LEU A 119 ? 0.6890 0.4359 0.6307 0.0325  0.1590  0.0432  146 LEU A CA  
832  C C   . LEU A 119 ? 0.7627 0.5194 0.6885 0.0404  0.1432  0.0400  146 LEU A C   
833  O O   . LEU A 119 ? 0.7424 0.5052 0.6482 0.0455  0.1487  0.0462  146 LEU A O   
834  C CB  . LEU A 119 ? 0.6842 0.4099 0.6068 0.0341  0.1574  0.0508  146 LEU A CB  
835  C CG  . LEU A 119 ? 0.7672 0.4763 0.6971 0.0275  0.1753  0.0581  146 LEU A CG  
836  C CD1 . LEU A 119 ? 0.7831 0.4701 0.6970 0.0310  0.1714  0.0631  146 LEU A CD1 
837  C CD2 . LEU A 119 ? 0.7250 0.4327 0.6382 0.0284  0.1950  0.0719  146 LEU A CD2 
838  N N   . ARG A 120 ? 0.6666 0.4225 0.5986 0.0411  0.1232  0.0303  147 ARG A N   
839  C CA  . ARG A 120 ? 0.6369 0.3967 0.5522 0.0472  0.1088  0.0280  147 ARG A CA  
840  C C   . ARG A 120 ? 0.6211 0.3977 0.5541 0.0491  0.1109  0.0216  147 ARG A C   
841  O O   . ARG A 120 ? 0.7698 0.5501 0.6847 0.0540  0.1090  0.0235  147 ARG A O   
842  C CB  . ARG A 120 ? 0.6145 0.3644 0.5275 0.0468  0.0872  0.0203  147 ARG A CB  
843  C CG  . ARG A 120 ? 0.6595 0.3928 0.5520 0.0451  0.0860  0.0242  147 ARG A CG  
844  C CD  . ARG A 120 ? 0.7144 0.4362 0.5838 0.0460  0.0677  0.0204  147 ARG A CD  
845  N NE  . ARG A 120 ? 0.6848 0.3917 0.5359 0.0439  0.0688  0.0214  147 ARG A NE  
846  C CZ  . ARG A 120 ? 0.7529 0.4486 0.6092 0.0395  0.0602  0.0133  147 ARG A CZ  
847  N NH1 . ARG A 120 ? 0.8424 0.5413 0.7230 0.0368  0.0473  0.0037  147 ARG A NH1 
848  N NH2 . ARG A 120 ? 0.7228 0.4049 0.5613 0.0381  0.0639  0.0132  147 ARG A NH2 
849  N N   . GLN A 121 ? 0.6836 0.4712 0.6545 0.0448  0.1156  0.0123  148 GLN A N   
850  C CA  . GLN A 121 ? 0.6684 0.4739 0.6603 0.0468  0.1218  0.0044  148 GLN A CA  
851  C C   . GLN A 121 ? 0.6897 0.4992 0.6610 0.0467  0.1443  0.0135  148 GLN A C   
852  O O   . GLN A 121 ? 0.6871 0.5054 0.6514 0.0513  0.1462  0.0105  148 GLN A O   
853  C CB  . GLN A 121 ? 0.5788 0.3988 0.6213 0.0413  0.1250  -0.0092 148 GLN A CB  
854  C CG  . GLN A 121 ? 0.5415 0.3827 0.6136 0.0443  0.1307  -0.0214 148 GLN A CG  
855  C CD  . GLN A 121 ? 0.5358 0.3766 0.6075 0.0546  0.1063  -0.0288 148 GLN A CD  
856  O OE1 . GLN A 121 ? 0.5867 0.4147 0.6509 0.0576  0.0824  -0.0292 148 GLN A OE1 
857  N NE2 . GLN A 121 ? 0.5350 0.3871 0.6121 0.0598  0.1125  -0.0349 148 GLN A NE2 
858  N N   . ALA A 122 ? 0.6446 0.4452 0.6037 0.0419  0.1607  0.0247  149 ALA A N   
859  C CA  . ALA A 122 ? 0.6255 0.4252 0.5570 0.0426  0.1796  0.0357  149 ALA A CA  
860  C C   . ALA A 122 ? 0.6817 0.4781 0.5753 0.0510  0.1694  0.0424  149 ALA A C   
861  O O   . ALA A 122 ? 0.6779 0.4820 0.5551 0.0541  0.1759  0.0428  149 ALA A O   
862  C CB  . ALA A 122 ? 0.5929 0.3769 0.5152 0.0369  0.1956  0.0483  149 ALA A CB  
863  N N   . ALA A 123 ? 0.6533 0.4393 0.5337 0.0541  0.1543  0.0462  150 ALA A N   
864  C CA  . ALA A 123 ? 0.7294 0.5150 0.5801 0.0604  0.1448  0.0503  150 ALA A CA  
865  C C   . ALA A 123 ? 0.7434 0.5386 0.5981 0.0626  0.1351  0.0398  150 ALA A C   
866  O O   . ALA A 123 ? 0.7212 0.5216 0.5557 0.0660  0.1352  0.0408  150 ALA A O   
867  C CB  . ALA A 123 ? 0.5521 0.3258 0.3929 0.0615  0.1329  0.0535  150 ALA A CB  
868  N N   . LEU A 124 ? 0.6655 0.4620 0.5468 0.0611  0.1252  0.0290  151 LEU A N   
869  C CA  . LEU A 124 ? 0.5819 0.3834 0.4691 0.0645  0.1150  0.0191  151 LEU A CA  
870  C C   . LEU A 124 ? 0.6472 0.4629 0.5409 0.0656  0.1299  0.0138  151 LEU A C   
871  O O   . LEU A 124 ? 0.7086 0.5271 0.5885 0.0689  0.1275  0.0102  151 LEU A O   
872  C CB  . LEU A 124 ? 0.6324 0.4310 0.5481 0.0646  0.0994  0.0091  151 LEU A CB  
873  C CG  . LEU A 124 ? 0.6513 0.4492 0.5746 0.0699  0.0850  -0.0006 151 LEU A CG  
874  C CD1 . LEU A 124 ? 0.5377 0.3208 0.4259 0.0708  0.0742  0.0049  151 LEU A CD1 
875  C CD2 . LEU A 124 ? 0.5374 0.3329 0.4913 0.0718  0.0679  -0.0099 151 LEU A CD2 
876  N N   . LYS A 125 ? 0.6058 0.4298 0.5198 0.0617  0.1468  0.0122  152 LYS A N   
877  C CA  . LYS A 125 ? 0.6112 0.4481 0.5278 0.0614  0.1650  0.0068  152 LYS A CA  
878  C C   . LYS A 125 ? 0.6003 0.4342 0.4737 0.0631  0.1729  0.0170  152 LYS A C   
879  O O   . LYS A 125 ? 0.5924 0.4338 0.4553 0.0655  0.1780  0.0104  152 LYS A O   
880  C CB  . LYS A 125 ? 0.5677 0.4119 0.5113 0.0542  0.1851  0.0047  152 LYS A CB  
881  C CG  . LYS A 125 ? 0.5853 0.4411 0.5260 0.0517  0.2093  0.0000  152 LYS A CG  
882  C CD  . LYS A 125 ? 0.5964 0.4604 0.5696 0.0421  0.2314  -0.0043 152 LYS A CD  
883  C CE  . LYS A 125 ? 0.6227 0.4930 0.5799 0.0375  0.2602  -0.0052 152 LYS A CE  
884  N NZ  . LYS A 125 ? 0.7005 0.5854 0.6630 0.0436  0.2599  -0.0212 152 LYS A NZ  
885  N N   . SER A 126 ? 0.5740 0.3970 0.4228 0.0628  0.1728  0.0318  153 SER A N   
886  C CA  . SER A 126 ? 0.6554 0.4763 0.4647 0.0665  0.1750  0.0413  153 SER A CA  
887  C C   . SER A 126 ? 0.6873 0.5125 0.4851 0.0707  0.1594  0.0346  153 SER A C   
888  O O   . SER A 126 ? 0.7094 0.5414 0.4886 0.0727  0.1629  0.0310  153 SER A O   
889  C CB  . SER A 126 ? 0.6570 0.4653 0.4490 0.0678  0.1735  0.0568  153 SER A CB  
890  O OG  . SER A 126 ? 0.8375 0.6377 0.6311 0.0634  0.1909  0.0651  153 SER A OG  
891  N N   . ALA A 127 ? 0.6526 0.4721 0.4595 0.0710  0.1429  0.0325  154 ALA A N   
892  C CA  . ALA A 127 ? 0.6637 0.4836 0.4597 0.0726  0.1295  0.0270  154 ALA A CA  
893  C C   . ALA A 127 ? 0.6306 0.4566 0.4361 0.0736  0.1306  0.0134  154 ALA A C   
894  O O   . ALA A 127 ? 0.6522 0.4818 0.4409 0.0746  0.1281  0.0088  154 ALA A O   
895  C CB  . ALA A 127 ? 0.7215 0.5302 0.5244 0.0710  0.1144  0.0270  154 ALA A CB  
896  N N   . ARG A 128 ? 0.6485 0.4767 0.4836 0.0735  0.1340  0.0051  155 ARG A N   
897  C CA  . ARG A 128 ? 0.5619 0.3965 0.4111 0.0759  0.1362  -0.0097 155 ARG A CA  
898  C C   . ARG A 128 ? 0.6485 0.4941 0.4802 0.0756  0.1545  -0.0122 155 ARG A C   
899  O O   . ARG A 128 ? 0.6696 0.5179 0.4906 0.0775  0.1538  -0.0217 155 ARG A O   
900  C CB  . ARG A 128 ? 0.5577 0.3960 0.4485 0.0771  0.1359  -0.0193 155 ARG A CB  
901  C CG  . ARG A 128 ? 0.5698 0.3952 0.4755 0.0792  0.1136  -0.0206 155 ARG A CG  
902  C CD  . ARG A 128 ? 0.6767 0.5096 0.6267 0.0812  0.1119  -0.0305 155 ARG A CD  
903  N NE  . ARG A 128 ? 0.6600 0.4788 0.6212 0.0848  0.0875  -0.0322 155 ARG A NE  
904  C CZ  . ARG A 128 ? 0.7138 0.5353 0.7058 0.0853  0.0792  -0.0360 155 ARG A CZ  
905  N NH1 . ARG A 128 ? 0.5587 0.3971 0.5771 0.0809  0.0949  -0.0388 155 ARG A NH1 
906  N NH2 . ARG A 128 ? 0.5711 0.3767 0.5660 0.0895  0.0543  -0.0371 155 ARG A NH2 
907  N N   . ASP A 129 ? 0.5961 0.4452 0.4217 0.0727  0.1713  -0.0037 156 ASP A N   
908  C CA  . ASP A 129 ? 0.6213 0.4773 0.4245 0.0716  0.1902  -0.0049 156 ASP A CA  
909  C C   . ASP A 129 ? 0.6228 0.4773 0.3840 0.0741  0.1837  0.0003  156 ASP A C   
910  O O   . ASP A 129 ? 0.6601 0.5202 0.4009 0.0746  0.1923  -0.0070 156 ASP A O   
911  C CB  . ASP A 129 ? 0.6262 0.4804 0.4270 0.0666  0.2097  0.0060  156 ASP A CB  
912  C CG  . ASP A 129 ? 0.9024 0.7645 0.7482 0.0623  0.2216  -0.0041 156 ASP A CG  
913  O OD1 . ASP A 129 ? 0.8569 0.7288 0.7327 0.0650  0.2180  -0.0213 156 ASP A OD1 
914  O OD2 . ASP A 129 ? 0.7327 0.5911 0.5861 0.0563  0.2344  0.0045  156 ASP A OD2 
915  N N   . MET A 130 ? 0.6116 0.4599 0.3607 0.0756  0.1686  0.0110  157 MET A N   
916  C CA  . MET A 130 ? 0.6455 0.4962 0.3617 0.0783  0.1601  0.0144  157 MET A CA  
917  C C   . MET A 130 ? 0.7164 0.5691 0.4371 0.0781  0.1451  0.0022  157 MET A C   
918  O O   . MET A 130 ? 0.7939 0.6508 0.4945 0.0789  0.1357  0.0030  157 MET A O   
919  C CB  . MET A 130 ? 0.6476 0.4931 0.3517 0.0805  0.1533  0.0309  157 MET A CB  
920  C CG  . MET A 130 ? 0.6724 0.5129 0.3964 0.0794  0.1396  0.0320  157 MET A CG  
921  S SD  . MET A 130 ? 0.8293 0.6651 0.5416 0.0831  0.1347  0.0485  157 MET A SD  
922  C CE  . MET A 130 ? 0.9144 0.7614 0.5935 0.0888  0.1297  0.0503  157 MET A CE  
923  N N   . TRP A 131 ? 0.6892 0.5383 0.4372 0.0770  0.1421  -0.0091 158 TRP A N   
924  C CA  . TRP A 131 ? 0.7039 0.5490 0.4554 0.0761  0.1297  -0.0210 158 TRP A CA  
925  C C   . TRP A 131 ? 0.7409 0.5802 0.4855 0.0734  0.1150  -0.0140 158 TRP A C   
926  O O   . TRP A 131 ? 0.7060 0.5463 0.4397 0.0707  0.1075  -0.0202 158 TRP A O   
927  C CB  . TRP A 131 ? 0.6169 0.4697 0.3493 0.0765  0.1343  -0.0331 158 TRP A CB  
928  C CG  . TRP A 131 ? 0.6365 0.4902 0.3863 0.0783  0.1440  -0.0489 158 TRP A CG  
929  C CD1 . TRP A 131 ? 0.6173 0.4669 0.4016 0.0805  0.1455  -0.0539 158 TRP A CD1 
930  C CD2 . TRP A 131 ? 0.7080 0.5682 0.4438 0.0789  0.1530  -0.0638 158 TRP A CD2 
931  N NE1 . TRP A 131 ? 0.6903 0.5448 0.4869 0.0830  0.1557  -0.0714 158 TRP A NE1 
932  C CE2 . TRP A 131 ? 0.6520 0.5121 0.4176 0.0817  0.1616  -0.0780 158 TRP A CE2 
933  C CE3 . TRP A 131 ? 0.6706 0.5372 0.3717 0.0778  0.1536  -0.0680 158 TRP A CE3 
934  C CZ2 . TRP A 131 ? 0.6746 0.5402 0.4364 0.0830  0.1733  -0.0965 158 TRP A CZ2 
935  C CZ3 . TRP A 131 ? 0.6947 0.5653 0.3878 0.0784  0.1641  -0.0860 158 TRP A CZ3 
936  C CH2 . TRP A 131 ? 0.7110 0.5807 0.4342 0.0808  0.1752  -0.1003 158 TRP A CH2 
937  N N   . ALA A 132 ? 0.6897 0.5232 0.4420 0.0729  0.1122  -0.0027 159 ALA A N   
938  C CA  . ALA A 132 ? 0.6747 0.5022 0.4224 0.0694  0.1011  0.0024  159 ALA A CA  
939  C C   . ALA A 132 ? 0.7685 0.5797 0.5266 0.0659  0.0910  -0.0044 159 ALA A C   
940  O O   . ALA A 132 ? 0.6751 0.4786 0.4497 0.0683  0.0900  -0.0106 159 ALA A O   
941  C CB  . ALA A 132 ? 0.6090 0.4338 0.3593 0.0703  0.1024  0.0151  159 ALA A CB  
942  N N   . ASP A 133 ? 0.7225 0.5277 0.4711 0.0601  0.0835  -0.0035 160 ASP A N   
943  C CA  . ASP A 133 ? 0.7198 0.5031 0.4710 0.0554  0.0740  -0.0068 160 ASP A CA  
944  C C   . ASP A 133 ? 0.7164 0.4854 0.4706 0.0547  0.0691  0.0019  160 ASP A C   
945  O O   . ASP A 133 ? 0.7887 0.5384 0.5492 0.0557  0.0606  0.0004  160 ASP A O   
946  C CB  . ASP A 133 ? 0.7965 0.5774 0.5349 0.0466  0.0707  -0.0105 160 ASP A CB  
947  C CG  . ASP A 133 ? 0.7446 0.5362 0.4805 0.0463  0.0726  -0.0223 160 ASP A CG  
948  O OD1 . ASP A 133 ? 0.8386 0.6260 0.5819 0.0511  0.0735  -0.0303 160 ASP A OD1 
949  O OD2 . ASP A 133 ? 0.7562 0.5614 0.4842 0.0412  0.0728  -0.0252 160 ASP A OD2 
950  N N   . TYR A 134 ? 0.7372 0.5141 0.4862 0.0539  0.0731  0.0103  161 TYR A N   
951  C CA  . TYR A 134 ? 0.7248 0.4888 0.4736 0.0526  0.0693  0.0171  161 TYR A CA  
952  C C   . TYR A 134 ? 0.6813 0.4580 0.4367 0.0573  0.0770  0.0235  161 TYR A C   
953  O O   . TYR A 134 ? 0.6837 0.4773 0.4363 0.0603  0.0846  0.0257  161 TYR A O   
954  C CB  . TYR A 134 ? 0.6674 0.4214 0.3995 0.0440  0.0673  0.0196  161 TYR A CB  
955  C CG  . TYR A 134 ? 0.7893 0.5243 0.5108 0.0368  0.0610  0.0152  161 TYR A CG  
956  C CD1 . TYR A 134 ? 0.7887 0.5323 0.5080 0.0325  0.0637  0.0086  161 TYR A CD1 
957  C CD2 . TYR A 134 ? 0.6902 0.3959 0.4017 0.0338  0.0515  0.0177  161 TYR A CD2 
958  C CE1 . TYR A 134 ? 0.8089 0.5313 0.5186 0.0245  0.0591  0.0046  161 TYR A CE1 
959  C CE2 . TYR A 134 ? 0.8427 0.5249 0.5407 0.0270  0.0459  0.0156  161 TYR A CE2 
960  C CZ  . TYR A 134 ? 0.8123 0.5022 0.5104 0.0218  0.0508  0.0091  161 TYR A CZ  
961  O OH  . TYR A 134 ? 0.8655 0.5285 0.5504 0.0136  0.0463  0.0070  161 TYR A OH  
962  N N   . ILE A 135 ? 0.6879 0.4545 0.4510 0.0580  0.0740  0.0265  162 ILE A N   
963  C CA  . ILE A 135 ? 0.6456 0.4174 0.4130 0.0602  0.0806  0.0329  162 ILE A CA  
964  C C   . ILE A 135 ? 0.7960 0.5542 0.5532 0.0558  0.0759  0.0354  162 ILE A C   
965  O O   . ILE A 135 ? 0.6958 0.4364 0.4484 0.0525  0.0659  0.0330  162 ILE A O   
966  C CB  . ILE A 135 ? 0.6523 0.4260 0.4409 0.0635  0.0837  0.0319  162 ILE A CB  
967  C CG1 . ILE A 135 ? 0.5703 0.3445 0.3622 0.0641  0.0910  0.0388  162 ILE A CG1 
968  C CG2 . ILE A 135 ? 0.6671 0.4279 0.4680 0.0629  0.0712  0.0259  162 ILE A CG2 
969  C CD1 . ILE A 135 ? 0.6126 0.3912 0.4261 0.0651  0.0988  0.0382  162 ILE A CD1 
970  N N   . LEU A 136 ? 0.7767 0.5416 0.5283 0.0564  0.0827  0.0397  163 LEU A N   
971  C CA  . LEU A 136 ? 0.6826 0.4369 0.4239 0.0522  0.0818  0.0402  163 LEU A CA  
972  C C   . LEU A 136 ? 0.7691 0.5212 0.5197 0.0558  0.0860  0.0435  163 LEU A C   
973  O O   . LEU A 136 ? 0.7605 0.5235 0.5169 0.0614  0.0939  0.0480  163 LEU A O   
974  C CB  . LEU A 136 ? 0.6781 0.4431 0.4105 0.0499  0.0870  0.0394  163 LEU A CB  
975  C CG  . LEU A 136 ? 0.6405 0.3985 0.3638 0.0454  0.0905  0.0381  163 LEU A CG  
976  C CD1 . LEU A 136 ? 0.6064 0.3412 0.3109 0.0359  0.0845  0.0355  163 LEU A CD1 
977  C CD2 . LEU A 136 ? 0.6987 0.4759 0.4242 0.0455  0.0975  0.0356  163 LEU A CD2 
978  N N   . PHE A 137 ? 0.7045 0.4408 0.4558 0.0528  0.0795  0.0411  164 PHE A N   
979  C CA  . PHE A 137 ? 0.7251 0.4562 0.4848 0.0541  0.0829  0.0419  164 PHE A CA  
980  C C   . PHE A 137 ? 0.7230 0.4468 0.4675 0.0515  0.0859  0.0403  164 PHE A C   
981  O O   . PHE A 137 ? 0.7498 0.4622 0.4757 0.0453  0.0808  0.0367  164 PHE A O   
982  C CB  . PHE A 137 ? 0.7636 0.4835 0.5343 0.0518  0.0731  0.0375  164 PHE A CB  
983  C CG  . PHE A 137 ? 0.7839 0.5143 0.5788 0.0547  0.0748  0.0371  164 PHE A CG  
984  C CD1 . PHE A 137 ? 0.6913 0.4268 0.5040 0.0559  0.0852  0.0398  164 PHE A CD1 
985  C CD2 . PHE A 137 ? 0.7207 0.4543 0.5210 0.0556  0.0674  0.0336  164 PHE A CD2 
986  C CE1 . PHE A 137 ? 0.6044 0.3501 0.4393 0.0566  0.0903  0.0386  164 PHE A CE1 
987  C CE2 . PHE A 137 ? 0.6202 0.3656 0.4454 0.0580  0.0714  0.0309  164 PHE A CE2 
988  C CZ  . PHE A 137 ? 0.6102 0.3626 0.4524 0.0578  0.0839  0.0332  164 PHE A CZ  
989  N N   . VAL A 138 ? 0.7348 0.4637 0.4860 0.0564  0.0952  0.0430  165 VAL A N   
990  C CA  . VAL A 138 ? 0.8237 0.5474 0.5664 0.0556  0.1002  0.0393  165 VAL A CA  
991  C C   . VAL A 138 ? 0.8879 0.6026 0.6425 0.0592  0.1042  0.0397  165 VAL A C   
992  O O   . VAL A 138 ? 0.8336 0.5534 0.6016 0.0658  0.1095  0.0465  165 VAL A O   
993  C CB  . VAL A 138 ? 0.7022 0.4434 0.4449 0.0599  0.1075  0.0402  165 VAL A CB  
994  C CG1 . VAL A 138 ? 0.5815 0.3190 0.3180 0.0580  0.1140  0.0332  165 VAL A CG1 
995  C CG2 . VAL A 138 ? 0.6914 0.4430 0.4269 0.0557  0.1042  0.0396  165 VAL A CG2 
996  N N   . ASP A 139 ? 0.7599 0.4584 0.5069 0.0542  0.1017  0.0325  166 ASP A N   
997  C CA  . ASP A 139 ? 0.8714 0.5591 0.6298 0.0565  0.1061  0.0307  166 ASP A CA  
998  C C   . ASP A 139 ? 0.8279 0.5202 0.5898 0.0645  0.1170  0.0318  166 ASP A C   
999  O O   . ASP A 139 ? 0.7981 0.4996 0.5512 0.0652  0.1206  0.0284  166 ASP A O   
1000 C CB  . ASP A 139 ? 0.8229 0.4919 0.5701 0.0489  0.0991  0.0204  166 ASP A CB  
1001 C CG  . ASP A 139 ? 1.0591 0.7232 0.8152 0.0442  0.0866  0.0188  166 ASP A CG  
1002 O OD1 . ASP A 139 ? 1.1082 0.7840 0.8788 0.0463  0.0853  0.0250  166 ASP A OD1 
1003 O OD2 . ASP A 139 ? 1.0771 0.7265 0.8268 0.0388  0.0778  0.0100  166 ASP A OD2 
1004 N N   . ALA A 140 ? 0.7945 0.4795 0.5714 0.0705  0.1223  0.0361  167 ALA A N   
1005 C CA  . ALA A 140 ? 0.7065 0.3949 0.4901 0.0817  0.1303  0.0394  167 ALA A CA  
1006 C C   . ALA A 140 ? 0.7638 0.4485 0.5429 0.0825  0.1351  0.0275  167 ALA A C   
1007 O O   . ALA A 140 ? 0.8676 0.5619 0.6546 0.0926  0.1405  0.0275  167 ALA A O   
1008 C CB  . ALA A 140 ? 0.8023 0.4757 0.5991 0.0871  0.1348  0.0475  167 ALA A CB  
1009 N N   . ASP A 141 ? 0.7242 0.3959 0.4908 0.0725  0.1331  0.0164  168 ASP A N   
1010 C CA  . ASP A 141 ? 0.7075 0.3754 0.4649 0.0713  0.1400  0.0033  168 ASP A CA  
1011 C C   . ASP A 141 ? 0.8099 0.4856 0.5448 0.0617  0.1396  -0.0022 168 ASP A C   
1012 O O   . ASP A 141 ? 0.9132 0.5835 0.6341 0.0570  0.1468  -0.0141 168 ASP A O   
1013 C CB  . ASP A 141 ? 0.7195 0.3627 0.4730 0.0665  0.1399  -0.0070 168 ASP A CB  
1014 C CG  . ASP A 141 ? 0.8586 0.4903 0.5973 0.0545  0.1276  -0.0096 168 ASP A CG  
1015 O OD1 . ASP A 141 ? 0.8791 0.5200 0.6118 0.0508  0.1195  -0.0027 168 ASP A OD1 
1016 O OD2 . ASP A 141 ? 1.0157 0.6286 0.7499 0.0494  0.1248  -0.0198 168 ASP A OD2 
1017 N N   . ASN A 142 ? 0.8063 0.4926 0.5362 0.0581  0.1327  0.0057  169 ASN A N   
1018 C CA  . ASN A 142 ? 0.7618 0.4526 0.4703 0.0487  0.1330  0.0025  169 ASN A CA  
1019 C C   . ASN A 142 ? 0.8508 0.5669 0.5720 0.0535  0.1420  0.0024  169 ASN A C   
1020 O O   . ASN A 142 ? 0.8240 0.5566 0.5636 0.0622  0.1393  0.0107  169 ASN A O   
1021 C CB  . ASN A 142 ? 0.8644 0.5510 0.5625 0.0427  0.1201  0.0096  169 ASN A CB  
1022 C CG  . ASN A 142 ? 0.9054 0.5693 0.5910 0.0370  0.1085  0.0069  169 ASN A CG  
1023 O OD1 . ASN A 142 ? 0.8247 0.4839 0.5051 0.0338  0.0962  0.0109  169 ASN A OD1 
1024 N ND2 . ASN A 142 ? 0.9712 0.6213 0.6541 0.0365  0.1113  -0.0015 169 ASN A ND2 
1025 N N   . LEU A 143 ? 0.7697 0.4894 0.4809 0.0473  0.1530  -0.0080 170 LEU A N   
1026 C CA  . LEU A 143 ? 0.7970 0.5441 0.5261 0.0508  0.1628  -0.0124 170 LEU A CA  
1027 C C   . LEU A 143 ? 0.7417 0.4947 0.4545 0.0374  0.1641  -0.0124 170 LEU A C   
1028 O O   . LEU A 143 ? 0.7602 0.4973 0.4447 0.0237  0.1701  -0.0182 170 LEU A O   
1029 C CB  . LEU A 143 ? 0.6985 0.4486 0.4348 0.0530  0.1778  -0.0267 170 LEU A CB  
1030 C CG  . LEU A 143 ? 0.7857 0.5673 0.5443 0.0548  0.1894  -0.0354 170 LEU A CG  
1031 C CD1 . LEU A 143 ? 0.8269 0.6328 0.6178 0.0709  0.1806  -0.0274 170 LEU A CD1 
1032 C CD2 . LEU A 143 ? 0.7739 0.5578 0.5415 0.0570  0.2058  -0.0520 170 LEU A CD2 
1033 N N   . ILE A 144 ? 0.7567 0.5299 0.4846 0.0409  0.1586  -0.0061 171 ILE A N   
1034 C CA  . ILE A 144 ? 0.7715 0.5492 0.4871 0.0281  0.1593  -0.0062 171 ILE A CA  
1035 C C   . ILE A 144 ? 0.8259 0.6327 0.5619 0.0259  0.1722  -0.0167 171 ILE A C   
1036 O O   . ILE A 144 ? 0.8112 0.6449 0.5722 0.0329  0.1681  -0.0160 171 ILE A O   
1037 C CB  . ILE A 144 ? 0.8714 0.6526 0.5906 0.0315  0.1454  0.0044  171 ILE A CB  
1038 C CG1 . ILE A 144 ? 0.7818 0.5412 0.4927 0.0362  0.1341  0.0128  171 ILE A CG1 
1039 C CG2 . ILE A 144 ? 0.8161 0.5922 0.5180 0.0171  0.1450  0.0043  171 ILE A CG2 
1040 C CD1 . ILE A 144 ? 0.7321 0.4613 0.4133 0.0258  0.1314  0.0112  171 ILE A CD1 
1041 N N   . LEU A 145 ? 0.8485 0.6512 0.5742 0.0157  0.1881  -0.0279 172 LEU A N   
1042 C CA  . LEU A 145 ? 0.7131 0.5467 0.4644 0.0129  0.2033  -0.0412 172 LEU A CA  
1043 C C   . LEU A 145 ? 0.7693 0.6181 0.5244 0.0012  0.2037  -0.0414 172 LEU A C   
1044 O O   . LEU A 145 ? 0.8931 0.7777 0.6839 0.0057  0.2059  -0.0488 172 LEU A O   
1045 C CB  . LEU A 145 ? 0.7639 0.5867 0.4986 0.0014  0.2235  -0.0541 172 LEU A CB  
1046 C CG  . LEU A 145 ? 0.9068 0.7360 0.6612 0.0144  0.2317  -0.0646 172 LEU A CG  
1047 C CD1 . LEU A 145 ? 0.7544 0.5817 0.4962 0.0002  0.2563  -0.0813 172 LEU A CD1 
1048 C CD2 . LEU A 145 ? 0.8433 0.7095 0.6487 0.0339  0.2269  -0.0676 172 LEU A CD2 
1049 N N   . ASN A 146 ? 0.7366 0.5581 0.4565 -0.0136 0.2006  -0.0341 173 ASN A N   
1050 C CA  . ASN A 146 ? 0.7916 0.6204 0.5111 -0.0273 0.2023  -0.0348 173 ASN A CA  
1051 C C   . ASN A 146 ? 0.8349 0.6817 0.5763 -0.0156 0.1848  -0.0283 173 ASN A C   
1052 O O   . ASN A 146 ? 0.8497 0.6771 0.5761 -0.0094 0.1699  -0.0167 173 ASN A O   
1053 C CB  . ASN A 146 ? 0.8027 0.5900 0.4745 -0.0450 0.2027  -0.0277 173 ASN A CB  
1054 C CG  . ASN A 146 ? 0.9139 0.7033 0.5827 -0.0628 0.2096  -0.0301 173 ASN A CG  
1055 O OD1 . ASN A 146 ? 0.9873 0.8112 0.6918 -0.0614 0.2105  -0.0370 173 ASN A OD1 
1056 N ND2 . ASN A 146 ? 1.0505 0.8008 0.6753 -0.0798 0.2134  -0.0244 173 ASN A ND2 
1057 N N   . PRO A 147 ? 0.8089 0.6935 0.5859 -0.0126 0.1861  -0.0367 174 PRO A N   
1058 C CA  . PRO A 147 ? 0.9593 0.8603 0.7521 -0.0014 0.1689  -0.0313 174 PRO A CA  
1059 C C   . PRO A 147 ? 0.8847 0.7664 0.6557 -0.0129 0.1619  -0.0255 174 PRO A C   
1060 O O   . PRO A 147 ? 0.8411 0.7272 0.6158 -0.0035 0.1476  -0.0197 174 PRO A O   
1061 C CB  . PRO A 147 ? 0.6917 0.6379 0.5263 0.0020  0.1720  -0.0448 174 PRO A CB  
1062 C CG  . PRO A 147 ? 0.6645 0.6203 0.5120 -0.0019 0.1906  -0.0567 174 PRO A CG  
1063 C CD  . PRO A 147 ? 0.6611 0.5771 0.4668 -0.0193 0.2028  -0.0530 174 PRO A CD  
1064 N N   . ASP A 148 ? 0.7729 0.6308 0.5192 -0.0326 0.1721  -0.0269 175 ASP A N   
1065 C CA  . ASP A 148 ? 0.9307 0.7654 0.6559 -0.0436 0.1657  -0.0216 175 ASP A CA  
1066 C C   . ASP A 148 ? 0.9208 0.7146 0.6119 -0.0406 0.1552  -0.0087 175 ASP A C   
1067 O O   . ASP A 148 ? 0.9087 0.6781 0.5807 -0.0481 0.1488  -0.0039 175 ASP A O   
1068 C CB  . ASP A 148 ? 0.8075 0.6340 0.5226 -0.0675 0.1819  -0.0290 175 ASP A CB  
1069 C CG  . ASP A 148 ? 0.8754 0.7462 0.6311 -0.0726 0.1917  -0.0445 175 ASP A CG  
1070 O OD1 . ASP A 148 ? 0.9091 0.8119 0.6951 -0.0594 0.1795  -0.0481 175 ASP A OD1 
1071 O OD2 . ASP A 148 ? 1.0471 0.9211 0.8040 -0.0902 0.2117  -0.0538 175 ASP A OD2 
1072 N N   . THR A 149 ? 0.8114 0.5976 0.4972 -0.0293 0.1525  -0.0041 176 THR A N   
1073 C CA  . THR A 149 ? 0.8851 0.6350 0.5419 -0.0274 0.1420  0.0058  176 THR A CA  
1074 C C   . THR A 149 ? 0.7758 0.5209 0.4363 -0.0198 0.1261  0.0122  176 THR A C   
1075 O O   . THR A 149 ? 0.7864 0.5014 0.4241 -0.0249 0.1180  0.0174  176 THR A O   
1076 C CB  . THR A 149 ? 0.9699 0.7184 0.6286 -0.0160 0.1413  0.0072  176 THR A CB  
1077 O OG1 . THR A 149 ? 0.8904 0.6377 0.5404 -0.0242 0.1571  -0.0003 176 THR A OG1 
1078 C CG2 . THR A 149 ? 0.8128 0.5292 0.4486 -0.0130 0.1276  0.0154  176 THR A CG2 
1079 N N   . LEU A 150 ? 0.7143 0.4877 0.4020 -0.0071 0.1214  0.0115  177 LEU A N   
1080 C CA  . LEU A 150 ? 0.7536 0.5244 0.4448 -0.0001 0.1092  0.0156  177 LEU A CA  
1081 C C   . LEU A 150 ? 0.8828 0.6446 0.5663 -0.0115 0.1076  0.0124  177 LEU A C   
1082 O O   . LEU A 150 ? 0.8627 0.6010 0.5342 -0.0117 0.0985  0.0161  177 LEU A O   
1083 C CB  . LEU A 150 ? 0.6763 0.4777 0.3917 0.0141  0.1066  0.0154  177 LEU A CB  
1084 C CG  . LEU A 150 ? 0.6829 0.4853 0.4014 0.0209  0.0974  0.0178  177 LEU A CG  
1085 C CD1 . LEU A 150 ? 0.7093 0.4859 0.4179 0.0237  0.0909  0.0238  177 LEU A CD1 
1086 C CD2 . LEU A 150 ? 0.6794 0.5078 0.4134 0.0342  0.0961  0.0193  177 LEU A CD2 
1087 N N   . SER A 151 ? 0.8198 0.5998 0.5129 -0.0212 0.1164  0.0043  178 SER A N   
1088 C CA  . SER A 151 ? 0.7185 0.4876 0.4050 -0.0347 0.1168  0.0000  178 SER A CA  
1089 C C   . SER A 151 ? 0.8318 0.5568 0.4848 -0.0473 0.1180  0.0059  178 SER A C   
1090 O O   . SER A 151 ? 0.8396 0.5388 0.4795 -0.0505 0.1100  0.0086  178 SER A O   
1091 C CB  . SER A 151 ? 0.6955 0.4945 0.4022 -0.0449 0.1275  -0.0116 178 SER A CB  
1092 O OG  . SER A 151 ? 0.8349 0.6735 0.5701 -0.0314 0.1231  -0.0164 178 SER A OG  
1093 N N   . LEU A 152 ? 0.7299 0.4435 0.3663 -0.0539 0.1276  0.0078  179 LEU A N   
1094 C CA  . LEU A 152 ? 0.7376 0.4057 0.3342 -0.0660 0.1281  0.0147  179 LEU A CA  
1095 C C   . LEU A 152 ? 0.9448 0.5841 0.5260 -0.0546 0.1091  0.0240  179 LEU A C   
1096 O O   . LEU A 152 ? 1.0450 0.6475 0.6013 -0.0605 0.1014  0.0294  179 LEU A O   
1097 C CB  . LEU A 152 ? 0.8971 0.5604 0.4767 -0.0732 0.1420  0.0137  179 LEU A CB  
1098 C CG  . LEU A 152 ? 0.9120 0.5971 0.5025 -0.0885 0.1642  0.0033  179 LEU A CG  
1099 C CD1 . LEU A 152 ? 0.9654 0.6499 0.5436 -0.0909 0.1776  0.0005  179 LEU A CD1 
1100 C CD2 . LEU A 152 ? 0.7772 0.4361 0.3458 -0.1103 0.1730  0.0034  179 LEU A CD2 
1101 N N   . LEU A 153 ? 0.7822 0.4372 0.3798 -0.0382 0.1012  0.0254  180 LEU A N   
1102 C CA  . LEU A 153 ? 0.7630 0.3967 0.3540 -0.0274 0.0836  0.0317  180 LEU A CA  
1103 C C   . LEU A 153 ? 0.9258 0.5575 0.5291 -0.0227 0.0738  0.0308  180 LEU A C   
1104 O O   . LEU A 153 ? 0.9249 0.5269 0.5152 -0.0198 0.0601  0.0351  180 LEU A O   
1105 C CB  . LEU A 153 ? 0.8694 0.5234 0.4801 -0.0132 0.0806  0.0319  180 LEU A CB  
1106 C CG  . LEU A 153 ? 0.8415 0.4911 0.4393 -0.0152 0.0868  0.0320  180 LEU A CG  
1107 C CD1 . LEU A 153 ? 0.6540 0.3275 0.2784 -0.0018 0.0864  0.0310  180 LEU A CD1 
1108 C CD2 . LEU A 153 ? 0.7835 0.3930 0.3460 -0.0193 0.0758  0.0369  180 LEU A CD2 
1109 N N   . ILE A 154 ? 0.8210 0.4837 0.4494 -0.0208 0.0794  0.0243  181 ILE A N   
1110 C CA  . ILE A 154 ? 0.8275 0.4891 0.4666 -0.0171 0.0720  0.0209  181 ILE A CA  
1111 C C   . ILE A 154 ? 0.8454 0.4726 0.4625 -0.0305 0.0707  0.0214  181 ILE A C   
1112 O O   . ILE A 154 ? 0.9618 0.5675 0.5769 -0.0264 0.0598  0.0216  181 ILE A O   
1113 C CB  . ILE A 154 ? 0.8751 0.5764 0.5399 -0.0136 0.0781  0.0129  181 ILE A CB  
1114 C CG1 . ILE A 154 ? 0.8183 0.5458 0.5002 0.0007  0.0781  0.0149  181 ILE A CG1 
1115 C CG2 . ILE A 154 ? 0.7806 0.4795 0.4529 -0.0119 0.0721  0.0067  181 ILE A CG2 
1116 C CD1 . ILE A 154 ? 0.7161 0.4798 0.4167 0.0054  0.0823  0.0091  181 ILE A CD1 
1117 N N   . ALA A 155 ? 0.8724 0.4920 0.4731 -0.0468 0.0829  0.0213  182 ALA A N   
1118 C CA  . ALA A 155 ? 0.9149 0.4996 0.4932 -0.0624 0.0849  0.0224  182 ALA A CA  
1119 C C   . ALA A 155 ? 0.9307 0.4645 0.4750 -0.0610 0.0715  0.0334  182 ALA A C   
1120 O O   . ALA A 155 ? 0.9752 0.4731 0.5024 -0.0678 0.0667  0.0359  182 ALA A O   
1121 C CB  . ALA A 155 ? 0.7752 0.3654 0.3451 -0.0822 0.1043  0.0190  182 ALA A CB  
1122 N N   . GLU A 156 ? 0.8807 0.4088 0.4145 -0.0519 0.0641  0.0396  183 GLU A N   
1123 C CA  . GLU A 156 ? 0.9777 0.4585 0.4783 -0.0491 0.0478  0.0496  183 GLU A CA  
1124 C C   . GLU A 156 ? 0.8798 0.3496 0.3964 -0.0338 0.0279  0.0492  183 GLU A C   
1125 O O   . GLU A 156 ? 1.0872 0.5140 0.5783 -0.0308 0.0116  0.0569  183 GLU A O   
1126 C CB  . GLU A 156 ? 1.0905 0.5715 0.5782 -0.0437 0.0440  0.0537  183 GLU A CB  
1127 C CG  . GLU A 156 ? 1.2441 0.7341 0.7155 -0.0579 0.0645  0.0524  183 GLU A CG  
1128 C CD  . GLU A 156 ? 1.3607 0.8126 0.7896 -0.0788 0.0755  0.0574  183 GLU A CD  
1129 O OE1 . GLU A 156 ? 1.1708 0.5755 0.5672 -0.0808 0.0622  0.0664  183 GLU A OE1 
1130 O OE2 . GLU A 156 ? 1.3553 0.8236 0.7839 -0.0934 0.0979  0.0522  183 GLU A OE2 
1131 N N   . ASN A 157 ? 0.8593 0.3658 0.4160 -0.0235 0.0289  0.0402  184 ASN A N   
1132 C CA  . ASN A 157 ? 0.9414 0.4428 0.5186 -0.0096 0.0143  0.0362  184 ASN A CA  
1133 C C   . ASN A 157 ? 1.0185 0.5007 0.5928 0.0043  -0.0060 0.0414  184 ASN A C   
1134 O O   . ASN A 157 ? 1.0025 0.4511 0.5694 0.0107  -0.0228 0.0437  184 ASN A O   
1135 C CB  . ASN A 157 ? 0.8333 0.3034 0.3991 -0.0174 0.0127  0.0349  184 ASN A CB  
1136 C CG  . ASN A 157 ? 0.9373 0.4096 0.5310 -0.0028 0.0016  0.0267  184 ASN A CG  
1137 O OD1 . ASN A 157 ? 0.9987 0.5059 0.6241 0.0102  0.0011  0.0197  184 ASN A OD1 
1138 N ND2 . ASN A 157 ? 0.9410 0.3738 0.5224 -0.0052 -0.0061 0.0270  184 ASN A ND2 
1139 N N   . LYS A 158 ? 0.9427 0.4465 0.5248 0.0094  -0.0056 0.0422  185 LYS A N   
1140 C CA  . LYS A 158 ? 0.9947 0.4910 0.5838 0.0227  -0.0245 0.0437  185 LYS A CA  
1141 C C   . LYS A 158 ? 0.9138 0.4525 0.5494 0.0351  -0.0217 0.0349  185 LYS A C   
1142 O O   . LYS A 158 ? 0.9652 0.5369 0.6185 0.0329  -0.0049 0.0304  185 LYS A O   
1143 C CB  . LYS A 158 ? 1.0622 0.5458 0.6219 0.0174  -0.0267 0.0504  185 LYS A CB  
1144 C CG  . LYS A 158 ? 0.9516 0.3918 0.4586 0.0029  -0.0258 0.0597  185 LYS A CG  
1145 C CD  . LYS A 158 ? 1.1080 0.5016 0.5939 0.0075  -0.0470 0.0658  185 LYS A CD  
1146 C CE  . LYS A 158 ? 1.0650 0.4085 0.4894 -0.0066 -0.0481 0.0777  185 LYS A CE  
1147 N NZ  . LYS A 158 ? 1.3498 0.6413 0.7485 0.0002  -0.0729 0.0860  185 LYS A NZ  
1148 N N   . THR A 159 ? 0.8745 0.4114 0.5294 0.0480  -0.0387 0.0324  186 THR A N   
1149 C CA  . THR A 159 ? 0.9524 0.5278 0.6513 0.0577  -0.0338 0.0239  186 THR A CA  
1150 C C   . THR A 159 ? 0.8415 0.4368 0.5435 0.0552  -0.0263 0.0258  186 THR A C   
1151 O O   . THR A 159 ? 0.8299 0.4576 0.5548 0.0562  -0.0111 0.0224  186 THR A O   
1152 C CB  . THR A 159 ? 0.7489 0.3194 0.4761 0.0721  -0.0530 0.0174  186 THR A CB  
1153 O OG1 . THR A 159 ? 0.9703 0.5204 0.6957 0.0754  -0.0591 0.0148  186 THR A OG1 
1154 C CG2 . THR A 159 ? 0.7714 0.3823 0.5451 0.0797  -0.0438 0.0075  186 THR A CG2 
1155 N N   . VAL A 160 ? 0.8595 0.4330 0.5361 0.0520  -0.0370 0.0311  187 VAL A N   
1156 C CA  . VAL A 160 ? 0.7555 0.3420 0.4298 0.0482  -0.0298 0.0321  187 VAL A CA  
1157 C C   . VAL A 160 ? 0.9313 0.4905 0.5582 0.0369  -0.0283 0.0391  187 VAL A C   
1158 O O   . VAL A 160 ? 0.9650 0.4899 0.5623 0.0361  -0.0456 0.0432  187 VAL A O   
1159 C CB  . VAL A 160 ? 0.7722 0.3639 0.4704 0.0566  -0.0450 0.0271  187 VAL A CB  
1160 C CG1 . VAL A 160 ? 0.7354 0.3360 0.4286 0.0514  -0.0370 0.0273  187 VAL A CG1 
1161 C CG2 . VAL A 160 ? 0.9144 0.5348 0.6620 0.0661  -0.0425 0.0188  187 VAL A CG2 
1162 N N   . VAL A 161 ? 0.8839 0.4576 0.5027 0.0283  -0.0079 0.0402  188 VAL A N   
1163 C CA  . VAL A 161 ? 0.9503 0.5032 0.5277 0.0160  -0.0010 0.0446  188 VAL A CA  
1164 C C   . VAL A 161 ? 0.8303 0.4070 0.4153 0.0133  0.0156  0.0417  188 VAL A C   
1165 O O   . VAL A 161 ? 0.8252 0.4337 0.4410 0.0176  0.0273  0.0389  188 VAL A O   
1166 C CB  . VAL A 161 ? 0.9501 0.4913 0.5083 0.0058  0.0088  0.0475  188 VAL A CB  
1167 C CG1 . VAL A 161 ? 0.7912 0.3691 0.3794 0.0058  0.0259  0.0428  188 VAL A CG1 
1168 C CG2 . VAL A 161 ? 0.8453 0.3623 0.3593 -0.0088 0.0176  0.0515  188 VAL A CG2 
1169 N N   . ALA A 162 ? 0.9520 0.5107 0.5066 0.0067  0.0161  0.0422  189 ALA A N   
1170 C CA  . ALA A 162 ? 0.8082 0.3840 0.3673 0.0045  0.0312  0.0382  189 ALA A CA  
1171 C C   . ALA A 162 ? 0.8585 0.4216 0.3825 -0.0090 0.0464  0.0383  189 ALA A C   
1172 O O   . ALA A 162 ? 1.0187 0.5480 0.5017 -0.0174 0.0406  0.0423  189 ALA A O   
1173 C CB  . ALA A 162 ? 0.7856 0.3547 0.3456 0.0092  0.0195  0.0346  189 ALA A CB  
1174 N N   . PRO A 163 ? 0.9236 0.5122 0.4625 -0.0112 0.0662  0.0338  190 PRO A N   
1175 C CA  . PRO A 163 ? 0.9049 0.4853 0.4157 -0.0242 0.0833  0.0308  190 PRO A CA  
1176 C C   . PRO A 163 ? 0.8990 0.4652 0.3884 -0.0254 0.0836  0.0262  190 PRO A C   
1177 O O   . PRO A 163 ? 1.0001 0.5797 0.5130 -0.0158 0.0802  0.0224  190 PRO A O   
1178 C CB  . PRO A 163 ? 0.8189 0.4377 0.3642 -0.0224 0.1014  0.0257  190 PRO A CB  
1179 C CG  . PRO A 163 ? 0.7510 0.3926 0.3338 -0.0071 0.0942  0.0260  190 PRO A CG  
1180 C CD  . PRO A 163 ? 0.8147 0.4402 0.3965 -0.0016 0.0740  0.0313  190 PRO A CD  
1181 N N   . MET A 164 ? 0.8810 0.3862 0.4513 -0.0446 0.1507  -0.0148 191 MET A N   
1182 C CA  . MET A 164 ? 0.9395 0.4304 0.4829 -0.0424 0.1526  -0.0202 191 MET A CA  
1183 C C   . MET A 164 ? 0.9687 0.4856 0.5437 -0.0430 0.1689  -0.0313 191 MET A C   
1184 O O   . MET A 164 ? 0.9718 0.4973 0.5549 -0.0520 0.1905  -0.0355 191 MET A O   
1185 C CB  . MET A 164 ? 0.9664 0.4183 0.4510 -0.0498 0.1629  -0.0163 191 MET A CB  
1186 C CG  . MET A 164 ? 0.9398 0.3741 0.3874 -0.0450 0.1587  -0.0228 191 MET A CG  
1187 S SD  . MET A 164 ? 1.2398 0.6313 0.6143 -0.0529 0.1790  -0.0197 191 MET A SD  
1188 C CE  . MET A 164 ? 1.1208 0.5330 0.5262 -0.0667 0.2164  -0.0281 191 MET A CE  
1189 N N   . LEU A 165 ? 0.9326 0.4620 0.5286 -0.0332 0.1597  -0.0364 192 LEU A N   
1190 C CA  . LEU A 165 ? 0.9440 0.4952 0.5713 -0.0302 0.1739  -0.0461 192 LEU A CA  
1191 C C   . LEU A 165 ? 0.9792 0.5097 0.5742 -0.0330 0.1849  -0.0567 192 LEU A C   
1192 O O   . LEU A 165 ? 0.9824 0.4886 0.5424 -0.0315 0.1723  -0.0585 192 LEU A O   
1193 C CB  . LEU A 165 ? 0.9225 0.4941 0.5907 -0.0176 0.1615  -0.0449 192 LEU A CB  
1194 C CG  . LEU A 165 ? 0.9138 0.5075 0.6116 -0.0125 0.1514  -0.0351 192 LEU A CG  
1195 C CD1 . LEU A 165 ? 0.8683 0.4776 0.6008 0.0008  0.1432  -0.0320 192 LEU A CD1 
1196 C CD2 . LEU A 165 ? 0.7134 0.3314 0.4318 -0.0171 0.1651  -0.0371 192 LEU A CD2 
1197 N N   . ASP A 166 ? 0.9687 0.5109 0.5763 -0.0363 0.2082  -0.0653 193 ASP A N   
1198 C CA  . ASP A 166 ? 0.9980 0.5219 0.5754 -0.0386 0.2226  -0.0774 193 ASP A CA  
1199 C C   . ASP A 166 ? 1.0393 0.5683 0.6395 -0.0283 0.2171  -0.0877 193 ASP A C   
1200 O O   . ASP A 166 ? 1.0184 0.5715 0.6675 -0.0195 0.2137  -0.0857 193 ASP A O   
1201 C CB  . ASP A 166 ? 1.1275 0.6627 0.7127 -0.0464 0.2529  -0.0838 193 ASP A CB  
1202 C CG  . ASP A 166 ? 1.2865 0.8101 0.8464 -0.0597 0.2639  -0.0754 193 ASP A CG  
1203 O OD1 . ASP A 166 ? 1.3014 0.7942 0.8151 -0.0625 0.2521  -0.0662 193 ASP A OD1 
1204 O OD2 . ASP A 166 ? 1.2909 0.8361 0.8794 -0.0672 0.2847  -0.0785 193 ASP A OD2 
1205 N N   . SER A 167 ? 1.1182 0.6221 0.6805 -0.0292 0.2167  -0.0990 194 SER A N   
1206 C CA  . SER A 167 ? 0.9824 0.4854 0.5629 -0.0222 0.2159  -0.1131 194 SER A CA  
1207 C C   . SER A 167 ? 1.0064 0.4935 0.5542 -0.0258 0.2371  -0.1297 194 SER A C   
1208 O O   . SER A 167 ? 1.1373 0.6124 0.6444 -0.0336 0.2513  -0.1285 194 SER A O   
1209 C CB  . SER A 167 ? 1.0595 0.5489 0.6311 -0.0193 0.1889  -0.1152 194 SER A CB  
1210 O OG  . SER A 167 ? 1.0666 0.5291 0.5788 -0.0237 0.1814  -0.1235 194 SER A OG  
1211 N N   . ARG A 168 ? 1.1658 0.6504 0.7310 -0.0200 0.2412  -0.1456 195 ARG A N   
1212 C CA  . ARG A 168 ? 1.1084 0.5768 0.6425 -0.0223 0.2614  -0.1647 195 ARG A CA  
1213 C C   . ARG A 168 ? 1.0733 0.5108 0.5370 -0.0275 0.2498  -0.1727 195 ARG A C   
1214 O O   . ARG A 168 ? 1.2615 0.6824 0.6829 -0.0304 0.2677  -0.1860 195 ARG A O   
1215 C CB  . ARG A 168 ? 1.1390 0.6096 0.7116 -0.0140 0.2681  -0.1810 195 ARG A CB  
1216 C CG  . ARG A 168 ? 1.0097 0.4692 0.5916 -0.0117 0.2430  -0.1867 195 ARG A CG  
1217 C CD  . ARG A 168 ? 1.0177 0.4711 0.6328 -0.0055 0.2529  -0.2050 195 ARG A CD  
1218 N NE  . ARG A 168 ? 1.1325 0.5749 0.7597 -0.0063 0.2306  -0.2120 195 ARG A NE  
1219 C CZ  . ARG A 168 ? 1.1332 0.5558 0.7225 -0.0126 0.2162  -0.2313 195 ARG A CZ  
1220 N NH1 . ARG A 168 ? 1.1048 0.5139 0.6352 -0.0169 0.2214  -0.2439 195 ARG A NH1 
1221 N NH2 . ARG A 168 ? 1.0487 0.4671 0.6604 -0.0144 0.1959  -0.2382 195 ARG A NH2 
1222 N N   . ALA A 169 ? 1.1923 0.6228 0.6417 -0.0273 0.2203  -0.1655 196 ALA A N   
1223 C CA  . ALA A 169 ? 1.1201 0.5244 0.5040 -0.0289 0.2036  -0.1730 196 ALA A CA  
1224 C C   . ALA A 169 ? 1.1867 0.5853 0.5419 -0.0304 0.1882  -0.1512 196 ALA A C   
1225 O O   . ALA A 169 ? 1.2194 0.6305 0.5976 -0.0329 0.1967  -0.1331 196 ALA A O   
1226 C CB  . ALA A 169 ? 1.1224 0.5239 0.5203 -0.0256 0.1801  -0.1912 196 ALA A CB  
1227 N N   . ALA A 170 ? 1.1578 0.5372 0.4624 -0.0279 0.1641  -0.1539 197 ALA A N   
1228 C CA  . ALA A 170 ? 1.2314 0.6015 0.5067 -0.0264 0.1473  -0.1334 197 ALA A CA  
1229 C C   . ALA A 170 ? 1.2873 0.6790 0.6186 -0.0234 0.1262  -0.1218 197 ALA A C   
1230 O O   . ALA A 170 ? 1.2080 0.5951 0.5270 -0.0220 0.1162  -0.1034 197 ALA A O   
1231 C CB  . ALA A 170 ? 1.2271 0.5723 0.4318 -0.0208 0.1251  -0.1401 197 ALA A CB  
1232 N N   . TYR A 171 ? 1.1436 0.5560 0.5342 -0.0219 0.1214  -0.1318 198 TYR A N   
1233 C CA  . TYR A 171 ? 1.0667 0.4992 0.5099 -0.0188 0.1051  -0.1207 198 TYR A CA  
1234 C C   . TYR A 171 ? 1.0321 0.4762 0.4956 -0.0204 0.1181  -0.0999 198 TYR A C   
1235 O O   . TYR A 171 ? 1.0858 0.5336 0.5527 -0.0244 0.1433  -0.0981 198 TYR A O   
1236 C CB  . TYR A 171 ? 0.9741 0.4227 0.4762 -0.0175 0.1064  -0.1332 198 TYR A CB  
1237 C CG  . TYR A 171 ? 1.0245 0.4927 0.5805 -0.0140 0.0937  -0.1215 198 TYR A CG  
1238 C CD1 . TYR A 171 ? 1.0235 0.5093 0.6178 -0.0118 0.1070  -0.1057 198 TYR A CD1 
1239 C CD2 . TYR A 171 ? 0.9205 0.3914 0.4896 -0.0124 0.0688  -0.1276 198 TYR A CD2 
1240 C CE1 . TYR A 171 ? 0.8378 0.3398 0.4750 -0.0075 0.0972  -0.0947 198 TYR A CE1 
1241 C CE2 . TYR A 171 ? 1.0008 0.4891 0.6187 -0.0094 0.0609  -0.1169 198 TYR A CE2 
1242 C CZ  . TYR A 171 ? 0.8781 0.3801 0.5267 -0.0067 0.0759  -0.0997 198 TYR A CZ  
1243 O OH  . TYR A 171 ? 0.9518 0.4695 0.6431 -0.0027 0.0696  -0.0887 198 TYR A OH  
1244 N N   . SER A 172 ? 1.0074 0.4589 0.4866 -0.0172 0.1004  -0.0861 199 SER A N   
1245 C CA  . SER A 172 ? 0.9890 0.4544 0.4942 -0.0182 0.1086  -0.0692 199 SER A CA  
1246 C C   . SER A 172 ? 1.0001 0.4782 0.5368 -0.0123 0.0869  -0.0609 199 SER A C   
1247 O O   . SER A 172 ? 1.0537 0.5313 0.5955 -0.0084 0.0676  -0.0683 199 SER A O   
1248 C CB  . SER A 172 ? 1.0447 0.4911 0.5043 -0.0237 0.1189  -0.0584 199 SER A CB  
1249 O OG  . SER A 172 ? 1.0106 0.4731 0.5006 -0.0273 0.1314  -0.0478 199 SER A OG  
1250 N N   . ASN A 173 ? 0.9885 0.4796 0.5480 -0.0119 0.0906  -0.0473 200 ASN A N   
1251 C CA  . ASN A 173 ? 0.8420 0.3474 0.4346 -0.0057 0.0746  -0.0393 200 ASN A CA  
1252 C C   . ASN A 173 ? 0.9671 0.4576 0.5307 -0.0033 0.0575  -0.0302 200 ASN A C   
1253 O O   . ASN A 173 ? 1.0344 0.5321 0.6128 -0.0011 0.0548  -0.0195 200 ASN A O   
1254 C CB  . ASN A 173 ? 0.8981 0.4273 0.5310 -0.0043 0.0866  -0.0315 200 ASN A CB  
1255 C CG  . ASN A 173 ? 0.9840 0.5118 0.6016 -0.0110 0.1014  -0.0263 200 ASN A CG  
1256 O OD1 . ASN A 173 ? 0.9641 0.4807 0.5569 -0.0177 0.1161  -0.0318 200 ASN A OD1 
1257 N ND2 . ASN A 173 ? 0.9245 0.4637 0.5579 -0.0099 0.0990  -0.0173 200 ASN A ND2 
1258 N N   . PHE A 174 ? 1.0050 0.4741 0.5253 -0.0021 0.0453  -0.0349 201 PHE A N   
1259 C CA  . PHE A 174 ? 1.0535 0.5066 0.5446 0.0039  0.0269  -0.0257 201 PHE A CA  
1260 C C   . PHE A 174 ? 1.0781 0.5146 0.5277 0.0085  0.0089  -0.0350 201 PHE A C   
1261 O O   . PHE A 174 ? 1.0781 0.5093 0.5094 0.0047  0.0155  -0.0480 201 PHE A O   
1262 C CB  . PHE A 174 ? 1.1000 0.5328 0.5593 -0.0002 0.0404  -0.0119 201 PHE A CB  
1263 C CG  . PHE A 174 ? 0.9930 0.3986 0.3972 -0.0059 0.0549  -0.0130 201 PHE A CG  
1264 C CD1 . PHE A 174 ? 1.1439 0.5558 0.5544 -0.0153 0.0799  -0.0200 201 PHE A CD1 
1265 C CD2 . PHE A 174 ? 1.0822 0.4556 0.4272 -0.0003 0.0445  -0.0063 201 PHE A CD2 
1266 C CE1 . PHE A 174 ? 1.1711 0.5580 0.5308 -0.0208 0.0967  -0.0213 201 PHE A CE1 
1267 C CE2 . PHE A 174 ? 1.1607 0.5064 0.4497 -0.0048 0.0605  -0.0057 201 PHE A CE2 
1268 C CZ  . PHE A 174 ? 1.1377 0.4903 0.4346 -0.0160 0.0879  -0.0137 201 PHE A CZ  
1269 N N   . TRP A 175 ? 1.0823 0.5120 0.5173 0.0182  -0.0147 -0.0295 202 TRP A N   
1270 C CA  . TRP A 175 ? 1.1447 0.5573 0.5310 0.0262  -0.0361 -0.0355 202 TRP A CA  
1271 C C   . TRP A 175 ? 1.1062 0.4881 0.4401 0.0336  -0.0398 -0.0170 202 TRP A C   
1272 O O   . TRP A 175 ? 1.2711 0.6525 0.6232 0.0357  -0.0379 -0.0031 202 TRP A O   
1273 C CB  . TRP A 175 ? 1.0570 0.4921 0.4770 0.0344  -0.0659 -0.0473 202 TRP A CB  
1274 C CG  . TRP A 175 ? 1.1375 0.6007 0.6167 0.0275  -0.0630 -0.0639 202 TRP A CG  
1275 C CD1 . TRP A 175 ? 1.1075 0.5761 0.6080 0.0173  -0.0388 -0.0698 202 TRP A CD1 
1276 C CD2 . TRP A 175 ? 1.1074 0.5957 0.6344 0.0308  -0.0838 -0.0765 202 TRP A CD2 
1277 N NE1 . TRP A 175 ? 0.9870 0.4780 0.5424 0.0145  -0.0425 -0.0836 202 TRP A NE1 
1278 C CE2 . TRP A 175 ? 0.9491 0.4529 0.5230 0.0212  -0.0690 -0.0885 202 TRP A CE2 
1279 C CE3 . TRP A 175 ? 1.1532 0.6530 0.6907 0.0413  -0.1128 -0.0791 202 TRP A CE3 
1280 C CZ2 . TRP A 175 ? 0.9546 0.4819 0.5848 0.0196  -0.0797 -0.1026 202 TRP A CZ2 
1281 C CZ3 . TRP A 175 ? 1.0867 0.6153 0.6839 0.0394  -0.1247 -0.0949 202 TRP A CZ3 
1282 C CH2 . TRP A 175 ? 0.9782 0.5188 0.6208 0.0276  -0.1070 -0.1063 202 TRP A CH2 
1283 N N   . CYS A 176 ? 1.2347 0.5886 0.5015 0.0385  -0.0446 -0.0168 203 CYS A N   
1284 C CA  . CYS A 176 ? 1.3842 0.7035 0.5951 0.0489  -0.0505 0.0022  203 CYS A CA  
1285 C C   . CYS A 176 ? 1.4937 0.8159 0.6938 0.0679  -0.0884 0.0012  203 CYS A C   
1286 O O   . CYS A 176 ? 1.4754 0.7717 0.6406 0.0803  -0.0967 0.0190  203 CYS A O   
1287 C CB  . CYS A 176 ? 1.3804 0.6625 0.5160 0.0458  -0.0319 0.0072  203 CYS A CB  
1288 S SG  . CYS A 176 ? 1.7124 0.9796 0.8504 0.0264  0.0146  0.0181  203 CYS A SG  
1289 N N   . GLY A 177 ? 1.4407 0.7938 0.6728 0.0708  -0.1111 -0.0195 204 GLY A N   
1290 C CA  . GLY A 177 ? 1.4427 0.8063 0.6731 0.0887  -0.1492 -0.0243 204 GLY A CA  
1291 C C   . GLY A 177 ? 1.3600 0.7692 0.6683 0.0856  -0.1648 -0.0446 204 GLY A C   
1292 O O   . GLY A 177 ? 1.3009 0.7282 0.6480 0.0708  -0.1497 -0.0590 204 GLY A O   
1293 N N   . MET A 178 ? 1.3407 0.7676 0.6736 0.1001  -0.1940 -0.0454 205 MET A N   
1294 C CA  . MET A 178 ? 1.3867 0.8573 0.7962 0.0978  -0.2094 -0.0645 205 MET A CA  
1295 C C   . MET A 178 ? 1.3992 0.8851 0.8045 0.1167  -0.2506 -0.0741 205 MET A C   
1296 O O   . MET A 178 ? 1.5101 0.9791 0.8814 0.1349  -0.2649 -0.0572 205 MET A O   
1297 C CB  . MET A 178 ? 1.2636 0.7509 0.7373 0.0932  -0.1936 -0.0535 205 MET A CB  
1298 C CG  . MET A 178 ? 1.3223 0.8525 0.8768 0.0895  -0.2034 -0.0710 205 MET A CG  
1299 S SD  . MET A 178 ? 1.3528 0.8995 0.9717 0.0868  -0.1835 -0.0564 205 MET A SD  
1300 C CE  . MET A 178 ? 0.9900 0.5160 0.5918 0.0705  -0.1440 -0.0452 205 MET A CE  
1301 N N   . THR A 179 ? 1.5030 1.0210 0.9449 0.1129  -0.2697 -0.1021 206 THR A N   
1302 C CA  . THR A 179 ? 1.4755 1.0166 0.9217 0.1301  -0.3118 -0.1168 206 THR A CA  
1303 C C   . THR A 179 ? 1.4837 1.0550 0.9997 0.1383  -0.3224 -0.1122 206 THR A C   
1304 O O   . THR A 179 ? 1.3656 0.9389 0.9235 0.1299  -0.2966 -0.0988 206 THR A O   
1305 C CB  . THR A 179 ? 1.3635 0.9315 0.8329 0.1206  -0.3278 -0.1523 206 THR A CB  
1306 O OG1 . THR A 179 ? 1.4848 1.0896 1.0494 0.1057  -0.3192 -0.1671 206 THR A OG1 
1307 C CG2 . THR A 179 ? 1.4243 0.9645 0.8420 0.1073  -0.3057 -0.1582 206 THR A CG2 
1308 N N   . SER A 180 ? 1.6663 1.2634 1.1949 0.1559  -0.3614 -0.1248 207 SER A N   
1309 C CA  . SER A 180 ? 1.5790 1.2099 1.1785 0.1651  -0.3735 -0.1243 207 SER A CA  
1310 C C   . SER A 180 ? 1.4756 1.1474 1.1708 0.1451  -0.3607 -0.1444 207 SER A C   
1311 O O   . SER A 180 ? 1.3543 1.0541 1.1145 0.1492  -0.3621 -0.1431 207 SER A O   
1312 C CB  . SER A 180 ? 1.5336 1.1851 1.1231 0.1909  -0.4208 -0.1346 207 SER A CB  
1313 O OG  . SER A 180 ? 1.5236 1.1962 1.1082 0.1871  -0.4457 -0.1658 207 SER A OG  
1314 N N   . GLN A 181 ? 1.4723 1.1458 1.1774 0.1241  -0.3461 -0.1622 208 GLN A N   
1315 C CA  . GLN A 181 ? 1.3309 1.0361 1.1228 0.1043  -0.3304 -0.1800 208 GLN A CA  
1316 C C   . GLN A 181 ? 1.2280 0.9105 1.0226 0.0855  -0.2866 -0.1669 208 GLN A C   
1317 O O   . GLN A 181 ? 1.3515 1.0497 1.2028 0.0680  -0.2696 -0.1808 208 GLN A O   
1318 C CB  . GLN A 181 ? 1.4298 1.1613 1.2458 0.0961  -0.3535 -0.2173 208 GLN A CB  
1319 C CG  . GLN A 181 ? 1.4061 1.1636 1.2150 0.1166  -0.4016 -0.2334 208 GLN A CG  
1320 C CD  . GLN A 181 ? 1.6278 1.4191 1.4743 0.1067  -0.4259 -0.2753 208 GLN A CD  
1321 O OE1 . GLN A 181 ? 1.7618 1.5511 1.6336 0.0840  -0.4053 -0.2923 208 GLN A OE1 
1322 N NE2 . GLN A 181 ? 1.6864 1.5096 1.5386 0.1245  -0.4708 -0.2934 208 GLN A NE2 
1323 N N   . GLY A 182 ? 1.2366 0.8824 0.9724 0.0892  -0.2679 -0.1405 209 GLY A N   
1324 C CA  . GLY A 182 ? 1.1537 0.7819 0.8923 0.0742  -0.2291 -0.1277 209 GLY A CA  
1325 C C   . GLY A 182 ? 1.2243 0.8334 0.9287 0.0615  -0.2158 -0.1382 209 GLY A C   
1326 O O   . GLY A 182 ? 1.2989 0.8979 1.0134 0.0496  -0.1846 -0.1304 209 GLY A O   
1327 N N   . TYR A 183 ? 1.3871 0.9916 1.0505 0.0650  -0.2386 -0.1562 210 TYR A N   
1328 C CA  . TYR A 183 ? 1.3604 0.9469 0.9907 0.0536  -0.2255 -0.1692 210 TYR A CA  
1329 C C   . TYR A 183 ? 1.2485 0.7959 0.7990 0.0575  -0.2097 -0.1482 210 TYR A C   
1330 O O   . TYR A 183 ? 1.3503 0.8818 0.8572 0.0714  -0.2188 -0.1288 210 TYR A O   
1331 C CB  . TYR A 183 ? 1.3899 0.9890 1.0085 0.0552  -0.2566 -0.2011 210 TYR A CB  
1332 C CG  . TYR A 183 ? 1.4839 1.1245 1.1841 0.0507  -0.2755 -0.2256 210 TYR A CG  
1333 C CD1 . TYR A 183 ? 1.5416 1.1992 1.3213 0.0370  -0.2522 -0.2251 210 TYR A CD1 
1334 C CD2 . TYR A 183 ? 1.4880 1.1515 1.1860 0.0604  -0.3163 -0.2493 210 TYR A CD2 
1335 C CE1 . TYR A 183 ? 1.5962 1.2908 1.4540 0.0310  -0.2655 -0.2475 210 TYR A CE1 
1336 C CE2 . TYR A 183 ? 1.6442 1.3496 1.4240 0.0546  -0.3330 -0.2742 210 TYR A CE2 
1337 C CZ  . TYR A 183 ? 1.6855 1.4054 1.5464 0.0387  -0.3057 -0.2731 210 TYR A CZ  
1338 O OH  . TYR A 183 ? 1.5125 1.2729 1.4580 0.0310  -0.3185 -0.2979 210 TYR A OH  
1339 N N   . TYR A 184 ? 1.1166 0.6479 0.6511 0.0451  -0.1839 -0.1525 211 TYR A N   
1340 C CA  . TYR A 184 ? 1.2767 0.7732 0.7405 0.0462  -0.1653 -0.1359 211 TYR A CA  
1341 C C   . TYR A 184 ? 1.4448 0.9222 0.8305 0.0586  -0.1889 -0.1405 211 TYR A C   
1342 O O   . TYR A 184 ? 1.4031 0.8921 0.7827 0.0608  -0.2129 -0.1658 211 TYR A O   
1343 C CB  . TYR A 184 ? 1.2176 0.7054 0.6856 0.0315  -0.1342 -0.1436 211 TYR A CB  
1344 C CG  . TYR A 184 ? 1.3605 0.8154 0.7569 0.0312  -0.1144 -0.1322 211 TYR A CG  
1345 C CD1 . TYR A 184 ? 1.3719 0.8132 0.7592 0.0297  -0.0907 -0.1067 211 TYR A CD1 
1346 C CD2 . TYR A 184 ? 1.3110 0.7491 0.6498 0.0317  -0.1183 -0.1484 211 TYR A CD2 
1347 C CE1 . TYR A 184 ? 1.4771 0.8898 0.8049 0.0274  -0.0699 -0.0973 211 TYR A CE1 
1348 C CE2 . TYR A 184 ? 1.5174 0.9250 0.7913 0.0308  -0.0966 -0.1376 211 TYR A CE2 
1349 C CZ  . TYR A 184 ? 1.5902 0.9855 0.8613 0.0280  -0.0715 -0.1118 211 TYR A CZ  
1350 O OH  . TYR A 184 ? 1.5684 0.9348 0.7808 0.0252  -0.0471 -0.1020 211 TYR A OH  
1351 N N   . LYS A 185 ? 1.4395 0.8867 0.7646 0.0669  -0.1815 -0.1159 212 LYS A N   
1352 C CA  . LYS A 185 ? 1.4608 0.8814 0.7002 0.0810  -0.1988 -0.1129 212 LYS A CA  
1353 C C   . LYS A 185 ? 1.5027 0.8842 0.6806 0.0757  -0.1654 -0.0946 212 LYS A C   
1354 O O   . LYS A 185 ? 1.6294 1.0000 0.8192 0.0711  -0.1420 -0.0724 212 LYS A O   
1355 C CB  . LYS A 185 ? 1.6234 1.0436 0.8504 0.1014  -0.2276 -0.0976 212 LYS A CB  
1356 C CG  . LYS A 185 ? 1.5816 0.9695 0.7136 0.1200  -0.2455 -0.0892 212 LYS A CG  
1357 C CD  . LYS A 185 ? 1.7413 1.1289 0.8683 0.1424  -0.2735 -0.0725 212 LYS A CD  
1358 C CE  . LYS A 185 ? 1.9887 1.3402 1.0162 0.1644  -0.2914 -0.0602 212 LYS A CE  
1359 N NZ  . LYS A 185 ? 1.8124 1.1625 0.8364 0.1894  -0.3196 -0.0433 212 LYS A NZ  
1360 N N   . ARG A 186 ? 1.7931 1.1548 0.9073 0.0757  -0.1622 -0.1057 213 ARG A N   
1361 C CA  . ARG A 186 ? 1.8509 1.1764 0.9069 0.0697  -0.1277 -0.0905 213 ARG A CA  
1362 C C   . ARG A 186 ? 1.8207 1.1082 0.7960 0.0859  -0.1343 -0.0659 213 ARG A C   
1363 O O   . ARG A 186 ? 1.7976 1.0808 0.7288 0.1039  -0.1675 -0.0698 213 ARG A O   
1364 C CB  . ARG A 186 ? 1.9152 1.2347 0.9391 0.0619  -0.1155 -0.1136 213 ARG A CB  
1365 C CG  . ARG A 186 ? 2.0410 1.3354 1.0378 0.0498  -0.0709 -0.1018 213 ARG A CG  
1366 C CD  . ARG A 186 ? 2.4208 1.7102 1.3897 0.0427  -0.0564 -0.1262 213 ARG A CD  
1367 N NE  . ARG A 186 ? 2.4100 1.6978 1.4049 0.0272  -0.0140 -0.1230 213 ARG A NE  
1368 C CZ  . ARG A 186 ? 2.5118 1.7949 1.4896 0.0201  0.0093  -0.1383 213 ARG A CZ  
1369 N NH1 . ARG A 186 ? 2.2964 1.5836 1.2436 0.0255  -0.0043 -0.1564 213 ARG A NH1 
1370 N NH2 . ARG A 186 ? 2.3005 1.5833 1.3047 0.0079  0.0468  -0.1344 213 ARG A NH2 
1371 N N   . THR A 187 ? 1.7745 1.0344 0.7323 0.0798  -0.1026 -0.0407 214 THR A N   
1372 C CA  . THR A 187 ? 1.8466 1.0663 0.7382 0.0916  -0.0980 -0.0134 214 THR A CA  
1373 C C   . THR A 187 ? 1.8995 1.0963 0.7601 0.0789  -0.0560 -0.0049 214 THR A C   
1374 O O   . THR A 187 ? 1.7764 0.9811 0.6591 0.0615  -0.0296 -0.0165 214 THR A O   
1375 C CB  . THR A 187 ? 1.8409 1.0528 0.7610 0.0944  -0.0962 0.0098  214 THR A CB  
1376 O OG1 . THR A 187 ? 1.7540 0.9625 0.7065 0.0743  -0.0565 0.0179  214 THR A OG1 
1377 C CG2 . THR A 187 ? 1.7616 1.0173 0.7596 0.0996  -0.1265 -0.0019 214 THR A CG2 
1378 N N   . PRO A 188 ? 1.9046 1.0737 0.7162 0.0878  -0.0483 0.0140  215 PRO A N   
1379 C CA  . PRO A 188 ? 1.9282 1.0751 0.7135 0.0749  -0.0066 0.0219  215 PRO A CA  
1380 C C   . PRO A 188 ? 1.7158 0.8564 0.5394 0.0561  0.0289  0.0326  215 PRO A C   
1381 O O   . PRO A 188 ? 1.7483 0.8844 0.5719 0.0406  0.0640  0.0303  215 PRO A O   
1382 C CB  . PRO A 188 ? 1.8210 0.9374 0.5490 0.0910  -0.0098 0.0420  215 PRO A CB  
1383 C CG  . PRO A 188 ? 1.7896 0.9212 0.5063 0.1134  -0.0572 0.0353  215 PRO A CG  
1384 C CD  . PRO A 188 ? 1.8918 1.0508 0.6687 0.1112  -0.0780 0.0256  215 PRO A CD  
1385 N N   . ALA A 189 ? 1.5685 0.7122 0.4284 0.0570  0.0202  0.0427  216 ALA A N   
1386 C CA  . ALA A 189 ? 1.7287 0.8693 0.6270 0.0395  0.0518  0.0518  216 ALA A CA  
1387 C C   . ALA A 189 ? 1.7192 0.8871 0.6595 0.0227  0.0676  0.0342  216 ALA A C   
1388 O O   . ALA A 189 ? 1.7298 0.8995 0.6997 0.0065  0.0987  0.0381  216 ALA A O   
1389 C CB  . ALA A 189 ? 1.6591 0.7977 0.5859 0.0463  0.0368  0.0657  216 ALA A CB  
1390 N N   . TYR A 190 ? 1.7123 0.9049 0.6635 0.0265  0.0469  0.0125  217 TYR A N   
1391 C CA  . TYR A 190 ? 1.5791 0.8122 0.6049 0.0131  0.0584  -0.0054 217 TYR A CA  
1392 C C   . TYR A 190 ? 1.5931 0.8195 0.6082 -0.0019 0.0984  -0.0100 217 TYR A C   
1393 O O   . TYR A 190 ? 1.4951 0.7408 0.5641 -0.0147 0.1211  -0.0099 217 TYR A O   
1394 C CB  . TYR A 190 ? 1.4741 0.7364 0.5251 0.0194  0.0301  -0.0292 217 TYR A CB  
1395 C CG  . TYR A 190 ? 1.3451 0.6454 0.4750 0.0083  0.0405  -0.0445 217 TYR A CG  
1396 C CD1 . TYR A 190 ? 1.3313 0.6365 0.4641 -0.0010 0.0642  -0.0598 217 TYR A CD1 
1397 C CD2 . TYR A 190 ? 1.2523 0.5816 0.4518 0.0087  0.0282  -0.0424 217 TYR A CD2 
1398 C CE1 . TYR A 190 ? 1.3069 0.6438 0.5099 -0.0082 0.0738  -0.0715 217 TYR A CE1 
1399 C CE2 . TYR A 190 ? 1.2853 0.6455 0.5512 0.0009  0.0385  -0.0533 217 TYR A CE2 
1400 C CZ  . TYR A 190 ? 1.3119 0.6751 0.5794 -0.0068 0.0607  -0.0672 217 TYR A CZ  
1401 O OH  . TYR A 190 ? 1.1684 0.5595 0.5002 -0.0117 0.0709  -0.0761 217 TYR A OH  
1402 N N   . ILE A 191 ? 1.5752 0.7808 0.5302 0.0006  0.1063  -0.0148 218 ILE A N   
1403 C CA  . ILE A 191 ? 1.5845 0.7937 0.5451 -0.0126 0.1430  -0.0222 218 ILE A CA  
1404 C C   . ILE A 191 ? 1.5634 0.7620 0.5380 -0.0257 0.1771  -0.0049 218 ILE A C   
1405 O O   . ILE A 191 ? 1.6195 0.8378 0.6372 -0.0392 0.2035  -0.0129 218 ILE A O   
1406 C CB  . ILE A 191 ? 1.6748 0.8727 0.5834 -0.0057 0.1413  -0.0296 218 ILE A CB  
1407 C CG1 . ILE A 191 ? 1.6484 0.8633 0.5549 0.0046  0.1073  -0.0524 218 ILE A CG1 
1408 C CG2 . ILE A 191 ? 1.4995 0.7016 0.4151 -0.0186 0.1802  -0.0373 218 ILE A CG2 
1409 C CD1 . ILE A 191 ? 1.7366 0.9800 0.7005 -0.0038 0.1119  -0.0757 218 ILE A CD1 
1410 N N   . PRO A 192 ? 1.6718 0.8419 0.6176 -0.0225 0.1786  0.0164  219 PRO A N   
1411 C CA  . PRO A 192 ? 1.6076 0.7694 0.5756 -0.0377 0.2123  0.0280  219 PRO A CA  
1412 C C   . PRO A 192 ? 1.4955 0.6809 0.5248 -0.0478 0.2165  0.0269  219 PRO A C   
1413 O O   . PRO A 192 ? 1.5043 0.7022 0.5701 -0.0639 0.2468  0.0242  219 PRO A O   
1414 C CB  . PRO A 192 ? 1.5525 0.6777 0.4787 -0.0285 0.2059  0.0490  219 PRO A CB  
1415 C CG  . PRO A 192 ? 1.5619 0.6760 0.4334 -0.0097 0.1786  0.0475  219 PRO A CG  
1416 C CD  . PRO A 192 ? 1.6127 0.7574 0.5071 -0.0048 0.1520  0.0289  219 PRO A CD  
1417 N N   . ILE A 193 ? 1.4641 0.6580 0.5067 -0.0383 0.1863  0.0283  220 ILE A N   
1418 C CA  . ILE A 193 ? 1.3989 0.6278 0.5166 -0.0453 0.1848  0.0246  220 ILE A CA  
1419 C C   . ILE A 193 ? 1.3111 0.5822 0.4825 -0.0515 0.1942  0.0044  220 ILE A C   
1420 O O   . ILE A 193 ? 1.3471 0.6441 0.5723 -0.0627 0.2125  0.0005  220 ILE A O   
1421 C CB  . ILE A 193 ? 1.3771 0.6167 0.5165 -0.0312 0.1466  0.0285  220 ILE A CB  
1422 C CG1 . ILE A 193 ? 1.3848 0.5828 0.4784 -0.0238 0.1396  0.0497  220 ILE A CG1 
1423 C CG2 . ILE A 193 ? 1.3021 0.5841 0.5229 -0.0362 0.1433  0.0222  220 ILE A CG2 
1424 C CD1 . ILE A 193 ? 1.3083 0.5160 0.4201 -0.0077 0.1023  0.0530  220 ILE A CD1 
1425 N N   . ARG A 194 ? 1.3378 0.6160 0.4958 -0.0436 0.1813  -0.0098 221 ARG A N   
1426 C CA  . ARG A 194 ? 1.3173 0.6315 0.5264 -0.0470 0.1887  -0.0288 221 ARG A CA  
1427 C C   . ARG A 194 ? 1.3006 0.6162 0.5112 -0.0598 0.2282  -0.0339 221 ARG A C   
1428 O O   . ARG A 194 ? 1.3536 0.7037 0.6252 -0.0651 0.2408  -0.0428 221 ARG A O   
1429 C CB  . ARG A 194 ? 1.2309 0.5455 0.4200 -0.0369 0.1680  -0.0445 221 ARG A CB  
1430 C CG  . ARG A 194 ? 1.2496 0.5930 0.4849 -0.0391 0.1773  -0.0644 221 ARG A CG  
1431 C CD  . ARG A 194 ? 1.1685 0.5485 0.4824 -0.0380 0.1678  -0.0646 221 ARG A CD  
1432 N NE  . ARG A 194 ? 1.2509 0.6539 0.6070 -0.0383 0.1793  -0.0810 221 ARG A NE  
1433 C CZ  . ARG A 194 ? 1.2609 0.6804 0.6471 -0.0441 0.2067  -0.0840 221 ARG A CZ  
1434 N NH1 . ARG A 194 ? 1.2227 0.6415 0.6066 -0.0527 0.2262  -0.0735 221 ARG A NH1 
1435 N NH2 . ARG A 194 ? 1.1876 0.6250 0.6100 -0.0411 0.2152  -0.0987 221 ARG A NH2 
1436 N N   . LYS A 195 ? 1.2943 0.5735 0.4388 -0.0638 0.2488  -0.0279 222 LYS A N   
1437 C CA  . LYS A 195 ? 1.3416 0.6221 0.4882 -0.0764 0.2884  -0.0328 222 LYS A CA  
1438 C C   . LYS A 195 ? 1.3201 0.6001 0.4923 -0.0907 0.3117  -0.0205 222 LYS A C   
1439 O O   . LYS A 195 ? 1.4168 0.7008 0.6009 -0.1020 0.3424  -0.0235 222 LYS A O   
1440 C CB  . LYS A 195 ? 1.5671 0.8220 0.6569 -0.0726 0.2934  -0.0319 222 LYS A CB  
1441 C CG  . LYS A 195 ? 1.3725 0.6330 0.4431 -0.0616 0.2758  -0.0495 222 LYS A CG  
1442 C CD  . LYS A 195 ? 1.8105 1.0469 0.8215 -0.0578 0.2822  -0.0482 222 LYS A CD  
1443 C CE  . LYS A 195 ? 1.7930 1.0388 0.7899 -0.0490 0.2677  -0.0698 222 LYS A CE  
1444 N NZ  . LYS A 195 ? 1.8952 1.1194 0.8307 -0.0444 0.2743  -0.0694 222 LYS A NZ  
1445 N N   . ARG A 196 ? 1.3744 0.6523 0.5621 -0.0904 0.2961  -0.0085 223 ARG A N   
1446 C CA  . ARG A 196 ? 1.3058 0.5798 0.5164 -0.1048 0.3162  0.0013  223 ARG A CA  
1447 C C   . ARG A 196 ? 1.4572 0.6966 0.6300 -0.1101 0.3347  0.0113  223 ARG A C   
1448 O O   . ARG A 196 ? 1.3837 0.6267 0.5829 -0.1256 0.3633  0.0106  223 ARG A O   
1449 C CB  . ARG A 196 ? 1.3837 0.7058 0.6719 -0.1166 0.3351  -0.0131 223 ARG A CB  
1450 C CG  . ARG A 196 ? 1.2876 0.6550 0.6425 -0.1079 0.3066  -0.0207 223 ARG A CG  
1451 C CD  . ARG A 196 ? 1.1486 0.5633 0.5767 -0.1173 0.3233  -0.0333 223 ARG A CD  
1452 N NE  . ARG A 196 ? 1.3748 0.8304 0.8582 -0.1058 0.2969  -0.0392 223 ARG A NE  
1453 C CZ  . ARG A 196 ? 1.3649 0.8466 0.8737 -0.0951 0.2904  -0.0498 223 ARG A CZ  
1454 N NH1 . ARG A 196 ? 1.3085 0.7833 0.7968 -0.0947 0.3075  -0.0587 223 ARG A NH1 
1455 N NH2 . ARG A 196 ? 1.4311 0.9440 0.9853 -0.0841 0.2679  -0.0514 223 ARG A NH2 
1456 N N   . ASP A 197 ? 1.4978 0.7048 0.6090 -0.0965 0.3183  0.0197  224 ASP A N   
1457 C CA  . ASP A 197 ? 1.4755 0.6444 0.5437 -0.0975 0.3326  0.0330  224 ASP A CA  
1458 C C   . ASP A 197 ? 1.5949 0.7425 0.6644 -0.0969 0.3242  0.0485  224 ASP A C   
1459 O O   . ASP A 197 ? 1.6679 0.7985 0.7416 -0.1080 0.3488  0.0549  224 ASP A O   
1460 C CB  . ASP A 197 ? 1.5737 0.7184 0.5746 -0.0811 0.3171  0.0363  224 ASP A CB  
1461 C CG  . ASP A 197 ? 1.7351 0.8949 0.7306 -0.0837 0.3331  0.0206  224 ASP A CG  
1462 O OD1 . ASP A 197 ? 1.7129 0.9031 0.7596 -0.0969 0.3556  0.0075  224 ASP A OD1 
1463 O OD2 . ASP A 197 ? 1.8007 0.9438 0.7422 -0.0716 0.3228  0.0204  224 ASP A OD2 
1464 N N   . ARG A 198 ? 1.7760 0.9247 0.8446 -0.0839 0.2905  0.0535  225 ARG A N   
1465 C CA  . ARG A 198 ? 1.6974 0.8364 0.7837 -0.0833 0.2806  0.0642  225 ARG A CA  
1466 C C   . ARG A 198 ? 1.5801 0.7568 0.7313 -0.0933 0.2791  0.0546  225 ARG A C   
1467 O O   . ARG A 198 ? 1.5504 0.7508 0.7151 -0.0868 0.2606  0.0474  225 ARG A O   
1468 C CB  . ARG A 198 ? 1.7718 0.8910 0.8204 -0.0611 0.2440  0.0755  225 ARG A CB  
1469 C CG  . ARG A 198 ? 2.0532 1.1369 1.0348 -0.0477 0.2409  0.0860  225 ARG A CG  
1470 C CD  . ARG A 198 ? 2.2180 1.2959 1.1687 -0.0240 0.1995  0.0913  225 ARG A CD  
1471 N NE  . ARG A 198 ? 2.3150 1.3879 1.2853 -0.0164 0.1816  0.1011  225 ARG A NE  
1472 C CZ  . ARG A 198 ? 2.2045 1.2780 1.1631 0.0036  0.1454  0.1052  225 ARG A CZ  
1473 N NH1 . ARG A 198 ? 2.1269 1.2065 1.0545 0.0176  0.1209  0.0994  225 ARG A NH1 
1474 N NH2 . ARG A 198 ? 1.9415 1.0119 0.9231 0.0097  0.1333  0.1134  225 ARG A NH2 
1475 N N   . ARG A 199 ? 1.5357 0.7178 0.7266 -0.1089 0.2989  0.0537  226 ARG A N   
1476 C CA  . ARG A 199 ? 1.5035 0.7217 0.7569 -0.1189 0.2982  0.0446  226 ARG A CA  
1477 C C   . ARG A 199 ? 1.2764 0.4852 0.5437 -0.1144 0.2800  0.0525  226 ARG A C   
1478 O O   . ARG A 199 ? 1.3286 0.5093 0.5804 -0.1161 0.2882  0.0605  226 ARG A O   
1479 C CB  . ARG A 199 ? 1.5290 0.7698 0.8267 -0.1414 0.3337  0.0324  226 ARG A CB  
1480 C CG  . ARG A 199 ? 1.3051 0.5657 0.6030 -0.1449 0.3518  0.0212  226 ARG A CG  
1481 C CD  . ARG A 199 ? 1.3790 0.6682 0.7294 -0.1662 0.3859  0.0076  226 ARG A CD  
1482 N NE  . ARG A 199 ? 1.5956 0.9061 0.9503 -0.1671 0.4033  -0.0043 226 ARG A NE  
1483 C CZ  . ARG A 199 ? 1.6513 1.0078 1.0502 -0.1654 0.4019  -0.0188 226 ARG A CZ  
1484 N NH1 . ARG A 199 ? 1.7458 1.1413 1.2001 -0.1588 0.3746  -0.0250 226 ARG A NH1 
1485 N NH2 . ARG A 199 ? 1.5422 0.9134 0.9416 -0.1648 0.4198  -0.0299 226 ARG A NH2 
1486 N N   . GLY A 200 ? 1.3709 0.6023 0.6679 -0.1080 0.2568  0.0499  227 GLY A N   
1487 C CA  . GLY A 200 ? 1.2122 0.4394 0.5268 -0.1018 0.2379  0.0548  227 GLY A CA  
1488 C C   . GLY A 200 ? 1.2650 0.5191 0.6017 -0.0861 0.2049  0.0519  227 GLY A C   
1489 O O   . GLY A 200 ? 1.2165 0.5054 0.5720 -0.0808 0.1961  0.0418  227 GLY A O   
1490 N N   . CYS A 201 ? 1.1324 0.3758 0.4745 -0.0772 0.1867  0.0584  228 CYS A N   
1491 C CA  . CYS A 201 ? 1.2838 0.5558 0.6513 -0.0600 0.1546  0.0552  228 CYS A CA  
1492 C C   . CYS A 201 ? 1.2661 0.5030 0.5845 -0.0414 0.1333  0.0695  228 CYS A C   
1493 O O   . CYS A 201 ? 1.2055 0.4219 0.5111 -0.0364 0.1316  0.0770  228 CYS A O   
1494 C CB  . CYS A 201 ? 1.0971 0.3906 0.5133 -0.0622 0.1492  0.0489  228 CYS A CB  
1495 S SG  . CYS A 201 ? 1.6642 1.0087 1.1422 -0.0797 0.1666  0.0297  228 CYS A SG  
1496 N N   . PHE A 202 ? 1.2912 0.5438 0.6009 -0.0290 0.1136  0.0662  229 PHE A N   
1497 C CA  . PHE A 202 ? 1.2910 0.5158 0.5523 -0.0110 0.0918  0.0767  229 PHE A CA  
1498 C C   . PHE A 202 ? 1.1671 0.4208 0.4627 0.0050  0.0601  0.0722  229 PHE A C   
1499 O O   . PHE A 202 ? 1.1662 0.4629 0.5093 0.0034  0.0541  0.0592  229 PHE A O   
1500 C CB  . PHE A 202 ? 1.1960 0.4136 0.4146 -0.0098 0.0941  0.0737  229 PHE A CB  
1501 C CG  . PHE A 202 ? 1.3070 0.5008 0.4953 -0.0262 0.1290  0.0764  229 PHE A CG  
1502 C CD1 . PHE A 202 ? 1.2910 0.4539 0.4437 -0.0244 0.1391  0.0857  229 PHE A CD1 
1503 C CD2 . PHE A 202 ? 1.2365 0.4616 0.4589 -0.0411 0.1491  0.0621  229 PHE A CD2 
1504 C CE1 . PHE A 202 ? 1.3607 0.5112 0.4996 -0.0393 0.1717  0.0848  229 PHE A CE1 
1505 C CE2 . PHE A 202 ? 1.3628 0.5694 0.5629 -0.0566 0.1832  0.0633  229 PHE A CE2 
1506 C CZ  . PHE A 202 ? 1.4515 0.6243 0.6147 -0.0559 0.1939  0.0731  229 PHE A CZ  
1507 N N   . ALA A 203 ? 1.1193 0.3482 0.3914 0.0211  0.0414  0.0835  230 ALA A N   
1508 C CA  . ALA A 203 ? 1.2951 0.5504 0.5978 0.0375  0.0114  0.0792  230 ALA A CA  
1509 C C   . ALA A 203 ? 1.2646 0.5377 0.5571 0.0451  -0.0075 0.0701  230 ALA A C   
1510 O O   . ALA A 203 ? 1.2806 0.5261 0.5169 0.0530  -0.0147 0.0757  230 ALA A O   
1511 C CB  . ALA A 203 ? 1.1637 0.3935 0.4488 0.0539  -0.0029 0.0916  230 ALA A CB  
1512 N N   . VAL A 204 ? 1.0809 0.3981 0.4256 0.0428  -0.0148 0.0556  231 VAL A N   
1513 C CA  . VAL A 204 ? 1.0828 0.4187 0.4269 0.0473  -0.0313 0.0431  231 VAL A CA  
1514 C C   . VAL A 204 ? 1.2271 0.5983 0.6243 0.0570  -0.0542 0.0351  231 VAL A C   
1515 O O   . VAL A 204 ? 1.2241 0.6120 0.6645 0.0561  -0.0499 0.0371  231 VAL A O   
1516 C CB  . VAL A 204 ? 1.0129 0.3643 0.3676 0.0321  -0.0111 0.0315  231 VAL A CB  
1517 C CG1 . VAL A 204 ? 1.1133 0.4307 0.4139 0.0231  0.0120  0.0381  231 VAL A CG1 
1518 C CG2 . VAL A 204 ? 0.9965 0.3790 0.4112 0.0229  0.0030  0.0275  231 VAL A CG2 
1519 N N   . PRO A 205 ? 1.0774 0.4616 0.4743 0.0657  -0.0777 0.0246  232 PRO A N   
1520 C CA  . PRO A 205 ? 0.9764 0.3957 0.4298 0.0730  -0.0970 0.0157  232 PRO A CA  
1521 C C   . PRO A 205 ? 0.9911 0.4445 0.5011 0.0615  -0.0853 0.0035  232 PRO A C   
1522 O O   . PRO A 205 ? 0.9605 0.4423 0.5202 0.0655  -0.0966 -0.0036 232 PRO A O   
1523 C CB  . PRO A 205 ? 1.1220 0.5419 0.5515 0.0854  -0.1267 0.0067  232 PRO A CB  
1524 C CG  . PRO A 205 ? 1.1287 0.5270 0.5042 0.0784  -0.1176 0.0030  232 PRO A CG  
1525 C CD  . PRO A 205 ? 1.0571 0.4234 0.3993 0.0702  -0.0890 0.0198  232 PRO A CD  
1526 N N   . MET A 206 ? 1.0457 0.4968 0.5512 0.0481  -0.0620 0.0012  233 MET A N   
1527 C CA  . MET A 206 ? 0.9916 0.4711 0.5465 0.0399  -0.0514 -0.0093 233 MET A CA  
1528 C C   . MET A 206 ? 0.9821 0.4584 0.5344 0.0286  -0.0237 -0.0058 233 MET A C   
1529 O O   . MET A 206 ? 1.0967 0.5525 0.6075 0.0230  -0.0132 -0.0059 233 MET A O   
1530 C CB  . MET A 206 ? 0.9439 0.4314 0.5008 0.0386  -0.0630 -0.0269 233 MET A CB  
1531 C CG  . MET A 206 ? 0.9364 0.4442 0.5379 0.0295  -0.0477 -0.0370 233 MET A CG  
1532 S SD  . MET A 206 ? 0.9482 0.4871 0.6217 0.0323  -0.0479 -0.0348 233 MET A SD  
1533 C CE  . MET A 206 ? 0.9986 0.5505 0.6901 0.0385  -0.0783 -0.0499 233 MET A CE  
1534 N N   . VAL A 207 ? 0.9762 0.4741 0.5726 0.0263  -0.0119 -0.0032 234 VAL A N   
1535 C CA  . VAL A 207 ? 0.8189 0.3249 0.4271 0.0179  0.0111  -0.0034 234 VAL A CA  
1536 C C   . VAL A 207 ? 0.8779 0.4114 0.5379 0.0197  0.0147  -0.0072 234 VAL A C   
1537 O O   . VAL A 207 ? 0.9244 0.4705 0.6130 0.0259  0.0042  -0.0058 234 VAL A O   
1538 C CB  . VAL A 207 ? 0.8585 0.3598 0.4600 0.0145  0.0236  0.0064  234 VAL A CB  
1539 C CG1 . VAL A 207 ? 0.9156 0.3840 0.4652 0.0111  0.0257  0.0116  234 VAL A CG1 
1540 C CG2 . VAL A 207 ? 0.8775 0.3911 0.5062 0.0219  0.0158  0.0126  234 VAL A CG2 
1541 N N   . HIS A 208 ? 0.8483 0.3900 0.5209 0.0150  0.0312  -0.0113 235 HIS A N   
1542 C CA  . HIS A 208 ? 0.7879 0.3498 0.5052 0.0180  0.0373  -0.0129 235 HIS A CA  
1543 C C   . HIS A 208 ? 0.8169 0.3870 0.5428 0.0159  0.0572  -0.0128 235 HIS A C   
1544 O O   . HIS A 208 ? 0.7398 0.3040 0.4424 0.0108  0.0662  -0.0128 235 HIS A O   
1545 C CB  . HIS A 208 ? 0.7490 0.3093 0.4795 0.0174  0.0282  -0.0248 235 HIS A CB  
1546 C CG  . HIS A 208 ? 0.9124 0.4578 0.6155 0.0115  0.0311  -0.0374 235 HIS A CG  
1547 N ND1 . HIS A 208 ? 0.8121 0.3591 0.5257 0.0087  0.0490  -0.0427 235 HIS A ND1 
1548 C CD2 . HIS A 208 ? 0.7906 0.3189 0.4540 0.0094  0.0188  -0.0460 235 HIS A CD2 
1549 C CE1 . HIS A 208 ? 0.9618 0.4932 0.6442 0.0039  0.0489  -0.0553 235 HIS A CE1 
1550 N NE2 . HIS A 208 ? 0.9140 0.4337 0.5632 0.0043  0.0304  -0.0573 235 HIS A NE2 
1551 N N   . SER A 209 ? 0.8011 0.3848 0.5631 0.0204  0.0650  -0.0123 236 SER A N   
1552 C CA  . SER A 209 ? 0.7553 0.3487 0.5322 0.0226  0.0823  -0.0120 236 SER A CA  
1553 C C   . SER A 209 ? 0.8078 0.4184 0.5884 0.0264  0.0885  -0.0030 236 SER A C   
1554 O O   . SER A 209 ? 0.8512 0.4786 0.6573 0.0356  0.0942  0.0043  236 SER A O   
1555 C CB  . SER A 209 ? 0.7876 0.3681 0.5427 0.0158  0.0902  -0.0237 236 SER A CB  
1556 O OG  . SER A 209 ? 0.9842 0.5518 0.7406 0.0134  0.0852  -0.0352 236 SER A OG  
1557 N N   . THR A 210 ? 0.7898 0.3957 0.5445 0.0197  0.0876  -0.0038 237 THR A N   
1558 C CA  . THR A 210 ? 0.7913 0.4146 0.5517 0.0209  0.0917  0.0007  237 THR A CA  
1559 C C   . THR A 210 ? 0.8000 0.4099 0.5360 0.0148  0.0832  0.0027  237 THR A C   
1560 O O   . THR A 210 ? 0.8014 0.3904 0.5076 0.0060  0.0844  -0.0006 237 THR A O   
1561 C CB  . THR A 210 ? 0.7788 0.4131 0.5420 0.0170  0.1063  -0.0053 237 THR A CB  
1562 O OG1 . THR A 210 ? 0.7633 0.4114 0.5529 0.0266  0.1140  -0.0053 237 THR A OG1 
1563 C CG2 . THR A 210 ? 0.6782 0.3315 0.4476 0.0153  0.1081  -0.0047 237 THR A CG2 
1564 N N   . PHE A 211 ? 0.8095 0.4289 0.5558 0.0206  0.0761  0.0086  238 PHE A N   
1565 C CA  . PHE A 211 ? 0.7864 0.3910 0.5126 0.0167  0.0686  0.0105  238 PHE A CA  
1566 C C   . PHE A 211 ? 0.7923 0.4156 0.5348 0.0227  0.0667  0.0132  238 PHE A C   
1567 O O   . PHE A 211 ? 0.7173 0.3626 0.4828 0.0323  0.0681  0.0162  238 PHE A O   
1568 C CB  . PHE A 211 ? 0.8429 0.4272 0.5556 0.0193  0.0550  0.0129  238 PHE A CB  
1569 C CG  . PHE A 211 ? 0.8557 0.4531 0.5963 0.0289  0.0486  0.0156  238 PHE A CG  
1570 C CD1 . PHE A 211 ? 0.6647 0.2708 0.4186 0.0363  0.0433  0.0207  238 PHE A CD1 
1571 C CD2 . PHE A 211 ? 0.7998 0.3994 0.5543 0.0297  0.0500  0.0121  238 PHE A CD2 
1572 C CE1 . PHE A 211 ? 0.8657 0.4834 0.6467 0.0441  0.0412  0.0237  238 PHE A CE1 
1573 C CE2 . PHE A 211 ? 0.7619 0.3717 0.5456 0.0365  0.0475  0.0145  238 PHE A CE2 
1574 C CZ  . PHE A 211 ? 1.0303 0.6496 0.8275 0.0435  0.0438  0.0210  238 PHE A CZ  
1575 N N   . LEU A 212 ? 0.8051 0.4166 0.5325 0.0175  0.0642  0.0123  239 LEU A N   
1576 C CA  . LEU A 212 ? 0.7416 0.3683 0.4797 0.0209  0.0629  0.0107  239 LEU A CA  
1577 C C   . LEU A 212 ? 0.8443 0.4545 0.5740 0.0257  0.0531  0.0145  239 LEU A C   
1578 O O   . LEU A 212 ? 0.8366 0.4180 0.5439 0.0209  0.0495  0.0161  239 LEU A O   
1579 C CB  . LEU A 212 ? 0.7408 0.3697 0.4749 0.0087  0.0714  0.0022  239 LEU A CB  
1580 C CG  . LEU A 212 ? 0.7817 0.4297 0.5281 0.0100  0.0698  -0.0047 239 LEU A CG  
1581 C CD1 . LEU A 212 ? 0.7240 0.4105 0.4938 0.0212  0.0692  -0.0060 239 LEU A CD1 
1582 C CD2 . LEU A 212 ? 0.7497 0.3906 0.4919 -0.0065 0.0784  -0.0150 239 LEU A CD2 
1583 N N   . ILE A 213 ? 0.6984 0.3258 0.4444 0.0367  0.0495  0.0166  240 ILE A N   
1584 C CA  . ILE A 213 ? 0.7727 0.3891 0.5162 0.0432  0.0419  0.0189  240 ILE A CA  
1585 C C   . ILE A 213 ? 0.7745 0.3979 0.5174 0.0429  0.0438  0.0119  240 ILE A C   
1586 O O   . ILE A 213 ? 0.7714 0.4217 0.5256 0.0464  0.0474  0.0082  240 ILE A O   
1587 C CB  . ILE A 213 ? 0.8001 0.4294 0.5634 0.0555  0.0389  0.0251  240 ILE A CB  
1588 C CG1 . ILE A 213 ? 0.7620 0.3868 0.5308 0.0539  0.0372  0.0281  240 ILE A CG1 
1589 C CG2 . ILE A 213 ? 0.6966 0.3157 0.4605 0.0627  0.0318  0.0262  240 ILE A CG2 
1590 C CD1 . ILE A 213 ? 0.7331 0.3690 0.5270 0.0630  0.0363  0.0327  240 ILE A CD1 
1591 N N   . ASP A 214 ? 0.8454 0.4440 0.5742 0.0397  0.0408  0.0096  241 ASP A N   
1592 C CA  . ASP A 214 ? 0.7076 0.3073 0.4356 0.0377  0.0428  0.0000  241 ASP A CA  
1593 C C   . ASP A 214 ? 0.7824 0.3899 0.5189 0.0523  0.0384  0.0012  241 ASP A C   
1594 O O   . ASP A 214 ? 0.7874 0.3736 0.5195 0.0578  0.0336  0.0049  241 ASP A O   
1595 C CB  . ASP A 214 ? 0.8799 0.4432 0.5886 0.0264  0.0452  -0.0028 241 ASP A CB  
1596 C CG  . ASP A 214 ? 0.9811 0.5451 0.6926 0.0194  0.0498  -0.0169 241 ASP A CG  
1597 O OD1 . ASP A 214 ? 0.9255 0.5136 0.6488 0.0277  0.0471  -0.0241 241 ASP A OD1 
1598 O OD2 . ASP A 214 ? 0.9930 0.5322 0.6939 0.0050  0.0571  -0.0215 241 ASP A OD2 
1599 N N   . LEU A 215 ? 0.7663 0.4045 0.5142 0.0601  0.0406  -0.0017 242 LEU A N   
1600 C CA  . LEU A 215 ? 0.7873 0.4349 0.5414 0.0745  0.0402  -0.0004 242 LEU A CA  
1601 C C   . LEU A 215 ? 0.7782 0.4169 0.5246 0.0748  0.0397  -0.0128 242 LEU A C   
1602 O O   . LEU A 215 ? 0.8737 0.5185 0.6232 0.0870  0.0409  -0.0135 242 LEU A O   
1603 C CB  . LEU A 215 ? 0.6778 0.3581 0.4405 0.0846  0.0445  0.0035  242 LEU A CB  
1604 C CG  . LEU A 215 ? 0.6626 0.3481 0.4359 0.0850  0.0469  0.0153  242 LEU A CG  
1605 C CD1 . LEU A 215 ? 0.6904 0.4033 0.4690 0.0958  0.0528  0.0208  242 LEU A CD1 
1606 C CD2 . LEU A 215 ? 0.6733 0.3453 0.4572 0.0889  0.0455  0.0237  242 LEU A CD2 
1607 N N   . ARG A 216 ? 0.7735 0.3970 0.5110 0.0612  0.0402  -0.0234 243 ARG A N   
1608 C CA  . ARG A 216 ? 0.8023 0.4092 0.5337 0.0597  0.0407  -0.0363 243 ARG A CA  
1609 C C   . ARG A 216 ? 0.8740 0.4432 0.5992 0.0633  0.0387  -0.0294 243 ARG A C   
1610 O O   . ARG A 216 ? 0.8787 0.4345 0.6022 0.0694  0.0393  -0.0368 243 ARG A O   
1611 C CB  . ARG A 216 ? 0.7123 0.3145 0.4412 0.0418  0.0440  -0.0514 243 ARG A CB  
1612 C CG  . ARG A 216 ? 0.8722 0.5138 0.6105 0.0379  0.0438  -0.0591 243 ARG A CG  
1613 C CD  . ARG A 216 ? 0.8608 0.4962 0.6034 0.0172  0.0485  -0.0733 243 ARG A CD  
1614 N NE  . ARG A 216 ? 0.8709 0.4716 0.6053 0.0058  0.0547  -0.0621 243 ARG A NE  
1615 C CZ  . ARG A 216 ? 0.9397 0.5094 0.6693 -0.0112 0.0630  -0.0689 243 ARG A CZ  
1616 N NH1 . ARG A 216 ? 0.8413 0.4101 0.5788 -0.0211 0.0660  -0.0890 243 ARG A NH1 
1617 N NH2 . ARG A 216 ? 0.8113 0.3484 0.5266 -0.0185 0.0693  -0.0556 243 ARG A NH2 
1618 N N   . LYS A 217 ? 0.9561 0.5081 0.6768 0.0611  0.0357  -0.0162 244 LYS A N   
1619 C CA  . LYS A 217 ? 0.8357 0.3529 0.5480 0.0670  0.0309  -0.0085 244 LYS A CA  
1620 C C   . LYS A 217 ? 0.8779 0.4079 0.6061 0.0852  0.0260  -0.0038 244 LYS A C   
1621 O O   . LYS A 217 ? 0.9033 0.4623 0.6467 0.0906  0.0256  0.0013  244 LYS A O   
1622 C CB  . LYS A 217 ? 0.8948 0.3933 0.5937 0.0609  0.0274  0.0031  244 LYS A CB  
1623 C CG  . LYS A 217 ? 0.9131 0.3999 0.5978 0.0423  0.0358  -0.0003 244 LYS A CG  
1624 C CD  . LYS A 217 ? 0.8550 0.3100 0.5287 0.0333  0.0433  -0.0087 244 LYS A CD  
1625 C CE  . LYS A 217 ? 0.9469 0.3716 0.6001 0.0169  0.0523  -0.0048 244 LYS A CE  
1626 N NZ  . LYS A 217 ? 1.0499 0.5037 0.7114 0.0045  0.0584  -0.0088 244 LYS A NZ  
1627 N N   . ALA A 218 ? 0.8560 0.3635 0.5831 0.0945  0.0239  -0.0056 245 ALA A N   
1628 C CA  . ALA A 218 ? 0.7889 0.3099 0.5358 0.1121  0.0208  -0.0028 245 ALA A CA  
1629 C C   . ALA A 218 ? 0.8947 0.4244 0.6537 0.1172  0.0116  0.0093  245 ALA A C   
1630 O O   . ALA A 218 ? 0.8399 0.3969 0.6236 0.1260  0.0125  0.0114  245 ALA A O   
1631 C CB  . ALA A 218 ? 0.7610 0.2527 0.5051 0.1221  0.0198  -0.0071 245 ALA A CB  
1632 N N   . ALA A 219 ? 0.9120 0.4185 0.6538 0.1112  0.0037  0.0164  246 ALA A N   
1633 C CA  . ALA A 219 ? 0.8350 0.3491 0.5858 0.1159  -0.0077 0.0247  246 ALA A CA  
1634 C C   . ALA A 219 ? 0.8399 0.3865 0.6066 0.1093  -0.0036 0.0254  246 ALA A C   
1635 O O   . ALA A 219 ? 0.8571 0.4191 0.6437 0.1141  -0.0106 0.0284  246 ALA A O   
1636 C CB  . ALA A 219 ? 0.8255 0.3054 0.5455 0.1116  -0.0164 0.0316  246 ALA A CB  
1637 N N   . SER A 220 ? 0.7810 0.3386 0.5414 0.0990  0.0074  0.0219  247 SER A N   
1638 C CA  . SER A 220 ? 0.8562 0.4416 0.6310 0.0953  0.0126  0.0241  247 SER A CA  
1639 C C   . SER A 220 ? 0.8038 0.4155 0.6084 0.1062  0.0175  0.0256  247 SER A C   
1640 O O   . SER A 220 ? 0.7902 0.4199 0.6119 0.1052  0.0211  0.0296  247 SER A O   
1641 C CB  . SER A 220 ? 0.7009 0.2954 0.4647 0.0857  0.0222  0.0198  247 SER A CB  
1642 O OG  . SER A 220 ? 0.8044 0.4117 0.5715 0.0914  0.0287  0.0135  247 SER A OG  
1643 N N   . ARG A 221 ? 0.7864 0.3988 0.5980 0.1164  0.0199  0.0221  248 ARG A N   
1644 C CA  . ARG A 221 ? 0.7668 0.4030 0.6066 0.1269  0.0280  0.0237  248 ARG A CA  
1645 C C   . ARG A 221 ? 0.8608 0.5048 0.7299 0.1299  0.0209  0.0274  248 ARG A C   
1646 O O   . ARG A 221 ? 0.8445 0.5105 0.7417 0.1330  0.0303  0.0302  248 ARG A O   
1647 C CB  . ARG A 221 ? 0.8057 0.4387 0.6460 0.1378  0.0324  0.0174  248 ARG A CB  
1648 C CG  . ARG A 221 ? 0.7622 0.3931 0.5780 0.1353  0.0397  0.0097  248 ARG A CG  
1649 C CD  . ARG A 221 ? 0.8558 0.4757 0.6691 0.1450  0.0421  0.0004  248 ARG A CD  
1650 N NE  . ARG A 221 ? 1.1531 0.7905 0.9919 0.1588  0.0502  0.0019  248 ARG A NE  
1651 C CZ  . ARG A 221 ? 1.1649 0.7953 1.0099 0.1703  0.0533  -0.0055 248 ARG A CZ  
1652 N NH1 . ARG A 221 ? 1.0250 0.6282 0.8519 0.1700  0.0485  -0.0146 248 ARG A NH1 
1653 N NH2 . ARG A 221 ? 1.3025 0.9526 1.1745 0.1822  0.0634  -0.0040 248 ARG A NH2 
1654 N N   . ASN A 222 ? 0.8704 0.4966 0.7332 0.1293  0.0046  0.0270  249 ASN A N   
1655 C CA  . ASN A 222 ? 0.7120 0.3484 0.6032 0.1331  -0.0066 0.0270  249 ASN A CA  
1656 C C   . ASN A 222 ? 0.6760 0.3182 0.5698 0.1220  -0.0097 0.0282  249 ASN A C   
1657 O O   . ASN A 222 ? 0.8245 0.4786 0.7451 0.1231  -0.0192 0.0252  249 ASN A O   
1658 C CB  . ASN A 222 ? 0.7971 0.4125 0.6775 0.1415  -0.0255 0.0260  249 ASN A CB  
1659 C CG  . ASN A 222 ? 0.9749 0.5829 0.8584 0.1545  -0.0225 0.0237  249 ASN A CG  
1660 O OD1 . ASN A 222 ? 0.8261 0.4536 0.7331 0.1600  -0.0089 0.0210  249 ASN A OD1 
1661 N ND2 . ASN A 222 ? 0.9295 0.5064 0.7871 0.1602  -0.0336 0.0252  249 ASN A ND2 
1662 N N   . LEU A 223 ? 0.6881 0.3238 0.5577 0.1116  -0.0022 0.0305  250 LEU A N   
1663 C CA  . LEU A 223 ? 0.6065 0.2460 0.4783 0.1018  -0.0027 0.0307  250 LEU A CA  
1664 C C   . LEU A 223 ? 0.7225 0.3856 0.6283 0.1015  0.0122  0.0328  250 LEU A C   
1665 O O   . LEU A 223 ? 0.6962 0.3695 0.6068 0.1063  0.0271  0.0369  250 LEU A O   
1666 C CB  . LEU A 223 ? 0.6984 0.3237 0.5354 0.0921  0.0017  0.0320  250 LEU A CB  
1667 C CG  . LEU A 223 ? 0.7921 0.3891 0.5924 0.0894  -0.0075 0.0315  250 LEU A CG  
1668 C CD1 . LEU A 223 ? 0.8215 0.4102 0.5964 0.0780  0.0013  0.0314  250 LEU A CD1 
1669 C CD2 . LEU A 223 ? 0.8752 0.4595 0.6683 0.0912  -0.0249 0.0305  250 LEU A CD2 
1670 N N   . ALA A 224 ? 0.7231 0.3928 0.6506 0.0960  0.0088  0.0297  251 ALA A N   
1671 C CA  . ALA A 224 ? 0.6371 0.3238 0.5989 0.0941  0.0252  0.0322  251 ALA A CA  
1672 C C   . ALA A 224 ? 0.7438 0.4272 0.7122 0.0838  0.0223  0.0275  251 ALA A C   
1673 O O   . ALA A 224 ? 0.7192 0.3985 0.6880 0.0805  0.0043  0.0183  251 ALA A O   
1674 C CB  . ALA A 224 ? 0.5667 0.2716 0.5720 0.1003  0.0279  0.0297  251 ALA A CB  
1675 N N   . PHE A 225 ? 0.6531 0.3374 0.6246 0.0802  0.0396  0.0333  252 PHE A N   
1676 C CA  . PHE A 225 ? 0.7034 0.3839 0.6874 0.0709  0.0407  0.0278  252 PHE A CA  
1677 C C   . PHE A 225 ? 0.6861 0.3791 0.7209 0.0676  0.0470  0.0230  252 PHE A C   
1678 O O   . PHE A 225 ? 0.7996 0.4910 0.8515 0.0588  0.0403  0.0116  252 PHE A O   
1679 C CB  . PHE A 225 ? 0.5905 0.2650 0.5595 0.0701  0.0570  0.0362  252 PHE A CB  
1680 C CG  . PHE A 225 ? 0.7501 0.4148 0.6767 0.0695  0.0508  0.0367  252 PHE A CG  
1681 C CD1 . PHE A 225 ? 0.7381 0.3905 0.6466 0.0614  0.0422  0.0286  252 PHE A CD1 
1682 C CD2 . PHE A 225 ? 0.7239 0.3923 0.6300 0.0763  0.0547  0.0436  252 PHE A CD2 
1683 C CE1 . PHE A 225 ? 0.7296 0.3736 0.6028 0.0594  0.0400  0.0289  252 PHE A CE1 
1684 C CE2 . PHE A 225 ? 0.6791 0.3404 0.5529 0.0735  0.0505  0.0419  252 PHE A CE2 
1685 C CZ  . PHE A 225 ? 0.7215 0.3705 0.5802 0.0646  0.0443  0.0353  252 PHE A CZ  
1686 N N   . TYR A 226 ? 0.6762 0.3819 0.7367 0.0739  0.0611  0.0299  253 TYR A N   
1687 C CA  . TYR A 226 ? 0.7050 0.4243 0.8197 0.0697  0.0713  0.0255  253 TYR A CA  
1688 C C   . TYR A 226 ? 0.6588 0.3931 0.7918 0.0791  0.0804  0.0309  253 TYR A C   
1689 O O   . TYR A 226 ? 0.8250 0.5559 0.9289 0.0886  0.0902  0.0427  253 TYR A O   
1690 C CB  . TYR A 226 ? 0.6578 0.3695 0.7890 0.0644  0.0963  0.0331  253 TYR A CB  
1691 C CG  . TYR A 226 ? 0.7614 0.4822 0.9518 0.0547  0.1065  0.0244  253 TYR A CG  
1692 C CD1 . TYR A 226 ? 0.6960 0.4159 0.9079 0.0422  0.0929  0.0061  253 TYR A CD1 
1693 C CD2 . TYR A 226 ? 0.8338 0.5646 1.0596 0.0572  0.1307  0.0329  253 TYR A CD2 
1694 C CE1 . TYR A 226 ? 0.8007 0.5307 1.0723 0.0312  0.1018  -0.0054 253 TYR A CE1 
1695 C CE2 . TYR A 226 ? 0.6140 0.3538 0.9000 0.0460  0.1426  0.0237  253 TYR A CE2 
1696 C CZ  . TYR A 226 ? 0.7831 0.5233 1.0941 0.0324  0.1274  0.0036  253 TYR A CZ  
1697 O OH  . TYR A 226 ? 0.8550 0.6059 1.2312 0.0192  0.1389  -0.0090 253 TYR A OH  
1698 N N   . PRO A 227 ? 0.7093 0.4620 0.8909 0.0772  0.0774  0.0208  254 PRO A N   
1699 C CA  . PRO A 227 ? 0.6682 0.4313 0.8899 0.0666  0.0625  0.0027  254 PRO A CA  
1700 C C   . PRO A 227 ? 0.7624 0.5231 0.9579 0.0689  0.0276  -0.0093 254 PRO A C   
1701 O O   . PRO A 227 ? 0.8512 0.6018 1.0038 0.0784  0.0176  -0.0027 254 PRO A O   
1702 C CB  . PRO A 227 ? 0.5715 0.3602 0.8540 0.0675  0.0736  -0.0021 254 PRO A CB  
1703 C CG  . PRO A 227 ? 0.5914 0.3828 0.8524 0.0824  0.0789  0.0088  254 PRO A CG  
1704 C CD  . PRO A 227 ? 0.7552 0.5236 0.9592 0.0865  0.0907  0.0255  254 PRO A CD  
1705 N N   . PRO A 228 ? 0.7931 0.5609 1.0107 0.0606  0.0091  -0.0270 255 PRO A N   
1706 C CA  . PRO A 228 ? 0.7544 0.5203 0.9444 0.0659  -0.0249 -0.0373 255 PRO A CA  
1707 C C   . PRO A 228 ? 0.6945 0.4749 0.8941 0.0804  -0.0375 -0.0367 255 PRO A C   
1708 O O   . PRO A 228 ? 0.7704 0.5716 1.0162 0.0835  -0.0238 -0.0362 255 PRO A O   
1709 C CB  . PRO A 228 ? 0.7606 0.5395 0.9860 0.0549  -0.0400 -0.0593 255 PRO A CB  
1710 C CG  . PRO A 228 ? 0.5914 0.3641 0.8415 0.0411  -0.0122 -0.0579 255 PRO A CG  
1711 C CD  . PRO A 228 ? 0.6054 0.3792 0.8681 0.0459  0.0187  -0.0387 255 PRO A CD  
1712 N N   . HIS A 229 ? 0.6878 0.4548 0.8426 0.0900  -0.0617 -0.0360 256 HIS A N   
1713 C CA  . HIS A 229 ? 0.6300 0.4050 0.7884 0.1062  -0.0747 -0.0344 256 HIS A CA  
1714 C C   . HIS A 229 ? 0.6774 0.4885 0.9016 0.1091  -0.0882 -0.0511 256 HIS A C   
1715 O O   . HIS A 229 ? 0.8355 0.6600 1.0845 0.1000  -0.1014 -0.0671 256 HIS A O   
1716 C CB  . HIS A 229 ? 0.7687 0.5181 0.8667 0.1156  -0.0990 -0.0308 256 HIS A CB  
1717 C CG  . HIS A 229 ? 0.7862 0.5349 0.8803 0.1340  -0.1097 -0.0261 256 HIS A CG  
1718 N ND1 . HIS A 229 ? 0.8898 0.6606 1.0169 0.1466  -0.1336 -0.0367 256 HIS A ND1 
1719 C CD2 . HIS A 229 ? 0.8150 0.5436 0.8783 0.1425  -0.1000 -0.0134 256 HIS A CD2 
1720 C CE1 . HIS A 229 ? 0.8484 0.6106 0.9642 0.1634  -0.1372 -0.0290 256 HIS A CE1 
1721 N NE2 . HIS A 229 ? 0.8305 0.5656 0.9073 0.1603  -0.1164 -0.0155 256 HIS A NE2 
1722 N N   . PRO A 230 ? 0.8085 0.6379 1.0656 0.1213  -0.0847 -0.0498 257 PRO A N   
1723 C CA  . PRO A 230 ? 0.8350 0.7046 1.1635 0.1243  -0.0965 -0.0672 257 PRO A CA  
1724 C C   . PRO A 230 ? 0.6954 0.5760 1.0239 0.1292  -0.1365 -0.0840 257 PRO A C   
1725 O O   . PRO A 230 ? 0.7244 0.6406 1.1150 0.1243  -0.1471 -0.1038 257 PRO A O   
1726 C CB  . PRO A 230 ? 0.6961 0.5747 1.0392 0.1420  -0.0902 -0.0605 257 PRO A CB  
1727 C CG  . PRO A 230 ? 0.6188 0.4704 0.9210 0.1399  -0.0602 -0.0417 257 PRO A CG  
1728 C CD  . PRO A 230 ? 0.7678 0.5856 1.0061 0.1309  -0.0648 -0.0344 257 PRO A CD  
1729 N N   . ASP A 231 ? 0.7902 0.6417 1.0509 0.1386  -0.1587 -0.0773 258 ASP A N   
1730 C CA  . ASP A 231 ? 0.8445 0.7023 1.0922 0.1465  -0.1978 -0.0908 258 ASP A CA  
1731 C C   . ASP A 231 ? 0.8536 0.6954 1.0670 0.1310  -0.2037 -0.0981 258 ASP A C   
1732 O O   . ASP A 231 ? 0.7857 0.6248 0.9694 0.1379  -0.2353 -0.1074 258 ASP A O   
1733 C CB  . ASP A 231 ? 0.9210 0.7535 1.1123 0.1692  -0.2184 -0.0779 258 ASP A CB  
1734 C CG  . ASP A 231 ? 0.9690 0.8175 1.1960 0.1875  -0.2164 -0.0738 258 ASP A CG  
1735 O OD1 . ASP A 231 ? 1.0074 0.8959 1.3092 0.1848  -0.2076 -0.0856 258 ASP A OD1 
1736 O OD2 . ASP A 231 ? 0.9835 0.8035 1.1652 0.2042  -0.2218 -0.0594 258 ASP A OD2 
1737 N N   . TYR A 232 ? 0.8465 0.6772 1.0616 0.1120  -0.1739 -0.0941 259 TYR A N   
1738 C CA  . TYR A 232 ? 0.8513 0.6646 1.0344 0.0977  -0.1758 -0.1011 259 TYR A CA  
1739 C C   . TYR A 232 ? 0.9234 0.7680 1.1593 0.0880  -0.1927 -0.1291 259 TYR A C   
1740 O O   . TYR A 232 ? 0.8208 0.6953 1.1302 0.0792  -0.1797 -0.1397 259 TYR A O   
1741 C CB  . TYR A 232 ? 0.7166 0.5097 0.8903 0.0831  -0.1387 -0.0880 259 TYR A CB  
1742 C CG  . TYR A 232 ? 0.7468 0.5174 0.8824 0.0704  -0.1367 -0.0924 259 TYR A CG  
1743 C CD1 . TYR A 232 ? 0.8367 0.5741 0.8989 0.0742  -0.1400 -0.0807 259 TYR A CD1 
1744 C CD2 . TYR A 232 ? 0.6698 0.4511 0.8453 0.0542  -0.1291 -0.1092 259 TYR A CD2 
1745 C CE1 . TYR A 232 ? 0.9131 0.6313 0.9422 0.0633  -0.1361 -0.0856 259 TYR A CE1 
1746 C CE2 . TYR A 232 ? 0.7163 0.4759 0.8578 0.0437  -0.1261 -0.1146 259 TYR A CE2 
1747 C CZ  . TYR A 232 ? 0.8708 0.6002 0.9390 0.0489  -0.1297 -0.1027 259 TYR A CZ  
1748 O OH  . TYR A 232 ? 0.9268 0.6361 0.9628 0.0392  -0.1248 -0.1089 259 TYR A OH  
1749 N N   . THR A 233 ? 0.9085 0.7460 1.1066 0.0892  -0.2208 -0.1422 260 THR A N   
1750 C CA  . THR A 233 ? 0.9574 0.8246 1.1992 0.0804  -0.2420 -0.1730 260 THR A CA  
1751 C C   . THR A 233 ? 0.9895 0.8342 1.1922 0.0663  -0.2420 -0.1838 260 THR A C   
1752 O O   . THR A 233 ? 1.0248 0.8893 1.2490 0.0601  -0.2644 -0.2120 260 THR A O   
1753 C CB  . THR A 233 ? 0.9011 0.7935 1.1441 0.1003  -0.2862 -0.1864 260 THR A CB  
1754 O OG1 . THR A 233 ? 1.1104 0.9683 1.2629 0.1156  -0.3053 -0.1731 260 THR A OG1 
1755 C CG2 . THR A 233 ? 0.9269 0.8463 1.2197 0.1148  -0.2861 -0.1794 260 THR A CG2 
1756 N N   . TRP A 234 ? 0.7957 0.6018 0.9439 0.0612  -0.2180 -0.1645 261 TRP A N   
1757 C CA  . TRP A 234 ? 0.9184 0.7007 1.0231 0.0506  -0.2171 -0.1735 261 TRP A CA  
1758 C C   . TRP A 234 ? 0.9788 0.7610 1.1303 0.0294  -0.1863 -0.1811 261 TRP A C   
1759 O O   . TRP A 234 ? 0.8792 0.6824 1.0992 0.0225  -0.1693 -0.1826 261 TRP A O   
1760 C CB  . TRP A 234 ? 0.8695 0.6115 0.8898 0.0582  -0.2097 -0.1497 261 TRP A CB  
1761 C CG  . TRP A 234 ? 1.0548 0.7895 1.0235 0.0785  -0.2394 -0.1428 261 TRP A CG  
1762 C CD1 . TRP A 234 ? 1.0195 0.7771 0.9961 0.0909  -0.2766 -0.1592 261 TRP A CD1 
1763 C CD2 . TRP A 234 ? 1.1612 0.8623 1.0635 0.0897  -0.2341 -0.1172 261 TRP A CD2 
1764 N NE1 . TRP A 234 ? 1.1470 0.8841 1.0619 0.1111  -0.2944 -0.1430 261 TRP A NE1 
1765 C CE2 . TRP A 234 ? 1.1654 0.8660 1.0348 0.1094  -0.2673 -0.1172 261 TRP A CE2 
1766 C CE3 . TRP A 234 ? 1.0898 0.7619 0.9593 0.0850  -0.2047 -0.0953 261 TRP A CE3 
1767 C CZ2 . TRP A 234 ? 1.0893 0.7560 0.8933 0.1235  -0.2688 -0.0945 261 TRP A CZ2 
1768 C CZ3 . TRP A 234 ? 1.1310 0.7737 0.9402 0.0969  -0.2071 -0.0759 261 TRP A CZ3 
1769 C CH2 . TRP A 234 ? 1.0928 0.7304 0.8693 0.1155  -0.2373 -0.0747 261 TRP A CH2 
1770 N N   . SER A 235 ? 0.8889 0.6455 1.0035 0.0198  -0.1770 -0.1857 262 SER A N   
1771 C CA  . SER A 235 ? 0.7753 0.5265 0.9304 0.0015  -0.1484 -0.1931 262 SER A CA  
1772 C C   . SER A 235 ? 0.8754 0.6134 1.0393 0.0011  -0.1113 -0.1646 262 SER A C   
1773 O O   . SER A 235 ? 0.8817 0.6055 1.0011 0.0122  -0.1061 -0.1408 262 SER A O   
1774 C CB  . SER A 235 ? 0.9368 0.6624 1.0464 -0.0060 -0.1481 -0.2054 262 SER A CB  
1775 O OG  . SER A 235 ? 1.4029 1.1405 1.4993 -0.0050 -0.1830 -0.2336 262 SER A OG  
1776 N N   . PHE A 236 ? 0.7825 0.5244 1.0041 -0.0118 -0.0851 -0.1679 263 PHE A N   
1777 C CA  . PHE A 236 ? 0.7359 0.4653 0.9660 -0.0112 -0.0492 -0.1416 263 PHE A CA  
1778 C C   . PHE A 236 ? 0.8463 0.5433 1.0214 -0.0104 -0.0336 -0.1282 263 PHE A C   
1779 O O   . PHE A 236 ? 1.0251 0.7072 1.2171 -0.0187 -0.0087 -0.1269 263 PHE A O   
1780 C CB  . PHE A 236 ? 0.7955 0.5341 1.1003 -0.0246 -0.0244 -0.1483 263 PHE A CB  
1781 C CG  . PHE A 236 ? 0.8122 0.5441 1.1304 -0.0204 0.0100  -0.1203 263 PHE A CG  
1782 C CD1 . PHE A 236 ? 0.7123 0.4617 1.0380 -0.0094 0.0102  -0.1058 263 PHE A CD1 
1783 C CD2 . PHE A 236 ? 0.7932 0.5008 1.1151 -0.0259 0.0421  -0.1088 263 PHE A CD2 
1784 C CE1 . PHE A 236 ? 0.8639 0.6072 1.1966 -0.0045 0.0415  -0.0812 263 PHE A CE1 
1785 C CE2 . PHE A 236 ? 0.8465 0.5476 1.1747 -0.0195 0.0724  -0.0822 263 PHE A CE2 
1786 C CZ  . PHE A 236 ? 0.8131 0.5326 1.1452 -0.0092 0.0720  -0.0688 263 PHE A CZ  
1787 N N   . ASP A 237 ? 0.9781 0.6638 1.0897 -0.0002 -0.0472 -0.1184 264 ASP A N   
1788 C CA  . ASP A 237 ? 1.0076 0.6670 1.0670 0.0009  -0.0348 -0.1077 264 ASP A CA  
1789 C C   . ASP A 237 ? 0.9268 0.5816 0.9594 0.0116  -0.0232 -0.0805 264 ASP A C   
1790 O O   . ASP A 237 ? 0.9507 0.6153 0.9760 0.0204  -0.0362 -0.0735 264 ASP A O   
1791 C CB  . ASP A 237 ? 0.9919 0.6402 0.9976 0.0017  -0.0582 -0.1215 264 ASP A CB  
1792 C CG  . ASP A 237 ? 1.1325 0.7556 1.0931 0.0000  -0.0426 -0.1158 264 ASP A CG  
1793 O OD1 . ASP A 237 ? 1.3608 0.9769 1.3299 0.0003  -0.0168 -0.0999 264 ASP A OD1 
1794 O OD2 . ASP A 237 ? 1.1364 0.7476 1.0522 -0.0005 -0.0564 -0.1275 264 ASP A OD2 
1795 N N   . ASP A 238 ? 0.8469 0.4874 0.8657 0.0118  0.0004  -0.0669 265 ASP A N   
1796 C CA  . ASP A 238 ? 0.7590 0.3996 0.7621 0.0211  0.0128  -0.0438 265 ASP A CA  
1797 C C   . ASP A 238 ? 0.8881 0.5212 0.8377 0.0271  -0.0017 -0.0382 265 ASP A C   
1798 O O   . ASP A 238 ? 0.8724 0.5110 0.8151 0.0349  -0.0037 -0.0262 265 ASP A O   
1799 C CB  . ASP A 238 ? 0.7306 0.3613 0.7353 0.0216  0.0394  -0.0318 265 ASP A CB  
1800 C CG  . ASP A 238 ? 0.9360 0.5501 0.9099 0.0176  0.0415  -0.0392 265 ASP A CG  
1801 O OD1 . ASP A 238 ? 1.0116 0.6201 0.9662 0.0122  0.0246  -0.0559 265 ASP A OD1 
1802 O OD2 . ASP A 238 ? 0.8286 0.4361 0.7969 0.0212  0.0601  -0.0284 265 ASP A OD2 
1803 N N   . ILE A 239 ? 0.9047 0.5230 0.8156 0.0235  -0.0100 -0.0470 266 ILE A N   
1804 C CA  . ILE A 239 ? 0.8582 0.4644 0.7170 0.0279  -0.0188 -0.0399 266 ILE A CA  
1805 C C   . ILE A 239 ? 0.8300 0.4384 0.6766 0.0337  -0.0447 -0.0443 266 ILE A C   
1806 O O   . ILE A 239 ? 0.8420 0.4417 0.6575 0.0402  -0.0503 -0.0336 266 ILE A O   
1807 C CB  . ILE A 239 ? 0.8469 0.4349 0.6658 0.0225  -0.0140 -0.0457 266 ILE A CB  
1808 C CG1 . ILE A 239 ? 0.9511 0.5351 0.7675 0.0170  -0.0277 -0.0668 266 ILE A CG1 
1809 C CG2 . ILE A 239 ? 0.7474 0.3350 0.5785 0.0203  0.0111  -0.0392 266 ILE A CG2 
1810 C CD1 . ILE A 239 ? 0.7787 0.3437 0.5513 0.0125  -0.0223 -0.0741 266 ILE A CD1 
1811 N N   . ILE A 240 ? 0.9279 0.5479 0.8001 0.0321  -0.0612 -0.0607 267 ILE A N   
1812 C CA  . ILE A 240 ? 0.8994 0.5255 0.7635 0.0408  -0.0886 -0.0652 267 ILE A CA  
1813 C C   . ILE A 240 ? 0.8468 0.4895 0.7451 0.0489  -0.0876 -0.0547 267 ILE A C   
1814 O O   . ILE A 240 ? 0.7564 0.3954 0.6339 0.0598  -0.1018 -0.0476 267 ILE A O   
1815 C CB  . ILE A 240 ? 0.8977 0.5367 0.7829 0.0370  -0.1090 -0.0894 267 ILE A CB  
1816 C CG1 . ILE A 240 ? 1.0815 0.7041 0.9379 0.0277  -0.1048 -0.1022 267 ILE A CG1 
1817 C CG2 . ILE A 240 ? 1.0084 0.6517 0.8722 0.0492  -0.1411 -0.0940 267 ILE A CG2 
1818 C CD1 . ILE A 240 ? 1.1220 0.7563 0.9936 0.0235  -0.1268 -0.1299 267 ILE A CD1 
1819 N N   . VAL A 241 ? 0.8193 0.4781 0.7689 0.0446  -0.0691 -0.0529 268 VAL A N   
1820 C CA  . VAL A 241 ? 0.7451 0.4197 0.7266 0.0522  -0.0638 -0.0432 268 VAL A CA  
1821 C C   . VAL A 241 ? 0.8534 0.5133 0.7956 0.0600  -0.0571 -0.0253 268 VAL A C   
1822 O O   . VAL A 241 ? 0.8542 0.5167 0.7933 0.0703  -0.0672 -0.0205 268 VAL A O   
1823 C CB  . VAL A 241 ? 0.7002 0.3887 0.7346 0.0457  -0.0392 -0.0415 268 VAL A CB  
1824 C CG1 . VAL A 241 ? 0.6857 0.3845 0.7375 0.0543  -0.0262 -0.0270 268 VAL A CG1 
1825 C CG2 . VAL A 241 ? 0.6476 0.3550 0.7347 0.0381  -0.0471 -0.0611 268 VAL A CG2 
1826 N N   . PHE A 242 ? 0.7305 0.3754 0.6446 0.0552  -0.0402 -0.0169 269 PHE A N   
1827 C CA  . PHE A 242 ? 0.8137 0.4466 0.6945 0.0602  -0.0335 -0.0034 269 PHE A CA  
1828 C C   . PHE A 242 ? 0.8218 0.4348 0.6570 0.0644  -0.0514 -0.0029 269 PHE A C   
1829 O O   . PHE A 242 ? 0.8430 0.4485 0.6636 0.0717  -0.0533 0.0053  269 PHE A O   
1830 C CB  . PHE A 242 ? 0.7281 0.3543 0.5940 0.0542  -0.0134 0.0027  269 PHE A CB  
1831 C CG  . PHE A 242 ? 0.7749 0.3945 0.6156 0.0576  -0.0057 0.0133  269 PHE A CG  
1832 C CD1 . PHE A 242 ? 0.8117 0.4428 0.6696 0.0650  0.0006  0.0202  269 PHE A CD1 
1833 C CD2 . PHE A 242 ? 0.8245 0.4270 0.6257 0.0527  -0.0038 0.0145  269 PHE A CD2 
1834 C CE1 . PHE A 242 ? 0.8410 0.4670 0.6769 0.0673  0.0064  0.0263  269 PHE A CE1 
1835 C CE2 . PHE A 242 ? 0.7379 0.3361 0.5216 0.0538  0.0033  0.0211  269 PHE A CE2 
1836 C CZ  . PHE A 242 ? 0.6994 0.3094 0.5003 0.0610  0.0072  0.0261  269 PHE A CZ  
1837 N N   . ALA A 243 ? 0.8021 0.4037 0.6120 0.0606  -0.0634 -0.0115 270 ALA A N   
1838 C CA  . ALA A 243 ? 0.7882 0.3672 0.5493 0.0664  -0.0797 -0.0090 270 ALA A CA  
1839 C C   . ALA A 243 ? 0.8139 0.4000 0.5877 0.0801  -0.1003 -0.0088 270 ALA A C   
1840 O O   . ALA A 243 ? 1.0208 0.5879 0.7647 0.0887  -0.1055 0.0011  270 ALA A O   
1841 C CB  . ALA A 243 ? 0.7558 0.3236 0.4866 0.0615  -0.0893 -0.0197 270 ALA A CB  
1842 N N   . PHE A 244 ? 0.7596 0.3726 0.5809 0.0822  -0.1111 -0.0202 271 PHE A N   
1843 C CA  . PHE A 244 ? 0.8235 0.4501 0.6674 0.0962  -0.1300 -0.0216 271 PHE A CA  
1844 C C   . PHE A 244 ? 0.8603 0.4897 0.7214 0.1024  -0.1158 -0.0098 271 PHE A C   
1845 O O   . PHE A 244 ? 0.8825 0.5091 0.7415 0.1164  -0.1282 -0.0058 271 PHE A O   
1846 C CB  . PHE A 244 ? 0.7975 0.4576 0.6985 0.0943  -0.1413 -0.0391 271 PHE A CB  
1847 C CG  . PHE A 244 ? 0.8512 0.5311 0.7804 0.1096  -0.1642 -0.0441 271 PHE A CG  
1848 C CD1 . PHE A 244 ? 0.8353 0.5099 0.7351 0.1217  -0.1953 -0.0497 271 PHE A CD1 
1849 C CD2 . PHE A 244 ? 0.8148 0.5194 0.7994 0.1135  -0.1546 -0.0432 271 PHE A CD2 
1850 C CE1 . PHE A 244 ? 0.8621 0.5577 0.7907 0.1384  -0.2183 -0.0546 271 PHE A CE1 
1851 C CE2 . PHE A 244 ? 0.8322 0.5581 0.8480 0.1286  -0.1751 -0.0490 271 PHE A CE2 
1852 C CZ  . PHE A 244 ? 0.8898 0.6123 0.8794 0.1416  -0.2080 -0.0549 271 PHE A CZ  
1853 N N   . SER A 245 ? 0.8498 0.4839 0.7259 0.0937  -0.0902 -0.0046 272 SER A N   
1854 C CA  . SER A 245 ? 0.8539 0.4907 0.7412 0.0996  -0.0762 0.0048  272 SER A CA  
1855 C C   . SER A 245 ? 0.8722 0.4791 0.7104 0.1038  -0.0764 0.0145  272 SER A C   
1856 O O   . SER A 245 ? 0.9020 0.5052 0.7428 0.1144  -0.0779 0.0187  272 SER A O   
1857 C CB  . SER A 245 ? 0.7959 0.4444 0.7041 0.0911  -0.0505 0.0083  272 SER A CB  
1858 O OG  . SER A 245 ? 0.6678 0.3205 0.5833 0.0978  -0.0378 0.0156  272 SER A OG  
1859 N N   . CYS A 246 ? 0.8845 0.4689 0.6800 0.0952  -0.0728 0.0172  273 CYS A N   
1860 C CA  . CYS A 246 ? 0.8891 0.4420 0.6393 0.0969  -0.0713 0.0256  273 CYS A CA  
1861 C C   . CYS A 246 ? 0.8813 0.4161 0.6100 0.1105  -0.0932 0.0282  273 CYS A C   
1862 O O   . CYS A 246 ? 1.0488 0.5606 0.7570 0.1179  -0.0928 0.0358  273 CYS A O   
1863 C CB  . CYS A 246 ? 0.8557 0.3906 0.5690 0.0837  -0.0608 0.0270  273 CYS A CB  
1864 S SG  . CYS A 246 ? 0.8598 0.4152 0.5953 0.0711  -0.0369 0.0251  273 CYS A SG  
1865 N N   . LYS A 247 ? 0.9418 0.4860 0.6747 0.1150  -0.1130 0.0210  274 LYS A N   
1866 C CA  . LYS A 247 ? 0.8984 0.4294 0.6110 0.1317  -0.1376 0.0233  274 LYS A CA  
1867 C C   . LYS A 247 ? 0.9756 0.5191 0.7235 0.1471  -0.1434 0.0247  274 LYS A C   
1868 O O   . LYS A 247 ? 1.1074 0.6253 0.8299 0.1608  -0.1507 0.0337  274 LYS A O   
1869 C CB  . LYS A 247 ? 0.8617 0.4094 0.5793 0.1336  -0.1599 0.0110  274 LYS A CB  
1870 C CG  . LYS A 247 ? 1.0521 0.5884 0.7433 0.1534  -0.1896 0.0128  274 LYS A CG  
1871 C CD  . LYS A 247 ? 1.3425 0.8294 0.9603 0.1574  -0.1871 0.0285  274 LYS A CD  
1872 C CE  . LYS A 247 ? 1.4534 0.9246 1.0415 0.1817  -0.2159 0.0344  274 LYS A CE  
1873 N NZ  . LYS A 247 ? 1.5559 0.9723 1.0719 0.1865  -0.2089 0.0534  274 LYS A NZ  
1874 N N   . GLN A 248 ? 0.8585 0.4393 0.6653 0.1454  -0.1379 0.0163  275 GLN A N   
1875 C CA  . GLN A 248 ? 0.7606 0.3567 0.6051 0.1597  -0.1402 0.0161  275 GLN A CA  
1876 C C   . GLN A 248 ? 0.8763 0.4516 0.7057 0.1604  -0.1204 0.0253  275 GLN A C   
1877 O O   . GLN A 248 ? 0.9614 0.5308 0.7984 0.1756  -0.1246 0.0279  275 GLN A O   
1878 C CB  . GLN A 248 ? 0.8754 0.5154 0.7864 0.1557  -0.1343 0.0050  275 GLN A CB  
1879 C CG  . GLN A 248 ? 0.9026 0.5662 0.8373 0.1524  -0.1528 -0.0084 275 GLN A CG  
1880 C CD  . GLN A 248 ? 0.8915 0.5500 0.8079 0.1693  -0.1858 -0.0113 275 GLN A CD  
1881 O OE1 . GLN A 248 ? 0.8044 0.4745 0.7451 0.1869  -0.1986 -0.0120 275 GLN A OE1 
1882 N NE2 . GLN A 248 ? 1.0498 0.6907 0.9212 0.1656  -0.1996 -0.0129 275 GLN A NE2 
1883 N N   . ALA A 249 ? 0.9586 0.5240 0.7690 0.1448  -0.0996 0.0285  276 ALA A N   
1884 C CA  . ALA A 249 ? 0.8682 0.4152 0.6628 0.1434  -0.0825 0.0338  276 ALA A CA  
1885 C C   . ALA A 249 ? 0.9304 0.4328 0.6732 0.1455  -0.0860 0.0420  276 ALA A C   
1886 O O   . ALA A 249 ? 1.0757 0.5589 0.8055 0.1436  -0.0727 0.0444  276 ALA A O   
1887 C CB  . ALA A 249 ? 0.8028 0.3607 0.5996 0.1272  -0.0609 0.0325  276 ALA A CB  
1888 N N   . GLU A 250 ? 0.9568 0.6121 0.7131 0.1850  -0.0303 0.0697  277 GLU A N   
1889 C CA  . GLU A 250 ? 0.9710 0.5591 0.6684 0.1793  -0.0336 0.0626  277 GLU A CA  
1890 C C   . GLU A 250 ? 0.8889 0.4710 0.5480 0.1578  -0.0125 0.0521  277 GLU A C   
1891 O O   . GLU A 250 ? 0.9831 0.5294 0.6084 0.1524  -0.0004 0.0393  277 GLU A O   
1892 C CB  . GLU A 250 ? 0.9759 0.5375 0.6719 0.1970  -0.0320 0.0545  277 GLU A CB  
1893 C CG  . GLU A 250 ? 1.2222 0.7856 0.9567 0.2204  -0.0560 0.0638  277 GLU A CG  
1894 C CD  . GLU A 250 ? 1.3909 0.9248 1.1233 0.2404  -0.0541 0.0558  277 GLU A CD  
1895 O OE1 . GLU A 250 ? 1.4788 0.9823 1.1745 0.2339  -0.0346 0.0429  277 GLU A OE1 
1896 O OE2 . GLU A 250 ? 1.4425 0.9841 1.2136 0.2627  -0.0721 0.0612  277 GLU A OE2 
1897 N N   . VAL A 251 ? 0.8312 0.4492 0.4999 0.1455  -0.0080 0.0569  278 VAL A N   
1898 C CA  . VAL A 251 ? 0.8562 0.4771 0.4970 0.1263  0.0089  0.0475  278 VAL A CA  
1899 C C   . VAL A 251 ? 0.9982 0.5804 0.6059 0.1123  -0.0011 0.0548  278 VAL A C   
1900 O O   . VAL A 251 ? 1.0241 0.6168 0.6474 0.1135  -0.0161 0.0678  278 VAL A O   
1901 C CB  . VAL A 251 ? 0.8198 0.5075 0.4914 0.1257  0.0223  0.0478  278 VAL A CB  
1902 C CG1 . VAL A 251 ? 0.7646 0.4569 0.4117 0.1073  0.0338  0.0396  278 VAL A CG1 
1903 C CG2 . VAL A 251 ? 0.7703 0.4908 0.4611 0.1393  0.0361  0.0374  278 VAL A CG2 
1904 N N   . GLN A 252 ? 1.0040 0.5406 0.5668 0.0985  0.0089  0.0455  279 GLN A N   
1905 C CA  . GLN A 252 ? 0.9076 0.3995 0.4301 0.0859  0.0039  0.0514  279 GLN A CA  
1906 C C   . GLN A 252 ? 0.9183 0.4436 0.4451 0.0697  0.0173  0.0475  279 GLN A C   
1907 O O   . GLN A 252 ? 1.0324 0.5783 0.5617 0.0596  0.0369  0.0328  279 GLN A O   
1908 C CB  . GLN A 252 ? 0.9536 0.3755 0.4253 0.0790  0.0128  0.0452  279 GLN A CB  
1909 C CG  . GLN A 252 ? 1.0824 0.4531 0.5045 0.0665  0.0128  0.0515  279 GLN A CG  
1910 C CD  . GLN A 252 ? 1.0992 0.4539 0.5126 0.0786  -0.0162 0.0676  279 GLN A CD  
1911 O OE1 . GLN A 252 ? 1.1674 0.5010 0.5804 0.0968  -0.0372 0.0749  279 GLN A OE1 
1912 N NE2 . GLN A 252 ? 1.1970 0.5627 0.6058 0.0693  -0.0187 0.0712  279 GLN A NE2 
1913 N N   . MET A 253 ? 0.9661 0.4970 0.4959 0.0681  0.0055  0.0589  280 MET A N   
1914 C CA  . MET A 253 ? 1.0592 0.6130 0.5890 0.0543  0.0173  0.0563  280 MET A CA  
1915 C C   . MET A 253 ? 0.9953 0.4979 0.4762 0.0379  0.0303  0.0491  280 MET A C   
1916 O O   . MET A 253 ? 0.9642 0.4066 0.4036 0.0383  0.0223  0.0546  280 MET A O   
1917 C CB  . MET A 253 ? 0.8170 0.3880 0.3662 0.0580  0.0016  0.0699  280 MET A CB  
1918 C CG  . MET A 253 ? 1.0850 0.7197 0.6888 0.0680  0.0013  0.0765  280 MET A CG  
1919 S SD  . MET A 253 ? 0.9807 0.6269 0.6153 0.0720  -0.0183 0.0925  280 MET A SD  
1920 C CE  . MET A 253 ? 1.2226 0.8344 0.8582 0.0844  -0.0452 0.0964  280 MET A CE  
1921 N N   . TYR A 254 ? 0.9150 0.4420 0.4010 0.0244  0.0510  0.0366  281 TYR A N   
1922 C CA  . TYR A 254 ? 0.9439 0.4306 0.3936 0.0066  0.0693  0.0280  281 TYR A CA  
1923 C C   . TYR A 254 ? 0.9698 0.4851 0.4293 -0.0025 0.0776  0.0263  281 TYR A C   
1924 O O   . TYR A 254 ? 0.8324 0.4070 0.3306 0.0029  0.0754  0.0263  281 TYR A O   
1925 C CB  . TYR A 254 ? 0.9289 0.4145 0.3808 -0.0042 0.0900  0.0089  281 TYR A CB  
1926 C CG  . TYR A 254 ? 1.0458 0.4870 0.4792 0.0023  0.0872  0.0088  281 TYR A CG  
1927 C CD1 . TYR A 254 ? 1.1048 0.4702 0.4889 -0.0045 0.0951  0.0123  281 TYR A CD1 
1928 C CD2 . TYR A 254 ? 1.1228 0.5951 0.5857 0.0168  0.0785  0.0058  281 TYR A CD2 
1929 C CE1 . TYR A 254 ? 1.0488 0.3696 0.4148 0.0037  0.0926  0.0135  281 TYR A CE1 
1930 C CE2 . TYR A 254 ? 1.0825 0.5135 0.5307 0.0246  0.0763  0.0050  281 TYR A CE2 
1931 C CZ  . TYR A 254 ? 1.1375 0.4922 0.5380 0.0184  0.0825  0.0092  281 TYR A CZ  
1932 O OH  . TYR A 254 ? 1.3699 0.6794 0.7545 0.0284  0.0804  0.0097  281 TYR A OH  
1933 N N   . VAL A 255 ? 1.0333 0.5032 0.4547 -0.0146 0.0888  0.0257  282 VAL A N   
1934 C CA  . VAL A 255 ? 0.9535 0.4443 0.3821 -0.0253 0.1035  0.0197  282 VAL A CA  
1935 C C   . VAL A 255 ? 1.0976 0.5605 0.5072 -0.0446 0.1322  0.0047  282 VAL A C   
1936 O O   . VAL A 255 ? 1.1068 0.5056 0.4727 -0.0499 0.1398  0.0071  282 VAL A O   
1937 C CB  . VAL A 255 ? 1.0691 0.5339 0.4733 -0.0218 0.0925  0.0323  282 VAL A CB  
1938 C CG1 . VAL A 255 ? 0.9725 0.3573 0.3132 -0.0237 0.0909  0.0387  282 VAL A CG1 
1939 C CG2 . VAL A 255 ? 1.0151 0.5054 0.4321 -0.0304 0.1088  0.0254  282 VAL A CG2 
1940 N N   . CYS A 256 ? 0.9913 0.5023 0.4359 -0.0543 0.1485  -0.0109 283 CYS A N   
1941 C CA  . CYS A 256 ? 1.0894 0.5843 0.5303 -0.0750 0.1781  -0.0282 283 CYS A CA  
1942 C C   . CYS A 256 ? 1.1216 0.6240 0.5635 -0.0826 0.1929  -0.0305 283 CYS A C   
1943 O O   . CYS A 256 ? 1.1285 0.6829 0.6019 -0.0736 0.1831  -0.0292 283 CYS A O   
1944 C CB  . CYS A 256 ? 0.9089 0.4569 0.3967 -0.0810 0.1847  -0.0504 283 CYS A CB  
1945 S SG  . CYS A 256 ? 1.7416 1.2859 1.2321 -0.0708 0.1699  -0.0520 283 CYS A SG  
1946 N N   . ASN A 257 ? 1.1873 0.6348 0.5931 -0.0981 0.2184  -0.0330 284 ASN A N   
1947 C CA  . ASN A 257 ? 1.0906 0.5382 0.4936 -0.1061 0.2380  -0.0367 284 ASN A CA  
1948 C C   . ASN A 257 ? 1.1664 0.6077 0.5828 -0.1296 0.2757  -0.0561 284 ASN A C   
1949 O O   . ASN A 257 ? 1.1807 0.5887 0.5727 -0.1400 0.3017  -0.0566 284 ASN A O   
1950 C CB  . ASN A 257 ? 1.0751 0.4559 0.4131 -0.0999 0.2341  -0.0186 284 ASN A CB  
1951 C CG  . ASN A 257 ? 1.3163 0.6183 0.6004 -0.1062 0.2449  -0.0129 284 ASN A CG  
1952 O OD1 . ASN A 257 ? 1.3537 0.6388 0.6335 -0.1152 0.2571  -0.0176 284 ASN A OD1 
1953 N ND2 . ASN A 257 ? 1.2981 0.5537 0.5451 -0.0991 0.2385  -0.0051 284 ASN A ND2 
1954 N N   . LYS A 258 ? 0.9916 0.4650 0.4486 -0.1387 0.2802  -0.0736 285 LYS A N   
1955 C CA  . LYS A 258 ? 1.1392 0.6041 0.6154 -0.1639 0.3161  -0.0941 285 LYS A CA  
1956 C C   . LYS A 258 ? 1.2289 0.7453 0.7518 -0.1730 0.3351  -0.1106 285 LYS A C   
1957 O O   . LYS A 258 ? 1.2921 0.7891 0.8227 -0.1949 0.3714  -0.1236 285 LYS A O   
1958 C CB  . LYS A 258 ? 1.0267 0.5187 0.5407 -0.1705 0.3118  -0.1126 285 LYS A CB  
1959 C CG  . LYS A 258 ? 1.0359 0.4662 0.5038 -0.1644 0.3017  -0.0986 285 LYS A CG  
1960 C CD  . LYS A 258 ? 1.0237 0.4800 0.5282 -0.1691 0.2968  -0.1186 285 LYS A CD  
1961 C CE  . LYS A 258 ? 1.1366 0.5312 0.5960 -0.1591 0.2856  -0.1033 285 LYS A CE  
1962 N NZ  . LYS A 258 ? 1.3206 0.7352 0.8124 -0.1623 0.2816  -0.1239 285 LYS A NZ  
1963 N N   . GLU A 259 ? 1.2310 0.8105 0.7864 -0.1561 0.3132  -0.1098 286 GLU A N   
1964 C CA  . GLU A 259 ? 1.1734 0.8002 0.7710 -0.1596 0.3282  -0.1229 286 GLU A CA  
1965 C C   . GLU A 259 ? 1.0734 0.7328 0.6730 -0.1350 0.3016  -0.1079 286 GLU A C   
1966 O O   . GLU A 259 ? 0.9450 0.5903 0.5165 -0.1185 0.2742  -0.0887 286 GLU A O   
1967 C CB  . GLU A 259 ? 0.9621 0.6602 0.6345 -0.1708 0.3344  -0.1537 286 GLU A CB  
1968 C CG  . GLU A 259 ? 0.9764 0.7187 0.6732 -0.1601 0.3038  -0.1605 286 GLU A CG  
1969 C CD  . GLU A 259 ? 1.2047 1.0091 0.9694 -0.1735 0.3096  -0.1952 286 GLU A CD  
1970 O OE1 . GLU A 259 ? 1.0157 0.8780 0.8308 -0.1733 0.3143  -0.2109 286 GLU A OE1 
1971 O OE2 . GLU A 259 ? 1.2284 1.0238 0.9979 -0.1835 0.3085  -0.2083 286 GLU A OE2 
1972 N N   . GLU A 260 ? 1.0263 0.7286 0.6629 -0.1328 0.3112  -0.1172 287 GLU A N   
1973 C CA  . GLU A 260 ? 0.8245 0.5603 0.4701 -0.1093 0.2880  -0.1044 287 GLU A CA  
1974 C C   . GLU A 260 ? 1.0496 0.8539 0.7369 -0.0934 0.2587  -0.1074 287 GLU A C   
1975 O O   . GLU A 260 ? 0.8728 0.7312 0.6090 -0.0987 0.2607  -0.1298 287 GLU A O   
1976 C CB  . GLU A 260 ? 0.8313 0.5920 0.5053 -0.1091 0.3076  -0.1138 287 GLU A CB  
1977 C CG  . GLU A 260 ? 1.4308 1.1366 1.0546 -0.1028 0.3136  -0.0968 287 GLU A CG  
1978 C CD  . GLU A 260 ? 1.3927 1.1338 1.0510 -0.0945 0.3252  -0.1042 287 GLU A CD  
1979 O OE1 . GLU A 260 ? 1.2384 1.0501 0.9619 -0.0920 0.3263  -0.1214 287 GLU A OE1 
1980 O OE2 . GLU A 260 ? 1.3808 1.0791 1.0009 -0.0891 0.3318  -0.0941 287 GLU A OE2 
1981 N N   . TYR A 261 ? 0.8989 0.7004 0.5666 -0.0740 0.2318  -0.0858 288 TYR A N   
1982 C CA  . TYR A 261 ? 0.7908 0.6518 0.4890 -0.0555 0.2062  -0.0838 288 TYR A CA  
1983 C C   . TYR A 261 ? 0.8237 0.7202 0.5401 -0.0337 0.1939  -0.0714 288 TYR A C   
1984 O O   . TYR A 261 ? 0.9637 0.9239 0.7196 -0.0205 0.1842  -0.0792 288 TYR A O   
1985 C CB  . TYR A 261 ? 0.8226 0.6567 0.4905 -0.0495 0.1876  -0.0683 288 TYR A CB  
1986 C CG  . TYR A 261 ? 0.8482 0.6417 0.4952 -0.0677 0.1982  -0.0782 288 TYR A CG  
1987 C CD1 . TYR A 261 ? 0.8593 0.6856 0.5372 -0.0779 0.2041  -0.1027 288 TYR A CD1 
1988 C CD2 . TYR A 261 ? 0.8361 0.5565 0.4319 -0.0738 0.2012  -0.0639 288 TYR A CD2 
1989 C CE1 . TYR A 261 ? 0.9142 0.6982 0.5742 -0.0949 0.2157  -0.1117 288 TYR A CE1 
1990 C CE2 . TYR A 261 ? 0.9692 0.6471 0.5430 -0.0881 0.2116  -0.0707 288 TYR A CE2 
1991 C CZ  . TYR A 261 ? 1.0338 0.7420 0.6406 -0.0994 0.2204  -0.0941 288 TYR A CZ  
1992 O OH  . TYR A 261 ? 1.0978 0.7587 0.6838 -0.1140 0.2327  -0.1007 288 TYR A OH  
1993 N N   . GLY A 262 ? 0.6967 0.5515 0.3841 -0.0289 0.1935  -0.0530 289 GLY A N   
1994 C CA  . GLY A 262 ? 0.7859 0.6669 0.4906 -0.0088 0.1838  -0.0405 289 GLY A CA  
1995 C C   . GLY A 262 ? 0.8116 0.6355 0.4803 -0.0080 0.1844  -0.0242 289 GLY A C   
1996 O O   . GLY A 262 ? 0.8034 0.5688 0.4311 -0.0222 0.1930  -0.0242 289 GLY A O   
1997 N N   . PHE A 263 ? 0.7806 0.6204 0.4636 0.0100  0.1745  -0.0105 290 PHE A N   
1998 C CA  . PHE A 263 ? 0.9036 0.6957 0.5612 0.0124  0.1738  0.0015  290 PHE A CA  
1999 C C   . PHE A 263 ? 0.7733 0.5699 0.4374 0.0282  0.1523  0.0239  290 PHE A C   
2000 O O   . PHE A 263 ? 0.7032 0.5479 0.3965 0.0425  0.1431  0.0312  290 PHE A O   
2001 C CB  . PHE A 263 ? 0.7167 0.5174 0.3910 0.0170  0.1906  -0.0072 290 PHE A CB  
2002 C CG  . PHE A 263 ? 0.7622 0.5599 0.4365 0.0007  0.2169  -0.0294 290 PHE A CG  
2003 C CD1 . PHE A 263 ? 0.8438 0.6966 0.5584 -0.0026 0.2239  -0.0465 290 PHE A CD1 
2004 C CD2 . PHE A 263 ? 0.9278 0.6676 0.5624 -0.0112 0.2355  -0.0343 290 PHE A CD2 
2005 C CE1 . PHE A 263 ? 0.8952 0.7465 0.6181 -0.0200 0.2512  -0.0678 290 PHE A CE1 
2006 C CE2 . PHE A 263 ? 1.0375 0.7723 0.6727 -0.0268 0.2650  -0.0533 290 PHE A CE2 
2007 C CZ  . PHE A 263 ? 1.1602 0.9516 0.8435 -0.0324 0.2740  -0.0700 290 PHE A CZ  
2008 N N   . LEU A 264 ? 0.8074 0.5526 0.4438 0.0257  0.1447  0.0341  291 LEU A N   
2009 C CA  . LEU A 264 ? 0.9109 0.6555 0.5589 0.0373  0.1269  0.0543  291 LEU A CA  
2010 C C   . LEU A 264 ? 0.8382 0.5348 0.4691 0.0363  0.1250  0.0573  291 LEU A C   
2011 O O   . LEU A 264 ? 1.0606 0.7119 0.6542 0.0247  0.1315  0.0458  291 LEU A O   
2012 C CB  . LEU A 264 ? 0.7877 0.5236 0.4262 0.0336  0.1112  0.0627  291 LEU A CB  
2013 C CG  . LEU A 264 ? 0.8567 0.5336 0.4576 0.0225  0.1003  0.0631  291 LEU A CG  
2014 C CD1 . LEU A 264 ? 0.8955 0.5785 0.5029 0.0245  0.0839  0.0733  291 LEU A CD1 
2015 C CD2 . LEU A 264 ? 1.0055 0.6450 0.5645 0.0082  0.1133  0.0468  291 LEU A CD2 
2016 N N   . PRO A 265 ? 0.8810 0.5834 0.5362 0.0484  0.1174  0.0721  292 PRO A N   
2017 C CA  . PRO A 265 ? 0.8262 0.4815 0.4683 0.0468  0.1140  0.0723  292 PRO A CA  
2018 C C   . PRO A 265 ? 0.9363 0.5508 0.5579 0.0377  0.0940  0.0761  292 PRO A C   
2019 O O   . PRO A 265 ? 0.9098 0.5398 0.5435 0.0376  0.0816  0.0859  292 PRO A O   
2020 C CB  . PRO A 265 ? 0.7742 0.4539 0.4565 0.0635  0.1147  0.0878  292 PRO A CB  
2021 C CG  . PRO A 265 ? 0.7533 0.4799 0.4610 0.0720  0.1092  0.1026  292 PRO A CG  
2022 C CD  . PRO A 265 ? 0.8811 0.6310 0.5749 0.0649  0.1136  0.0889  292 PRO A CD  
2023 N N   . VAL A 266 ? 0.9526 0.5151 0.5430 0.0313  0.0902  0.0665  293 VAL A N   
2024 C CA  . VAL A 266 ? 0.9126 0.4357 0.4842 0.0244  0.0666  0.0672  293 VAL A CA  
2025 C C   . VAL A 266 ? 0.8976 0.4334 0.5166 0.0300  0.0532  0.0821  293 VAL A C   
2026 O O   . VAL A 266 ? 1.0531 0.5892 0.6951 0.0364  0.0607  0.0854  293 VAL A O   
2027 C CB  . VAL A 266 ? 0.8858 0.3488 0.4058 0.0180  0.0648  0.0508  293 VAL A CB  
2028 C CG1 . VAL A 266 ? 0.9134 0.3387 0.4166 0.0134  0.0351  0.0494  293 VAL A CG1 
2029 C CG2 . VAL A 266 ? 1.0963 0.5433 0.5681 0.0116  0.0831  0.0385  293 VAL A CG2 
2030 N N   . PRO A 267 ? 1.0812 0.6270 0.7191 0.0282  0.0359  0.0915  294 PRO A N   
2031 C CA  . PRO A 267 ? 1.0179 0.5773 0.7071 0.0318  0.0278  0.1066  294 PRO A CA  
2032 C C   . PRO A 267 ? 0.9417 0.4582 0.6327 0.0270  0.0166  0.0985  294 PRO A C   
2033 O O   . PRO A 267 ? 0.9820 0.4546 0.6301 0.0201  0.0045  0.0810  294 PRO A O   
2034 C CB  . PRO A 267 ? 0.7911 0.3634 0.4935 0.0288  0.0111  0.1127  294 PRO A CB  
2035 C CG  . PRO A 267 ? 0.9059 0.4874 0.5723 0.0280  0.0171  0.1063  294 PRO A CG  
2036 C CD  . PRO A 267 ? 0.9071 0.4543 0.5245 0.0236  0.0261  0.0898  294 PRO A CD  
2037 N N   . LEU A 268 ? 1.0038 0.5305 0.7426 0.0312  0.0212  0.1114  295 LEU A N   
2038 C CA  . LEU A 268 ? 0.8457 0.3333 0.5953 0.0267  0.0134  0.1034  295 LEU A CA  
2039 C C   . LEU A 268 ? 1.0010 0.4814 0.7891 0.0175  -0.0096 0.1052  295 LEU A C   
2040 O O   . LEU A 268 ? 0.9935 0.5032 0.8056 0.0168  -0.0161 0.1158  295 LEU A O   
2041 C CB  . LEU A 268 ? 0.9342 0.4311 0.7143 0.0372  0.0352  0.1159  295 LEU A CB  
2042 C CG  . LEU A 268 ? 0.9199 0.4256 0.6710 0.0476  0.0563  0.1112  295 LEU A CG  
2043 C CD1 . LEU A 268 ? 0.9231 0.4447 0.7099 0.0624  0.0752  0.1280  295 LEU A CD1 
2044 C CD2 . LEU A 268 ? 0.9628 0.4215 0.6648 0.0415  0.0537  0.0856  295 LEU A CD2 
2045 N N   . ARG A 269 ? 1.0851 0.5267 0.8825 0.0106  -0.0218 0.0926  296 ARG A N   
2046 C CA  . ARG A 269 ? 0.9047 0.3383 0.7448 0.0000  -0.0461 0.0888  296 ARG A CA  
2047 C C   . ARG A 269 ? 0.9712 0.4365 0.8860 0.0008  -0.0313 0.1133  296 ARG A C   
2048 O O   . ARG A 269 ? 0.9882 0.4731 0.9152 0.0113  -0.0037 0.1328  296 ARG A O   
2049 C CB  . ARG A 269 ? 1.1508 0.5321 0.9782 -0.0081 -0.0647 0.0641  296 ARG A CB  
2050 C CG  . ARG A 269 ? 1.2383 0.5814 0.9880 -0.0091 -0.0832 0.0393  296 ARG A CG  
2051 C CD  . ARG A 269 ? 1.5825 0.8743 1.3209 -0.0160 -0.1033 0.0135  296 ARG A CD  
2052 N NE  . ARG A 269 ? 1.9666 1.2155 1.6201 -0.0143 -0.1179 -0.0097 296 ARG A NE  
2053 C CZ  . ARG A 269 ? 2.0230 1.2211 1.6432 -0.0172 -0.1339 -0.0358 296 ARG A CZ  
2054 N NH1 . ARG A 269 ? 1.8150 0.9982 1.4837 -0.0235 -0.1389 -0.0443 296 ARG A NH1 
2055 N NH2 . ARG A 269 ? 2.0841 1.2427 1.6181 -0.0134 -0.1438 -0.0540 296 ARG A NH2 
2056 N N   . ALA A 270 ? 0.9080 0.3777 0.8734 -0.0096 -0.0498 0.1121  297 ALA A N   
2057 C CA  . ALA A 270 ? 0.8704 0.3675 0.9099 -0.0110 -0.0332 0.1356  297 ALA A CA  
2058 C C   . ALA A 270 ? 0.9952 0.4690 1.0602 -0.0103 -0.0129 0.1433  297 ALA A C   
2059 O O   . ALA A 270 ? 0.9755 0.4701 1.0723 -0.0022 0.0154  0.1708  297 ALA A O   
2060 C CB  . ALA A 270 ? 0.8577 0.3615 0.9532 -0.0246 -0.0579 0.1276  297 ALA A CB  
2061 N N   . HIS A 271 ? 0.9164 0.3438 0.9640 -0.0171 -0.0264 0.1196  298 HIS A N   
2062 C CA  . HIS A 271 ? 0.9444 0.3418 1.0164 -0.0168 -0.0091 0.1233  298 HIS A CA  
2063 C C   . HIS A 271 ? 1.0040 0.3886 1.0222 -0.0010 0.0104  0.1242  298 HIS A C   
2064 O O   . HIS A 271 ? 1.0408 0.3880 1.0608 0.0001  0.0180  0.1166  298 HIS A O   
2065 C CB  . HIS A 271 ? 1.2279 0.5811 1.3207 -0.0338 -0.0350 0.0942  298 HIS A CB  
2066 C CG  . HIS A 271 ? 1.1137 0.4817 1.2808 -0.0500 -0.0506 0.0939  298 HIS A CG  
2067 N ND1 . HIS A 271 ? 1.0259 0.3665 1.2154 -0.0665 -0.0844 0.0630  298 HIS A ND1 
2068 C CD2 . HIS A 271 ? 0.9843 0.3934 1.2108 -0.0519 -0.0366 0.1194  298 HIS A CD2 
2069 C CE1 . HIS A 271 ? 1.2332 0.6007 1.4998 -0.0788 -0.0912 0.0689  298 HIS A CE1 
2070 N NE2 . HIS A 271 ? 1.0901 0.4986 1.3800 -0.0703 -0.0604 0.1038  298 HIS A NE2 
2071 N N   . SER A 272 ? 0.9456 0.3610 0.9204 0.0113  0.0191  0.1317  299 SER A N   
2072 C CA  . SER A 272 ? 0.9216 0.3349 0.8566 0.0270  0.0391  0.1332  299 SER A CA  
2073 C C   . SER A 272 ? 0.9130 0.3471 0.8832 0.0424  0.0677  0.1643  299 SER A C   
2074 O O   . SER A 272 ? 0.9834 0.4295 1.0038 0.0401  0.0748  0.1857  299 SER A O   
2075 C CB  . SER A 272 ? 1.0540 0.4930 0.9358 0.0324  0.0376  0.1274  299 SER A CB  
2076 O OG  . SER A 272 ? 1.2370 0.6505 1.0800 0.0204  0.0127  0.1018  299 SER A OG  
2077 N N   . THR A 273 ? 0.9104 0.3488 0.8538 0.0597  0.0851  0.1675  300 THR A N   
2078 C CA  . THR A 273 ? 0.9916 0.4428 0.9600 0.0789  0.1099  0.1955  300 THR A CA  
2079 C C   . THR A 273 ? 0.9328 0.4342 0.8766 0.0981  0.1210  0.2081  300 THR A C   
2080 O O   . THR A 273 ? 0.9626 0.4824 0.8696 0.0957  0.1130  0.1913  300 THR A O   
2081 C CB  . THR A 273 ? 0.9526 0.3606 0.9215 0.0865  0.1203  0.1880  300 THR A CB  
2082 O OG1 . THR A 273 ? 1.0622 0.4747 0.9866 0.0970  0.1235  0.1706  300 THR A OG1 
2083 C CG2 . THR A 273 ? 0.9912 0.3464 0.9744 0.0658  0.1047  0.1652  300 THR A CG2 
2084 N N   . LEU A 274 ? 0.7872 0.4363 0.7121 -0.0617 0.1754  -0.1283 301 LEU A N   
2085 C CA  . LEU A 274 ? 0.8013 0.4408 0.7031 -0.0452 0.1671  -0.0922 301 LEU A CA  
2086 C C   . LEU A 274 ? 0.7744 0.4037 0.6600 -0.0228 0.1580  -0.0714 301 LEU A C   
2087 O O   . LEU A 274 ? 0.9162 0.5613 0.7928 -0.0073 0.1415  -0.0512 301 LEU A O   
2088 C CB  . LEU A 274 ? 0.8141 0.4109 0.6990 -0.0528 0.1916  -0.0764 301 LEU A CB  
2089 C CG  . LEU A 274 ? 1.0620 0.6687 0.9619 -0.0757 0.2031  -0.0942 301 LEU A CG  
2090 C CD1 . LEU A 274 ? 0.8691 0.4206 0.7459 -0.0834 0.2348  -0.0792 301 LEU A CD1 
2091 C CD2 . LEU A 274 ? 0.9041 0.5560 0.8100 -0.0699 0.1782  -0.0899 301 LEU A CD2 
2092 N N   . GLN A 275 ? 0.8002 0.4047 0.6838 -0.0217 0.1697  -0.0783 302 GLN A N   
2093 C CA  . GLN A 275 ? 0.8281 0.4275 0.6994 -0.0005 0.1611  -0.0622 302 GLN A CA  
2094 C C   . GLN A 275 ? 0.9192 0.5616 0.7999 0.0081  0.1375  -0.0706 302 GLN A C   
2095 O O   . GLN A 275 ? 1.0187 0.6704 0.8906 0.0249  0.1258  -0.0527 302 GLN A O   
2096 C CB  . GLN A 275 ? 0.8652 0.4256 0.7312 -0.0013 0.1807  -0.0692 302 GLN A CB  
2097 C CG  . GLN A 275 ? 1.0682 0.6218 0.9213 0.0214  0.1741  -0.0531 302 GLN A CG  
2098 C CD  . GLN A 275 ? 1.2100 0.7287 1.0601 0.0204  0.1919  -0.0645 302 GLN A CD  
2099 O OE1 . GLN A 275 ? 1.1999 0.6979 1.0587 0.0007  0.2108  -0.0861 302 GLN A OE1 
2100 N NE2 . GLN A 275 ? 1.1813 0.6941 1.0209 0.0406  0.1873  -0.0523 302 GLN A NE2 
2101 N N   . ASP A 276 ? 0.9001 0.5690 0.7975 -0.0020 0.1316  -0.0993 303 ASP A N   
2102 C CA  . ASP A 276 ? 0.8070 0.5123 0.7052 0.0099  0.1102  -0.1061 303 ASP A CA  
2103 C C   . ASP A 276 ? 0.9148 0.6372 0.8059 0.0172  0.0966  -0.0865 303 ASP A C   
2104 O O   . ASP A 276 ? 0.8798 0.6119 0.7610 0.0317  0.0857  -0.0749 303 ASP A O   
2105 C CB  . ASP A 276 ? 0.8462 0.5811 0.7613 0.0014  0.1047  -0.1422 303 ASP A CB  
2106 C CG  . ASP A 276 ? 1.0615 0.7886 0.9849 -0.0028 0.1142  -0.1667 303 ASP A CG  
2107 O OD1 . ASP A 276 ? 1.1753 0.8910 1.0864 0.0112  0.1126  -0.1580 303 ASP A OD1 
2108 O OD2 . ASP A 276 ? 0.9895 0.7232 0.9336 -0.0211 0.1244  -0.1968 303 ASP A OD2 
2109 N N   . GLU A 277 ? 0.8495 0.5739 0.7456 0.0061  0.0995  -0.0837 304 GLU A N   
2110 C CA  . GLU A 277 ? 0.7661 0.5059 0.6566 0.0116  0.0878  -0.0670 304 GLU A CA  
2111 C C   . GLU A 277 ? 0.7750 0.5013 0.6535 0.0233  0.0883  -0.0397 304 GLU A C   
2112 O O   . GLU A 277 ? 0.8202 0.5617 0.6948 0.0328  0.0776  -0.0299 304 GLU A O   
2113 C CB  . GLU A 277 ? 0.7702 0.5134 0.6681 -0.0029 0.0927  -0.0707 304 GLU A CB  
2114 C CG  . GLU A 277 ? 0.8222 0.5854 0.7169 0.0013  0.0797  -0.0593 304 GLU A CG  
2115 C CD  . GLU A 277 ? 1.0189 0.8117 0.9167 0.0066  0.0641  -0.0752 304 GLU A CD  
2116 O OE1 . GLU A 277 ? 0.9807 0.7878 0.8891 0.0019  0.0633  -0.1011 304 GLU A OE1 
2117 O OE2 . GLU A 277 ? 1.1065 0.9080 0.9950 0.0167  0.0536  -0.0634 304 GLU A OE2 
2118 N N   . ALA A 278 ? 0.7894 0.4870 0.6615 0.0238  0.1021  -0.0289 305 ALA A N   
2119 C CA  . ALA A 278 ? 0.8763 0.5672 0.7379 0.0385  0.1012  -0.0061 305 ALA A CA  
2120 C C   . ALA A 278 ? 0.8804 0.5812 0.7423 0.0509  0.0946  -0.0042 305 ALA A C   
2121 O O   . ALA A 278 ? 0.8772 0.5957 0.7398 0.0594  0.0866  0.0065  305 ALA A O   
2122 C CB  . ALA A 278 ? 0.7302 0.3834 0.5781 0.0419  0.1181  0.0040  305 ALA A CB  
2123 N N   . GLU A 279 ? 0.8723 0.5629 0.7349 0.0511  0.0995  -0.0165 306 GLU A N   
2124 C CA  . GLU A 279 ? 0.9273 0.6255 0.7881 0.0630  0.0953  -0.0154 306 GLU A CA  
2125 C C   . GLU A 279 ? 0.7207 0.4438 0.5818 0.0639  0.0838  -0.0201 306 GLU A C   
2126 O O   . GLU A 279 ? 0.8029 0.5338 0.6609 0.0729  0.0819  -0.0128 306 GLU A O   
2127 C CB  . GLU A 279 ? 0.7934 0.4740 0.6530 0.0635  0.1036  -0.0291 306 GLU A CB  
2128 C CG  . GLU A 279 ? 0.9086 0.5558 0.7620 0.0670  0.1182  -0.0216 306 GLU A CG  
2129 C CD  . GLU A 279 ? 1.0652 0.6926 0.9192 0.0643  0.1285  -0.0387 306 GLU A CD  
2130 O OE1 . GLU A 279 ? 0.9974 0.6417 0.8584 0.0588  0.1226  -0.0590 306 GLU A OE1 
2131 O OE2 . GLU A 279 ? 1.0488 0.6433 0.8944 0.0694  0.1424  -0.0328 306 GLU A OE2 
2132 N N   . SER A 280 ? 0.7657 0.4997 0.6290 0.0558  0.0779  -0.0327 307 SER A N   
2133 C CA  . SER A 280 ? 0.7638 0.5150 0.6204 0.0607  0.0681  -0.0355 307 SER A CA  
2134 C C   . SER A 280 ? 0.7719 0.5310 0.6286 0.0612  0.0656  -0.0189 307 SER A C   
2135 O O   . SER A 280 ? 0.8308 0.5931 0.6797 0.0677  0.0652  -0.0141 307 SER A O   
2136 C CB  . SER A 280 ? 0.7385 0.5029 0.5975 0.0551  0.0611  -0.0542 307 SER A CB  
2137 O OG  . SER A 280 ? 0.9360 0.7119 0.7821 0.0642  0.0520  -0.0550 307 SER A OG  
2138 N N   . PHE A 281 ? 0.7988 0.5597 0.6633 0.0540  0.0660  -0.0114 308 PHE A N   
2139 C CA  . PHE A 281 ? 0.7687 0.5417 0.6363 0.0543  0.0631  0.0007  308 PHE A CA  
2140 C C   . PHE A 281 ? 0.7346 0.5098 0.6058 0.0624  0.0676  0.0099  308 PHE A C   
2141 O O   . PHE A 281 ? 0.7814 0.5700 0.6571 0.0629  0.0674  0.0135  308 PHE A O   
2142 C CB  . PHE A 281 ? 0.7228 0.4988 0.5951 0.0476  0.0618  0.0055  308 PHE A CB  
2143 C CG  . PHE A 281 ? 0.7452 0.5383 0.6228 0.0485  0.0577  0.0144  308 PHE A CG  
2144 C CD1 . PHE A 281 ? 0.6087 0.4137 0.4871 0.0432  0.0524  0.0113  308 PHE A CD1 
2145 C CD2 . PHE A 281 ? 0.7076 0.5065 0.5890 0.0562  0.0591  0.0236  308 PHE A CD2 
2146 C CE1 . PHE A 281 ? 0.6079 0.4296 0.4939 0.0418  0.0501  0.0158  308 PHE A CE1 
2147 C CE2 . PHE A 281 ? 0.7194 0.5412 0.6094 0.0569  0.0545  0.0265  308 PHE A CE2 
2148 C CZ  . PHE A 281 ? 0.7047 0.5378 0.5986 0.0479  0.0507  0.0219  308 PHE A CZ  
2149 N N   . MET A 282 ? 0.8261 0.5886 0.6966 0.0686  0.0731  0.0119  309 MET A N   
2150 C CA  . MET A 282 ? 0.9026 0.6707 0.7774 0.0788  0.0769  0.0176  309 MET A CA  
2151 C C   . MET A 282 ? 0.7855 0.5578 0.6583 0.0801  0.0799  0.0131  309 MET A C   
2152 O O   . MET A 282 ? 0.7098 0.4968 0.5911 0.0825  0.0834  0.0157  309 MET A O   
2153 C CB  . MET A 282 ? 0.6871 0.4353 0.5571 0.0872  0.0833  0.0193  309 MET A CB  
2154 C CG  . MET A 282 ? 0.6878 0.4441 0.5626 0.1007  0.0865  0.0235  309 MET A CG  
2155 S SD  . MET A 282 ? 1.0413 0.7737 0.9082 0.1078  0.0950  0.0177  309 MET A SD  
2156 C CE  . MET A 282 ? 0.8657 0.6008 0.7279 0.0991  0.0936  0.0062  309 MET A CE  
2157 N N   . HIS A 283 ? 0.6837 0.4442 0.5444 0.0792  0.0796  0.0048  310 HIS A N   
2158 C CA  . HIS A 283 ? 0.8782 0.6364 0.7278 0.0838  0.0840  0.0022  310 HIS A CA  
2159 C C   . HIS A 283 ? 0.8086 0.5739 0.6564 0.0789  0.0851  0.0058  310 HIS A C   
2160 O O   . HIS A 283 ? 0.8198 0.5820 0.6620 0.0808  0.0949  0.0076  310 HIS A O   
2161 C CB  . HIS A 283 ? 0.7768 0.5239 0.6099 0.0884  0.0808  -0.0095 310 HIS A CB  
2162 C CG  . HIS A 283 ? 0.7274 0.4663 0.5405 0.0984  0.0864  -0.0110 310 HIS A CG  
2163 N ND1 . HIS A 283 ? 0.8382 0.5719 0.6302 0.1033  0.0851  -0.0124 310 HIS A ND1 
2164 C CD2 . HIS A 283 ? 0.7855 0.5174 0.5923 0.1064  0.0951  -0.0106 310 HIS A CD2 
2165 C CE1 . HIS A 283 ? 0.8239 0.5443 0.5941 0.1145  0.0939  -0.0117 310 HIS A CE1 
2166 N NE2 . HIS A 283 ? 1.0068 0.7277 0.7873 0.1154  0.1000  -0.0111 310 HIS A NE2 
2167 N N   . VAL A 284 ? 0.7905 0.5625 0.6423 0.0716  0.0778  0.0061  311 VAL A N   
2168 C CA  . VAL A 284 ? 0.7801 0.5577 0.6323 0.0658  0.0801  0.0089  311 VAL A CA  
2169 C C   . VAL A 284 ? 0.7515 0.5456 0.6234 0.0618  0.0873  0.0122  311 VAL A C   
2170 O O   . VAL A 284 ? 0.8000 0.5933 0.6720 0.0577  0.0984  0.0113  311 VAL A O   
2171 C CB  . VAL A 284 ? 0.7798 0.5645 0.6351 0.0592  0.0702  0.0077  311 VAL A CB  
2172 C CG1 . VAL A 284 ? 0.6032 0.3935 0.4613 0.0523  0.0734  0.0096  311 VAL A CG1 
2173 C CG2 . VAL A 284 ? 0.6206 0.3963 0.4600 0.0634  0.0633  -0.0005 311 VAL A CG2 
2174 N N   . GLN A 285 ? 0.6948 0.5041 0.5830 0.0640  0.0826  0.0142  312 GLN A N   
2175 C CA  . GLN A 285 ? 0.7572 0.5914 0.6666 0.0642  0.0865  0.0132  312 GLN A CA  
2176 C C   . GLN A 285 ? 0.8352 0.6677 0.7466 0.0679  0.0990  0.0103  312 GLN A C   
2177 O O   . GLN A 285 ? 0.8484 0.6990 0.7763 0.0623  0.1086  0.0047  312 GLN A O   
2178 C CB  . GLN A 285 ? 0.7615 0.6084 0.6792 0.0730  0.0778  0.0168  312 GLN A CB  
2179 C CG  . GLN A 285 ? 0.8295 0.6682 0.7384 0.0706  0.0688  0.0210  312 GLN A CG  
2180 C CD  . GLN A 285 ? 0.7873 0.6339 0.6976 0.0817  0.0635  0.0266  312 GLN A CD  
2181 O OE1 . GLN A 285 ? 0.8398 0.6634 0.7367 0.0881  0.0649  0.0319  312 GLN A OE1 
2182 N NE2 . GLN A 285 ? 0.5965 0.4746 0.5212 0.0852  0.0588  0.0241  312 GLN A NE2 
2183 N N   . LEU A 286 ? 0.8768 0.6890 0.7731 0.0762  0.1005  0.0119  313 LEU A N   
2184 C CA  . LEU A 286 ? 0.7947 0.6014 0.6878 0.0802  0.1134  0.0094  313 LEU A CA  
2185 C C   . LEU A 286 ? 0.8041 0.5970 0.6838 0.0731  0.1267  0.0081  313 LEU A C   
2186 O O   . LEU A 286 ? 0.9387 0.7374 0.8269 0.0689  0.1425  0.0046  313 LEU A O   
2187 C CB  . LEU A 286 ? 0.7882 0.5739 0.6642 0.0906  0.1116  0.0095  313 LEU A CB  
2188 C CG  . LEU A 286 ? 0.7544 0.5423 0.6382 0.0994  0.1057  0.0109  313 LEU A CG  
2189 C CD1 . LEU A 286 ? 0.8453 0.6110 0.7133 0.1069  0.1081  0.0073  313 LEU A CD1 
2190 C CD2 . LEU A 286 ? 0.6697 0.4830 0.5748 0.1053  0.1093  0.0105  313 LEU A CD2 
2191 N N   . GLU A 287 ? 0.7755 0.5485 0.6328 0.0724  0.1222  0.0102  314 GLU A N   
2192 C CA  . GLU A 287 ? 0.9810 0.7315 0.8159 0.0703  0.1361  0.0112  314 GLU A CA  
2193 C C   . GLU A 287 ? 0.8969 0.6591 0.7505 0.0552  0.1472  0.0087  314 GLU A C   
2194 O O   . GLU A 287 ? 0.8915 0.6356 0.7343 0.0502  0.1683  0.0081  314 GLU A O   
2195 C CB  . GLU A 287 ? 0.7686 0.4994 0.5747 0.0775  0.1259  0.0123  314 GLU A CB  
2196 C CG  . GLU A 287 ? 0.8467 0.5658 0.6315 0.0925  0.1188  0.0093  314 GLU A CG  
2197 C CD  . GLU A 287 ? 1.2149 0.9130 0.9753 0.1026  0.1349  0.0107  314 GLU A CD  
2198 O OE1 . GLU A 287 ? 1.0774 0.7494 0.8058 0.1090  0.1460  0.0141  314 GLU A OE1 
2199 O OE2 . GLU A 287 ? 1.2286 0.9330 0.9986 0.1054  0.1380  0.0089  314 GLU A OE2 
2200 N N   . VAL A 288 ? 0.8389 0.6294 0.7190 0.0479  0.1352  0.0061  315 VAL A N   
2201 C CA  . VAL A 288 ? 0.8033 0.6132 0.7074 0.0331  0.1445  -0.0011 315 VAL A CA  
2202 C C   . VAL A 288 ? 0.9420 0.7735 0.8714 0.0282  0.1599  -0.0100 315 VAL A C   
2203 O O   . VAL A 288 ? 0.9308 0.7593 0.8678 0.0148  0.1816  -0.0177 315 VAL A O   
2204 C CB  . VAL A 288 ? 0.8101 0.6496 0.7350 0.0301  0.1260  -0.0033 315 VAL A CB  
2205 C CG1 . VAL A 288 ? 0.8448 0.7195 0.8039 0.0175  0.1329  -0.0162 315 VAL A CG1 
2206 C CG2 . VAL A 288 ? 0.6510 0.4711 0.5553 0.0292  0.1173  0.0016  315 VAL A CG2 
2207 N N   . MET A 289 ? 0.8257 0.6782 0.7686 0.0388  0.1510  -0.0106 316 MET A N   
2208 C CA  . MET A 289 ? 0.9222 0.8037 0.8931 0.0370  0.1627  -0.0216 316 MET A CA  
2209 C C   . MET A 289 ? 0.8701 0.7252 0.8253 0.0351  0.1867  -0.0215 316 MET A C   
2210 O O   . MET A 289 ? 0.8350 0.7137 0.8137 0.0331  0.1989  -0.0319 316 MET A O   
2211 C CB  . MET A 289 ? 0.7411 0.6477 0.7247 0.0537  0.1460  -0.0208 316 MET A CB  
2212 C CG  . MET A 289 ? 0.9427 0.8750 0.9386 0.0588  0.1255  -0.0206 316 MET A CG  
2213 S SD  . MET A 289 ? 0.9836 0.9349 0.9849 0.0832  0.1107  -0.0177 316 MET A SD  
2214 C CE  . MET A 289 ? 1.0833 0.9861 1.0522 0.0906  0.1151  -0.0058 316 MET A CE  
2215 N N   . VAL A 290 ? 0.8833 0.6918 0.7982 0.0378  0.1939  -0.0112 317 VAL A N   
2216 C CA  . VAL A 290 ? 0.8309 0.6091 0.7231 0.0385  0.2189  -0.0099 317 VAL A CA  
2217 C C   . VAL A 290 ? 0.9676 0.7437 0.8731 0.0182  0.2485  -0.0196 317 VAL A C   
2218 O O   . VAL A 290 ? 1.1316 0.9167 1.0525 0.0113  0.2706  -0.0287 317 VAL A O   
2219 C CB  . VAL A 290 ? 0.9368 0.6670 0.7769 0.0524  0.2166  0.0027  317 VAL A CB  
2220 C CG1 . VAL A 290 ? 1.0181 0.7113 0.8262 0.0559  0.2448  0.0057  317 VAL A CG1 
2221 C CG2 . VAL A 290 ? 0.9370 0.6727 0.7703 0.0688  0.1914  0.0066  317 VAL A CG2 
2222 N N   . LYS A 291 ? 1.0512 0.8152 0.9523 0.0072  0.2513  -0.0198 318 LYS A N   
2223 C CA  . LYS A 291 ? 0.9815 0.7361 0.8931 -0.0146 0.2829  -0.0304 318 LYS A CA  
2224 C C   . LYS A 291 ? 0.9490 0.7421 0.9006 -0.0312 0.2748  -0.0445 318 LYS A C   
2225 O O   . LYS A 291 ? 1.1258 0.9064 1.0841 -0.0511 0.2997  -0.0544 318 LYS A O   
2226 C CB  . LYS A 291 ? 0.9938 0.6795 0.8492 -0.0113 0.3044  -0.0172 318 LYS A CB  
2227 C CG  . LYS A 291 ? 1.2200 0.8665 1.0297 0.0082  0.3132  -0.0045 318 LYS A CG  
2228 C CD  . LYS A 291 ? 1.4576 1.0354 1.2038 0.0188  0.3312  0.0094  318 LYS A CD  
2229 C CE  . LYS A 291 ? 1.4871 1.0310 1.1838 0.0440  0.3339  0.0212  318 LYS A CE  
2230 N NZ  . LYS A 291 ? 1.3899 0.9374 1.0985 0.0367  0.3600  0.0155  318 LYS A NZ  
2231 N N   . HIS A 292 ? 0.8704 0.7068 0.8460 -0.0231 0.2428  -0.0462 319 HIS A N   
2232 C CA  . HIS A 292 ? 0.8335 0.7130 0.8463 -0.0345 0.2317  -0.0605 319 HIS A CA  
2233 C C   . HIS A 292 ? 0.8795 0.8196 0.9299 -0.0245 0.2106  -0.0703 319 HIS A C   
2234 O O   . HIS A 292 ? 0.8050 0.7443 0.8454 -0.0069 0.1999  -0.0610 319 HIS A O   
2235 C CB  . HIS A 292 ? 0.9128 0.7752 0.9036 -0.0294 0.2113  -0.0490 319 HIS A CB  
2236 C CG  . HIS A 292 ? 0.9473 0.7470 0.8898 -0.0276 0.2242  -0.0348 319 HIS A CG  
2237 N ND1 . HIS A 292 ? 1.2259 0.9894 1.1270 -0.0088 0.2187  -0.0182 319 HIS A ND1 
2238 C CD2 . HIS A 292 ? 0.9496 0.7169 0.8765 -0.0394 0.2416  -0.0360 319 HIS A CD2 
2239 C CE1 . HIS A 292 ? 1.2116 0.9256 1.0720 -0.0062 0.2306  -0.0097 319 HIS A CE1 
2240 N NE2 . HIS A 292 ? 1.1544 0.8661 1.0277 -0.0243 0.2456  -0.0188 319 HIS A NE2 
2241 N N   . PRO A 293 ? 0.7794 0.7720 0.8712 -0.0332 0.2043  -0.0903 320 PRO A N   
2242 C CA  . PRO A 293 ? 0.7468 0.7947 0.8647 -0.0159 0.1788  -0.0971 320 PRO A CA  
2243 C C   . PRO A 293 ? 0.7836 0.8133 0.8712 0.0039  0.1511  -0.0752 320 PRO A C   
2244 O O   . PRO A 293 ? 0.8841 0.8734 0.9419 0.0005  0.1489  -0.0612 320 PRO A O   
2245 C CB  . PRO A 293 ? 0.6604 0.7640 0.8222 -0.0294 0.1778  -0.1242 320 PRO A CB  
2246 C CG  . PRO A 293 ? 0.6869 0.7700 0.8577 -0.0585 0.2122  -0.1376 320 PRO A CG  
2247 C CD  . PRO A 293 ? 0.7200 0.7251 0.8371 -0.0583 0.2231  -0.1107 320 PRO A CD  
2248 N N   . PRO A 294 ? 0.7882 0.8447 0.8810 0.0255  0.1315  -0.0726 321 PRO A N   
2249 C CA  . PRO A 294 ? 0.8735 0.9069 0.9365 0.0421  0.1104  -0.0526 321 PRO A CA  
2250 C C   . PRO A 294 ? 0.8760 0.9185 0.9390 0.0373  0.0981  -0.0532 321 PRO A C   
2251 O O   . PRO A 294 ? 0.9042 0.9911 0.9963 0.0322  0.0953  -0.0713 321 PRO A O   
2252 C CB  . PRO A 294 ? 0.6901 0.7515 0.7605 0.0665  0.0973  -0.0529 321 PRO A CB  
2253 C CG  . PRO A 294 ? 0.8615 0.9811 0.9743 0.0638  0.1030  -0.0785 321 PRO A CG  
2254 C CD  . PRO A 294 ? 0.6944 0.8008 0.8184 0.0372  0.1295  -0.0884 321 PRO A CD  
2255 N N   . ALA A 295 ? 0.7551 0.7581 0.7867 0.0387  0.0909  -0.0359 322 ALA A N   
2256 C CA  . ALA A 295 ? 0.6579 0.6656 0.6855 0.0355  0.0790  -0.0345 322 ALA A CA  
2257 C C   . ALA A 295 ? 0.8359 0.8724 0.8660 0.0553  0.0606  -0.0330 322 ALA A C   
2258 O O   . ALA A 295 ? 0.6829 0.6974 0.6908 0.0707  0.0538  -0.0182 322 ALA A O   
2259 C CB  . ALA A 295 ? 0.5651 0.5257 0.5603 0.0322  0.0778  -0.0191 322 ALA A CB  
2260 N N   . GLU A 296 ? 0.6248 0.7090 0.6799 0.0561  0.0539  -0.0494 323 GLU A N   
2261 C CA  . GLU A 296 ? 0.7194 0.8342 0.7729 0.0806  0.0365  -0.0493 323 GLU A CA  
2262 C C   . GLU A 296 ? 0.7318 0.8213 0.7556 0.0864  0.0258  -0.0331 323 GLU A C   
2263 O O   . GLU A 296 ? 0.6531 0.7233 0.6710 0.0689  0.0287  -0.0308 323 GLU A O   
2264 C CB  . GLU A 296 ? 0.6572 0.8379 0.7477 0.0814  0.0310  -0.0762 323 GLU A CB  
2265 C CG  . GLU A 296 ? 0.8657 1.0789 0.9922 0.0730  0.0442  -0.0975 323 GLU A CG  
2266 C CD  . GLU A 296 ? 1.1081 1.3243 1.2296 0.0964  0.0418  -0.0918 323 GLU A CD  
2267 O OE1 . GLU A 296 ? 1.1301 1.3382 1.2254 0.1241  0.0271  -0.0770 323 GLU A OE1 
2268 O OE2 . GLU A 296 ? 1.0234 1.2470 1.1652 0.0874  0.0567  -0.1021 323 GLU A OE2 
2269 N N   . PRO A 297 ? 0.8816 0.9679 0.8839 0.1117  0.0155  -0.0218 324 PRO A N   
2270 C CA  . PRO A 297 ? 0.8286 0.8892 0.8013 0.1169  0.0092  -0.0069 324 PRO A CA  
2271 C C   . PRO A 297 ? 0.8096 0.9119 0.7907 0.1221  -0.0029 -0.0186 324 PRO A C   
2272 O O   . PRO A 297 ? 0.7972 0.9513 0.8092 0.1223  -0.0074 -0.0403 324 PRO A O   
2273 C CB  . PRO A 297 ? 0.8311 0.8658 0.7743 0.1431  0.0082  0.0095  324 PRO A CB  
2274 C CG  . PRO A 297 ? 0.6267 0.7024 0.5887 0.1621  0.0037  -0.0029 324 PRO A CG  
2275 C CD  . PRO A 297 ? 0.5992 0.6981 0.5987 0.1381  0.0119  -0.0206 324 PRO A CD  
2276 N N   . SER A 298 ? 0.8584 0.9394 0.8129 0.1256  -0.0071 -0.0063 325 SER A N   
2277 C CA  . SER A 298 ? 0.7138 0.8315 0.6695 0.1347  -0.0194 -0.0156 325 SER A CA  
2278 C C   . SER A 298 ? 0.7692 0.9214 0.7175 0.1703  -0.0313 -0.0195 325 SER A C   
2279 O O   . SER A 298 ? 0.9066 1.0325 0.8298 0.1922  -0.0290 -0.0044 325 SER A O   
2280 C CB  . SER A 298 ? 0.8233 0.9056 0.7479 0.1319  -0.0188 0.0001  325 SER A CB  
2281 O OG  . SER A 298 ? 0.7869 0.9013 0.7040 0.1471  -0.0310 -0.0061 325 SER A OG  
2282 N N   . ARG A 299 ? 0.8086 1.0207 0.7781 0.1781  -0.0441 -0.0417 326 ARG A N   
2283 C CA  . ARG A 299 ? 0.8774 1.1312 0.8384 0.2174  -0.0589 -0.0491 326 ARG A CA  
2284 C C   . ARG A 299 ? 0.9112 1.1380 0.8194 0.2470  -0.0652 -0.0283 326 ARG A C   
2285 O O   . ARG A 299 ? 1.0162 1.2701 0.9051 0.2868  -0.0777 -0.0308 326 ARG A O   
2286 C CB  . ARG A 299 ? 0.9624 1.2977 0.9681 0.2158  -0.0710 -0.0857 326 ARG A CB  
2287 C CG  . ARG A 299 ? 0.8975 1.2493 0.9087 0.2005  -0.0762 -0.0961 326 ARG A CG  
2288 C CD  . ARG A 299 ? 0.9962 1.4292 1.0591 0.1934  -0.0847 -0.1376 326 ARG A CD  
2289 N NE  . ARG A 299 ? 1.2385 1.6946 1.3020 0.1881  -0.0934 -0.1496 326 ARG A NE  
2290 C CZ  . ARG A 299 ? 1.3285 1.8249 1.3741 0.2216  -0.1129 -0.1578 326 ARG A CZ  
2291 N NH1 . ARG A 299 ? 1.2562 1.7731 1.2787 0.2657  -0.1260 -0.1544 326 ARG A NH1 
2292 N NH2 . ARG A 299 ? 1.3913 1.9068 1.4390 0.2134  -0.1193 -0.1697 326 ARG A NH2 
2293 N N   . PHE A 300 ? 0.8859 1.0601 0.7684 0.2305  -0.0556 -0.0089 327 PHE A N   
2294 C CA  . PHE A 300 ? 0.9883 1.1253 0.8173 0.2543  -0.0548 0.0130  327 PHE A CA  
2295 C C   . PHE A 300 ? 0.9858 1.0472 0.7784 0.2551  -0.0366 0.0409  327 PHE A C   
2296 O O   . PHE A 300 ? 1.1440 1.1651 0.8876 0.2766  -0.0303 0.0607  327 PHE A O   
2297 C CB  . PHE A 300 ? 0.9318 1.0681 0.7582 0.2354  -0.0556 0.0113  327 PHE A CB  
2298 C CG  . PHE A 300 ? 1.0444 1.2477 0.9146 0.2222  -0.0687 -0.0190 327 PHE A CG  
2299 C CD1 . PHE A 300 ? 0.9229 1.1865 0.7954 0.2509  -0.0870 -0.0376 327 PHE A CD1 
2300 C CD2 . PHE A 300 ? 1.0085 1.2136 0.9161 0.1823  -0.0619 -0.0307 327 PHE A CD2 
2301 C CE1 . PHE A 300 ? 0.8320 1.1591 0.7490 0.2358  -0.0971 -0.0700 327 PHE A CE1 
2302 C CE2 . PHE A 300 ? 1.0450 1.3049 0.9921 0.1679  -0.0696 -0.0595 327 PHE A CE2 
2303 C CZ  . PHE A 300 ? 1.0331 1.3553 0.9877 0.1925  -0.0867 -0.0806 327 PHE A CZ  
2304 N N   . ILE A 301 ? 0.9103 0.9501 0.7243 0.2323  -0.0260 0.0419  328 ILE A N   
2305 C CA  . ILE A 301 ? 0.9104 0.8842 0.6971 0.2307  -0.0085 0.0628  328 ILE A CA  
2306 C C   . ILE A 301 ? 1.1498 1.1293 0.9472 0.2440  -0.0082 0.0601  328 ILE A C   
2307 O O   . ILE A 301 ? 1.1941 1.2200 1.0327 0.2349  -0.0156 0.0411  328 ILE A O   
2308 C CB  . ILE A 301 ? 1.0615 1.0028 0.8617 0.1913  0.0039  0.0647  328 ILE A CB  
2309 C CG1 . ILE A 301 ? 1.0687 1.0202 0.8710 0.1750  0.0006  0.0608  328 ILE A CG1 
2310 C CG2 . ILE A 301 ? 1.2899 1.1651 1.0599 0.1898  0.0229  0.0828  328 ILE A CG2 
2311 C CD1 . ILE A 301 ? 0.8826 0.8161 0.7039 0.1395  0.0086  0.0572  328 ILE A CD1 
2312 N N   . SER A 302 ? 1.2850 1.2149 1.0451 0.2648  0.0029  0.0783  329 SER A N   
2313 C CA  . SER A 302 ? 1.2572 1.1818 1.0229 0.2770  0.0061  0.0781  329 SER A CA  
2314 C C   . SER A 302 ? 1.4024 1.2656 1.1608 0.2540  0.0259  0.0893  329 SER A C   
2315 O O   . SER A 302 ? 1.4367 1.2452 1.1618 0.2507  0.0407  0.1046  329 SER A O   
2316 C CB  . SER A 302 ? 1.3504 1.2689 1.0767 0.3259  0.0022  0.0877  329 SER A CB  
2317 O OG  . SER A 302 ? 1.4955 1.3476 1.1660 0.3395  0.0173  0.1113  329 SER A OG  
2318 N N   . ALA A 303 ? 1.4087 1.2826 1.1988 0.2377  0.0274  0.0795  330 ALA A N   
2319 C CA  . ALA A 303 ? 1.3846 1.2074 1.1689 0.2206  0.0440  0.0864  330 ALA A CA  
2320 C C   . ALA A 303 ? 1.5118 1.2917 1.2611 0.2496  0.0544  0.0999  330 ALA A C   
2321 O O   . ALA A 303 ? 1.3698 1.1712 1.1089 0.2835  0.0457  0.1006  330 ALA A O   
2322 C CB  . ALA A 303 ? 1.1834 1.0303 1.0067 0.1989  0.0424  0.0721  330 ALA A CB  
2323 N N   . PRO A 304 ? 1.6197 1.3393 1.3496 0.2381  0.0737  0.1090  331 PRO A N   
2324 C CA  . PRO A 304 ? 1.7180 1.3875 1.4112 0.2646  0.0876  0.1221  331 PRO A CA  
2325 C C   . PRO A 304 ? 1.6275 1.3150 1.3391 0.2757  0.0833  0.1146  331 PRO A C   
2326 O O   . PRO A 304 ? 1.5189 1.2348 1.2682 0.2528  0.0786  0.1009  331 PRO A O   
2327 C CB  . PRO A 304 ? 1.7414 1.3469 1.4194 0.2396  0.1116  0.1273  331 PRO A CB  
2328 C CG  . PRO A 304 ? 1.7083 1.3429 1.4274 0.2014  0.1058  0.1115  331 PRO A CG  
2329 C CD  . PRO A 304 ? 1.6217 1.3167 1.3622 0.2014  0.0847  0.1052  331 PRO A CD  
2330 N N   . THR A 305 ? 1.6417 1.3103 1.3225 0.3139  0.0858  0.1242  332 THR A N   
2331 C CA  . THR A 305 ? 1.6549 1.3394 1.3498 0.3292  0.0825  0.1173  332 THR A CA  
2332 C C   . THR A 305 ? 1.5981 1.2406 1.3006 0.3038  0.0995  0.1150  332 THR A C   
2333 O O   . THR A 305 ? 1.6268 1.2114 1.3083 0.2879  0.1183  0.1223  332 THR A O   
2334 C CB  . THR A 305 ? 1.7634 1.4282 1.4161 0.3796  0.0831  0.1292  332 THR A CB  
2335 O OG1 . THR A 305 ? 1.7976 1.4993 1.4371 0.4056  0.0671  0.1307  332 THR A OG1 
2336 C CG2 . THR A 305 ? 1.7453 1.4431 1.4185 0.3988  0.0754  0.1184  332 THR A CG2 
2337 N N   . LYS A 306 ? 1.4139 1.0887 1.1480 0.2994  0.0936  0.1022  333 LYS A N   
2338 C CA  . LYS A 306 ? 1.4386 1.0839 1.1824 0.2780  0.1064  0.0967  333 LYS A CA  
2339 C C   . LYS A 306 ? 1.3711 0.9958 1.1002 0.3062  0.1129  0.0992  333 LYS A C   
2340 O O   . LYS A 306 ? 1.3331 0.9953 1.0660 0.3359  0.1012  0.0972  333 LYS A O   
2341 C CB  . LYS A 306 ? 1.3775 1.0703 1.1648 0.2497  0.0974  0.0804  333 LYS A CB  
2342 C CG  . LYS A 306 ? 1.2252 0.9614 1.0318 0.2353  0.0844  0.0759  333 LYS A CG  
2343 C CD  . LYS A 306 ? 1.1898 0.9490 1.0271 0.2038  0.0823  0.0633  333 LYS A CD  
2344 C CE  . LYS A 306 ? 1.2634 0.9815 1.0919 0.1797  0.0925  0.0634  333 LYS A CE  
2345 N NZ  . LYS A 306 ? 1.1370 0.8778 0.9876 0.1544  0.0881  0.0527  333 LYS A NZ  
2346 N N   . THR A 307 ? 1.3675 0.9352 1.0816 0.2969  0.1317  0.1010  334 THR A N   
2347 C CA  . THR A 307 ? 1.4692 1.0069 1.1657 0.3224  0.1411  0.1036  334 THR A CA  
2348 C C   . THR A 307 ? 1.2835 0.8385 1.0112 0.3039  0.1413  0.0881  334 THR A C   
2349 O O   . THR A 307 ? 1.2157 0.7413 0.9478 0.2758  0.1529  0.0812  334 THR A O   
2350 C CB  . THR A 307 ? 1.5195 0.9719 1.1711 0.3282  0.1664  0.1164  334 THR A CB  
2351 O OG1 . THR A 307 ? 1.7509 1.1751 1.4139 0.2876  0.1802  0.1076  334 THR A OG1 
2352 C CG2 . THR A 307 ? 1.4720 0.9013 1.0844 0.3509  0.1687  0.1342  334 THR A CG2 
2353 N N   . PRO A 308 ? 1.2376 0.8418 0.9876 0.3187  0.1296  0.0800  335 PRO A N   
2354 C CA  . PRO A 308 ? 1.1830 0.8024 0.9590 0.3021  0.1315  0.0660  335 PRO A CA  
2355 C C   . PRO A 308 ? 1.1810 0.7485 0.9367 0.3131  0.1474  0.0665  335 PRO A C   
2356 O O   . PRO A 308 ? 1.3087 0.8389 1.0329 0.3428  0.1550  0.0773  335 PRO A O   
2357 C CB  . PRO A 308 ? 1.3045 0.9928 1.1094 0.3165  0.1170  0.0570  335 PRO A CB  
2358 C CG  . PRO A 308 ? 1.2935 1.0118 1.0946 0.3340  0.1042  0.0626  335 PRO A CG  
2359 C CD  . PRO A 308 ? 1.2606 0.9166 1.0166 0.3495  0.1135  0.0800  335 PRO A CD  
2360 N N   . ASP A 309 ? 1.2830 0.8466 1.0542 0.2907  0.1530  0.0541  336 ASP A N   
2361 C CA  . ASP A 309 ? 1.2358 0.7552 0.9929 0.2974  0.1679  0.0501  336 ASP A CA  
2362 C C   . ASP A 309 ? 1.2518 0.8055 1.0350 0.2876  0.1642  0.0349  336 ASP A C   
2363 O O   . ASP A 309 ? 1.1677 0.7743 0.9762 0.2784  0.1526  0.0297  336 ASP A O   
2364 C CB  . ASP A 309 ? 1.0395 0.4965 0.7776 0.2773  0.1857  0.0492  336 ASP A CB  
2365 C CG  . ASP A 309 ? 1.2944 0.7671 1.0549 0.2403  0.1832  0.0341  336 ASP A CG  
2366 O OD1 . ASP A 309 ? 1.4660 0.9904 1.2505 0.2310  0.1687  0.0281  336 ASP A OD1 
2367 O OD2 . ASP A 309 ? 1.3128 0.7445 1.0655 0.2212  0.1973  0.0268  336 ASP A OD2 
2368 N N   . LYS A 310 ? 1.2679 0.7877 1.0427 0.2895  0.1765  0.0274  337 LYS A N   
2369 C CA  . LYS A 310 ? 1.2887 0.8327 1.0814 0.2827  0.1757  0.0131  337 LYS A CA  
2370 C C   . LYS A 310 ? 1.1948 0.7201 0.9895 0.2543  0.1813  -0.0009 337 LYS A C   
2371 O O   . LYS A 310 ? 1.1753 0.7116 0.9773 0.2508  0.1825  -0.0134 337 LYS A O   
2372 C CB  . LYS A 310 ? 1.2616 0.7902 1.0450 0.3099  0.1833  0.0116  337 LYS A CB  
2373 C CG  . LYS A 310 ? 1.1973 0.7575 0.9826 0.3427  0.1751  0.0200  337 LYS A CG  
2374 C CD  . LYS A 310 ? 1.2766 0.9075 1.0954 0.3380  0.1637  0.0117  337 LYS A CD  
2375 C CE  . LYS A 310 ? 1.3274 1.0002 1.1548 0.3699  0.1547  0.0136  337 LYS A CE  
2376 N NZ  . LYS A 310 ? 1.3190 0.9709 1.1307 0.4033  0.1611  0.0132  337 LYS A NZ  
2377 N N   . MET A 311 ? 1.2620 0.7621 1.0502 0.2356  0.1848  -0.0009 338 MET A N   
2378 C CA  . MET A 311 ? 1.1469 0.6376 0.9404 0.2093  0.1882  -0.0185 338 MET A CA  
2379 C C   . MET A 311 ? 1.2103 0.6654 0.9966 0.2100  0.2023  -0.0339 338 MET A C   
2380 O O   . MET A 311 ? 1.3195 0.7828 1.1139 0.1949  0.2015  -0.0538 338 MET A O   
2381 C CB  . MET A 311 ? 1.0905 0.6295 0.9006 0.1975  0.1744  -0.0262 338 MET A CB  
2382 C CG  . MET A 311 ? 1.1414 0.7121 0.9600 0.1910  0.1624  -0.0152 338 MET A CG  
2383 S SD  . MET A 311 ? 1.0602 0.6756 0.8904 0.1814  0.1518  -0.0225 338 MET A SD  
2384 C CE  . MET A 311 ? 1.1964 0.8305 1.0311 0.2015  0.1556  -0.0204 338 MET A CE  
2385 N N   . GLY A 312 ? 1.2347 0.6497 1.0037 0.2296  0.2153  -0.0261 339 GLY A N   
2386 C CA  . GLY A 312 ? 1.0942 0.4710 0.8552 0.2317  0.2308  -0.0406 339 GLY A CA  
2387 C C   . GLY A 312 ? 1.0871 0.4885 0.8538 0.2478  0.2260  -0.0466 339 GLY A C   
2388 O O   . GLY A 312 ? 1.3900 0.7578 1.1472 0.2562  0.2391  -0.0558 339 GLY A O   
2389 N N   . PHE A 313 ? 1.2026 0.6589 0.9840 0.2514  0.2101  -0.0427 340 PHE A N   
2390 C CA  . PHE A 313 ? 1.2144 0.6949 1.0011 0.2670  0.2084  -0.0475 340 PHE A CA  
2391 C C   . PHE A 313 ? 1.3691 0.8361 1.1462 0.2978  0.2136  -0.0357 340 PHE A C   
2392 O O   . PHE A 313 ? 1.4748 0.9281 1.2419 0.3107  0.2135  -0.0202 340 PHE A O   
2393 C CB  . PHE A 313 ? 0.9894 0.5269 0.7927 0.2623  0.1952  -0.0451 340 PHE A CB  
2394 C CG  . PHE A 313 ? 1.0767 0.6277 0.8832 0.2392  0.1896  -0.0565 340 PHE A CG  
2395 C CD1 . PHE A 313 ? 1.1109 0.6639 0.9135 0.2362  0.1919  -0.0738 340 PHE A CD1 
2396 C CD2 . PHE A 313 ? 1.1101 0.6734 0.9214 0.2236  0.1812  -0.0507 340 PHE A CD2 
2397 C CE1 . PHE A 313 ? 1.0505 0.6177 0.8513 0.2209  0.1850  -0.0851 340 PHE A CE1 
2398 C CE2 . PHE A 313 ? 1.1623 0.7389 0.9739 0.2069  0.1750  -0.0618 340 PHE A CE2 
2399 C CZ  . PHE A 313 ? 0.9493 0.5282 0.7545 0.2070  0.1764  -0.0791 340 PHE A CZ  
2400 N N   . ASP A 314 ? 1.1932 0.6652 0.9712 0.3126  0.2179  -0.0439 341 ASP A N   
2401 C CA  . ASP A 314 ? 1.2564 0.7228 1.0267 0.3458  0.2213  -0.0353 341 ASP A CA  
2402 C C   . ASP A 314 ? 1.2805 0.8054 1.0685 0.3594  0.2079  -0.0260 341 ASP A C   
2403 O O   . ASP A 314 ? 1.3921 0.9183 1.1732 0.3883  0.2059  -0.0164 341 ASP A O   
2404 C CB  . ASP A 314 ? 1.3874 0.8450 1.1555 0.3571  0.2300  -0.0489 341 ASP A CB  
2405 C CG  . ASP A 314 ? 1.3996 0.7999 1.1523 0.3444  0.2446  -0.0623 341 ASP A CG  
2406 O OD1 . ASP A 314 ? 1.4934 0.8624 1.2394 0.3251  0.2491  -0.0621 341 ASP A OD1 
2407 O OD2 . ASP A 314 ? 1.6320 1.0202 1.3812 0.3525  0.2527  -0.0753 341 ASP A OD2 
2408 N N   . GLU A 315 ? 1.2644 0.8374 1.0741 0.3403  0.1995  -0.0305 342 GLU A N   
2409 C CA  . GLU A 315 ? 1.2951 0.9256 1.1268 0.3464  0.1895  -0.0261 342 GLU A CA  
2410 C C   . GLU A 315 ? 1.2153 0.8756 1.0617 0.3171  0.1850  -0.0293 342 GLU A C   
2411 O O   . GLU A 315 ? 1.2349 0.8838 1.0760 0.3004  0.1893  -0.0376 342 GLU A O   
2412 C CB  . GLU A 315 ? 1.2964 0.9625 1.1425 0.3689  0.1919  -0.0338 342 GLU A CB  
2413 C CG  . GLU A 315 ? 1.3038 1.0348 1.1783 0.3756  0.1832  -0.0349 342 GLU A CG  
2414 C CD  . GLU A 315 ? 1.3856 1.1196 1.2542 0.3964  0.1728  -0.0243 342 GLU A CD  
2415 O OE1 . GLU A 315 ? 1.4442 1.1777 1.3050 0.4310  0.1716  -0.0236 342 GLU A OE1 
2416 O OE2 . GLU A 315 ? 1.3551 1.0912 1.2240 0.3806  0.1657  -0.0168 342 GLU A OE2 
2417 N N   . VAL A 316 ? 1.0656 0.7629 0.9280 0.3134  0.1762  -0.0236 343 VAL A N   
2418 C CA  . VAL A 316 ? 1.1006 0.8258 0.9762 0.2884  0.1736  -0.0255 343 VAL A CA  
2419 C C   . VAL A 316 ? 1.1032 0.8850 1.0070 0.2930  0.1742  -0.0312 343 VAL A C   
2420 O O   . VAL A 316 ? 1.2287 1.0400 1.1468 0.3060  0.1665  -0.0294 343 VAL A O   
2421 C CB  . VAL A 316 ? 1.0265 0.7421 0.8974 0.2742  0.1649  -0.0163 343 VAL A CB  
2422 C CG1 . VAL A 316 ? 0.9575 0.6966 0.8385 0.2501  0.1634  -0.0184 343 VAL A CG1 
2423 C CG2 . VAL A 316 ? 1.1724 0.8342 1.0198 0.2687  0.1674  -0.0141 343 VAL A CG2 
2424 N N   . PHE A 317 ? 1.0235 0.8213 0.9348 0.2829  0.1845  -0.0400 344 PHE A N   
2425 C CA  . PHE A 317 ? 1.1426 0.9925 1.0832 0.2825  0.1912  -0.0494 344 PHE A CA  
2426 C C   . PHE A 317 ? 1.0309 0.8986 0.9816 0.2567  0.1942  -0.0491 344 PHE A C   
2427 O O   . PHE A 317 ? 1.0775 0.9153 1.0076 0.2405  0.1946  -0.0430 344 PHE A O   
2428 C CB  . PHE A 317 ? 1.0699 0.9230 1.0107 0.2875  0.2061  -0.0595 344 PHE A CB  
2429 C CG  . PHE A 317 ? 1.0253 0.8627 0.9578 0.3140  0.2050  -0.0617 344 PHE A CG  
2430 C CD1 . PHE A 317 ? 1.1323 1.0073 1.0865 0.3374  0.2033  -0.0691 344 PHE A CD1 
2431 C CD2 . PHE A 317 ? 1.1231 0.9096 1.0264 0.3165  0.2062  -0.0590 344 PHE A CD2 
2432 C CE1 . PHE A 317 ? 1.1821 1.0383 1.1246 0.3649  0.2031  -0.0705 344 PHE A CE1 
2433 C CE2 . PHE A 317 ? 1.3138 1.0802 1.2077 0.3403  0.2078  -0.0617 344 PHE A CE2 
2434 C CZ  . PHE A 317 ? 1.2970 1.0955 1.2085 0.3655  0.2065  -0.0658 344 PHE A CZ  
2435 N N   . MET A 318 ? 1.1141 1.0324 1.0975 0.2539  0.1971  -0.0582 345 MET A N   
2436 C CA  . MET A 318 ? 1.1028 1.0393 1.0994 0.2289  0.2041  -0.0607 345 MET A CA  
2437 C C   . MET A 318 ? 1.0632 1.0470 1.0933 0.2236  0.2218  -0.0783 345 MET A C   
2438 O O   . MET A 318 ? 1.0906 1.1246 1.1538 0.2357  0.2168  -0.0913 345 MET A O   
2439 C CB  . MET A 318 ? 1.2394 1.1914 1.2463 0.2261  0.1879  -0.0563 345 MET A CB  
2440 C CG  . MET A 318 ? 1.1382 1.0661 1.1304 0.2024  0.1880  -0.0476 345 MET A CG  
2441 S SD  . MET A 318 ? 1.3467 1.3021 1.3614 0.1754  0.2085  -0.0587 345 MET A SD  
2442 C CE  . MET A 318 ? 1.1941 1.2188 1.2571 0.1798  0.1995  -0.0749 345 MET A CE  
2443 N N   . ILE A 319 ? 1.0796 1.0478 1.0997 0.2071  0.2435  -0.0803 346 ILE A N   
2444 C CA  . ILE A 319 ? 1.0846 1.0902 1.1339 0.1973  0.2674  -0.0978 346 ILE A CA  
2445 C C   . ILE A 319 ? 1.1008 1.1322 1.1751 0.1725  0.2763  -0.1054 346 ILE A C   
2446 O O   . ILE A 319 ? 1.1062 1.1017 1.1564 0.1551  0.2821  -0.0944 346 ILE A O   
2447 C CB  . ILE A 319 ? 0.9702 0.9400 0.9906 0.1920  0.2907  -0.0951 346 ILE A CB  
2448 C CG1 . ILE A 319 ? 1.0887 1.0301 1.0828 0.2153  0.2805  -0.0890 346 ILE A CG1 
2449 C CG2 . ILE A 319 ? 0.8987 0.9052 0.9497 0.1811  0.3196  -0.1141 346 ILE A CG2 
2450 C CD1 . ILE A 319 ? 1.0497 0.9581 1.0123 0.2140  0.3010  -0.0877 346 ILE A CD1 
2451 N N   . ASN A 320 ? 1.0451 1.1401 1.1680 0.1721  0.2775  -0.1265 347 ASN A N   
2452 C CA  . ASN A 320 ? 1.0235 1.1504 1.1775 0.1476  0.2864  -0.1395 347 ASN A CA  
2453 C C   . ASN A 320 ? 1.0964 1.2906 1.3045 0.1404  0.3053  -0.1710 347 ASN A C   
2454 O O   . ASN A 320 ? 1.0158 1.2605 1.2522 0.1635  0.2917  -0.1856 347 ASN A O   
2455 C CB  . ASN A 320 ? 0.9752 1.1197 1.1368 0.1553  0.2571  -0.1354 347 ASN A CB  
2456 C CG  . ASN A 320 ? 1.0529 1.2430 1.2547 0.1326  0.2644  -0.1550 347 ASN A CG  
2457 O OD1 . ASN A 320 ? 1.0655 1.3210 1.3088 0.1423  0.2522  -0.1759 347 ASN A OD1 
2458 N ND2 . ASN A 320 ? 1.0579 1.2140 1.2465 0.1039  0.2848  -0.1499 347 ASN A ND2 
2459 N N   . LEU A 321 ? 1.1497 1.3436 1.3711 0.1092  0.3382  -0.1826 348 LEU A N   
2460 C CA  . LEU A 321 ? 1.0642 1.3262 1.3444 0.0948  0.3605  -0.2178 348 LEU A CA  
2461 C C   . LEU A 321 ? 1.0502 1.3841 1.3795 0.0978  0.3384  -0.2400 348 LEU A C   
2462 O O   . LEU A 321 ? 0.9812 1.3023 1.3011 0.0914  0.3233  -0.2303 348 LEU A O   
2463 C CB  . LEU A 321 ? 1.1485 1.3828 1.4270 0.0572  0.4049  -0.2240 348 LEU A CB  
2464 C CG  . LEU A 321 ? 1.2305 1.3971 1.4588 0.0552  0.4321  -0.2055 348 LEU A CG  
2465 C CD1 . LEU A 321 ? 1.3862 1.4984 1.5881 0.0240  0.4688  -0.1986 348 LEU A CD1 
2466 C CD2 . LEU A 321 ? 1.2288 1.4328 1.4850 0.0600  0.4525  -0.2267 348 LEU A CD2 
2467 N N   . ARG A 322 ? 1.0715 1.4848 1.4533 0.1098  0.3360  -0.2718 349 ARG A N   
2468 C CA  . ARG A 322 ? 1.1054 1.5963 1.5335 0.1201  0.3116  -0.2965 349 ARG A CA  
2469 C C   . ARG A 322 ? 1.1564 1.6694 1.6174 0.0823  0.3289  -0.3166 349 ARG A C   
2470 O O   . ARG A 322 ? 1.1733 1.7270 1.6545 0.0881  0.3049  -0.3268 349 ARG A O   
2471 C CB  . ARG A 322 ? 1.1505 1.7277 1.6299 0.1418  0.3079  -0.3314 349 ARG A CB  
2472 C CG  . ARG A 322 ? 1.1839 1.8458 1.7040 0.1655  0.2759  -0.3570 349 ARG A CG  
2473 C CD  . ARG A 322 ? 1.2861 2.0421 1.8644 0.1823  0.2783  -0.3991 349 ARG A CD  
2474 N NE  . ARG A 322 ? 1.4531 2.2379 2.0784 0.1401  0.3223  -0.4310 349 ARG A NE  
2475 C CZ  . ARG A 322 ? 1.5027 2.3523 2.1822 0.1135  0.3286  -0.4680 349 ARG A CZ  
2476 N NH1 . ARG A 322 ? 1.4826 2.3924 2.1862 0.1284  0.2950  -0.4857 349 ARG A NH1 
2477 N NH2 . ARG A 322 ? 1.2468 2.0902 1.9479 0.0704  0.3666  -0.4843 349 ARG A NH2 
2478 N N   . ARG A 323 ? 1.1047 1.5872 1.5677 0.0444  0.3718  -0.3221 350 ARG A N   
2479 C CA  . ARG A 323 ? 1.0779 1.5731 1.5703 0.0059  0.3942  -0.3421 350 ARG A CA  
2480 C C   . ARG A 323 ? 1.1369 1.5569 1.5781 -0.0041 0.3873  -0.3087 350 ARG A C   
2481 O O   . ARG A 323 ? 1.1978 1.6313 1.6613 -0.0288 0.3948  -0.3231 350 ARG A O   
2482 C CB  . ARG A 323 ? 1.0319 1.5201 1.5457 -0.0315 0.4489  -0.3630 350 ARG A CB  
2483 C CG  . ARG A 323 ? 1.2874 1.6734 1.7336 -0.0394 0.4767  -0.3271 350 ARG A CG  
2484 C CD  . ARG A 323 ? 1.2466 1.6225 1.7116 -0.0774 0.5357  -0.3487 350 ARG A CD  
2485 N NE  . ARG A 323 ? 1.3534 1.6268 1.7465 -0.0834 0.5645  -0.3140 350 ARG A NE  
2486 C CZ  . ARG A 323 ? 1.3534 1.5974 1.7160 -0.0694 0.5771  -0.3014 350 ARG A CZ  
2487 N NH1 . ARG A 323 ? 1.2225 1.5282 1.6202 -0.0494 0.5644  -0.3192 350 ARG A NH1 
2488 N NH2 . ARG A 323 ? 1.4679 1.6190 1.7611 -0.0729 0.6026  -0.2709 350 ARG A NH2 
2489 N N   . ARG A 324 ? 1.1241 1.4688 1.5000 0.0145  0.3735  -0.2675 351 ARG A N   
2490 C CA  . ARG A 324 ? 1.0969 1.3728 1.4236 0.0080  0.3656  -0.2370 351 ARG A CA  
2491 C C   . ARG A 324 ? 1.0764 1.3732 1.3997 0.0332  0.3199  -0.2272 351 ARG A C   
2492 O O   . ARG A 324 ? 1.0809 1.3379 1.3611 0.0579  0.2954  -0.1985 351 ARG A O   
2493 C CB  . ARG A 324 ? 1.2141 1.4039 1.4746 0.0145  0.3755  -0.2027 351 ARG A CB  
2494 C CG  . ARG A 324 ? 1.2009 1.3608 1.4538 -0.0072 0.4228  -0.2087 351 ARG A CG  
2495 C CD  . ARG A 324 ? 1.2912 1.4352 1.5545 -0.0443 0.4575  -0.2205 351 ARG A CD  
2496 N NE  . ARG A 324 ? 1.5340 1.6624 1.8025 -0.0675 0.5084  -0.2344 351 ARG A NE  
2497 C CZ  . ARG A 324 ? 1.6134 1.7190 1.8885 -0.1024 0.5504  -0.2467 351 ARG A CZ  
2498 N NH1 . ARG A 324 ? 1.5163 1.6141 1.7955 -0.1183 0.5467  -0.2479 351 ARG A NH1 
2499 N NH2 . ARG A 324 ? 1.4249 1.5118 1.7010 -0.1221 0.5999  -0.2582 351 ARG A NH2 
2500 N N   . GLN A 325 ? 1.0395 1.4005 1.4099 0.0258  0.3107  -0.2539 352 GLN A N   
2501 C CA  . GLN A 325 ? 1.0897 1.4751 1.4573 0.0508  0.2696  -0.2473 352 GLN A CA  
2502 C C   . GLN A 325 ? 1.0039 1.3217 1.3231 0.0449  0.2596  -0.2157 352 GLN A C   
2503 O O   . GLN A 325 ? 0.9561 1.2547 1.2446 0.0701  0.2294  -0.1933 352 GLN A O   
2504 C CB  . GLN A 325 ? 1.0391 1.5156 1.4692 0.0458  0.2624  -0.2875 352 GLN A CB  
2505 C CG  . GLN A 325 ? 1.2889 1.8470 1.7733 0.0555  0.2676  -0.3245 352 GLN A CG  
2506 C CD  . GLN A 325 ? 1.4232 2.0800 1.9678 0.0586  0.2521  -0.3663 352 GLN A CD  
2507 O OE1 . GLN A 325 ? 1.2340 1.8960 1.7757 0.0568  0.2346  -0.3648 352 GLN A OE1 
2508 N NE2 . GLN A 325 ? 1.4031 2.1426 2.0034 0.0645  0.2579  -0.4062 352 GLN A NE2 
2509 N N   . ASP A 326 ? 1.0242 1.3037 1.3352 0.0123  0.2866  -0.2144 353 ASP A N   
2510 C CA  . ASP A 326 ? 1.0431 1.2626 1.3102 0.0074  0.2778  -0.1874 353 ASP A CA  
2511 C C   . ASP A 326 ? 0.9735 1.1279 1.1825 0.0280  0.2655  -0.1521 353 ASP A C   
2512 O O   . ASP A 326 ? 0.9409 1.0712 1.1217 0.0408  0.2402  -0.1321 353 ASP A O   
2513 C CB  . ASP A 326 ? 0.9206 1.1039 1.1840 -0.0282 0.3136  -0.1922 353 ASP A CB  
2514 C CG  . ASP A 326 ? 1.3305 1.4813 1.5835 -0.0414 0.3528  -0.1936 353 ASP A CG  
2515 O OD1 . ASP A 326 ? 1.2187 1.3865 1.4768 -0.0252 0.3515  -0.1955 353 ASP A OD1 
2516 O OD2 . ASP A 326 ? 1.3933 1.4980 1.6296 -0.0667 0.3864  -0.1921 353 ASP A OD2 
2517 N N   . ARG A 327 ? 1.0237 1.1512 1.2158 0.0306  0.2842  -0.1466 354 ARG A N   
2518 C CA  . ARG A 327 ? 1.0130 1.0844 1.1537 0.0499  0.2732  -0.1184 354 ARG A CA  
2519 C C   . ARG A 327 ? 1.0517 1.1441 1.1925 0.0801  0.2399  -0.1120 354 ARG A C   
2520 O O   . ARG A 327 ? 0.9728 1.0269 1.0781 0.0925  0.2208  -0.0906 354 ARG A O   
2521 C CB  . ARG A 327 ? 1.0189 1.0644 1.1443 0.0482  0.3006  -0.1177 354 ARG A CB  
2522 C CG  . ARG A 327 ? 0.8643 0.8634 0.9669 0.0240  0.3362  -0.1148 354 ARG A CG  
2523 C CD  . ARG A 327 ? 1.0281 0.9946 1.1039 0.0291  0.3598  -0.1095 354 ARG A CD  
2524 N NE  . ARG A 327 ? 1.0875 0.9943 1.1241 0.0132  0.3937  -0.1004 354 ARG A NE  
2525 C CZ  . ARG A 327 ? 1.1957 1.0591 1.1933 0.0192  0.4161  -0.0910 354 ARG A CZ  
2526 N NH1 . ARG A 327 ? 1.1410 1.0159 1.1370 0.0380  0.4085  -0.0908 354 ARG A NH1 
2527 N NH2 . ARG A 327 ? 1.3710 1.1754 1.3264 0.0081  0.4477  -0.0813 354 ARG A NH2 
2528 N N   . ARG A 328 ? 0.9708 1.1231 1.1506 0.0932  0.2343  -0.1319 355 ARG A N   
2529 C CA  . ARG A 328 ? 0.9508 1.1178 1.1253 0.1261  0.2059  -0.1253 355 ARG A CA  
2530 C C   . ARG A 328 ? 0.9223 1.0850 1.0844 0.1338  0.1803  -0.1139 355 ARG A C   
2531 O O   . ARG A 328 ? 0.8752 0.9994 1.0023 0.1512  0.1639  -0.0927 355 ARG A O   
2532 C CB  . ARG A 328 ? 0.9419 1.1817 1.1620 0.1412  0.2038  -0.1523 355 ARG A CB  
2533 C CG  . ARG A 328 ? 1.0005 1.2544 1.2112 0.1803  0.1756  -0.1458 355 ARG A CG  
2534 C CD  . ARG A 328 ? 0.9842 1.3209 1.2420 0.1990  0.1692  -0.1762 355 ARG A CD  
2535 N NE  . ARG A 328 ? 1.2385 1.6029 1.5266 0.1883  0.1938  -0.1972 355 ARG A NE  
2536 C CZ  . ARG A 328 ? 1.1030 1.5224 1.4410 0.1638  0.2132  -0.2287 355 ARG A CZ  
2537 N NH1 . ARG A 328 ? 0.9626 1.4187 1.3283 0.1475  0.2095  -0.2450 355 ARG A NH1 
2538 N NH2 . ARG A 328 ? 1.1241 1.5619 1.4856 0.1540  0.2387  -0.2462 355 ARG A NH2 
2539 N N   . GLU A 329 ? 0.9462 1.1471 1.1370 0.1194  0.1786  -0.1292 356 GLU A N   
2540 C CA  . GLU A 329 ? 0.8840 1.0845 1.0636 0.1269  0.1552  -0.1200 356 GLU A CA  
2541 C C   . GLU A 329 ? 0.9313 1.0621 1.0662 0.1169  0.1542  -0.0932 356 GLU A C   
2542 O O   . GLU A 329 ? 0.9050 1.0127 1.0137 0.1321  0.1351  -0.0761 356 GLU A O   
2543 C CB  . GLU A 329 ? 1.0056 1.2619 1.2265 0.1106  0.1562  -0.1451 356 GLU A CB  
2544 C CG  . GLU A 329 ? 1.1443 1.4813 1.4169 0.1189  0.1572  -0.1790 356 GLU A CG  
2545 C CD  . GLU A 329 ? 1.3316 1.7232 1.6506 0.0943  0.1652  -0.2100 356 GLU A CD  
2546 O OE1 . GLU A 329 ? 1.1577 1.5267 1.4649 0.0783  0.1628  -0.2023 356 GLU A OE1 
2547 O OE2 . GLU A 329 ? 1.3073 1.7659 1.6764 0.0903  0.1748  -0.2443 356 GLU A OE2 
2548 N N   . ARG A 330 ? 0.8179 0.9143 0.9422 0.0925  0.1760  -0.0903 357 ARG A N   
2549 C CA  . ARG A 330 ? 0.7709 0.8065 0.8529 0.0863  0.1741  -0.0681 357 ARG A CA  
2550 C C   . ARG A 330 ? 0.9247 0.9223 0.9733 0.1059  0.1644  -0.0506 357 ARG A C   
2551 O O   . ARG A 330 ? 0.9996 0.9673 1.0224 0.1111  0.1500  -0.0358 357 ARG A O   
2552 C CB  . ARG A 330 ? 0.7975 0.8012 0.8681 0.0631  0.2009  -0.0685 357 ARG A CB  
2553 C CG  . ARG A 330 ? 0.8147 0.7664 0.8459 0.0574  0.1974  -0.0506 357 ARG A CG  
2554 C CD  . ARG A 330 ? 0.7036 0.6100 0.7058 0.0473  0.2229  -0.0453 357 ARG A CD  
2555 N NE  . ARG A 330 ? 0.9277 0.8034 0.8991 0.0634  0.2216  -0.0344 357 ARG A NE  
2556 C CZ  . ARG A 330 ? 0.9403 0.7816 0.8768 0.0740  0.2070  -0.0205 357 ARG A CZ  
2557 N NH1 . ARG A 330 ? 0.9284 0.7600 0.8551 0.0709  0.1928  -0.0142 357 ARG A NH1 
2558 N NH2 . ARG A 330 ? 1.1188 0.9380 1.0319 0.0877  0.2071  -0.0155 357 ARG A NH2 
2559 N N   . MET A 331 ? 0.9211 0.9206 0.9717 0.1156  0.1736  -0.0544 358 MET A N   
2560 C CA  . MET A 331 ? 0.8942 0.8588 0.9158 0.1335  0.1661  -0.0413 358 MET A CA  
2561 C C   . MET A 331 ? 0.9031 0.8766 0.9235 0.1555  0.1450  -0.0360 358 MET A C   
2562 O O   . MET A 331 ? 1.0355 0.9704 1.0278 0.1622  0.1359  -0.0222 358 MET A O   
2563 C CB  . MET A 331 ? 0.9212 0.8886 0.9467 0.1395  0.1818  -0.0484 358 MET A CB  
2564 C CG  . MET A 331 ? 1.1483 1.0898 1.1595 0.1221  0.2056  -0.0488 358 MET A CG  
2565 S SD  . MET A 331 ? 1.0605 0.9382 1.0200 0.1216  0.2012  -0.0305 358 MET A SD  
2566 C CE  . MET A 331 ? 0.9666 0.8299 0.9125 0.1450  0.1863  -0.0256 358 MET A CE  
2567 N N   . LEU A 332 ? 0.8487 0.8725 0.8982 0.1679  0.1382  -0.0483 359 LEU A N   
2568 C CA  . LEU A 332 ? 0.8613 0.8898 0.9022 0.1943  0.1195  -0.0418 359 LEU A CA  
2569 C C   . LEU A 332 ? 0.8855 0.8933 0.9085 0.1890  0.1075  -0.0294 359 LEU A C   
2570 O O   . LEU A 332 ? 0.9231 0.9000 0.9195 0.2048  0.0984  -0.0155 359 LEU A O   
2571 C CB  . LEU A 332 ? 0.8022 0.8963 0.8771 0.2121  0.1129  -0.0605 359 LEU A CB  
2572 C CG  . LEU A 332 ? 0.7888 0.9099 0.8832 0.2240  0.1224  -0.0745 359 LEU A CG  
2573 C CD1 . LEU A 332 ? 0.7423 0.9372 0.8727 0.2444  0.1124  -0.0969 359 LEU A CD1 
2574 C CD2 . LEU A 332 ? 0.7903 0.8644 0.8518 0.2448  0.1220  -0.0594 359 LEU A CD2 
2575 N N   . ARG A 333 ? 0.7589 0.7808 0.7951 0.1664  0.1097  -0.0348 360 ARG A N   
2576 C CA  . ARG A 333 ? 0.7759 0.7774 0.7951 0.1594  0.0996  -0.0237 360 ARG A CA  
2577 C C   . ARG A 333 ? 0.8267 0.7696 0.8126 0.1517  0.1027  -0.0083 360 ARG A C   
2578 O O   . ARG A 333 ? 0.9412 0.8575 0.9057 0.1576  0.0941  0.0033  360 ARG A O   
2579 C CB  . ARG A 333 ? 0.8925 0.9205 0.9336 0.1366  0.1031  -0.0348 360 ARG A CB  
2580 C CG  . ARG A 333 ? 0.9413 1.0332 1.0175 0.1432  0.0961  -0.0538 360 ARG A CG  
2581 C CD  . ARG A 333 ? 1.0573 1.1704 1.1567 0.1162  0.1040  -0.0675 360 ARG A CD  
2582 N NE  . ARG A 333 ? 1.3304 1.5080 1.4639 0.1220  0.0941  -0.0887 360 ARG A NE  
2583 C CZ  . ARG A 333 ? 1.4582 1.6497 1.5853 0.1332  0.0756  -0.0861 360 ARG A CZ  
2584 N NH1 . ARG A 333 ? 1.3438 1.4881 1.4334 0.1377  0.0670  -0.0627 360 ARG A NH1 
2585 N NH2 . ARG A 333 ? 1.4053 1.6622 1.5651 0.1404  0.0661  -0.1095 360 ARG A NH2 
2586 N N   . ALA A 334 ? 0.8825 0.8062 0.8632 0.1392  0.1160  -0.0098 361 ALA A N   
2587 C CA  . ALA A 334 ? 0.9853 0.8618 0.9365 0.1338  0.1174  -0.0003 361 ALA A CA  
2588 C C   . ALA A 334 ? 0.9430 0.7935 0.8773 0.1505  0.1137  0.0060  361 ALA A C   
2589 O O   . ALA A 334 ? 0.9308 0.7495 0.8455 0.1482  0.1096  0.0125  361 ALA A O   
2590 C CB  . ALA A 334 ? 0.8925 0.7558 0.8371 0.1231  0.1325  -0.0041 361 ALA A CB  
2591 N N   . LEU A 335 ? 0.8780 0.7414 0.8205 0.1671  0.1166  0.0023  362 LEU A N   
2592 C CA  . LEU A 335 ? 0.9562 0.7899 0.8807 0.1842  0.1158  0.0080  362 LEU A CA  
2593 C C   . LEU A 335 ? 0.8970 0.7204 0.8103 0.1964  0.1065  0.0173  362 LEU A C   
2594 O O   . LEU A 335 ? 0.8732 0.6549 0.7640 0.1991  0.1085  0.0244  362 LEU A O   
2595 C CB  . LEU A 335 ? 0.7921 0.6431 0.7272 0.2012  0.1215  0.0013  362 LEU A CB  
2596 C CG  . LEU A 335 ? 0.9327 0.7835 0.8714 0.1912  0.1344  -0.0064 362 LEU A CG  
2597 C CD1 . LEU A 335 ? 0.9158 0.7899 0.8690 0.2079  0.1406  -0.0147 362 LEU A CD1 
2598 C CD2 . LEU A 335 ? 0.9282 0.7337 0.8404 0.1851  0.1376  -0.0029 362 LEU A CD2 
2599 N N   . GLN A 336 ? 0.8669 0.7274 0.7945 0.2039  0.0981  0.0158  363 GLN A N   
2600 C CA  . GLN A 336 ? 0.8149 0.6646 0.7259 0.2188  0.0898  0.0257  363 GLN A CA  
2601 C C   . GLN A 336 ? 0.9077 0.7278 0.8039 0.1996  0.0891  0.0333  363 GLN A C   
2602 O O   . GLN A 336 ? 0.9948 0.7782 0.8665 0.2066  0.0907  0.0436  363 GLN A O   
2603 C CB  . GLN A 336 ? 0.8405 0.7444 0.7710 0.2326  0.0789  0.0187  363 GLN A CB  
2604 C CG  . GLN A 336 ? 1.1654 1.0631 1.0766 0.2460  0.0693  0.0287  363 GLN A CG  
2605 C CD  . GLN A 336 ? 1.4024 1.2579 1.2777 0.2755  0.0718  0.0425  363 GLN A CD  
2606 O OE1 . GLN A 336 ? 1.4400 1.2770 1.3084 0.2885  0.0788  0.0429  363 GLN A OE1 
2607 N NE2 . GLN A 336 ? 1.3351 1.1714 1.1843 0.2869  0.0680  0.0543  363 GLN A NE2 
2608 N N   . ALA A 337 ? 0.9295 0.7629 0.8389 0.1758  0.0888  0.0277  364 ALA A N   
2609 C CA  . ALA A 337 ? 0.7853 0.5950 0.6827 0.1584  0.0876  0.0321  364 ALA A CA  
2610 C C   . ALA A 337 ? 0.9272 0.6917 0.8057 0.1536  0.0951  0.0339  364 ALA A C   
2611 O O   . ALA A 337 ? 0.8461 0.5855 0.7115 0.1466  0.0959  0.0378  364 ALA A O   
2612 C CB  . ALA A 337 ? 0.7595 0.5889 0.6712 0.1377  0.0870  0.0252  364 ALA A CB  
2613 N N   . GLN A 338 ? 0.9261 0.6818 0.8045 0.1564  0.1018  0.0286  365 GLN A N   
2614 C CA  . GLN A 338 ? 0.8997 0.6178 0.7637 0.1522  0.1090  0.0253  365 GLN A CA  
2615 C C   . GLN A 338 ? 1.0342 0.7221 0.8840 0.1694  0.1163  0.0304  365 GLN A C   
2616 O O   . GLN A 338 ? 1.0359 0.6923 0.8762 0.1663  0.1249  0.0248  365 GLN A O   
2617 C CB  . GLN A 338 ? 0.8377 0.5602 0.7049 0.1471  0.1127  0.0156  365 GLN A CB  
2618 C CG  . GLN A 338 ? 0.8379 0.5778 0.7095 0.1327  0.1090  0.0118  365 GLN A CG  
2619 C CD  . GLN A 338 ? 0.8317 0.5722 0.6989 0.1329  0.1149  0.0046  365 GLN A CD  
2620 O OE1 . GLN A 338 ? 0.9120 0.6364 0.7661 0.1296  0.1152  -0.0028 365 GLN A OE1 
2621 N NE2 . GLN A 338 ? 0.8624 0.6234 0.7403 0.1376  0.1205  0.0050  365 GLN A NE2 
2622 N N   . GLU A 339 ? 1.0361 0.7324 0.8826 0.1891  0.1134  0.0395  366 GLU A N   
2623 C CA  . GLU A 339 ? 1.0757 0.7387 0.9016 0.2117  0.1212  0.0469  366 GLU A CA  
2624 C C   . GLU A 339 ? 0.9216 0.5746 0.7486 0.2196  0.1285  0.0400  366 GLU A C   
2625 O O   . GLU A 339 ? 1.0540 0.6623 0.8640 0.2219  0.1404  0.0396  366 GLU A O   
2626 C CB  . GLU A 339 ? 1.1772 0.7889 0.9794 0.2048  0.1319  0.0530  366 GLU A CB  
2627 C CG  . GLU A 339 ? 1.1988 0.8153 0.9936 0.2033  0.1267  0.0623  366 GLU A CG  
2628 C CD  . GLU A 339 ? 1.4916 1.0509 1.2569 0.2033  0.1426  0.0708  366 GLU A CD  
2629 O OE1 . GLU A 339 ? 1.6368 1.1536 1.3929 0.1968  0.1585  0.0657  366 GLU A OE1 
2630 O OE2 . GLU A 339 ? 1.4677 1.0229 1.2182 0.2093  0.1413  0.0815  366 GLU A OE2 
2631 N N   . ILE A 340 ? 0.9705 0.6648 0.8182 0.2225  0.1233  0.0330  367 ILE A N   
2632 C CA  . ILE A 340 ? 1.0382 0.7303 0.8890 0.2301  0.1299  0.0255  367 ILE A CA  
2633 C C   . ILE A 340 ? 1.1313 0.8615 0.9953 0.2539  0.1256  0.0245  367 ILE A C   
2634 O O   . ILE A 340 ? 1.0772 0.8543 0.9626 0.2512  0.1179  0.0209  367 ILE A O   
2635 C CB  . ILE A 340 ? 0.9445 0.6493 0.8066 0.2093  0.1315  0.0149  367 ILE A CB  
2636 C CG1 . ILE A 340 ? 1.0183 0.6942 0.8695 0.1892  0.1330  0.0116  367 ILE A CG1 
2637 C CG2 . ILE A 340 ? 1.0681 0.7709 0.9311 0.2188  0.1392  0.0072  367 ILE A CG2 
2638 C CD1 . ILE A 340 ? 0.9219 0.6107 0.7772 0.1740  0.1321  0.0020  367 ILE A CD1 
2639 N N   . GLU A 341 ? 1.2189 0.9307 1.0715 0.2772  0.1313  0.0253  368 GLU A N   
2640 C CA  . GLU A 341 ? 1.1160 0.8659 0.9810 0.3041  0.1270  0.0214  368 GLU A CA  
2641 C C   . GLU A 341 ? 1.0834 0.8496 0.9644 0.3014  0.1341  0.0092  368 GLU A C   
2642 O O   . GLU A 341 ? 1.1043 0.8337 0.9727 0.2937  0.1434  0.0074  368 GLU A O   
2643 C CB  . GLU A 341 ? 1.1662 0.8829 1.0024 0.3384  0.1286  0.0315  368 GLU A CB  
2644 C CG  . GLU A 341 ? 1.3471 1.1083 1.1938 0.3732  0.1208  0.0262  368 GLU A CG  
2645 C CD  . GLU A 341 ? 1.5458 1.2682 1.3545 0.4125  0.1219  0.0389  368 GLU A CD  
2646 O OE1 . GLU A 341 ? 1.5813 1.2370 1.3556 0.4090  0.1324  0.0525  368 GLU A OE1 
2647 O OE2 . GLU A 341 ? 1.6542 1.4121 1.4663 0.4479  0.1138  0.0343  368 GLU A OE2 
2648 N N   . CYS A 342 ? 1.1261 0.9494 1.0360 0.3070  0.1308  -0.0014 369 CYS A N   
2649 C CA  . CYS A 342 ? 1.1024 0.9453 1.0292 0.3027  0.1402  -0.0137 369 CYS A CA  
2650 C C   . CYS A 342 ? 1.0955 0.9813 1.0403 0.3315  0.1379  -0.0236 369 CYS A C   
2651 O O   . CYS A 342 ? 1.0523 0.9653 1.0017 0.3531  0.1267  -0.0235 369 CYS A O   
2652 C CB  . CYS A 342 ? 0.9138 0.7855 0.8620 0.2731  0.1447  -0.0214 369 CYS A CB  
2653 S SG  . CYS A 342 ? 1.1348 1.0828 1.1253 0.2726  0.1409  -0.0358 369 CYS A SG  
2654 N N   . ARG A 343 ? 1.1458 1.0398 1.0999 0.3336  0.1484  -0.0336 370 ARG A N   
2655 C CA  . ARG A 343 ? 1.0178 0.9621 0.9965 0.3569  0.1485  -0.0481 370 ARG A CA  
2656 C C   . ARG A 343 ? 0.9914 0.9877 1.0077 0.3328  0.1581  -0.0649 370 ARG A C   
2657 O O   . ARG A 343 ? 1.0219 1.0023 1.0358 0.3140  0.1728  -0.0673 370 ARG A O   
2658 C CB  . ARG A 343 ? 1.1073 1.0219 1.0692 0.3780  0.1561  -0.0486 370 ARG A CB  
2659 C CG  . ARG A 343 ? 1.2678 1.2379 1.2565 0.4037  0.1564  -0.0656 370 ARG A CG  
2660 C CD  . ARG A 343 ? 1.3187 1.2543 1.2844 0.4335  0.1606  -0.0634 370 ARG A CD  
2661 N NE  . ARG A 343 ? 1.3657 1.3592 1.3580 0.4617  0.1591  -0.0812 370 ARG A NE  
2662 C CZ  . ARG A 343 ? 1.5774 1.5553 1.5546 0.4957  0.1605  -0.0825 370 ARG A CZ  
2663 N NH1 . ARG A 343 ? 1.5528 1.4549 1.4883 0.5042  0.1658  -0.0673 370 ARG A NH1 
2664 N NH2 . ARG A 343 ? 1.6764 1.7172 1.6824 0.5217  0.1576  -0.1017 370 ARG A NH2 
2665 N N   . LEU A 344 ? 0.9708 1.0276 1.0198 0.3338  0.1514  -0.0776 371 LEU A N   
2666 C CA  . LEU A 344 ? 1.0216 1.1266 1.1087 0.3071  0.1641  -0.0958 371 LEU A CA  
2667 C C   . LEU A 344 ? 1.0019 1.1424 1.1135 0.3159  0.1775  -0.1145 371 LEU A C   
2668 O O   . LEU A 344 ? 1.0288 1.2225 1.1657 0.3415  0.1699  -0.1308 371 LEU A O   
2669 C CB  . LEU A 344 ? 1.0657 1.2274 1.1836 0.3050  0.1529  -0.1079 371 LEU A CB  
2670 C CG  . LEU A 344 ? 1.1733 1.3847 1.3342 0.2741  0.1691  -0.1300 371 LEU A CG  
2671 C CD1 . LEU A 344 ? 1.2123 1.3738 1.3537 0.2384  0.1856  -0.1174 371 LEU A CD1 
2672 C CD2 . LEU A 344 ? 1.2392 1.5122 1.4332 0.2755  0.1558  -0.1465 371 LEU A CD2 
2673 N N   . VAL A 345 ? 1.0934 1.2062 1.1962 0.2969  0.1973  -0.1134 372 VAL A N   
2674 C CA  . VAL A 345 ? 1.1256 1.2682 1.2501 0.3004  0.2144  -0.1310 372 VAL A CA  
2675 C C   . VAL A 345 ? 1.2301 1.4246 1.3968 0.2725  0.2329  -0.1523 372 VAL A C   
2676 O O   . VAL A 345 ? 1.1978 1.3681 1.3563 0.2419  0.2456  -0.1461 372 VAL A O   
2677 C CB  . VAL A 345 ? 0.9451 1.0298 1.0346 0.2956  0.2283  -0.1198 372 VAL A CB  
2678 C CG1 . VAL A 345 ? 0.9437 1.0591 1.0548 0.2978  0.2485  -0.1381 372 VAL A CG1 
2679 C CG2 . VAL A 345 ? 1.0370 1.0706 1.0891 0.3202  0.2131  -0.1032 372 VAL A CG2 
2680 N N   . GLU A 346 ? 1.3861 1.6521 1.5983 0.2835  0.2356  -0.1791 373 GLU A N   
2681 C CA  . GLU A 346 ? 1.2944 1.6134 1.5530 0.2545  0.2581  -0.2051 373 GLU A CA  
2682 C C   . GLU A 346 ? 1.1510 1.4408 1.3999 0.2334  0.2911  -0.2056 373 GLU A C   
2683 O O   . GLU A 346 ? 1.0961 1.3891 1.3436 0.2501  0.2979  -0.2109 373 GLU A O   
2684 C CB  . GLU A 346 ? 1.3367 1.7479 1.6506 0.2736  0.2511  -0.2388 373 GLU A CB  
2685 C CG  . GLU A 346 ? 1.4004 1.8739 1.7706 0.2402  0.2756  -0.2719 373 GLU A CG  
2686 C CD  . GLU A 346 ? 1.3982 1.9737 1.8289 0.2599  0.2676  -0.3115 373 GLU A CD  
2687 O OE1 . GLU A 346 ? 1.4175 2.0126 1.8410 0.3039  0.2411  -0.3105 373 GLU A OE1 
2688 O OE2 . GLU A 346 ? 1.3035 1.9394 1.7884 0.2322  0.2888  -0.3453 373 GLU A OE2 
2689 N N   . ALA A 347 ? 1.0752 1.3445 1.4507 0.3464  0.3237  -0.0679 374 ALA A N   
2690 C CA  . ALA A 347 ? 1.0952 1.3342 1.4439 0.3283  0.3472  -0.0578 374 ALA A CA  
2691 C C   . ALA A 347 ? 1.1233 1.3916 1.5127 0.3218  0.3731  -0.0648 374 ALA A C   
2692 O O   . ALA A 347 ? 1.2471 1.5613 1.6923 0.3254  0.3706  -0.0775 374 ALA A O   
2693 C CB  . ALA A 347 ? 1.1204 1.3342 1.4557 0.3086  0.3395  -0.0490 374 ALA A CB  
2694 N N   . VAL A 348 ? 1.0540 1.2962 1.4141 0.3119  0.3984  -0.0564 375 VAL A N   
2695 C CA  . VAL A 348 ? 1.1371 1.4019 1.5298 0.3030  0.4265  -0.0609 375 VAL A CA  
2696 C C   . VAL A 348 ? 1.1956 1.4550 1.6047 0.2774  0.4326  -0.0570 375 VAL A C   
2697 O O   . VAL A 348 ? 1.2881 1.5046 1.6542 0.2639  0.4368  -0.0437 375 VAL A O   
2698 C CB  . VAL A 348 ? 1.1784 1.4167 1.5298 0.3055  0.4522  -0.0540 375 VAL A CB  
2699 C CG1 . VAL A 348 ? 1.0016 1.2667 1.3895 0.2973  0.4822  -0.0591 375 VAL A CG1 
2700 C CG2 . VAL A 348 ? 1.0894 1.3254 1.4184 0.3306  0.4454  -0.0572 375 VAL A CG2 
2701 N N   . ASP A 349 ? 1.1188 1.4213 1.5896 0.2707  0.4330  -0.0687 376 ASP A N   
2702 C CA  . ASP A 349 ? 1.2252 1.5238 1.7164 0.2456  0.4401  -0.0666 376 ASP A CA  
2703 C C   . ASP A 349 ? 1.3378 1.6255 1.8225 0.2307  0.4753  -0.0606 376 ASP A C   
2704 O O   . ASP A 349 ? 1.3225 1.6475 1.8468 0.2320  0.4940  -0.0699 376 ASP A O   
2705 C CB  . ASP A 349 ? 1.1689 1.5183 1.7288 0.2424  0.4290  -0.0829 376 ASP A CB  
2706 C CG  . ASP A 349 ? 1.3900 1.7302 1.9681 0.2162  0.4324  -0.0813 376 ASP A CG  
2707 O OD1 . ASP A 349 ? 1.4377 1.7294 1.9714 0.2034  0.4384  -0.0663 376 ASP A OD1 
2708 O OD2 . ASP A 349 ? 1.4979 1.8789 2.1342 0.2086  0.4291  -0.0951 376 ASP A OD2 
2709 N N   . GLY A 350 ? 1.3937 1.6313 1.8281 0.2172  0.4846  -0.0447 377 GLY A N   
2710 C CA  . GLY A 350 ? 1.4405 1.6627 1.8613 0.2034  0.5184  -0.0373 377 GLY A CA  
2711 C C   . GLY A 350 ? 1.5237 1.7713 1.9971 0.1822  0.5363  -0.0431 377 GLY A C   
2712 O O   . GLY A 350 ? 1.5813 1.8389 2.0665 0.1746  0.5662  -0.0433 377 GLY A O   
2713 N N   . LYS A 351 ? 1.3920 1.6498 1.8973 0.1717  0.5193  -0.0481 378 LYS A N   
2714 C CA  . LYS A 351 ? 1.4511 1.7340 2.0095 0.1499  0.5352  -0.0554 378 LYS A CA  
2715 C C   . LYS A 351 ? 1.4606 1.8084 2.0844 0.1568  0.5414  -0.0740 378 LYS A C   
2716 O O   . LYS A 351 ? 1.3481 1.7199 2.0109 0.1405  0.5662  -0.0791 378 LYS A O   
2717 C CB  . LYS A 351 ? 1.4333 1.7078 2.0064 0.1376  0.5141  -0.0570 378 LYS A CB  
2718 C CG  . LYS A 351 ? 1.5267 1.8200 2.1507 0.1118  0.5303  -0.0641 378 LYS A CG  
2719 C CD  . LYS A 351 ? 1.4354 1.7149 2.0688 0.1008  0.5088  -0.0658 378 LYS A CD  
2720 C CE  . LYS A 351 ? 1.3852 1.6819 2.0697 0.0736  0.5254  -0.0741 378 LYS A CE  
2721 N NZ  . LYS A 351 ? 1.3218 1.6018 2.0140 0.0627  0.5053  -0.0766 378 LYS A NZ  
2722 N N   . ALA A 352 ? 1.4338 1.8112 2.0700 0.1812  0.5198  -0.0839 379 ALA A N   
2723 C CA  . ALA A 352 ? 1.2945 1.7362 1.9928 0.1910  0.5229  -0.1017 379 ALA A CA  
2724 C C   . ALA A 352 ? 1.1836 1.6364 1.8799 0.1966  0.5539  -0.1005 379 ALA A C   
2725 O O   . ALA A 352 ? 1.2072 1.7126 1.9596 0.1963  0.5671  -0.1135 379 ALA A O   
2726 C CB  . ALA A 352 ? 1.1399 1.6056 1.8459 0.2176  0.4914  -0.1109 379 ALA A CB  
2727 N N   . MET A 353 ? 1.3837 1.7894 2.0168 0.2019  0.5657  -0.0859 380 MET A N   
2728 C CA  . MET A 353 ? 1.4859 1.8980 2.1112 0.2088  0.5951  -0.0847 380 MET A CA  
2729 C C   . MET A 353 ? 1.3848 1.8031 2.0335 0.1836  0.6286  -0.0829 380 MET A C   
2730 O O   . MET A 353 ? 1.3036 1.6861 1.9325 0.1610  0.6351  -0.0723 380 MET A O   
2731 C CB  . MET A 353 ? 1.5065 1.8628 2.0541 0.2192  0.5981  -0.0700 380 MET A CB  
2732 C CG  . MET A 353 ? 1.4130 1.7582 1.9318 0.2431  0.5680  -0.0706 380 MET A CG  
2733 S SD  . MET A 353 ? 1.6165 1.8952 2.0441 0.2507  0.5723  -0.0540 380 MET A SD  
2734 C CE  . MET A 353 ? 1.5102 1.7993 1.9365 0.2563  0.6114  -0.0558 380 MET A CE  
2735 N N   . ASN A 354 ? 1.2724 1.7364 1.9634 0.1880  0.6505  -0.0928 381 ASN A N   
2736 C CA  . ASN A 354 ? 1.4066 1.8755 2.1145 0.1661  0.6869  -0.0901 381 ASN A CA  
2737 C C   . ASN A 354 ? 1.4620 1.8903 2.1100 0.1715  0.7127  -0.0769 381 ASN A C   
2738 O O   . ASN A 354 ? 1.5195 1.9262 2.1230 0.1938  0.7034  -0.0733 381 ASN A O   
2739 C CB  . ASN A 354 ? 1.2838 1.8263 2.0712 0.1662  0.6995  -0.1080 381 ASN A CB  
2740 C CG  . ASN A 354 ? 1.3634 1.9424 2.1628 0.1983  0.6956  -0.1176 381 ASN A CG  
2741 O OD1 . ASN A 354 ? 1.3716 1.9346 2.1370 0.2107  0.7159  -0.1118 381 ASN A OD1 
2742 N ND2 . ASN A 354 ? 1.3385 1.9664 2.1858 0.2125  0.6700  -0.1326 381 ASN A ND2 
2743 N N   . THR A 355 ? 1.3338 1.7504 1.9797 0.1499  0.7459  -0.0699 382 THR A N   
2744 C CA  . THR A 355 ? 1.5064 1.8805 2.0919 0.1519  0.7720  -0.0565 382 THR A CA  
2745 C C   . THR A 355 ? 1.5530 1.9516 2.1388 0.1784  0.7818  -0.0640 382 THR A C   
2746 O O   . THR A 355 ? 1.5655 1.9238 2.0893 0.1914  0.7865  -0.0552 382 THR A O   
2747 C CB  . THR A 355 ? 1.5928 1.9590 2.1857 0.1245  0.8083  -0.0494 382 THR A CB  
2748 O OG1 . THR A 355 ? 1.6253 1.9673 2.2190 0.1005  0.7991  -0.0427 382 THR A OG1 
2749 C CG2 . THR A 355 ? 1.5567 1.8729 2.0796 0.1259  0.8336  -0.0342 382 THR A CG2 
2750 N N   . SER A 356 ? 1.4606 1.9253 2.1155 0.1873  0.7843  -0.0806 383 SER A N   
2751 C CA  . SER A 356 ? 1.4276 1.9185 2.0868 0.2147  0.7937  -0.0883 383 SER A CA  
2752 C C   . SER A 356 ? 1.3418 1.8118 1.9621 0.2422  0.7638  -0.0883 383 SER A C   
2753 O O   . SER A 356 ? 1.3246 1.7735 1.9029 0.2614  0.7730  -0.0855 383 SER A O   
2754 C CB  . SER A 356 ? 1.4024 1.9725 2.1475 0.2190  0.7999  -0.1064 383 SER A CB  
2755 O OG  . SER A 356 ? 1.3326 1.9232 2.1158 0.1915  0.8285  -0.1069 383 SER A OG  
2756 N N   . GLN A 357 ? 1.3730 1.8471 2.0053 0.2441  0.7285  -0.0917 384 GLN A N   
2757 C CA  . GLN A 357 ? 1.3615 1.8133 1.9555 0.2682  0.7000  -0.0908 384 GLN A CA  
2758 C C   . GLN A 357 ? 1.3572 1.7368 1.8668 0.2655  0.7004  -0.0744 384 GLN A C   
2759 O O   . GLN A 357 ? 1.2353 1.5911 1.7021 0.2864  0.6920  -0.0726 384 GLN A O   
2760 C CB  . GLN A 357 ? 1.2240 1.6950 1.8487 0.2687  0.6635  -0.0973 384 GLN A CB  
2761 C CG  . GLN A 357 ? 1.1019 1.6468 1.8065 0.2772  0.6569  -0.1154 384 GLN A CG  
2762 C CD  . GLN A 357 ? 1.1630 1.7251 1.8961 0.2752  0.6218  -0.1220 384 GLN A CD  
2763 O OE1 . GLN A 357 ? 1.2189 1.7379 1.9144 0.2661  0.6034  -0.1129 384 GLN A OE1 
2764 N NE2 . GLN A 357 ? 0.9951 1.6214 1.7947 0.2842  0.6121  -0.1383 384 GLN A NE2 
2765 N N   . VAL A 358 ? 1.3595 1.7032 1.8436 0.2399  0.7101  -0.0623 385 VAL A N   
2766 C CA  . VAL A 358 ? 1.3363 1.6143 1.7403 0.2365  0.7133  -0.0466 385 VAL A CA  
2767 C C   . VAL A 358 ? 1.4814 1.7466 1.8529 0.2467  0.7429  -0.0448 385 VAL A C   
2768 O O   . VAL A 358 ? 1.4834 1.7105 1.7965 0.2603  0.7383  -0.0398 385 VAL A O   
2769 C CB  . VAL A 358 ? 1.4827 1.7281 1.8693 0.2079  0.7197  -0.0339 385 VAL A CB  
2770 C CG1 . VAL A 358 ? 1.5079 1.6879 1.8110 0.2056  0.7217  -0.0176 385 VAL A CG1 
2771 C CG2 . VAL A 358 ? 1.5035 1.7602 1.9220 0.1987  0.6907  -0.0366 385 VAL A CG2 
2772 N N   . GLU A 359 ? 1.5996 1.8970 2.0093 0.2400  0.7743  -0.0495 386 GLU A N   
2773 C CA  . GLU A 359 ? 1.5095 1.7996 1.8935 0.2508  0.8047  -0.0491 386 GLU A CA  
2774 C C   . GLU A 359 ? 1.4307 1.7420 1.8209 0.2823  0.7961  -0.0602 386 GLU A C   
2775 O O   . GLU A 359 ? 1.4060 1.6877 1.7456 0.2942  0.8039  -0.0577 386 GLU A O   
2776 C CB  . GLU A 359 ? 1.5962 1.9221 2.0268 0.2363  0.8400  -0.0525 386 GLU A CB  
2777 C CG  . GLU A 359 ? 1.6253 1.9270 2.0479 0.2046  0.8530  -0.0407 386 GLU A CG  
2778 C CD  . GLU A 359 ? 1.6639 2.0121 2.1498 0.1882  0.8822  -0.0468 386 GLU A CD  
2779 O OE1 . GLU A 359 ? 1.6624 2.0659 2.2008 0.2009  0.8862  -0.0609 386 GLU A OE1 
2780 O OE2 . GLU A 359 ? 1.7351 2.0637 2.2161 0.1618  0.8978  -0.0372 386 GLU A OE2 
2781 N N   . ALA A 360 ? 1.4096 1.7692 1.8565 0.2944  0.7743  -0.0724 387 ALA A N   
2782 C CA  . ALA A 360 ? 1.3525 1.7282 1.7986 0.3225  0.7547  -0.0819 387 ALA A CA  
2783 C C   . ALA A 360 ? 1.3680 1.6883 1.7451 0.3355  0.7383  -0.0746 387 ALA A C   
2784 O O   . ALA A 360 ? 1.3661 1.6725 1.7109 0.3533  0.7331  -0.0775 387 ALA A O   
2785 C CB  . ALA A 360 ? 1.3100 1.7446 1.8250 0.3315  0.7302  -0.0951 387 ALA A CB  
2786 N N   . LEU A 361 ? 1.2799 1.5665 1.6301 0.3228  0.7220  -0.0654 388 LEU A N   
2787 C CA  . LEU A 361 ? 1.3309 1.5637 1.6128 0.3298  0.7034  -0.0577 388 LEU A CA  
2788 C C   . LEU A 361 ? 1.4137 1.5916 1.6266 0.3188  0.7240  -0.0458 388 LEU A C   
2789 O O   . LEU A 361 ? 1.4410 1.5730 1.5937 0.3227  0.7108  -0.0395 388 LEU A O   
2790 C CB  . LEU A 361 ? 1.3511 1.5748 1.6338 0.3200  0.6695  -0.0536 388 LEU A CB  
2791 C CG  . LEU A 361 ? 1.3329 1.6085 1.6806 0.3291  0.6462  -0.0652 388 LEU A CG  
2792 C CD1 . LEU A 361 ? 1.1321 1.3925 1.4728 0.3192  0.6142  -0.0604 388 LEU A CD1 
2793 C CD2 . LEU A 361 ? 1.1748 1.4698 1.5301 0.3598  0.6389  -0.0749 388 LEU A CD2 
2794 N N   . GLY A 362 ? 1.4752 1.6575 1.6952 0.3049  0.7560  -0.0428 389 GLY A N   
2795 C CA  . GLY A 362 ? 1.4424 1.5750 1.5973 0.2953  0.7777  -0.0318 389 GLY A CA  
2796 C C   . GLY A 362 ? 1.5569 1.6406 1.6595 0.2785  0.7605  -0.0181 389 GLY A C   
2797 O O   . GLY A 362 ? 1.6015 1.6383 1.6373 0.2818  0.7576  -0.0118 389 GLY A O   
2798 N N   . ILE A 363 ? 1.5268 1.6214 1.6594 0.2606  0.7489  -0.0140 390 ILE A N   
2799 C CA  . ILE A 363 ? 1.5637 1.6168 1.6538 0.2460  0.7302  -0.0011 390 ILE A CA  
2800 C C   . ILE A 363 ? 1.5849 1.6152 1.6550 0.2237  0.7559  0.0110  390 ILE A C   
2801 O O   . ILE A 363 ? 1.5541 1.6132 1.6726 0.2107  0.7730  0.0092  390 ILE A O   
2802 C CB  . ILE A 363 ? 1.5585 1.6340 1.6905 0.2426  0.6988  -0.0040 390 ILE A CB  
2803 C CG1 . ILE A 363 ? 1.4576 1.5571 1.6098 0.2659  0.6749  -0.0158 390 ILE A CG1 
2804 C CG2 . ILE A 363 ? 1.5500 1.5824 1.6367 0.2295  0.6798  0.0096  390 ILE A CG2 
2805 C CD1 . ILE A 363 ? 1.3469 1.4810 1.5534 0.2651  0.6483  -0.0222 390 ILE A CD1 
2806 N N   . GLN A 364 ? 1.6616 1.6400 1.6596 0.2189  0.7588  0.0232  391 GLN A N   
2807 C CA  . GLN A 364 ? 1.6934 1.6429 1.6614 0.1992  0.7815  0.0367  391 GLN A CA  
2808 C C   . GLN A 364 ? 1.6745 1.5793 1.5892 0.1906  0.7592  0.0505  391 GLN A C   
2809 O O   . GLN A 364 ? 1.7394 1.6189 1.6080 0.2011  0.7397  0.0516  391 GLN A O   
2810 C CB  . GLN A 364 ? 1.7447 1.6749 1.6715 0.2027  0.8143  0.0384  391 GLN A CB  
2811 C CG  . GLN A 364 ? 1.7185 1.6172 1.6103 0.1831  0.8394  0.0532  391 GLN A CG  
2812 C CD  . GLN A 364 ? 1.8611 1.7348 1.7016 0.1878  0.8689  0.0554  391 GLN A CD  
2813 O OE1 . GLN A 364 ? 2.0052 1.8845 1.8369 0.2057  0.8715  0.0453  391 GLN A OE1 
2814 N NE2 . GLN A 364 ? 1.7994 1.6434 1.6035 0.1722  0.8917  0.0688  391 GLN A NE2 
2815 N N   . MET A 365 ? 1.6674 1.5629 1.5890 0.1718  0.7626  0.0609  392 MET A N   
2816 C CA  . MET A 365 ? 1.6424 1.4966 1.5154 0.1637  0.7435  0.0753  392 MET A CA  
2817 C C   . MET A 365 ? 1.7144 1.5222 1.5086 0.1638  0.7561  0.0861  392 MET A C   
2818 O O   . MET A 365 ? 1.8793 1.6818 1.6589 0.1617  0.7878  0.0870  392 MET A O   
2819 C CB  . MET A 365 ? 1.6093 1.4626 1.5082 0.1440  0.7493  0.0841  392 MET A CB  
2820 C CG  . MET A 365 ? 1.6507 1.4625 1.5035 0.1360  0.7313  0.0999  392 MET A CG  
2821 S SD  . MET A 365 ? 1.9193 1.7306 1.8087 0.1136  0.7409  0.1084  392 MET A SD  
2822 C CE  . MET A 365 ? 1.6643 1.4194 1.4821 0.1097  0.7225  0.1289  392 MET A CE  
2823 N N   . LEU A 366 ? 1.7058 1.4815 1.4490 0.1666  0.7307  0.0937  393 LEU A N   
2824 C CA  . LEU A 366 ? 1.7693 1.5004 1.4351 0.1654  0.7387  0.1045  393 LEU A CA  
2825 C C   . LEU A 366 ? 1.8366 1.5458 1.4842 0.1488  0.7649  0.1191  393 LEU A C   
2826 O O   . LEU A 366 ? 1.7475 1.4536 1.4123 0.1375  0.7581  0.1279  393 LEU A O   
2827 C CB  . LEU A 366 ? 1.7455 1.4509 1.3668 0.1692  0.7045  0.1105  393 LEU A CB  
2828 C CG  . LEU A 366 ? 1.8354 1.4969 1.3745 0.1691  0.7071  0.1199  393 LEU A CG  
2829 C CD1 . LEU A 366 ? 1.8187 1.4711 1.3271 0.1796  0.6759  0.1153  393 LEU A CD1 
2830 C CD2 . LEU A 366 ? 1.9083 1.5390 1.4119 0.1559  0.7106  0.1387  393 LEU A CD2 
2831 N N   . PRO A 367 ? 1.8518 1.5441 1.4642 0.1472  0.7956  0.1221  394 PRO A N   
2832 C CA  . PRO A 367 ? 1.8846 1.5582 1.4835 0.1313  0.8244  0.1359  394 PRO A CA  
2833 C C   . PRO A 367 ? 1.8945 1.5270 1.4419 0.1231  0.8109  0.1543  394 PRO A C   
2834 O O   . PRO A 367 ? 1.8607 1.4605 1.3414 0.1281  0.8015  0.1608  394 PRO A O   
2835 C CB  . PRO A 367 ? 1.7786 1.4395 1.3392 0.1353  0.8559  0.1342  394 PRO A CB  
2836 C CG  . PRO A 367 ? 1.7294 1.4164 1.3107 0.1524  0.8486  0.1160  394 PRO A CG  
2837 C CD  . PRO A 367 ? 1.7219 1.4121 1.3075 0.1600  0.8073  0.1124  394 PRO A CD  
2838 N N   . GLY A 368 ? 1.8009 1.4352 1.3790 0.1106  0.8096  0.1624  395 GLY A N   
2839 C CA  . GLY A 368 ? 1.7940 1.3893 1.3274 0.1029  0.8006  0.1812  395 GLY A CA  
2840 C C   . GLY A 368 ? 1.9118 1.5086 1.4572 0.1061  0.7621  0.1826  395 GLY A C   
2841 O O   . GLY A 368 ? 1.9505 1.5159 1.4606 0.1013  0.7531  0.1984  395 GLY A O   
2842 N N   . TYR A 369 ? 1.8175 1.4493 1.4101 0.1150  0.7395  0.1671  396 TYR A N   
2843 C CA  . TYR A 369 ? 1.7497 1.3833 1.3519 0.1189  0.7030  0.1681  396 TYR A CA  
2844 C C   . TYR A 369 ? 1.8295 1.4625 1.4672 0.1061  0.7041  0.1755  396 TYR A C   
2845 O O   . TYR A 369 ? 1.8231 1.4748 1.5082 0.0955  0.7270  0.1713  396 TYR A O   
2846 C CB  . TYR A 369 ? 1.7544 1.4261 1.4009 0.1313  0.6807  0.1498  396 TYR A CB  
2847 C CG  . TYR A 369 ? 1.7425 1.4213 1.4102 0.1340  0.6460  0.1498  396 TYR A CG  
2848 C CD1 . TYR A 369 ? 1.7793 1.4339 1.3987 0.1399  0.6195  0.1581  396 TYR A CD1 
2849 C CD2 . TYR A 369 ? 1.6663 1.3769 1.4021 0.1303  0.6401  0.1412  396 TYR A CD2 
2850 C CE1 . TYR A 369 ? 1.7644 1.4260 1.4027 0.1430  0.5891  0.1583  396 TYR A CE1 
2851 C CE2 . TYR A 369 ? 1.6920 1.4078 1.4452 0.1331  0.6093  0.1409  396 TYR A CE2 
2852 C CZ  . TYR A 369 ? 1.7320 1.4229 1.4361 0.1399  0.5844  0.1498  396 TYR A CZ  
2853 O OH  . TYR A 369 ? 1.6663 1.3631 1.3874 0.1435  0.5545  0.1495  396 TYR A OH  
2854 N N   . ARG A 370 ? 1.9369 1.5479 1.5508 0.1069  0.6795  0.1862  397 ARG A N   
2855 C CA  . ARG A 370 ? 1.9005 1.5091 1.5467 0.0972  0.6740  0.1919  397 ARG A CA  
2856 C C   . ARG A 370 ? 1.8687 1.4767 1.5104 0.1069  0.6347  0.1923  397 ARG A C   
2857 O O   . ARG A 370 ? 1.8508 1.4456 1.4454 0.1176  0.6160  0.1958  397 ARG A O   
2858 C CB  . ARG A 370 ? 1.8983 1.4657 1.5068 0.0848  0.6965  0.2118  397 ARG A CB  
2859 C CG  . ARG A 370 ? 1.8326 1.4039 1.4586 0.0719  0.7375  0.2112  397 ARG A CG  
2860 C CD  . ARG A 370 ? 2.0873 1.6126 1.6615 0.0618  0.7613  0.2323  397 ARG A CD  
2861 N NE  . ARG A 370 ? 2.1478 1.6777 1.7327 0.0509  0.8017  0.2314  397 ARG A NE  
2862 C CZ  . ARG A 370 ? 2.1372 1.6313 1.6822 0.0408  0.8303  0.2480  397 ARG A CZ  
2863 N NH1 . ARG A 370 ? 2.2172 1.6667 1.7078 0.0407  0.8233  0.2677  397 ARG A NH1 
2864 N NH2 . ARG A 370 ? 2.0005 1.5041 1.5603 0.0313  0.8672  0.2453  397 ARG A NH2 
2865 N N   . ASP A 371 ? 1.9222 1.5459 1.6142 0.1028  0.6226  0.1878  398 ASP A N   
2866 C CA  . ASP A 371 ? 1.8918 1.5175 1.5849 0.1121  0.5863  0.1873  398 ASP A CA  
2867 C C   . ASP A 371 ? 1.9658 1.5491 1.5933 0.1148  0.5759  0.2069  398 ASP A C   
2868 O O   . ASP A 371 ? 2.0000 1.5519 1.6042 0.1053  0.5943  0.2219  398 ASP A O   
2869 C CB  . ASP A 371 ? 1.9232 1.5673 1.6774 0.1052  0.5790  0.1807  398 ASP A CB  
2870 C CG  . ASP A 371 ? 1.9991 1.6412 1.7516 0.1145  0.5434  0.1819  398 ASP A CG  
2871 O OD1 . ASP A 371 ? 2.0332 1.6952 1.7865 0.1276  0.5199  0.1729  398 ASP A OD1 
2872 O OD2 . ASP A 371 ? 2.0534 1.6732 1.8033 0.1088  0.5398  0.1921  398 ASP A OD2 
2873 N N   . PRO A 372 ? 2.0651 1.6465 1.6609 0.1278  0.5476  0.2076  399 PRO A N   
2874 C CA  . PRO A 372 ? 1.9715 1.5163 1.5051 0.1316  0.5362  0.2259  399 PRO A CA  
2875 C C   . PRO A 372 ? 1.9847 1.5110 1.5256 0.1283  0.5282  0.2374  399 PRO A C   
2876 O O   . PRO A 372 ? 1.8380 1.3314 1.3276 0.1312  0.5232  0.2546  399 PRO A O   
2877 C CB  . PRO A 372 ? 1.8118 1.3695 1.3258 0.1454  0.5053  0.2198  399 PRO A CB  
2878 C CG  . PRO A 372 ? 1.8684 1.4583 1.4145 0.1480  0.5104  0.2011  399 PRO A CG  
2879 C CD  . PRO A 372 ? 1.9761 1.5877 1.5867 0.1394  0.5273  0.1920  399 PRO A CD  
2880 N N   . TYR A 373 ? 2.0835 1.6290 1.6848 0.1227  0.5267  0.2282  400 TYR A N   
2881 C CA  . TYR A 373 ? 2.0767 1.6044 1.6874 0.1202  0.5175  0.2370  400 TYR A CA  
2882 C C   . TYR A 373 ? 2.0943 1.6061 1.7274 0.1033  0.5475  0.2418  400 TYR A C   
2883 O O   . TYR A 373 ? 2.1540 1.6257 1.7499 0.0991  0.5581  0.2600  400 TYR A O   
2884 C CB  . TYR A 373 ? 2.1008 1.6597 1.7598 0.1272  0.4888  0.2227  400 TYR A CB  
2885 C CG  . TYR A 373 ? 2.1021 1.6788 1.7433 0.1425  0.4606  0.2169  400 TYR A CG  
2886 C CD1 . TYR A 373 ? 1.9259 1.4808 1.5128 0.1522  0.4424  0.2303  400 TYR A CD1 
2887 C CD2 . TYR A 373 ? 2.2016 1.8172 1.8802 0.1472  0.4524  0.1982  400 TYR A CD2 
2888 C CE1 . TYR A 373 ? 1.9605 1.5325 1.5324 0.1643  0.4174  0.2244  400 TYR A CE1 
2889 C CE2 . TYR A 373 ? 2.2138 1.8431 1.8754 0.1601  0.4281  0.1931  400 TYR A CE2 
2890 C CZ  . TYR A 373 ? 2.2067 1.8144 1.8157 0.1676  0.4110  0.2060  400 TYR A CZ  
2891 O OH  . TYR A 373 ? 2.2193 1.8416 1.8128 0.1785  0.3876  0.2004  400 TYR A OH  
2892 N N   . HIS A 374 ? 2.1507 1.6929 1.8435 0.0933  0.5619  0.2261  401 HIS A N   
2893 C CA  . HIS A 374 ? 2.0892 1.6201 1.8082 0.0750  0.5917  0.2289  401 HIS A CA  
2894 C C   . HIS A 374 ? 2.0532 1.5894 1.7708 0.0656  0.6260  0.2274  401 HIS A C   
2895 O O   . HIS A 374 ? 2.0606 1.5868 1.7966 0.0491  0.6543  0.2307  401 HIS A O   
2896 C CB  . HIS A 374 ? 2.0546 1.6158 1.8463 0.0678  0.5846  0.2124  401 HIS A CB  
2897 C CG  . HIS A 374 ? 2.0915 1.7038 1.9282 0.0763  0.5682  0.1909  401 HIS A CG  
2898 N ND1 . HIS A 374 ? 2.0150 1.6566 1.8702 0.0754  0.5847  0.1799  401 HIS A ND1 
2899 C CD2 . HIS A 374 ? 2.0977 1.7361 1.9639 0.0867  0.5375  0.1788  401 HIS A CD2 
2900 C CE1 . HIS A 374 ? 2.0224 1.7049 1.9155 0.0855  0.5645  0.1624  401 HIS A CE1 
2901 N NE2 . HIS A 374 ? 2.0801 1.7616 1.9803 0.0921  0.5358  0.1615  401 HIS A NE2 
2902 N N   . GLY A 375 ? 2.0775 1.6283 1.7738 0.0753  0.6253  0.2223  402 GLY A N   
2903 C CA  . GLY A 375 ? 1.9884 1.5382 1.6712 0.0688  0.6578  0.2232  402 GLY A CA  
2904 C C   . GLY A 375 ? 1.9119 1.5052 1.6585 0.0618  0.6752  0.2045  402 GLY A C   
2905 O O   . GLY A 375 ? 1.9726 1.5672 1.7118 0.0563  0.7046  0.2047  402 GLY A O   
2906 N N   . ARG A 376 ? 1.8587 1.4888 1.6670 0.0627  0.6581  0.1882  403 ARG A N   
2907 C CA  . ARG A 376 ? 1.7667 1.4417 1.6389 0.0567  0.6734  0.1701  403 ARG A CA  
2908 C C   . ARG A 376 ? 1.7656 1.4667 1.6325 0.0709  0.6718  0.1592  403 ARG A C   
2909 O O   . ARG A 376 ? 1.7291 1.4233 1.5597 0.0861  0.6487  0.1603  403 ARG A O   
2910 C CB  . ARG A 376 ? 1.7894 1.4966 1.7263 0.0549  0.6531  0.1555  403 ARG A CB  
2911 C CG  . ARG A 376 ? 1.8379 1.5215 1.7877 0.0394  0.6566  0.1633  403 ARG A CG  
2912 C CD  . ARG A 376 ? 1.8575 1.5715 1.8651 0.0399  0.6320  0.1478  403 ARG A CD  
2913 N NE  . ARG A 376 ? 1.9675 1.6535 1.9813 0.0268  0.6321  0.1553  403 ARG A NE  
2914 C CZ  . ARG A 376 ? 1.9137 1.6150 1.9690 0.0255  0.6114  0.1446  403 ARG A CZ  
2915 N NH1 . ARG A 376 ? 1.8729 1.6185 1.9678 0.0367  0.5881  0.1265  403 ARG A NH1 
2916 N NH2 . ARG A 376 ? 1.8855 1.5552 1.9409 0.0131  0.6144  0.1524  403 ARG A NH2 
2917 N N   . PRO A 377 ? 1.6981 1.4289 1.6007 0.0662  0.6969  0.1485  404 PRO A N   
2918 C CA  . PRO A 377 ? 1.6054 1.3609 1.5058 0.0809  0.6965  0.1372  404 PRO A CA  
2919 C C   . PRO A 377 ? 1.4945 1.2875 1.4346 0.0949  0.6656  0.1207  404 PRO A C   
2920 O O   . PRO A 377 ? 1.5630 1.3631 1.5305 0.0935  0.6433  0.1180  404 PRO A O   
2921 C CB  . PRO A 377 ? 1.5912 1.3707 1.5273 0.0710  0.7331  0.1303  404 PRO A CB  
2922 C CG  . PRO A 377 ? 1.5595 1.3125 1.4926 0.0503  0.7564  0.1435  404 PRO A CG  
2923 C CD  . PRO A 377 ? 1.6187 1.3565 1.5572 0.0469  0.7303  0.1483  404 PRO A CD  
2924 N N   . LEU A 378 ? 1.6027 1.4182 1.5445 0.1090  0.6647  0.1098  405 LEU A N   
2925 C CA  . LEU A 378 ? 1.6545 1.5052 1.6319 0.1237  0.6375  0.0944  405 LEU A CA  
2926 C C   . LEU A 378 ? 1.6382 1.5312 1.6927 0.1168  0.6366  0.0811  405 LEU A C   
2927 O O   . LEU A 378 ? 1.5811 1.4944 1.6723 0.1060  0.6634  0.0764  405 LEU A O   
2928 C CB  . LEU A 378 ? 1.6323 1.4984 1.6002 0.1390  0.6432  0.0851  405 LEU A CB  
2929 C CG  . LEU A 378 ? 1.5562 1.4548 1.5530 0.1566  0.6169  0.0703  405 LEU A CG  
2930 C CD1 . LEU A 378 ? 1.5820 1.4541 1.5289 0.1672  0.5879  0.0762  405 LEU A CD1 
2931 C CD2 . LEU A 378 ? 1.5336 1.4597 1.5480 0.1682  0.6333  0.0580  405 LEU A CD2 
2932 N N   . THR A 379 ? 1.5584 1.4662 1.6377 0.1230  0.6058  0.0745  406 THR A N   
2933 C CA  . THR A 379 ? 1.5134 1.4616 1.6640 0.1173  0.6003  0.0606  406 THR A CA  
2934 C C   . THR A 379 ? 1.4869 1.4833 1.6787 0.1334  0.5922  0.0426  406 THR A C   
2935 O O   . THR A 379 ? 1.4340 1.4279 1.5967 0.1503  0.5845  0.0413  406 THR A O   
2936 C CB  . THR A 379 ? 1.4330 1.3707 1.5888 0.1151  0.5718  0.0629  406 THR A CB  
2937 O OG1 . THR A 379 ? 1.4263 1.3774 1.5794 0.1341  0.5405  0.0558  406 THR A OG1 
2938 C CG2 . THR A 379 ? 1.2848 1.1682 1.3822 0.1072  0.5732  0.0831  406 THR A CG2 
2939 N N   . LYS A 380 ? 1.3749 1.6554 1.5797 -0.0808 0.7457  0.0056  407 LYS A N   
2940 C CA  . LYS A 380 ? 1.2485 1.6063 1.5259 -0.0569 0.7309  -0.0132 407 LYS A CA  
2941 C C   . LYS A 380 ? 1.2524 1.5793 1.5268 -0.0340 0.6823  -0.0176 407 LYS A C   
2942 O O   . LYS A 380 ? 1.2610 1.6100 1.5506 0.0027  0.6664  -0.0292 407 LYS A O   
2943 C CB  . LYS A 380 ? 1.2225 1.6644 1.5850 -0.0882 0.7436  -0.0196 407 LYS A CB  
2944 C CG  . LYS A 380 ? 1.3640 1.8601 1.7442 -0.1031 0.7831  -0.0194 407 LYS A CG  
2945 C CD  . LYS A 380 ? 1.3220 1.9067 1.7889 -0.1300 0.7819  -0.0273 407 LYS A CD  
2946 C CE  . LYS A 380 ? 1.3979 2.0340 1.8774 -0.1461 0.8132  -0.0243 407 LYS A CE  
2947 N NZ  . LYS A 380 ? 1.3321 2.0536 1.8952 -0.1743 0.8118  -0.0308 407 LYS A NZ  
2948 N N   . GLY A 381 ? 1.2348 1.5086 1.4882 -0.0549 0.6592  -0.0082 408 GLY A N   
2949 C CA  . GLY A 381 ? 1.3235 1.5684 1.5721 -0.0355 0.6152  -0.0117 408 GLY A CA  
2950 C C   . GLY A 381 ? 1.3277 1.5154 1.5137 0.0001  0.6022  -0.0108 408 GLY A C   
2951 O O   . GLY A 381 ? 1.3010 1.4970 1.4994 0.0295  0.5767  -0.0197 408 GLY A O   
2952 N N   . GLU A 382 ? 1.2972 1.4245 1.4134 -0.0031 0.6190  0.0003  409 GLU A N   
2953 C CA  . GLU A 382 ? 1.2944 1.3697 1.3493 0.0292  0.6089  -0.0006 409 GLU A CA  
2954 C C   . GLU A 382 ? 1.3315 1.4532 1.4085 0.0621  0.6191  -0.0154 409 GLU A C   
2955 O O   . GLU A 382 ? 1.2850 1.3822 1.3410 0.0933  0.5977  -0.0224 409 GLU A O   
2956 C CB  . GLU A 382 ? 1.3815 1.3939 1.3595 0.0193  0.6293  0.0132  409 GLU A CB  
2957 C CG  . GLU A 382 ? 1.4778 1.4313 1.4234 -0.0073 0.6165  0.0287  409 GLU A CG  
2958 C CD  . GLU A 382 ? 1.5637 1.4611 1.4361 -0.0186 0.6405  0.0445  409 GLU A CD  
2959 O OE1 . GLU A 382 ? 1.5756 1.4882 1.4276 -0.0109 0.6715  0.0433  409 GLU A OE1 
2960 O OE2 . GLU A 382 ? 1.5945 1.4323 1.4282 -0.0339 0.6282  0.0582  409 GLU A OE2 
2961 N N   . LEU A 383 ? 1.3490 1.5376 1.4694 0.0554  0.6522  -0.0207 410 LEU A N   
2962 C CA  . LEU A 383 ? 1.1602 1.4010 1.3108 0.0883  0.6625  -0.0364 410 LEU A CA  
2963 C C   . LEU A 383 ? 1.1332 1.4056 1.3358 0.1101  0.6279  -0.0467 410 LEU A C   
2964 O O   . LEU A 383 ? 1.1885 1.4480 1.3785 0.1460  0.6138  -0.0556 410 LEU A O   
2965 C CB  . LEU A 383 ? 1.2371 1.5534 1.4346 0.0733  0.7043  -0.0403 410 LEU A CB  
2966 C CG  . LEU A 383 ? 1.2243 1.6244 1.4881 0.1008  0.7127  -0.0582 410 LEU A CG  
2967 C CD1 . LEU A 383 ? 1.2833 1.6594 1.5064 0.1437  0.7163  -0.0686 410 LEU A CD1 
2968 C CD2 . LEU A 383 ? 1.1755 1.6535 1.4901 0.0770  0.7525  -0.0604 410 LEU A CD2 
2969 N N   . GLY A 384 ? 1.0908 1.4021 1.3495 0.0885  0.6135  -0.0456 411 GLY A N   
2970 C CA  . GLY A 384 ? 1.1056 1.4462 1.4098 0.1077  0.5797  -0.0535 411 GLY A CA  
2971 C C   . GLY A 384 ? 1.2215 1.4911 1.4787 0.1234  0.5437  -0.0495 411 GLY A C   
2972 O O   . GLY A 384 ? 1.2138 1.4878 1.4824 0.1534  0.5217  -0.0563 411 GLY A O   
2973 N N   . CYS A 385 ? 1.2720 1.4754 1.4765 0.1033  0.5374  -0.0381 412 CYS A N   
2974 C CA  . CYS A 385 ? 1.2744 1.4115 1.4328 0.1168  0.5055  -0.0347 412 CYS A CA  
2975 C C   . CYS A 385 ? 1.2332 1.3400 1.3516 0.1514  0.5064  -0.0411 412 CYS A C   
2976 O O   . CYS A 385 ? 1.1783 1.2667 1.2928 0.1740  0.4796  -0.0453 412 CYS A O   
2977 C CB  . CYS A 385 ? 1.2282 1.3027 1.3360 0.0913  0.5027  -0.0220 412 CYS A CB  
2978 S SG  . CYS A 385 ? 1.2050 1.2019 1.2571 0.1054  0.4652  -0.0184 412 CYS A SG  
2979 N N   . PHE A 386 ? 1.2762 1.3765 1.3631 0.1551  0.5378  -0.0424 413 PHE A N   
2980 C CA  . PHE A 386 ? 1.3335 1.4080 1.3830 0.1884  0.5413  -0.0516 413 PHE A CA  
2981 C C   . PHE A 386 ? 1.2780 1.4034 1.3791 0.2184  0.5364  -0.0648 413 PHE A C   
2982 O O   . PHE A 386 ? 1.2662 1.3611 1.3472 0.2473  0.5191  -0.0719 413 PHE A O   
2983 C CB  . PHE A 386 ? 1.3410 1.4079 1.3501 0.1852  0.5795  -0.0513 413 PHE A CB  
2984 C CG  . PHE A 386 ? 1.3834 1.4055 1.3350 0.2151  0.5814  -0.0604 413 PHE A CG  
2985 C CD1 . PHE A 386 ? 1.3268 1.3787 1.2995 0.2481  0.5887  -0.0763 413 PHE A CD1 
2986 C CD2 . PHE A 386 ? 1.4891 1.4389 1.3651 0.2110  0.5751  -0.0539 413 PHE A CD2 
2987 C CE1 . PHE A 386 ? 1.3868 1.3941 1.3051 0.2750  0.5901  -0.0868 413 PHE A CE1 
2988 C CE2 . PHE A 386 ? 1.4282 1.3371 1.2503 0.2371  0.5755  -0.0642 413 PHE A CE2 
2989 C CZ  . PHE A 386 ? 1.4538 1.3899 1.2964 0.2683  0.5834  -0.0812 413 PHE A CZ  
2990 N N   . LEU A 387 ? 1.1965 1.3990 1.3650 0.2121  0.5506  -0.0684 414 LEU A N   
2991 C CA  . LEU A 387 ? 1.1189 1.3749 1.3392 0.2431  0.5465  -0.0807 414 LEU A CA  
2992 C C   . LEU A 387 ? 1.0672 1.3112 1.3046 0.2556  0.5054  -0.0793 414 LEU A C   
2993 O O   . LEU A 387 ? 1.0765 1.3180 1.3192 0.2896  0.4930  -0.0871 414 LEU A O   
2994 C CB  . LEU A 387 ? 1.0539 1.4009 1.3456 0.2311  0.5698  -0.0849 414 LEU A CB  
2995 C CG  . LEU A 387 ? 1.1095 1.4835 1.3944 0.2251  0.6153  -0.0888 414 LEU A CG  
2996 C CD1 . LEU A 387 ? 1.0960 1.5643 1.4584 0.2071  0.6359  -0.0925 414 LEU A CD1 
2997 C CD2 . LEU A 387 ? 1.0770 1.4408 1.3368 0.2658  0.6282  -0.1021 414 LEU A CD2 
2998 N N   . SER A 388 ? 1.0827 1.3172 1.3271 0.2287  0.4846  -0.0693 415 SER A N   
2999 C CA  . SER A 388 ? 1.1167 1.3399 1.3737 0.2380  0.4470  -0.0669 415 SER A CA  
3000 C C   . SER A 388 ? 1.1046 1.2525 1.3034 0.2576  0.4285  -0.0662 415 SER A C   
3001 O O   . SER A 388 ? 1.1927 1.3347 1.3994 0.2835  0.4083  -0.0694 415 SER A O   
3002 C CB  . SER A 388 ? 1.0668 1.2926 1.3374 0.2040  0.4314  -0.0579 415 SER A CB  
3003 O OG  . SER A 388 ? 1.1128 1.4109 1.4427 0.1854  0.4448  -0.0604 415 SER A OG  
3004 N N   . HIS A 389 ? 1.0601 1.1489 1.1995 0.2451  0.4343  -0.0619 416 HIS A N   
3005 C CA  . HIS A 389 ? 1.1381 1.1582 1.2219 0.2625  0.4189  -0.0636 416 HIS A CA  
3006 C C   . HIS A 389 ? 1.2498 1.2695 1.3262 0.2972  0.4309  -0.0763 416 HIS A C   
3007 O O   . HIS A 389 ? 1.2108 1.1983 1.2742 0.3199  0.4109  -0.0804 416 HIS A O   
3008 C CB  . HIS A 389 ? 1.0316 0.9958 1.0544 0.2438  0.4247  -0.0577 416 HIS A CB  
3009 C CG  . HIS A 389 ? 1.1306 1.0786 1.1510 0.2156  0.4068  -0.0464 416 HIS A CG  
3010 N ND1 . HIS A 389 ? 1.1438 1.0498 1.1437 0.2156  0.3762  -0.0431 416 HIS A ND1 
3011 C CD2 . HIS A 389 ? 1.2053 1.1724 1.2413 0.1865  0.4160  -0.0387 416 HIS A CD2 
3012 C CE1 . HIS A 389 ? 1.0902 0.9923 1.0937 0.1901  0.3673  -0.0345 416 HIS A CE1 
3013 N NE2 . HIS A 389 ? 1.2320 1.1678 1.2561 0.1722  0.3905  -0.0317 416 HIS A NE2 
3014 N N   . TYR A 390 ? 1.1868 1.2411 1.2711 0.3013  0.4644  -0.0829 417 TYR A N   
3015 C CA  . TYR A 390 ? 1.1581 1.2171 1.2381 0.3361  0.4788  -0.0972 417 TYR A CA  
3016 C C   . TYR A 390 ? 1.1883 1.2800 1.3185 0.3635  0.4611  -0.1023 417 TYR A C   
3017 O O   . TYR A 390 ? 1.1584 1.2167 1.2698 0.3940  0.4516  -0.1108 417 TYR A O   
3018 C CB  . TYR A 390 ? 1.2913 1.3974 1.3829 0.3329  0.5201  -0.1030 417 TYR A CB  
3019 C CG  . TYR A 390 ? 1.3757 1.4926 1.4638 0.3694  0.5398  -0.1199 417 TYR A CG  
3020 C CD1 . TYR A 390 ? 1.5339 1.5935 1.5546 0.3823  0.5502  -0.1280 417 TYR A CD1 
3021 C CD2 . TYR A 390 ? 1.4067 1.5925 1.5588 0.3920  0.5479  -0.1290 417 TYR A CD2 
3022 C CE1 . TYR A 390 ? 1.5702 1.6387 1.5864 0.4140  0.5654  -0.1455 417 TYR A CE1 
3023 C CE2 . TYR A 390 ? 1.4229 1.6191 1.5728 0.4245  0.5619  -0.1459 417 TYR A CE2 
3024 C CZ  . TYR A 390 ? 1.5161 1.6526 1.5976 0.4323  0.5673  -0.1544 417 TYR A CZ  
3025 O OH  . TYR A 390 ? 1.4428 1.5887 1.5218 0.4586  0.5738  -0.1730 417 TYR A OH  
3026 N N   . ASN A 391 ? 1.1261 1.2807 1.3185 0.3531  0.4552  -0.0972 418 ASN A N   
3027 C CA  . ASN A 391 ? 1.0989 1.2875 1.3387 0.3798  0.4365  -0.1002 418 ASN A CA  
3028 C C   . ASN A 391 ? 1.1241 1.2529 1.3368 0.3881  0.4006  -0.0938 418 ASN A C   
3029 O O   . ASN A 391 ? 1.2649 1.3853 1.4857 0.4199  0.3870  -0.0980 418 ASN A O   
3030 C CB  . ASN A 391 ? 1.0877 1.3561 1.3964 0.3634  0.4350  -0.0961 418 ASN A CB  
3031 C CG  . ASN A 391 ? 1.1279 1.4654 1.4742 0.3578  0.4711  -0.1039 418 ASN A CG  
3032 O OD1 . ASN A 391 ? 1.0203 1.3589 1.3530 0.3781  0.4963  -0.1145 418 ASN A OD1 
3033 N ND2 . ASN A 391 ? 1.1361 1.5326 1.5302 0.3294  0.4745  -0.0997 418 ASN A ND2 
3034 N N   . ILE A 392 ? 1.0445 1.1311 1.2254 0.3601  0.3852  -0.0835 419 ILE A N   
3035 C CA  . ILE A 392 ? 1.1479 1.1775 1.3007 0.3646  0.3536  -0.0775 419 ILE A CA  
3036 C C   . ILE A 392 ? 1.1230 1.0877 1.2236 0.3868  0.3546  -0.0862 419 ILE A C   
3037 O O   . ILE A 392 ? 1.1557 1.0855 1.2470 0.4063  0.3341  -0.0863 419 ILE A O   
3038 C CB  . ILE A 392 ? 1.1447 1.1499 1.2781 0.3297  0.3393  -0.0663 419 ILE A CB  
3039 C CG1 . ILE A 392 ? 1.0574 1.1239 1.2432 0.3094  0.3349  -0.0597 419 ILE A CG1 
3040 C CG2 . ILE A 392 ? 1.0569 1.0033 1.1585 0.3326  0.3100  -0.0610 419 ILE A CG2 
3041 C CD1 . ILE A 392 ? 1.1229 1.1666 1.2935 0.2788  0.3185  -0.0501 419 ILE A CD1 
3042 N N   . TRP A 393 ? 1.1763 1.1220 1.2401 0.3836  0.3785  -0.0936 420 TRP A N   
3043 C CA  . TRP A 393 ? 1.2158 1.1027 1.2287 0.4051  0.3810  -0.1051 420 TRP A CA  
3044 C C   . TRP A 393 ? 1.3516 1.2523 1.3876 0.4443  0.3847  -0.1165 420 TRP A C   
3045 O O   . TRP A 393 ? 1.3472 1.1941 1.3552 0.4649  0.3701  -0.1225 420 TRP A O   
3046 C CB  . TRP A 393 ? 1.2158 1.0899 1.1869 0.3959  0.4087  -0.1113 420 TRP A CB  
3047 C CG  . TRP A 393 ? 1.2056 1.0630 1.1512 0.3603  0.4061  -0.0996 420 TRP A CG  
3048 C CD1 . TRP A 393 ? 1.0918 0.9290 1.0361 0.3395  0.3794  -0.0877 420 TRP A CD1 
3049 C CD2 . TRP A 393 ? 1.3490 1.2075 1.2656 0.3429  0.4316  -0.0982 420 TRP A CD2 
3050 N NE1 . TRP A 393 ? 1.0581 0.8830 0.9760 0.3121  0.3856  -0.0800 420 TRP A NE1 
3051 C CE2 . TRP A 393 ? 1.2402 1.0756 1.1392 0.3132  0.4170  -0.0851 420 TRP A CE2 
3052 C CE3 . TRP A 393 ? 1.2162 1.0923 1.1184 0.3499  0.4661  -0.1064 420 TRP A CE3 
3053 C CZ2 . TRP A 393 ? 1.1608 0.9860 1.0273 0.2914  0.4342  -0.0787 420 TRP A CZ2 
3054 C CZ3 . TRP A 393 ? 1.2220 1.0891 1.0902 0.3260  0.4845  -0.0992 420 TRP A CZ3 
3055 C CH2 . TRP A 393 ? 1.2971 1.1369 1.1471 0.2975  0.4678  -0.0849 420 TRP A CH2 
3056 N N   . LYS A 394 ? 1.2793 1.2518 1.3673 0.4552  0.4038  -0.1203 421 LYS A N   
3057 C CA  . LYS A 394 ? 1.2128 1.2056 1.3296 0.4956  0.4062  -0.1311 421 LYS A CA  
3058 C C   . LYS A 394 ? 1.2719 1.2488 1.4071 0.5088  0.3721  -0.1223 421 LYS A C   
3059 O O   . LYS A 394 ? 1.3544 1.2942 1.4771 0.5362  0.3596  -0.1290 421 LYS A O   
3060 C CB  . LYS A 394 ? 1.2857 1.3694 1.4629 0.5015  0.4314  -0.1359 421 LYS A CB  
3061 C CG  . LYS A 394 ? 1.4095 1.5174 1.5739 0.4810  0.4668  -0.1403 421 LYS A CG  
3062 C CD  . LYS A 394 ? 1.3188 1.5220 1.5516 0.4707  0.4854  -0.1391 421 LYS A CD  
3063 C CE  . LYS A 394 ? 1.2271 1.4846 1.5034 0.4994  0.4906  -0.1546 421 LYS A CE  
3064 N NZ  . LYS A 394 ? 1.4516 1.6949 1.6924 0.5070  0.5139  -0.1707 421 LYS A NZ  
3065 N N   . GLU A 395 ? 1.2205 1.2238 1.3836 0.4848  0.3539  -0.1071 422 GLU A N   
3066 C CA  . GLU A 395 ? 1.2080 1.2003 1.3872 0.4953  0.3224  -0.0967 422 GLU A CA  
3067 C C   . GLU A 395 ? 1.2171 1.1211 1.3413 0.4942  0.3014  -0.0932 422 GLU A C   
3068 O O   . GLU A 395 ? 1.2551 1.1308 1.3795 0.5150  0.2810  -0.0890 422 GLU A O   
3069 C CB  . GLU A 395 ? 1.1750 1.2163 1.3917 0.4674  0.3093  -0.0828 422 GLU A CB  
3070 C CG  . GLU A 395 ? 1.1127 1.1521 1.3474 0.4775  0.2780  -0.0708 422 GLU A CG  
3071 C CD  . GLU A 395 ? 1.2059 1.2957 1.4751 0.4500  0.2659  -0.0597 422 GLU A CD  
3072 O OE1 . GLU A 395 ? 1.2066 1.3486 1.5020 0.4295  0.2835  -0.0632 422 GLU A OE1 
3073 O OE2 . GLU A 395 ? 1.1304 1.2060 1.3988 0.4480  0.2394  -0.0476 422 GLU A OE2 
3074 N N   . VAL A 396 ? 1.1986 1.0585 1.2758 0.4699  0.3056  -0.0945 423 VAL A N   
3075 C CA  . VAL A 396 ? 1.3095 1.0888 1.3358 0.4676  0.2870  -0.0940 423 VAL A CA  
3076 C C   . VAL A 396 ? 1.3920 1.1275 1.3950 0.5028  0.2914  -0.1086 423 VAL A C   
3077 O O   . VAL A 396 ? 1.4519 1.1364 1.4388 0.5139  0.2704  -0.1062 423 VAL A O   
3078 C CB  . VAL A 396 ? 1.2500 0.9983 1.2332 0.4365  0.2910  -0.0942 423 VAL A CB  
3079 C CG1 . VAL A 396 ? 1.3910 1.0592 1.3211 0.4373  0.2756  -0.0990 423 VAL A CG1 
3080 C CG2 . VAL A 396 ? 1.2598 1.0364 1.2621 0.4035  0.2801  -0.0791 423 VAL A CG2 
3081 N N   . VAL A 397 ? 1.3732 1.1295 1.3745 0.5166  0.3170  -0.1240 424 VAL A N   
3082 C CA  . VAL A 397 ? 1.4364 1.1620 1.4203 0.5383  0.3147  -0.1396 424 VAL A CA  
3083 C C   . VAL A 397 ? 1.3197 1.0729 1.3490 0.5655  0.3031  -0.1380 424 VAL A C   
3084 O O   . VAL A 397 ? 1.3523 1.0590 1.3676 0.5809  0.2865  -0.1422 424 VAL A O   
3085 C CB  . VAL A 397 ? 1.3582 1.1036 1.3272 0.5408  0.3443  -0.1564 424 VAL A CB  
3086 C CG1 . VAL A 397 ? 1.3327 1.0488 1.2861 0.5647  0.3430  -0.1744 424 VAL A CG1 
3087 C CG2 . VAL A 397 ? 1.3578 1.0694 1.2755 0.5149  0.3529  -0.1563 424 VAL A CG2 
3088 N N   . ASP A 398 ? 1.3348 1.1638 1.4196 0.5710  0.3110  -0.1317 425 ASP A N   
3089 C CA  . ASP A 398 ? 1.2643 1.1263 1.3947 0.5981  0.2990  -0.1302 425 ASP A CA  
3090 C C   . ASP A 398 ? 1.2788 1.0954 1.4018 0.6009  0.2666  -0.1142 425 ASP A C   
3091 O O   . ASP A 398 ? 1.3145 1.1033 1.4386 0.6230  0.2514  -0.1157 425 ASP A O   
3092 C CB  . ASP A 398 ? 1.2572 1.2149 1.4500 0.5988  0.3120  -0.1266 425 ASP A CB  
3093 C CG  . ASP A 398 ? 1.5300 1.5308 1.7726 0.6291  0.3020  -0.1288 425 ASP A CG  
3094 O OD1 . ASP A 398 ? 1.7967 1.7557 2.0250 0.6518  0.2927  -0.1366 425 ASP A OD1 
3095 O OD2 . ASP A 398 ? 1.6226 1.6993 1.9197 0.6296  0.3029  -0.1230 425 ASP A OD2 
3096 N N   . ARG A 399 ? 1.2843 1.0917 1.3989 0.5782  0.2566  -0.0983 426 ARG A N   
3097 C CA  . ARG A 399 ? 1.2878 1.0528 1.3920 0.5769  0.2276  -0.0815 426 ARG A CA  
3098 C C   . ARG A 399 ? 1.3677 1.0429 1.4146 0.5645  0.2156  -0.0833 426 ARG A C   
3099 O O   . ARG A 399 ? 1.3757 1.0088 1.4100 0.5615  0.1925  -0.0699 426 ARG A O   
3100 C CB  . ARG A 399 ? 1.2184 1.0197 1.3424 0.5531  0.2200  -0.0643 426 ARG A CB  
3101 C CG  . ARG A 399 ? 1.0859 0.9755 1.2710 0.5614  0.2207  -0.0594 426 ARG A CG  
3102 C CD  . ARG A 399 ? 1.1620 1.0896 1.3628 0.5232  0.2117  -0.0468 426 ARG A CD  
3103 N NE  . ARG A 399 ? 1.1885 1.0707 1.3649 0.5091  0.1853  -0.0306 426 ARG A NE  
3104 C CZ  . ARG A 399 ? 1.3386 1.2290 1.5112 0.4739  0.1763  -0.0210 426 ARG A CZ  
3105 N NH1 . ARG A 399 ? 1.2240 1.1596 1.4131 0.4484  0.1900  -0.0254 426 ARG A NH1 
3106 N NH2 . ARG A 399 ? 1.3967 1.2474 1.5475 0.4639  0.1539  -0.0068 426 ARG A NH2 
3107 N N   . GLY A 400 ? 1.3400 0.9869 1.3520 0.5561  0.2302  -0.0993 427 GLY A N   
3108 C CA  . GLY A 400 ? 1.3351 0.9023 1.2954 0.5426  0.2178  -0.1031 427 GLY A CA  
3109 C C   . GLY A 400 ? 1.4674 1.0074 1.4074 0.5138  0.2049  -0.0892 427 GLY A C   
3110 O O   . GLY A 400 ? 1.5172 0.9992 1.4314 0.5043  0.1851  -0.0839 427 GLY A O   
3111 N N   . LEU A 401 ? 1.3434 0.9254 1.2964 0.4981  0.2162  -0.0834 428 LEU A N   
3112 C CA  . LEU A 401 ? 1.3615 0.9341 1.3039 0.4615  0.2005  -0.0703 428 LEU A CA  
3113 C C   . LEU A 401 ? 1.4118 0.9311 1.3043 0.4434  0.2014  -0.0807 428 LEU A C   
3114 O O   . LEU A 401 ? 1.4056 0.9360 1.2835 0.4399  0.2200  -0.0921 428 LEU A O   
3115 C CB  . LEU A 401 ? 1.3036 0.9484 1.2819 0.4411  0.2071  -0.0619 428 LEU A CB  
3116 C CG  . LEU A 401 ? 1.3360 1.0447 1.3671 0.4586  0.2077  -0.0550 428 LEU A CG  
3117 C CD1 . LEU A 401 ? 1.2758 1.0524 1.3399 0.4349  0.2154  -0.0499 428 LEU A CD1 
3118 C CD2 . LEU A 401 ? 1.2309 0.9212 1.2694 0.4669  0.1828  -0.0402 428 LEU A CD2 
3119 N N   . GLN A 402 ? 1.4205 0.8830 1.2863 0.4315  0.1813  -0.0764 429 GLN A N   
3120 C CA  . GLN A 402 ? 1.3448 0.7572 1.1648 0.4145  0.1785  -0.0873 429 GLN A CA  
3121 C C   . GLN A 402 ? 1.3519 0.7948 1.1701 0.3841  0.1811  -0.0832 429 GLN A C   
3122 O O   . GLN A 402 ? 1.4305 0.8694 1.2231 0.3802  0.1938  -0.0948 429 GLN A O   
3123 C CB  . GLN A 402 ? 1.4001 0.7503 1.1985 0.4059  0.1560  -0.0830 429 GLN A CB  
3124 C CG  . GLN A 402 ? 1.3152 0.6346 1.1131 0.4254  0.1487  -0.0877 429 GLN A CG  
3125 C CD  . GLN A 402 ? 1.7223 1.0252 1.4974 0.4372  0.1598  -0.1100 429 GLN A CD  
3126 O OE1 . GLN A 402 ? 1.5648 0.8610 1.3120 0.4254  0.1672  -0.1220 429 GLN A OE1 
3127 N NE2 . GLN A 402 ? 1.8359 1.1316 1.6214 0.4616  0.1606  -0.1158 429 GLN A NE2 
3128 N N   . LYS A 403 ? 1.3541 0.8257 1.1967 0.3634  0.1691  -0.0669 430 LYS A N   
3129 C CA  . LYS A 403 ? 1.2399 0.7406 1.0843 0.3365  0.1705  -0.0625 430 LYS A CA  
3130 C C   . LYS A 403 ? 1.2150 0.7797 1.1047 0.3317  0.1738  -0.0499 430 LYS A C   
3131 O O   . LYS A 403 ? 1.0471 0.6241 0.9608 0.3337  0.1613  -0.0384 430 LYS A O   
3132 C CB  . LYS A 403 ? 1.0923 0.5606 0.9166 0.3112  0.1506  -0.0583 430 LYS A CB  
3133 C CG  . LYS A 403 ? 1.2056 0.6596 1.0426 0.3073  0.1320  -0.0460 430 LYS A CG  
3134 C CD  . LYS A 403 ? 1.2938 0.7308 1.1181 0.2787  0.1157  -0.0418 430 LYS A CD  
3135 C CE  . LYS A 403 ? 1.4465 0.8671 1.2797 0.2725  0.0995  -0.0287 430 LYS A CE  
3136 N NZ  . LYS A 403 ? 1.4978 0.9152 1.3265 0.2432  0.0860  -0.0240 430 LYS A NZ  
3137 N N   . SER A 404 ? 1.2135 0.8172 1.1128 0.3246  0.1902  -0.0521 431 SER A N   
3138 C CA  . SER A 404 ? 0.9588 0.6241 0.9007 0.3170  0.1947  -0.0430 431 SER A CA  
3139 C C   . SER A 404 ? 1.0329 0.7125 0.9686 0.2910  0.1994  -0.0412 431 SER A C   
3140 O O   . SER A 404 ? 1.0963 0.7534 1.0000 0.2871  0.2094  -0.0486 431 SER A O   
3141 C CB  . SER A 404 ? 1.0043 0.7114 0.9747 0.3388  0.2142  -0.0482 431 SER A CB  
3142 O OG  . SER A 404 ? 1.1691 0.8559 1.1400 0.3675  0.2110  -0.0520 431 SER A OG  
3143 N N   . LEU A 405 ? 1.0262 0.7412 0.9902 0.2743  0.1916  -0.0315 432 LEU A N   
3144 C CA  . LEU A 405 ? 0.9217 0.6504 0.8840 0.2504  0.1945  -0.0291 432 LEU A CA  
3145 C C   . LEU A 405 ? 0.9428 0.7277 0.9422 0.2466  0.2099  -0.0278 432 LEU A C   
3146 O O   . LEU A 405 ? 0.9232 0.7471 0.9600 0.2523  0.2059  -0.0239 432 LEU A O   
3147 C CB  . LEU A 405 ? 0.9587 0.6818 0.9227 0.2322  0.1734  -0.0215 432 LEU A CB  
3148 C CG  . LEU A 405 ? 0.9184 0.6635 0.8914 0.2095  0.1734  -0.0183 432 LEU A CG  
3149 C CD1 . LEU A 405 ? 0.9160 0.6314 0.8539 0.2014  0.1803  -0.0228 432 LEU A CD1 
3150 C CD2 . LEU A 405 ? 0.8658 0.6126 0.8465 0.1969  0.1533  -0.0119 432 LEU A CD2 
3151 N N   . VAL A 406 ? 0.9342 0.7229 0.9226 0.2362  0.2272  -0.0306 433 VAL A N   
3152 C CA  . VAL A 406 ? 0.9727 0.8115 0.9940 0.2294  0.2454  -0.0304 433 VAL A CA  
3153 C C   . VAL A 406 ? 0.8513 0.6961 0.8745 0.2025  0.2425  -0.0253 433 VAL A C   
3154 O O   . VAL A 406 ? 0.8623 0.6689 0.8492 0.1925  0.2404  -0.0245 433 VAL A O   
3155 C CB  . VAL A 406 ? 0.9637 0.8027 0.9709 0.2392  0.2721  -0.0373 433 VAL A CB  
3156 C CG1 . VAL A 406 ? 0.9052 0.8014 0.9522 0.2301  0.2922  -0.0370 433 VAL A CG1 
3157 C CG2 . VAL A 406 ? 0.8956 0.7215 0.8964 0.2682  0.2740  -0.0447 433 VAL A CG2 
3158 N N   . PHE A 407 ? 0.8822 0.7743 0.9473 0.1918  0.2416  -0.0228 434 PHE A N   
3159 C CA  . PHE A 407 ? 0.8798 0.7800 0.9517 0.1668  0.2390  -0.0196 434 PHE A CA  
3160 C C   . PHE A 407 ? 0.9039 0.8429 1.0023 0.1549  0.2610  -0.0212 434 PHE A C   
3161 O O   . PHE A 407 ? 0.8911 0.8711 1.0207 0.1650  0.2727  -0.0246 434 PHE A O   
3162 C CB  . PHE A 407 ? 0.8981 0.8200 0.9956 0.1604  0.2172  -0.0169 434 PHE A CB  
3163 C CG  . PHE A 407 ? 0.9107 0.7941 0.9813 0.1611  0.1966  -0.0140 434 PHE A CG  
3164 C CD1 . PHE A 407 ? 0.9959 0.8316 1.0255 0.1584  0.1959  -0.0144 434 PHE A CD1 
3165 C CD2 . PHE A 407 ? 0.9653 0.8626 1.0518 0.1637  0.1779  -0.0106 434 PHE A CD2 
3166 C CE1 . PHE A 407 ? 1.1023 0.9088 1.1122 0.1575  0.1771  -0.0129 434 PHE A CE1 
3167 C CE2 . PHE A 407 ? 0.9237 0.7890 0.9875 0.1619  0.1611  -0.0078 434 PHE A CE2 
3168 C CZ  . PHE A 407 ? 1.0719 0.8937 1.0999 0.1583  0.1608  -0.0096 434 PHE A CZ  
3169 N N   . GLU A 408 ? 0.8928 0.8186 0.9796 0.1332  0.2666  -0.0188 435 GLU A N   
3170 C CA  . GLU A 408 ? 0.9561 0.9180 1.0723 0.1143  0.2835  -0.0194 435 GLU A CA  
3171 C C   . GLU A 408 ? 0.9466 0.9327 1.0929 0.0977  0.2668  -0.0201 435 GLU A C   
3172 O O   . GLU A 408 ? 1.0221 0.9972 1.1637 0.1019  0.2443  -0.0195 435 GLU A O   
3173 C CB  . GLU A 408 ? 0.9803 0.9074 1.0614 0.1007  0.3024  -0.0154 435 GLU A CB  
3174 C CG  . GLU A 408 ? 1.1302 1.0476 1.1877 0.1149  0.3247  -0.0163 435 GLU A CG  
3175 C CD  . GLU A 408 ? 1.2378 1.1253 1.2602 0.1001  0.3459  -0.0105 435 GLU A CD  
3176 O OE1 . GLU A 408 ? 1.3305 1.1961 1.3426 0.0806  0.3408  -0.0052 435 GLU A OE1 
3177 O OE2 . GLU A 408 ? 1.1056 0.9898 1.1085 0.1088  0.3679  -0.0112 435 GLU A OE2 
3178 N N   . ASP A 409 ? 0.9460 0.9659 1.1231 0.0777  0.2786  -0.0223 436 ASP A N   
3179 C CA  . ASP A 409 ? 1.0089 1.0625 1.2212 0.0630  0.2641  -0.0263 436 ASP A CA  
3180 C C   . ASP A 409 ? 1.0168 1.0394 1.2131 0.0398  0.2605  -0.0258 436 ASP A C   
3181 O O   . ASP A 409 ? 1.1018 1.1518 1.3274 0.0225  0.2546  -0.0312 436 ASP A O   
3182 C CB  . ASP A 409 ? 0.8317 0.9511 1.0967 0.0561  0.2758  -0.0319 436 ASP A CB  
3183 C CG  . ASP A 409 ? 0.9694 1.0922 1.2366 0.0396  0.3053  -0.0313 436 ASP A CG  
3184 O OD1 . ASP A 409 ? 1.0704 1.1411 1.2941 0.0348  0.3163  -0.0252 436 ASP A OD1 
3185 O OD2 . ASP A 409 ? 1.1268 1.3061 1.4394 0.0309  0.3175  -0.0366 436 ASP A OD2 
3186 N N   . ASP A 410 ? 1.0162 0.9818 1.1663 0.0402  0.2626  -0.0203 437 ASP A N   
3187 C CA  . ASP A 410 ? 1.0335 0.9656 1.1667 0.0213  0.2598  -0.0194 437 ASP A CA  
3188 C C   . ASP A 410 ? 1.0838 0.9591 1.1688 0.0320  0.2484  -0.0146 437 ASP A C   
3189 O O   . ASP A 410 ? 1.1986 1.0311 1.2484 0.0279  0.2574  -0.0090 437 ASP A O   
3190 C CB  . ASP A 410 ? 1.0969 1.0246 1.2307 0.0012  0.2847  -0.0165 437 ASP A CB  
3191 C CG  . ASP A 410 ? 1.3045 1.2073 1.4049 0.0106  0.3052  -0.0091 437 ASP A CG  
3192 O OD1 . ASP A 410 ? 1.2514 1.1496 1.3364 0.0335  0.3008  -0.0087 437 ASP A OD1 
3193 O OD2 . ASP A 410 ? 1.5259 1.4115 1.6131 -0.0055 0.3259  -0.0036 437 ASP A OD2 
3194 N N   . LEU A 411 ? 0.8933 0.7680 0.9756 0.0456  0.2275  -0.0166 438 LEU A N   
3195 C CA  . LEU A 411 ? 1.0683 0.8970 1.1101 0.0563  0.2158  -0.0135 438 LEU A CA  
3196 C C   . LEU A 411 ? 1.0513 0.8803 1.0986 0.0550  0.1933  -0.0175 438 LEU A C   
3197 O O   . LEU A 411 ? 1.0766 0.9424 1.1540 0.0537  0.1840  -0.0216 438 LEU A O   
3198 C CB  . LEU A 411 ? 1.0271 0.8481 1.0520 0.0766  0.2163  -0.0117 438 LEU A CB  
3199 C CG  . LEU A 411 ? 0.8645 0.7244 0.9192 0.0884  0.2120  -0.0140 438 LEU A CG  
3200 C CD1 . LEU A 411 ? 1.1923 1.0498 1.2470 0.0945  0.1889  -0.0147 438 LEU A CD1 
3201 C CD2 . LEU A 411 ? 0.8360 0.6895 0.8771 0.1052  0.2248  -0.0132 438 LEU A CD2 
3202 N N   . ARG A 412 ? 0.8696 0.6587 0.8864 0.0561  0.1848  -0.0163 439 ARG A N   
3203 C CA  . ARG A 412 ? 0.8298 0.6164 0.8483 0.0555  0.1655  -0.0208 439 ARG A CA  
3204 C C   . ARG A 412 ? 0.8144 0.5892 0.8157 0.0701  0.1522  -0.0196 439 ARG A C   
3205 O O   . ARG A 412 ? 0.9260 0.6685 0.8961 0.0785  0.1537  -0.0162 439 ARG A O   
3206 C CB  . ARG A 412 ? 0.8238 0.5760 0.8234 0.0482  0.1642  -0.0214 439 ARG A CB  
3207 C CG  . ARG A 412 ? 1.0392 0.7811 1.0319 0.0531  0.1449  -0.0261 439 ARG A CG  
3208 C CD  . ARG A 412 ? 1.0556 0.7547 1.0215 0.0528  0.1437  -0.0248 439 ARG A CD  
3209 N NE  . ARG A 412 ? 1.1582 0.8531 1.1354 0.0381  0.1517  -0.0274 439 ARG A NE  
3210 C CZ  . ARG A 412 ? 1.2422 0.9205 1.2180 0.0354  0.1434  -0.0334 439 ARG A CZ  
3211 N NH1 . ARG A 412 ? 0.9323 0.6004 0.8976 0.0474  0.1272  -0.0371 439 ARG A NH1 
3212 N NH2 . ARG A 412 ? 1.4143 1.0864 1.4007 0.0202  0.1516  -0.0366 439 ARG A NH2 
3213 N N   . PHE A 413 ? 0.8870 0.6873 0.9069 0.0718  0.1392  -0.0223 440 PHE A N   
3214 C CA  . PHE A 413 ? 0.6626 0.4539 0.6699 0.0824  0.1275  -0.0207 440 PHE A CA  
3215 C C   . PHE A 413 ? 0.6875 0.4583 0.6789 0.0820  0.1143  -0.0238 440 PHE A C   
3216 O O   . PHE A 413 ? 0.7110 0.4917 0.7135 0.0748  0.1087  -0.0286 440 PHE A O   
3217 C CB  . PHE A 413 ? 0.6384 0.4639 0.6700 0.0839  0.1203  -0.0201 440 PHE A CB  
3218 C CG  . PHE A 413 ? 0.8956 0.7406 0.9417 0.0903  0.1299  -0.0168 440 PHE A CG  
3219 C CD1 . PHE A 413 ? 0.8292 0.6591 0.8622 0.1037  0.1310  -0.0131 440 PHE A CD1 
3220 C CD2 . PHE A 413 ? 0.8248 0.7045 0.8992 0.0835  0.1370  -0.0188 440 PHE A CD2 
3221 C CE1 . PHE A 413 ? 0.9504 0.7992 0.9983 0.1128  0.1397  -0.0111 440 PHE A CE1 
3222 C CE2 . PHE A 413 ? 0.7524 0.6560 0.8444 0.0913  0.1451  -0.0166 440 PHE A CE2 
3223 C CZ  . PHE A 413 ? 0.9817 0.8697 1.0604 0.1073  0.1467  -0.0126 440 PHE A CZ  
3224 N N   . GLU A 414 ? 0.6787 0.4226 0.6449 0.0904  0.1088  -0.0224 441 GLU A N   
3225 C CA  . GLU A 414 ? 0.7535 0.4851 0.7090 0.0913  0.0943  -0.0261 441 GLU A CA  
3226 C C   . GLU A 414 ? 0.8254 0.5836 0.8005 0.0880  0.0831  -0.0281 441 GLU A C   
3227 O O   . GLU A 414 ? 0.8058 0.5839 0.7954 0.0874  0.0849  -0.0248 441 GLU A O   
3228 C CB  . GLU A 414 ? 0.7885 0.4870 0.7123 0.1001  0.0902  -0.0252 441 GLU A CB  
3229 C CG  . GLU A 414 ? 1.0042 0.6715 0.9006 0.1032  0.0950  -0.0237 441 GLU A CG  
3230 C CD  . GLU A 414 ? 1.1120 0.7736 1.0076 0.1024  0.0840  -0.0275 441 GLU A CD  
3231 O OE1 . GLU A 414 ? 1.2138 0.8950 1.1266 0.1009  0.0714  -0.0328 441 GLU A OE1 
3232 O OE2 . GLU A 414 ? 1.0016 0.6385 0.8787 0.1038  0.0885  -0.0248 441 GLU A OE2 
3233 N N   . ILE A 415 ? 0.7220 0.4809 0.6967 0.0866  0.0715  -0.0331 442 ILE A N   
3234 C CA  . ILE A 415 ? 0.7690 0.5535 0.7600 0.0819  0.0624  -0.0348 442 ILE A CA  
3235 C C   . ILE A 415 ? 0.7881 0.5629 0.7700 0.0841  0.0579  -0.0305 442 ILE A C   
3236 O O   . ILE A 415 ? 0.7746 0.5211 0.7352 0.0898  0.0562  -0.0306 442 ILE A O   
3237 C CB  . ILE A 415 ? 0.7441 0.5347 0.7389 0.0807  0.0528  -0.0428 442 ILE A CB  
3238 C CG1 . ILE A 415 ? 0.7390 0.5626 0.7526 0.0737  0.0470  -0.0450 442 ILE A CG1 
3239 C CG2 . ILE A 415 ? 0.6445 0.4091 0.6189 0.0875  0.0444  -0.0448 442 ILE A CG2 
3240 C CD1 . ILE A 415 ? 0.5990 0.4366 0.6214 0.0735  0.0398  -0.0548 442 ILE A CD1 
3241 N N   . PHE A 416 ? 0.7670 0.5627 0.7627 0.0792  0.0557  -0.0266 443 PHE A N   
3242 C CA  . PHE A 416 ? 0.7787 0.5625 0.7669 0.0794  0.0514  -0.0216 443 PHE A CA  
3243 C C   . PHE A 416 ? 0.8523 0.6101 0.8255 0.0890  0.0584  -0.0179 443 PHE A C   
3244 O O   . PHE A 416 ? 0.8627 0.5954 0.8200 0.0917  0.0545  -0.0178 443 PHE A O   
3245 C CB  . PHE A 416 ? 0.7188 0.4924 0.6990 0.0756  0.0406  -0.0267 443 PHE A CB  
3246 C CG  . PHE A 416 ? 0.8524 0.6539 0.8485 0.0685  0.0350  -0.0324 443 PHE A CG  
3247 C CD1 . PHE A 416 ? 0.7421 0.5750 0.7558 0.0613  0.0369  -0.0300 443 PHE A CD1 
3248 C CD2 . PHE A 416 ? 0.7730 0.5704 0.7654 0.0706  0.0276  -0.0409 443 PHE A CD2 
3249 C CE1 . PHE A 416 ? 0.7821 0.6423 0.8096 0.0559  0.0333  -0.0370 443 PHE A CE1 
3250 C CE2 . PHE A 416 ? 0.6657 0.4910 0.6749 0.0666  0.0230  -0.0478 443 PHE A CE2 
3251 C CZ  . PHE A 416 ? 0.7134 0.5704 0.7402 0.0590  0.0268  -0.0464 443 PHE A CZ  
3252 N N   . PHE A 417 ? 0.8086 0.5740 0.7878 0.0937  0.0692  -0.0162 444 PHE A N   
3253 C CA  . PHE A 417 ? 0.7530 0.4982 0.7194 0.1039  0.0786  -0.0144 444 PHE A CA  
3254 C C   . PHE A 417 ? 0.7962 0.5315 0.7599 0.1100  0.0764  -0.0094 444 PHE A C   
3255 O O   . PHE A 417 ? 0.8441 0.5487 0.7872 0.1171  0.0769  -0.0113 444 PHE A O   
3256 C CB  . PHE A 417 ? 0.8065 0.5715 0.7876 0.1053  0.0913  -0.0134 444 PHE A CB  
3257 C CG  . PHE A 417 ? 0.8371 0.5937 0.8133 0.1164  0.1029  -0.0113 444 PHE A CG  
3258 C CD1 . PHE A 417 ? 0.7645 0.4940 0.7169 0.1221  0.1116  -0.0140 444 PHE A CD1 
3259 C CD2 . PHE A 417 ? 0.8423 0.6195 0.8369 0.1226  0.1052  -0.0068 444 PHE A CD2 
3260 C CE1 . PHE A 417 ? 0.8460 0.5707 0.7941 0.1332  0.1242  -0.0135 444 PHE A CE1 
3261 C CE2 . PHE A 417 ? 0.8236 0.5965 0.8167 0.1353  0.1164  -0.0063 444 PHE A CE2 
3262 C CZ  . PHE A 417 ? 0.8806 0.6281 0.8510 0.1403  0.1269  -0.0103 444 PHE A CZ  
3263 N N   . LYS A 418 ? 0.8268 0.5854 0.8087 0.1078  0.0735  -0.0031 445 LYS A N   
3264 C CA  . LYS A 418 ? 0.6878 0.4341 0.6668 0.1155  0.0716  0.0036  445 LYS A CA  
3265 C C   . LYS A 418 ? 0.7705 0.4835 0.7303 0.1117  0.0628  0.0028  445 LYS A C   
3266 O O   . LYS A 418 ? 0.9088 0.5903 0.8526 0.1208  0.0640  0.0021  445 LYS A O   
3267 C CB  . LYS A 418 ? 0.7036 0.4805 0.7019 0.1131  0.0679  0.0121  445 LYS A CB  
3268 C CG  . LYS A 418 ? 0.6958 0.4579 0.6902 0.1228  0.0649  0.0215  445 LYS A CG  
3269 C CD  . LYS A 418 ? 0.7814 0.5767 0.7929 0.1232  0.0611  0.0308  445 LYS A CD  
3270 C CE  . LYS A 418 ? 0.7993 0.5748 0.8036 0.1344  0.0565  0.0423  445 LYS A CE  
3271 N NZ  . LYS A 418 ? 0.8961 0.7047 0.9143 0.1374  0.0515  0.0525  445 LYS A NZ  
3272 N N   . ARG A 419 ? 0.8520 0.5726 0.8141 0.0979  0.0542  0.0014  446 ARG A N   
3273 C CA  . ARG A 419 ? 0.8511 0.5452 0.7993 0.0908  0.0454  -0.0004 446 ARG A CA  
3274 C C   . ARG A 419 ? 0.9034 0.5675 0.8301 0.0957  0.0446  -0.0104 446 ARG A C   
3275 O O   . ARG A 419 ? 0.9275 0.5588 0.8372 0.0966  0.0402  -0.0129 446 ARG A O   
3276 C CB  . ARG A 419 ? 0.8705 0.5876 0.8302 0.0746  0.0379  -0.0010 446 ARG A CB  
3277 C CG  . ARG A 419 ? 1.0246 0.7639 0.9973 0.0674  0.0373  0.0099  446 ARG A CG  
3278 C CD  . ARG A 419 ? 1.0291 0.7851 1.0090 0.0502  0.0311  0.0087  446 ARG A CD  
3279 N NE  . ARG A 419 ? 0.8357 0.6252 0.8294 0.0471  0.0316  0.0006  446 ARG A NE  
3280 C CZ  . ARG A 419 ? 0.9765 0.7849 0.9790 0.0357  0.0270  -0.0053 446 ARG A CZ  
3281 N NH1 . ARG A 419 ? 1.1421 0.9427 1.1430 0.0233  0.0219  -0.0037 446 ARG A NH1 
3282 N NH2 . ARG A 419 ? 1.0920 0.9277 1.1064 0.0367  0.0277  -0.0137 446 ARG A NH2 
3283 N N   . ARG A 420 ? 0.8271 0.4991 0.7514 0.0989  0.0485  -0.0163 447 ARG A N   
3284 C CA  . ARG A 420 ? 0.8965 0.5405 0.7958 0.1040  0.0468  -0.0247 447 ARG A CA  
3285 C C   . ARG A 420 ? 0.9122 0.5289 0.7927 0.1178  0.0560  -0.0256 447 ARG A C   
3286 O O   . ARG A 420 ? 0.9686 0.5534 0.8243 0.1213  0.0519  -0.0325 447 ARG A O   
3287 C CB  . ARG A 420 ? 0.8924 0.5483 0.7911 0.1046  0.0487  -0.0283 447 ARG A CB  
3288 C CG  . ARG A 420 ? 0.7943 0.4694 0.7052 0.0945  0.0373  -0.0319 447 ARG A CG  
3289 C CD  . ARG A 420 ? 0.8412 0.5304 0.7573 0.0963  0.0408  -0.0334 447 ARG A CD  
3290 N NE  . ARG A 420 ? 0.9847 0.6479 0.8741 0.1044  0.0407  -0.0370 447 ARG A NE  
3291 C CZ  . ARG A 420 ? 1.0007 0.6638 0.8864 0.1074  0.0439  -0.0372 447 ARG A CZ  
3292 N NH1 . ARG A 420 ? 0.7546 0.4421 0.6631 0.1028  0.0474  -0.0362 447 ARG A NH1 
3293 N NH2 . ARG A 420 ? 0.8179 0.4532 0.6738 0.1152  0.0435  -0.0385 447 ARG A NH2 
3294 N N   . LEU A 421 ? 0.8594 0.4903 0.7521 0.1261  0.0682  -0.0201 448 LEU A N   
3295 C CA  . LEU A 421 ? 0.7992 0.4093 0.6776 0.1411  0.0786  -0.0218 448 LEU A CA  
3296 C C   . LEU A 421 ? 0.9672 0.5526 0.8402 0.1453  0.0729  -0.0206 448 LEU A C   
3297 O O   . LEU A 421 ? 0.9698 0.5220 0.8197 0.1555  0.0754  -0.0272 448 LEU A O   
3298 C CB  . LEU A 421 ? 0.8231 0.4617 0.7213 0.1485  0.0932  -0.0172 448 LEU A CB  
3299 C CG  . LEU A 421 ? 0.9409 0.5664 0.8295 0.1658  0.1065  -0.0198 448 LEU A CG  
3300 C CD1 . LEU A 421 ? 0.8417 0.4357 0.6953 0.1704  0.1113  -0.0286 448 LEU A CD1 
3301 C CD2 . LEU A 421 ? 0.9993 0.6619 0.9136 0.1705  0.1207  -0.0161 448 LEU A CD2 
3302 N N   . MET A 422 ? 0.9375 0.5357 0.8287 0.1376  0.0656  -0.0123 449 MET A N   
3303 C CA  . MET A 422 ? 0.9238 0.4928 0.8078 0.1399  0.0596  -0.0090 449 MET A CA  
3304 C C   . MET A 422 ? 0.9049 0.4390 0.7670 0.1300  0.0490  -0.0175 449 MET A C   
3305 O O   . MET A 422 ? 0.9866 0.4811 0.8300 0.1365  0.0472  -0.0218 449 MET A O   
3306 C CB  . MET A 422 ? 0.8556 0.4458 0.7602 0.1320  0.0544  0.0040  449 MET A CB  
3307 C CG  . MET A 422 ? 0.9613 0.5819 0.8861 0.1442  0.0620  0.0122  449 MET A CG  
3308 S SD  . MET A 422 ? 1.0356 0.6762 0.9763 0.1370  0.0542  0.0284  449 MET A SD  
3309 C CE  . MET A 422 ? 1.1241 0.7105 1.0449 0.1453  0.0489  0.0346  449 MET A CE  
3310 N N   . ASN A 423 ? 0.8689 0.4175 0.7338 0.1150  0.0411  -0.0213 450 ASN A N   
3311 C CA  . ASN A 423 ? 0.9462 0.4686 0.7940 0.1046  0.0293  -0.0310 450 ASN A CA  
3312 C C   . ASN A 423 ? 1.0659 0.5569 0.8833 0.1167  0.0314  -0.0434 450 ASN A C   
3313 O O   . ASN A 423 ? 1.1680 0.6232 0.9653 0.1143  0.0236  -0.0521 450 ASN A O   
3314 C CB  . ASN A 423 ? 0.8448 0.3966 0.7056 0.0892  0.0205  -0.0334 450 ASN A CB  
3315 C CG  . ASN A 423 ? 1.0015 0.5796 0.8873 0.0742  0.0172  -0.0237 450 ASN A CG  
3316 O OD1 . ASN A 423 ? 1.0490 0.6159 0.9377 0.0726  0.0189  -0.0144 450 ASN A OD1 
3317 N ND2 . ASN A 423 ? 0.9078 0.5199 0.8098 0.0641  0.0129  -0.0256 450 ASN A ND2 
3318 N N   . LEU A 424 ? 1.0317 0.5345 0.8437 0.1286  0.0422  -0.0446 451 LEU A N   
3319 C CA  . LEU A 424 ? 1.0514 0.5259 0.8304 0.1404  0.0464  -0.0554 451 LEU A CA  
3320 C C   . LEU A 424 ? 1.1048 0.5465 0.8694 0.1542  0.0531  -0.0590 451 LEU A C   
3321 O O   . LEU A 424 ? 1.1695 0.5740 0.9052 0.1573  0.0479  -0.0709 451 LEU A O   
3322 C CB  . LEU A 424 ? 0.9376 0.4319 0.7142 0.1486  0.0595  -0.0532 451 LEU A CB  
3323 C CG  . LEU A 424 ? 1.1332 0.5993 0.8724 0.1618  0.0675  -0.0625 451 LEU A CG  
3324 C CD1 . LEU A 424 ? 1.0067 0.4514 0.7170 0.1562  0.0521  -0.0728 451 LEU A CD1 
3325 C CD2 . LEU A 424 ? 1.0589 0.5441 0.7985 0.1693  0.0855  -0.0575 451 LEU A CD2 
3326 N N   . MET A 425 ? 0.9946 0.4499 0.7791 0.1639  0.0638  -0.0498 452 MET A N   
3327 C CA  . MET A 425 ? 1.0064 0.4319 0.7806 0.1804  0.0699  -0.0529 452 MET A CA  
3328 C C   . MET A 425 ? 1.1640 0.5500 0.9281 0.1724  0.0559  -0.0558 452 MET A C   
3329 O O   . MET A 425 ? 1.3127 0.6565 1.0523 0.1826  0.0561  -0.0664 452 MET A O   
3330 C CB  . MET A 425 ? 1.0464 0.4999 0.8491 0.1921  0.0805  -0.0413 452 MET A CB  
3331 C CG  . MET A 425 ? 1.0818 0.5745 0.8975 0.1983  0.0957  -0.0392 452 MET A CG  
3332 S SD  . MET A 425 ? 1.2401 0.7135 1.0220 0.2126  0.1108  -0.0530 452 MET A SD  
3333 C CE  . MET A 425 ? 1.0952 0.5340 0.8664 0.2359  0.1161  -0.0601 452 MET A CE  
3334 N N   . ARG A 426 ? 1.1462 0.5445 0.9284 0.1531  0.0445  -0.0473 453 ARG A N   
3335 C CA  . ARG A 426 ? 1.1086 0.4706 0.8828 0.1403  0.0319  -0.0490 453 ARG A CA  
3336 C C   . ARG A 426 ? 1.2218 0.5534 0.9680 0.1330  0.0222  -0.0667 453 ARG A C   
3337 O O   . ARG A 426 ? 1.2937 0.5788 1.0206 0.1324  0.0163  -0.0752 453 ARG A O   
3338 C CB  . ARG A 426 ? 1.2113 0.6001 1.0108 0.1188  0.0239  -0.0362 453 ARG A CB  
3339 C CG  . ARG A 426 ? 1.3731 0.7271 1.1678 0.1019  0.0131  -0.0346 453 ARG A CG  
3340 C CD  . ARG A 426 ? 1.4999 0.8150 1.2869 0.1159  0.0169  -0.0273 453 ARG A CD  
3341 N NE  . ARG A 426 ? 1.5575 0.8386 1.3412 0.0971  0.0076  -0.0215 453 ARG A NE  
3342 C CZ  . ARG A 426 ? 1.5067 0.8026 1.3070 0.0842  0.0064  -0.0032 453 ARG A CZ  
3343 N NH1 . ARG A 426 ? 1.5986 0.9434 1.4201 0.0889  0.0123  0.0095  453 ARG A NH1 
3344 N NH2 . ARG A 426 ? 1.5691 0.8291 1.3630 0.0650  -0.0007 0.0021  453 ARG A NH2 
3345 N N   . ASP A 427 ? 1.2305 0.5859 0.9729 0.1279  0.0192  -0.0729 454 ASP A N   
3346 C CA  . ASP A 427 ? 1.2430 0.5734 0.9569 0.1229  0.0081  -0.0901 454 ASP A CA  
3347 C C   . ASP A 427 ? 1.3905 0.6864 1.0694 0.1436  0.0168  -0.1026 454 ASP A C   
3348 O O   . ASP A 427 ? 1.3150 0.5725 0.9656 0.1419  0.0077  -0.1182 454 ASP A O   
3349 C CB  . ASP A 427 ? 1.1824 0.5476 0.9006 0.1151  0.0016  -0.0917 454 ASP A CB  
3350 C CG  . ASP A 427 ? 1.4672 0.8583 1.2127 0.0922  -0.0117 -0.0876 454 ASP A CG  
3351 O OD1 . ASP A 427 ? 1.5401 0.9269 1.3031 0.0810  -0.0130 -0.0799 454 ASP A OD1 
3352 O OD2 . ASP A 427 ? 1.4042 0.8198 1.1530 0.0860  -0.0206 -0.0918 454 ASP A OD2 
3353 N N   . VAL A 428 ? 1.3543 0.6652 1.0348 0.1627  0.0347  -0.0971 455 VAL A N   
3354 C CA  . VAL A 428 ? 1.2784 0.5619 0.9271 0.1836  0.0465  -0.1089 455 VAL A CA  
3355 C C   . VAL A 428 ? 1.3231 0.5611 0.9617 0.1922  0.0457  -0.1157 455 VAL A C   
3356 O O   . VAL A 428 ? 1.5472 0.7440 1.1511 0.1985  0.0428  -0.1331 455 VAL A O   
3357 C CB  . VAL A 428 ? 1.2679 0.5840 0.9274 0.1998  0.0676  -0.1005 455 VAL A CB  
3358 C CG1 . VAL A 428 ? 1.1702 0.4613 0.8058 0.2233  0.0831  -0.1110 455 VAL A CG1 
3359 C CG2 . VAL A 428 ? 1.1026 0.4460 0.7558 0.1940  0.0692  -0.0985 455 VAL A CG2 
3360 N N   . GLU A 429 ? 1.2356 0.4778 0.9021 0.1932  0.0476  -0.1022 456 GLU A N   
3361 C CA  . GLU A 429 ? 1.3531 0.5481 1.0102 0.2038  0.0469  -0.1064 456 GLU A CA  
3362 C C   . GLU A 429 ? 1.3478 0.4992 0.9894 0.1837  0.0285  -0.1156 456 GLU A C   
3363 O O   . GLU A 429 ? 1.6324 0.7309 1.2511 0.1918  0.0264  -0.1275 456 GLU A O   
3364 C CB  . GLU A 429 ? 1.4302 0.6413 1.1192 0.2109  0.0521  -0.0874 456 GLU A CB  
3365 C CG  . GLU A 429 ? 1.6977 0.9286 1.4125 0.1865  0.0405  -0.0711 456 GLU A CG  
3366 C CD  . GLU A 429 ? 1.7707 1.0288 1.5151 0.1954  0.0464  -0.0514 456 GLU A CD  
3367 O OE1 . GLU A 429 ? 1.8182 1.0954 1.5704 0.2186  0.0597  -0.0502 456 GLU A OE1 
3368 O OE2 . GLU A 429 ? 1.7113 0.9738 1.4709 0.1789  0.0380  -0.0373 456 GLU A OE2 
3369 N N   . ARG A 430 ? 1.4930 0.6660 1.1478 0.1573  0.0153  -0.1114 457 ARG A N   
3370 C CA  . ARG A 430 ? 1.4648 0.6032 1.1099 0.1346  -0.0022 -0.1205 457 ARG A CA  
3371 C C   . ARG A 430 ? 1.4882 0.5971 1.0957 0.1357  -0.0099 -0.1451 457 ARG A C   
3372 O O   . ARG A 430 ? 1.5892 0.6524 1.1795 0.1245  -0.0218 -0.1584 457 ARG A O   
3373 C CB  . ARG A 430 ? 1.3784 0.5570 1.0524 0.1070  -0.0127 -0.1100 457 ARG A CB  
3374 C CG  . ARG A 430 ? 1.2658 0.4171 0.9415 0.0793  -0.0285 -0.1144 457 ARG A CG  
3375 C CD  . ARG A 430 ? 1.2746 0.4614 0.9861 0.0590  -0.0298 -0.0945 457 ARG A CD  
3376 N NE  . ARG A 430 ? 1.4128 0.6617 1.1459 0.0614  -0.0251 -0.0864 457 ARG A NE  
3377 C CZ  . ARG A 430 ? 1.2674 0.5555 1.0300 0.0538  -0.0207 -0.0683 457 ARG A CZ  
3378 N NH1 . ARG A 430 ? 1.4626 0.7371 1.2358 0.0433  -0.0198 -0.0540 457 ARG A NH1 
3379 N NH2 . ARG A 430 ? 1.1248 0.4644 0.9039 0.0570  -0.0170 -0.0645 457 ARG A NH2 
3380 N N   . GLU A 431 ? 1.5657 0.6980 1.1579 0.1484  -0.0035 -0.1513 458 GLU A N   
3381 C CA  . GLU A 431 ? 1.6832 0.7909 1.2347 0.1516  -0.0106 -0.1736 458 GLU A CA  
3382 C C   . GLU A 431 ? 1.7109 0.7823 1.2288 0.1788  0.0038  -0.1865 458 GLU A C   
3383 O O   . GLU A 431 ? 1.6313 0.6774 1.1094 0.1837  -0.0008 -0.2067 458 GLU A O   
3384 C CB  . GLU A 431 ? 1.6688 0.8190 1.2167 0.1496  -0.0128 -0.1724 458 GLU A CB  
3385 C CG  . GLU A 431 ? 1.9013 1.0880 1.4799 0.1249  -0.0284 -0.1642 458 GLU A CG  
3386 C CD  . GLU A 431 ? 1.9887 1.1527 1.5597 0.1031  -0.0510 -0.1798 458 GLU A CD  
3387 O OE1 . GLU A 431 ? 1.8140 0.9386 1.3472 0.1079  -0.0576 -0.2000 458 GLU A OE1 
3388 O OE2 . GLU A 431 ? 2.0473 1.2348 1.6505 0.0804  -0.0618 -0.1729 458 GLU A OE2 
3389 N N   . GLY A 432 ? 1.7100 0.7805 1.2427 0.1975  0.0206  -0.1762 459 GLY A N   
3390 C CA  . GLY A 432 ? 1.7254 0.7732 1.2350 0.2239  0.0356  -0.1878 459 GLY A CA  
3391 C C   . GLY A 432 ? 1.6012 0.6698 1.0851 0.2392  0.0495  -0.1949 459 GLY A C   
3392 O O   . GLY A 432 ? 1.5876 0.6405 1.0428 0.2515  0.0554  -0.2107 459 GLY A O   
3393 N N   . LEU A 433 ? 1.5585 0.6731 1.0579 0.2349  0.0549  -0.1810 460 LEU A N   
3394 C CA  . LEU A 433 ? 1.4688 0.6029 0.9431 0.2466  0.0690  -0.1844 460 LEU A CA  
3395 C C   . LEU A 433 ? 1.5841 0.7232 1.0584 0.2733  0.0954  -0.1847 460 LEU A C   
3396 O O   . LEU A 433 ? 1.5738 0.7358 1.0867 0.2801  0.1050  -0.1709 460 LEU A O   
3397 C CB  . LEU A 433 ? 1.4609 0.6450 0.9585 0.2334  0.0682  -0.1668 460 LEU A CB  
3398 C CG  . LEU A 433 ? 1.5297 0.7355 1.0055 0.2436  0.0852  -0.1648 460 LEU A CG  
3399 C CD1 . LEU A 433 ? 1.6839 0.8586 1.1032 0.2465  0.0783  -0.1830 460 LEU A CD1 
3400 C CD2 . LEU A 433 ? 1.4134 0.6633 0.9166 0.2303  0.0837  -0.1464 460 LEU A CD2 
3401 N N   . ASP A 434 ? 1.6461 0.7727 1.0812 0.2870  0.1062  -0.1997 461 ASP A N   
3402 C CA  . ASP A 434 ? 1.5148 0.6609 0.9538 0.3096  0.1326  -0.2000 461 ASP A CA  
3403 C C   . ASP A 434 ? 1.5690 0.7537 1.0133 0.3119  0.1513  -0.1868 461 ASP A C   
3404 O O   . ASP A 434 ? 1.7436 0.9310 1.1524 0.3107  0.1574  -0.1904 461 ASP A O   
3405 C CB  . ASP A 434 ? 1.6611 0.7833 1.0571 0.3205  0.1372  -0.2208 461 ASP A CB  
3406 C CG  . ASP A 434 ? 1.8679 1.0127 1.2683 0.3440  0.1656  -0.2230 461 ASP A CG  
3407 O OD1 . ASP A 434 ? 1.8311 1.0077 1.2733 0.3526  0.1789  -0.2098 461 ASP A OD1 
3408 O OD2 . ASP A 434 ? 1.9966 1.1293 1.3588 0.3539  0.1744  -0.2387 461 ASP A OD2 
3409 N N   . TRP A 435 ? 1.5502 0.7751 1.0451 0.3103  0.1582  -0.1686 462 TRP A N   
3410 C CA  . TRP A 435 ? 1.5208 0.7952 1.0361 0.3040  0.1721  -0.1525 462 TRP A CA  
3411 C C   . TRP A 435 ? 1.4321 0.7396 0.9756 0.3225  0.1983  -0.1485 462 TRP A C   
3412 O O   . TRP A 435 ? 1.3269 0.6316 0.8953 0.3364  0.1991  -0.1500 462 TRP A O   
3413 C CB  . TRP A 435 ? 1.4741 0.7746 1.0274 0.2820  0.1555  -0.1349 462 TRP A CB  
3414 C CG  . TRP A 435 ? 1.3605 0.6756 0.9604 0.2837  0.1517  -0.1253 462 TRP A CG  
3415 C CD1 . TRP A 435 ? 1.2336 0.5199 0.8406 0.2803  0.1340  -0.1271 462 TRP A CD1 
3416 C CD2 . TRP A 435 ? 1.3570 0.7183 1.0008 0.2885  0.1654  -0.1117 462 TRP A CD2 
3417 N NE1 . TRP A 435 ? 1.2734 0.5835 0.9229 0.2843  0.1359  -0.1140 462 TRP A NE1 
3418 C CE2 . TRP A 435 ? 1.2063 0.5644 0.8798 0.2899  0.1540  -0.1053 462 TRP A CE2 
3419 C CE3 . TRP A 435 ? 1.4034 0.8083 1.0639 0.2907  0.1860  -0.1043 462 TRP A CE3 
3420 C CZ2 . TRP A 435 ? 1.1454 0.5443 0.8632 0.2954  0.1607  -0.0925 462 TRP A CZ2 
3421 C CZ3 . TRP A 435 ? 1.3079 0.7549 1.0161 0.2941  0.1928  -0.0931 462 TRP A CZ3 
3422 C CH2 . TRP A 435 ? 1.2664 0.7111 1.0022 0.2975  0.1794  -0.0876 462 TRP A CH2 
3423 N N   . ASP A 436 ? 1.4474 0.7864 0.9870 0.3226  0.2194  -0.1431 463 ASP A N   
3424 C CA  . ASP A 436 ? 1.4357 0.8180 1.0080 0.3354  0.2455  -0.1382 463 ASP A CA  
3425 C C   . ASP A 436 ? 1.3792 0.8111 0.9933 0.3184  0.2492  -0.1188 463 ASP A C   
3426 O O   . ASP A 436 ? 1.2901 0.7608 0.9509 0.3242  0.2578  -0.1120 463 ASP A O   
3427 C CB  . ASP A 436 ? 1.5318 0.9129 1.0665 0.3489  0.2723  -0.1492 463 ASP A CB  
3428 C CG  . ASP A 436 ? 1.7643 1.0997 1.2595 0.3698  0.2725  -0.1714 463 ASP A CG  
3429 O OD1 . ASP A 436 ? 1.7138 1.0345 1.2298 0.3793  0.2599  -0.1766 463 ASP A OD1 
3430 O OD2 . ASP A 436 ? 1.7843 1.1004 1.2285 0.3745  0.2836  -0.1827 463 ASP A OD2 
3431 N N   . LEU A 437 ? 1.3535 0.7843 0.9514 0.2984  0.2417  -0.1106 464 LEU A N   
3432 C CA  . LEU A 437 ? 1.2534 0.7249 0.8841 0.2816  0.2461  -0.0941 464 LEU A CA  
3433 C C   . LEU A 437 ? 1.2276 0.6850 0.8512 0.2618  0.2213  -0.0871 464 LEU A C   
3434 O O   . LEU A 437 ? 1.1842 0.6070 0.7638 0.2591  0.2105  -0.0932 464 LEU A O   
3435 C CB  . LEU A 437 ? 1.2666 0.7559 0.8807 0.2804  0.2737  -0.0910 464 LEU A CB  
3436 C CG  . LEU A 437 ? 1.2705 0.7930 0.9096 0.2605  0.2797  -0.0749 464 LEU A CG  
3437 C CD1 . LEU A 437 ? 1.1773 0.7487 0.8792 0.2598  0.2852  -0.0689 464 LEU A CD1 
3438 C CD2 . LEU A 437 ? 1.2808 0.8047 0.8878 0.2571  0.3053  -0.0718 464 LEU A CD2 
3439 N N   . ILE A 438 ? 1.1727 0.6589 0.8393 0.2491  0.2120  -0.0754 465 ILE A N   
3440 C CA  . ILE A 438 ? 1.1238 0.6043 0.7906 0.2313  0.1903  -0.0690 465 ILE A CA  
3441 C C   . ILE A 438 ? 1.0224 0.5398 0.7189 0.2179  0.1982  -0.0560 465 ILE A C   
3442 O O   . ILE A 438 ? 1.0898 0.6414 0.8308 0.2156  0.2005  -0.0502 465 ILE A O   
3443 C CB  . ILE A 438 ? 1.1358 0.6092 0.8234 0.2275  0.1674  -0.0697 465 ILE A CB  
3444 C CG1 . ILE A 438 ? 1.1116 0.5436 0.7699 0.2390  0.1597  -0.0834 465 ILE A CG1 
3445 C CG2 . ILE A 438 ? 1.1010 0.5744 0.7907 0.2096  0.1472  -0.0645 465 ILE A CG2 
3446 C CD1 . ILE A 438 ? 1.2001 0.6193 0.8752 0.2327  0.1383  -0.0833 465 ILE A CD1 
3447 N N   . TYR A 439 ? 1.0343 0.5429 0.7047 0.2095  0.2015  -0.0517 466 TYR A N   
3448 C CA  . TYR A 439 ? 1.0237 0.5588 0.7180 0.1953  0.2076  -0.0402 466 TYR A CA  
3449 C C   . TYR A 439 ? 1.0821 0.6295 0.8069 0.1838  0.1856  -0.0361 466 TYR A C   
3450 O O   . TYR A 439 ? 1.0260 0.5521 0.7352 0.1815  0.1648  -0.0393 466 TYR A O   
3451 C CB  . TYR A 439 ? 1.1209 0.6339 0.7740 0.1899  0.2138  -0.0354 466 TYR A CB  
3452 C CG  . TYR A 439 ? 1.3136 0.8248 0.9417 0.1958  0.2422  -0.0350 466 TYR A CG  
3453 C CD1 . TYR A 439 ? 1.2102 0.7555 0.8686 0.1894  0.2657  -0.0284 466 TYR A CD1 
3454 C CD2 . TYR A 439 ? 1.2269 0.7040 0.8007 0.2066  0.2457  -0.0418 466 TYR A CD2 
3455 C CE1 . TYR A 439 ? 1.1602 0.7077 0.7975 0.1930  0.2940  -0.0279 466 TYR A CE1 
3456 C CE2 . TYR A 439 ? 1.2480 0.7249 0.7963 0.2117  0.2737  -0.0414 466 TYR A CE2 
3457 C CZ  . TYR A 439 ? 1.2996 0.8126 0.8807 0.2045  0.2988  -0.0339 466 TYR A CZ  
3458 O OH  . TYR A 439 ? 1.5101 1.0267 1.0678 0.2080  0.3290  -0.0334 466 TYR A OH  
3459 N N   . VAL A 440 ? 0.9911 0.5756 0.7599 0.1764  0.1903  -0.0301 467 VAL A N   
3460 C CA  . VAL A 440 ? 1.0029 0.6027 0.7987 0.1642  0.1733  -0.0259 467 VAL A CA  
3461 C C   . VAL A 440 ? 1.0174 0.6239 0.8156 0.1513  0.1785  -0.0194 467 VAL A C   
3462 O O   . VAL A 440 ? 1.1243 0.7247 0.9219 0.1438  0.1630  -0.0181 467 VAL A O   
3463 C CB  . VAL A 440 ? 1.0439 0.6783 0.8843 0.1648  0.1713  -0.0245 467 VAL A CB  
3464 C CG1 . VAL A 440 ? 1.0561 0.7080 0.9214 0.1520  0.1552  -0.0210 467 VAL A CG1 
3465 C CG2 . VAL A 440 ? 0.9217 0.5412 0.7564 0.1782  0.1650  -0.0297 467 VAL A CG2 
3466 N N   . GLY A 441 ? 1.1151 0.7334 0.9163 0.1488  0.2007  -0.0158 468 GLY A N   
3467 C CA  . GLY A 441 ? 1.0747 0.6901 0.8714 0.1360  0.2086  -0.0090 468 GLY A CA  
3468 C C   . GLY A 441 ? 1.2818 0.8800 1.0454 0.1377  0.2314  -0.0055 468 GLY A C   
3469 O O   . GLY A 441 ? 1.3912 1.0095 1.1657 0.1419  0.2513  -0.0072 468 GLY A O   
3470 N N   . ARG A 442 ? 1.2388 0.8010 0.9610 0.1354  0.2291  -0.0005 469 ARG A N   
3471 C CA  . ARG A 442 ? 1.1778 0.7178 0.8588 0.1370  0.2501  0.0045  469 ARG A CA  
3472 C C   . ARG A 442 ? 1.1785 0.6862 0.8290 0.1284  0.2470  0.0147  469 ARG A C   
3473 O O   . ARG A 442 ? 1.2134 0.7165 0.8761 0.1236  0.2279  0.0158  469 ARG A O   
3474 C CB  . ARG A 442 ? 1.2530 0.7689 0.8927 0.1539  0.2476  -0.0029 469 ARG A CB  
3475 C CG  . ARG A 442 ? 1.2448 0.7310 0.8582 0.1599  0.2186  -0.0069 469 ARG A CG  
3476 C CD  . ARG A 442 ? 1.1302 0.5826 0.6878 0.1731  0.2175  -0.0126 469 ARG A CD  
3477 N NE  . ARG A 442 ? 1.2739 0.7008 0.8072 0.1766  0.1888  -0.0159 469 ARG A NE  
3478 C CZ  . ARG A 442 ? 1.3433 0.7376 0.8240 0.1862  0.1807  -0.0206 469 ARG A CZ  
3479 N NH1 . ARG A 442 ? 1.5305 0.9101 0.9721 0.1940  0.2000  -0.0226 469 ARG A NH1 
3480 N NH2 . ARG A 442 ? 1.3161 0.6949 0.7832 0.1883  0.1526  -0.0243 469 ARG A NH2 
3481 N N   . LYS A 443 ? 1.3845 0.8685 0.9935 0.1274  0.2666  0.0224  470 LYS A N   
3482 C CA  . LYS A 443 ? 1.2371 0.6797 0.8035 0.1231  0.2636  0.0340  470 LYS A CA  
3483 C C   . LYS A 443 ? 1.3698 0.7757 0.8742 0.1386  0.2568  0.0330  470 LYS A C   
3484 O O   . LYS A 443 ? 1.5761 0.9755 1.0491 0.1428  0.2779  0.0339  470 LYS A O   
3485 C CB  . LYS A 443 ? 1.2743 0.7149 0.8383 0.1066  0.2922  0.0465  470 LYS A CB  
3486 C CG  . LYS A 443 ? 1.2502 0.6442 0.7742 0.1009  0.2878  0.0606  470 LYS A CG  
3487 C CD  . LYS A 443 ? 1.4783 0.8733 1.0157 0.0789  0.3128  0.0722  470 LYS A CD  
3488 C CE  . LYS A 443 ? 1.3921 0.7318 0.8832 0.0746  0.3094  0.0881  470 LYS A CE  
3489 N NZ  . LYS A 443 ? 1.5632 0.8630 0.9826 0.0858  0.3160  0.0975  470 LYS A NZ  
3490 N N   . ARG A 444 ? 1.4417 0.8266 0.9291 0.1472  0.2274  0.0298  471 ARG A N   
3491 C CA  . ARG A 444 ? 1.3405 0.6927 0.7703 0.1617  0.2159  0.0267  471 ARG A CA  
3492 C C   . ARG A 444 ? 1.4379 0.7497 0.8096 0.1612  0.2258  0.0421  471 ARG A C   
3493 O O   . ARG A 444 ? 1.5026 0.7971 0.8725 0.1551  0.2196  0.0535  471 ARG A O   
3494 C CB  . ARG A 444 ? 1.2137 0.5622 0.6496 0.1694  0.1805  0.0180  471 ARG A CB  
3495 C CG  . ARG A 444 ? 1.4667 0.7809 0.8436 0.1829  0.1629  0.0153  471 ARG A CG  
3496 C CD  . ARG A 444 ? 1.2789 0.5964 0.6709 0.1876  0.1281  0.0071  471 ARG A CD  
3497 N NE  . ARG A 444 ? 1.5238 0.8102 0.8606 0.2000  0.1082  0.0055  471 ARG A NE  
3498 C CZ  . ARG A 444 ? 1.6119 0.8995 0.9530 0.2058  0.0768  -0.0015 471 ARG A CZ  
3499 N NH1 . ARG A 444 ? 1.4214 0.7386 0.8176 0.2001  0.0631  -0.0075 471 ARG A NH1 
3500 N NH2 . ARG A 444 ? 1.7257 0.9867 1.0143 0.2177  0.0587  -0.0030 471 ARG A NH2 
3501 N N   . MET A 445 ? 1.4419 0.7365 0.7635 0.1682  0.2416  0.0426  472 MET A N   
3502 C CA  . MET A 445 ? 1.4234 0.6782 0.6829 0.1676  0.2541  0.0590  472 MET A CA  
3503 C C   . MET A 445 ? 1.5672 0.7836 0.7642 0.1838  0.2288  0.0583  472 MET A C   
3504 O O   . MET A 445 ? 1.7986 0.9781 0.9515 0.1847  0.2250  0.0741  472 MET A O   
3505 C CB  . MET A 445 ? 1.6081 0.8694 0.8470 0.1637  0.2920  0.0619  472 MET A CB  
3506 C CG  . MET A 445 ? 1.7106 1.0137 1.0109 0.1473  0.3184  0.0629  472 MET A CG  
3507 S SD  . MET A 445 ? 1.7703 1.0662 1.0984 0.1257  0.3218  0.0806  472 MET A SD  
3508 C CE  . MET A 445 ? 1.5693 0.8158 0.8205 0.1195  0.3464  0.1031  472 MET A CE  
3509 N N   . GLN A 446 ? 1.4797 0.7025 0.6707 0.1963  0.2108  0.0405  473 GLN A N   
3510 C CA  . GLN A 446 ? 1.5480 0.7414 0.6883 0.2108  0.1812  0.0365  473 GLN A CA  
3511 C C   . GLN A 446 ? 1.6328 0.8309 0.8066 0.2112  0.1490  0.0365  473 GLN A C   
3512 O O   . GLN A 446 ? 1.5282 0.7542 0.7499 0.2107  0.1317  0.0221  473 GLN A O   
3513 C CB  . GLN A 446 ? 1.6295 0.8285 0.7557 0.2214  0.1733  0.0155  473 GLN A CB  
3514 C CG  . GLN A 446 ? 1.5499 0.7316 0.6452 0.2336  0.1355  0.0050  473 GLN A CG  
3515 C CD  . GLN A 446 ? 1.8162 0.9609 0.8505 0.2412  0.1232  0.0201  473 GLN A CD  
3516 O OE1 . GLN A 446 ? 1.9794 1.1204 1.0209 0.2457  0.0931  0.0216  473 GLN A OE1 
3517 N NE2 . GLN A 446 ? 2.1381 1.2557 1.1113 0.2437  0.1464  0.0316  473 GLN A NE2 
3518 N N   . VAL A 447 ? 1.6889 0.8586 0.8366 0.2127  0.1418  0.0530  474 VAL A N   
3519 C CA  . VAL A 447 ? 1.6881 0.8615 0.8668 0.2149  0.1138  0.0536  474 VAL A CA  
3520 C C   . VAL A 447 ? 1.6265 0.7690 0.7542 0.2318  0.0836  0.0568  474 VAL A C   
3521 O O   . VAL A 447 ? 1.5982 0.7471 0.7515 0.2373  0.0572  0.0547  474 VAL A O   
3522 C CB  . VAL A 447 ? 1.4532 0.6242 0.6621 0.2022  0.1289  0.0686  474 VAL A CB  
3523 C CG1 . VAL A 447 ? 1.4764 0.6871 0.7460 0.1859  0.1522  0.0626  474 VAL A CG1 
3524 C CG2 . VAL A 447 ? 1.6588 0.7852 0.8088 0.2005  0.1484  0.0905  474 VAL A CG2 
3525 N N   . GLU A 448 ? 1.5909 0.7023 0.6475 0.2413  0.0859  0.0614  475 GLU A N   
3526 C CA  . GLU A 448 ? 1.7984 0.8817 0.8044 0.2590  0.0546  0.0647  475 GLU A CA  
3527 C C   . GLU A 448 ? 1.7639 0.8733 0.7909 0.2675  0.0201  0.0419  475 GLU A C   
3528 O O   . GLU A 448 ? 1.7502 0.8554 0.7708 0.2800  -0.0123 0.0411  475 GLU A O   
3529 C CB  . GLU A 448 ? 1.8480 0.8910 0.7671 0.2667  0.0665  0.0759  475 GLU A CB  
3530 C CG  . GLU A 448 ? 2.1349 1.1878 1.0309 0.2674  0.0770  0.0589  475 GLU A CG  
3531 C CD  . GLU A 448 ? 2.3604 1.3752 1.1694 0.2738  0.0941  0.0704  475 GLU A CD  
3532 O OE1 . GLU A 448 ? 2.0557 1.0349 0.8066 0.2859  0.0770  0.0844  475 GLU A OE1 
3533 O OE2 . GLU A 448 ? 2.3489 1.3700 1.1467 0.2675  0.1250  0.0657  475 GLU A OE2 
3534 N N   . HIS A 449 ? 1.8263 0.9629 0.8800 0.2608  0.0261  0.0233  476 HIS A N   
3535 C CA  . HIS A 449 ? 1.7407 0.9008 0.8164 0.2645  -0.0036 0.0010  476 HIS A CA  
3536 C C   . HIS A 449 ? 1.7150 0.9111 0.8557 0.2507  0.0087  -0.0123 476 HIS A C   
3537 O O   . HIS A 449 ? 1.6898 0.8898 0.8427 0.2420  0.0405  -0.0075 476 HIS A O   
3538 C CB  . HIS A 449 ? 1.8307 0.9704 0.8417 0.2751  -0.0151 -0.0101 476 HIS A CB  
3539 C CG  . HIS A 449 ? 1.8864 1.0187 0.8732 0.2709  0.0152  -0.0156 476 HIS A CG  
3540 N ND1 . HIS A 449 ? 1.9124 1.0678 0.9377 0.2635  0.0216  -0.0343 476 HIS A ND1 
3541 C CD2 . HIS A 449 ? 1.9089 1.0132 0.8363 0.2741  0.0415  -0.0050 476 HIS A CD2 
3542 C CE1 . HIS A 449 ? 2.0208 1.1638 1.0135 0.2643  0.0499  -0.0362 476 HIS A CE1 
3543 N NE2 . HIS A 449 ? 2.0553 1.1697 0.9893 0.2700  0.0633  -0.0190 476 HIS A NE2 
3544 N N   . PRO A 450 ? 1.7161 0.9399 0.8997 0.2482  -0.0157 -0.0285 477 PRO A N   
3545 C CA  . PRO A 450 ? 1.4423 0.6967 0.6842 0.2355  -0.0053 -0.0394 477 PRO A CA  
3546 C C   . PRO A 450 ? 1.4985 0.7431 0.7169 0.2351  0.0121  -0.0498 477 PRO A C   
3547 O O   . PRO A 450 ? 1.7208 0.9412 0.8830 0.2440  0.0059  -0.0569 477 PRO A O   
3548 C CB  . PRO A 450 ? 1.3463 0.6262 0.6252 0.2335  -0.0378 -0.0540 477 PRO A CB  
3549 C CG  . PRO A 450 ? 1.5116 0.7732 0.7414 0.2467  -0.0654 -0.0573 477 PRO A CG  
3550 C CD  . PRO A 450 ? 1.5450 0.7762 0.7291 0.2564  -0.0539 -0.0367 477 PRO A CD  
3551 N N   . GLU A 451 ? 1.5146 0.7785 0.7758 0.2260  0.0336  -0.0514 478 GLU A N   
3552 C CA  . GLU A 451 ? 1.5788 0.8360 0.8259 0.2276  0.0511  -0.0622 478 GLU A CA  
3553 C C   . GLU A 451 ? 1.5583 0.8182 0.8153 0.2266  0.0284  -0.0831 478 GLU A C   
3554 O O   . GLU A 451 ? 1.4999 0.7775 0.7921 0.2203  0.0045  -0.0880 478 GLU A O   
3555 C CB  . GLU A 451 ? 1.6336 0.9123 0.9247 0.2204  0.0807  -0.0558 478 GLU A CB  
3556 C CG  . GLU A 451 ? 1.6040 0.8815 0.8895 0.2175  0.1046  -0.0362 478 GLU A CG  
3557 C CD  . GLU A 451 ? 1.5734 0.8755 0.9002 0.2105  0.1341  -0.0323 478 GLU A CD  
3558 O OE1 . GLU A 451 ? 1.7894 1.1098 1.1517 0.2096  0.1341  -0.0433 478 GLU A OE1 
3559 O OE2 . GLU A 451 ? 1.6312 0.9338 0.9547 0.2057  0.1569  -0.0179 478 GLU A OE2 
3560 N N   . LYS A 452 ? 1.6341 0.8755 0.8592 0.2323  0.0372  -0.0963 479 LYS A N   
3561 C CA  . LYS A 452 ? 1.5440 0.7775 0.7658 0.2313  0.0154  -0.1178 479 LYS A CA  
3562 C C   . LYS A 452 ? 1.5963 0.8535 0.8837 0.2196  0.0121  -0.1222 479 LYS A C   
3563 O O   . LYS A 452 ? 1.5477 0.8149 0.8642 0.2185  0.0351  -0.1176 479 LYS A O   
3564 C CB  . LYS A 452 ? 1.5906 0.7956 0.7620 0.2413  0.0287  -0.1316 479 LYS A CB  
3565 C CG  . LYS A 452 ? 1.6326 0.8227 0.7955 0.2395  0.0060  -0.1558 479 LYS A CG  
3566 C CD  . LYS A 452 ? 1.7146 0.8722 0.8185 0.2515  0.0174  -0.1717 479 LYS A CD  
3567 C CE  . LYS A 452 ? 1.6729 0.8115 0.7683 0.2480  -0.0065 -0.1976 479 LYS A CE  
3568 N NZ  . LYS A 452 ? 1.8114 0.9159 0.8472 0.2610  0.0044  -0.2160 479 LYS A NZ  
3569 N N   . ALA A 453 ? 1.5628 0.8301 0.8728 0.2110  -0.0166 -0.1308 480 ALA A N   
3570 C CA  . ALA A 453 ? 1.3704 0.6590 0.7389 0.1981  -0.0207 -0.1335 480 ALA A CA  
3571 C C   . ALA A 453 ? 1.5916 0.8588 0.9544 0.1976  -0.0169 -0.1493 480 ALA A C   
3572 O O   . ALA A 453 ? 1.6726 0.9106 0.9888 0.2041  -0.0230 -0.1646 480 ALA A O   
3573 C CB  . ALA A 453 ? 1.2720 0.5812 0.6673 0.1877  -0.0509 -0.1377 480 ALA A CB  
3574 N N   . VAL A 454 ? 1.4823 0.7623 0.8911 0.1907  -0.0073 -0.1458 481 VAL A N   
3575 C CA  . VAL A 454 ? 1.4875 0.7450 0.8970 0.1905  -0.0041 -0.1588 481 VAL A CA  
3576 C C   . VAL A 454 ? 1.5132 0.7698 0.9424 0.1741  -0.0310 -0.1700 481 VAL A C   
3577 O O   . VAL A 454 ? 1.5234 0.8095 0.9983 0.1610  -0.0385 -0.1609 481 VAL A O   
3578 C CB  . VAL A 454 ? 1.4812 0.7513 0.9282 0.1929  0.0190  -0.1479 481 VAL A CB  
3579 C CG1 . VAL A 454 ? 1.3677 0.6106 0.8164 0.1941  0.0194  -0.1605 481 VAL A CG1 
3580 C CG2 . VAL A 454 ? 1.3970 0.6718 0.8273 0.2071  0.0464  -0.1387 481 VAL A CG2 
3581 N N   . PRO A 455 ? 1.6000 0.8250 0.9966 0.1731  -0.0453 -0.1900 482 PRO A N   
3582 C CA  . PRO A 455 ? 1.6096 0.8352 1.0267 0.1541  -0.0710 -0.2015 482 PRO A CA  
3583 C C   . PRO A 455 ? 1.6505 0.8795 1.1142 0.1419  -0.0651 -0.1955 482 PRO A C   
3584 O O   . PRO A 455 ? 1.5934 0.8024 1.0566 0.1506  -0.0466 -0.1936 482 PRO A O   
3585 C CB  . PRO A 455 ? 1.6809 0.8649 1.0480 0.1575  -0.0826 -0.2256 482 PRO A CB  
3586 C CG  . PRO A 455 ? 1.5964 0.7682 0.9118 0.1785  -0.0690 -0.2251 482 PRO A CG  
3587 C CD  . PRO A 455 ? 1.6451 0.8344 0.9822 0.1883  -0.0395 -0.2043 482 PRO A CD  
3588 N N   . ARG A 456 ? 1.5634 0.8197 1.0673 0.1224  -0.0808 -0.1920 483 ARG A N   
3589 C CA  . ARG A 456 ? 1.4887 0.7494 1.0348 0.1062  -0.0794 -0.1860 483 ARG A CA  
3590 C C   . ARG A 456 ? 1.4009 0.6828 0.9779 0.1125  -0.0574 -0.1649 483 ARG A C   
3591 O O   . ARG A 456 ? 1.4967 0.7768 1.1020 0.1030  -0.0533 -0.1579 483 ARG A O   
3592 C CB  . ARG A 456 ? 1.6044 0.8161 1.1330 0.1023  -0.0814 -0.2006 483 ARG A CB  
3593 C CG  . ARG A 456 ? 1.6421 0.8323 1.1448 0.0911  -0.1057 -0.2239 483 ARG A CG  
3594 C CD  . ARG A 456 ? 1.6256 0.7583 1.1002 0.0925  -0.1045 -0.2406 483 ARG A CD  
3595 N NE  . ARG A 456 ? 1.7982 0.9022 1.2225 0.1175  -0.0931 -0.2506 483 ARG A NE  
3596 C CZ  . ARG A 456 ? 1.9281 1.0190 1.3448 0.1382  -0.0682 -0.2427 483 ARG A CZ  
3597 N NH1 . ARG A 456 ? 1.8610 0.9635 1.3159 0.1384  -0.0536 -0.2245 483 ARG A NH1 
3598 N NH2 . ARG A 456 ? 1.8262 0.8942 1.1958 0.1594  -0.0577 -0.2539 483 ARG A NH2 
3599 N N   . VAL A 457 ? 1.3460 0.6472 0.9176 0.1273  -0.0437 -0.1543 484 VAL A N   
3600 C CA  . VAL A 457 ? 1.3901 0.7165 0.9924 0.1322  -0.0243 -0.1358 484 VAL A CA  
3601 C C   . VAL A 457 ? 1.3315 0.6955 0.9466 0.1319  -0.0258 -0.1260 484 VAL A C   
3602 O O   . VAL A 457 ? 1.3440 0.7051 0.9313 0.1444  -0.0200 -0.1253 484 VAL A O   
3603 C CB  . VAL A 457 ? 1.4011 0.7092 0.9845 0.1518  -0.0013 -0.1336 484 VAL A CB  
3604 C CG1 . VAL A 457 ? 1.2319 0.5714 0.8516 0.1549  0.0159  -0.1156 484 VAL A CG1 
3605 C CG2 . VAL A 457 ? 1.2808 0.5468 0.8481 0.1556  -0.0007 -0.1455 484 VAL A CG2 
3606 N N   . ARG A 458 ? 1.2240 0.6214 0.8793 0.1181  -0.0328 -0.1183 485 ARG A N   
3607 C CA  . ARG A 458 ? 1.2261 0.6575 0.8960 0.1185  -0.0351 -0.1105 485 ARG A CA  
3608 C C   . ARG A 458 ? 1.1618 0.6044 0.8375 0.1294  -0.0133 -0.0969 485 ARG A C   
3609 O O   . ARG A 458 ? 1.1944 0.6340 0.8807 0.1325  0.0022  -0.0910 485 ARG A O   
3610 C CB  . ARG A 458 ? 1.3541 0.8202 1.0667 0.1014  -0.0463 -0.1077 485 ARG A CB  
3611 C CG  . ARG A 458 ? 1.4873 0.9561 1.1996 0.0895  -0.0700 -0.1213 485 ARG A CG  
3612 C CD  . ARG A 458 ? 1.3562 0.8591 1.1132 0.0700  -0.0768 -0.1187 485 ARG A CD  
3613 N NE  . ARG A 458 ? 1.5765 1.0641 1.3452 0.0585  -0.0693 -0.1148 485 ARG A NE  
3614 C CZ  . ARG A 458 ? 1.6622 1.1605 1.4517 0.0580  -0.0539 -0.1006 485 ARG A CZ  
3615 N NH1 . ARG A 458 ? 1.6908 1.2172 1.4944 0.0662  -0.0438 -0.0905 485 ARG A NH1 
3616 N NH2 . ARG A 458 ? 1.6899 1.1685 1.4848 0.0490  -0.0494 -0.0966 485 ARG A NH2 
3617 N N   . ASN A 459 ? 1.1651 0.6201 0.8338 0.1353  -0.0130 -0.0922 486 ASN A N   
3618 C CA  . ASN A 459 ? 1.1988 0.6666 0.8753 0.1419  0.0063  -0.0798 486 ASN A CA  
3619 C C   . ASN A 459 ? 1.1856 0.6313 0.8367 0.1536  0.0266  -0.0786 486 ASN A C   
3620 O O   . ASN A 459 ? 1.1420 0.6015 0.8100 0.1562  0.0450  -0.0695 486 ASN A O   
3621 C CB  . ASN A 459 ? 1.2501 0.7508 0.9733 0.1327  0.0118  -0.0710 486 ASN A CB  
3622 C CG  . ASN A 459 ? 1.1277 0.6554 0.8773 0.1220  -0.0048 -0.0723 486 ASN A CG  
3623 O OD1 . ASN A 459 ? 1.2133 0.7418 0.9511 0.1247  -0.0176 -0.0766 486 ASN A OD1 
3624 N ND2 . ASN A 459 ? 1.1721 0.7234 0.9569 0.1111  -0.0045 -0.0685 486 ASN A ND2 
3625 N N   . LEU A 460 ? 1.1509 0.5647 0.7620 0.1609  0.0235  -0.0891 487 LEU A N   
3626 C CA  . LEU A 460 ? 1.2048 0.5984 0.7886 0.1736  0.0437  -0.0902 487 LEU A CA  
3627 C C   . LEU A 460 ? 1.3430 0.7097 0.8730 0.1824  0.0404  -0.0970 487 LEU A C   
3628 O O   . LEU A 460 ? 1.3387 0.6909 0.8482 0.1800  0.0192  -0.1078 487 LEU A O   
3629 C CB  . LEU A 460 ? 1.1776 0.5546 0.7653 0.1761  0.0469  -0.0982 487 LEU A CB  
3630 C CG  . LEU A 460 ? 1.2011 0.5655 0.7721 0.1913  0.0705  -0.0995 487 LEU A CG  
3631 C CD1 . LEU A 460 ? 1.1288 0.5261 0.7329 0.1928  0.0904  -0.0854 487 LEU A CD1 
3632 C CD2 . LEU A 460 ? 1.3425 0.6826 0.9124 0.1962  0.0692  -0.1099 487 LEU A CD2 
3633 N N   . VAL A 461 ? 1.2843 0.6460 0.7911 0.1917  0.0614  -0.0905 488 VAL A N   
3634 C CA  . VAL A 461 ? 1.3477 0.6832 0.7980 0.2009  0.0620  -0.0940 488 VAL A CA  
3635 C C   . VAL A 461 ? 1.3718 0.6933 0.7964 0.2124  0.0883  -0.0967 488 VAL A C   
3636 O O   . VAL A 461 ? 1.3765 0.7146 0.8317 0.2138  0.1074  -0.0927 488 VAL A O   
3637 C CB  . VAL A 461 ? 1.3858 0.7276 0.8262 0.1999  0.0618  -0.0803 488 VAL A CB  
3638 C CG1 . VAL A 461 ? 1.3235 0.6756 0.7795 0.1932  0.0332  -0.0815 488 VAL A CG1 
3639 C CG2 . VAL A 461 ? 1.1773 0.5432 0.6522 0.1957  0.0845  -0.0657 488 VAL A CG2 
3640 N N   . GLU A 462 ? 1.4405 0.7335 0.8078 0.2216  0.0888  -0.1043 489 GLU A N   
3641 C CA  . GLU A 462 ? 1.4153 0.6965 0.7514 0.2335  0.1161  -0.1068 489 GLU A CA  
3642 C C   . GLU A 462 ? 1.5679 0.8625 0.9000 0.2322  0.1385  -0.0887 489 GLU A C   
3643 O O   . GLU A 462 ? 1.5447 0.8293 0.8483 0.2301  0.1307  -0.0800 489 GLU A O   
3644 C CB  . GLU A 462 ? 1.4467 0.6919 0.7188 0.2433  0.1085  -0.1226 489 GLU A CB  
3645 C CG  . GLU A 462 ? 1.6056 0.8330 0.8792 0.2428  0.0870  -0.1426 489 GLU A CG  
3646 C CD  . GLU A 462 ? 1.6883 0.8795 0.8970 0.2531  0.0815  -0.1612 489 GLU A CD  
3647 O OE1 . GLU A 462 ? 1.8300 1.0112 0.9927 0.2633  0.1005  -0.1587 489 GLU A OE1 
3648 O OE2 . GLU A 462 ? 1.7766 0.9491 0.9790 0.2498  0.0587  -0.1787 489 GLU A OE2 
3649 N N   . ALA A 463 ? 1.4860 0.8025 0.8471 0.2332  0.1655  -0.0831 490 ALA A N   
3650 C CA  . ALA A 463 ? 1.5603 0.8939 0.9290 0.2274  0.1875  -0.0659 490 ALA A CA  
3651 C C   . ALA A 463 ? 1.6874 0.9973 0.9930 0.2337  0.2043  -0.0627 490 ALA A C   
3652 O O   . ALA A 463 ? 1.5901 0.8899 0.8661 0.2450  0.2205  -0.0732 490 ALA A O   
3653 C CB  . ALA A 463 ? 1.4340 0.8022 0.8532 0.2266  0.2108  -0.0630 490 ALA A CB  
3654 N N   . ASP A 464 ? 1.5326 0.8319 0.8154 0.2274  0.2008  -0.0482 491 ASP A N   
3655 C CA  . ASP A 464 ? 1.7176 0.9952 0.9415 0.2307  0.2201  -0.0395 491 ASP A CA  
3656 C C   . ASP A 464 ? 1.6733 0.9756 0.9238 0.2216  0.2547  -0.0259 491 ASP A C   
3657 O O   . ASP A 464 ? 1.6244 0.9607 0.9320 0.2181  0.2653  -0.0288 491 ASP A O   
3658 C CB  . ASP A 464 ? 1.7626 1.0122 0.9459 0.2297  0.1977  -0.0296 491 ASP A CB  
3659 C CG  . ASP A 464 ? 1.9128 1.1394 1.0600 0.2396  0.1666  -0.0452 491 ASP A CG  
3660 O OD1 . ASP A 464 ? 1.9933 1.2217 1.1459 0.2455  0.1634  -0.0639 491 ASP A OD1 
3661 O OD2 . ASP A 464 ? 1.7349 0.9412 0.8488 0.2418  0.1447  -0.0394 491 ASP A OD2 
3662 N N   . TYR A 465 ? 1.6608 0.9465 0.8706 0.2171  0.2723  -0.0105 492 TYR A N   
3663 C CA  . TYR A 465 ? 1.6590 0.9683 0.8943 0.2050  0.3060  0.0025  492 TYR A CA  
3664 C C   . TYR A 465 ? 1.6384 0.9748 0.9412 0.1907  0.2980  0.0098  492 TYR A C   
3665 O O   . TYR A 465 ? 1.5628 0.8838 0.8659 0.1855  0.2757  0.0177  492 TYR A O   
3666 C CB  . TYR A 465 ? 1.5761 0.8557 0.7516 0.1998  0.3236  0.0203  492 TYR A CB  
3667 C CG  . TYR A 465 ? 1.7607 1.0640 0.9565 0.1855  0.3630  0.0323  492 TYR A CG  
3668 C CD1 . TYR A 465 ? 1.7431 1.0895 0.9836 0.1864  0.3866  0.0216  492 TYR A CD1 
3669 C CD2 . TYR A 465 ? 1.7843 1.0675 0.9566 0.1708  0.3762  0.0541  492 TYR A CD2 
3670 C CE1 . TYR A 465 ? 1.8191 1.1937 1.0832 0.1722  0.4223  0.0312  492 TYR A CE1 
3671 C CE2 . TYR A 465 ? 1.7558 1.0619 0.9492 0.1543  0.4128  0.0646  492 TYR A CE2 
3672 C CZ  . TYR A 465 ? 1.8729 1.2278 1.1139 0.1545  0.4358  0.0524  492 TYR A CZ  
3673 O OH  . TYR A 465 ? 1.8560 1.2401 1.1227 0.1369  0.4720  0.0616  492 TYR A OH  
3674 N N   . SER A 466 ? 1.6499 1.0278 1.0096 0.1859  0.3153  0.0058  493 SER A N   
3675 C CA  . SER A 466 ? 1.5461 0.9548 0.9710 0.1726  0.3095  0.0104  493 SER A CA  
3676 C C   . SER A 466 ? 1.5504 0.9905 1.0050 0.1593  0.3433  0.0184  493 SER A C   
3677 O O   . SER A 466 ? 1.6765 1.1213 1.1092 0.1623  0.3715  0.0181  493 SER A O   
3678 C CB  . SER A 466 ? 1.4984 0.9318 0.9707 0.1798  0.2908  -0.0039 493 SER A CB  
3679 O OG  . SER A 466 ? 1.4649 0.8704 0.9083 0.1906  0.2627  -0.0130 493 SER A OG  
3680 N N   . TYR A 467 ? 1.5597 1.0237 1.0655 0.1439  0.3409  0.0244  494 TYR A N   
3681 C CA  . TYR A 467 ? 1.6620 1.1530 1.1946 0.1266  0.3710  0.0331  494 TYR A CA  
3682 C C   . TYR A 467 ? 1.6691 1.2019 1.2735 0.1146  0.3644  0.0308  494 TYR A C   
3683 O O   . TYR A 467 ? 1.9522 1.4868 1.5743 0.0956  0.3686  0.0402  494 TYR A O   
3684 C CB  . TYR A 467 ? 1.7754 1.2274 1.2625 0.1133  0.3812  0.0507  494 TYR A CB  
3685 C CG  . TYR A 467 ? 1.9741 1.4426 1.4631 0.0972  0.4202  0.0599  494 TYR A CG  
3686 C CD1 . TYR A 467 ? 2.0750 1.5708 1.6138 0.0745  0.4320  0.0659  494 TYR A CD1 
3687 C CD2 . TYR A 467 ? 1.9905 1.4486 1.4315 0.1036  0.4457  0.0618  494 TYR A CD2 
3688 C CE1 . TYR A 467 ? 2.1731 1.6870 1.7172 0.0567  0.4684  0.0740  494 TYR A CE1 
3689 C CE2 . TYR A 467 ? 2.1120 1.5886 1.5560 0.0872  0.4837  0.0706  494 TYR A CE2 
3690 C CZ  . TYR A 467 ? 2.2384 1.7436 1.7358 0.0629  0.4951  0.0769  494 TYR A CZ  
3691 O OH  . TYR A 467 ? 2.2973 1.8238 1.8010 0.0437  0.5337  0.0852  494 TYR A OH  
3692 N N   . TRP A 468 ? 1.2644 0.8295 0.9090 0.1256  0.3537  0.0182  495 TRP A N   
3693 C CA  . TRP A 468 ? 1.4434 1.0542 1.1550 0.1163  0.3494  0.0152  495 TRP A CA  
3694 C C   . TRP A 468 ? 1.4167 1.0585 1.1589 0.1337  0.3440  0.0025  495 TRP A C   
3695 O O   . TRP A 468 ? 1.4080 1.0279 1.1205 0.1517  0.3358  -0.0048 495 TRP A O   
3696 C CB  . TRP A 468 ? 1.4721 1.0711 1.1975 0.1074  0.3222  0.0181  495 TRP A CB  
3697 C CG  . TRP A 468 ? 1.3940 0.9890 1.1275 0.0852  0.3314  0.0283  495 TRP A CG  
3698 C CD1 . TRP A 468 ? 1.3686 0.9844 1.1182 0.0689  0.3597  0.0337  495 TRP A CD1 
3699 C CD2 . TRP A 468 ? 1.3978 0.9643 1.1234 0.0766  0.3128  0.0337  495 TRP A CD2 
3700 N NE1 . TRP A 468 ? 1.4422 1.0399 1.1928 0.0491  0.3595  0.0425  495 TRP A NE1 
3701 C CE2 . TRP A 468 ? 1.4853 1.0517 1.2207 0.0550  0.3307  0.0424  495 TRP A CE2 
3702 C CE3 . TRP A 468 ? 1.3558 0.8985 1.0690 0.0851  0.2833  0.0313  495 TRP A CE3 
3703 C CZ2 . TRP A 468 ? 1.3299 0.8679 1.0603 0.0435  0.3193  0.0483  495 TRP A CZ2 
3704 C CZ3 . TRP A 468 ? 1.3084 0.8284 1.0189 0.0751  0.2725  0.0369  495 TRP A CZ3 
3705 C CH2 . TRP A 468 ? 1.3602 0.8755 1.0780 0.0554  0.2901  0.0452  495 TRP A CH2 
3706 N N   . THR A 469 ? 1.3123 1.0037 1.1133 0.1282  0.3479  -0.0002 496 THR A N   
3707 C CA  . THR A 469 ? 1.2453 0.9687 1.0814 0.1448  0.3413  -0.0102 496 THR A CA  
3708 C C   . THR A 469 ? 1.1733 0.9276 1.0600 0.1370  0.3222  -0.0104 496 THR A C   
3709 O O   . THR A 469 ? 1.1054 0.9042 1.0371 0.1427  0.3243  -0.0149 496 THR A O   
3710 C CB  . THR A 469 ? 1.1083 0.8705 0.9651 0.1521  0.3700  -0.0149 496 THR A CB  
3711 O OG1 . THR A 469 ? 1.2484 1.0438 1.1346 0.1304  0.3900  -0.0088 496 THR A OG1 
3712 C CG2 . THR A 469 ? 1.2809 1.0125 1.0843 0.1655  0.3870  -0.0180 496 THR A CG2 
3713 N N   . LEU A 470 ? 1.1453 0.8774 1.0243 0.1252  0.3031  -0.0058 497 LEU A N   
3714 C CA  . LEU A 470 ? 1.0046 0.7639 0.9261 0.1175  0.2848  -0.0068 497 LEU A CA  
3715 C C   . LEU A 470 ? 1.0531 0.8245 0.9910 0.1347  0.2680  -0.0125 497 LEU A C   
3716 O O   . LEU A 470 ? 1.0524 0.8663 1.0336 0.1366  0.2663  -0.0147 497 LEU A O   
3717 C CB  . LEU A 470 ? 0.9711 0.6998 0.8752 0.1059  0.2672  -0.0027 497 LEU A CB  
3718 C CG  . LEU A 470 ? 1.1125 0.8152 0.9924 0.0902  0.2790  0.0047  497 LEU A CG  
3719 C CD1 . LEU A 470 ? 1.1162 0.7827 0.9728 0.0881  0.2569  0.0068  497 LEU A CD1 
3720 C CD2 . LEU A 470 ? 1.2441 0.9818 1.1640 0.0704  0.2933  0.0061  497 LEU A CD2 
3721 N N   . ALA A 471 ? 0.9611 0.6944 0.8639 0.1468  0.2545  -0.0147 498 ALA A N   
3722 C CA  . ALA A 471 ? 1.0186 0.7534 0.9313 0.1610  0.2379  -0.0188 498 ALA A CA  
3723 C C   . ALA A 471 ? 1.0775 0.7702 0.9463 0.1759  0.2357  -0.0238 498 ALA A C   
3724 O O   . ALA A 471 ? 1.0296 0.6870 0.8585 0.1723  0.2336  -0.0232 498 ALA A O   
3725 C CB  . ALA A 471 ? 0.8875 0.6228 0.8134 0.1523  0.2136  -0.0166 498 ALA A CB  
3726 N N   . TYR A 472 ? 0.9982 0.6935 0.8736 0.1933  0.2352  -0.0292 499 TYR A N   
3727 C CA  . TYR A 472 ? 0.9230 0.5767 0.7581 0.2077  0.2318  -0.0365 499 TYR A CA  
3728 C C   . TYR A 472 ? 1.0770 0.7319 0.9286 0.2240  0.2232  -0.0407 499 TYR A C   
3729 O O   . TYR A 472 ? 0.9961 0.6882 0.8881 0.2288  0.2257  -0.0380 499 TYR A O   
3730 C CB  . TYR A 472 ? 0.9652 0.6089 0.7700 0.2154  0.2560  -0.0410 499 TYR A CB  
3731 C CG  . TYR A 472 ? 0.9678 0.6510 0.8028 0.2261  0.2792  -0.0435 499 TYR A CG  
3732 C CD1 . TYR A 472 ? 1.0223 0.7050 0.8622 0.2487  0.2816  -0.0522 499 TYR A CD1 
3733 C CD2 . TYR A 472 ? 1.1050 0.8259 0.9645 0.2137  0.2986  -0.0381 499 TYR A CD2 
3734 C CE1 . TYR A 472 ? 1.0990 0.8221 0.9695 0.2611  0.3023  -0.0557 499 TYR A CE1 
3735 C CE2 . TYR A 472 ? 1.0800 0.8437 0.9717 0.2228  0.3199  -0.0416 499 TYR A CE2 
3736 C CZ  . TYR A 472 ? 1.1234 0.8902 1.0214 0.2477  0.3215  -0.0505 499 TYR A CZ  
3737 O OH  . TYR A 472 ? 1.0496 0.8631 0.9827 0.2594  0.3422  -0.0550 499 TYR A OH  
3738 N N   . VAL A 473 ? 1.0849 0.6972 0.9037 0.2325  0.2119  -0.0474 500 VAL A N   
3739 C CA  . VAL A 473 ? 0.9806 0.5798 0.8046 0.2496  0.2051  -0.0523 500 VAL A CA  
3740 C C   . VAL A 473 ? 1.1951 0.7734 0.9904 0.2689  0.2217  -0.0641 500 VAL A C   
3741 O O   . VAL A 473 ? 1.1644 0.7182 0.9196 0.2665  0.2282  -0.0695 500 VAL A O   
3742 C CB  . VAL A 473 ? 1.0588 0.6227 0.8682 0.2430  0.1799  -0.0525 500 VAL A CB  
3743 C CG1 . VAL A 473 ? 1.0790 0.6277 0.8969 0.2586  0.1727  -0.0546 500 VAL A CG1 
3744 C CG2 . VAL A 473 ? 0.9366 0.5221 0.7687 0.2229  0.1660  -0.0424 500 VAL A CG2 
3745 N N   . ILE A 474 ? 1.2077 0.7961 1.0221 0.2894  0.2286  -0.0682 501 ILE A N   
3746 C CA  . ILE A 474 ? 1.1765 0.7508 0.9685 0.3109  0.2470  -0.0811 501 ILE A CA  
3747 C C   . ILE A 474 ? 1.2075 0.7523 0.9984 0.3319  0.2365  -0.0882 501 ILE A C   
3748 O O   . ILE A 474 ? 1.2808 0.8404 1.1057 0.3363  0.2254  -0.0806 501 ILE A O   
3749 C CB  . ILE A 474 ? 1.1379 0.7646 0.9590 0.3179  0.2741  -0.0806 501 ILE A CB  
3750 C CG1 . ILE A 474 ? 1.1637 0.7776 0.9574 0.3394  0.2962  -0.0952 501 ILE A CG1 
3751 C CG2 . ILE A 474 ? 1.0439 0.7162 0.9213 0.3258  0.2710  -0.0742 501 ILE A CG2 
3752 C CD1 . ILE A 474 ? 1.1756 0.8432 0.9955 0.3430  0.3261  -0.0953 501 ILE A CD1 
3753 N N   . SER A 475 ? 1.2768 0.7763 1.0253 0.3445  0.2393  -0.1027 502 SER A N   
3754 C CA  . SER A 475 ? 1.3386 0.7998 1.0798 0.3648  0.2301  -0.1115 502 SER A CA  
3755 C C   . SER A 475 ? 1.4305 0.9114 1.1867 0.3949  0.2515  -0.1206 502 SER A C   
3756 O O   . SER A 475 ? 1.4290 0.9488 1.1931 0.3988  0.2754  -0.1230 502 SER A O   
3757 C CB  . SER A 475 ? 1.2421 0.6407 0.9294 0.3623  0.2196  -0.1253 502 SER A CB  
3758 O OG  . SER A 475 ? 1.3757 0.7659 1.0272 0.3733  0.2395  -0.1398 502 SER A OG  
3759 N N   . LEU A 476 ? 1.2663 0.7200 1.0277 0.4165  0.2429  -0.1255 503 LEU A N   
3760 C CA  . LEU A 476 ? 1.3534 0.8262 1.1304 0.4455  0.2589  -0.1357 503 LEU A CA  
3761 C C   . LEU A 476 ? 1.4649 0.9248 1.2033 0.4501  0.2752  -0.1538 503 LEU A C   
3762 O O   . LEU A 476 ? 1.4462 0.9462 1.1985 0.4643  0.2991  -0.1605 503 LEU A O   
3763 C CB  . LEU A 476 ? 1.5250 0.9698 1.3134 0.4595  0.2390  -0.1358 503 LEU A CB  
3764 C CG  . LEU A 476 ? 1.4574 0.9279 1.2714 0.4891  0.2501  -0.1448 503 LEU A CG  
3765 C CD1 . LEU A 476 ? 1.5113 1.0560 1.3748 0.4985  0.2672  -0.1367 503 LEU A CD1 
3766 C CD2 . LEU A 476 ? 1.3554 0.7907 1.1777 0.5019  0.2286  -0.1424 503 LEU A CD2 
3767 N N   . GLN A 477 ? 1.4602 0.8670 1.1504 0.4376  0.2627  -0.1623 504 GLN A N   
3768 C CA  . GLN A 477 ? 1.6268 1.0193 1.2736 0.4404  0.2767  -0.1789 504 GLN A CA  
3769 C C   . GLN A 477 ? 1.6018 1.0307 1.2410 0.4325  0.3017  -0.1744 504 GLN A C   
3770 O O   . GLN A 477 ? 1.6327 1.0846 1.2636 0.4433  0.3260  -0.1835 504 GLN A O   
3771 C CB  . GLN A 477 ? 1.6040 0.9361 1.2026 0.4257  0.2552  -0.1875 504 GLN A CB  
3772 C CG  . GLN A 477 ? 1.8596 1.1745 1.4063 0.4260  0.2666  -0.2036 504 GLN A CG  
3773 C CD  . GLN A 477 ? 1.9199 1.1828 1.4217 0.4084  0.2433  -0.2104 504 GLN A CD  
3774 O OE1 . GLN A 477 ? 1.8451 1.0891 1.3566 0.3929  0.2207  -0.2020 504 GLN A OE1 
3775 N NE2 . GLN A 477 ? 2.0625 1.3047 1.5157 0.4102  0.2487  -0.2262 504 GLN A NE2 
3776 N N   . GLY A 478 ? 1.5479 0.9818 1.1898 0.4129  0.2970  -0.1601 505 GLY A N   
3777 C CA  . GLY A 478 ? 1.5889 1.0582 1.2266 0.3980  0.3164  -0.1524 505 GLY A CA  
3778 C C   . GLY A 478 ? 1.5779 1.1122 1.2632 0.4067  0.3422  -0.1475 505 GLY A C   
3779 O O   . GLY A 478 ? 1.5983 1.1582 1.2730 0.4040  0.3684  -0.1485 505 GLY A O   
3780 N N   . ALA A 479 ? 1.4065 0.9696 1.1446 0.4165  0.3350  -0.1417 506 ALA A N   
3781 C CA  . ALA A 479 ? 1.4419 1.0718 1.2306 0.4267  0.3572  -0.1391 506 ALA A CA  
3782 C C   . ALA A 479 ? 1.5059 1.1433 1.2838 0.4535  0.3824  -0.1569 506 ALA A C   
3783 O O   . ALA A 479 ? 1.4397 1.1282 1.2365 0.4543  0.4107  -0.1579 506 ALA A O   
3784 C CB  . ALA A 479 ? 1.3231 0.9792 1.1665 0.4344  0.3399  -0.1300 506 ALA A CB  
3785 N N   . ARG A 480 ? 1.4669 1.0608 1.2196 0.4675  0.3675  -0.1703 507 ARG A N   
3786 C CA  . ARG A 480 ? 1.4582 1.0608 1.2010 0.4865  0.3846  -0.1880 507 ARG A CA  
3787 C C   . ARG A 480 ? 1.5648 1.1629 1.2595 0.4756  0.4071  -0.1938 507 ARG A C   
3788 O O   . ARG A 480 ? 1.4925 1.1299 1.1943 0.4843  0.4342  -0.2017 507 ARG A O   
3789 C CB  . ARG A 480 ? 1.4316 0.9808 1.1540 0.5012  0.3627  -0.2015 507 ARG A CB  
3790 C CG  . ARG A 480 ? 1.5143 1.0660 1.2811 0.5162  0.3430  -0.1965 507 ARG A CG  
3791 C CD  . ARG A 480 ? 1.5921 1.0915 1.3369 0.5316  0.3278  -0.2119 507 ARG A CD  
3792 N NE  . ARG A 480 ? 1.6962 1.1903 1.4778 0.5461  0.3086  -0.2057 507 ARG A NE  
3793 C CZ  . ARG A 480 ? 1.7393 1.1867 1.5130 0.5362  0.2813  -0.1963 507 ARG A CZ  
3794 N NH1 . ARG A 480 ? 1.7000 1.1055 1.4351 0.5115  0.2688  -0.1934 507 ARG A NH1 
3795 N NH2 . ARG A 480 ? 1.6756 1.1193 1.4811 0.5510  0.2662  -0.1894 507 ARG A NH2 
3796 N N   . LYS A 481 ? 1.5509 1.1024 1.1959 0.4566  0.3959  -0.1898 508 LYS A N   
3797 C CA  . LYS A 481 ? 1.4578 0.9981 1.0493 0.4469  0.4142  -0.1939 508 LYS A CA  
3798 C C   . LYS A 481 ? 1.5446 1.1405 1.1562 0.4364  0.4461  -0.1824 508 LYS A C   
3799 O O   . LYS A 481 ? 1.5349 1.1475 1.1235 0.4373  0.4720  -0.1882 508 LYS A O   
3800 C CB  . LYS A 481 ? 1.4627 0.9462 1.0022 0.4287  0.3925  -0.1900 508 LYS A CB  
3801 C CG  . LYS A 481 ? 1.4941 0.9217 1.0072 0.4341  0.3629  -0.2032 508 LYS A CG  
3802 C CD  . LYS A 481 ? 1.6478 1.0274 1.1075 0.4157  0.3440  -0.2019 508 LYS A CD  
3803 C CE  . LYS A 481 ? 1.6620 0.9893 1.0937 0.4186  0.3172  -0.2176 508 LYS A CE  
3804 N NZ  . LYS A 481 ? 1.8015 1.0880 1.1811 0.4014  0.2987  -0.2187 508 LYS A NZ  
3805 N N   . LEU A 482 ? 1.5647 1.1900 1.2192 0.4247  0.4452  -0.1661 509 LEU A N   
3806 C CA  . LEU A 482 ? 1.5434 1.2238 1.2237 0.4093  0.4735  -0.1543 509 LEU A CA  
3807 C C   . LEU A 482 ? 1.4960 1.2384 1.2207 0.4259  0.4991  -0.1629 509 LEU A C   
3808 O O   . LEU A 482 ? 1.5106 1.2836 1.2270 0.4191  0.5290  -0.1635 509 LEU A O   
3809 C CB  . LEU A 482 ? 1.3585 1.0645 1.0860 0.3845  0.4539  -0.1348 509 LEU A CB  
3810 C CG  . LEU A 482 ? 1.5094 1.1657 1.2045 0.3635  0.4231  -0.1251 509 LEU A CG  
3811 C CD1 . LEU A 482 ? 1.3749 1.0629 1.1166 0.3391  0.4098  -0.1072 509 LEU A CD1 
3812 C CD2 . LEU A 482 ? 1.5835 1.2026 1.2112 0.3518  0.4320  -0.1246 509 LEU A CD2 
3813 N N   . LEU A 483 ? 1.4042 1.1673 1.1771 0.4463  0.4854  -0.1690 510 LEU A N   
3814 C CA  . LEU A 483 ? 1.4139 1.2379 1.2325 0.4641  0.5044  -0.1792 510 LEU A CA  
3815 C C   . LEU A 483 ? 1.4817 1.2908 1.2594 0.4775  0.5190  -0.1978 510 LEU A C   
3816 O O   . LEU A 483 ? 1.4432 1.3061 1.2441 0.4835  0.5461  -0.2054 510 LEU A O   
3817 C CB  . LEU A 483 ? 1.3372 1.1755 1.2077 0.4861  0.4820  -0.1819 510 LEU A CB  
3818 C CG  . LEU A 483 ? 1.3356 1.1881 1.2469 0.4764  0.4639  -0.1646 510 LEU A CG  
3819 C CD1 . LEU A 483 ? 1.3661 1.2130 1.3097 0.5000  0.4371  -0.1672 510 LEU A CD1 
3820 C CD2 . LEU A 483 ? 1.2358 1.1653 1.2005 0.4622  0.4865  -0.1550 510 LEU A CD2 
3821 N N   . ALA A 484 ? 1.5883 1.3275 1.3067 0.4815  0.5014  -0.2062 511 ALA A N   
3822 C CA  . ALA A 484 ? 1.6322 1.3537 1.3075 0.4938  0.5139  -0.2252 511 ALA A CA  
3823 C C   . ALA A 484 ? 1.5763 1.3152 1.2163 0.4765  0.5449  -0.2210 511 ALA A C   
3824 O O   . ALA A 484 ? 1.7298 1.4936 1.3615 0.4861  0.5686  -0.2343 511 ALA A O   
3825 C CB  . ALA A 484 ? 1.5651 1.2081 1.1856 0.4979  0.4858  -0.2347 511 ALA A CB  
3826 N N   . ALA A 485 ? 1.7570 1.4822 1.3752 0.4508  0.5454  -0.2025 512 ALA A N   
3827 C CA  . ALA A 485 ? 1.7528 1.4893 1.3346 0.4321  0.5741  -0.1948 512 ALA A CA  
3828 C C   . ALA A 485 ? 1.7340 1.5504 1.3690 0.4275  0.6078  -0.1915 512 ALA A C   
3829 O O   . ALA A 485 ? 1.8258 1.6586 1.4334 0.4159  0.6360  -0.1895 512 ALA A O   
3830 C CB  . ALA A 485 ? 1.8151 1.5173 1.3659 0.4062  0.5653  -0.1746 512 ALA A CB  
3831 N N   . GLU A 486 ? 1.7239 1.5914 1.4342 0.4354  0.6045  -0.1910 513 GLU A N   
3832 C CA  . GLU A 486 ? 1.7388 1.6901 1.5108 0.4305  0.6324  -0.1893 513 GLU A CA  
3833 C C   . GLU A 486 ? 1.7199 1.6872 1.4797 0.3961  0.6563  -0.1701 513 GLU A C   
3834 O O   . GLU A 486 ? 1.6474 1.6397 1.3896 0.3870  0.6862  -0.1715 513 GLU A O   
3835 C CB  . GLU A 486 ? 1.6977 1.6821 1.4740 0.4515  0.6524  -0.2107 513 GLU A CB  
3836 C CG  . GLU A 486 ? 1.5908 1.5636 1.3881 0.4857  0.6305  -0.2299 513 GLU A CG  
3837 C CD  . GLU A 486 ? 1.8146 1.7958 1.5940 0.5070  0.6474  -0.2536 513 GLU A CD  
3838 O OE1 . GLU A 486 ? 1.9960 2.0131 1.7636 0.4964  0.6797  -0.2556 513 GLU A OE1 
3839 O OE2 . GLU A 486 ? 2.0410 1.9913 1.8173 0.5335  0.6288  -0.2703 513 GLU A OE2 
3840 N N   . PRO A 487 ? 1.7203 1.6723 1.4882 0.3755  0.6444  -0.1517 514 PRO A N   
3841 C CA  . PRO A 487 ? 1.6788 1.6298 1.4252 0.3414  0.6642  -0.1324 514 PRO A CA  
3842 C C   . PRO A 487 ? 1.6645 1.6957 1.4744 0.3216  0.6919  -0.1255 514 PRO A C   
3843 O O   . PRO A 487 ? 1.7904 1.8216 1.5845 0.2907  0.7102  -0.1091 514 PRO A O   
3844 C CB  . PRO A 487 ? 1.7209 1.6257 1.4584 0.3303  0.6379  -0.1190 514 PRO A CB  
3845 C CG  . PRO A 487 ? 1.6249 1.5508 1.4210 0.3510  0.6138  -0.1268 514 PRO A CG  
3846 C CD  . PRO A 487 ? 1.5891 1.5226 1.3858 0.3824  0.6121  -0.1478 514 PRO A CD  
3847 N N   . LEU A 488 ? 1.5323 1.6311 1.4130 0.3377  0.6942  -0.1375 515 LEU A N   
3848 C CA  . LEU A 488 ? 1.5015 1.6822 1.4494 0.3171  0.7168  -0.1321 515 LEU A CA  
3849 C C   . LEU A 488 ? 1.5753 1.7838 1.5017 0.3011  0.7533  -0.1319 515 LEU A C   
3850 O O   . LEU A 488 ? 1.6101 1.8601 1.5645 0.2694  0.7739  -0.1195 515 LEU A O   
3851 C CB  . LEU A 488 ? 1.4434 1.6908 1.4704 0.3417  0.7072  -0.1466 515 LEU A CB  
3852 C CG  . LEU A 488 ? 1.3787 1.5979 1.4245 0.3611  0.6699  -0.1467 515 LEU A CG  
3853 C CD1 . LEU A 488 ? 1.2992 1.5863 1.4215 0.3857  0.6608  -0.1594 515 LEU A CD1 
3854 C CD2 . LEU A 488 ? 1.2752 1.4748 1.3269 0.3333  0.6588  -0.1270 515 LEU A CD2 
3855 N N   . SER A 489 ? 1.5567 1.7426 1.4335 0.3211  0.7614  -0.1457 516 SER A N   
3856 C CA  . SER A 489 ? 1.6913 1.9003 1.5402 0.3074  0.7961  -0.1457 516 SER A CA  
3857 C C   . SER A 489 ? 1.7495 1.8991 1.5255 0.2778  0.8048  -0.1245 516 SER A C   
3858 O O   . SER A 489 ? 1.6935 1.8641 1.4507 0.2574  0.8346  -0.1174 516 SER A O   
3859 C CB  . SER A 489 ? 1.6550 1.8588 1.4739 0.3398  0.8010  -0.1694 516 SER A CB  
3860 O OG  . SER A 489 ? 1.7209 1.8405 1.4747 0.3577  0.7753  -0.1740 516 SER A OG  
3861 N N   . LYS A 490 ? 1.6668 1.7437 1.4014 0.2754  0.7790  -0.1140 517 LYS A N   
3862 C CA  . LYS A 490 ? 1.7217 1.7346 1.3828 0.2515  0.7816  -0.0943 517 LYS A CA  
3863 C C   . LYS A 490 ? 1.6275 1.6068 1.2987 0.2356  0.7594  -0.0783 517 LYS A C   
3864 O O   . LYS A 490 ? 1.5534 1.4614 1.1673 0.2387  0.7379  -0.0727 517 LYS A O   
3865 C CB  . LYS A 490 ? 1.7500 1.6965 1.3262 0.2720  0.7713  -0.1034 517 LYS A CB  
3866 C CG  . LYS A 490 ? 1.7047 1.6279 1.2869 0.3067  0.7406  -0.1235 517 LYS A CG  
3867 C CD  . LYS A 490 ? 1.6779 1.5416 1.1807 0.3254  0.7308  -0.1359 517 LYS A CD  
3868 C CE  . LYS A 490 ? 1.6627 1.5080 1.1789 0.3579  0.7021  -0.1574 517 LYS A CE  
3869 N NZ  . LYS A 490 ? 1.8201 1.6043 1.2602 0.3733  0.6891  -0.1707 517 LYS A NZ  
3870 N N   . MET A 491 ? 1.6625 1.6964 1.4082 0.2178  0.7642  -0.0720 518 MET A N   
3871 C CA  . MET A 491 ? 1.7755 1.7901 1.5466 0.2087  0.7408  -0.0626 518 MET A CA  
3872 C C   . MET A 491 ? 1.7247 1.6809 1.4438 0.1783  0.7374  -0.0404 518 MET A C   
3873 O O   . MET A 491 ? 1.7820 1.7446 1.4863 0.1508  0.7654  -0.0266 518 MET A O   
3874 C CB  . MET A 491 ? 1.7291 1.8230 1.5964 0.1972  0.7452  -0.0638 518 MET A CB  
3875 C CG  . MET A 491 ? 1.5842 1.6652 1.4829 0.1804  0.7106  -0.0536 518 MET A CG  
3876 S SD  . MET A 491 ? 1.4412 1.6161 1.4523 0.1748  0.7062  -0.0598 518 MET A SD  
3877 C CE  . MET A 491 ? 1.5442 1.7395 1.5793 0.2260  0.6914  -0.0820 518 MET A CE  
3878 N N   . LEU A 492 ? 1.5921 1.4928 1.2871 0.1819  0.6960  -0.0367 519 LEU A N   
3879 C CA  . LEU A 492 ? 1.5915 1.4379 1.2481 0.1564  0.6790  -0.0171 519 LEU A CA  
3880 C C   . LEU A 492 ? 1.5887 1.4463 1.3027 0.1455  0.6454  -0.0137 519 LEU A C   
3881 O O   . LEU A 492 ? 1.5500 1.4481 1.3215 0.1612  0.6317  -0.0264 519 LEU A O   
3882 C CB  . LEU A 492 ? 1.6429 1.4130 1.2145 0.1718  0.6589  -0.0172 519 LEU A CB  
3883 C CG  . LEU A 492 ? 1.7898 1.5314 1.2842 0.1754  0.6887  -0.0148 519 LEU A CG  
3884 C CD1 . LEU A 492 ? 1.8269 1.4931 1.2417 0.1878  0.6607  -0.0142 519 LEU A CD1 
3885 C CD2 . LEU A 492 ? 1.9287 1.6770 1.4136 0.1421  0.7205  0.0062  519 LEU A CD2 
3886 N N   . PRO A 493 ? 1.5967 1.4198 1.2964 0.1200  0.6317  0.0030  520 PRO A N   
3887 C CA  . PRO A 493 ? 1.4794 1.3013 1.2197 0.1145  0.5948  0.0039  520 PRO A CA  
3888 C C   . PRO A 493 ? 1.4671 1.2588 1.1903 0.1431  0.5605  -0.0074 520 PRO A C   
3889 O O   . PRO A 493 ? 1.5775 1.3190 1.2361 0.1573  0.5547  -0.0091 520 PRO A O   
3890 C CB  . PRO A 493 ? 1.3967 1.1701 1.1022 0.0875  0.5884  0.0229  520 PRO A CB  
3891 C CG  . PRO A 493 ? 1.5020 1.2793 1.1819 0.0690  0.6297  0.0338  520 PRO A CG  
3892 C CD  . PRO A 493 ? 1.5878 1.3764 1.2393 0.0937  0.6520  0.0221  520 PRO A CD  
3893 N N   . VAL A 494 ? 1.3456 1.1687 1.1267 0.1505  0.5378  -0.0152 521 VAL A N   
3894 C CA  . VAL A 494 ? 1.4621 1.2636 1.2349 0.1774  0.5090  -0.0267 521 VAL A CA  
3895 C C   . VAL A 494 ? 1.5635 1.2974 1.2797 0.1759  0.4815  -0.0208 521 VAL A C   
3896 O O   . VAL A 494 ? 1.5112 1.2093 1.1881 0.1962  0.4679  -0.0295 521 VAL A O   
3897 C CB  . VAL A 494 ? 1.4727 1.3185 1.3161 0.1822  0.4894  -0.0324 521 VAL A CB  
3898 C CG1 . VAL A 494 ? 1.2840 1.1348 1.1558 0.1557  0.4731  -0.0214 521 VAL A CG1 
3899 C CG2 . VAL A 494 ? 1.3155 1.1352 1.1488 0.2084  0.4613  -0.0425 521 VAL A CG2 
3900 N N   . ASP A 495 ? 1.4657 1.1812 1.1769 0.1523  0.4728  -0.0069 522 ASP A N   
3901 C CA  . ASP A 495 ? 1.4645 1.1202 1.1247 0.1518  0.4468  -0.0012 522 ASP A CA  
3902 C C   . ASP A 495 ? 1.5979 1.2082 1.1820 0.1573  0.4596  0.0022  522 ASP A C   
3903 O O   . ASP A 495 ? 1.7050 1.2667 1.2424 0.1617  0.4367  0.0045  522 ASP A O   
3904 C CB  . ASP A 495 ? 1.6156 1.2636 1.2914 0.1276  0.4349  0.0118  522 ASP A CB  
3905 C CG  . ASP A 495 ? 1.7281 1.3816 1.3992 0.1042  0.4647  0.0247  522 ASP A CG  
3906 O OD1 . ASP A 495 ? 1.7541 1.4301 1.4212 0.1049  0.4967  0.0234  522 ASP A OD1 
3907 O OD2 . ASP A 495 ? 1.8180 1.4525 1.4892 0.0847  0.4569  0.0359  522 ASP A OD2 
3908 N N   . GLU A 496 ? 1.5765 1.2038 1.1469 0.1568  0.4954  0.0025  523 GLU A N   
3909 C CA  . GLU A 496 ? 1.6970 1.2859 1.1927 0.1662  0.5096  0.0029  523 GLU A CA  
3910 C C   . GLU A 496 ? 1.6979 1.2979 1.1843 0.1932  0.5186  -0.0164 523 GLU A C   
3911 O O   . GLU A 496 ? 1.7039 1.2639 1.1250 0.2068  0.5177  -0.0217 523 GLU A O   
3912 C CB  . GLU A 496 ? 1.6584 1.2520 1.1332 0.1461  0.5468  0.0178  523 GLU A CB  
3913 C CG  . GLU A 496 ? 1.8636 1.4350 1.3368 0.1192  0.5407  0.0378  523 GLU A CG  
3914 C CD  . GLU A 496 ? 1.7723 1.3381 1.2150 0.0986  0.5780  0.0542  523 GLU A CD  
3915 O OE1 . GLU A 496 ? 1.9499 1.5067 1.3426 0.1080  0.6020  0.0529  523 GLU A OE1 
3916 O OE2 . GLU A 496 ? 1.8219 1.3913 1.2893 0.0723  0.5841  0.0681  523 GLU A OE2 
3917 N N   . PHE A 497 ? 1.6777 1.3300 1.2268 0.2022  0.5262  -0.0277 524 PHE A N   
3918 C CA  . PHE A 497 ? 1.4666 1.1274 1.0108 0.2308  0.5332  -0.0473 524 PHE A CA  
3919 C C   . PHE A 497 ? 1.4549 1.0715 0.9739 0.2486  0.4969  -0.0582 524 PHE A C   
3920 O O   . PHE A 497 ? 1.5372 1.1266 1.0110 0.2689  0.4988  -0.0722 524 PHE A O   
3921 C CB  . PHE A 497 ? 1.4064 1.1342 1.0279 0.2377  0.5462  -0.0555 524 PHE A CB  
3922 C CG  . PHE A 497 ? 1.4764 1.2090 1.1044 0.2702  0.5428  -0.0760 524 PHE A CG  
3923 C CD1 . PHE A 497 ? 1.4873 1.2114 1.0729 0.2893  0.5672  -0.0888 524 PHE A CD1 
3924 C CD2 . PHE A 497 ? 1.4149 1.1581 1.0893 0.2823  0.5157  -0.0824 524 PHE A CD2 
3925 C CE1 . PHE A 497 ? 1.4872 1.2111 1.0780 0.3206  0.5638  -0.1091 524 PHE A CE1 
3926 C CE2 . PHE A 497 ? 1.4620 1.2033 1.1408 0.3128  0.5121  -0.1002 524 PHE A CE2 
3927 C CZ  . PHE A 497 ? 1.4382 1.1688 1.0760 0.3324  0.5359  -0.1143 524 PHE A CZ  
3928 N N   . LEU A 498 ? 1.4624 1.0714 1.0096 0.2404  0.4644  -0.0529 525 LEU A N   
3929 C CA  . LEU A 498 ? 1.5457 1.1144 1.0719 0.2532  0.4302  -0.0622 525 LEU A CA  
3930 C C   . LEU A 498 ? 1.5395 1.0518 0.9884 0.2536  0.4205  -0.0617 525 LEU A C   
3931 O O   . LEU A 498 ? 1.5336 1.0167 0.9453 0.2719  0.4128  -0.0771 525 LEU A O   
3932 C CB  . LEU A 498 ? 1.4152 0.9928 0.9889 0.2419  0.4005  -0.0554 525 LEU A CB  
3933 C CG  . LEU A 498 ? 1.3080 0.9426 0.9571 0.2393  0.4064  -0.0540 525 LEU A CG  
3934 C CD1 . LEU A 498 ? 1.2670 0.9040 0.9513 0.2280  0.3758  -0.0476 525 LEU A CD1 
3935 C CD2 . LEU A 498 ? 1.2671 0.9225 0.9382 0.2646  0.4146  -0.0693 525 LEU A CD2 
3936 N N   . PRO A 499 ? 1.5451 1.0380 0.9650 0.2355  0.4194  -0.0454 526 PRO A N   
3937 C CA  . PRO A 499 ? 1.6287 1.0690 0.9717 0.2390  0.4085  -0.0450 526 PRO A CA  
3938 C C   . PRO A 499 ? 1.6950 1.1227 0.9828 0.2537  0.4337  -0.0551 526 PRO A C   
3939 O O   . PRO A 499 ? 1.6983 1.0837 0.9243 0.2635  0.4198  -0.0627 526 PRO A O   
3940 C CB  . PRO A 499 ? 1.6389 1.0679 0.9684 0.2176  0.4098  -0.0230 526 PRO A CB  
3941 C CG  . PRO A 499 ? 1.4998 0.9655 0.9024 0.2032  0.4047  -0.0160 526 PRO A CG  
3942 C CD  . PRO A 499 ? 1.4588 0.9721 0.9125 0.2119  0.4240  -0.0272 526 PRO A CD  
3943 N N   . VAL A 500 ? 1.6143 1.0800 0.9226 0.2555  0.4704  -0.0565 527 VAL A N   
3944 C CA  . VAL A 500 ? 1.6634 1.1230 0.9259 0.2735  0.4952  -0.0706 527 VAL A CA  
3945 C C   . VAL A 500 ? 1.6278 1.0754 0.8933 0.2979  0.4775  -0.0949 527 VAL A C   
3946 O O   . VAL A 500 ? 1.6554 1.0667 0.8602 0.3128  0.4744  -0.1092 527 VAL A O   
3947 C CB  . VAL A 500 ? 1.7070 1.2185 1.0008 0.2700  0.5395  -0.0678 527 VAL A CB  
3948 C CG1 . VAL A 500 ? 1.6790 1.1901 0.9325 0.2923  0.5658  -0.0863 527 VAL A CG1 
3949 C CG2 . VAL A 500 ? 1.7066 1.2201 0.9855 0.2436  0.5593  -0.0437 527 VAL A CG2 
3950 N N   . MET A 501 ? 1.5891 1.0637 0.9226 0.3019  0.4641  -0.0998 528 MET A N   
3951 C CA  . MET A 501 ? 1.6071 1.0706 0.9478 0.3255  0.4516  -0.1217 528 MET A CA  
3952 C C   . MET A 501 ? 1.5980 1.0078 0.9003 0.3276  0.4136  -0.1295 528 MET A C   
3953 O O   . MET A 501 ? 1.6273 1.0107 0.9065 0.3466  0.4062  -0.1499 528 MET A O   
3954 C CB  . MET A 501 ? 1.5202 1.0271 0.9423 0.3294  0.4483  -0.1222 528 MET A CB  
3955 C CG  . MET A 501 ? 1.4796 1.0444 0.9428 0.3339  0.4858  -0.1218 528 MET A CG  
3956 S SD  . MET A 501 ? 1.7749 1.3360 1.1874 0.3579  0.5220  -0.1411 528 MET A SD  
3957 C CE  . MET A 501 ? 1.5461 1.0777 0.9608 0.3849  0.4931  -0.1649 528 MET A CE  
3958 N N   . PHE A 502 ? 1.5282 0.9215 0.8244 0.3089  0.3892  -0.1150 529 PHE A N   
3959 C CA  . PHE A 502 ? 1.6187 0.9640 0.8707 0.3097  0.3561  -0.1227 529 PHE A CA  
3960 C C   . PHE A 502 ? 1.6892 1.0041 0.8685 0.3044  0.3576  -0.1162 529 PHE A C   
3961 O O   . PHE A 502 ? 1.6911 0.9742 0.8404 0.2995  0.3274  -0.1160 529 PHE A O   
3962 C CB  . PHE A 502 ? 1.5626 0.9087 0.8575 0.2968  0.3222  -0.1153 529 PHE A CB  
3963 C CG  . PHE A 502 ? 1.6553 1.0268 0.9834 0.2767  0.3229  -0.0928 529 PHE A CG  
3964 C CD1 . PHE A 502 ? 1.5687 0.9845 0.9630 0.2708  0.3344  -0.0849 529 PHE A CD1 
3965 C CD2 . PHE A 502 ? 1.7223 1.0717 1.0163 0.2644  0.3089  -0.0808 529 PHE A CD2 
3966 C CE1 . PHE A 502 ? 1.5266 0.9631 0.9511 0.2516  0.3337  -0.0667 529 PHE A CE1 
3967 C CE2 . PHE A 502 ? 1.6307 0.9985 0.9548 0.2469  0.3087  -0.0616 529 PHE A CE2 
3968 C CZ  . PHE A 502 ? 1.5085 0.9190 0.8976 0.2396  0.3214  -0.0553 529 PHE A CZ  
3969 N N   . ASP A 503 ? 1.6801 1.0057 0.8309 0.3054  0.3925  -0.1104 530 ASP A N   
3970 C CA  . ASP A 503 ? 1.7673 1.0597 0.8357 0.3068  0.3996  -0.1083 530 ASP A CA  
3971 C C   . ASP A 503 ? 1.8704 1.1398 0.9148 0.2908  0.3763  -0.0889 530 ASP A C   
3972 O O   . ASP A 503 ? 1.7670 0.9979 0.7512 0.2949  0.3550  -0.0929 530 ASP A O   
3973 C CB  . ASP A 503 ? 1.7920 1.0487 0.8063 0.3263  0.3884  -0.1340 530 ASP A CB  
3974 C CG  . ASP A 503 ? 2.0047 1.2395 0.9360 0.3332  0.4101  -0.1362 530 ASP A CG  
3975 O OD1 . ASP A 503 ? 2.1206 1.3691 1.0380 0.3229  0.4372  -0.1165 530 ASP A OD1 
3976 O OD2 . ASP A 503 ? 2.0866 1.2955 0.9747 0.3451  0.3963  -0.1555 530 ASP A OD2 
3977 N N   . LYS A 504 ? 1.7126 1.0065 0.8047 0.2734  0.3799  -0.0686 531 LYS A N   
3978 C CA  . LYS A 504 ? 1.6505 0.9239 0.7248 0.2594  0.3610  -0.0491 531 LYS A CA  
3979 C C   . LYS A 504 ? 1.7857 1.0694 0.8569 0.2437  0.3904  -0.0256 531 LYS A C   
3980 O O   . LYS A 504 ? 1.7660 1.0271 0.8156 0.2333  0.3781  -0.0078 531 LYS A O   
3981 C CB  . LYS A 504 ? 1.7655 1.0495 0.8994 0.2516  0.3286  -0.0477 531 LYS A CB  
3982 C CG  . LYS A 504 ? 1.7583 1.0237 0.8880 0.2619  0.2941  -0.0669 531 LYS A CG  
3983 C CD  . LYS A 504 ? 1.7523 0.9756 0.8089 0.2675  0.2725  -0.0697 531 LYS A CD  
3984 C CE  . LYS A 504 ? 1.8128 1.0224 0.8759 0.2719  0.2344  -0.0871 531 LYS A CE  
3985 N NZ  . LYS A 504 ? 2.0216 1.1961 1.0199 0.2761  0.2089  -0.0895 531 LYS A NZ  
3986 N N   . HIS A 505 ? 1.8050 1.1220 0.8981 0.2416  0.4287  -0.0253 532 HIS A N   
3987 C CA  . HIS A 505 ? 1.7628 1.0922 0.8588 0.2228  0.4583  -0.0032 532 HIS A CA  
3988 C C   . HIS A 505 ? 1.8030 1.0896 0.8100 0.2220  0.4684  0.0098  532 HIS A C   
3989 O O   . HIS A 505 ? 1.9057 1.1732 0.8537 0.2379  0.4737  -0.0025 532 HIS A O   
3990 C CB  . HIS A 505 ? 1.6822 1.0625 0.8229 0.2212  0.4977  -0.0082 532 HIS A CB  
3991 C CG  . HIS A 505 ? 1.7367 1.1423 0.9108 0.1965  0.5229  0.0124  532 HIS A CG  
3992 N ND1 . HIS A 505 ? 1.8690 1.2599 0.9944 0.1836  0.5527  0.0298  532 HIS A ND1 
3993 C CD2 . HIS A 505 ? 1.7205 1.1632 0.9702 0.1808  0.5222  0.0181  532 HIS A CD2 
3994 C CE1 . HIS A 505 ? 1.9529 1.3698 1.1247 0.1598  0.5697  0.0451  532 HIS A CE1 
3995 N NE2 . HIS A 505 ? 1.8893 1.3390 1.1371 0.1580  0.5510  0.0374  532 HIS A NE2 
3996 N N   . PRO A 506 ? 1.8809 1.1487 0.8732 0.2044  0.4703  0.0345  533 PRO A N   
3997 C CA  . PRO A 506 ? 1.9770 1.1976 0.8790 0.2048  0.4759  0.0497  533 PRO A CA  
3998 C C   . PRO A 506 ? 1.9209 1.1501 0.7828 0.2028  0.5225  0.0534  533 PRO A C   
3999 O O   . PRO A 506 ? 2.0434 1.2372 0.8213 0.2122  0.5269  0.0557  533 PRO A O   
4000 C CB  . PRO A 506 ? 1.8799 1.0797 0.7896 0.1860  0.4662  0.0755  533 PRO A CB  
4001 C CG  . PRO A 506 ? 1.8734 1.1205 0.8749 0.1699  0.4770  0.0755  533 PRO A CG  
4002 C CD  . PRO A 506 ? 1.7945 1.0779 0.8479 0.1845  0.4645  0.0491  533 PRO A CD  
4003 N N   . VAL A 507 ? 1.8931 1.1707 0.8116 0.1908  0.5576  0.0537  534 VAL A N   
4004 C CA  . VAL A 507 ? 2.0466 1.3406 0.9342 0.1872  0.6055  0.0567  534 VAL A CA  
4005 C C   . VAL A 507 ? 2.0627 1.3713 0.9353 0.2128  0.6097  0.0282  534 VAL A C   
4006 O O   . VAL A 507 ? 2.0758 1.4230 1.0095 0.2234  0.6097  0.0080  534 VAL A O   
4007 C CB  . VAL A 507 ? 2.0057 1.3533 0.9665 0.1649  0.6401  0.0649  534 VAL A CB  
4008 C CG1 . VAL A 507 ? 1.9934 1.3712 0.9413 0.1587  0.6807  0.0660  534 VAL A CG1 
4009 C CG2 . VAL A 507 ? 1.9025 1.2313 0.8795 0.1383  0.6330  0.0912  534 VAL A CG2 
4010 N N   . SER A 508 ? 2.0538 1.3349 0.8550 0.2217  0.6065  0.0265  535 SER A N   
4011 C CA  . SER A 508 ? 2.2631 1.5596 1.0549 0.2433  0.6067  -0.0011 535 SER A CA  
4012 C C   . SER A 508 ? 2.2749 1.6333 1.1162 0.2397  0.6463  -0.0086 535 SER A C   
4013 O O   . SER A 508 ? 2.2223 1.6072 1.0881 0.2584  0.6476  -0.0343 535 SER A O   
4014 C CB  . SER A 508 ? 2.2055 1.4594 0.9073 0.2519  0.5943  -0.0008 535 SER A CB  
4015 O OG  . SER A 508 ? 2.3923 1.5948 1.0524 0.2587  0.5533  0.0017  535 SER A OG  
4016 N N   . GLU A 509 ? 2.2524 1.6346 1.1106 0.2157  0.6776  0.0130  536 GLU A N   
4017 C CA  . GLU A 509 ? 2.1402 1.5876 1.0483 0.2106  0.7154  0.0060  536 GLU A CA  
4018 C C   . GLU A 509 ? 2.1892 1.6872 1.1885 0.2176  0.7160  -0.0104 536 GLU A C   
4019 O O   . GLU A 509 ? 2.1515 1.6988 1.1888 0.2300  0.7325  -0.0300 536 GLU A O   
4020 C CB  . GLU A 509 ? 2.0999 1.5608 1.0094 0.1794  0.7460  0.0335  536 GLU A CB  
4021 C CG  . GLU A 509 ? 2.2241 1.6376 1.0440 0.1723  0.7481  0.0518  536 GLU A CG  
4022 C CD  . GLU A 509 ? 2.6000 2.0300 1.3799 0.1860  0.7655  0.0365  536 GLU A CD  
4023 O OE1 . GLU A 509 ? 2.5767 2.0614 1.4047 0.1973  0.7822  0.0139  536 GLU A OE1 
4024 O OE2 . GLU A 509 ? 2.5300 1.9189 1.2300 0.1864  0.7618  0.0468  536 GLU A OE2 
4025 N N   . TYR A 510 ? 2.1684 1.6559 1.2035 0.2109  0.6973  -0.0030 537 TYR A N   
4026 C CA  . TYR A 510 ? 2.0353 1.5690 1.1557 0.2183  0.6946  -0.0175 537 TYR A CA  
4027 C C   . TYR A 510 ? 1.9410 1.4669 1.0612 0.2498  0.6709  -0.0455 537 TYR A C   
4028 O O   . TYR A 510 ? 1.8891 1.4623 1.0627 0.2638  0.6798  -0.0639 537 TYR A O   
4029 C CB  . TYR A 510 ? 1.9114 1.4322 1.0640 0.2035  0.6793  -0.0030 537 TYR A CB  
4030 C CG  . TYR A 510 ? 1.9885 1.5170 1.1525 0.1701  0.7009  0.0238  537 TYR A CG  
4031 C CD1 . TYR A 510 ? 2.0494 1.6087 1.2126 0.1535  0.7348  0.0325  537 TYR A CD1 
4032 C CD2 . TYR A 510 ? 1.9784 1.4899 1.1698 0.1516  0.6747  0.0392  537 TYR A CD2 
4033 C CE1 . TYR A 510 ? 1.9515 1.5145 1.1265 0.1205  0.7529  0.0567  537 TYR A CE1 
4034 C CE2 . TYR A 510 ? 2.0483 1.5613 1.2498 0.1205  0.6930  0.0625  537 TYR A CE2 
4035 C CZ  . TYR A 510 ? 2.0969 1.6315 1.2846 0.1049  0.7369  0.0719  537 TYR A CZ  
4036 O OH  . TYR A 510 ? 2.2165 1.7500 1.4167 0.0711  0.7529  0.0951  537 TYR A OH  
4037 N N   . LYS A 511 ? 1.9798 1.4458 1.0409 0.2609  0.6389  -0.0493 538 LYS A N   
4038 C CA  . LYS A 511 ? 2.0281 1.4797 1.0859 0.2873  0.6132  -0.0757 538 LYS A CA  
4039 C C   . LYS A 511 ? 2.0012 1.4706 1.0403 0.3030  0.6291  -0.0947 538 LYS A C   
4040 O O   . LYS A 511 ? 2.1437 1.6169 1.2015 0.3243  0.6155  -0.1186 538 LYS A O   
4041 C CB  . LYS A 511 ? 1.9638 1.3498 0.9591 0.2919  0.5756  -0.0756 538 LYS A CB  
4042 C CG  . LYS A 511 ? 1.9650 1.3356 0.9832 0.2761  0.5521  -0.0579 538 LYS A CG  
4043 C CD  . LYS A 511 ? 2.0507 1.3657 1.0148 0.2799  0.5104  -0.0584 538 LYS A CD  
4044 C CE  . LYS A 511 ? 2.1018 1.3771 0.9707 0.2795  0.5205  -0.0486 538 LYS A CE  
4045 N NZ  . LYS A 511 ? 2.1746 1.4007 0.9953 0.2823  0.4775  -0.0470 538 LYS A NZ  
4046 N N   . ALA A 512 ? 2.1947 1.6741 1.1975 0.2926  0.6574  -0.0847 539 ALA A N   
4047 C CA  . ALA A 512 ? 2.0167 1.5158 0.9998 0.3073  0.6749  -0.1037 539 ALA A CA  
4048 C C   . ALA A 512 ? 2.0371 1.6043 1.0992 0.3161  0.6972  -0.1185 539 ALA A C   
4049 O O   . ALA A 512 ? 2.1424 1.7234 1.2047 0.3372  0.7004  -0.1428 539 ALA A O   
4050 C CB  . ALA A 512 ? 2.0908 1.5846 1.0141 0.2923  0.7002  -0.0876 539 ALA A CB  
4051 N N   . HIS A 513 ? 2.0242 1.6353 1.1542 0.3007  0.7117  -0.1053 540 HIS A N   
4052 C CA  . HIS A 513 ? 1.9126 1.5931 1.1228 0.3098  0.7294  -0.1192 540 HIS A CA  
4053 C C   . HIS A 513 ? 1.8784 1.5549 1.1280 0.3353  0.7011  -0.1402 540 HIS A C   
4054 O O   . HIS A 513 ? 1.9021 1.6281 1.2073 0.3511  0.7108  -0.1569 540 HIS A O   
4055 C CB  . HIS A 513 ? 1.8422 1.5712 1.1163 0.2847  0.7486  -0.0997 540 HIS A CB  
4056 C CG  . HIS A 513 ? 2.0401 1.7830 1.2885 0.2576  0.7804  -0.0797 540 HIS A CG  
4057 N ND1 . HIS A 513 ? 2.2232 1.9185 1.4222 0.2342  0.7767  -0.0541 540 HIS A ND1 
4058 C CD2 . HIS A 513 ? 1.9220 1.7207 1.1877 0.2497  0.8161  -0.0812 540 HIS A CD2 
4059 C CE1 . HIS A 513 ? 2.1236 1.8411 1.3094 0.2122  0.8082  -0.0394 540 HIS A CE1 
4060 N NE2 . HIS A 513 ? 1.9619 1.7439 1.1879 0.2203  0.8332  -0.0556 540 HIS A NE2 
4061 N N   . PHE A 514 ? 1.9822 1.6338 0.9487 0.2998  0.5644  -0.2369 541 PHE A N   
4062 C CA  . PHE A 514 ? 1.9688 1.6163 0.9755 0.3282  0.5325  -0.2486 541 PHE A CA  
4063 C C   . PHE A 514 ? 1.9922 1.5926 0.9561 0.3460  0.5100  -0.2514 541 PHE A C   
4064 O O   . PHE A 514 ? 2.1431 1.6793 1.0604 0.3435  0.4939  -0.2329 541 PHE A O   
4065 C CB  . PHE A 514 ? 1.8599 1.4731 0.8888 0.3270  0.5143  -0.2307 541 PHE A CB  
4066 C CG  . PHE A 514 ? 1.8240 1.4870 0.9014 0.3109  0.5347  -0.2314 541 PHE A CG  
4067 C CD1 . PHE A 514 ? 1.8507 1.5062 0.9034 0.2798  0.5617  -0.2148 541 PHE A CD1 
4068 C CD2 . PHE A 514 ? 1.8540 1.5696 1.0006 0.3260  0.5268  -0.2491 541 PHE A CD2 
4069 C CE1 . PHE A 514 ? 1.8198 1.5229 0.9202 0.2620  0.5820  -0.2181 541 PHE A CE1 
4070 C CE2 . PHE A 514 ? 1.8828 1.6513 1.0773 0.3116  0.5443  -0.2536 541 PHE A CE2 
4071 C CZ  . PHE A 514 ? 1.7627 1.5269 0.9362 0.2786  0.5727  -0.2392 541 PHE A CZ  
4072 N N   . SER A 515 ? 2.0164 1.6507 0.9976 0.3642  0.5085  -0.2768 542 SER A N   
4073 C CA  . SER A 515 ? 2.0731 1.6711 1.0135 0.3781  0.4928  -0.2839 542 SER A CA  
4074 C C   . SER A 515 ? 2.1490 1.6862 1.0883 0.3915  0.4576  -0.2766 542 SER A C   
4075 O O   . SER A 515 ? 2.2615 1.7500 1.1538 0.3920  0.4429  -0.2709 542 SER A O   
4076 C CB  . SER A 515 ? 2.0058 1.6537 0.9688 0.3943  0.5008  -0.3143 542 SER A CB  
4077 O OG  . SER A 515 ? 1.9595 1.6351 0.9837 0.4108  0.4915  -0.3270 542 SER A OG  
4078 N N   . LEU A 516 ? 1.9797 1.5215 0.9705 0.4017  0.4438  -0.2780 543 LEU A N   
4079 C CA  . LEU A 516 ? 1.9616 1.4507 0.9570 0.4118  0.4130  -0.2731 543 LEU A CA  
4080 C C   . LEU A 516 ? 1.9598 1.4292 0.9721 0.4009  0.4047  -0.2519 543 LEU A C   
4081 O O   . LEU A 516 ? 2.0312 1.5367 1.0886 0.4003  0.4123  -0.2503 543 LEU A O   
4082 C CB  . LEU A 516 ? 1.9583 1.4595 0.9934 0.4336  0.4025  -0.2908 543 LEU A CB  
4083 C CG  . LEU A 516 ? 2.0001 1.4468 1.0408 0.4410  0.3744  -0.2869 543 LEU A CG  
4084 C CD1 . LEU A 516 ? 2.0103 1.4075 1.0022 0.4344  0.3616  -0.2868 543 LEU A CD1 
4085 C CD2 . LEU A 516 ? 1.8723 1.3253 0.9409 0.4626  0.3682  -0.3032 543 LEU A CD2 
4086 N N   . ARG A 517 ? 1.9421 1.3575 0.9193 0.3932  0.3882  -0.2380 544 ARG A N   
4087 C CA  . ARG A 517 ? 1.8986 1.2900 0.8857 0.3828  0.3785  -0.2186 544 ARG A CA  
4088 C C   . ARG A 517 ? 1.9019 1.2462 0.8897 0.3878  0.3480  -0.2189 544 ARG A C   
4089 O O   . ARG A 517 ? 1.8909 1.1962 0.8437 0.3806  0.3341  -0.2111 544 ARG A O   
4090 C CB  . ARG A 517 ? 1.8523 1.2266 0.7923 0.3652  0.3913  -0.2006 544 ARG A CB  
4091 C CG  . ARG A 517 ? 1.8771 1.2962 0.8108 0.3545  0.4256  -0.2016 544 ARG A CG  
4092 C CD  . ARG A 517 ? 1.9152 1.3071 0.7976 0.3342  0.4401  -0.1797 544 ARG A CD  
4093 N NE  . ARG A 517 ? 2.0505 1.3906 0.8692 0.3373  0.4231  -0.1731 544 ARG A NE  
4094 C CZ  . ARG A 517 ? 2.0912 1.4325 0.8652 0.3391  0.4311  -0.1790 544 ARG A CZ  
4095 N NH1 . ARG A 517 ? 2.0385 1.4290 0.8234 0.3368  0.4569  -0.1920 544 ARG A NH1 
4096 N NH2 . ARG A 517 ? 2.1119 1.4082 0.8302 0.3441  0.4119  -0.1738 544 ARG A NH2 
4097 N N   . ASN A 518 ? 1.8336 1.1832 0.8615 0.3997  0.3379  -0.2288 545 ASN A N   
4098 C CA  . ASN A 518 ? 1.8822 1.1910 0.9141 0.4015  0.3134  -0.2328 545 ASN A CA  
4099 C C   . ASN A 518 ? 1.8090 1.1117 0.8831 0.3987  0.3019  -0.2217 545 ASN A C   
4100 O O   . ASN A 518 ? 1.7308 1.0101 0.8211 0.4010  0.2870  -0.2264 545 ASN A O   
4101 C CB  . ASN A 518 ? 1.8973 1.2048 0.9326 0.4154  0.3116  -0.2525 545 ASN A CB  
4102 C CG  . ASN A 518 ? 1.9385 1.2814 1.0149 0.4303  0.3209  -0.2569 545 ASN A CG  
4103 O OD1 . ASN A 518 ? 1.7834 1.1660 0.8838 0.4301  0.3335  -0.2499 545 ASN A OD1 
4104 N ND2 . ASN A 518 ? 1.9434 1.2724 1.0273 0.4436  0.3147  -0.2700 545 ASN A ND2 
4105 N N   . LEU A 519 ? 1.7691 1.0921 0.8605 0.3922  0.3099  -0.2074 546 LEU A N   
4106 C CA  . LEU A 519 ? 1.7653 1.0889 0.8986 0.3904  0.2997  -0.1973 546 LEU A CA  
4107 C C   . LEU A 519 ? 1.7385 1.0193 0.8612 0.3783  0.2786  -0.1908 546 LEU A C   
4108 O O   . LEU A 519 ? 1.8939 1.1549 0.9804 0.3695  0.2753  -0.1869 546 LEU A O   
4109 C CB  . LEU A 519 ? 1.6283 0.9892 0.7839 0.3859  0.3154  -0.1871 546 LEU A CB  
4110 C CG  . LEU A 519 ? 1.5645 0.9438 0.7711 0.3880  0.3087  -0.1798 546 LEU A CG  
4111 C CD1 . LEU A 519 ? 1.5508 0.9654 0.7922 0.4062  0.3113  -0.1904 546 LEU A CD1 
4112 C CD2 . LEU A 519 ? 1.5341 0.9377 0.7526 0.3771  0.3223  -0.1697 546 LEU A CD2 
4113 N N   . HIS A 520 ? 1.6486 0.9165 0.8014 0.3781  0.2643  -0.1906 547 HIS A N   
4114 C CA  . HIS A 520 ? 1.8178 1.0546 0.9712 0.3645  0.2449  -0.1876 547 HIS A CA  
4115 C C   . HIS A 520 ? 1.7296 0.9800 0.9154 0.3588  0.2422  -0.1720 547 HIS A C   
4116 O O   . HIS A 520 ? 1.5198 0.7834 0.7432 0.3625  0.2408  -0.1676 547 HIS A O   
4117 C CB  . HIS A 520 ? 1.7423 0.9558 0.9071 0.3631  0.2344  -0.1982 547 HIS A CB  
4118 C CG  . HIS A 520 ? 1.8403 1.0421 0.9787 0.3703  0.2385  -0.2155 547 HIS A CG  
4119 N ND1 . HIS A 520 ? 1.8962 1.0836 0.9970 0.3653  0.2337  -0.2272 547 HIS A ND1 
4120 C CD2 . HIS A 520 ? 2.0002 1.2024 1.1432 0.3836  0.2459  -0.2241 547 HIS A CD2 
4121 C CE1 . HIS A 520 ? 1.8329 1.0143 0.9190 0.3736  0.2389  -0.2429 547 HIS A CE1 
4122 N NE2 . HIS A 520 ? 1.9557 1.1442 1.0665 0.3849  0.2466  -0.2412 547 HIS A NE2 
4123 N N   . ALA A 521 ? 1.5414 0.7868 0.7094 0.3508  0.2410  -0.1638 548 ALA A N   
4124 C CA  . ALA A 521 ? 1.6309 0.8893 0.8266 0.3456  0.2405  -0.1501 548 ALA A CA  
4125 C C   . ALA A 521 ? 1.6462 0.8785 0.8372 0.3338  0.2194  -0.1473 548 ALA A C   
4126 O O   . ALA A 521 ? 1.5216 0.7299 0.6716 0.3308  0.2111  -0.1518 548 ALA A O   
4127 C CB  . ALA A 521 ? 1.6150 0.8917 0.7959 0.3462  0.2615  -0.1429 548 ALA A CB  
4128 N N   . PHE A 522 ? 1.4777 0.7191 0.7108 0.3283  0.2098  -0.1410 549 PHE A N   
4129 C CA  . PHE A 522 ? 1.4798 0.7063 0.7198 0.3168  0.1892  -0.1401 549 PHE A CA  
4130 C C   . PHE A 522 ? 1.4455 0.6891 0.7155 0.3142  0.1896  -0.1266 549 PHE A C   
4131 O O   . PHE A 522 ? 1.4368 0.7057 0.7257 0.3204  0.2060  -0.1199 549 PHE A O   
4132 C CB  . PHE A 522 ? 1.4119 0.6326 0.6767 0.3084  0.1763  -0.1495 549 PHE A CB  
4133 C CG  . PHE A 522 ? 1.5834 0.7870 0.8245 0.3101  0.1781  -0.1649 549 PHE A CG  
4134 C CD1 . PHE A 522 ? 1.6318 0.8408 0.8775 0.3201  0.1920  -0.1664 549 PHE A CD1 
4135 C CD2 . PHE A 522 ? 1.5673 0.7518 0.7824 0.3029  0.1646  -0.1802 549 PHE A CD2 
4136 C CE1 . PHE A 522 ? 1.6443 0.8353 0.8684 0.3219  0.1938  -0.1816 549 PHE A CE1 
4137 C CE2 . PHE A 522 ? 1.5704 0.7412 0.7663 0.3034  0.1666  -0.1970 549 PHE A CE2 
4138 C CZ  . PHE A 522 ? 1.5971 0.7689 0.7973 0.3125  0.1818  -0.1971 549 PHE A CZ  
4139 N N   . SER A 523 ? 1.3642 0.5979 0.6413 0.3054  0.1708  -0.1252 550 SER A N   
4140 C CA  . SER A 523 ? 1.3243 0.5726 0.6321 0.3021  0.1680  -0.1139 550 SER A CA  
4141 C C   . SER A 523 ? 1.4188 0.6719 0.7600 0.2912  0.1459  -0.1169 550 SER A C   
4142 O O   . SER A 523 ? 1.4240 0.6618 0.7516 0.2854  0.1305  -0.1289 550 SER A O   
4143 C CB  . SER A 523 ? 1.4479 0.6747 0.7184 0.3042  0.1710  -0.1069 550 SER A CB  
4144 O OG  . SER A 523 ? 1.4284 0.6719 0.7353 0.2983  0.1672  -0.0958 550 SER A OG  
4145 N N   . VAL A 524 ? 1.2587 0.5378 0.6451 0.2882  0.1452  -0.1085 551 VAL A N   
4146 C CA  . VAL A 524 ? 1.3450 0.6328 0.7639 0.2772  0.1263  -0.1109 551 VAL A CA  
4147 C C   . VAL A 524 ? 1.3876 0.6605 0.7894 0.2753  0.1087  -0.1118 551 VAL A C   
4148 O O   . VAL A 524 ? 1.5323 0.7927 0.9112 0.2818  0.1139  -0.1030 551 VAL A O   
4149 C CB  . VAL A 524 ? 1.3131 0.6345 0.7811 0.2765  0.1301  -0.1016 551 VAL A CB  
4150 C CG1 . VAL A 524 ? 1.3491 0.6800 0.8489 0.2644  0.1140  -0.1060 551 VAL A CG1 
4151 C CG2 . VAL A 524 ? 1.3032 0.6380 0.7789 0.2851  0.1466  -0.0998 551 VAL A CG2 
4152 N N   . GLU A 525 ? 1.4000 0.6716 0.8099 0.2671  0.0886  -0.1238 552 GLU A N   
4153 C CA  . GLU A 525 ? 1.3601 0.6208 0.7540 0.2692  0.0669  -0.1272 552 GLU A CA  
4154 C C   . GLU A 525 ? 1.2224 0.5063 0.6597 0.2592  0.0487  -0.1355 552 GLU A C   
4155 O O   . GLU A 525 ? 1.3063 0.5952 0.7545 0.2498  0.0429  -0.1528 552 GLU A O   
4156 C CB  . GLU A 525 ? 1.4253 0.6596 0.7673 0.2750  0.0570  -0.1416 552 GLU A CB  
4157 C CG  . GLU A 525 ? 1.4529 0.6772 0.7737 0.2820  0.0296  -0.1483 552 GLU A CG  
4158 C CD  . GLU A 525 ? 1.6444 0.8648 0.9589 0.2867  0.0290  -0.1250 552 GLU A CD  
4159 O OE1 . GLU A 525 ? 1.6798 0.8902 0.9764 0.2877  0.0512  -0.1083 552 GLU A OE1 
4160 O OE2 . GLU A 525 ? 1.5099 0.7389 0.8390 0.2879  0.0070  -0.1244 552 GLU A OE2 
4161 N N   . PRO A 526 ? 1.3240 0.6223 0.7870 0.2599  0.0406  -0.1255 553 PRO A N   
4162 C CA  . PRO A 526 ? 1.2874 0.5786 0.7426 0.2672  0.0481  -0.1072 553 PRO A CA  
4163 C C   . PRO A 526 ? 1.2361 0.5454 0.7147 0.2664  0.0736  -0.0958 553 PRO A C   
4164 O O   . PRO A 526 ? 1.3097 0.6372 0.8111 0.2623  0.0822  -0.0994 553 PRO A O   
4165 C CB  . PRO A 526 ? 1.1251 0.4326 0.6111 0.2651  0.0272  -0.1063 553 PRO A CB  
4166 C CG  . PRO A 526 ? 1.0865 0.4244 0.6155 0.2544  0.0206  -0.1195 553 PRO A CG  
4167 C CD  . PRO A 526 ? 1.2481 0.5715 0.7522 0.2515  0.0233  -0.1351 553 PRO A CD  
4168 N N   . LEU A 527 ? 1.2338 0.5366 0.7050 0.2711  0.0864  -0.0835 554 LEU A N   
4169 C CA  . LEU A 527 ? 1.2604 0.5858 0.7535 0.2734  0.1104  -0.0778 554 LEU A CA  
4170 C C   . LEU A 527 ? 1.2211 0.5896 0.7736 0.2686  0.1056  -0.0767 554 LEU A C   
4171 O O   . LEU A 527 ? 1.1108 0.4892 0.6876 0.2627  0.0873  -0.0771 554 LEU A O   
4172 C CB  . LEU A 527 ? 1.2461 0.5691 0.7254 0.2703  0.1259  -0.0662 554 LEU A CB  
4173 C CG  . LEU A 527 ? 1.3436 0.6390 0.7677 0.2706  0.1367  -0.0633 554 LEU A CG  
4174 C CD1 . LEU A 527 ? 1.2540 0.5439 0.6641 0.2601  0.1496  -0.0494 554 LEU A CD1 
4175 C CD2 . LEU A 527 ? 1.2828 0.5856 0.6983 0.2796  0.1575  -0.0713 554 LEU A CD2 
4176 N N   . LEU A 528 ? 1.1937 0.5890 0.7673 0.2733  0.1213  -0.0764 555 LEU A N   
4177 C CA  . LEU A 528 ? 1.1475 0.5829 0.7704 0.2723  0.1181  -0.0755 555 LEU A CA  
4178 C C   . LEU A 528 ? 1.1343 0.5977 0.7825 0.2785  0.1311  -0.0728 555 LEU A C   
4179 O O   . LEU A 528 ? 1.0334 0.5325 0.7229 0.2788  0.1262  -0.0730 555 LEU A O   
4180 C CB  . LEU A 528 ? 0.9915 0.4368 0.6188 0.2758  0.1233  -0.0781 555 LEU A CB  
4181 C CG  . LEU A 528 ? 1.1735 0.5909 0.7790 0.2680  0.1153  -0.0844 555 LEU A CG  
4182 C CD1 . LEU A 528 ? 1.1124 0.5323 0.7205 0.2715  0.1233  -0.0850 555 LEU A CD1 
4183 C CD2 . LEU A 528 ? 1.1301 0.5471 0.7518 0.2561  0.0962  -0.0890 555 LEU A CD2 
4184 N N   . ILE A 529 ? 1.1156 0.5640 0.7393 0.2830  0.1494  -0.0723 556 ILE A N   
4185 C CA  . ILE A 529 ? 1.0453 0.5280 0.6966 0.2848  0.1664  -0.0739 556 ILE A CA  
4186 C C   . ILE A 529 ? 1.0729 0.5423 0.7065 0.2661  0.1732  -0.0666 556 ILE A C   
4187 O O   . ILE A 529 ? 1.2886 0.7251 0.8767 0.2627  0.1786  -0.0627 556 ILE A O   
4188 C CB  . ILE A 529 ? 1.0848 0.5976 0.7408 0.3005  0.1860  -0.0817 556 ILE A CB  
4189 C CG1 . ILE A 529 ? 1.1412 0.6962 0.8376 0.3063  0.1729  -0.0829 556 ILE A CG1 
4190 C CG2 . ILE A 529 ? 1.0066 0.5564 0.6795 0.2938  0.2075  -0.0860 556 ILE A CG2 
4191 C CD1 . ILE A 529 ? 1.2528 0.8424 0.9567 0.3211  0.1842  -0.0892 556 ILE A CD1 
4192 N N   . TYR A 530 ? 0.9990 0.4905 0.6653 0.2538  0.1739  -0.0649 557 TYR A N   
4193 C CA  . TYR A 530 ? 1.0305 0.5050 0.6815 0.2337  0.1837  -0.0572 557 TYR A CA  
4194 C C   . TYR A 530 ? 1.1102 0.6344 0.8033 0.2237  0.2054  -0.0654 557 TYR A C   
4195 O O   . TYR A 530 ? 1.1045 0.6785 0.8434 0.2348  0.2049  -0.0768 557 TYR A O   
4196 C CB  . TYR A 530 ? 1.0329 0.4750 0.6793 0.2258  0.1603  -0.0488 557 TYR A CB  
4197 C CG  . TYR A 530 ? 1.0622 0.4604 0.6665 0.2342  0.1385  -0.0445 557 TYR A CG  
4198 C CD1 . TYR A 530 ? 1.1149 0.4659 0.6619 0.2301  0.1395  -0.0352 557 TYR A CD1 
4199 C CD2 . TYR A 530 ? 1.1751 0.5806 0.7958 0.2457  0.1178  -0.0515 557 TYR A CD2 
4200 C CE1 . TYR A 530 ? 1.2308 0.5491 0.7412 0.2397  0.1178  -0.0354 557 TYR A CE1 
4201 C CE2 . TYR A 530 ? 1.2627 0.6358 0.8501 0.2510  0.0986  -0.0527 557 TYR A CE2 
4202 C CZ  . TYR A 530 ? 1.3820 0.7145 0.9159 0.2491  0.0973  -0.0459 557 TYR A CZ  
4203 O OH  . TYR A 530 ? 1.4609 0.7683 0.9634 0.2564  0.0763  -0.0511 557 TYR A OH  
4204 N N   . PRO A 531 ? 1.3023 0.8152 0.9797 0.2026  0.2258  -0.0615 558 PRO A N   
4205 C CA  . PRO A 531 ? 1.2358 0.7996 0.9584 0.1876  0.2476  -0.0734 558 PRO A CA  
4206 C C   . PRO A 531 ? 1.1200 0.6988 0.8871 0.1809  0.2326  -0.0762 558 PRO A C   
4207 O O   . PRO A 531 ? 1.1315 0.6669 0.8829 0.1790  0.2110  -0.0648 558 PRO A O   
4208 C CB  . PRO A 531 ? 1.2666 0.7976 0.9503 0.1618  0.2737  -0.0659 558 PRO A CB  
4209 C CG  . PRO A 531 ? 1.2523 0.7288 0.8702 0.1714  0.2682  -0.0526 558 PRO A CG  
4210 C CD  . PRO A 531 ? 1.1659 0.6206 0.7805 0.1914  0.2330  -0.0477 558 PRO A CD  
4211 N N   . THR A 532 ? 1.1234 0.7687 0.9472 0.1793  0.2432  -0.0940 559 THR A N   
4212 C CA  . THR A 532 ? 1.0792 0.7451 0.9486 0.1710  0.2319  -0.1001 559 THR A CA  
4213 C C   . THR A 532 ? 1.1323 0.7592 0.9884 0.1388  0.2446  -0.0938 559 THR A C   
4214 O O   . THR A 532 ? 1.1739 0.7586 1.0212 0.1341  0.2260  -0.0838 559 THR A O   
4215 C CB  . THR A 532 ? 0.9962 0.7481 0.9284 0.1794  0.2400  -0.1240 559 THR A CB  
4216 O OG1 . THR A 532 ? 1.0355 0.8234 0.9759 0.1649  0.2720  -0.1377 559 THR A OG1 
4217 C CG2 . THR A 532 ? 1.0589 0.8368 0.9968 0.2150  0.2248  -0.1272 559 THR A CG2 
4218 N N   . HIS A 533 ? 1.2167 0.8548 1.0688 0.1164  0.2776  -0.1003 560 HIS A N   
4219 C CA  . HIS A 533 ? 1.3625 0.9554 1.1937 0.0822  0.2971  -0.0937 560 HIS A CA  
4220 C C   . HIS A 533 ? 1.4674 0.9988 1.2258 0.0735  0.3144  -0.0758 560 HIS A C   
4221 O O   . HIS A 533 ? 1.4069 0.9639 1.1542 0.0808  0.3296  -0.0808 560 HIS A O   
4222 C CB  . HIS A 533 ? 1.2098 0.8656 1.0959 0.0559  0.3268  -0.1185 560 HIS A CB  
4223 C CG  . HIS A 533 ? 1.1887 0.9123 1.1469 0.0652  0.3110  -0.1394 560 HIS A CG  
4224 N ND1 . HIS A 533 ? 1.2334 1.0233 1.2278 0.0978  0.2955  -0.1524 560 HIS A ND1 
4225 C CD2 . HIS A 533 ? 1.1799 0.9129 1.1771 0.0474  0.3087  -0.1500 560 HIS A CD2 
4226 C CE1 . HIS A 533 ? 1.2255 1.0655 1.2773 0.1007  0.2838  -0.1695 560 HIS A CE1 
4227 N NE2 . HIS A 533 ? 1.1154 0.9248 1.1727 0.0698  0.2912  -0.1696 560 HIS A NE2 
4228 N N   . TYR A 534 ? 1.6474 1.0967 1.3533 0.0608  0.3113  -0.0554 561 TYR A N   
4229 C CA  . TYR A 534 ? 1.7804 1.1646 1.4110 0.0494  0.3308  -0.0375 561 TYR A CA  
4230 C C   . TYR A 534 ? 1.7787 1.1499 1.4052 0.0085  0.3719  -0.0408 561 TYR A C   
4231 O O   . TYR A 534 ? 1.7942 1.1968 1.4733 -0.0116 0.3810  -0.0562 561 TYR A O   
4232 C CB  . TYR A 534 ? 1.7921 1.0897 1.3577 0.0643  0.3024  -0.0129 561 TYR A CB  
4233 C CG  . TYR A 534 ? 1.8188 1.1239 1.3764 0.0994  0.2686  -0.0108 561 TYR A CG  
4234 C CD1 . TYR A 534 ? 1.7376 1.0765 1.3434 0.1183  0.2372  -0.0193 561 TYR A CD1 
4235 C CD2 . TYR A 534 ? 1.7236 1.0019 1.2249 0.1118  0.2699  -0.0018 561 TYR A CD2 
4236 C CE1 . TYR A 534 ? 1.5968 0.9402 1.1950 0.1456  0.2103  -0.0191 561 TYR A CE1 
4237 C CE2 . TYR A 534 ? 1.7005 0.9846 1.1959 0.1401  0.2412  -0.0030 561 TYR A CE2 
4238 C CZ  . TYR A 534 ? 1.5840 0.8995 1.1281 0.1554  0.2126  -0.0117 561 TYR A CZ  
4239 O OH  . TYR A 534 ? 1.5047 0.8238 1.0425 0.1789  0.1879  -0.0144 561 TYR A OH  
4240 N N   . THR A 535 ? 1.8082 1.1329 1.3702 -0.0054 0.3986  -0.0277 562 THR A N   
4241 C CA  . THR A 535 ? 1.8405 1.1441 1.3887 -0.0483 0.4430  -0.0295 562 THR A CA  
4242 C C   . THR A 535 ? 1.7698 1.0008 1.2996 -0.0661 0.4389  -0.0169 562 THR A C   
4243 O O   . THR A 535 ? 1.8988 1.0481 1.3685 -0.0483 0.4133  0.0075  562 THR A O   
4244 C CB  . THR A 535 ? 1.8372 1.0910 1.3059 -0.0569 0.4701  -0.0132 562 THR A CB  
4245 O OG1 . THR A 535 ? 1.8283 1.1470 1.3128 -0.0363 0.4706  -0.0258 562 THR A OG1 
4246 C CG2 . THR A 535 ? 1.6303 0.8692 1.0878 -0.1058 0.5225  -0.0178 562 THR A CG2 
4247 N N   . GLY A 536 ? 1.6908 0.9536 1.2733 -0.0998 0.4634  -0.0363 563 GLY A N   
4248 C CA  . GLY A 536 ? 1.7354 0.9357 1.3105 -0.1185 0.4615  -0.0297 563 GLY A CA  
4249 C C   . GLY A 536 ? 1.7775 1.0262 1.4255 -0.1019 0.4269  -0.0457 563 GLY A C   
4250 O O   . GLY A 536 ? 1.7999 1.0207 1.4639 -0.1228 0.4309  -0.0504 563 GLY A O   
4251 N N   . ASP A 537 ? 2.0345 1.3506 1.7234 -0.0654 0.3943  -0.0541 564 ASP A N   
4252 C CA  . ASP A 537 ? 1.9840 1.3525 1.7418 -0.0489 0.3634  -0.0701 564 ASP A CA  
4253 C C   . ASP A 537 ? 1.8413 1.2986 1.6815 -0.0741 0.3871  -0.1043 564 ASP A C   
4254 O O   . ASP A 537 ? 1.7844 1.2921 1.6424 -0.0932 0.4208  -0.1203 564 ASP A O   
4255 C CB  . ASP A 537 ? 1.8748 1.2884 1.6487 -0.0056 0.3276  -0.0698 564 ASP A CB  
4256 C CG  . ASP A 537 ? 1.9543 1.2916 1.6543 0.0193  0.3021  -0.0421 564 ASP A CG  
4257 O OD1 . ASP A 537 ? 2.1224 1.3737 1.7528 0.0070  0.3129  -0.0217 564 ASP A OD1 
4258 O OD2 . ASP A 537 ? 1.8415 1.2042 1.5513 0.0513  0.2719  -0.0417 564 ASP A OD2 
4259 N N   . ASP A 538 ? 1.6875 1.1685 1.5797 -0.0730 0.3685  -0.1181 565 ASP A N   
4260 C CA  . ASP A 538 ? 1.5685 1.1379 1.5425 -0.0946 0.3866  -0.1541 565 ASP A CA  
4261 C C   . ASP A 538 ? 1.4315 1.1112 1.4600 -0.0680 0.3794  -0.1755 565 ASP A C   
4262 O O   . ASP A 538 ? 1.4240 1.1246 1.4612 -0.0289 0.3442  -0.1699 565 ASP A O   
4263 C CB  . ASP A 538 ? 1.5462 1.1117 1.5583 -0.0950 0.3642  -0.1633 565 ASP A CB  
4264 C CG  . ASP A 538 ? 1.6180 1.2661 1.7104 -0.1229 0.3852  -0.2026 565 ASP A CG  
4265 O OD1 . ASP A 538 ? 1.7449 1.4450 1.8594 -0.1477 0.4211  -0.2226 565 ASP A OD1 
4266 O OD2 . ASP A 538 ? 1.5713 1.2368 1.7065 -0.1198 0.3656  -0.2162 565 ASP A OD2 
4267 N N   . GLY A 539 ? 1.2393 0.9883 1.3024 -0.0888 0.4136  -0.2011 566 GLY A N   
4268 C CA  . GLY A 539 ? 1.1292 0.9815 1.2390 -0.0614 0.4094  -0.2232 566 GLY A CA  
4269 C C   . GLY A 539 ? 1.2112 1.0549 1.2744 -0.0444 0.4173  -0.2094 566 GLY A C   
4270 O O   . GLY A 539 ? 1.3730 1.2930 1.4663 -0.0157 0.4114  -0.2254 566 GLY A O   
4271 N N   . TYR A 540 ? 1.3534 1.1049 1.3412 -0.0588 0.4299  -0.1809 567 TYR A N   
4272 C CA  . TYR A 540 ? 1.4826 1.2221 1.4223 -0.0437 0.4378  -0.1683 567 TYR A CA  
4273 C C   . TYR A 540 ? 1.4670 1.2863 1.4392 -0.0613 0.4762  -0.1973 567 TYR A C   
4274 O O   . TYR A 540 ? 1.3664 1.1972 1.3564 -0.1042 0.5118  -0.2134 567 TYR A O   
4275 C CB  . TYR A 540 ? 1.5793 1.2031 1.4294 -0.0571 0.4442  -0.1334 567 TYR A CB  
4276 C CG  . TYR A 540 ? 1.6303 1.2365 1.4252 -0.0481 0.4580  -0.1216 567 TYR A CG  
4277 C CD1 . TYR A 540 ? 1.6711 1.2703 1.4411 -0.0072 0.4283  -0.1092 567 TYR A CD1 
4278 C CD2 . TYR A 540 ? 1.6539 1.2483 1.4200 -0.0824 0.5024  -0.1240 567 TYR A CD2 
4279 C CE1 . TYR A 540 ? 1.7800 1.3627 1.4995 0.0012  0.4404  -0.1005 567 TYR A CE1 
4280 C CE2 . TYR A 540 ? 1.7357 1.3155 1.4501 -0.0735 0.5151  -0.1143 567 TYR A CE2 
4281 C CZ  . TYR A 540 ? 1.8815 1.4559 1.5733 -0.0306 0.4829  -0.1029 567 TYR A CZ  
4282 O OH  . TYR A 540 ? 1.6988 1.2589 1.3396 -0.0213 0.4950  -0.0954 567 TYR A OH  
4283 N N   . VAL A 541 ? 1.5627 1.4375 1.5429 -0.0282 0.4697  -0.2060 568 VAL A N   
4284 C CA  . VAL A 541 ? 1.5204 1.4811 1.5330 -0.0353 0.5014  -0.2364 568 VAL A CA  
4285 C C   . VAL A 541 ? 1.5922 1.5291 1.5487 -0.0135 0.5045  -0.2217 568 VAL A C   
4286 O O   . VAL A 541 ? 1.6392 1.5585 1.5748 0.0275  0.4727  -0.2073 568 VAL A O   
4287 C CB  . VAL A 541 ? 1.4543 1.5315 1.5489 -0.0088 0.4883  -0.2728 568 VAL A CB  
4288 C CG1 . VAL A 541 ? 1.3473 1.5140 1.4680 -0.0043 0.5150  -0.3040 568 VAL A CG1 
4289 C CG2 . VAL A 541 ? 1.2640 1.3766 1.4190 -0.0359 0.4915  -0.2944 568 VAL A CG2 
4290 N N   . SER A 542 ? 1.9341 1.8702 1.8656 -0.0428 0.5446  -0.2269 569 SER A N   
4291 C CA  . SER A 542 ? 1.9843 1.9024 1.8624 -0.0266 0.5532  -0.2167 569 SER A CA  
4292 C C   . SER A 542 ? 2.0258 2.0400 1.9430 -0.0396 0.5909  -0.2535 569 SER A C   
4293 O O   . SER A 542 ? 2.2479 2.2505 2.1448 -0.0815 0.6322  -0.2570 569 SER A O   
4294 C CB  . SER A 542 ? 2.2430 2.0469 2.0329 -0.0484 0.5640  -0.1806 569 SER A CB  
4295 O OG  . SER A 542 ? 2.2954 2.0862 2.0344 -0.0327 0.5725  -0.1732 569 SER A OG  
4296 N N   . ASP A 543 ? 1.5849 1.6934 1.5557 -0.0023 0.5772  -0.2817 570 ASP A N   
4297 C CA  . ASP A 543 ? 1.4870 1.7001 1.5013 -0.0070 0.6085  -0.3220 570 ASP A CA  
4298 C C   . ASP A 543 ? 1.5894 1.7853 1.5489 -0.0026 0.6296  -0.3161 570 ASP A C   
4299 O O   . ASP A 543 ? 1.6298 1.9060 1.6180 -0.0140 0.6619  -0.3489 570 ASP A O   
4300 C CB  . ASP A 543 ? 1.4112 1.7256 1.4908 0.0400  0.5837  -0.3530 570 ASP A CB  
4301 C CG  . ASP A 543 ? 1.4474 1.8110 1.5953 0.0302  0.5728  -0.3723 570 ASP A CG  
4302 O OD1 . ASP A 543 ? 1.5594 1.8845 1.7095 -0.0172 0.5888  -0.3659 570 ASP A OD1 
4303 O OD2 . ASP A 543 ? 1.3647 1.7943 1.5553 0.0716  0.5379  -0.3852 570 ASP A OD2 
4304 N N   . THR A 544 ? 1.6528 1.7518 1.5366 0.0133  0.6126  -0.2785 571 THR A N   
4305 C CA  . THR A 544 ? 1.7168 1.7925 1.5426 0.0176  0.6313  -0.2716 571 THR A CA  
4306 C C   . THR A 544 ? 1.7780 1.8312 1.5729 -0.0367 0.6798  -0.2703 571 THR A C   
4307 O O   . THR A 544 ? 1.8330 1.9484 1.6385 -0.0476 0.7137  -0.2957 571 THR A O   
4308 C CB  . THR A 544 ? 1.6550 1.6294 1.4062 0.0453  0.5999  -0.2328 571 THR A CB  
4309 O OG1 . THR A 544 ? 1.8305 1.7191 1.5544 0.0266  0.5840  -0.2022 571 THR A OG1 
4310 C CG2 . THR A 544 ? 1.5473 1.5472 1.3186 0.1019  0.5600  -0.2378 571 THR A CG2 
4311 N N   . GLU A 545 ? 2.0440 1.9200 2.0591 -0.1417 0.1356  -0.0706 572 GLU A N   
4312 C CA  . GLU A 545 ? 1.9947 1.9188 1.9196 -0.1335 0.1604  -0.0325 572 GLU A CA  
4313 C C   . GLU A 545 ? 2.0584 1.9192 1.9902 -0.1507 0.1821  0.0435  572 GLU A C   
4314 O O   . GLU A 545 ? 2.0998 1.9130 1.9781 -0.1504 0.1758  0.1104  572 GLU A O   
4315 C CB  . GLU A 545 ? 2.0432 2.0097 1.8580 -0.1074 0.1390  -0.0108 572 GLU A CB  
4316 C CG  . GLU A 545 ? 2.1703 2.1845 1.8798 -0.0895 0.1709  0.0362  572 GLU A CG  
4317 C CD  . GLU A 545 ? 2.1802 2.2859 1.8850 -0.0864 0.1989  -0.0241 572 GLU A CD  
4318 O OE1 . GLU A 545 ? 2.0930 2.2654 1.8256 -0.0840 0.1850  -0.1084 572 GLU A OE1 
4319 O OE2 . GLU A 545 ? 2.1203 2.2295 1.7978 -0.0897 0.2391  0.0093  572 GLU A OE2 
4320 N N   . THR A 546 ? 2.1917 2.0547 2.1938 -0.1666 0.2109  0.0301  573 THR A N   
4321 C CA  . THR A 546 ? 2.1943 2.0183 2.2160 -0.1883 0.2349  0.0875  573 THR A CA  
4322 C C   . THR A 546 ? 2.2127 2.0789 2.1713 -0.1902 0.2799  0.1103  573 THR A C   
4323 O O   . THR A 546 ? 2.1868 2.0363 2.1719 -0.2130 0.3095  0.1434  573 THR A O   
4324 C CB  . THR A 546 ? 2.0827 1.8945 2.2230 -0.2014 0.2400  0.0652  573 THR A CB  
4325 O OG1 . THR A 546 ? 2.0424 1.9051 2.2272 -0.1887 0.2537  -0.0036 573 THR A OG1 
4326 C CG2 . THR A 546 ? 1.9678 1.7130 2.1636 -0.2043 0.2027  0.0760  573 THR A CG2 
4327 N N   . SER A 547 ? 2.1735 2.0997 2.0496 -0.1671 0.2873  0.0915  574 SER A N   
4328 C CA  . SER A 547 ? 2.2730 2.2360 2.0698 -0.1615 0.3315  0.1201  574 SER A CA  
4329 C C   . SER A 547 ? 2.3454 2.3318 2.2054 -0.1824 0.3717  0.1023  574 SER A C   
4330 O O   . SER A 547 ? 2.3232 2.2937 2.1651 -0.1987 0.4115  0.1466  574 SER A O   
4331 C CB  . SER A 547 ? 2.2639 2.1665 1.9849 -0.1626 0.3483  0.2048  574 SER A CB  
4332 O OG  . SER A 547 ? 2.2442 2.0799 2.0316 -0.1985 0.3606  0.2381  574 SER A OG  
4333 N N   . VAL A 548 ? 2.1912 2.2155 2.1290 -0.1818 0.3662  0.0352  575 VAL A N   
4334 C CA  . VAL A 548 ? 2.0871 2.1436 2.0908 -0.1948 0.4036  0.0125  575 VAL A CA  
4335 C C   . VAL A 548 ? 1.9121 2.0387 1.9181 -0.1788 0.4144  -0.0614 575 VAL A C   
4336 O O   . VAL A 548 ? 1.7373 1.8663 1.7933 -0.1713 0.3928  -0.1162 575 VAL A O   
4337 C CB  . VAL A 548 ? 1.9101 1.9319 2.0319 -0.2108 0.3948  0.0130  575 VAL A CB  
4338 C CG1 . VAL A 548 ? 1.7672 1.7584 1.9433 -0.1985 0.3541  -0.0218 575 VAL A CG1 
4339 C CG2 . VAL A 548 ? 1.6092 1.6800 1.8004 -0.2160 0.4333  -0.0141 575 VAL A CG2 
4340 N N   . VAL A 549 ? 1.9404 2.1217 1.8926 -0.1755 0.4530  -0.0656 576 VAL A N   
4341 C CA  . VAL A 549 ? 1.8916 2.1469 1.8339 -0.1627 0.4678  -0.1373 576 VAL A CA  
4342 C C   . VAL A 549 ? 1.8282 2.0864 1.8897 -0.1703 0.4844  -0.1905 576 VAL A C   
4343 O O   . VAL A 549 ? 1.8385 2.0667 1.9756 -0.1820 0.4968  -0.1634 576 VAL A O   
4344 C CB  . VAL A 549 ? 1.9158 2.2254 1.7700 -0.1564 0.5089  -0.1212 576 VAL A CB  
4345 C CG1 . VAL A 549 ? 1.9276 2.3238 1.7536 -0.1424 0.5200  -0.1976 576 VAL A CG1 
4346 C CG2 . VAL A 549 ? 1.9305 2.2201 1.6709 -0.1435 0.5039  -0.0500 576 VAL A CG2 
4347 N N   . TRP A 550 ? 1.7524 2.0521 1.8319 -0.1620 0.4885  -0.2688 577 TRP A N   
4348 C CA  . TRP A 550 ? 1.7177 2.0109 1.9092 -0.1635 0.5132  -0.3202 577 TRP A CA  
4349 C C   . TRP A 550 ? 1.7823 2.1147 1.9969 -0.1669 0.5634  -0.3226 577 TRP A C   
4350 O O   . TRP A 550 ? 1.7368 2.0524 2.0477 -0.1659 0.5852  -0.3227 577 TRP A O   
4351 C CB  . TRP A 550 ? 1.7364 2.0567 1.9417 -0.1588 0.5135  -0.4098 577 TRP A CB  
4352 C CG  . TRP A 550 ? 1.8156 2.2228 1.9637 -0.1584 0.5439  -0.4664 577 TRP A CG  
4353 C CD1 . TRP A 550 ? 1.8775 2.3525 1.9132 -0.1523 0.5289  -0.4737 577 TRP A CD1 
4354 C CD2 . TRP A 550 ? 1.8460 2.2872 2.0447 -0.1612 0.5966  -0.5225 577 TRP A CD2 
4355 N NE1 . TRP A 550 ? 1.9433 2.4970 1.9552 -0.1531 0.5667  -0.5340 577 TRP A NE1 
4356 C CE2 . TRP A 550 ? 1.9248 2.4547 2.0369 -0.1611 0.6096  -0.5662 577 TRP A CE2 
4357 C CE3 . TRP A 550 ? 1.8185 2.2274 2.1259 -0.1598 0.6362  -0.5380 577 TRP A CE3 
4358 C CZ2 . TRP A 550 ? 1.9744 2.5558 2.1069 -0.1656 0.6608  -0.6287 577 TRP A CZ2 
4359 C CZ3 . TRP A 550 ? 1.8694 2.3253 2.1981 -0.1613 0.6893  -0.5965 577 TRP A CZ3 
4360 C CH2 . TRP A 550 ? 1.9454 2.4839 2.1879 -0.1671 0.7012  -0.6433 577 TRP A CH2 
4361 N N   . ASN A 551 ? 1.8314 2.2208 1.9577 -0.1670 0.5840  -0.3225 578 ASN A N   
4362 C CA  . ASN A 551 ? 1.8575 2.2898 2.0023 -0.1704 0.6350  -0.3356 578 ASN A CA  
4363 C C   . ASN A 551 ? 1.8230 2.2281 2.0245 -0.1810 0.6499  -0.2754 578 ASN A C   
4364 O O   . ASN A 551 ? 1.8013 2.2224 2.0860 -0.1805 0.6827  -0.2924 578 ASN A O   
4365 C CB  . ASN A 551 ? 1.9478 2.4427 1.9751 -0.1662 0.6526  -0.3366 578 ASN A CB  
4366 C CG  . ASN A 551 ? 2.0206 2.5652 2.0640 -0.1694 0.7071  -0.3646 578 ASN A CG  
4367 O OD1 . ASN A 551 ? 2.0488 2.5980 2.1838 -0.1706 0.7320  -0.4133 578 ASN A OD1 
4368 N ND2 . ASN A 551 ? 2.1041 2.6822 2.0576 -0.1682 0.7310  -0.3312 578 ASN A ND2 
4369 N N   . ASN A 552 ? 1.8707 2.2395 2.0307 -0.1908 0.6291  -0.2072 579 ASN A N   
4370 C CA  . ASN A 552 ? 1.8536 2.2051 2.0673 -0.2080 0.6422  -0.1560 579 ASN A CA  
4371 C C   . ASN A 552 ? 1.9072 2.2004 2.0857 -0.2192 0.6081  -0.0962 579 ASN A C   
4372 O O   . ASN A 552 ? 1.9223 2.1863 2.0456 -0.2091 0.5725  -0.0941 579 ASN A O   
4373 C CB  . ASN A 552 ? 1.9814 2.3767 2.1647 -0.2194 0.6933  -0.1429 579 ASN A CB  
4374 C CG  . ASN A 552 ? 2.1136 2.5226 2.1652 -0.2135 0.7057  -0.1305 579 ASN A CG  
4375 O OD1 . ASN A 552 ? 2.1143 2.4852 2.0924 -0.2168 0.6947  -0.0776 579 ASN A OD1 
4376 N ND2 . ASN A 552 ? 2.1484 2.6138 2.1677 -0.2016 0.7327  -0.1776 579 ASN A ND2 
4377 N N   . GLU A 553 ? 1.9873 2.2686 2.2000 -0.2419 0.6218  -0.0510 580 GLU A N   
4378 C CA  . GLU A 553 ? 1.9178 2.1413 2.1140 -0.2588 0.5974  0.0027  580 GLU A CA  
4379 C C   . GLU A 553 ? 1.8363 2.0253 1.9061 -0.2539 0.5949  0.0374  580 GLU A C   
4380 O O   . GLU A 553 ? 1.9251 2.1241 1.9249 -0.2597 0.6365  0.0623  580 GLU A O   
4381 C CB  . GLU A 553 ? 1.8052 2.0402 2.0532 -0.2910 0.6272  0.0344  580 GLU A CB  
4382 C CG  . GLU A 553 ? 1.6373 1.9304 2.0050 -0.2893 0.6365  0.0045  580 GLU A CG  
4383 C CD  . GLU A 553 ? 1.7073 1.9834 2.1539 -0.2707 0.5925  -0.0076 580 GLU A CD  
4384 O OE1 . GLU A 553 ? 1.6496 1.8778 2.0940 -0.2812 0.5593  0.0230  580 GLU A OE1 
4385 O OE2 . GLU A 553 ? 1.6540 1.9599 2.1636 -0.2442 0.5960  -0.0465 580 GLU A OE2 
4386 N N   . ARG B 15  ? 1.3232 0.8795 0.4232 0.1354  0.0030  0.0256  42  ARG B N   
4387 C CA  . ARG B 15  ? 1.4376 1.0063 0.5520 0.1352  -0.0176 0.0231  42  ARG B CA  
4388 C C   . ARG B 15  ? 1.3466 0.9196 0.4926 0.1332  -0.0136 0.0288  42  ARG B C   
4389 O O   . ARG B 15  ? 1.4987 1.0726 0.6616 0.1280  -0.0085 0.0212  42  ARG B O   
4390 C CB  . ARG B 15  ? 1.4386 1.0125 0.5500 0.1302  -0.0306 0.0056  42  ARG B CB  
4391 C CG  . ARG B 15  ? 1.7699 1.3471 0.8542 0.1321  -0.0458 -0.0003 42  ARG B CG  
4392 C CD  . ARG B 15  ? 1.7196 1.3105 0.8064 0.1371  -0.0648 0.0074  42  ARG B CD  
4393 N NE  . ARG B 15  ? 1.7855 1.3889 0.9017 0.1345  -0.0754 0.0061  42  ARG B NE  
4394 C CZ  . ARG B 15  ? 1.8702 1.4895 0.9945 0.1381  -0.0942 0.0095  42  ARG B CZ  
4395 N NH1 . ARG B 15  ? 1.5152 1.1407 0.6207 0.1445  -0.1057 0.0142  42  ARG B NH1 
4396 N NH2 . ARG B 15  ? 1.4570 1.0874 0.6090 0.1357  -0.1016 0.0083  42  ARG B NH2 
4397 N N   . TRP B 16  ? 1.1783 0.7528 0.3313 0.1378  -0.0158 0.0421  43  TRP B N   
4398 C CA  . TRP B 16  ? 1.1670 0.7459 0.3489 0.1363  -0.0139 0.0473  43  TRP B CA  
4399 C C   . TRP B 16  ? 1.1702 0.7635 0.3673 0.1349  -0.0331 0.0391  43  TRP B C   
4400 O O   . TRP B 16  ? 1.1997 0.8021 0.3881 0.1382  -0.0513 0.0369  43  TRP B O   
4401 C CB  . TRP B 16  ? 1.1172 0.6915 0.3014 0.1417  -0.0108 0.0631  43  TRP B CB  
4402 C CG  . TRP B 16  ? 1.1488 0.7284 0.3617 0.1408  -0.0117 0.0674  43  TRP B CG  
4403 C CD1 . TRP B 16  ? 1.1634 0.7403 0.3957 0.1352  0.0029  0.0684  43  TRP B CD1 
4404 C CD2 . TRP B 16  ? 1.1437 0.7335 0.3690 0.1458  -0.0281 0.0708  43  TRP B CD2 
4405 N NE1 . TRP B 16  ? 1.1333 0.7164 0.3878 0.1361  -0.0033 0.0721  43  TRP B NE1 
4406 C CE2 . TRP B 16  ? 1.0945 0.6854 0.3456 0.1429  -0.0219 0.0737  43  TRP B CE2 
4407 C CE3 . TRP B 16  ? 1.1789 0.7785 0.3967 0.1529  -0.0474 0.0717  43  TRP B CE3 
4408 C CZ2 . TRP B 16  ? 1.0220 0.6220 0.2908 0.1472  -0.0336 0.0774  43  TRP B CZ2 
4409 C CZ3 . TRP B 16  ? 1.0887 0.6991 0.3259 0.1575  -0.0592 0.0756  43  TRP B CZ3 
4410 C CH2 . TRP B 16  ? 1.1672 0.7770 0.4292 0.1548  -0.0518 0.0784  43  TRP B CH2 
4411 N N   . SER B 17  ? 1.0663 0.6628 0.2862 0.1297  -0.0292 0.0347  44  SER B N   
4412 C CA  . SER B 17  ? 1.0391 0.6489 0.2760 0.1278  -0.0457 0.0283  44  SER B CA  
4413 C C   . SER B 17  ? 1.0262 0.6379 0.2898 0.1264  -0.0382 0.0340  44  SER B C   
4414 O O   . SER B 17  ? 1.1675 0.7727 0.4389 0.1221  -0.0223 0.0330  44  SER B O   
4415 C CB  . SER B 17  ? 1.1377 0.7488 0.3704 0.1212  -0.0515 0.0118  44  SER B CB  
4416 O OG  . SER B 17  ? 1.3907 1.0153 0.6383 0.1185  -0.0687 0.0055  44  SER B OG  
4417 N N   . PRO B 18  ? 1.0311 0.6525 0.3092 0.1303  -0.0492 0.0402  45  PRO B N   
4418 C CA  . PRO B 18  ? 1.0207 0.6476 0.3326 0.1277  -0.0413 0.0450  45  PRO B CA  
4419 C C   . PRO B 18  ? 1.0183 0.6584 0.3619 0.1185  -0.0412 0.0337  45  PRO B C   
4420 O O   . PRO B 18  ? 1.0978 0.7472 0.4442 0.1147  -0.0531 0.0232  45  PRO B O   
4421 C CB  . PRO B 18  ? 0.9527 0.5894 0.2739 0.1351  -0.0548 0.0526  45  PRO B CB  
4422 C CG  . PRO B 18  ? 0.9737 0.6200 0.2792 0.1380  -0.0742 0.0463  45  PRO B CG  
4423 C CD  . PRO B 18  ? 1.0521 0.6853 0.3261 0.1366  -0.0688 0.0419  45  PRO B CD  
4424 N N   . GLU B 19  ? 0.9611 0.6012 0.3278 0.1145  -0.0273 0.0361  46  GLU B N   
4425 C CA  . GLU B 19  ? 0.8996 0.5517 0.2977 0.1070  -0.0262 0.0280  46  GLU B CA  
4426 C C   . GLU B 19  ? 0.9359 0.6037 0.3642 0.1072  -0.0342 0.0311  46  GLU B C   
4427 O O   . GLU B 19  ? 1.0353 0.7012 0.4657 0.1123  -0.0327 0.0408  46  GLU B O   
4428 C CB  . GLU B 19  ? 0.8508 0.4971 0.2575 0.1034  -0.0076 0.0286  46  GLU B CB  
4429 C CG  . GLU B 19  ? 1.1153 0.7483 0.4964 0.1032  0.0020  0.0239  46  GLU B CG  
4430 C CD  . GLU B 19  ? 1.1865 0.8207 0.5664 0.0993  -0.0042 0.0109  46  GLU B CD  
4431 O OE1 . GLU B 19  ? 1.0726 0.7169 0.4799 0.0945  -0.0068 0.0059  46  GLU B OE1 
4432 O OE2 . GLU B 19  ? 1.2891 0.9126 0.6393 0.1009  -0.0061 0.0055  46  GLU B OE2 
4433 N N   . SER B 20  ? 0.9776 0.6596 0.4282 0.1018  -0.0419 0.0229  47  SER B N   
4434 C CA  . SER B 20  ? 0.7930 0.4915 0.2733 0.1017  -0.0484 0.0249  47  SER B CA  
4435 C C   . SER B 20  ? 0.8556 0.5533 0.3558 0.1003  -0.0350 0.0300  47  SER B C   
4436 O O   . SER B 20  ? 0.9003 0.5885 0.3963 0.0977  -0.0219 0.0300  47  SER B O   
4437 C CB  . SER B 20  ? 0.7805 0.4936 0.2793 0.0946  -0.0578 0.0149  47  SER B CB  
4438 O OG  . SER B 20  ? 0.8558 0.5648 0.3647 0.0878  -0.0476 0.0093  47  SER B OG  
4439 N N   . PRO B 21  ? 0.7504 0.4588 0.2722 0.1023  -0.0382 0.0341  48  PRO B N   
4440 C CA  . PRO B 21  ? 0.7738 0.4816 0.3134 0.1006  -0.0265 0.0380  48  PRO B CA  
4441 C C   . PRO B 21  ? 0.7631 0.4761 0.3195 0.0932  -0.0197 0.0316  48  PRO B C   
4442 O O   . PRO B 21  ? 0.8607 0.5801 0.4224 0.0892  -0.0251 0.0243  48  PRO B O   
4443 C CB  . PRO B 21  ? 0.7169 0.4364 0.2753 0.1046  -0.0336 0.0413  48  PRO B CB  
4444 C CG  . PRO B 21  ? 0.7380 0.4598 0.2821 0.1115  -0.0468 0.0432  48  PRO B CG  
4445 C CD  . PRO B 21  ? 0.8550 0.5762 0.3838 0.1075  -0.0522 0.0359  48  PRO B CD  
4446 N N   . LEU B 22  ? 0.8433 0.5532 0.4079 0.0914  -0.0075 0.0345  49  LEU B N   
4447 C CA  . LEU B 22  ? 0.7168 0.4337 0.2996 0.0863  -0.0014 0.0300  49  LEU B CA  
4448 C C   . LEU B 22  ? 0.7077 0.4392 0.3156 0.0849  -0.0067 0.0290  49  LEU B C   
4449 O O   . LEU B 22  ? 0.7519 0.4871 0.3664 0.0881  -0.0100 0.0332  49  LEU B O   
4450 C CB  . LEU B 22  ? 0.6716 0.3842 0.2564 0.0849  0.0123  0.0331  49  LEU B CB  
4451 C CG  . LEU B 22  ? 0.9056 0.6058 0.4689 0.0855  0.0212  0.0342  49  LEU B CG  
4452 C CD1 . LEU B 22  ? 0.6824 0.3844 0.2553 0.0829  0.0343  0.0367  49  LEU B CD1 
4453 C CD2 . LEU B 22  ? 0.8280 0.5252 0.3815 0.0850  0.0201  0.0273  49  LEU B CD2 
4454 N N   . GLN B 23  ? 0.7702 0.5087 0.3910 0.0806  -0.0069 0.0238  50  GLN B N   
4455 C CA  . GLN B 23  ? 0.7841 0.5361 0.4282 0.0789  -0.0094 0.0234  50  GLN B CA  
4456 C C   . GLN B 23  ? 0.8676 0.6218 0.5228 0.0791  -0.0005 0.0269  50  GLN B C   
4457 O O   . GLN B 23  ? 0.7042 0.4520 0.3533 0.0787  0.0082  0.0281  50  GLN B O   
4458 C CB  . GLN B 23  ? 0.7322 0.4884 0.3852 0.0738  -0.0108 0.0177  50  GLN B CB  
4459 C CG  . GLN B 23  ? 0.7798 0.5345 0.4234 0.0714  -0.0202 0.0126  50  GLN B CG  
4460 C CD  . GLN B 23  ? 0.8848 0.6422 0.5391 0.0650  -0.0213 0.0070  50  GLN B CD  
4461 O OE1 . GLN B 23  ? 0.9169 0.6860 0.5907 0.0624  -0.0223 0.0077  50  GLN B OE1 
4462 N NE2 . GLN B 23  ? 0.8689 0.6140 0.5093 0.0622  -0.0202 0.0016  50  GLN B NE2 
4463 N N   . ALA B 24  ? 0.7727 0.5373 0.4446 0.0795  -0.0027 0.0280  51  ALA B N   
4464 C CA  . ALA B 24  ? 0.7556 0.5230 0.4375 0.0793  0.0043  0.0302  51  ALA B CA  
4465 C C   . ALA B 24  ? 0.6982 0.4684 0.3863 0.0760  0.0113  0.0282  51  ALA B C   
4466 O O   . ALA B 24  ? 0.7188 0.4897 0.4074 0.0744  0.0103  0.0253  51  ALA B O   
4467 C CB  . ALA B 24  ? 0.6715 0.4497 0.3691 0.0808  0.0006  0.0306  51  ALA B CB  
4468 N N   . PRO B 25  ? 0.8048 0.5766 0.4976 0.0752  0.0183  0.0296  52  PRO B N   
4469 C CA  . PRO B 25  ? 0.6378 0.4157 0.3382 0.0736  0.0240  0.0282  52  PRO B CA  
4470 C C   . PRO B 25  ? 0.7488 0.5360 0.4619 0.0731  0.0211  0.0269  52  PRO B C   
4471 O O   . PRO B 25  ? 0.8017 0.5942 0.5220 0.0733  0.0166  0.0270  52  PRO B O   
4472 C CB  . PRO B 25  ? 0.7145 0.4958 0.4199 0.0721  0.0298  0.0295  52  PRO B CB  
4473 C CG  . PRO B 25  ? 0.6412 0.4115 0.3355 0.0724  0.0299  0.0319  52  PRO B CG  
4474 C CD  . PRO B 25  ? 0.6361 0.4032 0.3263 0.0755  0.0215  0.0324  52  PRO B CD  
4475 N N   . ARG B 26  ? 0.6971 0.4858 0.4125 0.0732  0.0246  0.0260  53  ARG B N   
4476 C CA  . ARG B 26  ? 0.7457 0.5401 0.4706 0.0727  0.0233  0.0257  53  ARG B CA  
4477 C C   . ARG B 26  ? 0.6893 0.4949 0.4247 0.0736  0.0267  0.0272  53  ARG B C   
4478 O O   . ARG B 26  ? 0.6386 0.4473 0.3744 0.0751  0.0315  0.0277  53  ARG B O   
4479 C CB  . ARG B 26  ? 0.7337 0.5200 0.4528 0.0732  0.0253  0.0243  53  ARG B CB  
4480 C CG  . ARG B 26  ? 0.7666 0.5423 0.4749 0.0713  0.0207  0.0213  53  ARG B CG  
4481 C CD  . ARG B 26  ? 0.7605 0.5242 0.4562 0.0730  0.0251  0.0190  53  ARG B CD  
4482 N NE  . ARG B 26  ? 0.8497 0.6116 0.5370 0.0755  0.0294  0.0198  53  ARG B NE  
4483 C CZ  . ARG B 26  ? 0.7554 0.5077 0.4299 0.0777  0.0341  0.0179  53  ARG B CZ  
4484 N NH1 . ARG B 26  ? 0.9138 0.6553 0.5811 0.0782  0.0347  0.0143  53  ARG B NH1 
4485 N NH2 . ARG B 26  ? 0.9605 0.7130 0.6286 0.0792  0.0392  0.0194  53  ARG B NH2 
4486 N N   . VAL B 27  ? 0.7140 0.5270 0.4578 0.0729  0.0241  0.0277  54  VAL B N   
4487 C CA  . VAL B 27  ? 0.6994 0.5230 0.4509 0.0736  0.0263  0.0283  54  VAL B CA  
4488 C C   . VAL B 27  ? 0.6873 0.5165 0.4450 0.0741  0.0262  0.0299  54  VAL B C   
4489 O O   . VAL B 27  ? 0.6626 0.4911 0.4229 0.0726  0.0235  0.0299  54  VAL B O   
4490 C CB  . VAL B 27  ? 0.6319 0.4574 0.3852 0.0728  0.0247  0.0273  54  VAL B CB  
4491 C CG1 . VAL B 27  ? 0.7162 0.5517 0.4756 0.0728  0.0267  0.0264  54  VAL B CG1 
4492 C CG2 . VAL B 27  ? 0.7082 0.5247 0.4534 0.0720  0.0256  0.0269  54  VAL B CG2 
4493 N N   . LEU B 28  ? 0.6875 0.5232 0.4476 0.0763  0.0291  0.0314  55  LEU B N   
4494 C CA  . LEU B 28  ? 0.6376 0.4786 0.4016 0.0775  0.0299  0.0339  55  LEU B CA  
4495 C C   . LEU B 28  ? 0.6530 0.5053 0.4210 0.0778  0.0297  0.0330  55  LEU B C   
4496 O O   . LEU B 28  ? 0.6268 0.4854 0.3950 0.0784  0.0301  0.0314  55  LEU B O   
4497 C CB  . LEU B 28  ? 0.5974 0.4373 0.3591 0.0814  0.0330  0.0370  55  LEU B CB  
4498 C CG  . LEU B 28  ? 0.7049 0.5498 0.4683 0.0838  0.0345  0.0410  55  LEU B CG  
4499 C CD1 . LEU B 28  ? 0.6882 0.5248 0.4519 0.0805  0.0351  0.0428  55  LEU B CD1 
4500 C CD2 . LEU B 28  ? 0.5713 0.4175 0.3321 0.0901  0.0371  0.0446  55  LEU B CD2 
4501 N N   . ILE B 29  ? 0.5945 0.4499 0.3658 0.0770  0.0292  0.0335  56  ILE B N   
4502 C CA  . ILE B 29  ? 0.5971 0.4620 0.3704 0.0778  0.0296  0.0321  56  ILE B CA  
4503 C C   . ILE B 29  ? 0.6678 0.5388 0.4398 0.0804  0.0319  0.0358  56  ILE B C   
4504 O O   . ILE B 29  ? 0.7253 0.5942 0.4982 0.0801  0.0339  0.0394  56  ILE B O   
4505 C CB  . ILE B 29  ? 0.6658 0.5315 0.4431 0.0769  0.0288  0.0304  56  ILE B CB  
4506 C CG1 . ILE B 29  ? 0.5691 0.4276 0.3457 0.0759  0.0260  0.0279  56  ILE B CG1 
4507 C CG2 . ILE B 29  ? 0.5667 0.4405 0.3441 0.0784  0.0302  0.0282  56  ILE B CG2 
4508 C CD1 . ILE B 29  ? 0.5333 0.3937 0.3146 0.0770  0.0246  0.0267  56  ILE B CD1 
4509 N N   . ALA B 30  ? 0.6244 0.5034 0.3942 0.0827  0.0317  0.0352  57  ALA B N   
4510 C CA  . ALA B 30  ? 0.7324 0.6182 0.4988 0.0867  0.0331  0.0393  57  ALA B CA  
4511 C C   . ALA B 30  ? 0.7593 0.6540 0.5237 0.0869  0.0332  0.0371  57  ALA B C   
4512 O O   . ALA B 30  ? 0.6810 0.5811 0.4454 0.0854  0.0312  0.0314  57  ALA B O   
4513 C CB  . ALA B 30  ? 0.5841 0.4761 0.3495 0.0902  0.0318  0.0400  57  ALA B CB  
4514 N N   . LEU B 31  ? 0.6448 0.5399 0.4066 0.0885  0.0363  0.0414  58  LEU B N   
4515 C CA  . LEU B 31  ? 0.7639 0.6667 0.5222 0.0893  0.0378  0.0396  58  LEU B CA  
4516 C C   . LEU B 31  ? 0.6919 0.6000 0.4415 0.0940  0.0397  0.0455  58  LEU B C   
4517 O O   . LEU B 31  ? 0.6161 0.5182 0.3640 0.0950  0.0436  0.0527  58  LEU B O   
4518 C CB  . LEU B 31  ? 0.8112 0.7111 0.5747 0.0868  0.0411  0.0394  58  LEU B CB  
4519 C CG  . LEU B 31  ? 1.0006 0.9080 0.7601 0.0886  0.0449  0.0385  58  LEU B CG  
4520 C CD1 . LEU B 31  ? 0.8706 0.7832 0.6251 0.0896  0.0423  0.0309  58  LEU B CD1 
4521 C CD2 . LEU B 31  ? 0.8876 0.7950 0.6557 0.0866  0.0485  0.0385  58  LEU B CD2 
4522 N N   . LEU B 32  ? 0.8442 0.7629 0.5875 0.0966  0.0368  0.0425  59  LEU B N   
4523 C CA  . LEU B 32  ? 0.7439 0.6695 0.4762 0.1019  0.0378  0.0475  59  LEU B CA  
4524 C C   . LEU B 32  ? 0.6210 0.5507 0.3474 0.1013  0.0409  0.0441  59  LEU B C   
4525 O O   . LEU B 32  ? 0.8793 0.8130 0.6062 0.0989  0.0386  0.0352  59  LEU B O   
4526 C CB  . LEU B 32  ? 0.6881 0.6259 0.4165 0.1056  0.0317  0.0458  59  LEU B CB  
4527 C CG  . LEU B 32  ? 0.8097 0.7483 0.5452 0.1068  0.0283  0.0467  59  LEU B CG  
4528 C CD1 . LEU B 32  ? 0.7627 0.7180 0.4939 0.1124  0.0227  0.0470  59  LEU B CD1 
4529 C CD2 . LEU B 32  ? 0.8452 0.7701 0.5822 0.1093  0.0323  0.0550  59  LEU B CD2 
4530 N N   . ALA B 33  ? 0.6253 0.5530 0.3458 0.1035  0.0469  0.0511  60  ALA B N   
4531 C CA  . ALA B 33  ? 0.7028 0.6346 0.4177 0.1035  0.0518  0.0486  60  ALA B CA  
4532 C C   . ALA B 33  ? 0.7709 0.7074 0.4693 0.1091  0.0546  0.0553  60  ALA B C   
4533 O O   . ALA B 33  ? 0.7206 0.6510 0.4156 0.1112  0.0587  0.0656  60  ALA B O   
4534 C CB  . ALA B 33  ? 0.6231 0.5492 0.3485 0.0996  0.0583  0.0504  60  ALA B CB  
4535 N N   . ARG B 34  ? 0.6729 0.6188 0.3598 0.1116  0.0525  0.0493  61  ARG B N   
4536 C CA  . ARG B 34  ? 0.8141 0.7652 0.4824 0.1172  0.0557  0.0546  61  ARG B CA  
4537 C C   . ARG B 34  ? 0.8090 0.7654 0.4695 0.1168  0.0588  0.0459  61  ARG B C   
4538 O O   . ARG B 34  ? 0.7366 0.6970 0.3973 0.1149  0.0530  0.0345  61  ARG B O   
4539 C CB  . ARG B 34  ? 0.6368 0.5963 0.2937 0.1229  0.0475  0.0566  61  ARG B CB  
4540 C CG  . ARG B 34  ? 0.7442 0.7090 0.3790 0.1297  0.0502  0.0625  61  ARG B CG  
4541 C CD  . ARG B 34  ? 0.6967 0.6756 0.3195 0.1353  0.0398  0.0602  61  ARG B CD  
4542 N NE  . ARG B 34  ? 0.7732 0.7571 0.3721 0.1422  0.0421  0.0655  61  ARG B NE  
4543 C CZ  . ARG B 34  ? 0.8125 0.8106 0.3961 0.1481  0.0333  0.0638  61  ARG B CZ  
4544 N NH1 . ARG B 34  ? 0.7657 0.7765 0.3577 0.1471  0.0217  0.0565  61  ARG B NH1 
4545 N NH2 . ARG B 34  ? 0.7841 0.7850 0.3436 0.1549  0.0362  0.0696  61  ARG B NH2 
4546 N N   . ASN B 35  ? 0.7337 0.6890 0.3868 0.1185  0.0685  0.0511  62  ASN B N   
4547 C CA  . ASN B 35  ? 0.6563 0.6161 0.3006 0.1195  0.0736  0.0435  62  ASN B CA  
4548 C C   . ASN B 35  ? 0.7212 0.6788 0.3802 0.1154  0.0722  0.0318  62  ASN B C   
4549 O O   . ASN B 35  ? 0.7495 0.7090 0.4017 0.1156  0.0689  0.0205  62  ASN B O   
4550 C CB  . ASN B 35  ? 0.6951 0.6632 0.3167 0.1242  0.0685  0.0390  62  ASN B CB  
4551 C CG  . ASN B 35  ? 0.7234 0.6934 0.3266 0.1303  0.0716  0.0515  62  ASN B CG  
4552 O OD1 . ASN B 35  ? 0.7715 0.7370 0.3723 0.1311  0.0824  0.0609  62  ASN B OD1 
4553 N ND2 . ASN B 35  ? 0.8979 0.8750 0.4883 0.1346  0.0621  0.0521  62  ASN B ND2 
4554 N N   . ALA B 36  ? 0.8336 0.7858 0.5121 0.1116  0.0747  0.0347  63  ALA B N   
4555 C CA  . ALA B 36  ? 0.7181 0.6666 0.4111 0.1087  0.0725  0.0259  63  ALA B CA  
4556 C C   . ALA B 36  ? 0.7339 0.6832 0.4396 0.1085  0.0811  0.0269  63  ALA B C   
4557 O O   . ALA B 36  ? 0.8189 0.7650 0.5380 0.1072  0.0792  0.0215  63  ALA B O   
4558 C CB  . ALA B 36  ? 0.5888 0.5316 0.2943 0.1048  0.0647  0.0269  63  ALA B CB  
4559 N N   . ALA B 37  ? 0.8456 0.8000 0.5479 0.1099  0.0905  0.0339  64  ALA B N   
4560 C CA  . ALA B 37  ? 0.7603 0.7195 0.4779 0.1091  0.0991  0.0353  64  ALA B CA  
4561 C C   . ALA B 37  ? 0.7309 0.6922 0.4519 0.1130  0.1006  0.0244  64  ALA B C   
4562 O O   . ALA B 37  ? 0.8363 0.8010 0.5752 0.1129  0.1031  0.0234  64  ALA B O   
4563 C CB  . ALA B 37  ? 0.6475 0.6128 0.3581 0.1098  0.1106  0.0439  64  ALA B CB  
4564 N N   . HIS B 38  ? 0.7647 0.7236 0.4682 0.1167  0.0988  0.0160  65  HIS B N   
4565 C CA  . HIS B 38  ? 0.6842 0.6410 0.3882 0.1210  0.1009  0.0050  65  HIS B CA  
4566 C C   . HIS B 38  ? 0.8096 0.7579 0.5280 0.1193  0.0934  0.0002  65  HIS B C   
4567 O O   . HIS B 38  ? 0.7930 0.7395 0.5194 0.1234  0.0964  -0.0053 65  HIS B O   
4568 C CB  . HIS B 38  ? 0.6538 0.6074 0.3339 0.1239  0.0996  -0.0040 65  HIS B CB  
4569 C CG  . HIS B 38  ? 0.7592 0.7071 0.4314 0.1197  0.0879  -0.0074 65  HIS B CG  
4570 N ND1 . HIS B 38  ? 0.8735 0.8256 0.5377 0.1177  0.0834  0.0000  65  HIS B ND1 
4571 C CD2 . HIS B 38  ? 0.8613 0.8001 0.5332 0.1171  0.0803  -0.0171 65  HIS B CD2 
4572 C CE1 . HIS B 38  ? 0.8293 0.7782 0.4904 0.1143  0.0731  -0.0053 65  HIS B CE1 
4573 N NE2 . HIS B 38  ? 0.8684 0.8091 0.5342 0.1130  0.0714  -0.0158 65  HIS B NE2 
4574 N N   . ALA B 39  ? 0.7319 0.6747 0.4531 0.1141  0.0843  0.0028  66  ALA B N   
4575 C CA  . ALA B 39  ? 0.7822 0.7154 0.5130 0.1121  0.0773  -0.0016 66  ALA B CA  
4576 C C   . ALA B 39  ? 0.7894 0.7235 0.5390 0.1093  0.0753  0.0056  66  ALA B C   
4577 O O   . ALA B 39  ? 0.7314 0.6591 0.4902 0.1099  0.0719  0.0027  66  ALA B O   
4578 C CB  . ALA B 39  ? 0.8283 0.7550 0.5493 0.1079  0.0687  -0.0055 66  ALA B CB  
4579 N N   . LEU B 40  ? 0.7744 0.7149 0.5282 0.1064  0.0772  0.0148  67  LEU B N   
4580 C CA  . LEU B 40  ? 0.7782 0.7184 0.5478 0.1023  0.0743  0.0207  67  LEU B CA  
4581 C C   . LEU B 40  ? 0.7354 0.6800 0.5218 0.1043  0.0758  0.0192  67  LEU B C   
4582 O O   . LEU B 40  ? 0.7145 0.6540 0.5096 0.1026  0.0695  0.0191  67  LEU B O   
4583 C CB  . LEU B 40  ? 0.6309 0.5755 0.4008 0.0987  0.0783  0.0303  67  LEU B CB  
4584 C CG  . LEU B 40  ? 0.7566 0.6965 0.5115 0.0978  0.0754  0.0339  67  LEU B CG  
4585 C CD1 . LEU B 40  ? 0.8101 0.7512 0.5642 0.0953  0.0810  0.0442  67  LEU B CD1 
4586 C CD2 . LEU B 40  ? 0.6212 0.5526 0.3773 0.0956  0.0662  0.0321  67  LEU B CD2 
4587 N N   . PRO B 41  ? 0.8401 0.7952 0.6317 0.1087  0.0838  0.0182  68  PRO B N   
4588 C CA  . PRO B 41  ? 0.7545 0.7170 0.5645 0.1117  0.0842  0.0172  68  PRO B CA  
4589 C C   . PRO B 41  ? 0.7824 0.7336 0.5926 0.1157  0.0773  0.0114  68  PRO B C   
4590 O O   . PRO B 41  ? 0.8297 0.7832 0.6537 0.1163  0.0729  0.0127  68  PRO B O   
4591 C CB  . PRO B 41  ? 0.6720 0.6468 0.4835 0.1177  0.0948  0.0154  68  PRO B CB  
4592 C CG  . PRO B 41  ? 0.6392 0.6159 0.4371 0.1146  0.1008  0.0194  68  PRO B CG  
4593 C CD  . PRO B 41  ? 0.6235 0.5859 0.4049 0.1115  0.0931  0.0185  68  PRO B CD  
4594 N N   . THR B 42  ? 0.7472 0.6859 0.5417 0.1182  0.0761  0.0049  69  THR B N   
4595 C CA  . THR B 42  ? 0.7568 0.6809 0.5489 0.1208  0.0706  -0.0003 69  THR B CA  
4596 C C   . THR B 42  ? 0.7410 0.6544 0.5292 0.1139  0.0624  0.0016  69  THR B C   
4597 O O   . THR B 42  ? 0.7716 0.6774 0.5649 0.1142  0.0573  0.0021  69  THR B O   
4598 C CB  . THR B 42  ? 0.5863 0.5003 0.3633 0.1254  0.0741  -0.0092 69  THR B CB  
4599 O OG1 . THR B 42  ? 0.7719 0.6958 0.5516 0.1329  0.0829  -0.0112 69  THR B OG1 
4600 C CG2 . THR B 42  ? 0.9416 0.8377 0.7160 0.1280  0.0700  -0.0142 69  THR B CG2 
4601 N N   . THR B 43  ? 0.7708 0.6845 0.5497 0.1084  0.0614  0.0031  70  THR B N   
4602 C CA  . THR B 43  ? 0.8092 0.7150 0.5851 0.1026  0.0547  0.0047  70  THR B CA  
4603 C C   . THR B 43  ? 0.7968 0.7052 0.5843 0.0996  0.0515  0.0115  70  THR B C   
4604 O O   . THR B 43  ? 0.6053 0.5051 0.3943 0.0976  0.0462  0.0117  70  THR B O   
4605 C CB  . THR B 43  ? 0.6686 0.5772 0.4331 0.0993  0.0544  0.0051  70  THR B CB  
4606 O OG1 . THR B 43  ? 0.8156 0.7203 0.5681 0.1006  0.0552  -0.0030 70  THR B OG1 
4607 C CG2 . THR B 43  ? 0.9186 0.8227 0.6830 0.0942  0.0483  0.0080  70  THR B CG2 
4608 N N   . LEU B 44  ? 0.6822 0.6016 0.4772 0.0985  0.0550  0.0169  71  LEU B N   
4609 C CA  . LEU B 44  ? 0.7816 0.7028 0.5871 0.0943  0.0519  0.0221  71  LEU B CA  
4610 C C   . LEU B 44  ? 0.6695 0.5925 0.4866 0.0972  0.0489  0.0208  71  LEU B C   
4611 O O   . LEU B 44  ? 0.6895 0.6084 0.5106 0.0944  0.0432  0.0225  71  LEU B O   
4612 C CB  . LEU B 44  ? 0.5804 0.5113 0.3907 0.0910  0.0573  0.0279  71  LEU B CB  
4613 C CG  . LEU B 44  ? 0.7028 0.6299 0.5005 0.0889  0.0590  0.0314  71  LEU B CG  
4614 C CD1 . LEU B 44  ? 0.7441 0.6772 0.5453 0.0854  0.0652  0.0383  71  LEU B CD1 
4615 C CD2 . LEU B 44  ? 0.6492 0.5656 0.4422 0.0862  0.0524  0.0319  71  LEU B CD2 
4616 N N   . GLY B 45  ? 0.6991 0.6286 0.5210 0.1037  0.0526  0.0178  72  GLY B N   
4617 C CA  . GLY B 45  ? 0.6989 0.6304 0.5310 0.1087  0.0492  0.0168  72  GLY B CA  
4618 C C   . GLY B 45  ? 0.7636 0.6780 0.5873 0.1101  0.0429  0.0148  72  GLY B C   
4619 O O   . GLY B 45  ? 0.7874 0.7007 0.6167 0.1112  0.0371  0.0165  72  GLY B O   
4620 N N   . ALA B 46  ? 0.7673 0.6685 0.5769 0.1095  0.0439  0.0111  73  ALA B N   
4621 C CA  . ALA B 46  ? 0.7753 0.6593 0.5765 0.1091  0.0394  0.0095  73  ALA B CA  
4622 C C   . ALA B 46  ? 0.7329 0.6141 0.5337 0.1026  0.0342  0.0135  73  ALA B C   
4623 O O   . ALA B 46  ? 0.8767 0.7484 0.6755 0.1032  0.0298  0.0146  73  ALA B O   
4624 C CB  . ALA B 46  ? 0.5936 0.4666 0.3816 0.1076  0.0419  0.0039  73  ALA B CB  
4625 N N   . LEU B 47  ? 0.6894 0.5774 0.4907 0.0970  0.0351  0.0161  74  LEU B N   
4626 C CA  . LEU B 47  ? 0.7419 0.6259 0.5419 0.0916  0.0311  0.0193  74  LEU B CA  
4627 C C   . LEU B 47  ? 0.7795 0.6678 0.5886 0.0913  0.0271  0.0221  74  LEU B C   
4628 O O   . LEU B 47  ? 0.7603 0.6406 0.5659 0.0895  0.0225  0.0231  74  LEU B O   
4629 C CB  . LEU B 47  ? 0.7444 0.6331 0.5420 0.0874  0.0337  0.0217  74  LEU B CB  
4630 C CG  . LEU B 47  ? 0.8060 0.6924 0.5937 0.0870  0.0356  0.0190  74  LEU B CG  
4631 C CD1 . LEU B 47  ? 0.7677 0.6590 0.5527 0.0847  0.0372  0.0230  74  LEU B CD1 
4632 C CD2 . LEU B 47  ? 0.6371 0.5127 0.4188 0.0854  0.0325  0.0163  74  LEU B CD2 
4633 N N   . GLU B 48  ? 0.7141 0.6161 0.5350 0.0928  0.0288  0.0230  75  GLU B N   
4634 C CA  . GLU B 48  ? 0.7209 0.6305 0.5525 0.0922  0.0240  0.0246  75  GLU B CA  
4635 C C   . GLU B 48  ? 0.7815 0.6834 0.6098 0.0977  0.0181  0.0237  75  GLU B C   
4636 O O   . GLU B 48  ? 0.8627 0.7609 0.6894 0.0955  0.0120  0.0249  75  GLU B O   
4637 C CB  . GLU B 48  ? 0.7771 0.7057 0.6242 0.0940  0.0274  0.0250  75  GLU B CB  
4638 C CG  . GLU B 48  ? 0.8890 0.8253 0.7389 0.0891  0.0346  0.0269  75  GLU B CG  
4639 C CD  . GLU B 48  ? 0.9481 0.9035 0.8128 0.0918  0.0398  0.0270  75  GLU B CD  
4640 O OE1 . GLU B 48  ? 0.6848 0.6483 0.5584 0.0986  0.0374  0.0252  75  GLU B OE1 
4641 O OE2 . GLU B 48  ? 0.9691 0.9318 0.8365 0.0877  0.0468  0.0294  75  GLU B OE2 
4642 N N   . ARG B 49  ? 0.7621 0.6596 0.5875 0.1052  0.0202  0.0217  76  ARG B N   
4643 C CA  . ARG B 49  ? 0.6442 0.5337 0.4664 0.1124  0.0158  0.0219  76  ARG B CA  
4644 C C   . ARG B 49  ? 0.7469 0.6153 0.5531 0.1106  0.0143  0.0220  76  ARG B C   
4645 O O   . ARG B 49  ? 0.8880 0.7451 0.6881 0.1168  0.0122  0.0227  76  ARG B O   
4646 C CB  . ARG B 49  ? 0.7038 0.5953 0.5294 0.1221  0.0199  0.0196  76  ARG B CB  
4647 C CG  . ARG B 49  ? 0.6759 0.5908 0.5192 0.1249  0.0224  0.0197  76  ARG B CG  
4648 C CD  . ARG B 49  ? 0.6209 0.5371 0.4669 0.1363  0.0271  0.0172  76  ARG B CD  
4649 N NE  . ARG B 49  ? 0.7794 0.6852 0.6146 0.1358  0.0347  0.0131  76  ARG B NE  
4650 C CZ  . ARG B 49  ? 0.8475 0.7653 0.6868 0.1347  0.0417  0.0113  76  ARG B CZ  
4651 N NH1 . ARG B 49  ? 0.5526 0.4928 0.4079 0.1333  0.0434  0.0137  76  ARG B NH1 
4652 N NH2 . ARG B 49  ? 0.7954 0.7025 0.6220 0.1344  0.0473  0.0068  76  ARG B NH2 
4653 N N   . LEU B 50  ? 0.7367 0.5998 0.5363 0.1028  0.0158  0.0218  77  LEU B N   
4654 C CA  . LEU B 50  ? 0.5821 0.4284 0.3687 0.1002  0.0148  0.0222  77  LEU B CA  
4655 C C   . LEU B 50  ? 0.8116 0.6540 0.5952 0.1015  0.0085  0.0252  77  LEU B C   
4656 O O   . LEU B 50  ? 0.8197 0.6718 0.6091 0.0988  0.0046  0.0263  77  LEU B O   
4657 C CB  . LEU B 50  ? 0.7024 0.5485 0.4855 0.0925  0.0172  0.0218  77  LEU B CB  
4658 C CG  . LEU B 50  ? 0.7186 0.5654 0.4995 0.0906  0.0223  0.0186  77  LEU B CG  
4659 C CD1 . LEU B 50  ? 0.6032 0.4523 0.3818 0.0848  0.0233  0.0194  77  LEU B CD1 
4660 C CD2 . LEU B 50  ? 0.5918 0.4247 0.3646 0.0919  0.0242  0.0157  77  LEU B CD2 
4661 N N   . ARG B 51  ? 0.8229 0.6500 0.5960 0.1054  0.0075  0.0265  78  ARG B N   
4662 C CA  . ARG B 51  ? 0.7703 0.5923 0.5369 0.1078  0.0014  0.0299  78  ARG B CA  
4663 C C   . ARG B 51  ? 0.8495 0.6636 0.6062 0.1004  0.0019  0.0304  78  ARG B C   
4664 O O   . ARG B 51  ? 0.7534 0.5520 0.4978 0.0992  0.0047  0.0316  78  ARG B O   
4665 C CB  . ARG B 51  ? 0.7338 0.5408 0.4912 0.1162  0.0009  0.0323  78  ARG B CB  
4666 C CG  . ARG B 51  ? 0.8932 0.7111 0.6604 0.1264  -0.0032 0.0333  78  ARG B CG  
4667 C CD  . ARG B 51  ? 0.8207 0.6217 0.5767 0.1364  -0.0046 0.0371  78  ARG B CD  
4668 N NE  . ARG B 51  ? 0.9088 0.6908 0.6572 0.1373  0.0033  0.0354  78  ARG B NE  
4669 C CZ  . ARG B 51  ? 0.8280 0.6102 0.5823 0.1442  0.0070  0.0330  78  ARG B CZ  
4670 N NH1 . ARG B 51  ? 0.7260 0.5283 0.4952 0.1516  0.0042  0.0326  78  ARG B NH1 
4671 N NH2 . ARG B 51  ? 0.8301 0.5922 0.5753 0.1433  0.0141  0.0304  78  ARG B NH2 
4672 N N   . HIS B 52  ? 0.7632 0.5880 0.5259 0.0953  0.0001  0.0295  79  HIS B N   
4673 C CA  . HIS B 52  ? 0.6785 0.4979 0.4333 0.0896  0.0003  0.0295  79  HIS B CA  
4674 C C   . HIS B 52  ? 0.7122 0.5427 0.4743 0.0865  -0.0044 0.0285  79  HIS B C   
4675 O O   . HIS B 52  ? 0.6611 0.5045 0.4364 0.0852  -0.0036 0.0275  79  HIS B O   
4676 C CB  . HIS B 52  ? 0.6069 0.4242 0.3612 0.0849  0.0071  0.0282  79  HIS B CB  
4677 C CG  . HIS B 52  ? 0.7110 0.5227 0.4576 0.0807  0.0086  0.0283  79  HIS B CG  
4678 N ND1 . HIS B 52  ? 0.8751 0.6924 0.6257 0.0774  0.0086  0.0275  79  HIS B ND1 
4679 C CD2 . HIS B 52  ? 0.7321 0.5325 0.4671 0.0796  0.0110  0.0293  79  HIS B CD2 
4680 C CE1 . HIS B 52  ? 0.8060 0.6156 0.5477 0.0755  0.0107  0.0276  79  HIS B CE1 
4681 N NE2 . HIS B 52  ? 0.7106 0.5112 0.4432 0.0766  0.0124  0.0286  79  HIS B NE2 
4682 N N   . PRO B 53  ? 0.7429 0.5682 0.4963 0.0847  -0.0087 0.0284  80  PRO B N   
4683 C CA  . PRO B 53  ? 0.6463 0.4808 0.4062 0.0805  -0.0139 0.0263  80  PRO B CA  
4684 C C   . PRO B 53  ? 0.8173 0.6567 0.5861 0.0747  -0.0089 0.0250  80  PRO B C   
4685 O O   . PRO B 53  ? 0.8448 0.6762 0.6078 0.0727  -0.0032 0.0252  80  PRO B O   
4686 C CB  . PRO B 53  ? 0.7324 0.5553 0.4761 0.0791  -0.0174 0.0255  80  PRO B CB  
4687 C CG  . PRO B 53  ? 0.6540 0.4658 0.3850 0.0850  -0.0167 0.0286  80  PRO B CG  
4688 C CD  . PRO B 53  ? 0.6583 0.4686 0.3944 0.0861  -0.0090 0.0299  80  PRO B CD  
4689 N N   . ARG B 54  ? 0.7411 0.5945 0.5244 0.0722  -0.0107 0.0241  81  ARG B N   
4690 C CA  . ARG B 54  ? 0.7125 0.5698 0.5038 0.0670  -0.0052 0.0242  81  ARG B CA  
4691 C C   . ARG B 54  ? 0.6869 0.5343 0.4715 0.0606  -0.0052 0.0225  81  ARG B C   
4692 O O   . ARG B 54  ? 0.7572 0.6001 0.5417 0.0581  0.0008  0.0236  81  ARG B O   
4693 C CB  . ARG B 54  ? 0.7966 0.6717 0.6054 0.0656  -0.0058 0.0241  81  ARG B CB  
4694 C CG  . ARG B 54  ? 0.8072 0.6907 0.6227 0.0723  -0.0026 0.0256  81  ARG B CG  
4695 C CD  . ARG B 54  ? 0.8362 0.7395 0.6693 0.0728  -0.0044 0.0252  81  ARG B CD  
4696 N NE  . ARG B 54  ? 1.1216 1.0324 0.9610 0.0784  0.0014  0.0261  81  ARG B NE  
4697 C CZ  . ARG B 54  ? 1.1804 1.1089 1.0348 0.0819  0.0014  0.0260  81  ARG B CZ  
4698 N NH1 . ARG B 54  ? 1.0276 0.9710 0.8946 0.0800  -0.0048 0.0251  81  ARG B NH1 
4699 N NH2 . ARG B 54  ? 1.0756 1.0078 0.9324 0.0877  0.0077  0.0261  81  ARG B NH2 
4700 N N   . GLU B 55  ? 0.7611 0.6041 0.5388 0.0587  -0.0118 0.0197  82  GLU B N   
4701 C CA  . GLU B 55  ? 0.6981 0.5279 0.4660 0.0535  -0.0113 0.0171  82  GLU B CA  
4702 C C   . GLU B 55  ? 0.7909 0.6061 0.5448 0.0571  -0.0054 0.0184  82  GLU B C   
4703 O O   . GLU B 55  ? 0.7703 0.5743 0.5175 0.0545  -0.0020 0.0170  82  GLU B O   
4704 C CB  . GLU B 55  ? 0.7594 0.5883 0.5211 0.0507  -0.0204 0.0128  82  GLU B CB  
4705 C CG  . GLU B 55  ? 0.8795 0.7060 0.6295 0.0577  -0.0253 0.0137  82  GLU B CG  
4706 C CD  . GLU B 55  ? 1.1670 1.0095 0.9283 0.0628  -0.0303 0.0160  82  GLU B CD  
4707 O OE1 . GLU B 55  ? 1.2011 1.0584 0.9804 0.0609  -0.0294 0.0164  82  GLU B OE1 
4708 O OE2 . GLU B 55  ? 1.2539 1.0936 1.0055 0.0693  -0.0345 0.0177  82  GLU B OE2 
4709 N N   . ARG B 56  ? 0.8083 0.6235 0.5583 0.0629  -0.0038 0.0208  83  ARG B N   
4710 C CA  . ARG B 56  ? 0.7072 0.5133 0.4480 0.0656  0.0025  0.0222  83  ARG B CA  
4711 C C   . ARG B 56  ? 0.7113 0.5239 0.4605 0.0672  0.0084  0.0247  83  ARG B C   
4712 O O   . ARG B 56  ? 0.7774 0.5876 0.5226 0.0696  0.0126  0.0258  83  ARG B O   
4713 C CB  . ARG B 56  ? 0.8113 0.6116 0.5409 0.0694  0.0011  0.0229  83  ARG B CB  
4714 C CG  . ARG B 56  ? 0.8236 0.6190 0.5428 0.0691  -0.0060 0.0209  83  ARG B CG  
4715 C CD  . ARG B 56  ? 0.5896 0.3738 0.2975 0.0661  -0.0050 0.0175  83  ARG B CD  
4716 N NE  . ARG B 56  ? 0.8548 0.6284 0.5491 0.0689  0.0011  0.0185  83  ARG B NE  
4717 C CZ  . ARG B 56  ? 0.9557 0.7182 0.6380 0.0682  0.0042  0.0157  83  ARG B CZ  
4718 N NH1 . ARG B 56  ? 0.8528 0.6106 0.5334 0.0645  0.0014  0.0113  83  ARG B NH1 
4719 N NH2 . ARG B 56  ? 0.8547 0.6105 0.5267 0.0712  0.0108  0.0171  83  ARG B NH2 
4720 N N   . THR B 57  ? 0.7068 0.5289 0.4678 0.0655  0.0087  0.0255  84  THR B N   
4721 C CA  . THR B 57  ? 0.7243 0.5534 0.4917 0.0672  0.0136  0.0277  84  THR B CA  
4722 C C   . THR B 57  ? 0.6431 0.4727 0.4149 0.0645  0.0169  0.0293  84  THR B C   
4723 O O   . THR B 57  ? 0.6726 0.5025 0.4488 0.0600  0.0149  0.0285  84  THR B O   
4724 C CB  . THR B 57  ? 0.6246 0.4643 0.4003 0.0693  0.0123  0.0278  84  THR B CB  
4725 O OG1 . THR B 57  ? 0.8382 0.6740 0.6086 0.0722  0.0091  0.0270  84  THR B OG1 
4726 C CG2 . THR B 57  ? 0.5341 0.3795 0.3126 0.0713  0.0172  0.0290  84  THR B CG2 
4727 N N   . ALA B 58  ? 0.6382 0.4680 0.4086 0.0669  0.0218  0.0317  85  ALA B N   
4728 C CA  . ALA B 58  ? 0.7988 0.6275 0.5712 0.0659  0.0258  0.0348  85  ALA B CA  
4729 C C   . ALA B 58  ? 0.7420 0.5814 0.5181 0.0689  0.0289  0.0375  85  ALA B C   
4730 O O   . ALA B 58  ? 0.7304 0.5755 0.5056 0.0719  0.0284  0.0362  85  ALA B O   
4731 C CB  . ALA B 58  ? 0.5751 0.3917 0.3390 0.0679  0.0288  0.0359  85  ALA B CB  
4732 N N   . LEU B 59  ? 0.7150 0.5561 0.4942 0.0675  0.0324  0.0410  86  LEU B N   
4733 C CA  . LEU B 59  ? 0.6800 0.5313 0.4609 0.0702  0.0356  0.0436  86  LEU B CA  
4734 C C   . LEU B 59  ? 0.7030 0.5496 0.4774 0.0734  0.0398  0.0489  86  LEU B C   
4735 O O   . LEU B 59  ? 0.8574 0.6932 0.6298 0.0712  0.0425  0.0519  86  LEU B O   
4736 C CB  . LEU B 59  ? 0.5333 0.3927 0.3229 0.0666  0.0371  0.0440  86  LEU B CB  
4737 C CG  . LEU B 59  ? 0.7693 0.6362 0.5665 0.0657  0.0328  0.0396  86  LEU B CG  
4738 C CD1 . LEU B 59  ? 0.6559 0.5341 0.4638 0.0631  0.0353  0.0404  86  LEU B CD1 
4739 C CD2 . LEU B 59  ? 0.6184 0.4887 0.4120 0.0707  0.0313  0.0367  86  LEU B CD2 
4740 N N   . TRP B 60  ? 0.7126 0.5668 0.4832 0.0787  0.0402  0.0498  87  TRP B N   
4741 C CA  . TRP B 60  ? 0.7122 0.5655 0.4761 0.0839  0.0431  0.0554  87  TRP B CA  
4742 C C   . TRP B 60  ? 0.7020 0.5676 0.4642 0.0862  0.0445  0.0567  87  TRP B C   
4743 O O   . TRP B 60  ? 0.7847 0.6605 0.5474 0.0874  0.0416  0.0522  87  TRP B O   
4744 C CB  . TRP B 60  ? 0.5945 0.4479 0.3550 0.0890  0.0411  0.0546  87  TRP B CB  
4745 C CG  . TRP B 60  ? 0.8756 0.7267 0.6296 0.0961  0.0436  0.0609  87  TRP B CG  
4746 C CD1 . TRP B 60  ? 0.7149 0.5515 0.4646 0.0991  0.0463  0.0646  87  TRP B CD1 
4747 C CD2 . TRP B 60  ? 0.8478 0.7108 0.5976 0.1022  0.0433  0.0643  87  TRP B CD2 
4748 N NE1 . TRP B 60  ? 0.7965 0.6350 0.5401 0.1077  0.0480  0.0710  87  TRP B NE1 
4749 C CE2 . TRP B 60  ? 0.6546 0.5105 0.3981 0.1096  0.0456  0.0711  87  TRP B CE2 
4750 C CE3 . TRP B 60  ? 0.6753 0.5537 0.4248 0.1024  0.0411  0.0620  87  TRP B CE3 
4751 C CZ2 . TRP B 60  ? 0.6910 0.5565 0.4284 0.1179  0.0451  0.0763  87  TRP B CZ2 
4752 C CZ3 . TRP B 60  ? 0.7909 0.6789 0.5337 0.1094  0.0404  0.0661  87  TRP B CZ3 
4753 C CH2 . TRP B 60  ? 0.6945 0.5769 0.4314 0.1174  0.0420  0.0736  87  TRP B CH2 
4754 N N   . VAL B 61  ? 0.7474 0.6111 0.5066 0.0862  0.0493  0.0626  88  VAL B N   
4755 C CA  . VAL B 61  ? 0.7207 0.5951 0.4767 0.0879  0.0518  0.0639  88  VAL B CA  
4756 C C   . VAL B 61  ? 0.6184 0.4901 0.3634 0.0936  0.0554  0.0723  88  VAL B C   
4757 O O   . VAL B 61  ? 0.8151 0.6737 0.5574 0.0929  0.0597  0.0787  88  VAL B O   
4758 C CB  . VAL B 61  ? 0.7562 0.6330 0.5198 0.0821  0.0557  0.0634  88  VAL B CB  
4759 C CG1 . VAL B 61  ? 0.6456 0.5337 0.4046 0.0847  0.0592  0.0640  88  VAL B CG1 
4760 C CG2 . VAL B 61  ? 0.6363 0.5152 0.4105 0.0780  0.0515  0.0562  88  VAL B CG2 
4761 N N   . ALA B 62  ? 0.6334 0.5165 0.3708 0.0993  0.0535  0.0722  89  ALA B N   
4762 C CA  . ALA B 62  ? 0.7013 0.5843 0.4260 0.1063  0.0559  0.0805  89  ALA B CA  
4763 C C   . ALA B 62  ? 0.8098 0.7054 0.5271 0.1079  0.0572  0.0795  89  ALA B C   
4764 O O   . ALA B 62  ? 0.7608 0.6683 0.4796 0.1076  0.0525  0.0714  89  ALA B O   
4765 C CB  . ALA B 62  ? 0.6134 0.5000 0.3344 0.1140  0.0506  0.0815  89  ALA B CB  
4766 N N   . THR B 63  ? 0.7314 0.6228 0.4395 0.1094  0.0641  0.0877  90  THR B N   
4767 C CA  . THR B 63  ? 0.7954 0.6974 0.4935 0.1115  0.0667  0.0876  90  THR B CA  
4768 C C   . THR B 63  ? 0.7763 0.6744 0.4568 0.1190  0.0705  0.0990  90  THR B C   
4769 O O   . THR B 63  ? 0.8858 0.7688 0.5638 0.1198  0.0751  0.1083  90  THR B O   
4770 C CB  . THR B 63  ? 0.7163 0.6193 0.4221 0.1046  0.0738  0.0854  90  THR B CB  
4771 O OG1 . THR B 63  ? 0.8795 0.7937 0.5752 0.1074  0.0762  0.0830  90  THR B OG1 
4772 C CG2 . THR B 63  ? 0.7386 0.6290 0.4457 0.1005  0.0828  0.0949  90  THR B CG2 
4773 N N   . ASP B 64  ? 0.6776 0.5881 0.3443 0.1247  0.0684  0.0982  91  ASP B N   
4774 C CA  . ASP B 64  ? 0.8903 0.7992 0.5371 0.1336  0.0704  0.1091  91  ASP B CA  
4775 C C   . ASP B 64  ? 0.6714 0.5967 0.3039 0.1377  0.0673  0.1044  91  ASP B C   
4776 O O   . ASP B 64  ? 0.7321 0.6689 0.3708 0.1342  0.0621  0.0920  91  ASP B O   
4777 C CB  . ASP B 64  ? 0.7427 0.6482 0.3871 0.1417  0.0642  0.1145  91  ASP B CB  
4778 C CG  . ASP B 64  ? 0.8346 0.7545 0.4894 0.1421  0.0532  0.1037  91  ASP B CG  
4779 O OD1 . ASP B 64  ? 0.7625 0.6997 0.4100 0.1458  0.0464  0.0987  91  ASP B OD1 
4780 O OD2 . ASP B 64  ? 0.7645 0.6785 0.4344 0.1380  0.0515  0.1000  91  ASP B OD2 
4781 N N   . HIS B 65  ? 0.7344 0.6589 0.3459 0.1453  0.0708  0.1143  92  HIS B N   
4782 C CA  . HIS B 65  ? 0.8325 0.7717 0.4254 0.1505  0.0678  0.1110  92  HIS B CA  
4783 C C   . HIS B 65  ? 0.8545 0.7994 0.4503 0.1435  0.0727  0.1008  92  HIS B C   
4784 O O   . HIS B 65  ? 0.9120 0.8698 0.5050 0.1431  0.0663  0.0889  92  HIS B O   
4785 C CB  . HIS B 65  ? 0.7735 0.7291 0.3652 0.1556  0.0537  0.1037  92  HIS B CB  
4786 C CG  . HIS B 65  ? 0.9015 0.8554 0.4891 0.1652  0.0486  0.1139  92  HIS B CG  
4787 N ND1 . HIS B 65  ? 0.7839 0.7315 0.3889 0.1644  0.0459  0.1145  92  HIS B ND1 
4788 C CD2 . HIS B 65  ? 0.8745 0.8323 0.4419 0.1772  0.0458  0.1241  92  HIS B CD2 
4789 C CE1 . HIS B 65  ? 0.7482 0.6958 0.3450 0.1757  0.0422  0.1244  92  HIS B CE1 
4790 N NE2 . HIS B 65  ? 0.7951 0.7490 0.3692 0.1839  0.0416  0.1307  92  HIS B NE2 
4791 N N   . ASN B 66  ? 0.7926 0.7278 0.3944 0.1378  0.0846  0.1052  93  ASN B N   
4792 C CA  . ASN B 66  ? 0.8899 0.8305 0.4989 0.1319  0.0905  0.0962  93  ASN B CA  
4793 C C   . ASN B 66  ? 0.9001 0.8434 0.4885 0.1354  0.1004  0.1011  93  ASN B C   
4794 O O   . ASN B 66  ? 0.8580 0.7925 0.4366 0.1370  0.1094  0.1145  93  ASN B O   
4795 C CB  . ASN B 66  ? 0.8567 0.7892 0.4891 0.1231  0.0967  0.0966  93  ASN B CB  
4796 C CG  . ASN B 66  ? 0.7488 0.6800 0.4006 0.1192  0.0873  0.0888  93  ASN B CG  
4797 O OD1 . ASN B 66  ? 0.8004 0.7395 0.4572 0.1184  0.0807  0.0771  93  ASN B OD1 
4798 N ND2 . ASN B 66  ? 0.8028 0.7224 0.4643 0.1166  0.0874  0.0953  93  ASN B ND2 
4799 N N   . MET B 67  ? 0.8840 0.8381 0.4649 0.1365  0.0996  0.0900  94  MET B N   
4800 C CA  . MET B 67  ? 0.8516 0.8092 0.4150 0.1390  0.1108  0.0921  94  MET B CA  
4801 C C   . MET B 67  ? 0.8175 0.7761 0.3982 0.1327  0.1221  0.0882  94  MET B C   
4802 O O   . MET B 67  ? 0.9314 0.8919 0.5022 0.1337  0.1349  0.0930  94  MET B O   
4803 C CB  . MET B 67  ? 0.7365 0.7048 0.2788 0.1445  0.1041  0.0815  94  MET B CB  
4804 C CG  . MET B 67  ? 0.7556 0.7270 0.2743 0.1527  0.0956  0.0879  94  MET B CG  
4805 S SD  . MET B 67  ? 1.0989 1.0634 0.5908 0.1593  0.1086  0.1068  94  MET B SD  
4806 C CE  . MET B 67  ? 1.1500 1.1181 0.6228 0.1695  0.0942  0.1141  94  MET B CE  
4807 N N   . ASP B 68  ? 0.8870 0.8456 0.4930 0.1270  0.1179  0.0801  95  ASP B N   
4808 C CA  . ASP B 68  ? 0.7577 0.7194 0.3838 0.1218  0.1267  0.0765  95  ASP B CA  
4809 C C   . ASP B 68  ? 0.8571 0.8120 0.5047 0.1146  0.1294  0.0848  95  ASP B C   
4810 O O   . ASP B 68  ? 0.9592 0.9043 0.6030 0.1141  0.1268  0.0941  95  ASP B O   
4811 C CB  . ASP B 68  ? 0.7067 0.6730 0.3436 0.1216  0.1199  0.0609  95  ASP B CB  
4812 C CG  . ASP B 68  ? 0.9250 0.8862 0.5741 0.1189  0.1065  0.0566  95  ASP B CG  
4813 O OD1 . ASP B 68  ? 0.8431 0.7983 0.4925 0.1179  0.1022  0.0649  95  ASP B OD1 
4814 O OD2 . ASP B 68  ? 0.9205 0.8826 0.5781 0.1181  0.1011  0.0451  95  ASP B OD2 
4815 N N   . ASN B 69  ? 0.8507 0.8106 0.5208 0.1094  0.1343  0.0808  96  ASN B N   
4816 C CA  . ASN B 69  ? 0.8810 0.8365 0.5726 0.1012  0.1367  0.0868  96  ASN B CA  
4817 C C   . ASN B 69  ? 0.8467 0.7981 0.5547 0.0984  0.1243  0.0801  96  ASN B C   
4818 O O   . ASN B 69  ? 0.8028 0.7574 0.5328 0.0929  0.1243  0.0773  96  ASN B O   
4819 C CB  . ASN B 69  ? 0.7362 0.7028 0.4442 0.0968  0.1488  0.0869  96  ASN B CB  
4820 C CG  . ASN B 69  ? 0.9401 0.9184 0.6596 0.1001  0.1467  0.0743  96  ASN B CG  
4821 O OD1 . ASN B 69  ? 1.0549 1.0327 0.7620 0.1065  0.1403  0.0657  96  ASN B OD1 
4822 N ND2 . ASN B 69  ? 0.9670 0.9559 0.7106 0.0957  0.1521  0.0729  96  ASN B ND2 
4823 N N   . THR B 70  ? 0.8715 0.8170 0.5685 0.1024  0.1137  0.0777  97  THR B N   
4824 C CA  . THR B 70  ? 0.7944 0.7359 0.5045 0.1002  0.1027  0.0714  97  THR B CA  
4825 C C   . THR B 70  ? 0.7217 0.6543 0.4459 0.0935  0.1028  0.0777  97  THR B C   
4826 O O   . THR B 70  ? 0.7634 0.6968 0.5058 0.0890  0.0995  0.0729  97  THR B O   
4827 C CB  . THR B 70  ? 0.8137 0.7529 0.5100 0.1051  0.0926  0.0685  97  THR B CB  
4828 O OG1 . THR B 70  ? 0.7871 0.7341 0.4737 0.1091  0.0905  0.0590  97  THR B OG1 
4829 C CG2 . THR B 70  ? 0.7465 0.6800 0.4556 0.1022  0.0832  0.0648  97  THR B CG2 
4830 N N   . SER B 71  ? 0.6861 0.6090 0.4009 0.0932  0.1066  0.0885  98  SER B N   
4831 C CA  . SER B 71  ? 0.8938 0.8046 0.6193 0.0867  0.1068  0.0937  98  SER B CA  
4832 C C   . SER B 71  ? 0.7976 0.7132 0.5422 0.0777  0.1140  0.0936  98  SER B C   
4833 O O   . SER B 71  ? 0.8258 0.7370 0.5857 0.0711  0.1105  0.0916  98  SER B O   
4834 C CB  . SER B 71  ? 0.6239 0.5207 0.3331 0.0893  0.1109  0.1058  98  SER B CB  
4835 O OG  . SER B 71  ? 1.1273 1.0259 0.8258 0.0896  0.1224  0.1135  98  SER B OG  
4836 N N   . THR B 72  ? 0.7433 0.6694 0.4874 0.0773  0.1242  0.0956  99  THR B N   
4837 C CA  . THR B 72  ? 0.8030 0.7387 0.5681 0.0689  0.1312  0.0949  99  THR B CA  
4838 C C   . THR B 72  ? 0.7994 0.7461 0.5835 0.0685  0.1232  0.0839  99  THR B C   
4839 O O   . THR B 72  ? 0.7684 0.7170 0.5716 0.0610  0.1209  0.0823  99  THR B O   
4840 C CB  . THR B 72  ? 0.8469 0.7941 0.6073 0.0700  0.1444  0.0986  99  THR B CB  
4841 O OG1 . THR B 72  ? 0.9490 0.8840 0.6903 0.0702  0.1524  0.1104  99  THR B OG1 
4842 C CG2 . THR B 72  ? 0.6443 0.6059 0.4299 0.0613  0.1519  0.0976  99  THR B CG2 
4843 N N   . VAL B 73  ? 0.7607 0.7141 0.5389 0.0767  0.1186  0.0762  100 VAL B N   
4844 C CA  . VAL B 73  ? 0.7846 0.7455 0.5778 0.0780  0.1114  0.0665  100 VAL B CA  
4845 C C   . VAL B 73  ? 0.7462 0.6964 0.5453 0.0745  0.1006  0.0648  100 VAL B C   
4846 O O   . VAL B 73  ? 0.7894 0.7443 0.6060 0.0708  0.0966  0.0612  100 VAL B O   
4847 C CB  . VAL B 73  ? 0.6900 0.6542 0.4716 0.0870  0.1089  0.0588  100 VAL B CB  
4848 C CG1 . VAL B 73  ? 0.6530 0.6200 0.4475 0.0891  0.1013  0.0498  100 VAL B CG1 
4849 C CG2 . VAL B 73  ? 0.5778 0.5530 0.3535 0.0908  0.1203  0.0593  100 VAL B CG2 
4850 N N   . LEU B 74  ? 0.7794 0.7162 0.5638 0.0763  0.0958  0.0673  101 LEU B N   
4851 C CA  . LEU B 74  ? 0.7257 0.6519 0.5136 0.0740  0.0867  0.0655  101 LEU B CA  
4852 C C   . LEU B 74  ? 0.8127 0.7339 0.6129 0.0651  0.0883  0.0693  101 LEU B C   
4853 O O   . LEU B 74  ? 0.8139 0.7347 0.6258 0.0615  0.0819  0.0648  101 LEU B O   
4854 C CB  . LEU B 74  ? 0.7307 0.6462 0.5015 0.0785  0.0828  0.0683  101 LEU B CB  
4855 C CG  . LEU B 74  ? 0.7435 0.6621 0.5058 0.0849  0.0762  0.0614  101 LEU B CG  
4856 C CD1 . LEU B 74  ? 0.7588 0.6718 0.5056 0.0894  0.0736  0.0656  101 LEU B CD1 
4857 C CD2 . LEU B 74  ? 0.6669 0.5836 0.4393 0.0834  0.0683  0.0543  101 LEU B CD2 
4858 N N   . ARG B 75  ? 0.8542 0.7704 0.6507 0.0609  0.0968  0.0775  102 ARG B N   
4859 C CA  . ARG B 75  ? 0.7558 0.6640 0.5624 0.0509  0.0986  0.0806  102 ARG B CA  
4860 C C   . ARG B 75  ? 0.7422 0.6665 0.5716 0.0440  0.0987  0.0758  102 ARG B C   
4861 O O   . ARG B 75  ? 0.9424 0.8633 0.7829 0.0366  0.0940  0.0731  102 ARG B O   
4862 C CB  . ARG B 75  ? 0.6246 0.5221 0.4216 0.0475  0.1092  0.0911  102 ARG B CB  
4863 C CG  . ARG B 75  ? 1.1140 1.0239 0.9220 0.0405  0.1205  0.0945  102 ARG B CG  
4864 C CD  . ARG B 75  ? 1.3820 1.2755 1.1854 0.0322  0.1299  0.1042  102 ARG B CD  
4865 N NE  . ARG B 75  ? 1.2698 1.1477 1.0793 0.0242  0.1247  0.1024  102 ARG B NE  
4866 C CZ  . ARG B 75  ? 1.4316 1.2907 1.2383 0.0155  0.1315  0.1090  102 ARG B CZ  
4867 N NH1 . ARG B 75  ? 1.6036 1.4566 1.4018 0.0132  0.1443  0.1192  102 ARG B NH1 
4868 N NH2 . ARG B 75  ? 1.1851 1.0292 0.9962 0.0087  0.1258  0.1054  102 ARG B NH2 
4869 N N   . GLU B 76  ? 0.6682 0.6109 0.5046 0.0470  0.1036  0.0739  103 GLU B N   
4870 C CA  . GLU B 76  ? 0.7400 0.7015 0.5997 0.0424  0.1032  0.0693  103 GLU B CA  
4871 C C   . GLU B 76  ? 0.8470 0.8106 0.7133 0.0461  0.0908  0.0612  103 GLU B C   
4872 O O   . GLU B 76  ? 0.8238 0.7958 0.7073 0.0405  0.0860  0.0579  103 GLU B O   
4873 C CB  . GLU B 76  ? 0.6619 0.6426 0.5268 0.0469  0.1123  0.0692  103 GLU B CB  
4874 C CG  . GLU B 76  ? 1.0802 1.0621 0.9422 0.0414  0.1263  0.0777  103 GLU B CG  
4875 C CD  . GLU B 76  ? 1.2724 1.2733 1.1372 0.0469  0.1363  0.0773  103 GLU B CD  
4876 O OE1 . GLU B 76  ? 1.1210 1.1350 0.9934 0.0545  0.1323  0.0699  103 GLU B OE1 
4877 O OE2 . GLU B 76  ? 1.1998 1.2012 1.0581 0.0441  0.1489  0.0846  103 GLU B OE2 
4878 N N   . TRP B 77  ? 0.7825 0.7387 0.6346 0.0552  0.0853  0.0581  104 TRP B N   
4879 C CA  . TRP B 77  ? 0.7732 0.7278 0.6285 0.0587  0.0746  0.0516  104 TRP B CA  
4880 C C   . TRP B 77  ? 0.8088 0.7493 0.6626 0.0527  0.0676  0.0518  104 TRP B C   
4881 O O   . TRP B 77  ? 0.7864 0.7302 0.6502 0.0504  0.0604  0.0477  104 TRP B O   
4882 C CB  . TRP B 77  ? 0.6994 0.6481 0.5395 0.0681  0.0718  0.0484  104 TRP B CB  
4883 C CG  . TRP B 77  ? 0.7355 0.6803 0.5769 0.0716  0.0624  0.0426  104 TRP B CG  
4884 C CD1 . TRP B 77  ? 0.5969 0.5512 0.4490 0.0756  0.0593  0.0381  104 TRP B CD1 
4885 C CD2 . TRP B 77  ? 0.6566 0.5865 0.4872 0.0721  0.0555  0.0413  104 TRP B CD2 
4886 N NE1 . TRP B 77  ? 0.6830 0.6273 0.5301 0.0782  0.0510  0.0347  104 TRP B NE1 
4887 C CE2 . TRP B 77  ? 0.8299 0.7599 0.6644 0.0756  0.0489  0.0364  104 TRP B CE2 
4888 C CE3 . TRP B 77  ? 0.5760 0.4931 0.3944 0.0706  0.0547  0.0443  104 TRP B CE3 
4889 C CZ2 . TRP B 77  ? 0.6314 0.5488 0.4575 0.0764  0.0425  0.0344  104 TRP B CZ2 
4890 C CZ3 . TRP B 77  ? 0.6541 0.5610 0.4662 0.0719  0.0481  0.0417  104 TRP B CZ3 
4891 C CH2 . TRP B 77  ? 0.6911 0.5981 0.5068 0.0742  0.0425  0.0368  104 TRP B CH2 
4892 N N   . LEU B 78  ? 0.7790 0.7035 0.6193 0.0509  0.0698  0.0564  105 LEU B N   
4893 C CA  . LEU B 78  ? 0.7551 0.6641 0.5922 0.0461  0.0645  0.0562  105 LEU B CA  
4894 C C   . LEU B 78  ? 0.7747 0.6864 0.6262 0.0350  0.0653  0.0561  105 LEU B C   
4895 O O   . LEU B 78  ? 0.8288 0.7354 0.6837 0.0309  0.0580  0.0520  105 LEU B O   
4896 C CB  . LEU B 78  ? 0.6730 0.5649 0.4931 0.0483  0.0678  0.0619  105 LEU B CB  
4897 C CG  . LEU B 78  ? 0.6696 0.5586 0.4765 0.0578  0.0640  0.0604  105 LEU B CG  
4898 C CD1 . LEU B 78  ? 0.6845 0.5619 0.4765 0.0613  0.0679  0.0671  105 LEU B CD1 
4899 C CD2 . LEU B 78  ? 0.5479 0.4314 0.3550 0.0588  0.0552  0.0548  105 LEU B CD2 
4900 N N   . VAL B 79  ? 0.6807 0.6010 0.5405 0.0294  0.0742  0.0603  106 VAL B N   
4901 C CA  . VAL B 79  ? 0.7866 0.7129 0.6631 0.0171  0.0753  0.0594  106 VAL B CA  
4902 C C   . VAL B 79  ? 0.7250 0.6700 0.6186 0.0168  0.0663  0.0521  106 VAL B C   
4903 O O   . VAL B 79  ? 0.7642 0.7098 0.6674 0.0080  0.0606  0.0483  106 VAL B O   
4904 C CB  . VAL B 79  ? 0.7452 0.6811 0.6291 0.0115  0.0879  0.0654  106 VAL B CB  
4905 C CG1 . VAL B 79  ? 0.7017 0.6552 0.6101 -0.0007 0.0885  0.0626  106 VAL B CG1 
4906 C CG2 . VAL B 79  ? 0.6977 0.6104 0.5652 0.0084  0.0961  0.0735  106 VAL B CG2 
4907 N N   . ALA B 80  ? 0.7092 0.6683 0.6055 0.0270  0.0645  0.0497  107 ALA B N   
4908 C CA  . ALA B 80  ? 0.6402 0.6180 0.5525 0.0293  0.0568  0.0441  107 ALA B CA  
4909 C C   . ALA B 80  ? 0.6256 0.5931 0.5294 0.0340  0.0450  0.0396  107 ALA B C   
4910 O O   . ALA B 80  ? 0.7815 0.7618 0.6967 0.0351  0.0371  0.0355  107 ALA B O   
4911 C CB  . ALA B 80  ? 0.6043 0.5999 0.5228 0.0391  0.0614  0.0438  107 ALA B CB  
4912 N N   . VAL B 81  ? 0.5940 0.5400 0.4781 0.0374  0.0437  0.0405  108 VAL B N   
4913 C CA  . VAL B 81  ? 0.7541 0.6898 0.6288 0.0419  0.0342  0.0368  108 VAL B CA  
4914 C C   . VAL B 81  ? 0.8029 0.7180 0.6656 0.0364  0.0319  0.0368  108 VAL B C   
4915 O O   . VAL B 81  ? 0.9189 0.8244 0.7723 0.0396  0.0251  0.0340  108 VAL B O   
4916 C CB  . VAL B 81  ? 0.8231 0.7542 0.6860 0.0529  0.0345  0.0366  108 VAL B CB  
4917 C CG1 . VAL B 81  ? 0.6842 0.6328 0.5571 0.0592  0.0376  0.0357  108 VAL B CG1 
4918 C CG2 . VAL B 81  ? 0.7864 0.7040 0.6344 0.0540  0.0404  0.0402  108 VAL B CG2 
4919 N N   . LYS B 82  ? 0.7701 0.6769 0.6319 0.0286  0.0380  0.0401  109 LYS B N   
4920 C CA  . LYS B 82  ? 0.8129 0.6972 0.6613 0.0253  0.0372  0.0403  109 LYS B CA  
4921 C C   . LYS B 82  ? 0.8775 0.7581 0.7270 0.0204  0.0280  0.0342  109 LYS B C   
4922 O O   . LYS B 82  ? 0.9380 0.8027 0.7737 0.0232  0.0245  0.0323  109 LYS B O   
4923 C CB  . LYS B 82  ? 0.8020 0.6765 0.6498 0.0176  0.0461  0.0453  109 LYS B CB  
4924 C CG  . LYS B 82  ? 0.9367 0.7861 0.7664 0.0199  0.0491  0.0485  109 LYS B CG  
4925 C CD  . LYS B 82  ? 1.2495 1.0823 1.0744 0.0137  0.0443  0.0437  109 LYS B CD  
4926 C CE  . LYS B 82  ? 1.2466 1.0540 1.0544 0.0172  0.0488  0.0473  109 LYS B CE  
4927 N NZ  . LYS B 82  ? 1.1250 0.9230 0.9309 0.0139  0.0590  0.0549  109 LYS B NZ  
4928 N N   . SER B 83  ? 0.8639 0.7608 0.7298 0.0134  0.0241  0.0308  110 SER B N   
4929 C CA  . SER B 83  ? 0.8279 0.7226 0.6944 0.0074  0.0146  0.0245  110 SER B CA  
4930 C C   . SER B 83  ? 0.7363 0.6313 0.5942 0.0167  0.0057  0.0215  110 SER B C   
4931 O O   . SER B 83  ? 0.9147 0.8014 0.7650 0.0140  -0.0017 0.0168  110 SER B O   
4932 C CB  . SER B 83  ? 0.8103 0.7274 0.6988 -0.0022 0.0116  0.0214  110 SER B CB  
4933 O OG  . SER B 83  ? 0.9732 0.9150 0.8752 0.0054  0.0093  0.0219  110 SER B OG  
4934 N N   . LEU B 84  ? 0.8291 0.7318 0.6866 0.0273  0.0067  0.0240  111 LEU B N   
4935 C CA  . LEU B 84  ? 0.8183 0.7205 0.6681 0.0359  -0.0007 0.0221  111 LEU B CA  
4936 C C   . LEU B 84  ? 0.8099 0.6909 0.6396 0.0405  0.0006  0.0228  111 LEU B C   
4937 O O   . LEU B 84  ? 0.8069 0.6836 0.6276 0.0459  -0.0048 0.0213  111 LEU B O   
4938 C CB  . LEU B 84  ? 0.8770 0.7947 0.7351 0.0449  0.0004  0.0239  111 LEU B CB  
4939 C CG  . LEU B 84  ? 0.9448 0.8866 0.8247 0.0423  0.0017  0.0240  111 LEU B CG  
4940 C CD1 . LEU B 84  ? 0.8155 0.7682 0.7002 0.0528  0.0051  0.0258  111 LEU B CD1 
4941 C CD2 . LEU B 84  ? 0.9635 0.9191 0.8543 0.0382  -0.0085 0.0199  111 LEU B CD2 
4942 N N   . TYR B 85  ? 0.8413 0.7096 0.6639 0.0390  0.0079  0.0254  112 TYR B N   
4943 C CA  . TYR B 85  ? 0.7269 0.5798 0.5338 0.0446  0.0102  0.0266  112 TYR B CA  
4944 C C   . TYR B 85  ? 0.7034 0.5380 0.4994 0.0403  0.0109  0.0250  112 TYR B C   
4945 O O   . TYR B 85  ? 0.8070 0.6374 0.6068 0.0324  0.0119  0.0240  112 TYR B O   
4946 C CB  . TYR B 85  ? 0.6840 0.5384 0.4902 0.0492  0.0177  0.0310  112 TYR B CB  
4947 C CG  . TYR B 85  ? 0.7790 0.6465 0.5906 0.0551  0.0173  0.0313  112 TYR B CG  
4948 C CD1 . TYR B 85  ? 0.8642 0.7278 0.6677 0.0613  0.0157  0.0304  112 TYR B CD1 
4949 C CD2 . TYR B 85  ? 0.7297 0.6124 0.5542 0.0544  0.0194  0.0321  112 TYR B CD2 
4950 C CE1 . TYR B 85  ? 0.7796 0.6514 0.5865 0.0664  0.0159  0.0299  112 TYR B CE1 
4951 C CE2 . TYR B 85  ? 0.7789 0.6715 0.6072 0.0608  0.0198  0.0317  112 TYR B CE2 
4952 C CZ  . TYR B 85  ? 0.7437 0.6294 0.5625 0.0668  0.0178  0.0304  112 TYR B CZ  
4953 O OH  . TYR B 85  ? 0.5778 0.4698 0.3989 0.0729  0.0187  0.0294  112 TYR B OH  
4954 N N   . HIS B 86  ? 0.7556 0.5786 0.5382 0.0455  0.0110  0.0246  113 HIS B N   
4955 C CA  . HIS B 86  ? 0.7711 0.5757 0.5416 0.0438  0.0126  0.0228  113 HIS B CA  
4956 C C   . HIS B 86  ? 0.6833 0.4791 0.4542 0.0418  0.0199  0.0263  113 HIS B C   
4957 O O   . HIS B 86  ? 0.7454 0.5270 0.5119 0.0363  0.0210  0.0242  113 HIS B O   
4958 C CB  . HIS B 86  ? 0.7471 0.5447 0.5054 0.0510  0.0136  0.0228  113 HIS B CB  
4959 C CG  . HIS B 86  ? 0.7171 0.4965 0.4628 0.0516  0.0167  0.0212  113 HIS B CG  
4960 N ND1 . HIS B 86  ? 0.8647 0.6329 0.6010 0.0479  0.0130  0.0158  113 HIS B ND1 
4961 C CD2 . HIS B 86  ? 0.7673 0.5381 0.5078 0.0564  0.0234  0.0241  113 HIS B CD2 
4962 C CE1 . HIS B 86  ? 0.7376 0.4894 0.4630 0.0504  0.0180  0.0150  113 HIS B CE1 
4963 N NE2 . HIS B 86  ? 0.6549 0.4086 0.3834 0.0561  0.0244  0.0204  113 HIS B NE2 
4964 N N   . SER B 87  ? 0.6866 0.4893 0.4613 0.0463  0.0250  0.0317  114 SER B N   
4965 C CA  . SER B 87  ? 0.8773 0.6723 0.6510 0.0459  0.0321  0.0367  114 SER B CA  
4966 C C   . SER B 87  ? 0.7463 0.5556 0.5256 0.0503  0.0354  0.0416  114 SER B C   
4967 O O   . SER B 87  ? 0.7478 0.5691 0.5291 0.0548  0.0328  0.0406  114 SER B O   
4968 C CB  . SER B 87  ? 0.7284 0.5060 0.4892 0.0514  0.0357  0.0380  114 SER B CB  
4969 O OG  . SER B 87  ? 0.8114 0.5962 0.5692 0.0602  0.0362  0.0398  114 SER B OG  
4970 N N   . VAL B 88  ? 0.6768 0.4828 0.4567 0.0489  0.0416  0.0470  115 VAL B N   
4971 C CA  . VAL B 88  ? 0.8347 0.6526 0.6169 0.0531  0.0456  0.0520  115 VAL B CA  
4972 C C   . VAL B 88  ? 0.8157 0.6215 0.5884 0.0572  0.0520  0.0589  115 VAL B C   
4973 O O   . VAL B 88  ? 0.8854 0.6759 0.6555 0.0525  0.0560  0.0615  115 VAL B O   
4974 C CB  . VAL B 88  ? 0.6730 0.5041 0.4676 0.0468  0.0472  0.0523  115 VAL B CB  
4975 C CG1 . VAL B 88  ? 0.6676 0.5068 0.4608 0.0509  0.0533  0.0581  115 VAL B CG1 
4976 C CG2 . VAL B 88  ? 0.6570 0.5026 0.4608 0.0462  0.0407  0.0464  115 VAL B CG2 
4977 N N   . GLU B 89  ? 0.7323 0.5447 0.4995 0.0660  0.0526  0.0620  116 GLU B N   
4978 C CA  . GLU B 89  ? 0.8796 0.6843 0.6373 0.0722  0.0578  0.0696  116 GLU B CA  
4979 C C   . GLU B 89  ? 0.8768 0.6949 0.6345 0.0744  0.0609  0.0741  116 GLU B C   
4980 O O   . GLU B 89  ? 0.8016 0.6361 0.5631 0.0760  0.0576  0.0703  116 GLU B O   
4981 C CB  . GLU B 89  ? 0.8105 0.6138 0.5612 0.0818  0.0555  0.0697  116 GLU B CB  
4982 C CG  . GLU B 89  ? 1.1279 0.9253 0.8687 0.0905  0.0598  0.0782  116 GLU B CG  
4983 C CD  . GLU B 89  ? 1.2166 1.0035 0.9514 0.0984  0.0596  0.0788  116 GLU B CD  
4984 O OE1 . GLU B 89  ? 0.9869 0.7714 0.7245 0.0965  0.0567  0.0723  116 GLU B OE1 
4985 O OE2 . GLU B 89  ? 1.1253 0.9067 0.8521 0.1073  0.0627  0.0862  116 GLU B OE2 
4986 N N   . TRP B 90  ? 0.7467 0.5560 0.4984 0.0744  0.0677  0.0820  117 TRP B N   
4987 C CA  . TRP B 90  ? 0.7435 0.5631 0.4932 0.0753  0.0723  0.0869  117 TRP B CA  
4988 C C   . TRP B 90  ? 0.8793 0.6905 0.6142 0.0841  0.0764  0.0965  117 TRP B C   
4989 O O   . TRP B 90  ? 0.8241 0.6154 0.5528 0.0836  0.0815  0.1026  117 TRP B O   
4990 C CB  . TRP B 90  ? 0.6997 0.5185 0.4583 0.0645  0.0780  0.0878  117 TRP B CB  
4991 C CG  . TRP B 90  ? 0.8915 0.7195 0.6478 0.0646  0.0850  0.0936  117 TRP B CG  
4992 C CD1 . TRP B 90  ? 0.7290 0.5478 0.4829 0.0593  0.0945  0.1013  117 TRP B CD1 
4993 C CD2 . TRP B 90  ? 0.8126 0.6595 0.5675 0.0698  0.0842  0.0918  117 TRP B CD2 
4994 N NE1 . TRP B 90  ? 0.7920 0.6240 0.5428 0.0615  0.0999  0.1049  117 TRP B NE1 
4995 C CE2 . TRP B 90  ? 0.8184 0.6676 0.5694 0.0682  0.0934  0.0987  117 TRP B CE2 
4996 C CE3 . TRP B 90  ? 0.8195 0.6801 0.5753 0.0752  0.0771  0.0847  117 TRP B CE3 
4997 C CZ2 . TRP B 90  ? 0.8450 0.7101 0.5919 0.0726  0.0956  0.0982  117 TRP B CZ2 
4998 C CZ3 . TRP B 90  ? 1.0076 0.8826 0.7598 0.0789  0.0789  0.0838  117 TRP B CZ3 
4999 C CH2 . TRP B 90  ? 0.8198 0.6972 0.5671 0.0780  0.0879  0.0903  117 TRP B CH2 
5000 N N   . ARG B 91  ? 0.8453 0.6708 0.5737 0.0924  0.0740  0.0976  118 ARG B N   
5001 C CA  . ARG B 91  ? 0.8378 0.6595 0.5514 0.1030  0.0758  0.1064  118 ARG B CA  
5002 C C   . ARG B 91  ? 0.8708 0.7061 0.5767 0.1058  0.0782  0.1098  118 ARG B C   
5003 O O   . ARG B 91  ? 0.8447 0.6967 0.5475 0.1116  0.0725  0.1061  118 ARG B O   
5004 C CB  . ARG B 91  ? 0.7374 0.5648 0.4494 0.1120  0.0684  0.1036  118 ARG B CB  
5005 C CG  . ARG B 91  ? 1.2508 1.0641 0.9680 0.1106  0.0671  0.1004  118 ARG B CG  
5006 C CD  . ARG B 91  ? 1.0227 0.8449 0.7402 0.1195  0.0611  0.0976  118 ARG B CD  
5007 N NE  . ARG B 91  ? 1.1309 0.9601 0.8382 0.1313  0.0603  0.1050  118 ARG B NE  
5008 C CZ  . ARG B 91  ? 1.1700 1.0045 0.8762 0.1416  0.0568  0.1061  118 ARG B CZ  
5009 N NH1 . ARG B 91  ? 1.0323 0.8643 0.7461 0.1413  0.0550  0.1005  118 ARG B NH1 
5010 N NH2 . ARG B 91  ? 0.9256 0.7695 0.6229 0.1528  0.0551  0.1131  118 ARG B NH2 
5011 N N   . PRO B 92  ? 0.9037 0.7324 0.6060 0.1012  0.0869  0.1163  119 PRO B N   
5012 C CA  . PRO B 92  ? 0.8810 0.7210 0.5729 0.1047  0.0908  0.1204  119 PRO B CA  
5013 C C   . PRO B 92  ? 0.8356 0.6659 0.5075 0.1147  0.0943  0.1328  119 PRO B C   
5014 O O   . PRO B 92  ? 0.9237 0.7347 0.5905 0.1177  0.0966  0.1400  119 PRO B O   
5015 C CB  . PRO B 92  ? 0.8076 0.6464 0.5081 0.0936  0.0997  0.1210  119 PRO B CB  
5016 C CG  . PRO B 92  ? 0.8627 0.6805 0.5690 0.0867  0.1031  0.1241  119 PRO B CG  
5017 C CD  . PRO B 92  ? 0.7942 0.6071 0.5038 0.0906  0.0940  0.1185  119 PRO B CD  
5018 N N   . ALA B 93  ? 0.8962 0.7395 0.5552 0.1206  0.0948  0.1353  120 ALA B N   
5019 C CA  . ALA B 93  ? 0.9339 0.7701 0.5712 0.1311  0.0981  0.1480  120 ALA B CA  
5020 C C   . ALA B 93  ? 0.8894 0.7384 0.5147 0.1319  0.1026  0.1495  120 ALA B C   
5021 O O   . ALA B 93  ? 0.9379 0.8064 0.5597 0.1361  0.0955  0.1421  120 ALA B O   
5022 C CB  . ALA B 93  ? 0.8246 0.6672 0.4553 0.1437  0.0878  0.1482  120 ALA B CB  
5023 N N   . GLU B 94  ? 1.0505 0.8878 0.6691 0.1274  0.1152  0.1588  121 GLU B N   
5024 C CA  . GLU B 94  ? 1.0361 0.8852 0.6445 0.1268  0.1218  0.1598  121 GLU B CA  
5025 C C   . GLU B 94  ? 0.8824 0.7384 0.4648 0.1404  0.1181  0.1657  121 GLU B C   
5026 O O   . GLU B 94  ? 1.1390 1.0142 0.7157 0.1433  0.1135  0.1579  121 GLU B O   
5027 C CB  . GLU B 94  ? 0.8372 0.6723 0.4456 0.1180  0.1374  0.1692  121 GLU B CB  
5028 C CG  . GLU B 94  ? 1.1107 0.9413 0.7454 0.1038  0.1402  0.1630  121 GLU B CG  
5029 C CD  . GLU B 94  ? 1.3458 1.1979 1.0000 0.0991  0.1335  0.1476  121 GLU B CD  
5030 O OE1 . GLU B 94  ? 1.3524 1.2210 1.0034 0.1003  0.1363  0.1438  121 GLU B OE1 
5031 O OE2 . GLU B 94  ? 1.2086 1.0600 0.8797 0.0951  0.1257  0.1395  121 GLU B OE2 
5032 N N   . GLU B 95  ? 0.9475 0.7876 0.5131 0.1493  0.1197  0.1793  122 GLU B N   
5033 C CA  . GLU B 95  ? 0.9438 0.7910 0.4835 0.1635  0.1153  0.1862  122 GLU B CA  
5034 C C   . GLU B 95  ? 0.9418 0.7949 0.4825 0.1744  0.1013  0.1842  122 GLU B C   
5035 O O   . GLU B 95  ? 1.0040 0.8443 0.5575 0.1736  0.0996  0.1849  122 GLU B O   
5036 C CB  . GLU B 95  ? 0.9853 0.8130 0.5057 0.1673  0.1266  0.2031  122 GLU B CB  
5037 C CG  . GLU B 95  ? 1.1375 0.9639 0.6537 0.1580  0.1411  0.2060  122 GLU B CG  
5038 C CD  . GLU B 95  ? 1.3470 1.1976 0.8530 0.1609  0.1380  0.1982  122 GLU B CD  
5039 O OE1 . GLU B 95  ? 1.3985 1.2619 0.8936 0.1711  0.1260  0.1956  122 GLU B OE1 
5040 O OE2 . GLU B 95  ? 1.4905 1.3476 0.9997 0.1529  0.1476  0.1942  122 GLU B OE2 
5041 N N   . PRO B 96  ? 1.0318 0.9053 0.5593 0.1844  0.0909  0.1812  123 PRO B N   
5042 C CA  . PRO B 96  ? 0.8751 0.7656 0.3887 0.1851  0.0904  0.1770  123 PRO B CA  
5043 C C   . PRO B 96  ? 0.9590 0.8658 0.4853 0.1757  0.0879  0.1604  123 PRO B C   
5044 O O   . PRO B 96  ? 1.0153 0.9259 0.5647 0.1695  0.0818  0.1499  123 PRO B O   
5045 C CB  . PRO B 96  ? 0.9048 0.8112 0.4094 0.1974  0.0766  0.1769  123 PRO B CB  
5046 C CG  . PRO B 96  ? 0.8428 0.7527 0.3621 0.2008  0.0672  0.1731  123 PRO B CG  
5047 C CD  . PRO B 96  ? 0.8328 0.7162 0.3627 0.1952  0.0775  0.1798  123 PRO B CD  
5048 N N   . ARG B 97  ? 0.9115 0.8275 0.4253 0.1740  0.0924  0.1566  124 ARG B N   
5049 C CA  . ARG B 97  ? 1.0242 0.9538 0.5515 0.1654  0.0906  0.1399  124 ARG B CA  
5050 C C   . ARG B 97  ? 0.8369 0.7871 0.3590 0.1695  0.0762  0.1273  124 ARG B C   
5051 O O   . ARG B 97  ? 0.9917 0.9512 0.5238 0.1629  0.0738  0.1126  124 ARG B O   
5052 C CB  . ARG B 97  ? 0.8464 0.7751 0.3643 0.1612  0.1042  0.1409  124 ARG B CB  
5053 C CG  . ARG B 97  ? 1.0797 0.9910 0.6069 0.1541  0.1191  0.1516  124 ARG B CG  
5054 C CD  . ARG B 97  ? 1.1171 1.0333 0.6457 0.1475  0.1319  0.1481  124 ARG B CD  
5055 N NE  . ARG B 97  ? 1.2644 1.1858 0.7628 0.1550  0.1372  0.1526  124 ARG B NE  
5056 C CZ  . ARG B 97  ? 1.4385 1.3690 0.9320 0.1528  0.1461  0.1469  124 ARG B CZ  
5057 N NH1 . ARG B 97  ? 1.2108 1.1472 0.7284 0.1442  0.1504  0.1364  124 ARG B NH1 
5058 N NH2 . ARG B 97  ? 1.2397 1.1748 0.7126 0.1572  0.1480  0.1488  124 ARG B NH2 
5059 N N   . SER B 98  ? 0.8867 0.8442 0.3941 0.1803  0.0665  0.1324  125 SER B N   
5060 C CA  . SER B 98  ? 0.9616 0.9408 0.4657 0.1831  0.0518  0.1201  125 SER B CA  
5061 C C   . SER B 98  ? 0.9664 0.9525 0.4669 0.1941  0.0409  0.1276  125 SER B C   
5062 O O   . SER B 98  ? 0.8709 0.8453 0.3671 0.2003  0.0448  0.1417  125 SER B O   
5063 C CB  . SER B 98  ? 0.8648 0.8547 0.3460 0.1848  0.0520  0.1146  125 SER B CB  
5064 O OG  . SER B 98  ? 1.1689 1.1491 0.6365 0.1882  0.0609  0.1273  125 SER B OG  
5065 N N   . TYR B 99  ? 0.8741 0.8794 0.3860 0.1933  0.0272  0.1158  126 TYR B N   
5066 C CA  . TYR B 99  ? 0.8739 0.8903 0.3873 0.2038  0.0162  0.1214  126 TYR B CA  
5067 C C   . TYR B 99  ? 0.9833 1.0115 0.4783 0.2129  0.0100  0.1263  126 TYR B C   
5068 O O   . TYR B 99  ? 1.0806 1.1195 0.5624 0.2100  0.0074  0.1179  126 TYR B O   
5069 C CB  . TYR B 99  ? 0.8173 0.8535 0.3528 0.1978  0.0039  0.1060  126 TYR B CB  
5070 C CG  . TYR B 99  ? 0.9294 0.9536 0.4930 0.1882  0.0083  0.1018  126 TYR B CG  
5071 C CD1 . TYR B 99  ? 0.9408 0.9593 0.5175 0.1935  0.0078  0.1097  126 TYR B CD1 
5072 C CD2 . TYR B 99  ? 0.7858 0.8038 0.3611 0.1749  0.0132  0.0900  126 TYR B CD2 
5073 C CE1 . TYR B 99  ? 0.7834 0.7907 0.3831 0.1849  0.0117  0.1055  126 TYR B CE1 
5074 C CE2 . TYR B 99  ? 0.7623 0.7697 0.3611 0.1669  0.0165  0.0866  126 TYR B CE2 
5075 C CZ  . TYR B 99  ? 0.7434 0.7456 0.3537 0.1716  0.0157  0.0942  126 TYR B CZ  
5076 O OH  . TYR B 99  ? 0.7732 0.7646 0.4042 0.1639  0.0189  0.0906  126 TYR B OH  
5077 N N   . PRO B 100 ? 0.9846 1.0103 0.4790 0.2240  0.0076  0.1391  127 PRO B N   
5078 C CA  . PRO B 100 ? 0.9045 0.9405 0.3819 0.2332  0.0018  0.1445  127 PRO B CA  
5079 C C   . PRO B 100 ? 0.9896 1.0582 0.4655 0.2346  -0.0150 0.1318  127 PRO B C   
5080 O O   . PRO B 100 ? 0.9927 1.0720 0.4525 0.2405  -0.0208 0.1336  127 PRO B O   
5081 C CB  . PRO B 100 ? 0.9356 0.9606 0.4165 0.2453  0.0029  0.1602  127 PRO B CB  
5082 C CG  . PRO B 100 ? 1.0326 1.0345 0.5286 0.2403  0.0132  0.1641  127 PRO B CG  
5083 C CD  . PRO B 100 ? 0.8206 0.8323 0.3286 0.2291  0.0106  0.1491  127 PRO B CD  
5084 N N   . ASP B 101 ? 0.9785 1.0631 0.4703 0.2289  -0.0231 0.1190  128 ASP B N   
5085 C CA  . ASP B 101 ? 0.9343 1.0509 0.4272 0.2276  -0.0392 0.1051  128 ASP B CA  
5086 C C   . ASP B 101 ? 0.9728 1.0939 0.4641 0.2138  -0.0397 0.0869  128 ASP B C   
5087 O O   . ASP B 101 ? 0.9481 1.0939 0.4432 0.2095  -0.0525 0.0727  128 ASP B O   
5088 C CB  . ASP B 101 ? 0.8854 1.0214 0.3990 0.2329  -0.0498 0.1045  128 ASP B CB  
5089 C CG  . ASP B 101 ? 0.9737 1.1008 0.5054 0.2254  -0.0448 0.1001  128 ASP B CG  
5090 O OD1 . ASP B 101 ? 0.9208 1.0209 0.4535 0.2175  -0.0312 0.1015  128 ASP B OD1 
5091 O OD2 . ASP B 101 ? 0.9332 1.0788 0.4886 0.2230  -0.0531 0.0930  128 ASP B OD2 
5092 N N   . GLU B 102 ? 1.0174 1.1154 0.5038 0.2067  -0.0258 0.0866  129 GLU B N   
5093 C CA  . GLU B 102 ? 0.9941 1.0928 0.4790 0.1949  -0.0245 0.0696  129 GLU B CA  
5094 C C   . GLU B 102 ? 0.9440 1.0473 0.4072 0.1931  -0.0254 0.0625  129 GLU B C   
5095 O O   . GLU B 102 ? 0.9727 1.0678 0.4208 0.1991  -0.0197 0.0736  129 GLU B O   
5096 C CB  . GLU B 102 ? 0.9488 1.0214 0.4464 0.1867  -0.0090 0.0711  129 GLU B CB  
5097 C CG  . GLU B 102 ? 0.8868 0.9436 0.3638 0.1867  0.0045  0.0750  129 GLU B CG  
5098 C CD  . GLU B 102 ? 1.1020 1.1380 0.5972 0.1774  0.0182  0.0747  129 GLU B CD  
5099 O OE1 . GLU B 102 ? 0.9406 0.9691 0.4592 0.1744  0.0192  0.0781  129 GLU B OE1 
5100 O OE2 . GLU B 102 ? 1.0226 1.0510 0.5085 0.1735  0.0279  0.0706  129 GLU B OE2 
5101 N N   . GLU B 103 ? 0.9576 1.0736 0.4187 0.1846  -0.0328 0.0436  130 GLU B N   
5102 C CA  . GLU B 103 ? 0.8827 0.9991 0.3230 0.1810  -0.0319 0.0337  130 GLU B CA  
5103 C C   . GLU B 103 ? 1.0350 1.1295 0.4710 0.1750  -0.0161 0.0299  130 GLU B C   
5104 O O   . GLU B 103 ? 1.1115 1.2006 0.5290 0.1746  -0.0102 0.0273  130 GLU B O   
5105 C CB  . GLU B 103 ? 0.9840 1.1223 0.4235 0.1736  -0.0470 0.0136  130 GLU B CB  
5106 C CG  . GLU B 103 ? 1.1234 1.2892 0.5701 0.1786  -0.0640 0.0151  130 GLU B CG  
5107 C CD  . GLU B 103 ? 1.1456 1.3339 0.5968 0.1682  -0.0785 -0.0063 130 GLU B CD  
5108 O OE1 . GLU B 103 ? 1.2548 1.4340 0.7005 0.1576  -0.0750 -0.0224 130 GLU B OE1 
5109 O OE2 . GLU B 103 ? 1.0031 1.2181 0.4642 0.1706  -0.0931 -0.0073 130 GLU B OE2 
5110 N N   . GLY B 104 ? 0.9649 1.0473 0.4191 0.1705  -0.0090 0.0295  131 GLY B N   
5111 C CA  . GLY B 104 ? 0.8497 0.9125 0.3080 0.1644  0.0057  0.0262  131 GLY B CA  
5112 C C   . GLY B 104 ? 0.9108 0.9615 0.4017 0.1575  0.0108  0.0283  131 GLY B C   
5113 O O   . GLY B 104 ? 0.9815 1.0385 0.4911 0.1565  0.0028  0.0301  131 GLY B O   
5114 N N   . PRO B 105 ? 0.9033 0.9375 0.4014 0.1532  0.0241  0.0281  132 PRO B N   
5115 C CA  . PRO B 105 ? 0.7955 0.8180 0.3228 0.1472  0.0287  0.0308  132 PRO B CA  
5116 C C   . PRO B 105 ? 0.8467 0.8725 0.3943 0.1382  0.0204  0.0166  132 PRO B C   
5117 O O   . PRO B 105 ? 0.8479 0.8676 0.4183 0.1345  0.0208  0.0198  132 PRO B O   
5118 C CB  . PRO B 105 ? 0.7953 0.8040 0.3229 0.1453  0.0440  0.0321  132 PRO B CB  
5119 C CG  . PRO B 105 ? 0.9506 0.9638 0.4536 0.1473  0.0457  0.0226  132 PRO B CG  
5120 C CD  . PRO B 105 ? 0.7740 0.8010 0.2539 0.1544  0.0358  0.0258  132 PRO B CD  
5121 N N   . LYS B 106 ? 0.8198 0.8536 0.3588 0.1341  0.0134  0.0010  133 LYS B N   
5122 C CA  . LYS B 106 ? 0.8944 0.9307 0.4511 0.1245  0.0057  -0.0124 133 LYS B CA  
5123 C C   . LYS B 106 ? 0.8815 0.9385 0.4395 0.1242  -0.0089 -0.0152 133 LYS B C   
5124 O O   . LYS B 106 ? 0.9980 1.0597 0.5701 0.1152  -0.0157 -0.0267 133 LYS B O   
5125 C CB  . LYS B 106 ? 0.8081 0.8369 0.3571 0.1182  0.0081  -0.0293 133 LYS B CB  
5126 C CG  . LYS B 106 ? 0.8964 0.9068 0.4496 0.1184  0.0222  -0.0278 133 LYS B CG  
5127 C CD  . LYS B 106 ? 0.8442 0.8455 0.4239 0.1159  0.0259  -0.0194 133 LYS B CD  
5128 C CE  . LYS B 106 ? 0.9530 0.9413 0.5374 0.1181  0.0393  -0.0143 133 LYS B CE  
5129 N NZ  . LYS B 106 ? 0.9586 0.9394 0.5670 0.1156  0.0419  -0.0061 133 LYS B NZ  
5130 N N   . HIS B 107 ? 0.8521 0.9220 0.3963 0.1340  -0.0136 -0.0047 134 HIS B N   
5131 C CA  . HIS B 107 ? 0.8734 0.9666 0.4211 0.1358  -0.0279 -0.0058 134 HIS B CA  
5132 C C   . HIS B 107 ? 0.8920 0.9856 0.4638 0.1377  -0.0284 0.0048  134 HIS B C   
5133 O O   . HIS B 107 ? 0.8310 0.9123 0.4036 0.1448  -0.0203 0.0198  134 HIS B O   
5134 C CB  . HIS B 107 ? 0.9050 1.0124 0.4259 0.1475  -0.0334 0.0015  134 HIS B CB  
5135 C CG  . HIS B 107 ? 0.9997 1.1336 0.5250 0.1522  -0.0483 0.0030  134 HIS B CG  
5136 N ND1 . HIS B 107 ? 0.9356 1.0794 0.4468 0.1667  -0.0520 0.0182  134 HIS B ND1 
5137 C CD2 . HIS B 107 ? 0.7617 0.9155 0.3047 0.1446  -0.0601 -0.0084 134 HIS B CD2 
5138 C CE1 . HIS B 107 ? 0.8889 1.0592 0.4097 0.1691  -0.0662 0.0159  134 HIS B CE1 
5139 N NE2 . HIS B 107 ? 0.7510 0.9289 0.2920 0.1551  -0.0712 -0.0004 134 HIS B NE2 
5140 N N   . TRP B 108 ? 0.7808 0.8882 0.3719 0.1308  -0.0372 -0.0035 135 TRP B N   
5141 C CA  . TRP B 108 ? 0.7969 0.9071 0.4107 0.1327  -0.0380 0.0049  135 TRP B CA  
5142 C C   . TRP B 108 ? 0.9035 1.0387 0.5138 0.1436  -0.0487 0.0122  135 TRP B C   
5143 O O   . TRP B 108 ? 0.8087 0.9688 0.4273 0.1401  -0.0603 0.0033  135 TRP B O   
5144 C CB  . TRP B 108 ? 0.7165 0.8270 0.3538 0.1195  -0.0396 -0.0071 135 TRP B CB  
5145 C CG  . TRP B 108 ? 0.7010 0.7847 0.3459 0.1127  -0.0282 -0.0085 135 TRP B CG  
5146 C CD1 . TRP B 108 ? 0.7180 0.7879 0.3566 0.1049  -0.0236 -0.0194 135 TRP B CD1 
5147 C CD2 . TRP B 108 ? 0.6878 0.7555 0.3472 0.1139  -0.0202 0.0012  135 TRP B CD2 
5148 N NE1 . TRP B 108 ? 0.8352 0.8834 0.4846 0.1020  -0.0138 -0.0163 135 TRP B NE1 
5149 C CE2 . TRP B 108 ? 0.7766 0.8235 0.4386 0.1068  -0.0120 -0.0041 135 TRP B CE2 
5150 C CE3 . TRP B 108 ? 0.6789 0.7475 0.3487 0.1209  -0.0195 0.0134  135 TRP B CE3 
5151 C CZ2 . TRP B 108 ? 0.7639 0.7932 0.4386 0.1058  -0.0041 0.0023  135 TRP B CZ2 
5152 C CZ3 . TRP B 108 ? 0.7700 0.8189 0.4513 0.1192  -0.0110 0.0189  135 TRP B CZ3 
5153 C CH2 . TRP B 108 ? 0.7693 0.7998 0.4530 0.1114  -0.0040 0.0133  135 TRP B CH2 
5154 N N   . SER B 109 ? 0.8095 0.9383 0.4077 0.1571  -0.0446 0.0288  136 SER B N   
5155 C CA  . SER B 109 ? 0.7212 0.8705 0.3154 0.1705  -0.0537 0.0386  136 SER B CA  
5156 C C   . SER B 109 ? 0.8927 1.0454 0.5125 0.1730  -0.0540 0.0443  136 SER B C   
5157 O O   . SER B 109 ? 0.7688 0.9040 0.4055 0.1655  -0.0458 0.0432  136 SER B O   
5158 C CB  . SER B 109 ? 0.8829 1.0203 0.4517 0.1846  -0.0481 0.0550  136 SER B CB  
5159 O OG  . SER B 109 ? 0.8928 1.0034 0.4676 0.1870  -0.0352 0.0675  136 SER B OG  
5160 N N   . ASP B 110 ? 0.7020 0.8785 0.3239 0.1846  -0.0637 0.0504  137 ASP B N   
5161 C CA  . ASP B 110 ? 0.9384 1.1203 0.5839 0.1889  -0.0638 0.0559  137 ASP B CA  
5162 C C   . ASP B 110 ? 0.8672 1.0180 0.5108 0.1964  -0.0510 0.0710  137 ASP B C   
5163 O O   . ASP B 110 ? 0.7397 0.8821 0.4031 0.1936  -0.0460 0.0717  137 ASP B O   
5164 C CB  . ASP B 110 ? 0.7448 0.9609 0.3927 0.2019  -0.0770 0.0597  137 ASP B CB  
5165 C CG  . ASP B 110 ? 1.0724 1.3230 0.7319 0.1914  -0.0901 0.0428  137 ASP B CG  
5166 O OD1 . ASP B 110 ? 0.9761 1.2203 0.6405 0.1739  -0.0881 0.0282  137 ASP B OD1 
5167 O OD2 . ASP B 110 ? 1.0038 1.2877 0.6677 0.2005  -0.1025 0.0439  137 ASP B OD2 
5168 N N   . SER B 111 ? 0.8023 0.9354 0.4219 0.2049  -0.0451 0.0827  138 SER B N   
5169 C CA  . SER B 111 ? 0.8418 0.9430 0.4593 0.2092  -0.0321 0.0958  138 SER B CA  
5170 C C   . SER B 111 ? 0.9026 0.9812 0.5304 0.1938  -0.0220 0.0886  138 SER B C   
5171 O O   . SER B 111 ? 0.9384 0.9970 0.5769 0.1929  -0.0139 0.0938  138 SER B O   
5172 C CB  . SER B 111 ? 0.7154 0.8028 0.3043 0.2205  -0.0274 0.1101  138 SER B CB  
5173 O OG  . SER B 111 ? 1.0243 1.1306 0.6026 0.2372  -0.0367 0.1191  138 SER B OG  
5174 N N   . ARG B 112 ? 0.8130 0.8944 0.4374 0.1822  -0.0226 0.0762  139 ARG B N   
5175 C CA  . ARG B 112 ? 0.7888 0.8520 0.4245 0.1687  -0.0144 0.0685  139 ARG B CA  
5176 C C   . ARG B 112 ? 0.7466 0.8161 0.4075 0.1607  -0.0174 0.0598  139 ARG B C   
5177 O O   . ARG B 112 ? 0.7134 0.7646 0.3862 0.1554  -0.0100 0.0606  139 ARG B O   
5178 C CB  . ARG B 112 ? 0.7946 0.8589 0.4188 0.1604  -0.0141 0.0576  139 ARG B CB  
5179 C CG  . ARG B 112 ? 0.6330 0.6786 0.2669 0.1485  -0.0054 0.0505  139 ARG B CG  
5180 C CD  . ARG B 112 ? 0.7661 0.8146 0.3889 0.1419  -0.0059 0.0384  139 ARG B CD  
5181 N NE  . ARG B 112 ? 0.6636 0.6935 0.2925 0.1338  0.0036  0.0340  139 ARG B NE  
5182 C CZ  . ARG B 112 ? 0.7605 0.7880 0.3823 0.1282  0.0055  0.0232  139 ARG B CZ  
5183 N NH1 . ARG B 112 ? 0.8209 0.8618 0.4277 0.1283  -0.0011 0.0145  139 ARG B NH1 
5184 N NH2 . ARG B 112 ? 0.7473 0.7587 0.3768 0.1227  0.0141  0.0205  139 ARG B NH2 
5185 N N   . TYR B 113 ? 0.8190 0.9150 0.4878 0.1593  -0.0281 0.0514  140 TYR B N   
5186 C CA  . TYR B 113 ? 0.7198 0.8241 0.4127 0.1523  -0.0303 0.0443  140 TYR B CA  
5187 C C   . TYR B 113 ? 0.7461 0.8415 0.4491 0.1607  -0.0256 0.0555  140 TYR B C   
5188 O O   . TYR B 113 ? 0.7907 0.8736 0.5080 0.1541  -0.0200 0.0532  140 TYR B O   
5189 C CB  . TYR B 113 ? 0.7400 0.8781 0.4400 0.1508  -0.0428 0.0353  140 TYR B CB  
5190 C CG  . TYR B 113 ? 0.7721 0.9166 0.4720 0.1362  -0.0467 0.0189  140 TYR B CG  
5191 C CD1 . TYR B 113 ? 0.6801 0.8066 0.3893 0.1228  -0.0401 0.0105  140 TYR B CD1 
5192 C CD2 . TYR B 113 ? 0.7590 0.9263 0.4481 0.1360  -0.0571 0.0115  140 TYR B CD2 
5193 C CE1 . TYR B 113 ? 0.6336 0.7623 0.3415 0.1100  -0.0429 -0.0044 140 TYR B CE1 
5194 C CE2 . TYR B 113 ? 0.7192 0.8897 0.4070 0.1221  -0.0604 -0.0046 140 TYR B CE2 
5195 C CZ  . TYR B 113 ? 0.7996 0.9495 0.4968 0.1093  -0.0527 -0.0123 140 TYR B CZ  
5196 O OH  . TYR B 113 ? 0.8501 0.9996 0.5445 0.0960  -0.0552 -0.0281 140 TYR B OH  
5197 N N   . GLU B 114 ? 0.6693 0.7697 0.3635 0.1760  -0.0276 0.0676  141 GLU B N   
5198 C CA  . GLU B 114 ? 0.7316 0.8221 0.4335 0.1856  -0.0230 0.0780  141 GLU B CA  
5199 C C   . GLU B 114 ? 0.7676 0.8230 0.4667 0.1817  -0.0109 0.0831  141 GLU B C   
5200 O O   . GLU B 114 ? 0.9126 0.9569 0.6247 0.1795  -0.0060 0.0831  141 GLU B O   
5201 C CB  . GLU B 114 ? 0.7747 0.8739 0.4642 0.2041  -0.0270 0.0909  141 GLU B CB  
5202 C CG  . GLU B 114 ? 0.9293 1.0104 0.6217 0.2157  -0.0201 0.1031  141 GLU B CG  
5203 C CD  . GLU B 114 ? 0.8806 0.9673 0.5589 0.2356  -0.0235 0.1170  141 GLU B CD  
5204 O OE1 . GLU B 114 ? 0.9486 1.0551 0.6145 0.2404  -0.0320 0.1174  141 GLU B OE1 
5205 O OE2 . GLU B 114 ? 1.1205 1.1907 0.7989 0.2469  -0.0178 0.1275  141 GLU B OE2 
5206 N N   . HIS B 115 ? 0.7198 0.7586 0.4018 0.1805  -0.0057 0.0873  142 HIS B N   
5207 C CA  . HIS B 115 ? 0.6648 0.6731 0.3452 0.1762  0.0053  0.0922  142 HIS B CA  
5208 C C   . HIS B 115 ? 0.7038 0.7053 0.3993 0.1618  0.0080  0.0812  142 HIS B C   
5209 O O   . HIS B 115 ? 0.7081 0.6914 0.4113 0.1590  0.0141  0.0831  142 HIS B O   
5210 C CB  . HIS B 115 ? 0.6273 0.6234 0.2879 0.1768  0.0106  0.0982  142 HIS B CB  
5211 C CG  . HIS B 115 ? 0.7284 0.6960 0.3884 0.1719  0.0219  0.1038  142 HIS B CG  
5212 N ND1 . HIS B 115 ? 0.7589 0.7073 0.4194 0.1775  0.0276  0.1137  142 HIS B ND1 
5213 C CD2 . HIS B 115 ? 0.6775 0.6337 0.3374 0.1616  0.0285  0.1001  142 HIS B CD2 
5214 C CE1 . HIS B 115 ? 0.8046 0.7312 0.4653 0.1695  0.0367  0.1155  142 HIS B CE1 
5215 N NE2 . HIS B 115 ? 0.7863 0.7188 0.4477 0.1602  0.0372  0.1077  142 HIS B NE2 
5216 N N   . VAL B 116 ? 0.6707 0.6855 0.3694 0.1528  0.0035  0.0694  143 VAL B N   
5217 C CA  . VAL B 116 ? 0.7063 0.7133 0.4174 0.1402  0.0061  0.0597  143 VAL B CA  
5218 C C   . VAL B 116 ? 0.7492 0.7605 0.4772 0.1386  0.0046  0.0569  143 VAL B C   
5219 O O   . VAL B 116 ? 0.7661 0.7621 0.5023 0.1326  0.0096  0.0552  143 VAL B O   
5220 C CB  . VAL B 116 ? 0.6700 0.6876 0.3784 0.1318  0.0022  0.0479  143 VAL B CB  
5221 C CG1 . VAL B 116 ? 0.6370 0.6479 0.3587 0.1202  0.0038  0.0380  143 VAL B CG1 
5222 C CG2 . VAL B 116 ? 0.6367 0.6455 0.3288 0.1325  0.0066  0.0502  143 VAL B CG2 
5223 N N   . MET B 117 ? 0.6916 0.7253 0.4251 0.1444  -0.0021 0.0565  144 MET B N   
5224 C CA  . MET B 117 ? 0.6368 0.6770 0.3869 0.1441  -0.0023 0.0547  144 MET B CA  
5225 C C   . MET B 117 ? 0.6741 0.6936 0.4240 0.1512  0.0048  0.0641  144 MET B C   
5226 O O   . MET B 117 ? 0.6945 0.7029 0.4535 0.1461  0.0091  0.0614  144 MET B O   
5227 C CB  . MET B 117 ? 0.5807 0.6524 0.3378 0.1505  -0.0108 0.0534  144 MET B CB  
5228 C CG  . MET B 117 ? 0.6235 0.7163 0.3893 0.1388  -0.0173 0.0403  144 MET B CG  
5229 S SD  . MET B 117 ? 0.7785 0.9133 0.5567 0.1446  -0.0281 0.0377  144 MET B SD  
5230 C CE  . MET B 117 ? 0.7642 0.9101 0.5212 0.1537  -0.0361 0.0415  144 MET B CE  
5231 N N   . LYS B 118 ? 0.6213 0.6335 0.3591 0.1630  0.0063  0.0750  145 LYS B N   
5232 C CA  . LYS B 118 ? 0.6509 0.6396 0.3863 0.1693  0.0135  0.0836  145 LYS B CA  
5233 C C   . LYS B 118 ? 0.7696 0.7325 0.5037 0.1586  0.0205  0.0816  145 LYS B C   
5234 O O   . LYS B 118 ? 0.7606 0.7068 0.4990 0.1578  0.0255  0.0824  145 LYS B O   
5235 C CB  . LYS B 118 ? 0.5999 0.5823 0.3200 0.1829  0.0145  0.0962  145 LYS B CB  
5236 C CG  . LYS B 118 ? 0.5994 0.6062 0.3208 0.1970  0.0076  0.1004  145 LYS B CG  
5237 C CD  . LYS B 118 ? 0.7328 0.7278 0.4365 0.2118  0.0097  0.1147  145 LYS B CD  
5238 C CE  . LYS B 118 ? 0.6829 0.7017 0.3882 0.2285  0.0026  0.1201  145 LYS B CE  
5239 N NZ  . LYS B 118 ? 0.9526 0.9573 0.6379 0.2440  0.0048  0.1352  145 LYS B NZ  
5240 N N   . LEU B 119 ? 0.6742 0.6344 0.4024 0.1508  0.0209  0.0786  146 LEU B N   
5241 C CA  . LEU B 119 ? 0.7082 0.6483 0.4373 0.1411  0.0267  0.0763  146 LEU B CA  
5242 C C   . LEU B 119 ? 0.6638 0.6038 0.4059 0.1325  0.0261  0.0673  146 LEU B C   
5243 O O   . LEU B 119 ? 0.7332 0.6559 0.4783 0.1293  0.0303  0.0677  146 LEU B O   
5244 C CB  . LEU B 119 ? 0.7226 0.6639 0.4442 0.1359  0.0273  0.0742  146 LEU B CB  
5245 C CG  . LEU B 119 ? 0.7573 0.6901 0.4643 0.1418  0.0316  0.0844  146 LEU B CG  
5246 C CD1 . LEU B 119 ? 0.8060 0.7423 0.5064 0.1365  0.0331  0.0811  146 LEU B CD1 
5247 C CD2 . LEU B 119 ? 0.6755 0.5839 0.3819 0.1414  0.0392  0.0917  146 LEU B CD2 
5248 N N   . ARG B 120 ? 0.6590 0.6173 0.4079 0.1284  0.0209  0.0592  147 ARG B N   
5249 C CA  . ARG B 120 ? 0.7203 0.6777 0.4801 0.1204  0.0211  0.0516  147 ARG B CA  
5250 C C   . ARG B 120 ? 0.6864 0.6413 0.4524 0.1252  0.0232  0.0543  147 ARG B C   
5251 O O   . ARG B 120 ? 0.6951 0.6382 0.4653 0.1202  0.0263  0.0516  147 ARG B O   
5252 C CB  . ARG B 120 ? 0.6725 0.6492 0.4377 0.1145  0.0158  0.0428  147 ARG B CB  
5253 C CG  . ARG B 120 ? 0.6211 0.5971 0.3795 0.1090  0.0146  0.0380  147 ARG B CG  
5254 C CD  . ARG B 120 ? 0.7249 0.7083 0.4895 0.0994  0.0119  0.0274  147 ARG B CD  
5255 N NE  . ARG B 120 ? 0.7573 0.7388 0.5139 0.0954  0.0112  0.0222  147 ARG B NE  
5256 C CZ  . ARG B 120 ? 0.7127 0.7095 0.4639 0.0954  0.0063  0.0175  147 ARG B CZ  
5257 N NH1 . ARG B 120 ? 0.8061 0.8236 0.5605 0.0986  0.0006  0.0174  147 ARG B NH1 
5258 N NH2 . ARG B 120 ? 0.5237 0.5157 0.2659 0.0925  0.0070  0.0126  147 ARG B NH2 
5259 N N   . GLN B 121 ? 0.6812 0.6473 0.4471 0.1359  0.0215  0.0597  148 GLN B N   
5260 C CA  . GLN B 121 ? 0.6163 0.5785 0.3871 0.1427  0.0248  0.0629  148 GLN B CA  
5261 C C   . GLN B 121 ? 0.7207 0.6537 0.4834 0.1441  0.0311  0.0679  148 GLN B C   
5262 O O   . GLN B 121 ? 0.6784 0.6002 0.4441 0.1431  0.0349  0.0662  148 GLN B O   
5263 C CB  . GLN B 121 ? 0.6207 0.6012 0.3926 0.1561  0.0216  0.0685  148 GLN B CB  
5264 C CG  . GLN B 121 ? 0.6795 0.6594 0.4580 0.1649  0.0253  0.0711  148 GLN B CG  
5265 C CD  . GLN B 121 ? 0.6387 0.6326 0.4317 0.1578  0.0257  0.0629  148 GLN B CD  
5266 O OE1 . GLN B 121 ? 0.7043 0.7149 0.5043 0.1482  0.0215  0.0559  148 GLN B OE1 
5267 N NE2 . GLN B 121 ? 0.5575 0.5429 0.3539 0.1621  0.0315  0.0637  148 GLN B NE2 
5268 N N   . ALA B 122 ? 0.7076 0.6283 0.4597 0.1456  0.0326  0.0737  149 ALA B N   
5269 C CA  . ALA B 122 ? 0.7063 0.5995 0.4517 0.1447  0.0386  0.0778  149 ALA B CA  
5270 C C   . ALA B 122 ? 0.6312 0.5135 0.3805 0.1326  0.0399  0.0709  149 ALA B C   
5271 O O   . ALA B 122 ? 0.7478 0.6124 0.4960 0.1312  0.0435  0.0704  149 ALA B O   
5272 C CB  . ALA B 122 ? 0.5776 0.4618 0.3120 0.1468  0.0406  0.0854  149 ALA B CB  
5273 N N   . ALA B 123 ? 0.5802 0.4723 0.3332 0.1244  0.0369  0.0652  150 ALA B N   
5274 C CA  . ALA B 123 ? 0.7355 0.6192 0.4923 0.1146  0.0373  0.0591  150 ALA B CA  
5275 C C   . ALA B 123 ? 0.7825 0.6676 0.5447 0.1136  0.0373  0.0545  150 ALA B C   
5276 O O   . ALA B 123 ? 0.6806 0.5518 0.4421 0.1092  0.0391  0.0521  150 ALA B O   
5277 C CB  . ALA B 123 ? 0.5416 0.4351 0.3003 0.1081  0.0345  0.0544  150 ALA B CB  
5278 N N   . LEU B 124 ? 0.7370 0.6400 0.5047 0.1174  0.0353  0.0531  151 LEU B N   
5279 C CA  . LEU B 124 ? 0.6890 0.5951 0.4625 0.1166  0.0368  0.0494  151 LEU B CA  
5280 C C   . LEU B 124 ? 0.6092 0.5006 0.3787 0.1234  0.0415  0.0529  151 LEU B C   
5281 O O   . LEU B 124 ? 0.5869 0.4674 0.3553 0.1202  0.0443  0.0498  151 LEU B O   
5282 C CB  . LEU B 124 ? 0.6691 0.6008 0.4516 0.1189  0.0340  0.0474  151 LEU B CB  
5283 C CG  . LEU B 124 ? 0.6916 0.6312 0.4823 0.1188  0.0368  0.0444  151 LEU B CG  
5284 C CD1 . LEU B 124 ? 0.5707 0.4986 0.3606 0.1087  0.0390  0.0393  151 LEU B CD1 
5285 C CD2 . LEU B 124 ? 0.6755 0.6442 0.4776 0.1195  0.0333  0.0420  151 LEU B CD2 
5286 N N   . LYS B 125 ? 0.6906 0.5799 0.4562 0.1333  0.0426  0.0594  152 LYS B N   
5287 C CA  . LYS B 125 ? 0.7767 0.6475 0.5365 0.1402  0.0477  0.0625  152 LYS B CA  
5288 C C   . LYS B 125 ? 0.6763 0.5214 0.4282 0.1328  0.0499  0.0612  152 LYS B C   
5289 O O   . LYS B 125 ? 0.7266 0.5566 0.4746 0.1326  0.0534  0.0586  152 LYS B O   
5290 C CB  . LYS B 125 ? 0.6694 0.5399 0.4248 0.1528  0.0487  0.0708  152 LYS B CB  
5291 C CG  . LYS B 125 ? 0.6464 0.4913 0.3931 0.1600  0.0548  0.0744  152 LYS B CG  
5292 C CD  . LYS B 125 ? 0.7449 0.5871 0.4857 0.1738  0.0561  0.0838  152 LYS B CD  
5293 C CE  . LYS B 125 ? 0.6179 0.4277 0.3475 0.1790  0.0630  0.0873  152 LYS B CE  
5294 N NZ  . LYS B 125 ? 1.0698 0.8731 0.8008 0.1826  0.0672  0.0822  152 LYS B NZ  
5295 N N   . SER B 126 ? 0.6771 0.5183 0.4268 0.1265  0.0480  0.0623  153 SER B N   
5296 C CA  . SER B 126 ? 0.7008 0.5219 0.4458 0.1185  0.0493  0.0606  153 SER B CA  
5297 C C   . SER B 126 ? 0.7503 0.5700 0.4974 0.1110  0.0478  0.0534  153 SER B C   
5298 O O   . SER B 126 ? 0.7317 0.5341 0.4736 0.1075  0.0492  0.0509  153 SER B O   
5299 C CB  . SER B 126 ? 0.6579 0.4808 0.4030 0.1132  0.0480  0.0630  153 SER B CB  
5300 O OG  . SER B 126 ? 1.0757 0.8805 0.8178 0.1063  0.0499  0.0626  153 SER B OG  
5301 N N   . ALA B 127 ? 0.6558 0.4924 0.4093 0.1082  0.0448  0.0499  154 ALA B N   
5302 C CA  . ALA B 127 ? 0.6520 0.4862 0.4058 0.1019  0.0438  0.0443  154 ALA B CA  
5303 C C   . ALA B 127 ? 0.7060 0.5334 0.4560 0.1057  0.0475  0.0427  154 ALA B C   
5304 O O   . ALA B 127 ? 0.7623 0.5765 0.5061 0.1018  0.0479  0.0393  154 ALA B O   
5305 C CB  . ALA B 127 ? 0.5456 0.3967 0.3060 0.0982  0.0410  0.0415  154 ALA B CB  
5306 N N   . ARG B 128 ? 0.7881 0.6253 0.5414 0.1138  0.0502  0.0449  155 ARG B N   
5307 C CA  . ARG B 128 ? 0.6480 0.4798 0.3982 0.1190  0.0552  0.0434  155 ARG B CA  
5308 C C   . ARG B 128 ? 0.8155 0.6223 0.5545 0.1216  0.0582  0.0438  155 ARG B C   
5309 O O   . ARG B 128 ? 0.7591 0.5534 0.4906 0.1210  0.0612  0.0400  155 ARG B O   
5310 C CB  . ARG B 128 ? 0.7009 0.5514 0.4593 0.1286  0.0574  0.0462  155 ARG B CB  
5311 C CG  . ARG B 128 ? 0.6035 0.4800 0.3738 0.1250  0.0547  0.0444  155 ARG B CG  
5312 C CD  . ARG B 128 ? 0.6089 0.5056 0.3887 0.1344  0.0572  0.0461  155 ARG B CD  
5313 N NE  . ARG B 128 ? 0.6054 0.5282 0.3979 0.1292  0.0547  0.0433  155 ARG B NE  
5314 C CZ  . ARG B 128 ? 0.7018 0.6479 0.5038 0.1331  0.0506  0.0448  155 ARG B CZ  
5315 N NH1 . ARG B 128 ? 0.5808 0.5278 0.3802 0.1435  0.0486  0.0504  155 ARG B NH1 
5316 N NH2 . ARG B 128 ? 0.6098 0.5785 0.4234 0.1261  0.0484  0.0407  155 ARG B NH2 
5317 N N   . ASP B 129 ? 0.7341 0.5323 0.4707 0.1240  0.0579  0.0482  156 ASP B N   
5318 C CA  . ASP B 129 ? 0.8092 0.5815 0.5352 0.1259  0.0615  0.0485  156 ASP B CA  
5319 C C   . ASP B 129 ? 0.7412 0.4981 0.4610 0.1147  0.0590  0.0431  156 ASP B C   
5320 O O   . ASP B 129 ? 0.9326 0.6684 0.6424 0.1144  0.0618  0.0400  156 ASP B O   
5321 C CB  . ASP B 129 ? 0.9098 0.6760 0.6344 0.1305  0.0625  0.0556  156 ASP B CB  
5322 C CG  . ASP B 129 ? 1.0455 0.8235 0.7732 0.1443  0.0649  0.0613  156 ASP B CG  
5323 O OD1 . ASP B 129 ? 0.9670 0.7568 0.6990 0.1502  0.0665  0.0591  156 ASP B OD1 
5324 O OD2 . ASP B 129 ? 0.9014 0.6778 0.6274 0.1495  0.0651  0.0683  156 ASP B OD2 
5325 N N   . MET B 130 ? 0.7548 0.5219 0.4801 0.1060  0.0538  0.0417  157 MET B N   
5326 C CA  . MET B 130 ? 0.8574 0.6145 0.5788 0.0964  0.0502  0.0368  157 MET B CA  
5327 C C   . MET B 130 ? 0.8283 0.5886 0.5464 0.0940  0.0485  0.0318  157 MET B C   
5328 O O   . MET B 130 ? 0.7734 0.5278 0.4875 0.0871  0.0444  0.0279  157 MET B O   
5329 C CB  . MET B 130 ? 0.7543 0.5204 0.4835 0.0895  0.0458  0.0384  157 MET B CB  
5330 C CG  . MET B 130 ? 0.8050 0.5910 0.5421 0.0883  0.0424  0.0381  157 MET B CG  
5331 S SD  . MET B 130 ? 0.9410 0.7368 0.6865 0.0827  0.0391  0.0401  157 MET B SD  
5332 C CE  . MET B 130 ? 0.8266 0.6068 0.5695 0.0748  0.0376  0.0375  157 MET B CE  
5333 N N   . TRP B 131 ? 0.6782 0.4487 0.3979 0.0997  0.0517  0.0323  158 TRP B N   
5334 C CA  . TRP B 131 ? 0.8095 0.5811 0.5243 0.0981  0.0524  0.0285  158 TRP B CA  
5335 C C   . TRP B 131 ? 0.8172 0.5977 0.5357 0.0911  0.0470  0.0277  158 TRP B C   
5336 O O   . TRP B 131 ? 0.7787 0.5529 0.4893 0.0876  0.0453  0.0248  158 TRP B O   
5337 C CB  . TRP B 131 ? 0.6998 0.4509 0.3998 0.0976  0.0539  0.0239  158 TRP B CB  
5338 C CG  . TRP B 131 ? 0.7690 0.5151 0.4633 0.1060  0.0615  0.0232  158 TRP B CG  
5339 C CD1 . TRP B 131 ? 0.7353 0.4966 0.4381 0.1134  0.0666  0.0262  158 TRP B CD1 
5340 C CD2 . TRP B 131 ? 0.7954 0.5207 0.4746 0.1084  0.0653  0.0186  158 TRP B CD2 
5341 N NE1 . TRP B 131 ? 0.7080 0.4605 0.4031 0.1212  0.0738  0.0244  158 TRP B NE1 
5342 C CE2 . TRP B 131 ? 0.8283 0.5570 0.5075 0.1184  0.0735  0.0195  158 TRP B CE2 
5343 C CE3 . TRP B 131 ? 0.7071 0.4120 0.3726 0.1028  0.0623  0.0131  158 TRP B CE3 
5344 C CZ2 . TRP B 131 ? 0.8067 0.5172 0.4717 0.1240  0.0797  0.0152  158 TRP B CZ2 
5345 C CZ3 . TRP B 131 ? 0.8923 0.5783 0.5426 0.1072  0.0677  0.0082  158 TRP B CZ3 
5346 C CH2 . TRP B 131 ? 0.8519 0.5399 0.5015 0.1181  0.0768  0.0093  158 TRP B CH2 
5347 N N   . ALA B 132 ? 0.7466 0.5408 0.4759 0.0900  0.0446  0.0304  159 ALA B N   
5348 C CA  . ALA B 132 ? 0.8116 0.6134 0.5445 0.0848  0.0406  0.0296  159 ALA B CA  
5349 C C   . ALA B 132 ? 0.7831 0.5915 0.5159 0.0848  0.0436  0.0289  159 ALA B C   
5350 O O   . ALA B 132 ? 0.7058 0.5204 0.4409 0.0888  0.0486  0.0294  159 ALA B O   
5351 C CB  . ALA B 132 ? 0.5351 0.3486 0.2780 0.0840  0.0382  0.0319  159 ALA B CB  
5352 N N   . ASP B 133 ? 0.7220 0.5288 0.4523 0.0804  0.0411  0.0278  160 ASP B N   
5353 C CA  . ASP B 133 ? 0.7654 0.5769 0.4957 0.0787  0.0445  0.0276  160 ASP B CA  
5354 C C   . ASP B 133 ? 0.7162 0.5427 0.4585 0.0770  0.0445  0.0280  160 ASP B C   
5355 O O   . ASP B 133 ? 0.6917 0.5281 0.4392 0.0763  0.0487  0.0276  160 ASP B O   
5356 C CB  . ASP B 133 ? 0.7644 0.5653 0.4850 0.0755  0.0422  0.0272  160 ASP B CB  
5357 C CG  . ASP B 133 ? 0.7125 0.4995 0.4186 0.0768  0.0423  0.0261  160 ASP B CG  
5358 O OD1 . ASP B 133 ? 0.8591 0.6441 0.5606 0.0794  0.0482  0.0255  160 ASP B OD1 
5359 O OD2 . ASP B 133 ? 0.9004 0.6795 0.5997 0.0757  0.0365  0.0255  160 ASP B OD2 
5360 N N   . TYR B 134 ? 0.6608 0.4902 0.4077 0.0759  0.0398  0.0280  161 TYR B N   
5361 C CA  . TYR B 134 ? 0.6980 0.5397 0.4536 0.0739  0.0390  0.0272  161 TYR B CA  
5362 C C   . TYR B 134 ? 0.6449 0.4931 0.4052 0.0766  0.0363  0.0284  161 TYR B C   
5363 O O   . TYR B 134 ? 0.6707 0.5118 0.4284 0.0780  0.0346  0.0298  161 TYR B O   
5364 C CB  . TYR B 134 ? 0.5911 0.4272 0.3446 0.0698  0.0372  0.0257  161 TYR B CB  
5365 C CG  . TYR B 134 ? 0.7427 0.5705 0.4899 0.0666  0.0406  0.0255  161 TYR B CG  
5366 C CD1 . TYR B 134 ? 0.6576 0.4715 0.3937 0.0677  0.0401  0.0270  161 TYR B CD1 
5367 C CD2 . TYR B 134 ? 0.7495 0.5831 0.5010 0.0621  0.0443  0.0240  161 TYR B CD2 
5368 C CE1 . TYR B 134 ? 0.7265 0.5315 0.4543 0.0653  0.0440  0.0278  161 TYR B CE1 
5369 C CE2 . TYR B 134 ? 0.7837 0.6083 0.5288 0.0584  0.0488  0.0246  161 TYR B CE2 
5370 C CZ  . TYR B 134 ? 0.7460 0.5557 0.4784 0.0605  0.0489  0.0271  161 TYR B CZ  
5371 O OH  . TYR B 134 ? 0.7634 0.5627 0.4870 0.0573  0.0541  0.0287  161 TYR B OH  
5372 N N   . ILE B 135 ? 0.5836 0.4457 0.3507 0.0767  0.0361  0.0277  162 ILE B N   
5373 C CA  . ILE B 135 ? 0.5680 0.4365 0.3376 0.0788  0.0337  0.0289  162 ILE B CA  
5374 C C   . ILE B 135 ? 0.5630 0.4376 0.3350 0.0750  0.0320  0.0253  162 ILE B C   
5375 O O   . ILE B 135 ? 0.6557 0.5385 0.4311 0.0720  0.0326  0.0223  162 ILE B O   
5376 C CB  . ILE B 135 ? 0.6776 0.5566 0.4498 0.0844  0.0345  0.0318  162 ILE B CB  
5377 C CG1 . ILE B 135 ? 0.5378 0.4232 0.3102 0.0864  0.0324  0.0335  162 ILE B CG1 
5378 C CG2 . ILE B 135 ? 0.5208 0.4142 0.2990 0.0843  0.0356  0.0299  162 ILE B CG2 
5379 C CD1 . ILE B 135 ? 0.6543 0.5452 0.4260 0.0936  0.0332  0.0385  162 ILE B CD1 
5380 N N   . LEU B 136 ? 0.6781 0.5485 0.4488 0.0747  0.0303  0.0250  163 LEU B N   
5381 C CA  . LEU B 136 ? 0.6288 0.5021 0.4002 0.0722  0.0293  0.0210  163 LEU B CA  
5382 C C   . LEU B 136 ? 0.6846 0.5681 0.4564 0.0749  0.0285  0.0216  163 LEU B C   
5383 O O   . LEU B 136 ? 0.6203 0.5020 0.3914 0.0775  0.0289  0.0249  163 LEU B O   
5384 C CB  . LEU B 136 ? 0.6078 0.4697 0.3770 0.0715  0.0287  0.0203  163 LEU B CB  
5385 C CG  . LEU B 136 ? 0.5654 0.4275 0.3344 0.0707  0.0285  0.0162  163 LEU B CG  
5386 C CD1 . LEU B 136 ? 0.6195 0.4772 0.3867 0.0661  0.0296  0.0118  163 LEU B CD1 
5387 C CD2 . LEU B 136 ? 0.5484 0.4033 0.3173 0.0733  0.0277  0.0170  163 LEU B CD2 
5388 N N   . PHE B 137 ? 0.6722 0.5669 0.4447 0.0737  0.0275  0.0182  164 PHE B N   
5389 C CA  . PHE B 137 ? 0.6428 0.5472 0.4128 0.0764  0.0264  0.0181  164 PHE B CA  
5390 C C   . PHE B 137 ? 0.6464 0.5470 0.4136 0.0743  0.0267  0.0129  164 PHE B C   
5391 O O   . PHE B 137 ? 0.6634 0.5593 0.4308 0.0698  0.0266  0.0073  164 PHE B O   
5392 C CB  . PHE B 137 ? 0.7011 0.6217 0.4725 0.0768  0.0240  0.0165  164 PHE B CB  
5393 C CG  . PHE B 137 ? 0.6532 0.5794 0.4263 0.0824  0.0241  0.0227  164 PHE B CG  
5394 C CD1 . PHE B 137 ? 0.5634 0.4927 0.3320 0.0888  0.0241  0.0285  164 PHE B CD1 
5395 C CD2 . PHE B 137 ? 0.6031 0.5305 0.3817 0.0817  0.0250  0.0231  164 PHE B CD2 
5396 C CE1 . PHE B 137 ? 0.5589 0.4904 0.3279 0.0951  0.0247  0.0346  164 PHE B CE1 
5397 C CE2 . PHE B 137 ? 0.6755 0.6070 0.4553 0.0883  0.0258  0.0286  164 PHE B CE2 
5398 C CZ  . PHE B 137 ? 0.6351 0.5678 0.4100 0.0954  0.0254  0.0344  164 PHE B CZ  
5399 N N   . VAL B 138 ? 0.6404 0.5417 0.4049 0.0777  0.0280  0.0149  165 VAL B N   
5400 C CA  . VAL B 138 ? 0.6699 0.5691 0.4312 0.0776  0.0292  0.0100  165 VAL B CA  
5401 C C   . VAL B 138 ? 0.6933 0.6029 0.4487 0.0810  0.0299  0.0109  165 VAL B C   
5402 O O   . VAL B 138 ? 0.8136 0.7253 0.5687 0.0843  0.0318  0.0176  165 VAL B O   
5403 C CB  . VAL B 138 ? 0.6384 0.5280 0.4030 0.0790  0.0313  0.0116  165 VAL B CB  
5404 C CG1 . VAL B 138 ? 0.6168 0.5042 0.3786 0.0804  0.0333  0.0061  165 VAL B CG1 
5405 C CG2 . VAL B 138 ? 0.6684 0.5476 0.4363 0.0768  0.0301  0.0122  165 VAL B CG2 
5406 N N   . ASP B 139 ? 0.7229 0.6378 0.4724 0.0797  0.0286  0.0041  166 ASP B N   
5407 C CA  . ASP B 139 ? 0.7263 0.6500 0.4671 0.0834  0.0295  0.0044  166 ASP B CA  
5408 C C   . ASP B 139 ? 0.7655 0.6839 0.5054 0.0864  0.0349  0.0054  166 ASP B C   
5409 O O   . ASP B 139 ? 0.8033 0.7126 0.5474 0.0855  0.0366  0.0019  166 ASP B O   
5410 C CB  . ASP B 139 ? 0.8546 0.7851 0.5879 0.0807  0.0262  -0.0047 166 ASP B CB  
5411 C CG  . ASP B 139 ? 0.9844 0.9278 0.7194 0.0790  0.0206  -0.0047 166 ASP B CG  
5412 O OD1 . ASP B 139 ? 1.0369 0.9808 0.7798 0.0796  0.0199  0.0013  166 ASP B OD1 
5413 O OD2 . ASP B 139 ? 0.9736 0.9277 0.7020 0.0775  0.0167  -0.0110 166 ASP B OD2 
5414 N N   . ALA B 140 ? 0.8173 0.7421 0.5517 0.0904  0.0380  0.0107  167 ALA B N   
5415 C CA  . ALA B 140 ? 0.8032 0.7261 0.5393 0.0929  0.0443  0.0130  167 ALA B CA  
5416 C C   . ALA B 140 ? 0.7625 0.6832 0.4943 0.0940  0.0469  0.0043  167 ALA B C   
5417 O O   . ALA B 140 ? 0.8730 0.7922 0.6100 0.0964  0.0520  0.0049  167 ALA B O   
5418 C CB  . ALA B 140 ? 0.6595 0.5891 0.3888 0.0962  0.0482  0.0208  167 ALA B CB  
5419 N N   . ASP B 141 ? 0.8113 0.7320 0.5345 0.0924  0.0436  -0.0041 168 ASP B N   
5420 C CA  . ASP B 141 ? 0.7625 0.6773 0.4799 0.0934  0.0463  -0.0137 168 ASP B CA  
5421 C C   . ASP B 141 ? 0.8345 0.7360 0.5575 0.0899  0.0441  -0.0198 168 ASP B C   
5422 O O   . ASP B 141 ? 0.8347 0.7273 0.5527 0.0910  0.0466  -0.0279 168 ASP B O   
5423 C CB  . ASP B 141 ? 0.6166 0.5377 0.3182 0.0932  0.0445  -0.0207 168 ASP B CB  
5424 C CG  . ASP B 141 ? 0.9276 0.8542 0.6279 0.0878  0.0365  -0.0232 168 ASP B CG  
5425 O OD1 . ASP B 141 ? 1.0698 0.9950 0.7812 0.0847  0.0334  -0.0189 168 ASP B OD1 
5426 O OD2 . ASP B 141 ? 0.7928 0.7266 0.4811 0.0867  0.0332  -0.0298 168 ASP B OD2 
5427 N N   . ASN B 142 ? 0.7753 0.6738 0.5071 0.0861  0.0403  -0.0159 169 ASN B N   
5428 C CA  . ASN B 142 ? 0.7927 0.6772 0.5282 0.0827  0.0390  -0.0202 169 ASN B CA  
5429 C C   . ASN B 142 ? 0.7677 0.6442 0.5110 0.0873  0.0420  -0.0163 169 ASN B C   
5430 O O   . ASN B 142 ? 0.7792 0.6608 0.5305 0.0890  0.0420  -0.0084 169 ASN B O   
5431 C CB  . ASN B 142 ? 0.8856 0.7712 0.6261 0.0769  0.0344  -0.0177 169 ASN B CB  
5432 C CG  . ASN B 142 ? 0.8180 0.7137 0.5533 0.0721  0.0305  -0.0227 169 ASN B CG  
5433 O OD1 . ASN B 142 ? 0.7863 0.6877 0.5266 0.0682  0.0271  -0.0207 169 ASN B OD1 
5434 N ND2 . ASN B 142 ? 0.8600 0.7596 0.5853 0.0727  0.0308  -0.0296 169 ASN B ND2 
5435 N N   . LEU B 143 ? 0.7163 0.5799 0.4571 0.0895  0.0444  -0.0221 170 LEU B N   
5436 C CA  . LEU B 143 ? 0.7437 0.6010 0.4916 0.0958  0.0468  -0.0191 170 LEU B CA  
5437 C C   . LEU B 143 ? 0.7157 0.5578 0.4654 0.0933  0.0441  -0.0182 170 LEU B C   
5438 O O   . LEU B 143 ? 0.8027 0.6298 0.5454 0.0908  0.0447  -0.0245 170 LEU B O   
5439 C CB  . LEU B 143 ? 0.6269 0.4794 0.3699 0.1025  0.0521  -0.0253 170 LEU B CB  
5440 C CG  . LEU B 143 ? 0.7881 0.6346 0.5387 0.1108  0.0545  -0.0232 170 LEU B CG  
5441 C CD1 . LEU B 143 ? 0.9647 0.8273 0.7289 0.1132  0.0538  -0.0143 170 LEU B CD1 
5442 C CD2 . LEU B 143 ? 0.8017 0.6437 0.5466 0.1185  0.0608  -0.0301 170 LEU B CD2 
5443 N N   . ILE B 144 ? 0.7126 0.5573 0.4704 0.0937  0.0414  -0.0107 171 ILE B N   
5444 C CA  . ILE B 144 ? 0.7978 0.6286 0.5555 0.0920  0.0391  -0.0086 171 ILE B CA  
5445 C C   . ILE B 144 ? 0.6458 0.4688 0.4062 0.1006  0.0401  -0.0072 171 ILE B C   
5446 O O   . ILE B 144 ? 0.7774 0.6075 0.5458 0.1044  0.0378  -0.0014 171 ILE B O   
5447 C CB  . ILE B 144 ? 0.7700 0.6071 0.5325 0.0881  0.0355  -0.0021 171 ILE B CB  
5448 C CG1 . ILE B 144 ? 0.7833 0.6322 0.5449 0.0828  0.0348  -0.0025 171 ILE B CG1 
5449 C CG2 . ILE B 144 ? 0.6848 0.5069 0.4436 0.0852  0.0340  -0.0007 171 ILE B CG2 
5450 C CD1 . ILE B 144 ? 0.7282 0.5730 0.4835 0.0767  0.0349  -0.0088 171 ILE B CD1 
5451 N N   . LEU B 145 ? 0.7475 0.5559 0.5010 0.1039  0.0433  -0.0129 172 LEU B N   
5452 C CA  . LEU B 145 ? 0.8102 0.6111 0.5660 0.1144  0.0447  -0.0116 172 LEU B CA  
5453 C C   . LEU B 145 ? 0.7495 0.5391 0.5051 0.1162  0.0410  -0.0055 172 LEU B C   
5454 O O   . LEU B 145 ? 0.8599 0.6547 0.6225 0.1245  0.0389  -0.0008 172 LEU B O   
5455 C CB  . LEU B 145 ? 0.9060 0.6900 0.6522 0.1182  0.0499  -0.0196 172 LEU B CB  
5456 C CG  . LEU B 145 ? 1.0310 0.8254 0.7790 0.1254  0.0547  -0.0240 172 LEU B CG  
5457 C CD1 . LEU B 145 ? 0.8900 0.6625 0.6285 0.1323  0.0597  -0.0309 172 LEU B CD1 
5458 C CD2 . LEU B 145 ? 1.0909 0.9059 0.8536 0.1331  0.0540  -0.0174 172 LEU B CD2 
5459 N N   . ASN B 146 ? 0.8074 0.5829 0.5552 0.1084  0.0403  -0.0055 173 ASN B N   
5460 C CA  . ASN B 146 ? 0.8720 0.6350 0.6163 0.1096  0.0376  0.0007  173 ASN B CA  
5461 C C   . ASN B 146 ? 0.8104 0.5900 0.5621 0.1076  0.0325  0.0068  173 ASN B C   
5462 O O   . ASN B 146 ? 0.7339 0.5216 0.4867 0.0992  0.0319  0.0066  173 ASN B O   
5463 C CB  . ASN B 146 ? 0.8948 0.6381 0.6285 0.1007  0.0401  -0.0013 173 ASN B CB  
5464 C CG  . ASN B 146 ? 0.8091 0.5353 0.5356 0.1027  0.0390  0.0055  173 ASN B CG  
5465 O OD1 . ASN B 146 ? 0.9068 0.6393 0.6362 0.1094  0.0346  0.0118  173 ASN B OD1 
5466 N ND2 . ASN B 146 ? 0.9141 0.6186 0.6303 0.0964  0.0431  0.0041  173 ASN B ND2 
5467 N N   . PRO B 147 ? 0.7700 0.5552 0.5269 0.1153  0.0286  0.0119  174 PRO B N   
5468 C CA  . PRO B 147 ? 0.7890 0.5885 0.5520 0.1124  0.0235  0.0164  174 PRO B CA  
5469 C C   . PRO B 147 ? 0.8997 0.6881 0.6536 0.1068  0.0218  0.0195  174 PRO B C   
5470 O O   . PRO B 147 ? 0.8056 0.6035 0.5623 0.1031  0.0185  0.0219  174 PRO B O   
5471 C CB  . PRO B 147 ? 0.7500 0.5583 0.5209 0.1223  0.0192  0.0197  174 PRO B CB  
5472 C CG  . PRO B 147 ? 0.6409 0.4442 0.4126 0.1312  0.0232  0.0167  174 PRO B CG  
5473 C CD  . PRO B 147 ? 0.7533 0.5335 0.5114 0.1274  0.0282  0.0133  174 PRO B CD  
5474 N N   . ASP B 148 ? 0.7857 0.5534 0.5282 0.1058  0.0247  0.0195  175 ASP B N   
5475 C CA  . ASP B 148 ? 0.8794 0.6362 0.6124 0.1002  0.0248  0.0228  175 ASP B CA  
5476 C C   . ASP B 148 ? 0.8675 0.6254 0.6000 0.0894  0.0290  0.0192  175 ASP B C   
5477 O O   . ASP B 148 ? 0.8867 0.6366 0.6125 0.0841  0.0307  0.0213  175 ASP B O   
5478 C CB  . ASP B 148 ? 0.7922 0.5248 0.5124 0.1047  0.0264  0.0262  175 ASP B CB  
5479 C CG  . ASP B 148 ? 0.9910 0.7238 0.7109 0.1168  0.0210  0.0310  175 ASP B CG  
5480 O OD1 . ASP B 148 ? 1.0976 0.8473 0.8241 0.1186  0.0148  0.0331  175 ASP B OD1 
5481 O OD2 . ASP B 148 ? 1.1210 0.8369 0.8340 0.1246  0.0226  0.0326  175 ASP B OD2 
5482 N N   . THR B 149 ? 0.7819 0.5510 0.5213 0.0866  0.0307  0.0138  176 THR B N   
5483 C CA  . THR B 149 ? 0.7951 0.5675 0.5348 0.0771  0.0337  0.0098  176 THR B CA  
5484 C C   . THR B 149 ? 0.7371 0.5187 0.4787 0.0727  0.0325  0.0130  176 THR B C   
5485 O O   . THR B 149 ? 0.7782 0.5563 0.5172 0.0658  0.0355  0.0125  176 THR B O   
5486 C CB  . THR B 149 ? 0.7918 0.5777 0.5375 0.0765  0.0341  0.0043  176 THR B CB  
5487 O OG1 . THR B 149 ? 0.8307 0.6078 0.5740 0.0821  0.0358  0.0009  176 THR B OG1 
5488 C CG2 . THR B 149 ? 0.7422 0.5324 0.4879 0.0673  0.0361  -0.0007 176 THR B CG2 
5489 N N   . LEU B 150 ? 0.7201 0.5134 0.4665 0.0762  0.0288  0.0161  177 LEU B N   
5490 C CA  . LEU B 150 ? 0.6742 0.4738 0.4212 0.0731  0.0282  0.0187  177 LEU B CA  
5491 C C   . LEU B 150 ? 0.8544 0.6404 0.5918 0.0720  0.0293  0.0220  177 LEU B C   
5492 O O   . LEU B 150 ? 0.7706 0.5573 0.5063 0.0672  0.0323  0.0224  177 LEU B O   
5493 C CB  . LEU B 150 ? 0.6071 0.4177 0.3597 0.0766  0.0244  0.0208  177 LEU B CB  
5494 C CG  . LEU B 150 ? 0.6736 0.4883 0.4257 0.0745  0.0238  0.0230  177 LEU B CG  
5495 C CD1 . LEU B 150 ? 0.7188 0.5414 0.4737 0.0706  0.0270  0.0214  177 LEU B CD1 
5496 C CD2 . LEU B 150 ? 0.6073 0.4297 0.3647 0.0767  0.0203  0.0244  177 LEU B CD2 
5497 N N   . SER B 151 ? 0.8368 0.6110 0.5677 0.0772  0.0271  0.0249  178 SER B N   
5498 C CA  . SER B 151 ? 0.7196 0.4794 0.4384 0.0770  0.0283  0.0290  178 SER B CA  
5499 C C   . SER B 151 ? 0.8179 0.5651 0.5312 0.0708  0.0351  0.0282  178 SER B C   
5500 O O   . SER B 151 ? 0.7411 0.4835 0.4481 0.0665  0.0389  0.0303  178 SER B O   
5501 C CB  . SER B 151 ? 0.6993 0.4500 0.4116 0.0854  0.0237  0.0328  178 SER B CB  
5502 O OG  . SER B 151 ? 0.8443 0.6087 0.5631 0.0894  0.0171  0.0331  178 SER B OG  
5503 N N   . LEU B 152 ? 0.7598 0.5015 0.4752 0.0697  0.0373  0.0247  179 LEU B N   
5504 C CA  . LEU B 152 ? 0.7981 0.5265 0.5088 0.0620  0.0439  0.0229  179 LEU B CA  
5505 C C   . LEU B 152 ? 0.8055 0.5487 0.5243 0.0526  0.0470  0.0194  179 LEU B C   
5506 O O   . LEU B 152 ? 0.9177 0.6544 0.6333 0.0452  0.0528  0.0201  179 LEU B O   
5507 C CB  . LEU B 152 ? 0.7577 0.4758 0.4683 0.0629  0.0453  0.0185  179 LEU B CB  
5508 C CG  . LEU B 152 ? 0.8876 0.5913 0.5912 0.0739  0.0428  0.0220  179 LEU B CG  
5509 C CD1 . LEU B 152 ? 0.6679 0.3643 0.3729 0.0760  0.0446  0.0163  179 LEU B CD1 
5510 C CD2 . LEU B 152 ? 0.6448 0.3254 0.3335 0.0756  0.0456  0.0289  179 LEU B CD2 
5511 N N   . LEU B 153 ? 0.7912 0.5550 0.5208 0.0531  0.0437  0.0162  180 LEU B N   
5512 C CA  . LEU B 153 ? 0.7143 0.4946 0.4522 0.0464  0.0456  0.0135  180 LEU B CA  
5513 C C   . LEU B 153 ? 0.8246 0.6077 0.5602 0.0464  0.0475  0.0181  180 LEU B C   
5514 O O   . LEU B 153 ? 0.8331 0.6219 0.5721 0.0400  0.0522  0.0173  180 LEU B O   
5515 C CB  . LEU B 153 ? 0.7324 0.5322 0.4797 0.0488  0.0415  0.0103  180 LEU B CB  
5516 C CG  . LEU B 153 ? 0.7217 0.5218 0.4707 0.0481  0.0404  0.0045  180 LEU B CG  
5517 C CD1 . LEU B 153 ? 0.6329 0.4518 0.3886 0.0517  0.0367  0.0030  180 LEU B CD1 
5518 C CD2 . LEU B 153 ? 0.7567 0.5544 0.5067 0.0382  0.0440  -0.0012 180 LEU B CD2 
5519 N N   . ILE B 154 ? 0.8904 0.6706 0.6209 0.0535  0.0440  0.0222  181 ILE B N   
5520 C CA  . ILE B 154 ? 0.7494 0.5288 0.4744 0.0541  0.0460  0.0258  181 ILE B CA  
5521 C C   . ILE B 154 ? 0.6697 0.4331 0.3839 0.0502  0.0520  0.0287  181 ILE B C   
5522 O O   . ILE B 154 ? 0.8244 0.5901 0.5369 0.0469  0.0574  0.0300  181 ILE B O   
5523 C CB  . ILE B 154 ? 0.7853 0.5631 0.5055 0.0614  0.0401  0.0284  181 ILE B CB  
5524 C CG1 . ILE B 154 ? 0.6976 0.4910 0.4284 0.0637  0.0362  0.0262  181 ILE B CG1 
5525 C CG2 . ILE B 154 ? 0.6254 0.3975 0.3353 0.0622  0.0422  0.0313  181 ILE B CG2 
5526 C CD1 . ILE B 154 ? 0.6990 0.4916 0.4271 0.0686  0.0308  0.0279  181 ILE B CD1 
5527 N N   . ALA B 155 ? 0.8200 0.5661 0.5264 0.0510  0.0521  0.0301  182 ALA B N   
5528 C CA  . ALA B 155 ? 0.8769 0.6036 0.5702 0.0480  0.0584  0.0343  182 ALA B CA  
5529 C C   . ALA B 155 ? 0.8086 0.5372 0.5075 0.0368  0.0668  0.0319  182 ALA B C   
5530 O O   . ALA B 155 ? 0.9243 0.6408 0.6137 0.0326  0.0741  0.0358  182 ALA B O   
5531 C CB  . ALA B 155 ? 0.7074 0.4136 0.3909 0.0528  0.0565  0.0368  182 ALA B CB  
5532 N N   . GLU B 156 ? 0.7018 0.4462 0.4155 0.0315  0.0662  0.0255  183 GLU B N   
5533 C CA  . GLU B 156 ? 0.7915 0.5413 0.5130 0.0197  0.0731  0.0220  183 GLU B CA  
5534 C C   . GLU B 156 ? 0.7233 0.4912 0.4519 0.0169  0.0774  0.0229  183 GLU B C   
5535 O O   . GLU B 156 ? 0.7970 0.5702 0.5322 0.0068  0.0846  0.0212  183 GLU B O   
5536 C CB  . GLU B 156 ? 0.8335 0.5956 0.5676 0.0152  0.0697  0.0141  183 GLU B CB  
5537 C CG  . GLU B 156 ? 1.0393 0.7829 0.7665 0.0178  0.0671  0.0120  183 GLU B CG  
5538 C CD  . GLU B 156 ? 1.0700 0.7850 0.7850 0.0127  0.0740  0.0145  183 GLU B CD  
5539 O OE1 . GLU B 156 ? 0.8934 0.6059 0.6090 0.0025  0.0816  0.0151  183 GLU B OE1 
5540 O OE2 . GLU B 156 ? 1.1194 0.8140 0.8243 0.0192  0.0723  0.0160  183 GLU B OE2 
5541 N N   . ASN B 157 ? 0.8218 0.5993 0.5499 0.0254  0.0737  0.0251  184 ASN B N   
5542 C CA  . ASN B 157 ? 0.8226 0.6145 0.5551 0.0255  0.0783  0.0263  184 ASN B CA  
5543 C C   . ASN B 157 ? 0.8416 0.6585 0.5933 0.0188  0.0804  0.0213  184 ASN B C   
5544 O O   . ASN B 157 ? 0.8301 0.6569 0.5877 0.0136  0.0880  0.0216  184 ASN B O   
5545 C CB  . ASN B 157 ? 0.6548 0.4314 0.3737 0.0230  0.0870  0.0315  184 ASN B CB  
5546 C CG  . ASN B 157 ? 0.8378 0.6252 0.5563 0.0270  0.0911  0.0331  184 ASN B CG  
5547 O OD1 . ASN B 157 ? 0.8918 0.6898 0.6141 0.0345  0.0859  0.0318  184 ASN B OD1 
5548 N ND2 . ASN B 157 ? 0.8960 0.6795 0.6094 0.0220  0.1015  0.0360  184 ASN B ND2 
5549 N N   . LYS B 158 ? 0.7825 0.6110 0.5440 0.0191  0.0737  0.0166  185 LYS B N   
5550 C CA  . LYS B 158 ? 0.7390 0.5945 0.5182 0.0151  0.0729  0.0118  185 LYS B CA  
5551 C C   . LYS B 158 ? 0.7448 0.6168 0.5291 0.0255  0.0681  0.0130  185 LYS B C   
5552 O O   . LYS B 158 ? 0.8670 0.7285 0.6419 0.0340  0.0645  0.0162  185 LYS B O   
5553 C CB  . LYS B 158 ? 0.7546 0.6124 0.5391 0.0088  0.0685  0.0055  185 LYS B CB  
5554 C CG  . LYS B 158 ? 0.8103 0.6464 0.5877 -0.0010 0.0734  0.0040  185 LYS B CG  
5555 C CD  . LYS B 158 ? 0.8008 0.6394 0.5829 -0.0115 0.0830  0.0048  185 LYS B CD  
5556 C CE  . LYS B 158 ? 0.7539 0.5669 0.5274 -0.0218 0.0888  0.0040  185 LYS B CE  
5557 N NZ  . LYS B 158 ? 1.0252 0.8396 0.8030 -0.0332 0.0997  0.0055  185 LYS B NZ  
5558 N N   . THR B 159 ? 0.7179 0.6160 0.5174 0.0246  0.0680  0.0105  186 THR B N   
5559 C CA  . THR B 159 ? 0.6911 0.6036 0.4950 0.0352  0.0636  0.0121  186 THR B CA  
5560 C C   . THR B 159 ? 0.6625 0.5807 0.4682 0.0379  0.0551  0.0096  186 THR B C   
5561 O O   . THR B 159 ? 0.7692 0.6837 0.5697 0.0468  0.0512  0.0125  186 THR B O   
5562 C CB  . THR B 159 ? 0.6481 0.5872 0.4672 0.0359  0.0672  0.0116  186 THR B CB  
5563 O OG1 . THR B 159 ? 0.7829 0.7169 0.6000 0.0330  0.0766  0.0138  186 THR B OG1 
5564 C CG2 . THR B 159 ? 0.6237 0.5727 0.4445 0.0489  0.0638  0.0146  186 THR B CG2 
5565 N N   . VAL B 160 ? 0.6697 0.5961 0.4816 0.0298  0.0528  0.0040  187 VAL B N   
5566 C CA  . VAL B 160 ? 0.7108 0.6407 0.5216 0.0315  0.0455  0.0008  187 VAL B CA  
5567 C C   . VAL B 160 ? 0.7080 0.6230 0.5139 0.0220  0.0460  -0.0044 187 VAL B C   
5568 O O   . VAL B 160 ? 0.7321 0.6545 0.5452 0.0114  0.0478  -0.0097 187 VAL B O   
5569 C CB  . VAL B 160 ? 0.7698 0.7292 0.5927 0.0328  0.0408  -0.0020 187 VAL B CB  
5570 C CG1 . VAL B 160 ? 0.5946 0.5555 0.4128 0.0343  0.0339  -0.0054 187 VAL B CG1 
5571 C CG2 . VAL B 160 ? 0.6397 0.6113 0.4665 0.0440  0.0410  0.0038  187 VAL B CG2 
5572 N N   . VAL B 161 ? 0.7087 0.6028 0.5029 0.0256  0.0445  -0.0031 188 VAL B N   
5573 C CA  . VAL B 161 ? 0.7113 0.5878 0.4990 0.0193  0.0453  -0.0075 188 VAL B CA  
5574 C C   . VAL B 161 ? 0.7174 0.5904 0.4995 0.0256  0.0401  -0.0091 188 VAL B C   
5575 O O   . VAL B 161 ? 0.6682 0.5417 0.4476 0.0348  0.0378  -0.0043 188 VAL B O   
5576 C CB  . VAL B 161 ? 0.6342 0.4850 0.4120 0.0182  0.0508  -0.0033 188 VAL B CB  
5577 C CG1 . VAL B 161 ? 0.6397 0.4807 0.4095 0.0290  0.0489  0.0032  188 VAL B CG1 
5578 C CG2 . VAL B 161 ? 0.5923 0.4231 0.3632 0.0123  0.0524  -0.0076 188 VAL B CG2 
5579 N N   . ALA B 162 ? 0.6227 0.4924 0.4030 0.0200  0.0390  -0.0164 189 ALA B N   
5580 C CA  . ALA B 162 ? 0.6587 0.5246 0.4327 0.0255  0.0355  -0.0189 189 ALA B CA  
5581 C C   . ALA B 162 ? 0.7172 0.5580 0.4823 0.0231  0.0384  -0.0223 189 ALA B C   
5582 O O   . ALA B 162 ? 0.7102 0.5399 0.4744 0.0138  0.0421  -0.0261 189 ALA B O   
5583 C CB  . ALA B 162 ? 0.5893 0.4757 0.3670 0.0232  0.0308  -0.0255 189 ALA B CB  
5584 N N   . PRO B 163 ? 0.6484 0.4792 0.4070 0.0315  0.0375  -0.0208 190 PRO B N   
5585 C CA  . PRO B 163 ? 0.7460 0.5536 0.4961 0.0315  0.0403  -0.0244 190 PRO B CA  
5586 C C   . PRO B 163 ? 0.7914 0.6018 0.5387 0.0277  0.0391  -0.0345 190 PRO B C   
5587 O O   . PRO B 163 ? 0.7844 0.6116 0.5327 0.0317  0.0355  -0.0363 190 PRO B O   
5588 C CB  . PRO B 163 ? 0.7788 0.5806 0.5260 0.0433  0.0394  -0.0183 190 PRO B CB  
5589 C CG  . PRO B 163 ? 0.6983 0.5223 0.4513 0.0478  0.0357  -0.0154 190 PRO B CG  
5590 C CD  . PRO B 163 ? 0.6357 0.4752 0.3952 0.0417  0.0348  -0.0150 190 PRO B CD  
5591 N N   . MET B 164 ? 0.7911 0.5836 0.5333 0.0197  0.0424  -0.0413 191 MET B N   
5592 C CA  . MET B 164 ? 0.8079 0.5998 0.5452 0.0152  0.0414  -0.0525 191 MET B CA  
5593 C C   . MET B 164 ? 0.8845 0.6680 0.6139 0.0267  0.0418  -0.0533 191 MET B C   
5594 O O   . MET B 164 ? 0.8645 0.6242 0.5873 0.0316  0.0458  -0.0521 191 MET B O   
5595 C CB  . MET B 164 ? 0.7605 0.5311 0.4935 0.0030  0.0457  -0.0600 191 MET B CB  
5596 C CG  . MET B 164 ? 0.7856 0.5565 0.5132 -0.0037 0.0440  -0.0735 191 MET B CG  
5597 S SD  . MET B 164 ? 1.0500 0.7886 0.7697 -0.0180 0.0501  -0.0838 191 MET B SD  
5598 C CE  . MET B 164 ? 1.0136 0.7158 0.7192 -0.0039 0.0560  -0.0798 191 MET B CE  
5599 N N   . LEU B 165 ? 0.8754 0.6787 0.6053 0.0316  0.0381  -0.0546 192 LEU B N   
5600 C CA  . LEU B 165 ? 0.7408 0.5400 0.4640 0.0419  0.0395  -0.0559 192 LEU B CA  
5601 C C   . LEU B 165 ? 0.7933 0.5824 0.5060 0.0377  0.0408  -0.0688 192 LEU B C   
5602 O O   . LEU B 165 ? 0.9013 0.6981 0.6131 0.0272  0.0380  -0.0769 192 LEU B O   
5603 C CB  . LEU B 165 ? 0.7516 0.5751 0.4786 0.0488  0.0363  -0.0506 192 LEU B CB  
5604 C CG  . LEU B 165 ? 0.7727 0.6054 0.5092 0.0523  0.0350  -0.0389 192 LEU B CG  
5605 C CD1 . LEU B 165 ? 0.8598 0.7129 0.5985 0.0583  0.0327  -0.0340 192 LEU B CD1 
5606 C CD2 . LEU B 165 ? 0.7017 0.5176 0.4391 0.0585  0.0379  -0.0330 192 LEU B CD2 
5607 N N   . ASP B 166 ? 0.9175 0.6899 0.6225 0.0461  0.0451  -0.0711 193 ASP B N   
5608 C CA  . ASP B 166 ? 0.8902 0.6473 0.5828 0.0435  0.0477  -0.0840 193 ASP B CA  
5609 C C   . ASP B 166 ? 0.9194 0.6940 0.6058 0.0485  0.0462  -0.0889 193 ASP B C   
5610 O O   . ASP B 166 ? 0.9427 0.7338 0.6333 0.0577  0.0458  -0.0810 193 ASP B O   
5611 C CB  . ASP B 166 ? 0.9515 0.6788 0.6377 0.0516  0.0542  -0.0841 193 ASP B CB  
5612 C CG  . ASP B 166 ? 1.3112 1.0176 0.9998 0.0472  0.0563  -0.0788 193 ASP B CG  
5613 O OD1 . ASP B 166 ? 1.4104 1.1236 1.1047 0.0355  0.0538  -0.0778 193 ASP B OD1 
5614 O OD2 . ASP B 166 ? 1.4017 1.0858 1.0863 0.0561  0.0607  -0.0753 193 ASP B OD2 
5615 N N   . SER B 167 ? 0.9156 0.6855 0.5907 0.0417  0.0456  -0.1023 194 SER B N   
5616 C CA  . SER B 167 ? 0.9007 0.6844 0.5657 0.0460  0.0446  -0.1086 194 SER B CA  
5617 C C   . SER B 167 ? 0.9346 0.6944 0.5834 0.0455  0.0492  -0.1229 194 SER B C   
5618 O O   . SER B 167 ? 0.9542 0.6868 0.6004 0.0407  0.0528  -0.1279 194 SER B O   
5619 C CB  . SER B 167 ? 0.9045 0.7151 0.5704 0.0376  0.0364  -0.1113 194 SER B CB  
5620 O OG  . SER B 167 ? 0.8750 0.6791 0.5359 0.0236  0.0334  -0.1244 194 SER B OG  
5621 N N   . ARG B 168 ? 1.0355 0.8041 0.6719 0.0508  0.0498  -0.1294 195 ARG B N   
5622 C CA  . ARG B 168 ? 0.9973 0.7445 0.6157 0.0505  0.0542  -0.1448 195 ARG B CA  
5623 C C   . ARG B 168 ? 0.9946 0.7351 0.6058 0.0335  0.0491  -0.1592 195 ARG B C   
5624 O O   . ARG B 168 ? 1.0825 0.7992 0.6785 0.0307  0.0528  -0.1734 195 ARG B O   
5625 C CB  . ARG B 168 ? 0.8522 0.6131 0.4577 0.0603  0.0562  -0.1479 195 ARG B CB  
5626 C CG  . ARG B 168 ? 0.9284 0.7190 0.5299 0.0545  0.0477  -0.1492 195 ARG B CG  
5627 C CD  . ARG B 168 ? 0.8860 0.6874 0.4713 0.0643  0.0509  -0.1521 195 ARG B CD  
5628 N NE  . ARG B 168 ? 1.0222 0.8538 0.6052 0.0622  0.0431  -0.1479 195 ARG B NE  
5629 C CZ  . ARG B 168 ? 0.8746 0.7162 0.4442 0.0540  0.0354  -0.1592 195 ARG B CZ  
5630 N NH1 . ARG B 168 ? 0.9215 0.7453 0.4787 0.0452  0.0346  -0.1766 195 ARG B NH1 
5631 N NH2 . ARG B 168 ? 1.0061 0.8760 0.5744 0.0546  0.0282  -0.1529 195 ARG B NH2 
5632 N N   . ALA B 169 ? 0.9101 0.6713 0.5322 0.0222  0.0410  -0.1564 196 ALA B N   
5633 C CA  . ALA B 169 ? 0.8436 0.6061 0.4619 0.0050  0.0350  -0.1702 196 ALA B CA  
5634 C C   . ALA B 169 ? 0.8980 0.6647 0.5349 -0.0065 0.0322  -0.1638 196 ALA B C   
5635 O O   . ALA B 169 ? 0.9271 0.6884 0.5756 -0.0008 0.0359  -0.1503 196 ALA B O   
5636 C CB  . ALA B 169 ? 0.8045 0.5979 0.4150 0.0035  0.0265  -0.1759 196 ALA B CB  
5637 N N   . ALA B 170 ? 0.8931 0.6708 0.5326 -0.0231 0.0256  -0.1739 197 ALA B N   
5638 C CA  . ALA B 170 ? 0.8317 0.6169 0.4896 -0.0352 0.0235  -0.1689 197 ALA B CA  
5639 C C   . ALA B 170 ? 0.9492 0.7669 0.6230 -0.0283 0.0188  -0.1534 197 ALA B C   
5640 O O   . ALA B 170 ? 1.0116 0.8336 0.7010 -0.0340 0.0194  -0.1458 197 ALA B O   
5641 C CB  . ALA B 170 ? 0.8728 0.6662 0.5316 -0.0552 0.0173  -0.1845 197 ALA B CB  
5642 N N   . TYR B 171 ? 0.9759 0.8150 0.6449 -0.0162 0.0151  -0.1486 198 TYR B N   
5643 C CA  . TYR B 171 ? 0.8503 0.7170 0.5324 -0.0090 0.0112  -0.1341 198 TYR B CA  
5644 C C   . TYR B 171 ? 0.8801 0.7333 0.5724 -0.0019 0.0178  -0.1199 198 TYR B C   
5645 O O   . TYR B 171 ? 0.9555 0.7838 0.6416 0.0053  0.0249  -0.1180 198 TYR B O   
5646 C CB  . TYR B 171 ? 0.6988 0.5835 0.3706 0.0038  0.0083  -0.1306 198 TYR B CB  
5647 C CG  . TYR B 171 ? 0.7890 0.6952 0.4719 0.0134  0.0063  -0.1144 198 TYR B CG  
5648 C CD1 . TYR B 171 ? 0.6592 0.5956 0.3499 0.0111  -0.0020 -0.1117 198 TYR B CD1 
5649 C CD2 . TYR B 171 ? 0.9454 0.8416 0.6310 0.0250  0.0128  -0.1020 198 TYR B CD2 
5650 C CE1 . TYR B 171 ? 0.7559 0.7082 0.4552 0.0205  -0.0030 -0.0971 198 TYR B CE1 
5651 C CE2 . TYR B 171 ? 0.8834 0.7961 0.5780 0.0326  0.0114  -0.0882 198 TYR B CE2 
5652 C CZ  . TYR B 171 ? 0.7614 0.7004 0.4620 0.0306  0.0040  -0.0857 198 TYR B CZ  
5653 O OH  . TYR B 171 ? 0.8652 0.8173 0.5734 0.0388  0.0033  -0.0721 198 TYR B OH  
5654 N N   . SER B 172 ? 0.7985 0.6692 0.5065 -0.0035 0.0152  -0.1103 199 SER B N   
5655 C CA  . SER B 172 ? 0.8176 0.6802 0.5345 0.0035  0.0200  -0.0965 199 SER B CA  
5656 C C   . SER B 172 ? 0.8734 0.7644 0.6031 0.0058  0.0152  -0.0869 199 SER B C   
5657 O O   . SER B 172 ? 0.8896 0.8057 0.6217 0.0028  0.0084  -0.0905 199 SER B O   
5658 C CB  . SER B 172 ? 0.7601 0.5973 0.4806 -0.0051 0.0258  -0.0975 199 SER B CB  
5659 O OG  . SER B 172 ? 0.8304 0.6582 0.5561 0.0030  0.0300  -0.0846 199 SER B OG  
5660 N N   . ASN B 173 ? 0.7604 0.6469 0.4975 0.0120  0.0186  -0.0748 200 ASN B N   
5661 C CA  . ASN B 173 ? 0.6615 0.5706 0.4094 0.0161  0.0155  -0.0651 200 ASN B CA  
5662 C C   . ASN B 173 ? 0.8070 0.7269 0.5681 0.0057  0.0144  -0.0660 200 ASN B C   
5663 O O   . ASN B 173 ? 0.7826 0.7092 0.5530 0.0089  0.0157  -0.0568 200 ASN B O   
5664 C CB  . ASN B 173 ? 0.7371 0.6366 0.4863 0.0267  0.0195  -0.0530 200 ASN B CB  
5665 C CG  . ASN B 173 ? 0.8564 0.7295 0.6052 0.0248  0.0254  -0.0515 200 ASN B CG  
5666 O OD1 . ASN B 173 ? 0.8364 0.6901 0.5774 0.0221  0.0283  -0.0583 200 ASN B OD1 
5667 N ND2 . ASN B 173 ? 0.7653 0.6364 0.5209 0.0268  0.0273  -0.0424 200 ASN B ND2 
5668 N N   . PHE B 174 ? 0.7648 0.6871 0.5274 -0.0073 0.0127  -0.0773 201 PHE B N   
5669 C CA  . PHE B 174 ? 0.8836 0.8184 0.6609 -0.0185 0.0127  -0.0785 201 PHE B CA  
5670 C C   . PHE B 174 ? 0.7926 0.7411 0.5720 -0.0320 0.0075  -0.0925 201 PHE B C   
5671 O O   . PHE B 174 ? 0.7813 0.7158 0.5485 -0.0362 0.0069  -0.1027 201 PHE B O   
5672 C CB  . PHE B 174 ? 0.8750 0.7835 0.6540 -0.0240 0.0213  -0.0751 201 PHE B CB  
5673 C CG  . PHE B 174 ? 0.8391 0.7215 0.6100 -0.0352 0.0252  -0.0854 201 PHE B CG  
5674 C CD1 . PHE B 174 ? 0.7977 0.6535 0.5533 -0.0288 0.0279  -0.0874 201 PHE B CD1 
5675 C CD2 . PHE B 174 ? 0.8157 0.6996 0.5947 -0.0521 0.0269  -0.0929 201 PHE B CD2 
5676 C CE1 . PHE B 174 ? 0.9305 0.7591 0.6773 -0.0380 0.0322  -0.0968 201 PHE B CE1 
5677 C CE2 . PHE B 174 ? 0.8262 0.6823 0.5965 -0.0631 0.0312  -0.1025 201 PHE B CE2 
5678 C CZ  . PHE B 174 ? 0.8357 0.6627 0.5890 -0.0554 0.0339  -0.1044 201 PHE B CZ  
5679 N N   . TRP B 175 ? 0.7797 0.7568 0.5753 -0.0388 0.0038  -0.0932 202 TRP B N   
5680 C CA  . TRP B 175 ? 0.7403 0.7339 0.5432 -0.0548 -0.0010 -0.1065 202 TRP B CA  
5681 C C   . TRP B 175 ? 0.8776 0.8642 0.6939 -0.0696 0.0061  -0.1075 202 TRP B C   
5682 O O   . TRP B 175 ? 0.9055 0.8908 0.7301 -0.0655 0.0119  -0.0967 202 TRP B O   
5683 C CB  . TRP B 175 ? 0.8236 0.8607 0.6374 -0.0519 -0.0113 -0.1071 202 TRP B CB  
5684 C CG  . TRP B 175 ? 0.8565 0.9039 0.6575 -0.0364 -0.0180 -0.1035 202 TRP B CG  
5685 C CD1 . TRP B 175 ? 0.8516 0.8757 0.6335 -0.0264 -0.0156 -0.1013 202 TRP B CD1 
5686 C CD2 . TRP B 175 ? 0.8789 0.9631 0.6852 -0.0287 -0.0277 -0.1011 202 TRP B CD2 
5687 N NE1 . TRP B 175 ? 0.9677 1.0107 0.7420 -0.0141 -0.0223 -0.0975 202 TRP B NE1 
5688 C CE2 . TRP B 175 ? 0.8041 0.8830 0.5920 -0.0147 -0.0301 -0.0969 202 TRP B CE2 
5689 C CE3 . TRP B 175 ? 0.8778 0.9997 0.7029 -0.0315 -0.0343 -0.1015 202 TRP B CE3 
5690 C CZ2 . TRP B 175 ? 0.6928 0.7998 0.4782 -0.0035 -0.0387 -0.0926 202 TRP B CZ2 
5691 C CZ3 . TRP B 175 ? 0.7612 0.9126 0.5849 -0.0193 -0.0437 -0.0975 202 TRP B CZ3 
5692 C CH2 . TRP B 175 ? 0.8909 1.0333 0.6938 -0.0055 -0.0458 -0.0928 202 TRP B CH2 
5693 N N   . CYS B 176 ? 0.9754 0.9571 0.7929 -0.0874 0.0060  -0.1209 203 CYS B N   
5694 C CA  . CYS B 176 ? 1.0835 1.0610 0.9148 -0.1039 0.0132  -0.1226 203 CYS B CA  
5695 C C   . CYS B 176 ? 1.1068 1.1281 0.9613 -0.1145 0.0073  -0.1274 203 CYS B C   
5696 O O   . CYS B 176 ? 0.9248 0.9529 0.7956 -0.1238 0.0139  -0.1241 203 CYS B O   
5697 C CB  . CYS B 176 ? 0.9306 0.8726 0.7506 -0.1190 0.0186  -0.1338 203 CYS B CB  
5698 S SG  . CYS B 176 ? 1.1096 1.0005 0.9170 -0.1155 0.0328  -0.1236 203 CYS B SG  
5699 N N   . GLY B 177 ? 1.0617 1.1143 0.9181 -0.1129 -0.0048 -0.1349 204 GLY B N   
5700 C CA  . GLY B 177 ? 0.8498 0.9487 0.7294 -0.1210 -0.0121 -0.1394 204 GLY B CA  
5701 C C   . GLY B 177 ? 0.9848 1.1184 0.8648 -0.1039 -0.0237 -0.1349 204 GLY B C   
5702 O O   . GLY B 177 ? 1.0451 1.1669 0.9054 -0.0902 -0.0274 -0.1325 204 GLY B O   
5703 N N   . MET B 178 ? 1.0054 1.1823 0.9087 -0.1045 -0.0288 -0.1333 205 MET B N   
5704 C CA  . MET B 178 ? 0.9604 1.1739 0.8664 -0.0884 -0.0402 -0.1286 205 MET B CA  
5705 C C   . MET B 178 ? 1.0033 1.2656 0.9330 -0.0998 -0.0500 -0.1382 205 MET B C   
5706 O O   . MET B 178 ? 1.1567 1.4308 1.1083 -0.1154 -0.0447 -0.1418 205 MET B O   
5707 C CB  . MET B 178 ? 0.7923 1.0079 0.7024 -0.0687 -0.0351 -0.1109 205 MET B CB  
5708 C CG  . MET B 178 ? 0.9655 1.2031 0.8689 -0.0481 -0.0448 -0.1035 205 MET B CG  
5709 S SD  . MET B 178 ? 1.0124 1.2496 0.9205 -0.0264 -0.0381 -0.0839 205 MET B SD  
5710 C CE  . MET B 178 ? 0.6419 0.8229 0.5274 -0.0229 -0.0264 -0.0776 205 MET B CE  
5711 N N   . THR B 179 ? 1.1207 1.4127 1.0460 -0.0919 -0.0642 -0.1419 206 THR B N   
5712 C CA  . THR B 179 ? 1.1491 1.4868 1.0924 -0.1041 -0.0766 -0.1545 206 THR B CA  
5713 C C   . THR B 179 ? 1.2311 1.6183 1.2015 -0.0945 -0.0814 -0.1464 206 THR B C   
5714 O O   . THR B 179 ? 1.2860 1.7179 1.2686 -0.0967 -0.0952 -0.1539 206 THR B O   
5715 C CB  . THR B 179 ? 1.1560 1.5013 1.0781 -0.1005 -0.0906 -0.1638 206 THR B CB  
5716 O OG1 . THR B 179 ? 1.1442 1.4995 1.0548 -0.0749 -0.0959 -0.1502 206 THR B OG1 
5717 C CG2 . THR B 179 ? 1.2652 1.5619 1.1599 -0.1084 -0.0853 -0.1723 206 THR B CG2 
5718 N N   . SER B 180 ? 1.0817 1.4625 1.0613 -0.0830 -0.0707 -0.1316 207 SER B N   
5719 C CA  . SER B 180 ? 1.1611 1.5855 1.1662 -0.0718 -0.0730 -0.1231 207 SER B CA  
5720 C C   . SER B 180 ? 1.1619 1.6146 1.1597 -0.0501 -0.0870 -0.1173 207 SER B C   
5721 O O   . SER B 180 ? 0.9044 1.3964 0.9219 -0.0381 -0.0913 -0.1106 207 SER B O   
5722 C CB  . SER B 180 ? 1.2023 1.6670 1.2403 -0.0923 -0.0749 -0.1340 207 SER B CB  
5723 O OG  . SER B 180 ? 1.3893 1.8858 1.4301 -0.1020 -0.0909 -0.1484 207 SER B OG  
5724 N N   . GLN B 181 ? 1.1848 1.6172 1.1537 -0.0443 -0.0935 -0.1195 208 GLN B N   
5725 C CA  . GLN B 181 ? 1.0078 1.4546 0.9620 -0.0214 -0.1037 -0.1108 208 GLN B CA  
5726 C C   . GLN B 181 ? 1.0233 1.4233 0.9469 -0.0077 -0.0966 -0.1008 208 GLN B C   
5727 O O   . GLN B 181 ? 1.0520 1.4552 0.9578 0.0099  -0.1034 -0.0936 208 GLN B O   
5728 C CB  . GLN B 181 ? 0.9577 1.4354 0.9063 -0.0266 -0.1211 -0.1237 208 GLN B CB  
5729 C CG  . GLN B 181 ? 1.1394 1.6709 1.1202 -0.0394 -0.1308 -0.1340 208 GLN B CG  
5730 C CD  . GLN B 181 ? 1.1240 1.6898 1.0974 -0.0410 -0.1501 -0.1454 208 GLN B CD  
5731 O OE1 . GLN B 181 ? 1.0705 1.6257 1.0152 -0.0267 -0.1568 -0.1418 208 GLN B OE1 
5732 N NE2 . GLN B 181 ? 1.2144 1.8220 1.2133 -0.0590 -0.1591 -0.1595 208 GLN B NE2 
5733 N N   . GLY B 182 ? 0.9787 1.3360 0.8957 -0.0154 -0.0830 -0.0998 209 GLY B N   
5734 C CA  . GLY B 182 ? 1.0202 1.3347 0.9117 -0.0041 -0.0755 -0.0909 209 GLY B CA  
5735 C C   . GLY B 182 ? 0.9831 1.2687 0.8507 -0.0126 -0.0761 -0.1009 209 GLY B C   
5736 O O   . GLY B 182 ? 1.0125 1.2626 0.8608 -0.0048 -0.0688 -0.0944 209 GLY B O   
5737 N N   . TYR B 183 ? 1.0637 1.3635 0.9320 -0.0285 -0.0842 -0.1170 210 TYR B N   
5738 C CA  . TYR B 183 ? 0.9950 1.2687 0.8387 -0.0354 -0.0853 -0.1279 210 TYR B CA  
5739 C C   . TYR B 183 ? 1.0282 1.2626 0.8708 -0.0511 -0.0732 -0.1342 210 TYR B C   
5740 O O   . TYR B 183 ? 0.9147 1.1507 0.7778 -0.0632 -0.0671 -0.1354 210 TYR B O   
5741 C CB  . TYR B 183 ? 1.0939 1.3986 0.9363 -0.0455 -0.0999 -0.1437 210 TYR B CB  
5742 C CG  . TYR B 183 ? 1.1988 1.5473 1.0444 -0.0305 -0.1134 -0.1379 210 TYR B CG  
5743 C CD1 . TYR B 183 ? 1.2222 1.5656 1.0512 -0.0074 -0.1135 -0.1226 210 TYR B CD1 
5744 C CD2 . TYR B 183 ? 1.2426 1.6376 1.1080 -0.0393 -0.1260 -0.1473 210 TYR B CD2 
5745 C CE1 . TYR B 183 ? 1.1468 1.5276 0.9766 0.0078  -0.1254 -0.1161 210 TYR B CE1 
5746 C CE2 . TYR B 183 ? 1.2441 1.6804 1.1121 -0.0238 -0.1391 -0.1413 210 TYR B CE2 
5747 C CZ  . TYR B 183 ? 1.2809 1.7084 1.1300 0.0004  -0.1386 -0.1252 210 TYR B CZ  
5748 O OH  . TYR B 183 ? 1.1525 1.6182 1.0022 0.0173  -0.1512 -0.1180 210 TYR B OH  
5749 N N   . TYR B 184 ? 0.9549 1.1539 0.7729 -0.0499 -0.0691 -0.1376 211 TYR B N   
5750 C CA  . TYR B 184 ? 1.0009 1.1599 0.8144 -0.0625 -0.0581 -0.1434 211 TYR B CA  
5751 C C   . TYR B 184 ? 1.0770 1.2422 0.8996 -0.0862 -0.0612 -0.1613 211 TYR B C   
5752 O O   . TYR B 184 ? 0.9124 1.1041 0.7339 -0.0928 -0.0730 -0.1733 211 TYR B O   
5753 C CB  . TYR B 184 ? 0.8868 1.0106 0.6723 -0.0546 -0.0540 -0.1441 211 TYR B CB  
5754 C CG  . TYR B 184 ? 0.9946 1.0768 0.7731 -0.0661 -0.0437 -0.1513 211 TYR B CG  
5755 C CD1 . TYR B 184 ? 1.0643 1.1179 0.8454 -0.0618 -0.0319 -0.1404 211 TYR B CD1 
5756 C CD2 . TYR B 184 ? 0.9265 0.9970 0.6945 -0.0808 -0.0460 -0.1691 211 TYR B CD2 
5757 C CE1 . TYR B 184 ? 0.9763 0.9914 0.7499 -0.0705 -0.0228 -0.1458 211 TYR B CE1 
5758 C CE2 . TYR B 184 ? 0.9671 0.9968 0.7275 -0.0900 -0.0360 -0.1751 211 TYR B CE2 
5759 C CZ  . TYR B 184 ? 1.2774 1.2798 1.0407 -0.0842 -0.0244 -0.1628 211 TYR B CZ  
5760 O OH  . TYR B 184 ? 1.3952 1.3566 1.1500 -0.0917 -0.0148 -0.1678 211 TYR B OH  
5761 N N   . LYS B 185 ? 1.0457 1.1853 0.8763 -0.0994 -0.0503 -0.1630 212 LYS B N   
5762 C CA  . LYS B 185 ? 1.0477 1.1876 0.8881 -0.1238 -0.0505 -0.1788 212 LYS B CA  
5763 C C   . LYS B 185 ? 1.1676 1.2560 0.9965 -0.1323 -0.0373 -0.1813 212 LYS B C   
5764 O O   . LYS B 185 ? 1.1339 1.1989 0.9628 -0.1240 -0.0267 -0.1681 212 LYS B O   
5765 C CB  . LYS B 185 ? 1.0736 1.2486 0.9458 -0.1336 -0.0508 -0.1766 212 LYS B CB  
5766 C CG  . LYS B 185 ? 1.1757 1.3563 1.0617 -0.1609 -0.0510 -0.1930 212 LYS B CG  
5767 C CD  . LYS B 185 ? 1.1620 1.3810 1.0814 -0.1687 -0.0502 -0.1890 212 LYS B CD  
5768 C CE  . LYS B 185 ? 1.2533 1.4798 1.1891 -0.1980 -0.0495 -0.2052 212 LYS B CE  
5769 N NZ  . LYS B 185 ? 1.2342 1.5011 1.2047 -0.2056 -0.0476 -0.2011 212 LYS B NZ  
5770 N N   . ARG B 186 ? 1.3560 1.4262 1.1740 -0.1483 -0.0382 -0.1983 213 ARG B N   
5771 C CA  . ARG B 186 ? 1.4514 1.4701 1.2559 -0.1557 -0.0260 -0.2018 213 ARG B CA  
5772 C C   . ARG B 186 ? 1.4013 1.4142 1.2246 -0.1774 -0.0184 -0.2053 213 ARG B C   
5773 O O   . ARG B 186 ? 1.4373 1.4770 1.2759 -0.1961 -0.0245 -0.2175 213 ARG B O   
5774 C CB  . ARG B 186 ? 1.5494 1.5464 1.3298 -0.1608 -0.0294 -0.2186 213 ARG B CB  
5775 C CG  . ARG B 186 ? 1.6660 1.6066 1.4287 -0.1635 -0.0167 -0.2212 213 ARG B CG  
5776 C CD  . ARG B 186 ? 1.7290 1.6485 1.4635 -0.1506 -0.0181 -0.2268 213 ARG B CD  
5777 N NE  . ARG B 186 ? 1.8288 1.7544 1.5578 -0.1261 -0.0177 -0.2104 213 ARG B NE  
5778 C CZ  . ARG B 186 ? 1.7896 1.6817 1.5049 -0.1118 -0.0085 -0.2020 213 ARG B CZ  
5779 N NH1 . ARG B 186 ? 1.6136 1.4623 1.3174 -0.1171 0.0010  -0.2079 213 ARG B NH1 
5780 N NH2 . ARG B 186 ? 1.6161 1.5187 1.3297 -0.0917 -0.0088 -0.1874 213 ARG B NH2 
5781 N N   . THR B 187 ? 1.0117 0.9906 0.8336 -0.1751 -0.0050 -0.1944 214 THR B N   
5782 C CA  . THR B 187 ? 1.1415 1.1064 0.9768 -0.1941 0.0052  -0.1951 214 THR B CA  
5783 C C   . THR B 187 ? 1.2901 1.1970 1.1044 -0.1993 0.0162  -0.1989 214 THR B C   
5784 O O   . THR B 187 ? 1.0794 0.9589 0.8718 -0.1837 0.0174  -0.1965 214 THR B O   
5785 C CB  . THR B 187 ? 1.2361 1.2120 1.0876 -0.1858 0.0124  -0.1770 214 THR B CB  
5786 O OG1 . THR B 187 ? 1.2595 1.1960 1.0938 -0.1702 0.0214  -0.1643 214 THR B OG1 
5787 C CG2 . THR B 187 ? 1.2374 1.2628 1.1030 -0.1718 0.0021  -0.1699 214 THR B CG2 
5788 N N   . PRO B 188 ? 1.3525 1.2391 1.1730 -0.2209 0.0251  -0.2047 215 PRO B N   
5789 C CA  . PRO B 188 ? 1.3223 1.1502 1.1214 -0.2250 0.0361  -0.2077 215 PRO B CA  
5790 C C   . PRO B 188 ? 1.2088 1.0044 0.9961 -0.2056 0.0460  -0.1896 215 PRO B C   
5791 O O   . PRO B 188 ? 1.3638 1.1123 1.1301 -0.2017 0.0532  -0.1906 215 PRO B O   
5792 C CB  . PRO B 188 ? 1.2809 1.0999 1.0930 -0.2534 0.0439  -0.2156 215 PRO B CB  
5793 C CG  . PRO B 188 ? 1.3001 1.1766 1.1385 -0.2665 0.0332  -0.2236 215 PRO B CG  
5794 C CD  . PRO B 188 ? 1.3232 1.2396 1.1701 -0.2436 0.0252  -0.2103 215 PRO B CD  
5795 N N   . ALA B 189 ? 0.9714 0.7906 0.7710 -0.1928 0.0463  -0.1735 216 ALA B N   
5796 C CA  . ALA B 189 ? 1.0851 0.8762 0.8743 -0.1756 0.0548  -0.1567 216 ALA B CA  
5797 C C   . ALA B 189 ? 1.1348 0.9229 0.9091 -0.1513 0.0494  -0.1512 216 ALA B C   
5798 O O   . ALA B 189 ? 1.1821 0.9446 0.9459 -0.1369 0.0555  -0.1391 216 ALA B O   
5799 C CB  . ALA B 189 ? 0.9668 0.7819 0.7744 -0.1736 0.0585  -0.1425 216 ALA B CB  
5800 N N   . TYR B 190 ? 0.9195 0.7335 0.6924 -0.1468 0.0383  -0.1597 217 TYR B N   
5801 C CA  . TYR B 190 ? 0.9782 0.7924 0.7385 -0.1244 0.0342  -0.1536 217 TYR B CA  
5802 C C   . TYR B 190 ? 1.0812 0.8494 0.8191 -0.1172 0.0407  -0.1559 217 TYR B C   
5803 O O   . TYR B 190 ? 1.1423 0.8949 0.8729 -0.1001 0.0446  -0.1439 217 TYR B O   
5804 C CB  . TYR B 190 ? 0.9809 0.8311 0.7421 -0.1218 0.0217  -0.1622 217 TYR B CB  
5805 C CG  . TYR B 190 ? 0.9163 0.7705 0.6664 -0.0993 0.0184  -0.1541 217 TYR B CG  
5806 C CD1 . TYR B 190 ? 1.0034 0.8826 0.7635 -0.0858 0.0159  -0.1398 217 TYR B CD1 
5807 C CD2 . TYR B 190 ? 0.9381 0.7701 0.6677 -0.0918 0.0189  -0.1608 217 TYR B CD2 
5808 C CE1 . TYR B 190 ? 1.0086 0.8903 0.7591 -0.0670 0.0138  -0.1323 217 TYR B CE1 
5809 C CE2 . TYR B 190 ? 0.9716 0.8084 0.6924 -0.0722 0.0171  -0.1531 217 TYR B CE2 
5810 C CZ  . TYR B 190 ? 0.9810 0.8426 0.7127 -0.0607 0.0145  -0.1388 217 TYR B CZ  
5811 O OH  . TYR B 190 ? 1.0021 0.8675 0.7255 -0.0430 0.0135  -0.1311 217 TYR B OH  
5812 N N   . ILE B 191 ? 1.0440 0.7909 0.7711 -0.1298 0.0416  -0.1717 218 ILE B N   
5813 C CA  . ILE B 191 ? 1.0539 0.7567 0.7589 -0.1216 0.0481  -0.1750 218 ILE B CA  
5814 C C   . ILE B 191 ? 1.1393 0.8051 0.8402 -0.1165 0.0594  -0.1624 218 ILE B C   
5815 O O   . ILE B 191 ? 1.0840 0.7297 0.7730 -0.0981 0.0626  -0.1551 218 ILE B O   
5816 C CB  . ILE B 191 ? 1.0822 0.7668 0.7759 -0.1378 0.0476  -0.1956 218 ILE B CB  
5817 C CG1 . ILE B 191 ? 1.1232 0.8481 0.8201 -0.1423 0.0349  -0.2077 218 ILE B CG1 
5818 C CG2 . ILE B 191 ? 1.0999 0.7400 0.7699 -0.1267 0.0543  -0.1996 218 ILE B CG2 
5819 C CD1 . ILE B 191 ? 1.0679 0.8070 0.7541 -0.1207 0.0295  -0.2041 218 ILE B CD1 
5820 N N   . PRO B 192 ? 1.1423 0.7983 0.8520 -0.1313 0.0659  -0.1591 219 PRO B N   
5821 C CA  . PRO B 192 ? 1.1826 0.8032 0.8854 -0.1243 0.0764  -0.1455 219 PRO B CA  
5822 C C   . PRO B 192 ? 1.1204 0.7555 0.8268 -0.1036 0.0747  -0.1281 219 PRO B C   
5823 O O   . PRO B 192 ? 1.1109 0.7175 0.8053 -0.0892 0.0799  -0.1190 219 PRO B O   
5824 C CB  . PRO B 192 ? 1.1588 0.7764 0.8729 -0.1459 0.0828  -0.1453 219 PRO B CB  
5825 C CG  . PRO B 192 ? 1.1621 0.7948 0.8827 -0.1665 0.0779  -0.1638 219 PRO B CG  
5826 C CD  . PRO B 192 ? 1.0614 0.7334 0.7856 -0.1561 0.0651  -0.1687 219 PRO B CD  
5827 N N   . ILE B 193 ? 1.0501 0.7286 0.7726 -0.1015 0.0676  -0.1234 220 ILE B N   
5828 C CA  . ILE B 193 ? 1.0461 0.7380 0.7713 -0.0825 0.0656  -0.1084 220 ILE B CA  
5829 C C   . ILE B 193 ? 1.0166 0.7072 0.7311 -0.0647 0.0613  -0.1091 220 ILE B C   
5830 O O   . ILE B 193 ? 1.1331 0.8103 0.8413 -0.0489 0.0636  -0.0988 220 ILE B O   
5831 C CB  . ILE B 193 ? 0.9763 0.7126 0.7206 -0.0848 0.0599  -0.1039 220 ILE B CB  
5832 C CG1 . ILE B 193 ? 1.0761 0.8146 0.8322 -0.1013 0.0659  -0.1019 220 ILE B CG1 
5833 C CG2 . ILE B 193 ? 0.8332 0.5816 0.5788 -0.0658 0.0575  -0.0900 220 ILE B CG2 
5834 C CD1 . ILE B 193 ? 1.0026 0.7853 0.7786 -0.1031 0.0611  -0.0982 220 ILE B CD1 
5835 N N   . ARG B 194 ? 1.0437 0.7494 0.7560 -0.0672 0.0551  -0.1214 221 ARG B N   
5836 C CA  . ARG B 194 ? 1.0679 0.7747 0.7699 -0.0511 0.0519  -0.1225 221 ARG B CA  
5837 C C   . ARG B 194 ? 1.0320 0.6975 0.7178 -0.0425 0.0593  -0.1232 221 ARG B C   
5838 O O   . ARG B 194 ? 1.0630 0.7264 0.7438 -0.0250 0.0596  -0.1169 221 ARG B O   
5839 C CB  . ARG B 194 ? 0.8885 0.6167 0.5882 -0.0572 0.0446  -0.1366 221 ARG B CB  
5840 C CG  . ARG B 194 ? 1.0081 0.7370 0.6952 -0.0420 0.0426  -0.1392 221 ARG B CG  
5841 C CD  . ARG B 194 ? 0.9481 0.7017 0.6421 -0.0263 0.0393  -0.1254 221 ARG B CD  
5842 N NE  . ARG B 194 ? 0.8672 0.6206 0.5498 -0.0124 0.0392  -0.1271 221 ARG B NE  
5843 C CZ  . ARG B 194 ? 0.9966 0.7282 0.6721 0.0007  0.0453  -0.1224 221 ARG B CZ  
5844 N NH1 . ARG B 194 ? 1.0084 0.7159 0.6857 0.0029  0.0510  -0.1151 221 ARG B NH1 
5845 N NH2 . ARG B 194 ? 0.9101 0.6452 0.5764 0.0123  0.0458  -0.1248 221 ARG B NH2 
5846 N N   . LYS B 195 ? 1.0276 0.6601 0.7056 -0.0542 0.0657  -0.1305 222 LYS B N   
5847 C CA  . LYS B 195 ? 1.1263 0.7160 0.7878 -0.0456 0.0733  -0.1314 222 LYS B CA  
5848 C C   . LYS B 195 ? 1.0284 0.5954 0.6889 -0.0376 0.0797  -0.1162 222 LYS B C   
5849 O O   . LYS B 195 ? 1.2254 0.7566 0.8726 -0.0283 0.0860  -0.1149 222 LYS B O   
5850 C CB  . LYS B 195 ? 1.2673 0.8272 0.9179 -0.0619 0.0777  -0.1473 222 LYS B CB  
5851 C CG  . LYS B 195 ? 1.2577 0.8262 0.9002 -0.0647 0.0729  -0.1643 222 LYS B CG  
5852 C CD  . LYS B 195 ? 1.4420 0.9740 1.0715 -0.0804 0.0783  -0.1803 222 LYS B CD  
5853 C CE  . LYS B 195 ? 1.4996 1.0374 1.1175 -0.0826 0.0736  -0.1985 222 LYS B CE  
5854 N NZ  . LYS B 195 ? 1.7099 1.2109 1.3146 -0.0997 0.0786  -0.2157 222 LYS B NZ  
5855 N N   . ARG B 196 ? 1.0700 0.6566 0.7433 -0.0401 0.0782  -0.1048 223 ARG B N   
5856 C CA  . ARG B 196 ? 1.1303 0.6966 0.8012 -0.0344 0.0839  -0.0905 223 ARG B CA  
5857 C C   . ARG B 196 ? 1.2360 0.7598 0.8958 -0.0458 0.0934  -0.0931 223 ARG B C   
5858 O O   . ARG B 196 ? 1.2989 0.7925 0.9485 -0.0369 0.0994  -0.0831 223 ARG B O   
5859 C CB  . ARG B 196 ? 1.0338 0.5938 0.6989 -0.0115 0.0833  -0.0806 223 ARG B CB  
5860 C CG  . ARG B 196 ? 0.9536 0.5528 0.6304 -0.0011 0.0754  -0.0745 223 ARG B CG  
5861 C CD  . ARG B 196 ? 0.9841 0.5776 0.6572 0.0194  0.0751  -0.0645 223 ARG B CD  
5862 N NE  . ARG B 196 ? 1.2762 0.9052 0.9603 0.0277  0.0683  -0.0596 223 ARG B NE  
5863 C CZ  . ARG B 196 ? 1.2060 0.8500 0.8911 0.0363  0.0653  -0.0640 223 ARG B CZ  
5864 N NH1 . ARG B 196 ? 1.2000 0.8280 0.8754 0.0390  0.0683  -0.0738 223 ARG B NH1 
5865 N NH2 . ARG B 196 ? 1.2105 0.8849 0.9054 0.0421  0.0600  -0.0585 223 ARG B NH2 
5866 N N   . ASP B 197 ? 1.1723 0.6929 0.8334 -0.0657 0.0948  -0.1066 224 ASP B N   
5867 C CA  . ASP B 197 ? 1.0999 0.5827 0.7533 -0.0807 0.1046  -0.1084 224 ASP B CA  
5868 C C   . ASP B 197 ? 1.2353 0.7270 0.8986 -0.0897 0.1084  -0.0967 224 ASP B C   
5869 O O   . ASP B 197 ? 1.3491 0.8062 1.0029 -0.0931 0.1179  -0.0893 224 ASP B O   
5870 C CB  . ASP B 197 ? 1.3058 0.7844 0.9589 -0.1013 0.1046  -0.1274 224 ASP B CB  
5871 C CG  . ASP B 197 ? 1.4441 0.8981 1.0806 -0.0934 0.1047  -0.1394 224 ASP B CG  
5872 O OD1 . ASP B 197 ? 1.4564 0.8936 1.0823 -0.0719 0.1064  -0.1320 224 ASP B OD1 
5873 O OD2 . ASP B 197 ? 1.2392 0.6916 0.8734 -0.1085 0.1032  -0.1566 224 ASP B OD2 
5874 N N   . ARG B 198 ? 1.1779 0.7150 0.8595 -0.0929 0.1017  -0.0948 225 ARG B N   
5875 C CA  . ARG B 198 ? 1.0534 0.6055 0.7450 -0.0964 0.1045  -0.0825 225 ARG B CA  
5876 C C   . ARG B 198 ? 1.0921 0.6669 0.7867 -0.0758 0.0982  -0.0708 225 ARG B C   
5877 O O   . ARG B 198 ? 1.1934 0.8004 0.8966 -0.0693 0.0892  -0.0746 225 ARG B O   
5878 C CB  . ARG B 198 ? 0.9590 0.5462 0.6705 -0.1162 0.1024  -0.0898 225 ARG B CB  
5879 C CG  . ARG B 198 ? 1.2512 0.8203 0.9632 -0.1403 0.1088  -0.1018 225 ARG B CG  
5880 C CD  . ARG B 198 ? 1.5756 1.1893 1.3102 -0.1575 0.1031  -0.1114 225 ARG B CD  
5881 N NE  . ARG B 198 ? 1.5552 1.2016 1.3062 -0.1564 0.1034  -0.1004 225 ARG B NE  
5882 C CZ  . ARG B 198 ? 1.3978 1.0897 1.1706 -0.1657 0.0978  -0.1051 225 ARG B CZ  
5883 N NH1 . ARG B 198 ? 1.3245 1.0376 1.1060 -0.1772 0.0902  -0.1205 225 ARG B NH1 
5884 N NH2 . ARG B 198 ? 1.1793 0.8964 0.9650 -0.1625 0.0998  -0.0943 225 ARG B NH2 
5885 N N   . ARG B 199 ? 0.9060 0.4630 0.5923 -0.0657 0.1028  -0.0567 226 ARG B N   
5886 C CA  . ARG B 199 ? 1.0553 0.6313 0.7438 -0.0478 0.0971  -0.0456 226 ARG B CA  
5887 C C   . ARG B 199 ? 1.0227 0.6193 0.7209 -0.0529 0.0989  -0.0371 226 ARG B C   
5888 O O   . ARG B 199 ? 0.9878 0.5727 0.6858 -0.0666 0.1072  -0.0353 226 ARG B O   
5889 C CB  . ARG B 199 ? 1.1085 0.6529 0.7802 -0.0303 0.0992  -0.0362 226 ARG B CB  
5890 C CG  . ARG B 199 ? 1.0292 0.5574 0.6925 -0.0206 0.0972  -0.0437 226 ARG B CG  
5891 C CD  . ARG B 199 ? 1.3086 0.8113 0.9581 -0.0011 0.0984  -0.0336 226 ARG B CD  
5892 N NE  . ARG B 199 ? 1.6412 1.1305 1.2841 0.0093  0.0974  -0.0409 226 ARG B NE  
5893 C CZ  . ARG B 199 ? 1.7558 1.2668 1.4041 0.0235  0.0907  -0.0417 226 ARG B CZ  
5894 N NH1 . ARG B 199 ? 1.6278 1.1733 1.2880 0.0286  0.0839  -0.0358 226 ARG B NH1 
5895 N NH2 . ARG B 199 ? 1.6328 1.1297 1.2743 0.0326  0.0916  -0.0488 226 ARG B NH2 
5896 N N   . GLY B 200 ? 1.0291 0.6554 0.7353 -0.0420 0.0920  -0.0320 227 GLY B N   
5897 C CA  . GLY B 200 ? 0.9895 0.6366 0.7042 -0.0440 0.0932  -0.0244 227 GLY B CA  
5898 C C   . GLY B 200 ? 0.9587 0.6470 0.6891 -0.0407 0.0848  -0.0273 227 GLY B C   
5899 O O   . GLY B 200 ? 0.9463 0.6456 0.6785 -0.0339 0.0776  -0.0327 227 GLY B O   
5900 N N   . CYS B 201 ? 0.9486 0.6590 0.6894 -0.0447 0.0864  -0.0232 228 CYS B N   
5901 C CA  . CYS B 201 ? 0.9101 0.6589 0.6660 -0.0416 0.0796  -0.0250 228 CYS B CA  
5902 C C   . CYS B 201 ? 0.8077 0.5796 0.5799 -0.0577 0.0816  -0.0322 228 CYS B C   
5903 O O   . CYS B 201 ? 0.9669 0.7378 0.7431 -0.0672 0.0896  -0.0290 228 CYS B O   
5904 C CB  . CYS B 201 ? 0.7613 0.5187 0.5164 -0.0307 0.0795  -0.0145 228 CYS B CB  
5905 S SG  . CYS B 201 ? 1.4595 1.1976 1.1990 -0.0122 0.0751  -0.0069 228 CYS B SG  
5906 N N   . PHE B 202 ? 0.8468 0.6410 0.6285 -0.0607 0.0743  -0.0417 229 PHE B N   
5907 C CA  . PHE B 202 ? 0.9518 0.7687 0.7493 -0.0769 0.0743  -0.0507 229 PHE B CA  
5908 C C   . PHE B 202 ? 0.8636 0.7231 0.6778 -0.0723 0.0677  -0.0504 229 PHE B C   
5909 O O   . PHE B 202 ? 0.8666 0.7375 0.6786 -0.0587 0.0601  -0.0487 229 PHE B O   
5910 C CB  . PHE B 202 ? 0.8109 0.6196 0.6048 -0.0856 0.0707  -0.0635 229 PHE B CB  
5911 C CG  . PHE B 202 ? 0.8785 0.6427 0.6546 -0.0881 0.0771  -0.0642 229 PHE B CG  
5912 C CD1 . PHE B 202 ? 0.9246 0.6684 0.7000 -0.1047 0.0864  -0.0665 229 PHE B CD1 
5913 C CD2 . PHE B 202 ? 0.9255 0.6681 0.6860 -0.0735 0.0746  -0.0619 229 PHE B CD2 
5914 C CE1 . PHE B 202 ? 1.0323 0.7320 0.7898 -0.1058 0.0928  -0.0663 229 PHE B CE1 
5915 C CE2 . PHE B 202 ? 1.0188 0.7205 0.7632 -0.0737 0.0806  -0.0620 229 PHE B CE2 
5916 C CZ  . PHE B 202 ? 1.0736 0.7523 0.8154 -0.0894 0.0897  -0.0640 229 PHE B CZ  
5917 N N   . ALA B 203 ? 0.9503 0.8330 0.7813 -0.0833 0.0713  -0.0518 230 ALA B N   
5918 C CA  . ALA B 203 ? 0.9058 0.8310 0.7546 -0.0792 0.0652  -0.0523 230 ALA B CA  
5919 C C   . ALA B 203 ? 0.8571 0.8029 0.7116 -0.0832 0.0549  -0.0635 230 ALA B C   
5920 O O   . ALA B 203 ? 0.8423 0.7859 0.7001 -0.0992 0.0551  -0.0739 230 ALA B O   
5921 C CB  . ALA B 203 ? 0.7435 0.6894 0.6102 -0.0898 0.0726  -0.0510 230 ALA B CB  
5922 N N   . VAL B 204 ? 0.8131 0.7773 0.6671 -0.0689 0.0460  -0.0617 231 VAL B N   
5923 C CA  . VAL B 204 ? 0.7640 0.7472 0.6195 -0.0700 0.0355  -0.0713 231 VAL B CA  
5924 C C   . VAL B 204 ? 0.7699 0.7917 0.6376 -0.0593 0.0282  -0.0678 231 VAL B C   
5925 O O   . VAL B 204 ? 0.7522 0.7777 0.6212 -0.0466 0.0304  -0.0573 231 VAL B O   
5926 C CB  . VAL B 204 ? 0.7608 0.7183 0.5958 -0.0616 0.0322  -0.0728 231 VAL B CB  
5927 C CG1 . VAL B 204 ? 0.7254 0.6477 0.5491 -0.0729 0.0381  -0.0793 231 VAL B CG1 
5928 C CG2 . VAL B 204 ? 0.7091 0.6540 0.5348 -0.0440 0.0339  -0.0606 231 VAL B CG2 
5929 N N   . PRO B 205 ? 0.7491 0.7997 0.6247 -0.0638 0.0189  -0.0767 232 PRO B N   
5930 C CA  . PRO B 205 ? 0.7322 0.8203 0.6187 -0.0522 0.0111  -0.0729 232 PRO B CA  
5931 C C   . PRO B 205 ? 0.7051 0.7881 0.5762 -0.0342 0.0054  -0.0670 232 PRO B C   
5932 O O   . PRO B 205 ? 0.7546 0.8636 0.6317 -0.0224 -0.0001 -0.0618 232 PRO B O   
5933 C CB  . PRO B 205 ? 0.7222 0.8421 0.6215 -0.0650 0.0027  -0.0855 232 PRO B CB  
5934 C CG  . PRO B 205 ? 0.8362 0.9284 0.7210 -0.0773 0.0029  -0.0963 232 PRO B CG  
5935 C CD  . PRO B 205 ? 0.8100 0.8612 0.6858 -0.0806 0.0152  -0.0911 232 PRO B CD  
5936 N N   . MET B 206 ? 0.7117 0.7624 0.5635 -0.0314 0.0071  -0.0672 233 MET B N   
5937 C CA  . MET B 206 ? 0.6777 0.7248 0.5156 -0.0161 0.0025  -0.0624 233 MET B CA  
5938 C C   . MET B 206 ? 0.8796 0.8889 0.7008 -0.0122 0.0083  -0.0592 233 MET B C   
5939 O O   . MET B 206 ? 0.8655 0.8536 0.6792 -0.0213 0.0109  -0.0667 233 MET B O   
5940 C CB  . MET B 206 ? 0.7632 0.8283 0.5960 -0.0175 -0.0074 -0.0715 233 MET B CB  
5941 C CG  . MET B 206 ? 0.8467 0.9030 0.6617 -0.0036 -0.0104 -0.0673 233 MET B CG  
5942 S SD  . MET B 206 ? 0.8233 0.8977 0.6410 0.0153  -0.0128 -0.0528 233 MET B SD  
5943 C CE  . MET B 206 ? 0.7811 0.9006 0.6110 0.0140  -0.0240 -0.0580 233 MET B CE  
5944 N N   . VAL B 207 ? 0.7632 0.7645 0.5793 0.0015  0.0103  -0.0484 234 VAL B N   
5945 C CA  . VAL B 207 ? 0.7975 0.7708 0.5989 0.0082  0.0135  -0.0449 234 VAL B CA  
5946 C C   . VAL B 207 ? 0.7868 0.7685 0.5829 0.0224  0.0101  -0.0375 234 VAL B C   
5947 O O   . VAL B 207 ? 0.7369 0.7377 0.5404 0.0288  0.0079  -0.0316 234 VAL B O   
5948 C CB  . VAL B 207 ? 0.6734 0.6224 0.4739 0.0081  0.0214  -0.0387 234 VAL B CB  
5949 C CG1 . VAL B 207 ? 0.6886 0.6223 0.4898 -0.0056 0.0260  -0.0454 234 VAL B CG1 
5950 C CG2 . VAL B 207 ? 0.7148 0.6757 0.5247 0.0132  0.0233  -0.0302 234 VAL B CG2 
5951 N N   . HIS B 208 ? 0.7877 0.7546 0.5711 0.0276  0.0104  -0.0375 235 HIS B N   
5952 C CA  . HIS B 208 ? 0.7198 0.6932 0.4969 0.0396  0.0082  -0.0307 235 HIS B CA  
5953 C C   . HIS B 208 ? 0.6531 0.6040 0.4200 0.0444  0.0123  -0.0284 235 HIS B C   
5954 O O   . HIS B 208 ? 0.7265 0.6575 0.4924 0.0406  0.0166  -0.0303 235 HIS B O   
5955 C CB  . HIS B 208 ? 0.6521 0.6472 0.4251 0.0405  0.0011  -0.0358 235 HIS B CB  
5956 C CG  . HIS B 208 ? 0.7253 0.7139 0.4891 0.0332  -0.0003 -0.0475 235 HIS B CG  
5957 N ND1 . HIS B 208 ? 0.7296 0.7049 0.4794 0.0382  0.0016  -0.0487 235 HIS B ND1 
5958 C CD2 . HIS B 208 ? 0.6111 0.6040 0.3775 0.0211  -0.0029 -0.0591 235 HIS B CD2 
5959 C CE1 . HIS B 208 ? 0.8231 0.7936 0.5659 0.0304  0.0003  -0.0608 235 HIS B CE1 
5960 N NE2 . HIS B 208 ? 0.6076 0.5877 0.3600 0.0194  -0.0027 -0.0675 235 HIS B NE2 
5961 N N   . SER B 209 ? 0.7220 0.6771 0.4818 0.0533  0.0114  -0.0237 236 SER B N   
5962 C CA  . SER B 209 ? 0.7892 0.7288 0.5413 0.0586  0.0154  -0.0212 236 SER B CA  
5963 C C   . SER B 209 ? 0.7112 0.6368 0.4684 0.0612  0.0196  -0.0136 236 SER B C   
5964 O O   . SER B 209 ? 0.8608 0.7888 0.6192 0.0674  0.0203  -0.0053 236 SER B O   
5965 C CB  . SER B 209 ? 0.7027 0.6300 0.4474 0.0540  0.0170  -0.0310 236 SER B CB  
5966 O OG  . SER B 209 ? 0.9249 0.8649 0.6627 0.0514  0.0127  -0.0390 236 SER B OG  
5967 N N   . THR B 210 ? 0.7885 0.6983 0.5475 0.0565  0.0222  -0.0165 237 THR B N   
5968 C CA  . THR B 210 ? 0.6808 0.5778 0.4432 0.0586  0.0251  -0.0102 237 THR B CA  
5969 C C   . THR B 210 ? 0.7633 0.6577 0.5312 0.0525  0.0258  -0.0105 237 THR B C   
5970 O O   . THR B 210 ? 0.7600 0.6475 0.5273 0.0453  0.0268  -0.0167 237 THR B O   
5971 C CB  . THR B 210 ? 0.7497 0.6297 0.5080 0.0606  0.0279  -0.0116 237 THR B CB  
5972 O OG1 . THR B 210 ? 0.8033 0.6877 0.5583 0.0668  0.0286  -0.0101 237 THR B OG1 
5973 C CG2 . THR B 210 ? 0.7289 0.5970 0.4902 0.0622  0.0294  -0.0057 237 THR B CG2 
5974 N N   . PHE B 211 ? 0.7320 0.6310 0.5046 0.0550  0.0260  -0.0040 238 PHE B N   
5975 C CA  . PHE B 211 ? 0.7202 0.6180 0.4977 0.0500  0.0280  -0.0036 238 PHE B CA  
5976 C C   . PHE B 211 ? 0.7350 0.6275 0.5130 0.0550  0.0297  0.0038  238 PHE B C   
5977 O O   . PHE B 211 ? 0.6188 0.5124 0.3953 0.0615  0.0286  0.0084  238 PHE B O   
5978 C CB  . PHE B 211 ? 0.6234 0.5418 0.4083 0.0459  0.0260  -0.0070 238 PHE B CB  
5979 C CG  . PHE B 211 ? 0.8197 0.7562 0.6069 0.0533  0.0227  -0.0031 238 PHE B CG  
5980 C CD1 . PHE B 211 ? 0.7660 0.7114 0.5485 0.0562  0.0189  -0.0052 238 PHE B CD1 
5981 C CD2 . PHE B 211 ? 0.7145 0.6579 0.5068 0.0580  0.0237  0.0029  238 PHE B CD2 
5982 C CE1 . PHE B 211 ? 0.8493 0.8096 0.6318 0.0638  0.0161  -0.0003 238 PHE B CE1 
5983 C CE2 . PHE B 211 ? 0.8042 0.7616 0.5973 0.0661  0.0211  0.0072  238 PHE B CE2 
5984 C CZ  . PHE B 211 ? 0.8743 0.8399 0.6622 0.0690  0.0171  0.0061  238 PHE B CZ  
5985 N N   . LEU B 212 ? 0.6740 0.5597 0.4531 0.0514  0.0328  0.0048  239 LEU B N   
5986 C CA  . LEU B 212 ? 0.6464 0.5240 0.4232 0.0552  0.0347  0.0105  239 LEU B CA  
5987 C C   . LEU B 212 ? 0.6466 0.5348 0.4291 0.0541  0.0374  0.0116  239 LEU B C   
5988 O O   . LEU B 212 ? 0.6987 0.5903 0.4851 0.0472  0.0401  0.0085  239 LEU B O   
5989 C CB  . LEU B 212 ? 0.6928 0.5502 0.4624 0.0535  0.0366  0.0113  239 LEU B CB  
5990 C CG  . LEU B 212 ? 0.6663 0.5144 0.4310 0.0568  0.0380  0.0162  239 LEU B CG  
5991 C CD1 . LEU B 212 ? 0.6833 0.5286 0.4459 0.0628  0.0345  0.0190  239 LEU B CD1 
5992 C CD2 . LEU B 212 ? 0.6219 0.4529 0.3789 0.0538  0.0407  0.0169  239 LEU B CD2 
5993 N N   . ILE B 213 ? 0.5604 0.4535 0.3438 0.0608  0.0373  0.0158  240 ILE B N   
5994 C CA  . ILE B 213 ? 0.5920 0.4949 0.3806 0.0623  0.0406  0.0174  240 ILE B CA  
5995 C C   . ILE B 213 ? 0.7359 0.6228 0.5169 0.0643  0.0443  0.0205  240 ILE B C   
5996 O O   . ILE B 213 ? 0.6737 0.5484 0.4476 0.0683  0.0425  0.0229  240 ILE B O   
5997 C CB  . ILE B 213 ? 0.6624 0.5810 0.4559 0.0699  0.0385  0.0198  240 ILE B CB  
5998 C CG1 . ILE B 213 ? 0.5031 0.4376 0.3012 0.0686  0.0337  0.0167  240 ILE B CG1 
5999 C CG2 . ILE B 213 ? 0.5022 0.4328 0.3027 0.0729  0.0424  0.0211  240 ILE B CG2 
6000 C CD1 . ILE B 213 ? 0.6292 0.5803 0.4309 0.0772  0.0311  0.0200  240 ILE B CD1 
6001 N N   . ASP B 214 ? 0.7360 0.6237 0.5182 0.0610  0.0496  0.0202  241 ASP B N   
6002 C CA  . ASP B 214 ? 0.7611 0.6340 0.5339 0.0628  0.0537  0.0227  241 ASP B CA  
6003 C C   . ASP B 214 ? 0.7169 0.5977 0.4923 0.0701  0.0566  0.0246  241 ASP B C   
6004 O O   . ASP B 214 ? 0.7374 0.6324 0.5209 0.0699  0.0613  0.0241  241 ASP B O   
6005 C CB  . ASP B 214 ? 0.7920 0.6592 0.5623 0.0554  0.0593  0.0219  241 ASP B CB  
6006 C CG  . ASP B 214 ? 0.8773 0.7271 0.6339 0.0574  0.0631  0.0247  241 ASP B CG  
6007 O OD1 . ASP B 214 ? 0.8936 0.7367 0.6435 0.0639  0.0611  0.0261  241 ASP B OD1 
6008 O OD2 . ASP B 214 ? 0.9100 0.7518 0.6612 0.0520  0.0683  0.0254  241 ASP B OD2 
6009 N N   . LEU B 215 ? 0.6288 0.4999 0.3976 0.0764  0.0542  0.0266  242 LEU B N   
6010 C CA  . LEU B 215 ? 0.6895 0.5627 0.4582 0.0844  0.0572  0.0284  242 LEU B CA  
6011 C C   . LEU B 215 ? 0.7275 0.5897 0.4871 0.0855  0.0634  0.0283  242 LEU B C   
6012 O O   . LEU B 215 ? 0.7977 0.6592 0.5556 0.0928  0.0671  0.0290  242 LEU B O   
6013 C CB  . LEU B 215 ? 0.6439 0.5077 0.4078 0.0895  0.0531  0.0304  242 LEU B CB  
6014 C CG  . LEU B 215 ? 0.6702 0.5444 0.4408 0.0894  0.0480  0.0312  242 LEU B CG  
6015 C CD1 . LEU B 215 ? 0.6287 0.4916 0.3938 0.0931  0.0456  0.0338  242 LEU B CD1 
6016 C CD2 . LEU B 215 ? 0.6436 0.5400 0.4253 0.0932  0.0485  0.0317  242 LEU B CD2 
6017 N N   . ARG B 216 ? 0.7724 0.6247 0.5244 0.0793  0.0651  0.0275  243 ARG B N   
6018 C CA  . ARG B 216 ? 0.6219 0.4662 0.3645 0.0799  0.0721  0.0275  243 ARG B CA  
6019 C C   . ARG B 216 ? 0.7857 0.6482 0.5395 0.0788  0.0799  0.0273  243 ARG B C   
6020 O O   . ARG B 216 ? 0.7543 0.6168 0.5046 0.0832  0.0872  0.0274  243 ARG B O   
6021 C CB  . ARG B 216 ? 0.6695 0.4967 0.3985 0.0744  0.0714  0.0279  243 ARG B CB  
6022 C CG  . ARG B 216 ? 0.7139 0.5271 0.4344 0.0749  0.0631  0.0278  243 ARG B CG  
6023 C CD  . ARG B 216 ? 0.7027 0.5023 0.4118 0.0707  0.0614  0.0289  243 ARG B CD  
6024 N NE  . ARG B 216 ? 0.7424 0.5474 0.4583 0.0647  0.0638  0.0295  243 ARG B NE  
6025 C CZ  . ARG B 216 ? 0.9129 0.7114 0.6219 0.0606  0.0700  0.0312  243 ARG B CZ  
6026 N NH1 . ARG B 216 ? 0.8846 0.6718 0.5782 0.0626  0.0743  0.0328  243 ARG B NH1 
6027 N NH2 . ARG B 216 ? 0.6546 0.4569 0.3710 0.0540  0.0724  0.0311  243 ARG B NH2 
6028 N N   . LYS B 217 ? 0.7380 0.6168 0.5057 0.0729  0.0786  0.0264  244 LYS B N   
6029 C CA  . LYS B 217 ? 0.6418 0.5412 0.4231 0.0697  0.0855  0.0255  244 LYS B CA  
6030 C C   . LYS B 217 ? 0.6659 0.5842 0.4584 0.0794  0.0873  0.0260  244 LYS B C   
6031 O O   . LYS B 217 ? 0.7914 0.7129 0.5864 0.0863  0.0812  0.0267  244 LYS B O   
6032 C CB  . LYS B 217 ? 0.7600 0.6722 0.5535 0.0600  0.0822  0.0232  244 LYS B CB  
6033 C CG  . LYS B 217 ? 0.7773 0.6696 0.5601 0.0512  0.0814  0.0230  244 LYS B CG  
6034 C CD  . LYS B 217 ? 0.7303 0.6077 0.5009 0.0482  0.0900  0.0253  244 LYS B CD  
6035 C CE  . LYS B 217 ? 0.8447 0.7116 0.6120 0.0371  0.0925  0.0252  244 LYS B CE  
6036 N NZ  . LYS B 217 ? 0.7879 0.6404 0.5488 0.0364  0.0841  0.0245  244 LYS B NZ  
6037 N N   . ALA B 218 ? 0.7535 0.6842 0.5524 0.0807  0.0965  0.0259  245 ALA B N   
6038 C CA  . ALA B 218 ? 0.6362 0.5857 0.4462 0.0918  0.0992  0.0266  245 ALA B CA  
6039 C C   . ALA B 218 ? 0.6199 0.5977 0.4500 0.0923  0.0929  0.0259  245 ALA B C   
6040 O O   . ALA B 218 ? 0.7679 0.7552 0.6030 0.1037  0.0899  0.0277  245 ALA B O   
6041 C CB  . ALA B 218 ? 0.5469 0.5062 0.3611 0.0927  0.1115  0.0265  245 ALA B CB  
6042 N N   . ALA B 219 ? 0.6337 0.6241 0.4739 0.0801  0.0907  0.0233  246 ALA B N   
6043 C CA  . ALA B 219 ? 0.6781 0.6970 0.5364 0.0792  0.0840  0.0214  246 ALA B CA  
6044 C C   . ALA B 219 ? 0.7178 0.7292 0.5695 0.0841  0.0734  0.0224  246 ALA B C   
6045 O O   . ALA B 219 ? 0.6242 0.6582 0.4873 0.0882  0.0674  0.0222  246 ALA B O   
6046 C CB  . ALA B 219 ? 0.5754 0.6063 0.4445 0.0632  0.0845  0.0170  246 ALA B CB  
6047 N N   . SER B 220 ? 0.6721 0.6540 0.5058 0.0838  0.0713  0.0237  247 SER B N   
6048 C CA  . SER B 220 ? 0.6755 0.6501 0.5031 0.0880  0.0629  0.0251  247 SER B CA  
6049 C C   . SER B 220 ? 0.7506 0.7299 0.5785 0.1024  0.0617  0.0293  247 SER B C   
6050 O O   . SER B 220 ? 0.6761 0.6587 0.5033 0.1065  0.0552  0.0310  247 SER B O   
6051 C CB  . SER B 220 ? 0.6393 0.5836 0.4497 0.0847  0.0616  0.0256  247 SER B CB  
6052 O OG  . SER B 220 ? 0.6887 0.6151 0.4880 0.0906  0.0663  0.0279  247 SER B OG  
6053 N N   . ARG B 221 ? 0.6615 0.6397 0.4893 0.1106  0.0687  0.0311  248 ARG B N   
6054 C CA  . ARG B 221 ? 0.7253 0.7052 0.5526 0.1254  0.0686  0.0354  248 ARG B CA  
6055 C C   . ARG B 221 ? 0.7051 0.7167 0.5483 0.1314  0.0638  0.0366  248 ARG B C   
6056 O O   . ARG B 221 ? 0.6574 0.6693 0.4983 0.1438  0.0611  0.0413  248 ARG B O   
6057 C CB  . ARG B 221 ? 0.6723 0.6457 0.4967 0.1334  0.0781  0.0360  248 ARG B CB  
6058 C CG  . ARG B 221 ? 0.7375 0.6800 0.5439 0.1286  0.0824  0.0344  248 ARG B CG  
6059 C CD  . ARG B 221 ? 0.7792 0.7136 0.5798 0.1380  0.0918  0.0344  248 ARG B CD  
6060 N NE  . ARG B 221 ? 1.0258 0.9523 0.8225 0.1522  0.0917  0.0376  248 ARG B NE  
6061 C CZ  . ARG B 221 ? 1.1141 1.0111 0.8940 0.1545  0.0903  0.0383  248 ARG B CZ  
6062 N NH1 . ARG B 221 ? 0.8428 0.7183 0.6094 0.1442  0.0877  0.0358  248 ARG B NH1 
6063 N NH2 . ARG B 221 ? 0.9568 0.8458 0.7334 0.1674  0.0913  0.0417  248 ARG B NH2 
6064 N N   . ASN B 222 ? 0.6597 0.6977 0.5184 0.1228  0.0623  0.0327  249 ASN B N   
6065 C CA  . ASN B 222 ? 0.5471 0.6196 0.4223 0.1274  0.0566  0.0328  249 ASN B CA  
6066 C C   . ASN B 222 ? 0.6207 0.6984 0.4940 0.1212  0.0465  0.0309  249 ASN B C   
6067 O O   . ASN B 222 ? 0.5861 0.6918 0.4702 0.1254  0.0399  0.0309  249 ASN B O   
6068 C CB  . ASN B 222 ? 0.6641 0.7666 0.5597 0.1208  0.0608  0.0285  249 ASN B CB  
6069 C CG  . ASN B 222 ? 0.7302 0.8329 0.6292 0.1289  0.0717  0.0304  249 ASN B CG  
6070 O OD1 . ASN B 222 ? 0.7088 0.8059 0.6032 0.1449  0.0737  0.0351  249 ASN B OD1 
6071 N ND2 . ASN B 222 ? 0.7610 0.8686 0.6669 0.1181  0.0796  0.0268  249 ASN B ND2 
6072 N N   . LEU B 223 ? 0.5949 0.6477 0.4547 0.1121  0.0450  0.0292  250 LEU B N   
6073 C CA  . LEU B 223 ? 0.6702 0.7252 0.5261 0.1073  0.0366  0.0273  250 LEU B CA  
6074 C C   . LEU B 223 ? 0.6355 0.6847 0.4817 0.1202  0.0324  0.0338  250 LEU B C   
6075 O O   . LEU B 223 ? 0.5943 0.6232 0.4309 0.1288  0.0364  0.0391  250 LEU B O   
6076 C CB  . LEU B 223 ? 0.5694 0.5994 0.4143 0.0952  0.0374  0.0239  250 LEU B CB  
6077 C CG  . LEU B 223 ? 0.7338 0.7622 0.5841 0.0824  0.0426  0.0188  250 LEU B CG  
6078 C CD1 . LEU B 223 ? 0.5842 0.5839 0.4208 0.0744  0.0434  0.0173  250 LEU B CD1 
6079 C CD2 . LEU B 223 ? 0.6139 0.6705 0.4795 0.0734  0.0392  0.0127  250 LEU B CD2 
6080 N N   . ALA B 224 ? 0.5494 0.6157 0.3968 0.1210  0.0244  0.0331  251 ALA B N   
6081 C CA  . ALA B 224 ? 0.5753 0.6369 0.4121 0.1330  0.0206  0.0400  251 ALA B CA  
6082 C C   . ALA B 224 ? 0.6000 0.6710 0.4322 0.1281  0.0127  0.0370  251 ALA B C   
6083 O O   . ALA B 224 ? 0.6632 0.7597 0.5057 0.1218  0.0075  0.0307  251 ALA B O   
6084 C CB  . ALA B 224 ? 0.5063 0.5875 0.3506 0.1488  0.0199  0.0458  251 ALA B CB  
6085 N N   . PHE B 225 ? 0.6123 0.6628 0.4289 0.1302  0.0123  0.0409  252 PHE B N   
6086 C CA  . PHE B 225 ? 0.5206 0.5793 0.3298 0.1283  0.0057  0.0391  252 PHE B CA  
6087 C C   . PHE B 225 ? 0.5632 0.6404 0.3697 0.1421  0.0001  0.0456  252 PHE B C   
6088 O O   . PHE B 225 ? 0.6908 0.7861 0.4946 0.1411  -0.0072 0.0426  252 PHE B O   
6089 C CB  . PHE B 225 ? 0.5808 0.6121 0.3752 0.1250  0.0086  0.0409  252 PHE B CB  
6090 C CG  . PHE B 225 ? 0.7565 0.7715 0.5523 0.1124  0.0123  0.0345  252 PHE B CG  
6091 C CD1 . PHE B 225 ? 0.5824 0.6015 0.3783 0.1019  0.0095  0.0262  252 PHE B CD1 
6092 C CD2 . PHE B 225 ? 0.5989 0.5933 0.3944 0.1117  0.0186  0.0367  252 PHE B CD2 
6093 C CE1 . PHE B 225 ? 0.6548 0.6573 0.4508 0.0921  0.0131  0.0213  252 PHE B CE1 
6094 C CE2 . PHE B 225 ? 0.6973 0.6774 0.4928 0.1015  0.0213  0.0318  252 PHE B CE2 
6095 C CZ  . PHE B 225 ? 0.6867 0.6705 0.4826 0.0923  0.0187  0.0246  252 PHE B CZ  
6096 N N   . TYR B 226 ? 0.6236 0.6956 0.4293 0.1555  0.0035  0.0544  253 TYR B N   
6097 C CA  . TYR B 226 ? 0.5901 0.6761 0.3913 0.1711  -0.0011 0.0625  253 TYR B CA  
6098 C C   . TYR B 226 ? 0.7297 0.8138 0.5369 0.1845  0.0037  0.0692  253 TYR B C   
6099 O O   . TYR B 226 ? 0.7463 0.8048 0.5515 0.1829  0.0120  0.0703  253 TYR B O   
6100 C CB  . TYR B 226 ? 0.5906 0.6564 0.3713 0.1758  -0.0006 0.0699  253 TYR B CB  
6101 C CG  . TYR B 226 ? 0.6704 0.7534 0.4433 0.1900  -0.0072 0.0774  253 TYR B CG  
6102 C CD1 . TYR B 226 ? 0.7144 0.8233 0.4860 0.1872  -0.0167 0.0723  253 TYR B CD1 
6103 C CD2 . TYR B 226 ? 0.6653 0.7380 0.4309 0.2068  -0.0042 0.0894  253 TYR B CD2 
6104 C CE1 . TYR B 226 ? 0.7531 0.8791 0.5158 0.2010  -0.0237 0.0794  253 TYR B CE1 
6105 C CE2 . TYR B 226 ? 0.7478 0.8357 0.5047 0.2214  -0.0105 0.0975  253 TYR B CE2 
6106 C CZ  . TYR B 226 ? 0.7891 0.9047 0.5443 0.2186  -0.0206 0.0926  253 TYR B CZ  
6107 O OH  . TYR B 226 ? 0.9268 1.0584 0.6715 0.2339  -0.0277 0.1009  253 TYR B OH  
6108 N N   . PRO B 227 ? 0.7538 0.8644 0.5682 0.1981  -0.0012 0.0734  254 PRO B N   
6109 C CA  . PRO B 227 ? 0.7421 0.8878 0.5605 0.2008  -0.0123 0.0715  254 PRO B CA  
6110 C C   . PRO B 227 ? 0.7446 0.9192 0.5830 0.1866  -0.0163 0.0592  254 PRO B C   
6111 O O   . PRO B 227 ? 0.6740 0.8405 0.5223 0.1768  -0.0095 0.0539  254 PRO B O   
6112 C CB  . PRO B 227 ? 0.5695 0.7291 0.3900 0.2225  -0.0141 0.0817  254 PRO B CB  
6113 C CG  . PRO B 227 ? 0.6316 0.7782 0.4614 0.2265  -0.0043 0.0829  254 PRO B CG  
6114 C CD  . PRO B 227 ? 0.7471 0.8541 0.5656 0.2138  0.0042  0.0806  254 PRO B CD  
6115 N N   . PRO B 228 ? 0.7241 0.9312 0.5677 0.1842  -0.0269 0.0540  255 PRO B N   
6116 C CA  . PRO B 228 ? 0.7409 0.9768 0.6056 0.1699  -0.0303 0.0421  255 PRO B CA  
6117 C C   . PRO B 228 ? 0.7000 0.9542 0.5867 0.1755  -0.0257 0.0430  255 PRO B C   
6118 O O   . PRO B 228 ? 0.7762 1.0344 0.6640 0.1939  -0.0242 0.0524  255 PRO B O   
6119 C CB  . PRO B 228 ? 0.6459 0.9158 0.5108 0.1710  -0.0438 0.0384  255 PRO B CB  
6120 C CG  . PRO B 228 ? 0.6156 0.8633 0.4537 0.1781  -0.0458 0.0452  255 PRO B CG  
6121 C CD  . PRO B 228 ? 0.6634 0.8795 0.4915 0.1916  -0.0361 0.0578  255 PRO B CD  
6122 N N   . HIS B 229 ? 0.6258 0.8896 0.5292 0.1594  -0.0224 0.0334  256 HIS B N   
6123 C CA  . HIS B 229 ? 0.5614 0.8454 0.4871 0.1623  -0.0168 0.0331  256 HIS B CA  
6124 C C   . HIS B 229 ? 0.6292 0.9587 0.5712 0.1761  -0.0257 0.0355  256 HIS B C   
6125 O O   . HIS B 229 ? 0.6157 0.9688 0.5569 0.1752  -0.0377 0.0325  256 HIS B O   
6126 C CB  . HIS B 229 ? 0.5867 0.8767 0.5271 0.1406  -0.0128 0.0220  256 HIS B CB  
6127 C CG  . HIS B 229 ? 0.6275 0.9330 0.5888 0.1415  -0.0040 0.0217  256 HIS B CG  
6128 N ND1 . HIS B 229 ? 0.7065 1.0587 0.6938 0.1437  -0.0079 0.0189  256 HIS B ND1 
6129 C CD2 . HIS B 229 ? 0.5133 0.7950 0.4733 0.1407  0.0086  0.0238  256 HIS B CD2 
6130 C CE1 . HIS B 229 ? 0.5840 0.9404 0.5856 0.1443  0.0031  0.0195  256 HIS B CE1 
6131 N NE2 . HIS B 229 ? 0.5974 0.9105 0.5815 0.1426  0.0132  0.0224  256 HIS B NE2 
6132 N N   . PRO B 230 ? 0.6545 0.9974 0.6107 0.1902  -0.0202 0.0410  257 PRO B N   
6133 C CA  . PRO B 230 ? 0.5751 0.9637 0.5487 0.2057  -0.0286 0.0441  257 PRO B CA  
6134 C C   . PRO B 230 ? 0.5824 1.0185 0.5784 0.1918  -0.0389 0.0330  257 PRO B C   
6135 O O   . PRO B 230 ? 0.7355 1.2100 0.7405 0.2024  -0.0508 0.0344  257 PRO B O   
6136 C CB  . PRO B 230 ? 0.5276 0.9191 0.5155 0.2182  -0.0173 0.0488  257 PRO B CB  
6137 C CG  . PRO B 230 ? 0.5285 0.8658 0.4939 0.2186  -0.0056 0.0534  257 PRO B CG  
6138 C CD  . PRO B 230 ? 0.5192 0.8319 0.4716 0.1962  -0.0062 0.0460  257 PRO B CD  
6139 N N   . ASP B 231 ? 0.5930 1.0263 0.5976 0.1680  -0.0348 0.0221  258 ASP B N   
6140 C CA  . ASP B 231 ? 0.6077 1.0812 0.6332 0.1506  -0.0431 0.0100  258 ASP B CA  
6141 C C   . ASP B 231 ? 0.6516 1.1150 0.6601 0.1362  -0.0527 0.0023  258 ASP B C   
6142 O O   . ASP B 231 ? 0.6437 1.1351 0.6664 0.1192  -0.0599 -0.0094 258 ASP B O   
6143 C CB  . ASP B 231 ? 0.5313 1.0077 0.5769 0.1322  -0.0318 0.0026  258 ASP B CB  
6144 C CG  . ASP B 231 ? 0.5996 1.0965 0.6664 0.1453  -0.0228 0.0081  258 ASP B CG  
6145 O OD1 . ASP B 231 ? 0.7151 1.2458 0.7934 0.1643  -0.0297 0.0135  258 ASP B OD1 
6146 O OD2 . ASP B 231 ? 0.8157 1.2947 0.8866 0.1377  -0.0088 0.0074  258 ASP B OD2 
6147 N N   . TYR B 232 ? 0.6801 1.1042 0.6588 0.1421  -0.0525 0.0080  259 TYR B N   
6148 C CA  . TYR B 232 ? 0.6085 1.0207 0.5691 0.1299  -0.0601 0.0008  259 TYR B CA  
6149 C C   . TYR B 232 ? 0.7196 1.1715 0.6819 0.1361  -0.0765 -0.0016 259 TYR B C   
6150 O O   . TYR B 232 ? 0.6759 1.1420 0.6346 0.1577  -0.0819 0.0086  259 TYR B O   
6151 C CB  . TYR B 232 ? 0.5735 0.9370 0.5036 0.1364  -0.0548 0.0086  259 TYR B CB  
6152 C CG  . TYR B 232 ? 0.7337 1.0795 0.6445 0.1234  -0.0593 0.0011  259 TYR B CG  
6153 C CD1 . TYR B 232 ? 0.7979 1.1240 0.7090 0.1028  -0.0538 -0.0089 259 TYR B CD1 
6154 C CD2 . TYR B 232 ? 0.6565 1.0035 0.5472 0.1329  -0.0684 0.0044  259 TYR B CD2 
6155 C CE1 . TYR B 232 ? 0.8710 1.1798 0.7642 0.0923  -0.0571 -0.0161 259 TYR B CE1 
6156 C CE2 . TYR B 232 ? 0.7333 1.0640 0.6056 0.1219  -0.0715 -0.0029 259 TYR B CE2 
6157 C CZ  . TYR B 232 ? 0.7912 1.1029 0.6654 0.1019  -0.0658 -0.0135 259 TYR B CZ  
6158 O OH  . TYR B 232 ? 0.7854 1.0800 0.6412 0.0922  -0.0681 -0.0211 259 TYR B OH  
6159 N N   . THR B 233 ? 0.6849 1.1539 0.6513 0.1172  -0.0847 -0.0154 260 THR B N   
6160 C CA  . THR B 233 ? 0.7068 1.2154 0.6742 0.1203  -0.1017 -0.0202 260 THR B CA  
6161 C C   . THR B 233 ? 0.7024 1.1960 0.6483 0.1057  -0.1082 -0.0309 260 THR B C   
6162 O O   . THR B 233 ? 0.6943 1.2214 0.6436 0.0997  -0.1221 -0.0405 260 THR B O   
6163 C CB  . THR B 233 ? 0.6187 1.1813 0.6213 0.1123  -0.1082 -0.0288 260 THR B CB  
6164 O OG1 . THR B 233 ? 0.8067 1.3622 0.8239 0.0866  -0.1003 -0.0409 260 THR B OG1 
6165 C CG2 . THR B 233 ? 0.6077 1.1931 0.6307 0.1320  -0.1040 -0.0175 260 THR B CG2 
6166 N N   . TRP B 234 ? 0.7410 1.1862 0.6650 0.1001  -0.0987 -0.0299 261 TRP B N   
6167 C CA  . TRP B 234 ? 0.6243 1.0508 0.5278 0.0865  -0.1022 -0.0403 261 TRP B CA  
6168 C C   . TRP B 234 ? 0.7634 1.1676 0.6351 0.1023  -0.1042 -0.0309 261 TRP B C   
6169 O O   . TRP B 234 ? 0.9032 1.3113 0.7694 0.1232  -0.1052 -0.0170 261 TRP B O   
6170 C CB  . TRP B 234 ? 0.6333 1.0234 0.5370 0.0679  -0.0897 -0.0469 261 TRP B CB  
6171 C CG  . TRP B 234 ? 0.8826 1.2928 0.8146 0.0496  -0.0874 -0.0571 261 TRP B CG  
6172 C CD1 . TRP B 234 ? 0.9532 1.4111 0.9087 0.0432  -0.0972 -0.0652 261 TRP B CD1 
6173 C CD2 . TRP B 234 ? 0.8271 1.2109 0.7670 0.0351  -0.0740 -0.0599 261 TRP B CD2 
6174 N NE1 . TRP B 234 ? 0.9677 1.4299 0.9459 0.0244  -0.0897 -0.0729 261 TRP B NE1 
6175 C CE2 . TRP B 234 ? 0.8449 1.2608 0.8127 0.0196  -0.0753 -0.0694 261 TRP B CE2 
6176 C CE3 . TRP B 234 ? 0.8725 1.2097 0.7985 0.0338  -0.0613 -0.0551 261 TRP B CE3 
6177 C CZ2 . TRP B 234 ? 0.8742 1.2744 0.8543 0.0031  -0.0634 -0.0733 261 TRP B CZ2 
6178 C CZ3 . TRP B 234 ? 0.8320 1.1545 0.7696 0.0186  -0.0508 -0.0591 261 TRP B CZ3 
6179 C CH2 . TRP B 234 ? 0.9228 1.2753 0.8862 0.0035  -0.0513 -0.0678 261 TRP B CH2 
6180 N N   . SER B 235 ? 0.7859 1.1654 0.6362 0.0923  -0.1040 -0.0384 262 SER B N   
6181 C CA  . SER B 235 ? 0.6833 1.0441 0.5032 0.1051  -0.1055 -0.0309 262 SER B CA  
6182 C C   . SER B 235 ? 0.7532 1.0751 0.5627 0.1159  -0.0921 -0.0166 262 SER B C   
6183 O O   . SER B 235 ? 0.8507 1.1514 0.6711 0.1091  -0.0812 -0.0160 262 SER B O   
6184 C CB  . SER B 235 ? 0.6441 0.9900 0.4447 0.0911  -0.1078 -0.0442 262 SER B CB  
6185 O OG  . SER B 235 ? 1.1567 1.5379 0.9641 0.0808  -0.1213 -0.0584 262 SER B OG  
6186 N N   . PHE B 236 ? 0.8498 1.1623 0.6373 0.1325  -0.0930 -0.0049 263 PHE B N   
6187 C CA  . PHE B 236 ? 0.8666 1.1427 0.6425 0.1425  -0.0810 0.0087  263 PHE B CA  
6188 C C   . PHE B 236 ? 0.8895 1.1298 0.6524 0.1302  -0.0722 0.0032  263 PHE B C   
6189 O O   . PHE B 236 ? 0.9823 1.2037 0.7222 0.1355  -0.0696 0.0080  263 PHE B O   
6190 C CB  . PHE B 236 ? 0.7991 1.0760 0.5543 0.1627  -0.0844 0.0227  263 PHE B CB  
6191 C CG  . PHE B 236 ? 0.7197 0.9661 0.4689 0.1749  -0.0730 0.0382  263 PHE B CG  
6192 C CD1 . PHE B 236 ? 0.6145 0.8647 0.3810 0.1834  -0.0694 0.0455  263 PHE B CD1 
6193 C CD2 . PHE B 236 ? 0.8179 1.0321 0.5439 0.1776  -0.0655 0.0451  263 PHE B CD2 
6194 C CE1 . PHE B 236 ? 0.7314 0.9518 0.4912 0.1939  -0.0590 0.0585  263 PHE B CE1 
6195 C CE2 . PHE B 236 ? 0.9345 1.1205 0.6555 0.1871  -0.0551 0.0586  263 PHE B CE2 
6196 C CZ  . PHE B 236 ? 0.7958 0.9838 0.5331 0.1951  -0.0521 0.0650  263 PHE B CZ  
6197 N N   . ASP B 237 ? 0.8816 1.1128 0.6591 0.1143  -0.0670 -0.0064 264 ASP B N   
6198 C CA  . ASP B 237 ? 0.8521 1.0510 0.6205 0.1030  -0.0588 -0.0120 264 ASP B CA  
6199 C C   . ASP B 237 ? 0.8154 0.9899 0.5944 0.1018  -0.0473 -0.0061 264 ASP B C   
6200 O O   . ASP B 237 ? 0.9016 1.0871 0.7002 0.0995  -0.0461 -0.0063 264 ASP B O   
6201 C CB  . ASP B 237 ? 0.8434 1.0497 0.6166 0.0848  -0.0630 -0.0294 264 ASP B CB  
6202 C CG  . ASP B 237 ? 1.0291 1.2025 0.7886 0.0759  -0.0556 -0.0356 264 ASP B CG  
6203 O OD1 . ASP B 237 ? 1.2046 1.3516 0.9552 0.0822  -0.0469 -0.0267 264 ASP B OD1 
6204 O OD2 . ASP B 237 ? 1.0858 1.2602 0.8439 0.0624  -0.0585 -0.0498 264 ASP B OD2 
6205 N N   . ASP B 238 ? 0.7612 0.9039 0.5272 0.1030  -0.0389 -0.0015 265 ASP B N   
6206 C CA  . ASP B 238 ? 0.7231 0.8431 0.4959 0.1045  -0.0292 0.0058  265 ASP B CA  
6207 C C   . ASP B 238 ? 0.7664 0.8799 0.5538 0.0906  -0.0251 -0.0026 265 ASP B C   
6208 O O   . ASP B 238 ? 0.7576 0.8698 0.5579 0.0914  -0.0208 0.0012  265 ASP B O   
6209 C CB  . ASP B 238 ? 0.6276 0.7188 0.3842 0.1084  -0.0221 0.0123  265 ASP B CB  
6210 C CG  . ASP B 238 ? 0.8152 0.8938 0.5624 0.0986  -0.0206 0.0030  265 ASP B CG  
6211 O OD1 . ASP B 238 ? 0.7813 0.8738 0.5285 0.0908  -0.0267 -0.0081 265 ASP B OD1 
6212 O OD2 . ASP B 238 ? 0.8700 0.9249 0.6100 0.0988  -0.0134 0.0063  265 ASP B OD2 
6213 N N   . ILE B 239 ? 0.7715 0.8792 0.5557 0.0781  -0.0258 -0.0139 266 ILE B N   
6214 C CA  . ILE B 239 ? 0.6051 0.7022 0.4006 0.0650  -0.0210 -0.0208 266 ILE B CA  
6215 C C   . ILE B 239 ? 0.7079 0.8321 0.5223 0.0582  -0.0250 -0.0262 266 ILE B C   
6216 O O   . ILE B 239 ? 0.8157 0.9346 0.6426 0.0510  -0.0194 -0.0272 266 ILE B O   
6217 C CB  . ILE B 239 ? 0.7533 0.8327 0.5386 0.0545  -0.0197 -0.0309 266 ILE B CB  
6218 C CG1 . ILE B 239 ? 0.8029 0.9023 0.5838 0.0487  -0.0285 -0.0420 266 ILE B CG1 
6219 C CG2 . ILE B 239 ? 0.6183 0.6739 0.3877 0.0616  -0.0148 -0.0253 266 ILE B CG2 
6220 C CD1 . ILE B 239 ? 0.6959 0.7774 0.4686 0.0368  -0.0267 -0.0542 266 ILE B CD1 
6221 N N   . ILE B 240 ? 0.8123 0.9671 0.6294 0.0604  -0.0346 -0.0295 267 ILE B N   
6222 C CA  . ILE B 240 ? 0.6511 0.8372 0.4893 0.0546  -0.0389 -0.0343 267 ILE B CA  
6223 C C   . ILE B 240 ? 0.6859 0.8810 0.5368 0.0662  -0.0352 -0.0232 267 ILE B C   
6224 O O   . ILE B 240 ? 0.7559 0.9612 0.6253 0.0600  -0.0314 -0.0249 267 ILE B O   
6225 C CB  . ILE B 240 ? 0.7258 0.9449 0.5632 0.0546  -0.0517 -0.0411 267 ILE B CB  
6226 C CG1 . ILE B 240 ? 0.8773 1.0841 0.6985 0.0440  -0.0547 -0.0528 267 ILE B CG1 
6227 C CG2 . ILE B 240 ? 0.8898 1.1445 0.7521 0.0465  -0.0564 -0.0474 267 ILE B CG2 
6228 C CD1 . ILE B 240 ? 0.9852 1.2240 0.8038 0.0420  -0.0680 -0.0617 267 ILE B CD1 
6229 N N   . VAL B 241 ? 0.7516 0.9415 0.5920 0.0831  -0.0352 -0.0116 268 VAL B N   
6230 C CA  . VAL B 241 ? 0.6924 0.8874 0.5422 0.0957  -0.0313 -0.0011 268 VAL B CA  
6231 C C   . VAL B 241 ? 0.7174 0.8876 0.5723 0.0904  -0.0201 0.0005  268 VAL B C   
6232 O O   . VAL B 241 ? 0.7597 0.9410 0.6304 0.0913  -0.0161 0.0020  268 VAL B O   
6233 C CB  . VAL B 241 ? 0.6432 0.8296 0.4770 0.1138  -0.0323 0.0110  268 VAL B CB  
6234 C CG1 . VAL B 241 ? 0.5431 0.7180 0.3813 0.1253  -0.0246 0.0215  268 VAL B CG1 
6235 C CG2 . VAL B 241 ? 0.6771 0.8958 0.5096 0.1231  -0.0437 0.0119  268 VAL B CG2 
6236 N N   . PHE B 242 ? 0.7363 0.8734 0.5775 0.0854  -0.0147 0.0002  269 PHE B N   
6237 C CA  . PHE B 242 ? 0.7063 0.8195 0.5500 0.0808  -0.0051 0.0019  269 PHE B CA  
6238 C C   . PHE B 242 ? 0.7277 0.8478 0.5850 0.0655  -0.0026 -0.0070 269 PHE B C   
6239 O O   . PHE B 242 ? 0.6893 0.8056 0.5554 0.0638  0.0043  -0.0050 269 PHE B O   
6240 C CB  . PHE B 242 ? 0.5987 0.6782 0.4256 0.0797  -0.0010 0.0037  269 PHE B CB  
6241 C CG  . PHE B 242 ? 0.6674 0.7230 0.4950 0.0756  0.0074  0.0054  269 PHE B CG  
6242 C CD1 . PHE B 242 ? 0.7021 0.7527 0.5325 0.0839  0.0123  0.0127  269 PHE B CD1 
6243 C CD2 . PHE B 242 ? 0.6505 0.6879 0.4744 0.0642  0.0103  -0.0005 269 PHE B CD2 
6244 C CE1 . PHE B 242 ? 0.7377 0.7669 0.5666 0.0803  0.0194  0.0138  269 PHE B CE1 
6245 C CE2 . PHE B 242 ? 0.6704 0.6865 0.4932 0.0615  0.0173  0.0017  269 PHE B CE2 
6246 C CZ  . PHE B 242 ? 0.6522 0.6650 0.4772 0.0692  0.0215  0.0086  269 PHE B CZ  
6247 N N   . ALA B 243 ? 0.6555 0.7837 0.5132 0.0537  -0.0076 -0.0170 270 ALA B N   
6248 C CA  . ALA B 243 ? 0.7068 0.8412 0.5777 0.0376  -0.0050 -0.0257 270 ALA B CA  
6249 C C   . ALA B 243 ? 0.7240 0.8911 0.6166 0.0384  -0.0051 -0.0250 270 ALA B C   
6250 O O   . ALA B 243 ? 0.7419 0.9075 0.6457 0.0306  0.0026  -0.0258 270 ALA B O   
6251 C CB  . ALA B 243 ? 0.6474 0.7866 0.5145 0.0253  -0.0113 -0.0375 270 ALA B CB  
6252 N N   . PHE B 244 ? 0.6981 0.8957 0.5966 0.0486  -0.0133 -0.0230 271 PHE B N   
6253 C CA  . PHE B 244 ? 0.6437 0.8763 0.5645 0.0523  -0.0139 -0.0216 271 PHE B CA  
6254 C C   . PHE B 244 ? 0.7103 0.9315 0.6336 0.0634  -0.0042 -0.0117 271 PHE B C   
6255 O O   . PHE B 244 ? 0.6909 0.9299 0.6325 0.0611  0.0010  -0.0120 271 PHE B O   
6256 C CB  . PHE B 244 ? 0.5577 0.8238 0.4814 0.0637  -0.0258 -0.0205 271 PHE B CB  
6257 C CG  . PHE B 244 ? 0.6447 0.9529 0.5937 0.0681  -0.0281 -0.0200 271 PHE B CG  
6258 C CD1 . PHE B 244 ? 0.6857 1.0264 0.6550 0.0529  -0.0326 -0.0308 271 PHE B CD1 
6259 C CD2 . PHE B 244 ? 0.6353 0.9508 0.5884 0.0873  -0.0254 -0.0091 271 PHE B CD2 
6260 C CE1 . PHE B 244 ? 0.6559 1.0392 0.6512 0.0570  -0.0346 -0.0305 271 PHE B CE1 
6261 C CE2 . PHE B 244 ? 0.5515 0.9075 0.5291 0.0930  -0.0271 -0.0085 271 PHE B CE2 
6262 C CZ  . PHE B 244 ? 0.6099 1.0017 0.6097 0.0779  -0.0318 -0.0191 271 PHE B CZ  
6263 N N   . SER B 245 ? 0.7133 0.9053 0.6183 0.0750  -0.0014 -0.0034 272 SER B N   
6264 C CA  . SER B 245 ? 0.5833 0.7599 0.4876 0.0845  0.0078  0.0047  272 SER B CA  
6265 C C   . SER B 245 ? 0.6220 0.7814 0.5294 0.0719  0.0177  0.0016  272 SER B C   
6266 O O   . SER B 245 ? 0.7321 0.8930 0.6469 0.0761  0.0255  0.0051  272 SER B O   
6267 C CB  . SER B 245 ? 0.6032 0.7493 0.4865 0.0960  0.0087  0.0126  272 SER B CB  
6268 O OG  . SER B 245 ? 0.5305 0.6634 0.4124 0.1064  0.0163  0.0199  272 SER B OG  
6269 N N   . CYS B 246 ? 0.6436 0.7857 0.5440 0.0573  0.0181  -0.0047 273 CYS B N   
6270 C CA  . CYS B 246 ? 0.5794 0.7032 0.4805 0.0457  0.0274  -0.0067 273 CYS B CA  
6271 C C   . CYS B 246 ? 0.7169 0.8684 0.6396 0.0352  0.0308  -0.0118 273 CYS B C   
6272 O O   . CYS B 246 ? 0.7792 0.9251 0.7065 0.0320  0.0406  -0.0098 273 CYS B O   
6273 C CB  . CYS B 246 ? 0.5616 0.6577 0.4485 0.0347  0.0269  -0.0114 273 CYS B CB  
6274 S SG  . CYS B 246 ? 0.6591 0.7237 0.5229 0.0454  0.0246  -0.0058 273 CYS B SG  
6275 N N   . LYS B 247 ? 0.5768 0.7595 0.5129 0.0291  0.0228  -0.0186 274 LYS B N   
6276 C CA  . LYS B 247 ? 0.6738 0.8873 0.6336 0.0176  0.0255  -0.0242 274 LYS B CA  
6277 C C   . LYS B 247 ? 0.5841 0.8214 0.5595 0.0298  0.0305  -0.0179 274 LYS B C   
6278 O O   . LYS B 247 ? 0.6437 0.8892 0.6326 0.0225  0.0402  -0.0185 274 LYS B O   
6279 C CB  . LYS B 247 ? 0.6034 0.8481 0.5743 0.0094  0.0141  -0.0334 274 LYS B CB  
6280 C CG  . LYS B 247 ? 1.0565 1.2790 1.0144 -0.0058 0.0110  -0.0420 274 LYS B CG  
6281 C CD  . LYS B 247 ? 1.2041 1.4528 1.1651 -0.0088 -0.0025 -0.0504 274 LYS B CD  
6282 C CE  . LYS B 247 ? 1.2185 1.4388 1.1609 -0.0198 -0.0051 -0.0583 274 LYS B CE  
6283 N NZ  . LYS B 247 ? 1.2584 1.5008 1.1983 -0.0203 -0.0186 -0.0662 274 LYS B NZ  
6284 N N   . GLN B 248 ? 0.5663 0.8137 0.5392 0.0490  0.0250  -0.0115 275 GLN B N   
6285 C CA  . GLN B 248 ? 0.4831 0.7516 0.4696 0.0632  0.0299  -0.0054 275 GLN B CA  
6286 C C   . GLN B 248 ? 0.4977 0.7353 0.4735 0.0678  0.0428  0.0005  275 GLN B C   
6287 O O   . GLN B 248 ? 0.7224 0.9750 0.7117 0.0720  0.0514  0.0026  275 GLN B O   
6288 C CB  . GLN B 248 ? 0.6148 0.8970 0.5981 0.0836  0.0208  0.0006  275 GLN B CB  
6289 C CG  . GLN B 248 ? 0.5830 0.8971 0.5743 0.0808  0.0069  -0.0049 275 GLN B CG  
6290 C CD  . GLN B 248 ? 0.6884 1.0468 0.7091 0.0691  0.0054  -0.0127 275 GLN B CD  
6291 O OE1 . GLN B 248 ? 0.7037 1.0945 0.7446 0.0789  0.0072  -0.0098 275 GLN B OE1 
6292 N NE2 . GLN B 248 ? 0.6917 1.0516 0.7155 0.0478  0.0026  -0.0230 275 GLN B NE2 
6293 N N   . ALA B 249 ? 0.6128 0.8090 0.5647 0.0673  0.0444  0.0029  276 ALA B N   
6294 C CA  . ALA B 249 ? 0.6218 0.7875 0.5615 0.0691  0.0555  0.0071  276 ALA B CA  
6295 C C   . ALA B 249 ? 0.7065 0.8626 0.6482 0.0512  0.0639  0.0029  276 ALA B C   
6296 O O   . ALA B 249 ? 0.6714 0.8020 0.6013 0.0515  0.0730  0.0061  276 ALA B O   
6297 C CB  . ALA B 249 ? 0.5330 0.6607 0.4476 0.0755  0.0530  0.0113  276 ALA B CB  
6298 N N   . GLU B 250 ? 0.7543 0.9292 0.7095 0.0356  0.0610  -0.0043 277 GLU B N   
6299 C CA  . GLU B 250 ? 0.7441 0.9068 0.7000 0.0171  0.0691  -0.0082 277 GLU B CA  
6300 C C   . GLU B 250 ? 0.7165 0.8333 0.6465 0.0143  0.0711  -0.0062 277 GLU B C   
6301 O O   . GLU B 250 ? 0.8168 0.9128 0.7393 0.0073  0.0809  -0.0045 277 GLU B O   
6302 C CB  . GLU B 250 ? 0.7402 0.9168 0.7097 0.0152  0.0819  -0.0062 277 GLU B CB  
6303 C CG  . GLU B 250 ? 0.8663 1.0927 0.8662 0.0133  0.0805  -0.0100 277 GLU B CG  
6304 C CD  . GLU B 250 ? 1.3009 1.5432 1.3149 0.0145  0.0943  -0.0072 277 GLU B CD  
6305 O OE1 . GLU B 250 ? 1.4526 1.6653 1.4503 0.0163  0.1050  -0.0025 277 GLU B OE1 
6306 O OE2 . GLU B 250 ? 1.4212 1.7071 1.4626 0.0138  0.0944  -0.0098 277 GLU B OE2 
6307 N N   . VAL B 251 ? 0.6982 0.8004 0.6144 0.0202  0.0619  -0.0059 278 VAL B N   
6308 C CA  . VAL B 251 ? 0.6248 0.6882 0.5189 0.0182  0.0620  -0.0046 278 VAL B CA  
6309 C C   . VAL B 251 ? 0.8453 0.9047 0.7387 0.0045  0.0571  -0.0121 278 VAL B C   
6310 O O   . VAL B 251 ? 0.7546 0.8303 0.6522 0.0054  0.0478  -0.0164 278 VAL B O   
6311 C CB  . VAL B 251 ? 0.6568 0.7061 0.5366 0.0336  0.0564  0.0005  278 VAL B CB  
6312 C CG1 . VAL B 251 ? 0.6324 0.6465 0.4926 0.0311  0.0558  0.0012  278 VAL B CG1 
6313 C CG2 . VAL B 251 ? 0.6295 0.6789 0.5083 0.0466  0.0617  0.0069  278 VAL B CG2 
6314 N N   . GLN B 252 ? 0.8285 0.8649 0.7150 -0.0076 0.0635  -0.0138 279 GLN B N   
6315 C CA  . GLN B 252 ? 0.6581 0.6854 0.5420 -0.0207 0.0603  -0.0213 279 GLN B CA  
6316 C C   . GLN B 252 ? 0.7688 0.7690 0.6333 -0.0141 0.0549  -0.0204 279 GLN B C   
6317 O O   . GLN B 252 ? 0.8646 0.8386 0.7145 -0.0076 0.0583  -0.0143 279 GLN B O   
6318 C CB  . GLN B 252 ? 0.6270 0.6378 0.5104 -0.0360 0.0705  -0.0227 279 GLN B CB  
6319 C CG  . GLN B 252 ? 0.8095 0.8047 0.6880 -0.0498 0.0685  -0.0307 279 GLN B CG  
6320 C CD  . GLN B 252 ? 0.9240 0.9493 0.8172 -0.0567 0.0596  -0.0405 279 GLN B CD  
6321 O OE1 . GLN B 252 ? 0.7406 0.7985 0.6544 -0.0636 0.0602  -0.0438 279 GLN B OE1 
6322 N NE2 . GLN B 252 ? 0.7401 0.7564 0.6228 -0.0545 0.0513  -0.0454 279 GLN B NE2 
6323 N N   . MET B 253 ? 0.7139 0.7220 0.5783 -0.0156 0.0464  -0.0267 280 MET B N   
6324 C CA  . MET B 253 ? 0.7402 0.7243 0.5876 -0.0109 0.0423  -0.0271 280 MET B CA  
6325 C C   . MET B 253 ? 0.7051 0.6612 0.5436 -0.0225 0.0468  -0.0315 280 MET B C   
6326 O O   . MET B 253 ? 0.7848 0.7456 0.6311 -0.0369 0.0493  -0.0383 280 MET B O   
6327 C CB  . MET B 253 ? 0.6826 0.6852 0.5310 -0.0073 0.0324  -0.0321 280 MET B CB  
6328 C CG  . MET B 253 ? 0.8661 0.8806 0.7132 0.0089  0.0279  -0.0250 280 MET B CG  
6329 S SD  . MET B 253 ? 0.8094 0.8490 0.6570 0.0132  0.0167  -0.0297 280 MET B SD  
6330 C CE  . MET B 253 ? 1.1011 1.1794 0.9711 0.0042  0.0141  -0.0358 280 MET B CE  
6331 N N   . TYR B 254 ? 0.6787 0.6055 0.5011 -0.0161 0.0481  -0.0274 281 TYR B N   
6332 C CA  . TYR B 254 ? 0.8254 0.7217 0.6369 -0.0237 0.0527  -0.0299 281 TYR B CA  
6333 C C   . TYR B 254 ? 0.7661 0.6467 0.5651 -0.0169 0.0479  -0.0321 281 TYR B C   
6334 O O   . TYR B 254 ? 0.7322 0.6177 0.5278 -0.0048 0.0434  -0.0281 281 TYR B O   
6335 C CB  . TYR B 254 ? 0.7071 0.5806 0.5103 -0.0218 0.0606  -0.0216 281 TYR B CB  
6336 C CG  . TYR B 254 ? 0.7111 0.5942 0.5241 -0.0305 0.0683  -0.0198 281 TYR B CG  
6337 C CD1 . TYR B 254 ? 0.8123 0.6851 0.6271 -0.0458 0.0751  -0.0237 281 TYR B CD1 
6338 C CD2 . TYR B 254 ? 0.8401 0.7413 0.6601 -0.0235 0.0698  -0.0141 281 TYR B CD2 
6339 C CE1 . TYR B 254 ? 0.8401 0.7228 0.6646 -0.0545 0.0834  -0.0217 281 TYR B CE1 
6340 C CE2 . TYR B 254 ? 0.8631 0.7744 0.6923 -0.0307 0.0780  -0.0124 281 TYR B CE2 
6341 C CZ  . TYR B 254 ? 0.9502 0.8534 0.7822 -0.0465 0.0849  -0.0160 281 TYR B CZ  
6342 O OH  . TYR B 254 ? 1.0778 0.9924 0.9200 -0.0544 0.0943  -0.0141 281 TYR B OH  
6343 N N   . VAL B 255 ? 0.8243 0.6849 0.6163 -0.0251 0.0498  -0.0387 282 VAL B N   
6344 C CA  . VAL B 255 ? 0.8034 0.6438 0.5823 -0.0185 0.0478  -0.0407 282 VAL B CA  
6345 C C   . VAL B 255 ? 0.8515 0.6570 0.6191 -0.0210 0.0548  -0.0384 282 VAL B C   
6346 O O   . VAL B 255 ? 0.7256 0.5210 0.4945 -0.0336 0.0604  -0.0412 282 VAL B O   
6347 C CB  . VAL B 255 ? 0.9027 0.7515 0.6812 -0.0238 0.0427  -0.0521 282 VAL B CB  
6348 C CG1 . VAL B 255 ? 0.7343 0.5807 0.5175 -0.0414 0.0456  -0.0614 282 VAL B CG1 
6349 C CG2 . VAL B 255 ? 0.7484 0.5759 0.5129 -0.0158 0.0421  -0.0541 282 VAL B CG2 
6350 N N   . CYS B 256 ? 0.9168 0.7045 0.6739 -0.0091 0.0546  -0.0327 283 CYS B N   
6351 C CA  . CYS B 256 ? 0.9191 0.6737 0.6640 -0.0080 0.0602  -0.0290 283 CYS B CA  
6352 C C   . CYS B 256 ? 0.9097 0.6468 0.6451 -0.0023 0.0589  -0.0340 283 CYS B C   
6353 O O   . CYS B 256 ? 0.8722 0.6208 0.6082 0.0075  0.0539  -0.0344 283 CYS B O   
6354 C CB  . CYS B 256 ? 0.7025 0.4513 0.4429 0.0024  0.0610  -0.0176 283 CYS B CB  
6355 S SG  . CYS B 256 ? 1.6539 1.4215 1.4029 -0.0013 0.0635  -0.0114 283 CYS B SG  
6356 N N   . ASN B 257 ? 0.9115 0.6201 0.6378 -0.0082 0.0644  -0.0376 284 ASN B N   
6357 C CA  . ASN B 257 ? 0.8625 0.5500 0.5783 -0.0018 0.0647  -0.0424 284 ASN B CA  
6358 C C   . ASN B 257 ? 0.9756 0.6280 0.6785 0.0040  0.0705  -0.0357 284 ASN B C   
6359 O O   . ASN B 257 ? 0.9637 0.5906 0.6566 0.0057  0.0736  -0.0406 284 ASN B O   
6360 C CB  . ASN B 257 ? 0.8057 0.4902 0.5207 -0.0139 0.0653  -0.0561 284 ASN B CB  
6361 C CG  . ASN B 257 ? 0.9912 0.6576 0.7050 -0.0304 0.0721  -0.0593 284 ASN B CG  
6362 O OD1 . ASN B 257 ? 0.9422 0.6052 0.6582 -0.0340 0.0763  -0.0510 284 ASN B OD1 
6363 N ND2 . ASN B 257 ? 1.0915 0.7457 0.8012 -0.0412 0.0736  -0.0716 284 ASN B ND2 
6364 N N   . LYS B 258 ? 0.9986 0.6484 0.7002 0.0080  0.0718  -0.0246 285 LYS B N   
6365 C CA  . LYS B 258 ? 1.0071 0.6237 0.6948 0.0134  0.0771  -0.0170 285 LYS B CA  
6366 C C   . LYS B 258 ? 1.0784 0.6809 0.7584 0.0294  0.0749  -0.0160 285 LYS B C   
6367 O O   . LYS B 258 ? 1.2479 0.8184 0.9149 0.0341  0.0796  -0.0129 285 LYS B O   
6368 C CB  . LYS B 258 ? 0.8610 0.4816 0.5474 0.0165  0.0775  -0.0054 285 LYS B CB  
6369 C CG  . LYS B 258 ? 0.7501 0.3796 0.4423 0.0016  0.0823  -0.0052 285 LYS B CG  
6370 C CD  . LYS B 258 ? 0.7147 0.3468 0.4030 0.0065  0.0832  0.0060  285 LYS B CD  
6371 C CE  . LYS B 258 ? 0.9585 0.6025 0.6539 -0.0072 0.0890  0.0063  285 LYS B CE  
6372 N NZ  . LYS B 258 ? 0.9679 0.6136 0.6572 -0.0016 0.0905  0.0165  285 LYS B NZ  
6373 N N   . GLU B 259 ? 1.0573 0.6831 0.7450 0.0383  0.0685  -0.0180 286 GLU B N   
6374 C CA  . GLU B 259 ? 1.1315 0.7494 0.8151 0.0529  0.0670  -0.0183 286 GLU B CA  
6375 C C   . GLU B 259 ? 0.9718 0.6175 0.6653 0.0552  0.0622  -0.0250 286 GLU B C   
6376 O O   . GLU B 259 ? 0.9409 0.6098 0.6428 0.0463  0.0596  -0.0285 286 GLU B O   
6377 C CB  . GLU B 259 ? 1.0986 0.7129 0.7791 0.0672  0.0644  -0.0067 286 GLU B CB  
6378 C CG  . GLU B 259 ? 1.0851 0.7239 0.7734 0.0668  0.0595  0.0002  286 GLU B CG  
6379 C CD  . GLU B 259 ? 1.3195 0.9524 1.0024 0.0793  0.0565  0.0107  286 GLU B CD  
6380 O OE1 . GLU B 259 ? 1.3240 0.9576 1.0079 0.0923  0.0534  0.0119  286 GLU B OE1 
6381 O OE2 . GLU B 259 ? 1.2200 0.8485 0.8975 0.0762  0.0571  0.0175  286 GLU B OE2 
6382 N N   . GLU B 260 ? 0.9981 0.6415 0.6900 0.0679  0.0616  -0.0263 287 GLU B N   
6383 C CA  . GLU B 260 ? 0.8574 0.5250 0.5565 0.0711  0.0585  -0.0318 287 GLU B CA  
6384 C C   . GLU B 260 ? 0.9576 0.6531 0.6677 0.0759  0.0530  -0.0241 287 GLU B C   
6385 O O   . GLU B 260 ? 0.9616 0.6557 0.6730 0.0842  0.0512  -0.0155 287 GLU B O   
6386 C CB  . GLU B 260 ? 0.7856 0.4415 0.4796 0.0833  0.0613  -0.0358 287 GLU B CB  
6387 C CG  . GLU B 260 ? 1.1282 0.8021 0.8248 0.0837  0.0607  -0.0445 287 GLU B CG  
6388 C CD  . GLU B 260 ? 1.2675 0.9298 0.9589 0.0967  0.0648  -0.0486 287 GLU B CD  
6389 O OE1 . GLU B 260 ? 1.3448 1.0113 1.0414 0.1102  0.0642  -0.0412 287 GLU B OE1 
6390 O OE2 . GLU B 260 ? 1.3085 0.9581 0.9907 0.0936  0.0686  -0.0596 287 GLU B OE2 
6391 N N   . TYR B 261 ? 0.9073 0.6273 0.6245 0.0707  0.0502  -0.0273 288 TYR B N   
6392 C CA  . TYR B 261 ? 0.7646 0.5090 0.4914 0.0740  0.0458  -0.0207 288 TYR B CA  
6393 C C   . TYR B 261 ? 0.8191 0.5818 0.5505 0.0800  0.0448  -0.0230 288 TYR B C   
6394 O O   . TYR B 261 ? 0.7729 0.5469 0.5109 0.0876  0.0429  -0.0171 288 TYR B O   
6395 C CB  . TYR B 261 ? 0.7379 0.4957 0.4691 0.0636  0.0438  -0.0197 288 TYR B CB  
6396 C CG  . TYR B 261 ? 0.8618 0.6040 0.5891 0.0563  0.0462  -0.0175 288 TYR B CG  
6397 C CD1 . TYR B 261 ? 0.8311 0.5634 0.5558 0.0609  0.0462  -0.0090 288 TYR B CD1 
6398 C CD2 . TYR B 261 ? 0.8338 0.5720 0.5598 0.0442  0.0486  -0.0239 288 TYR B CD2 
6399 C CE1 . TYR B 261 ? 0.9021 0.6193 0.6214 0.0543  0.0495  -0.0062 288 TYR B CE1 
6400 C CE2 . TYR B 261 ? 0.7523 0.4768 0.4755 0.0365  0.0523  -0.0214 288 TYR B CE2 
6401 C CZ  . TYR B 261 ? 0.9937 0.7068 0.7126 0.0419  0.0532  -0.0122 288 TYR B CZ  
6402 O OH  . TYR B 261 ? 1.1019 0.8006 0.8162 0.0343  0.0580  -0.0091 288 TYR B OH  
6403 N N   . GLY B 262 ? 0.7955 0.5617 0.5232 0.0763  0.0461  -0.0316 289 GLY B N   
6404 C CA  . GLY B 262 ? 0.7580 0.5408 0.4877 0.0821  0.0463  -0.0334 289 GLY B CA  
6405 C C   . GLY B 262 ? 0.8804 0.6645 0.6022 0.0771  0.0474  -0.0439 289 GLY B C   
6406 O O   . GLY B 262 ? 0.9221 0.6922 0.6372 0.0692  0.0482  -0.0511 289 GLY B O   
6407 N N   . PHE B 263 ? 0.8235 0.6246 0.5453 0.0814  0.0477  -0.0448 290 PHE B N   
6408 C CA  . PHE B 263 ? 0.7904 0.5944 0.5022 0.0789  0.0486  -0.0547 290 PHE B CA  
6409 C C   . PHE B 263 ? 0.7803 0.6092 0.4936 0.0775  0.0454  -0.0519 290 PHE B C   
6410 O O   . PHE B 263 ? 0.8201 0.6619 0.5421 0.0808  0.0443  -0.0423 290 PHE B O   
6411 C CB  . PHE B 263 ? 0.7988 0.5942 0.5042 0.0886  0.0545  -0.0597 290 PHE B CB  
6412 C CG  . PHE B 263 ? 0.9042 0.6732 0.6067 0.0925  0.0582  -0.0619 290 PHE B CG  
6413 C CD1 . PHE B 263 ? 0.8569 0.6217 0.5683 0.1001  0.0586  -0.0528 290 PHE B CD1 
6414 C CD2 . PHE B 263 ? 0.9126 0.6602 0.6026 0.0889  0.0610  -0.0733 290 PHE B CD2 
6415 C CE1 . PHE B 263 ? 0.9890 0.7288 0.6963 0.1054  0.0617  -0.0537 290 PHE B CE1 
6416 C CE2 . PHE B 263 ? 1.0896 0.8096 0.7755 0.0935  0.0652  -0.0746 290 PHE B CE2 
6417 C CZ  . PHE B 263 ? 1.0808 0.7970 0.7751 0.1025  0.0655  -0.0642 290 PHE B CZ  
6418 N N   . LEU B 264 ? 0.8876 0.7222 0.5914 0.0728  0.0438  -0.0605 291 LEU B N   
6419 C CA  . LEU B 264 ? 0.8109 0.6680 0.5129 0.0726  0.0404  -0.0580 291 LEU B CA  
6420 C C   . LEU B 264 ? 0.7282 0.5873 0.4150 0.0718  0.0407  -0.0690 291 LEU B C   
6421 O O   . LEU B 264 ? 0.8165 0.6612 0.4960 0.0664  0.0409  -0.0802 291 LEU B O   
6422 C CB  . LEU B 264 ? 0.8373 0.7061 0.5463 0.0650  0.0342  -0.0546 291 LEU B CB  
6423 C CG  . LEU B 264 ? 0.7548 0.6259 0.4603 0.0543  0.0295  -0.0644 291 LEU B CG  
6424 C CD1 . LEU B 264 ? 0.7242 0.6124 0.4398 0.0499  0.0242  -0.0585 291 LEU B CD1 
6425 C CD2 . LEU B 264 ? 0.7997 0.6475 0.5040 0.0478  0.0321  -0.0720 291 LEU B CD2 
6426 N N   . PRO B 265 ? 0.8879 0.7629 0.5683 0.0769  0.0410  -0.0665 292 PRO B N   
6427 C CA  . PRO B 265 ? 0.7724 0.6508 0.4356 0.0763  0.0406  -0.0771 292 PRO B CA  
6428 C C   . PRO B 265 ? 0.7909 0.6802 0.4508 0.0667  0.0318  -0.0832 292 PRO B C   
6429 O O   . PRO B 265 ? 0.7902 0.6898 0.4615 0.0625  0.0267  -0.0769 292 PRO B O   
6430 C CB  . PRO B 265 ? 0.7630 0.6560 0.4209 0.0851  0.0441  -0.0695 292 PRO B CB  
6431 C CG  . PRO B 265 ? 0.7297 0.6325 0.4024 0.0862  0.0424  -0.0554 292 PRO B CG  
6432 C CD  . PRO B 265 ? 0.8360 0.7250 0.5230 0.0834  0.0425  -0.0537 292 PRO B CD  
6433 N N   . VAL B 266 ? 0.8198 0.7076 0.4641 0.0633  0.0302  -0.0963 293 VAL B N   
6434 C CA  . VAL B 266 ? 0.8796 0.7813 0.5201 0.0539  0.0209  -0.1038 293 VAL B CA  
6435 C C   . VAL B 266 ? 0.7993 0.7258 0.4325 0.0599  0.0165  -0.0973 293 VAL B C   
6436 O O   . VAL B 266 ? 0.7850 0.7125 0.4039 0.0680  0.0210  -0.0967 293 VAL B O   
6437 C CB  . VAL B 266 ? 0.8539 0.7425 0.4799 0.0464  0.0203  -0.1220 293 VAL B CB  
6438 C CG1 . VAL B 266 ? 0.7196 0.6271 0.3427 0.0360  0.0095  -0.1304 293 VAL B CG1 
6439 C CG2 . VAL B 266 ? 0.9217 0.7825 0.5542 0.0409  0.0253  -0.1270 293 VAL B CG2 
6440 N N   . PRO B 267 ? 0.8930 0.8391 0.5351 0.0569  0.0087  -0.0916 294 PRO B N   
6441 C CA  . PRO B 267 ? 0.8239 0.7916 0.4586 0.0644  0.0047  -0.0832 294 PRO B CA  
6442 C C   . PRO B 267 ? 0.9040 0.8791 0.5156 0.0657  0.0016  -0.0932 294 PRO B C   
6443 O O   . PRO B 267 ? 0.9022 0.8750 0.5066 0.0571  -0.0028 -0.1084 294 PRO B O   
6444 C CB  . PRO B 267 ? 0.6888 0.6751 0.3378 0.0597  -0.0041 -0.0793 294 PRO B CB  
6445 C CG  . PRO B 267 ? 0.7556 0.7279 0.4228 0.0527  -0.0011 -0.0792 294 PRO B CG  
6446 C CD  . PRO B 267 ? 0.7399 0.6889 0.3998 0.0478  0.0042  -0.0912 294 PRO B CD  
6447 N N   . LEU B 268 ? 0.8882 0.8711 0.4870 0.0761  0.0044  -0.0845 295 LEU B N   
6448 C CA  . LEU B 268 ? 0.8661 0.8558 0.4397 0.0793  0.0026  -0.0920 295 LEU B CA  
6449 C C   . LEU B 268 ? 0.8771 0.8924 0.4448 0.0785  -0.0102 -0.0920 295 LEU B C   
6450 O O   . LEU B 268 ? 0.8839 0.9120 0.4686 0.0755  -0.0171 -0.0868 295 LEU B O   
6451 C CB  . LEU B 268 ? 0.9032 0.8892 0.4649 0.0909  0.0129  -0.0819 295 LEU B CB  
6452 C CG  . LEU B 268 ? 0.8644 0.8291 0.4303 0.0931  0.0254  -0.0833 295 LEU B CG  
6453 C CD1 . LEU B 268 ? 0.9810 0.9475 0.5401 0.1035  0.0353  -0.0709 295 LEU B CD1 
6454 C CD2 . LEU B 268 ? 0.8668 0.8182 0.4183 0.0893  0.0272  -0.1016 295 LEU B CD2 
6455 N N   . ARG B 269 ? 0.9450 0.9689 0.4877 0.0821  -0.0133 -0.0980 296 ARG B N   
6456 C CA  . ARG B 269 ? 0.9592 1.0093 0.4929 0.0832  -0.0263 -0.0982 296 ARG B CA  
6457 C C   . ARG B 269 ? 0.9461 1.0067 0.4717 0.0968  -0.0246 -0.0794 296 ARG B C   
6458 O O   . ARG B 269 ? 1.0728 1.1200 0.5959 0.1041  -0.0127 -0.0685 296 ARG B O   
6459 C CB  . ARG B 269 ? 1.1786 1.2322 0.6871 0.0791  -0.0319 -0.1159 296 ARG B CB  
6460 C CG  . ARG B 269 ? 1.1063 1.1432 0.6198 0.0655  -0.0314 -0.1350 296 ARG B CG  
6461 C CD  . ARG B 269 ? 1.4873 1.5259 0.9742 0.0608  -0.0371 -0.1540 296 ARG B CD  
6462 N NE  . ARG B 269 ? 1.7283 1.7509 1.2211 0.0460  -0.0379 -0.1727 296 ARG B NE  
6463 C CZ  . ARG B 269 ? 1.8103 1.8302 1.2835 0.0379  -0.0432 -0.1926 296 ARG B CZ  
6464 N NH1 . ARG B 269 ? 1.7636 1.7972 1.2087 0.0436  -0.0487 -0.1972 296 ARG B NH1 
6465 N NH2 . ARG B 269 ? 1.6839 1.6856 1.1644 0.0237  -0.0427 -0.2085 296 ARG B NH2 
6466 N N   . ALA B 270 ? 0.8442 0.9293 0.3660 0.1002  -0.0366 -0.0755 297 ALA B N   
6467 C CA  . ALA B 270 ? 1.0114 1.1051 0.5265 0.1136  -0.0357 -0.0564 297 ALA B CA  
6468 C C   . ALA B 270 ? 1.0065 1.0919 0.4927 0.1228  -0.0269 -0.0515 297 ALA B C   
6469 O O   . ALA B 270 ? 0.8147 0.8936 0.2985 0.1320  -0.0183 -0.0345 297 ALA B O   
6470 C CB  . ALA B 270 ? 0.8096 0.9325 0.3240 0.1168  -0.0512 -0.0545 297 ALA B CB  
6471 N N   . HIS B 271 ? 1.0590 1.1437 0.5227 0.1201  -0.0282 -0.0662 298 HIS B N   
6472 C CA  . HIS B 271 ? 0.8687 0.9467 0.3025 0.1287  -0.0193 -0.0630 298 HIS B CA  
6473 C C   . HIS B 271 ? 0.9684 1.0223 0.4037 0.1266  -0.0034 -0.0676 298 HIS B C   
6474 O O   . HIS B 271 ? 1.0605 1.1085 0.4708 0.1312  0.0042  -0.0714 298 HIS B O   
6475 C CB  . HIS B 271 ? 1.1652 1.2579 0.5697 0.1289  -0.0301 -0.0762 298 HIS B CB  
6476 C CG  . HIS B 271 ? 1.3304 1.4478 0.7316 0.1341  -0.0442 -0.0675 298 HIS B CG  
6477 N ND1 . HIS B 271 ? 1.2614 1.3964 0.6507 0.1299  -0.0582 -0.0789 298 HIS B ND1 
6478 C CD2 . HIS B 271 ? 0.8853 1.0115 0.2966 0.1429  -0.0461 -0.0482 298 HIS B CD2 
6479 C CE1 . HIS B 271 ? 1.3171 1.4724 0.7099 0.1369  -0.0685 -0.0665 298 HIS B CE1 
6480 N NE2 . HIS B 271 ? 1.1628 1.3122 0.5686 0.1451  -0.0610 -0.0478 298 HIS B NE2 
6481 N N   . SER B 272 ? 0.8640 0.9050 0.3275 0.1206  0.0019  -0.0670 299 SER B N   
6482 C CA  . SER B 272 ? 0.8996 0.9200 0.3680 0.1204  0.0166  -0.0691 299 SER B CA  
6483 C C   . SER B 272 ? 0.9849 1.0012 0.4547 0.1292  0.0290  -0.0503 299 SER B C   
6484 O O   . SER B 272 ? 1.0406 1.0657 0.5115 0.1343  0.0265  -0.0350 299 SER B O   
6485 C CB  . SER B 272 ? 0.9408 0.9492 0.4374 0.1112  0.0166  -0.0754 299 SER B CB  
6486 O OG  . SER B 272 ? 1.0425 1.0542 0.5392 0.1015  0.0056  -0.0920 299 SER B OG  
6487 N N   . THR B 273 ? 0.9606 0.9633 0.4311 0.1309  0.0429  -0.0515 300 THR B N   
6488 C CA  . THR B 273 ? 0.9550 0.9543 0.4271 0.1376  0.0564  -0.0356 300 THR B CA  
6489 C C   . THR B 273 ? 0.8950 0.8847 0.3987 0.1340  0.0624  -0.0301 300 THR B C   
6490 O O   . THR B 273 ? 1.0579 1.0410 0.5788 0.1277  0.0578  -0.0392 300 THR B O   
6491 C CB  . THR B 273 ? 0.8210 0.8162 0.2706 0.1431  0.0689  -0.0401 300 THR B CB  
6492 O OG1 . THR B 273 ? 0.9229 0.9058 0.3838 0.1403  0.0757  -0.0523 300 THR B OG1 
6493 C CG2 . THR B 273 ? 0.8538 0.8570 0.2702 0.1455  0.0616  -0.0499 300 THR B CG2 
6494 N N   . LEU B 274 ? 0.8679 0.8564 0.3780 0.1379  0.0727  -0.0148 301 LEU B N   
6495 C CA  . LEU B 274 ? 0.7873 0.7682 0.3259 0.1347  0.0788  -0.0099 301 LEU B CA  
6496 C C   . LEU B 274 ? 0.8963 0.8693 0.4405 0.1345  0.0868  -0.0213 301 LEU B C   
6497 O O   . LEU B 274 ? 0.8323 0.7982 0.3985 0.1307  0.0859  -0.0248 301 LEU B O   
6498 C CB  . LEU B 274 ? 0.7284 0.7102 0.2714 0.1377  0.0886  0.0078  301 LEU B CB  
6499 C CG  . LEU B 274 ? 0.9729 0.9580 0.5144 0.1387  0.0819  0.0212  301 LEU B CG  
6500 C CD1 . LEU B 274 ? 0.9527 0.9338 0.5013 0.1397  0.0931  0.0376  301 LEU B CD1 
6501 C CD2 . LEU B 274 ? 0.8791 0.8635 0.4398 0.1337  0.0697  0.0180  301 LEU B CD2 
6502 N N   . GLN B 275 ? 0.9398 0.9134 0.4629 0.1395  0.0950  -0.0272 302 GLN B N   
6503 C CA  . GLN B 275 ? 0.8753 0.8408 0.4014 0.1411  0.1030  -0.0391 302 GLN B CA  
6504 C C   . GLN B 275 ? 1.0184 0.9741 0.5474 0.1360  0.0931  -0.0549 302 GLN B C   
6505 O O   . GLN B 275 ? 0.9858 0.9312 0.5300 0.1356  0.0965  -0.0611 302 GLN B O   
6506 C CB  . GLN B 275 ? 0.7971 0.7650 0.2962 0.1480  0.1133  -0.0435 302 GLN B CB  
6507 C CG  . GLN B 275 ? 0.8635 0.8225 0.3630 0.1516  0.1224  -0.0567 302 GLN B CG  
6508 C CD  . GLN B 275 ? 0.9826 0.9427 0.4506 0.1582  0.1309  -0.0643 302 GLN B CD  
6509 O OE1 . GLN B 275 ? 1.2086 1.1769 0.6536 0.1600  0.1301  -0.0588 302 GLN B OE1 
6510 N NE2 . GLN B 275 ? 1.1296 1.0807 0.5951 0.1626  0.1393  -0.0770 302 GLN B NE2 
6511 N N   . ASP B 276 ? 0.9191 0.8782 0.4338 0.1320  0.0808  -0.0614 303 ASP B N   
6512 C CA  . ASP B 276 ? 0.9258 0.8763 0.4455 0.1246  0.0710  -0.0755 303 ASP B CA  
6513 C C   . ASP B 276 ? 0.9077 0.8524 0.4573 0.1198  0.0682  -0.0700 303 ASP B C   
6514 O O   . ASP B 276 ? 0.9544 0.8853 0.5139 0.1167  0.0685  -0.0791 303 ASP B O   
6515 C CB  . ASP B 276 ? 0.9282 0.8890 0.4325 0.1200  0.0573  -0.0809 303 ASP B CB  
6516 C CG  . ASP B 276 ? 0.9827 0.9475 0.4543 0.1240  0.0583  -0.0898 303 ASP B CG  
6517 O OD1 . ASP B 276 ? 1.3041 1.2623 0.7644 0.1304  0.0708  -0.0923 303 ASP B OD1 
6518 O OD2 . ASP B 276 ? 1.0194 0.9952 0.4764 0.1211  0.0465  -0.0947 303 ASP B OD2 
6519 N N   . GLU B 277 ? 1.0016 0.9553 0.5644 0.1195  0.0657  -0.0551 304 GLU B N   
6520 C CA  . GLU B 277 ? 0.8531 0.8017 0.4422 0.1153  0.0631  -0.0495 304 GLU B CA  
6521 C C   . GLU B 277 ? 0.7856 0.7256 0.3897 0.1187  0.0735  -0.0472 304 GLU B C   
6522 O O   . GLU B 277 ? 0.8668 0.7964 0.4863 0.1157  0.0719  -0.0508 304 GLU B O   
6523 C CB  . GLU B 277 ? 0.8525 0.8113 0.4496 0.1152  0.0590  -0.0345 304 GLU B CB  
6524 C CG  . GLU B 277 ? 0.9917 0.9457 0.6134 0.1107  0.0557  -0.0293 304 GLU B CG  
6525 C CD  . GLU B 277 ? 1.0245 0.9752 0.6512 0.1035  0.0459  -0.0391 304 GLU B CD  
6526 O OE1 . GLU B 277 ? 1.0480 1.0085 0.6649 0.1012  0.0375  -0.0427 304 GLU B OE1 
6527 O OE2 . GLU B 277 ? 1.0071 0.9462 0.6475 0.1000  0.0467  -0.0430 304 GLU B OE2 
6528 N N   . ALA B 278 ? 0.8913 0.8363 0.4910 0.1251  0.0843  -0.0410 305 ALA B N   
6529 C CA  . ALA B 278 ? 0.8070 0.7485 0.4230 0.1288  0.0941  -0.0387 305 ALA B CA  
6530 C C   . ALA B 278 ? 0.9279 0.8562 0.5422 0.1310  0.0963  -0.0529 305 ALA B C   
6531 O O   . ALA B 278 ? 0.7663 0.6869 0.3987 0.1313  0.0969  -0.0533 305 ALA B O   
6532 C CB  . ALA B 278 ? 0.6936 0.6453 0.3041 0.1346  0.1063  -0.0306 305 ALA B CB  
6533 N N   . GLU B 279 ? 0.8315 0.7559 0.4227 0.1328  0.0975  -0.0647 306 GLU B N   
6534 C CA  . GLU B 279 ? 0.8775 0.7855 0.4643 0.1348  0.1000  -0.0792 306 GLU B CA  
6535 C C   . GLU B 279 ? 0.8929 0.7876 0.4870 0.1267  0.0895  -0.0858 306 GLU B C   
6536 O O   . GLU B 279 ? 0.9264 0.8046 0.5265 0.1281  0.0918  -0.0928 306 GLU B O   
6537 C CB  . GLU B 279 ? 0.7712 0.6769 0.3291 0.1380  0.1036  -0.0914 306 GLU B CB  
6538 C CG  . GLU B 279 ? 0.8403 0.7557 0.3903 0.1474  0.1174  -0.0869 306 GLU B CG  
6539 C CD  . GLU B 279 ? 1.0101 0.9231 0.5280 0.1507  0.1209  -0.0990 306 GLU B CD  
6540 O OE1 . GLU B 279 ? 1.1863 1.0864 0.6901 0.1463  0.1139  -0.1139 306 GLU B OE1 
6541 O OE2 . GLU B 279 ? 1.1105 1.0340 0.6166 0.1572  0.1310  -0.0940 306 GLU B OE2 
6542 N N   . SER B 280 ? 0.8913 0.7928 0.4851 0.1186  0.0786  -0.0830 307 SER B N   
6543 C CA  . SER B 280 ? 0.7692 0.6602 0.3712 0.1098  0.0697  -0.0885 307 SER B CA  
6544 C C   . SER B 280 ? 0.8879 0.7719 0.5137 0.1104  0.0709  -0.0804 307 SER B C   
6545 O O   . SER B 280 ? 0.7744 0.6410 0.4050 0.1080  0.0703  -0.0869 307 SER B O   
6546 C CB  . SER B 280 ? 0.8373 0.7419 0.4369 0.1023  0.0585  -0.0859 307 SER B CB  
6547 O OG  . SER B 280 ? 0.9565 0.8525 0.5632 0.0928  0.0508  -0.0927 307 SER B OG  
6548 N N   . PHE B 281 ? 0.8266 0.7229 0.4661 0.1133  0.0728  -0.0663 308 PHE B N   
6549 C CA  . PHE B 281 ? 0.9041 0.7953 0.5649 0.1140  0.0735  -0.0590 308 PHE B CA  
6550 C C   . PHE B 281 ? 0.7853 0.6677 0.4507 0.1224  0.0822  -0.0621 308 PHE B C   
6551 O O   . PHE B 281 ? 0.8515 0.7230 0.5294 0.1234  0.0815  -0.0613 308 PHE B O   
6552 C CB  . PHE B 281 ? 0.7996 0.7054 0.4732 0.1141  0.0731  -0.0444 308 PHE B CB  
6553 C CG  . PHE B 281 ? 0.8730 0.7749 0.5672 0.1141  0.0725  -0.0376 308 PHE B CG  
6554 C CD1 . PHE B 281 ? 0.7430 0.6386 0.4447 0.1078  0.0648  -0.0362 308 PHE B CD1 
6555 C CD2 . PHE B 281 ? 0.7188 0.6245 0.4247 0.1205  0.0795  -0.0330 308 PHE B CD2 
6556 C CE1 . PHE B 281 ? 0.7189 0.6105 0.4366 0.1082  0.0638  -0.0303 308 PHE B CE1 
6557 C CE2 . PHE B 281 ? 0.6835 0.5872 0.4074 0.1206  0.0775  -0.0274 308 PHE B CE2 
6558 C CZ  . PHE B 281 ? 0.8550 0.7507 0.5834 0.1146  0.0695  -0.0260 308 PHE B CZ  
6559 N N   . MET B 282 ? 0.7788 0.6663 0.4341 0.1295  0.0909  -0.0651 309 MET B N   
6560 C CA  . MET B 282 ? 0.7836 0.6635 0.4426 0.1390  0.0998  -0.0695 309 MET B CA  
6561 C C   . MET B 282 ? 0.8881 0.7437 0.5392 0.1385  0.0980  -0.0820 309 MET B C   
6562 O O   . MET B 282 ? 0.9242 0.7682 0.5850 0.1447  0.1011  -0.0826 309 MET B O   
6563 C CB  . MET B 282 ? 0.7049 0.5946 0.3516 0.1463  0.1102  -0.0717 309 MET B CB  
6564 C CG  . MET B 282 ? 0.8546 0.7378 0.5037 0.1578  0.1207  -0.0776 309 MET B CG  
6565 S SD  . MET B 282 ? 0.9990 0.8571 0.6221 0.1603  0.1228  -0.0970 309 MET B SD  
6566 C CE  . MET B 282 ? 1.0566 0.9251 0.6531 0.1544  0.1209  -0.1012 309 MET B CE  
6567 N N   . HIS B 283 ? 0.8424 0.6898 0.4756 0.1310  0.0927  -0.0921 310 HIS B N   
6568 C CA  . HIS B 283 ? 0.8504 0.6726 0.4759 0.1278  0.0909  -0.1043 310 HIS B CA  
6569 C C   . HIS B 283 ? 0.8936 0.7059 0.5348 0.1222  0.0848  -0.0989 310 HIS B C   
6570 O O   . HIS B 283 ? 0.8906 0.6797 0.5311 0.1233  0.0863  -0.1047 310 HIS B O   
6571 C CB  . HIS B 283 ? 0.8115 0.6307 0.4162 0.1187  0.0856  -0.1166 310 HIS B CB  
6572 C CG  . HIS B 283 ? 0.8190 0.6106 0.4137 0.1138  0.0849  -0.1310 310 HIS B CG  
6573 N ND1 . HIS B 283 ? 0.9185 0.7010 0.5172 0.1013  0.0767  -0.1337 310 HIS B ND1 
6574 C CD2 . HIS B 283 ? 0.9165 0.6864 0.4972 0.1195  0.0922  -0.1435 310 HIS B CD2 
6575 C CE1 . HIS B 283 ? 0.9437 0.6990 0.5312 0.0984  0.0790  -0.1471 310 HIS B CE1 
6576 N NE2 . HIS B 283 ? 0.9961 0.7421 0.5719 0.1096  0.0882  -0.1534 310 HIS B NE2 
6577 N N   . VAL B 284 ? 0.8309 0.6587 0.4849 0.1168  0.0784  -0.0877 311 VAL B N   
6578 C CA  . VAL B 284 ? 0.7977 0.6177 0.4664 0.1127  0.0736  -0.0813 311 VAL B CA  
6579 C C   . VAL B 284 ? 0.8444 0.6579 0.5253 0.1233  0.0789  -0.0758 311 VAL B C   
6580 O O   . VAL B 284 ? 0.7614 0.5559 0.4457 0.1236  0.0781  -0.0765 311 VAL B O   
6581 C CB  . VAL B 284 ? 0.8527 0.6915 0.5317 0.1065  0.0669  -0.0705 311 VAL B CB  
6582 C CG1 . VAL B 284 ? 0.7856 0.6160 0.4776 0.1026  0.0626  -0.0644 311 VAL B CG1 
6583 C CG2 . VAL B 284 ? 0.9476 0.7951 0.6152 0.0979  0.0611  -0.0757 311 VAL B CG2 
6584 N N   . GLN B 285 ? 0.7794 0.6092 0.4672 0.1320  0.0845  -0.0700 312 GLN B N   
6585 C CA  . GLN B 285 ? 0.7562 0.5847 0.4574 0.1430  0.0892  -0.0654 312 GLN B CA  
6586 C C   . GLN B 285 ? 0.8797 0.6853 0.5711 0.1512  0.0951  -0.0755 312 GLN B C   
6587 O O   . GLN B 285 ? 0.9612 0.7543 0.6604 0.1580  0.0956  -0.0732 312 GLN B O   
6588 C CB  . GLN B 285 ? 0.6847 0.5378 0.3958 0.1493  0.0950  -0.0584 312 GLN B CB  
6589 C CG  . GLN B 285 ? 0.7458 0.6180 0.4663 0.1417  0.0903  -0.0478 312 GLN B CG  
6590 C CD  . GLN B 285 ? 0.8429 0.7372 0.5690 0.1455  0.0974  -0.0421 312 GLN B CD  
6591 O OE1 . GLN B 285 ? 0.9598 0.8576 0.6728 0.1486  0.1041  -0.0472 312 GLN B OE1 
6592 N NE2 . GLN B 285 ? 0.7092 0.6179 0.4539 0.1446  0.0964  -0.0318 312 GLN B NE2 
6593 N N   . LEU B 286 ? 0.8495 0.6484 0.5225 0.1512  0.0995  -0.0869 313 LEU B N   
6594 C CA  . LEU B 286 ? 0.8800 0.6530 0.5407 0.1581  0.1054  -0.0983 313 LEU B CA  
6595 C C   . LEU B 286 ? 0.8646 0.6099 0.5218 0.1513  0.1003  -0.1016 313 LEU B C   
6596 O O   . LEU B 286 ? 0.9117 0.6353 0.5693 0.1597  0.1039  -0.1029 313 LEU B O   
6597 C CB  . LEU B 286 ? 0.8137 0.5840 0.4524 0.1569  0.1098  -0.1112 313 LEU B CB  
6598 C CG  . LEU B 286 ? 0.8691 0.6615 0.5057 0.1653  0.1180  -0.1100 313 LEU B CG  
6599 C CD1 . LEU B 286 ? 0.8062 0.5915 0.4166 0.1632  0.1212  -0.1242 313 LEU B CD1 
6600 C CD2 . LEU B 286 ? 0.8313 0.6255 0.4802 0.1815  0.1275  -0.1068 313 LEU B CD2 
6601 N N   . GLU B 287 ? 0.8453 0.5910 0.4990 0.1363  0.0924  -0.1025 314 GLU B N   
6602 C CA  . GLU B 287 ? 0.9206 0.6417 0.5717 0.1277  0.0884  -0.1051 314 GLU B CA  
6603 C C   . GLU B 287 ? 0.9780 0.6943 0.6443 0.1332  0.0869  -0.0931 314 GLU B C   
6604 O O   . GLU B 287 ? 1.0479 0.7368 0.7104 0.1343  0.0883  -0.0947 314 GLU B O   
6605 C CB  . GLU B 287 ? 0.8499 0.5800 0.4987 0.1111  0.0802  -0.1070 314 GLU B CB  
6606 C CG  . GLU B 287 ? 0.8882 0.6207 0.5195 0.1046  0.0798  -0.1203 314 GLU B CG  
6607 C CD  . GLU B 287 ? 1.0357 0.7364 0.6502 0.1041  0.0847  -0.1353 314 GLU B CD  
6608 O OE1 . GLU B 287 ? 1.1043 0.7834 0.7168 0.0942  0.0826  -0.1395 314 GLU B OE1 
6609 O OE2 . GLU B 287 ? 1.2546 0.9506 0.8572 0.1135  0.0916  -0.1429 314 GLU B OE2 
6610 N N   . VAL B 288 ? 0.9534 0.6952 0.6358 0.1363  0.0842  -0.0811 315 VAL B N   
6611 C CA  . VAL B 288 ? 0.7845 0.5249 0.4809 0.1423  0.0820  -0.0701 315 VAL B CA  
6612 C C   . VAL B 288 ? 0.9401 0.6663 0.6368 0.1582  0.0884  -0.0710 315 VAL B C   
6613 O O   . VAL B 288 ? 0.9839 0.6897 0.6808 0.1626  0.0878  -0.0677 315 VAL B O   
6614 C CB  . VAL B 288 ? 0.8343 0.6057 0.5472 0.1424  0.0783  -0.0589 315 VAL B CB  
6615 C CG1 . VAL B 288 ? 0.8411 0.6142 0.5682 0.1514  0.0766  -0.0491 315 VAL B CG1 
6616 C CG2 . VAL B 288 ? 0.6797 0.4603 0.3932 0.1283  0.0714  -0.0560 315 VAL B CG2 
6617 N N   . MET B 289 ? 0.8992 0.6357 0.5951 0.1680  0.0953  -0.0753 316 MET B N   
6618 C CA  . MET B 289 ? 0.8910 0.6195 0.5902 0.1855  0.1020  -0.0756 316 MET B CA  
6619 C C   . MET B 289 ? 0.9145 0.6046 0.5959 0.1894  0.1069  -0.0856 316 MET B C   
6620 O O   . MET B 289 ? 0.8918 0.5706 0.5745 0.2055  0.1126  -0.0857 316 MET B O   
6621 C CB  . MET B 289 ? 0.7589 0.5115 0.4631 0.1945  0.1092  -0.0773 316 MET B CB  
6622 C CG  . MET B 289 ? 0.8558 0.6445 0.5793 0.1922  0.1061  -0.0665 316 MET B CG  
6623 S SD  . MET B 289 ? 1.1088 0.9253 0.8407 0.2039  0.1168  -0.0671 316 MET B SD  
6624 C CE  . MET B 289 ? 1.0623 0.8695 0.7678 0.1972  0.1221  -0.0802 316 MET B CE  
6625 N N   . VAL B 290 ? 1.0001 0.6698 0.6657 0.1753  0.1049  -0.0941 317 VAL B N   
6626 C CA  . VAL B 290 ? 1.0263 0.6558 0.6745 0.1767  0.1097  -0.1040 317 VAL B CA  
6627 C C   . VAL B 290 ? 1.0376 0.6453 0.6899 0.1835  0.1086  -0.0951 317 VAL B C   
6628 O O   . VAL B 290 ? 1.2833 0.8677 0.9303 0.1983  0.1149  -0.0967 317 VAL B O   
6629 C CB  . VAL B 290 ? 1.1346 0.7505 0.7676 0.1573  0.1068  -0.1149 317 VAL B CB  
6630 C CG1 . VAL B 290 ? 1.0399 0.6111 0.6558 0.1560  0.1116  -0.1244 317 VAL B CG1 
6631 C CG2 . VAL B 290 ? 1.1360 0.7707 0.7608 0.1533  0.1082  -0.1246 317 VAL B CG2 
6632 N N   . LYS B 291 ? 1.1047 0.7195 0.7657 0.1741  0.1009  -0.0852 318 LYS B N   
6633 C CA  . LYS B 291 ? 1.0894 0.6833 0.7516 0.1789  0.0992  -0.0760 318 LYS B CA  
6634 C C   . LYS B 291 ? 0.9696 0.5906 0.6505 0.1852  0.0927  -0.0614 318 LYS B C   
6635 O O   . LYS B 291 ? 1.0636 0.6704 0.7452 0.1914  0.0906  -0.0527 318 LYS B O   
6636 C CB  . LYS B 291 ? 1.2453 0.8152 0.8968 0.1611  0.0968  -0.0782 318 LYS B CB  
6637 C CG  . LYS B 291 ? 1.4334 0.9698 1.0655 0.1541  0.1031  -0.0929 318 LYS B CG  
6638 C CD  . LYS B 291 ? 1.5899 1.1074 1.2149 0.1342  0.1009  -0.0950 318 LYS B CD  
6639 C CE  . LYS B 291 ? 1.6230 1.1077 1.2294 0.1251  0.1067  -0.1110 318 LYS B CE  
6640 N NZ  . LYS B 291 ? 1.4499 0.9203 1.0521 0.1035  0.1048  -0.1138 318 LYS B NZ  
6641 N N   . HIS B 292 ? 0.8630 0.7790 0.4920 0.0634  -0.0472 -0.0196 319 HIS B N   
6642 C CA  . HIS B 292 ? 0.8785 0.8032 0.5226 0.0673  -0.0544 -0.0199 319 HIS B CA  
6643 C C   . HIS B 292 ? 0.8633 0.7903 0.5365 0.0748  -0.0502 -0.0228 319 HIS B C   
6644 O O   . HIS B 292 ? 0.8809 0.8031 0.5594 0.0770  -0.0397 -0.0239 319 HIS B O   
6645 C CB  . HIS B 292 ? 0.8240 0.7631 0.4609 0.0642  -0.0532 -0.0213 319 HIS B CB  
6646 C CG  . HIS B 292 ? 0.9567 0.8983 0.5689 0.0563  -0.0538 -0.0206 319 HIS B CG  
6647 N ND1 . HIS B 292 ? 1.1051 1.0494 0.7059 0.0524  -0.0461 -0.0229 319 HIS B ND1 
6648 C CD2 . HIS B 292 ? 0.8446 0.7868 0.4421 0.0512  -0.0604 -0.0189 319 HIS B CD2 
6649 C CE1 . HIS B 292 ? 0.9628 0.9122 0.5466 0.0443  -0.0478 -0.0236 319 HIS B CE1 
6650 N NE2 . HIS B 292 ? 0.9720 0.9190 0.5526 0.0433  -0.0553 -0.0207 319 HIS B NE2 
6651 N N   . PRO B 293 ? 0.7790 0.7133 0.4719 0.0785  -0.0576 -0.0249 320 PRO B N   
6652 C CA  . PRO B 293 ? 0.6894 0.6303 0.4131 0.0829  -0.0507 -0.0297 320 PRO B CA  
6653 C C   . PRO B 293 ? 0.7925 0.7376 0.5124 0.0807  -0.0373 -0.0312 320 PRO B C   
6654 O O   . PRO B 293 ? 0.8656 0.8133 0.5628 0.0773  -0.0376 -0.0293 320 PRO B O   
6655 C CB  . PRO B 293 ? 0.6481 0.5980 0.3902 0.0855  -0.0641 -0.0331 320 PRO B CB  
6656 C CG  . PRO B 293 ? 0.7052 0.6464 0.4261 0.0860  -0.0787 -0.0289 320 PRO B CG  
6657 C CD  . PRO B 293 ? 0.7138 0.6481 0.4020 0.0790  -0.0730 -0.0238 320 PRO B CD  
6658 N N   . PRO B 294 ? 0.8803 0.8247 0.6203 0.0834  -0.0246 -0.0350 321 PRO B N   
6659 C CA  . PRO B 294 ? 0.7437 0.6860 0.4745 0.0829  -0.0109 -0.0360 321 PRO B CA  
6660 C C   . PRO B 294 ? 0.7830 0.7337 0.5113 0.0806  -0.0158 -0.0373 321 PRO B C   
6661 O O   . PRO B 294 ? 0.7164 0.6751 0.4646 0.0796  -0.0246 -0.0404 321 PRO B O   
6662 C CB  . PRO B 294 ? 0.6403 0.5773 0.3960 0.0855  0.0042  -0.0403 321 PRO B CB  
6663 C CG  . PRO B 294 ? 0.7281 0.6736 0.5156 0.0867  -0.0052 -0.0437 321 PRO B CG  
6664 C CD  . PRO B 294 ? 0.8602 0.8044 0.6312 0.0874  -0.0210 -0.0389 321 PRO B CD  
6665 N N   . ALA B 295 ? 0.7444 0.6931 0.4471 0.0808  -0.0110 -0.0357 322 ALA B N   
6666 C CA  . ALA B 295 ? 0.6294 0.5837 0.3252 0.0797  -0.0141 -0.0367 322 ALA B CA  
6667 C C   . ALA B 295 ? 0.6651 0.6156 0.3816 0.0796  -0.0040 -0.0416 322 ALA B C   
6668 O O   . ALA B 295 ? 0.7569 0.6953 0.4708 0.0820  0.0126  -0.0428 322 ALA B O   
6669 C CB  . ALA B 295 ? 0.7205 0.6736 0.3847 0.0823  -0.0102 -0.0349 322 ALA B CB  
6670 N N   . GLU B 296 ? 0.6869 0.6460 0.4223 0.0765  -0.0134 -0.0450 323 GLU B N   
6671 C CA  . GLU B 296 ? 0.7738 0.7320 0.5358 0.0741  -0.0049 -0.0518 323 GLU B CA  
6672 C C   . GLU B 296 ? 0.8686 0.8164 0.6123 0.0739  0.0069  -0.0525 323 GLU B C   
6673 O O   . GLU B 296 ? 0.7475 0.6956 0.4638 0.0758  0.0011  -0.0490 323 GLU B O   
6674 C CB  . GLU B 296 ? 0.7396 0.7116 0.5274 0.0714  -0.0213 -0.0568 323 GLU B CB  
6675 C CG  . GLU B 296 ? 1.1233 1.1027 0.9308 0.0739  -0.0325 -0.0573 323 GLU B CG  
6676 C CD  . GLU B 296 ? 1.2205 1.1976 1.0535 0.0749  -0.0181 -0.0610 323 GLU B CD  
6677 O OE1 . GLU B 296 ? 1.2460 1.2247 1.1045 0.0715  -0.0060 -0.0685 323 GLU B OE1 
6678 O OE2 . GLU B 296 ? 1.1247 1.0973 0.9517 0.0785  -0.0176 -0.0568 323 GLU B OE2 
6679 N N   . PRO B 297 ? 0.8034 0.7406 0.5608 0.0719  0.0245  -0.0574 324 PRO B N   
6680 C CA  . PRO B 297 ? 0.7237 0.6451 0.4602 0.0724  0.0376  -0.0582 324 PRO B CA  
6681 C C   . PRO B 297 ? 0.8170 0.7453 0.5641 0.0670  0.0291  -0.0632 324 PRO B C   
6682 O O   . PRO B 297 ? 0.8521 0.7979 0.6218 0.0636  0.0121  -0.0663 324 PRO B O   
6683 C CB  . PRO B 297 ? 0.7052 0.6094 0.4537 0.0708  0.0615  -0.0621 324 PRO B CB  
6684 C CG  . PRO B 297 ? 0.6664 0.5868 0.4593 0.0659  0.0572  -0.0677 324 PRO B CG  
6685 C CD  . PRO B 297 ? 0.7141 0.6509 0.5049 0.0695  0.0355  -0.0627 324 PRO B CD  
6686 N N   . SER B 298 ? 0.8093 0.7207 0.5365 0.0673  0.0411  -0.0642 325 SER B N   
6687 C CA  . SER B 298 ? 0.8462 0.7598 0.5806 0.0617  0.0357  -0.0696 325 SER B CA  
6688 C C   . SER B 298 ? 0.8364 0.7546 0.6147 0.0518  0.0421  -0.0804 325 SER B C   
6689 O O   . SER B 298 ? 0.9339 0.8452 0.7301 0.0493  0.0591  -0.0836 325 SER B O   
6690 C CB  . SER B 298 ? 0.7853 0.6756 0.4829 0.0656  0.0486  -0.0678 325 SER B CB  
6691 O OG  . SER B 298 ? 0.9192 0.8050 0.6274 0.0582  0.0502  -0.0749 325 SER B OG  
6692 N N   . ARG B 299 ? 0.8479 0.7788 0.6444 0.0462  0.0280  -0.0870 326 ARG B N   
6693 C CA  . ARG B 299 ? 0.8653 0.8037 0.7058 0.0360  0.0325  -0.1000 326 ARG B CA  
6694 C C   . ARG B 299 ? 0.8773 0.7909 0.7135 0.0292  0.0596  -0.1051 326 ARG B C   
6695 O O   . ARG B 299 ? 0.9969 0.9138 0.8715 0.0195  0.0717  -0.1164 326 ARG B O   
6696 C CB  . ARG B 299 ? 0.8653 0.8211 0.7204 0.0328  0.0092  -0.1065 326 ARG B CB  
6697 C CG  . ARG B 299 ? 0.9817 0.9523 0.8875 0.0227  0.0082  -0.1225 326 ARG B CG  
6698 C CD  . ARG B 299 ? 1.1551 1.1368 1.0651 0.0205  -0.0142 -0.1289 326 ARG B CD  
6699 N NE  . ARG B 299 ? 1.3483 1.3400 1.2387 0.0303  -0.0393 -0.1204 326 ARG B NE  
6700 C CZ  . ARG B 299 ? 1.3524 1.3487 1.2319 0.0319  -0.0602 -0.1219 326 ARG B CZ  
6701 N NH1 . ARG B 299 ? 1.3208 1.3145 1.2079 0.0246  -0.0612 -0.1320 326 ARG B NH1 
6702 N NH2 . ARG B 299 ? 1.1540 1.1552 1.0123 0.0406  -0.0794 -0.1133 326 ARG B NH2 
6703 N N   . PHE B 300 ? 0.9654 0.8535 0.7554 0.0346  0.0703  -0.0977 327 PHE B N   
6704 C CA  . PHE B 300 ? 1.0333 0.8908 0.8091 0.0298  0.0962  -0.1015 327 PHE B CA  
6705 C C   . PHE B 300 ? 0.9823 0.8108 0.7253 0.0375  0.1192  -0.0941 327 PHE B C   
6706 O O   . PHE B 300 ? 0.9983 0.7976 0.7332 0.0328  0.1451  -0.0979 327 PHE B O   
6707 C CB  . PHE B 300 ? 0.8475 0.6924 0.5914 0.0313  0.0907  -0.1004 327 PHE B CB  
6708 C CG  . PHE B 300 ? 0.9129 0.7846 0.6729 0.0290  0.0628  -0.1037 327 PHE B CG  
6709 C CD1 . PHE B 300 ? 0.8044 0.6880 0.6027 0.0168  0.0575  -0.1169 327 PHE B CD1 
6710 C CD2 . PHE B 300 ? 0.9709 0.8552 0.7074 0.0390  0.0421  -0.0945 327 PHE B CD2 
6711 C CE1 . PHE B 300 ? 0.8880 0.7932 0.6969 0.0165  0.0308  -0.1201 327 PHE B CE1 
6712 C CE2 . PHE B 300 ? 0.9188 0.8229 0.6651 0.0376  0.0179  -0.0970 327 PHE B CE2 
6713 C CZ  . PHE B 300 ? 0.8755 0.7889 0.6561 0.0273  0.0115  -0.1094 327 PHE B CZ  
6714 N N   . ILE B 301 ? 0.9472 0.7809 0.6694 0.0490  0.1111  -0.0843 328 ILE B N   
6715 C CA  . ILE B 301 ? 0.9131 0.7211 0.6036 0.0581  0.1296  -0.0778 328 ILE B CA  
6716 C C   . ILE B 301 ? 0.9760 0.7976 0.6956 0.0568  0.1312  -0.0781 328 ILE B C   
6717 O O   . ILE B 301 ? 0.9651 0.8158 0.7053 0.0574  0.1100  -0.0768 328 ILE B O   
6718 C CB  . ILE B 301 ? 0.8950 0.6982 0.5373 0.0731  0.1193  -0.0678 328 ILE B CB  
6719 C CG1 . ILE B 301 ? 0.9763 0.7682 0.5901 0.0761  0.1163  -0.0676 328 ILE B CG1 
6720 C CG2 . ILE B 301 ? 1.2208 0.9955 0.8283 0.0839  0.1374  -0.0627 328 ILE B CG2 
6721 C CD1 . ILE B 301 ? 1.0852 0.8748 0.6546 0.0919  0.1073  -0.0596 328 ILE B CD1 
6722 N N   . SER B 302 ? 1.1176 0.9150 0.8354 0.0558  0.1571  -0.0797 329 SER B N   
6723 C CA  . SER B 302 ? 1.0799 0.8839 0.8184 0.0565  0.1624  -0.0794 329 SER B CA  
6724 C C   . SER B 302 ? 1.1206 0.8965 0.8121 0.0695  0.1743  -0.0708 329 SER B C   
6725 O O   . SER B 302 ? 1.2355 0.9761 0.8880 0.0746  0.1926  -0.0689 329 SER B O   
6726 C CB  . SER B 302 ? 1.1144 0.9156 0.8954 0.0439  0.1839  -0.0902 329 SER B CB  
6727 O OG  . SER B 302 ? 1.2709 1.0999 1.0971 0.0324  0.1714  -0.1003 329 SER B OG  
6728 N N   . ALA B 303 ? 1.2418 1.0315 0.9344 0.0757  0.1633  -0.0661 330 ALA B N   
6729 C CA  . ALA B 303 ? 1.3002 1.0655 0.9516 0.0880  0.1730  -0.0596 330 ALA B CA  
6730 C C   . ALA B 303 ? 1.2115 0.9499 0.8682 0.0856  0.2023  -0.0626 330 ALA B C   
6731 O O   . ALA B 303 ? 1.0790 0.8305 0.7822 0.0747  0.2095  -0.0695 330 ALA B O   
6732 C CB  . ALA B 303 ? 1.1531 0.9414 0.8047 0.0938  0.1519  -0.0547 330 ALA B CB  
6733 N N   . PRO B 304 ? 1.4384 1.1386 1.0474 0.0964  0.2199  -0.0583 331 PRO B N   
6734 C CA  . PRO B 304 ? 1.3758 1.0448 0.9842 0.0945  0.2507  -0.0607 331 PRO B CA  
6735 C C   . PRO B 304 ? 1.3280 1.0155 0.9688 0.0925  0.2487  -0.0617 331 PRO B C   
6736 O O   . PRO B 304 ? 1.2256 0.9336 0.8638 0.0988  0.2271  -0.0573 331 PRO B O   
6737 C CB  . PRO B 304 ? 1.2199 0.8449 0.7608 0.1110  0.2627  -0.0543 331 PRO B CB  
6738 C CG  . PRO B 304 ? 1.2830 0.9276 0.7990 0.1225  0.2335  -0.0490 331 PRO B CG  
6739 C CD  . PRO B 304 ? 1.3574 1.0397 0.9097 0.1119  0.2131  -0.0518 331 PRO B CD  
6740 N N   . THR B 305 ? 1.4769 1.1562 1.1489 0.0832  0.2726  -0.0682 332 THR B N   
6741 C CA  . THR B 305 ? 1.3867 1.0814 1.0914 0.0818  0.2739  -0.0701 332 THR B CA  
6742 C C   . THR B 305 ? 1.3463 1.0132 1.0054 0.0958  0.2802  -0.0627 332 THR B C   
6743 O O   . THR B 305 ? 1.4325 1.0570 1.0426 0.1038  0.2994  -0.0594 332 THR B O   
6744 C CB  . THR B 305 ? 1.4513 1.1429 1.1999 0.0690  0.3012  -0.0802 332 THR B CB  
6745 O OG1 . THR B 305 ? 1.3087 1.0276 1.1006 0.0558  0.2936  -0.0889 332 THR B OG1 
6746 C CG2 . THR B 305 ? 1.3080 1.0181 1.0932 0.0688  0.3018  -0.0830 332 THR B CG2 
6747 N N   . LYS B 306 ? 1.2835 0.9723 0.9560 0.0994  0.2635  -0.0605 333 LYS B N   
6748 C CA  . LYS B 306 ? 1.3941 1.0601 1.0297 0.1114  0.2681  -0.0552 333 LYS B CA  
6749 C C   . LYS B 306 ? 1.1933 0.8529 0.8566 0.1081  0.2888  -0.0591 333 LYS B C   
6750 O O   . LYS B 306 ? 1.3206 1.0053 1.0391 0.0974  0.2916  -0.0661 333 LYS B O   
6751 C CB  . LYS B 306 ? 1.3679 1.0586 0.9940 0.1176  0.2366  -0.0503 333 LYS B CB  
6752 C CG  . LYS B 306 ? 1.0991 0.8346 0.7724 0.1086  0.2122  -0.0527 333 LYS B CG  
6753 C CD  . LYS B 306 ? 1.1331 0.8870 0.7868 0.1135  0.1835  -0.0477 333 LYS B CD  
6754 C CE  . LYS B 306 ? 1.0650 0.8064 0.6750 0.1203  0.1794  -0.0447 333 LYS B CE  
6755 N NZ  . LYS B 306 ? 1.0578 0.8203 0.6525 0.1239  0.1529  -0.0416 333 LYS B NZ  
6756 N N   . THR B 307 ? 1.2442 0.8699 0.8682 0.1184  0.3032  -0.0553 334 THR B N   
6757 C CA  . THR B 307 ? 1.4303 1.0436 1.0720 0.1173  0.3256  -0.0583 334 THR B CA  
6758 C C   . THR B 307 ? 1.2207 0.8273 0.8342 0.1289  0.3143  -0.0531 334 THR B C   
6759 O O   . THR B 307 ? 1.3230 0.8989 0.8789 0.1409  0.3148  -0.0480 334 THR B O   
6760 C CB  . THR B 307 ? 1.4073 0.9735 1.0245 0.1172  0.3643  -0.0602 334 THR B CB  
6761 O OG1 . THR B 307 ? 1.5890 1.1157 1.1363 0.1303  0.3664  -0.0536 334 THR B OG1 
6762 C CG2 . THR B 307 ? 1.2416 0.8172 0.8978 0.1021  0.3785  -0.0679 334 THR B CG2 
6763 N N   . PRO B 308 ? 1.2542 0.8870 0.9041 0.1266  0.3037  -0.0547 335 PRO B N   
6764 C CA  . PRO B 308 ? 1.1940 0.8214 0.8172 0.1361  0.2908  -0.0502 335 PRO B CA  
6765 C C   . PRO B 308 ? 1.2312 0.8196 0.8297 0.1434  0.3175  -0.0499 335 PRO B C   
6766 O O   . PRO B 308 ? 1.2048 0.7781 0.8217 0.1393  0.3464  -0.0541 335 PRO B O   
6767 C CB  . PRO B 308 ? 1.1399 0.8086 0.8130 0.1303  0.2700  -0.0523 335 PRO B CB  
6768 C CG  . PRO B 308 ? 0.9712 0.6562 0.6994 0.1205  0.2850  -0.0599 335 PRO B CG  
6769 C CD  . PRO B 308 ? 1.1347 0.8053 0.8516 0.1157  0.2996  -0.0615 335 PRO B CD  
6770 N N   . ASP B 309 ? 1.2683 0.8405 0.8246 0.1541  0.3078  -0.0458 336 ASP B N   
6771 C CA  . ASP B 309 ? 1.1833 0.7187 0.7127 0.1624  0.3290  -0.0452 336 ASP B CA  
6772 C C   . ASP B 309 ? 1.2756 0.8217 0.8032 0.1665  0.3104  -0.0439 336 ASP B C   
6773 O O   . ASP B 309 ? 1.2084 0.7905 0.7602 0.1615  0.2834  -0.0435 336 ASP B O   
6774 C CB  . ASP B 309 ? 1.1802 0.6791 0.6571 0.1690  0.3317  -0.0383 336 ASP B CB  
6775 C CG  . ASP B 309 ? 1.3673 0.8736 0.8088 0.1764  0.3014  -0.0347 336 ASP B CG  
6776 O OD1 . ASP B 309 ? 1.5477 1.0826 0.9971 0.1765  0.2828  -0.0385 336 ASP B OD1 
6777 O OD2 . ASP B 309 ? 1.4933 0.9766 0.8997 0.1825  0.2962  -0.0286 336 ASP B OD2 
6778 N N   . LYS B 310 ? 1.3711 0.8834 0.8680 0.1753  0.3252  -0.0432 337 LYS B N   
6779 C CA  . LYS B 310 ? 1.2010 0.7171 0.6904 0.1794  0.3096  -0.0423 337 LYS B CA  
6780 C C   . LYS B 310 ? 1.2686 0.7688 0.7046 0.1874  0.2913  -0.0388 337 LYS B C   
6781 O O   . LYS B 310 ? 1.2871 0.7798 0.7072 0.1915  0.2833  -0.0387 337 LYS B O   
6782 C CB  . LYS B 310 ? 1.2169 0.7119 0.7159 0.1823  0.3341  -0.0441 337 LYS B CB  
6783 C CG  . LYS B 310 ? 1.1084 0.6326 0.6745 0.1730  0.3429  -0.0482 337 LYS B CG  
6784 C CD  . LYS B 310 ? 1.3503 0.9152 0.9521 0.1685  0.3134  -0.0483 337 LYS B CD  
6785 C CE  . LYS B 310 ? 1.3258 0.9214 0.9940 0.1619  0.3192  -0.0537 337 LYS B CE  
6786 N NZ  . LYS B 310 ? 1.1864 0.7640 0.8677 0.1664  0.3462  -0.0572 337 LYS B NZ  
6787 N N   . MET B 311 ? 1.2936 0.7933 0.7090 0.1881  0.2807  -0.0355 338 MET B N   
6788 C CA  . MET B 311 ? 1.3473 0.8411 0.7248 0.1947  0.2585  -0.0325 338 MET B CA  
6789 C C   . MET B 311 ? 1.3681 0.8285 0.7181 0.2015  0.2643  -0.0286 338 MET B C   
6790 O O   . MET B 311 ? 1.4004 0.8590 0.7249 0.2074  0.2452  -0.0289 338 MET B O   
6791 C CB  . MET B 311 ? 1.3454 0.8674 0.7210 0.1940  0.2324  -0.0369 338 MET B CB  
6792 C CG  . MET B 311 ? 1.2756 0.8291 0.6665 0.1890  0.2202  -0.0393 338 MET B CG  
6793 S SD  . MET B 311 ? 1.3544 0.9426 0.7500 0.1835  0.1886  -0.0426 338 MET B SD  
6794 C CE  . MET B 311 ? 1.3101 0.9043 0.7445 0.1755  0.1932  -0.0416 338 MET B CE  
6795 N N   . GLY B 312 ? 1.3007 0.7349 0.6559 0.2006  0.2905  -0.0254 339 GLY B N   
6796 C CA  . GLY B 312 ? 1.1599 0.5600 0.4877 0.2071  0.2979  -0.0211 339 GLY B CA  
6797 C C   . GLY B 312 ? 1.3717 0.7714 0.7053 0.2076  0.2991  -0.0239 339 GLY B C   
6798 O O   . GLY B 312 ? 1.6406 1.0106 0.9555 0.2120  0.3098  -0.0204 339 GLY B O   
6799 N N   . PHE B 313 ? 1.2644 0.6933 0.6205 0.2038  0.2887  -0.0298 340 PHE B N   
6800 C CA  . PHE B 313 ? 1.4036 0.8298 0.7661 0.2046  0.2913  -0.0326 340 PHE B CA  
6801 C C   . PHE B 313 ? 1.3211 0.7380 0.7142 0.2021  0.3204  -0.0325 340 PHE B C   
6802 O O   . PHE B 313 ? 1.3547 0.7788 0.7755 0.1969  0.3366  -0.0331 340 PHE B O   
6803 C CB  . PHE B 313 ? 1.2290 0.6852 0.6066 0.2016  0.2740  -0.0387 340 PHE B CB  
6804 C CG  . PHE B 313 ? 1.3050 0.7731 0.6558 0.2022  0.2453  -0.0403 340 PHE B CG  
6805 C CD1 . PHE B 313 ? 1.3089 0.7656 0.6338 0.2051  0.2327  -0.0417 340 PHE B CD1 
6806 C CD2 . PHE B 313 ? 1.3185 0.8111 0.6728 0.1991  0.2310  -0.0412 340 PHE B CD2 
6807 C CE1 . PHE B 313 ? 1.3152 0.7873 0.6222 0.2040  0.2066  -0.0452 340 PHE B CE1 
6808 C CE2 . PHE B 313 ? 1.2794 0.7876 0.6154 0.1986  0.2047  -0.0437 340 PHE B CE2 
6809 C CZ  . PHE B 313 ? 1.2804 0.7798 0.5947 0.2006  0.1927  -0.0463 340 PHE B CZ  
6810 N N   . ASP B 314 ? 1.1520 0.5540 0.5419 0.2053  0.3269  -0.0326 341 ASP B N   
6811 C CA  . ASP B 314 ? 1.4110 0.8093 0.8352 0.2033  0.3532  -0.0339 341 ASP B CA  
6812 C C   . ASP B 314 ? 1.3696 0.8014 0.8437 0.2001  0.3549  -0.0413 341 ASP B C   
6813 O O   . ASP B 314 ? 1.4426 0.8833 0.9584 0.1965  0.3759  -0.0445 341 ASP B O   
6814 C CB  . ASP B 314 ? 1.4003 0.7748 0.8075 0.2086  0.3582  -0.0321 341 ASP B CB  
6815 C CG  . ASP B 314 ? 1.4107 0.7498 0.7686 0.2134  0.3569  -0.0251 341 ASP B CG  
6816 O OD1 . ASP B 314 ? 1.5341 0.8689 0.8688 0.2142  0.3470  -0.0221 341 ASP B OD1 
6817 O OD2 . ASP B 314 ? 1.8427 1.1574 1.1848 0.2175  0.3652  -0.0227 341 ASP B OD2 
6818 N N   . GLU B 315 ? 1.3566 0.8074 0.8282 0.2016  0.3329  -0.0448 342 GLU B N   
6819 C CA  . GLU B 315 ? 1.3086 0.8043 0.8394 0.1925  0.3187  -0.0459 342 GLU B CA  
6820 C C   . GLU B 315 ? 1.2444 0.7654 0.7687 0.1871  0.2845  -0.0439 342 GLU B C   
6821 O O   . GLU B 315 ? 1.2343 0.7407 0.7160 0.1901  0.2712  -0.0429 342 GLU B O   
6822 C CB  . GLU B 315 ? 1.1370 0.6369 0.6986 0.1951  0.3240  -0.0479 342 GLU B CB  
6823 C CG  . GLU B 315 ? 1.2717 0.8156 0.8923 0.1890  0.3082  -0.0498 342 GLU B CG  
6824 C CD  . GLU B 315 ? 1.3075 0.8765 0.9749 0.1827  0.3193  -0.0537 342 GLU B CD  
6825 O OE1 . GLU B 315 ? 1.2414 0.8215 0.9040 0.1765  0.3107  -0.0524 342 GLU B OE1 
6826 O OE2 . GLU B 315 ? 1.2545 0.8327 0.9645 0.1838  0.3367  -0.0590 342 GLU B OE2 
6827 N N   . VAL B 316 ? 1.2609 0.8198 0.8278 0.1788  0.2712  -0.0442 343 VAL B N   
6828 C CA  . VAL B 316 ? 1.1980 0.7834 0.7656 0.1724  0.2406  -0.0424 343 VAL B CA  
6829 C C   . VAL B 316 ? 1.1819 0.7952 0.7955 0.1687  0.2288  -0.0431 343 VAL B C   
6830 O O   . VAL B 316 ? 1.1293 0.7652 0.7875 0.1659  0.2332  -0.0455 343 VAL B O   
6831 C CB  . VAL B 316 ? 1.2089 0.8102 0.7760 0.1674  0.2338  -0.0419 343 VAL B CB  
6832 C CG1 . VAL B 316 ? 1.0631 0.6937 0.6358 0.1602  0.2040  -0.0404 343 VAL B CG1 
6833 C CG2 . VAL B 316 ? 1.0027 0.5737 0.5188 0.1740  0.2434  -0.0413 343 VAL B CG2 
6834 N N   . PHE B 317 ? 1.2135 0.8238 0.8150 0.1693  0.2137  -0.0417 344 PHE B N   
6835 C CA  . PHE B 317 ? 1.0258 0.6561 0.6614 0.1682  0.2007  -0.0418 344 PHE B CA  
6836 C C   . PHE B 317 ? 0.9890 0.6436 0.6269 0.1599  0.1744  -0.0396 344 PHE B C   
6837 O O   . PHE B 317 ? 1.0687 0.7215 0.6758 0.1551  0.1643  -0.0383 344 PHE B O   
6838 C CB  . PHE B 317 ? 1.0484 0.6560 0.6665 0.1739  0.2012  -0.0413 344 PHE B CB  
6839 C CG  . PHE B 317 ? 1.1561 0.7389 0.7728 0.1829  0.2275  -0.0435 344 PHE B CG  
6840 C CD1 . PHE B 317 ? 1.1231 0.7165 0.7835 0.1882  0.2396  -0.0466 344 PHE B CD1 
6841 C CD2 . PHE B 317 ? 1.2939 0.8429 0.8651 0.1867  0.2398  -0.0432 344 PHE B CD2 
6842 C CE1 . PHE B 317 ? 1.1493 0.7201 0.8095 0.1961  0.2659  -0.0492 344 PHE B CE1 
6843 C CE2 . PHE B 317 ? 1.3314 0.8541 0.8978 0.1952  0.2655  -0.0450 344 PHE B CE2 
6844 C CZ  . PHE B 317 ? 1.2727 0.8064 0.8843 0.1994  0.2796  -0.0478 344 PHE B CZ  
6845 N N   . MET B 318 ? 1.0538 0.7311 0.7280 0.1593  0.1632  -0.0400 345 MET B N   
6846 C CA  . MET B 318 ? 0.9530 0.6493 0.6283 0.1525  0.1389  -0.0376 345 MET B CA  
6847 C C   . MET B 318 ? 0.9857 0.6855 0.6802 0.1572  0.1288  -0.0373 345 MET B C   
6848 O O   . MET B 318 ? 0.9557 0.6701 0.6899 0.1633  0.1326  -0.0406 345 MET B O   
6849 C CB  . MET B 318 ? 1.0466 0.7699 0.7453 0.1472  0.1338  -0.0385 345 MET B CB  
6850 C CG  . MET B 318 ? 1.0110 0.7462 0.6916 0.1387  0.1134  -0.0356 345 MET B CG  
6851 S SD  . MET B 318 ? 1.1982 0.9601 0.9097 0.1363  0.0923  -0.0350 345 MET B SD  
6852 C CE  . MET B 318 ? 0.9027 0.6875 0.6593 0.1376  0.1023  -0.0399 345 MET B CE  
6853 N N   . ILE B 319 ? 0.9352 0.6207 0.6012 0.1549  0.1163  -0.0344 346 ILE B N   
6854 C CA  . ILE B 319 ? 0.9318 0.6125 0.6057 0.1608  0.1066  -0.0333 346 ILE B CA  
6855 C C   . ILE B 319 ? 0.9086 0.6107 0.5964 0.1572  0.0865  -0.0317 346 ILE B C   
6856 O O   . ILE B 319 ? 0.9334 0.6402 0.6014 0.1469  0.0759  -0.0294 346 ILE B O   
6857 C CB  . ILE B 319 ? 1.0024 0.6520 0.6349 0.1592  0.1047  -0.0311 346 ILE B CB  
6858 C CG1 . ILE B 319 ? 1.0243 0.6514 0.6364 0.1620  0.1233  -0.0330 346 ILE B CG1 
6859 C CG2 . ILE B 319 ? 0.9891 0.6269 0.6267 0.1681  0.0984  -0.0300 346 ILE B CG2 
6860 C CD1 . ILE B 319 ? 0.9837 0.5798 0.5548 0.1596  0.1217  -0.0324 346 ILE B CD1 
6861 N N   . ASN B 320 ? 0.9203 0.6356 0.6419 0.1664  0.0810  -0.0337 347 ASN B N   
6862 C CA  . ASN B 320 ? 0.8454 0.5780 0.5785 0.1657  0.0610  -0.0327 347 ASN B CA  
6863 C C   . ASN B 320 ? 0.8590 0.5901 0.6111 0.1801  0.0530  -0.0344 347 ASN B C   
6864 O O   . ASN B 320 ? 0.8614 0.5995 0.6450 0.1906  0.0633  -0.0397 347 ASN B O   
6865 C CB  . ASN B 320 ? 0.8177 0.5816 0.5822 0.1615  0.0600  -0.0360 347 ASN B CB  
6866 C CG  . ASN B 320 ? 0.8283 0.6098 0.6067 0.1629  0.0391  -0.0360 347 ASN B CG  
6867 O OD1 . ASN B 320 ? 0.8599 0.6611 0.6771 0.1714  0.0347  -0.0415 347 ASN B OD1 
6868 N ND2 . ASN B 320 ? 0.8864 0.6607 0.6332 0.1547  0.0261  -0.0307 347 ASN B ND2 
6869 N N   . LEU B 321 ? 0.8706 0.5914 0.6023 0.1813  0.0352  -0.0304 348 LEU B N   
6870 C CA  . LEU B 321 ? 0.8857 0.6053 0.6321 0.1971  0.0232  -0.0321 348 LEU B CA  
6871 C C   . LEU B 321 ? 0.9674 0.7215 0.7533 0.2011  0.0106  -0.0370 348 LEU B C   
6872 O O   . LEU B 321 ? 0.9344 0.7014 0.7160 0.1904  0.0029  -0.0353 348 LEU B O   
6873 C CB  . LEU B 321 ? 0.9670 0.6550 0.6686 0.1972  0.0106  -0.0255 348 LEU B CB  
6874 C CG  . LEU B 321 ? 1.1460 0.8082 0.8380 0.2141  0.0078  -0.0252 348 LEU B CG  
6875 C CD1 . LEU B 321 ? 1.1850 0.8083 0.8231 0.2093  0.0004  -0.0180 348 LEU B CD1 
6876 C CD2 . LEU B 321 ? 1.2412 0.9243 0.9707 0.2330  -0.0058 -0.0306 348 LEU B CD2 
6877 N N   . ARG B 322 ? 0.8841 0.6542 0.7098 0.2169  0.0082  -0.0443 349 ARG B N   
6878 C CA  . ARG B 322 ? 1.0234 0.8308 0.8945 0.2202  -0.0017 -0.0521 349 ARG B CA  
6879 C C   . ARG B 322 ? 0.9040 0.7120 0.7579 0.2205  -0.0260 -0.0488 349 ARG B C   
6880 O O   . ARG B 322 ? 1.0136 0.8479 0.8897 0.2154  -0.0338 -0.0526 349 ARG B O   
6881 C CB  . ARG B 322 ? 0.9173 0.7434 0.8360 0.2380  -0.0008 -0.0624 349 ARG B CB  
6882 C CG  . ARG B 322 ? 1.1799 1.0491 1.1540 0.2389  -0.0066 -0.0736 349 ARG B CG  
6883 C CD  . ARG B 322 ? 1.2870 1.1803 1.3165 0.2521  0.0021  -0.0865 349 ARG B CD  
6884 N NE  . ARG B 322 ? 1.5171 1.4036 1.5480 0.2743  -0.0133 -0.0891 349 ARG B NE  
6885 C CZ  . ARG B 322 ? 1.5459 1.4171 1.5766 0.2862  -0.0019 -0.0899 349 ARG B CZ  
6886 N NH1 . ARG B 322 ? 1.4578 1.3188 1.4873 0.2781  0.0253  -0.0886 349 ARG B NH1 
6887 N NH2 . ARG B 322 ? 1.4395 1.3035 1.4685 0.3081  -0.0184 -0.0922 349 ARG B NH2 
6888 N N   . ARG B 323 ? 1.0075 0.7836 0.8189 0.2260  -0.0372 -0.0418 350 ARG B N   
6889 C CA  . ARG B 323 ? 1.0508 0.8214 0.8394 0.2265  -0.0584 -0.0380 350 ARG B CA  
6890 C C   . ARG B 323 ? 0.9633 0.7357 0.7295 0.2059  -0.0563 -0.0326 350 ARG B C   
6891 O O   . ARG B 323 ? 1.0230 0.7997 0.7800 0.2043  -0.0718 -0.0311 350 ARG B O   
6892 C CB  . ARG B 323 ? 0.9265 0.6560 0.6694 0.2365  -0.0674 -0.0314 350 ARG B CB  
6893 C CG  . ARG B 323 ? 1.0952 0.7889 0.7882 0.2220  -0.0551 -0.0226 350 ARG B CG  
6894 C CD  . ARG B 323 ? 0.9855 0.6365 0.6292 0.2292  -0.0655 -0.0160 350 ARG B CD  
6895 N NE  . ARG B 323 ? 1.2776 0.8958 0.8750 0.2124  -0.0537 -0.0092 350 ARG B NE  
6896 C CZ  . ARG B 323 ? 1.3187 0.9050 0.8921 0.2149  -0.0435 -0.0072 350 ARG B CZ  
6897 N NH1 . ARG B 323 ? 1.2570 0.8369 0.8448 0.2349  -0.0435 -0.0103 350 ARG B NH1 
6898 N NH2 . ARG B 323 ? 1.4173 0.9782 0.9522 0.1970  -0.0332 -0.0030 350 ARG B NH2 
6899 N N   . ARG B 324 ? 0.9346 0.7038 0.6913 0.1915  -0.0381 -0.0302 351 ARG B N   
6900 C CA  . ARG B 324 ? 0.9807 0.7540 0.7179 0.1734  -0.0358 -0.0263 351 ARG B CA  
6901 C C   . ARG B 324 ? 0.9040 0.7117 0.6799 0.1685  -0.0302 -0.0322 351 ARG B C   
6902 O O   . ARG B 324 ? 0.9029 0.7154 0.6825 0.1600  -0.0138 -0.0329 351 ARG B O   
6903 C CB  . ARG B 324 ? 1.0695 0.8197 0.7720 0.1619  -0.0215 -0.0217 351 ARG B CB  
6904 C CG  . ARG B 324 ? 1.0052 0.7184 0.6660 0.1634  -0.0252 -0.0163 351 ARG B CG  
6905 C CD  . ARG B 324 ? 1.2536 0.9482 0.8825 0.1493  -0.0121 -0.0139 351 ARG B CD  
6906 N NE  . ARG B 324 ? 1.2330 0.8926 0.8188 0.1453  -0.0156 -0.0093 351 ARG B NE  
6907 C CZ  . ARG B 324 ? 1.2764 0.9058 0.8423 0.1499  -0.0091 -0.0083 351 ARG B CZ  
6908 N NH1 . ARG B 324 ? 1.5217 1.1520 1.1063 0.1593  0.0013  -0.0114 351 ARG B NH1 
6909 N NH2 . ARG B 324 ? 1.1856 0.7810 0.7102 0.1444  -0.0117 -0.0043 351 ARG B NH2 
6910 N N   . GLN B 325 ? 1.0460 0.8755 0.8488 0.1746  -0.0446 -0.0369 352 GLN B N   
6911 C CA  . GLN B 325 ? 0.8827 0.7439 0.7249 0.1702  -0.0396 -0.0439 352 GLN B CA  
6912 C C   . GLN B 325 ? 0.8833 0.7478 0.7059 0.1543  -0.0354 -0.0398 352 GLN B C   
6913 O O   . GLN B 325 ? 0.9551 0.8327 0.7946 0.1475  -0.0212 -0.0429 352 GLN B O   
6914 C CB  . GLN B 325 ? 0.9250 0.8088 0.8003 0.1806  -0.0581 -0.0514 352 GLN B CB  
6915 C CG  . GLN B 325 ? 1.0570 0.9733 0.9750 0.1749  -0.0534 -0.0602 352 GLN B CG  
6916 C CD  . GLN B 325 ? 1.3335 1.2733 1.2844 0.1850  -0.0738 -0.0694 352 GLN B CD  
6917 O OE1 . GLN B 325 ? 1.3959 1.3264 1.3345 0.1980  -0.0930 -0.0685 352 GLN B OE1 
6918 N NE2 . GLN B 325 ? 1.3173 1.2861 1.3086 0.1794  -0.0701 -0.0789 352 GLN B NE2 
6919 N N   . ASP B 326 ? 0.8875 0.7387 0.6731 0.1487  -0.0466 -0.0332 353 ASP B N   
6920 C CA  . ASP B 326 ? 0.8885 0.7452 0.6565 0.1349  -0.0439 -0.0301 353 ASP B CA  
6921 C C   . ASP B 326 ? 0.9660 0.8147 0.7188 0.1265  -0.0255 -0.0283 353 ASP B C   
6922 O O   . ASP B 326 ? 0.8691 0.7303 0.6288 0.1202  -0.0165 -0.0300 353 ASP B O   
6923 C CB  . ASP B 326 ? 0.8482 0.6906 0.5794 0.1306  -0.0575 -0.0241 353 ASP B CB  
6924 C CG  . ASP B 326 ? 1.2436 1.0974 0.9858 0.1363  -0.0757 -0.0262 353 ASP B CG  
6925 O OD1 . ASP B 326 ? 1.1591 1.0342 0.9403 0.1435  -0.0791 -0.0334 353 ASP B OD1 
6926 O OD2 . ASP B 326 ? 1.4707 1.3113 1.1818 0.1334  -0.0862 -0.0213 353 ASP B OD2 
6927 N N   . ARG B 327 ? 0.9099 0.7355 0.6392 0.1273  -0.0201 -0.0251 354 ARG B N   
6928 C CA  . ARG B 327 ? 0.9053 0.7218 0.6191 0.1212  -0.0040 -0.0245 354 ARG B CA  
6929 C C   . ARG B 327 ? 0.9062 0.7335 0.6492 0.1252  0.0114  -0.0294 354 ARG B C   
6930 O O   . ARG B 327 ? 0.8743 0.7029 0.6092 0.1197  0.0227  -0.0298 354 ARG B O   
6931 C CB  . ARG B 327 ? 0.8763 0.6653 0.5644 0.1228  -0.0010 -0.0218 354 ARG B CB  
6932 C CG  . ARG B 327 ? 0.8352 0.6079 0.4881 0.1155  -0.0111 -0.0173 354 ARG B CG  
6933 C CD  . ARG B 327 ? 0.9545 0.6978 0.5812 0.1154  -0.0051 -0.0158 354 ARG B CD  
6934 N NE  . ARG B 327 ? 1.3723 1.0957 0.9653 0.1078  -0.0127 -0.0121 354 ARG B NE  
6935 C CZ  . ARG B 327 ? 1.3060 1.0002 0.8708 0.1050  -0.0086 -0.0108 354 ARG B CZ  
6936 N NH1 . ARG B 327 ? 1.2627 0.9444 0.8277 0.1099  0.0018  -0.0126 354 ARG B NH1 
6937 N NH2 . ARG B 327 ? 1.3611 1.0360 0.8951 0.0966  -0.0140 -0.0079 354 ARG B NH2 
6938 N N   . ARG B 328 ? 0.8484 0.6825 0.6248 0.1353  0.0124  -0.0337 355 ARG B N   
6939 C CA  . ARG B 328 ? 0.8176 0.6609 0.6242 0.1380  0.0298  -0.0393 355 ARG B CA  
6940 C C   . ARG B 328 ? 0.8503 0.7128 0.6716 0.1311  0.0328  -0.0421 355 ARG B C   
6941 O O   . ARG B 328 ? 0.7218 0.5804 0.5386 0.1273  0.0496  -0.0429 355 ARG B O   
6942 C CB  . ARG B 328 ? 0.7483 0.6005 0.5931 0.1499  0.0285  -0.0452 355 ARG B CB  
6943 C CG  . ARG B 328 ? 0.7448 0.6058 0.6239 0.1520  0.0494  -0.0522 355 ARG B CG  
6944 C CD  . ARG B 328 ? 0.7526 0.6227 0.6691 0.1647  0.0485  -0.0591 355 ARG B CD  
6945 N NE  . ARG B 328 ? 0.8258 0.7184 0.7688 0.1703  0.0271  -0.0639 355 ARG B NE  
6946 C CZ  . ARG B 328 ? 0.8546 0.7409 0.7878 0.1806  0.0078  -0.0619 355 ARG B CZ  
6947 N NH1 . ARG B 328 ? 0.7846 0.6423 0.6831 0.1851  0.0080  -0.0551 355 ARG B NH1 
6948 N NH2 . ARG B 328 ? 0.8255 0.7320 0.7819 0.1869  -0.0121 -0.0672 355 ARG B NH2 
6949 N N   . GLU B 329 ? 0.7698 0.6500 0.6050 0.1302  0.0166  -0.0436 356 GLU B N   
6950 C CA  . GLU B 329 ? 0.7614 0.6585 0.6102 0.1236  0.0188  -0.0467 356 GLU B CA  
6951 C C   . GLU B 329 ? 0.8096 0.6981 0.6217 0.1152  0.0230  -0.0414 356 GLU B C   
6952 O O   . GLU B 329 ? 0.8345 0.7253 0.6486 0.1115  0.0357  -0.0432 356 GLU B O   
6953 C CB  . GLU B 329 ? 0.8994 0.8148 0.7658 0.1250  -0.0016 -0.0495 356 GLU B CB  
6954 C CG  . GLU B 329 ? 1.0374 0.9662 0.9436 0.1352  -0.0088 -0.0571 356 GLU B CG  
6955 C CD  . GLU B 329 ? 1.2915 1.2351 1.2080 0.1384  -0.0322 -0.0599 356 GLU B CD  
6956 O OE1 . GLU B 329 ? 1.3656 1.3086 1.2591 0.1315  -0.0405 -0.0556 356 GLU B OE1 
6957 O OE2 . GLU B 329 ? 1.1559 1.1115 1.1027 0.1489  -0.0427 -0.0669 356 GLU B OE2 
6958 N N   . ARG B 330 ? 0.7827 0.6605 0.5608 0.1124  0.0129  -0.0355 357 ARG B N   
6959 C CA  . ARG B 330 ? 0.7078 0.5819 0.4542 0.1051  0.0152  -0.0322 357 ARG B CA  
6960 C C   . ARG B 330 ? 0.8637 0.7240 0.5960 0.1060  0.0333  -0.0326 357 ARG B C   
6961 O O   . ARG B 330 ? 0.8943 0.7554 0.6142 0.1036  0.0404  -0.0330 357 ARG B O   
6962 C CB  . ARG B 330 ? 0.7589 0.6254 0.4754 0.1007  0.0023  -0.0276 357 ARG B CB  
6963 C CG  . ARG B 330 ? 0.7837 0.6539 0.4737 0.0928  0.0015  -0.0262 357 ARG B CG  
6964 C CD  . ARG B 330 ? 0.9114 0.7716 0.5725 0.0867  -0.0057 -0.0235 357 ARG B CD  
6965 N NE  . ARG B 330 ? 1.1573 1.0011 0.8024 0.0868  0.0033  -0.0241 357 ARG B NE  
6966 C CZ  . ARG B 330 ? 1.0795 0.9223 0.7050 0.0834  0.0092  -0.0261 357 ARG B CZ  
6967 N NH1 . ARG B 330 ? 1.0802 0.9379 0.6994 0.0803  0.0075  -0.0276 357 ARG B NH1 
6968 N NH2 . ARG B 330 ? 1.0567 0.8830 0.6677 0.0843  0.0162  -0.0274 357 ARG B NH2 
6969 N N   . MET B 331 ? 0.8775 0.7226 0.6086 0.1108  0.0407  -0.0327 358 MET B N   
6970 C CA  . MET B 331 ? 0.7803 0.6085 0.4945 0.1129  0.0578  -0.0332 358 MET B CA  
6971 C C   . MET B 331 ? 0.8773 0.7075 0.6108 0.1154  0.0749  -0.0368 358 MET B C   
6972 O O   . MET B 331 ? 0.8862 0.7065 0.5988 0.1154  0.0861  -0.0368 358 MET B O   
6973 C CB  . MET B 331 ? 0.9388 0.7489 0.6483 0.1179  0.0624  -0.0327 358 MET B CB  
6974 C CG  . MET B 331 ? 0.9868 0.7867 0.6679 0.1139  0.0502  -0.0295 358 MET B CG  
6975 S SD  . MET B 331 ? 1.0364 0.8296 0.6769 0.1072  0.0512  -0.0296 358 MET B SD  
6976 C CE  . MET B 331 ? 0.9190 0.6919 0.5509 0.1151  0.0722  -0.0319 358 MET B CE  
6977 N N   . LEU B 332 ? 0.7538 0.5958 0.5265 0.1177  0.0775  -0.0407 359 LEU B N   
6978 C CA  . LEU B 332 ? 0.8200 0.6637 0.6143 0.1178  0.0961  -0.0455 359 LEU B CA  
6979 C C   . LEU B 332 ? 0.8731 0.7236 0.6585 0.1124  0.0951  -0.0453 359 LEU B C   
6980 O O   . LEU B 332 ? 0.8566 0.6949 0.6326 0.1123  0.1129  -0.0465 359 LEU B O   
6981 C CB  . LEU B 332 ? 0.7230 0.5841 0.5666 0.1202  0.0965  -0.0520 359 LEU B CB  
6982 C CG  . LEU B 332 ? 0.8133 0.6679 0.6689 0.1279  0.0992  -0.0532 359 LEU B CG  
6983 C CD1 . LEU B 332 ? 0.7213 0.5991 0.6287 0.1316  0.0953  -0.0613 359 LEU B CD1 
6984 C CD2 . LEU B 332 ? 0.7499 0.5802 0.5905 0.1308  0.1236  -0.0530 359 LEU B CD2 
6985 N N   . ARG B 333 ? 0.6992 0.5662 0.4842 0.1085  0.0752  -0.0438 360 ARG B N   
6986 C CA  . ARG B 333 ? 0.7345 0.6064 0.5056 0.1042  0.0731  -0.0430 360 ARG B CA  
6987 C C   . ARG B 333 ? 0.8660 0.7212 0.5941 0.1057  0.0787  -0.0394 360 ARG B C   
6988 O O   . ARG B 333 ? 0.8894 0.7372 0.6037 0.1064  0.0891  -0.0400 360 ARG B O   
6989 C CB  . ARG B 333 ? 0.6884 0.5786 0.4625 0.1005  0.0506  -0.0416 360 ARG B CB  
6990 C CG  . ARG B 333 ? 0.6685 0.5767 0.4828 0.1002  0.0422  -0.0466 360 ARG B CG  
6991 C CD  . ARG B 333 ? 0.8012 0.7231 0.6110 0.0969  0.0216  -0.0451 360 ARG B CD  
6992 N NE  . ARG B 333 ? 1.0132 0.9463 0.8471 0.1002  0.0058  -0.0476 360 ARG B NE  
6993 C CZ  . ARG B 333 ? 1.1218 1.0506 0.9395 0.1025  -0.0093 -0.0431 360 ARG B CZ  
6994 N NH1 . ARG B 333 ? 0.7997 0.7162 0.5808 0.0995  -0.0105 -0.0368 360 ARG B NH1 
6995 N NH2 . ARG B 333 ? 1.1367 1.0727 0.9747 0.1082  -0.0235 -0.0460 360 ARG B NH2 
6996 N N   . ALA B 334 ? 0.8356 0.6838 0.5413 0.1068  0.0717  -0.0365 361 ALA B N   
6997 C CA  . ALA B 334 ? 0.8156 0.6509 0.4824 0.1090  0.0746  -0.0351 361 ALA B CA  
6998 C C   . ALA B 334 ? 0.8570 0.6689 0.5116 0.1155  0.0960  -0.0365 361 ALA B C   
6999 O O   . ALA B 334 ? 0.8670 0.6684 0.4946 0.1194  0.1023  -0.0367 361 ALA B O   
7000 C CB  . ALA B 334 ? 0.7392 0.5723 0.3885 0.1070  0.0632  -0.0335 361 ALA B CB  
7001 N N   . LEU B 335 ? 0.8501 0.6521 0.5225 0.1180  0.1077  -0.0376 362 LEU B N   
7002 C CA  . LEU B 335 ? 0.8468 0.6231 0.5058 0.1242  0.1303  -0.0387 362 LEU B CA  
7003 C C   . LEU B 335 ? 0.9330 0.7050 0.6006 0.1239  0.1462  -0.0408 362 LEU B C   
7004 O O   . LEU B 335 ? 0.9558 0.7040 0.5931 0.1292  0.1609  -0.0406 362 LEU B O   
7005 C CB  . LEU B 335 ? 0.8004 0.5686 0.4793 0.1268  0.1399  -0.0400 362 LEU B CB  
7006 C CG  . LEU B 335 ? 1.0172 0.7814 0.6817 0.1278  0.1279  -0.0380 362 LEU B CG  
7007 C CD1 . LEU B 335 ? 0.9615 0.7178 0.6476 0.1318  0.1377  -0.0394 362 LEU B CD1 
7008 C CD2 . LEU B 335 ? 0.8721 0.6166 0.4903 0.1314  0.1288  -0.0371 362 LEU B CD2 
7009 N N   . GLN B 336 ? 0.9200 0.7127 0.6266 0.1179  0.1433  -0.0435 363 GLN B N   
7010 C CA  . GLN B 336 ? 0.9293 0.7181 0.6464 0.1153  0.1588  -0.0467 363 GLN B CA  
7011 C C   . GLN B 336 ? 0.9015 0.6828 0.5821 0.1170  0.1554  -0.0441 363 GLN B C   
7012 O O   . GLN B 336 ? 1.0331 0.7914 0.6944 0.1199  0.1741  -0.0447 363 GLN B O   
7013 C CB  . GLN B 336 ? 0.7770 0.5935 0.5433 0.1080  0.1515  -0.0515 363 GLN B CB  
7014 C CG  . GLN B 336 ? 0.9714 0.7848 0.7538 0.1029  0.1685  -0.0567 363 GLN B CG  
7015 C CD  . GLN B 336 ? 1.3433 1.1870 1.1666 0.0956  0.1544  -0.0619 363 GLN B CD  
7016 O OE1 . GLN B 336 ? 1.2875 1.1525 1.1209 0.0956  0.1306  -0.0605 363 GLN B OE1 
7017 N NE2 . GLN B 336 ? 1.3863 1.2298 1.2313 0.0892  0.1696  -0.0684 363 GLN B NE2 
7018 N N   . ALA B 337 ? 0.8609 0.6599 0.5305 0.1158  0.1325  -0.0415 364 ALA B N   
7019 C CA  . ALA B 337 ? 0.7877 0.5835 0.4249 0.1187  0.1275  -0.0399 364 ALA B CA  
7020 C C   . ALA B 337 ? 1.0483 0.8160 0.6402 0.1289  0.1378  -0.0387 364 ALA B C   
7021 O O   . ALA B 337 ? 1.0653 0.8171 0.6296 0.1347  0.1455  -0.0386 364 ALA B O   
7022 C CB  . ALA B 337 ? 0.7408 0.5618 0.3762 0.1151  0.1023  -0.0382 364 ALA B CB  
7023 N N   . GLN B 338 ? 0.8502 0.6095 0.4315 0.1323  0.1374  -0.0382 365 GLN B N   
7024 C CA  . GLN B 338 ? 0.8959 0.6278 0.4335 0.1431  0.1454  -0.0381 365 GLN B CA  
7025 C C   . GLN B 338 ? 0.9603 0.6588 0.4908 0.1481  0.1729  -0.0385 365 GLN B C   
7026 O O   . GLN B 338 ? 1.0445 0.7150 0.5369 0.1581  0.1813  -0.0383 365 GLN B O   
7027 C CB  . GLN B 338 ? 0.9347 0.6717 0.4619 0.1437  0.1320  -0.0384 365 GLN B CB  
7028 C CG  . GLN B 338 ? 1.1221 0.8888 0.6522 0.1379  0.1075  -0.0387 365 GLN B CG  
7029 C CD  . GLN B 338 ? 1.0416 0.8117 0.5644 0.1356  0.0965  -0.0399 365 GLN B CD  
7030 O OE1 . GLN B 338 ? 1.1059 0.8744 0.5995 0.1399  0.0887  -0.0430 365 GLN B OE1 
7031 N NE2 . GLN B 338 ? 0.8905 0.6653 0.4398 0.1292  0.0953  -0.0384 365 GLN B NE2 
7032 N N   . GLU B 339 ? 1.0018 0.7025 0.5678 0.1412  0.1872  -0.0398 366 GLU B N   
7033 C CA  . GLU B 339 ? 1.1017 0.7722 0.6671 0.1434  0.2166  -0.0413 366 GLU B CA  
7034 C C   . GLU B 339 ? 1.0695 0.7251 0.6280 0.1482  0.2234  -0.0410 366 GLU B C   
7035 O O   . GLU B 339 ? 1.0034 0.6229 0.5295 0.1564  0.2431  -0.0406 366 GLU B O   
7036 C CB  . GLU B 339 ? 1.1161 0.7515 0.6367 0.1518  0.2333  -0.0403 366 GLU B CB  
7037 C CG  . GLU B 339 ? 1.1898 0.8351 0.7157 0.1474  0.2298  -0.0408 366 GLU B CG  
7038 C CD  . GLU B 339 ? 1.4522 1.0564 0.9345 0.1558  0.2510  -0.0401 366 GLU B CD  
7039 O OE1 . GLU B 339 ? 1.5595 1.1356 1.0000 0.1672  0.2539  -0.0370 366 GLU B OE1 
7040 O OE2 . GLU B 339 ? 1.5265 1.1280 1.0209 0.1494  0.2614  -0.0418 366 GLU B OE2 
7041 N N   . ILE B 340 ? 1.0948 0.7751 0.6807 0.1436  0.2071  -0.0411 367 ILE B N   
7042 C CA  . ILE B 340 ? 1.1301 0.7988 0.7128 0.1474  0.2113  -0.0409 367 ILE B CA  
7043 C C   . ILE B 340 ? 1.0153 0.7013 0.6508 0.1413  0.2167  -0.0437 367 ILE B C   
7044 O O   . ILE B 340 ? 1.0174 0.7350 0.6878 0.1345  0.2001  -0.0447 367 ILE B O   
7045 C CB  . ILE B 340 ? 1.0667 0.7453 0.6295 0.1487  0.1870  -0.0393 367 ILE B CB  
7046 C CG1 . ILE B 340 ? 0.9659 0.6322 0.4801 0.1558  0.1801  -0.0389 367 ILE B CG1 
7047 C CG2 . ILE B 340 ? 1.0148 0.6788 0.5737 0.1521  0.1919  -0.0395 367 ILE B CG2 
7048 C CD1 . ILE B 340 ? 0.9138 0.5950 0.4129 0.1546  0.1561  -0.0395 367 ILE B CD1 
7049 N N   . GLU B 341 ? 0.9839 0.6489 0.6244 0.1447  0.2400  -0.0456 368 GLU B N   
7050 C CA  . GLU B 341 ? 1.0545 0.7354 0.7451 0.1414  0.2469  -0.0498 368 GLU B CA  
7051 C C   . GLU B 341 ? 1.1336 0.8072 0.8169 0.1471  0.2419  -0.0483 368 GLU B C   
7052 O O   . GLU B 341 ? 1.2213 0.8663 0.8607 0.1538  0.2466  -0.0456 368 GLU B O   
7053 C CB  . GLU B 341 ? 1.0443 0.7084 0.7514 0.1402  0.2800  -0.0545 368 GLU B CB  
7054 C CG  . GLU B 341 ? 1.2998 0.9863 1.0666 0.1364  0.2880  -0.0614 368 GLU B CG  
7055 C CD  . GLU B 341 ? 1.4012 1.0697 1.1835 0.1339  0.3241  -0.0673 368 GLU B CD  
7056 O OE1 . GLU B 341 ? 1.2377 0.8691 0.9767 0.1364  0.3441  -0.0645 368 GLU B OE1 
7057 O OE2 . GLU B 341 ? 1.5070 1.1978 1.3441 0.1297  0.3328  -0.0754 368 GLU B OE2 
7058 N N   . CYS B 342 ? 0.9322 0.6303 0.6566 0.1453  0.2316  -0.0506 369 CYS B N   
7059 C CA  . CYS B 342 ? 1.0787 0.7699 0.7959 0.1507  0.2247  -0.0490 369 CYS B CA  
7060 C C   . CYS B 342 ? 1.0536 0.7583 0.8194 0.1530  0.2328  -0.0542 369 CYS B C   
7061 O O   . CYS B 342 ? 1.1199 0.8489 0.9309 0.1490  0.2359  -0.0597 369 CYS B O   
7062 C CB  . CYS B 342 ? 1.0163 0.7223 0.7212 0.1482  0.1944  -0.0452 369 CYS B CB  
7063 S SG  . CYS B 342 ? 1.1478 0.8927 0.9033 0.1442  0.1730  -0.0473 369 CYS B SG  
7064 N N   . ARG B 343 ? 1.0124 0.7016 0.7687 0.1600  0.2357  -0.0533 370 ARG B N   
7065 C CA  . ARG B 343 ? 0.9786 0.6812 0.7774 0.1649  0.2386  -0.0581 370 ARG B CA  
7066 C C   . ARG B 343 ? 1.0615 0.7785 0.8622 0.1666  0.2096  -0.0552 370 ARG B C   
7067 O O   . ARG B 343 ? 1.1113 0.8088 0.8724 0.1682  0.2000  -0.0501 370 ARG B O   
7068 C CB  . ARG B 343 ? 0.9292 0.6024 0.7153 0.1729  0.2624  -0.0591 370 ARG B CB  
7069 C CG  . ARG B 343 ? 0.9463 0.6348 0.7802 0.1794  0.2686  -0.0654 370 ARG B CG  
7070 C CD  . ARG B 343 ? 1.0276 0.6845 0.8444 0.1879  0.2921  -0.0659 370 ARG B CD  
7071 N NE  . ARG B 343 ? 1.2338 0.9069 1.0961 0.1960  0.2961  -0.0724 370 ARG B NE  
7072 C CZ  . ARG B 343 ? 1.3668 1.0415 1.2283 0.2040  0.2783  -0.0707 370 ARG B CZ  
7073 N NH1 . ARG B 343 ? 1.3324 0.9927 1.1508 0.2032  0.2567  -0.0630 370 ARG B NH1 
7074 N NH2 . ARG B 343 ? 1.2822 0.9728 1.1870 0.2133  0.2828  -0.0776 370 ARG B NH2 
7075 N N   . LEU B 344 ? 0.9629 0.7118 0.8074 0.1661  0.1960  -0.0593 371 LEU B N   
7076 C CA  . LEU B 344 ? 0.9474 0.7070 0.7921 0.1688  0.1690  -0.0566 371 LEU B CA  
7077 C C   . LEU B 344 ? 0.9424 0.6903 0.7921 0.1800  0.1718  -0.0577 371 LEU B C   
7078 O O   . LEU B 344 ? 0.9773 0.7357 0.8666 0.1867  0.1847  -0.0648 371 LEU B O   
7079 C CB  . LEU B 344 ? 0.8687 0.6639 0.7554 0.1667  0.1531  -0.0612 371 LEU B CB  
7080 C CG  . LEU B 344 ? 1.0720 0.8771 0.9593 0.1709  0.1251  -0.0589 371 LEU B CG  
7081 C CD1 . LEU B 344 ? 1.1028 0.8948 0.9428 0.1636  0.1097  -0.0503 371 LEU B CD1 
7082 C CD2 . LEU B 344 ? 1.2063 1.0463 1.1405 0.1717  0.1123  -0.0659 371 LEU B CD2 
7083 N N   . VAL B 345 ? 0.9543 0.6804 0.7646 0.1818  0.1604  -0.0516 372 VAL B N   
7084 C CA  . VAL B 345 ? 0.9912 0.7010 0.7982 0.1928  0.1610  -0.0516 372 VAL B CA  
7085 C C   . VAL B 345 ? 1.0474 0.7657 0.8558 0.1960  0.1347  -0.0494 372 VAL B C   
7086 O O   . VAL B 345 ? 0.9978 0.7100 0.7747 0.1882  0.1188  -0.0439 372 VAL B O   
7087 C CB  . VAL B 345 ? 0.9376 0.6095 0.6941 0.1924  0.1705  -0.0471 372 VAL B CB  
7088 C CG1 . VAL B 345 ? 0.9336 0.5865 0.6864 0.2042  0.1725  -0.0475 372 VAL B CG1 
7089 C CG2 . VAL B 345 ? 0.9982 0.6573 0.7456 0.1903  0.1955  -0.0488 372 VAL B CG2 
7090 N N   . GLU B 346 ? 0.9827 0.7140 0.8264 0.2083  0.1304  -0.0543 373 GLU B N   
7091 C CA  . GLU B 346 ? 0.9893 0.7245 0.8314 0.2146  0.1055  -0.0525 373 GLU B CA  
7092 C C   . GLU B 346 ? 0.9395 0.6372 0.7335 0.2175  0.1012  -0.0458 373 GLU B C   
7093 O O   . GLU B 346 ? 1.0098 0.6873 0.7976 0.2262  0.1143  -0.0468 373 GLU B O   
7094 C CB  . GLU B 346 ? 0.9792 0.7397 0.8730 0.2295  0.1011  -0.0611 373 GLU B CB  
7095 C CG  . GLU B 346 ? 1.2080 1.0087 1.1489 0.2254  0.0967  -0.0685 373 GLU B CG  
7096 C CD  . GLU B 346 ? 1.4597 1.2873 1.4449 0.2405  0.0808  -0.0772 373 GLU B CD  
7097 O OE1 . GLU B 346 ? 1.5516 1.3664 1.5330 0.2560  0.0760  -0.0776 373 GLU B OE1 
7098 O OE2 . GLU B 346 ? 1.4135 1.2744 1.4362 0.2376  0.0724  -0.0842 373 GLU B OE2 
7099 N N   . ALA B 347 ? 1.1112 0.6489 0.8031 0.1323  0.0614  -0.0444 374 ALA B N   
7100 C CA  . ALA B 347 ? 1.0419 0.5387 0.6978 0.1251  0.0596  -0.0467 374 ALA B CA  
7101 C C   . ALA B 347 ? 1.0890 0.5495 0.7371 0.1403  0.0505  -0.0440 374 ALA B C   
7102 O O   . ALA B 347 ? 1.2132 0.6777 0.8756 0.1514  0.0401  -0.0377 374 ALA B O   
7103 C CB  . ALA B 347 ? 1.0345 0.5242 0.6662 0.1010  0.0546  -0.0427 374 ALA B CB  
7104 N N   . VAL B 348 ? 1.1081 0.5323 0.7332 0.1419  0.0534  -0.0499 375 VAL B N   
7105 C CA  . VAL B 348 ? 1.2758 0.6564 0.8871 0.1557  0.0446  -0.0476 375 VAL B CA  
7106 C C   . VAL B 348 ? 1.2520 0.5998 0.8327 0.1400  0.0337  -0.0366 375 VAL B C   
7107 O O   . VAL B 348 ? 1.2883 0.6235 0.8455 0.1166  0.0375  -0.0373 375 VAL B O   
7108 C CB  . VAL B 348 ? 1.3153 0.6652 0.9110 0.1619  0.0521  -0.0592 375 VAL B CB  
7109 C CG1 . VAL B 348 ? 1.3400 0.6388 0.9190 0.1762  0.0424  -0.0566 375 VAL B CG1 
7110 C CG2 . VAL B 348 ? 1.2160 0.5978 0.8378 0.1785  0.0652  -0.0692 375 VAL B CG2 
7111 N N   . ASP B 349 ? 1.2684 0.6030 0.8489 0.1531  0.0204  -0.0266 376 ASP B N   
7112 C CA  . ASP B 349 ? 1.5247 0.8222 1.0700 0.1414  0.0106  -0.0138 376 ASP B CA  
7113 C C   . ASP B 349 ? 1.6125 0.8473 1.1274 0.1467  0.0085  -0.0131 376 ASP B C   
7114 O O   . ASP B 349 ? 1.4732 0.6847 0.9896 0.1715  -0.0012 -0.0106 376 ASP B O   
7115 C CB  . ASP B 349 ? 1.3987 0.7095 0.9528 0.1547  -0.0046 -0.0036 376 ASP B CB  
7116 C CG  . ASP B 349 ? 1.5817 0.8674 1.0980 0.1379  -0.0114 0.0103  376 ASP B CG  
7117 O OD1 . ASP B 349 ? 1.6909 0.9437 1.1753 0.1163  -0.0035 0.0127  376 ASP B OD1 
7118 O OD2 . ASP B 349 ? 1.5759 0.8758 1.0946 0.1458  -0.0240 0.0178  376 ASP B OD2 
7119 N N   . GLY B 350 ? 1.8644 1.0718 1.3536 0.1234  0.0171  -0.0166 377 GLY B N   
7120 C CA  . GLY B 350 ? 1.9480 1.0931 1.4091 0.1254  0.0167  -0.0180 377 GLY B CA  
7121 C C   . GLY B 350 ? 1.9860 1.0779 1.4145 0.1302  0.0050  -0.0009 377 GLY B C   
7122 O O   . GLY B 350 ? 2.0789 1.1188 1.4906 0.1452  0.0003  -0.0002 377 GLY B O   
7123 N N   . LYS B 351 ? 1.7566 0.8584 1.1731 0.1191  0.0003  0.0132  378 LYS B N   
7124 C CA  . LYS B 351 ? 1.8388 0.8899 1.2188 0.1260  -0.0114 0.0315  378 LYS B CA  
7125 C C   . LYS B 351 ? 1.8246 0.8735 1.2184 0.1644  -0.0283 0.0344  378 LYS B C   
7126 O O   . LYS B 351 ? 1.8349 0.8266 1.1988 0.1795  -0.0386 0.0449  378 LYS B O   
7127 C CB  . LYS B 351 ? 1.9135 0.9814 1.2768 0.1071  -0.0121 0.0445  378 LYS B CB  
7128 C CG  . LYS B 351 ? 1.9111 0.9597 1.2473 0.0694  0.0030  0.0471  378 LYS B CG  
7129 C CD  . LYS B 351 ? 2.0187 1.1169 1.3860 0.0499  0.0166  0.0291  378 LYS B CD  
7130 C CE  . LYS B 351 ? 1.9598 1.0500 1.3075 0.0125  0.0303  0.0301  378 LYS B CE  
7131 N NZ  . LYS B 351 ? 1.6057 0.7186 0.9422 0.0012  0.0304  0.0421  378 LYS B NZ  
7132 N N   . ALA B 352 ? 1.7273 0.8370 1.1671 0.1807  -0.0311 0.0247  379 ALA B N   
7133 C CA  . ALA B 352 ? 1.6826 0.8001 1.1453 0.2168  -0.0464 0.0239  379 ALA B CA  
7134 C C   . ALA B 352 ? 1.7654 0.8560 1.2373 0.2380  -0.0441 0.0131  379 ALA B C   
7135 O O   . ALA B 352 ? 1.8886 0.9770 1.3768 0.2699  -0.0573 0.0121  379 ALA B O   
7136 C CB  . ALA B 352 ? 1.6353 0.8282 1.1489 0.2241  -0.0475 0.0157  379 ALA B CB  
7137 N N   . MET B 353 ? 1.8522 0.9237 1.3150 0.2222  -0.0286 0.0033  380 MET B N   
7138 C CA  . MET B 353 ? 1.9083 0.9547 1.3781 0.2419  -0.0250 -0.0095 380 MET B CA  
7139 C C   . MET B 353 ? 2.0656 1.0316 1.4937 0.2513  -0.0345 -0.0003 380 MET B C   
7140 O O   . MET B 353 ? 2.0203 0.9393 1.4077 0.2266  -0.0311 0.0089  380 MET B O   
7141 C CB  . MET B 353 ? 1.8803 0.9371 1.3538 0.2223  -0.0064 -0.0254 380 MET B CB  
7142 C CG  . MET B 353 ? 1.7923 0.9224 1.3042 0.2166  0.0043  -0.0348 380 MET B CG  
7143 S SD  . MET B 353 ? 1.8399 0.9772 1.3508 0.2014  0.0232  -0.0543 380 MET B SD  
7144 C CE  . MET B 353 ? 1.6754 0.7738 1.1865 0.2328  0.0234  -0.0674 380 MET B CE  
7145 N N   . ASN B 354 ? 2.1419 1.0916 1.5812 0.2870  -0.0458 -0.0029 381 ASN B N   
7146 C CA  . ASN B 354 ? 2.3051 1.1742 1.7059 0.3001  -0.0545 0.0040  381 ASN B CA  
7147 C C   . ASN B 354 ? 2.3746 1.2097 1.7688 0.2951  -0.0407 -0.0128 381 ASN B C   
7148 O O   . ASN B 354 ? 2.2564 1.1346 1.6785 0.2892  -0.0266 -0.0306 381 ASN B O   
7149 C CB  . ASN B 354 ? 2.3030 1.1675 1.7184 0.3432  -0.0744 0.0071  381 ASN B CB  
7150 C CG  . ASN B 354 ? 2.2605 1.1774 1.7314 0.3700  -0.0703 -0.0136 381 ASN B CG  
7151 O OD1 . ASN B 354 ? 2.3558 1.2690 1.8353 0.3691  -0.0553 -0.0303 381 ASN B OD1 
7152 N ND2 . ASN B 354 ? 2.1002 1.0667 1.6092 0.3941  -0.0832 -0.0136 381 ASN B ND2 
7153 N N   . THR B 355 ? 2.2244 0.9780 1.5782 0.2980  -0.0450 -0.0070 382 THR B N   
7154 C CA  . THR B 355 ? 2.1902 0.9039 1.5341 0.2926  -0.0337 -0.0242 382 THR B CA  
7155 C C   . THR B 355 ? 2.1970 0.9383 1.5781 0.3257  -0.0316 -0.0454 382 THR B C   
7156 O O   . THR B 355 ? 2.1559 0.8982 1.5420 0.3192  -0.0183 -0.0653 382 THR B O   
7157 C CB  . THR B 355 ? 2.1448 0.7608 1.4394 0.2919  -0.0398 -0.0130 382 THR B CB  
7158 O OG1 . THR B 355 ? 2.2874 0.8926 1.5859 0.3273  -0.0579 -0.0020 382 THR B OG1 
7159 C CG2 . THR B 355 ? 2.1654 0.7532 1.4219 0.2540  -0.0362 0.0067  382 THR B CG2 
7160 N N   . SER B 356 ? 2.1796 0.9459 1.5877 0.3616  -0.0443 -0.0426 383 SER B N   
7161 C CA  . SER B 356 ? 2.0720 0.8702 1.5199 0.3935  -0.0401 -0.0630 383 SER B CA  
7162 C C   . SER B 356 ? 2.0393 0.9153 1.5242 0.3802  -0.0220 -0.0774 383 SER B C   
7163 O O   . SER B 356 ? 2.0342 0.9186 1.5303 0.3864  -0.0081 -0.0975 383 SER B O   
7164 C CB  . SER B 356 ? 2.0840 0.8994 1.5585 0.4330  -0.0584 -0.0572 383 SER B CB  
7165 O OG  . SER B 356 ? 2.3453 1.1065 1.7908 0.4404  -0.0754 -0.0412 383 SER B OG  
7166 N N   . GLN B 357 ? 2.0797 1.0105 1.5808 0.3627  -0.0218 -0.0673 384 GLN B N   
7167 C CA  . GLN B 357 ? 1.9041 0.9039 1.4362 0.3489  -0.0047 -0.0782 384 GLN B CA  
7168 C C   . GLN B 357 ? 1.8826 0.8659 1.3886 0.3191  0.0099  -0.0877 384 GLN B C   
7169 O O   . GLN B 357 ? 1.8274 0.8472 1.3504 0.3178  0.0252  -0.1032 384 GLN B O   
7170 C CB  . GLN B 357 ? 2.0138 1.0676 1.5649 0.3353  -0.0092 -0.0649 384 GLN B CB  
7171 C CG  . GLN B 357 ? 2.0176 1.0982 1.6004 0.3638  -0.0250 -0.0587 384 GLN B CG  
7172 C CD  . GLN B 357 ? 2.1290 1.2353 1.7110 0.3484  -0.0359 -0.0423 384 GLN B CD  
7173 O OE1 . GLN B 357 ? 2.0465 1.1495 1.6037 0.3166  -0.0304 -0.0348 384 GLN B OE1 
7174 N NE2 . GLN B 357 ? 2.0601 1.1939 1.6705 0.3717  -0.0519 -0.0383 384 GLN B NE2 
7175 N N   . VAL B 358 ? 1.9630 0.8919 1.4275 0.2950  0.0056  -0.0789 385 VAL B N   
7176 C CA  . VAL B 358 ? 1.9672 0.8785 1.4094 0.2666  0.0172  -0.0905 385 VAL B CA  
7177 C C   . VAL B 358 ? 1.9997 0.8792 1.4367 0.2837  0.0234  -0.1119 385 VAL B C   
7178 O O   . VAL B 358 ? 1.9682 0.8694 1.4082 0.2753  0.0357  -0.1297 385 VAL B O   
7179 C CB  . VAL B 358 ? 1.9022 0.7606 1.3049 0.2365  0.0123  -0.0767 385 VAL B CB  
7180 C CG1 . VAL B 358 ? 1.8660 0.7075 1.2509 0.2069  0.0230  -0.0917 385 VAL B CG1 
7181 C CG2 . VAL B 358 ? 1.8334 0.7274 1.2399 0.2198  0.0081  -0.0574 385 VAL B CG2 
7182 N N   . GLU B 359 ? 1.9344 0.7616 1.3620 0.3100  0.0141  -0.1111 386 GLU B N   
7183 C CA  . GLU B 359 ? 1.9470 0.7416 1.3699 0.3296  0.0195  -0.1328 386 GLU B CA  
7184 C C   . GLU B 359 ? 1.9865 0.8419 1.4480 0.3557  0.0303  -0.1483 386 GLU B C   
7185 O O   . GLU B 359 ? 1.9624 0.8140 1.4204 0.3620  0.0415  -0.1700 386 GLU B O   
7186 C CB  . GLU B 359 ? 2.1038 0.8381 1.5140 0.3503  0.0060  -0.1259 386 GLU B CB  
7187 C CG  . GLU B 359 ? 2.2198 0.8903 1.5904 0.3232  -0.0016 -0.1097 386 GLU B CG  
7188 C CD  . GLU B 359 ? 2.4690 1.0989 1.8335 0.3435  -0.0168 -0.0950 386 GLU B CD  
7189 O OE1 . GLU B 359 ? 2.3631 1.0127 1.7559 0.3786  -0.0219 -0.1013 386 GLU B OE1 
7190 O OE2 . GLU B 359 ? 2.6254 1.2046 1.9568 0.3244  -0.0228 -0.0771 386 GLU B OE2 
7191 N N   . ALA B 360 ? 2.0339 0.9451 1.5318 0.3705  0.0278  -0.1383 387 ALA B N   
7192 C CA  . ALA B 360 ? 1.9514 0.9228 1.4895 0.3929  0.0409  -0.1517 387 ALA B CA  
7193 C C   . ALA B 360 ? 1.9751 0.9879 1.5132 0.3720  0.0593  -0.1626 387 ALA B C   
7194 O O   . ALA B 360 ? 1.9295 0.9697 1.4829 0.3881  0.0747  -0.1790 387 ALA B O   
7195 C CB  . ALA B 360 ? 1.8227 0.8473 1.4025 0.4070  0.0341  -0.1388 387 ALA B CB  
7196 N N   . LEU B 361 ? 1.9520 0.9699 1.4719 0.3376  0.0583  -0.1537 388 LEU B N   
7197 C CA  . LEU B 361 ? 1.9054 0.9572 1.4201 0.3177  0.0724  -0.1635 388 LEU B CA  
7198 C C   . LEU B 361 ? 1.9059 0.9106 1.3829 0.3039  0.0742  -0.1802 388 LEU B C   
7199 O O   . LEU B 361 ? 1.7700 0.7982 1.2378 0.2877  0.0830  -0.1901 388 LEU B O   
7200 C CB  . LEU B 361 ? 1.8204 0.9085 1.3398 0.2893  0.0699  -0.1474 388 LEU B CB  
7201 C CG  . LEU B 361 ? 1.7860 0.9200 1.3421 0.2992  0.0660  -0.1317 388 LEU B CG  
7202 C CD1 . LEU B 361 ? 1.4691 0.6325 1.0252 0.2705  0.0631  -0.1176 388 LEU B CD1 
7203 C CD2 . LEU B 361 ? 1.5930 0.7783 1.1857 0.3218  0.0810  -0.1406 388 LEU B CD2 
7204 N N   . GLY B 362 ? 1.7898 0.7280 1.2450 0.3106  0.0653  -0.1842 389 GLY B N   
7205 C CA  . GLY B 362 ? 1.8223 0.7119 1.2440 0.2967  0.0661  -0.2022 389 GLY B CA  
7206 C C   . GLY B 362 ? 1.8727 0.7586 1.2756 0.2562  0.0631  -0.1982 389 GLY B C   
7207 O O   . GLY B 362 ? 1.8709 0.7579 1.2589 0.2412  0.0679  -0.2166 389 GLY B O   
7208 N N   . ILE B 363 ? 1.8422 0.7255 1.2458 0.2388  0.0550  -0.1757 390 ILE B N   
7209 C CA  . ILE B 363 ? 1.8192 0.7081 1.2108 0.2001  0.0539  -0.1705 390 ILE B CA  
7210 C C   . ILE B 363 ? 1.8421 0.6564 1.2035 0.1808  0.0480  -0.1717 390 ILE B C   
7211 O O   . ILE B 363 ? 1.9300 0.6935 1.2800 0.1908  0.0407  -0.1584 390 ILE B O   
7212 C CB  . ILE B 363 ? 1.7883 0.7176 1.1961 0.1908  0.0507  -0.1463 390 ILE B CB  
7213 C CG1 . ILE B 363 ? 1.8464 0.8482 1.2862 0.2067  0.0579  -0.1462 390 ILE B CG1 
7214 C CG2 . ILE B 363 ? 1.6520 0.5847 1.0478 0.1515  0.0505  -0.1415 390 ILE B CG2 
7215 C CD1 . ILE B 363 ? 1.6657 0.7066 1.1244 0.2014  0.0538  -0.1248 390 ILE B CD1 
7216 N N   . GLN B 364 ? 1.8107 0.6172 1.1590 0.1534  0.0509  -0.1882 391 GLN B N   
7217 C CA  . GLN B 364 ? 1.8623 0.6016 1.1855 0.1283  0.0477  -0.1915 391 GLN B CA  
7218 C C   . GLN B 364 ? 1.9001 0.6666 1.2243 0.0882  0.0504  -0.1963 391 GLN B C   
7219 O O   . GLN B 364 ? 1.9039 0.7207 1.2387 0.0844  0.0535  -0.2130 391 GLN B O   
7220 C CB  . GLN B 364 ? 1.9680 0.6561 1.2757 0.1407  0.0476  -0.2171 391 GLN B CB  
7221 C CG  . GLN B 364 ? 2.0137 0.6763 1.3228 0.1829  0.0455  -0.2164 391 GLN B CG  
7222 C CD  . GLN B 364 ? 2.2636 0.9083 1.5730 0.1934  0.0458  -0.2412 391 GLN B CD  
7223 O OE1 . GLN B 364 ? 2.2774 0.9088 1.5768 0.1696  0.0463  -0.2605 391 GLN B OE1 
7224 N NE2 . GLN B 364 ? 2.1401 0.7864 1.4631 0.2292  0.0452  -0.2423 391 GLN B NE2 
7225 N N   . MET B 365 ? 1.8843 0.6184 1.1971 0.0595  0.0497  -0.1814 392 MET B N   
7226 C CA  . MET B 365 ? 1.8064 0.5666 1.1239 0.0201  0.0532  -0.1866 392 MET B CA  
7227 C C   . MET B 365 ? 2.0191 0.7628 1.3319 0.0047  0.0533  -0.2184 392 MET B C   
7228 O O   . MET B 365 ? 1.9865 0.6722 1.2837 0.0145  0.0513  -0.2318 392 MET B O   
7229 C CB  . MET B 365 ? 1.8308 0.5519 1.1344 -0.0074 0.0553  -0.1644 392 MET B CB  
7230 C CG  . MET B 365 ? 1.8887 0.6456 1.2026 -0.0478 0.0609  -0.1671 392 MET B CG  
7231 S SD  . MET B 365 ? 1.9428 0.6409 1.2353 -0.0844 0.0680  -0.1456 392 MET B SD  
7232 C CE  . MET B 365 ? 2.0698 0.6798 1.3427 -0.0962 0.0688  -0.1654 392 MET B CE  
7233 N N   . LEU B 366 ? 1.8563 0.6523 1.1831 -0.0178 0.0544  -0.2321 393 LEU B N   
7234 C CA  . LEU B 366 ? 1.9336 0.7193 1.2579 -0.0361 0.0521  -0.2640 393 LEU B CA  
7235 C C   . LEU B 366 ? 2.0306 0.7422 1.3412 -0.0649 0.0538  -0.2654 393 LEU B C   
7236 O O   . LEU B 366 ? 2.0833 0.7858 1.3949 -0.0915 0.0589  -0.2462 393 LEU B O   
7237 C CB  . LEU B 366 ? 1.8371 0.6929 1.1807 -0.0574 0.0511  -0.2757 393 LEU B CB  
7238 C CG  . LEU B 366 ? 1.9114 0.7683 1.2560 -0.0758 0.0457  -0.3116 393 LEU B CG  
7239 C CD1 . LEU B 366 ? 1.7471 0.6803 1.1042 -0.0683 0.0411  -0.3257 393 LEU B CD1 
7240 C CD2 . LEU B 366 ? 2.0746 0.9075 1.4264 -0.1208 0.0480  -0.3161 393 LEU B CD2 
7241 N N   . PRO B 367 ? 2.1529 0.8083 1.4491 -0.0605 0.0508  -0.2872 394 PRO B N   
7242 C CA  . PRO B 367 ? 2.1084 0.6886 1.3929 -0.0859 0.0534  -0.2857 394 PRO B CA  
7243 C C   . PRO B 367 ? 2.0972 0.6880 1.3940 -0.1347 0.0578  -0.2942 394 PRO B C   
7244 O O   . PRO B 367 ? 2.1891 0.8158 1.5001 -0.1498 0.0536  -0.3240 394 PRO B O   
7245 C CB  . PRO B 367 ? 2.0806 0.6384 1.3668 -0.0684 0.0470  -0.3108 394 PRO B CB  
7246 C CG  . PRO B 367 ? 2.0424 0.6345 1.3255 -0.0253 0.0441  -0.3162 394 PRO B CG  
7247 C CD  . PRO B 367 ? 2.1020 0.7604 1.3922 -0.0290 0.0461  -0.3118 394 PRO B CD  
7248 N N   . GLY B 368 ? 2.0587 0.6211 1.3507 -0.1585 0.0662  -0.2679 395 GLY B N   
7249 C CA  . GLY B 368 ? 2.1217 0.6929 1.4285 -0.2063 0.0739  -0.2726 395 GLY B CA  
7250 C C   . GLY B 368 ? 2.2266 0.8749 1.5536 -0.2204 0.0777  -0.2630 395 GLY B C   
7251 O O   . GLY B 368 ? 2.1432 0.8128 1.4892 -0.2595 0.0837  -0.2730 395 GLY B O   
7252 N N   . TYR B 369 ? 2.0856 0.7817 1.4142 -0.1898 0.0746  -0.2446 396 TYR B N   
7253 C CA  . TYR B 369 ? 1.9915 0.7646 1.3418 -0.2005 0.0774  -0.2356 396 TYR B CA  
7254 C C   . TYR B 369 ? 2.0822 0.8358 1.4265 -0.2292 0.0899  -0.2091 396 TYR B C   
7255 O O   . TYR B 369 ? 2.1574 0.8499 1.4746 -0.2224 0.0940  -0.1842 396 TYR B O   
7256 C CB  . TYR B 369 ? 1.9840 0.8073 1.3373 -0.1612 0.0718  -0.2222 396 TYR B CB  
7257 C CG  . TYR B 369 ? 1.9685 0.8583 1.3397 -0.1709 0.0757  -0.2070 396 TYR B CG  
7258 C CD1 . TYR B 369 ? 1.9499 0.9058 1.3470 -0.1874 0.0742  -0.2259 396 TYR B CD1 
7259 C CD2 . TYR B 369 ? 1.9802 0.8659 1.3416 -0.1625 0.0797  -0.1752 396 TYR B CD2 
7260 C CE1 . TYR B 369 ? 1.8007 0.8155 1.2144 -0.1948 0.0777  -0.2133 396 TYR B CE1 
7261 C CE2 . TYR B 369 ? 1.9688 0.9134 1.3455 -0.1710 0.0832  -0.1632 396 TYR B CE2 
7262 C CZ  . TYR B 369 ? 1.8256 0.8340 1.2290 -0.1872 0.0828  -0.1823 396 TYR B CZ  
7263 O OH  . TYR B 369 ? 1.7163 0.7822 1.1356 -0.1942 0.0863  -0.1718 396 TYR B OH  
7264 N N   . ARG B 370 ? 2.0503 0.8569 1.4186 -0.2599 0.0959  -0.2149 397 ARG B N   
7265 C CA  . ARG B 370 ? 2.1020 0.9024 1.4665 -0.2882 0.1101  -0.1915 397 ARG B CA  
7266 C C   . ARG B 370 ? 2.1019 0.9912 1.4937 -0.2932 0.1112  -0.1907 397 ARG B C   
7267 O O   . ARG B 370 ? 1.9420 0.8913 1.3616 -0.2935 0.1037  -0.2161 397 ARG B O   
7268 C CB  . ARG B 370 ? 2.1994 0.9542 1.5662 -0.3337 0.1224  -0.2023 397 ARG B CB  
7269 C CG  . ARG B 370 ? 2.1255 0.7780 1.4584 -0.3330 0.1255  -0.1935 397 ARG B CG  
7270 C CD  . ARG B 370 ? 2.3038 0.9099 1.6395 -0.3821 0.1411  -0.2005 397 ARG B CD  
7271 N NE  . ARG B 370 ? 2.6188 1.1471 1.9294 -0.3753 0.1440  -0.1810 397 ARG B NE  
7272 C CZ  . ARG B 370 ? 2.6890 1.1837 2.0062 -0.4072 0.1561  -0.1785 397 ARG B CZ  
7273 N NH1 . ARG B 370 ? 2.6938 1.2262 2.0444 -0.4496 0.1673  -0.1949 397 ARG B NH1 
7274 N NH2 . ARG B 370 ? 2.7650 1.1882 2.0566 -0.3956 0.1569  -0.1597 397 ARG B NH2 
7275 N N   . ASP B 371 ? 2.2883 1.1838 1.6694 -0.2947 0.1195  -0.1617 398 ASP B N   
7276 C CA  . ASP B 371 ? 2.1183 1.0917 1.5230 -0.3011 0.1225  -0.1591 398 ASP B CA  
7277 C C   . ASP B 371 ? 2.1508 1.1625 1.5883 -0.3398 0.1291  -0.1845 398 ASP B C   
7278 O O   . ASP B 371 ? 2.3069 1.2781 1.7414 -0.3751 0.1424  -0.1857 398 ASP B O   
7279 C CB  . ASP B 371 ? 2.1832 1.1416 1.5656 -0.3042 0.1330  -0.1255 398 ASP B CB  
7280 C CG  . ASP B 371 ? 2.3164 1.3523 1.7209 -0.3088 0.1365  -0.1220 398 ASP B CG  
7281 O OD1 . ASP B 371 ? 2.2675 1.3688 1.7057 -0.3103 0.1310  -0.1446 398 ASP B OD1 
7282 O OD2 . ASP B 371 ? 2.3256 1.3551 1.7112 -0.3093 0.1441  -0.0966 398 ASP B OD2 
7283 N N   . PRO B 372 ? 1.9451 1.0332 1.4146 -0.3345 0.1204  -0.2054 399 PRO B N   
7284 C CA  . PRO B 372 ? 1.9548 1.0860 1.4600 -0.3696 0.1245  -0.2317 399 PRO B CA  
7285 C C   . PRO B 372 ? 1.9984 1.1405 1.5123 -0.4047 0.1442  -0.2190 399 PRO B C   
7286 O O   . PRO B 372 ? 1.8543 1.0278 1.4006 -0.4379 0.1505  -0.2408 399 PRO B O   
7287 C CB  . PRO B 372 ? 1.8510 1.0632 1.3819 -0.3473 0.1098  -0.2488 399 PRO B CB  
7288 C CG  . PRO B 372 ? 1.9806 1.1756 1.4884 -0.3044 0.0975  -0.2408 399 PRO B CG  
7289 C CD  . PRO B 372 ? 1.9504 1.0844 1.4250 -0.2953 0.1055  -0.2084 399 PRO B CD  
7290 N N   . TYR B 373 ? 2.1315 1.2501 1.6179 -0.3984 0.1541  -0.1859 400 TYR B N   
7291 C CA  . TYR B 373 ? 2.0295 1.1598 1.5191 -0.4294 0.1744  -0.1726 400 TYR B CA  
7292 C C   . TYR B 373 ? 2.1207 1.1664 1.5670 -0.4414 0.1897  -0.1435 400 TYR B C   
7293 O O   . TYR B 373 ? 2.1820 1.2153 1.6265 -0.4769 0.2109  -0.1359 400 TYR B O   
7294 C CB  . TYR B 373 ? 2.0485 1.2444 1.5461 -0.4110 0.1724  -0.1610 400 TYR B CB  
7295 C CG  . TYR B 373 ? 2.0294 1.3075 1.5680 -0.4002 0.1588  -0.1875 400 TYR B CG  
7296 C CD1 . TYR B 373 ? 2.0170 1.3543 1.5951 -0.4281 0.1659  -0.2080 400 TYR B CD1 
7297 C CD2 . TYR B 373 ? 2.0126 1.3086 1.5499 -0.3615 0.1393  -0.1921 400 TYR B CD2 
7298 C CE1 . TYR B 373 ? 1.9665 1.3767 1.5796 -0.4154 0.1515  -0.2318 400 TYR B CE1 
7299 C CE2 . TYR B 373 ? 2.1185 1.4843 1.6875 -0.3502 0.1270  -0.2142 400 TYR B CE2 
7300 C CZ  . TYR B 373 ? 2.0859 1.5076 1.6916 -0.3762 0.1319  -0.2339 400 TYR B CZ  
7301 O OH  . TYR B 373 ? 2.1297 1.6189 1.7646 -0.3623 0.1178  -0.2555 400 TYR B OH  
7302 N N   . HIS B 374 ? 2.2894 1.2760 1.6997 -0.4114 0.1798  -0.1270 401 HIS B N   
7303 C CA  . HIS B 374 ? 2.3858 1.2872 1.7497 -0.4164 0.1909  -0.0978 401 HIS B CA  
7304 C C   . HIS B 374 ? 2.4567 1.2788 1.7978 -0.4048 0.1829  -0.1001 401 HIS B C   
7305 O O   . HIS B 374 ? 2.5027 1.2469 1.8020 -0.4044 0.1898  -0.0753 401 HIS B O   
7306 C CB  . HIS B 374 ? 2.4196 1.3230 1.7532 -0.3869 0.1874  -0.0665 401 HIS B CB  
7307 C CG  . HIS B 374 ? 2.3836 1.3559 1.7333 -0.3973 0.1965  -0.0621 401 HIS B CG  
7308 N ND1 . HIS B 374 ? 2.3376 1.2963 1.6710 -0.4278 0.2188  -0.0460 401 HIS B ND1 
7309 C CD2 . HIS B 374 ? 2.3497 1.4033 1.7292 -0.3809 0.1871  -0.0721 401 HIS B CD2 
7310 C CE1 . HIS B 374 ? 2.3557 1.3867 1.7093 -0.4289 0.2223  -0.0477 401 HIS B CE1 
7311 N NE2 . HIS B 374 ? 2.3674 1.4556 1.7496 -0.4006 0.2027  -0.0634 401 HIS B NE2 
7312 N N   . GLY B 375 ? 2.3458 1.1833 1.7103 -0.3941 0.1684  -0.1290 402 GLY B N   
7313 C CA  . GLY B 375 ? 2.2780 1.0416 1.6232 -0.3845 0.1616  -0.1355 402 GLY B CA  
7314 C C   . GLY B 375 ? 2.2229 0.9341 1.5290 -0.3442 0.1521  -0.1103 402 GLY B C   
7315 O O   . GLY B 375 ? 2.3585 0.9925 1.6403 -0.3385 0.1502  -0.1086 402 GLY B O   
7316 N N   . ARG B 376 ? 2.2869 1.0384 1.5882 -0.3154 0.1454  -0.0919 403 ARG B N   
7317 C CA  . ARG B 376 ? 2.2485 0.9612 1.5178 -0.2765 0.1354  -0.0679 403 ARG B CA  
7318 C C   . ARG B 376 ? 2.1510 0.8823 1.4336 -0.2380 0.1176  -0.0843 403 ARG B C   
7319 O O   . ARG B 376 ? 2.0528 0.8473 1.3681 -0.2360 0.1123  -0.1083 403 ARG B O   
7320 C CB  . ARG B 376 ? 2.2784 1.0298 1.5397 -0.2657 0.1364  -0.0431 403 ARG B CB  
7321 C CG  . ARG B 376 ? 2.3557 1.0852 1.5960 -0.2998 0.1556  -0.0236 403 ARG B CG  
7322 C CD  . ARG B 376 ? 2.5073 1.2767 1.7377 -0.2866 0.1550  -0.0016 403 ARG B CD  
7323 N NE  . ARG B 376 ? 2.5335 1.2868 1.7439 -0.2425 0.1376  0.0146  403 ARG B NE  
7324 C CZ  . ARG B 376 ? 2.3980 1.2131 1.6311 -0.2130 0.1238  0.0103  403 ARG B CZ  
7325 N NH1 . ARG B 376 ? 2.2041 1.0981 1.4759 -0.2207 0.1248  -0.0074 403 ARG B NH1 
7326 N NH2 . ARG B 376 ? 2.4732 1.2700 1.6907 -0.1748 0.1087  0.0238  403 ARG B NH2 
7327 N N   . PRO B 377 ? 2.1338 0.8107 1.3908 -0.2060 0.1087  -0.0719 404 PRO B N   
7328 C CA  . PRO B 377 ? 2.0737 0.7691 1.3437 -0.1684 0.0944  -0.0870 404 PRO B CA  
7329 C C   . PRO B 377 ? 2.0418 0.8170 1.3340 -0.1441 0.0873  -0.0836 404 PRO B C   
7330 O O   . PRO B 377 ? 1.9918 0.8066 1.2887 -0.1549 0.0919  -0.0699 404 PRO B O   
7331 C CB  . PRO B 377 ? 2.0834 0.6995 1.3202 -0.1414 0.0882  -0.0707 404 PRO B CB  
7332 C CG  . PRO B 377 ? 2.1279 0.6715 1.3328 -0.1713 0.0999  -0.0535 404 PRO B CG  
7333 C CD  . PRO B 377 ? 2.1323 0.7235 1.3465 -0.2035 0.1120  -0.0453 404 PRO B CD  
7334 N N   . LEU B 378 ? 1.9895 0.7874 1.2952 -0.1119 0.0775  -0.0966 405 LEU B N   
7335 C CA  . LEU B 378 ? 1.9624 0.8317 1.2901 -0.0886 0.0722  -0.0937 405 LEU B CA  
7336 C C   . LEU B 378 ? 1.8295 0.6892 1.1439 -0.0669 0.0674  -0.0658 405 LEU B C   
7337 O O   . LEU B 378 ? 1.8290 0.6313 1.1216 -0.0475 0.0621  -0.0548 405 LEU B O   
7338 C CB  . LEU B 378 ? 1.8356 0.7256 1.1782 -0.0604 0.0658  -0.1140 405 LEU B CB  
7339 C CG  . LEU B 378 ? 1.7947 0.7551 1.1611 -0.0362 0.0624  -0.1122 405 LEU B CG  
7340 C CD1 . LEU B 378 ? 1.7297 0.7408 1.1156 -0.0401 0.0634  -0.1367 405 LEU B CD1 
7341 C CD2 . LEU B 378 ? 1.6945 0.6400 1.0596 0.0031  0.0562  -0.1053 405 LEU B CD2 
7342 N N   . THR B 379 ? 1.7230 0.6389 1.0507 -0.0689 0.0680  -0.0555 406 THR B N   
7343 C CA  . THR B 379 ? 1.8109 0.7244 1.1269 -0.0510 0.0623  -0.0309 406 THR B CA  
7344 C C   . THR B 379 ? 1.8199 0.7704 1.1578 -0.0130 0.0522  -0.0327 406 THR B C   
7345 O O   . THR B 379 ? 1.8281 0.8174 1.1909 -0.0037 0.0527  -0.0509 406 THR B O   
7346 C CB  . THR B 379 ? 1.7637 0.7172 1.0819 -0.0731 0.0684  -0.0201 406 THR B CB  
7347 O OG1 . THR B 379 ? 1.5836 0.6128 0.9349 -0.0624 0.0655  -0.0279 406 THR B OG1 
7348 C CG2 . THR B 379 ? 1.6418 0.5887 0.9572 -0.1144 0.0817  -0.0288 406 THR B CG2 
7349 N N   . LYS B 380 ? 1.8192 0.7572 1.1469 0.0091  0.0433  -0.0136 407 LYS B N   
7350 C CA  . LYS B 380 ? 1.7636 0.7415 1.1173 0.0431  0.0344  -0.0147 407 LYS B CA  
7351 C C   . LYS B 380 ? 1.6567 0.7125 1.0423 0.0380  0.0378  -0.0207 407 LYS B C   
7352 O O   . LYS B 380 ? 1.6707 0.7663 1.0848 0.0583  0.0365  -0.0303 407 LYS B O   
7353 C CB  . LYS B 380 ? 1.8786 0.8313 1.2163 0.0656  0.0220  0.0060  407 LYS B CB  
7354 C CG  . LYS B 380 ? 1.6582 0.5309 0.9636 0.0784  0.0162  0.0136  407 LYS B CG  
7355 C CD  . LYS B 380 ? 1.9049 0.7698 1.2283 0.1078  0.0121  -0.0016 407 LYS B CD  
7356 C CE  . LYS B 380 ? 2.3088 1.0921 1.6002 0.1238  0.0048  0.0062  407 LYS B CE  
7357 N NZ  . LYS B 380 ? 2.2627 1.0360 1.5709 0.1516  0.0026  -0.0113 407 LYS B NZ  
7358 N N   . GLY B 381 ? 1.5738 0.6508 0.9549 0.0112  0.0434  -0.0153 408 GLY B N   
7359 C CA  . GLY B 381 ? 1.5463 0.6936 0.9565 0.0062  0.0465  -0.0216 408 GLY B CA  
7360 C C   . GLY B 381 ? 1.6275 0.8044 1.0580 0.0010  0.0529  -0.0429 408 GLY B C   
7361 O O   . GLY B 381 ? 1.4936 0.7177 0.9501 0.0155  0.0528  -0.0498 408 GLY B O   
7362 N N   . GLU B 382 ? 1.5062 0.6541 0.9237 -0.0197 0.0584  -0.0538 409 GLU B N   
7363 C CA  . GLU B 382 ? 1.4004 0.5716 0.8325 -0.0224 0.0618  -0.0760 409 GLU B CA  
7364 C C   . GLU B 382 ? 1.6218 0.7871 1.0605 0.0086  0.0586  -0.0839 409 GLU B C   
7365 O O   . GLU B 382 ? 1.3964 0.5980 0.8506 0.0168  0.0609  -0.0979 409 GLU B O   
7366 C CB  . GLU B 382 ? 1.5535 0.6901 0.9711 -0.0504 0.0664  -0.0880 409 GLU B CB  
7367 C CG  . GLU B 382 ? 1.4107 0.5591 0.8264 -0.0840 0.0729  -0.0836 409 GLU B CG  
7368 C CD  . GLU B 382 ? 1.7817 0.8879 1.1845 -0.1133 0.0787  -0.0939 409 GLU B CD  
7369 O OE1 . GLU B 382 ? 1.8738 0.9304 1.2633 -0.1065 0.0764  -0.1010 409 GLU B OE1 
7370 O OE2 . GLU B 382 ? 1.7311 0.8544 1.1390 -0.1435 0.0862  -0.0960 409 GLU B OE2 
7371 N N   . LEU B 383 ? 1.5283 0.6479 0.9541 0.0271  0.0538  -0.0751 410 LEU B N   
7372 C CA  . LEU B 383 ? 1.4679 0.5842 0.9029 0.0585  0.0520  -0.0827 410 LEU B CA  
7373 C C   . LEU B 383 ? 1.4801 0.6545 0.9443 0.0781  0.0524  -0.0791 410 LEU B C   
7374 O O   . LEU B 383 ? 1.4064 0.6090 0.8853 0.0912  0.0576  -0.0916 410 LEU B O   
7375 C CB  . LEU B 383 ? 1.5719 0.6286 0.9892 0.0757  0.0453  -0.0731 410 LEU B CB  
7376 C CG  . LEU B 383 ? 1.6558 0.7129 1.0872 0.1121  0.0428  -0.0785 410 LEU B CG  
7377 C CD1 . LEU B 383 ? 1.5990 0.6502 1.0296 0.1167  0.0493  -0.1013 410 LEU B CD1 
7378 C CD2 . LEU B 383 ? 1.6306 0.6331 1.0462 0.1307  0.0333  -0.0662 410 LEU B CD2 
7379 N N   . GLY B 384 ? 1.4190 0.6102 0.8905 0.0800  0.0475  -0.0623 411 GLY B N   
7380 C CA  . GLY B 384 ? 1.3936 0.6380 0.8958 0.0965  0.0477  -0.0594 411 GLY B CA  
7381 C C   . GLY B 384 ? 1.3490 0.6442 0.8666 0.0847  0.0557  -0.0679 411 GLY B C   
7382 O O   . GLY B 384 ? 1.2850 0.6154 0.8248 0.1002  0.0609  -0.0729 411 GLY B O   
7383 N N   . CYS B 385 ? 1.3538 0.6529 0.8600 0.0575  0.0574  -0.0697 412 CYS B N   
7384 C CA  . CYS B 385 ? 1.3890 0.7342 0.9080 0.0475  0.0630  -0.0789 412 CYS B CA  
7385 C C   . CYS B 385 ? 1.2823 0.6291 0.8002 0.0575  0.0680  -0.0958 412 CYS B C   
7386 O O   . CYS B 385 ? 1.2929 0.6776 0.8251 0.0672  0.0730  -0.1001 412 CYS B O   
7387 C CB  . CYS B 385 ? 1.3288 0.6765 0.8375 0.0170  0.0635  -0.0802 412 CYS B CB  
7388 S SG  . CYS B 385 ? 1.5679 0.9787 1.0962 0.0065  0.0670  -0.0868 412 CYS B SG  
7389 N N   . PHE B 386 ? 1.3258 0.6287 0.8243 0.0560  0.0670  -0.1053 413 PHE B N   
7390 C CA  . PHE B 386 ? 1.3382 0.6383 0.8312 0.0677  0.0710  -0.1229 413 PHE B CA  
7391 C C   . PHE B 386 ? 1.2893 0.6034 0.7965 0.0980  0.0763  -0.1209 413 PHE B C   
7392 O O   . PHE B 386 ? 1.3244 0.6676 0.8367 0.1083  0.0832  -0.1288 413 PHE B O   
7393 C CB  . PHE B 386 ? 1.4648 0.7095 0.9350 0.0613  0.0681  -0.1338 413 PHE B CB  
7394 C CG  . PHE B 386 ? 1.3721 0.6134 0.8320 0.0678  0.0706  -0.1559 413 PHE B CG  
7395 C CD1 . PHE B 386 ? 1.3402 0.5739 0.7990 0.0959  0.0751  -0.1621 413 PHE B CD1 
7396 C CD2 . PHE B 386 ? 1.4724 0.7197 0.9241 0.0463  0.0682  -0.1719 413 PHE B CD2 
7397 C CE1 . PHE B 386 ? 1.5132 0.7427 0.9577 0.1029  0.0775  -0.1831 413 PHE B CE1 
7398 C CE2 . PHE B 386 ? 1.4303 0.6747 0.8696 0.0535  0.0682  -0.1938 413 PHE B CE2 
7399 C CZ  . PHE B 386 ? 1.4942 0.7284 0.9275 0.0820  0.0730  -0.1990 413 PHE B CZ  
7400 N N   . LEU B 387 ? 1.3626 0.6566 0.8764 0.1132  0.0734  -0.1103 414 LEU B N   
7401 C CA  . LEU B 387 ? 1.3023 0.6123 0.8357 0.1415  0.0792  -0.1096 414 LEU B CA  
7402 C C   . LEU B 387 ? 1.2576 0.6225 0.8168 0.1443  0.0855  -0.1031 414 LEU B C   
7403 O O   . LEU B 387 ? 1.1735 0.5603 0.7468 0.1623  0.0959  -0.1071 414 LEU B O   
7404 C CB  . LEU B 387 ? 1.2995 0.5822 0.8391 0.1568  0.0717  -0.0995 414 LEU B CB  
7405 C CG  . LEU B 387 ? 1.4645 0.6860 0.9786 0.1598  0.0663  -0.1052 414 LEU B CG  
7406 C CD1 . LEU B 387 ? 1.4523 0.6489 0.9720 0.1779  0.0569  -0.0933 414 LEU B CD1 
7407 C CD2 . LEU B 387 ? 1.3987 0.6091 0.9056 0.1742  0.0746  -0.1242 414 LEU B CD2 
7408 N N   . SER B 388 ? 1.2484 0.6345 0.8135 0.1265  0.0809  -0.0933 415 SER B N   
7409 C CA  . SER B 388 ? 1.1549 0.5895 0.7433 0.1276  0.0866  -0.0881 415 SER B CA  
7410 C C   . SER B 388 ? 1.0980 0.5527 0.6789 0.1269  0.0958  -0.0985 415 SER B C   
7411 O O   . SER B 388 ? 1.1318 0.6123 0.7272 0.1408  0.1064  -0.0980 415 SER B O   
7412 C CB  . SER B 388 ? 1.1203 0.5697 0.7128 0.1086  0.0790  -0.0778 415 SER B CB  
7413 O OG  . SER B 388 ? 1.2414 0.6693 0.8342 0.1107  0.0695  -0.0676 415 SER B OG  
7414 N N   . HIS B 389 ? 1.1241 0.5668 0.6818 0.1108  0.0920  -0.1083 416 HIS B N   
7415 C CA  . HIS B 389 ? 1.1939 0.6528 0.7396 0.1126  0.0975  -0.1201 416 HIS B CA  
7416 C C   . HIS B 389 ? 1.2107 0.6536 0.7456 0.1339  0.1059  -0.1301 416 HIS B C   
7417 O O   . HIS B 389 ? 1.1454 0.6081 0.6759 0.1456  0.1154  -0.1339 416 HIS B O   
7418 C CB  . HIS B 389 ? 1.2464 0.6974 0.7735 0.0906  0.0892  -0.1314 416 HIS B CB  
7419 C CG  . HIS B 389 ? 1.2298 0.7041 0.7676 0.0703  0.0838  -0.1242 416 HIS B CG  
7420 N ND1 . HIS B 389 ? 1.0716 0.5810 0.6122 0.0643  0.0834  -0.1281 416 HIS B ND1 
7421 C CD2 . HIS B 389 ? 1.2236 0.6906 0.7680 0.0558  0.0790  -0.1137 416 HIS B CD2 
7422 C CE1 . HIS B 389 ? 1.1841 0.7088 0.7358 0.0469  0.0792  -0.1215 416 HIS B CE1 
7423 N NE2 . HIS B 389 ? 1.2084 0.7078 0.7610 0.0408  0.0770  -0.1125 416 HIS B NE2 
7424 N N   . TYR B 390 ? 1.2371 0.6424 0.7652 0.1403  0.1032  -0.1341 417 TYR B N   
7425 C CA  . TYR B 390 ? 1.3352 0.7239 0.8537 0.1620  0.1117  -0.1450 417 TYR B CA  
7426 C C   . TYR B 390 ? 1.2469 0.6635 0.7890 0.1832  0.1256  -0.1371 417 TYR B C   
7427 O O   . TYR B 390 ? 1.1958 0.6207 0.7291 0.1982  0.1384  -0.1447 417 TYR B O   
7428 C CB  . TYR B 390 ? 1.3051 0.6461 0.8150 0.1655  0.1050  -0.1495 417 TYR B CB  
7429 C CG  . TYR B 390 ? 1.2963 0.6192 0.8008 0.1909  0.1137  -0.1607 417 TYR B CG  
7430 C CD1 . TYR B 390 ? 1.4056 0.7116 0.8823 0.1947  0.1165  -0.1802 417 TYR B CD1 
7431 C CD2 . TYR B 390 ? 1.2824 0.6067 0.8105 0.2119  0.1186  -0.1536 417 TYR B CD2 
7432 C CE1 . TYR B 390 ? 1.3839 0.6733 0.8539 0.2189  0.1256  -0.1917 417 TYR B CE1 
7433 C CE2 . TYR B 390 ? 1.3183 0.6287 0.8440 0.2361  0.1280  -0.1650 417 TYR B CE2 
7434 C CZ  . TYR B 390 ? 1.5065 0.7986 1.0018 0.2395  0.1322  -0.1838 417 TYR B CZ  
7435 O OH  . TYR B 390 ? 1.6501 0.9283 1.1413 0.2646  0.1426  -0.1965 417 TYR B OH  
7436 N N   . ASN B 391 ? 1.2361 0.6676 0.8081 0.1842  0.1239  -0.1226 418 ASN B N   
7437 C CA  . ASN B 391 ? 1.2066 0.6677 0.8083 0.2014  0.1374  -0.1160 418 ASN B CA  
7438 C C   . ASN B 391 ? 1.1939 0.6894 0.7967 0.1986  0.1490  -0.1127 418 ASN B C   
7439 O O   . ASN B 391 ? 1.1832 0.6956 0.7963 0.2138  0.1663  -0.1124 418 ASN B O   
7440 C CB  . ASN B 391 ? 1.1148 0.5864 0.7494 0.2014  0.1296  -0.1033 418 ASN B CB  
7441 C CG  . ASN B 391 ? 1.2646 0.7003 0.8970 0.2095  0.1182  -0.1047 418 ASN B CG  
7442 O OD1 . ASN B 391 ? 1.3682 0.7735 0.9823 0.2199  0.1202  -0.1158 418 ASN B OD1 
7443 N ND2 . ASN B 391 ? 1.2844 0.7212 0.9331 0.2060  0.1057  -0.0938 418 ASN B ND2 
7444 N N   . ILE B 392 ? 1.1632 0.6685 0.7551 0.1799  0.1409  -0.1101 419 ILE B N   
7445 C CA  . ILE B 392 ? 1.0808 0.6140 0.6694 0.1790  0.1501  -0.1070 419 ILE B CA  
7446 C C   . ILE B 392 ? 1.1036 0.6275 0.6587 0.1898  0.1587  -0.1191 419 ILE B C   
7447 O O   . ILE B 392 ? 1.2216 0.7609 0.7742 0.2020  0.1749  -0.1159 419 ILE B O   
7448 C CB  . ILE B 392 ? 1.1317 0.6785 0.7187 0.1583  0.1378  -0.1028 419 ILE B CB  
7449 C CG1 . ILE B 392 ? 1.0623 0.6208 0.6802 0.1501  0.1313  -0.0907 419 ILE B CG1 
7450 C CG2 . ILE B 392 ? 1.0868 0.6575 0.6653 0.1599  0.1454  -0.1008 419 ILE B CG2 
7451 C CD1 . ILE B 392 ? 1.0196 0.5972 0.6399 0.1323  0.1230  -0.0862 419 ILE B CD1 
7452 N N   . TRP B 393 ? 1.1347 0.6320 0.6622 0.1852  0.1484  -0.1334 420 TRP B N   
7453 C CA  . TRP B 393 ? 1.1713 0.6572 0.6648 0.1972  0.1545  -0.1480 420 TRP B CA  
7454 C C   . TRP B 393 ? 1.2781 0.7601 0.7754 0.2205  0.1734  -0.1487 420 TRP B C   
7455 O O   . TRP B 393 ? 1.2674 0.7565 0.7444 0.2342  0.1877  -0.1518 420 TRP B O   
7456 C CB  . TRP B 393 ? 1.2924 0.7468 0.7620 0.1880  0.1398  -0.1654 420 TRP B CB  
7457 C CG  . TRP B 393 ? 1.3196 0.7764 0.7904 0.1629  0.1228  -0.1662 420 TRP B CG  
7458 C CD1 . TRP B 393 ? 1.2074 0.6942 0.6881 0.1507  0.1187  -0.1576 420 TRP B CD1 
7459 C CD2 . TRP B 393 ? 1.3996 0.8268 0.8626 0.1464  0.1093  -0.1766 420 TRP B CD2 
7460 N NE1 . TRP B 393 ? 1.2427 0.7244 0.7238 0.1279  0.1042  -0.1628 420 TRP B NE1 
7461 C CE2 . TRP B 393 ? 1.3300 0.7747 0.8003 0.1236  0.0989  -0.1738 420 TRP B CE2 
7462 C CE3 . TRP B 393 ? 1.2983 0.6844 0.7493 0.1485  0.1060  -0.1883 420 TRP B CE3 
7463 C CZ2 . TRP B 393 ? 1.2560 0.6798 0.7227 0.1013  0.0873  -0.1817 420 TRP B CZ2 
7464 C CZ3 . TRP B 393 ? 1.3339 0.6951 0.7797 0.1264  0.0935  -0.1954 420 TRP B CZ3 
7465 C CH2 . TRP B 393 ? 1.4046 0.7855 0.8588 0.1022  0.0852  -0.1918 420 TRP B CH2 
7466 N N   . LYS B 394 ? 1.2870 0.7579 0.8097 0.2263  0.1739  -0.1461 421 LYS B N   
7467 C CA  . LYS B 394 ? 1.2068 0.6796 0.7419 0.2487  0.1924  -0.1474 421 LYS B CA  
7468 C C   . LYS B 394 ? 1.1799 0.6883 0.7372 0.2543  0.2116  -0.1340 421 LYS B C   
7469 O O   . LYS B 394 ? 1.3024 0.8168 0.8511 0.2704  0.2326  -0.1366 421 LYS B O   
7470 C CB  . LYS B 394 ? 1.2102 0.6679 0.7731 0.2541  0.1857  -0.1465 421 LYS B CB  
7471 C CG  . LYS B 394 ? 1.2588 0.6795 0.8016 0.2676  0.1841  -0.1632 421 LYS B CG  
7472 C CD  . LYS B 394 ? 1.4503 0.8569 1.0219 0.2767  0.1774  -0.1605 421 LYS B CD  
7473 C CE  . LYS B 394 ? 1.5988 0.9753 1.1579 0.2980  0.1826  -0.1770 421 LYS B CE  
7474 N NZ  . LYS B 394 ? 1.7552 1.1173 1.3425 0.3105  0.1746  -0.1743 421 LYS B NZ  
7475 N N   . GLU B 395 ? 1.2458 0.7763 0.8305 0.2406  0.2060  -0.1198 422 GLU B N   
7476 C CA  . GLU B 395 ? 1.1759 0.7371 0.7841 0.2435  0.2241  -0.1071 422 GLU B CA  
7477 C C   . GLU B 395 ? 1.2487 0.8146 0.8216 0.2448  0.2345  -0.1057 422 GLU B C   
7478 O O   . GLU B 395 ? 1.2088 0.7880 0.7849 0.2547  0.2574  -0.0991 422 GLU B O   
7479 C CB  . GLU B 395 ? 1.0713 0.6524 0.7156 0.2284  0.2135  -0.0946 422 GLU B CB  
7480 C CG  . GLU B 395 ? 1.2096 0.8201 0.8815 0.2290  0.2315  -0.0823 422 GLU B CG  
7481 C CD  . GLU B 395 ? 1.2502 0.8801 0.9620 0.2162  0.2208  -0.0730 422 GLU B CD  
7482 O OE1 . GLU B 395 ? 1.3629 0.9841 1.0815 0.2094  0.2006  -0.0750 422 GLU B OE1 
7483 O OE2 . GLU B 395 ? 1.1278 0.7797 0.8622 0.2130  0.2329  -0.0636 422 GLU B OE2 
7484 N N   . VAL B 396 ? 1.2265 0.7818 0.7657 0.2351  0.2180  -0.1119 423 VAL B N   
7485 C CA  . VAL B 396 ? 1.2640 0.8224 0.7653 0.2392  0.2238  -0.1122 423 VAL B CA  
7486 C C   . VAL B 396 ? 1.3615 0.9074 0.8317 0.2597  0.2423  -0.1207 423 VAL B C   
7487 O O   . VAL B 396 ? 1.4316 0.9848 0.8833 0.2699  0.2608  -0.1135 423 VAL B O   
7488 C CB  . VAL B 396 ? 1.2278 0.7793 0.7029 0.2260  0.1999  -0.1218 423 VAL B CB  
7489 C CG1 . VAL B 396 ? 1.3724 0.9229 0.8016 0.2356  0.2025  -0.1273 423 VAL B CG1 
7490 C CG2 . VAL B 396 ? 1.1083 0.6778 0.6102 0.2074  0.1870  -0.1114 423 VAL B CG2 
7491 N N   . VAL B 397 ? 1.3715 0.8961 0.8337 0.2668  0.2387  -0.1359 424 VAL B N   
7492 C CA  . VAL B 397 ? 1.3214 0.8328 0.7512 0.2871  0.2555  -0.1471 424 VAL B CA  
7493 C C   . VAL B 397 ? 1.3516 0.8769 0.8093 0.3011  0.2844  -0.1383 424 VAL B C   
7494 O O   . VAL B 397 ? 1.4152 0.9404 0.8466 0.3168  0.3072  -0.1392 424 VAL B O   
7495 C CB  . VAL B 397 ? 1.3353 0.8169 0.7478 0.2898  0.2412  -0.1682 424 VAL B CB  
7496 C CG1 . VAL B 397 ? 1.3527 0.8204 0.7336 0.3126  0.2593  -0.1818 424 VAL B CG1 
7497 C CG2 . VAL B 397 ? 1.3320 0.8026 0.7171 0.2747  0.2156  -0.1788 424 VAL B CG2 
7498 N N   . ASP B 398 ? 1.2629 0.8019 0.7739 0.2958  0.2845  -0.1302 425 ASP B N   
7499 C CA  . ASP B 398 ? 1.3508 0.9084 0.8970 0.3077  0.3114  -0.1240 425 ASP B CA  
7500 C C   . ASP B 398 ? 1.4059 0.9848 0.9553 0.3051  0.3329  -0.1071 425 ASP B C   
7501 O O   . ASP B 398 ? 1.3921 0.9774 0.9371 0.3181  0.3623  -0.1047 425 ASP B O   
7502 C CB  . ASP B 398 ? 1.3202 0.8891 0.9239 0.3031  0.3018  -0.1213 425 ASP B CB  
7503 C CG  . ASP B 398 ? 1.6317 1.1746 1.2316 0.3092  0.2844  -0.1363 425 ASP B CG  
7504 O OD1 . ASP B 398 ? 1.7169 1.2334 1.2724 0.3158  0.2808  -0.1503 425 ASP B OD1 
7505 O OD2 . ASP B 398 ? 1.7244 1.2712 1.3641 0.3081  0.2734  -0.1346 425 ASP B OD2 
7506 N N   . ARG B 399 ? 1.3120 0.9002 0.8682 0.2886  0.3199  -0.0952 426 ARG B N   
7507 C CA  . ARG B 399 ? 1.2582 0.8614 0.8169 0.2853  0.3384  -0.0784 426 ARG B CA  
7508 C C   . ARG B 399 ? 1.4070 0.9958 0.9034 0.2919  0.3428  -0.0768 426 ARG B C   
7509 O O   . ARG B 399 ? 1.4663 1.0608 0.9551 0.2928  0.3613  -0.0619 426 ARG B O   
7510 C CB  . ARG B 399 ? 1.2230 0.8420 0.8179 0.2664  0.3224  -0.0673 426 ARG B CB  
7511 C CG  . ARG B 399 ? 1.1914 0.8290 0.8494 0.2611  0.3206  -0.0662 426 ARG B CG  
7512 C CD  . ARG B 399 ? 1.1615 0.8084 0.8440 0.2429  0.2966  -0.0604 426 ARG B CD  
7513 N NE  . ARG B 399 ? 1.1275 0.7833 0.8074 0.2341  0.3025  -0.0472 426 ARG B NE  
7514 C CZ  . ARG B 399 ? 1.2407 0.9047 0.9353 0.2193  0.2846  -0.0421 426 ARG B CZ  
7515 N NH1 . ARG B 399 ? 1.3280 0.9931 1.0389 0.2104  0.2604  -0.0478 426 ARG B NH1 
7516 N NH2 . ARG B 399 ? 1.3142 0.9834 1.0050 0.2140  0.2918  -0.0307 426 ARG B NH2 
7517 N N   . GLY B 400 ? 1.2821 0.8513 0.7337 0.2970  0.3257  -0.0920 427 GLY B N   
7518 C CA  . GLY B 400 ? 1.3356 0.8926 0.7265 0.3054  0.3259  -0.0931 427 GLY B CA  
7519 C C   . GLY B 400 ? 1.5161 1.0799 0.8992 0.2940  0.3100  -0.0827 427 GLY B C   
7520 O O   . GLY B 400 ? 1.6056 1.1645 0.9483 0.3028  0.3181  -0.0749 427 GLY B O   
7521 N N   . LEU B 401 ? 1.4572 1.0313 0.8762 0.2761  0.2877  -0.0823 428 LEU B N   
7522 C CA  . LEU B 401 ? 1.3802 0.9634 0.7971 0.2653  0.2721  -0.0741 428 LEU B CA  
7523 C C   . LEU B 401 ? 1.4571 1.0306 0.8232 0.2695  0.2521  -0.0872 428 LEU B C   
7524 O O   . LEU B 401 ? 1.5882 1.1546 0.9484 0.2642  0.2327  -0.1049 428 LEU B O   
7525 C CB  . LEU B 401 ? 1.3289 0.9253 0.7946 0.2456  0.2539  -0.0731 428 LEU B CB  
7526 C CG  . LEU B 401 ? 1.2691 0.8755 0.7876 0.2419  0.2665  -0.0665 428 LEU B CG  
7527 C CD1 . LEU B 401 ? 1.2743 0.8888 0.8289 0.2246  0.2442  -0.0684 428 LEU B CD1 
7528 C CD2 . LEU B 401 ? 1.1778 0.7964 0.7165 0.2439  0.2907  -0.0490 428 LEU B CD2 
7529 N N   . GLN B 402 ? 1.3471 0.9195 0.6771 0.2792  0.2562  -0.0789 429 GLN B N   
7530 C CA  . GLN B 402 ? 1.4944 1.0606 0.7749 0.2866  0.2363  -0.0927 429 GLN B CA  
7531 C C   . GLN B 402 ? 1.5020 1.0822 0.8016 0.2692  0.2056  -0.1015 429 GLN B C   
7532 O O   . GLN B 402 ? 1.5184 1.0957 0.8021 0.2657  0.1849  -0.1218 429 GLN B O   
7533 C CB  . GLN B 402 ? 1.5808 1.1408 0.8156 0.3041  0.2480  -0.0797 429 GLN B CB  
7534 C CG  . GLN B 402 ? 1.6800 1.2263 0.8952 0.3199  0.2833  -0.0679 429 GLN B CG  
7535 C CD  . GLN B 402 ? 1.8672 1.4001 1.0563 0.3312  0.2893  -0.0858 429 GLN B CD  
7536 O OE1 . GLN B 402 ? 1.8798 1.4076 1.0439 0.3329  0.2662  -0.1072 429 GLN B OE1 
7537 N NE2 . GLN B 402 ? 1.8425 1.3705 1.0396 0.3388  0.3210  -0.0786 429 GLN B NE2 
7538 N N   . LYS B 403 ? 1.4615 1.0572 0.7959 0.2574  0.2033  -0.0878 430 LYS B N   
7539 C CA  . LYS B 403 ? 1.4093 1.0211 0.7657 0.2402  0.1777  -0.0951 430 LYS B CA  
7540 C C   . LYS B 403 ? 1.3146 0.9376 0.7254 0.2232  0.1809  -0.0844 430 LYS B C   
7541 O O   . LYS B 403 ? 1.3392 0.9663 0.7686 0.2251  0.1970  -0.0671 430 LYS B O   
7542 C CB  . LYS B 403 ? 1.3753 0.9974 0.7089 0.2469  0.1660  -0.0921 430 LYS B CB  
7543 C CG  . LYS B 403 ? 1.3516 0.9689 0.6759 0.2597  0.1861  -0.0697 430 LYS B CG  
7544 C CD  . LYS B 403 ? 1.4559 1.0828 0.7638 0.2657  0.1708  -0.0668 430 LYS B CD  
7545 C CE  . LYS B 403 ? 1.5414 1.1572 0.8384 0.2779  0.1917  -0.0429 430 LYS B CE  
7546 N NZ  . LYS B 403 ? 1.5140 1.1384 0.8034 0.2832  0.1759  -0.0388 430 LYS B NZ  
7547 N N   . SER B 404 ? 1.3097 0.9360 0.7444 0.2065  0.1657  -0.0951 431 SER B N   
7548 C CA  . SER B 404 ? 1.1342 0.7699 0.6154 0.1910  0.1654  -0.0870 431 SER B CA  
7549 C C   . SER B 404 ? 1.0755 0.7240 0.5692 0.1728  0.1432  -0.0952 431 SER B C   
7550 O O   . SER B 404 ? 1.1413 0.7871 0.6165 0.1682  0.1284  -0.1112 431 SER B O   
7551 C CB  . SER B 404 ? 1.1439 0.7665 0.6429 0.1900  0.1728  -0.0891 431 SER B CB  
7552 O OG  . SER B 404 ? 1.3594 0.9737 0.8506 0.2067  0.1954  -0.0832 431 SER B OG  
7553 N N   . LEU B 405 ? 1.1374 0.8008 0.6641 0.1619  0.1417  -0.0854 432 LEU B N   
7554 C CA  . LEU B 405 ? 1.0658 0.7429 0.6084 0.1435  0.1244  -0.0916 432 LEU B CA  
7555 C C   . LEU B 405 ? 1.0076 0.6787 0.5775 0.1305  0.1235  -0.0891 432 LEU B C   
7556 O O   . LEU B 405 ? 0.9571 0.6274 0.5488 0.1342  0.1343  -0.0779 432 LEU B O   
7557 C CB  . LEU B 405 ? 1.0219 0.7200 0.5772 0.1421  0.1220  -0.0839 432 LEU B CB  
7558 C CG  . LEU B 405 ? 1.0638 0.7800 0.6381 0.1237  0.1069  -0.0901 432 LEU B CG  
7559 C CD1 . LEU B 405 ? 1.0501 0.7690 0.6076 0.1158  0.0921  -0.1081 432 LEU B CD1 
7560 C CD2 . LEU B 405 ? 1.0251 0.7606 0.6100 0.1265  0.1056  -0.0836 432 LEU B CD2 
7561 N N   . VAL B 406 ? 1.0138 0.6802 0.5823 0.1155  0.1105  -0.0997 433 VAL B N   
7562 C CA  . VAL B 406 ? 1.0575 0.7108 0.6422 0.1048  0.1083  -0.0974 433 VAL B CA  
7563 C C   . VAL B 406 ? 1.1343 0.8016 0.7333 0.0853  0.0976  -0.0976 433 VAL B C   
7564 O O   . VAL B 406 ? 1.0441 0.7197 0.6341 0.0745  0.0885  -0.1084 433 VAL B O   
7565 C CB  . VAL B 406 ? 1.0490 0.6748 0.6148 0.1044  0.1054  -0.1086 433 VAL B CB  
7566 C CG1 . VAL B 406 ? 1.0439 0.6517 0.6230 0.0950  0.1021  -0.1045 433 VAL B CG1 
7567 C CG2 . VAL B 406 ? 1.0013 0.6145 0.5515 0.1252  0.1175  -0.1097 433 VAL B CG2 
7568 N N   . PHE B 407 ? 1.0501 0.7217 0.6720 0.0811  0.0990  -0.0869 434 PHE B N   
7569 C CA  . PHE B 407 ? 0.9883 0.6724 0.6220 0.0640  0.0910  -0.0858 434 PHE B CA  
7570 C C   . PHE B 407 ? 0.9716 0.6342 0.6065 0.0548  0.0872  -0.0825 434 PHE B C   
7571 O O   . PHE B 407 ? 0.9849 0.6299 0.6232 0.0650  0.0906  -0.0774 434 PHE B O   
7572 C CB  . PHE B 407 ? 1.0180 0.7245 0.6741 0.0671  0.0939  -0.0767 434 PHE B CB  
7573 C CG  . PHE B 407 ? 1.0028 0.7306 0.6570 0.0717  0.0944  -0.0794 434 PHE B CG  
7574 C CD1 . PHE B 407 ? 1.1088 0.8465 0.7495 0.0651  0.0868  -0.0910 434 PHE B CD1 
7575 C CD2 . PHE B 407 ? 0.9990 0.7366 0.6666 0.0829  0.1022  -0.0707 434 PHE B CD2 
7576 C CE1 . PHE B 407 ? 1.1043 0.8617 0.7429 0.0725  0.0851  -0.0936 434 PHE B CE1 
7577 C CE2 . PHE B 407 ? 0.9372 0.6895 0.6001 0.0892  0.1022  -0.0718 434 PHE B CE2 
7578 C CZ  . PHE B 407 ? 0.9191 0.6817 0.5667 0.0854  0.0927  -0.0831 434 PHE B CZ  
7579 N N   . GLU B 408 ? 1.0297 0.6940 0.6615 0.0362  0.0805  -0.0854 435 GLU B N   
7580 C CA  . GLU B 408 ? 0.9314 0.5784 0.5633 0.0270  0.0770  -0.0784 435 GLU B CA  
7581 C C   . GLU B 408 ? 0.9309 0.6016 0.5795 0.0232  0.0753  -0.0714 435 GLU B C   
7582 O O   . GLU B 408 ? 1.1180 0.8152 0.7800 0.0283  0.0776  -0.0722 435 GLU B O   
7583 C CB  . GLU B 408 ? 1.1048 0.7323 0.7185 0.0081  0.0735  -0.0852 435 GLU B CB  
7584 C CG  . GLU B 408 ? 1.1292 0.7255 0.7264 0.0127  0.0740  -0.0921 435 GLU B CG  
7585 C CD  . GLU B 408 ? 1.2501 0.8238 0.8315 -0.0083 0.0714  -0.0996 435 GLU B CD  
7586 O OE1 . GLU B 408 ? 1.4322 1.0212 1.0167 -0.0274 0.0708  -0.1013 435 GLU B OE1 
7587 O OE2 . GLU B 408 ? 1.2129 0.7531 0.7800 -0.0063 0.0711  -0.1045 435 GLU B OE2 
7588 N N   . ASP B 409 ? 0.9776 0.6365 0.6230 0.0150  0.0711  -0.0648 436 ASP B N   
7589 C CA  . ASP B 409 ? 0.9191 0.5966 0.5795 0.0157  0.0685  -0.0585 436 ASP B CA  
7590 C C   . ASP B 409 ? 0.9252 0.6145 0.5787 -0.0027 0.0666  -0.0601 436 ASP B C   
7591 O O   . ASP B 409 ? 0.9429 0.6409 0.6018 -0.0033 0.0632  -0.0552 436 ASP B O   
7592 C CB  . ASP B 409 ? 0.9438 0.6029 0.6073 0.0258  0.0637  -0.0494 436 ASP B CB  
7593 C CG  . ASP B 409 ? 1.0475 0.6720 0.6856 0.0175  0.0592  -0.0451 436 ASP B CG  
7594 O OD1 . ASP B 409 ? 1.2029 0.8149 0.8226 0.0027  0.0619  -0.0496 436 ASP B OD1 
7595 O OD2 . ASP B 409 ? 1.1053 0.7142 0.7420 0.0259  0.0526  -0.0373 436 ASP B OD2 
7596 N N   . ASP B 410 ? 0.9622 0.6543 0.6052 -0.0176 0.0690  -0.0684 437 ASP B N   
7597 C CA  . ASP B 410 ? 1.1440 0.8494 0.7821 -0.0366 0.0702  -0.0711 437 ASP B CA  
7598 C C   . ASP B 410 ? 0.9679 0.6990 0.6129 -0.0455 0.0727  -0.0849 437 ASP B C   
7599 O O   . ASP B 410 ? 1.1383 0.8646 0.7747 -0.0629 0.0751  -0.0918 437 ASP B O   
7600 C CB  . ASP B 410 ? 1.3339 1.0058 0.9480 -0.0510 0.0708  -0.0648 437 ASP B CB  
7601 C CG  . ASP B 410 ? 1.7556 1.3953 1.3562 -0.0536 0.0717  -0.0675 437 ASP B CG  
7602 O OD1 . ASP B 410 ? 1.5674 1.2122 1.1762 -0.0428 0.0713  -0.0748 437 ASP B OD1 
7603 O OD2 . ASP B 410 ? 1.9036 1.5105 1.4832 -0.0662 0.0733  -0.0625 437 ASP B OD2 
7604 N N   . LEU B 411 ? 0.9328 0.6919 0.5946 -0.0333 0.0719  -0.0894 438 LEU B N   
7605 C CA  . LEU B 411 ? 1.0768 0.8616 0.7455 -0.0362 0.0713  -0.1029 438 LEU B CA  
7606 C C   . LEU B 411 ? 0.9217 0.7410 0.6081 -0.0301 0.0707  -0.1058 438 LEU B C   
7607 O O   . LEU B 411 ? 1.0438 0.8646 0.7385 -0.0189 0.0708  -0.0977 438 LEU B O   
7608 C CB  . LEU B 411 ? 1.1152 0.8906 0.7786 -0.0223 0.0697  -0.1069 438 LEU B CB  
7609 C CG  . LEU B 411 ? 1.0163 0.7777 0.6810 -0.0015 0.0717  -0.0963 438 LEU B CG  
7610 C CD1 . LEU B 411 ? 1.2896 1.0750 0.9671 0.0130  0.0724  -0.0960 438 LEU B CD1 
7611 C CD2 . LEU B 411 ? 1.0717 0.8075 0.7215 0.0061  0.0725  -0.0982 438 LEU B CD2 
7612 N N   . ARG B 412 ? 0.9754 0.8229 0.6695 -0.0376 0.0695  -0.1189 439 ARG B N   
7613 C CA  . ARG B 412 ? 0.8719 0.7533 0.5831 -0.0316 0.0683  -0.1245 439 ARG B CA  
7614 C C   . ARG B 412 ? 0.9269 0.8221 0.6421 -0.0152 0.0631  -0.1317 439 ARG B C   
7615 O O   . ARG B 412 ? 1.0297 0.9273 0.7394 -0.0185 0.0594  -0.1418 439 ARG B O   
7616 C CB  . ARG B 412 ? 0.8435 0.7506 0.5625 -0.0510 0.0710  -0.1351 439 ARG B CB  
7617 C CG  . ARG B 412 ? 1.2024 1.1474 0.9407 -0.0438 0.0692  -0.1443 439 ARG B CG  
7618 C CD  . ARG B 412 ? 0.9676 0.9423 0.7165 -0.0634 0.0737  -0.1575 439 ARG B CD  
7619 N NE  . ARG B 412 ? 1.1030 1.0650 0.8410 -0.0802 0.0823  -0.1500 439 ARG B NE  
7620 C CZ  . ARG B 412 ? 1.3054 1.2887 1.0485 -0.0988 0.0904  -0.1580 439 ARG B CZ  
7621 N NH1 . ARG B 412 ? 1.1818 1.2045 0.9465 -0.1038 0.0909  -0.1756 439 ARG B NH1 
7622 N NH2 . ARG B 412 ? 1.4201 1.3856 1.1457 -0.1118 0.0984  -0.1485 439 ARG B NH2 
7623 N N   . PHE B 413 ? 0.9694 0.8718 0.6925 0.0025  0.0625  -0.1268 440 PHE B N   
7624 C CA  . PHE B 413 ? 0.8461 0.7548 0.5668 0.0215  0.0583  -0.1296 440 PHE B CA  
7625 C C   . PHE B 413 ? 0.8472 0.7920 0.5807 0.0234  0.0519  -0.1439 440 PHE B C   
7626 O O   . PHE B 413 ? 0.8631 0.8281 0.6121 0.0177  0.0532  -0.1475 440 PHE B O   
7627 C CB  . PHE B 413 ? 0.7505 0.6447 0.4728 0.0394  0.0625  -0.1160 440 PHE B CB  
7628 C CG  . PHE B 413 ? 0.8477 0.7109 0.5609 0.0419  0.0685  -0.1039 440 PHE B CG  
7629 C CD1 . PHE B 413 ? 0.7514 0.6033 0.4714 0.0334  0.0718  -0.0964 440 PHE B CD1 
7630 C CD2 . PHE B 413 ? 0.9056 0.7522 0.6031 0.0546  0.0705  -0.1009 440 PHE B CD2 
7631 C CE1 . PHE B 413 ? 0.7776 0.6043 0.4932 0.0377  0.0762  -0.0868 440 PHE B CE1 
7632 C CE2 . PHE B 413 ? 0.9521 0.7730 0.6442 0.0580  0.0773  -0.0912 440 PHE B CE2 
7633 C CZ  . PHE B 413 ? 0.9368 0.7489 0.6402 0.0497  0.0798  -0.0844 440 PHE B CZ  
7634 N N   . GLU B 414 ? 0.8077 0.7615 0.5343 0.0330  0.0444  -0.1532 441 GLU B N   
7635 C CA  . GLU B 414 ? 0.8171 0.8064 0.5565 0.0402  0.0357  -0.1675 441 GLU B CA  
7636 C C   . GLU B 414 ? 0.8738 0.8623 0.6144 0.0635  0.0347  -0.1595 441 GLU B C   
7637 O O   . GLU B 414 ? 0.8644 0.8243 0.5940 0.0745  0.0410  -0.1435 441 GLU B O   
7638 C CB  . GLU B 414 ? 0.8211 0.8200 0.5513 0.0444  0.0251  -0.1815 441 GLU B CB  
7639 C CG  . GLU B 414 ? 1.0191 1.0327 0.7589 0.0191  0.0238  -0.1971 441 GLU B CG  
7640 C CD  . GLU B 414 ? 1.1907 1.2494 0.9593 0.0088  0.0209  -0.2140 441 GLU B CD  
7641 O OE1 . GLU B 414 ? 1.1356 1.2187 0.9144 0.0270  0.0139  -0.2189 441 GLU B OE1 
7642 O OE2 . GLU B 414 ? 1.0841 1.1530 0.8650 -0.0170 0.0267  -0.2221 441 GLU B OE2 
7643 N N   . ILE B 415 ? 0.7816 0.8022 0.5376 0.0709  0.0275  -0.1713 442 ILE B N   
7644 C CA  . ILE B 415 ? 0.7531 0.7708 0.5094 0.0942  0.0256  -0.1648 442 ILE B CA  
7645 C C   . ILE B 415 ? 0.9141 0.9108 0.6441 0.1165  0.0210  -0.1574 442 ILE B C   
7646 O O   . ILE B 415 ? 0.9064 0.9083 0.6233 0.1179  0.0129  -0.1663 442 ILE B O   
7647 C CB  . ILE B 415 ? 0.7478 0.8054 0.5268 0.0988  0.0178  -0.1812 442 ILE B CB  
7648 C CG1 . ILE B 415 ? 0.7507 0.7998 0.5305 0.1224  0.0167  -0.1736 442 ILE B CG1 
7649 C CG2 . ILE B 415 ? 0.7587 0.8460 0.5396 0.1025  0.0042  -0.1996 442 ILE B CG2 
7650 C CD1 . ILE B 415 ? 0.7436 0.8297 0.5482 0.1279  0.0105  -0.1895 442 ILE B CD1 
7651 N N   . PHE B 416 ? 0.7903 0.7611 0.5110 0.1333  0.0270  -0.1413 443 PHE B N   
7652 C CA  . PHE B 416 ? 0.8131 0.7587 0.5042 0.1557  0.0264  -0.1306 443 PHE B CA  
7653 C C   . PHE B 416 ? 0.9190 0.8440 0.5886 0.1496  0.0311  -0.1262 443 PHE B C   
7654 O O   . PHE B 416 ? 0.9910 0.9073 0.6333 0.1648  0.0257  -0.1267 443 PHE B O   
7655 C CB  . PHE B 416 ? 0.8339 0.7998 0.5157 0.1763  0.0100  -0.1423 443 PHE B CB  
7656 C CG  . PHE B 416 ? 0.8763 0.8666 0.5813 0.1840  0.0036  -0.1501 443 PHE B CG  
7657 C CD1 . PHE B 416 ? 0.8576 0.8311 0.5728 0.1876  0.0133  -0.1382 443 PHE B CD1 
7658 C CD2 . PHE B 416 ? 0.8250 0.8564 0.5441 0.1876  -0.0123 -0.1715 443 PHE B CD2 
7659 C CE1 . PHE B 416 ? 0.8193 0.8136 0.5552 0.1958  0.0073  -0.1471 443 PHE B CE1 
7660 C CE2 . PHE B 416 ? 0.8181 0.8738 0.5602 0.1963  -0.0179 -0.1803 443 PHE B CE2 
7661 C CZ  . PHE B 416 ? 0.8126 0.8482 0.5615 0.2010  -0.0080 -0.1679 443 PHE B CZ  
7662 N N   . PHE B 417 ? 0.8677 0.7837 0.5475 0.1292  0.0404  -0.1225 444 PHE B N   
7663 C CA  . PHE B 417 ? 0.8182 0.7153 0.4803 0.1230  0.0442  -0.1207 444 PHE B CA  
7664 C C   . PHE B 417 ? 0.8439 0.7107 0.4784 0.1426  0.0522  -0.1063 444 PHE B C   
7665 O O   . PHE B 417 ? 0.9704 0.8295 0.5788 0.1509  0.0483  -0.1105 444 PHE B O   
7666 C CB  . PHE B 417 ? 0.8541 0.7419 0.5312 0.1020  0.0532  -0.1159 444 PHE B CB  
7667 C CG  . PHE B 417 ? 0.8872 0.7495 0.5474 0.0992  0.0592  -0.1112 444 PHE B CG  
7668 C CD1 . PHE B 417 ? 0.8403 0.7050 0.4921 0.0881  0.0528  -0.1238 444 PHE B CD1 
7669 C CD2 . PHE B 417 ? 0.8169 0.6531 0.4719 0.1074  0.0718  -0.0954 444 PHE B CD2 
7670 C CE1 . PHE B 417 ? 0.8976 0.7367 0.5334 0.0870  0.0580  -0.1207 444 PHE B CE1 
7671 C CE2 . PHE B 417 ? 0.8306 0.6452 0.4717 0.1067  0.0777  -0.0926 444 PHE B CE2 
7672 C CZ  . PHE B 417 ? 0.8726 0.6874 0.5028 0.0973  0.0704  -0.1052 444 PHE B CZ  
7673 N N   . LYS B 418 ? 0.8415 0.6905 0.4812 0.1497  0.0643  -0.0900 445 LYS B N   
7674 C CA  . LYS B 418 ? 0.8670 0.6854 0.4832 0.1647  0.0772  -0.0744 445 LYS B CA  
7675 C C   . LYS B 418 ? 1.0358 0.8494 0.6180 0.1881  0.0704  -0.0745 445 LYS B C   
7676 O O   . LYS B 418 ? 1.0601 0.8571 0.6112 0.1979  0.0739  -0.0720 445 LYS B O   
7677 C CB  . LYS B 418 ? 0.8584 0.6616 0.4928 0.1653  0.0917  -0.0587 445 LYS B CB  
7678 C CG  . LYS B 418 ? 0.9058 0.6782 0.5199 0.1788  0.1090  -0.0416 445 LYS B CG  
7679 C CD  . LYS B 418 ? 0.8771 0.6368 0.5171 0.1750  0.1240  -0.0284 445 LYS B CD  
7680 C CE  . LYS B 418 ? 0.9512 0.6810 0.5730 0.1869  0.1445  -0.0112 445 LYS B CE  
7681 N NZ  . LYS B 418 ? 1.1003 0.8194 0.7535 0.1799  0.1601  -0.0002 445 LYS B NZ  
7682 N N   . ARG B 419 ? 0.9837 0.8113 0.5693 0.1990  0.0601  -0.0780 446 ARG B N   
7683 C CA  . ARG B 419 ? 0.9542 0.7769 0.5052 0.2243  0.0509  -0.0780 446 ARG B CA  
7684 C C   . ARG B 419 ? 0.9817 0.8236 0.5165 0.2250  0.0340  -0.0971 446 ARG B C   
7685 O O   . ARG B 419 ? 1.0994 0.9277 0.5952 0.2435  0.0303  -0.0959 446 ARG B O   
7686 C CB  . ARG B 419 ? 0.9460 0.7806 0.5075 0.2371  0.0415  -0.0792 446 ARG B CB  
7687 C CG  . ARG B 419 ? 0.9659 0.7672 0.5191 0.2508  0.0564  -0.0574 446 ARG B CG  
7688 C CD  . ARG B 419 ? 1.0440 0.8519 0.5964 0.2704  0.0438  -0.0596 446 ARG B CD  
7689 N NE  . ARG B 419 ? 0.9849 0.8289 0.5784 0.2573  0.0333  -0.0764 446 ARG B NE  
7690 C CZ  . ARG B 419 ? 1.0713 0.9329 0.6737 0.2716  0.0194  -0.0852 446 ARG B CZ  
7691 N NH1 . ARG B 419 ? 1.1657 1.0107 0.7379 0.3007  0.0120  -0.0783 446 ARG B NH1 
7692 N NH2 . ARG B 419 ? 1.0693 0.9653 0.7100 0.2575  0.0131  -0.1013 446 ARG B NH2 
7693 N N   . ARG B 420 ? 0.9663 0.8388 0.5295 0.2044  0.0240  -0.1154 447 ARG B N   
7694 C CA  . ARG B 420 ? 1.0338 0.9268 0.5878 0.2022  0.0074  -0.1364 447 ARG B CA  
7695 C C   . ARG B 420 ? 1.1196 0.9888 0.6479 0.1990  0.0142  -0.1352 447 ARG B C   
7696 O O   . ARG B 420 ? 1.1089 0.9796 0.6097 0.2101  0.0024  -0.1466 447 ARG B O   
7697 C CB  . ARG B 420 ? 0.9057 0.8352 0.4988 0.1779  -0.0009 -0.1552 447 ARG B CB  
7698 C CG  . ARG B 420 ? 0.8961 0.8590 0.5113 0.1853  -0.0131 -0.1649 447 ARG B CG  
7699 C CD  . ARG B 420 ? 0.8608 0.8551 0.5172 0.1590  -0.0129 -0.1779 447 ARG B CD  
7700 N NE  . ARG B 420 ? 0.9447 0.9628 0.6104 0.1416  -0.0223 -0.1992 447 ARG B NE  
7701 C CZ  . ARG B 420 ? 1.0108 1.0596 0.7096 0.1181  -0.0229 -0.2137 447 ARG B CZ  
7702 N NH1 . ARG B 420 ? 0.9133 0.9749 0.6371 0.1105  -0.0154 -0.2101 447 ARG B NH1 
7703 N NH2 . ARG B 420 ? 1.0665 1.1330 0.7730 0.1014  -0.0301 -0.2328 447 ARG B NH2 
7704 N N   . LEU B 421 ? 1.0867 0.9343 0.6235 0.1856  0.0320  -0.1228 448 LEU B N   
7705 C CA  . LEU B 421 ? 1.0710 0.8953 0.5852 0.1841  0.0394  -0.1221 448 LEU B CA  
7706 C C   . LEU B 421 ? 1.1279 0.9241 0.6014 0.2092  0.0491  -0.1079 448 LEU B C   
7707 O O   . LEU B 421 ? 1.1589 0.9444 0.5994 0.2186  0.0460  -0.1148 448 LEU B O   
7708 C CB  . LEU B 421 ? 1.0842 0.8960 0.6219 0.1641  0.0540  -0.1143 448 LEU B CB  
7709 C CG  . LEU B 421 ? 1.1404 0.9286 0.6602 0.1620  0.0619  -0.1150 448 LEU B CG  
7710 C CD1 . LEU B 421 ? 0.9683 0.7659 0.4765 0.1557  0.0461  -0.1372 448 LEU B CD1 
7711 C CD2 . LEU B 421 ? 1.0327 0.8105 0.5784 0.1449  0.0739  -0.1068 448 LEU B CD2 
7712 N N   . MET B 422 ? 1.1112 0.8937 0.5850 0.2198  0.0618  -0.0884 449 MET B N   
7713 C CA  . MET B 422 ? 1.1743 0.9268 0.6082 0.2422  0.0751  -0.0721 449 MET B CA  
7714 C C   . MET B 422 ? 1.2565 1.0113 0.6485 0.2661  0.0585  -0.0795 449 MET B C   
7715 O O   . MET B 422 ? 1.3978 1.1296 0.7453 0.2834  0.0651  -0.0737 449 MET B O   
7716 C CB  . MET B 422 ? 1.0538 0.7903 0.5004 0.2462  0.0924  -0.0502 449 MET B CB  
7717 C CG  . MET B 422 ? 1.1881 0.9174 0.6695 0.2272  0.1111  -0.0411 449 MET B CG  
7718 S SD  . MET B 422 ? 1.2729 0.9822 0.7707 0.2309  0.1319  -0.0178 449 MET B SD  
7719 C CE  . MET B 422 ? 1.2681 0.9407 0.7174 0.2517  0.1542  0.0002  449 MET B CE  
7720 N N   . ASN B 423 ? 1.1450 0.9284 0.5495 0.2687  0.0367  -0.0930 450 ASN B N   
7721 C CA  . ASN B 423 ? 1.2574 1.0471 0.6245 0.2932  0.0170  -0.1024 450 ASN B CA  
7722 C C   . ASN B 423 ? 1.3025 1.1020 0.6516 0.2904  0.0034  -0.1243 450 ASN B C   
7723 O O   . ASN B 423 ? 1.5080 1.2974 0.8101 0.3130  -0.0053 -0.1277 450 ASN B O   
7724 C CB  . ASN B 423 ? 1.1263 0.9483 0.5181 0.2975  -0.0032 -0.1130 450 ASN B CB  
7725 C CG  . ASN B 423 ? 1.2580 1.0658 0.6611 0.3049  0.0083  -0.0927 450 ASN B CG  
7726 O OD1 . ASN B 423 ? 1.3324 1.1036 0.7153 0.3124  0.0295  -0.0695 450 ASN B OD1 
7727 N ND2 . ASN B 423 ? 1.1707 1.0077 0.6077 0.3021  -0.0045 -0.1023 450 ASN B ND2 
7728 N N   . LEU B 424 ? 1.2514 1.0682 0.6353 0.2631  0.0012  -0.1395 451 LEU B N   
7729 C CA  . LEU B 424 ? 1.2840 1.1058 0.6539 0.2574  -0.0101 -0.1610 451 LEU B CA  
7730 C C   . LEU B 424 ? 1.3478 1.1326 0.6760 0.2679  0.0061  -0.1511 451 LEU B C   
7731 O O   . LEU B 424 ? 1.4459 1.2250 0.7338 0.2834  -0.0043 -0.1629 451 LEU B O   
7732 C CB  . LEU B 424 ? 1.1655 1.0061 0.5807 0.2246  -0.0119 -0.1756 451 LEU B CB  
7733 C CG  . LEU B 424 ? 1.1511 0.9902 0.5560 0.2144  -0.0205 -0.1972 451 LEU B CG  
7734 C CD1 . LEU B 424 ? 1.1264 0.9888 0.5124 0.2283  -0.0468 -0.2209 451 LEU B CD1 
7735 C CD2 . LEU B 424 ? 1.3097 1.1598 0.7571 0.1812  -0.0187 -0.2072 451 LEU B CD2 
7736 N N   . MET B 425 ? 1.2742 1.0354 0.6125 0.2603  0.0317  -0.1308 452 MET B N   
7737 C CA  . MET B 425 ? 1.3096 1.0383 0.6132 0.2702  0.0505  -0.1212 452 MET B CA  
7738 C C   . MET B 425 ? 1.4465 1.1561 0.6949 0.3013  0.0534  -0.1099 452 MET B C   
7739 O O   . MET B 425 ? 1.5379 1.2292 0.7422 0.3152  0.0569  -0.1137 452 MET B O   
7740 C CB  . MET B 425 ? 1.2215 0.9341 0.5530 0.2575  0.0768  -0.1016 452 MET B CB  
7741 C CG  . MET B 425 ? 1.3845 1.1108 0.7637 0.2292  0.0744  -0.1105 452 MET B CG  
7742 S SD  . MET B 425 ? 1.3158 1.0418 0.6862 0.2182  0.0619  -0.1364 452 MET B SD  
7743 C CE  . MET B 425 ? 1.3011 0.9916 0.6351 0.2338  0.0847  -0.1269 452 MET B CE  
7744 N N   . ARG B 426 ? 1.4522 1.1632 0.6994 0.3136  0.0521  -0.0959 453 ARG B N   
7745 C CA  . ARG B 426 ? 1.4822 1.1711 0.6729 0.3446  0.0540  -0.0829 453 ARG B CA  
7746 C C   . ARG B 426 ? 1.4954 1.1971 0.6471 0.3621  0.0258  -0.1054 453 ARG B C   
7747 O O   . ARG B 426 ? 1.6094 1.2884 0.7029 0.3843  0.0288  -0.1025 453 ARG B O   
7748 C CB  . ARG B 426 ? 1.3717 1.0585 0.5729 0.3533  0.0556  -0.0651 453 ARG B CB  
7749 C CG  . ARG B 426 ? 1.5735 1.2207 0.7247 0.3781  0.0752  -0.0383 453 ARG B CG  
7750 C CD  . ARG B 426 ? 1.7036 1.3436 0.8742 0.3816  0.0807  -0.0195 453 ARG B CD  
7751 N NE  . ARG B 426 ? 1.7275 1.3758 0.9594 0.3540  0.0954  -0.0146 453 ARG B NE  
7752 C CZ  . ARG B 426 ? 1.6410 1.3187 0.9223 0.3392  0.0811  -0.0253 453 ARG B CZ  
7753 N NH1 . ARG B 426 ? 1.4892 1.1936 0.7718 0.3481  0.0529  -0.0418 453 ARG B NH1 
7754 N NH2 . ARG B 426 ? 1.3794 1.0614 0.7100 0.3157  0.0953  -0.0202 453 ARG B NH2 
7755 N N   . ASP B 427 ? 1.4390 1.1787 0.6229 0.3518  -0.0016 -0.1293 454 ASP B N   
7756 C CA  . ASP B 427 ? 1.4894 1.2477 0.6456 0.3654  -0.0311 -0.1554 454 ASP B CA  
7757 C C   . ASP B 427 ? 1.4898 1.2368 0.6237 0.3598  -0.0290 -0.1709 454 ASP B C   
7758 O O   . ASP B 427 ? 1.5845 1.3235 0.6660 0.3818  -0.0412 -0.1814 454 ASP B O   
7759 C CB  . ASP B 427 ? 1.4692 1.2746 0.6754 0.3505  -0.0575 -0.1795 454 ASP B CB  
7760 C CG  . ASP B 427 ? 1.6601 1.4793 0.8833 0.3616  -0.0640 -0.1688 454 ASP B CG  
7761 O OD1 . ASP B 427 ? 1.7628 1.5512 0.9603 0.3789  -0.0474 -0.1414 454 ASP B OD1 
7762 O OD2 . ASP B 427 ? 1.6757 1.5358 0.9389 0.3528  -0.0848 -0.1884 454 ASP B OD2 
7763 N N   . VAL B 428 ? 1.4679 1.2123 0.6387 0.3320  -0.0143 -0.1730 455 VAL B N   
7764 C CA  . VAL B 428 ? 1.4983 1.2285 0.6511 0.3262  -0.0110 -0.1878 455 VAL B CA  
7765 C C   . VAL B 428 ? 1.5853 1.2787 0.6766 0.3514  0.0079  -0.1726 455 VAL B C   
7766 O O   . VAL B 428 ? 1.7935 1.4783 0.8398 0.3657  -0.0015 -0.1887 455 VAL B O   
7767 C CB  . VAL B 428 ? 1.4410 1.1692 0.6431 0.2948  0.0041  -0.1873 455 VAL B CB  
7768 C CG1 . VAL B 428 ? 1.4488 1.1535 0.6280 0.2932  0.0126  -0.1977 455 VAL B CG1 
7769 C CG2 . VAL B 428 ? 1.2908 1.0535 0.5447 0.2693  -0.0151 -0.2066 455 VAL B CG2 
7770 N N   . GLU B 429 ? 1.5380 1.2091 0.6264 0.3568  0.0356  -0.1421 456 GLU B N   
7771 C CA  . GLU B 429 ? 1.5464 1.1824 0.5778 0.3794  0.0585  -0.1251 456 GLU B CA  
7772 C C   . GLU B 429 ? 1.8074 1.4402 0.7871 0.4081  0.0416  -0.1238 456 GLU B C   
7773 O O   . GLU B 429 ? 1.7888 1.4076 0.7333 0.4205  0.0439  -0.1239 456 GLU B O   
7774 C CB  . GLU B 429 ? 1.5165 1.1333 0.5658 0.3755  0.0916  -0.0929 456 GLU B CB  
7775 C CG  . GLU B 429 ? 1.9642 1.5449 0.9585 0.3966  0.1204  -0.0726 456 GLU B CG  
7776 C CD  . GLU B 429 ? 2.1039 1.6686 1.1242 0.3892  0.1539  -0.0429 456 GLU B CD  
7777 O OE1 . GLU B 429 ? 1.9346 1.5162 1.0145 0.3685  0.1524  -0.0393 456 GLU B OE1 
7778 O OE2 . GLU B 429 ? 2.1451 1.6812 1.1279 0.4031  0.1818  -0.0240 456 GLU B OE2 
7779 N N   . ARG B 430 ? 1.8024 1.4502 0.7831 0.4183  0.0232  -0.1221 457 ARG B N   
7780 C CA  . ARG B 430 ? 1.7843 1.4308 0.7237 0.4461  0.0041  -0.1195 457 ARG B CA  
7781 C C   . ARG B 430 ? 1.8130 1.4784 0.7419 0.4488  -0.0237 -0.1485 457 ARG B C   
7782 O O   . ARG B 430 ? 1.9611 1.6133 0.8457 0.4707  -0.0289 -0.1449 457 ARG B O   
7783 C CB  . ARG B 430 ? 1.7108 1.3758 0.6618 0.4554  -0.0151 -0.1184 457 ARG B CB  
7784 C CG  . ARG B 430 ? 1.9333 1.5854 0.8382 0.4886  -0.0272 -0.1051 457 ARG B CG  
7785 C CD  . ARG B 430 ? 1.8492 1.4616 0.7311 0.5001  0.0031  -0.0678 457 ARG B CD  
7786 N NE  . ARG B 430 ? 2.0165 1.6391 0.9471 0.4831  0.0109  -0.0612 457 ARG B NE  
7787 C CZ  . ARG B 430 ? 1.9329 1.5282 0.8693 0.4834  0.0363  -0.0310 457 ARG B CZ  
7788 N NH1 . ARG B 430 ? 2.0162 1.5663 0.8940 0.5044  0.0596  -0.0041 457 ARG B NH1 
7789 N NH2 . ARG B 430 ? 1.5700 1.1827 0.5717 0.4616  0.0394  -0.0283 457 ARG B NH2 
7790 N N   . GLU B 431 ? 1.8000 1.4947 0.7687 0.4261  -0.0407 -0.1777 458 GLU B N   
7791 C CA  . GLU B 431 ? 1.8769 1.5906 0.8428 0.4242  -0.0667 -0.2083 458 GLU B CA  
7792 C C   . GLU B 431 ? 1.9147 1.6074 0.8691 0.4148  -0.0502 -0.2136 458 GLU B C   
7793 O O   . GLU B 431 ? 1.8335 1.5361 0.7800 0.4141  -0.0691 -0.2382 458 GLU B O   
7794 C CB  . GLU B 431 ? 1.7034 1.4588 0.7200 0.4027  -0.0928 -0.2387 458 GLU B CB  
7795 C CG  . GLU B 431 ? 2.1013 1.8828 1.1380 0.4099  -0.1084 -0.2364 458 GLU B CG  
7796 C CD  . GLU B 431 ? 2.1452 1.9316 1.1468 0.4427  -0.1292 -0.2323 458 GLU B CD  
7797 O OE1 . GLU B 431 ? 2.1945 1.9786 1.1670 0.4552  -0.1422 -0.2432 458 GLU B OE1 
7798 O OE2 . GLU B 431 ? 2.0856 1.8769 1.0878 0.4572  -0.1330 -0.2189 458 GLU B OE2 
7799 N N   . GLY B 432 ? 1.8146 1.4796 0.7694 0.4081  -0.0160 -0.1924 459 GLY B N   
7800 C CA  . GLY B 432 ? 1.6860 1.3312 0.6313 0.4015  0.0011  -0.1969 459 GLY B CA  
7801 C C   . GLY B 432 ? 1.7117 1.3711 0.6892 0.3778  -0.0129 -0.2282 459 GLY B C   
7802 O O   . GLY B 432 ? 1.7029 1.3523 0.6652 0.3773  -0.0130 -0.2426 459 GLY B O   
7803 N N   . LEU B 433 ? 1.6793 1.3600 0.6999 0.3579  -0.0241 -0.2395 460 LEU B N   
7804 C CA  . LEU B 433 ? 1.6257 1.3170 0.6776 0.3333  -0.0372 -0.2691 460 LEU B CA  
7805 C C   . LEU B 433 ? 1.6776 1.3395 0.7331 0.3225  -0.0121 -0.2659 460 LEU B C   
7806 O O   . LEU B 433 ? 1.7048 1.3493 0.7668 0.3220  0.0148  -0.2424 460 LEU B O   
7807 C CB  . LEU B 433 ? 1.6613 1.3784 0.7579 0.3140  -0.0489 -0.2777 460 LEU B CB  
7808 C CG  . LEU B 433 ? 1.6205 1.3487 0.7572 0.2838  -0.0609 -0.3056 460 LEU B CG  
7809 C CD1 . LEU B 433 ? 1.4882 1.2346 0.6173 0.2839  -0.0897 -0.3380 460 LEU B CD1 
7810 C CD2 . LEU B 433 ? 1.4512 1.2087 0.6502 0.2589  -0.0643 -0.3007 460 LEU B CD2 
7811 N N   . ASP B 434 ? 1.6327 1.2890 0.6855 0.3145  -0.0213 -0.2904 461 ASP B N   
7812 C CA  . ASP B 434 ? 1.6385 1.2672 0.6983 0.3040  -0.0016 -0.2922 461 ASP B CA  
7813 C C   . ASP B 434 ? 1.7558 1.3866 0.8584 0.2771  -0.0054 -0.3033 461 ASP B C   
7814 O O   . ASP B 434 ? 1.8668 1.5116 0.9872 0.2605  -0.0285 -0.3304 461 ASP B O   
7815 C CB  . ASP B 434 ? 1.6996 1.3182 0.7367 0.3077  -0.0100 -0.3146 461 ASP B CB  
7816 C CG  . ASP B 434 ? 1.8310 1.4197 0.8745 0.2999  0.0097  -0.3175 461 ASP B CG  
7817 O OD1 . ASP B 434 ? 1.9295 1.5046 0.9908 0.2956  0.0323  -0.2983 461 ASP B OD1 
7818 O OD2 . ASP B 434 ? 1.8111 1.3898 0.8427 0.2987  0.0019  -0.3397 461 ASP B OD2 
7819 N N   . TRP B 435 ? 1.6388 1.2605 0.7701 0.2682  0.0173  -0.2791 462 TRP B N   
7820 C CA  . TRP B 435 ? 1.6185 1.2500 0.8081 0.2374  0.0153  -0.2780 462 TRP B CA  
7821 C C   . TRP B 435 ? 1.4764 1.0816 0.6842 0.2302  0.0394  -0.2635 462 TRP B C   
7822 O O   . TRP B 435 ? 1.4899 1.0800 0.6800 0.2474  0.0617  -0.2451 462 TRP B O   
7823 C CB  . TRP B 435 ? 1.4267 1.0873 0.6477 0.2309  0.0124  -0.2608 462 TRP B CB  
7824 C CG  . TRP B 435 ? 1.4274 1.0803 0.6462 0.2438  0.0364  -0.2288 462 TRP B CG  
7825 C CD1 . TRP B 435 ? 1.3448 0.9949 0.5261 0.2696  0.0436  -0.2143 462 TRP B CD1 
7826 C CD2 . TRP B 435 ? 1.3438 0.9896 0.5999 0.2309  0.0565  -0.2077 462 TRP B CD2 
7827 N NE1 . TRP B 435 ? 1.3026 0.9441 0.4988 0.2714  0.0684  -0.1859 462 TRP B NE1 
7828 C CE2 . TRP B 435 ? 1.2600 0.9010 0.5033 0.2483  0.0755  -0.1826 462 TRP B CE2 
7829 C CE3 . TRP B 435 ? 1.3215 0.9632 0.6190 0.2069  0.0596  -0.2078 462 TRP B CE3 
7830 C CZ2 . TRP B 435 ? 1.2676 0.9040 0.5431 0.2413  0.0964  -0.1603 462 TRP B CZ2 
7831 C CZ3 . TRP B 435 ? 1.3146 0.9514 0.6398 0.2026  0.0788  -0.1848 462 TRP B CZ3 
7832 C CH2 . TRP B 435 ? 1.4749 1.1109 0.7913 0.2192  0.0964  -0.1627 462 TRP B CH2 
7833 N N   . ASP B 436 ? 1.4095 1.0095 0.6536 0.2047  0.0349  -0.2721 463 ASP B N   
7834 C CA  . ASP B 436 ? 1.4035 0.9806 0.6705 0.1966  0.0534  -0.2590 463 ASP B CA  
7835 C C   . ASP B 436 ? 1.3385 0.9288 0.6537 0.1745  0.0553  -0.2430 463 ASP B C   
7836 O O   . ASP B 436 ? 1.2932 0.8744 0.6264 0.1754  0.0725  -0.2229 463 ASP B O   
7837 C CB  . ASP B 436 ? 1.4826 1.0311 0.7442 0.1881  0.0484  -0.2812 463 ASP B CB  
7838 C CG  . ASP B 436 ? 1.6710 1.2035 0.8834 0.2103  0.0470  -0.2996 463 ASP B CG  
7839 O OD1 . ASP B 436 ? 1.7743 1.3078 0.9560 0.2349  0.0602  -0.2877 463 ASP B OD1 
7840 O OD2 . ASP B 436 ? 1.5882 1.1057 0.7913 0.2027  0.0335  -0.3263 463 ASP B OD2 
7841 N N   . LEU B 437 ? 1.2852 0.8985 0.6220 0.1554  0.0380  -0.2525 464 LEU B N   
7842 C CA  . LEU B 437 ? 1.2635 0.8882 0.6427 0.1326  0.0391  -0.2406 464 LEU B CA  
7843 C C   . LEU B 437 ? 1.2845 0.9473 0.6784 0.1254  0.0248  -0.2447 464 LEU B C   
7844 O O   . LEU B 437 ? 1.3364 1.0138 0.7219 0.1227  0.0071  -0.2673 464 LEU B O   
7845 C CB  . LEU B 437 ? 1.1969 0.7999 0.5929 0.1089  0.0354  -0.2521 464 LEU B CB  
7846 C CG  . LEU B 437 ? 1.3830 0.9935 0.8168 0.0839  0.0365  -0.2411 464 LEU B CG  
7847 C CD1 . LEU B 437 ? 1.1322 0.7362 0.5787 0.0916  0.0529  -0.2145 464 LEU B CD1 
7848 C CD2 . LEU B 437 ? 1.5391 1.1235 0.9810 0.0608  0.0320  -0.2544 464 LEU B CD2 
7849 N N   . ILE B 438 ? 1.2106 0.8906 0.6283 0.1227  0.0316  -0.2247 465 ILE B N   
7850 C CA  . ILE B 438 ? 1.2527 0.9694 0.6885 0.1169  0.0198  -0.2273 465 ILE B CA  
7851 C C   . ILE B 438 ? 1.1790 0.9040 0.6540 0.0935  0.0245  -0.2171 465 ILE B C   
7852 O O   . ILE B 438 ? 1.1367 0.8547 0.6226 0.0963  0.0382  -0.1958 465 ILE B O   
7853 C CB  . ILE B 438 ? 1.2285 0.9582 0.6480 0.1416  0.0228  -0.2132 465 ILE B CB  
7854 C CG1 . ILE B 438 ? 1.1871 0.9061 0.5603 0.1662  0.0185  -0.2225 465 ILE B CG1 
7855 C CG2 . ILE B 438 ? 1.1303 0.8974 0.5713 0.1367  0.0098  -0.2169 465 ILE B CG2 
7856 C CD1 . ILE B 438 ? 1.2452 0.9713 0.5950 0.1917  0.0216  -0.2079 465 ILE B CD1 
7857 N N   . TYR B 439 ? 1.1705 0.9111 0.6664 0.0701  0.0136  -0.2331 466 TYR B N   
7858 C CA  . TYR B 439 ? 1.1219 0.8707 0.6505 0.0471  0.0184  -0.2246 466 TYR B CA  
7859 C C   . TYR B 439 ? 1.1547 0.9372 0.7004 0.0526  0.0178  -0.2148 466 TYR B C   
7860 O O   . TYR B 439 ? 1.1826 0.9966 0.7324 0.0563  0.0052  -0.2280 466 TYR B O   
7861 C CB  . TYR B 439 ? 1.1291 0.8849 0.6743 0.0194  0.0097  -0.2451 466 TYR B CB  
7862 C CG  . TYR B 439 ? 1.3233 1.0391 0.8591 0.0066  0.0132  -0.2512 466 TYR B CG  
7863 C CD1 . TYR B 439 ? 1.3061 0.9945 0.8500 -0.0067 0.0248  -0.2358 466 TYR B CD1 
7864 C CD2 . TYR B 439 ? 1.2863 0.9904 0.8041 0.0086  0.0035  -0.2735 466 TYR B CD2 
7865 C CE1 . TYR B 439 ? 1.2341 0.8818 0.7680 -0.0168 0.0274  -0.2407 466 TYR B CE1 
7866 C CE2 . TYR B 439 ? 1.2648 0.9289 0.7742 -0.0028 0.0066  -0.2801 466 TYR B CE2 
7867 C CZ  . TYR B 439 ? 1.2149 0.8497 0.7324 -0.0152 0.0189  -0.2630 466 TYR B CZ  
7868 O OH  . TYR B 439 ? 1.4028 0.9937 0.9103 -0.0246 0.0214  -0.2689 466 TYR B OH  
7869 N N   . VAL B 440 ? 1.0967 0.8728 0.6535 0.0540  0.0302  -0.1932 467 VAL B N   
7870 C CA  . VAL B 440 ? 1.0700 0.8751 0.6476 0.0543  0.0302  -0.1853 467 VAL B CA  
7871 C C   . VAL B 440 ? 1.0629 0.8824 0.6682 0.0274  0.0302  -0.1888 467 VAL B C   
7872 O O   . VAL B 440 ? 1.0410 0.8928 0.6654 0.0239  0.0263  -0.1918 467 VAL B O   
7873 C CB  . VAL B 440 ? 1.0611 0.8542 0.6380 0.0696  0.0430  -0.1622 467 VAL B CB  
7874 C CG1 . VAL B 440 ? 1.0423 0.8633 0.6352 0.0753  0.0413  -0.1565 467 VAL B CG1 
7875 C CG2 . VAL B 440 ? 1.0385 0.8103 0.5861 0.0927  0.0485  -0.1570 467 VAL B CG2 
7876 N N   . GLY B 441 ? 1.0745 0.8692 0.6803 0.0093  0.0351  -0.1884 468 GLY B N   
7877 C CA  . GLY B 441 ? 1.0037 0.8064 0.6291 -0.0177 0.0368  -0.1919 468 GLY B CA  
7878 C C   . GLY B 441 ? 1.2608 1.0333 0.8782 -0.0361 0.0376  -0.2000 468 GLY B C   
7879 O O   . GLY B 441 ? 1.2831 1.0187 0.8830 -0.0286 0.0419  -0.1925 468 GLY B O   
7880 N N   . ARG B 442 ? 1.2394 1.0266 0.8709 -0.0601 0.0343  -0.2159 469 ARG B N   
7881 C CA  . ARG B 442 ? 1.1979 0.9552 0.8229 -0.0796 0.0348  -0.2263 469 ARG B CA  
7882 C C   . ARG B 442 ? 1.2787 1.0583 0.9275 -0.1106 0.0364  -0.2387 469 ARG B C   
7883 O O   . ARG B 442 ? 1.2463 1.0649 0.9157 -0.1148 0.0374  -0.2390 469 ARG B O   
7884 C CB  . ARG B 442 ? 1.2907 1.0401 0.8998 -0.0679 0.0244  -0.2443 469 ARG B CB  
7885 C CG  . ARG B 442 ? 1.2916 1.0868 0.9100 -0.0586 0.0109  -0.2629 469 ARG B CG  
7886 C CD  . ARG B 442 ? 1.2043 1.0016 0.8228 -0.0699 -0.0008 -0.2912 469 ARG B CD  
7887 N NE  . ARG B 442 ? 1.2405 1.0864 0.8716 -0.0620 -0.0162 -0.3109 469 ARG B NE  
7888 C CZ  . ARG B 442 ? 1.3707 1.2327 1.0090 -0.0707 -0.0303 -0.3397 469 ARG B CZ  
7889 N NH1 . ARG B 442 ? 1.3601 1.1914 0.9941 -0.0892 -0.0299 -0.3529 469 ARG B NH1 
7890 N NH2 . ARG B 442 ? 1.3808 1.2903 1.0315 -0.0600 -0.0461 -0.3567 469 ARG B NH2 
7891 N N   . LYS B 443 ? 1.3391 1.0928 0.9856 -0.1326 0.0378  -0.2498 470 LYS B N   
7892 C CA  . LYS B 443 ? 1.2572 1.0284 0.9272 -0.1656 0.0416  -0.2640 470 LYS B CA  
7893 C C   . LYS B 443 ? 1.3234 1.1040 1.0007 -0.1730 0.0295  -0.2935 470 LYS B C   
7894 O O   . LYS B 443 ? 1.3847 1.1238 1.0472 -0.1803 0.0291  -0.2996 470 LYS B O   
7895 C CB  . LYS B 443 ? 1.3459 1.0729 1.0069 -0.1893 0.0563  -0.2495 470 LYS B CB  
7896 C CG  . LYS B 443 ? 1.3250 1.0694 1.0097 -0.2255 0.0653  -0.2602 470 LYS B CG  
7897 C CD  . LYS B 443 ? 1.4907 1.1824 1.1582 -0.2474 0.0808  -0.2431 470 LYS B CD  
7898 C CE  . LYS B 443 ? 1.4610 1.1691 1.1509 -0.2853 0.0939  -0.2520 470 LYS B CE  
7899 N NZ  . LYS B 443 ? 1.6025 1.2527 1.2695 -0.3067 0.1100  -0.2335 470 LYS B NZ  
7900 N N   . ARG B 444 ? 1.3703 1.2052 1.0708 -0.1698 0.0183  -0.3130 471 ARG B N   
7901 C CA  . ARG B 444 ? 1.3388 1.1907 1.0496 -0.1757 0.0035  -0.3443 471 ARG B CA  
7902 C C   . ARG B 444 ? 1.2644 1.1068 0.9965 -0.2160 0.0113  -0.3589 471 ARG B C   
7903 O O   . ARG B 444 ? 1.3595 1.2294 1.1200 -0.2396 0.0216  -0.3595 471 ARG B O   
7904 C CB  . ARG B 444 ? 1.1734 1.0892 0.9066 -0.1617 -0.0113 -0.3610 471 ARG B CB  
7905 C CG  . ARG B 444 ? 1.4068 1.3485 1.1539 -0.1663 -0.0301 -0.3962 471 ARG B CG  
7906 C CD  . ARG B 444 ? 1.4464 1.4514 1.2139 -0.1479 -0.0466 -0.4111 471 ARG B CD  
7907 N NE  . ARG B 444 ? 1.5983 1.6347 1.3841 -0.1533 -0.0668 -0.4476 471 ARG B NE  
7908 C CZ  . ARG B 444 ? 1.5932 1.6842 1.3956 -0.1357 -0.0866 -0.4667 471 ARG B CZ  
7909 N NH1 . ARG B 444 ? 1.4939 1.6118 1.2962 -0.1112 -0.0882 -0.4524 471 ARG B NH1 
7910 N NH2 . ARG B 444 ? 1.7334 1.8519 1.5534 -0.1421 -0.1064 -0.5020 471 ARG B NH2 
7911 N N   . MET B 445 ? 1.3261 1.1277 1.0440 -0.2244 0.0080  -0.3707 472 MET B N   
7912 C CA  . MET B 445 ? 1.3697 1.1535 1.1057 -0.2637 0.0161  -0.3849 472 MET B CA  
7913 C C   . MET B 445 ? 1.5679 1.3916 1.3347 -0.2776 0.0004  -0.4240 472 MET B C   
7914 O O   . MET B 445 ? 1.5868 1.4152 1.3829 -0.3145 0.0083  -0.4392 472 MET B O   
7915 C CB  . MET B 445 ? 1.4999 1.2084 1.2035 -0.2674 0.0229  -0.3748 472 MET B CB  
7916 C CG  . MET B 445 ? 1.5954 1.2632 1.2691 -0.2516 0.0356  -0.3382 472 MET B CG  
7917 S SD  . MET B 445 ? 1.7574 1.4303 1.4442 -0.2764 0.0572  -0.3142 472 MET B SD  
7918 C CE  . MET B 445 ? 1.4351 1.0533 1.1216 -0.3186 0.0710  -0.3196 472 MET B CE  
7919 N N   . GLN B 446 ? 1.5086 1.3606 1.2690 -0.2492 -0.0213 -0.4410 473 GLN B N   
7920 C CA  . GLN B 446 ? 1.6237 1.5187 1.4121 -0.2571 -0.0408 -0.4803 473 GLN B CA  
7921 C C   . GLN B 446 ? 1.6435 1.6122 1.4615 -0.2450 -0.0504 -0.4873 473 GLN B C   
7922 O O   . GLN B 446 ? 1.6394 1.6268 1.4380 -0.2082 -0.0641 -0.4826 473 GLN B O   
7923 C CB  . GLN B 446 ? 1.7061 1.5792 1.4617 -0.2320 -0.0604 -0.4961 473 GLN B CB  
7924 C CG  . GLN B 446 ? 1.6595 1.5650 1.4400 -0.2438 -0.0819 -0.5400 473 GLN B CG  
7925 C CD  . GLN B 446 ? 1.8079 1.7878 1.6113 -0.2250 -0.1026 -0.5580 473 GLN B CD  
7926 O OE1 . GLN B 446 ? 1.8364 1.8679 1.6889 -0.2481 -0.1080 -0.5826 473 GLN B OE1 
7927 N NE2 . GLN B 446 ? 1.8415 1.8269 1.6098 -0.1826 -0.1137 -0.5458 473 GLN B NE2 
7928 N N   . VAL B 447 ? 1.7015 1.7108 1.5664 -0.2757 -0.0419 -0.4984 474 VAL B N   
7929 C CA  . VAL B 447 ? 1.7032 1.7841 1.6021 -0.2668 -0.0487 -0.5062 474 VAL B CA  
7930 C C   . VAL B 447 ? 1.7146 1.8546 1.6663 -0.2884 -0.0621 -0.5475 474 VAL B C   
7931 O O   . VAL B 447 ? 1.6785 1.8831 1.6660 -0.2835 -0.0681 -0.5584 474 VAL B O   
7932 C CB  . VAL B 447 ? 1.5534 1.6396 1.4629 -0.2784 -0.0242 -0.4791 474 VAL B CB  
7933 C CG1 . VAL B 447 ? 1.4798 1.5138 1.3413 -0.2550 -0.0139 -0.4406 474 VAL B CG1 
7934 C CG2 . VAL B 447 ? 1.5188 1.5931 1.4553 -0.3261 -0.0019 -0.4829 474 VAL B CG2 
7935 N N   . GLU B 448 ? 1.8558 1.9768 1.8159 -0.3120 -0.0675 -0.5725 475 GLU B N   
7936 C CA  . GLU B 448 ? 1.8494 2.0286 1.8658 -0.3362 -0.0800 -0.6145 475 GLU B CA  
7937 C C   . GLU B 448 ? 1.7197 1.9501 1.7390 -0.3012 -0.1152 -0.6414 475 GLU B C   
7938 O O   . GLU B 448 ? 1.6288 1.9313 1.6980 -0.3053 -0.1279 -0.6686 475 GLU B O   
7939 C CB  . GLU B 448 ? 1.8573 1.9960 1.8822 -0.3739 -0.0745 -0.6336 475 GLU B CB  
7940 C CG  . GLU B 448 ? 1.9436 2.0456 1.9805 -0.4170 -0.0396 -0.6147 475 GLU B CG  
7941 C CD  . GLU B 448 ? 2.0635 2.0969 2.0459 -0.4036 -0.0199 -0.5686 475 GLU B CD  
7942 O OE1 . GLU B 448 ? 2.0187 2.0190 1.9537 -0.3674 -0.0320 -0.5550 475 GLU B OE1 
7943 O OE2 . GLU B 448 ? 2.0751 2.0890 2.0620 -0.4290 0.0078  -0.5464 475 GLU B OE2 
7944 N N   . HIS B 449 ? 1.7876 1.9824 1.7533 -0.2658 -0.1312 -0.6346 476 HIS B N   
7945 C CA  . HIS B 449 ? 1.7634 1.9973 1.7171 -0.2260 -0.1634 -0.6527 476 HIS B CA  
7946 C C   . HIS B 449 ? 1.7371 1.9410 1.6339 -0.1825 -0.1620 -0.6166 476 HIS B C   
7947 O O   . HIS B 449 ? 1.7396 1.8815 1.5984 -0.1816 -0.1426 -0.5864 476 HIS B O   
7948 C CB  . HIS B 449 ? 1.6488 1.8719 1.5911 -0.2251 -0.1877 -0.6876 476 HIS B CB  
7949 C CG  . HIS B 449 ? 1.7592 1.9013 1.6493 -0.2241 -0.1780 -0.6726 476 HIS B CG  
7950 N ND1 . HIS B 449 ? 1.8342 1.9378 1.6617 -0.1837 -0.1823 -0.6506 476 HIS B ND1 
7951 C CD2 . HIS B 449 ? 1.7799 1.8717 1.6718 -0.2580 -0.1636 -0.6771 476 HIS B CD2 
7952 C CE1 . HIS B 449 ? 1.8430 1.8798 1.6384 -0.1918 -0.1714 -0.6433 476 HIS B CE1 
7953 N NE2 . HIS B 449 ? 1.7941 1.8205 1.6262 -0.2358 -0.1608 -0.6588 476 HIS B NE2 
7954 N N   . PRO B 450 ? 1.6395 1.8859 1.5307 -0.1460 -0.1818 -0.6191 477 PRO B N   
7955 C CA  . PRO B 450 ? 1.5225 1.7413 1.3636 -0.1071 -0.1774 -0.5835 477 PRO B CA  
7956 C C   . PRO B 450 ? 1.6345 1.7931 1.4141 -0.0860 -0.1806 -0.5741 477 PRO B C   
7957 O O   . PRO B 450 ? 1.7177 1.8737 1.4848 -0.0822 -0.2003 -0.6018 477 PRO B O   
7958 C CB  . PRO B 450 ? 1.3070 1.5854 1.1577 -0.0742 -0.2021 -0.5957 477 PRO B CB  
7959 C CG  . PRO B 450 ? 1.3458 1.6727 1.2341 -0.0865 -0.2278 -0.6421 477 PRO B CG  
7960 C CD  . PRO B 450 ? 1.4501 1.7717 1.3822 -0.1384 -0.2089 -0.6544 477 PRO B CD  
7961 N N   . GLU B 451 ? 1.7368 1.8487 1.4794 -0.0723 -0.1607 -0.5361 478 GLU B N   
7962 C CA  . GLU B 451 ? 1.7603 1.8173 1.4452 -0.0496 -0.1601 -0.5241 478 GLU B CA  
7963 C C   . GLU B 451 ? 1.6440 1.7179 1.2927 -0.0067 -0.1836 -0.5309 478 GLU B C   
7964 O O   . GLU B 451 ? 1.7018 1.8152 1.3589 0.0134  -0.1928 -0.5268 478 GLU B O   
7965 C CB  . GLU B 451 ? 1.7772 1.7873 1.4387 -0.0456 -0.1329 -0.4826 478 GLU B CB  
7966 C CG  . GLU B 451 ? 1.7753 1.7627 1.4641 -0.0846 -0.1100 -0.4728 478 GLU B CG  
7967 C CD  . GLU B 451 ? 1.7107 1.6553 1.3772 -0.0782 -0.0866 -0.4337 478 GLU B CD  
7968 O OE1 . GLU B 451 ? 1.6620 1.6045 1.3028 -0.0468 -0.0860 -0.4137 478 GLU B OE1 
7969 O OE2 . GLU B 451 ? 1.6224 1.5347 1.2971 -0.1045 -0.0690 -0.4232 478 GLU B OE2 
7970 N N   . LYS B 452 ? 1.6041 1.6454 1.2096 0.0083  -0.1930 -0.5413 479 LYS B N   
7971 C CA  . LYS B 452 ? 1.5477 1.6025 1.1132 0.0476  -0.2174 -0.5525 479 LYS B CA  
7972 C C   . LYS B 452 ? 1.5577 1.6007 1.0871 0.0825  -0.2077 -0.5163 479 LYS B C   
7973 O O   . LYS B 452 ? 1.6582 1.6546 1.1600 0.0872  -0.1843 -0.4863 479 LYS B O   
7974 C CB  . LYS B 452 ? 1.5962 1.6122 1.1188 0.0549  -0.2253 -0.5696 479 LYS B CB  
7975 C CG  . LYS B 452 ? 1.5956 1.6240 1.0791 0.0918  -0.2491 -0.5778 479 LYS B CG  
7976 C CD  . LYS B 452 ? 1.6244 1.6181 1.0790 0.0910  -0.2540 -0.5924 479 LYS B CD  
7977 C CE  . LYS B 452 ? 1.6850 1.6907 1.1030 0.1259  -0.2747 -0.5951 479 LYS B CE  
7978 N NZ  . LYS B 452 ? 1.7059 1.6822 1.0983 0.1239  -0.2805 -0.6128 479 LYS B NZ  
7979 N N   . ALA B 453 ? 1.5554 1.6402 1.0863 0.1072  -0.2260 -0.5200 480 ALA B N   
7980 C CA  . ALA B 453 ? 1.4305 1.5039 0.9286 0.1401  -0.2178 -0.4868 480 ALA B CA  
7981 C C   . ALA B 453 ? 1.5657 1.5964 0.9928 0.1730  -0.2184 -0.4769 480 ALA B C   
7982 O O   . ALA B 453 ? 1.5684 1.5960 0.9710 0.1808  -0.2362 -0.5005 480 ALA B O   
7983 C CB  . ALA B 453 ? 1.2979 1.4249 0.8151 0.1594  -0.2391 -0.4952 480 ALA B CB  
7984 N N   . VAL B 454 ? 1.4539 1.4518 0.8509 0.1907  -0.1968 -0.4400 481 VAL B N   
7985 C CA  . VAL B 454 ? 1.5584 1.5149 0.8878 0.2221  -0.1913 -0.4255 481 VAL B CA  
7986 C C   . VAL B 454 ? 1.6277 1.6025 0.9253 0.2601  -0.2096 -0.4214 481 VAL B C   
7987 O O   . VAL B 454 ? 1.6056 1.5900 0.9124 0.2704  -0.2036 -0.4001 481 VAL B O   
7988 C CB  . VAL B 454 ? 1.4884 1.4010 0.8060 0.2202  -0.1568 -0.3880 481 VAL B CB  
7989 C CG1 . VAL B 454 ? 1.5006 1.3740 0.7502 0.2526  -0.1485 -0.3732 481 VAL B CG1 
7990 C CG2 . VAL B 454 ? 1.4326 1.3255 0.7805 0.1850  -0.1410 -0.3914 481 VAL B CG2 
7991 N N   . PRO B 455 ? 1.6046 1.5830 0.8771 0.2774  -0.2282 -0.4326 482 PRO B N   
7992 C CA  . PRO B 455 ? 1.6473 1.6417 0.8956 0.3126  -0.2453 -0.4241 482 PRO B CA  
7993 C C   . PRO B 455 ? 1.7302 1.6839 0.9281 0.3401  -0.2233 -0.3849 482 PRO B C   
7994 O O   . PRO B 455 ? 1.8059 1.7163 0.9735 0.3390  -0.1983 -0.3672 482 PRO B O   
7995 C CB  . PRO B 455 ? 1.5669 1.5651 0.7940 0.3226  -0.2665 -0.4451 482 PRO B CB  
7996 C CG  . PRO B 455 ? 1.6378 1.6366 0.8954 0.2872  -0.2659 -0.4717 482 PRO B CG  
7997 C CD  . PRO B 455 ? 1.5274 1.4948 0.7920 0.2662  -0.2356 -0.4552 482 PRO B CD  
7998 N N   . ARG B 456 ? 1.6936 1.6621 0.8854 0.3646  -0.2324 -0.3722 483 ARG B N   
7999 C CA  . ARG B 456 ? 1.6912 1.6279 0.8413 0.3925  -0.2159 -0.3361 483 ARG B CA  
8000 C C   . ARG B 456 ? 1.6846 1.5981 0.8454 0.3777  -0.1849 -0.3133 483 ARG B C   
8001 O O   . ARG B 456 ? 1.5690 1.4562 0.7015 0.3971  -0.1687 -0.2834 483 ARG B O   
8002 C CB  . ARG B 456 ? 1.7889 1.6839 0.8751 0.4175  -0.2069 -0.3182 483 ARG B CB  
8003 C CG  . ARG B 456 ? 1.6498 1.5611 0.7127 0.4414  -0.2367 -0.3343 483 ARG B CG  
8004 C CD  . ARG B 456 ? 1.8614 1.7327 0.8676 0.4554  -0.2252 -0.3246 483 ARG B CD  
8005 N NE  . ARG B 456 ? 2.1320 1.9917 1.1496 0.4277  -0.2124 -0.3381 483 ARG B NE  
8006 C CZ  . ARG B 456 ? 2.0943 1.9771 1.1350 0.4109  -0.2321 -0.3721 483 ARG B CZ  
8007 N NH1 . ARG B 456 ? 1.8607 1.7838 0.9193 0.4175  -0.2657 -0.3974 483 ARG B NH1 
8008 N NH2 . ARG B 456 ? 2.1296 1.9944 1.1775 0.3869  -0.2176 -0.3816 483 ARG B NH2 
8009 N N   . VAL B 457 ? 1.6808 1.6015 0.8853 0.3429  -0.1746 -0.3242 484 VAL B N   
8010 C CA  . VAL B 457 ? 1.5280 1.4328 0.7666 0.3216  -0.1443 -0.2974 484 VAL B CA  
8011 C C   . VAL B 457 ? 1.5095 1.4585 0.8164 0.2974  -0.1527 -0.3091 484 VAL B C   
8012 O O   . VAL B 457 ? 1.4538 1.4292 0.7976 0.2718  -0.1636 -0.3359 484 VAL B O   
8013 C CB  . VAL B 457 ? 1.6710 1.5435 0.9098 0.2998  -0.1209 -0.2929 484 VAL B CB  
8014 C CG1 . VAL B 457 ? 1.5758 1.4319 0.8456 0.2826  -0.0916 -0.2643 484 VAL B CG1 
8015 C CG2 . VAL B 457 ? 1.4642 1.2984 0.6357 0.3242  -0.1140 -0.2874 484 VAL B CG2 
8016 N N   . ARG B 458 ? 1.4096 1.3654 0.7329 0.3049  -0.1465 -0.2896 485 ARG B N   
8017 C CA  . ARG B 458 ? 1.2601 1.2594 0.6447 0.2860  -0.1538 -0.3004 485 ARG B CA  
8018 C C   . ARG B 458 ? 1.3061 1.2986 0.7330 0.2493  -0.1301 -0.2922 485 ARG B C   
8019 O O   . ARG B 458 ? 1.3029 1.2562 0.7149 0.2454  -0.1057 -0.2683 485 ARG B O   
8020 C CB  . ARG B 458 ? 1.3593 1.3656 0.7432 0.3100  -0.1563 -0.2836 485 ARG B CB  
8021 C CG  . ARG B 458 ? 1.4707 1.5316 0.9081 0.3033  -0.1740 -0.3032 485 ARG B CG  
8022 C CD  . ARG B 458 ? 1.6328 1.6945 1.0551 0.3368  -0.1818 -0.2890 485 ARG B CD  
8023 N NE  . ARG B 458 ? 1.7992 1.8289 1.1533 0.3733  -0.1901 -0.2788 485 ARG B NE  
8024 C CZ  . ARG B 458 ? 1.8764 1.8908 1.1986 0.4076  -0.1953 -0.2615 485 ARG B CZ  
8025 N NH1 . ARG B 458 ? 1.8413 1.8700 1.1954 0.4117  -0.1943 -0.2538 485 ARG B NH1 
8026 N NH2 . ARG B 458 ? 1.7506 1.7320 1.0048 0.4394  -0.2009 -0.2515 485 ARG B NH2 
8027 N N   . ASN B 459 ? 1.2359 1.2678 0.7158 0.2226  -0.1376 -0.3128 486 ASN B N   
8028 C CA  . ASN B 459 ? 1.2239 1.2535 0.7445 0.1879  -0.1176 -0.3063 486 ASN B CA  
8029 C C   . ASN B 459 ? 1.3044 1.2972 0.8110 0.1696  -0.1034 -0.3039 486 ASN B C   
8030 O O   . ASN B 459 ? 1.2490 1.2227 0.7723 0.1495  -0.0828 -0.2884 486 ASN B O   
8031 C CB  . ASN B 459 ? 1.1662 1.1832 0.6957 0.1918  -0.0987 -0.2774 486 ASN B CB  
8032 C CG  . ASN B 459 ? 1.1970 1.2496 0.7463 0.2072  -0.1115 -0.2808 486 ASN B CG  
8033 O OD1 . ASN B 459 ? 1.1232 1.2205 0.7135 0.1936  -0.1232 -0.3026 486 ASN B OD1 
8034 N ND2 . ASN B 459 ? 1.2006 1.2327 0.7215 0.2361  -0.1083 -0.2597 486 ASN B ND2 
8035 N N   . LEU B 460 ? 1.3814 1.3635 0.8568 0.1778  -0.1151 -0.3200 487 LEU B N   
8036 C CA  . LEU B 460 ? 1.3172 1.2636 0.7777 0.1633  -0.1036 -0.3211 487 LEU B CA  
8037 C C   . LEU B 460 ? 1.2559 1.2201 0.7251 0.1492  -0.1232 -0.3563 487 LEU B C   
8038 O O   . LEU B 460 ? 1.3469 1.3382 0.8062 0.1655  -0.1474 -0.3776 487 LEU B O   
8039 C CB  . LEU B 460 ? 1.3393 1.2433 0.7442 0.1902  -0.0931 -0.3030 487 LEU B CB  
8040 C CG  . LEU B 460 ? 1.4777 1.3412 0.8693 0.1782  -0.0758 -0.2982 487 LEU B CG  
8041 C CD1 . LEU B 460 ? 1.2482 1.0991 0.6728 0.1563  -0.0536 -0.2775 487 LEU B CD1 
8042 C CD2 . LEU B 460 ? 1.4702 1.2990 0.8059 0.2072  -0.0668 -0.2853 487 LEU B CD2 
8043 N N   . VAL B 461 ? 1.2973 1.2450 0.7852 0.1192  -0.1134 -0.3630 488 VAL B N   
8044 C CA  . VAL B 461 ? 1.3964 1.3552 0.8970 0.1002  -0.1288 -0.3966 488 VAL B CA  
8045 C C   . VAL B 461 ? 1.3843 1.2938 0.8638 0.0896  -0.1157 -0.3948 488 VAL B C   
8046 O O   . VAL B 461 ? 1.4171 1.2912 0.8853 0.0905  -0.0938 -0.3682 488 VAL B O   
8047 C CB  . VAL B 461 ? 1.2882 1.2853 0.8481 0.0660  -0.1315 -0.4126 488 VAL B CB  
8048 C CG1 . VAL B 461 ? 1.2380 1.2876 0.8225 0.0778  -0.1453 -0.4177 488 VAL B CG1 
8049 C CG2 . VAL B 461 ? 1.1212 1.0941 0.7024 0.0398  -0.1056 -0.3905 488 VAL B CG2 
8050 N N   . GLU B 462 ? 1.4701 1.3786 0.9464 0.0799  -0.1304 -0.4252 489 GLU B N   
8051 C CA  . GLU B 462 ? 1.4814 1.3432 0.9418 0.0678  -0.1199 -0.4281 489 GLU B CA  
8052 C C   . GLU B 462 ? 1.4894 1.3391 0.9897 0.0309  -0.1034 -0.4209 489 GLU B C   
8053 O O   . GLU B 462 ? 1.5486 1.4310 1.0919 0.0055  -0.1083 -0.4336 489 GLU B O   
8054 C CB  . GLU B 462 ? 1.6698 1.5336 1.1168 0.0672  -0.1416 -0.4655 489 GLU B CB  
8055 C CG  . GLU B 462 ? 1.8033 1.6778 1.2044 0.1051  -0.1603 -0.4747 489 GLU B CG  
8056 C CD  . GLU B 462 ? 1.8842 1.7605 1.2708 0.1046  -0.1836 -0.5142 489 GLU B CD  
8057 O OE1 . GLU B 462 ? 1.9691 1.8362 1.3839 0.0730  -0.1839 -0.5345 489 GLU B OE1 
8058 O OE2 . GLU B 462 ? 1.8806 1.7659 1.2294 0.1344  -0.2002 -0.5220 489 GLU B OE2 
8059 N N   . ALA B 463 ? 1.6134 1.4158 1.0983 0.0289  -0.0834 -0.4006 490 ALA B N   
8060 C CA  . ALA B 463 ? 1.6012 1.3855 1.1154 -0.0012 -0.0667 -0.3879 490 ALA B CA  
8061 C C   . ALA B 463 ? 1.6369 1.4023 1.1635 -0.0299 -0.0711 -0.4130 490 ALA B C   
8062 O O   . ALA B 463 ? 1.5481 1.2781 1.0472 -0.0232 -0.0734 -0.4242 490 ALA B O   
8063 C CB  . ALA B 463 ? 1.4704 1.2131 0.9645 0.0105  -0.0458 -0.3569 490 ALA B CB  
8064 N N   . ASP B 464 ? 1.5992 1.3870 1.1671 -0.0622 -0.0710 -0.4222 491 ASP B N   
8065 C CA  . ASP B 464 ? 1.6783 1.4428 1.2626 -0.0952 -0.0700 -0.4413 491 ASP B CA  
8066 C C   . ASP B 464 ? 1.5269 1.2474 1.1133 -0.1125 -0.0471 -0.4144 491 ASP B C   
8067 O O   . ASP B 464 ? 1.5316 1.2357 1.1013 -0.0942 -0.0351 -0.3851 491 ASP B O   
8068 C CB  . ASP B 464 ? 1.7499 1.5645 1.3784 -0.1215 -0.0817 -0.4684 491 ASP B CB  
8069 C CG  . ASP B 464 ? 1.7134 1.5669 1.3377 -0.1036 -0.1083 -0.4998 491 ASP B CG  
8070 O OD1 . ASP B 464 ? 1.6554 1.4969 1.2380 -0.0694 -0.1163 -0.4970 491 ASP B OD1 
8071 O OD2 . ASP B 464 ? 1.6988 1.5956 1.3614 -0.1236 -0.1211 -0.5276 491 ASP B OD2 
8072 N N   . TYR B 465 ? 1.4270 1.1270 1.0335 -0.1474 -0.0411 -0.4239 492 TYR B N   
8073 C CA  . TYR B 465 ? 1.5228 1.1737 1.1245 -0.1622 -0.0212 -0.3991 492 TYR B CA  
8074 C C   . TYR B 465 ? 1.4746 1.1465 1.0892 -0.1621 -0.0085 -0.3701 492 TYR B C   
8075 O O   . TYR B 465 ? 1.4294 1.1473 1.0749 -0.1773 -0.0089 -0.3752 492 TYR B O   
8076 C CB  . TYR B 465 ? 1.4758 1.1022 1.0971 -0.2020 -0.0167 -0.4151 492 TYR B CB  
8077 C CG  . TYR B 465 ? 1.5866 1.1510 1.1942 -0.2147 0.0017  -0.3909 492 TYR B CG  
8078 C CD1 . TYR B 465 ? 1.5605 1.0739 1.1331 -0.1912 0.0048  -0.3771 492 TYR B CD1 
8079 C CD2 . TYR B 465 ? 1.6720 1.2288 1.3005 -0.2491 0.0161  -0.3822 492 TYR B CD2 
8080 C CE1 . TYR B 465 ? 1.6356 1.0925 1.1953 -0.1996 0.0192  -0.3554 492 TYR B CE1 
8081 C CE2 . TYR B 465 ? 1.7315 1.2281 1.3421 -0.2584 0.0316  -0.3588 492 TYR B CE2 
8082 C CZ  . TYR B 465 ? 1.6794 1.1263 1.2560 -0.2327 0.0317  -0.3457 492 TYR B CZ  
8083 O OH  . TYR B 465 ? 1.6306 1.0178 1.1890 -0.2388 0.0446  -0.3229 492 TYR B OH  
8084 N N   . SER B 466 ? 1.5329 1.1726 1.1250 -0.1442 0.0025  -0.3414 493 SER B N   
8085 C CA  . SER B 466 ? 1.4633 1.1178 1.0631 -0.1404 0.0135  -0.3138 493 SER B CA  
8086 C C   . SER B 466 ? 1.5653 1.1672 1.1527 -0.1490 0.0282  -0.2907 493 SER B C   
8087 O O   . SER B 466 ? 1.5688 1.1215 1.1371 -0.1484 0.0294  -0.2928 493 SER B O   
8088 C CB  . SER B 466 ? 1.4106 1.0863 0.9969 -0.1046 0.0099  -0.3014 493 SER B CB  
8089 O OG  . SER B 466 ? 1.2333 0.9487 0.8222 -0.0922 -0.0055 -0.3227 493 SER B OG  
8090 N N   . TYR B 467 ? 1.6201 1.2317 1.2168 -0.1551 0.0385  -0.2690 494 TYR B N   
8091 C CA  . TYR B 467 ? 1.7352 1.3001 1.3212 -0.1678 0.0510  -0.2487 494 TYR B CA  
8092 C C   . TYR B 467 ? 1.6827 1.2439 1.2600 -0.1482 0.0571  -0.2203 494 TYR B C   
8093 O O   . TYR B 467 ? 1.9565 1.4816 1.5231 -0.1558 0.0656  -0.2022 494 TYR B O   
8094 C CB  . TYR B 467 ? 1.7568 1.3268 1.3611 -0.2052 0.0597  -0.2524 494 TYR B CB  
8095 C CG  . TYR B 467 ? 1.8418 1.3490 1.4285 -0.2238 0.0705  -0.2405 494 TYR B CG  
8096 C CD1 . TYR B 467 ? 1.8491 1.3137 1.4268 -0.2347 0.0682  -0.2557 494 TYR B CD1 
8097 C CD2 . TYR B 467 ? 1.9807 1.4687 1.5576 -0.2294 0.0822  -0.2144 494 TYR B CD2 
8098 C CE1 . TYR B 467 ? 2.0815 1.4831 1.6409 -0.2505 0.0780  -0.2438 494 TYR B CE1 
8099 C CE2 . TYR B 467 ? 2.1732 1.5996 1.7290 -0.2441 0.0913  -0.2018 494 TYR B CE2 
8100 C CZ  . TYR B 467 ? 2.3053 1.6873 1.8527 -0.2546 0.0895  -0.2158 494 TYR B CZ  
8101 O OH  . TYR B 467 ? 2.4344 1.7497 1.9587 -0.2682 0.0986  -0.2023 494 TYR B OH  
8102 N N   . TRP B 468 ? 1.2517 0.8469 0.8323 -0.1231 0.0527  -0.2159 495 TRP B N   
8103 C CA  . TRP B 468 ? 1.3094 0.9027 0.8859 -0.1055 0.0579  -0.1916 495 TRP B CA  
8104 C C   . TRP B 468 ? 1.2736 0.8666 0.8394 -0.0732 0.0545  -0.1886 495 TRP B C   
8105 O O   . TRP B 468 ? 1.5199 1.1211 1.0797 -0.0630 0.0478  -0.2047 495 TRP B O   
8106 C CB  . TRP B 468 ? 1.4085 1.0465 1.0046 -0.1109 0.0603  -0.1853 495 TRP B CB  
8107 C CG  . TRP B 468 ? 1.3285 0.9643 0.9320 -0.1406 0.0683  -0.1822 495 TRP B CG  
8108 C CD1 . TRP B 468 ? 1.2655 0.8553 0.8545 -0.1578 0.0755  -0.1739 495 TRP B CD1 
8109 C CD2 . TRP B 468 ? 1.4064 1.0865 1.0316 -0.1558 0.0714  -0.1870 495 TRP B CD2 
8110 N NE1 . TRP B 468 ? 1.3400 0.9420 0.9381 -0.1841 0.0843  -0.1721 495 TRP B NE1 
8111 C CE2 . TRP B 468 ? 1.3812 1.0405 1.0032 -0.1834 0.0823  -0.1810 495 TRP B CE2 
8112 C CE3 . TRP B 468 ? 1.2749 1.0088 0.9209 -0.1477 0.0665  -0.1956 495 TRP B CE3 
8113 C CZ2 . TRP B 468 ? 1.3299 1.0238 0.9701 -0.2040 0.0901  -0.1843 495 TRP B CZ2 
8114 C CZ3 . TRP B 468 ? 1.1887 0.9573 0.8549 -0.1667 0.0723  -0.2000 495 TRP B CZ3 
8115 C CH2 . TRP B 468 ? 1.3710 1.1212 1.0349 -0.1950 0.0848  -0.1947 495 TRP B CH2 
8116 N N   . THR B 469 ? 1.2798 0.8637 0.8431 -0.0574 0.0595  -0.1683 496 THR B N   
8117 C CA  . THR B 469 ? 1.3330 0.9195 0.8909 -0.0283 0.0604  -0.1620 496 THR B CA  
8118 C C   . THR B 469 ? 1.2430 0.8560 0.8154 -0.0189 0.0639  -0.1455 496 THR B C   
8119 O O   . THR B 469 ? 1.2046 0.8076 0.7773 -0.0018 0.0683  -0.1323 496 THR B O   
8120 C CB  . THR B 469 ? 1.1947 0.7365 0.7374 -0.0162 0.0636  -0.1565 496 THR B CB  
8121 O OG1 . THR B 469 ? 1.3033 0.8189 0.8462 -0.0261 0.0664  -0.1420 496 THR B OG1 
8122 C CG2 . THR B 469 ? 1.2361 0.7520 0.7628 -0.0205 0.0596  -0.1757 496 THR B CG2 
8123 N N   . LEU B 470 ? 1.1825 0.8311 0.7697 -0.0299 0.0621  -0.1479 497 LEU B N   
8124 C CA  . LEU B 470 ? 1.1733 0.8456 0.7748 -0.0231 0.0650  -0.1343 497 LEU B CA  
8125 C C   . LEU B 470 ? 1.1340 0.8173 0.7363 0.0025  0.0667  -0.1293 497 LEU B C   
8126 O O   . LEU B 470 ? 1.0048 0.6832 0.6134 0.0140  0.0716  -0.1152 497 LEU B O   
8127 C CB  . LEU B 470 ? 0.9581 0.6675 0.5750 -0.0382 0.0627  -0.1412 497 LEU B CB  
8128 C CG  . LEU B 470 ? 1.3455 1.0496 0.9642 -0.0665 0.0643  -0.1467 497 LEU B CG  
8129 C CD1 . LEU B 470 ? 1.2762 1.0247 0.9136 -0.0780 0.0622  -0.1593 497 LEU B CD1 
8130 C CD2 . LEU B 470 ? 1.2818 0.9641 0.8958 -0.0736 0.0701  -0.1295 497 LEU B CD2 
8131 N N   . ALA B 471 ? 1.0610 0.7590 0.6564 0.0116  0.0630  -0.1410 498 ALA B N   
8132 C CA  . ALA B 471 ? 1.0389 0.7449 0.6299 0.0354  0.0665  -0.1354 498 ALA B CA  
8133 C C   . ALA B 471 ? 1.0282 0.7324 0.5983 0.0453  0.0616  -0.1501 498 ALA B C   
8134 O O   . ALA B 471 ? 1.1901 0.9099 0.7594 0.0352  0.0519  -0.1662 498 ALA B O   
8135 C CB  . ALA B 471 ? 1.0671 0.8054 0.6739 0.0392  0.0662  -0.1298 498 ALA B CB  
8136 N N   . TYR B 472 ? 0.9909 0.6777 0.5447 0.0650  0.0683  -0.1458 499 TYR B N   
8137 C CA  . TYR B 472 ? 1.0803 0.7626 0.6081 0.0771  0.0641  -0.1596 499 TYR B CA  
8138 C C   . TYR B 472 ? 1.1375 0.8131 0.6501 0.1022  0.0755  -0.1488 499 TYR B C   
8139 O O   . TYR B 472 ? 1.1024 0.7690 0.6264 0.1080  0.0878  -0.1333 499 TYR B O   
8140 C CB  . TYR B 472 ? 1.0307 0.6846 0.5458 0.0686  0.0607  -0.1733 499 TYR B CB  
8141 C CG  . TYR B 472 ? 1.0915 0.7128 0.6062 0.0732  0.0711  -0.1631 499 TYR B CG  
8142 C CD1 . TYR B 472 ? 1.1158 0.7209 0.6132 0.0949  0.0804  -0.1610 499 TYR B CD1 
8143 C CD2 . TYR B 472 ? 1.1199 0.7267 0.6503 0.0571  0.0716  -0.1562 499 TYR B CD2 
8144 C CE1 . TYR B 472 ? 1.2026 0.7817 0.7038 0.1007  0.0892  -0.1536 499 TYR B CE1 
8145 C CE2 . TYR B 472 ? 1.1378 0.7154 0.6682 0.0640  0.0786  -0.1476 499 TYR B CE2 
8146 C CZ  . TYR B 472 ? 1.2139 0.7796 0.7322 0.0860  0.0870  -0.1472 499 TYR B CZ  
8147 O OH  . TYR B 472 ? 1.1953 0.7356 0.7176 0.0945  0.0935  -0.1405 499 TYR B OH  
8148 N N   . VAL B 473 ? 1.1897 0.8707 0.6763 0.1171  0.0714  -0.1575 500 VAL B N   
8149 C CA  . VAL B 473 ? 1.0472 0.7177 0.5104 0.1412  0.0838  -0.1488 500 VAL B CA  
8150 C C   . VAL B 473 ? 1.1375 0.7831 0.5731 0.1488  0.0849  -0.1620 500 VAL B C   
8151 O O   . VAL B 473 ? 1.1866 0.8319 0.6079 0.1434  0.0706  -0.1821 500 VAL B O   
8152 C CB  . VAL B 473 ? 1.0908 0.7799 0.5362 0.1560  0.0791  -0.1478 500 VAL B CB  
8153 C CG1 . VAL B 473 ? 1.2557 0.9303 0.6756 0.1796  0.0962  -0.1344 500 VAL B CG1 
8154 C CG2 . VAL B 473 ? 1.1537 0.8677 0.6276 0.1474  0.0751  -0.1393 500 VAL B CG2 
8155 N N   . ILE B 474 ? 1.1720 0.7980 0.6026 0.1611  0.1018  -0.1524 501 ILE B N   
8156 C CA  . ILE B 474 ? 1.2486 0.8492 0.6538 0.1705  0.1054  -0.1647 501 ILE B CA  
8157 C C   . ILE B 474 ? 1.2689 0.8641 0.6455 0.1956  0.1220  -0.1572 501 ILE B C   
8158 O O   . ILE B 474 ? 1.2391 0.8409 0.6280 0.2027  0.1378  -0.1379 501 ILE B O   
8159 C CB  . ILE B 474 ? 1.1325 0.7117 0.5587 0.1623  0.1111  -0.1627 501 ILE B CB  
8160 C CG1 . ILE B 474 ? 1.2238 0.7748 0.6237 0.1717  0.1126  -0.1789 501 ILE B CG1 
8161 C CG2 . ILE B 474 ? 1.1532 0.7358 0.6047 0.1689  0.1284  -0.1418 501 ILE B CG2 
8162 C CD1 . ILE B 474 ? 1.4003 0.9261 0.8179 0.1639  0.1139  -0.1799 501 ILE B CD1 
8163 N N   . SER B 475 ? 1.2633 0.8459 0.6004 0.2085  0.1189  -0.1730 502 SER B N   
8164 C CA  . SER B 475 ? 1.3209 0.8945 0.6231 0.2330  0.1363  -0.1672 502 SER B CA  
8165 C C   . SER B 475 ? 1.4218 0.9727 0.7236 0.2408  0.1532  -0.1691 502 SER B C   
8166 O O   . SER B 475 ? 1.4758 1.0135 0.7947 0.2298  0.1467  -0.1795 502 SER B O   
8167 C CB  . SER B 475 ? 1.3417 0.9148 0.5953 0.2462  0.1231  -0.1840 502 SER B CB  
8168 O OG  . SER B 475 ? 1.4842 1.0410 0.7225 0.2434  0.1119  -0.2088 502 SER B OG  
8169 N N   . LEU B 476 ? 1.3732 0.9187 0.6553 0.2606  0.1763  -0.1586 503 LEU B N   
8170 C CA  . LEU B 476 ? 1.3898 0.9170 0.6700 0.2715  0.1943  -0.1624 503 LEU B CA  
8171 C C   . LEU B 476 ? 1.4707 0.9772 0.7197 0.2755  0.1816  -0.1889 503 LEU B C   
8172 O O   . LEU B 476 ? 1.6145 1.1037 0.8764 0.2746  0.1843  -0.1979 503 LEU B O   
8173 C CB  . LEU B 476 ? 1.5419 1.0686 0.8008 0.2920  0.2230  -0.1483 503 LEU B CB  
8174 C CG  . LEU B 476 ? 1.5184 1.0314 0.7790 0.3050  0.2457  -0.1519 503 LEU B CG  
8175 C CD1 . LEU B 476 ? 1.4168 0.9353 0.7365 0.2933  0.2493  -0.1452 503 LEU B CD1 
8176 C CD2 . LEU B 476 ? 1.3994 0.9128 0.6343 0.3241  0.2763  -0.1384 503 LEU B CD2 
8177 N N   . GLN B 477 ? 1.4449 0.9523 0.6530 0.2806  0.1663  -0.2027 504 GLN B N   
8178 C CA  . GLN B 477 ? 1.4438 0.9332 0.6249 0.2814  0.1502  -0.2312 504 GLN B CA  
8179 C C   . GLN B 477 ? 1.6013 1.0855 0.8187 0.2561  0.1314  -0.2421 504 GLN B C   
8180 O O   . GLN B 477 ? 1.5851 1.0446 0.8015 0.2541  0.1288  -0.2583 504 GLN B O   
8181 C CB  . GLN B 477 ? 1.5501 1.0476 0.6854 0.2907  0.1337  -0.2444 504 GLN B CB  
8182 C CG  . GLN B 477 ? 1.6884 1.1743 0.8042 0.2866  0.1116  -0.2761 504 GLN B CG  
8183 C CD  . GLN B 477 ? 1.8786 1.3855 0.9672 0.2915  0.0903  -0.2862 504 GLN B CD  
8184 O OE1 . GLN B 477 ? 1.9862 1.5118 1.0650 0.2999  0.0915  -0.2696 504 GLN B OE1 
8185 N NE2 . GLN B 477 ? 1.9730 1.4760 1.0503 0.2866  0.0702  -0.3141 504 GLN B NE2 
8186 N N   . GLY B 478 ? 1.4670 0.9720 0.7154 0.2369  0.1194  -0.2329 505 GLY B N   
8187 C CA  . GLY B 478 ? 1.3513 0.8510 0.6312 0.2115  0.1037  -0.2413 505 GLY B CA  
8188 C C   . GLY B 478 ? 1.4656 0.9457 0.7750 0.2068  0.1151  -0.2320 505 GLY B C   
8189 O O   . GLY B 478 ? 1.5096 0.9664 0.8262 0.1948  0.1064  -0.2446 505 GLY B O   
8190 N N   . ALA B 479 ? 1.4200 0.9085 0.7472 0.2166  0.1341  -0.2102 506 ALA B N   
8191 C CA  . ALA B 479 ? 1.4037 0.8771 0.7603 0.2158  0.1436  -0.2021 506 ALA B CA  
8192 C C   . ALA B 479 ? 1.4688 0.9119 0.8051 0.2308  0.1501  -0.2181 506 ALA B C   
8193 O O   . ALA B 479 ? 1.5392 0.9591 0.8918 0.2261  0.1471  -0.2219 506 ALA B O   
8194 C CB  . ALA B 479 ? 1.4708 0.9641 0.8531 0.2240  0.1625  -0.1786 506 ALA B CB  
8195 N N   . ARG B 480 ? 1.5228 0.9638 0.8208 0.2501  0.1588  -0.2278 507 ARG B N   
8196 C CA  . ARG B 480 ? 1.5715 0.9840 0.8468 0.2659  0.1653  -0.2458 507 ARG B CA  
8197 C C   . ARG B 480 ? 1.5831 0.9685 0.8473 0.2526  0.1437  -0.2699 507 ARG B C   
8198 O O   . ARG B 480 ? 1.5640 0.9190 0.8318 0.2558  0.1445  -0.2803 507 ARG B O   
8199 C CB  . ARG B 480 ? 1.4745 0.8910 0.7051 0.2893  0.1793  -0.2514 507 ARG B CB  
8200 C CG  . ARG B 480 ? 1.5450 0.9802 0.7846 0.3043  0.2070  -0.2291 507 ARG B CG  
8201 C CD  . ARG B 480 ? 1.6782 1.1089 0.8765 0.3280  0.2249  -0.2361 507 ARG B CD  
8202 N NE  . ARG B 480 ? 1.7332 1.1824 0.9446 0.3391  0.2540  -0.2140 507 ARG B NE  
8203 C CZ  . ARG B 480 ? 1.7786 1.2454 0.9713 0.3435  0.2634  -0.1982 507 ARG B CZ  
8204 N NH1 . ARG B 480 ? 1.5447 1.0158 0.7045 0.3405  0.2446  -0.2018 507 ARG B NH1 
8205 N NH2 . ARG B 480 ? 1.6582 1.1384 0.8673 0.3511  0.2920  -0.1785 507 ARG B NH2 
8206 N N   . LYS B 481 ? 1.4949 0.8906 0.7474 0.2376  0.1244  -0.2798 508 LYS B N   
8207 C CA  . LYS B 481 ? 1.4772 0.8493 0.7214 0.2221  0.1044  -0.3048 508 LYS B CA  
8208 C C   . LYS B 481 ? 1.5547 0.9063 0.8346 0.2015  0.0991  -0.2988 508 LYS B C   
8209 O O   . LYS B 481 ? 1.7018 1.0164 0.9771 0.1983  0.0944  -0.3145 508 LYS B O   
8210 C CB  . LYS B 481 ? 1.5502 0.9459 0.7832 0.2092  0.0849  -0.3160 508 LYS B CB  
8211 C CG  . LYS B 481 ? 1.4968 0.9065 0.6856 0.2309  0.0851  -0.3258 508 LYS B CG  
8212 C CD  . LYS B 481 ? 1.5002 0.9310 0.6804 0.2183  0.0607  -0.3426 508 LYS B CD  
8213 C CE  . LYS B 481 ? 1.5752 1.0176 0.7059 0.2424  0.0576  -0.3531 508 LYS B CE  
8214 N NZ  . LYS B 481 ? 1.5872 1.0532 0.7142 0.2312  0.0302  -0.3731 508 LYS B NZ  
8215 N N   . LEU B 482 ? 1.5366 0.9091 0.8495 0.1879  0.0998  -0.2762 509 LEU B N   
8216 C CA  . LEU B 482 ? 1.4444 0.7971 0.7861 0.1689  0.0947  -0.2683 509 LEU B CA  
8217 C C   . LEU B 482 ? 1.5334 0.8551 0.8814 0.1845  0.1057  -0.2640 509 LEU B C   
8218 O O   . LEU B 482 ? 1.6116 0.8958 0.9626 0.1757  0.0991  -0.2707 509 LEU B O   
8219 C CB  . LEU B 482 ? 1.4560 0.8397 0.8281 0.1553  0.0947  -0.2449 509 LEU B CB  
8220 C CG  . LEU B 482 ? 1.3116 0.7295 0.6828 0.1412  0.0839  -0.2477 509 LEU B CG  
8221 C CD1 . LEU B 482 ? 1.2621 0.7068 0.6643 0.1293  0.0853  -0.2251 509 LEU B CD1 
8222 C CD2 . LEU B 482 ? 1.3379 0.7427 0.7021 0.1197  0.0670  -0.2705 509 LEU B CD2 
8223 N N   . LEU B 483 ? 1.5337 0.8699 0.8846 0.2080  0.1231  -0.2532 510 LEU B N   
8224 C CA  . LEU B 483 ? 1.4179 0.7305 0.7784 0.2259  0.1339  -0.2515 510 LEU B CA  
8225 C C   . LEU B 483 ? 1.6170 0.8915 0.9480 0.2368  0.1321  -0.2772 510 LEU B C   
8226 O O   . LEU B 483 ? 1.6225 0.8614 0.9601 0.2415  0.1309  -0.2815 510 LEU B O   
8227 C CB  . LEU B 483 ? 1.4221 0.7638 0.7947 0.2474  0.1550  -0.2372 510 LEU B CB  
8228 C CG  . LEU B 483 ? 1.3777 0.7547 0.7840 0.2394  0.1587  -0.2123 510 LEU B CG  
8229 C CD1 . LEU B 483 ? 1.3377 0.7397 0.7551 0.2601  0.1819  -0.2018 510 LEU B CD1 
8230 C CD2 . LEU B 483 ? 1.3743 0.7390 0.8120 0.2280  0.1492  -0.2011 510 LEU B CD2 
8231 N N   . ALA B 484 ? 1.6606 0.9402 0.9569 0.2421  0.1308  -0.2954 511 ALA B N   
8232 C CA  . ALA B 484 ? 1.6212 0.8659 0.8862 0.2535  0.1285  -0.3229 511 ALA B CA  
8233 C C   . ALA B 484 ? 1.6360 0.8412 0.9014 0.2318  0.1098  -0.3384 511 ALA B C   
8234 O O   . ALA B 484 ? 1.7147 0.8803 0.9635 0.2407  0.1085  -0.3586 511 ALA B O   
8235 C CB  . ALA B 484 ? 1.5887 0.8502 0.8135 0.2636  0.1287  -0.3390 511 ALA B CB  
8236 N N   . ALA B 485 ? 1.6574 0.8709 0.9412 0.2034  0.0967  -0.3299 512 ALA B N   
8237 C CA  . ALA B 485 ? 1.7537 0.9291 1.0396 0.1793  0.0818  -0.3427 512 ALA B CA  
8238 C C   . ALA B 485 ? 1.7544 0.8864 1.0551 0.1817  0.0847  -0.3333 512 ALA B C   
8239 O O   . ALA B 485 ? 1.6674 0.7552 0.9635 0.1662  0.0752  -0.3457 512 ALA B O   
8240 C CB  . ALA B 485 ? 1.6261 0.8261 0.9297 0.1482  0.0703  -0.3346 512 ALA B CB  
8241 N N   . GLU B 486 ? 1.7352 0.8779 1.0538 0.2009  0.0972  -0.3128 513 GLU B N   
8242 C CA  . GLU B 486 ? 1.7608 0.8685 1.0964 0.2052  0.0977  -0.3003 513 GLU B CA  
8243 C C   . GLU B 486 ? 1.7249 0.8117 1.0706 0.1740  0.0852  -0.2903 513 GLU B C   
8244 O O   . GLU B 486 ? 1.8651 0.8993 1.2017 0.1651  0.0781  -0.2990 513 GLU B O   
8245 C CB  . GLU B 486 ? 1.6893 0.7486 1.0076 0.2250  0.0997  -0.3202 513 GLU B CB  
8246 C CG  . GLU B 486 ? 2.0114 1.0395 1.3474 0.2400  0.1018  -0.3069 513 GLU B CG  
8247 C CD  . GLU B 486 ? 2.2656 1.2396 1.5836 0.2581  0.1017  -0.3285 513 GLU B CD  
8248 O OE1 . GLU B 486 ? 2.1001 1.0741 1.3976 0.2607  0.1021  -0.3524 513 GLU B OE1 
8249 O OE2 . GLU B 486 ? 2.4676 1.4056 1.7960 0.2692  0.0996  -0.3204 513 GLU B OE2 
8250 N N   . PRO B 487 ? 1.6237 0.7486 0.9868 0.1566  0.0833  -0.2722 514 PRO B N   
8251 C CA  . PRO B 487 ? 1.6445 0.7522 1.0147 0.1257  0.0738  -0.2633 514 PRO B CA  
8252 C C   . PRO B 487 ? 1.6699 0.7420 1.0497 0.1287  0.0731  -0.2439 514 PRO B C   
8253 O O   . PRO B 487 ? 1.8385 0.8835 1.2171 0.1043  0.0669  -0.2368 514 PRO B O   
8254 C CB  . PRO B 487 ? 1.6274 0.7920 1.0131 0.1121  0.0738  -0.2506 514 PRO B CB  
8255 C CG  . PRO B 487 ? 1.4447 0.6461 0.8400 0.1392  0.0847  -0.2402 514 PRO B CG  
8256 C CD  . PRO B 487 ? 1.5276 0.7106 0.9041 0.1644  0.0910  -0.2586 514 PRO B CD  
8257 N N   . LEU B 488 ? 1.5897 0.6611 0.9784 0.1581  0.0794  -0.2353 515 LEU B N   
8258 C CA  . LEU B 488 ? 1.6586 0.6983 1.0560 0.1645  0.0759  -0.2171 515 LEU B CA  
8259 C C   . LEU B 488 ? 1.8140 0.7821 1.1906 0.1613  0.0698  -0.2270 515 LEU B C   
8260 O O   . LEU B 488 ? 1.9029 0.8338 1.2761 0.1504  0.0636  -0.2121 515 LEU B O   
8261 C CB  . LEU B 488 ? 1.6825 0.7448 1.0999 0.1980  0.0833  -0.2088 515 LEU B CB  
8262 C CG  . LEU B 488 ? 1.5390 0.6685 0.9783 0.2027  0.0919  -0.1995 515 LEU B CG  
8263 C CD1 . LEU B 488 ? 1.4642 0.6124 0.9301 0.2317  0.0986  -0.1898 515 LEU B CD1 
8264 C CD2 . LEU B 488 ? 1.4375 0.5935 0.8855 0.1759  0.0863  -0.1835 515 LEU B CD2 
8265 N N   . SER B 489 ? 1.8343 0.7792 1.1941 0.1710  0.0716  -0.2522 516 SER B N   
8266 C CA  . SER B 489 ? 1.8569 0.7302 1.1963 0.1663  0.0658  -0.2647 516 SER B CA  
8267 C C   . SER B 489 ? 1.8340 0.6845 1.1632 0.1263  0.0593  -0.2685 516 SER B C   
8268 O O   . SER B 489 ? 1.8624 0.6490 1.1778 0.1155  0.0550  -0.2699 516 SER B O   
8269 C CB  . SER B 489 ? 1.7841 0.6417 1.1081 0.1872  0.0694  -0.2937 516 SER B CB  
8270 O OG  . SER B 489 ? 1.9553 0.8503 1.2715 0.1761  0.0706  -0.3123 516 SER B OG  
8271 N N   . LYS B 490 ? 1.7965 0.6969 1.1333 0.1045  0.0593  -0.2705 517 LYS B N   
8272 C CA  . LYS B 490 ? 1.8039 0.6958 1.1383 0.0653  0.0545  -0.2758 517 LYS B CA  
8273 C C   . LYS B 490 ? 1.7489 0.6889 1.1012 0.0474  0.0557  -0.2536 517 LYS B C   
8274 O O   . LYS B 490 ? 1.7147 0.6981 1.0751 0.0282  0.0544  -0.2616 517 LYS B O   
8275 C CB  . LYS B 490 ? 1.8898 0.7963 1.2160 0.0563  0.0510  -0.3080 517 LYS B CB  
8276 C CG  . LYS B 490 ? 1.8293 0.7636 1.1483 0.0897  0.0547  -0.3221 517 LYS B CG  
8277 C CD  . LYS B 490 ? 1.7678 0.7088 1.0718 0.0832  0.0489  -0.3557 517 LYS B CD  
8278 C CE  . LYS B 490 ? 1.7519 0.7170 1.0421 0.1180  0.0545  -0.3680 517 LYS B CE  
8279 N NZ  . LYS B 490 ? 2.0345 1.0119 1.3057 0.1141  0.0472  -0.4003 517 LYS B NZ  
8280 N N   . MET B 491 ? 1.7842 0.7170 1.1425 0.0557  0.0572  -0.2265 518 MET B N   
8281 C CA  . MET B 491 ? 1.6738 0.6532 1.0486 0.0449  0.0585  -0.2049 518 MET B CA  
8282 C C   . MET B 491 ? 1.6636 0.6478 1.0394 0.0052  0.0578  -0.2067 518 MET B C   
8283 O O   . MET B 491 ? 1.8033 0.7357 1.1666 -0.0162 0.0574  -0.2079 518 MET B O   
8284 C CB  . MET B 491 ? 1.8102 0.7683 1.1862 0.0591  0.0575  -0.1783 518 MET B CB  
8285 C CG  . MET B 491 ? 1.7483 0.7523 1.1398 0.0509  0.0581  -0.1566 518 MET B CG  
8286 S SD  . MET B 491 ? 1.7834 0.8684 1.2008 0.0693  0.0622  -0.1577 518 MET B SD  
8287 C CE  . MET B 491 ? 1.7181 0.7907 1.1400 0.1113  0.0642  -0.1601 518 MET B CE  
8288 N N   . LEU B 492 ? 1.5845 0.6313 0.9766 -0.0044 0.0585  -0.2075 519 LEU B N   
8289 C CA  . LEU B 492 ? 1.5833 0.6518 0.9834 -0.0392 0.0584  -0.2124 519 LEU B CA  
8290 C C   . LEU B 492 ? 1.5574 0.6871 0.9759 -0.0376 0.0603  -0.1963 519 LEU B C   
8291 O O   . LEU B 492 ? 1.5519 0.7150 0.9773 -0.0115 0.0609  -0.1925 519 LEU B O   
8292 C CB  . LEU B 492 ? 1.6523 0.7366 1.0531 -0.0491 0.0539  -0.2436 519 LEU B CB  
8293 C CG  . LEU B 492 ? 1.6484 0.7486 1.0604 -0.0868 0.0522  -0.2571 519 LEU B CG  
8294 C CD1 . LEU B 492 ? 1.8006 0.8362 1.2029 -0.1126 0.0545  -0.2610 519 LEU B CD1 
8295 C CD2 . LEU B 492 ? 1.6303 0.7694 1.0470 -0.0854 0.0445  -0.2863 519 LEU B CD2 
8296 N N   . PRO B 493 ? 1.6682 0.8121 1.0946 -0.0648 0.0625  -0.1868 520 PRO B N   
8297 C CA  . PRO B 493 ? 1.5557 0.7568 0.9994 -0.0629 0.0640  -0.1732 520 PRO B CA  
8298 C C   . PRO B 493 ? 1.4638 0.7196 0.9197 -0.0500 0.0613  -0.1876 520 PRO B C   
8299 O O   . PRO B 493 ? 1.5137 0.7782 0.9689 -0.0582 0.0575  -0.2105 520 PRO B O   
8300 C CB  . PRO B 493 ? 1.5075 0.7139 0.9566 -0.0986 0.0677  -0.1702 520 PRO B CB  
8301 C CG  . PRO B 493 ? 1.6423 0.7801 1.0721 -0.1137 0.0704  -0.1681 520 PRO B CG  
8302 C CD  . PRO B 493 ? 1.6636 0.7690 1.0831 -0.0983 0.0657  -0.1869 520 PRO B CD  
8303 N N   . VAL B 494 ? 1.3054 0.5964 0.7714 -0.0291 0.0630  -0.1741 521 VAL B N   
8304 C CA  . VAL B 494 ? 1.2729 0.6072 0.7449 -0.0116 0.0622  -0.1838 521 VAL B CA  
8305 C C   . VAL B 494 ? 1.4333 0.8073 0.9144 -0.0306 0.0580  -0.1983 521 VAL B C   
8306 O O   . VAL B 494 ? 1.5428 0.9353 1.0192 -0.0226 0.0538  -0.2162 521 VAL B O   
8307 C CB  . VAL B 494 ? 1.3930 0.7560 0.8777 0.0098  0.0665  -0.1648 521 VAL B CB  
8308 C CG1 . VAL B 494 ? 1.3889 0.7716 0.8872 -0.0055 0.0669  -0.1481 521 VAL B CG1 
8309 C CG2 . VAL B 494 ? 1.3454 0.7492 0.8334 0.0264  0.0680  -0.1723 521 VAL B CG2 
8310 N N   . ASP B 495 ? 1.4348 0.8230 0.9283 -0.0549 0.0589  -0.1916 522 ASP B N   
8311 C CA  . ASP B 495 ? 1.4947 0.9226 1.0017 -0.0740 0.0547  -0.2070 522 ASP B CA  
8312 C C   . ASP B 495 ? 1.5874 0.9954 1.0896 -0.0926 0.0497  -0.2319 522 ASP B C   
8313 O O   . ASP B 495 ? 1.6927 1.1366 1.2083 -0.1061 0.0439  -0.2498 522 ASP B O   
8314 C CB  . ASP B 495 ? 1.4377 0.8855 0.9600 -0.0954 0.0593  -0.1941 522 ASP B CB  
8315 C CG  . ASP B 495 ? 1.6971 1.0979 1.2105 -0.1172 0.0651  -0.1851 522 ASP B CG  
8316 O OD1 . ASP B 495 ? 1.9527 1.3029 1.4481 -0.1089 0.0655  -0.1817 522 ASP B OD1 
8317 O OD2 . ASP B 495 ? 1.8422 1.2550 1.3650 -0.1419 0.0701  -0.1811 522 ASP B OD2 
8318 N N   . GLU B 496 ? 1.6373 0.9898 1.1229 -0.0936 0.0510  -0.2348 523 GLU B N   
8319 C CA  . GLU B 496 ? 1.6252 0.9539 1.1047 -0.1072 0.0454  -0.2612 523 GLU B CA  
8320 C C   . GLU B 496 ? 1.5841 0.8969 1.0444 -0.0798 0.0405  -0.2751 523 GLU B C   
8321 O O   . GLU B 496 ? 1.5022 0.8158 0.9582 -0.0848 0.0323  -0.3021 523 GLU B O   
8322 C CB  . GLU B 496 ? 1.6690 0.9393 1.1417 -0.1312 0.0510  -0.2572 523 GLU B CB  
8323 C CG  . GLU B 496 ? 1.6904 0.9712 1.1786 -0.1638 0.0581  -0.2475 523 GLU B CG  
8324 C CD  . GLU B 496 ? 1.6787 0.8961 1.1559 -0.1888 0.0652  -0.2440 523 GLU B CD  
8325 O OE1 . GLU B 496 ? 1.9345 1.1064 1.3985 -0.1877 0.0618  -0.2586 523 GLU B OE1 
8326 O OE2 . GLU B 496 ? 1.6931 0.9037 1.1725 -0.2092 0.0747  -0.2263 523 GLU B OE2 
8327 N N   . PHE B 497 ? 1.5216 0.8217 0.9708 -0.0509 0.0454  -0.2588 524 PHE B N   
8328 C CA  . PHE B 497 ? 1.4510 0.7385 0.8814 -0.0232 0.0439  -0.2711 524 PHE B CA  
8329 C C   . PHE B 497 ? 1.4863 0.8228 0.9146 -0.0109 0.0382  -0.2852 524 PHE B C   
8330 O O   . PHE B 497 ? 1.5525 0.8814 0.9630 -0.0007 0.0325  -0.3077 524 PHE B O   
8331 C CB  . PHE B 497 ? 1.3848 0.6563 0.8105 0.0040  0.0523  -0.2498 524 PHE B CB  
8332 C CG  . PHE B 497 ? 1.4127 0.6866 0.8230 0.0353  0.0547  -0.2591 524 PHE B CG  
8333 C CD1 . PHE B 497 ? 1.4893 0.7261 0.8794 0.0421  0.0521  -0.2807 524 PHE B CD1 
8334 C CD2 . PHE B 497 ? 1.4548 0.7664 0.8699 0.0573  0.0612  -0.2465 524 PHE B CD2 
8335 C CE1 . PHE B 497 ? 1.4561 0.6954 0.8292 0.0715  0.0563  -0.2896 524 PHE B CE1 
8336 C CE2 . PHE B 497 ? 1.3784 0.6915 0.7775 0.0850  0.0667  -0.2539 524 PHE B CE2 
8337 C CZ  . PHE B 497 ? 1.4938 0.7717 0.8709 0.0927  0.0646  -0.2754 524 PHE B CZ  
8338 N N   . LEU B 498 ? 1.4394 0.8238 0.8827 -0.0102 0.0390  -0.2727 525 LEU B N   
8339 C CA  . LEU B 498 ? 1.4918 0.9200 0.9305 0.0025  0.0326  -0.2844 525 LEU B CA  
8340 C C   . LEU B 498 ? 1.5333 0.9751 0.9744 -0.0167 0.0190  -0.3132 525 LEU B C   
8341 O O   . LEU B 498 ? 1.4984 0.9457 0.9200 -0.0021 0.0109  -0.3335 525 LEU B O   
8342 C CB  . LEU B 498 ? 1.2836 0.7558 0.7390 0.0073  0.0365  -0.2640 525 LEU B CB  
8343 C CG  . LEU B 498 ? 1.3097 0.7750 0.7684 0.0250  0.0488  -0.2374 525 LEU B CG  
8344 C CD1 . LEU B 498 ? 1.2444 0.7538 0.7193 0.0292  0.0512  -0.2217 525 LEU B CD1 
8345 C CD2 . LEU B 498 ? 1.2632 0.7090 0.7006 0.0535  0.0551  -0.2392 525 LEU B CD2 
8346 N N   . PRO B 499 ? 1.5114 0.9600 0.9752 -0.0485 0.0161  -0.3177 526 PRO B N   
8347 C CA  . PRO B 499 ? 1.5488 1.0112 1.0198 -0.0678 0.0028  -0.3489 526 PRO B CA  
8348 C C   . PRO B 499 ? 1.6017 1.0202 1.0528 -0.0675 -0.0024 -0.3724 526 PRO B C   
8349 O O   . PRO B 499 ? 1.5626 0.9966 1.0112 -0.0708 -0.0164 -0.4019 526 PRO B O   
8350 C CB  . PRO B 499 ? 1.5260 0.9945 1.0268 -0.1039 0.0069  -0.3447 526 PRO B CB  
8351 C CG  . PRO B 499 ? 1.4890 0.9730 0.9978 -0.0972 0.0175  -0.3135 526 PRO B CG  
8352 C CD  . PRO B 499 ? 1.5075 0.9601 0.9930 -0.0680 0.0245  -0.2961 526 PRO B CD  
8353 N N   . VAL B 500 ? 1.5189 0.8831 0.9561 -0.0627 0.0070  -0.3617 527 VAL B N   
8354 C CA  . VAL B 500 ? 1.6195 0.9399 1.0344 -0.0564 0.0026  -0.3841 527 VAL B CA  
8355 C C   . VAL B 500 ? 1.6139 0.9503 1.0017 -0.0217 -0.0021 -0.3945 527 VAL B C   
8356 O O   . VAL B 500 ? 1.5310 0.8615 0.9026 -0.0183 -0.0133 -0.4242 527 VAL B O   
8357 C CB  . VAL B 500 ? 1.6727 0.9307 1.0788 -0.0553 0.0138  -0.3685 527 VAL B CB  
8358 C CG1 . VAL B 500 ? 1.6089 0.8226 0.9887 -0.0398 0.0106  -0.3901 527 VAL B CG1 
8359 C CG2 . VAL B 500 ? 1.6508 0.8829 1.0755 -0.0920 0.0176  -0.3631 527 VAL B CG2 
8360 N N   . MET B 501 ? 1.6020 0.9594 0.9837 0.0038  0.0068  -0.3709 528 MET B N   
8361 C CA  . MET B 501 ? 1.5537 0.9199 0.9058 0.0375  0.0073  -0.3765 528 MET B CA  
8362 C C   . MET B 501 ? 1.6510 1.0626 0.9947 0.0427  -0.0070 -0.3947 528 MET B C   
8363 O O   . MET B 501 ? 1.6695 1.0796 0.9812 0.0656  -0.0114 -0.4104 528 MET B O   
8364 C CB  . MET B 501 ? 1.5125 0.8861 0.8639 0.0608  0.0233  -0.3455 528 MET B CB  
8365 C CG  . MET B 501 ? 1.5481 0.8754 0.8985 0.0680  0.0355  -0.3331 528 MET B CG  
8366 S SD  . MET B 501 ? 1.6320 0.9098 0.9509 0.0823  0.0336  -0.3610 528 MET B SD  
8367 C CE  . MET B 501 ? 1.5187 0.8234 0.8065 0.1199  0.0404  -0.3634 528 MET B CE  
8368 N N   . PHE B 502 ? 1.6835 1.1357 1.0533 0.0241  -0.0149 -0.3936 529 PHE B N   
8369 C CA  . PHE B 502 ? 1.7028 1.1956 1.0674 0.0271  -0.0328 -0.4165 529 PHE B CA  
8370 C C   . PHE B 502 ? 1.7238 1.2182 1.1083 -0.0037 -0.0483 -0.4476 529 PHE B C   
8371 O O   . PHE B 502 ? 1.7430 1.2808 1.1398 -0.0098 -0.0643 -0.4652 529 PHE B O   
8372 C CB  . PHE B 502 ? 1.6572 1.2006 1.0356 0.0336  -0.0334 -0.3987 529 PHE B CB  
8373 C CG  . PHE B 502 ? 1.6681 1.2273 1.0866 0.0074  -0.0274 -0.3818 529 PHE B CG  
8374 C CD1 . PHE B 502 ? 1.6431 1.2295 1.0920 -0.0208 -0.0387 -0.3991 529 PHE B CD1 
8375 C CD2 . PHE B 502 ? 1.6482 1.1995 1.0746 0.0121  -0.0105 -0.3495 529 PHE B CD2 
8376 C CE1 . PHE B 502 ? 1.6059 1.2080 1.0889 -0.0440 -0.0311 -0.3836 529 PHE B CE1 
8377 C CE2 . PHE B 502 ? 1.4843 1.0504 0.9428 -0.0101 -0.0054 -0.3345 529 PHE B CE2 
8378 C CZ  . PHE B 502 ? 1.4935 1.0843 0.9786 -0.0379 -0.0147 -0.3510 529 PHE B CZ  
8379 N N   . ASP B 503 ? 1.7140 1.1611 1.1031 -0.0228 -0.0437 -0.4550 530 ASP B N   
8380 C CA  . ASP B 503 ? 1.7286 1.1635 1.1285 -0.0488 -0.0571 -0.4895 530 ASP B CA  
8381 C C   . ASP B 503 ? 1.7095 1.1896 1.1507 -0.0797 -0.0661 -0.4996 530 ASP B C   
8382 O O   . ASP B 503 ? 1.7027 1.2093 1.1531 -0.0890 -0.0846 -0.5324 530 ASP B O   
8383 C CB  . ASP B 503 ? 1.7858 1.2189 1.1523 -0.0277 -0.0730 -0.5214 530 ASP B CB  
8384 C CG  . ASP B 503 ? 1.7563 1.1572 1.1282 -0.0514 -0.0836 -0.5567 530 ASP B CG  
8385 O OD1 . ASP B 503 ? 1.9734 1.3476 1.3729 -0.0839 -0.0761 -0.5537 530 ASP B OD1 
8386 O OD2 . ASP B 503 ? 1.9113 1.3116 1.2579 -0.0375 -0.0991 -0.5877 530 ASP B OD2 
8387 N N   . LYS B 504 ? 1.7088 1.1994 1.1762 -0.0953 -0.0529 -0.4725 531 LYS B N   
8388 C CA  . LYS B 504 ? 1.4491 0.9787 0.9585 -0.1274 -0.0563 -0.4797 531 LYS B CA  
8389 C C   . LYS B 504 ? 1.5799 1.0745 1.1102 -0.1610 -0.0396 -0.4647 531 LYS B C   
8390 O O   . LYS B 504 ? 1.6039 1.1273 1.1696 -0.1907 -0.0377 -0.4683 531 LYS B O   
8391 C CB  . LYS B 504 ? 1.5422 1.1301 1.0638 -0.1138 -0.0574 -0.4631 531 LYS B CB  
8392 C CG  . LYS B 504 ? 1.6681 1.2946 1.1703 -0.0829 -0.0754 -0.4782 531 LYS B CG  
8393 C CD  . LYS B 504 ? 1.5486 1.2084 1.0687 -0.0969 -0.0978 -0.5188 531 LYS B CD  
8394 C CE  . LYS B 504 ? 1.4497 1.1525 0.9496 -0.0642 -0.1172 -0.5304 531 LYS B CE  
8395 N NZ  . LYS B 504 ? 1.6368 1.3821 1.1492 -0.0520 -0.1134 -0.5063 531 LYS B NZ  
8396 N N   . HIS B 505 ? 1.6128 1.0464 1.1211 -0.1560 -0.0272 -0.4480 532 HIS B N   
8397 C CA  . HIS B 505 ? 1.6517 1.0443 1.1722 -0.1853 -0.0120 -0.4323 532 HIS B CA  
8398 C C   . HIS B 505 ? 1.6800 1.0558 1.2202 -0.2223 -0.0165 -0.4621 532 HIS B C   
8399 O O   . HIS B 505 ? 1.6166 0.9787 1.1467 -0.2188 -0.0293 -0.4923 532 HIS B O   
8400 C CB  . HIS B 505 ? 1.6388 0.9680 1.1292 -0.1671 -0.0011 -0.4108 532 HIS B CB  
8401 C CG  . HIS B 505 ? 1.6721 0.9652 1.1681 -0.1866 0.0150  -0.3832 532 HIS B CG  
8402 N ND1 . HIS B 505 ? 1.7198 0.9640 1.2204 -0.2183 0.0210  -0.3891 532 HIS B ND1 
8403 C CD2 . HIS B 505 ? 1.5567 0.8535 1.0518 -0.1782 0.0260  -0.3495 532 HIS B CD2 
8404 C CE1 . HIS B 505 ? 1.7832 1.0014 1.2818 -0.2274 0.0352  -0.3586 532 HIS B CE1 
8405 N NE2 . HIS B 505 ? 1.6926 0.9435 1.1883 -0.2031 0.0375  -0.3353 532 HIS B NE2 
8406 N N   . PRO B 506 ? 1.7669 1.1433 1.3351 -0.2588 -0.0054 -0.4554 533 PRO B N   
8407 C CA  . PRO B 506 ? 1.7476 1.1108 1.3397 -0.2978 -0.0076 -0.4849 533 PRO B CA  
8408 C C   . PRO B 506 ? 1.7330 1.0148 1.3025 -0.3046 -0.0036 -0.4906 533 PRO B C   
8409 O O   . PRO B 506 ? 1.9041 1.1739 1.4794 -0.3173 -0.0149 -0.5255 533 PRO B O   
8410 C CB  . PRO B 506 ? 1.6915 1.0733 1.3151 -0.3325 0.0087  -0.4690 533 PRO B CB  
8411 C CG  . PRO B 506 ? 1.5817 0.9503 1.1840 -0.3125 0.0222  -0.4269 533 PRO B CG  
8412 C CD  . PRO B 506 ? 1.5866 0.9787 1.1666 -0.2672 0.0102  -0.4229 533 PRO B CD  
8413 N N   . VAL B 507 ? 1.7189 0.9439 1.2628 -0.2955 0.0109  -0.4586 534 VAL B N   
8414 C CA  . VAL B 507 ? 1.7864 0.9289 1.3078 -0.3002 0.0154  -0.4612 534 VAL B CA  
8415 C C   . VAL B 507 ? 1.9545 1.0830 1.4492 -0.2665 0.0008  -0.4824 534 VAL B C   
8416 O O   . VAL B 507 ? 1.8658 0.9903 1.3346 -0.2287 0.0015  -0.4645 534 VAL B O   
8417 C CB  . VAL B 507 ? 1.7898 0.8788 1.2893 -0.2938 0.0324  -0.4204 534 VAL B CB  
8418 C CG1 . VAL B 507 ? 2.0144 1.0144 1.4916 -0.2999 0.0366  -0.4237 534 VAL B CG1 
8419 C CG2 . VAL B 507 ? 1.8126 0.9201 1.3329 -0.3238 0.0474  -0.3983 534 VAL B CG2 
8420 N N   . SER B 508 ? 2.0244 1.1464 1.5262 -0.2805 -0.0118 -0.5218 535 SER B N   
8421 C CA  . SER B 508 ? 2.0826 1.1887 1.5558 -0.2499 -0.0256 -0.5454 535 SER B CA  
8422 C C   . SER B 508 ? 2.0760 1.1018 1.5159 -0.2321 -0.0167 -0.5319 535 SER B C   
8423 O O   . SER B 508 ? 2.0681 1.0837 1.4790 -0.1964 -0.0228 -0.5395 535 SER B O   
8424 C CB  . SER B 508 ? 2.0936 1.2079 1.5828 -0.2716 -0.0423 -0.5931 535 SER B CB  
8425 O OG  . SER B 508 ? 2.2006 1.3943 1.7213 -0.2828 -0.0537 -0.6087 535 SER B OG  
8426 N N   . GLU B 509 ? 2.0836 1.0520 1.5258 -0.2551 -0.0019 -0.5119 536 GLU B N   
8427 C CA  . GLU B 509 ? 2.1305 1.0217 1.5416 -0.2356 0.0055  -0.4970 536 GLU B CA  
8428 C C   . GLU B 509 ? 2.0612 0.9670 1.4535 -0.1947 0.0110  -0.4643 536 GLU B C   
8429 O O   . GLU B 509 ? 2.1469 1.0164 1.5129 -0.1625 0.0108  -0.4631 536 GLU B O   
8430 C CB  . GLU B 509 ? 2.2598 1.0928 1.6799 -0.2673 0.0190  -0.4782 536 GLU B CB  
8431 C CG  . GLU B 509 ? 2.3775 1.1386 1.7731 -0.2440 0.0244  -0.4589 536 GLU B CG  
8432 C CD  . GLU B 509 ? 2.5721 1.2761 1.9759 -0.2739 0.0358  -0.4410 536 GLU B CD  
8433 O OE1 . GLU B 509 ? 2.7131 1.4343 2.1392 -0.3123 0.0436  -0.4368 536 GLU B OE1 
8434 O OE2 . GLU B 509 ? 2.6180 1.2614 2.0063 -0.2580 0.0375  -0.4308 536 GLU B OE2 
8435 N N   . TYR B 510 ? 2.0676 1.0269 1.4750 -0.1956 0.0163  -0.4390 537 TYR B N   
8436 C CA  . TYR B 510 ? 1.9974 0.9771 1.3920 -0.1588 0.0208  -0.4104 537 TYR B CA  
8437 C C   . TYR B 510 ? 1.9479 0.9633 1.3288 -0.1237 0.0114  -0.4278 537 TYR B C   
8438 O O   . TYR B 510 ? 2.0072 1.0032 1.3671 -0.0897 0.0147  -0.4188 537 TYR B O   
8439 C CB  . TYR B 510 ? 1.9668 0.9992 1.3820 -0.1691 0.0271  -0.3842 537 TYR B CB  
8440 C CG  . TYR B 510 ? 2.0120 1.0091 1.4331 -0.1969 0.0396  -0.3596 537 TYR B CG  
8441 C CD1 . TYR B 510 ? 1.9812 0.8992 1.3874 -0.2100 0.0450  -0.3580 537 TYR B CD1 
8442 C CD2 . TYR B 510 ? 1.8191 0.8592 1.2570 -0.2090 0.0464  -0.3374 537 TYR B CD2 
8443 C CE1 . TYR B 510 ? 2.0400 0.9219 1.4454 -0.2345 0.0574  -0.3334 537 TYR B CE1 
8444 C CE2 . TYR B 510 ? 1.7867 0.7941 1.2246 -0.2335 0.0588  -0.3144 537 TYR B CE2 
8445 C CZ  . TYR B 510 ? 1.9398 0.8675 1.3600 -0.2461 0.0645  -0.3116 537 TYR B CZ  
8446 O OH  . TYR B 510 ? 1.9406 0.8317 1.3550 -0.2697 0.0779  -0.2867 537 TYR B OH  
8447 N N   . LYS B 511 ? 1.9131 0.9812 1.3050 -0.1310 -0.0002 -0.4530 538 LYS B N   
8448 C CA  . LYS B 511 ? 1.8873 0.9881 1.2605 -0.0982 -0.0094 -0.4696 538 LYS B CA  
8449 C C   . LYS B 511 ? 1.8984 0.9483 1.2440 -0.0821 -0.0139 -0.4948 538 LYS B C   
8450 O O   . LYS B 511 ? 1.8929 0.9557 1.2142 -0.0482 -0.0162 -0.5021 538 LYS B O   
8451 C CB  . LYS B 511 ? 1.7949 0.9595 1.1842 -0.1100 -0.0235 -0.4927 538 LYS B CB  
8452 C CG  . LYS B 511 ? 1.9111 1.1322 1.3273 -0.1213 -0.0198 -0.4705 538 LYS B CG  
8453 C CD  . LYS B 511 ? 1.8372 1.1201 1.2715 -0.1318 -0.0358 -0.4963 538 LYS B CD  
8454 C CE  . LYS B 511 ? 1.7216 0.9903 1.1764 -0.1684 -0.0447 -0.5294 538 LYS B CE  
8455 N NZ  . LYS B 511 ? 1.7044 1.0402 1.1856 -0.1810 -0.0607 -0.5538 538 LYS B NZ  
8456 N N   . ALA B 512 ? 1.9770 0.9675 1.3244 -0.1055 -0.0139 -0.5084 539 ALA B N   
8457 C CA  . ALA B 512 ? 2.0025 0.9416 1.3257 -0.0899 -0.0181 -0.5329 539 ALA B CA  
8458 C C   . ALA B 512 ? 2.0395 0.9479 1.3417 -0.0526 -0.0068 -0.5104 539 ALA B C   
8459 O O   . ALA B 512 ? 1.9510 0.8549 1.2402 -0.0251 -0.0091 -0.5249 539 ALA B O   
8460 C CB  . ALA B 512 ? 1.9784 0.8725 1.3233 -0.1235 -0.0200 -0.5455 539 ALA B CB  
8461 N N   . HIS B 513 ? 2.0821 0.9811 1.3894 -0.0504 0.0053  -0.4738 540 HIS B N   
8462 C CA  . HIS B 513 ? 2.0180 0.8930 1.3099 -0.0147 0.0151  -0.4531 540 HIS B CA  
8463 C C   . HIS B 513 ? 1.9363 0.8665 1.2193 0.0202  0.0177  -0.4488 540 HIS B C   
8464 O O   . HIS B 513 ? 1.9054 0.8202 1.1756 0.0526  0.0258  -0.4401 540 HIS B O   
8465 C CB  . HIS B 513 ? 2.0899 0.9474 1.3949 -0.0224 0.0248  -0.4149 540 HIS B CB  
8466 C CG  . HIS B 513 ? 2.1367 0.9290 1.4435 -0.0529 0.0258  -0.4136 540 HIS B CG  
8467 N ND1 . HIS B 513 ? 2.2380 1.0393 1.5637 -0.0940 0.0258  -0.4112 540 HIS B ND1 
8468 C CD2 . HIS B 513 ? 1.9868 0.7133 1.2860 -0.0476 0.0276  -0.4113 540 HIS B CD2 
8469 C CE1 . HIS B 513 ? 2.2346 0.9663 1.5556 -0.1147 0.0294  -0.4087 540 HIS B CE1 
8470 N NE2 . HIS B 513 ? 2.0334 0.7265 1.3435 -0.0857 0.0292  -0.4062 540 HIS B NE2 
8471 N N   . PHE B 514 ? 1.8910 0.8836 1.1807 0.0147  0.0117  -0.4547 541 PHE B N   
8472 C CA  . PHE B 514 ? 1.8976 0.9410 1.1763 0.0455  0.0151  -0.4491 541 PHE B CA  
8473 C C   . PHE B 514 ? 2.0077 1.0671 1.2638 0.0531  0.0032  -0.4850 541 PHE B C   
8474 O O   . PHE B 514 ? 2.0116 1.1000 1.2769 0.0312  -0.0100 -0.5023 541 PHE B O   
8475 C CB  . PHE B 514 ? 1.6973 0.7984 0.9985 0.0370  0.0175  -0.4237 541 PHE B CB  
8476 C CG  . PHE B 514 ? 1.6686 0.7579 0.9889 0.0321  0.0280  -0.3890 541 PHE B CG  
8477 C CD1 . PHE B 514 ? 1.7080 0.7720 1.0449 -0.0003 0.0268  -0.3815 541 PHE B CD1 
8478 C CD2 . PHE B 514 ? 1.7681 0.8722 1.0892 0.0596  0.0392  -0.3646 541 PHE B CD2 
8479 C CE1 . PHE B 514 ? 1.7546 0.8066 1.1036 -0.0029 0.0352  -0.3498 541 PHE B CE1 
8480 C CE2 . PHE B 514 ? 1.6660 0.7611 1.0043 0.0563  0.0462  -0.3349 541 PHE B CE2 
8481 C CZ  . PHE B 514 ? 1.6932 0.7615 1.0429 0.0261  0.0434  -0.3273 541 PHE B CZ  
8482 N N   . SER B 515 ? 2.1931 1.2419 1.4252 0.0846  0.0078  -0.4952 542 SER B N   
8483 C CA  . SER B 515 ? 2.3130 1.3869 1.5323 0.0925  -0.0029 -0.5252 542 SER B CA  
8484 C C   . SER B 515 ? 2.2257 1.3603 1.4347 0.1002  -0.0087 -0.5251 542 SER B C   
8485 O O   . SER B 515 ? 2.2150 1.3756 1.4283 0.0827  -0.0254 -0.5465 542 SER B O   
8486 C CB  . SER B 515 ? 2.1263 1.1855 1.3303 0.1237  0.0071  -0.5297 542 SER B CB  
8487 O OG  . SER B 515 ? 2.2246 1.2983 1.4222 0.1516  0.0243  -0.5025 542 SER B OG  
8488 N N   . LEU B 516 ? 2.0063 1.1650 1.2040 0.1265  0.0049  -0.5010 543 LEU B N   
8489 C CA  . LEU B 516 ? 1.8681 1.0812 1.0530 0.1386  0.0017  -0.4969 543 LEU B CA  
8490 C C   . LEU B 516 ? 1.8817 1.1203 1.0887 0.1222  0.0015  -0.4744 543 LEU B C   
8491 O O   . LEU B 516 ? 1.9211 1.1579 1.1480 0.1238  0.0163  -0.4437 543 LEU B O   
8492 C CB  . LEU B 516 ? 1.7490 0.9778 0.9138 0.1741  0.0192  -0.4816 543 LEU B CB  
8493 C CG  . LEU B 516 ? 1.8492 1.1292 0.9961 0.1898  0.0187  -0.4739 543 LEU B CG  
8494 C CD1 . LEU B 516 ? 1.7937 1.0986 0.9318 0.1795  -0.0041 -0.5015 543 LEU B CD1 
8495 C CD2 . LEU B 516 ? 1.7397 1.0268 0.8654 0.2217  0.0380  -0.4622 543 LEU B CD2 
8496 N N   . ARG B 517 ? 1.8261 1.1012 1.0420 0.1051  -0.0154 -0.4869 544 ARG B N   
8497 C CA  . ARG B 517 ? 1.7492 1.0644 0.9988 0.0865  -0.0166 -0.4654 544 ARG B CA  
8498 C C   . ARG B 517 ? 1.7240 1.0909 0.9586 0.1008  -0.0267 -0.4697 544 ARG B C   
8499 O O   . ARG B 517 ? 1.6068 1.0031 0.8537 0.0843  -0.0450 -0.4880 544 ARG B O   
8500 C CB  . ARG B 517 ? 1.6263 0.9338 0.9100 0.0466  -0.0268 -0.4765 544 ARG B CB  
8501 C CG  . ARG B 517 ? 1.8613 1.1084 1.1516 0.0328  -0.0192 -0.4765 544 ARG B CG  
8502 C CD  . ARG B 517 ? 1.7792 1.0172 1.1017 -0.0088 -0.0261 -0.4850 544 ARG B CD  
8503 N NE  . ARG B 517 ? 1.7938 1.0481 1.1183 -0.0244 -0.0454 -0.5227 544 ARG B NE  
8504 C CZ  . ARG B 517 ? 1.8563 1.0721 1.1675 -0.0298 -0.0540 -0.5546 544 ARG B CZ  
8505 N NH1 . ARG B 517 ? 1.7959 0.9522 1.0886 -0.0193 -0.0447 -0.5534 544 ARG B NH1 
8506 N NH2 . ARG B 517 ? 1.8015 1.0396 1.1195 -0.0453 -0.0734 -0.5899 544 ARG B NH2 
8507 N N   . ASN B 518 ? 1.7445 1.1223 0.9534 0.1320  -0.0142 -0.4523 545 ASN B N   
8508 C CA  . ASN B 518 ? 1.7068 1.1237 0.8901 0.1520  -0.0217 -0.4544 545 ASN B CA  
8509 C C   . ASN B 518 ? 1.6374 1.0875 0.8378 0.1568  -0.0108 -0.4199 545 ASN B C   
8510 O O   . ASN B 518 ? 1.7200 1.1838 0.8930 0.1831  -0.0022 -0.4068 545 ASN B O   
8511 C CB  . ASN B 518 ? 1.6770 1.0872 0.8221 0.1817  -0.0142 -0.4589 545 ASN B CB  
8512 C CG  . ASN B 518 ? 1.8543 1.2408 0.9931 0.2004  0.0128  -0.4344 545 ASN B CG  
8513 O OD1 . ASN B 518 ? 1.8713 1.2361 1.0324 0.1908  0.0236  -0.4195 545 ASN B OD1 
8514 N ND2 . ASN B 518 ? 1.7578 1.1519 0.8707 0.2259  0.0242  -0.4288 545 ASN B ND2 
8515 N N   . LEU B 519 ? 1.6862 1.1477 0.9304 0.1311  -0.0102 -0.4053 546 LEU B N   
8516 C CA  . LEU B 519 ? 1.5442 1.0349 0.8084 0.1332  -0.0003 -0.3743 546 LEU B CA  
8517 C C   . LEU B 519 ? 1.6181 1.1543 0.8851 0.1321  -0.0171 -0.3806 546 LEU B C   
8518 O O   . LEU B 519 ? 1.4959 1.0482 0.7832 0.1100  -0.0348 -0.4011 546 LEU B O   
8519 C CB  . LEU B 519 ? 1.5719 1.0536 0.8781 0.1081  0.0076  -0.3564 546 LEU B CB  
8520 C CG  . LEU B 519 ? 1.4710 0.9716 0.7978 0.1119  0.0217  -0.3229 546 LEU B CG  
8521 C CD1 . LEU B 519 ? 1.4379 0.9203 0.7481 0.1377  0.0414  -0.3056 546 LEU B CD1 
8522 C CD2 . LEU B 519 ? 1.5243 1.0196 0.8892 0.0841  0.0238  -0.3111 546 LEU B CD2 
8523 N N   . HIS B 520 ? 1.7887 1.3452 1.0367 0.1559  -0.0111 -0.3634 547 HIS B N   
8524 C CA  . HIS B 520 ? 1.6998 1.2984 0.9504 0.1591  -0.0260 -0.3648 547 HIS B CA  
8525 C C   . HIS B 520 ? 1.6361 1.2558 0.9306 0.1421  -0.0192 -0.3414 547 HIS B C   
8526 O O   . HIS B 520 ? 1.6354 1.2547 0.9317 0.1533  -0.0021 -0.3135 547 HIS B O   
8527 C CB  . HIS B 520 ? 1.8071 1.4112 1.0117 0.1938  -0.0222 -0.3562 547 HIS B CB  
8528 C CG  . HIS B 520 ? 1.8999 1.4800 1.0549 0.2138  -0.0249 -0.3764 547 HIS B CG  
8529 N ND1 . HIS B 520 ? 2.0032 1.5542 1.1296 0.2335  -0.0024 -0.3637 547 HIS B ND1 
8530 C CD2 . HIS B 520 ? 1.8833 1.4709 1.0222 0.2146  -0.0466 -0.4062 547 HIS B CD2 
8531 C CE1 . HIS B 520 ? 2.0546 1.6008 1.1573 0.2426  -0.0090 -0.3805 547 HIS B CE1 
8532 N NE2 . HIS B 520 ? 2.0138 1.5806 1.1224 0.2314  -0.0360 -0.4063 547 HIS B NE2 
8533 N N   . ALA B 521 ? 1.5636 1.2021 0.8943 0.1142  -0.0318 -0.3537 548 ALA B N   
8534 C CA  . ALA B 521 ? 1.4160 1.0735 0.7876 0.0957  -0.0254 -0.3347 548 ALA B CA  
8535 C C   . ALA B 521 ? 1.4449 1.1501 0.8326 0.0939  -0.0415 -0.3422 548 ALA B C   
8536 O O   . ALA B 521 ? 1.4921 1.2168 0.8780 0.0906  -0.0617 -0.3700 548 ALA B O   
8537 C CB  . ALA B 521 ? 1.4385 1.0775 0.8408 0.0633  -0.0225 -0.3394 548 ALA B CB  
8538 N N   . PHE B 522 ? 1.4092 1.1338 0.8143 0.0968  -0.0334 -0.3188 549 PHE B N   
8539 C CA  . PHE B 522 ? 1.3808 1.1504 0.8060 0.0956  -0.0466 -0.3233 549 PHE B CA  
8540 C C   . PHE B 522 ? 1.3447 1.1259 0.8081 0.0780  -0.0348 -0.3033 549 PHE B C   
8541 O O   . PHE B 522 ? 1.3264 1.0813 0.7940 0.0732  -0.0172 -0.2830 549 PHE B O   
8542 C CB  . PHE B 522 ? 1.3643 1.1462 0.7567 0.1295  -0.0518 -0.3161 549 PHE B CB  
8543 C CG  . PHE B 522 ? 1.3871 1.1530 0.7325 0.1510  -0.0608 -0.3322 549 PHE B CG  
8544 C CD1 . PHE B 522 ? 1.4035 1.1918 0.7432 0.1516  -0.0860 -0.3637 549 PHE B CD1 
8545 C CD2 . PHE B 522 ? 1.4219 1.1522 0.7296 0.1710  -0.0440 -0.3173 549 PHE B CD2 
8546 C CE1 . PHE B 522 ? 1.4061 1.1792 0.6988 0.1726  -0.0957 -0.3800 549 PHE B CE1 
8547 C CE2 . PHE B 522 ? 1.5305 1.2453 0.7910 0.1917  -0.0509 -0.3326 549 PHE B CE2 
8548 C CZ  . PHE B 522 ? 1.3794 1.1145 0.6302 0.1931  -0.0775 -0.3639 549 PHE B CZ  
8549 N N   . SER B 523 ? 1.3832 1.2057 0.8747 0.0693  -0.0456 -0.3109 550 SER B N   
8550 C CA  . SER B 523 ? 1.2430 1.0813 0.7689 0.0542  -0.0357 -0.2948 550 SER B CA  
8551 C C   . SER B 523 ? 1.2729 1.1477 0.8047 0.0718  -0.0433 -0.2903 550 SER B C   
8552 O O   . SER B 523 ? 1.2004 1.1023 0.7268 0.0834  -0.0618 -0.3090 550 SER B O   
8553 C CB  . SER B 523 ? 1.2024 1.0541 0.7645 0.0189  -0.0378 -0.3101 550 SER B CB  
8554 O OG  . SER B 523 ? 1.1273 0.9989 0.7194 0.0064  -0.0291 -0.2964 550 SER B OG  
8555 N N   . VAL B 524 ? 1.2234 1.0975 0.7659 0.0750  -0.0299 -0.2662 551 VAL B N   
8556 C CA  . VAL B 524 ? 1.1842 1.0908 0.7376 0.0887  -0.0359 -0.2617 551 VAL B CA  
8557 C C   . VAL B 524 ? 1.1694 1.1193 0.7617 0.0683  -0.0471 -0.2821 551 VAL B C   
8558 O O   . VAL B 524 ? 1.1664 1.1167 0.7837 0.0390  -0.0407 -0.2872 551 VAL B O   
8559 C CB  . VAL B 524 ? 1.2883 1.1823 0.8480 0.0933  -0.0184 -0.2333 551 VAL B CB  
8560 C CG1 . VAL B 524 ? 1.2811 1.2014 0.8465 0.1115  -0.0244 -0.2282 551 VAL B CG1 
8561 C CG2 . VAL B 524 ? 1.2737 1.1263 0.8030 0.1078  -0.0041 -0.2148 551 VAL B CG2 
8562 N N   . GLU B 525 ? 1.3165 1.3026 0.9137 0.0841  -0.0635 -0.2940 552 GLU B N   
8563 C CA  . GLU B 525 ? 1.3028 1.3366 0.9414 0.0667  -0.0742 -0.3156 552 GLU B CA  
8564 C C   . GLU B 525 ? 1.2788 1.3450 0.9315 0.0848  -0.0796 -0.3107 552 GLU B C   
8565 O O   . GLU B 525 ? 1.2256 1.2978 0.8556 0.1151  -0.0933 -0.3116 552 GLU B O   
8566 C CB  . GLU B 525 ? 1.1503 1.2054 0.7899 0.0642  -0.0952 -0.3476 552 GLU B CB  
8567 C CG  . GLU B 525 ? 1.2563 1.3664 0.9443 0.0454  -0.1063 -0.3734 552 GLU B CG  
8568 C CD  . GLU B 525 ? 1.4184 1.5301 1.1422 0.0071  -0.0881 -0.3716 552 GLU B CD  
8569 O OE1 . GLU B 525 ? 1.4211 1.4892 1.1307 -0.0083 -0.0724 -0.3582 552 GLU B OE1 
8570 O OE2 . GLU B 525 ? 1.4435 1.5998 1.2085 -0.0066 -0.0893 -0.3837 552 GLU B OE2 
8571 N N   . PRO B 526 ? 1.1731 1.2586 0.8604 0.0684  -0.0694 -0.3057 553 PRO B N   
8572 C CA  . PRO B 526 ? 1.0775 1.1565 0.7886 0.0339  -0.0530 -0.3030 553 PRO B CA  
8573 C C   . PRO B 526 ? 1.0712 1.1010 0.7605 0.0325  -0.0340 -0.2751 553 PRO B C   
8574 O O   . PRO B 526 ? 1.0448 1.0508 0.7073 0.0567  -0.0313 -0.2576 553 PRO B O   
8575 C CB  . PRO B 526 ? 0.9568 1.0786 0.7061 0.0267  -0.0513 -0.3077 553 PRO B CB  
8576 C CG  . PRO B 526 ? 0.9733 1.0988 0.7093 0.0607  -0.0575 -0.2961 553 PRO B CG  
8577 C CD  . PRO B 526 ? 1.1868 1.3010 0.8888 0.0861  -0.0737 -0.3016 553 PRO B CD  
8578 N N   . LEU B 527 ? 0.9315 0.9455 0.6320 0.0048  -0.0205 -0.2707 554 LEU B N   
8579 C CA  . LEU B 527 ? 0.9407 0.9104 0.6230 0.0041  -0.0050 -0.2465 554 LEU B CA  
8580 C C   . LEU B 527 ? 0.9509 0.9226 0.6373 0.0172  0.0029  -0.2267 554 LEU B C   
8581 O O   . LEU B 527 ? 1.0651 1.0687 0.7758 0.0129  0.0025  -0.2305 554 LEU B O   
8582 C CB  . LEU B 527 ? 0.9076 0.8605 0.5999 -0.0273 0.0059  -0.2462 554 LEU B CB  
8583 C CG  . LEU B 527 ? 1.1046 1.0436 0.7910 -0.0426 0.0007  -0.2637 554 LEU B CG  
8584 C CD1 . LEU B 527 ? 1.1813 1.1040 0.8791 -0.0753 0.0126  -0.2624 554 LEU B CD1 
8585 C CD2 . LEU B 527 ? 1.1419 1.0416 0.7938 -0.0240 -0.0006 -0.2574 554 LEU B CD2 
8586 N N   . LEU B 528 ? 0.8906 0.8287 0.5550 0.0331  0.0106  -0.2069 555 LEU B N   
8587 C CA  . LEU B 528 ? 0.9464 0.8812 0.6150 0.0449  0.0187  -0.1883 555 LEU B CA  
8588 C C   . LEU B 528 ? 0.9808 0.8973 0.6582 0.0285  0.0317  -0.1744 555 LEU B C   
8589 O O   . LEU B 528 ? 0.9305 0.8489 0.6171 0.0337  0.0374  -0.1624 555 LEU B O   
8590 C CB  . LEU B 528 ? 0.9211 0.8324 0.5636 0.0718  0.0209  -0.1749 555 LEU B CB  
8591 C CG  . LEU B 528 ? 0.9828 0.9069 0.6077 0.0936  0.0076  -0.1850 555 LEU B CG  
8592 C CD1 . LEU B 528 ? 0.9635 0.8590 0.5587 0.1188  0.0144  -0.1679 555 LEU B CD1 
8593 C CD2 . LEU B 528 ? 0.8840 0.8468 0.5299 0.0985  -0.0026 -0.1946 555 LEU B CD2 
8594 N N   . ILE B 529 ? 0.9534 0.8505 0.6267 0.0099  0.0354  -0.1763 556 ILE B N   
8595 C CA  . ILE B 529 ? 0.9518 0.8279 0.6282 -0.0035 0.0457  -0.1628 556 ILE B CA  
8596 C C   . ILE B 529 ? 0.9834 0.8593 0.6656 -0.0311 0.0471  -0.1723 556 ILE B C   
8597 O O   . ILE B 529 ? 0.9705 0.8406 0.6466 -0.0393 0.0427  -0.1852 556 ILE B O   
8598 C CB  . ILE B 529 ? 0.9411 0.7786 0.5996 0.0078  0.0517  -0.1484 556 ILE B CB  
8599 C CG1 . ILE B 529 ? 1.0255 0.8629 0.6852 0.0290  0.0558  -0.1347 556 ILE B CG1 
8600 C CG2 . ILE B 529 ? 0.9063 0.7184 0.5638 -0.0081 0.0581  -0.1397 556 ILE B CG2 
8601 C CD1 . ILE B 529 ? 1.0810 0.8880 0.7345 0.0362  0.0644  -0.1197 556 ILE B CD1 
8602 N N   . TYR B 530 ? 0.9055 0.7861 0.5981 -0.0458 0.0539  -0.1661 557 TYR B N   
8603 C CA  . TYR B 530 ? 1.0100 0.8875 0.7060 -0.0734 0.0591  -0.1713 557 TYR B CA  
8604 C C   . TYR B 530 ? 1.0484 0.8947 0.7328 -0.0795 0.0674  -0.1531 557 TYR B C   
8605 O O   . TYR B 530 ? 0.9071 0.7474 0.5899 -0.0640 0.0680  -0.1399 557 TYR B O   
8606 C CB  . TYR B 530 ? 0.9349 0.8568 0.6544 -0.0861 0.0599  -0.1844 557 TYR B CB  
8607 C CG  . TYR B 530 ? 0.9556 0.9124 0.6898 -0.0813 0.0495  -0.2054 557 TYR B CG  
8608 C CD1 . TYR B 530 ? 1.0287 1.0088 0.7683 -0.0566 0.0409  -0.2077 557 TYR B CD1 
8609 C CD2 . TYR B 530 ? 1.1339 1.0993 0.8763 -0.1012 0.0475  -0.2233 557 TYR B CD2 
8610 C CE1 . TYR B 530 ? 1.1790 1.1910 0.9295 -0.0491 0.0288  -0.2270 557 TYR B CE1 
8611 C CE2 . TYR B 530 ? 1.0322 1.0330 0.7900 -0.0957 0.0352  -0.2449 557 TYR B CE2 
8612 C CZ  . TYR B 530 ? 1.1343 1.1587 0.8948 -0.0683 0.0249  -0.2464 557 TYR B CZ  
8613 O OH  . TYR B 530 ? 1.2016 1.2611 0.9749 -0.0598 0.0102  -0.2679 557 TYR B OH  
8614 N N   . PRO B 531 ? 1.1433 0.9680 0.8192 -0.1017 0.0733  -0.1520 558 PRO B N   
8615 C CA  . PRO B 531 ? 1.0821 0.8765 0.7431 -0.1058 0.0794  -0.1342 558 PRO B CA  
8616 C C   . PRO B 531 ? 1.2108 1.0302 0.8803 -0.1113 0.0843  -0.1306 558 PRO B C   
8617 O O   . PRO B 531 ? 1.2217 1.0800 0.9094 -0.1180 0.0857  -0.1429 558 PRO B O   
8618 C CB  . PRO B 531 ? 1.0772 0.8390 0.7237 -0.1284 0.0847  -0.1351 558 PRO B CB  
8619 C CG  . PRO B 531 ? 1.2999 1.0718 0.9549 -0.1338 0.0802  -0.1541 558 PRO B CG  
8620 C CD  . PRO B 531 ? 1.1505 0.9721 0.8276 -0.1230 0.0742  -0.1666 558 PRO B CD  
8621 N N   . THR B 532 ? 1.1786 0.9760 0.8347 -0.1070 0.0861  -0.1146 559 THR B N   
8622 C CA  . THR B 532 ? 1.2264 1.0447 0.8869 -0.1084 0.0893  -0.1111 559 THR B CA  
8623 C C   . THR B 532 ? 1.5070 1.3258 1.1581 -0.1342 0.1000  -0.1123 559 THR B C   
8624 O O   . THR B 532 ? 1.3580 1.2137 1.0246 -0.1440 0.1054  -0.1236 559 THR B O   
8625 C CB  . THR B 532 ? 1.0274 0.8244 0.6780 -0.0928 0.0851  -0.0957 559 THR B CB  
8626 O OG1 . THR B 532 ? 1.3900 1.1429 1.0182 -0.0950 0.0846  -0.0846 559 THR B OG1 
8627 C CG2 . THR B 532 ? 1.0137 0.8214 0.6807 -0.0692 0.0784  -0.0959 559 THR B CG2 
8628 N N   . HIS B 533 ? 1.7446 1.5218 1.3699 -0.1450 0.1041  -0.1007 560 HIS B N   
8629 C CA  . HIS B 533 ? 1.8633 1.6323 1.4718 -0.1684 0.1164  -0.0967 560 HIS B CA  
8630 C C   . HIS B 533 ? 1.7410 1.5265 1.3618 -0.1945 0.1271  -0.1111 560 HIS B C   
8631 O O   . HIS B 533 ? 1.9384 1.7195 1.5476 -0.2169 0.1409  -0.1086 560 HIS B O   
8632 C CB  . HIS B 533 ? 1.8545 1.5673 1.4276 -0.1698 0.1167  -0.0780 560 HIS B CB  
8633 C CG  . HIS B 533 ? 1.9497 1.6496 1.5129 -0.1459 0.1059  -0.0652 560 HIS B CG  
8634 N ND1 . HIS B 533 ? 2.0582 1.7134 1.6008 -0.1347 0.0989  -0.0517 560 HIS B ND1 
8635 C CD2 . HIS B 533 ? 1.7847 1.5124 1.3592 -0.1310 0.1004  -0.0658 560 HIS B CD2 
8636 C CE1 . HIS B 533 ? 1.9250 1.5844 1.4690 -0.1144 0.0892  -0.0451 560 HIS B CE1 
8637 N NE2 . HIS B 533 ? 1.8410 1.5429 1.4039 -0.1127 0.0901  -0.0535 560 HIS B NE2 
8638 N N   . TYR B 534 ? 2.1149 1.5676 1.1625 0.1062  0.3559  0.4001  561 TYR B N   
8639 C CA  . TYR B 534 ? 2.0743 1.7870 1.2783 0.2121  0.3372  0.4285  561 TYR B CA  
8640 C C   . TYR B 534 ? 2.0391 1.8352 1.4611 0.2751  0.3666  0.3049  561 TYR B C   
8641 O O   . TYR B 534 ? 1.8555 1.6829 1.3695 0.4284  0.3633  0.3630  561 TYR B O   
8642 C CB  . TYR B 534 ? 2.2159 1.7719 1.3163 0.3823  0.3116  0.6116  561 TYR B CB  
8643 C CG  . TYR B 534 ? 2.2833 2.1033 1.3662 0.3705  0.2630  0.7189  561 TYR B CG  
8644 C CD1 . TYR B 534 ? 2.1285 2.2846 1.3963 0.4162  0.2449  0.7069  561 TYR B CD1 
8645 C CD2 . TYR B 534 ? 2.5304 2.2715 1.4152 0.3052  0.2310  0.8322  561 TYR B CD2 
8646 C CE1 . TYR B 534 ? 2.1621 2.5609 1.4137 0.4037  0.1976  0.8026  561 TYR B CE1 
8647 C CE2 . TYR B 534 ? 2.5943 2.5787 1.4600 0.2925  0.1859  0.9299  561 TYR B CE2 
8648 C CZ  . TYR B 534 ? 2.4090 2.7207 1.4571 0.3437  0.1700  0.9124  561 TYR B CZ  
8649 O OH  . TYR B 534 ? 2.4775 3.0303 1.5040 0.3310  0.1219  1.0098  561 TYR B OH  
8650 N N   . THR B 535 ? 2.0968 1.9421 1.6028 0.1548  0.3930  0.1385  562 THR B N   
8651 C CA  . THR B 535 ? 1.9442 1.9081 1.6687 0.1806  0.4134  0.0049  562 THR B CA  
8652 C C   . THR B 535 ? 1.7289 2.0723 1.6366 0.2022  0.3753  0.0043  562 THR B C   
8653 O O   . THR B 535 ? 1.5130 2.1110 1.5614 0.0979  0.3615  -0.1264 562 THR B O   
8654 C CB  . THR B 535 ? 1.8863 1.8661 1.6557 0.0240  0.4381  -0.1772 562 THR B CB  
8655 O OG1 . THR B 535 ? 1.8528 2.0796 1.5927 -0.1310 0.4114  -0.2161 562 THR B OG1 
8656 C CG2 . THR B 535 ? 1.9404 1.5362 1.5534 0.0100  0.4759  -0.1834 562 THR B CG2 
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