data_9EVL
# 
_entry.id   9EVL 
# 
_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   9EVL         pdb_00009evl 10.2210/pdb9evl/pdb 
WWPDB D_1292136071 ?            ?                   
# 
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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'  
2 2 'Structure model' 'Derived calculations' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                  
2 2 'Structure model' citation_author           
3 2 'Structure model' pdbx_struct_assembly_gen  
4 2 'Structure model' pdbx_struct_assembly_prop 
5 2 'Structure model' pdbx_struct_oper_list     
# 
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'                    
12 2 'Structure model' '_pdbx_struct_assembly_prop.value'  
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EVL 
_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 introduced by recombinant expression vector' 
2 non-polymer syn 'MERCURY (II) ION'                     200.590   9 ?        ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                         35.453    7 ?        ? ? ? 
4 non-polymer syn "GALACTOSE-URIDINE-5'-DIPHOSPHATE"     566.302   2 ?        ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   2 ?        ? ? ? 
6 non-polymer syn 'CALCIUM ION'                          40.078    2 ?        ? ? ? 
7 water       nat water                                  18.015    4 ?        ? ? ? 
# 
_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 'MERCURY (II) ION'                     HG  
3 'CHLORIDE ION'                         CL  
4 "GALACTOSE-URIDINE-5'-DIPHOSPHATE"     GDU 
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
6 'CALCIUM ION'                          CA  
7 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          ? 
_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  
HG  non-polymer         . 'MERCURY (II) ION'                     ?                     'Hg 2'              200.590 
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 
PHE 'L-peptide linking' y PHENYLALANINE                          ?                     'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                ?                     'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                 ?                     'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                              ?                     'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                             ?                     'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                               ?                     'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                 ?                     'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   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 ?   ?   ?   A . n 
A 1 536 GLY 536 563 ?   ?   ?   A . n 
A 1 537 ASP 537 564 ?   ?   ?   A . n 
A 1 538 ASP 538 565 ?   ?   ?   A . n 
A 1 539 GLY 539 566 ?   ?   ?   A . n 
A 1 540 TYR 540 567 ?   ?   ?   A . n 
A 1 541 VAL 541 568 ?   ?   ?   A . n 
A 1 542 SER 542 569 ?   ?   ?   A . n 
A 1 543 ASP 543 570 ?   ?   ?   A . n 
A 1 544 THR 544 571 ?   ?   ?   A . n 
A 1 545 GLU 545 572 ?   ?   ?   A . n 
A 1 546 THR 546 573 ?   ?   ?   A . n 
A 1 547 SER 547 574 ?   ?   ?   A . n 
A 1 548 VAL 548 575 ?   ?   ?   A . n 
A 1 549 VAL 549 576 ?   ?   ?   A . n 
A 1 550 TRP 550 577 ?   ?   ?   A . n 
A 1 551 ASN 551 578 ?   ?   ?   A . n 
A 1 552 ASN 552 579 ?   ?   ?   A . n 
A 1 553 GLU 553 580 ?   ?   ?   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 ?   ?   ?   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' ? 
# 
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 HG  1 701 4   HG  HG  A . 
D 2 HG  1 702 5   HG  HG  A . 
E 2 HG  1 703 8   HG  HG  A . 
F 2 HG  1 704 12  HG  HG  A . 
G 2 HG  1 705 18  HG  HG  A . 
H 3 CL  1 706 2   CL  CL  A . 
I 3 CL  1 707 3   CL  CL  A . 
J 3 CL  1 708 4   CL  CL  A . 
K 3 CL  1 709 9   CL  CL  A . 
L 4 GDU 1 710 600 GDU GDU A . 
M 5 MES 1 711 611 MES MES A . 
N 5 MES 1 712 613 MES MES A . 
O 6 CA  1 713 1   CA  CA  A . 
P 2 HG  1 701 1   HG  HG  B . 
Q 2 HG  1 702 2   HG  HG  B . 
R 2 HG  1 703 17  HG  HG  B . 
S 2 HG  1 704 19  HG  HG  B . 
T 3 CL  1 705 5   CL  CL  B . 
U 3 CL  1 706 6   CL  CL  B . 
V 3 CL  1 707 7   CL  CL  B . 
W 4 GDU 1 708 600 GDU GDU B . 
X 6 CA  1 709 2   CA  CA  B . 
Y 7 HOH 1 801 2   HOH HOH A . 
Y 7 HOH 2 802 6   HOH HOH A . 
Z 7 HOH 1 801 1   HOH HOH B . 
Z 7 HOH 2 802 5   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          ? ? ? ? ? ? ? ? ? ? ? HKL2Map ? ? ? .                  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                     9EVL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     220.187 
_cell.length_a_esd                 ? 
_cell.length_b                     220.187 
_cell.length_b_esd                 ? 
_cell.length_c                     220.187 
_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                         9EVL 
_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                   9EVL 
_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             3.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.07 
_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' 
_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         2021-03-15 
_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   0.7749 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.7749 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EVL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.8 
_reflns.d_resolution_low                               49.24 
_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                                     84831 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                23.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.2 
_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                                0.051 
_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                              0.169 
_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                                    2.8 
_reflns_shell.d_res_low                                     2.91 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4551 
_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                               23.3 
_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                               1.093 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.599 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.609 
_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                                 9EVL 
_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                            2.80 
_refine.ls_d_res_low                             49.24 
_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                     84831 
_refine.ls_number_reflns_R_free                  4203 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2040 
_refine.ls_R_factor_R_free                       0.2389 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2021 
_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                          1.33 
_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          SAD 
_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                 31.02 
_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                            0.46 
_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                       2.80 
_refine_hist.d_res_low                        49.24 
_refine_hist.number_atoms_solvent             4 
_refine_hist.number_atoms_total               8621 
_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        8503 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         114 
_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' ? 0.003  ? 8837  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.564  ? 12003 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.355 ? 3325  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 1282  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 1536  ? 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' 2.80 2.83  . . 114 2737 100.00 . . . . 0.3580 . . . . . . . . . . . 0.3483 
'X-RAY DIFFRACTION' 2.83 2.87  . . 128 2675 100.00 . . . . 0.3303 . . . . . . . . . . . 0.3544 
'X-RAY DIFFRACTION' 2.87 2.90  . . 162 2683 100.00 . . . . 0.3409 . . . . . . . . . . . 0.3643 
'X-RAY DIFFRACTION' 2.90 2.94  . . 122 2713 100.00 . . . . 0.4312 . . . . . . . . . . . 0.4515 
'X-RAY DIFFRACTION' 2.94 2.98  . . 114 2668 100.00 . . . . 0.3869 . . . . . . . . . . . 0.4304 
'X-RAY DIFFRACTION' 2.98 3.02  . . 144 2753 100.00 . . . . 0.3444 . . . . . . . . . . . 0.3929 
'X-RAY DIFFRACTION' 3.02 3.06  . . 116 2646 100.00 . . . . 0.3043 . . . . . . . . . . . 0.3466 
'X-RAY DIFFRACTION' 3.06 3.11  . . 112 2720 100.00 . . . . 0.2834 . . . . . . . . . . . 0.2818 
'X-RAY DIFFRACTION' 3.11 3.15  . . 152 2726 100.00 . . . . 0.2722 . . . . . . . . . . . 0.2983 
'X-RAY DIFFRACTION' 3.15 3.20  . . 104 2644 100.00 . . . . 0.2602 . . . . . . . . . . . 0.2870 
'X-RAY DIFFRACTION' 3.21 3.26  . . 112 2748 100.00 . . . . 0.2675 . . . . . . . . . . . 0.3025 
'X-RAY DIFFRACTION' 3.26 3.32  . . 174 2641 100.00 . . . . 0.2549 . . . . . . . . . . . 0.2858 
'X-RAY DIFFRACTION' 3.32 3.38  . . 140 2721 100.00 . . . . 0.2545 . . . . . . . . . . . 0.2698 
'X-RAY DIFFRACTION' 3.38 3.45  . . 160 2654 100.00 . . . . 0.2487 . . . . . . . . . . . 0.3237 
'X-RAY DIFFRACTION' 3.45 3.53  . . 150 2669 100.00 . . . . 0.2458 . . . . . . . . . . . 0.3063 
'X-RAY DIFFRACTION' 3.53 3.61  . . 190 2682 100.00 . . . . 0.2211 . . . . . . . . . . . 0.2587 
'X-RAY DIFFRACTION' 3.61 3.70  . . 138 2650 100.00 . . . . 0.2108 . . . . . . . . . . . 0.2358 
'X-RAY DIFFRACTION' 3.70 3.80  . . 122 2733 100.00 . . . . 0.1950 . . . . . . . . . . . 0.2510 
'X-RAY DIFFRACTION' 3.80 3.91  . . 154 2671 100.00 . . . . 0.1835 . . . . . . . . . . . 0.3097 
'X-RAY DIFFRACTION' 3.91 4.04  . . 148 2676 100.00 . . . . 0.1727 . . . . . . . . . . . 0.2713 
'X-RAY DIFFRACTION' 4.04 4.18  . . 168 2652 100.00 . . . . 0.1990 . . . . . . . . . . . 0.2215 
'X-RAY DIFFRACTION' 4.18 4.35  . . 150 2671 100.00 . . . . 0.1793 . . . . . . . . . . . 0.2160 
'X-RAY DIFFRACTION' 4.35 4.55  . . 110 2728 100.00 . . . . 0.1621 . . . . . . . . . . . 0.1723 
'X-RAY DIFFRACTION' 4.55 4.79  . . 138 2690 100.00 . . . . 0.1570 . . . . . . . . . . . 0.2036 
'X-RAY DIFFRACTION' 4.79 5.09  . . 176 2675 100.00 . . . . 0.1622 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 5.09 5.48  . . 148 2649 100.00 . . . . 0.1908 . . . . . . . . . . . 0.2057 
'X-RAY DIFFRACTION' 5.48 6.03  . . 156 2679 100.00 . . . . 0.2080 . . . . . . . . . . . 0.2260 
'X-RAY DIFFRACTION' 6.03 6.89  . . 116 2708 100.00 . . . . 0.1901 . . . . . . . . . . . 0.2929 
'X-RAY DIFFRACTION' 6.90 8.68  . . 118 2732 100.00 . . . . 0.1724 . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 8.69 49.24 . . 167 2634 99.00  . . . . 0.1627 . . . . . . . . . . . 0.1757 
# 
_struct.entry_id                     9EVL 
_struct.title                        
'Crystal Structure of human Collagen Hydroxylysine Galactosyltransferase GLT25D1/COLGALT1: Hg2+ soak for experimental phasing' 
_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        9EVL 
_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 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 6 ? 
P N N 2 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 2 ? 
T N N 3 ? 
U N N 3 ? 
V N N 3 ? 
W N N 4 ? 
X N N 6 ? 
Y N N 7 ? 
Z N N 7 ? 
# 
_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 9EVL A 3 ? 591 ? Q8NBJ5 30 ? 618 ? 30 618 
2 1 9EVL 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 9EVL GLY A 1   ? UNP Q8NBJ5 ? ? 'cloning artifact' 28  1  
1 9EVL SER A 2   ? UNP Q8NBJ5 ? ? 'cloning artifact' 29  2  
1 9EVL ALA A 592 ? UNP Q8NBJ5 ? ? 'cloning artifact' 619 3  
1 9EVL ALA A 593 ? UNP Q8NBJ5 ? ? 'cloning artifact' 620 4  
1 9EVL ALA A 594 ? UNP Q8NBJ5 ? ? 'cloning artifact' 621 5  
2 9EVL GLY B 1   ? UNP Q8NBJ5 ? ? 'cloning artifact' 28  6  
2 9EVL SER B 2   ? UNP Q8NBJ5 ? ? 'cloning artifact' 29  7  
2 9EVL ALA B 592 ? UNP Q8NBJ5 ? ? 'cloning artifact' 619 8  
2 9EVL ALA B 593 ? UNP Q8NBJ5 ? ? 'cloning artifact' 620 9  
2 9EVL ALA B 594 ? UNP Q8NBJ5 ? ? 'cloning artifact' 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)' 7730  ? 
1 MORE         -322  ? 
1 'SSA (A^2)'  45060 ? 
# 
_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,T,U,V,W,X,Y,Z 
# 
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 'light scattering' 'SEC-MALS confirms dimers in solution' 
2 1 microscopy         'mass photometry confirms dimers'      
3 1 SAXS               'SEC-SAXS confirms elongated 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 ? GLU A 250 ? ASP A 264 GLU A 277 1 ? 14 
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 ? ARG A 430 ? PHE A 443 ARG A 457 1 ? 15 
HELX_P HELX_P15 AB6 LEU A 476 ? ALA A 485 ? LEU A 503 ALA A 512 1 ? 10 
HELX_P HELX_P16 AB7 GLU A 486 ? LYS A 490 ? GLU A 513 LYS A 517 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 ? ALA A 512 ? VAL A 534 ALA A 539 1 ? 6  
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 ? ALA B 155 ? ASP B 175 ALA B 182 1 ? 8  
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 ? ALA B 360 ? ASN B 381 ALA B 387 1 ? 7  
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 ? GLU B 431 ? PHE B 443 GLU B 458 1 ? 16 
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 ? ALA B 512 ? VAL B 534 ALA B 539 1 ? 6  
# 
_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  ? ? ? ? ? ? ? 2.040 ? ? 
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 O CA  .   CA ? ? A ASP 168 A CA  713 1_555  ? ? ? ? ? ? ? 2.689 ? ? 
metalc2  metalc ? ? A ASP 141 OD2 ? ? ? 1_555 O CA  .   CA ? ? A ASP 168 A CA  713 1_555  ? ? ? ? ? ? ? 2.313 ? ? 
metalc3  metalc ? ? A CYS 176 SG  ? ? ? 1_555 D HG  .   HG ? ? A CYS 203 A HG  702 1_555  ? ? ? ? ? ? ? 3.075 ? ? 
metalc4  metalc ? ? A CYS 246 SG  ? ? ? 1_555 C HG  .   HG ? ? A CYS 273 A HG  701 1_555  ? ? ? ? ? ? ? 2.572 ? ? 
metalc5  metalc ? ? A MET 253 SD  ? ? ? 1_555 C HG  .   HG ? ? A MET 280 A HG  701 1_555  ? ? ? ? ? ? ? 2.855 ? ? 
metalc6  metalc ? ? A HIS 271 ND1 ? ? ? 1_555 S HG  .   HG ? ? A HIS 298 B HG  704 19_555 ? ? ? ? ? ? ? 2.362 ? ? 
metalc7  metalc ? ? A HIS 283 NE2 ? ? ? 1_555 F HG  .   HG ? ? A HIS 310 A HG  704 1_555  ? ? ? ? ? ? ? 2.589 ? ? 
metalc8  metalc ? ? A CYS 342 O   ? ? ? 1_555 G HG  .   HG ? ? A CYS 369 A HG  705 1_555  ? ? ? ? ? ? ? 2.822 ? ? 
metalc9  metalc ? ? A CYS 342 SG  ? ? ? 1_555 G HG  .   HG ? ? A CYS 369 A HG  705 1_555  ? ? ? ? ? ? ? 2.595 ? ? 
metalc10 metalc ? ? A CYS 385 SG  ? ? ? 1_555 E HG  .   HG ? ? A CYS 412 A HG  703 1_555  ? ? ? ? ? ? ? 2.444 ? ? 
metalc11 metalc ? ? A GLU 408 OE2 ? ? ? 1_555 E HG  .   HG ? ? A GLU 435 A HG  703 1_555  ? ? ? ? ? ? ? 2.714 ? ? 
metalc12 metalc ? ? A PHE 413 O   ? ? ? 1_555 F HG  .   HG ? ? A PHE 440 A HG  704 1_555  ? ? ? ? ? ? ? 3.161 ? ? 
metalc13 metalc ? ? L GDU .   O1A ? ? ? 1_555 O CA  .   CA ? ? A GDU 710 A CA  713 1_555  ? ? ? ? ? ? ? 2.352 ? ? 
metalc14 metalc ? ? L GDU .   O1B ? ? ? 1_555 O CA  .   CA ? ? A GDU 710 A CA  713 1_555  ? ? ? ? ? ? ? 2.197 ? ? 
metalc15 metalc ? ? O CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? A CA  713 A HOH 802 1_555  ? ? ? ? ? ? ? 3.010 ? ? 
metalc16 metalc ? ? B ASP 141 OD1 ? ? ? 1_555 X CA  .   CA ? ? B ASP 168 B CA  709 1_555  ? ? ? ? ? ? ? 2.578 ? ? 
metalc17 metalc ? ? B ASP 141 OD2 ? ? ? 1_555 X CA  .   CA ? ? B ASP 168 B CA  709 1_555  ? ? ? ? ? ? ? 2.199 ? ? 
metalc18 metalc ? ? B CYS 176 SG  ? ? ? 1_555 Q HG  .   HG ? ? B CYS 203 B HG  702 1_555  ? ? ? ? ? ? ? 3.020 ? ? 
metalc19 metalc ? ? B CYS 246 SG  ? ? ? 1_555 P HG  .   HG ? ? B CYS 273 B HG  701 1_555  ? ? ? ? ? ? ? 2.537 ? ? 
metalc20 metalc ? ? B MET 253 SD  ? ? ? 1_555 P HG  .   HG ? ? B MET 280 B HG  701 1_555  ? ? ? ? ? ? ? 2.552 ? ? 
metalc21 metalc ? ? B HIS 271 ND1 ? ? ? 1_555 S HG  .   HG ? ? B HIS 298 B HG  704 1_555  ? ? ? ? ? ? ? 2.195 ? ? 
metalc22 metalc ? ? B CYS 342 SG  ? ? ? 1_555 R HG  .   HG ? ? B CYS 369 B HG  703 1_555  ? ? ? ? ? ? ? 2.517 ? ? 
metalc23 metalc ? ? W GDU .   O1A ? ? ? 1_555 X CA  .   CA ? ? B GDU 708 B CA  709 1_555  ? ? ? ? ? ? ? 2.515 ? ? 
metalc24 metalc ? ? W GDU .   O2B ? ? ? 1_555 X CA  .   CA ? ? B GDU 708 B CA  709 1_555  ? ? ? ? ? ? ? 2.252 ? ? 
# 
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 ? O CA . ? A CA 713 ? 1_555  OD2 ? A ASP 141 ? A ASP 168 ? 1_555 51.1  ? 
2  OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O1A ? L GDU .   ? A GDU 710 ? 1_555 87.9  ? 
3  OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O1A ? L GDU .   ? A GDU 710 ? 1_555 97.5  ? 
4  OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O1B ? L GDU .   ? A GDU 710 ? 1_555 162.0 ? 
5  OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O1B ? L GDU .   ? A GDU 710 ? 1_555 130.0 ? 
6  O1A ? L GDU .   ? A GDU 710 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O1B ? L GDU .   ? A GDU 710 ? 1_555 74.0  ? 
7  OD1 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O   ? Y HOH .   ? A HOH 802 ? 1_555 102.2 ? 
8  OD2 ? A ASP 141 ? A ASP 168 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O   ? Y HOH .   ? A HOH 802 ? 1_555 144.7 ? 
9  O1A ? L GDU .   ? A GDU 710 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O   ? Y HOH .   ? A HOH 802 ? 1_555 104.7 ? 
10 O1B ? L GDU .   ? A GDU 710 ? 1_555 CA ? O CA . ? A CA 713 ? 1_555  O   ? Y HOH .   ? A HOH 802 ? 1_555 83.0  ? 
11 SG  ? A CYS 246 ? A CYS 273 ? 1_555 HG ? C HG . ? A HG 701 ? 1_555  SD  ? A MET 253 ? A MET 280 ? 1_555 112.2 ? 
12 ND1 ? A HIS 271 ? A HIS 298 ? 1_555 HG ? S HG . ? B HG 704 ? 19_555 ND1 ? B HIS 271 ? B HIS 298 ? 1_555 24.2  ? 
13 NE2 ? A HIS 283 ? A HIS 310 ? 1_555 HG ? F HG . ? A HG 704 ? 1_555  O   ? A PHE 413 ? A PHE 440 ? 1_555 68.9  ? 
14 O   ? A CYS 342 ? A CYS 369 ? 1_555 HG ? G HG . ? A HG 705 ? 1_555  SG  ? A CYS 342 ? A CYS 369 ? 1_555 71.7  ? 
15 SG  ? A CYS 385 ? A CYS 412 ? 1_555 HG ? E HG . ? A HG 703 ? 1_555  OE2 ? A GLU 408 ? A GLU 435 ? 1_555 109.4 ? 
16 OD1 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? X CA . ? B CA 709 ? 1_555  OD2 ? B ASP 141 ? B ASP 168 ? 1_555 53.4  ? 
17 OD1 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? X CA . ? B CA 709 ? 1_555  O1A ? W GDU .   ? B GDU 708 ? 1_555 91.1  ? 
18 OD2 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? X CA . ? B CA 709 ? 1_555  O1A ? W GDU .   ? B GDU 708 ? 1_555 76.4  ? 
19 OD1 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? X CA . ? B CA 709 ? 1_555  O2B ? W GDU .   ? B GDU 708 ? 1_555 156.7 ? 
20 OD2 ? B ASP 141 ? B ASP 168 ? 1_555 CA ? X CA . ? B CA 709 ? 1_555  O2B ? W GDU .   ? B GDU 708 ? 1_555 120.9 ? 
21 O1A ? W GDU .   ? B GDU 708 ? 1_555 CA ? X CA . ? B CA 709 ? 1_555  O2B ? W GDU .   ? B GDU 708 ? 1_555 66.1  ? 
22 SG  ? B CYS 246 ? B CYS 273 ? 1_555 HG ? P HG . ? B HG 701 ? 1_555  SD  ? B MET 253 ? B MET 280 ? 1_555 99.4  ? 
# 
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 -3.09 
2 TYR 226 A . ? TYR 253 A PRO 227 A ? PRO 254 A 1 -4.68 
3 GLU 525 A . ? GLU 552 A PRO 526 A ? PRO 553 A 1 -1.27 
4 GLU 95  B . ? GLU 122 B PRO 96  B ? PRO 123 B 1 -3.46 
5 TYR 226 B . ? TYR 253 B PRO 227 B ? PRO 254 B 1 -4.84 
6 GLU 525 B . ? GLU 552 B PRO 526 B ? PRO 553 B 1 3.43  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
AA7 ? 8 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 7 ? 
AB2 ? 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 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? parallel      
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? parallel      
AA7 7 8 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? parallel      
AB1 6 7 ? anti-parallel 
AB2 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  ? ALA A 93  ? VAL A 115 ALA A 120 
AA1 2 THR A 57  ? ASP A 64  ? THR A 84  ASP A 91  
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 ? VAL A 204 ? CYS A 228 VAL A 231 
AA2 1 LEU A 165 ? ASP A 166 ? LEU A 192 ASP A 193 
AA2 2 GLY A 262 ? PHE A 263 ? GLY A 289 PHE A 290 
AA3 1 PHE A 174 ? TRP A 175 ? PHE A 201 TRP A 202 
AA3 2 MET A 206 ? VAL A 207 ? MET A 233 VAL A 234 
AA4 1 GLY A 177 ? MET A 178 ? GLY A 204 MET A 205 
AA4 2 TYR A 184 ? LYS A 185 ? TYR A 211 LYS A 212 
AA5 1 ARG A 343 ? GLU A 346 ? ARG A 370 GLU A 373 
AA5 2 GLU A 315 ? ASN A 320 ? GLU A 342 ASN A 347 
AA5 3 LYS A 403 ? PHE A 407 ? LYS A 430 PHE A 434 
AA5 4 ALA A 471 ? SER A 475 ? ALA A 498 SER A 502 
AA5 5 LEU A 437 ? GLY A 441 ? LEU A 464 GLY A 468 
AA5 6 ALA A 521 ? VAL A 524 ? ALA A 548 VAL A 551 
AA5 7 LEU A 460 ? GLU A 462 ? LEU A 487 GLU A 489 
AA6 1 LEU A 411 ? PHE A 413 ? LEU A 438 PHE A 440 
AA6 2 ILE A 529 ? PRO A 531 ? ILE A 556 PRO A 558 
AA7 1 VAL B 88  ? ALA B 93  ? VAL B 115 ALA B 120 
AA7 2 THR B 57  ? ASP B 64  ? THR B 84  ASP B 91  
AA7 3 VAL B 27  ? ALA B 33  ? VAL B 54  ALA B 60  
AA7 4 TYR B 134 ? VAL B 138 ? TYR B 161 VAL B 165 
AA7 5 THR B 210 ? ASP B 214 ? THR B 237 ASP B 241 
AA7 6 VAL B 160 ? PRO B 163 ? VAL B 187 PRO B 190 
AA7 7 MET B 253 ? CYS B 256 ? MET B 280 CYS B 283 
AA7 8 CYS B 201 ? VAL B 204 ? CYS B 228 VAL B 231 
AA8 1 PHE B 174 ? TRP B 175 ? PHE B 201 TRP B 202 
AA8 2 MET B 206 ? VAL B 207 ? MET B 233 VAL B 234 
AA9 1 GLY B 177 ? MET B 178 ? GLY B 204 MET B 205 
AA9 2 TYR B 184 ? LYS B 185 ? TYR B 211 LYS B 212 
AB1 1 ARG B 343 ? GLU B 346 ? ARG B 370 GLU B 373 
AB1 2 GLU B 315 ? ASN B 320 ? GLU B 342 ASN B 347 
AB1 3 LYS B 403 ? PHE B 407 ? LYS B 430 PHE B 434 
AB1 4 ALA B 471 ? SER B 475 ? ALA B 498 SER B 502 
AB1 5 LEU B 437 ? GLY B 441 ? LEU B 464 GLY B 468 
AB1 6 ALA B 521 ? VAL B 524 ? ALA B 548 VAL B 551 
AB1 7 LEU B 460 ? GLU B 462 ? LEU B 487 GLU B 489 
AB2 1 LEU B 411 ? PHE B 413 ? LEU B 438 PHE B 440 
AB2 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 ARG A 91  ? O ARG A 118 N VAL A 61  ? N VAL A 88  
AA1 2 3 O ALA A 58  ? O ALA A 85  N ILE A 29  ? N ILE A 56  
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 VAL A 160 ? N VAL A 187 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 ASP A 166 ? N ASP A 193 O GLY A 262 ? O GLY A 289 
AA3 1 2 N TRP A 175 ? N TRP A 202 O MET A 206 ? O MET A 233 
AA4 1 2 N GLY A 177 ? N GLY A 204 O LYS A 185 ? O LYS A 212 
AA5 1 2 O ARG A 343 ? O ARG A 370 N VAL A 316 ? N VAL A 343 
AA5 2 3 N PHE A 317 ? N PHE A 344 O LEU A 405 ? O LEU A 432 
AA5 3 4 N VAL A 406 ? N VAL A 433 O TYR A 472 ? O TYR A 499 
AA5 4 5 O VAL A 473 ? O VAL A 500 N ILE A 438 ? N ILE A 465 
AA5 5 6 N LEU A 437 ? N LEU A 464 O PHE A 522 ? O PHE A 549 
AA5 6 7 O SER A 523 ? O SER A 550 N VAL A 461 ? N VAL A 488 
AA6 1 2 N ARG A 412 ? N ARG A 439 O TYR A 530 ? O TYR A 557 
AA7 1 2 O GLU B 89  ? O GLU B 116 N LEU B 59  ? N LEU B 86  
AA7 2 3 O TRP B 60  ? O TRP B 87  N LEU B 31  ? N LEU B 58  
AA7 3 4 N LEU B 28  ? N LEU B 55  O LEU B 136 ? O LEU B 163 
AA7 4 5 N ILE B 135 ? N ILE B 162 O ILE B 213 ? O ILE B 240 
AA7 5 6 O LEU B 212 ? O LEU B 239 N VAL B 161 ? N VAL B 188 
AA7 6 7 N ALA B 162 ? N ALA B 189 O CYS B 256 ? O CYS B 283 
AA7 7 8 O VAL B 255 ? O VAL B 282 N PHE B 202 ? N PHE B 229 
AA8 1 2 N TRP B 175 ? N TRP B 202 O MET B 206 ? O MET B 233 
AA9 1 2 N GLY B 177 ? N GLY B 204 O LYS B 185 ? O LYS B 212 
AB1 1 2 O ARG B 343 ? O ARG B 370 N VAL B 316 ? N VAL B 343 
AB1 2 3 N PHE B 317 ? N PHE B 344 O LEU B 405 ? O LEU B 432 
AB1 3 4 N VAL B 406 ? N VAL B 433 O TYR B 472 ? O TYR B 499 
AB1 4 5 O VAL B 473 ? O VAL B 500 N ILE B 438 ? N ILE B 465 
AB1 5 6 N LEU B 437 ? N LEU B 464 O PHE B 522 ? O PHE B 549 
AB1 6 7 O SER B 523 ? O SER B 550 N VAL B 461 ? N VAL B 488 
AB2 1 2 N ARG B 412 ? N ARG B 439 O TYR B 530 ? O TYR B 557 
# 
_pdbx_entry_details.entry_id                   9EVL 
_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 
# 
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  ? ? -86.27  41.63   
2  1 ALA A 196 ? ? -129.25 -167.95 
3  1 ASN A 200 ? ? -90.12  44.81   
4  1 SER A 236 ? ? 69.65   -63.90  
5  1 TYR A 400 ? ? -122.39 -58.29  
6  1 PRO A 404 ? ? -67.79  -172.45 
7  1 GLU A 435 ? ? -120.05 -156.59 
8  1 ASP A 491 ? ? -86.66  -150.60 
9  1 TYR A 494 ? ? -144.38 12.32   
10 1 THR A 496 ? ? -141.42 40.88   
11 1 GLU A 513 ? ? 54.43   73.81   
12 1 ARG A 544 ? ? -110.68 66.73   
13 1 ALA B 196 ? ? -128.31 -166.08 
14 1 ASN B 200 ? ? -86.70  42.41   
15 1 SER B 207 ? ? 66.11   -1.50   
16 1 SER B 236 ? ? 77.12   -65.88  
17 1 HIS B 298 ? ? -89.62  35.63   
18 1 HIS B 401 ? ? -144.07 -9.50   
19 1 PRO B 404 ? ? -67.53  -177.16 
20 1 GLU B 435 ? ? -102.73 -163.39 
21 1 GLU B 475 ? ? -67.28  -70.88  
22 1 ASP B 491 ? ? -86.87  -155.09 
23 1 TYR B 494 ? ? -149.56 -4.90   
24 1 GLU B 513 ? ? 32.82   68.36   
25 1 SER B 542 ? ? -82.79  -74.20  
# 
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 44.9806 56.1960 81.9793  0.8258 ? 0.1548  ? 0.0062  ? 0.5549 ? 0.0348  ? 0.4071 ? 2.4755 ? 
-0.2707 ? -0.2389 ? 2.8274 ? 0.9575  ? 3.3517 ? -0.2927 ? -0.4629 ? 0.0035  ? 0.2558  ? 0.1686  ? 0.0972  ? -0.5319 ? 0.2220  ? 
0.1314  ? 
2  'X-RAY DIFFRACTION' ? refined 22.5494 66.6544 98.2940  1.0618 ? 0.1984  ? 0.1087  ? 1.1837 ? -0.0743 ? 0.8617 ? 1.2339 ? 
-0.7807 ? -1.0909 ? 2.9302 ? 2.5442  ? 2.4450 ? -0.0305 ? 0.0533  ? -0.1553 ? 0.0232  ? -0.4799 ? 0.9237  ? -0.0363 ? -0.7899 ? 
0.4371  ? 
3  'X-RAY DIFFRACTION' ? refined 4.3009  92.5196 93.9402  1.5389 ? 0.5226  ? -0.0761 ? 1.9886 ? 0.0873  ? 1.5887 ? 1.9900 ? 1.8612 
? 0.6322  ? 6.0552 ? -0.9077 ? 2.8951 ? -0.3819 ? 0.7921  ? 1.2797  ? -0.3239 ? 0.1911  ? 0.8633  ? -0.9174 ? -1.2906 ? 0.2758  ? 
4  'X-RAY DIFFRACTION' ? refined 22.8200 86.6247 105.0549 1.2358 ? 0.3120  ? 0.2253  ? 1.1153 ? -0.1349 ? 0.8036 ? 2.6034 ? 0.6305 
? 0.3705  ? 2.6295 ? -0.4436 ? 3.4515 ? 0.2742  ? -0.4855 ? 0.6129  ? 0.1734  ? -0.2419 ? 0.6481  ? -0.9793 ? -0.5288 ? -0.0493 ? 
5  'X-RAY DIFFRACTION' ? refined 22.5229 94.0341 100.6088 1.7545 ? 0.3461  ? 0.1106  ? 1.0568 ? -0.1110 ? 1.1303 ? 1.7906 ? 
-1.9024 ? 0.1783  ? 5.6636 ? 0.7301  ? 0.9105 ? -0.1466 ? 0.1989  ? 0.4546  ? -0.2958 ? -0.1604 ? 1.3116  ? -1.1012 ? -0.2194 ? 
0.2950  ? 
6  'X-RAY DIFFRACTION' ? refined 47.5177 23.5157 64.2842  0.6565 ? 0.0447  ? 0.1403  ? 0.4255 ? 0.0669  ? 0.5816 ? 1.8940 ? 
-0.1701 ? 0.0152  ? 2.0919 ? 0.3875  ? 2.0755 ? -0.1246 ? -0.2037 ? -0.4731 ? 0.1841  ? 0.0884  ? 0.0497  ? 0.2184  ? 0.1195  ? 
0.0120  ? 
7  'X-RAY DIFFRACTION' ? refined 34.7845 19.3381 45.6642  0.9855 ? -0.0285 ? -0.0436 ? 0.7113 ? -0.1146 ? 0.7551 ? 4.4982 ? 
-0.4115 ? -2.5497 ? 2.9796 ? -0.5979 ? 7.4492 ? -0.5289 ? 0.9333  ? -0.5500 ? -0.5227 ? 0.0646  ? -0.1654 ? 0.7461  ? -0.9999 ? 
0.4440  ? 
8  'X-RAY DIFFRACTION' ? refined 29.9135 24.3829 61.2734  0.7242 ? -0.0173 ? 0.1099  ? 0.5742 ? 0.0439  ? 0.8213 ? 2.9025 ? 0.2486 
? 0.1747  ? 3.6265 ? -0.5224 ? 1.9674 ? -0.0847 ? 0.1569  ? -0.1294 ? -0.4263 ? 0.2330  ? 0.8899  ? -0.1835 ? -0.3996 ? -0.0331 ? 
9  'X-RAY DIFFRACTION' ? refined 49.5095 12.2356 49.0791  0.9072 ? -0.0391 ? 0.1559  ? 0.5783 ? -0.0609 ? 0.8523 ? 2.6367 ? 
-1.8643 ? -0.5507 ? 1.3218 ? 0.7066  ? 2.8081 ? 0.0691  ? 0.1994  ? -0.3960 ? -0.5630 ? -0.0605 ? -0.4190 ? 0.3346  ? 0.1059  ? 
0.0724  ? 
10 'X-RAY DIFFRACTION' ? refined 67.3154 6.8782  29.7620  1.2837 ? 0.1453  ? 0.2057  ? 0.9255 ? -0.0066 ? 1.0097 ? 1.3095 ? 
-0.0731 ? -1.2064 ? 1.1035 ? 2.0085  ? 5.0944 ? -0.2692 ? 0.3993  ? -0.0779 ? -0.2977 ? 0.2338  ? 0.0764  ? 0.1896  ? 0.6602  ? 
-0.0266 ? 
11 'X-RAY DIFFRACTION' ? refined 53.7138 -4.9817 33.1341  1.4849 ? 0.0292  ? 0.2343  ? 0.8451 ? -0.1847 ? 1.3263 ? 2.8966 ? 0.6564 
? -0.5001 ? 2.7783 ? -0.9443 ? 4.3528 ? -0.2850 ? 0.6652  ? -0.8220 ? -0.3359 ? -0.2286 ? 0.7828  ? 1.2153  ? -0.1834 ? 0.4076  ? 
12 'X-RAY DIFFRACTION' ? refined 63.7017 -5.8490 19.9902  1.9028 ? 0.1945  ? 0.1881  ? 1.2635 ? -0.2240 ? 1.1347 ? 2.6126 ? 0.0936 
? -0.5906 ? 3.7258 ? 0.4701  ? 5.0569 ? -0.1785 ? 1.0634  ? -0.7953 ? -1.3376 ? -0.0915 ? 0.5324  ? 1.2541  ? 0.0772  ? 0.2801  ? 
13 'X-RAY DIFFRACTION' ? refined 54.1753 -3.6591 21.3744  1.5531 ? 0.0201  ? -0.0027 ? 1.2235 ? -0.3655 ? 1.2728 ? 1.1795 ? 
-1.3038 ? -0.6294 ? 5.8673 ? 4.8263  ? 7.7468 ? -0.2496 ? 1.2370  ? -0.7785 ? -0.6235 ? -0.4421 ? 1.0529  ? 0.8514  ? 0.2353  ? 
0.6976  ? 
# 
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 300 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 301 through 373 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 374 through 407 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 408 through 528 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 529 through 561 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 42 through 190 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 191 through 236 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 237 through 283 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 284 through 318 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 319 through 426 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 427 through 497 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 498 through 528 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 529 through 561 )
;
# 
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 THR 562 ? A THR 535 
18  1 Y 1 A GLY 563 ? A GLY 536 
19  1 Y 1 A ASP 564 ? A ASP 537 
20  1 Y 1 A ASP 565 ? A ASP 538 
21  1 Y 1 A GLY 566 ? A GLY 539 
22  1 Y 1 A TYR 567 ? A TYR 540 
23  1 Y 1 A VAL 568 ? A VAL 541 
24  1 Y 1 A SER 569 ? A SER 542 
25  1 Y 1 A ASP 570 ? A ASP 543 
26  1 Y 1 A THR 571 ? A THR 544 
27  1 Y 1 A GLU 572 ? A GLU 545 
28  1 Y 1 A THR 573 ? A THR 546 
29  1 Y 1 A SER 574 ? A SER 547 
30  1 Y 1 A VAL 575 ? A VAL 548 
31  1 Y 1 A VAL 576 ? A VAL 549 
32  1 Y 1 A TRP 577 ? A TRP 550 
33  1 Y 1 A ASN 578 ? A ASN 551 
34  1 Y 1 A ASN 579 ? A ASN 552 
35  1 Y 1 A GLU 580 ? A GLU 553 
36  1 Y 1 A HIS 581 ? A HIS 554 
37  1 Y 1 A VAL 582 ? A VAL 555 
38  1 Y 1 A LYS 583 ? A LYS 556 
39  1 Y 1 A THR 584 ? A THR 557 
40  1 Y 1 A ASP 585 ? A ASP 558 
41  1 Y 1 A TRP 586 ? A TRP 559 
42  1 Y 1 A ASP 587 ? A ASP 560 
43  1 Y 1 A ARG 588 ? A ARG 561 
44  1 Y 1 A ALA 589 ? A ALA 562 
45  1 Y 1 A LYS 590 ? A LYS 563 
46  1 Y 1 A SER 591 ? A SER 564 
47  1 Y 1 A GLN 592 ? A GLN 565 
48  1 Y 1 A LYS 593 ? A LYS 566 
49  1 Y 1 A MET 594 ? A MET 567 
50  1 Y 1 A ARG 595 ? A ARG 568 
51  1 Y 1 A GLU 596 ? A GLU 569 
52  1 Y 1 A GLN 597 ? A GLN 570 
53  1 Y 1 A GLN 598 ? A GLN 571 
54  1 Y 1 A ALA 599 ? A ALA 572 
55  1 Y 1 A LEU 600 ? A LEU 573 
56  1 Y 1 A SER 601 ? A SER 574 
57  1 Y 1 A ARG 602 ? A ARG 575 
58  1 Y 1 A GLU 603 ? A GLU 576 
59  1 Y 1 A ALA 604 ? A ALA 577 
60  1 Y 1 A LYS 605 ? A LYS 578 
61  1 Y 1 A ASN 606 ? A ASN 579 
62  1 Y 1 A SER 607 ? A SER 580 
63  1 Y 1 A ASP 608 ? A ASP 581 
64  1 Y 1 A VAL 609 ? A VAL 582 
65  1 Y 1 A LEU 610 ? A LEU 583 
66  1 Y 1 A GLN 611 ? A GLN 584 
67  1 Y 1 A SER 612 ? A SER 585 
68  1 Y 1 A PRO 613 ? A PRO 586 
69  1 Y 1 A LEU 614 ? A LEU 587 
70  1 Y 1 A ASP 615 ? A ASP 588 
71  1 Y 1 A SER 616 ? A SER 589 
72  1 Y 1 A ALA 617 ? A ALA 590 
73  1 Y 1 A ALA 618 ? A ALA 591 
74  1 Y 1 A ALA 619 ? A ALA 592 
75  1 Y 1 A ALA 620 ? A ALA 593 
76  1 Y 1 A ALA 621 ? A ALA 594 
77  1 Y 1 B GLY 28  ? B GLY 1   
78  1 Y 1 B SER 29  ? B SER 2   
79  1 Y 1 B ALA 30  ? B ALA 3   
80  1 Y 1 B PRO 31  ? B PRO 4   
81  1 Y 1 B PRO 32  ? B PRO 5   
82  1 Y 1 B GLY 33  ? B GLY 6   
83  1 Y 1 B ALA 34  ? B ALA 7   
84  1 Y 1 B ASP 35  ? B ASP 8   
85  1 Y 1 B ALA 36  ? B ALA 9   
86  1 Y 1 B TYR 37  ? B TYR 10  
87  1 Y 1 B PHE 38  ? B PHE 11  
88  1 Y 1 B PRO 39  ? B PRO 12  
89  1 Y 1 B GLU 40  ? B GLU 13  
90  1 Y 1 B GLU 41  ? B GLU 14  
91  1 Y 1 B THR 562 ? B THR 535 
92  1 Y 1 B GLY 563 ? B GLY 536 
93  1 Y 1 B ASP 564 ? B ASP 537 
94  1 Y 1 B ASP 565 ? B ASP 538 
95  1 Y 1 B GLY 566 ? B GLY 539 
96  1 Y 1 B TYR 567 ? B TYR 540 
97  1 Y 1 B VAL 568 ? B VAL 541 
98  1 Y 1 B SER 569 ? B SER 542 
99  1 Y 1 B ASP 570 ? B ASP 543 
100 1 Y 1 B THR 571 ? B THR 544 
101 1 Y 1 B GLU 572 ? B GLU 545 
102 1 Y 1 B THR 573 ? B THR 546 
103 1 Y 1 B SER 574 ? B SER 547 
104 1 Y 1 B VAL 575 ? B VAL 548 
105 1 Y 1 B VAL 576 ? B VAL 549 
106 1 Y 1 B TRP 577 ? B TRP 550 
107 1 Y 1 B ASN 578 ? B ASN 551 
108 1 Y 1 B ASN 579 ? B ASN 552 
109 1 Y 1 B GLU 580 ? B GLU 553 
110 1 Y 1 B HIS 581 ? B HIS 554 
111 1 Y 1 B VAL 582 ? B VAL 555 
112 1 Y 1 B LYS 583 ? B LYS 556 
113 1 Y 1 B THR 584 ? B THR 557 
114 1 Y 1 B ASP 585 ? B ASP 558 
115 1 Y 1 B TRP 586 ? B TRP 559 
116 1 Y 1 B ASP 587 ? B ASP 560 
117 1 Y 1 B ARG 588 ? B ARG 561 
118 1 Y 1 B ALA 589 ? B ALA 562 
119 1 Y 1 B LYS 590 ? B LYS 563 
120 1 Y 1 B SER 591 ? B SER 564 
121 1 Y 1 B GLN 592 ? B GLN 565 
122 1 Y 1 B LYS 593 ? B LYS 566 
123 1 Y 1 B MET 594 ? B MET 567 
124 1 Y 1 B ARG 595 ? B ARG 568 
125 1 Y 1 B GLU 596 ? B GLU 569 
126 1 Y 1 B GLN 597 ? B GLN 570 
127 1 Y 1 B GLN 598 ? B GLN 571 
128 1 Y 1 B ALA 599 ? B ALA 572 
129 1 Y 1 B LEU 600 ? B LEU 573 
130 1 Y 1 B SER 601 ? B SER 574 
131 1 Y 1 B ARG 602 ? B ARG 575 
132 1 Y 1 B GLU 603 ? B GLU 576 
133 1 Y 1 B ALA 604 ? B ALA 577 
134 1 Y 1 B LYS 605 ? B LYS 578 
135 1 Y 1 B ASN 606 ? B ASN 579 
136 1 Y 1 B SER 607 ? B SER 580 
137 1 Y 1 B ASP 608 ? B ASP 581 
138 1 Y 1 B VAL 609 ? B VAL 582 
139 1 Y 1 B LEU 610 ? B LEU 583 
140 1 Y 1 B GLN 611 ? B GLN 584 
141 1 Y 1 B SER 612 ? B SER 585 
142 1 Y 1 B PRO 613 ? B PRO 586 
143 1 Y 1 B LEU 614 ? B LEU 587 
144 1 Y 1 B ASP 615 ? B ASP 588 
145 1 Y 1 B SER 616 ? B SER 589 
146 1 Y 1 B ALA 617 ? B ALA 590 
147 1 Y 1 B ALA 618 ? B ALA 591 
148 1 Y 1 B ALA 619 ? B ALA 592 
149 1 Y 1 B ALA 620 ? B ALA 593 
150 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 
HG  HG     HG N N 199 
HIS N      N  N N 200 
HIS CA     C  N S 201 
HIS C      C  N N 202 
HIS O      O  N N 203 
HIS CB     C  N N 204 
HIS CG     C  Y N 205 
HIS ND1    N  Y N 206 
HIS CD2    C  Y N 207 
HIS CE1    C  Y N 208 
HIS NE2    N  Y N 209 
HIS OXT    O  N N 210 
HIS H      H  N N 211 
HIS H2     H  N N 212 
HIS HA     H  N N 213 
HIS HB2    H  N N 214 
HIS HB3    H  N N 215 
HIS HD1    H  N N 216 
HIS HD2    H  N N 217 
HIS HE1    H  N N 218 
HIS HE2    H  N N 219 
HIS HXT    H  N N 220 
HOH O      O  N N 221 
HOH H1     H  N N 222 
HOH H2     H  N N 223 
ILE N      N  N N 224 
ILE CA     C  N S 225 
ILE C      C  N N 226 
ILE O      O  N N 227 
ILE CB     C  N S 228 
ILE CG1    C  N N 229 
ILE CG2    C  N N 230 
ILE CD1    C  N N 231 
ILE OXT    O  N N 232 
ILE H      H  N N 233 
ILE H2     H  N N 234 
ILE HA     H  N N 235 
ILE HB     H  N N 236 
ILE HG12   H  N N 237 
ILE HG13   H  N N 238 
ILE HG21   H  N N 239 
ILE HG22   H  N N 240 
ILE HG23   H  N N 241 
ILE HD11   H  N N 242 
ILE HD12   H  N N 243 
ILE HD13   H  N N 244 
ILE HXT    H  N N 245 
LEU N      N  N N 246 
LEU CA     C  N S 247 
LEU C      C  N N 248 
LEU O      O  N N 249 
LEU CB     C  N N 250 
LEU CG     C  N N 251 
LEU CD1    C  N N 252 
LEU CD2    C  N N 253 
LEU OXT    O  N N 254 
LEU H      H  N N 255 
LEU H2     H  N N 256 
LEU HA     H  N N 257 
LEU HB2    H  N N 258 
LEU HB3    H  N N 259 
LEU HG     H  N N 260 
LEU HD11   H  N N 261 
LEU HD12   H  N N 262 
LEU HD13   H  N N 263 
LEU HD21   H  N N 264 
LEU HD22   H  N N 265 
LEU HD23   H  N N 266 
LEU HXT    H  N N 267 
LYS N      N  N N 268 
LYS CA     C  N S 269 
LYS C      C  N N 270 
LYS O      O  N N 271 
LYS CB     C  N N 272 
LYS CG     C  N N 273 
LYS CD     C  N N 274 
LYS CE     C  N N 275 
LYS NZ     N  N N 276 
LYS OXT    O  N N 277 
LYS H      H  N N 278 
LYS H2     H  N N 279 
LYS HA     H  N N 280 
LYS HB2    H  N N 281 
LYS HB3    H  N N 282 
LYS HG2    H  N N 283 
LYS HG3    H  N N 284 
LYS HD2    H  N N 285 
LYS HD3    H  N N 286 
LYS HE2    H  N N 287 
LYS HE3    H  N N 288 
LYS HZ1    H  N N 289 
LYS HZ2    H  N N 290 
LYS HZ3    H  N N 291 
LYS HXT    H  N N 292 
MES O1     O  N N 293 
MES C2     C  N N 294 
MES C3     C  N N 295 
MES N4     N  N N 296 
MES C5     C  N N 297 
MES C6     C  N N 298 
MES C7     C  N N 299 
MES C8     C  N N 300 
MES S      S  N N 301 
MES O1S    O  N N 302 
MES O2S    O  N N 303 
MES O3S    O  N N 304 
MES H21    H  N N 305 
MES H22    H  N N 306 
MES H31    H  N N 307 
MES H32    H  N N 308 
MES HN4    H  N N 309 
MES H51    H  N N 310 
MES H52    H  N N 311 
MES H61    H  N N 312 
MES H62    H  N N 313 
MES H71    H  N N 314 
MES H72    H  N N 315 
MES H81    H  N N 316 
MES H82    H  N N 317 
MET N      N  N N 318 
MET CA     C  N S 319 
MET C      C  N N 320 
MET O      O  N N 321 
MET CB     C  N N 322 
MET CG     C  N N 323 
MET SD     S  N N 324 
MET CE     C  N N 325 
MET OXT    O  N N 326 
MET H      H  N N 327 
MET H2     H  N N 328 
MET HA     H  N N 329 
MET HB2    H  N N 330 
MET HB3    H  N N 331 
MET HG2    H  N N 332 
MET HG3    H  N N 333 
MET HE1    H  N N 334 
MET HE2    H  N N 335 
MET HE3    H  N N 336 
MET HXT    H  N N 337 
PHE N      N  N N 338 
PHE CA     C  N S 339 
PHE C      C  N N 340 
PHE O      O  N N 341 
PHE CB     C  N N 342 
PHE CG     C  Y N 343 
PHE CD1    C  Y N 344 
PHE CD2    C  Y N 345 
PHE CE1    C  Y N 346 
PHE CE2    C  Y N 347 
PHE CZ     C  Y N 348 
PHE OXT    O  N N 349 
PHE H      H  N N 350 
PHE H2     H  N N 351 
PHE HA     H  N N 352 
PHE HB2    H  N N 353 
PHE HB3    H  N N 354 
PHE HD1    H  N N 355 
PHE HD2    H  N N 356 
PHE HE1    H  N N 357 
PHE HE2    H  N N 358 
PHE HZ     H  N N 359 
PHE HXT    H  N N 360 
PRO N      N  N N 361 
PRO CA     C  N S 362 
PRO C      C  N N 363 
PRO O      O  N N 364 
PRO CB     C  N N 365 
PRO CG     C  N N 366 
PRO CD     C  N N 367 
PRO OXT    O  N N 368 
PRO H      H  N N 369 
PRO HA     H  N N 370 
PRO HB2    H  N N 371 
PRO HB3    H  N N 372 
PRO HG2    H  N N 373 
PRO HG3    H  N N 374 
PRO HD2    H  N N 375 
PRO HD3    H  N N 376 
PRO HXT    H  N N 377 
SER N      N  N N 378 
SER CA     C  N S 379 
SER C      C  N N 380 
SER O      O  N N 381 
SER CB     C  N N 382 
SER OG     O  N N 383 
SER OXT    O  N N 384 
SER H      H  N N 385 
SER H2     H  N N 386 
SER HA     H  N N 387 
SER HB2    H  N N 388 
SER HB3    H  N N 389 
SER HG     H  N N 390 
SER HXT    H  N N 391 
THR N      N  N N 392 
THR CA     C  N S 393 
THR C      C  N N 394 
THR O      O  N N 395 
THR CB     C  N R 396 
THR OG1    O  N N 397 
THR CG2    C  N N 398 
THR OXT    O  N N 399 
THR H      H  N N 400 
THR H2     H  N N 401 
THR HA     H  N N 402 
THR HB     H  N N 403 
THR HG1    H  N N 404 
THR HG21   H  N N 405 
THR HG22   H  N N 406 
THR HG23   H  N N 407 
THR HXT    H  N N 408 
TRP N      N  N N 409 
TRP CA     C  N S 410 
TRP C      C  N N 411 
TRP O      O  N N 412 
TRP CB     C  N N 413 
TRP CG     C  Y N 414 
TRP CD1    C  Y N 415 
TRP CD2    C  Y N 416 
TRP NE1    N  Y N 417 
TRP CE2    C  Y N 418 
TRP CE3    C  Y N 419 
TRP CZ2    C  Y N 420 
TRP CZ3    C  Y N 421 
TRP CH2    C  Y N 422 
TRP OXT    O  N N 423 
TRP H      H  N N 424 
TRP H2     H  N N 425 
TRP HA     H  N N 426 
TRP HB2    H  N N 427 
TRP HB3    H  N N 428 
TRP HD1    H  N N 429 
TRP HE1    H  N N 430 
TRP HE3    H  N N 431 
TRP HZ2    H  N N 432 
TRP HZ3    H  N N 433 
TRP HH2    H  N N 434 
TRP HXT    H  N N 435 
TYR N      N  N N 436 
TYR CA     C  N S 437 
TYR C      C  N N 438 
TYR O      O  N N 439 
TYR CB     C  N N 440 
TYR CG     C  Y N 441 
TYR CD1    C  Y N 442 
TYR CD2    C  Y N 443 
TYR CE1    C  Y N 444 
TYR CE2    C  Y N 445 
TYR CZ     C  Y N 446 
TYR OH     O  N N 447 
TYR OXT    O  N N 448 
TYR H      H  N N 449 
TYR H2     H  N N 450 
TYR HA     H  N N 451 
TYR HB2    H  N N 452 
TYR HB3    H  N N 453 
TYR HD1    H  N N 454 
TYR HD2    H  N N 455 
TYR HE1    H  N N 456 
TYR HE2    H  N N 457 
TYR HH     H  N N 458 
TYR HXT    H  N N 459 
VAL N      N  N N 460 
VAL CA     C  N S 461 
VAL C      C  N N 462 
VAL O      O  N N 463 
VAL CB     C  N N 464 
VAL CG1    C  N N 465 
VAL CG2    C  N N 466 
VAL OXT    O  N N 467 
VAL H      H  N N 468 
VAL H2     H  N N 469 
VAL HA     H  N N 470 
VAL HB     H  N N 471 
VAL HG11   H  N N 472 
VAL HG12   H  N N 473 
VAL HG13   H  N N 474 
VAL HG21   H  N N 475 
VAL HG22   H  N N 476 
VAL HG23   H  N N 477 
VAL HXT    H  N N 478 
# 
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 
VAL N     CA     sing N N 445 
VAL N     H      sing N N 446 
VAL N     H2     sing N N 447 
VAL CA    C      sing N N 448 
VAL CA    CB     sing N N 449 
VAL CA    HA     sing N N 450 
VAL C     O      doub N N 451 
VAL C     OXT    sing N N 452 
VAL CB    CG1    sing N N 453 
VAL CB    CG2    sing N N 454 
VAL CB    HB     sing N N 455 
VAL CG1   HG11   sing N N 456 
VAL CG1   HG12   sing N N 457 
VAL CG1   HG13   sing N N 458 
VAL CG2   HG21   sing N N 459 
VAL CG2   HG22   sing N N 460 
VAL CG2   HG23   sing N N 461 
VAL OXT   HXT    sing N N 462 
# 
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 
'Other private'                            'United States' ?              5 
# 
_atom_sites.entry_id                    9EVL 
_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]   0.004542 
_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]   0.004542 
_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]   0.004542 
_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 
HG 
MN 
N  
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  ? 25.631  35.026  49.736  1.00 140.72 ? 44  SER A N     1 
ATOM   2    C  CA    . SER A 1 17  ? 25.593  34.925  51.192  1.00 151.40 ? 44  SER A CA    1 
ATOM   3    C  C     . SER A 1 17  ? 26.327  36.099  51.839  1.00 157.61 ? 44  SER A C     1 
ATOM   4    O  O     . SER A 1 17  ? 27.428  36.455  51.418  1.00 154.41 ? 44  SER A O     1 
ATOM   5    C  CB    . SER A 1 17  ? 26.199  33.599  51.653  1.00 145.91 ? 44  SER A CB    1 
ATOM   6    O  OG    . SER A 1 17  ? 26.066  33.440  53.056  1.00 144.48 ? 44  SER A OG    1 
ATOM   7    N  N     . PRO A 1 18  ? 25.714  36.701  52.863  1.00 139.26 ? 45  PRO A N     1 
ATOM   8    C  CA    . PRO A 1 18  ? 26.299  37.901  53.476  1.00 128.83 ? 45  PRO A CA    1 
ATOM   9    C  C     . PRO A 1 18  ? 27.199  37.598  54.664  1.00 113.00 ? 45  PRO A C     1 
ATOM   10   O  O     . PRO A 1 18  ? 26.834  36.823  55.554  1.00 116.17 ? 45  PRO A O     1 
ATOM   11   C  CB    . PRO A 1 18  ? 25.061  38.694  53.906  1.00 120.27 ? 45  PRO A CB    1 
ATOM   12   C  CG    . PRO A 1 18  ? 24.076  37.620  54.275  1.00 134.53 ? 45  PRO A CG    1 
ATOM   13   C  CD    . PRO A 1 18  ? 24.369  36.417  53.392  1.00 131.09 ? 45  PRO A CD    1 
ATOM   14   N  N     . GLU A 1 19  ? 28.378  38.212  54.690  1.00 85.99  ? 46  GLU A N     1 
ATOM   15   C  CA    . GLU A 1 19  ? 29.262  38.069  55.836  1.00 84.04  ? 46  GLU A CA    1 
ATOM   16   C  C     . GLU A 1 19  ? 28.674  38.790  57.041  1.00 78.09  ? 46  GLU A C     1 
ATOM   17   O  O     . GLU A 1 19  ? 28.111  39.881  56.918  1.00 102.66 ? 46  GLU A O     1 
ATOM   18   C  CB    . GLU A 1 19  ? 30.651  38.622  55.513  1.00 75.40  ? 46  GLU A CB    1 
ATOM   19   C  CG    . GLU A 1 19  ? 31.423  37.787  54.502  1.00 96.63  ? 46  GLU A CG    1 
ATOM   20   C  CD    . GLU A 1 19  ? 31.799  36.419  55.043  1.00 87.45  ? 46  GLU A CD    1 
ATOM   21   O  OE1   . GLU A 1 19  ? 32.392  36.361  56.142  1.00 86.05  ? 46  GLU A OE1   1 
ATOM   22   O  OE2   . GLU A 1 19  ? 31.493  35.407  54.374  1.00 76.78  ? 46  GLU A OE2   1 
ATOM   23   N  N     . SER A 1 20  ? 28.801  38.171  58.211  1.00 76.72  ? 47  SER A N     1 
ATOM   24   C  CA    . SER A 1 20  ? 28.290  38.768  59.431  1.00 71.45  ? 47  SER A CA    1 
ATOM   25   C  C     . SER A 1 20  ? 29.119  39.995  59.799  1.00 65.21  ? 47  SER A C     1 
ATOM   26   O  O     . SER A 1 20  ? 30.232  40.175  59.300  1.00 71.46  ? 47  SER A O     1 
ATOM   27   C  CB    . SER A 1 20  ? 28.313  37.750  60.571  1.00 82.78  ? 47  SER A CB    1 
ATOM   28   O  OG    . SER A 1 20  ? 29.632  37.310  60.844  1.00 81.10  ? 47  SER A OG    1 
ATOM   29   N  N     . PRO A 1 21  ? 28.591  40.867  60.658  1.00 64.58  ? 48  PRO A N     1 
ATOM   30   C  CA    . PRO A 1 21  ? 29.394  42.001  61.128  1.00 76.64  ? 48  PRO A CA    1 
ATOM   31   C  C     . PRO A 1 21  ? 30.613  41.527  61.904  1.00 71.34  ? 48  PRO A C     1 
ATOM   32   O  O     . PRO A 1 21  ? 30.615  40.455  62.513  1.00 73.64  ? 48  PRO A O     1 
ATOM   33   C  CB    . PRO A 1 21  ? 28.429  42.776  62.033  1.00 62.40  ? 48  PRO A CB    1 
ATOM   34   C  CG    . PRO A 1 21  ? 27.080  42.358  61.601  1.00 65.36  ? 48  PRO A CG    1 
ATOM   35   C  CD    . PRO A 1 21  ? 27.203  40.938  61.144  1.00 66.46  ? 48  PRO A CD    1 
ATOM   36   N  N     . LEU A 1 22  ? 31.664  42.336  61.862  1.00 63.73  ? 49  LEU A N     1 
ATOM   37   C  CA    . LEU A 1 22  ? 32.805  42.099  62.726  1.00 65.70  ? 49  LEU A CA    1 
ATOM   38   C  C     . LEU A 1 22  ? 32.414  42.342  64.176  1.00 59.71  ? 49  LEU A C     1 
ATOM   39   O  O     . LEU A 1 22  ? 31.514  43.129  64.477  1.00 76.63  ? 49  LEU A O     1 
ATOM   40   C  CB    . LEU A 1 22  ? 33.970  43.007  62.342  1.00 60.36  ? 49  LEU A CB    1 
ATOM   41   C  CG    . LEU A 1 22  ? 34.494  42.850  60.917  1.00 61.16  ? 49  LEU A CG    1 
ATOM   42   C  CD1   . LEU A 1 22  ? 35.646  43.806  60.682  1.00 53.81  ? 49  LEU A CD1   1 
ATOM   43   C  CD2   . LEU A 1 22  ? 34.918  41.412  60.664  1.00 68.82  ? 49  LEU A CD2   1 
ATOM   44   N  N     . GLN A 1 23  ? 33.093  41.645  65.080  1.00 68.36  ? 50  GLN A N     1 
ATOM   45   C  CA    . GLN A 1 23  ? 32.904  41.912  66.494  1.00 61.47  ? 50  GLN A CA    1 
ATOM   46   C  C     . GLN A 1 23  ? 33.563  43.239  66.862  1.00 59.17  ? 50  GLN A C     1 
ATOM   47   O  O     . GLN A 1 23  ? 34.380  43.786  66.115  1.00 70.54  ? 50  GLN A O     1 
ATOM   48   C  CB    . GLN A 1 23  ? 33.479  40.774  67.335  1.00 54.67  ? 50  GLN A CB    1 
ATOM   49   C  CG    . GLN A 1 23  ? 32.792  39.435  67.126  1.00 70.38  ? 50  GLN A CG    1 
ATOM   50   C  CD    . GLN A 1 23  ? 33.212  38.398  68.156  1.00 74.14  ? 50  GLN A CD    1 
ATOM   51   O  OE1   . GLN A 1 23  ? 33.027  38.588  69.358  1.00 73.70  ? 50  GLN A OE1   1 
ATOM   52   N  NE2   . GLN A 1 23  ? 33.790  37.298  67.686  1.00 69.36  ? 50  GLN A NE2   1 
ATOM   53   N  N     . ALA A 1 24  ? 33.194  43.765  68.024  1.00 57.13  ? 51  ALA A N     1 
ATOM   54   C  CA    . ALA A 1 24  ? 33.790  45.010  68.478  1.00 59.93  ? 51  ALA A CA    1 
ATOM   55   C  C     . ALA A 1 24  ? 35.251  44.780  68.863  1.00 72.64  ? 51  ALA A C     1 
ATOM   56   O  O     . ALA A 1 24  ? 35.641  43.657  69.203  1.00 70.25  ? 51  ALA A O     1 
ATOM   57   C  CB    . ALA A 1 24  ? 33.021  45.577  69.666  1.00 63.74  ? 51  ALA A CB    1 
ATOM   58   N  N     . PRO A 1 25  ? 36.081  45.823  68.800  1.00 66.81  ? 52  PRO A N     1 
ATOM   59   C  CA    . PRO A 1 25  ? 37.501  45.656  69.134  1.00 64.67  ? 52  PRO A CA    1 
ATOM   60   C  C     . PRO A 1 25  ? 37.699  45.244  70.583  1.00 71.07  ? 52  PRO A C     1 
ATOM   61   O  O     . PRO A 1 25  ? 36.934  45.621  71.474  1.00 66.92  ? 52  PRO A O     1 
ATOM   62   C  CB    . PRO A 1 25  ? 38.094  47.041  68.865  1.00 62.03  ? 52  PRO A CB    1 
ATOM   63   C  CG    . PRO A 1 25  ? 37.175  47.639  67.841  1.00 57.56  ? 52  PRO A CG    1 
ATOM   64   C  CD    . PRO A 1 25  ? 35.807  47.135  68.192  1.00 65.90  ? 52  PRO A CD    1 
ATOM   65   N  N     . ARG A 1 26  ? 38.751  44.459  70.804  1.00 66.51  ? 53  ARG A N     1 
ATOM   66   C  CA    . ARG A 1 26  ? 39.074  43.946  72.128  1.00 68.59  ? 53  ARG A CA    1 
ATOM   67   C  C     . ARG A 1 26  ? 39.790  45.023  72.934  1.00 68.05  ? 53  ARG A C     1 
ATOM   68   O  O     . ARG A 1 26  ? 40.863  45.488  72.536  1.00 72.35  ? 53  ARG A O     1 
ATOM   69   C  CB    . ARG A 1 26  ? 39.933  42.690  72.000  1.00 75.95  ? 53  ARG A CB    1 
ATOM   70   C  CG    . ARG A 1 26  ? 39.210  41.509  71.352  1.00 73.04  ? 53  ARG A CG    1 
ATOM   71   C  CD    . ARG A 1 26  ? 40.102  40.751  70.369  1.00 69.43  ? 53  ARG A CD    1 
ATOM   72   N  NE    . ARG A 1 26  ? 40.250  41.484  69.118  1.00 72.51  ? 53  ARG A NE    1 
ATOM   73   C  CZ    . ARG A 1 26  ? 40.669  40.956  67.977  1.00 59.47  ? 53  ARG A CZ    1 
ATOM   74   N  NH1   . ARG A 1 26  ? 41.031  39.686  67.891  1.00 64.02  ? 53  ARG A NH1   1 
ATOM   75   N  NH2   . ARG A 1 26  ? 40.707  41.718  66.889  1.00 76.93  ? 53  ARG A NH2   1 
ATOM   76   N  N     . VAL A 1 27  ? 39.200  45.418  74.062  1.00 66.43  ? 54  VAL A N     1 
ATOM   77   C  CA    . VAL A 1 27  ? 39.732  46.472  74.920  1.00 60.67  ? 54  VAL A CA    1 
ATOM   78   C  C     . VAL A 1 27  ? 40.033  45.892  76.298  1.00 73.45  ? 54  VAL A C     1 
ATOM   79   O  O     . VAL A 1 27  ? 39.169  45.257  76.916  1.00 73.14  ? 54  VAL A O     1 
ATOM   80   C  CB    . VAL A 1 27  ? 38.754  47.655  75.040  1.00 67.63  ? 54  VAL A CB    1 
ATOM   81   C  CG1   . VAL A 1 27  ? 39.322  48.735  75.957  1.00 62.38  ? 54  VAL A CG1   1 
ATOM   82   C  CG2   . VAL A 1 27  ? 38.443  48.229  73.672  1.00 81.07  ? 54  VAL A CG2   1 
ATOM   83   N  N     . LEU A 1 28  ? 41.255  46.111  76.777  1.00 71.40  ? 55  LEU A N     1 
ATOM   84   C  CA    . LEU A 1 28  ? 41.617  45.839  78.162  1.00 69.19  ? 55  LEU A CA    1 
ATOM   85   C  C     . LEU A 1 28  ? 41.593  47.158  78.925  1.00 70.03  ? 55  LEU A C     1 
ATOM   86   O  O     . LEU A 1 28  ? 42.264  48.118  78.532  1.00 72.32  ? 55  LEU A O     1 
ATOM   87   C  CB    . LEU A 1 28  ? 42.995  45.181  78.262  1.00 60.19  ? 55  LEU A CB    1 
ATOM   88   C  CG    . LEU A 1 28  ? 43.537  45.072  79.694  1.00 69.66  ? 55  LEU A CG    1 
ATOM   89   C  CD1   . LEU A 1 28  ? 42.715  44.096  80.516  1.00 73.47  ? 55  LEU A CD1   1 
ATOM   90   C  CD2   . LEU A 1 28  ? 44.999  44.682  79.718  1.00 69.56  ? 55  LEU A CD2   1 
ATOM   91   N  N     . ILE A 1 29  ? 40.813  47.211  79.998  1.00 66.39  ? 56  ILE A N     1 
ATOM   92   C  CA    . ILE A 1 29  ? 40.696  48.409  80.821  1.00 70.62  ? 56  ILE A CA    1 
ATOM   93   C  C     . ILE A 1 29  ? 41.643  48.264  82.004  1.00 69.87  ? 56  ILE A C     1 
ATOM   94   O  O     . ILE A 1 29  ? 41.493  47.346  82.821  1.00 72.84  ? 56  ILE A O     1 
ATOM   95   C  CB    . ILE A 1 29  ? 39.251  48.630  81.289  1.00 71.92  ? 56  ILE A CB    1 
ATOM   96   C  CG1   . ILE A 1 29  ? 38.324  48.787  80.081  1.00 64.59  ? 56  ILE A CG1   1 
ATOM   97   C  CG2   . ILE A 1 29  ? 39.168  49.851  82.189  1.00 62.32  ? 56  ILE A CG2   1 
ATOM   98   C  CD1   . ILE A 1 29  ? 36.888  49.086  80.460  1.00 65.34  ? 56  ILE A CD1   1 
ATOM   99   N  N     . ALA A 1 30  ? 42.628  49.154  82.085  1.00 75.02  ? 57  ALA A N     1 
ATOM   100  C  CA    . ALA A 1 30  ? 43.659  49.096  83.113  1.00 65.54  ? 57  ALA A CA    1 
ATOM   101  C  C     . ALA A 1 30  ? 43.334  50.103  84.203  1.00 66.90  ? 57  ALA A C     1 
ATOM   102  O  O     . ALA A 1 30  ? 43.153  51.293  83.923  1.00 79.85  ? 57  ALA A O     1 
ATOM   103  C  CB    . ALA A 1 30  ? 45.044  49.379  82.527  1.00 65.90  ? 57  ALA A CB    1 
ATOM   104  N  N     . LEU A 1 31  ? 43.272  49.627  85.443  1.00 75.72  ? 58  LEU A N     1 
ATOM   105  C  CA    . LEU A 1 31  ? 42.800  50.428  86.568  1.00 79.32  ? 58  LEU A CA    1 
ATOM   106  C  C     . LEU A 1 31  ? 43.775  50.289  87.735  1.00 77.60  ? 58  LEU A C     1 
ATOM   107  O  O     . LEU A 1 31  ? 43.779  49.268  88.430  1.00 71.39  ? 58  LEU A O     1 
ATOM   108  C  CB    . LEU A 1 31  ? 41.392  50.002  86.969  1.00 74.53  ? 58  LEU A CB    1 
ATOM   109  C  CG    . LEU A 1 31  ? 40.859  50.590  88.276  1.00 86.36  ? 58  LEU A CG    1 
ATOM   110  C  CD1   . LEU A 1 31  ? 40.717  52.097  88.162  1.00 98.34  ? 58  LEU A CD1   1 
ATOM   111  C  CD2   . LEU A 1 31  ? 39.537  49.947  88.652  1.00 98.49  ? 58  LEU A CD2   1 
ATOM   112  N  N     . LEU A 1 32  ? 44.602  51.311  87.945  1.00 77.21  ? 59  LEU A N     1 
ATOM   113  C  CA    . LEU A 1 32  ? 45.392  51.428  89.164  1.00 74.98  ? 59  LEU A CA    1 
ATOM   114  C  C     . LEU A 1 32  ? 44.562  52.163  90.209  1.00 77.04  ? 59  LEU A C     1 
ATOM   115  O  O     . LEU A 1 32  ? 43.986  53.216  89.918  1.00 77.41  ? 59  LEU A O     1 
ATOM   116  C  CB    . LEU A 1 32  ? 46.704  52.178  88.916  1.00 68.31  ? 59  LEU A CB    1 
ATOM   117  C  CG    . LEU A 1 32  ? 47.908  51.473  88.278  1.00 76.36  ? 59  LEU A CG    1 
ATOM   118  C  CD1   . LEU A 1 32  ? 47.684  51.167  86.795  1.00 57.58  ? 59  LEU A CD1   1 
ATOM   119  C  CD2   . LEU A 1 32  ? 49.165  52.308  88.472  1.00 85.85  ? 59  LEU A CD2   1 
ATOM   120  N  N     . ALA A 1 33  ? 44.502  51.615  91.421  1.00 68.78  ? 60  ALA A N     1 
ATOM   121  C  CA    . ALA A 1 33  ? 43.660  52.185  92.466  1.00 73.31  ? 60  ALA A CA    1 
ATOM   122  C  C     . ALA A 1 33  ? 44.427  52.228  93.779  1.00 85.72  ? 60  ALA A C     1 
ATOM   123  O  O     . ALA A 1 33  ? 44.816  51.182  94.307  1.00 75.94  ? 60  ALA A O     1 
ATOM   124  C  CB    . ALA A 1 33  ? 42.363  51.383  92.624  1.00 80.55  ? 60  ALA A CB    1 
ATOM   125  N  N     . ARG A 1 34  ? 44.644  53.436  94.300  1.00 81.17  ? 61  ARG A N     1 
ATOM   126  C  CA    . ARG A 1 34  ? 45.178  53.639  95.643  1.00 78.58  ? 61  ARG A CA    1 
ATOM   127  C  C     . ARG A 1 34  ? 44.318  54.678  96.341  1.00 83.78  ? 61  ARG A C     1 
ATOM   128  O  O     . ARG A 1 34  ? 44.139  55.783  95.817  1.00 77.12  ? 61  ARG A O     1 
ATOM   129  C  CB    . ARG A 1 34  ? 46.639  54.101  95.618  1.00 73.56  ? 61  ARG A CB    1 
ATOM   130  C  CG    . ARG A 1 34  ? 47.225  54.306  97.010  1.00 77.27  ? 61  ARG A CG    1 
ATOM   131  C  CD    . ARG A 1 34  ? 48.555  55.051  96.997  1.00 67.55  ? 61  ARG A CD    1 
ATOM   132  N  NE    . ARG A 1 34  ? 49.102  55.169  98.344  1.00 84.93  ? 61  ARG A NE    1 
ATOM   133  C  CZ    . ARG A 1 34  ? 50.144  55.920  98.679  1.00 86.18  ? 61  ARG A CZ    1 
ATOM   134  N  NH1   . ARG A 1 34  ? 50.798  56.638  97.781  1.00 84.80  ? 61  ARG A NH1   1 
ATOM   135  N  NH2   . ARG A 1 34  ? 50.534  55.960  99.951  1.00 85.58  ? 61  ARG A NH2   1 
ATOM   136  N  N     . ASN A 1 35  ? 43.798  54.325  97.517  1.00 80.00  ? 62  ASN A N     1 
ATOM   137  C  CA    . ASN A 1 35  ? 42.980  55.220  98.335  1.00 81.03  ? 62  ASN A CA    1 
ATOM   138  C  C     . ASN A 1 35  ? 41.886  55.882  97.497  1.00 85.03  ? 62  ASN A C     1 
ATOM   139  O  O     . ASN A 1 35  ? 41.809  57.106  97.368  1.00 82.20  ? 62  ASN A O     1 
ATOM   140  C  CB    . ASN A 1 35  ? 43.857  56.266  99.026  1.00 72.45  ? 62  ASN A CB    1 
ATOM   141  C  CG    . ASN A 1 35  ? 44.814  55.657  100.023 1.00 87.80  ? 62  ASN A CG    1 
ATOM   142  O  OD1   . ASN A 1 35  ? 44.408  54.925  100.924 1.00 92.49  ? 62  ASN A OD1   1 
ATOM   143  N  ND2   . ASN A 1 35  ? 46.096  55.954  99.867  1.00 94.24  ? 62  ASN A ND2   1 
ATOM   144  N  N     . ALA A 1 36  ? 41.037  55.036  96.908  1.00 85.01  ? 63  ALA A N     1 
ATOM   145  C  CA    . ALA A 1 36  ? 40.020  55.497  95.972  1.00 84.59  ? 63  ALA A CA    1 
ATOM   146  C  C     . ALA A 1 36  ? 38.631  54.983  96.329  1.00 83.99  ? 63  ALA A C     1 
ATOM   147  O  O     . ALA A 1 36  ? 37.714  55.075  95.506  1.00 94.99  ? 63  ALA A O     1 
ATOM   148  C  CB    . ALA A 1 36  ? 40.380  55.086  94.544  1.00 75.03  ? 63  ALA A CB    1 
ATOM   149  N  N     . ALA A 1 37  ? 38.454  54.449  97.540  1.00 82.76  ? 64  ALA A N     1 
ATOM   150  C  CA    . ALA A 1 37  ? 37.153  53.920  97.934  1.00 81.76  ? 64  ALA A CA    1 
ATOM   151  C  C     . ALA A 1 37  ? 36.066  54.983  97.863  1.00 91.11  ? 64  ALA A C     1 
ATOM   152  O  O     . ALA A 1 37  ? 34.902  54.663  97.597  1.00 97.73  ? 64  ALA A O     1 
ATOM   153  C  CB    . ALA A 1 37  ? 37.228  53.334  99.342  1.00 88.67  ? 64  ALA A CB    1 
ATOM   154  N  N     . HIS A 1 38  ? 36.424  56.249  98.093  1.00 89.64  ? 65  HIS A N     1 
ATOM   155  C  CA    . HIS A 1 38  ? 35.442  57.326  98.021  1.00 81.53  ? 65  HIS A CA    1 
ATOM   156  C  C     . HIS A 1 38  ? 34.877  57.480  96.616  1.00 93.45  ? 65  HIS A C     1 
ATOM   157  O  O     . HIS A 1 38  ? 33.753  57.965  96.448  1.00 95.39  ? 65  HIS A O     1 
ATOM   158  C  CB    . HIS A 1 38  ? 36.074  58.642  98.467  1.00 77.60  ? 65  HIS A CB    1 
ATOM   159  C  CG    . HIS A 1 38  ? 37.228  59.066  97.616  1.00 87.55  ? 65  HIS A CG    1 
ATOM   160  N  ND1   . HIS A 1 38  ? 38.525  58.680  97.877  1.00 101.39 ? 65  HIS A ND1   1 
ATOM   161  C  CD2   . HIS A 1 38  ? 37.280  59.825  96.496  1.00 91.75  ? 65  HIS A CD2   1 
ATOM   162  C  CE1   . HIS A 1 38  ? 39.327  59.190  96.959  1.00 91.03  ? 65  HIS A CE1   1 
ATOM   163  N  NE2   . HIS A 1 38  ? 38.597  59.888  96.109  1.00 91.41  ? 65  HIS A NE2   1 
ATOM   164  N  N     . ALA A 1 39  ? 35.636  57.071  95.599  1.00 88.38  ? 66  ALA A N     1 
ATOM   165  C  CA    . ALA A 1 39  ? 35.243  57.282  94.217  1.00 85.62  ? 66  ALA A CA    1 
ATOM   166  C  C     . ALA A 1 39  ? 34.860  56.007  93.485  1.00 88.37  ? 66  ALA A C     1 
ATOM   167  O  O     . ALA A 1 39  ? 34.095  56.080  92.519  1.00 89.02  ? 66  ALA A O     1 
ATOM   168  C  CB    . ALA A 1 39  ? 36.376  57.974  93.446  1.00 80.08  ? 66  ALA A CB    1 
ATOM   169  N  N     . LEU A 1 40  ? 35.354  54.851  93.929  1.00 90.37  ? 67  LEU A N     1 
ATOM   170  C  CA    . LEU A 1 40  ? 35.143  53.613  93.181  1.00 88.16  ? 67  LEU A CA    1 
ATOM   171  C  C     . LEU A 1 40  ? 33.677  53.276  92.926  1.00 88.08  ? 67  LEU A C     1 
ATOM   172  O  O     . LEU A 1 40  ? 33.369  52.841  91.802  1.00 86.19  ? 67  LEU A O     1 
ATOM   173  C  CB    . LEU A 1 40  ? 35.848  52.451  93.892  1.00 85.25  ? 67  LEU A CB    1 
ATOM   174  C  CG    . LEU A 1 40  ? 37.366  52.423  93.720  1.00 80.89  ? 67  LEU A CG    1 
ATOM   175  C  CD1   . LEU A 1 40  ? 37.958  51.190  94.381  1.00 84.16  ? 67  LEU A CD1   1 
ATOM   176  C  CD2   . LEU A 1 40  ? 37.728  52.471  92.250  1.00 72.33  ? 67  LEU A CD2   1 
ATOM   177  N  N     . PRO A 1 41  ? 32.743  53.424  93.876  1.00 90.73  ? 68  PRO A N     1 
ATOM   178  C  CA    . PRO A 1 41  ? 31.332  53.167  93.532  1.00 90.04  ? 68  PRO A CA    1 
ATOM   179  C  C     . PRO A 1 41  ? 30.857  53.965  92.330  1.00 89.68  ? 68  PRO A C     1 
ATOM   180  O  O     . PRO A 1 41  ? 30.286  53.394  91.394  1.00 96.63  ? 68  PRO A O     1 
ATOM   181  C  CB    . PRO A 1 41  ? 30.590  53.557  94.815  1.00 82.81  ? 68  PRO A CB    1 
ATOM   182  C  CG    . PRO A 1 41  ? 31.571  53.314  95.890  1.00 87.10  ? 68  PRO A CG    1 
ATOM   183  C  CD    . PRO A 1 41  ? 32.903  53.701  95.315  1.00 85.09  ? 68  PRO A CD    1 
ATOM   184  N  N     . THR A 1 42  ? 31.106  55.276  92.322  1.00 91.92  ? 69  THR A N     1 
ATOM   185  C  CA    . THR A 1 42  ? 30.689  56.105  91.195  1.00 84.31  ? 69  THR A CA    1 
ATOM   186  C  C     . THR A 1 42  ? 31.544  55.835  89.960  1.00 89.14  ? 69  THR A C     1 
ATOM   187  O  O     . THR A 1 42  ? 31.032  55.807  88.834  1.00 84.68  ? 69  THR A O     1 
ATOM   188  C  CB    . THR A 1 42  ? 30.747  57.581  91.600  1.00 81.67  ? 69  THR A CB    1 
ATOM   189  O  OG1   . THR A 1 42  ? 29.624  57.892  92.435  1.00 85.67  ? 69  THR A OG1   1 
ATOM   190  C  CG2   . THR A 1 42  ? 30.717  58.481  90.394  1.00 92.91  ? 69  THR A CG2   1 
ATOM   191  N  N     . THR A 1 43  ? 32.844  55.609  90.152  1.00 96.27  ? 70  THR A N     1 
ATOM   192  C  CA    . THR A 1 43  ? 33.737  55.393  89.018  1.00 72.45  ? 70  THR A CA    1 
ATOM   193  C  C     . THR A 1 43  ? 33.496  54.034  88.369  1.00 78.67  ? 70  THR A C     1 
ATOM   194  O  O     . THR A 1 43  ? 33.326  53.940  87.147  1.00 83.74  ? 70  THR A O     1 
ATOM   195  C  CB    . THR A 1 43  ? 35.193  55.531  89.469  1.00 67.29  ? 70  THR A CB    1 
ATOM   196  O  OG1   . THR A 1 43  ? 35.552  56.919  89.503  1.00 79.44  ? 70  THR A OG1   1 
ATOM   197  C  CG2   . THR A 1 43  ? 36.122  54.797  88.521  1.00 89.89  ? 70  THR A CG2   1 
ATOM   198  N  N     . LEU A 1 44  ? 33.482  52.966  89.171  1.00 83.46  ? 71  LEU A N     1 
ATOM   199  C  CA    . LEU A 1 44  ? 33.273  51.631  88.618  1.00 88.64  ? 71  LEU A CA    1 
ATOM   200  C  C     . LEU A 1 44  ? 31.886  51.483  88.008  1.00 92.23  ? 71  LEU A C     1 
ATOM   201  O  O     . LEU A 1 44  ? 31.713  50.729  87.043  1.00 85.13  ? 71  LEU A O     1 
ATOM   202  C  CB    . LEU A 1 44  ? 33.497  50.574  89.699  1.00 80.64  ? 71  LEU A CB    1 
ATOM   203  C  CG    . LEU A 1 44  ? 34.942  50.513  90.192  1.00 82.21  ? 71  LEU A CG    1 
ATOM   204  C  CD1   . LEU A 1 44  ? 35.085  49.616  91.414  1.00 75.23  ? 71  LEU A CD1   1 
ATOM   205  C  CD2   . LEU A 1 44  ? 35.847  50.047  89.062  1.00 75.67  ? 71  LEU A CD2   1 
ATOM   206  N  N     . GLY A 1 45  ? 30.892  52.187  88.552  1.00 81.74  ? 72  GLY A N     1 
ATOM   207  C  CA    . GLY A 1 45  ? 29.577  52.182  87.935  1.00 82.45  ? 72  GLY A CA    1 
ATOM   208  C  C     . GLY A 1 45  ? 29.597  52.755  86.532  1.00 84.83  ? 72  GLY A C     1 
ATOM   209  O  O     . GLY A 1 45  ? 28.945  52.229  85.626  1.00 90.31  ? 72  GLY A O     1 
ATOM   210  N  N     . ALA A 1 46  ? 30.356  53.833  86.329  1.00 78.15  ? 73  ALA A N     1 
ATOM   211  C  CA    . ALA A 1 46  ? 30.451  54.426  85.000  1.00 74.62  ? 73  ALA A CA    1 
ATOM   212  C  C     . ALA A 1 46  ? 31.101  53.476  84.006  1.00 74.38  ? 73  ALA A C     1 
ATOM   213  O  O     . ALA A 1 46  ? 30.742  53.477  82.822  1.00 78.44  ? 73  ALA A O     1 
ATOM   214  C  CB    . ALA A 1 46  ? 31.234  55.738  85.059  1.00 72.89  ? 73  ALA A CB    1 
ATOM   215  N  N     . LEU A 1 47  ? 32.059  52.666  84.462  1.00 75.79  ? 74  LEU A N     1 
ATOM   216  C  CA    . LEU A 1 47  ? 32.752  51.761  83.551  1.00 76.46  ? 74  LEU A CA    1 
ATOM   217  C  C     . LEU A 1 47  ? 31.876  50.574  83.177  1.00 80.24  ? 74  LEU A C     1 
ATOM   218  O  O     . LEU A 1 47  ? 31.799  50.202  82.001  1.00 78.70  ? 74  LEU A O     1 
ATOM   219  C  CB    . LEU A 1 47  ? 34.061  51.283  84.178  1.00 69.80  ? 74  LEU A CB    1 
ATOM   220  C  CG    . LEU A 1 47  ? 35.127  52.359  84.385  1.00 76.09  ? 74  LEU A CG    1 
ATOM   221  C  CD1   . LEU A 1 47  ? 36.420  51.746  84.892  1.00 65.14  ? 74  LEU A CD1   1 
ATOM   222  C  CD2   . LEU A 1 47  ? 35.361  53.121  83.093  1.00 70.58  ? 74  LEU A CD2   1 
ATOM   223  N  N     . GLU A 1 48  ? 31.205  49.967  84.161  1.00 84.54  ? 75  GLU A N     1 
ATOM   224  C  CA    . GLU A 1 48  ? 30.362  48.815  83.871  1.00 89.43  ? 75  GLU A CA    1 
ATOM   225  C  C     . GLU A 1 48  ? 29.192  49.168  82.964  1.00 82.13  ? 75  GLU A C     1 
ATOM   226  O  O     . GLU A 1 48  ? 28.545  48.261  82.432  1.00 99.48  ? 75  GLU A O     1 
ATOM   227  C  CB    . GLU A 1 48  ? 29.852  48.189  85.173  1.00 74.30  ? 75  GLU A CB    1 
ATOM   228  C  CG    . GLU A 1 48  ? 28.868  49.047  85.942  1.00 82.06  ? 75  GLU A CG    1 
ATOM   229  C  CD    . GLU A 1 48  ? 28.395  48.384  87.224  1.00 96.73  ? 75  GLU A CD    1 
ATOM   230  O  OE1   . GLU A 1 48  ? 29.166  47.593  87.806  1.00 97.61  ? 75  GLU A OE1   1 
ATOM   231  O  OE2   . GLU A 1 48  ? 27.249  48.649  87.650  1.00 103.68 ? 75  GLU A OE2   1 
ATOM   232  N  N     . ARG A 1 49  ? 28.918  50.456  82.761  1.00 76.49  ? 76  ARG A N     1 
ATOM   233  C  CA    . ARG A 1 49  ? 27.847  50.903  81.884  1.00 77.07  ? 76  ARG A CA    1 
ATOM   234  C  C     . ARG A 1 49  ? 28.373  51.483  80.573  1.00 85.05  ? 76  ARG A C     1 
ATOM   235  O  O     . ARG A 1 49  ? 27.640  52.185  79.870  1.00 81.09  ? 76  ARG A O     1 
ATOM   236  C  CB    . ARG A 1 49  ? 26.971  51.920  82.614  1.00 60.70  ? 76  ARG A CB    1 
ATOM   237  C  CG    . ARG A 1 49  ? 26.265  51.330  83.827  1.00 84.91  ? 76  ARG A CG    1 
ATOM   238  C  CD    . ARG A 1 49  ? 25.169  52.242  84.353  1.00 75.91  ? 76  ARG A CD    1 
ATOM   239  N  NE    . ARG A 1 49  ? 25.687  53.276  85.240  1.00 92.59  ? 76  ARG A NE    1 
ATOM   240  C  CZ    . ARG A 1 49  ? 25.841  53.129  86.549  1.00 101.18 ? 76  ARG A CZ    1 
ATOM   241  N  NH1   . ARG A 1 49  ? 25.557  51.987  87.156  1.00 95.07  ? 76  ARG A NH1   1 
ATOM   242  N  NH2   . ARG A 1 49  ? 26.288  54.156  87.268  1.00 94.06  ? 76  ARG A NH2   1 
ATOM   243  N  N     . LEU A 1 50  ? 29.630  51.204  80.231  1.00 73.35  ? 77  LEU A N     1 
ATOM   244  C  CA    . LEU A 1 50  ? 30.166  51.625  78.943  1.00 72.00  ? 77  LEU A CA    1 
ATOM   245  C  C     . LEU A 1 50  ? 29.472  50.868  77.819  1.00 76.33  ? 77  LEU A C     1 
ATOM   246  O  O     . LEU A 1 50  ? 29.372  49.641  77.859  1.00 85.77  ? 77  LEU A O     1 
ATOM   247  C  CB    . LEU A 1 50  ? 31.671  51.372  78.879  1.00 70.58  ? 77  LEU A CB    1 
ATOM   248  C  CG    . LEU A 1 50  ? 32.633  52.297  79.612  1.00 80.45  ? 77  LEU A CG    1 
ATOM   249  C  CD1   . LEU A 1 50  ? 33.990  51.625  79.714  1.00 67.19  ? 77  LEU A CD1   1 
ATOM   250  C  CD2   . LEU A 1 50  ? 32.744  53.623  78.878  1.00 65.19  ? 77  LEU A CD2   1 
ATOM   251  N  N     . ARG A 1 51  ? 28.992  51.594  76.811  1.00 75.83  ? 78  ARG A N     1 
ATOM   252  C  CA    . ARG A 1 51  ? 28.383  50.931  75.664  1.00 75.31  ? 78  ARG A CA    1 
ATOM   253  C  C     . ARG A 1 51  ? 29.464  50.305  74.799  1.00 77.43  ? 78  ARG A C     1 
ATOM   254  O  O     . ARG A 1 51  ? 29.815  50.846  73.753  1.00 81.09  ? 78  ARG A O     1 
ATOM   255  C  CB    . ARG A 1 51  ? 27.525  51.911  74.856  1.00 86.02  ? 78  ARG A CB    1 
ATOM   256  C  CG    . ARG A 1 51  ? 26.104  52.090  75.411  1.00 79.56  ? 78  ARG A CG    1 
ATOM   257  C  CD    . ARG A 1 51  ? 25.278  52.976  74.497  1.00 78.58  ? 78  ARG A CD    1 
ATOM   258  N  NE    . ARG A 1 51  ? 25.557  54.396  74.693  1.00 89.59  ? 78  ARG A NE    1 
ATOM   259  C  CZ    . ARG A 1 51  ? 24.864  55.192  75.499  1.00 99.11  ? 78  ARG A CZ    1 
ATOM   260  N  NH1   . ARG A 1 51  ? 23.840  54.740  76.206  1.00 90.56  ? 78  ARG A NH1   1 
ATOM   261  N  NH2   . ARG A 1 51  ? 25.207  56.474  75.599  1.00 102.96 ? 78  ARG A NH2   1 
ATOM   262  N  N     . HIS A 1 52  ? 30.011  49.178  75.243  1.00 69.59  ? 79  HIS A N     1 
ATOM   263  C  CA    . HIS A 1 52  ? 31.041  48.429  74.539  1.00 77.46  ? 79  HIS A CA    1 
ATOM   264  C  C     . HIS A 1 52  ? 30.902  47.002  75.060  1.00 81.50  ? 79  HIS A C     1 
ATOM   265  O  O     . HIS A 1 52  ? 30.876  46.801  76.287  1.00 84.44  ? 79  HIS A O     1 
ATOM   266  C  CB    . HIS A 1 52  ? 32.463  48.943  74.763  1.00 67.53  ? 79  HIS A CB    1 
ATOM   267  C  CG    . HIS A 1 52  ? 33.500  48.209  73.978  1.00 75.17  ? 79  HIS A CG    1 
ATOM   268  N  ND1   . HIS A 1 52  ? 33.670  48.383  72.621  1.00 89.37  ? 79  HIS A ND1   1 
ATOM   269  C  CD2   . HIS A 1 52  ? 34.416  47.289  74.363  1.00 75.21  ? 79  HIS A CD2   1 
ATOM   270  C  CE1   . HIS A 1 52  ? 34.645  47.594  72.204  1.00 79.06  ? 79  HIS A CE1   1 
ATOM   271  N  NE2   . HIS A 1 52  ? 35.112  46.919  73.240  1.00 72.04  ? 79  HIS A NE2   1 
ATOM   272  N  N     . PRO A 1 53  ? 30.834  46.011  74.173  1.00 71.54  ? 80  PRO A N     1 
ATOM   273  C  CA    . PRO A 1 53  ? 30.522  44.640  74.596  1.00 81.08  ? 80  PRO A CA    1 
ATOM   274  C  C     . PRO A 1 53  ? 31.459  44.141  75.690  1.00 89.15  ? 80  PRO A C     1 
ATOM   275  O  O     . PRO A 1 53  ? 32.687  44.177  75.555  1.00 95.36  ? 80  PRO A O     1 
ATOM   276  C  CB    . PRO A 1 53  ? 30.686  43.831  73.303  1.00 69.11  ? 80  PRO A CB    1 
ATOM   277  C  CG    . PRO A 1 53  ? 30.521  44.821  72.200  1.00 68.52  ? 80  PRO A CG    1 
ATOM   278  C  CD    . PRO A 1 53  ? 31.059  46.111  72.722  1.00 66.93  ? 80  PRO A CD    1 
ATOM   279  N  N     . ARG A 1 54  ? 30.866  43.658  76.784  1.00 83.16  ? 81  ARG A N     1 
ATOM   280  C  CA    . ARG A 1 54  ? 31.665  43.137  77.887  1.00 85.59  ? 81  ARG A CA    1 
ATOM   281  C  C     . ARG A 1 54  ? 32.471  41.912  77.473  1.00 81.51  ? 81  ARG A C     1 
ATOM   282  O  O     . ARG A 1 54  ? 33.579  41.699  77.981  1.00 86.45  ? 81  ARG A O     1 
ATOM   283  C  CB    . ARG A 1 54  ? 30.768  42.804  79.080  1.00 90.15  ? 81  ARG A CB    1 
ATOM   284  C  CG    . ARG A 1 54  ? 30.260  44.018  79.845  1.00 84.89  ? 81  ARG A CG    1 
ATOM   285  C  CD    . ARG A 1 54  ? 29.711  43.598  81.197  1.00 97.63  ? 81  ARG A CD    1 
ATOM   286  N  NE    . ARG A 1 54  ? 29.335  44.732  82.031  1.00 95.69  ? 81  ARG A NE    1 
ATOM   287  C  CZ    . ARG A 1 54  ? 28.087  45.139  82.222  1.00 96.28  ? 81  ARG A CZ    1 
ATOM   288  N  NH1   . ARG A 1 54  ? 27.067  44.537  81.633  1.00 101.64 ? 81  ARG A NH1   1 
ATOM   289  N  NH2   . ARG A 1 54  ? 27.857  46.169  83.032  1.00 99.03  ? 81  ARG A NH2   1 
ATOM   290  N  N     . GLU A 1 55  ? 31.942  41.096  76.557  1.00 87.63  ? 82  GLU A N     1 
ATOM   291  C  CA    . GLU A 1 55  ? 32.710  39.951  76.081  1.00 84.08  ? 82  GLU A CA    1 
ATOM   292  C  C     . GLU A 1 55  ? 33.919  40.379  75.260  1.00 82.74  ? 82  GLU A C     1 
ATOM   293  O  O     . GLU A 1 55  ? 34.851  39.586  75.092  1.00 96.76  ? 82  GLU A O     1 
ATOM   294  C  CB    . GLU A 1 55  ? 31.825  39.007  75.261  1.00 79.50  ? 82  GLU A CB    1 
ATOM   295  C  CG    . GLU A 1 55  ? 31.425  39.524  73.884  1.00 90.96  ? 82  GLU A CG    1 
ATOM   296  C  CD    . GLU A 1 55  ? 30.111  40.283  73.892  1.00 100.05 ? 82  GLU A CD    1 
ATOM   297  O  OE1   . GLU A 1 55  ? 29.657  40.693  74.984  1.00 107.06 ? 82  GLU A OE1   1 
ATOM   298  O  OE2   . GLU A 1 55  ? 29.529  40.464  72.801  1.00 98.94  ? 82  GLU A OE2   1 
ATOM   299  N  N     . ARG A 1 56  ? 33.927  41.612  74.752  1.00 86.01  ? 83  ARG A N     1 
ATOM   300  C  CA    . ARG A 1 56  ? 35.083  42.181  74.074  1.00 71.51  ? 83  ARG A CA    1 
ATOM   301  C  C     . ARG A 1 56  ? 35.885  43.098  74.988  1.00 78.45  ? 83  ARG A C     1 
ATOM   302  O  O     . ARG A 1 56  ? 36.696  43.895  74.505  1.00 82.49  ? 83  ARG A O     1 
ATOM   303  C  CB    . ARG A 1 56  ? 34.641  42.939  72.823  1.00 74.70  ? 83  ARG A CB    1 
ATOM   304  C  CG    . ARG A 1 56  ? 33.693  42.156  71.939  1.00 82.40  ? 83  ARG A CG    1 
ATOM   305  C  CD    . ARG A 1 56  ? 34.340  40.892  71.428  1.00 52.91  ? 83  ARG A CD    1 
ATOM   306  N  NE    . ARG A 1 56  ? 35.345  41.175  70.413  1.00 66.83  ? 83  ARG A NE    1 
ATOM   307  C  CZ    . ARG A 1 56  ? 36.075  40.248  69.809  1.00 70.38  ? 83  ARG A CZ    1 
ATOM   308  N  NH1   . ARG A 1 56  ? 35.939  38.965  70.099  1.00 75.84  ? 83  ARG A NH1   1 
ATOM   309  N  NH2   . ARG A 1 56  ? 36.966  40.618  68.893  1.00 71.30  ? 83  ARG A NH2   1 
ATOM   310  N  N     . THR A 1 57  ? 35.667  43.005  76.298  1.00 84.42  ? 84  THR A N     1 
ATOM   311  C  CA    . THR A 1 57  ? 36.342  43.837  77.281  1.00 64.33  ? 84  THR A CA    1 
ATOM   312  C  C     . THR A 1 57  ? 36.971  42.950  78.344  1.00 74.17  ? 84  THR A C     1 
ATOM   313  O  O     . THR A 1 57  ? 36.369  41.964  78.780  1.00 75.82  ? 84  THR A O     1 
ATOM   314  C  CB    . THR A 1 57  ? 35.366  44.821  77.936  1.00 82.89  ? 84  THR A CB    1 
ATOM   315  O  OG1   . THR A 1 57  ? 34.652  45.534  76.919  1.00 91.30  ? 84  THR A OG1   1 
ATOM   316  C  CG2   . THR A 1 57  ? 36.111  45.820  78.822  1.00 81.07  ? 84  THR A CG2   1 
ATOM   317  N  N     . ALA A 1 58  ? 38.186  43.302  78.754  1.00 75.39  ? 85  ALA A N     1 
ATOM   318  C  CA    . ALA A 1 58  ? 38.869  42.622  79.842  1.00 67.63  ? 85  ALA A CA    1 
ATOM   319  C  C     . ALA A 1 58  ? 39.325  43.651  80.864  1.00 71.91  ? 85  ALA A C     1 
ATOM   320  O  O     . ALA A 1 58  ? 39.481  44.836  80.555  1.00 69.76  ? 85  ALA A O     1 
ATOM   321  C  CB    . ALA A 1 58  ? 40.065  41.807  79.341  1.00 77.47  ? 85  ALA A CB    1 
ATOM   322  N  N     . LEU A 1 59  ? 39.549  43.178  82.087  1.00 71.14  ? 86  LEU A N     1 
ATOM   323  C  CA    . LEU A 1 59  ? 39.841  44.033  83.227  1.00 61.63  ? 86  LEU A CA    1 
ATOM   324  C  C     . LEU A 1 59  ? 41.209  43.702  83.803  1.00 74.15  ? 86  LEU A C     1 
ATOM   325  O  O     . LEU A 1 59  ? 41.590  42.530  83.891  1.00 76.88  ? 86  LEU A O     1 
ATOM   326  C  CB    . LEU A 1 59  ? 38.766  43.876  84.306  1.00 67.86  ? 86  LEU A CB    1 
ATOM   327  C  CG    . LEU A 1 59  ? 37.334  44.145  83.838  1.00 79.15  ? 86  LEU A CG    1 
ATOM   328  C  CD1   . LEU A 1 59  ? 36.332  43.820  84.940  1.00 76.82  ? 86  LEU A CD1   1 
ATOM   329  C  CD2   . LEU A 1 59  ? 37.184  45.590  83.369  1.00 72.75  ? 86  LEU A CD2   1 
ATOM   330  N  N     . TRP A 1 60  ? 41.936  44.742  84.206  1.00 73.18  ? 87  TRP A N     1 
ATOM   331  C  CA    . TRP A 1 60  ? 43.257  44.601  84.816  1.00 71.77  ? 87  TRP A CA    1 
ATOM   332  C  C     . TRP A 1 60  ? 43.328  45.589  85.970  1.00 68.93  ? 87  TRP A C     1 
ATOM   333  O  O     . TRP A 1 60  ? 43.358  46.802  85.741  1.00 75.48  ? 87  TRP A O     1 
ATOM   334  C  CB    . TRP A 1 60  ? 44.363  44.863  83.795  1.00 64.74  ? 87  TRP A CB    1 
ATOM   335  C  CG    . TRP A 1 60  ? 45.753  44.544  84.258  1.00 71.57  ? 87  TRP A CG    1 
ATOM   336  C  CD1   . TRP A 1 60  ? 46.472  43.417  83.976  1.00 69.13  ? 87  TRP A CD1   1 
ATOM   337  C  CD2   . TRP A 1 60  ? 46.605  45.370  85.065  1.00 80.30  ? 87  TRP A CD2   1 
ATOM   338  N  NE1   . TRP A 1 60  ? 47.713  43.487  84.562  1.00 70.00  ? 87  TRP A NE1   1 
ATOM   339  C  CE2   . TRP A 1 60  ? 47.819  44.675  85.236  1.00 78.11  ? 87  TRP A CE2   1 
ATOM   340  C  CE3   . TRP A 1 60  ? 46.458  46.628  85.661  1.00 67.62  ? 87  TRP A CE3   1 
ATOM   341  C  CZ2   . TRP A 1 60  ? 48.878  45.195  85.980  1.00 74.40  ? 87  TRP A CZ2   1 
ATOM   342  C  CZ3   . TRP A 1 60  ? 47.511  47.142  86.397  1.00 63.52  ? 87  TRP A CZ3   1 
ATOM   343  C  CH2   . TRP A 1 60  ? 48.704  46.425  86.553  1.00 74.75  ? 87  TRP A CH2   1 
ATOM   344  N  N     . VAL A 1 61  ? 43.354  45.082  87.202  1.00 68.66  ? 88  VAL A N     1 
ATOM   345  C  CA    . VAL A 1 61  ? 43.217  45.905  88.399  1.00 70.46  ? 88  VAL A CA    1 
ATOM   346  C  C     . VAL A 1 61  ? 44.402  45.659  89.324  1.00 76.08  ? 88  VAL A C     1 
ATOM   347  O  O     . VAL A 1 61  ? 44.695  44.511  89.680  1.00 77.60  ? 88  VAL A O     1 
ATOM   348  C  CB    . VAL A 1 61  ? 41.895  45.616  89.131  1.00 61.43  ? 88  VAL A CB    1 
ATOM   349  C  CG1   . VAL A 1 61  ? 41.812  46.434  90.405  1.00 78.07  ? 88  VAL A CG1   1 
ATOM   350  C  CG2   . VAL A 1 61  ? 40.720  45.916  88.227  1.00 71.49  ? 88  VAL A CG2   1 
ATOM   351  N  N     . ALA A 1 62  ? 45.067  46.741  89.727  1.00 68.50  ? 89  ALA A N     1 
ATOM   352  C  CA    . ALA A 1 62  ? 46.184  46.676  90.659  1.00 78.52  ? 89  ALA A CA    1 
ATOM   353  C  C     . ALA A 1 62  ? 45.963  47.704  91.757  1.00 84.77  ? 89  ALA A C     1 
ATOM   354  O  O     . ALA A 1 62  ? 45.635  48.861  91.471  1.00 82.34  ? 89  ALA A O     1 
ATOM   355  C  CB    . ALA A 1 62  ? 47.521  46.928  89.953  1.00 62.46  ? 89  ALA A CB    1 
ATOM   356  N  N     . THR A 1 63  ? 46.145  47.281  93.008  1.00 77.29  ? 90  THR A N     1 
ATOM   357  C  CA    . THR A 1 63  ? 45.927  48.153  94.153  1.00 81.77  ? 90  THR A CA    1 
ATOM   358  C  C     . THR A 1 63  ? 46.916  47.811  95.259  1.00 79.56  ? 90  THR A C     1 
ATOM   359  O  O     . THR A 1 63  ? 47.213  46.637  95.498  1.00 86.64  ? 90  THR A O     1 
ATOM   360  C  CB    . THR A 1 63  ? 44.487  48.041  94.673  1.00 79.30  ? 90  THR A CB    1 
ATOM   361  O  OG1   . THR A 1 63  ? 44.364  48.772  95.899  1.00 85.88  ? 90  THR A OG1   1 
ATOM   362  C  CG2   . THR A 1 63  ? 44.106  46.588  94.907  1.00 77.23  ? 90  THR A CG2   1 
ATOM   363  N  N     . ASP A 1 64  ? 47.413  48.846  95.931  1.00 75.35  ? 91  ASP A N     1 
ATOM   364  C  CA    . ASP A 1 64  ? 48.408  48.709  96.987  1.00 80.02  ? 91  ASP A CA    1 
ATOM   365  C  C     . ASP A 1 64  ? 48.503  50.037  97.726  1.00 89.77  ? 91  ASP A C     1 
ATOM   366  O  O     . ASP A 1 64  ? 48.005  51.065  97.259  1.00 83.92  ? 91  ASP A O     1 
ATOM   367  C  CB    . ASP A 1 64  ? 49.772  48.294  96.427  1.00 83.64  ? 91  ASP A CB    1 
ATOM   368  C  CG    . ASP A 1 64  ? 50.157  49.081  95.189  1.00 85.59  ? 91  ASP A CG    1 
ATOM   369  O  OD1   . ASP A 1 64  ? 50.442  50.291  95.317  1.00 93.79  ? 91  ASP A OD1   1 
ATOM   370  O  OD2   . ASP A 1 64  ? 50.171  48.492  94.085  1.00 80.07  ? 91  ASP A OD2   1 
ATOM   371  N  N     . HIS A 1 65  ? 49.147  49.996  98.894  1.00 99.28  ? 92  HIS A N     1 
ATOM   372  C  CA    . HIS A 1 65  ? 49.389  51.186  99.712  1.00 98.91  ? 92  HIS A CA    1 
ATOM   373  C  C     . HIS A 1 65  ? 48.082  51.902  100.048 1.00 99.09  ? 92  HIS A C     1 
ATOM   374  O  O     . HIS A 1 65  ? 47.955  53.121  99.908  1.00 92.35  ? 92  HIS A O     1 
ATOM   375  C  CB    . HIS A 1 65  ? 50.375  52.132  99.022  1.00 87.02  ? 92  HIS A CB    1 
ATOM   376  C  CG    . HIS A 1 65  ? 51.688  51.494  98.692  1.00 97.60  ? 92  HIS A CG    1 
ATOM   377  N  ND1   . HIS A 1 65  ? 51.938  50.895  97.476  1.00 86.63  ? 92  HIS A ND1   1 
ATOM   378  C  CD2   . HIS A 1 65  ? 52.817  51.347  99.425  1.00 96.77  ? 92  HIS A CD2   1 
ATOM   379  C  CE1   . HIS A 1 65  ? 53.168  50.413  97.472  1.00 87.80  ? 92  HIS A CE1   1 
ATOM   380  N  NE2   . HIS A 1 65  ? 53.724  50.674  98.642  1.00 93.07  ? 92  HIS A NE2   1 
ATOM   381  N  N     . ASN A 1 66  ? 47.105  51.131  100.512 1.00 99.31  ? 93  ASN A N     1 
ATOM   382  C  CA    . ASN A 1 66  ? 45.770  51.640  100.791 1.00 85.49  ? 93  ASN A CA    1 
ATOM   383  C  C     . ASN A 1 66  ? 45.623  51.905  102.282 1.00 96.96  ? 93  ASN A C     1 
ATOM   384  O  O     . ASN A 1 66  ? 45.847  51.009  103.102 1.00 92.79  ? 93  ASN A O     1 
ATOM   385  C  CB    . ASN A 1 66  ? 44.705  50.655  100.315 1.00 79.72  ? 93  ASN A CB    1 
ATOM   386  C  CG    . ASN A 1 66  ? 44.598  50.606  98.809  1.00 92.28  ? 93  ASN A CG    1 
ATOM   387  O  OD1   . ASN A 1 66  ? 44.759  51.621  98.134  1.00 100.91 ? 93  ASN A OD1   1 
ATOM   388  N  ND2   . ASN A 1 66  ? 44.330  49.423  98.269  1.00 88.68  ? 93  ASN A ND2   1 
ATOM   389  N  N     . MET A 1 67  ? 45.245  53.134  102.628 1.00 101.11 ? 94  MET A N     1 
ATOM   390  C  CA    . MET A 1 67  ? 44.861  53.457  103.993 1.00 88.08  ? 94  MET A CA    1 
ATOM   391  C  C     . MET A 1 67  ? 43.364  53.287  104.226 1.00 87.69  ? 94  MET A C     1 
ATOM   392  O  O     . MET A 1 67  ? 42.935  53.191  105.381 1.00 103.92 ? 94  MET A O     1 
ATOM   393  C  CB    . MET A 1 67  ? 45.287  54.890  104.338 1.00 83.02  ? 94  MET A CB    1 
ATOM   394  C  CG    . MET A 1 67  ? 45.475  55.140  105.832 1.00 126.40 ? 94  MET A CG    1 
ATOM   395  S  SD    . MET A 1 67  ? 46.906  54.295  106.549 1.00 115.06 ? 94  MET A SD    1 
ATOM   396  C  CE    . MET A 1 67  ? 48.244  55.137  105.706 1.00 111.86 ? 94  MET A CE    1 
ATOM   397  N  N     . ASP A 1 68  ? 42.568  53.237  103.160 1.00 87.42  ? 95  ASP A N     1 
ATOM   398  C  CA    . ASP A 1 68  ? 41.136  52.988  103.226 1.00 94.57  ? 95  ASP A CA    1 
ATOM   399  C  C     . ASP A 1 68  ? 40.841  51.567  102.742 1.00 97.45  ? 95  ASP A C     1 
ATOM   400  O  O     . ASP A 1 68  ? 41.751  50.793  102.424 1.00 94.74  ? 95  ASP A O     1 
ATOM   401  C  CB    . ASP A 1 68  ? 40.380  54.034  102.399 1.00 79.58  ? 95  ASP A CB    1 
ATOM   402  C  CG    . ASP A 1 68  ? 40.741  53.987  100.923 1.00 92.13  ? 95  ASP A CG    1 
ATOM   403  O  OD1   . ASP A 1 68  ? 41.675  53.248  100.559 1.00 99.41  ? 95  ASP A OD1   1 
ATOM   404  O  OD2   . ASP A 1 68  ? 40.086  54.693  100.122 1.00 97.29  ? 95  ASP A OD2   1 
ATOM   405  N  N     . ASN A 1 69  ? 39.556  51.223  102.660 1.00 94.40  ? 96  ASN A N     1 
ATOM   406  C  CA    . ASN A 1 69  ? 39.131  49.900  102.196 1.00 100.54 ? 96  ASN A CA    1 
ATOM   407  C  C     . ASN A 1 69  ? 39.005  49.823  100.678 1.00 101.28 ? 96  ASN A C     1 
ATOM   408  O  O     . ASN A 1 69  ? 38.053  49.231  100.157 1.00 102.18 ? 96  ASN A O     1 
ATOM   409  C  CB    . ASN A 1 69  ? 37.818  49.516  102.868 1.00 96.99  ? 96  ASN A CB    1 
ATOM   410  C  CG    . ASN A 1 69  ? 36.681  50.449  102.500 1.00 102.89 ? 96  ASN A CG    1 
ATOM   411  O  OD1   . ASN A 1 69  ? 36.895  51.631  102.232 1.00 108.50 ? 96  ASN A OD1   1 
ATOM   412  N  ND2   . ASN A 1 69  ? 35.463  49.921  102.484 1.00 100.37 ? 96  ASN A ND2   1 
ATOM   413  N  N     . THR A 1 70  ? 39.952  50.414  99.944  1.00 90.63  ? 97  THR A N     1 
ATOM   414  C  CA    . THR A 1 70  ? 39.927  50.328  98.487  1.00 88.35  ? 97  THR A CA    1 
ATOM   415  C  C     . THR A 1 70  ? 39.995  48.880  98.022  1.00 87.27  ? 97  THR A C     1 
ATOM   416  O  O     . THR A 1 70  ? 39.272  48.478  97.103  1.00 93.58  ? 97  THR A O     1 
ATOM   417  C  CB    . THR A 1 70  ? 41.087  51.133  97.897  1.00 87.80  ? 97  THR A CB    1 
ATOM   418  O  OG1   . THR A 1 70  ? 40.838  52.535  98.068  1.00 89.04  ? 97  THR A OG1   1 
ATOM   419  C  CG2   . THR A 1 70  ? 41.273  50.819  96.417  1.00 80.13  ? 97  THR A CG2   1 
ATOM   420  N  N     . SER A 1 71  ? 40.850  48.077  98.661  1.00 97.02  ? 98  SER A N     1 
ATOM   421  C  CA    . SER A 1 71  ? 41.024  46.687  98.254  1.00 94.22  ? 98  SER A CA    1 
ATOM   422  C  C     . SER A 1 71  ? 39.733  45.891  98.380  1.00 96.40  ? 98  SER A C     1 
ATOM   423  O  O     . SER A 1 71  ? 39.486  44.978  97.585  1.00 92.22  ? 98  SER A O     1 
ATOM   424  C  CB    . SER A 1 71  ? 42.127  46.038  99.090  1.00 105.83 ? 98  SER A CB    1 
ATOM   425  O  OG    . SER A 1 71  ? 42.264  44.665  98.774  1.00 123.56 ? 98  SER A OG    1 
ATOM   426  N  N     . THR A 1 72  ? 38.897  46.221  99.365  1.00 103.71 ? 99  THR A N     1 
ATOM   427  C  CA    . THR A 1 72  ? 37.668  45.467  99.583  1.00 90.81  ? 99  THR A CA    1 
ATOM   428  C  C     . THR A 1 72  ? 36.581  45.848  98.589  1.00 89.62  ? 99  THR A C     1 
ATOM   429  O  O     . THR A 1 72  ? 35.796  44.988  98.175  1.00 102.94 ? 99  THR A O     1 
ATOM   430  C  CB    . THR A 1 72  ? 37.169  45.681  101.011 1.00 93.60  ? 99  THR A CB    1 
ATOM   431  O  OG1   . THR A 1 72  ? 38.250  45.468  101.928 1.00 103.06 ? 99  THR A OG1   1 
ATOM   432  C  CG2   . THR A 1 72  ? 36.038  44.721  101.334 1.00 89.14  ? 99  THR A CG2   1 
ATOM   433  N  N     . VAL A 1 73  ? 36.518  47.121  98.196  1.00 91.03  ? 100 VAL A N     1 
ATOM   434  C  CA    . VAL A 1 73  ? 35.521  47.549  97.218  1.00 94.14  ? 100 VAL A CA    1 
ATOM   435  C  C     . VAL A 1 73  ? 35.810  46.933  95.855  1.00 95.95  ? 100 VAL A C     1 
ATOM   436  O  O     . VAL A 1 73  ? 34.893  46.502  95.145  1.00 94.85  ? 100 VAL A O     1 
ATOM   437  C  CB    . VAL A 1 73  ? 35.473  49.087  97.147  1.00 89.97  ? 100 VAL A CB    1 
ATOM   438  C  CG1   . VAL A 1 73  ? 34.493  49.547  96.085  1.00 83.85  ? 100 VAL A CG1   1 
ATOM   439  C  CG2   . VAL A 1 73  ? 35.112  49.668  98.509  1.00 81.55  ? 100 VAL A CG2   1 
ATOM   440  N  N     . LEU A 1 74  ? 37.087  46.870  95.475  1.00 89.91  ? 101 LEU A N     1 
ATOM   441  C  CA    . LEU A 1 74  ? 37.458  46.270  94.198  1.00 86.91  ? 101 LEU A CA    1 
ATOM   442  C  C     . LEU A 1 74  ? 37.128  44.782  94.171  1.00 95.11  ? 101 LEU A C     1 
ATOM   443  O  O     . LEU A 1 74  ? 36.565  44.278  93.192  1.00 96.24  ? 101 LEU A O     1 
ATOM   444  C  CB    . LEU A 1 74  ? 38.946  46.495  93.930  1.00 89.13  ? 101 LEU A CB    1 
ATOM   445  C  CG    . LEU A 1 74  ? 39.388  47.904  93.537  1.00 91.44  ? 101 LEU A CG    1 
ATOM   446  C  CD1   . LEU A 1 74  ? 40.899  48.034  93.650  1.00 75.19  ? 101 LEU A CD1   1 
ATOM   447  C  CD2   . LEU A 1 74  ? 38.919  48.234  92.123  1.00 77.22  ? 101 LEU A CD2   1 
ATOM   448  N  N     . ARG A 1 75  ? 37.478  44.061  95.239  1.00 96.46  ? 102 ARG A N     1 
ATOM   449  C  CA    . ARG A 1 75  ? 37.226  42.624  95.271  1.00 97.44  ? 102 ARG A CA    1 
ATOM   450  C  C     . ARG A 1 75  ? 35.733  42.330  95.261  1.00 102.78 ? 102 ARG A C     1 
ATOM   451  O  O     . ARG A 1 75  ? 35.275  41.430  94.548  1.00 100.30 ? 102 ARG A O     1 
ATOM   452  C  CB    . ARG A 1 75  ? 37.887  42.001  96.501  1.00 102.84 ? 102 ARG A CB    1 
ATOM   453  C  CG    . ARG A 1 75  ? 37.952  40.479  96.466  1.00 109.07 ? 102 ARG A CG    1 
ATOM   454  C  CD    . ARG A 1 75  ? 38.584  39.903  97.731  1.00 112.82 ? 102 ARG A CD    1 
ATOM   455  N  NE    . ARG A 1 75  ? 39.922  40.429  97.983  1.00 130.82 ? 102 ARG A NE    1 
ATOM   456  C  CZ    . ARG A 1 75  ? 40.210  41.344  98.900  1.00 134.68 ? 102 ARG A CZ    1 
ATOM   457  N  NH1   . ARG A 1 75  ? 39.276  41.854  99.687  1.00 124.43 ? 102 ARG A NH1   1 
ATOM   458  N  NH2   . ARG A 1 75  ? 41.468  41.756  99.033  1.00 121.21 ? 102 ARG A NH2   1 
ATOM   459  N  N     . GLU A 1 76  ? 34.959  43.084  96.046  1.00 104.43 ? 103 GLU A N     1 
ATOM   460  C  CA    . GLU A 1 76  ? 33.507  42.943  96.025  1.00 106.54 ? 103 GLU A CA    1 
ATOM   461  C  C     . GLU A 1 76  ? 32.956  43.153  94.620  1.00 102.39 ? 103 GLU A C     1 
ATOM   462  O  O     . GLU A 1 76  ? 32.006  42.476  94.207  1.00 102.49 ? 103 GLU A O     1 
ATOM   463  C  CB    . GLU A 1 76  ? 32.882  43.938  97.005  1.00 103.97 ? 103 GLU A CB    1 
ATOM   464  C  CG    . GLU A 1 76  ? 31.365  43.909  97.059  1.00 119.40 ? 103 GLU A CG    1 
ATOM   465  C  CD    . GLU A 1 76  ? 30.793  45.058  97.867  1.00 136.94 ? 103 GLU A CD    1 
ATOM   466  O  OE1   . GLU A 1 76  ? 31.486  46.088  98.009  1.00 144.18 ? 103 GLU A OE1   1 
ATOM   467  O  OE2   . GLU A 1 76  ? 29.653  44.933  98.360  1.00 137.99 ? 103 GLU A OE2   1 
ATOM   468  N  N     . TRP A 1 77  ? 33.551  44.075  93.865  1.00 94.78  ? 104 TRP A N     1 
ATOM   469  C  CA    . TRP A 1 77  ? 33.062  44.379  92.526  1.00 95.28  ? 104 TRP A CA    1 
ATOM   470  C  C     . TRP A 1 77  ? 33.540  43.352  91.507  1.00 98.04  ? 104 TRP A C     1 
ATOM   471  O  O     . TRP A 1 77  ? 32.750  42.889  90.676  1.00 93.29  ? 104 TRP A O     1 
ATOM   472  C  CB    . TRP A 1 77  ? 33.505  45.787  92.128  1.00 82.47  ? 104 TRP A CB    1 
ATOM   473  C  CG    . TRP A 1 77  ? 33.040  46.231  90.779  1.00 89.81  ? 104 TRP A CG    1 
ATOM   474  C  CD1   . TRP A 1 77  ? 31.767  46.568  90.419  1.00 94.20  ? 104 TRP A CD1   1 
ATOM   475  C  CD2   . TRP A 1 77  ? 33.849  46.413  89.610  1.00 86.79  ? 104 TRP A CD2   1 
ATOM   476  N  NE1   . TRP A 1 77  ? 31.732  46.938  89.095  1.00 92.33  ? 104 TRP A NE1   1 
ATOM   477  C  CE2   . TRP A 1 77  ? 32.998  46.852  88.577  1.00 80.53  ? 104 TRP A CE2   1 
ATOM   478  C  CE3   . TRP A 1 77  ? 35.209  46.244  89.337  1.00 87.88  ? 104 TRP A CE3   1 
ATOM   479  C  CZ2   . TRP A 1 77  ? 33.462  47.124  87.294  1.00 87.29  ? 104 TRP A CZ2   1 
ATOM   480  C  CZ3   . TRP A 1 77  ? 35.669  46.517  88.062  1.00 80.15  ? 104 TRP A CZ3   1 
ATOM   481  C  CH2   . TRP A 1 77  ? 34.798  46.949  87.056  1.00 77.28  ? 104 TRP A CH2   1 
ATOM   482  N  N     . LEU A 1 78  ? 34.823  42.982  91.559  1.00 101.87 ? 105 LEU A N     1 
ATOM   483  C  CA    . LEU A 1 78  ? 35.365  42.032  90.591  1.00 91.28  ? 105 LEU A CA    1 
ATOM   484  C  C     . LEU A 1 78  ? 34.665  40.682  90.683  1.00 100.68 ? 105 LEU A C     1 
ATOM   485  O  O     . LEU A 1 78  ? 34.369  40.059  89.656  1.00 100.31 ? 105 LEU A O     1 
ATOM   486  C  CB    . LEU A 1 78  ? 36.868  41.860  90.801  1.00 84.06  ? 105 LEU A CB    1 
ATOM   487  C  CG    . LEU A 1 78  ? 37.776  42.972  90.286  1.00 76.13  ? 105 LEU A CG    1 
ATOM   488  C  CD1   . LEU A 1 78  ? 39.224  42.563  90.452  1.00 78.10  ? 105 LEU A CD1   1 
ATOM   489  C  CD2   . LEU A 1 78  ? 37.472  43.287  88.833  1.00 83.00  ? 105 LEU A CD2   1 
ATOM   490  N  N     . VAL A 1 79  ? 34.399  40.210  91.904  1.00 97.01  ? 106 VAL A N     1 
ATOM   491  C  CA    . VAL A 1 79  ? 33.711  38.932  92.068  1.00 99.59  ? 106 VAL A CA    1 
ATOM   492  C  C     . VAL A 1 79  ? 32.323  38.984  91.445  1.00 91.94  ? 106 VAL A C     1 
ATOM   493  O  O     . VAL A 1 79  ? 31.832  37.980  90.913  1.00 101.54 ? 106 VAL A O     1 
ATOM   494  C  CB    . VAL A 1 79  ? 33.656  38.548  93.561  1.00 90.84  ? 106 VAL A CB    1 
ATOM   495  C  CG1   . VAL A 1 79  ? 32.786  37.319  93.772  1.00 99.67  ? 106 VAL A CG1   1 
ATOM   496  C  CG2   . VAL A 1 79  ? 35.058  38.296  94.091  1.00 89.12  ? 106 VAL A CG2   1 
ATOM   497  N  N     . ALA A 1 80  ? 31.684  40.154  91.466  1.00 89.00  ? 107 ALA A N     1 
ATOM   498  C  CA    . ALA A 1 80  ? 30.339  40.293  90.923  1.00 92.84  ? 107 ALA A CA    1 
ATOM   499  C  C     . ALA A 1 80  ? 30.316  40.409  89.404  1.00 97.77  ? 107 ALA A C     1 
ATOM   500  O  O     . ALA A 1 80  ? 29.287  40.103  88.791  1.00 102.95 ? 107 ALA A O     1 
ATOM   501  C  CB    . ALA A 1 80  ? 29.650  41.513  91.536  1.00 91.60  ? 107 ALA A CB    1 
ATOM   502  N  N     . VAL A 1 81  ? 31.413  40.840  88.784  1.00 91.88  ? 108 VAL A N     1 
ATOM   503  C  CA    . VAL A 1 81  ? 31.455  41.072  87.346  1.00 86.76  ? 108 VAL A CA    1 
ATOM   504  C  C     . VAL A 1 81  ? 32.440  40.164  86.631  1.00 88.01  ? 108 VAL A C     1 
ATOM   505  O  O     . VAL A 1 81  ? 32.563  40.254  85.405  1.00 94.00  ? 108 VAL A O     1 
ATOM   506  C  CB    . VAL A 1 81  ? 31.771  42.547  87.023  1.00 93.51  ? 108 VAL A CB    1 
ATOM   507  C  CG1   . VAL A 1 81  ? 30.742  43.471  87.660  1.00 78.04  ? 108 VAL A CG1   1 
ATOM   508  C  CG2   . VAL A 1 81  ? 33.185  42.901  87.473  1.00 79.28  ? 108 VAL A CG2   1 
ATOM   509  N  N     . LYS A 1 82  ? 33.156  39.300  87.357  1.00 92.73  ? 109 LYS A N     1 
ATOM   510  C  CA    . LYS A 1 82  ? 34.142  38.431  86.720  1.00 93.26  ? 109 LYS A CA    1 
ATOM   511  C  C     . LYS A 1 82  ? 33.515  37.615  85.596  1.00 85.00  ? 109 LYS A C     1 
ATOM   512  O  O     . LYS A 1 82  ? 34.081  37.513  84.503  1.00 96.45  ? 109 LYS A O     1 
ATOM   513  C  CB    . LYS A 1 82  ? 34.780  37.509  87.763  1.00 95.22  ? 109 LYS A CB    1 
ATOM   514  C  CG    . LYS A 1 82  ? 35.915  36.645  87.229  1.00 102.42 ? 109 LYS A CG    1 
ATOM   515  C  CD    . LYS A 1 82  ? 36.629  35.905  88.354  1.00 113.80 ? 109 LYS A CD    1 
ATOM   516  C  CE    . LYS A 1 82  ? 37.746  35.015  87.819  1.00 115.75 ? 109 LYS A CE    1 
ATOM   517  N  NZ    . LYS A 1 82  ? 38.817  35.795  87.132  1.00 116.28 ? 109 LYS A NZ    1 
ATOM   518  N  N     . SER A 1 83  ? 32.328  37.054  85.838  1.00 98.16  ? 110 SER A N     1 
ATOM   519  C  CA    . SER A 1 83  ? 31.670  36.179  84.875  1.00 95.63  ? 110 SER A CA    1 
ATOM   520  C  C     . SER A 1 83  ? 31.195  36.907  83.625  1.00 97.62  ? 110 SER A C     1 
ATOM   521  O  O     . SER A 1 83  ? 30.859  36.245  82.636  1.00 108.01 ? 110 SER A O     1 
ATOM   522  C  CB    . SER A 1 83  ? 30.479  35.483  85.537  1.00 86.81  ? 110 SER A CB    1 
ATOM   523  O  OG    . SER A 1 83  ? 29.527  36.431  85.984  1.00 102.11 ? 110 SER A OG    1 
ATOM   524  N  N     . LEU A 1 84  ? 31.158  38.237  83.635  1.00 89.36  ? 111 LEU A N     1 
ATOM   525  C  CA    . LEU A 1 84  ? 30.619  38.994  82.515  1.00 87.94  ? 111 LEU A CA    1 
ATOM   526  C  C     . LEU A 1 84  ? 31.683  39.454  81.528  1.00 94.40  ? 111 LEU A C     1 
ATOM   527  O  O     . LEU A 1 84  ? 31.332  39.905  80.432  1.00 92.46  ? 111 LEU A O     1 
ATOM   528  C  CB    . LEU A 1 84  ? 29.850  40.216  83.031  1.00 91.84  ? 111 LEU A CB    1 
ATOM   529  C  CG    . LEU A 1 84  ? 28.909  39.969  84.211  1.00 95.31  ? 111 LEU A CG    1 
ATOM   530  C  CD1   . LEU A 1 84  ? 28.261  41.268  84.642  1.00 96.10  ? 111 LEU A CD1   1 
ATOM   531  C  CD2   . LEU A 1 84  ? 27.858  38.929  83.858  1.00 105.25 ? 111 LEU A CD2   1 
ATOM   532  N  N     . TYR A 1 85  ? 32.961  39.347  81.876  1.00 88.57  ? 112 TYR A N     1 
ATOM   533  C  CA    . TYR A 1 85  ? 34.031  39.916  81.074  1.00 83.21  ? 112 TYR A CA    1 
ATOM   534  C  C     . TYR A 1 85  ? 34.937  38.821  80.525  1.00 85.21  ? 112 TYR A C     1 
ATOM   535  O  O     . TYR A 1 85  ? 34.983  37.700  81.039  1.00 82.78  ? 112 TYR A O     1 
ATOM   536  C  CB    . TYR A 1 85  ? 34.848  40.928  81.890  1.00 77.57  ? 112 TYR A CB    1 
ATOM   537  C  CG    . TYR A 1 85  ? 34.116  42.228  82.114  1.00 81.42  ? 112 TYR A CG    1 
ATOM   538  C  CD1   . TYR A 1 85  ? 33.257  42.389  83.193  1.00 83.48  ? 112 TYR A CD1   1 
ATOM   539  C  CD2   . TYR A 1 85  ? 34.267  43.291  81.232  1.00 86.10  ? 112 TYR A CD2   1 
ATOM   540  C  CE1   . TYR A 1 85  ? 32.576  43.577  83.393  1.00 88.32  ? 112 TYR A CE1   1 
ATOM   541  C  CE2   . TYR A 1 85  ? 33.592  44.479  81.423  1.00 84.38  ? 112 TYR A CE2   1 
ATOM   542  C  CZ    . TYR A 1 85  ? 32.747  44.620  82.504  1.00 78.09  ? 112 TYR A CZ    1 
ATOM   543  O  OH    . TYR A 1 85  ? 32.073  45.808  82.688  1.00 82.84  ? 112 TYR A OH    1 
ATOM   544  N  N     . HIS A 1 86  ? 35.663  39.175  79.462  1.00 80.05  ? 113 HIS A N     1 
ATOM   545  C  CA    . HIS A 1 86  ? 36.540  38.216  78.801  1.00 71.42  ? 113 HIS A CA    1 
ATOM   546  C  C     . HIS A 1 86  ? 37.600  37.679  79.756  1.00 77.32  ? 113 HIS A C     1 
ATOM   547  O  O     . HIS A 1 86  ? 37.920  36.483  79.731  1.00 81.06  ? 113 HIS A O     1 
ATOM   548  C  CB    . HIS A 1 86  ? 37.185  38.868  77.579  1.00 76.76  ? 113 HIS A CB    1 
ATOM   549  C  CG    . HIS A 1 86  ? 38.193  38.003  76.888  1.00 71.39  ? 113 HIS A CG    1 
ATOM   550  N  ND1   . HIS A 1 86  ? 39.552  38.165  77.057  1.00 74.05  ? 113 HIS A ND1   1 
ATOM   551  C  CD2   . HIS A 1 86  ? 38.041  36.975  76.022  1.00 71.66  ? 113 HIS A CD2   1 
ATOM   552  C  CE1   . HIS A 1 86  ? 40.194  37.269  76.328  1.00 68.91  ? 113 HIS A CE1   1 
ATOM   553  N  NE2   . HIS A 1 86  ? 39.300  36.535  75.690  1.00 79.11  ? 113 HIS A NE2   1 
ATOM   554  N  N     . SER A 1 87  ? 38.150  38.540  80.609  1.00 79.93  ? 114 SER A N     1 
ATOM   555  C  CA    . SER A 1 87  ? 39.151  38.115  81.578  1.00 71.38  ? 114 SER A CA    1 
ATOM   556  C  C     . SER A 1 87  ? 39.230  39.148  82.691  1.00 77.67  ? 114 SER A C     1 
ATOM   557  O  O     . SER A 1 87  ? 38.815  40.298  82.525  1.00 77.43  ? 114 SER A O     1 
ATOM   558  C  CB    . SER A 1 87  ? 40.526  37.934  80.930  1.00 62.47  ? 114 SER A CB    1 
ATOM   559  O  OG    . SER A 1 87  ? 41.226  39.167  80.898  1.00 81.52  ? 114 SER A OG    1 
ATOM   560  N  N     . VAL A 1 88  ? 39.778  38.719  83.828  1.00 75.62  ? 115 VAL A N     1 
ATOM   561  C  CA    . VAL A 1 88  ? 39.987  39.581  84.988  1.00 72.43  ? 115 VAL A CA    1 
ATOM   562  C  C     . VAL A 1 88  ? 41.336  39.228  85.600  1.00 81.51  ? 115 VAL A C     1 
ATOM   563  O  O     . VAL A 1 88  ? 41.528  38.103  86.075  1.00 101.18 ? 115 VAL A O     1 
ATOM   564  C  CB    . VAL A 1 88  ? 38.876  39.432  86.044  1.00 77.59  ? 115 VAL A CB    1 
ATOM   565  C  CG1   . VAL A 1 88  ? 39.321  40.040  87.368  1.00 80.67  ? 115 VAL A CG1   1 
ATOM   566  C  CG2   . VAL A 1 88  ? 37.582  40.080  85.564  1.00 73.09  ? 115 VAL A CG2   1 
ATOM   567  N  N     . GLU A 1 89  ? 42.270  40.174  85.578  1.00 75.81  ? 116 GLU A N     1 
ATOM   568  C  CA    . GLU A 1 89  ? 43.522  40.052  86.307  1.00 68.77  ? 116 GLU A CA    1 
ATOM   569  C  C     . GLU A 1 89  ? 43.465  40.963  87.525  1.00 90.37  ? 116 GLU A C     1 
ATOM   570  O  O     . GLU A 1 89  ? 42.961  42.088  87.446  1.00 84.24  ? 116 GLU A O     1 
ATOM   571  C  CB    . GLU A 1 89  ? 44.728  40.398  85.428  1.00 67.13  ? 116 GLU A CB    1 
ATOM   572  C  CG    . GLU A 1 89  ? 46.067  39.972  86.030  1.00 83.15  ? 116 GLU A CG    1 
ATOM   573  C  CD    . GLU A 1 89  ? 47.245  40.200  85.097  1.00 101.58 ? 116 GLU A CD    1 
ATOM   574  O  OE1   . GLU A 1 89  ? 47.033  40.274  83.865  1.00 98.87  ? 116 GLU A OE1   1 
ATOM   575  O  OE2   . GLU A 1 89  ? 48.386  40.312  85.600  1.00 105.63 ? 116 GLU A OE2   1 
ATOM   576  N  N     . TRP A 1 90  ? 43.981  40.474  88.649  1.00 89.03  ? 117 TRP A N     1 
ATOM   577  C  CA    . TRP A 1 90  ? 43.751  41.095  89.950  1.00 77.42  ? 117 TRP A CA    1 
ATOM   578  C  C     . TRP A 1 90  ? 45.049  41.034  90.744  1.00 85.03  ? 117 TRP A C     1 
ATOM   579  O  O     . TRP A 1 90  ? 45.528  39.943  91.067  1.00 98.93  ? 117 TRP A O     1 
ATOM   580  C  CB    . TRP A 1 90  ? 42.601  40.379  90.664  1.00 85.18  ? 117 TRP A CB    1 
ATOM   581  C  CG    . TRP A 1 90  ? 42.418  40.641  92.129  1.00 91.26  ? 117 TRP A CG    1 
ATOM   582  C  CD1   . TRP A 1 90  ? 42.406  39.707  93.121  1.00 85.96  ? 117 TRP A CD1   1 
ATOM   583  C  CD2   . TRP A 1 90  ? 42.180  41.903  92.765  1.00 94.07  ? 117 TRP A CD2   1 
ATOM   584  N  NE1   . TRP A 1 90  ? 42.189  40.305  94.336  1.00 92.60  ? 117 TRP A NE1   1 
ATOM   585  C  CE2   . TRP A 1 90  ? 42.049  41.654  94.147  1.00 94.93  ? 117 TRP A CE2   1 
ATOM   586  C  CE3   . TRP A 1 90  ? 42.077  43.219  92.306  1.00 87.04  ? 117 TRP A CE3   1 
ATOM   587  C  CZ2   . TRP A 1 90  ? 41.818  42.670  95.073  1.00 87.07  ? 117 TRP A CZ2   1 
ATOM   588  C  CZ3   . TRP A 1 90  ? 41.845  44.227  93.229  1.00 90.62  ? 117 TRP A CZ3   1 
ATOM   589  C  CH2   . TRP A 1 90  ? 41.720  43.946  94.595  1.00 94.06  ? 117 TRP A CH2   1 
ATOM   590  N  N     . ARG A 1 91  ? 45.633  42.200  91.035  1.00 78.28  ? 118 ARG A N     1 
ATOM   591  C  CA    . ARG A 1 91  ? 46.925  42.301  91.715  1.00 77.86  ? 118 ARG A CA    1 
ATOM   592  C  C     . ARG A 1 91  ? 46.783  43.155  92.970  1.00 89.46  ? 118 ARG A C     1 
ATOM   593  O  O     . ARG A 1 91  ? 46.993  44.379  92.928  1.00 90.20  ? 118 ARG A O     1 
ATOM   594  C  CB    . ARG A 1 91  ? 47.991  42.873  90.778  1.00 80.55  ? 118 ARG A CB    1 
ATOM   595  C  CG    . ARG A 1 91  ? 48.437  41.911  89.685  1.00 93.56  ? 118 ARG A CG    1 
ATOM   596  C  CD    . ARG A 1 91  ? 49.444  42.540  88.721  1.00 94.84  ? 118 ARG A CD    1 
ATOM   597  N  NE    . ARG A 1 91  ? 50.624  43.065  89.400  1.00 107.56 ? 118 ARG A NE    1 
ATOM   598  C  CZ    . ARG A 1 91  ? 51.776  43.341  88.801  1.00 111.26 ? 118 ARG A CZ    1 
ATOM   599  N  NH1   . ARG A 1 91  ? 51.955  43.113  87.508  1.00 83.80  ? 118 ARG A NH1   1 
ATOM   600  N  NH2   . ARG A 1 91  ? 52.774  43.853  89.518  1.00 89.07  ? 118 ARG A NH2   1 
ATOM   601  N  N     . PRO A 1 92  ? 46.419  42.556  94.114  1.00 91.89  ? 119 PRO A N     1 
ATOM   602  C  CA    . PRO A 1 92  ? 46.359  43.323  95.366  1.00 90.65  ? 119 PRO A CA    1 
ATOM   603  C  C     . PRO A 1 92  ? 47.617  43.185  96.214  1.00 89.65  ? 119 PRO A C     1 
ATOM   604  O  O     . PRO A 1 92  ? 48.330  42.181  96.121  1.00 89.36  ? 119 PRO A O     1 
ATOM   605  C  CB    . PRO A 1 92  ? 45.149  42.709  96.074  1.00 97.48  ? 119 PRO A CB    1 
ATOM   606  C  CG    . PRO A 1 92  ? 45.215  41.267  95.666  1.00 75.59  ? 119 PRO A CG    1 
ATOM   607  C  CD    . PRO A 1 92  ? 45.772  41.239  94.253  1.00 88.36  ? 119 PRO A CD    1 
ATOM   608  N  N     . ALA A 1 93  ? 47.892  44.184  97.054  1.00 93.48  ? 120 ALA A N     1 
ATOM   609  C  CA    . ALA A 1 93  ? 49.033  44.127  97.970  1.00 91.99  ? 120 ALA A CA    1 
ATOM   610  C  C     . ALA A 1 93  ? 48.658  44.918  99.221  1.00 93.63  ? 120 ALA A C     1 
ATOM   611  O  O     . ALA A 1 93  ? 48.676  46.152  99.205  1.00 98.92  ? 120 ALA A O     1 
ATOM   612  C  CB    . ALA A 1 93  ? 50.296  44.672  97.318  1.00 83.94  ? 120 ALA A CB    1 
ATOM   613  N  N     . GLU A 1 94  ? 48.330  44.202  100.299 1.00 89.60  ? 121 GLU A N     1 
ATOM   614  C  CA    . GLU A 1 94  ? 47.869  44.865  101.516 1.00 110.76 ? 121 GLU A CA    1 
ATOM   615  C  C     . GLU A 1 94  ? 49.013  45.576  102.233 1.00 104.82 ? 121 GLU A C     1 
ATOM   616  O  O     . GLU A 1 94  ? 48.885  46.742  102.622 1.00 113.94 ? 121 GLU A O     1 
ATOM   617  C  CB    . GLU A 1 94  ? 47.194  43.853  102.446 1.00 98.49  ? 121 GLU A CB    1 
ATOM   618  C  CG    . GLU A 1 94  ? 46.033  43.097  101.811 1.00 105.82 ? 121 GLU A CG    1 
ATOM   619  C  CD    . GLU A 1 94  ? 44.917  44.016  101.346 1.00 139.45 ? 121 GLU A CD    1 
ATOM   620  O  OE1   . GLU A 1 94  ? 44.562  44.950  102.098 1.00 140.94 ? 121 GLU A OE1   1 
ATOM   621  O  OE2   . GLU A 1 94  ? 44.401  43.807  100.225 1.00 134.24 ? 121 GLU A OE2   1 
ATOM   622  N  N     . GLU A 1 95  ? 50.139  44.889  102.424 1.00 107.39 ? 122 GLU A N     1 
ATOM   623  C  CA    . GLU A 1 95  ? 51.241  45.496  103.152 1.00 99.80  ? 122 GLU A CA    1 
ATOM   624  C  C     . GLU A 1 95  ? 52.358  45.906  102.200 1.00 105.34 ? 122 GLU A C     1 
ATOM   625  O  O     . GLU A 1 95  ? 52.683  45.163  101.267 1.00 111.74 ? 122 GLU A O     1 
ATOM   626  C  CB    . GLU A 1 95  ? 51.806  44.533  104.204 1.00 117.26 ? 122 GLU A CB    1 
ATOM   627  C  CG    . GLU A 1 95  ? 50.804  44.105  105.270 1.00 114.16 ? 122 GLU A CG    1 
ATOM   628  C  CD    . GLU A 1 95  ? 50.417  45.236  106.205 1.00 126.50 ? 122 GLU A CD    1 
ATOM   629  O  OE1   . GLU A 1 95  ? 51.155  46.244  106.266 1.00 139.21 ? 122 GLU A OE1   1 
ATOM   630  O  OE2   . GLU A 1 95  ? 49.371  45.118  106.881 1.00 115.34 ? 122 GLU A OE2   1 
ATOM   631  N  N     . PRO A 1 96  ? 52.955  47.087  102.401 1.00 100.75 ? 123 PRO A N     1 
ATOM   632  C  CA    . PRO A 1 96  ? 52.625  48.097  103.412 1.00 90.08  ? 123 PRO A CA    1 
ATOM   633  C  C     . PRO A 1 96  ? 51.497  49.003  102.943 1.00 109.07 ? 123 PRO A C     1 
ATOM   634  O  O     . PRO A 1 96  ? 51.114  48.978  101.770 1.00 113.39 ? 123 PRO A O     1 
ATOM   635  C  CB    . PRO A 1 96  ? 53.943  48.861  103.561 1.00 90.19  ? 123 PRO A CB    1 
ATOM   636  C  CG    . PRO A 1 96  ? 54.501  48.849  102.166 1.00 97.77  ? 123 PRO A CG    1 
ATOM   637  C  CD    . PRO A 1 96  ? 54.121  47.496  101.595 1.00 102.55 ? 123 PRO A CD    1 
ATOM   638  N  N     . ARG A 1 97  ? 50.953  49.828  103.832 1.00 95.90  ? 124 ARG A N     1 
ATOM   639  C  CA    . ARG A 1 97  ? 49.890  50.752  103.467 1.00 96.19  ? 124 ARG A CA    1 
ATOM   640  C  C     . ARG A 1 97  ? 50.412  52.120  103.048 1.00 98.35  ? 124 ARG A C     1 
ATOM   641  O  O     . ARG A 1 97  ? 49.610  52.987  102.683 1.00 103.29 ? 124 ARG A O     1 
ATOM   642  C  CB    . ARG A 1 97  ? 48.903  50.897  104.626 1.00 91.48  ? 124 ARG A CB    1 
ATOM   643  C  CG    . ARG A 1 97  ? 48.305  49.570  105.067 1.00 95.22  ? 124 ARG A CG    1 
ATOM   644  C  CD    . ARG A 1 97  ? 47.046  49.767  105.890 1.00 107.34 ? 124 ARG A CD    1 
ATOM   645  N  NE    . ARG A 1 97  ? 47.288  50.556  107.091 1.00 126.81 ? 124 ARG A NE    1 
ATOM   646  C  CZ    . ARG A 1 97  ? 46.356  50.865  107.982 1.00 132.91 ? 124 ARG A CZ    1 
ATOM   647  N  NH1   . ARG A 1 97  ? 45.103  50.462  107.839 1.00 129.19 ? 124 ARG A NH1   1 
ATOM   648  N  NH2   . ARG A 1 97  ? 46.688  51.597  109.042 1.00 130.36 ? 124 ARG A NH2   1 
ATOM   649  N  N     . SER A 1 98  ? 51.727  52.326  103.072 1.00 101.58 ? 125 SER A N     1 
ATOM   650  C  CA    . SER A 1 98  ? 52.320  53.591  102.664 1.00 92.77  ? 125 SER A CA    1 
ATOM   651  C  C     . SER A 1 98  ? 53.778  53.359  102.289 1.00 98.38  ? 125 SER A C     1 
ATOM   652  O  O     . SER A 1 98  ? 54.415  52.416  102.768 1.00 93.68  ? 125 SER A O     1 
ATOM   653  C  CB    . SER A 1 98  ? 52.202  54.641  103.772 1.00 85.47  ? 125 SER A CB    1 
ATOM   654  O  OG    . SER A 1 98  ? 52.600  54.103  105.015 1.00 93.00  ? 125 SER A OG    1 
ATOM   655  N  N     . TYR A 1 99  ? 54.297  54.235  101.422 1.00 93.61  ? 126 TYR A N     1 
ATOM   656  C  CA    . TYR A 1 99  ? 55.666  54.101  100.940 1.00 97.49  ? 126 TYR A CA    1 
ATOM   657  C  C     . TYR A 1 99  ? 56.659  54.542  102.015 1.00 93.76  ? 126 TYR A C     1 
ATOM   658  O  O     . TYR A 1 99  ? 56.408  55.515  102.730 1.00 111.03 ? 126 TYR A O     1 
ATOM   659  C  CB    . TYR A 1 99  ? 55.873  54.929  99.677  1.00 95.25  ? 126 TYR A CB    1 
ATOM   660  C  CG    . TYR A 1 99  ? 55.163  54.376  98.460  1.00 95.65  ? 126 TYR A CG    1 
ATOM   661  C  CD1   . TYR A 1 99  ? 53.846  54.726  98.180  1.00 92.80  ? 126 TYR A CD1   1 
ATOM   662  C  CD2   . TYR A 1 99  ? 55.807  53.505  97.590  1.00 79.25  ? 126 TYR A CD2   1 
ATOM   663  C  CE1   . TYR A 1 99  ? 53.193  54.228  97.069  1.00 82.53  ? 126 TYR A CE1   1 
ATOM   664  C  CE2   . TYR A 1 99  ? 55.160  53.004  96.477  1.00 85.61  ? 126 TYR A CE2   1 
ATOM   665  C  CZ    . TYR A 1 99  ? 53.854  53.369  96.222  1.00 80.78  ? 126 TYR A CZ    1 
ATOM   666  O  OH    . TYR A 1 99  ? 53.209  52.869  95.118  1.00 84.52  ? 126 TYR A OH    1 
ATOM   667  N  N     . PRO A 1 100 ? 57.792  53.845  102.149 1.00 94.72  ? 127 PRO A N     1 
ATOM   668  C  CA    . PRO A 1 100 ? 58.773  54.222  103.182 1.00 104.75 ? 127 PRO A CA    1 
ATOM   669  C  C     . PRO A 1 100 ? 59.463  55.557  102.934 1.00 102.91 ? 127 PRO A C     1 
ATOM   670  O  O     . PRO A 1 100 ? 60.166  56.039  103.831 1.00 109.69 ? 127 PRO A O     1 
ATOM   671  C  CB    . PRO A 1 100 ? 59.784  53.066  103.146 1.00 97.74  ? 127 PRO A CB    1 
ATOM   672  C  CG    . PRO A 1 100 ? 59.047  51.927  102.507 1.00 95.21  ? 127 PRO A CG    1 
ATOM   673  C  CD    . PRO A 1 100 ? 58.137  52.570  101.501 1.00 96.35  ? 127 PRO A CD    1 
ATOM   674  N  N     . ASP A 1 101 ? 59.294  56.170  101.761 1.00 98.85  ? 128 ASP A N     1 
ATOM   675  C  CA    . ASP A 1 101 ? 59.930  57.448  101.458 1.00 99.98  ? 128 ASP A CA    1 
ATOM   676  C  C     . ASP A 1 101 ? 58.910  58.553  101.197 1.00 106.54 ? 128 ASP A C     1 
ATOM   677  O  O     . ASP A 1 101 ? 59.260  59.595  100.631 1.00 102.25 ? 128 ASP A O     1 
ATOM   678  C  CB    . ASP A 1 101 ? 60.876  57.304  100.263 1.00 112.91 ? 128 ASP A CB    1 
ATOM   679  C  CG    . ASP A 1 101 ? 60.142  57.041  98.961  1.00 104.21 ? 128 ASP A CG    1 
ATOM   680  O  OD1   . ASP A 1 101 ? 58.983  56.575  99.005  1.00 102.99 ? 128 ASP A OD1   1 
ATOM   681  O  OD2   . ASP A 1 101 ? 60.730  57.301  97.889  1.00 108.52 ? 128 ASP A OD2   1 
ATOM   682  N  N     . GLU A 1 102 ? 57.658  58.347  101.595 1.00 103.59 ? 129 GLU A N     1 
ATOM   683  C  CA    . GLU A 1 102 ? 56.605  59.320  101.359 1.00 92.30  ? 129 GLU A CA    1 
ATOM   684  C  C     . GLU A 1 102 ? 56.471  60.274  102.541 1.00 99.45  ? 129 GLU A C     1 
ATOM   685  O  O     . GLU A 1 102 ? 56.889  59.983  103.665 1.00 99.91  ? 129 GLU A O     1 
ATOM   686  C  CB    . GLU A 1 102 ? 55.268  58.621  101.112 1.00 94.82  ? 129 GLU A CB    1 
ATOM   687  C  CG    . GLU A 1 102 ? 54.557  58.188  102.384 1.00 93.39  ? 129 GLU A CG    1 
ATOM   688  C  CD    . GLU A 1 102 ? 53.154  57.670  102.125 1.00 98.61  ? 129 GLU A CD    1 
ATOM   689  O  OE1   . GLU A 1 102 ? 52.928  57.076  101.046 1.00 99.92  ? 129 GLU A OE1   1 
ATOM   690  O  OE2   . GLU A 1 102 ? 52.278  57.865  102.998 1.00 96.46  ? 129 GLU A OE2   1 
ATOM   691  N  N     . GLU A 1 103 ? 55.878  61.433  102.265 1.00 105.11 ? 130 GLU A N     1 
ATOM   692  C  CA    . GLU A 1 103 ? 55.546  62.414  103.285 1.00 91.14  ? 130 GLU A CA    1 
ATOM   693  C  C     . GLU A 1 103 ? 54.055  62.459  103.573 1.00 90.09  ? 130 GLU A C     1 
ATOM   694  O  O     . GLU A 1 103 ? 53.620  63.255  104.409 1.00 93.08  ? 130 GLU A O     1 
ATOM   695  C  CB    . GLU A 1 103 ? 56.030  63.803  102.855 1.00 103.54 ? 130 GLU A CB    1 
ATOM   696  C  CG    . GLU A 1 103 ? 57.514  63.886  102.547 1.00 94.92  ? 130 GLU A CG    1 
ATOM   697  C  CD    . GLU A 1 103 ? 57.861  65.138  101.770 1.00 112.14 ? 130 GLU A CD    1 
ATOM   698  O  OE1   . GLU A 1 103 ? 56.974  66.002  101.614 1.00 110.58 ? 130 GLU A OE1   1 
ATOM   699  O  OE2   . GLU A 1 103 ? 59.014  65.258  101.307 1.00 122.13 ? 130 GLU A OE2   1 
ATOM   700  N  N     . GLY A 1 104 ? 53.267  61.629  102.901 1.00 88.68  ? 131 GLY A N     1 
ATOM   701  C  CA    . GLY A 1 104 ? 51.834  61.615  103.050 1.00 85.95  ? 131 GLY A CA    1 
ATOM   702  C  C     . GLY A 1 104 ? 51.206  60.806  101.935 1.00 91.49  ? 131 GLY A C     1 
ATOM   703  O  O     . GLY A 1 104 ? 51.887  60.363  101.006 1.00 95.24  ? 131 GLY A O     1 
ATOM   704  N  N     . PRO A 1 105 ? 49.890  60.592  102.006 1.00 94.19  ? 132 PRO A N     1 
ATOM   705  C  CA    . PRO A 1 105 ? 49.221  59.812  100.953 1.00 89.11  ? 132 PRO A CA    1 
ATOM   706  C  C     . PRO A 1 105 ? 49.149  60.529  99.614  1.00 88.63  ? 132 PRO A C     1 
ATOM   707  O  O     . PRO A 1 105 ? 49.025  59.862  98.577  1.00 82.01  ? 132 PRO A O     1 
ATOM   708  C  CB    . PRO A 1 105 ? 47.822  59.571  101.533 1.00 78.38  ? 132 PRO A CB    1 
ATOM   709  C  CG    . PRO A 1 105 ? 47.603  60.725  102.440 1.00 87.76  ? 132 PRO A CG    1 
ATOM   710  C  CD    . PRO A 1 105 ? 48.948  61.033  103.047 1.00 90.21  ? 132 PRO A CD    1 
ATOM   711  N  N     . LYS A 1 106 ? 49.222  61.857  99.597  1.00 91.55  ? 133 LYS A N     1 
ATOM   712  C  CA    . LYS A 1 106 ? 49.179  62.617  98.356  1.00 91.28  ? 133 LYS A CA    1 
ATOM   713  C  C     . LYS A 1 106 ? 50.562  63.058  97.893  1.00 81.73  ? 133 LYS A C     1 
ATOM   714  O  O     . LYS A 1 106 ? 50.665  63.841  96.946  1.00 98.65  ? 133 LYS A O     1 
ATOM   715  C  CB    . LYS A 1 106 ? 48.253  63.827  98.510  1.00 82.71  ? 133 LYS A CB    1 
ATOM   716  C  CG    . LYS A 1 106 ? 46.800  63.449  98.755  1.00 80.18  ? 133 LYS A CG    1 
ATOM   717  C  CD    . LYS A 1 106 ? 46.319  62.458  97.708  1.00 75.28  ? 133 LYS A CD    1 
ATOM   718  C  CE    . LYS A 1 106 ? 45.039  61.753  98.133  1.00 96.91  ? 133 LYS A CE    1 
ATOM   719  N  NZ    . LYS A 1 106 ? 44.564  60.769  97.108  1.00 83.28  ? 133 LYS A NZ    1 
ATOM   720  N  N     . HIS A 1 107 ? 51.622  62.570  98.533  1.00 89.68  ? 134 HIS A N     1 
ATOM   721  C  CA    . HIS A 1 107 ? 52.984  62.858  98.107  1.00 82.58  ? 134 HIS A CA    1 
ATOM   722  C  C     . HIS A 1 107 ? 53.445  61.789  97.127  1.00 89.70  ? 134 HIS A C     1 
ATOM   723  O  O     . HIS A 1 107 ? 53.325  60.590  97.404  1.00 93.39  ? 134 HIS A O     1 
ATOM   724  C  CB    . HIS A 1 107 ? 53.933  62.915  99.305  1.00 97.96  ? 134 HIS A CB    1 
ATOM   725  C  CG    . HIS A 1 107 ? 55.370  63.103  98.926  1.00 101.73 ? 134 HIS A CG    1 
ATOM   726  N  ND1   . HIS A 1 107 ? 56.409  62.560  99.653  1.00 100.15 ? 134 HIS A ND1   1 
ATOM   727  C  CD2   . HIS A 1 107 ? 55.942  63.776  97.900  1.00 99.62  ? 134 HIS A CD2   1 
ATOM   728  C  CE1   . HIS A 1 107 ? 57.557  62.887  99.088  1.00 106.35 ? 134 HIS A CE1   1 
ATOM   729  N  NE2   . HIS A 1 107 ? 57.303  63.624  98.022  1.00 95.90  ? 134 HIS A NE2   1 
ATOM   730  N  N     . TRP A 1 108 ? 53.974  62.227  95.986  1.00 97.91  ? 135 TRP A N     1 
ATOM   731  C  CA    . TRP A 1 108 ? 54.448  61.331  94.930  1.00 95.63  ? 135 TRP A CA    1 
ATOM   732  C  C     . TRP A 1 108 ? 55.963  61.200  95.047  1.00 99.86  ? 135 TRP A C     1 
ATOM   733  O  O     . TRP A 1 108 ? 56.721  61.959  94.441  1.00 100.18 ? 135 TRP A O     1 
ATOM   734  C  CB    . TRP A 1 108 ? 54.038  61.850  93.558  1.00 89.32  ? 135 TRP A CB    1 
ATOM   735  C  CG    . TRP A 1 108 ? 52.634  61.510  93.198  1.00 81.53  ? 135 TRP A CG    1 
ATOM   736  C  CD1   . TRP A 1 108 ? 51.514  62.209  93.528  1.00 84.21  ? 135 TRP A CD1   1 
ATOM   737  C  CD2   . TRP A 1 108 ? 52.194  60.377  92.440  1.00 89.27  ? 135 TRP A CD2   1 
ATOM   738  N  NE1   . TRP A 1 108 ? 50.399  61.585  93.019  1.00 90.86  ? 135 TRP A NE1   1 
ATOM   739  C  CE2   . TRP A 1 108 ? 50.789  60.457  92.348  1.00 85.22  ? 135 TRP A CE2   1 
ATOM   740  C  CE3   . TRP A 1 108 ? 52.852  59.305  91.828  1.00 75.13  ? 135 TRP A CE3   1 
ATOM   741  C  CZ2   . TRP A 1 108 ? 50.029  59.506  91.670  1.00 84.17  ? 135 TRP A CZ2   1 
ATOM   742  C  CZ3   . TRP A 1 108 ? 52.098  58.362  91.160  1.00 80.00  ? 135 TRP A CZ3   1 
ATOM   743  C  CH2   . TRP A 1 108 ? 50.700  58.468  91.084  1.00 83.18  ? 135 TRP A CH2   1 
ATOM   744  N  N     . SER A 1 109 ? 56.405  60.220  95.832  1.00 87.48  ? 136 SER A N     1 
ATOM   745  C  CA    . SER A 1 109 ? 57.827  59.950  95.954  1.00 93.11  ? 136 SER A CA    1 
ATOM   746  C  C     . SER A 1 109 ? 58.324  59.183  94.730  1.00 99.27  ? 136 SER A C     1 
ATOM   747  O  O     . SER A 1 109 ? 57.550  58.770  93.861  1.00 95.24  ? 136 SER A O     1 
ATOM   748  C  CB    . SER A 1 109 ? 58.120  59.162  97.229  1.00 98.73  ? 136 SER A CB    1 
ATOM   749  O  OG    . SER A 1 109 ? 57.816  57.787  97.058  1.00 95.05  ? 136 SER A OG    1 
ATOM   750  N  N     . ASP A 1 110 ? 59.644  58.993  94.663  1.00 96.20  ? 137 ASP A N     1 
ATOM   751  C  CA    . ASP A 1 110 ? 60.207  58.249  93.542  1.00 95.72  ? 137 ASP A CA    1 
ATOM   752  C  C     . ASP A 1 110 ? 59.795  56.784  93.581  1.00 100.19 ? 137 ASP A C     1 
ATOM   753  O  O     . ASP A 1 110 ? 59.605  56.171  92.525  1.00 93.41  ? 137 ASP A O     1 
ATOM   754  C  CB    . ASP A 1 110 ? 61.730  58.382  93.526  1.00 101.72 ? 137 ASP A CB    1 
ATOM   755  C  CG    . ASP A 1 110 ? 62.186  59.777  93.139  1.00 103.63 ? 137 ASP A CG    1 
ATOM   756  O  OD1   . ASP A 1 110 ? 61.315  60.636  92.885  1.00 107.28 ? 137 ASP A OD1   1 
ATOM   757  O  OD2   . ASP A 1 110 ? 63.412  60.014  93.088  1.00 103.80 ? 137 ASP A OD2   1 
ATOM   758  N  N     . SER A 1 111 ? 59.644  56.210  94.778  1.00 98.17  ? 138 SER A N     1 
ATOM   759  C  CA    . SER A 1 111 ? 59.145  54.842  94.875  1.00 89.00  ? 138 SER A CA    1 
ATOM   760  C  C     . SER A 1 111 ? 57.716  54.746  94.358  1.00 90.18  ? 138 SER A C     1 
ATOM   761  O  O     . SER A 1 111 ? 57.348  53.763  93.704  1.00 90.92  ? 138 SER A O     1 
ATOM   762  C  CB    . SER A 1 111 ? 59.229  54.351  96.320  1.00 87.59  ? 138 SER A CB    1 
ATOM   763  O  OG    . SER A 1 111 ? 60.576  54.276  96.756  1.00 106.07 ? 138 SER A OG    1 
ATOM   764  N  N     . ARG A 1 112 ? 56.898  55.763  94.638  1.00 91.04  ? 139 ARG A N     1 
ATOM   765  C  CA    . ARG A 1 112 ? 55.530  55.779  94.133  1.00 87.51  ? 139 ARG A CA    1 
ATOM   766  C  C     . ARG A 1 112 ? 55.515  55.975  92.621  1.00 84.95  ? 139 ARG A C     1 
ATOM   767  O  O     . ARG A 1 112 ? 54.800  55.271  91.900  1.00 83.32  ? 139 ARG A O     1 
ATOM   768  C  CB    . ARG A 1 112 ? 54.729  56.876  94.840  1.00 83.31  ? 139 ARG A CB    1 
ATOM   769  C  CG    . ARG A 1 112 ? 53.237  56.866  94.529  1.00 83.72  ? 139 ARG A CG    1 
ATOM   770  C  CD    . ARG A 1 112 ? 52.529  58.059  95.163  1.00 86.42  ? 139 ARG A CD    1 
ATOM   771  N  NE    . ARG A 1 112 ? 51.090  58.036  94.926  1.00 76.84  ? 139 ARG A NE    1 
ATOM   772  C  CZ    . ARG A 1 112 ? 50.219  58.843  95.517  1.00 79.93  ? 139 ARG A CZ    1 
ATOM   773  N  NH1   . ARG A 1 112 ? 50.607  59.766  96.383  1.00 83.60  ? 139 ARG A NH1   1 
ATOM   774  N  NH2   . ARG A 1 112 ? 48.925  58.718  95.235  1.00 88.10  ? 139 ARG A NH2   1 
ATOM   775  N  N     . TYR A 1 113 ? 56.302  56.933  92.126  1.00 84.41  ? 140 TYR A N     1 
ATOM   776  C  CA    . TYR A 1 113 ? 56.468  57.098  90.685  1.00 80.07  ? 140 TYR A CA    1 
ATOM   777  C  C     . TYR A 1 113 ? 56.950  55.807  90.038  1.00 84.16  ? 140 TYR A C     1 
ATOM   778  O  O     . TYR A 1 113 ? 56.392  55.355  89.032  1.00 83.18  ? 140 TYR A O     1 
ATOM   779  C  CB    . TYR A 1 113 ? 57.460  58.225  90.400  1.00 82.38  ? 140 TYR A CB    1 
ATOM   780  C  CG    . TYR A 1 113 ? 56.864  59.613  90.351  1.00 88.28  ? 140 TYR A CG    1 
ATOM   781  C  CD1   . TYR A 1 113 ? 55.641  59.849  89.732  1.00 78.78  ? 140 TYR A CD1   1 
ATOM   782  C  CD2   . TYR A 1 113 ? 57.538  60.693  90.913  1.00 84.25  ? 140 TYR A CD2   1 
ATOM   783  C  CE1   . TYR A 1 113 ? 55.106  61.122  89.681  1.00 83.55  ? 140 TYR A CE1   1 
ATOM   784  C  CE2   . TYR A 1 113 ? 57.013  61.968  90.867  1.00 80.30  ? 140 TYR A CE2   1 
ATOM   785  C  CZ    . TYR A 1 113 ? 55.799  62.179  90.251  1.00 89.40  ? 140 TYR A CZ    1 
ATOM   786  O  OH    . TYR A 1 113 ? 55.282  63.455  90.209  1.00 92.47  ? 140 TYR A OH    1 
ATOM   787  N  N     . GLU A 1 114 ? 57.992  55.199  90.608  1.00 86.95  ? 141 GLU A N     1 
ATOM   788  C  CA    . GLU A 1 114 ? 58.552  53.979  90.035  1.00 80.65  ? 141 GLU A CA    1 
ATOM   789  C  C     . GLU A 1 114 ? 57.531  52.851  90.029  1.00 78.19  ? 141 GLU A C     1 
ATOM   790  O  O     . GLU A 1 114 ? 57.366  52.154  89.021  1.00 82.78  ? 141 GLU A O     1 
ATOM   791  C  CB    . GLU A 1 114 ? 59.803  53.561  90.808  1.00 83.98  ? 141 GLU A CB    1 
ATOM   792  C  CG    . GLU A 1 114 ? 60.330  52.188  90.429  1.00 95.83  ? 141 GLU A CG    1 
ATOM   793  C  CD    . GLU A 1 114 ? 61.520  51.771  91.267  1.00 90.92  ? 141 GLU A CD    1 
ATOM   794  O  OE1   . GLU A 1 114 ? 62.353  52.645  91.594  1.00 95.80  ? 141 GLU A OE1   1 
ATOM   795  O  OE2   . GLU A 1 114 ? 61.615  50.572  91.607  1.00 100.91 ? 141 GLU A OE2   1 
ATOM   796  N  N     . HIS A 1 115 ? 56.833  52.652  91.150  1.00 75.62  ? 142 HIS A N     1 
ATOM   797  C  CA    . HIS A 1 115 ? 55.862  51.565  91.221  1.00 79.86  ? 142 HIS A CA    1 
ATOM   798  C  C     . HIS A 1 115 ? 54.706  51.788  90.254  1.00 77.46  ? 142 HIS A C     1 
ATOM   799  O  O     . HIS A 1 115 ? 54.253  50.845  89.595  1.00 79.08  ? 142 HIS A O     1 
ATOM   800  C  CB    . HIS A 1 115 ? 55.340  51.411  92.649  1.00 86.59  ? 142 HIS A CB    1 
ATOM   801  C  CG    . HIS A 1 115 ? 54.381  50.275  92.817  1.00 78.17  ? 142 HIS A CG    1 
ATOM   802  N  ND1   . HIS A 1 115 ? 54.775  48.955  92.757  1.00 76.08  ? 142 HIS A ND1   1 
ATOM   803  C  CD2   . HIS A 1 115 ? 53.044  50.260  93.030  1.00 77.71  ? 142 HIS A CD2   1 
ATOM   804  C  CE1   . HIS A 1 115 ? 53.722  48.177  92.936  1.00 86.42  ? 142 HIS A CE1   1 
ATOM   805  N  NE2   . HIS A 1 115 ? 52.659  48.943  93.102  1.00 85.21  ? 142 HIS A NE2   1 
ATOM   806  N  N     . VAL A 1 116 ? 54.223  53.028  90.148  1.00 84.34  ? 143 VAL A N     1 
ATOM   807  C  CA    . VAL A 1 116 ? 53.105  53.320  89.255  1.00 86.22  ? 143 VAL A CA    1 
ATOM   808  C  C     . VAL A 1 116 ? 53.512  53.117  87.799  1.00 81.41  ? 143 VAL A C     1 
ATOM   809  O  O     . VAL A 1 116 ? 52.742  52.576  86.994  1.00 77.24  ? 143 VAL A O     1 
ATOM   810  C  CB    . VAL A 1 116 ? 52.576  54.743  89.515  1.00 80.09  ? 143 VAL A CB    1 
ATOM   811  C  CG1   . VAL A 1 116 ? 51.660  55.191  88.396  1.00 59.83  ? 143 VAL A CG1   1 
ATOM   812  C  CG2   . VAL A 1 116 ? 51.838  54.787  90.847  1.00 72.96  ? 143 VAL A CG2   1 
ATOM   813  N  N     . MET A 1 117 ? 54.731  53.529  87.439  1.00 82.51  ? 144 MET A N     1 
ATOM   814  C  CA    . MET A 1 117 ? 55.226  53.267  86.091  1.00 74.47  ? 144 MET A CA    1 
ATOM   815  C  C     . MET A 1 117 ? 55.335  51.772  85.823  1.00 67.10  ? 144 MET A C     1 
ATOM   816  O  O     . MET A 1 117 ? 55.028  51.311  84.718  1.00 77.55  ? 144 MET A O     1 
ATOM   817  C  CB    . MET A 1 117 ? 56.580  53.942  85.876  1.00 80.68  ? 144 MET A CB    1 
ATOM   818  C  CG    . MET A 1 117 ? 56.506  55.447  85.708  1.00 79.20  ? 144 MET A CG    1 
ATOM   819  S  SD    . MET A 1 117 ? 58.083  56.152  85.193  1.00 81.21  ? 144 MET A SD    1 
ATOM   820  C  CE    . MET A 1 117 ? 58.487  57.174  86.607  1.00 85.63  ? 144 MET A CE    1 
ATOM   821  N  N     . LYS A 1 118 ? 55.769  50.996  86.820  1.00 81.38  ? 145 LYS A N     1 
ATOM   822  C  CA    . LYS A 1 118 ? 55.869  49.552  86.631  1.00 84.38  ? 145 LYS A CA    1 
ATOM   823  C  C     . LYS A 1 118 ? 54.492  48.922  86.461  1.00 75.56  ? 145 LYS A C     1 
ATOM   824  O  O     . LYS A 1 118 ? 54.319  48.005  85.650  1.00 68.66  ? 145 LYS A O     1 
ATOM   825  C  CB    . LYS A 1 118 ? 56.620  48.913  87.804  1.00 64.62  ? 145 LYS A CB    1 
ATOM   826  C  CG    . LYS A 1 118 ? 58.080  49.340  87.901  1.00 61.81  ? 145 LYS A CG    1 
ATOM   827  C  CD    . LYS A 1 118 ? 58.914  48.404  88.754  1.00 78.67  ? 145 LYS A CD    1 
ATOM   828  C  CE    . LYS A 1 118 ? 60.397  48.765  88.676  1.00 71.00  ? 145 LYS A CE    1 
ATOM   829  N  NZ    . LYS A 1 118 ? 61.270  47.724  89.301  1.00 91.33  ? 145 LYS A NZ    1 
ATOM   830  N  N     . LEU A 1 119 ? 53.495  49.418  87.197  1.00 69.00  ? 146 LEU A N     1 
ATOM   831  C  CA    . LEU A 1 119 ? 52.151  48.867  87.071  1.00 73.57  ? 146 LEU A CA    1 
ATOM   832  C  C     . LEU A 1 119 ? 51.561  49.154  85.696  1.00 79.23  ? 146 LEU A C     1 
ATOM   833  O  O     . LEU A 1 119 ? 50.923  48.280  85.100  1.00 75.73  ? 146 LEU A O     1 
ATOM   834  C  CB    . LEU A 1 119 ? 51.252  49.419  88.177  1.00 79.16  ? 146 LEU A CB    1 
ATOM   835  C  CG    . LEU A 1 119 ? 51.507  48.877  89.586  1.00 72.83  ? 146 LEU A CG    1 
ATOM   836  C  CD1   . LEU A 1 119 ? 50.623  49.580  90.594  1.00 78.89  ? 146 LEU A CD1   1 
ATOM   837  C  CD2   . LEU A 1 119 ? 51.267  47.385  89.623  1.00 67.19  ? 146 LEU A CD2   1 
ATOM   838  N  N     . ARG A 1 120 ? 51.766  50.367  85.170  1.00 67.32  ? 147 ARG A N     1 
ATOM   839  C  CA    . ARG A 1 120 ? 51.236  50.674  83.845  1.00 65.95  ? 147 ARG A CA    1 
ATOM   840  C  C     . ARG A 1 120 ? 51.957  49.876  82.768  1.00 74.36  ? 147 ARG A C     1 
ATOM   841  O  O     . ARG A 1 120 ? 51.327  49.395  81.818  1.00 80.90  ? 147 ARG A O     1 
ATOM   842  C  CB    . ARG A 1 120 ? 51.328  52.174  83.567  1.00 68.41  ? 147 ARG A CB    1 
ATOM   843  C  CG    . ARG A 1 120 ? 50.383  52.996  84.424  1.00 77.46  ? 147 ARG A CG    1 
ATOM   844  C  CD    . ARG A 1 120 ? 50.109  54.361  83.829  1.00 62.84  ? 147 ARG A CD    1 
ATOM   845  N  NE    . ARG A 1 120 ? 49.048  55.038  84.563  1.00 69.74  ? 147 ARG A NE    1 
ATOM   846  C  CZ    . ARG A 1 120 ? 49.235  56.041  85.410  1.00 70.09  ? 147 ARG A CZ    1 
ATOM   847  N  NH1   . ARG A 1 120 ? 50.432  56.569  85.606  1.00 75.61  ? 147 ARG A NH1   1 
ATOM   848  N  NH2   . ARG A 1 120 ? 48.194  56.526  86.079  1.00 78.31  ? 147 ARG A NH2   1 
ATOM   849  N  N     . GLN A 1 121 ? 53.276  49.725  82.901  1.00 72.42  ? 148 GLN A N     1 
ATOM   850  C  CA    . GLN A 1 121 ? 54.019  48.844  82.006  1.00 59.31  ? 148 GLN A CA    1 
ATOM   851  C  C     . GLN A 1 121 ? 53.496  47.415  82.085  1.00 71.52  ? 148 GLN A C     1 
ATOM   852  O  O     . GLN A 1 121 ? 53.347  46.742  81.058  1.00 68.40  ? 148 GLN A O     1 
ATOM   853  C  CB    . GLN A 1 121 ? 55.504  48.884  82.356  1.00 62.88  ? 148 GLN A CB    1 
ATOM   854  C  CG    . GLN A 1 121 ? 56.372  48.045  81.449  1.00 60.46  ? 148 GLN A CG    1 
ATOM   855  C  CD    . GLN A 1 121 ? 56.488  48.639  80.065  1.00 63.75  ? 148 GLN A CD    1 
ATOM   856  O  OE1   . GLN A 1 121 ? 56.298  49.844  79.877  1.00 64.38  ? 148 GLN A OE1   1 
ATOM   857  N  NE2   . GLN A 1 121 ? 56.797  47.799  79.085  1.00 66.30  ? 148 GLN A NE2   1 
ATOM   858  N  N     . ALA A 1 122 ? 53.213  46.937  83.300  1.00 72.29  ? 149 ALA A N     1 
ATOM   859  C  CA    . ALA A 1 122 ? 52.684  45.587  83.465  1.00 62.39  ? 149 ALA A CA    1 
ATOM   860  C  C     . ALA A 1 122 ? 51.316  45.448  82.813  1.00 64.97  ? 149 ALA A C     1 
ATOM   861  O  O     . ALA A 1 122 ? 51.003  44.407  82.224  1.00 72.89  ? 149 ALA A O     1 
ATOM   862  C  CB    . ALA A 1 122 ? 52.609  45.232  84.949  1.00 61.10  ? 149 ALA A CB    1 
ATOM   863  N  N     . ALA A 1 123 ? 50.483  46.488  82.910  1.00 63.86  ? 150 ALA A N     1 
ATOM   864  C  CA    . ALA A 1 123 ? 49.187  46.460  82.240  1.00 76.48  ? 150 ALA A CA    1 
ATOM   865  C  C     . ALA A 1 123 ? 49.350  46.456  80.724  1.00 75.19  ? 150 ALA A C     1 
ATOM   866  O  O     . ALA A 1 123 ? 48.601  45.772  80.015  1.00 69.64  ? 150 ALA A O     1 
ATOM   867  C  CB    . ALA A 1 123 ? 48.338  47.649  82.691  1.00 63.73  ? 150 ALA A CB    1 
ATOM   868  N  N     . LEU A 1 124 ? 50.322  47.213  80.208  1.00 69.53  ? 151 LEU A N     1 
ATOM   869  C  CA    . LEU A 1 124 ? 50.572  47.219  78.770  1.00 60.83  ? 151 LEU A CA    1 
ATOM   870  C  C     . LEU A 1 124 ? 51.049  45.853  78.289  1.00 71.77  ? 151 LEU A C     1 
ATOM   871  O  O     . LEU A 1 124 ? 50.617  45.372  77.234  1.00 66.43  ? 151 LEU A O     1 
ATOM   872  C  CB    . LEU A 1 124 ? 51.594  48.304  78.426  1.00 61.17  ? 151 LEU A CB    1 
ATOM   873  C  CG    . LEU A 1 124 ? 51.978  48.493  76.956  1.00 60.91  ? 151 LEU A CG    1 
ATOM   874  C  CD1   . LEU A 1 124 ? 50.771  48.885  76.128  1.00 58.40  ? 151 LEU A CD1   1 
ATOM   875  C  CD2   . LEU A 1 124 ? 53.065  49.539  76.833  1.00 63.54  ? 151 LEU A CD2   1 
ATOM   876  N  N     . LYS A 1 125 ? 51.939  45.210  79.047  1.00 63.67  ? 152 LYS A N     1 
ATOM   877  C  CA    . LYS A 1 125 ? 52.382  43.872  78.673  1.00 64.60  ? 152 LYS A CA    1 
ATOM   878  C  C     . LYS A 1 125 ? 51.221  42.887  78.706  1.00 74.70  ? 152 LYS A C     1 
ATOM   879  O  O     . LYS A 1 125 ? 51.110  42.015  77.834  1.00 66.73  ? 152 LYS A O     1 
ATOM   880  C  CB    . LYS A 1 125 ? 53.516  43.414  79.596  1.00 63.25  ? 152 LYS A CB    1 
ATOM   881  C  CG    . LYS A 1 125 ? 53.980  41.971  79.369  1.00 56.17  ? 152 LYS A CG    1 
ATOM   882  C  CD    . LYS A 1 125 ? 55.152  41.620  80.275  1.00 54.01  ? 152 LYS A CD    1 
ATOM   883  C  CE    . LYS A 1 125 ? 55.526  40.150  80.176  1.00 55.60  ? 152 LYS A CE    1 
ATOM   884  N  NZ    . LYS A 1 125 ? 56.140  39.808  78.865  1.00 79.76  ? 152 LYS A NZ    1 
ATOM   885  N  N     . SER A 1 126 ? 50.337  43.018  79.699  1.00 66.78  ? 153 SER A N     1 
ATOM   886  C  CA    . SER A 1 126 ? 49.159  42.159  79.760  1.00 67.23  ? 153 SER A CA    1 
ATOM   887  C  C     . SER A 1 126 ? 48.299  42.326  78.514  1.00 70.01  ? 153 SER A C     1 
ATOM   888  O  O     . SER A 1 126 ? 47.929  41.343  77.861  1.00 73.54  ? 153 SER A O     1 
ATOM   889  C  CB    . SER A 1 126 ? 48.353  42.467  81.020  1.00 65.87  ? 153 SER A CB    1 
ATOM   890  O  OG    . SER A 1 126 ? 49.043  42.028  82.177  1.00 85.38  ? 153 SER A OG    1 
ATOM   891  N  N     . ALA A 1 127 ? 47.983  43.572  78.162  1.00 64.99  ? 154 ALA A N     1 
ATOM   892  C  CA    . ALA A 1 127 ? 47.190  43.820  76.964  1.00 69.73  ? 154 ALA A CA    1 
ATOM   893  C  C     . ALA A 1 127 ? 47.843  43.208  75.732  1.00 66.10  ? 154 ALA A C     1 
ATOM   894  O  O     . ALA A 1 127 ? 47.163  42.602  74.896  1.00 67.97  ? 154 ALA A O     1 
ATOM   895  C  CB    . ALA A 1 127 ? 46.981  45.321  76.784  1.00 60.58  ? 154 ALA A CB    1 
ATOM   896  N  N     . ARG A 1 128 ? 49.165  43.333  75.613  1.00 67.38  ? 155 ARG A N     1 
ATOM   897  C  CA    . ARG A 1 128 ? 49.855  42.744  74.472  1.00 57.73  ? 155 ARG A CA    1 
ATOM   898  C  C     . ARG A 1 128 ? 49.798  41.221  74.514  1.00 68.64  ? 155 ARG A C     1 
ATOM   899  O  O     . ARG A 1 128 ? 49.534  40.578  73.491  1.00 67.64  ? 155 ARG A O     1 
ATOM   900  C  CB    . ARG A 1 128 ? 51.303  43.229  74.430  1.00 54.77  ? 155 ARG A CB    1 
ATOM   901  C  CG    . ARG A 1 128 ? 51.472  44.699  74.059  1.00 55.11  ? 155 ARG A CG    1 
ATOM   902  C  CD    . ARG A 1 128 ? 52.857  45.205  74.458  1.00 69.00  ? 155 ARG A CD    1 
ATOM   903  N  NE    . ARG A 1 128 ? 53.162  46.523  73.914  1.00 61.35  ? 155 ARG A NE    1 
ATOM   904  C  CZ    . ARG A 1 128 ? 54.153  47.295  74.339  1.00 72.80  ? 155 ARG A CZ    1 
ATOM   905  N  NH1   . ARG A 1 128 ? 54.922  46.936  75.357  1.00 68.04  ? 155 ARG A NH1   1 
ATOM   906  N  NH2   . ARG A 1 128 ? 54.381  48.456  73.730  1.00 64.49  ? 155 ARG A NH2   1 
ATOM   907  N  N     . ASP A 1 129 ? 50.023  40.625  75.689  1.00 69.51  ? 156 ASP A N     1 
ATOM   908  C  CA    . ASP A 1 129 ? 50.079  39.166  75.777  1.00 67.38  ? 156 ASP A CA    1 
ATOM   909  C  C     . ASP A 1 129 ? 48.721  38.522  75.511  1.00 62.84  ? 156 ASP A C     1 
ATOM   910  O  O     . ASP A 1 129 ? 48.662  37.401  74.993  1.00 79.17  ? 156 ASP A O     1 
ATOM   911  C  CB    . ASP A 1 129 ? 50.611  38.739  77.145  1.00 63.81  ? 156 ASP A CB    1 
ATOM   912  C  CG    . ASP A 1 129 ? 52.078  39.097  77.342  1.00 78.76  ? 156 ASP A CG    1 
ATOM   913  O  OD1   . ASP A 1 129 ? 52.740  39.474  76.348  1.00 83.86  ? 156 ASP A OD1   1 
ATOM   914  O  OD2   . ASP A 1 129 ? 52.568  39.012  78.491  1.00 77.70  ? 156 ASP A OD2   1 
ATOM   915  N  N     . MET A 1 130 ? 47.628  39.204  75.845  1.00 62.82  ? 157 MET A N     1 
ATOM   916  C  CA    . MET A 1 130 ? 46.290  38.691  75.591  1.00 52.94  ? 157 MET A CA    1 
ATOM   917  C  C     . MET A 1 130 ? 45.739  39.121  74.235  1.00 72.29  ? 157 MET A C     1 
ATOM   918  O  O     . MET A 1 130 ? 44.554  38.899  73.966  1.00 75.88  ? 157 MET A O     1 
ATOM   919  C  CB    . MET A 1 130 ? 45.337  39.133  76.702  1.00 54.67  ? 157 MET A CB    1 
ATOM   920  C  CG    . MET A 1 130 ? 44.987  40.608  76.684  1.00 58.03  ? 157 MET A CG    1 
ATOM   921  S  SD    . MET A 1 130 ? 44.064  41.065  78.154  1.00 74.51  ? 157 MET A SD    1 
ATOM   922  C  CE    . MET A 1 130 ? 42.756  39.845  78.112  1.00 80.58  ? 157 MET A CE    1 
ATOM   923  N  N     . TRP A 1 131 ? 46.567  39.737  73.385  1.00 65.14  ? 158 TRP A N     1 
ATOM   924  C  CA    . TRP A 1 131 ? 46.190  40.062  72.007  1.00 68.13  ? 158 TRP A CA    1 
ATOM   925  C  C     . TRP A 1 131 ? 44.998  41.017  71.957  1.00 75.55  ? 158 TRP A C     1 
ATOM   926  O  O     . TRP A 1 131 ? 44.119  40.900  71.100  1.00 69.34  ? 158 TRP A O     1 
ATOM   927  C  CB    . TRP A 1 131 ? 45.905  38.793  71.200  1.00 59.97  ? 158 TRP A CB    1 
ATOM   928  C  CG    . TRP A 1 131 ? 47.095  38.257  70.459  1.00 64.00  ? 158 TRP A CG    1 
ATOM   929  C  CD1   . TRP A 1 131 ? 48.305  38.866  70.299  1.00 71.25  ? 158 TRP A CD1   1 
ATOM   930  C  CD2   . TRP A 1 131 ? 47.181  37.005  69.763  1.00 65.68  ? 158 TRP A CD2   1 
ATOM   931  N  NE1   . TRP A 1 131 ? 49.142  38.070  69.550  1.00 68.05  ? 158 TRP A NE1   1 
ATOM   932  C  CE2   . TRP A 1 131 ? 48.476  36.922  69.210  1.00 63.87  ? 158 TRP A CE2   1 
ATOM   933  C  CE3   . TRP A 1 131 ? 46.289  35.949  69.554  1.00 55.06  ? 158 TRP A CE3   1 
ATOM   934  C  CZ2   . TRP A 1 131 ? 48.899  35.829  68.461  1.00 63.27  ? 158 TRP A CZ2   1 
ATOM   935  C  CZ3   . TRP A 1 131 ? 46.715  34.858  68.819  1.00 64.20  ? 158 TRP A CZ3   1 
ATOM   936  C  CH2   . TRP A 1 131 ? 48.007  34.807  68.279  1.00 71.86  ? 158 TRP A CH2   1 
ATOM   937  N  N     . ALA A 1 132 ? 44.963  41.967  72.887  1.00 63.78  ? 159 ALA A N     1 
ATOM   938  C  CA    . ALA A 1 132 ? 43.939  42.998  72.860  1.00 62.49  ? 159 ALA A CA    1 
ATOM   939  C  C     . ALA A 1 132 ? 44.215  44.004  71.747  1.00 67.27  ? 159 ALA A C     1 
ATOM   940  O  O     . ALA A 1 132 ? 45.360  44.235  71.353  1.00 64.57  ? 159 ALA A O     1 
ATOM   941  C  CB    . ALA A 1 132 ? 43.873  43.719  74.204  1.00 55.08  ? 159 ALA A CB    1 
ATOM   942  N  N     . ASP A 1 133 ? 43.143  44.602  71.230  1.00 67.23  ? 160 ASP A N     1 
ATOM   943  C  CA    . ASP A 1 133 ? 43.306  45.662  70.242  1.00 70.17  ? 160 ASP A CA    1 
ATOM   944  C  C     . ASP A 1 133 ? 43.686  46.981  70.902  1.00 67.93  ? 160 ASP A C     1 
ATOM   945  O  O     . ASP A 1 133 ? 44.505  47.736  70.366  1.00 66.49  ? 160 ASP A O     1 
ATOM   946  C  CB    . ASP A 1 133 ? 42.023  45.827  69.425  1.00 74.90  ? 160 ASP A CB    1 
ATOM   947  C  CG    . ASP A 1 133 ? 41.648  44.568  68.669  1.00 75.81  ? 160 ASP A CG    1 
ATOM   948  O  OD1   . ASP A 1 133 ? 42.557  43.933  68.089  1.00 70.19  ? 160 ASP A OD1   1 
ATOM   949  O  OD2   . ASP A 1 133 ? 40.446  44.215  68.665  1.00 71.29  ? 160 ASP A OD2   1 
ATOM   950  N  N     . TYR A 1 134 ? 43.108  47.264  72.067  1.00 72.03  ? 161 TYR A N     1 
ATOM   951  C  CA    . TYR A 1 134 ? 43.327  48.520  72.764  1.00 68.82  ? 161 TYR A CA    1 
ATOM   952  C  C     . TYR A 1 134 ? 43.572  48.250  74.241  1.00 67.02  ? 161 TYR A C     1 
ATOM   953  O  O     . TYR A 1 134 ? 43.134  47.236  74.790  1.00 65.10  ? 161 TYR A O     1 
ATOM   954  C  CB    . TYR A 1 134 ? 42.126  49.463  72.615  1.00 63.27  ? 161 TYR A CB    1 
ATOM   955  C  CG    . TYR A 1 134 ? 41.903  49.981  71.216  1.00 73.51  ? 161 TYR A CG    1 
ATOM   956  C  CD1   . TYR A 1 134 ? 42.558  51.120  70.769  1.00 62.17  ? 161 TYR A CD1   1 
ATOM   957  C  CD2   . TYR A 1 134 ? 41.028  49.338  70.346  1.00 68.03  ? 161 TYR A CD2   1 
ATOM   958  C  CE1   . TYR A 1 134 ? 42.360  51.603  69.494  1.00 75.30  ? 161 TYR A CE1   1 
ATOM   959  C  CE2   . TYR A 1 134 ? 40.822  49.814  69.061  1.00 73.98  ? 161 TYR A CE2   1 
ATOM   960  C  CZ    . TYR A 1 134 ? 41.493  50.948  68.640  1.00 74.50  ? 161 TYR A CZ    1 
ATOM   961  O  OH    . TYR A 1 134 ? 41.303  51.440  67.368  1.00 76.25  ? 161 TYR A OH    1 
ATOM   962  N  N     . ILE A 1 135 ? 44.275  49.179  74.884  1.00 62.88  ? 162 ILE A N     1 
ATOM   963  C  CA    . ILE A 1 135 ? 44.310  49.268  76.338  1.00 59.66  ? 162 ILE A CA    1 
ATOM   964  C  C     . ILE A 1 135 ? 43.828  50.658  76.731  1.00 68.82  ? 162 ILE A C     1 
ATOM   965  O  O     . ILE A 1 135 ? 44.317  51.668  76.210  1.00 66.37  ? 162 ILE A O     1 
ATOM   966  C  CB    . ILE A 1 135 ? 45.708  48.970  76.912  1.00 61.35  ? 162 ILE A CB    1 
ATOM   967  C  CG1   . ILE A 1 135 ? 45.702  49.144  78.435  1.00 56.44  ? 162 ILE A CG1   1 
ATOM   968  C  CG2   . ILE A 1 135 ? 46.775  49.844  76.270  1.00 59.75  ? 162 ILE A CG2   1 
ATOM   969  C  CD1   . ILE A 1 135 ? 46.885  48.503  79.123  1.00 59.48  ? 162 ILE A CD1   1 
ATOM   970  N  N     . LEU A 1 136 ? 42.845  50.706  77.618  1.00 68.28  ? 163 LEU A N     1 
ATOM   971  C  CA    . LEU A 1 136 ? 42.259  51.953  78.086  1.00 60.60  ? 163 LEU A CA    1 
ATOM   972  C  C     . LEU A 1 136 ? 42.654  52.137  79.544  1.00 70.51  ? 163 LEU A C     1 
ATOM   973  O  O     . LEU A 1 136 ? 42.209  51.382  80.414  1.00 69.62  ? 163 LEU A O     1 
ATOM   974  C  CB    . LEU A 1 136 ? 40.745  51.931  77.926  1.00 61.45  ? 163 LEU A CB    1 
ATOM   975  C  CG    . LEU A 1 136 ? 40.002  53.151  78.460  1.00 73.35  ? 163 LEU A CG    1 
ATOM   976  C  CD1   . LEU A 1 136 ? 40.222  54.342  77.531  1.00 69.97  ? 163 LEU A CD1   1 
ATOM   977  C  CD2   . LEU A 1 136 ? 38.522  52.837  78.636  1.00 59.97  ? 163 LEU A CD2   1 
ATOM   978  N  N     . PHE A 1 137 ? 43.499  53.127  79.806  1.00 71.33  ? 164 PHE A N     1 
ATOM   979  C  CA    . PHE A 1 137 ? 43.855  53.497  81.169  1.00 62.86  ? 164 PHE A CA    1 
ATOM   980  C  C     . PHE A 1 137 ? 42.814  54.466  81.706  1.00 67.30  ? 164 PHE A C     1 
ATOM   981  O  O     . PHE A 1 137 ? 42.460  55.438  81.034  1.00 76.55  ? 164 PHE A O     1 
ATOM   982  C  CB    . PHE A 1 137 ? 45.248  54.128  81.223  1.00 68.44  ? 164 PHE A CB    1 
ATOM   983  C  CG    . PHE A 1 137 ? 46.368  53.131  81.151  1.00 67.78  ? 164 PHE A CG    1 
ATOM   984  C  CD1   . PHE A 1 137 ? 46.878  52.561  82.307  1.00 59.90  ? 164 PHE A CD1   1 
ATOM   985  C  CD2   . PHE A 1 137 ? 46.916  52.767  79.927  1.00 66.57  ? 164 PHE A CD2   1 
ATOM   986  C  CE1   . PHE A 1 137 ? 47.915  51.643  82.252  1.00 67.30  ? 164 PHE A CE1   1 
ATOM   987  C  CE2   . PHE A 1 137 ? 47.958  51.851  79.859  1.00 61.20  ? 164 PHE A CE2   1 
ATOM   988  C  CZ    . PHE A 1 137 ? 48.457  51.285  81.025  1.00 72.45  ? 164 PHE A CZ    1 
ATOM   989  N  N     . VAL A 1 138 ? 42.306  54.182  82.902  1.00 70.20  ? 165 VAL A N     1 
ATOM   990  C  CA    . VAL A 1 138 ? 41.336  55.038  83.576  1.00 73.70  ? 165 VAL A CA    1 
ATOM   991  C  C     . VAL A 1 138 ? 41.783  55.193  85.022  1.00 72.08  ? 165 VAL A C     1 
ATOM   992  O  O     . VAL A 1 138 ? 41.861  54.201  85.757  1.00 74.65  ? 165 VAL A O     1 
ATOM   993  C  CB    . VAL A 1 138 ? 39.909  54.464  83.518  1.00 67.96  ? 165 VAL A CB    1 
ATOM   994  C  CG1   . VAL A 1 138 ? 38.919  55.444  84.144  1.00 56.03  ? 165 VAL A CG1   1 
ATOM   995  C  CG2   . VAL A 1 138 ? 39.516  54.132  82.084  1.00 64.92  ? 165 VAL A CG2   1 
ATOM   996  N  N     . ASP A 1 139 ? 42.088  56.424  85.425  1.00 61.04  ? 166 ASP A N     1 
ATOM   997  C  CA    . ASP A 1 139 ? 42.411  56.689  86.821  1.00 70.11  ? 166 ASP A CA    1 
ATOM   998  C  C     . ASP A 1 139 ? 41.207  56.397  87.704  1.00 73.12  ? 166 ASP A C     1 
ATOM   999  O  O     . ASP A 1 139 ? 40.061  56.659  87.327  1.00 77.50  ? 166 ASP A O     1 
ATOM   1000 C  CB    . ASP A 1 139 ? 42.854  58.139  87.002  1.00 81.95  ? 166 ASP A CB    1 
ATOM   1001 C  CG    . ASP A 1 139 ? 44.328  58.335  86.715  1.00 91.63  ? 166 ASP A CG    1 
ATOM   1002 O  OD1   . ASP A 1 139 ? 45.012  57.328  86.427  1.00 68.93  ? 166 ASP A OD1   1 
ATOM   1003 O  OD2   . ASP A 1 139 ? 44.798  59.498  86.785  1.00 92.22  ? 166 ASP A OD2   1 
ATOM   1004 N  N     . ALA A 1 140 ? 41.476  55.867  88.898  1.00 67.13  ? 167 ALA A N     1 
ATOM   1005 C  CA    . ALA A 1 140 ? 40.406  55.380  89.763  1.00 71.39  ? 167 ALA A CA    1 
ATOM   1006 C  C     . ALA A 1 140 ? 39.405  56.463  90.148  1.00 77.44  ? 167 ALA A C     1 
ATOM   1007 O  O     . ALA A 1 140 ? 38.291  56.132  90.567  1.00 85.82  ? 167 ALA A O     1 
ATOM   1008 C  CB    . ALA A 1 140 ? 40.998  54.751  91.024  1.00 76.68  ? 167 ALA A CB    1 
ATOM   1009 N  N     . ASP A 1 141 ? 39.764  57.742  90.021  1.00 77.27  ? 168 ASP A N     1 
ATOM   1010 C  CA    . ASP A 1 141 ? 38.852  58.834  90.343  1.00 77.01  ? 168 ASP A CA    1 
ATOM   1011 C  C     . ASP A 1 141 ? 38.408  59.604  89.099  1.00 81.61  ? 168 ASP A C     1 
ATOM   1012 O  O     . ASP A 1 141 ? 38.032  60.773  89.192  1.00 83.91  ? 168 ASP A O     1 
ATOM   1013 C  CB    . ASP A 1 141 ? 39.473  59.781  91.375  1.00 70.24  ? 168 ASP A CB    1 
ATOM   1014 C  CG    . ASP A 1 141 ? 40.761  60.440  90.892  1.00 81.06  ? 168 ASP A CG    1 
ATOM   1015 O  OD1   . ASP A 1 141 ? 41.277  60.068  89.822  1.00 85.51  ? 168 ASP A OD1   1 
ATOM   1016 O  OD2   . ASP A 1 141 ? 41.262  61.342  91.596  1.00 88.71  ? 168 ASP A OD2   1 
ATOM   1017 N  N     . ASN A 1 142 ? 38.428  58.957  87.934  1.00 81.23  ? 169 ASN A N     1 
ATOM   1018 C  CA    . ASN A 1 142 ? 37.984  59.564  86.683  1.00 77.66  ? 169 ASN A CA    1 
ATOM   1019 C  C     . ASN A 1 142 ? 36.605  59.017  86.329  1.00 76.43  ? 169 ASN A C     1 
ATOM   1020 O  O     . ASN A 1 142 ? 36.441  57.807  86.123  1.00 77.93  ? 169 ASN A O     1 
ATOM   1021 C  CB    . ASN A 1 142 ? 38.977  59.294  85.552  1.00 76.83  ? 169 ASN A CB    1 
ATOM   1022 C  CG    . ASN A 1 142 ? 40.253  60.112  85.679  1.00 76.72  ? 169 ASN A CG    1 
ATOM   1023 O  OD1   . ASN A 1 142 ? 40.962  60.321  84.699  1.00 76.63  ? 169 ASN A OD1   1 
ATOM   1024 N  ND2   . ASN A 1 142 ? 40.547  60.579  86.888  1.00 75.85  ? 169 ASN A ND2   1 
ATOM   1025 N  N     . LEU A 1 143 ? 35.621  59.905  86.260  1.00 73.22  ? 170 LEU A N     1 
ATOM   1026 C  CA    . LEU A 1 143 ? 34.223  59.523  86.076  1.00 77.76  ? 170 LEU A CA    1 
ATOM   1027 C  C     . LEU A 1 143 ? 33.885  59.628  84.595  1.00 76.57  ? 170 LEU A C     1 
ATOM   1028 O  O     . LEU A 1 143 ? 33.590  60.714  84.094  1.00 85.26  ? 170 LEU A O     1 
ATOM   1029 C  CB    . LEU A 1 143 ? 33.312  60.402  86.926  1.00 77.62  ? 170 LEU A CB    1 
ATOM   1030 C  CG    . LEU A 1 143 ? 31.806  60.195  86.776  1.00 83.69  ? 170 LEU A CG    1 
ATOM   1031 C  CD1   . LEU A 1 143 ? 31.452  58.736  86.985  1.00 80.33  ? 170 LEU A CD1   1 
ATOM   1032 C  CD2   . LEU A 1 143 ? 31.050  61.079  87.756  1.00 89.96  ? 170 LEU A CD2   1 
ATOM   1033 N  N     . ILE A 1 144 ? 33.915  58.493  83.898  1.00 76.40  ? 171 ILE A N     1 
ATOM   1034 C  CA    . ILE A 1 144 ? 33.591  58.442  82.475  1.00 73.97  ? 171 ILE A CA    1 
ATOM   1035 C  C     . ILE A 1 144 ? 32.075  58.424  82.307  1.00 77.84  ? 171 ILE A C     1 
ATOM   1036 O  O     . ILE A 1 144 ? 31.481  57.373  82.038  1.00 81.16  ? 171 ILE A O     1 
ATOM   1037 C  CB    . ILE A 1 144 ? 34.245  57.218  81.804  1.00 71.38  ? 171 ILE A CB    1 
ATOM   1038 C  CG1   . ILE A 1 144 ? 35.715  57.098  82.219  1.00 65.15  ? 171 ILE A CG1   1 
ATOM   1039 C  CG2   . ILE A 1 144 ? 34.142  57.313  80.294  1.00 68.00  ? 171 ILE A CG2   1 
ATOM   1040 C  CD1   . ILE A 1 144 ? 36.541  58.346  81.938  1.00 63.87  ? 171 ILE A CD1   1 
ATOM   1041 N  N     . LEU A 1 145 ? 31.444  59.593  82.465  1.00 82.30  ? 172 LEU A N     1 
ATOM   1042 C  CA    . LEU A 1 145 ? 29.985  59.674  82.426  1.00 78.47  ? 172 LEU A CA    1 
ATOM   1043 C  C     . LEU A 1 145 ? 29.428  59.172  81.102  1.00 85.60  ? 172 LEU A C     1 
ATOM   1044 O  O     . LEU A 1 145 ? 28.426  58.446  81.079  1.00 93.07  ? 172 LEU A O     1 
ATOM   1045 C  CB    . LEU A 1 145 ? 29.521  61.111  82.665  1.00 80.01  ? 172 LEU A CB    1 
ATOM   1046 C  CG    . LEU A 1 145 ? 29.095  61.544  84.068  1.00 99.56  ? 172 LEU A CG    1 
ATOM   1047 C  CD1   . LEU A 1 145 ? 28.200  62.774  83.984  1.00 91.08  ? 172 LEU A CD1   1 
ATOM   1048 C  CD2   . LEU A 1 145 ? 28.396  60.418  84.814  1.00 93.76  ? 172 LEU A CD2   1 
ATOM   1049 N  N     . ASN A 1 146 ? 30.052  59.554  79.994  1.00 79.91  ? 173 ASN A N     1 
ATOM   1050 C  CA    . ASN A 1 146 ? 29.503  59.259  78.675  1.00 75.77  ? 173 ASN A CA    1 
ATOM   1051 C  C     . ASN A 1 146 ? 29.719  57.789  78.340  1.00 78.62  ? 173 ASN A C     1 
ATOM   1052 O  O     . ASN A 1 146 ? 30.868  57.361  78.188  1.00 82.73  ? 173 ASN A O     1 
ATOM   1053 C  CB    . ASN A 1 146 ? 30.157  60.146  77.620  1.00 83.07  ? 173 ASN A CB    1 
ATOM   1054 C  CG    . ASN A 1 146 ? 29.484  60.045  76.263  1.00 85.79  ? 173 ASN A CG    1 
ATOM   1055 O  OD1   . ASN A 1 146 ? 28.937  59.004  75.899  1.00 89.36  ? 173 ASN A OD1   1 
ATOM   1056 N  ND2   . ASN A 1 146 ? 29.528  61.135  75.501  1.00 83.94  ? 173 ASN A ND2   1 
ATOM   1057 N  N     . PRO A 1 147 ? 28.657  56.994  78.195  1.00 79.75  ? 174 PRO A N     1 
ATOM   1058 C  CA    . PRO A 1 147 ? 28.849  55.562  77.913  1.00 83.53  ? 174 PRO A CA    1 
ATOM   1059 C  C     . PRO A 1 147 ? 29.490  55.291  76.565  1.00 79.90  ? 174 PRO A C     1 
ATOM   1060 O  O     . PRO A 1 147 ? 29.953  54.167  76.338  1.00 90.04  ? 174 PRO A O     1 
ATOM   1061 C  CB    . PRO A 1 147 ? 27.422  54.992  77.972  1.00 81.82  ? 174 PRO A CB    1 
ATOM   1062 C  CG    . PRO A 1 147 ? 26.589  56.057  78.640  1.00 78.64  ? 174 PRO A CG    1 
ATOM   1063 C  CD    . PRO A 1 147 ? 27.237  57.361  78.282  1.00 63.71  ? 174 PRO A CD    1 
ATOM   1064 N  N     . ASP A 1 148 ? 29.534  56.276  75.669  1.00 79.99  ? 175 ASP A N     1 
ATOM   1065 C  CA    . ASP A 1 148 ? 30.091  56.103  74.334  1.00 83.17  ? 175 ASP A CA    1 
ATOM   1066 C  C     . ASP A 1 148 ? 31.533  56.581  74.218  1.00 80.98  ? 175 ASP A C     1 
ATOM   1067 O  O     . ASP A 1 148 ? 32.100  56.528  73.122  1.00 72.17  ? 175 ASP A O     1 
ATOM   1068 C  CB    . ASP A 1 148 ? 29.223  56.836  73.306  1.00 70.47  ? 175 ASP A CB    1 
ATOM   1069 C  CG    . ASP A 1 148 ? 27.812  56.286  73.239  1.00 86.63  ? 175 ASP A CG    1 
ATOM   1070 O  OD1   . ASP A 1 148 ? 27.630  55.081  73.511  1.00 97.19  ? 175 ASP A OD1   1 
ATOM   1071 O  OD2   . ASP A 1 148 ? 26.882  57.056  72.914  1.00 95.83  ? 175 ASP A OD2   1 
ATOM   1072 N  N     . THR A 1 149 ? 32.136  57.040  75.319  1.00 82.46  ? 176 THR A N     1 
ATOM   1073 C  CA    . THR A 1 149 ? 33.494  57.576  75.268  1.00 81.14  ? 176 THR A CA    1 
ATOM   1074 C  C     . THR A 1 149 ? 34.463  56.585  74.638  1.00 73.29  ? 176 THR A C     1 
ATOM   1075 O  O     . THR A 1 149 ? 35.292  56.961  73.800  1.00 74.64  ? 176 THR A O     1 
ATOM   1076 C  CB    . THR A 1 149 ? 33.959  57.945  76.675  1.00 78.08  ? 176 THR A CB    1 
ATOM   1077 O  OG1   . THR A 1 149 ? 33.025  58.860  77.257  1.00 83.09  ? 176 THR A OG1   1 
ATOM   1078 C  CG2   . THR A 1 149 ? 35.346  58.585  76.632  1.00 73.95  ? 176 THR A CG2   1 
ATOM   1079 N  N     . LEU A 1 150 ? 34.366  55.313  75.023  1.00 72.15  ? 177 LEU A N     1 
ATOM   1080 C  CA    . LEU A 1 150 ? 35.248  54.295  74.465  1.00 64.62  ? 177 LEU A CA    1 
ATOM   1081 C  C     . LEU A 1 150 ? 35.041  54.162  72.964  1.00 74.02  ? 177 LEU A C     1 
ATOM   1082 O  O     . LEU A 1 150 ? 35.998  54.230  72.183  1.00 74.51  ? 177 LEU A O     1 
ATOM   1083 C  CB    . LEU A 1 150 ? 35.002  52.964  75.168  1.00 62.03  ? 177 LEU A CB    1 
ATOM   1084 C  CG    . LEU A 1 150 ? 35.836  51.765  74.739  1.00 65.10  ? 177 LEU A CG    1 
ATOM   1085 C  CD1   . LEU A 1 150 ? 37.296  52.161  74.582  1.00 65.61  ? 177 LEU A CD1   1 
ATOM   1086 C  CD2   . LEU A 1 150 ? 35.669  50.648  75.765  1.00 63.87  ? 177 LEU A CD2   1 
ATOM   1087 N  N     . SER A 1 151 ? 33.789  53.976  72.542  1.00 75.45  ? 178 SER A N     1 
ATOM   1088 C  CA    . SER A 1 151 ? 33.490  53.884  71.118  1.00 65.61  ? 178 SER A CA    1 
ATOM   1089 C  C     . SER A 1 151 ? 34.013  55.104  70.367  1.00 77.45  ? 178 SER A C     1 
ATOM   1090 O  O     . SER A 1 151 ? 34.643  54.972  69.309  1.00 77.34  ? 178 SER A O     1 
ATOM   1091 C  CB    . SER A 1 151 ? 31.982  53.731  70.912  1.00 75.54  ? 178 SER A CB    1 
ATOM   1092 O  OG    . SER A 1 151 ? 31.454  52.702  71.730  1.00 80.33  ? 178 SER A OG    1 
ATOM   1093 N  N     . LEU A 1 152 ? 33.780  56.298  70.911  1.00 74.95  ? 179 LEU A N     1 
ATOM   1094 C  CA    . LEU A 1 152 ? 34.216  57.518  70.240  1.00 61.28  ? 179 LEU A CA    1 
ATOM   1095 C  C     . LEU A 1 152 ? 35.734  57.572  70.112  1.00 69.64  ? 179 LEU A C     1 
ATOM   1096 O  O     . LEU A 1 152 ? 36.259  57.917  69.047  1.00 73.84  ? 179 LEU A O     1 
ATOM   1097 C  CB    . LEU A 1 152 ? 33.692  58.736  70.996  1.00 75.47  ? 179 LEU A CB    1 
ATOM   1098 C  CG    . LEU A 1 152 ? 32.169  58.887  71.036  1.00 76.05  ? 179 LEU A CG    1 
ATOM   1099 C  CD1   . LEU A 1 152 ? 31.764  59.946  72.049  1.00 76.03  ? 179 LEU A CD1   1 
ATOM   1100 C  CD2   . LEU A 1 152 ? 31.616  59.219  69.650  1.00 55.63  ? 179 LEU A CD2   1 
ATOM   1101 N  N     . LEU A 1 153 ? 36.456  57.232  71.185  1.00 69.57  ? 180 LEU A N     1 
ATOM   1102 C  CA    . LEU A 1 153 ? 37.917  57.240  71.130  1.00 67.00  ? 180 LEU A CA    1 
ATOM   1103 C  C     . LEU A 1 153 ? 38.446  56.264  70.082  1.00 75.21  ? 180 LEU A C     1 
ATOM   1104 O  O     . LEU A 1 153 ? 39.366  56.594  69.325  1.00 74.61  ? 180 LEU A O     1 
ATOM   1105 C  CB    . LEU A 1 153 ? 38.495  56.915  72.507  1.00 73.14  ? 180 LEU A CB    1 
ATOM   1106 C  CG    . LEU A 1 153 ? 38.362  57.998  73.579  1.00 81.14  ? 180 LEU A CG    1 
ATOM   1107 C  CD1   . LEU A 1 153 ? 38.683  57.431  74.951  1.00 64.99  ? 180 LEU A CD1   1 
ATOM   1108 C  CD2   . LEU A 1 153 ? 39.261  59.182  73.265  1.00 69.34  ? 180 LEU A CD2   1 
ATOM   1109 N  N     . ILE A 1 154 ? 37.878  55.056  70.021  1.00 63.93  ? 181 ILE A N     1 
ATOM   1110 C  CA    . ILE A 1 154 ? 38.298  54.093  69.008  1.00 67.19  ? 181 ILE A CA    1 
ATOM   1111 C  C     . ILE A 1 154 ? 38.044  54.627  67.604  1.00 70.94  ? 181 ILE A C     1 
ATOM   1112 O  O     . ILE A 1 154 ? 38.777  54.300  66.663  1.00 72.84  ? 181 ILE A O     1 
ATOM   1113 C  CB    . ILE A 1 154 ? 37.581  52.747  69.221  1.00 69.70  ? 181 ILE A CB    1 
ATOM   1114 C  CG1   . ILE A 1 154 ? 37.849  52.208  70.622  1.00 72.13  ? 181 ILE A CG1   1 
ATOM   1115 C  CG2   . ILE A 1 154 ? 38.024  51.737  68.173  1.00 64.88  ? 181 ILE A CG2   1 
ATOM   1116 C  CD1   . ILE A 1 154 ? 37.289  50.814  70.840  1.00 67.82  ? 181 ILE A CD1   1 
ATOM   1117 N  N     . ALA A 1 155 ? 37.014  55.459  67.437  1.00 72.89  ? 182 ALA A N     1 
ATOM   1118 C  CA    . ALA A 1 155 ? 36.626  55.891  66.099  1.00 70.52  ? 182 ALA A CA    1 
ATOM   1119 C  C     . ALA A 1 155 ? 37.662  56.810  65.467  1.00 72.09  ? 182 ALA A C     1 
ATOM   1120 O  O     . ALA A 1 155 ? 37.790  56.842  64.239  1.00 74.07  ? 182 ALA A O     1 
ATOM   1121 C  CB    . ALA A 1 155 ? 35.267  56.585  66.145  1.00 72.24  ? 182 ALA A CB    1 
ATOM   1122 N  N     . GLU A 1 156 ? 38.411  57.556  66.274  1.00 74.70  ? 183 GLU A N     1 
ATOM   1123 C  CA    . GLU A 1 156 ? 39.358  58.505  65.706  1.00 74.53  ? 183 GLU A CA    1 
ATOM   1124 C  C     . GLU A 1 156 ? 40.581  57.835  65.092  1.00 62.52  ? 183 GLU A C     1 
ATOM   1125 O  O     . GLU A 1 156 ? 41.374  58.525  64.445  1.00 84.23  ? 183 GLU A O     1 
ATOM   1126 C  CB    . GLU A 1 156 ? 39.788  59.509  66.775  1.00 71.96  ? 183 GLU A CB    1 
ATOM   1127 C  CG    . GLU A 1 156 ? 38.627  60.247  67.421  1.00 70.60  ? 183 GLU A CG    1 
ATOM   1128 C  CD    . GLU A 1 156 ? 37.895  61.179  66.463  1.00 86.88  ? 183 GLU A CD    1 
ATOM   1129 O  OE1   . GLU A 1 156 ? 38.423  61.456  65.358  1.00 79.65  ? 183 GLU A OE1   1 
ATOM   1130 O  OE2   . GLU A 1 156 ? 36.788  61.641  66.826  1.00 71.63  ? 183 GLU A OE2   1 
ATOM   1131 N  N     . ASN A 1 157 ? 40.739  56.525  65.266  1.00 60.13  ? 184 ASN A N     1 
ATOM   1132 C  CA    . ASN A 1 157 ? 41.849  55.760  64.694  1.00 67.02  ? 184 ASN A CA    1 
ATOM   1133 C  C     . ASN A 1 157 ? 43.195  56.435  64.960  1.00 75.14  ? 184 ASN A C     1 
ATOM   1134 O  O     . ASN A 1 157 ? 43.993  56.680  64.051  1.00 70.62  ? 184 ASN A O     1 
ATOM   1135 C  CB    . ASN A 1 157 ? 41.639  55.524  63.200  1.00 55.12  ? 184 ASN A CB    1 
ATOM   1136 C  CG    . ASN A 1 157 ? 42.635  54.532  62.618  1.00 70.41  ? 184 ASN A CG    1 
ATOM   1137 O  OD1   . ASN A 1 157 ? 43.299  53.794  63.349  1.00 80.41  ? 184 ASN A OD1   1 
ATOM   1138 N  ND2   . ASN A 1 157 ? 42.747  54.516  61.294  1.00 76.90  ? 184 ASN A ND2   1 
ATOM   1139 N  N     . LYS A 1 158 ? 43.440  56.741  66.229  1.00 71.92  ? 185 LYS A N     1 
ATOM   1140 C  CA    . LYS A 1 158 ? 44.718  57.266  66.682  1.00 70.46  ? 185 LYS A CA    1 
ATOM   1141 C  C     . LYS A 1 158 ? 45.439  56.211  67.508  1.00 71.11  ? 185 LYS A C     1 
ATOM   1142 O  O     . LYS A 1 158 ? 44.828  55.272  68.028  1.00 77.99  ? 185 LYS A O     1 
ATOM   1143 C  CB    . LYS A 1 158 ? 44.528  58.539  67.509  1.00 78.57  ? 185 LYS A CB    1 
ATOM   1144 C  CG    . LYS A 1 158 ? 43.805  59.646  66.770  1.00 63.44  ? 185 LYS A CG    1 
ATOM   1145 C  CD    . LYS A 1 158 ? 44.640  60.149  65.617  1.00 74.26  ? 185 LYS A CD    1 
ATOM   1146 C  CE    . LYS A 1 158 ? 44.032  61.392  65.001  1.00 72.12  ? 185 LYS A CE    1 
ATOM   1147 N  NZ    . LYS A 1 158 ? 44.816  61.826  63.816  1.00 105.46 ? 185 LYS A NZ    1 
ATOM   1148 N  N     . THR A 1 159 ? 46.758  56.373  67.623  1.00 62.99  ? 186 THR A N     1 
ATOM   1149 C  CA    . THR A 1 159 ? 47.533  55.409  68.394  1.00 64.31  ? 186 THR A CA    1 
ATOM   1150 C  C     . THR A 1 159 ? 47.502  55.730  69.884  1.00 72.09  ? 186 THR A C     1 
ATOM   1151 O  O     . THR A 1 159 ? 47.411  54.817  70.711  1.00 70.24  ? 186 THR A O     1 
ATOM   1152 C  CB    . THR A 1 159 ? 48.972  55.353  67.883  1.00 66.18  ? 186 THR A CB    1 
ATOM   1153 O  OG1   . THR A 1 159 ? 48.976  54.999  66.494  1.00 67.58  ? 186 THR A OG1   1 
ATOM   1154 C  CG2   . THR A 1 159 ? 49.765  54.313  68.657  1.00 66.52  ? 186 THR A CG2   1 
ATOM   1155 N  N     . VAL A 1 160 ? 47.573  57.010  70.248  1.00 67.89  ? 187 VAL A N     1 
ATOM   1156 C  CA    . VAL A 1 160 ? 47.403  57.453  71.630  1.00 68.91  ? 187 VAL A CA    1 
ATOM   1157 C  C     . VAL A 1 160 ? 46.460  58.651  71.619  1.00 72.85  ? 187 VAL A C     1 
ATOM   1158 O  O     . VAL A 1 160 ? 46.853  59.757  71.223  1.00 67.06  ? 187 VAL A O     1 
ATOM   1159 C  CB    . VAL A 1 160 ? 48.735  57.817  72.301  1.00 76.68  ? 187 VAL A CB    1 
ATOM   1160 C  CG1   . VAL A 1 160 ? 48.494  58.299  73.721  1.00 54.55  ? 187 VAL A CG1   1 
ATOM   1161 C  CG2   . VAL A 1 160 ? 49.679  56.629  72.305  1.00 70.00  ? 187 VAL A CG2   1 
ATOM   1162 N  N     . VAL A 1 161 ? 45.222  58.436  72.057  1.00 69.02  ? 188 VAL A N     1 
ATOM   1163 C  CA    . VAL A 1 161 ? 44.212  59.484  72.084  1.00 74.73  ? 188 VAL A CA    1 
ATOM   1164 C  C     . VAL A 1 161 ? 43.574  59.500  73.465  1.00 72.18  ? 188 VAL A C     1 
ATOM   1165 O  O     . VAL A 1 161 ? 43.438  58.464  74.125  1.00 66.84  ? 188 VAL A O     1 
ATOM   1166 C  CB    . VAL A 1 161 ? 43.144  59.292  70.977  1.00 63.73  ? 188 VAL A CB    1 
ATOM   1167 C  CG1   . VAL A 1 161 ? 42.310  58.058  71.241  1.00 63.15  ? 188 VAL A CG1   1 
ATOM   1168 C  CG2   . VAL A 1 161 ? 42.263  60.519  70.863  1.00 59.98  ? 188 VAL A CG2   1 
ATOM   1169 N  N     . ALA A 1 162 ? 43.199  60.694  73.912  1.00 70.26  ? 189 ALA A N     1 
ATOM   1170 C  CA    . ALA A 1 162 ? 42.616  60.859  75.229  1.00 73.01  ? 189 ALA A CA    1 
ATOM   1171 C  C     . ALA A 1 162 ? 41.349  61.696  75.141  1.00 74.04  ? 189 ALA A C     1 
ATOM   1172 O  O     . ALA A 1 162 ? 41.266  62.617  74.322  1.00 69.16  ? 189 ALA A O     1 
ATOM   1173 C  CB    . ALA A 1 162 ? 43.605  61.528  76.190  1.00 62.80  ? 189 ALA A CB    1 
ATOM   1174 N  N     . PRO A 1 163 ? 40.343  61.392  75.958  1.00 66.66  ? 190 PRO A N     1 
ATOM   1175 C  CA    . PRO A 1 163 ? 39.155  62.251  76.019  1.00 64.38  ? 190 PRO A CA    1 
ATOM   1176 C  C     . PRO A 1 163 ? 39.372  63.378  77.016  1.00 78.04  ? 190 PRO A C     1 
ATOM   1177 O  O     . PRO A 1 163 ? 39.864  63.150  78.122  1.00 71.54  ? 190 PRO A O     1 
ATOM   1178 C  CB    . PRO A 1 163 ? 38.055  61.295  76.488  1.00 73.00  ? 190 PRO A CB    1 
ATOM   1179 C  CG    . PRO A 1 163 ? 38.785  60.290  77.330  1.00 62.29  ? 190 PRO A CG    1 
ATOM   1180 C  CD    . PRO A 1 163 ? 40.179  60.161  76.751  1.00 70.40  ? 190 PRO A CD    1 
ATOM   1181 N  N     . MET A 1 164 ? 39.026  64.599  76.612  1.00 71.65  ? 191 MET A N     1 
ATOM   1182 C  CA    . MET A 1 164 ? 39.168  65.733  77.510  1.00 67.78  ? 191 MET A CA    1 
ATOM   1183 C  C     . MET A 1 164 ? 38.129  65.636  78.619  1.00 84.40  ? 191 MET A C     1 
ATOM   1184 O  O     . MET A 1 164 ? 36.920  65.694  78.361  1.00 86.96  ? 191 MET A O     1 
ATOM   1185 C  CB    . MET A 1 164 ? 39.033  67.050  76.757  1.00 65.07  ? 191 MET A CB    1 
ATOM   1186 C  CG    . MET A 1 164 ? 39.408  68.250  77.639  1.00 72.00  ? 191 MET A CG    1 
ATOM   1187 S  SD    . MET A 1 164 ? 39.063  69.859  76.898  1.00 80.17  ? 191 MET A SD    1 
ATOM   1188 C  CE    . MET A 1 164 ? 37.274  69.890  76.976  1.00 77.13  ? 191 MET A CE    1 
ATOM   1189 N  N     . LEU A 1 165 ? 38.604  65.499  79.852  1.00 81.69  ? 192 LEU A N     1 
ATOM   1190 C  CA    . LEU A 1 165 ? 37.741  65.412  81.017  1.00 71.96  ? 192 LEU A CA    1 
ATOM   1191 C  C     . LEU A 1 165 ? 37.580  66.788  81.648  1.00 83.18  ? 192 LEU A C     1 
ATOM   1192 O  O     . LEU A 1 165 ? 38.546  67.547  81.773  1.00 82.34  ? 192 LEU A O     1 
ATOM   1193 C  CB    . LEU A 1 165 ? 38.303  64.419  82.031  1.00 72.93  ? 192 LEU A CB    1 
ATOM   1194 C  CG    . LEU A 1 165 ? 38.492  63.016  81.453  1.00 82.33  ? 192 LEU A CG    1 
ATOM   1195 C  CD1   . LEU A 1 165 ? 38.975  62.047  82.524  1.00 70.54  ? 192 LEU A CD1   1 
ATOM   1196 C  CD2   . LEU A 1 165 ? 37.199  62.524  80.820  1.00 66.19  ? 192 LEU A CD2   1 
ATOM   1197 N  N     . ASP A 1 166 ? 36.345  67.113  82.018  1.00 82.64  ? 193 ASP A N     1 
ATOM   1198 C  CA    . ASP A 1 166 ? 36.050  68.387  82.653  1.00 76.88  ? 193 ASP A CA    1 
ATOM   1199 C  C     . ASP A 1 166 ? 36.402  68.342  84.136  1.00 88.22  ? 193 ASP A C     1 
ATOM   1200 O  O     . ASP A 1 166 ? 36.271  67.311  84.800  1.00 80.27  ? 193 ASP A O     1 
ATOM   1201 C  CB    . ASP A 1 166 ? 34.570  68.741  82.481  1.00 84.80  ? 193 ASP A CB    1 
ATOM   1202 C  CG    . ASP A 1 166 ? 34.163  68.865  81.028  1.00 105.09 ? 193 ASP A CG    1 
ATOM   1203 O  OD1   . ASP A 1 166 ? 34.795  69.659  80.298  1.00 113.26 ? 193 ASP A OD1   1 
ATOM   1204 O  OD2   . ASP A 1 166 ? 33.211  68.171  80.615  1.00 109.34 ? 193 ASP A OD2   1 
ATOM   1205 N  N     . SER A 1 167 ? 36.865  69.477  84.651  1.00 91.76  ? 194 SER A N     1 
ATOM   1206 C  CA    . SER A 1 167 ? 37.131  69.659  86.070  1.00 85.16  ? 194 SER A CA    1 
ATOM   1207 C  C     . SER A 1 167 ? 36.504  70.975  86.509  1.00 83.59  ? 194 SER A C     1 
ATOM   1208 O  O     . SER A 1 167 ? 35.985  71.741  85.694  1.00 96.12  ? 194 SER A O     1 
ATOM   1209 C  CB    . SER A 1 167 ? 38.639  69.638  86.369  1.00 83.45  ? 194 SER A CB    1 
ATOM   1210 O  OG    . SER A 1 167 ? 39.257  70.860  86.005  1.00 84.45  ? 194 SER A OG    1 
ATOM   1211 N  N     . ARG A 1 168 ? 36.552  71.239  87.816  1.00 92.15  ? 195 ARG A N     1 
ATOM   1212 C  CA    . ARG A 1 168 ? 35.997  72.481  88.342  1.00 91.15  ? 195 ARG A CA    1 
ATOM   1213 C  C     . ARG A 1 168 ? 36.817  73.699  87.938  1.00 86.92  ? 195 ARG A C     1 
ATOM   1214 O  O     . ARG A 1 168 ? 36.323  74.827  88.047  1.00 92.67  ? 195 ARG A O     1 
ATOM   1215 C  CB    . ARG A 1 168 ? 35.904  72.414  89.865  1.00 88.37  ? 195 ARG A CB    1 
ATOM   1216 C  CG    . ARG A 1 168 ? 37.261  72.285  90.536  1.00 79.60  ? 195 ARG A CG    1 
ATOM   1217 C  CD    . ARG A 1 168 ? 37.148  72.258  92.046  1.00 86.49  ? 195 ARG A CD    1 
ATOM   1218 N  NE    . ARG A 1 168 ? 38.454  72.053  92.659  1.00 92.14  ? 195 ARG A NE    1 
ATOM   1219 C  CZ    . ARG A 1 168 ? 39.319  73.025  92.911  1.00 94.41  ? 195 ARG A CZ    1 
ATOM   1220 N  NH1   . ARG A 1 168 ? 39.038  74.289  92.637  1.00 109.73 ? 195 ARG A NH1   1 
ATOM   1221 N  NH2   . ARG A 1 168 ? 40.496  72.722  93.448  1.00 94.02  ? 195 ARG A NH2   1 
ATOM   1222 N  N     . ALA A 1 169 ? 38.053  73.498  87.485  1.00 91.71  ? 196 ALA A N     1 
ATOM   1223 C  CA    . ALA A 1 169 ? 38.926  74.602  87.108  1.00 86.47  ? 196 ALA A CA    1 
ATOM   1224 C  C     . ALA A 1 169 ? 39.511  74.376  85.722  1.00 94.82  ? 196 ALA A C     1 
ATOM   1225 O  O     . ALA A 1 169 ? 39.069  73.481  84.993  1.00 91.05  ? 196 ALA A O     1 
ATOM   1226 C  CB    . ALA A 1 169 ? 40.046  74.777  88.133  1.00 79.28  ? 196 ALA A CB    1 
ATOM   1227 N  N     . ALA A 1 170 ? 40.514  75.178  85.354  1.00 89.80  ? 197 ALA A N     1 
ATOM   1228 C  CA    . ALA A 1 170 ? 41.143  75.040  84.046  1.00 89.32  ? 197 ALA A CA    1 
ATOM   1229 C  C     . ALA A 1 170 ? 41.878  73.716  83.878  1.00 97.42  ? 197 ALA A C     1 
ATOM   1230 O  O     . ALA A 1 170 ? 42.211  73.356  82.742  1.00 98.93  ? 197 ALA A O     1 
ATOM   1231 C  CB    . ALA A 1 170 ? 42.109  76.203  83.807  1.00 76.87  ? 197 ALA A CB    1 
ATOM   1232 N  N     . TYR A 1 171 ? 42.136  72.988  84.966  1.00 83.61  ? 198 TYR A N     1 
ATOM   1233 C  CA    . TYR A 1 171 ? 42.843  71.717  84.873  1.00 85.66  ? 198 TYR A CA    1 
ATOM   1234 C  C     . TYR A 1 171 ? 42.082  70.732  83.996  1.00 86.78  ? 198 TYR A C     1 
ATOM   1235 O  O     . TYR A 1 171 ? 40.857  70.614  84.077  1.00 97.63  ? 198 TYR A O     1 
ATOM   1236 C  CB    . TYR A 1 171 ? 43.050  71.117  86.266  1.00 83.54  ? 198 TYR A CB    1 
ATOM   1237 C  CG    . TYR A 1 171 ? 43.808  69.802  86.270  1.00 85.39  ? 198 TYR A CG    1 
ATOM   1238 C  CD1   . TYR A 1 171 ? 43.145  68.589  86.102  1.00 80.96  ? 198 TYR A CD1   1 
ATOM   1239 C  CD2   . TYR A 1 171 ? 45.185  69.773  86.451  1.00 72.48  ? 198 TYR A CD2   1 
ATOM   1240 C  CE1   . TYR A 1 171 ? 43.832  67.387  86.105  1.00 69.13  ? 198 TYR A CE1   1 
ATOM   1241 C  CE2   . TYR A 1 171 ? 45.879  68.576  86.457  1.00 77.36  ? 198 TYR A CE2   1 
ATOM   1242 C  CZ    . TYR A 1 171 ? 45.199  67.384  86.286  1.00 71.33  ? 198 TYR A CZ    1 
ATOM   1243 O  OH    . TYR A 1 171 ? 45.889  66.188  86.299  1.00 70.31  ? 198 TYR A OH    1 
ATOM   1244 N  N     . SER A 1 172 ? 42.824  70.024  83.150  1.00 78.64  ? 199 SER A N     1 
ATOM   1245 C  CA    . SER A 1 172 ? 42.300  68.889  82.406  1.00 71.79  ? 199 SER A CA    1 
ATOM   1246 C  C     . SER A 1 172 ? 43.436  67.890  82.232  1.00 72.61  ? 199 SER A C     1 
ATOM   1247 O  O     . SER A 1 172 ? 44.570  68.128  82.659  1.00 82.75  ? 199 SER A O     1 
ATOM   1248 C  CB    . SER A 1 172 ? 41.707  69.326  81.061  1.00 96.77  ? 199 SER A CB    1 
ATOM   1249 O  OG    . SER A 1 172 ? 41.053  68.248  80.412  1.00 84.03  ? 199 SER A OG    1 
ATOM   1250 N  N     . ASN A 1 173 ? 43.130  66.762  81.597  1.00 74.63  ? 200 ASN A N     1 
ATOM   1251 C  CA    . ASN A 1 173 ? 44.117  65.695  81.434  1.00 74.72  ? 200 ASN A CA    1 
ATOM   1252 C  C     . ASN A 1 173 ? 44.931  65.833  80.151  1.00 76.27  ? 200 ASN A C     1 
ATOM   1253 O  O     . ASN A 1 173 ? 45.148  64.847  79.440  1.00 69.88  ? 200 ASN A O     1 
ATOM   1254 C  CB    . ASN A 1 173 ? 43.421  64.338  81.497  1.00 75.04  ? 200 ASN A CB    1 
ATOM   1255 C  CG    . ASN A 1 173 ? 42.338  64.187  80.453  1.00 73.68  ? 200 ASN A CG    1 
ATOM   1256 O  OD1   . ASN A 1 173 ? 41.591  65.122  80.177  1.00 75.66  ? 200 ASN A OD1   1 
ATOM   1257 N  ND2   . ASN A 1 173 ? 42.246  63.001  79.867  1.00 78.08  ? 200 ASN A ND2   1 
ATOM   1258 N  N     . PHE A 1 174 ? 45.403  67.039  79.834  1.00 69.96  ? 201 PHE A N     1 
ATOM   1259 C  CA    . PHE A 1 174 ? 46.280  67.241  78.689  1.00 80.50  ? 201 PHE A CA    1 
ATOM   1260 C  C     . PHE A 1 174 ? 47.048  68.540  78.877  1.00 82.52  ? 201 PHE A C     1 
ATOM   1261 O  O     . PHE A 1 174 ? 46.628  69.427  79.624  1.00 85.68  ? 201 PHE A O     1 
ATOM   1262 C  CB    . PHE A 1 174 ? 45.497  67.271  77.367  1.00 87.00  ? 201 PHE A CB    1 
ATOM   1263 C  CG    . PHE A 1 174 ? 44.721  68.542  77.146  1.00 71.16  ? 201 PHE A CG    1 
ATOM   1264 C  CD1   . PHE A 1 174 ? 43.471  68.715  77.720  1.00 85.78  ? 201 PHE A CD1   1 
ATOM   1265 C  CD2   . PHE A 1 174 ? 45.240  69.564  76.367  1.00 81.05  ? 201 PHE A CD2   1 
ATOM   1266 C  CE1   . PHE A 1 174 ? 42.754  69.884  77.522  1.00 88.41  ? 201 PHE A CE1   1 
ATOM   1267 C  CE2   . PHE A 1 174 ? 44.527  70.739  76.165  1.00 87.58  ? 201 PHE A CE2   1 
ATOM   1268 C  CZ    . PHE A 1 174 ? 43.283  70.895  76.742  1.00 88.19  ? 201 PHE A CZ    1 
ATOM   1269 N  N     . TRP A 1 175 ? 48.186  68.631  78.195  1.00 85.06  ? 202 TRP A N     1 
ATOM   1270 C  CA    . TRP A 1 175 ? 48.944  69.867  78.071  1.00 84.16  ? 202 TRP A CA    1 
ATOM   1271 C  C     . TRP A 1 175 ? 48.937  70.309  76.615  1.00 90.75  ? 202 TRP A C     1 
ATOM   1272 O  O     . TRP A 1 175 ? 48.889  69.483  75.702  1.00 95.09  ? 202 TRP A O     1 
ATOM   1273 C  CB    . TRP A 1 175 ? 50.398  69.702  78.528  1.00 90.60  ? 202 TRP A CB    1 
ATOM   1274 C  CG    . TRP A 1 175 ? 50.594  69.220  79.929  1.00 92.41  ? 202 TRP A CG    1 
ATOM   1275 C  CD1   . TRP A 1 175 ? 49.629  68.942  80.851  1.00 85.67  ? 202 TRP A CD1   1 
ATOM   1276 C  CD2   . TRP A 1 175 ? 51.848  68.953  80.567  1.00 90.17  ? 202 TRP A CD2   1 
ATOM   1277 N  NE1   . TRP A 1 175 ? 50.205  68.520  82.024  1.00 95.17  ? 202 TRP A NE1   1 
ATOM   1278 C  CE2   . TRP A 1 175 ? 51.567  68.518  81.875  1.00 83.72  ? 202 TRP A CE2   1 
ATOM   1279 C  CE3   . TRP A 1 175 ? 53.182  69.041  80.157  1.00 96.85  ? 202 TRP A CE3   1 
ATOM   1280 C  CZ2   . TRP A 1 175 ? 52.569  68.172  82.778  1.00 91.15  ? 202 TRP A CZ2   1 
ATOM   1281 C  CZ3   . TRP A 1 175 ? 54.177  68.697  81.055  1.00 96.90  ? 202 TRP A CZ3   1 
ATOM   1282 C  CH2   . TRP A 1 175 ? 53.865  68.269  82.349  1.00 88.69  ? 202 TRP A CH2   1 
ATOM   1283 N  N     . CYS A 1 176 ? 48.996  71.618  76.396  1.00 103.38 ? 203 CYS A N     1 
ATOM   1284 C  CA    . CYS A 1 176 ? 49.131  72.127  75.040  1.00 99.78  ? 203 CYS A CA    1 
ATOM   1285 C  C     . CYS A 1 176 ? 50.571  72.430  74.658  1.00 108.58 ? 203 CYS A C     1 
ATOM   1286 O  O     . CYS A 1 176 ? 50.883  72.469  73.462  1.00 111.75 ? 203 CYS A O     1 
ATOM   1287 C  CB    . CYS A 1 176 ? 48.273  73.381  74.852  1.00 107.83 ? 203 CYS A CB    1 
ATOM   1288 S  SG    . CYS A 1 176 ? 46.778  73.082  73.873  1.00 125.27 ? 203 CYS A SG    1 
ATOM   1289 N  N     . GLY A 1 177 ? 51.452  72.631  75.637  1.00 109.62 ? 204 GLY A N     1 
ATOM   1290 C  CA    . GLY A 1 177 ? 52.849  72.875  75.354  1.00 104.93 ? 204 GLY A CA    1 
ATOM   1291 C  C     . GLY A 1 177 ? 53.737  72.150  76.344  1.00 101.10 ? 204 GLY A C     1 
ATOM   1292 O  O     . GLY A 1 177 ? 53.299  71.719  77.413  1.00 104.12 ? 204 GLY A O     1 
ATOM   1293 N  N     . MET A 1 178 ? 55.005  72.023  75.964  1.00 100.36 ? 205 MET A N     1 
ATOM   1294 C  CA    . MET A 1 178 ? 56.005  71.397  76.819  1.00 104.43 ? 205 MET A CA    1 
ATOM   1295 C  C     . MET A 1 178 ? 57.351  72.056  76.560  1.00 107.34 ? 205 MET A C     1 
ATOM   1296 O  O     . MET A 1 178 ? 57.726  72.271  75.403  1.00 109.18 ? 205 MET A O     1 
ATOM   1297 C  CB    . MET A 1 178 ? 56.086  69.887  76.568  1.00 94.01  ? 205 MET A CB    1 
ATOM   1298 C  CG    . MET A 1 178 ? 57.087  69.169  77.462  1.00 110.61 ? 205 MET A CG    1 
ATOM   1299 S  SD    . MET A 1 178 ? 57.130  67.387  77.197  1.00 106.07 ? 205 MET A SD    1 
ATOM   1300 C  CE    . MET A 1 178 ? 55.480  66.926  77.711  1.00 93.17  ? 205 MET A CE    1 
ATOM   1301 N  N     . THR A 1 179 ? 58.068  72.379  77.634  1.00 114.27 ? 206 THR A N     1 
ATOM   1302 C  CA    . THR A 1 179 ? 59.368  73.015  77.496  1.00 118.87 ? 206 THR A CA    1 
ATOM   1303 C  C     . THR A 1 179 ? 60.407  72.003  77.016  1.00 129.86 ? 206 THR A C     1 
ATOM   1304 O  O     . THR A 1 179 ? 60.158  70.795  76.939  1.00 127.36 ? 206 THR A O     1 
ATOM   1305 C  CB    . THR A 1 179 ? 59.821  73.625  78.821  1.00 118.54 ? 206 THR A CB    1 
ATOM   1306 O  OG1   . THR A 1 179 ? 60.410  72.604  79.637  1.00 122.90 ? 206 THR A OG1   1 
ATOM   1307 C  CG2   . THR A 1 179 ? 58.639  74.233  79.561  1.00 121.81 ? 206 THR A CG2   1 
ATOM   1308 N  N     . SER A 1 180 ? 61.597  72.514  76.699  1.00 155.23 ? 207 SER A N     1 
ATOM   1309 C  CA    . SER A 1 180 ? 62.711  71.659  76.307  1.00 154.01 ? 207 SER A CA    1 
ATOM   1310 C  C     . SER A 1 180 ? 63.220  70.791  77.449  1.00 149.22 ? 207 SER A C     1 
ATOM   1311 O  O     . SER A 1 180 ? 64.109  69.963  77.224  1.00 148.98 ? 207 SER A O     1 
ATOM   1312 C  CB    . SER A 1 180 ? 63.852  72.513  75.750  1.00 153.44 ? 207 SER A CB    1 
ATOM   1313 O  OG    . SER A 1 180 ? 64.129  73.614  76.601  1.00 163.26 ? 207 SER A OG    1 
ATOM   1314 N  N     . GLN A 1 181 ? 62.681  70.956  78.658  1.00 132.59 ? 208 GLN A N     1 
ATOM   1315 C  CA    . GLN A 1 181 ? 63.062  70.151  79.808  1.00 129.58 ? 208 GLN A CA    1 
ATOM   1316 C  C     . GLN A 1 181 ? 61.916  69.309  80.354  1.00 122.19 ? 208 GLN A C     1 
ATOM   1317 O  O     . GLN A 1 181 ? 62.121  68.561  81.317  1.00 116.01 ? 208 GLN A O     1 
ATOM   1318 C  CB    . GLN A 1 181 ? 63.622  71.051  80.918  1.00 121.55 ? 208 GLN A CB    1 
ATOM   1319 C  CG    . GLN A 1 181 ? 64.877  71.807  80.507  1.00 135.05 ? 208 GLN A CG    1 
ATOM   1320 C  CD    . GLN A 1 181 ? 65.085  73.078  81.306  1.00 140.78 ? 208 GLN A CD    1 
ATOM   1321 O  OE1   . GLN A 1 181 ? 64.264  73.435  82.150  1.00 151.19 ? 208 GLN A OE1   1 
ATOM   1322 N  NE2   . GLN A 1 181 ? 66.186  73.773  81.038  1.00 140.96 ? 208 GLN A NE2   1 
ATOM   1323 N  N     . GLY A 1 182 ? 60.725  69.406  79.773  1.00 122.02 ? 209 GLY A N     1 
ATOM   1324 C  CA    . GLY A 1 182 ? 59.611  68.567  80.157  1.00 104.22 ? 209 GLY A CA    1 
ATOM   1325 C  C     . GLY A 1 182 ? 58.623  69.168  81.132  1.00 112.36 ? 209 GLY A C     1 
ATOM   1326 O  O     . GLY A 1 182 ? 57.943  68.412  81.834  1.00 112.26 ? 209 GLY A O     1 
ATOM   1327 N  N     . TYR A 1 183 ? 58.514  70.490  81.198  1.00 121.58 ? 210 TYR A N     1 
ATOM   1328 C  CA    . TYR A 1 183 ? 57.600  71.153  82.116  1.00 117.95 ? 210 TYR A CA    1 
ATOM   1329 C  C     . TYR A 1 183 ? 56.344  71.605  81.381  1.00 108.82 ? 210 TYR A C     1 
ATOM   1330 O  O     . TYR A 1 183 ? 56.334  71.759  80.157  1.00 102.57 ? 210 TYR A O     1 
ATOM   1331 C  CB    . TYR A 1 183 ? 58.279  72.354  82.783  1.00 125.46 ? 210 TYR A CB    1 
ATOM   1332 C  CG    . TYR A 1 183 ? 59.596  72.025  83.451  1.00 127.43 ? 210 TYR A CG    1 
ATOM   1333 C  CD1   . TYR A 1 183 ? 59.779  70.820  84.118  1.00 134.51 ? 210 TYR A CD1   1 
ATOM   1334 C  CD2   . TYR A 1 183 ? 60.659  72.916  83.407  1.00 127.26 ? 210 TYR A CD2   1 
ATOM   1335 C  CE1   . TYR A 1 183 ? 60.982  70.515  84.726  1.00 136.40 ? 210 TYR A CE1   1 
ATOM   1336 C  CE2   . TYR A 1 183 ? 61.865  72.620  84.013  1.00 132.67 ? 210 TYR A CE2   1 
ATOM   1337 C  CZ    . TYR A 1 183 ? 62.021  71.418  84.670  1.00 138.90 ? 210 TYR A CZ    1 
ATOM   1338 O  OH    . TYR A 1 183 ? 63.221  71.120  85.275  1.00 145.93 ? 210 TYR A OH    1 
ATOM   1339 N  N     . TYR A 1 184 ? 55.275  71.812  82.149  1.00 111.77 ? 211 TYR A N     1 
ATOM   1340 C  CA    . TYR A 1 184 ? 54.033  72.312  81.574  1.00 101.28 ? 211 TYR A CA    1 
ATOM   1341 C  C     . TYR A 1 184 ? 54.255  73.686  80.950  1.00 110.69 ? 211 TYR A C     1 
ATOM   1342 O  O     . TYR A 1 184 ? 55.117  74.458  81.380  1.00 117.51 ? 211 TYR A O     1 
ATOM   1343 C  CB    . TYR A 1 184 ? 52.935  72.385  82.639  1.00 96.71  ? 211 TYR A CB    1 
ATOM   1344 C  CG    . TYR A 1 184 ? 51.674  73.064  82.151  1.00 106.93 ? 211 TYR A CG    1 
ATOM   1345 C  CD1   . TYR A 1 184 ? 50.806  72.417  81.279  1.00 103.15 ? 211 TYR A CD1   1 
ATOM   1346 C  CD2   . TYR A 1 184 ? 51.361  74.357  82.549  1.00 105.53 ? 211 TYR A CD2   1 
ATOM   1347 C  CE1   . TYR A 1 184 ? 49.656  73.041  80.823  1.00 111.27 ? 211 TYR A CE1   1 
ATOM   1348 C  CE2   . TYR A 1 184 ? 50.216  74.988  82.098  1.00 112.84 ? 211 TYR A CE2   1 
ATOM   1349 C  CZ    . TYR A 1 184 ? 49.367  74.327  81.237  1.00 111.28 ? 211 TYR A CZ    1 
ATOM   1350 O  OH    . TYR A 1 184 ? 48.225  74.955  80.788  1.00 105.12 ? 211 TYR A OH    1 
ATOM   1351 N  N     . LYS A 1 185 ? 53.469  73.986  79.920  1.00 110.82 ? 212 LYS A N     1 
ATOM   1352 C  CA    . LYS A 1 185 ? 53.614  75.240  79.191  1.00 113.23 ? 212 LYS A CA    1 
ATOM   1353 C  C     . LYS A 1 185 ? 52.245  75.699  78.720  1.00 118.04 ? 212 LYS A C     1 
ATOM   1354 O  O     . LYS A 1 185 ? 51.559  74.966  77.999  1.00 115.81 ? 212 LYS A O     1 
ATOM   1355 C  CB    . LYS A 1 185 ? 54.565  75.069  78.005  1.00 117.00 ? 212 LYS A CB    1 
ATOM   1356 C  CG    . LYS A 1 185 ? 54.792  76.323  77.175  1.00 117.03 ? 212 LYS A CG    1 
ATOM   1357 C  CD    . LYS A 1 185 ? 55.683  76.007  75.985  1.00 116.19 ? 212 LYS A CD    1 
ATOM   1358 C  CE    . LYS A 1 185 ? 55.953  77.231  75.131  1.00 129.55 ? 212 LYS A CE    1 
ATOM   1359 N  NZ    . LYS A 1 185 ? 56.786  76.881  73.945  1.00 123.22 ? 212 LYS A NZ    1 
ATOM   1360 N  N     . ARG A 1 186 ? 51.848  76.900  79.133  1.00 114.59 ? 213 ARG A N     1 
ATOM   1361 C  CA    . ARG A 1 186 ? 50.637  77.503  78.600  1.00 113.38 ? 213 ARG A CA    1 
ATOM   1362 C  C     . ARG A 1 186 ? 50.853  77.909  77.147  1.00 113.90 ? 213 ARG A C     1 
ATOM   1363 O  O     . ARG A 1 186 ? 51.950  78.305  76.742  1.00 119.36 ? 213 ARG A O     1 
ATOM   1364 C  CB    . ARG A 1 186 ? 50.229  78.726  79.421  1.00 106.96 ? 213 ARG A CB    1 
ATOM   1365 C  CG    . ARG A 1 186 ? 49.921  78.428  80.877  1.00 135.53 ? 213 ARG A CG    1 
ATOM   1366 C  CD    . ARG A 1 186 ? 49.663  79.711  81.656  1.00 135.35 ? 213 ARG A CD    1 
ATOM   1367 N  NE    . ARG A 1 186 ? 49.376  79.450  83.062  1.00 130.67 ? 213 ARG A NE    1 
ATOM   1368 C  CZ    . ARG A 1 186 ? 49.134  80.392  83.963  1.00 153.22 ? 213 ARG A CZ    1 
ATOM   1369 N  NH1   . ARG A 1 186 ? 49.141  81.675  83.641  1.00 147.63 ? 213 ARG A NH1   1 
ATOM   1370 N  NH2   . ARG A 1 186 ? 48.879  80.038  85.220  1.00 156.66 ? 213 ARG A NH2   1 
ATOM   1371 N  N     . THR A 1 187 ? 49.801  77.779  76.355  1.00 110.76 ? 214 THR A N     1 
ATOM   1372 C  CA    . THR A 1 187 ? 49.771  78.212  74.968  1.00 111.20 ? 214 THR A CA    1 
ATOM   1373 C  C     . THR A 1 187 ? 48.471  78.958  74.726  1.00 117.37 ? 214 THR A C     1 
ATOM   1374 O  O     . THR A 1 187 ? 47.502  78.790  75.475  1.00 117.74 ? 214 THR A O     1 
ATOM   1375 C  CB    . THR A 1 187 ? 49.868  77.028  73.992  1.00 111.52 ? 214 THR A CB    1 
ATOM   1376 O  OG1   . THR A 1 187 ? 48.593  76.380  73.907  1.00 108.60 ? 214 THR A OG1   1 
ATOM   1377 C  CG2   . THR A 1 187 ? 50.921  76.028  74.448  1.00 106.02 ? 214 THR A CG2   1 
ATOM   1378 N  N     . PRO A 1 188 ? 48.414  79.798  73.688  1.00 122.53 ? 215 PRO A N     1 
ATOM   1379 C  CA    . PRO A 1 188 ? 47.140  80.455  73.349  1.00 125.96 ? 215 PRO A CA    1 
ATOM   1380 C  C     . PRO A 1 188 ? 46.022  79.480  73.021  1.00 108.74 ? 215 PRO A C     1 
ATOM   1381 O  O     . PRO A 1 188 ? 44.852  79.883  73.006  1.00 118.79 ? 215 PRO A O     1 
ATOM   1382 C  CB    . PRO A 1 188 ? 47.504  81.315  72.132  1.00 130.17 ? 215 PRO A CB    1 
ATOM   1383 C  CG    . PRO A 1 188 ? 48.965  81.578  72.288  1.00 128.36 ? 215 PRO A CG    1 
ATOM   1384 C  CD    . PRO A 1 188 ? 49.537  80.329  72.894  1.00 122.43 ? 215 PRO A CD    1 
ATOM   1385 N  N     . ALA A 1 189 ? 46.339  78.214  72.769  1.00 109.40 ? 216 ALA A N     1 
ATOM   1386 C  CA    . ALA A 1 189 ? 45.345  77.251  72.323  1.00 113.51 ? 216 ALA A CA    1 
ATOM   1387 C  C     . ALA A 1 189 ? 44.707  76.464  73.460  1.00 116.57 ? 216 ALA A C     1 
ATOM   1388 O  O     . ALA A 1 189 ? 43.704  75.780  73.225  1.00 116.01 ? 216 ALA A O     1 
ATOM   1389 C  CB    . ALA A 1 189 ? 45.975  76.275  71.324  1.00 111.73 ? 216 ALA A CB    1 
ATOM   1390 N  N     . TYR A 1 190 ? 45.251  76.538  74.677  1.00 119.22 ? 217 TYR A N     1 
ATOM   1391 C  CA    . TYR A 1 190 ? 44.744  75.695  75.757  1.00 112.63 ? 217 TYR A CA    1 
ATOM   1392 C  C     . TYR A 1 190 ? 43.314  76.071  76.128  1.00 106.18 ? 217 TYR A C     1 
ATOM   1393 O  O     . TYR A 1 190 ? 42.437  75.203  76.217  1.00 92.84  ? 217 TYR A O     1 
ATOM   1394 C  CB    . TYR A 1 190 ? 45.656  75.783  76.982  1.00 105.07 ? 217 TYR A CB    1 
ATOM   1395 C  CG    . TYR A 1 190 ? 45.274  74.810  78.076  1.00 92.83  ? 217 TYR A CG    1 
ATOM   1396 C  CD1   . TYR A 1 190 ? 44.318  75.140  79.028  1.00 95.43  ? 217 TYR A CD1   1 
ATOM   1397 C  CD2   . TYR A 1 190 ? 45.859  73.554  78.148  1.00 95.31  ? 217 TYR A CD2   1 
ATOM   1398 C  CE1   . TYR A 1 190 ? 43.958  74.249  80.021  1.00 99.92  ? 217 TYR A CE1   1 
ATOM   1399 C  CE2   . TYR A 1 190 ? 45.506  72.656  79.140  1.00 98.20  ? 217 TYR A CE2   1 
ATOM   1400 C  CZ    . TYR A 1 190 ? 44.555  73.008  80.074  1.00 95.83  ? 217 TYR A CZ    1 
ATOM   1401 O  OH    . TYR A 1 190 ? 44.200  72.120  81.066  1.00 98.10  ? 217 TYR A OH    1 
ATOM   1402 N  N     . ILE A 1 191 ? 43.063  77.363  76.356  1.00 102.27 ? 218 ILE A N     1 
ATOM   1403 C  CA    . ILE A 1 191 ? 41.736  77.788  76.803  1.00 99.83  ? 218 ILE A CA    1 
ATOM   1404 C  C     . ILE A 1 191 ? 40.653  77.492  75.772  1.00 100.39 ? 218 ILE A C     1 
ATOM   1405 O  O     . ILE A 1 191 ? 39.601  76.955  76.154  1.00 102.13 ? 218 ILE A O     1 
ATOM   1406 C  CB    . ILE A 1 191 ? 41.770  79.273  77.221  1.00 99.42  ? 218 ILE A CB    1 
ATOM   1407 C  CG1   . ILE A 1 191 ? 42.769  79.481  78.362  1.00 91.62  ? 218 ILE A CG1   1 
ATOM   1408 C  CG2   . ILE A 1 191 ? 40.383  79.734  77.638  1.00 91.37  ? 218 ILE A CG2   1 
ATOM   1409 C  CD1   . ILE A 1 191 ? 42.509  78.597  79.569  1.00 94.84  ? 218 ILE A CD1   1 
ATOM   1410 N  N     . PRO A 1 192 ? 40.827  77.801  74.478  1.00 109.50 ? 219 PRO A N     1 
ATOM   1411 C  CA    . PRO A 1 192 ? 39.759  77.467  73.517  1.00 103.12 ? 219 PRO A CA    1 
ATOM   1412 C  C     . PRO A 1 192 ? 39.436  75.986  73.472  1.00 99.85  ? 219 PRO A C     1 
ATOM   1413 O  O     . PRO A 1 192 ? 38.265  75.615  73.319  1.00 97.36  ? 219 PRO A O     1 
ATOM   1414 C  CB    . PRO A 1 192 ? 40.327  77.964  72.181  1.00 97.93  ? 219 PRO A CB    1 
ATOM   1415 C  CG    . PRO A 1 192 ? 41.295  79.024  72.559  1.00 104.61 ? 219 PRO A CG    1 
ATOM   1416 C  CD    . PRO A 1 192 ? 41.924  78.538  73.825  1.00 105.60 ? 219 PRO A CD    1 
ATOM   1417 N  N     . ILE A 1 193 ? 40.448  75.128  73.605  1.00 96.24  ? 220 ILE A N     1 
ATOM   1418 C  CA    . ILE A 1 193 ? 40.208  73.690  73.658  1.00 95.05  ? 220 ILE A CA    1 
ATOM   1419 C  C     . ILE A 1 193 ? 39.512  73.315  74.959  1.00 98.85  ? 220 ILE A C     1 
ATOM   1420 O  O     . ILE A 1 193 ? 38.547  72.541  74.964  1.00 106.18 ? 220 ILE A O     1 
ATOM   1421 C  CB    . ILE A 1 193 ? 41.533  72.924  73.486  1.00 92.71  ? 220 ILE A CB    1 
ATOM   1422 C  CG1   . ILE A 1 193 ? 42.108  73.138  72.087  1.00 81.51  ? 220 ILE A CG1   1 
ATOM   1423 C  CG2   . ILE A 1 193 ? 41.342  71.442  73.766  1.00 92.45  ? 220 ILE A CG2   1 
ATOM   1424 C  CD1   . ILE A 1 193 ? 43.469  72.498  71.886  1.00 84.93  ? 220 ILE A CD1   1 
ATOM   1425 N  N     . ARG A 1 194 ? 39.985  73.864  76.082  1.00 93.62  ? 221 ARG A N     1 
ATOM   1426 C  CA    . ARG A 1 194 ? 39.444  73.500  77.387  1.00 95.16  ? 221 ARG A CA    1 
ATOM   1427 C  C     . ARG A 1 194 ? 37.970  73.867  77.517  1.00 99.75  ? 221 ARG A C     1 
ATOM   1428 O  O     . ARG A 1 194 ? 37.207  73.144  78.169  1.00 97.66  ? 221 ARG A O     1 
ATOM   1429 C  CB    . ARG A 1 194 ? 40.268  74.170  78.489  1.00 84.29  ? 221 ARG A CB    1 
ATOM   1430 C  CG    . ARG A 1 194 ? 39.742  73.954  79.893  1.00 88.36  ? 221 ARG A CG    1 
ATOM   1431 C  CD    . ARG A 1 194 ? 39.691  72.482  80.256  1.00 93.07  ? 221 ARG A CD    1 
ATOM   1432 N  NE    . ARG A 1 194 ? 39.103  72.281  81.575  1.00 98.80  ? 221 ARG A NE    1 
ATOM   1433 C  CZ    . ARG A 1 194 ? 37.802  72.170  81.804  1.00 101.52 ? 221 ARG A CZ    1 
ATOM   1434 N  NH1   . ARG A 1 194 ? 36.921  72.216  80.817  1.00 102.46 ? 221 ARG A NH1   1 
ATOM   1435 N  NH2   . ARG A 1 194 ? 37.374  72.014  83.054  1.00 89.71  ? 221 ARG A NH2   1 
ATOM   1436 N  N     . LYS A 1 195 ? 37.547  74.968  76.901  1.00 94.14  ? 222 LYS A N     1 
ATOM   1437 C  CA    . LYS A 1 195 ? 36.163  75.418  76.970  1.00 86.47  ? 222 LYS A CA    1 
ATOM   1438 C  C     . LYS A 1 195 ? 35.310  74.910  75.812  1.00 104.76 ? 222 LYS A C     1 
ATOM   1439 O  O     . LYS A 1 195 ? 34.188  75.396  75.630  1.00 104.82 ? 222 LYS A O     1 
ATOM   1440 C  CB    . LYS A 1 195 ? 36.112  76.948  77.020  1.00 96.90  ? 222 LYS A CB    1 
ATOM   1441 C  CG    . LYS A 1 195 ? 36.880  77.539  78.190  1.00 106.38 ? 222 LYS A CG    1 
ATOM   1442 C  CD    . LYS A 1 195 ? 36.609  79.023  78.360  1.00 115.95 ? 222 LYS A CD    1 
ATOM   1443 C  CE    . LYS A 1 195 ? 37.262  79.545  79.635  1.00 122.86 ? 222 LYS A CE    1 
ATOM   1444 N  NZ    . LYS A 1 195 ? 36.889  80.954  79.941  1.00 123.97 ? 222 LYS A NZ    1 
ATOM   1445 N  N     . ARG A 1 196 ? 35.817  73.946  75.037  1.00 95.38  ? 223 ARG A N     1 
ATOM   1446 C  CA    . ARG A 1 196 ? 35.132  73.413  73.855  1.00 90.22  ? 223 ARG A CA    1 
ATOM   1447 C  C     . ARG A 1 196 ? 34.726  74.513  72.873  1.00 106.10 ? 223 ARG A C     1 
ATOM   1448 O  O     . ARG A 1 196 ? 33.683  74.424  72.221  1.00 100.23 ? 223 ARG A O     1 
ATOM   1449 C  CB    . ARG A 1 196 ? 33.912  72.572  74.242  1.00 93.47  ? 223 ARG A CB    1 
ATOM   1450 C  CG    . ARG A 1 196 ? 34.253  71.198  74.803  1.00 84.66  ? 223 ARG A CG    1 
ATOM   1451 C  CD    . ARG A 1 196 ? 32.997  70.402  75.116  1.00 87.86  ? 223 ARG A CD    1 
ATOM   1452 N  NE    . ARG A 1 196 ? 33.302  69.195  75.875  1.00 108.20 ? 223 ARG A NE    1 
ATOM   1453 C  CZ    . ARG A 1 196 ? 33.375  69.137  77.199  1.00 104.03 ? 223 ARG A CZ    1 
ATOM   1454 N  NH1   . ARG A 1 196 ? 33.147  70.200  77.954  1.00 89.96  ? 223 ARG A NH1   1 
ATOM   1455 N  NH2   . ARG A 1 196 ? 33.688  67.983  77.781  1.00 120.42 ? 223 ARG A NH2   1 
ATOM   1456 N  N     . ASP A 1 197 ? 35.543  75.563  72.759  1.00 98.79  ? 224 ASP A N     1 
ATOM   1457 C  CA    . ASP A 1 197 ? 35.336  76.542  71.698  1.00 90.29  ? 224 ASP A CA    1 
ATOM   1458 C  C     . ASP A 1 197 ? 35.827  76.004  70.358  1.00 101.94 ? 224 ASP A C     1 
ATOM   1459 O  O     . ASP A 1 197 ? 35.114  76.080  69.352  1.00 111.44 ? 224 ASP A O     1 
ATOM   1460 C  CB    . ASP A 1 197 ? 36.037  77.857  72.045  1.00 108.98 ? 224 ASP A CB    1 
ATOM   1461 C  CG    . ASP A 1 197 ? 35.309  78.637  73.126  1.00 120.27 ? 224 ASP A CG    1 
ATOM   1462 O  OD1   . ASP A 1 197 ? 34.240  78.168  73.576  1.00 116.90 ? 224 ASP A OD1   1 
ATOM   1463 O  OD2   . ASP A 1 197 ? 35.804  79.718  73.523  1.00 106.64 ? 224 ASP A OD2   1 
ATOM   1464 N  N     . ARG A 1 198 ? 37.049  75.469  70.329  1.00 113.25 ? 225 ARG A N     1 
ATOM   1465 C  CA    . ARG A 1 198 ? 37.539  74.675  69.206  1.00 101.70 ? 225 ARG A CA    1 
ATOM   1466 C  C     . ARG A 1 198 ? 37.260  73.211  69.523  1.00 99.02  ? 225 ARG A C     1 
ATOM   1467 O  O     . ARG A 1 198 ? 37.898  72.631  70.409  1.00 111.30 ? 225 ARG A O     1 
ATOM   1468 C  CB    . ARG A 1 198 ? 39.034  74.899  68.969  1.00 107.24 ? 225 ARG A CB    1 
ATOM   1469 C  CG    . ARG A 1 198 ? 39.416  76.224  68.317  1.00 125.96 ? 225 ARG A CG    1 
ATOM   1470 C  CD    . ARG A 1 198 ? 40.941  76.365  68.154  1.00 143.36 ? 225 ARG A CD    1 
ATOM   1471 N  NE    . ARG A 1 198 ? 41.486  75.547  67.072  1.00 162.64 ? 225 ARG A NE    1 
ATOM   1472 C  CZ    . ARG A 1 198 ? 42.751  75.576  66.668  1.00 151.82 ? 225 ARG A CZ    1 
ATOM   1473 N  NH1   . ARG A 1 198 ? 43.643  76.371  67.240  1.00 131.88 ? 225 ARG A NH1   1 
ATOM   1474 N  NH2   . ARG A 1 198 ? 43.131  74.790  65.661  1.00 105.55 ? 225 ARG A NH2   1 
ATOM   1475 N  N     . ARG A 1 199 ? 36.304  72.615  68.819  1.00 102.53 ? 226 ARG A N     1 
ATOM   1476 C  CA    . ARG A 1 199 ? 35.975  71.208  69.004  1.00 96.33  ? 226 ARG A CA    1 
ATOM   1477 C  C     . ARG A 1 199 ? 36.705  70.364  67.969  1.00 86.47  ? 226 ARG A C     1 
ATOM   1478 O  O     . ARG A 1 199 ? 36.813  70.749  66.802  1.00 92.73  ? 226 ARG A O     1 
ATOM   1479 C  CB    . ARG A 1 199 ? 34.466  70.973  68.901  1.00 90.67  ? 226 ARG A CB    1 
ATOM   1480 C  CG    . ARG A 1 199 ? 33.680  71.459  70.107  1.00 94.81  ? 226 ARG A CG    1 
ATOM   1481 C  CD    . ARG A 1 199 ? 32.183  71.289  69.896  1.00 99.78  ? 226 ARG A CD    1 
ATOM   1482 N  NE    . ARG A 1 199 ? 31.407  71.901  70.969  1.00 120.45 ? 226 ARG A NE    1 
ATOM   1483 C  CZ    . ARG A 1 199 ? 30.876  71.236  71.986  1.00 129.18 ? 226 ARG A CZ    1 
ATOM   1484 N  NH1   . ARG A 1 199 ? 31.004  69.923  72.095  1.00 123.21 ? 226 ARG A NH1   1 
ATOM   1485 N  NH2   . ARG A 1 199 ? 30.197  71.904  72.916  1.00 123.23 ? 226 ARG A NH2   1 
ATOM   1486 N  N     . GLY A 1 200 ? 37.205  69.218  68.401  1.00 95.61  ? 227 GLY A N     1 
ATOM   1487 C  CA    . GLY A 1 200 ? 37.892  68.303  67.515  1.00 92.24  ? 227 GLY A CA    1 
ATOM   1488 C  C     . GLY A 1 200 ? 38.997  67.582  68.259  1.00 88.02  ? 227 GLY A C     1 
ATOM   1489 O  O     . GLY A 1 200 ? 39.124  67.688  69.475  1.00 93.73  ? 227 GLY A O     1 
ATOM   1490 N  N     . CYS A 1 201 ? 39.793  66.836  67.498  1.00 79.21  ? 228 CYS A N     1 
ATOM   1491 C  CA    . CYS A 1 201 ? 40.933  66.109  68.041  1.00 81.00  ? 228 CYS A CA    1 
ATOM   1492 C  C     . CYS A 1 201 ? 42.210  66.860  67.686  1.00 86.40  ? 228 CYS A C     1 
ATOM   1493 O  O     . CYS A 1 201 ? 42.508  67.060  66.505  1.00 89.31  ? 228 CYS A O     1 
ATOM   1494 C  CB    . CYS A 1 201 ? 40.981  64.679  67.508  1.00 66.94  ? 228 CYS A CB    1 
ATOM   1495 S  SG    . CYS A 1 201 ? 39.558  63.653  67.972  1.00 103.41 ? 228 CYS A SG    1 
ATOM   1496 N  N     . PHE A 1 202 ? 42.961  67.265  68.705  1.00 84.32  ? 229 PHE A N     1 
ATOM   1497 C  CA    . PHE A 1 202 ? 44.128  68.116  68.534  1.00 82.54  ? 229 PHE A CA    1 
ATOM   1498 C  C     . PHE A 1 202 ? 45.384  67.372  68.958  1.00 79.71  ? 229 PHE A C     1 
ATOM   1499 O  O     . PHE A 1 202 ? 45.372  66.623  69.939  1.00 82.17  ? 229 PHE A O     1 
ATOM   1500 C  CB    . PHE A 1 202 ? 43.973  69.407  69.346  1.00 79.78  ? 229 PHE A CB    1 
ATOM   1501 C  CG    . PHE A 1 202 ? 42.668  70.105  69.110  1.00 90.35  ? 229 PHE A CG    1 
ATOM   1502 C  CD1   . PHE A 1 202 ? 42.498  70.926  68.012  1.00 82.90  ? 229 PHE A CD1   1 
ATOM   1503 C  CD2   . PHE A 1 202 ? 41.604  69.925  69.975  1.00 95.02  ? 229 PHE A CD2   1 
ATOM   1504 C  CE1   . PHE A 1 202 ? 41.297  71.564  67.788  1.00 92.42  ? 229 PHE A CE1   1 
ATOM   1505 C  CE2   . PHE A 1 202 ? 40.398  70.560  69.756  1.00 91.92  ? 229 PHE A CE2   1 
ATOM   1506 C  CZ    . PHE A 1 202 ? 40.244  71.379  68.661  1.00 99.50  ? 229 PHE A CZ    1 
ATOM   1507 N  N     . ALA A 1 203 ? 46.464  67.575  68.209  1.00 79.69  ? 230 ALA A N     1 
ATOM   1508 C  CA    . ALA A 1 203 ? 47.743  66.954  68.528  1.00 87.91  ? 230 ALA A CA    1 
ATOM   1509 C  C     . ALA A 1 203 ? 48.422  67.743  69.641  1.00 88.88  ? 230 ALA A C     1 
ATOM   1510 O  O     . ALA A 1 203 ? 48.718  68.930  69.475  1.00 81.08  ? 230 ALA A O     1 
ATOM   1511 C  CB    . ALA A 1 203 ? 48.627  66.888  67.285  1.00 84.79  ? 230 ALA A CB    1 
ATOM   1512 N  N     . VAL A 1 204 ? 48.660  67.088  70.774  1.00 85.50  ? 231 VAL A N     1 
ATOM   1513 C  CA    . VAL A 1 204 ? 49.219  67.753  71.949  1.00 75.88  ? 231 VAL A CA    1 
ATOM   1514 C  C     . VAL A 1 204 ? 50.438  66.970  72.413  1.00 81.53  ? 231 VAL A C     1 
ATOM   1515 O  O     . VAL A 1 204 ? 50.600  65.789  72.071  1.00 93.28  ? 231 VAL A O     1 
ATOM   1516 C  CB    . VAL A 1 204 ? 48.175  67.874  73.082  1.00 72.99  ? 231 VAL A CB    1 
ATOM   1517 C  CG1   . VAL A 1 204 ? 46.971  68.662  72.607  1.00 69.08  ? 231 VAL A CG1   1 
ATOM   1518 C  CG2   . VAL A 1 204 ? 47.770  66.500  73.569  1.00 73.18  ? 231 VAL A CG2   1 
ATOM   1519 N  N     . PRO A 1 205 ? 51.325  67.601  73.184  1.00 77.51  ? 232 PRO A N     1 
ATOM   1520 C  CA    . PRO A 1 205 ? 52.517  66.900  73.676  1.00 72.28  ? 232 PRO A CA    1 
ATOM   1521 C  C     . PRO A 1 205 ? 52.319  66.115  74.964  1.00 81.97  ? 232 PRO A C     1 
ATOM   1522 O  O     . PRO A 1 205 ? 53.299  65.558  75.472  1.00 83.79  ? 232 PRO A O     1 
ATOM   1523 C  CB    . PRO A 1 205 ? 53.497  68.058  73.902  1.00 76.84  ? 232 PRO A CB    1 
ATOM   1524 C  CG    . PRO A 1 205 ? 52.622  69.171  74.348  1.00 83.06  ? 232 PRO A CG    1 
ATOM   1525 C  CD    . PRO A 1 205 ? 51.364  69.036  73.521  1.00 84.97  ? 232 PRO A CD    1 
ATOM   1526 N  N     . MET A 1 206 ? 51.102  66.046  75.501  1.00 80.95  ? 233 MET A N     1 
ATOM   1527 C  CA    . MET A 1 206 ? 50.882  65.379  76.778  1.00 74.22  ? 233 MET A CA    1 
ATOM   1528 C  C     . MET A 1 206 ? 49.407  65.050  76.945  1.00 76.59  ? 233 MET A C     1 
ATOM   1529 O  O     . MET A 1 206 ? 48.556  65.933  76.807  1.00 83.53  ? 233 MET A O     1 
ATOM   1530 C  CB    . MET A 1 206 ? 51.354  66.262  77.937  1.00 80.49  ? 233 MET A CB    1 
ATOM   1531 C  CG    . MET A 1 206 ? 50.979  65.739  79.309  1.00 79.30  ? 233 MET A CG    1 
ATOM   1532 S  SD    . MET A 1 206 ? 51.938  64.295  79.792  1.00 76.72  ? 233 MET A SD    1 
ATOM   1533 C  CE    . MET A 1 206 ? 53.531  65.037  80.122  1.00 89.31  ? 233 MET A CE    1 
ATOM   1534 N  N     . VAL A 1 207 ? 49.114  63.782  77.235  1.00 74.88  ? 234 VAL A N     1 
ATOM   1535 C  CA    . VAL A 1 207 ? 47.809  63.348  77.719  1.00 72.89  ? 234 VAL A CA    1 
ATOM   1536 C  C     . VAL A 1 207 ? 48.052  62.344  78.834  1.00 69.20  ? 234 VAL A C     1 
ATOM   1537 O  O     . VAL A 1 207 ? 49.070  61.646  78.849  1.00 85.54  ? 234 VAL A O     1 
ATOM   1538 C  CB    . VAL A 1 207 ? 46.925  62.716  76.621  1.00 67.53  ? 234 VAL A CB    1 
ATOM   1539 C  CG1   . VAL A 1 207 ? 46.505  63.755  75.597  1.00 76.22  ? 234 VAL A CG1   1 
ATOM   1540 C  CG2   . VAL A 1 207 ? 47.643  61.550  75.963  1.00 68.44  ? 234 VAL A CG2   1 
ATOM   1541 N  N     . HIS A 1 208 ? 47.115  62.272  79.774  1.00 75.16  ? 235 HIS A N     1 
ATOM   1542 C  CA    . HIS A 1 208 ? 47.273  61.390  80.924  1.00 70.97  ? 235 HIS A CA    1 
ATOM   1543 C  C     . HIS A 1 208 ? 45.910  61.164  81.562  1.00 68.75  ? 235 HIS A C     1 
ATOM   1544 O  O     . HIS A 1 208 ? 44.881  61.605  81.044  1.00 75.97  ? 235 HIS A O     1 
ATOM   1545 C  CB    . HIS A 1 208 ? 48.273  61.972  81.924  1.00 71.05  ? 235 HIS A CB    1 
ATOM   1546 C  CG    . HIS A 1 208 ? 47.923  63.349  82.391  1.00 78.87  ? 235 HIS A CG    1 
ATOM   1547 N  ND1   . HIS A 1 208 ? 46.960  63.587  83.347  1.00 75.51  ? 235 HIS A ND1   1 
ATOM   1548 C  CD2   . HIS A 1 208 ? 48.404  64.561  82.030  1.00 68.45  ? 235 HIS A CD2   1 
ATOM   1549 C  CE1   . HIS A 1 208 ? 46.866  64.887  83.558  1.00 77.76  ? 235 HIS A CE1   1 
ATOM   1550 N  NE2   . HIS A 1 208 ? 47.734  65.501  82.774  1.00 71.80  ? 235 HIS A NE2   1 
ATOM   1551 N  N     . SER A 1 209 ? 45.917  60.448  82.690  1.00 83.31  ? 236 SER A N     1 
ATOM   1552 C  CA    . SER A 1 209 ? 44.729  60.143  83.483  1.00 79.65  ? 236 SER A CA    1 
ATOM   1553 C  C     . SER A 1 209 ? 43.808  59.164  82.764  1.00 74.36  ? 236 SER A C     1 
ATOM   1554 O  O     . SER A 1 209 ? 43.605  58.044  83.245  1.00 78.81  ? 236 SER A O     1 
ATOM   1555 C  CB    . SER A 1 209 ? 43.986  61.428  83.863  1.00 71.90  ? 236 SER A CB    1 
ATOM   1556 O  OG    . SER A 1 209 ? 44.800  62.244  84.694  1.00 81.45  ? 236 SER A OG    1 
ATOM   1557 N  N     . THR A 1 210 ? 43.251  59.557  81.619  1.00 80.39  ? 237 THR A N     1 
ATOM   1558 C  CA    . THR A 1 210 ? 42.432  58.659  80.811  1.00 78.00  ? 237 THR A CA    1 
ATOM   1559 C  C     . THR A 1 210 ? 42.839  58.791  79.353  1.00 68.82  ? 237 THR A C     1 
ATOM   1560 O  O     . THR A 1 210 ? 42.715  59.871  78.768  1.00 68.27  ? 237 THR A O     1 
ATOM   1561 C  CB    . THR A 1 210 ? 40.938  58.954  80.975  1.00 68.66  ? 237 THR A CB    1 
ATOM   1562 O  OG1   . THR A 1 210 ? 40.542  58.691  82.327  1.00 73.79  ? 237 THR A OG1   1 
ATOM   1563 C  CG2   . THR A 1 210 ? 40.125  58.073  80.046  1.00 53.24  ? 237 THR A CG2   1 
ATOM   1564 N  N     . PHE A 1 211 ? 43.312  57.694  78.768  1.00 73.79  ? 238 PHE A N     1 
ATOM   1565 C  CA    . PHE A 1 211 ? 43.717  57.688  77.370  1.00 70.73  ? 238 PHE A CA    1 
ATOM   1566 C  C     . PHE A 1 211 ? 43.672  56.261  76.849  1.00 64.45  ? 238 PHE A C     1 
ATOM   1567 O  O     . PHE A 1 211 ? 43.667  55.298  77.620  1.00 74.04  ? 238 PHE A O     1 
ATOM   1568 C  CB    . PHE A 1 211 ? 45.116  58.289  77.183  1.00 69.84  ? 238 PHE A CB    1 
ATOM   1569 C  CG    . PHE A 1 211 ? 46.173  57.635  78.024  1.00 75.36  ? 238 PHE A CG    1 
ATOM   1570 C  CD1   . PHE A 1 211 ? 46.462  58.114  79.290  1.00 71.71  ? 238 PHE A CD1   1 
ATOM   1571 C  CD2   . PHE A 1 211 ? 46.878  56.543  77.551  1.00 66.74  ? 238 PHE A CD2   1 
ATOM   1572 C  CE1   . PHE A 1 211 ? 47.428  57.515  80.071  1.00 76.11  ? 238 PHE A CE1   1 
ATOM   1573 C  CE2   . PHE A 1 211 ? 47.847  55.940  78.328  1.00 82.03  ? 238 PHE A CE2   1 
ATOM   1574 C  CZ    . PHE A 1 211 ? 48.117  56.428  79.596  1.00 67.70  ? 238 PHE A CZ    1 
ATOM   1575 N  N     . LEU A 1 212 ? 43.663  56.144  75.524  1.00 71.75  ? 239 LEU A N     1 
ATOM   1576 C  CA    . LEU A 1 212 ? 43.525  54.874  74.826  1.00 53.71  ? 239 LEU A CA    1 
ATOM   1577 C  C     . LEU A 1 212 ? 44.745  54.650  73.943  1.00 68.01  ? 239 LEU A C     1 
ATOM   1578 O  O     . LEU A 1 212 ? 45.123  55.536  73.168  1.00 77.64  ? 239 LEU A O     1 
ATOM   1579 C  CB    . LEU A 1 212 ? 42.250  54.872  73.978  1.00 58.61  ? 239 LEU A CB    1 
ATOM   1580 C  CG    . LEU A 1 212 ? 41.853  53.573  73.278  1.00 68.36  ? 239 LEU A CG    1 
ATOM   1581 C  CD1   . LEU A 1 212 ? 41.503  52.499  74.296  1.00 68.60  ? 239 LEU A CD1   1 
ATOM   1582 C  CD2   . LEU A 1 212 ? 40.692  53.817  72.330  1.00 69.64  ? 239 LEU A CD2   1 
ATOM   1583 N  N     . ILE A 1 213 ? 45.355  53.470  74.053  1.00 59.90  ? 240 ILE A N     1 
ATOM   1584 C  CA    . ILE A 1 213 ? 46.477  53.085  73.203  1.00 61.41  ? 240 ILE A CA    1 
ATOM   1585 C  C     . ILE A 1 213 ? 45.995  52.052  72.195  1.00 63.30  ? 240 ILE A C     1 
ATOM   1586 O  O     . ILE A 1 213 ? 45.245  51.133  72.543  1.00 74.21  ? 240 ILE A O     1 
ATOM   1587 C  CB    . ILE A 1 213 ? 47.665  52.534  74.013  1.00 60.26  ? 240 ILE A CB    1 
ATOM   1588 C  CG1   . ILE A 1 213 ? 47.935  53.412  75.233  1.00 68.75  ? 240 ILE A CG1   1 
ATOM   1589 C  CG2   . ILE A 1 213 ? 48.908  52.458  73.136  1.00 52.66  ? 240 ILE A CG2   1 
ATOM   1590 C  CD1   . ILE A 1 213 ? 49.167  52.997  76.021  1.00 69.71  ? 240 ILE A CD1   1 
ATOM   1591 N  N     . ASP A 1 214 ? 46.433  52.205  70.946  1.00 66.86  ? 241 ASP A N     1 
ATOM   1592 C  CA    . ASP A 1 214 ? 46.023  51.344  69.837  1.00 56.75  ? 241 ASP A CA    1 
ATOM   1593 C  C     . ASP A 1 214 ? 47.110  50.292  69.636  1.00 67.28  ? 241 ASP A C     1 
ATOM   1594 O  O     . ASP A 1 214 ? 48.111  50.536  68.957  1.00 71.49  ? 241 ASP A O     1 
ATOM   1595 C  CB    . ASP A 1 214 ? 45.792  52.175  68.577  1.00 65.87  ? 241 ASP A CB    1 
ATOM   1596 C  CG    . ASP A 1 214 ? 45.015  51.426  67.502  1.00 83.15  ? 241 ASP A CG    1 
ATOM   1597 O  OD1   . ASP A 1 214 ? 45.040  50.172  67.502  1.00 71.41  ? 241 ASP A OD1   1 
ATOM   1598 O  OD2   . ASP A 1 214 ? 44.378  52.102  66.657  1.00 77.10  ? 241 ASP A OD2   1 
ATOM   1599 N  N     . LEU A 1 215 ? 46.913  49.113  70.218  1.00 67.93  ? 242 LEU A N     1 
ATOM   1600 C  CA    . LEU A 1 215 ? 47.912  48.058  70.108  1.00 62.86  ? 242 LEU A CA    1 
ATOM   1601 C  C     . LEU A 1 215 ? 47.856  47.317  68.778  1.00 60.97  ? 242 LEU A C     1 
ATOM   1602 O  O     . LEU A 1 215 ? 48.639  46.383  68.574  1.00 64.68  ? 242 LEU A O     1 
ATOM   1603 C  CB    . LEU A 1 215 ? 47.762  47.073  71.264  1.00 53.63  ? 242 LEU A CB    1 
ATOM   1604 C  CG    . LEU A 1 215 ? 47.740  47.769  72.626  1.00 66.46  ? 242 LEU A CG    1 
ATOM   1605 C  CD1   . LEU A 1 215 ? 47.715  46.747  73.726  1.00 66.42  ? 242 LEU A CD1   1 
ATOM   1606 C  CD2   . LEU A 1 215 ? 48.933  48.696  72.786  1.00 72.54  ? 242 LEU A CD2   1 
ATOM   1607 N  N     . ARG A 1 216 ? 46.946  47.695  67.878  1.00 73.67  ? 243 ARG A N     1 
ATOM   1608 C  CA    . ARG A 1 216 ? 47.024  47.199  66.509  1.00 68.53  ? 243 ARG A CA    1 
ATOM   1609 C  C     . ARG A 1 216 ? 48.154  47.873  65.745  1.00 63.95  ? 243 ARG A C     1 
ATOM   1610 O  O     . ARG A 1 216 ? 48.703  47.287  64.806  1.00 62.65  ? 243 ARG A O     1 
ATOM   1611 C  CB    . ARG A 1 216 ? 45.704  47.430  65.775  1.00 58.14  ? 243 ARG A CB    1 
ATOM   1612 C  CG    . ARG A 1 216 ? 44.469  46.842  66.451  1.00 66.42  ? 243 ARG A CG    1 
ATOM   1613 C  CD    . ARG A 1 216 ? 43.223  47.369  65.761  1.00 58.44  ? 243 ARG A CD    1 
ATOM   1614 N  NE    . ARG A 1 216 ? 43.277  48.823  65.654  1.00 74.15  ? 243 ARG A NE    1 
ATOM   1615 C  CZ    . ARG A 1 216 ? 42.748  49.527  64.663  1.00 70.06  ? 243 ARG A CZ    1 
ATOM   1616 N  NH1   . ARG A 1 216 ? 42.096  48.941  63.673  1.00 65.65  ? 243 ARG A NH1   1 
ATOM   1617 N  NH2   . ARG A 1 216 ? 42.893  50.850  64.656  1.00 72.41  ? 243 ARG A NH2   1 
ATOM   1618 N  N     . LYS A 1 217 ? 48.512  49.095  66.133  1.00 69.92  ? 244 LYS A N     1 
ATOM   1619 C  CA    . LYS A 1 217 ? 49.513  49.871  65.413  1.00 62.14  ? 244 LYS A CA    1 
ATOM   1620 C  C     . LYS A 1 217 ? 50.912  49.347  65.714  1.00 67.94  ? 244 LYS A C     1 
ATOM   1621 O  O     . LYS A 1 217 ? 51.265  49.110  66.873  1.00 76.76  ? 244 LYS A O     1 
ATOM   1622 C  CB    . LYS A 1 217 ? 49.399  51.346  65.793  1.00 66.50  ? 244 LYS A CB    1 
ATOM   1623 C  CG    . LYS A 1 217 ? 48.021  51.949  65.532  1.00 70.58  ? 244 LYS A CG    1 
ATOM   1624 C  CD    . LYS A 1 217 ? 47.814  52.268  64.053  1.00 59.23  ? 244 LYS A CD    1 
ATOM   1625 C  CE    . LYS A 1 217 ? 46.340  52.475  63.735  1.00 57.41  ? 244 LYS A CE    1 
ATOM   1626 N  NZ    . LYS A 1 217 ? 45.714  53.535  64.569  1.00 68.33  ? 244 LYS A NZ    1 
ATOM   1627 N  N     . ALA A 1 218 ? 51.708  49.164  64.661  1.00 55.48  ? 245 ALA A N     1 
ATOM   1628 C  CA    . ALA A 1 218 ? 53.066  48.665  64.839  1.00 71.78  ? 245 ALA A CA    1 
ATOM   1629 C  C     . ALA A 1 218 ? 53.901  49.611  65.686  1.00 77.51  ? 245 ALA A C     1 
ATOM   1630 O  O     . ALA A 1 218 ? 54.807  49.169  66.402  1.00 71.74  ? 245 ALA A O     1 
ATOM   1631 C  CB    . ALA A 1 218 ? 53.731  48.445  63.477  1.00 61.87  ? 245 ALA A CB    1 
ATOM   1632 N  N     . ALA A 1 219 ? 53.614  50.913  65.620  1.00 75.10  ? 246 ALA A N     1 
ATOM   1633 C  CA    . ALA A 1 219 ? 54.386  51.873  66.400  1.00 76.42  ? 246 ALA A CA    1 
ATOM   1634 C  C     . ALA A 1 219 ? 54.186  51.677  67.897  1.00 76.07  ? 246 ALA A C     1 
ATOM   1635 O  O     . ALA A 1 219 ? 55.102  51.957  68.680  1.00 80.78  ? 246 ALA A O     1 
ATOM   1636 C  CB    . ALA A 1 219 ? 54.021  53.301  66.002  1.00 74.69  ? 246 ALA A CB    1 
ATOM   1637 N  N     . SER A 1 220 ? 53.013  51.187  68.313  1.00 67.86  ? 247 SER A N     1 
ATOM   1638 C  CA    . SER A 1 220 ? 52.747  51.003  69.735  1.00 68.97  ? 247 SER A CA    1 
ATOM   1639 C  C     . SER A 1 220 ? 53.693  49.994  70.374  1.00 72.27  ? 247 SER A C     1 
ATOM   1640 O  O     . SER A 1 220 ? 53.880  50.023  71.596  1.00 71.31  ? 247 SER A O     1 
ATOM   1641 C  CB    . SER A 1 220 ? 51.298  50.565  69.950  1.00 60.20  ? 247 SER A CB    1 
ATOM   1642 O  OG    . SER A 1 220 ? 51.138  49.186  69.686  1.00 63.78  ? 247 SER A OG    1 
ATOM   1643 N  N     . ARG A 1 221 ? 54.299  49.113  69.573  1.00 65.33  ? 248 ARG A N     1 
ATOM   1644 C  CA    . ARG A 1 221 ? 55.295  48.182  70.091  1.00 65.08  ? 248 ARG A CA    1 
ATOM   1645 C  C     . ARG A 1 221 ? 56.446  48.903  70.782  1.00 71.94  ? 248 ARG A C     1 
ATOM   1646 O  O     . ARG A 1 221 ? 57.087  48.333  71.673  1.00 69.68  ? 248 ARG A O     1 
ATOM   1647 C  CB    . ARG A 1 221 ? 55.843  47.315  68.958  1.00 68.48  ? 248 ARG A CB    1 
ATOM   1648 C  CG    . ARG A 1 221 ? 54.842  46.381  68.302  1.00 66.16  ? 248 ARG A CG    1 
ATOM   1649 C  CD    . ARG A 1 221 ? 55.536  45.577  67.214  1.00 76.04  ? 248 ARG A CD    1 
ATOM   1650 N  NE    . ARG A 1 221 ? 56.855  45.138  67.657  1.00 99.43  ? 248 ARG A NE    1 
ATOM   1651 C  CZ    . ARG A 1 221 ? 57.790  44.632  66.863  1.00 101.27 ? 248 ARG A CZ    1 
ATOM   1652 N  NH1   . ARG A 1 221 ? 57.586  44.478  65.564  1.00 73.38  ? 248 ARG A NH1   1 
ATOM   1653 N  NH2   . ARG A 1 221 ? 58.962  44.278  67.386  1.00 105.44 ? 248 ARG A NH2   1 
ATOM   1654 N  N     . ASN A 1 222 ? 56.729  50.143  70.387  1.00 68.00  ? 249 ASN A N     1 
ATOM   1655 C  CA    . ASN A 1 222 ? 57.846  50.908  70.926  1.00 71.04  ? 249 ASN A CA    1 
ATOM   1656 C  C     . ASN A 1 222 ? 57.481  51.746  72.151  1.00 68.65  ? 249 ASN A C     1 
ATOM   1657 O  O     . ASN A 1 222 ? 58.371  52.355  72.752  1.00 69.68  ? 249 ASN A O     1 
ATOM   1658 C  CB    . ASN A 1 222 ? 58.431  51.809  69.833  1.00 61.86  ? 249 ASN A CB    1 
ATOM   1659 C  CG    . ASN A 1 222 ? 58.951  51.018  68.649  1.00 83.39  ? 249 ASN A CG    1 
ATOM   1660 O  OD1   . ASN A 1 222 ? 59.423  49.892  68.803  1.00 84.12  ? 249 ASN A OD1   1 
ATOM   1661 N  ND2   . ASN A 1 222 ? 58.867  51.602  67.459  1.00 84.05  ? 249 ASN A ND2   1 
ATOM   1662 N  N     . LEU A 1 223 ? 56.209  51.797  72.534  1.00 68.11  ? 250 LEU A N     1 
ATOM   1663 C  CA    . LEU A 1 223 ? 55.805  52.524  73.729  1.00 64.93  ? 250 LEU A CA    1 
ATOM   1664 C  C     . LEU A 1 223 ? 56.151  51.726  74.981  1.00 66.75  ? 250 LEU A C     1 
ATOM   1665 O  O     . LEU A 1 223 ? 56.037  50.496  75.003  1.00 73.94  ? 250 LEU A O     1 
ATOM   1666 C  CB    . LEU A 1 223 ? 54.305  52.814  73.688  1.00 59.51  ? 250 LEU A CB    1 
ATOM   1667 C  CG    . LEU A 1 223 ? 53.815  53.621  72.483  1.00 60.85  ? 250 LEU A CG    1 
ATOM   1668 C  CD1   . LEU A 1 223 ? 52.321  53.888  72.584  1.00 62.81  ? 250 LEU A CD1   1 
ATOM   1669 C  CD2   . LEU A 1 223 ? 54.579  54.927  72.368  1.00 61.22  ? 250 LEU A CD2   1 
ATOM   1670 N  N     . ALA A 1 224 ? 56.575  52.431  76.029  1.00 70.83  ? 251 ALA A N     1 
ATOM   1671 C  CA    . ALA A 1 224 ? 56.915  51.786  77.296  1.00 73.15  ? 251 ALA A CA    1 
ATOM   1672 C  C     . ALA A 1 224 ? 56.706  52.770  78.434  1.00 70.63  ? 251 ALA A C     1 
ATOM   1673 O  O     . ALA A 1 224 ? 57.291  53.858  78.430  1.00 71.83  ? 251 ALA A O     1 
ATOM   1674 C  CB    . ALA A 1 224 ? 58.357  51.279  77.293  1.00 56.83  ? 251 ALA A CB    1 
ATOM   1675 N  N     . PHE A 1 225 ? 55.875  52.385  79.406  1.00 69.45  ? 252 PHE A N     1 
ATOM   1676 C  CA    . PHE A 1 225 ? 55.730  53.193  80.611  1.00 68.96  ? 252 PHE A CA    1 
ATOM   1677 C  C     . PHE A 1 225 ? 56.954  53.079  81.508  1.00 65.11  ? 252 PHE A C     1 
ATOM   1678 O  O     . PHE A 1 225 ? 57.271  54.021  82.244  1.00 74.14  ? 252 PHE A O     1 
ATOM   1679 C  CB    . PHE A 1 225 ? 54.470  52.785  81.376  1.00 63.05  ? 252 PHE A CB    1 
ATOM   1680 C  CG    . PHE A 1 225 ? 53.197  53.186  80.690  1.00 68.59  ? 252 PHE A CG    1 
ATOM   1681 C  CD1   . PHE A 1 225 ? 52.697  54.468  80.831  1.00 74.97  ? 252 PHE A CD1   1 
ATOM   1682 C  CD2   . PHE A 1 225 ? 52.509  52.288  79.897  1.00 65.99  ? 252 PHE A CD2   1 
ATOM   1683 C  CE1   . PHE A 1 225 ? 51.532  54.842  80.201  1.00 58.70  ? 252 PHE A CE1   1 
ATOM   1684 C  CE2   . PHE A 1 225 ? 51.343  52.657  79.262  1.00 68.83  ? 252 PHE A CE2   1 
ATOM   1685 C  CZ    . PHE A 1 225 ? 50.854  53.938  79.413  1.00 63.45  ? 252 PHE A CZ    1 
ATOM   1686 N  N     . TYR A 1 226 ? 57.653  51.943  81.459  1.00 67.12  ? 253 TYR A N     1 
ATOM   1687 C  CA    . TYR A 1 226 ? 58.858  51.720  82.240  1.00 69.78  ? 253 TYR A CA    1 
ATOM   1688 C  C     . TYR A 1 226 ? 59.744  50.734  81.495  1.00 72.00  ? 253 TYR A C     1 
ATOM   1689 O  O     . TYR A 1 226 ? 59.224  49.802  80.864  1.00 83.58  ? 253 TYR A O     1 
ATOM   1690 C  CB    . TYR A 1 226 ? 58.541  51.179  83.639  1.00 80.55  ? 253 TYR A CB    1 
ATOM   1691 C  CG    . TYR A 1 226 ? 59.669  51.351  84.632  1.00 74.15  ? 253 TYR A CG    1 
ATOM   1692 C  CD1   . TYR A 1 226 ? 59.877  52.570  85.267  1.00 73.53  ? 253 TYR A CD1   1 
ATOM   1693 C  CD2   . TYR A 1 226 ? 60.525  50.299  84.936  1.00 77.23  ? 253 TYR A CD2   1 
ATOM   1694 C  CE1   . TYR A 1 226 ? 60.907  52.739  86.175  1.00 82.72  ? 253 TYR A CE1   1 
ATOM   1695 C  CE2   . TYR A 1 226 ? 61.561  50.458  85.846  1.00 82.84  ? 253 TYR A CE2   1 
ATOM   1696 C  CZ    . TYR A 1 226 ? 61.745  51.681  86.463  1.00 90.87  ? 253 TYR A CZ    1 
ATOM   1697 O  OH    . TYR A 1 226 ? 62.769  51.852  87.368  1.00 99.96  ? 253 TYR A OH    1 
ATOM   1698 N  N     . PRO A 1 227 ? 61.064  50.907  81.535  1.00 74.51  ? 254 PRO A N     1 
ATOM   1699 C  CA    . PRO A 1 227 ? 61.809  52.016  82.150  1.00 80.45  ? 254 PRO A CA    1 
ATOM   1700 C  C     . PRO A 1 227 ? 61.818  53.238  81.234  1.00 81.96  ? 254 PRO A C     1 
ATOM   1701 O  O     . PRO A 1 227 ? 61.260  53.170  80.142  1.00 82.04  ? 254 PRO A O     1 
ATOM   1702 C  CB    . PRO A 1 227 ? 63.203  51.405  82.364  1.00 78.35  ? 254 PRO A CB    1 
ATOM   1703 C  CG    . PRO A 1 227 ? 63.340  50.400  81.258  1.00 72.93  ? 254 PRO A CG    1 
ATOM   1704 C  CD    . PRO A 1 227 ? 61.958  49.825  81.082  1.00 73.01  ? 254 PRO A CD    1 
ATOM   1705 N  N     . PRO A 1 228 ? 62.400  54.369  81.642  1.00 83.97  ? 255 PRO A N     1 
ATOM   1706 C  CA    . PRO A 1 228 ? 62.500  55.509  80.724  1.00 86.51  ? 255 PRO A CA    1 
ATOM   1707 C  C     . PRO A 1 228 ? 63.353  55.169  79.513  1.00 85.58  ? 255 PRO A C     1 
ATOM   1708 O  O     . PRO A 1 228 ? 64.228  54.301  79.567  1.00 85.57  ? 255 PRO A O     1 
ATOM   1709 C  CB    . PRO A 1 228 ? 63.158  56.600  81.577  1.00 85.56  ? 255 PRO A CB    1 
ATOM   1710 C  CG    . PRO A 1 228 ? 62.845  56.223  82.983  1.00 83.41  ? 255 PRO A CG    1 
ATOM   1711 C  CD    . PRO A 1 228 ? 62.832  54.725  83.007  1.00 75.98  ? 255 PRO A CD    1 
ATOM   1712 N  N     . HIS A 1 229 ? 63.082  55.862  78.410  1.00 81.03  ? 256 HIS A N     1 
ATOM   1713 C  CA    . HIS A 1 229 ? 63.882  55.678  77.210  1.00 75.22  ? 256 HIS A CA    1 
ATOM   1714 C  C     . HIS A 1 229 ? 65.343  55.993  77.523  1.00 84.06  ? 256 HIS A C     1 
ATOM   1715 O  O     . HIS A 1 229 ? 65.626  56.906  78.306  1.00 92.68  ? 256 HIS A O     1 
ATOM   1716 C  CB    . HIS A 1 229 ? 63.369  56.575  76.081  1.00 79.52  ? 256 HIS A CB    1 
ATOM   1717 C  CG    . HIS A 1 229 ? 63.906  56.220  74.727  1.00 89.45  ? 256 HIS A CG    1 
ATOM   1718 N  ND1   . HIS A 1 229 ? 65.132  56.659  74.273  1.00 82.07  ? 256 HIS A ND1   1 
ATOM   1719 C  CD2   . HIS A 1 229 ? 63.381  55.473  73.727  1.00 99.89  ? 256 HIS A CD2   1 
ATOM   1720 C  CE1   . HIS A 1 229 ? 65.338  56.197  73.053  1.00 95.83  ? 256 HIS A CE1   1 
ATOM   1721 N  NE2   . HIS A 1 229 ? 64.291  55.472  72.698  1.00 99.87  ? 256 HIS A NE2   1 
ATOM   1722 N  N     . PRO A 1 230 ? 66.295  55.251  76.951  1.00 87.83  ? 257 PRO A N     1 
ATOM   1723 C  CA    . PRO A 1 230 ? 67.712  55.471  77.297  1.00 90.94  ? 257 PRO A CA    1 
ATOM   1724 C  C     . PRO A 1 230 ? 68.207  56.893  77.060  1.00 83.73  ? 257 PRO A C     1 
ATOM   1725 O  O     . PRO A 1 230 ? 69.276  57.242  77.574  1.00 104.05 ? 257 PRO A O     1 
ATOM   1726 C  CB    . PRO A 1 230 ? 68.450  54.470  76.399  1.00 84.23  ? 257 PRO A CB    1 
ATOM   1727 C  CG    . PRO A 1 230 ? 67.440  53.391  76.146  1.00 77.37  ? 257 PRO A CG    1 
ATOM   1728 C  CD    . PRO A 1 230 ? 66.114  54.088  76.064  1.00 73.79  ? 257 PRO A CD    1 
ATOM   1729 N  N     . ASP A 1 231 ? 67.477  57.718  76.311  1.00 92.13  ? 258 ASP A N     1 
ATOM   1730 C  CA    . ASP A 1 231 ? 67.837  59.117  76.114  1.00 97.95  ? 258 ASP A CA    1 
ATOM   1731 C  C     . ASP A 1 231 ? 67.123  60.055  77.081  1.00 99.48  ? 258 ASP A C     1 
ATOM   1732 O  O     . ASP A 1 231 ? 67.347  61.268  77.026  1.00 101.11 ? 258 ASP A O     1 
ATOM   1733 C  CB    . ASP A 1 231 ? 67.535  59.544  74.672  1.00 104.14 ? 258 ASP A CB    1 
ATOM   1734 C  CG    . ASP A 1 231 ? 68.269  58.700  73.645  1.00 105.97 ? 258 ASP A CG    1 
ATOM   1735 O  OD1   . ASP A 1 231 ? 69.329  58.136  73.991  1.00 103.59 ? 258 ASP A OD1   1 
ATOM   1736 O  OD2   . ASP A 1 231 ? 67.788  58.606  72.493  1.00 95.35  ? 258 ASP A OD2   1 
ATOM   1737 N  N     . TYR A 1 232 ? 66.276  59.524  77.961  1.00 85.17  ? 259 TYR A N     1 
ATOM   1738 C  CA    . TYR A 1 232 ? 65.475  60.357  78.850  1.00 89.37  ? 259 TYR A CA    1 
ATOM   1739 C  C     . TYR A 1 232 ? 66.375  61.061  79.858  1.00 94.61  ? 259 TYR A C     1 
ATOM   1740 O  O     . TYR A 1 232 ? 67.112  60.410  80.607  1.00 96.30  ? 259 TYR A O     1 
ATOM   1741 C  CB    . TYR A 1 232 ? 64.428  59.501  79.560  1.00 79.72  ? 259 TYR A CB    1 
ATOM   1742 C  CG    . TYR A 1 232 ? 63.409  60.282  80.354  1.00 83.91  ? 259 TYR A CG    1 
ATOM   1743 C  CD1   . TYR A 1 232 ? 62.298  60.839  79.736  1.00 85.83  ? 259 TYR A CD1   1 
ATOM   1744 C  CD2   . TYR A 1 232 ? 63.551  60.455  81.726  1.00 84.74  ? 259 TYR A CD2   1 
ATOM   1745 C  CE1   . TYR A 1 232 ? 61.358  61.550  80.459  1.00 90.60  ? 259 TYR A CE1   1 
ATOM   1746 C  CE2   . TYR A 1 232 ? 62.619  61.167  82.458  1.00 78.55  ? 259 TYR A CE2   1 
ATOM   1747 C  CZ    . TYR A 1 232 ? 61.523  61.709  81.819  1.00 86.11  ? 259 TYR A CZ    1 
ATOM   1748 O  OH    . TYR A 1 232 ? 60.591  62.417  82.541  1.00 95.64  ? 259 TYR A OH    1 
ATOM   1749 N  N     . THR A 1 233 ? 66.314  62.394  79.878  1.00 96.04  ? 260 THR A N     1 
ATOM   1750 C  CA    . THR A 1 233 ? 67.132  63.197  80.780  1.00 103.10 ? 260 THR A CA    1 
ATOM   1751 C  C     . THR A 1 233 ? 66.289  64.130  81.643  1.00 112.10 ? 260 THR A C     1 
ATOM   1752 O  O     . THR A 1 233 ? 66.810  65.122  82.162  1.00 123.42 ? 260 THR A O     1 
ATOM   1753 C  CB    . THR A 1 233 ? 68.164  64.009  79.993  1.00 108.95 ? 260 THR A CB    1 
ATOM   1754 O  OG1   . THR A 1 233 ? 67.502  64.750  78.959  1.00 119.58 ? 260 THR A OG1   1 
ATOM   1755 C  CG2   . THR A 1 233 ? 69.203  63.090  79.368  1.00 115.29 ? 260 THR A CG2   1 
ATOM   1756 N  N     . TRP A 1 234 ? 65.003  63.834  81.808  1.00 102.59 ? 261 TRP A N     1 
ATOM   1757 C  CA    . TRP A 1 234 ? 64.087  64.693  82.535  1.00 96.84  ? 261 TRP A CA    1 
ATOM   1758 C  C     . TRP A 1 234 ? 63.827  64.123  83.927  1.00 99.90  ? 261 TRP A C     1 
ATOM   1759 O  O     . TRP A 1 234 ? 64.461  63.153  84.359  1.00 95.54  ? 261 TRP A O     1 
ATOM   1760 C  CB    . TRP A 1 234 ? 62.801  64.868  81.727  1.00 93.16  ? 261 TRP A CB    1 
ATOM   1761 C  CG    . TRP A 1 234 ? 63.020  65.593  80.436  1.00 103.70 ? 261 TRP A CG    1 
ATOM   1762 C  CD1   . TRP A 1 234 ? 64.073  66.400  80.121  1.00 111.58 ? 261 TRP A CD1   1 
ATOM   1763 C  CD2   . TRP A 1 234 ? 62.171  65.573  79.282  1.00 108.31 ? 261 TRP A CD2   1 
ATOM   1764 N  NE1   . TRP A 1 234 ? 63.930  66.890  78.846  1.00 110.31 ? 261 TRP A NE1   1 
ATOM   1765 C  CE2   . TRP A 1 234 ? 62.770  66.397  78.309  1.00 107.08 ? 261 TRP A CE2   1 
ATOM   1766 C  CE3   . TRP A 1 234 ? 60.962  64.941  78.978  1.00 104.61 ? 261 TRP A CE3   1 
ATOM   1767 C  CZ2   . TRP A 1 234 ? 62.202  66.606  77.055  1.00 108.48 ? 261 TRP A CZ2   1 
ATOM   1768 C  CZ3   . TRP A 1 234 ? 60.397  65.151  77.732  1.00 100.70 ? 261 TRP A CZ3   1 
ATOM   1769 C  CH2   . TRP A 1 234 ? 61.018  65.975  76.786  1.00 100.04 ? 261 TRP A CH2   1 
ATOM   1770 N  N     . SER A 1 235 ? 62.888  64.735  84.646  1.00 93.55  ? 262 SER A N     1 
ATOM   1771 C  CA    . SER A 1 235 ? 62.600  64.313  86.008  1.00 94.00  ? 262 SER A CA    1 
ATOM   1772 C  C     . SER A 1 235 ? 61.903  62.958  86.010  1.00 85.91  ? 262 SER A C     1 
ATOM   1773 O  O     . SER A 1 235 ? 61.330  62.516  85.009  1.00 95.30  ? 262 SER A O     1 
ATOM   1774 C  CB    . SER A 1 235 ? 61.737  65.350  86.728  1.00 107.06 ? 262 SER A CB    1 
ATOM   1775 O  OG    . SER A 1 235 ? 60.549  65.616  86.006  1.00 131.77 ? 262 SER A OG    1 
ATOM   1776 N  N     . PHE A 1 236 ? 61.955  62.298  87.165  1.00 87.40  ? 263 PHE A N     1 
ATOM   1777 C  CA    . PHE A 1 236 ? 61.437  60.939  87.312  1.00 85.46  ? 263 PHE A CA    1 
ATOM   1778 C  C     . PHE A 1 236 ? 59.923  60.962  87.547  1.00 86.41  ? 263 PHE A C     1 
ATOM   1779 O  O     . PHE A 1 236 ? 59.404  60.466  88.546  1.00 107.01 ? 263 PHE A O     1 
ATOM   1780 C  CB    . PHE A 1 236 ? 62.175  60.235  88.443  1.00 86.46  ? 263 PHE A CB    1 
ATOM   1781 C  CG    . PHE A 1 236 ? 62.015  58.747  88.447  1.00 85.18  ? 263 PHE A CG    1 
ATOM   1782 C  CD1   . PHE A 1 236 ? 62.188  58.018  87.284  1.00 91.04  ? 263 PHE A CD1   1 
ATOM   1783 C  CD2   . PHE A 1 236 ? 61.720  58.071  89.618  1.00 77.68  ? 263 PHE A CD2   1 
ATOM   1784 C  CE1   . PHE A 1 236 ? 62.059  56.640  87.286  1.00 92.44  ? 263 PHE A CE1   1 
ATOM   1785 C  CE2   . PHE A 1 236 ? 61.592  56.692  89.625  1.00 90.29  ? 263 PHE A CE2   1 
ATOM   1786 C  CZ    . PHE A 1 236 ? 61.762  55.978  88.458  1.00 88.21  ? 263 PHE A CZ    1 
ATOM   1787 N  N     . ASP A 1 237 ? 59.216  61.565  86.590  1.00 93.79  ? 264 ASP A N     1 
ATOM   1788 C  CA    . ASP A 1 237 ? 57.769  61.726  86.629  1.00 88.59  ? 264 ASP A CA    1 
ATOM   1789 C  C     . ASP A 1 237 ? 57.115  60.738  85.668  1.00 92.28  ? 264 ASP A C     1 
ATOM   1790 O  O     . ASP A 1 237 ? 57.567  60.574  84.530  1.00 91.49  ? 264 ASP A O     1 
ATOM   1791 C  CB    . ASP A 1 237 ? 57.393  63.169  86.264  1.00 89.85  ? 264 ASP A CB    1 
ATOM   1792 C  CG    . ASP A 1 237 ? 55.927  63.472  86.496  1.00 102.52 ? 264 ASP A CG    1 
ATOM   1793 O  OD1   . ASP A 1 237 ? 55.189  62.580  86.981  1.00 113.70 ? 264 ASP A OD1   1 
ATOM   1794 O  OD2   . ASP A 1 237 ? 55.509  64.613  86.199  1.00 109.97 ? 264 ASP A OD2   1 
ATOM   1795 N  N     . ASP A 1 238 ? 56.036  60.093  86.126  1.00 87.25  ? 265 ASP A N     1 
ATOM   1796 C  CA    . ASP A 1 238 ? 55.455  58.985  85.369  1.00 75.91  ? 265 ASP A CA    1 
ATOM   1797 C  C     . ASP A 1 238 ? 54.855  59.447  84.041  1.00 77.70  ? 265 ASP A C     1 
ATOM   1798 O  O     . ASP A 1 238 ? 55.024  58.778  83.014  1.00 86.42  ? 265 ASP A O     1 
ATOM   1799 C  CB    . ASP A 1 238 ? 54.408  58.257  86.216  1.00 61.47  ? 265 ASP A CB    1 
ATOM   1800 C  CG    . ASP A 1 238 ? 53.257  59.156  86.645  1.00 85.24  ? 265 ASP A CG    1 
ATOM   1801 O  OD1   . ASP A 1 238 ? 53.401  60.399  86.600  1.00 85.52  ? 265 ASP A OD1   1 
ATOM   1802 O  OD2   . ASP A 1 238 ? 52.208  58.609  87.051  1.00 83.11  ? 265 ASP A OD2   1 
ATOM   1803 N  N     . ILE A 1 239 ? 54.174  60.593  84.028  1.00 79.08  ? 266 ILE A N     1 
ATOM   1804 C  CA    . ILE A 1 239 ? 53.521  61.034  82.798  1.00 79.92  ? 266 ILE A CA    1 
ATOM   1805 C  C     . ILE A 1 239 ? 54.539  61.565  81.798  1.00 74.61  ? 266 ILE A C     1 
ATOM   1806 O  O     . ILE A 1 239 ? 54.399  61.359  80.589  1.00 85.47  ? 266 ILE A O     1 
ATOM   1807 C  CB    . ILE A 1 239 ? 52.434  62.079  83.106  1.00 82.71  ? 266 ILE A CB    1 
ATOM   1808 C  CG1   . ILE A 1 239 ? 53.004  63.226  83.940  1.00 84.36  ? 266 ILE A CG1   1 
ATOM   1809 C  CG2   . ILE A 1 239 ? 51.277  61.432  83.827  1.00 64.55  ? 266 ILE A CG2   1 
ATOM   1810 C  CD1   . ILE A 1 239 ? 52.024  64.349  84.167  1.00 66.72  ? 266 ILE A CD1   1 
ATOM   1811 N  N     . ILE A 1 240 ? 55.574  62.256  82.277  1.00 84.01  ? 267 ILE A N     1 
ATOM   1812 C  CA    . ILE A 1 240 ? 56.594  62.775  81.373  1.00 78.98  ? 267 ILE A CA    1 
ATOM   1813 C  C     . ILE A 1 240 ? 57.398  61.631  80.768  1.00 82.74  ? 267 ILE A C     1 
ATOM   1814 O  O     . ILE A 1 240 ? 57.767  61.667  79.587  1.00 71.51  ? 267 ILE A O     1 
ATOM   1815 C  CB    . ILE A 1 240 ? 57.498  63.776  82.112  1.00 85.00  ? 267 ILE A CB    1 
ATOM   1816 C  CG1   . ILE A 1 240 ? 56.654  64.756  82.922  1.00 98.17  ? 267 ILE A CG1   1 
ATOM   1817 C  CG2   . ILE A 1 240 ? 58.352  64.539  81.131  1.00 90.57  ? 267 ILE A CG2   1 
ATOM   1818 C  CD1   . ILE A 1 240 ? 57.474  65.735  83.731  1.00 115.62 ? 267 ILE A CD1   1 
ATOM   1819 N  N     . VAL A 1 241 ? 57.681  60.598  81.566  1.00 90.10  ? 268 VAL A N     1 
ATOM   1820 C  CA    . VAL A 1 241 ? 58.406  59.438  81.055  1.00 80.02  ? 268 VAL A CA    1 
ATOM   1821 C  C     . VAL A 1 241 ? 57.639  58.794  79.909  1.00 71.95  ? 268 VAL A C     1 
ATOM   1822 O  O     . VAL A 1 241 ? 58.224  58.435  78.877  1.00 85.16  ? 268 VAL A O     1 
ATOM   1823 C  CB    . VAL A 1 241 ? 58.686  58.438  82.192  1.00 75.54  ? 268 VAL A CB    1 
ATOM   1824 C  CG1   . VAL A 1 241 ? 58.822  57.028  81.651  1.00 64.30  ? 268 VAL A CG1   1 
ATOM   1825 C  CG2   . VAL A 1 241 ? 59.954  58.831  82.929  1.00 76.41  ? 268 VAL A CG2   1 
ATOM   1826 N  N     . PHE A 1 242 ? 56.320  58.647  80.059  1.00 75.82  ? 269 PHE A N     1 
ATOM   1827 C  CA    . PHE A 1 242 ? 55.525  58.122  78.955  1.00 73.75  ? 269 PHE A CA    1 
ATOM   1828 C  C     . PHE A 1 242 ? 55.514  59.092  77.784  1.00 78.35  ? 269 PHE A C     1 
ATOM   1829 O  O     . PHE A 1 242 ? 55.647  58.677  76.627  1.00 73.34  ? 269 PHE A O     1 
ATOM   1830 C  CB    . PHE A 1 242 ? 54.099  57.819  79.409  1.00 61.11  ? 269 PHE A CB    1 
ATOM   1831 C  CG    . PHE A 1 242 ? 53.297  57.037  78.403  1.00 63.50  ? 269 PHE A CG    1 
ATOM   1832 C  CD1   . PHE A 1 242 ? 53.846  55.936  77.765  1.00 71.53  ? 269 PHE A CD1   1 
ATOM   1833 C  CD2   . PHE A 1 242 ? 51.992  57.396  78.103  1.00 66.34  ? 269 PHE A CD2   1 
ATOM   1834 C  CE1   . PHE A 1 242 ? 53.114  55.212  76.837  1.00 66.19  ? 269 PHE A CE1   1 
ATOM   1835 C  CE2   . PHE A 1 242 ? 51.249  56.674  77.181  1.00 64.67  ? 269 PHE A CE2   1 
ATOM   1836 C  CZ    . PHE A 1 242 ? 51.812  55.581  76.546  1.00 69.84  ? 269 PHE A CZ    1 
ATOM   1837 N  N     . ALA A 1 243 ? 55.372  60.389  78.069  1.00 77.66  ? 270 ALA A N     1 
ATOM   1838 C  CA    . ALA A 1 243 ? 55.343  61.391  77.007  1.00 71.66  ? 270 ALA A CA    1 
ATOM   1839 C  C     . ALA A 1 243 ? 56.597  61.317  76.146  1.00 72.88  ? 270 ALA A C     1 
ATOM   1840 O  O     . ALA A 1 243 ? 56.520  61.299  74.912  1.00 80.35  ? 270 ALA A O     1 
ATOM   1841 C  CB    . ALA A 1 243 ? 55.181  62.785  77.613  1.00 73.01  ? 270 ALA A CB    1 
ATOM   1842 N  N     . PHE A 1 244 ? 57.767  61.260  76.786  1.00 76.20  ? 271 PHE A N     1 
ATOM   1843 C  CA    . PHE A 1 244 ? 59.015  61.146  76.044  1.00 73.76  ? 271 PHE A CA    1 
ATOM   1844 C  C     . PHE A 1 244 ? 59.107  59.824  75.291  1.00 80.45  ? 271 PHE A C     1 
ATOM   1845 O  O     . PHE A 1 244 ? 59.813  59.742  74.282  1.00 83.12  ? 271 PHE A O     1 
ATOM   1846 C  CB    . PHE A 1 244 ? 60.195  61.302  76.999  1.00 70.10  ? 271 PHE A CB    1 
ATOM   1847 C  CG    . PHE A 1 244 ? 61.528  61.341  76.316  1.00 81.99  ? 271 PHE A CG    1 
ATOM   1848 C  CD1   . PHE A 1 244 ? 61.967  62.497  75.696  1.00 81.90  ? 271 PHE A CD1   1 
ATOM   1849 C  CD2   . PHE A 1 244 ? 62.348  60.224  76.303  1.00 83.90  ? 271 PHE A CD2   1 
ATOM   1850 C  CE1   . PHE A 1 244 ? 63.196  62.538  75.068  1.00 88.51  ? 271 PHE A CE1   1 
ATOM   1851 C  CE2   . PHE A 1 244 ? 63.581  60.259  75.682  1.00 85.68  ? 271 PHE A CE2   1 
ATOM   1852 C  CZ    . PHE A 1 244 ? 64.006  61.417  75.063  1.00 89.27  ? 271 PHE A CZ    1 
ATOM   1853 N  N     . SER A 1 245 ? 58.405  58.786  75.758  1.00 80.59  ? 272 SER A N     1 
ATOM   1854 C  CA    . SER A 1 245 ? 58.442  57.501  75.065  1.00 71.51  ? 272 SER A CA    1 
ATOM   1855 C  C     . SER A 1 245 ? 57.725  57.578  73.722  1.00 83.75  ? 272 SER A C     1 
ATOM   1856 O  O     . SER A 1 245 ? 58.192  57.009  72.727  1.00 85.98  ? 272 SER A O     1 
ATOM   1857 C  CB    . SER A 1 245 ? 57.825  56.409  75.938  1.00 73.16  ? 272 SER A CB    1 
ATOM   1858 O  OG    . SER A 1 245 ? 57.820  55.165  75.257  1.00 54.54  ? 272 SER A OG    1 
ATOM   1859 N  N     . CYS A 1 246 ? 56.585  58.270  73.674  1.00 76.55  ? 273 CYS A N     1 
ATOM   1860 C  CA    . CYS A 1 246 ? 55.894  58.454  72.404  1.00 78.77  ? 273 CYS A CA    1 
ATOM   1861 C  C     . CYS A 1 246 ? 56.686  59.358  71.474  1.00 77.42  ? 273 CYS A C     1 
ATOM   1862 O  O     . CYS A 1 246 ? 56.647  59.175  70.253  1.00 83.01  ? 273 CYS A O     1 
ATOM   1863 C  CB    . CYS A 1 246 ? 54.499  59.024  72.638  1.00 64.91  ? 273 CYS A CB    1 
ATOM   1864 S  SG    . CYS A 1 246 ? 53.514  58.063  73.801  1.00 84.58  ? 273 CYS A SG    1 
ATOM   1865 N  N     . LYS A 1 247 ? 57.406  60.333  72.029  1.00 80.55  ? 274 LYS A N     1 
ATOM   1866 C  CA    . LYS A 1 247 ? 58.261  61.176  71.203  1.00 83.33  ? 274 LYS A CA    1 
ATOM   1867 C  C     . LYS A 1 247 ? 59.309  60.333  70.486  1.00 72.15  ? 274 LYS A C     1 
ATOM   1868 O  O     . LYS A 1 247 ? 59.457  60.413  69.261  1.00 86.92  ? 274 LYS A O     1 
ATOM   1869 C  CB    . LYS A 1 247 ? 58.913  62.258  72.066  1.00 78.71  ? 274 LYS A CB    1 
ATOM   1870 C  CG    . LYS A 1 247 ? 59.686  63.310  71.290  1.00 98.35  ? 274 LYS A CG    1 
ATOM   1871 C  CD    . LYS A 1 247 ? 58.802  64.037  70.292  1.00 110.18 ? 274 LYS A CD    1 
ATOM   1872 C  CE    . LYS A 1 247 ? 59.583  65.113  69.545  1.00 125.13 ? 274 LYS A CE    1 
ATOM   1873 N  NZ    . LYS A 1 247 ? 58.798  65.711  68.424  1.00 123.69 ? 274 LYS A NZ    1 
ATOM   1874 N  N     . GLN A 1 248 ? 60.023  59.488  71.234  1.00 79.74  ? 275 GLN A N     1 
ATOM   1875 C  CA    . GLN A 1 248 ? 61.006  58.600  70.623  1.00 85.60  ? 275 GLN A CA    1 
ATOM   1876 C  C     . GLN A 1 248 ? 60.355  57.614  69.661  1.00 83.43  ? 275 GLN A C     1 
ATOM   1877 O  O     . GLN A 1 248 ? 60.973  57.212  68.670  1.00 77.57  ? 275 GLN A O     1 
ATOM   1878 C  CB    . GLN A 1 248 ? 61.776  57.849  71.709  1.00 75.61  ? 275 GLN A CB    1 
ATOM   1879 C  CG    . GLN A 1 248 ? 62.568  58.758  72.622  1.00 83.76  ? 275 GLN A CG    1 
ATOM   1880 C  CD    . GLN A 1 248 ? 63.450  59.720  71.851  1.00 90.36  ? 275 GLN A CD    1 
ATOM   1881 O  OE1   . GLN A 1 248 ? 63.229  60.931  71.870  1.00 92.34  ? 275 GLN A OE1   1 
ATOM   1882 N  NE2   . GLN A 1 248 ? 64.460  59.186  71.171  1.00 102.70 ? 275 GLN A NE2   1 
ATOM   1883 N  N     . ALA A 1 249 ? 59.118  57.207  69.936  1.00 80.99  ? 276 ALA A N     1 
ATOM   1884 C  CA    . ALA A 1 249 ? 58.418  56.286  69.052  1.00 78.84  ? 276 ALA A CA    1 
ATOM   1885 C  C     . ALA A 1 249 ? 57.806  56.981  67.845  1.00 79.66  ? 276 ALA A C     1 
ATOM   1886 O  O     . ALA A 1 249 ? 57.301  56.295  66.949  1.00 75.86  ? 276 ALA A O     1 
ATOM   1887 C  CB    . ALA A 1 249 ? 57.326  55.543  69.828  1.00 71.26  ? 276 ALA A CB    1 
ATOM   1888 N  N     . GLU A 1 250 ? 57.853  58.316  67.805  1.00 84.68  ? 277 GLU A N     1 
ATOM   1889 C  CA    . GLU A 1 250 ? 57.203  59.124  66.770  1.00 77.74  ? 277 GLU A CA    1 
ATOM   1890 C  C     . GLU A 1 250 ? 55.694  58.904  66.749  1.00 68.23  ? 277 GLU A C     1 
ATOM   1891 O  O     . GLU A 1 250 ? 55.052  59.027  65.703  1.00 83.40  ? 277 GLU A O     1 
ATOM   1892 C  CB    . GLU A 1 250 ? 57.816  58.871  65.387  1.00 79.93  ? 277 GLU A CB    1 
ATOM   1893 C  CG    . GLU A 1 250 ? 59.223  59.439  65.247  1.00 87.99  ? 277 GLU A CG    1 
ATOM   1894 C  CD    . GLU A 1 250 ? 59.875  59.094  63.926  1.00 100.08 ? 277 GLU A CD    1 
ATOM   1895 O  OE1   . GLU A 1 250 ? 59.261  58.355  63.126  1.00 126.93 ? 277 GLU A OE1   1 
ATOM   1896 O  OE2   . GLU A 1 250 ? 61.007  59.565  63.691  1.00 92.29  ? 277 GLU A OE2   1 
ATOM   1897 N  N     . VAL A 1 251 ? 55.122  58.592  67.908  1.00 56.33  ? 278 VAL A N     1 
ATOM   1898 C  CA    . VAL A 1 251 ? 53.681  58.441  68.073  1.00 71.06  ? 278 VAL A CA    1 
ATOM   1899 C  C     . VAL A 1 251 ? 53.122  59.765  68.573  1.00 85.60  ? 278 VAL A C     1 
ATOM   1900 O  O     . VAL A 1 251 ? 53.548  60.272  69.620  1.00 96.46  ? 278 VAL A O     1 
ATOM   1901 C  CB    . VAL A 1 251 ? 53.344  57.299  69.045  1.00 65.75  ? 278 VAL A CB    1 
ATOM   1902 C  CG1   . VAL A 1 251 ? 51.846  57.220  69.272  1.00 56.86  ? 278 VAL A CG1   1 
ATOM   1903 C  CG2   . VAL A 1 251 ? 53.871  55.980  68.510  1.00 75.01  ? 278 VAL A CG2   1 
ATOM   1904 N  N     . GLN A 1 252 ? 52.170  60.327  67.831  1.00 88.09  ? 279 GLN A N     1 
ATOM   1905 C  CA    . GLN A 1 252 ? 51.569  61.608  68.182  1.00 74.31  ? 279 GLN A CA    1 
ATOM   1906 C  C     . GLN A 1 252 ? 50.405  61.405  69.146  1.00 80.95  ? 279 GLN A C     1 
ATOM   1907 O  O     . GLN A 1 252 ? 49.526  60.572  68.902  1.00 89.14  ? 279 GLN A O     1 
ATOM   1908 C  CB    . GLN A 1 252 ? 51.091  62.334  66.926  1.00 76.59  ? 279 GLN A CB    1 
ATOM   1909 C  CG    . GLN A 1 252 ? 50.558  63.726  67.193  1.00 94.85  ? 279 GLN A CG    1 
ATOM   1910 C  CD    . GLN A 1 252 ? 51.627  64.662  67.711  1.00 97.48  ? 279 GLN A CD    1 
ATOM   1911 O  OE1   . GLN A 1 252 ? 52.559  65.017  66.988  1.00 104.11 ? 279 GLN A OE1   1 
ATOM   1912 N  NE2   . GLN A 1 252 ? 51.505  65.062  68.974  1.00 93.58  ? 279 GLN A NE2   1 
ATOM   1913 N  N     . MET A 1 253 ? 50.405  62.168  70.236  1.00 86.02  ? 280 MET A N     1 
ATOM   1914 C  CA    . MET A 1 253 ? 49.321  62.134  71.209  1.00 82.52  ? 280 MET A CA    1 
ATOM   1915 C  C     . MET A 1 253 ? 48.214  63.089  70.795  1.00 77.68  ? 280 MET A C     1 
ATOM   1916 O  O     . MET A 1 253 ? 48.479  64.198  70.321  1.00 83.67  ? 280 MET A O     1 
ATOM   1917 C  CB    . MET A 1 253 ? 49.824  62.514  72.601  1.00 74.98  ? 280 MET A CB    1 
ATOM   1918 C  CG    . MET A 1 253 ? 50.678  61.462  73.262  1.00 91.66  ? 280 MET A CG    1 
ATOM   1919 S  SD    . MET A 1 253 ? 51.826  62.193  74.442  1.00 144.09 ? 280 MET A SD    1 
ATOM   1920 C  CE    . MET A 1 253 ? 52.901  63.091  73.321  1.00 96.00  ? 280 MET A CE    1 
ATOM   1921 N  N     . TYR A 1 254 ? 46.969  62.661  70.990  1.00 80.29  ? 281 TYR A N     1 
ATOM   1922 C  CA    . TYR A 1 254 ? 45.813  63.478  70.655  1.00 69.22  ? 281 TYR A CA    1 
ATOM   1923 C  C     . TYR A 1 254 ? 44.884  63.596  71.851  1.00 76.16  ? 281 TYR A C     1 
ATOM   1924 O  O     . TYR A 1 254 ? 44.834  62.715  72.715  1.00 74.94  ? 281 TYR A O     1 
ATOM   1925 C  CB    . TYR A 1 254 ? 45.039  62.905  69.464  1.00 69.23  ? 281 TYR A CB    1 
ATOM   1926 C  CG    . TYR A 1 254 ? 45.726  63.110  68.136  1.00 77.30  ? 281 TYR A CG    1 
ATOM   1927 C  CD1   . TYR A 1 254 ? 46.647  62.191  67.656  1.00 82.00  ? 281 TYR A CD1   1 
ATOM   1928 C  CD2   . TYR A 1 254 ? 45.455  64.224  67.364  1.00 76.96  ? 281 TYR A CD2   1 
ATOM   1929 C  CE1   . TYR A 1 254 ? 47.276  62.378  66.444  1.00 75.96  ? 281 TYR A CE1   1 
ATOM   1930 C  CE2   . TYR A 1 254 ? 46.079  64.420  66.151  1.00 89.57  ? 281 TYR A CE2   1 
ATOM   1931 C  CZ    . TYR A 1 254 ? 46.988  63.497  65.695  1.00 86.16  ? 281 TYR A CZ    1 
ATOM   1932 O  OH    . TYR A 1 254 ? 47.608  63.701  64.483  1.00 95.10  ? 281 TYR A OH    1 
ATOM   1933 N  N     . VAL A 1 255 ? 44.156  64.709  71.893  1.00 84.03  ? 282 VAL A N     1 
ATOM   1934 C  CA    . VAL A 1 255 ? 43.049  64.907  72.818  1.00 72.75  ? 282 VAL A CA    1 
ATOM   1935 C  C     . VAL A 1 255 ? 41.847  65.372  72.008  1.00 82.31  ? 282 VAL A C     1 
ATOM   1936 O  O     . VAL A 1 255 ? 41.979  66.201  71.100  1.00 80.26  ? 282 VAL A O     1 
ATOM   1937 C  CB    . VAL A 1 255 ? 43.396  65.919  73.931  1.00 77.14  ? 282 VAL A CB    1 
ATOM   1938 C  CG1   . VAL A 1 255 ? 43.776  67.269  73.337  1.00 65.09  ? 282 VAL A CG1   1 
ATOM   1939 C  CG2   . VAL A 1 255 ? 42.236  66.058  74.913  1.00 70.70  ? 282 VAL A CG2   1 
ATOM   1940 N  N     . CYS A 1 256 ? 40.681  64.810  72.309  1.00 75.46  ? 283 CYS A N     1 
ATOM   1941 C  CA    . CYS A 1 256 ? 39.451  65.155  71.614  1.00 80.15  ? 283 CYS A CA    1 
ATOM   1942 C  C     . CYS A 1 256 ? 38.476  65.776  72.602  1.00 83.34  ? 283 CYS A C     1 
ATOM   1943 O  O     . CYS A 1 256 ? 38.330  65.291  73.729  1.00 80.25  ? 283 CYS A O     1 
ATOM   1944 C  CB    . CYS A 1 256 ? 38.820  63.925  70.950  1.00 70.01  ? 283 CYS A CB    1 
ATOM   1945 S  SG    . CYS A 1 256 ? 39.935  62.982  69.861  1.00 105.46 ? 283 CYS A SG    1 
ATOM   1946 N  N     . ASN A 1 257 ? 37.826  66.863  72.183  1.00 77.19  ? 284 ASN A N     1 
ATOM   1947 C  CA    . ASN A 1 257 ? 36.817  67.533  72.994  1.00 81.93  ? 284 ASN A CA    1 
ATOM   1948 C  C     . ASN A 1 257 ? 35.522  67.708  72.213  1.00 86.62  ? 284 ASN A C     1 
ATOM   1949 O  O     . ASN A 1 257 ? 34.802  68.693  72.400  1.00 90.12  ? 284 ASN A O     1 
ATOM   1950 C  CB    . ASN A 1 257 ? 37.324  68.883  73.502  1.00 78.45  ? 284 ASN A CB    1 
ATOM   1951 C  CG    . ASN A 1 257 ? 37.726  69.822  72.378  1.00 92.97  ? 284 ASN A CG    1 
ATOM   1952 O  OD1   . ASN A 1 257 ? 37.604  69.494  71.196  1.00 90.74  ? 284 ASN A OD1   1 
ATOM   1953 N  ND2   . ASN A 1 257 ? 38.206  71.006  72.746  1.00 91.15  ? 284 ASN A ND2   1 
ATOM   1954 N  N     . LYS A 1 258 ? 35.215  66.755  71.332  1.00 79.48  ? 285 LYS A N     1 
ATOM   1955 C  CA    . LYS A 1 258 ? 34.051  66.897  70.466  1.00 83.33  ? 285 LYS A CA    1 
ATOM   1956 C  C     . LYS A 1 258 ? 32.755  66.889  71.263  1.00 81.92  ? 285 LYS A C     1 
ATOM   1957 O  O     . LYS A 1 258 ? 31.789  67.557  70.876  1.00 93.28  ? 285 LYS A O     1 
ATOM   1958 C  CB    . LYS A 1 258 ? 34.060  65.793  69.408  1.00 89.41  ? 285 LYS A CB    1 
ATOM   1959 C  CG    . LYS A 1 258 ? 35.326  65.798  68.559  1.00 78.68  ? 285 LYS A CG    1 
ATOM   1960 C  CD    . LYS A 1 258 ? 35.303  64.736  67.482  1.00 74.74  ? 285 LYS A CD    1 
ATOM   1961 C  CE    . LYS A 1 258 ? 36.511  64.878  66.568  1.00 82.29  ? 285 LYS A CE    1 
ATOM   1962 N  NZ    . LYS A 1 258 ? 36.454  63.964  65.389  1.00 86.43  ? 285 LYS A NZ    1 
ATOM   1963 N  N     . GLU A 1 259 ? 32.715  66.163  72.377  1.00 85.82  ? 286 GLU A N     1 
ATOM   1964 C  CA    . GLU A 1 259 ? 31.558  66.202  73.258  1.00 99.58  ? 286 GLU A CA    1 
ATOM   1965 C  C     . GLU A 1 259 ? 32.004  65.942  74.690  1.00 89.41  ? 286 GLU A C     1 
ATOM   1966 O  O     . GLU A 1 259 ? 33.178  65.687  74.966  1.00 77.16  ? 286 GLU A O     1 
ATOM   1967 C  CB    . GLU A 1 259 ? 30.487  65.199  72.818  1.00 94.48  ? 286 GLU A CB    1 
ATOM   1968 C  CG    . GLU A 1 259 ? 31.038  63.943  72.189  1.00 97.03  ? 286 GLU A CG    1 
ATOM   1969 C  CD    . GLU A 1 259 ? 29.941  63.048  71.642  1.00 114.14 ? 286 GLU A CD    1 
ATOM   1970 O  OE1   . GLU A 1 259 ? 29.026  62.695  72.417  1.00 103.28 ? 286 GLU A OE1   1 
ATOM   1971 O  OE2   . GLU A 1 259 ? 29.993  62.704  70.439  1.00 111.45 ? 286 GLU A OE2   1 
ATOM   1972 N  N     . GLU A 1 260 ? 31.046  66.035  75.608  1.00 93.37  ? 287 GLU A N     1 
ATOM   1973 C  CA    . GLU A 1 260 ? 31.324  65.792  77.016  1.00 91.51  ? 287 GLU A CA    1 
ATOM   1974 C  C     . GLU A 1 260 ? 31.610  64.313  77.225  1.00 94.33  ? 287 GLU A C     1 
ATOM   1975 O  O     . GLU A 1 260 ? 30.794  63.459  76.863  1.00 93.41  ? 287 GLU A O     1 
ATOM   1976 C  CB    . GLU A 1 260 ? 30.142  66.242  77.871  1.00 100.09 ? 287 GLU A CB    1 
ATOM   1977 C  CG    . GLU A 1 260 ? 30.443  66.328  79.358  1.00 113.58 ? 287 GLU A CG    1 
ATOM   1978 C  CD    . GLU A 1 260 ? 29.256  66.821  80.161  1.00 130.62 ? 287 GLU A CD    1 
ATOM   1979 O  OE1   . GLU A 1 260 ? 28.212  66.133  80.160  1.00 136.52 ? 287 GLU A OE1   1 
ATOM   1980 O  OE2   . GLU A 1 260 ? 29.361  67.903  80.783  1.00 125.36 ? 287 GLU A OE2   1 
ATOM   1981 N  N     . TYR A 1 261 ? 32.775  64.005  77.797  1.00 97.98  ? 288 TYR A N     1 
ATOM   1982 C  CA    . TYR A 1 261 ? 33.160  62.624  78.064  1.00 82.55  ? 288 TYR A CA    1 
ATOM   1983 C  C     . TYR A 1 261 ? 33.026  62.277  79.542  1.00 81.88  ? 288 TYR A C     1 
ATOM   1984 O  O     . TYR A 1 261 ? 32.310  61.335  79.896  1.00 86.17  ? 288 TYR A O     1 
ATOM   1985 C  CB    . TYR A 1 261 ? 34.592  62.366  77.580  1.00 79.13  ? 288 TYR A CB    1 
ATOM   1986 C  CG    . TYR A 1 261 ? 34.771  62.595  76.099  1.00 74.82  ? 288 TYR A CG    1 
ATOM   1987 C  CD1   . TYR A 1 261 ? 34.185  61.745  75.169  1.00 73.84  ? 288 TYR A CD1   1 
ATOM   1988 C  CD2   . TYR A 1 261 ? 35.522  63.662  75.630  1.00 71.51  ? 288 TYR A CD2   1 
ATOM   1989 C  CE1   . TYR A 1 261 ? 34.342  61.956  73.809  1.00 78.88  ? 288 TYR A CE1   1 
ATOM   1990 C  CE2   . TYR A 1 261 ? 35.683  63.881  74.276  1.00 77.75  ? 288 TYR A CE2   1 
ATOM   1991 C  CZ    . TYR A 1 261 ? 35.092  63.026  73.370  1.00 79.93  ? 288 TYR A CZ    1 
ATOM   1992 O  OH    . TYR A 1 261 ? 35.256  63.244  72.024  1.00 86.16  ? 288 TYR A OH    1 
ATOM   1993 N  N     . GLY A 1 262 ? 33.690  63.027  80.411  1.00 80.51  ? 289 GLY A N     1 
ATOM   1994 C  CA    . GLY A 1 262 ? 33.640  62.712  81.822  1.00 73.91  ? 289 GLY A CA    1 
ATOM   1995 C  C     . GLY A 1 262 ? 34.218  63.825  82.664  1.00 83.08  ? 289 GLY A C     1 
ATOM   1996 O  O     . GLY A 1 262 ? 34.513  64.916  82.173  1.00 84.17  ? 289 GLY A O     1 
ATOM   1997 N  N     . PHE A 1 263 ? 34.385  63.529  83.951  1.00 83.47  ? 290 PHE A N     1 
ATOM   1998 C  CA    . PHE A 1 263 ? 34.756  64.535  84.931  1.00 79.92  ? 290 PHE A CA    1 
ATOM   1999 C  C     . PHE A 1 263 ? 35.924  64.043  85.773  1.00 77.79  ? 290 PHE A C     1 
ATOM   2000 O  O     . PHE A 1 263 ? 36.108  62.839  85.972  1.00 76.42  ? 290 PHE A O     1 
ATOM   2001 C  CB    . PHE A 1 263 ? 33.557  64.900  85.814  1.00 80.94  ? 290 PHE A CB    1 
ATOM   2002 C  CG    . PHE A 1 263 ? 32.450  65.590  85.064  1.00 87.06  ? 290 PHE A CG    1 
ATOM   2003 C  CD1   . PHE A 1 263 ? 31.574  64.866  84.266  1.00 82.65  ? 290 PHE A CD1   1 
ATOM   2004 C  CD2   . PHE A 1 263 ? 32.291  66.963  85.149  1.00 90.92  ? 290 PHE A CD2   1 
ATOM   2005 C  CE1   . PHE A 1 263 ? 30.565  65.497  83.568  1.00 83.59  ? 290 PHE A CE1   1 
ATOM   2006 C  CE2   . PHE A 1 263 ? 31.279  67.600  84.456  1.00 100.28 ? 290 PHE A CE2   1 
ATOM   2007 C  CZ    . PHE A 1 263 ? 30.415  66.865  83.665  1.00 103.32 ? 290 PHE A CZ    1 
ATOM   2008 N  N     . LEU A 1 264 ? 36.713  64.997  86.269  1.00 83.40  ? 291 LEU A N     1 
ATOM   2009 C  CA    . LEU A 1 264 ? 38.005  64.718  86.868  1.00 73.99  ? 291 LEU A CA    1 
ATOM   2010 C  C     . LEU A 1 264 ? 38.203  65.635  88.072  1.00 87.14  ? 291 LEU A C     1 
ATOM   2011 O  O     . LEU A 1 264 ? 37.920  66.845  87.980  1.00 97.61  ? 291 LEU A O     1 
ATOM   2012 C  CB    . LEU A 1 264 ? 39.099  64.950  85.821  1.00 72.63  ? 291 LEU A CB    1 
ATOM   2013 C  CG    . LEU A 1 264 ? 40.270  63.978  85.684  1.00 80.73  ? 291 LEU A CG    1 
ATOM   2014 C  CD1   . LEU A 1 264 ? 41.122  64.390  84.516  1.00 72.09  ? 291 LEU A CD1   1 
ATOM   2015 C  CD2   . LEU A 1 264 ? 41.101  63.956  86.954  1.00 115.09 ? 291 LEU A CD2   1 
ATOM   2016 N  N     . PRO A 1 265 ? 38.666  65.121  89.208  1.00 93.55  ? 292 PRO A N     1 
ATOM   2017 C  CA    . PRO A 1 265 ? 39.023  66.017  90.313  1.00 82.46  ? 292 PRO A CA    1 
ATOM   2018 C  C     . PRO A 1 265 ? 40.408  66.607  90.098  1.00 81.96  ? 292 PRO A C     1 
ATOM   2019 O  O     . PRO A 1 265 ? 41.314  65.950  89.580  1.00 84.93  ? 292 PRO A O     1 
ATOM   2020 C  CB    . PRO A 1 265 ? 38.985  65.098  91.541  1.00 70.38  ? 292 PRO A CB    1 
ATOM   2021 C  CG    . PRO A 1 265 ? 39.324  63.763  91.004  1.00 73.41  ? 292 PRO A CG    1 
ATOM   2022 C  CD    . PRO A 1 265 ? 38.767  63.705  89.596  1.00 89.26  ? 292 PRO A CD    1 
ATOM   2023 N  N     . VAL A 1 266 ? 40.558  67.867  90.480  1.00 75.71  ? 293 VAL A N     1 
ATOM   2024 C  CA    . VAL A 1 266 ? 41.862  68.526  90.352  1.00 80.48  ? 293 VAL A CA    1 
ATOM   2025 C  C     . VAL A 1 266 ? 42.819  67.937  91.384  1.00 75.63  ? 293 VAL A C     1 
ATOM   2026 O  O     . VAL A 1 266 ? 42.456  67.832  92.569  1.00 87.09  ? 293 VAL A O     1 
ATOM   2027 C  CB    . VAL A 1 266 ? 41.716  70.038  90.535  1.00 81.61  ? 293 VAL A CB    1 
ATOM   2028 C  CG1   . VAL A 1 266 ? 43.046  70.728  90.293  1.00 74.44  ? 293 VAL A CG1   1 
ATOM   2029 C  CG2   . VAL A 1 266 ? 40.643  70.590  89.603  1.00 82.98  ? 293 VAL A CG2   1 
ATOM   2030 N  N     . PRO A 1 267 ? 44.026  67.530  90.992  1.00 85.66  ? 294 PRO A N     1 
ATOM   2031 C  CA    . PRO A 1 267 ? 44.970  66.962  91.963  1.00 81.71  ? 294 PRO A CA    1 
ATOM   2032 C  C     . PRO A 1 267 ? 45.302  67.931  93.090  1.00 89.30  ? 294 PRO A C     1 
ATOM   2033 O  O     . PRO A 1 267 ? 45.194  69.152  92.957  1.00 86.91  ? 294 PRO A O     1 
ATOM   2034 C  CB    . PRO A 1 267 ? 46.207  66.653  91.110  1.00 73.70  ? 294 PRO A CB    1 
ATOM   2035 C  CG    . PRO A 1 267 ? 45.659  66.430  89.738  1.00 73.40  ? 294 PRO A CG    1 
ATOM   2036 C  CD    . PRO A 1 267 ? 44.515  67.402  89.608  1.00 79.15  ? 294 PRO A CD    1 
ATOM   2037 N  N     . LEU A 1 268 ? 45.715  67.361  94.217  1.00 76.13  ? 295 LEU A N     1 
ATOM   2038 C  CA    . LEU A 1 268 ? 46.000  68.108  95.433  1.00 87.50  ? 295 LEU A CA    1 
ATOM   2039 C  C     . LEU A 1 268 ? 47.500  68.129  95.708  1.00 97.84  ? 295 LEU A C     1 
ATOM   2040 O  O     . LEU A 1 268 ? 48.277  67.371  95.120  1.00 93.93  ? 295 LEU A O     1 
ATOM   2041 C  CB    . LEU A 1 268 ? 45.246  67.502  96.624  1.00 98.91  ? 295 LEU A CB    1 
ATOM   2042 C  CG    . LEU A 1 268 ? 43.717  67.558  96.600  1.00 90.09  ? 295 LEU A CG    1 
ATOM   2043 C  CD1   . LEU A 1 268 ? 43.137  66.570  97.595  1.00 93.96  ? 295 LEU A CD1   1 
ATOM   2044 C  CD2   . LEU A 1 268 ? 43.226  68.968  96.907  1.00 83.47  ? 295 LEU A CD2   1 
ATOM   2045 N  N     . ARG A 1 269 ? 47.899  69.014  96.624  1.00 91.34  ? 296 ARG A N     1 
ATOM   2046 C  CA    . ARG A 1 269 ? 49.299  69.151  96.995  1.00 85.22  ? 296 ARG A CA    1 
ATOM   2047 C  C     . ARG A 1 269 ? 49.801  67.886  97.695  1.00 91.48  ? 296 ARG A C     1 
ATOM   2048 O  O     . ARG A 1 269 ? 49.027  67.020  98.116  1.00 92.68  ? 296 ARG A O     1 
ATOM   2049 C  CB    . ARG A 1 269 ? 49.503  70.357  97.911  1.00 106.34 ? 296 ARG A CB    1 
ATOM   2050 C  CG    . ARG A 1 269 ? 49.479  71.716  97.230  1.00 105.85 ? 296 ARG A CG    1 
ATOM   2051 C  CD    . ARG A 1 269 ? 50.147  72.737  98.143  1.00 120.06 ? 296 ARG A CD    1 
ATOM   2052 N  NE    . ARG A 1 269 ? 49.425  74.002  98.216  1.00 128.88 ? 296 ARG A NE    1 
ATOM   2053 C  CZ    . ARG A 1 269 ? 49.550  74.876  99.207  1.00 144.46 ? 296 ARG A CZ    1 
ATOM   2054 N  NH1   . ARG A 1 269 ? 50.338  74.639  100.244 1.00 139.20 ? 296 ARG A NH1   1 
ATOM   2055 N  NH2   . ARG A 1 269 ? 48.861  76.014  99.160  1.00 141.69 ? 296 ARG A NH2   1 
ATOM   2056 N  N     . ALA A 1 270 ? 51.128  67.800  97.836  1.00 84.02  ? 297 ALA A N     1 
ATOM   2057 C  CA    . ALA A 1 270 ? 51.743  66.619  98.437  1.00 93.92  ? 297 ALA A CA    1 
ATOM   2058 C  C     . ALA A 1 270 ? 51.334  66.435  99.895  1.00 102.68 ? 297 ALA A C     1 
ATOM   2059 O  O     . ALA A 1 270 ? 51.326  65.306  100.402 1.00 92.61  ? 297 ALA A O     1 
ATOM   2060 C  CB    . ALA A 1 270 ? 53.266  66.710  98.323  1.00 82.14  ? 297 ALA A CB    1 
ATOM   2061 N  N     . HIS A 1 271 ? 50.994  67.521  100.588 1.00 85.59  ? 298 HIS A N     1 
ATOM   2062 C  CA    . HIS A 1 271 ? 50.638  67.445  101.997 1.00 104.08 ? 298 HIS A CA    1 
ATOM   2063 C  C     . HIS A 1 271 ? 49.142  67.615  102.230 1.00 101.71 ? 298 HIS A C     1 
ATOM   2064 O  O     . HIS A 1 271 ? 48.725  67.976  103.335 1.00 98.67  ? 298 HIS A O     1 
ATOM   2065 C  CB    . HIS A 1 271 ? 51.434  68.470  102.801 1.00 108.21 ? 298 HIS A CB    1 
ATOM   2066 C  CG    . HIS A 1 271 ? 52.900  68.175  102.856 1.00 104.63 ? 298 HIS A CG    1 
ATOM   2067 N  ND1   . HIS A 1 271 ? 53.775  68.881  103.653 1.00 109.14 ? 298 HIS A ND1   1 
ATOM   2068 C  CD2   . HIS A 1 271 ? 53.645  67.246  102.210 1.00 91.32  ? 298 HIS A CD2   1 
ATOM   2069 C  CE1   . HIS A 1 271 ? 54.996  68.401  103.494 1.00 112.99 ? 298 HIS A CE1   1 
ATOM   2070 N  NE2   . HIS A 1 271 ? 54.944  67.408  102.625 1.00 97.61  ? 298 HIS A NE2   1 
ATOM   2071 N  N     . SER A 1 272 ? 48.326  67.356  101.212 1.00 96.47  ? 299 SER A N     1 
ATOM   2072 C  CA    . SER A 1 272 ? 46.891  67.284  101.417 1.00 99.20  ? 299 SER A CA    1 
ATOM   2073 C  C     . SER A 1 272 ? 46.524  65.957  102.079 1.00 106.55 ? 299 SER A C     1 
ATOM   2074 O  O     . SER A 1 272 ? 47.345  65.043  102.210 1.00 113.14 ? 299 SER A O     1 
ATOM   2075 C  CB    . SER A 1 272 ? 46.147  67.453  100.094 1.00 105.84 ? 299 SER A CB    1 
ATOM   2076 O  OG    . SER A 1 272 ? 46.204  68.797  99.648  1.00 108.54 ? 299 SER A OG    1 
ATOM   2077 N  N     . THR A 1 273 ? 45.267  65.854  102.493 1.00 98.02  ? 300 THR A N     1 
ATOM   2078 C  CA    . THR A 1 273 ? 44.796  64.725  103.278 1.00 98.41  ? 300 THR A CA    1 
ATOM   2079 C  C     . THR A 1 273 ? 43.878  63.835  102.451 1.00 92.26  ? 300 THR A C     1 
ATOM   2080 O  O     . THR A 1 273 ? 43.406  64.207  101.373 1.00 90.43  ? 300 THR A O     1 
ATOM   2081 C  CB    . THR A 1 273 ? 44.059  65.210  104.527 1.00 88.48  ? 300 THR A CB    1 
ATOM   2082 O  OG1   . THR A 1 273 ? 42.745  65.640  104.155 1.00 92.06  ? 300 THR A OG1   1 
ATOM   2083 C  CG2   . THR A 1 273 ? 44.807  66.370  105.160 1.00 100.74 ? 300 THR A CG2   1 
ATOM   2084 N  N     . LEU A 1 274 ? 43.630  62.635  102.984 1.00 86.81  ? 301 LEU A N     1 
ATOM   2085 C  CA    . LEU A 1 274 ? 42.686  61.719  102.351 1.00 87.26  ? 301 LEU A CA    1 
ATOM   2086 C  C     . LEU A 1 274 ? 41.283  62.312  102.319 1.00 77.74  ? 301 LEU A C     1 
ATOM   2087 O  O     . LEU A 1 274 ? 40.569  62.178  101.318 1.00 92.68  ? 301 LEU A O     1 
ATOM   2088 C  CB    . LEU A 1 274 ? 42.680  60.376  103.083 1.00 71.84  ? 301 LEU A CB    1 
ATOM   2089 C  CG    . LEU A 1 274 ? 43.969  59.554  103.044 1.00 84.66  ? 301 LEU A CG    1 
ATOM   2090 C  CD1   . LEU A 1 274 ? 43.932  58.423  104.062 1.00 93.13  ? 301 LEU A CD1   1 
ATOM   2091 C  CD2   . LEU A 1 274 ? 44.190  59.004  101.651 1.00 72.09  ? 301 LEU A CD2   1 
ATOM   2092 N  N     . GLN A 1 275 ? 40.867  62.969  103.406 1.00 81.73  ? 302 GLN A N     1 
ATOM   2093 C  CA    . GLN A 1 275 ? 39.537  63.565  103.434 1.00 81.10  ? 302 GLN A CA    1 
ATOM   2094 C  C     . GLN A 1 275 ? 39.413  64.682  102.413 1.00 86.68  ? 302 GLN A C     1 
ATOM   2095 O  O     . GLN A 1 275 ? 38.328  64.896  101.859 1.00 92.27  ? 302 GLN A O     1 
ATOM   2096 C  CB    . GLN A 1 275 ? 39.211  64.089  104.830 1.00 80.59  ? 302 GLN A CB    1 
ATOM   2097 C  CG    . GLN A 1 275 ? 37.769  64.550  104.983 1.00 91.86  ? 302 GLN A CG    1 
ATOM   2098 C  CD    . GLN A 1 275 ? 37.533  65.327  106.265 1.00 106.82 ? 302 GLN A CD    1 
ATOM   2099 O  OE1   . GLN A 1 275 ? 38.476  65.752  106.934 1.00 111.20 ? 302 GLN A OE1   1 
ATOM   2100 N  NE2   . GLN A 1 275 ? 36.265  65.516  106.615 1.00 105.44 ? 302 GLN A NE2   1 
ATOM   2101 N  N     . ASP A 1 276 ? 40.505  65.403  102.153 1.00 88.87  ? 303 ASP A N     1 
ATOM   2102 C  CA    . ASP A 1 276 ? 40.503  66.371  101.062 1.00 92.84  ? 303 ASP A CA    1 
ATOM   2103 C  C     . ASP A 1 276 ? 40.174  65.693  99.740  1.00 88.93  ? 303 ASP A C     1 
ATOM   2104 O  O     . ASP A 1 276 ? 39.305  66.152  98.991  1.00 85.93  ? 303 ASP A O     1 
ATOM   2105 C  CB    . ASP A 1 276 ? 41.856  67.074  100.977 1.00 90.02  ? 303 ASP A CB    1 
ATOM   2106 C  CG    . ASP A 1 276 ? 42.082  68.024  102.121 1.00 98.69  ? 303 ASP A CG    1 
ATOM   2107 O  OD1   . ASP A 1 276 ? 41.080  68.536  102.667 1.00 94.49  ? 303 ASP A OD1   1 
ATOM   2108 O  OD2   . ASP A 1 276 ? 43.259  68.260  102.468 1.00 100.11 ? 303 ASP A OD2   1 
ATOM   2109 N  N     . GLU A 1 277 ? 40.861  64.587  99.442  1.00 80.93  ? 304 GLU A N     1 
ATOM   2110 C  CA    . GLU A 1 277 ? 40.589  63.856  98.211  1.00 88.04  ? 304 GLU A CA    1 
ATOM   2111 C  C     . GLU A 1 277 ? 39.158  63.337  98.184  1.00 84.02  ? 304 GLU A C     1 
ATOM   2112 O  O     . GLU A 1 277 ? 38.488  63.393  97.145  1.00 72.94  ? 304 GLU A O     1 
ATOM   2113 C  CB    . GLU A 1 277 ? 41.578  62.701  98.059  1.00 92.32  ? 304 GLU A CB    1 
ATOM   2114 C  CG    . GLU A 1 277 ? 41.487  61.985  96.722  1.00 77.35  ? 304 GLU A CG    1 
ATOM   2115 C  CD    . GLU A 1 277 ? 42.057  62.806  95.590  1.00 93.99  ? 304 GLU A CD    1 
ATOM   2116 O  OE1   . GLU A 1 277 ? 43.118  63.429  95.795  1.00 88.25  ? 304 GLU A OE1   1 
ATOM   2117 O  OE2   . GLU A 1 277 ? 41.445  62.832  94.500  1.00 109.67 ? 304 GLU A OE2   1 
ATOM   2118 N  N     . ALA A 1 278 ? 38.671  62.828  99.318  1.00 74.68  ? 305 ALA A N     1 
ATOM   2119 C  CA    . ALA A 1 278 ? 37.312  62.298  99.359  1.00 86.04  ? 305 ALA A CA    1 
ATOM   2120 C  C     . ALA A 1 278 ? 36.288  63.396  99.112  1.00 91.53  ? 305 ALA A C     1 
ATOM   2121 O  O     . ALA A 1 278 ? 35.335  63.207  98.346  1.00 91.04  ? 305 ALA A O     1 
ATOM   2122 C  CB    . ALA A 1 278 ? 37.051  61.617  100.700 1.00 72.49  ? 305 ALA A CB    1 
ATOM   2123 N  N     . GLU A 1 279 ? 36.474  64.557  99.741  1.00 80.87  ? 306 GLU A N     1 
ATOM   2124 C  CA    . GLU A 1 279 ? 35.526  65.648  99.562  1.00 83.99  ? 306 GLU A CA    1 
ATOM   2125 C  C     . GLU A 1 279 ? 35.713  66.348  98.222  1.00 84.04  ? 306 GLU A C     1 
ATOM   2126 O  O     . GLU A 1 279 ? 34.747  66.889  97.671  1.00 93.76  ? 306 GLU A O     1 
ATOM   2127 C  CB    . GLU A 1 279 ? 35.649  66.637  100.723 1.00 90.65  ? 306 GLU A CB    1 
ATOM   2128 C  CG    . GLU A 1 279 ? 35.260  66.030  102.070 1.00 96.49  ? 306 GLU A CG    1 
ATOM   2129 C  CD    . GLU A 1 279 ? 35.319  67.025  103.215 1.00 101.11 ? 306 GLU A CD    1 
ATOM   2130 O  OE1   . GLU A 1 279 ? 35.765  68.170  102.992 1.00 83.82  ? 306 GLU A OE1   1 
ATOM   2131 O  OE2   . GLU A 1 279 ? 34.914  66.658  104.339 1.00 99.91  ? 306 GLU A OE2   1 
ATOM   2132 N  N     . SER A 1 280 ? 36.932  66.334  97.676  1.00 86.95  ? 307 SER A N     1 
ATOM   2133 C  CA    . SER A 1 280 ? 37.155  66.911  96.354  1.00 74.93  ? 307 SER A CA    1 
ATOM   2134 C  C     . SER A 1 280 ? 36.430  66.117  95.274  1.00 82.21  ? 307 SER A C     1 
ATOM   2135 O  O     . SER A 1 280 ? 35.882  66.703  94.333  1.00 88.94  ? 307 SER A O     1 
ATOM   2136 C  CB    . SER A 1 280 ? 38.654  66.986  96.056  1.00 68.31  ? 307 SER A CB    1 
ATOM   2137 O  OG    . SER A 1 280 ? 38.894  67.368  94.713  1.00 83.12  ? 307 SER A OG    1 
ATOM   2138 N  N     . PHE A 1 281 ? 36.408  64.784  95.390  1.00 93.32  ? 308 PHE A N     1 
ATOM   2139 C  CA    . PHE A 1 281 ? 35.666  63.980  94.420  1.00 94.61  ? 308 PHE A CA    1 
ATOM   2140 C  C     . PHE A 1 281 ? 34.162  64.112  94.614  1.00 91.73  ? 308 PHE A C     1 
ATOM   2141 O  O     . PHE A 1 281 ? 33.404  64.013  93.642  1.00 89.19  ? 308 PHE A O     1 
ATOM   2142 C  CB    . PHE A 1 281 ? 36.073  62.508  94.502  1.00 86.32  ? 308 PHE A CB    1 
ATOM   2143 C  CG    . PHE A 1 281 ? 35.321  61.622  93.545  1.00 86.35  ? 308 PHE A CG    1 
ATOM   2144 C  CD1   . PHE A 1 281 ? 35.736  61.492  92.227  1.00 88.38  ? 308 PHE A CD1   1 
ATOM   2145 C  CD2   . PHE A 1 281 ? 34.191  60.931  93.957  1.00 77.14  ? 308 PHE A CD2   1 
ATOM   2146 C  CE1   . PHE A 1 281 ? 35.043  60.683  91.339  1.00 74.13  ? 308 PHE A CE1   1 
ATOM   2147 C  CE2   . PHE A 1 281 ? 33.494  60.122  93.075  1.00 85.57  ? 308 PHE A CE2   1 
ATOM   2148 C  CZ    . PHE A 1 281 ? 33.921  59.996  91.767  1.00 72.76  ? 308 PHE A CZ    1 
ATOM   2149 N  N     . MET A 1 282 ? 33.711  64.313  95.854  1.00 96.29  ? 309 MET A N     1 
ATOM   2150 C  CA    . MET A 1 282 ? 32.298  64.593  96.082  1.00 90.35  ? 309 MET A CA    1 
ATOM   2151 C  C     . MET A 1 282 ? 31.863  65.842  95.327  1.00 91.66  ? 309 MET A C     1 
ATOM   2152 O  O     . MET A 1 282 ? 30.759  65.893  94.772  1.00 84.12  ? 309 MET A O     1 
ATOM   2153 C  CB    . MET A 1 282 ? 32.032  64.751  97.577  1.00 70.68  ? 309 MET A CB    1 
ATOM   2154 C  CG    . MET A 1 282 ? 30.616  65.182  97.905  1.00 82.83  ? 309 MET A CG    1 
ATOM   2155 S  SD    . MET A 1 282 ? 30.578  66.376  99.254  1.00 109.61 ? 309 MET A SD    1 
ATOM   2156 C  CE    . MET A 1 282 ? 31.584  67.692  98.561  1.00 97.10  ? 309 MET A CE    1 
ATOM   2157 N  N     . HIS A 1 283 ? 32.727  66.859  95.285  1.00 86.09  ? 310 HIS A N     1 
ATOM   2158 C  CA    . HIS A 1 283 ? 32.408  68.064  94.533  1.00 85.99  ? 310 HIS A CA    1 
ATOM   2159 C  C     . HIS A 1 283 ? 32.271  67.774  93.044  1.00 91.07  ? 310 HIS A C     1 
ATOM   2160 O  O     . HIS A 1 283 ? 31.508  68.452  92.347  1.00 91.53  ? 310 HIS A O     1 
ATOM   2161 C  CB    . HIS A 1 283 ? 33.475  69.129  94.778  1.00 82.60  ? 310 HIS A CB    1 
ATOM   2162 C  CG    . HIS A 1 283 ? 33.196  70.424  94.086  1.00 79.23  ? 310 HIS A CG    1 
ATOM   2163 N  ND1   . HIS A 1 283 ? 33.810  70.784  92.906  1.00 86.73  ? 310 HIS A ND1   1 
ATOM   2164 C  CD2   . HIS A 1 283 ? 32.357  71.438  94.400  1.00 82.06  ? 310 HIS A CD2   1 
ATOM   2165 C  CE1   . HIS A 1 283 ? 33.365  71.969  92.525  1.00 101.01 ? 310 HIS A CE1   1 
ATOM   2166 N  NE2   . HIS A 1 283 ? 32.481  72.387  93.413  1.00 103.35 ? 310 HIS A NE2   1 
ATOM   2167 N  N     . VAL A 1 284 ? 33.000  66.777  92.537  1.00 86.08  ? 311 VAL A N     1 
ATOM   2168 C  CA    . VAL A 1 284 ? 32.803  66.350  91.155  1.00 92.12  ? 311 VAL A CA    1 
ATOM   2169 C  C     . VAL A 1 284 ? 31.391  65.805  90.967  1.00 89.59  ? 311 VAL A C     1 
ATOM   2170 O  O     . VAL A 1 284 ? 30.732  66.086  89.959  1.00 81.73  ? 311 VAL A O     1 
ATOM   2171 C  CB    . VAL A 1 284 ? 33.872  65.315  90.753  1.00 86.10  ? 311 VAL A CB    1 
ATOM   2172 C  CG1   . VAL A 1 284 ? 33.555  64.736  89.393  1.00 70.63  ? 311 VAL A CG1   1 
ATOM   2173 C  CG2   . VAL A 1 284 ? 35.254  65.947  90.745  1.00 91.78  ? 311 VAL A CG2   1 
ATOM   2174 N  N     . GLN A 1 285 ? 30.900  65.027  91.937  1.00 87.27  ? 312 GLN A N     1 
ATOM   2175 C  CA    . GLN A 1 285 ? 29.531  64.525  91.856  1.00 81.97  ? 312 GLN A CA    1 
ATOM   2176 C  C     . GLN A 1 285 ? 28.522  65.663  91.926  1.00 86.92  ? 312 GLN A C     1 
ATOM   2177 O  O     . GLN A 1 285 ? 27.499  65.639  91.232  1.00 87.92  ? 312 GLN A O     1 
ATOM   2178 C  CB    . GLN A 1 285 ? 29.265  63.520  92.974  1.00 79.46  ? 312 GLN A CB    1 
ATOM   2179 C  CG    . GLN A 1 285 ? 30.262  62.388  93.053  1.00 92.52  ? 312 GLN A CG    1 
ATOM   2180 C  CD    . GLN A 1 285 ? 29.867  61.358  94.086  1.00 85.32  ? 312 GLN A CD    1 
ATOM   2181 O  OE1   . GLN A 1 285 ? 30.526  61.207  95.114  1.00 85.48  ? 312 GLN A OE1   1 
ATOM   2182 N  NE2   . GLN A 1 285 ? 28.784  60.639  93.816  1.00 83.22  ? 312 GLN A NE2   1 
ATOM   2183 N  N     . LEU A 1 286 ? 28.787  66.663  92.772  1.00 88.68  ? 313 LEU A N     1 
ATOM   2184 C  CA    . LEU A 1 286 ? 27.917  67.833  92.832  1.00 82.95  ? 313 LEU A CA    1 
ATOM   2185 C  C     . LEU A 1 286 ? 27.912  68.577  91.503  1.00 89.14  ? 313 LEU A C     1 
ATOM   2186 O  O     . LEU A 1 286 ? 26.851  68.976  91.010  1.00 103.08 ? 313 LEU A O     1 
ATOM   2187 C  CB    . LEU A 1 286 ? 28.363  68.762  93.962  1.00 80.92  ? 313 LEU A CB    1 
ATOM   2188 C  CG    . LEU A 1 286 ? 28.399  68.208  95.386  1.00 74.31  ? 313 LEU A CG    1 
ATOM   2189 C  CD1   . LEU A 1 286 ? 28.923  69.266  96.351  1.00 81.50  ? 313 LEU A CD1   1 
ATOM   2190 C  CD2   . LEU A 1 286 ? 27.027  67.735  95.813  1.00 75.99  ? 313 LEU A CD2   1 
ATOM   2191 N  N     . GLU A 1 287 ? 29.093  68.769  90.908  1.00 88.49  ? 314 GLU A N     1 
ATOM   2192 C  CA    . GLU A 1 287 ? 29.183  69.455  89.623  1.00 88.77  ? 314 GLU A CA    1 
ATOM   2193 C  C     . GLU A 1 287 ? 28.430  68.702  88.534  1.00 88.97  ? 314 GLU A C     1 
ATOM   2194 O  O     . GLU A 1 287 ? 27.828  69.317  87.646  1.00 96.93  ? 314 GLU A O     1 
ATOM   2195 C  CB    . GLU A 1 287 ? 30.648  69.638  89.230  1.00 87.13  ? 314 GLU A CB    1 
ATOM   2196 C  CG    . GLU A 1 287 ? 31.362  70.767  89.953  1.00 78.82  ? 314 GLU A CG    1 
ATOM   2197 C  CD    . GLU A 1 287 ? 30.842  72.137  89.554  1.00 103.14 ? 314 GLU A CD    1 
ATOM   2198 O  OE1   . GLU A 1 287 ? 29.760  72.532  90.041  1.00 103.26 ? 314 GLU A OE1   1 
ATOM   2199 O  OE2   . GLU A 1 287 ? 31.511  72.816  88.744  1.00 100.58 ? 314 GLU A OE2   1 
ATOM   2200 N  N     . VAL A 1 288 ? 28.463  67.368  88.577  1.00 92.69  ? 315 VAL A N     1 
ATOM   2201 C  CA    . VAL A 1 288 ? 27.703  66.575  87.614  1.00 96.55  ? 315 VAL A CA    1 
ATOM   2202 C  C     . VAL A 1 288 ? 26.211  66.847  87.761  1.00 101.64 ? 315 VAL A C     1 
ATOM   2203 O  O     . VAL A 1 288 ? 25.494  67.011  86.766  1.00 102.45 ? 315 VAL A O     1 
ATOM   2204 C  CB    . VAL A 1 288 ? 28.030  65.078  87.779  1.00 90.30  ? 315 VAL A CB    1 
ATOM   2205 C  CG1   . VAL A 1 288 ? 26.861  64.215  87.323  1.00 99.15  ? 315 VAL A CG1   1 
ATOM   2206 C  CG2   . VAL A 1 288 ? 29.283  64.722  86.996  1.00 86.12  ? 315 VAL A CG2   1 
ATOM   2207 N  N     . MET A 1 289 ? 25.725  66.926  89.001  1.00 93.59  ? 316 MET A N     1 
ATOM   2208 C  CA    . MET A 1 289 ? 24.297  67.084  89.251  1.00 96.83  ? 316 MET A CA    1 
ATOM   2209 C  C     . MET A 1 289 ? 23.781  68.482  88.947  1.00 102.74 ? 316 MET A C     1 
ATOM   2210 O  O     . MET A 1 289 ? 22.597  68.744  89.185  1.00 103.57 ? 316 MET A O     1 
ATOM   2211 C  CB    . MET A 1 289 ? 23.978  66.718  90.698  1.00 81.58  ? 316 MET A CB    1 
ATOM   2212 C  CG    . MET A 1 289 ? 24.115  65.237  90.977  1.00 92.61  ? 316 MET A CG    1 
ATOM   2213 S  SD    . MET A 1 289 ? 23.737  64.836  92.684  1.00 109.97 ? 316 MET A SD    1 
ATOM   2214 C  CE    . MET A 1 289 ? 24.804  65.996  93.530  1.00 88.99  ? 316 MET A CE    1 
ATOM   2215 N  N     . VAL A 1 290 ? 24.619  69.382  88.434  1.00 98.60  ? 317 VAL A N     1 
ATOM   2216 C  CA    . VAL A 1 290 ? 24.133  70.695  88.025  1.00 96.88  ? 317 VAL A CA    1 
ATOM   2217 C  C     . VAL A 1 290 ? 23.326  70.581  86.736  1.00 104.36 ? 317 VAL A C     1 
ATOM   2218 O  O     . VAL A 1 290 ? 22.139  70.921  86.694  1.00 115.30 ? 317 VAL A O     1 
ATOM   2219 C  CB    . VAL A 1 290 ? 25.304  71.681  87.871  1.00 99.94  ? 317 VAL A CB    1 
ATOM   2220 C  CG1   . VAL A 1 290 ? 24.806  73.018  87.345  1.00 90.13  ? 317 VAL A CG1   1 
ATOM   2221 C  CG2   . VAL A 1 290 ? 26.024  71.856  89.198  1.00 85.13  ? 317 VAL A CG2   1 
ATOM   2222 N  N     . LYS A 1 291 ? 23.958  70.090  85.670  1.00 106.70 ? 318 LYS A N     1 
ATOM   2223 C  CA    . LYS A 1 291 ? 23.317  69.981  84.366  1.00 98.36  ? 318 LYS A CA    1 
ATOM   2224 C  C     . LYS A 1 291 ? 23.038  68.544  83.947  1.00 102.74 ? 318 LYS A C     1 
ATOM   2225 O  O     . LYS A 1 291 ? 22.534  68.327  82.840  1.00 121.13 ? 318 LYS A O     1 
ATOM   2226 C  CB    . LYS A 1 291 ? 24.173  70.667  83.295  1.00 102.37 ? 318 LYS A CB    1 
ATOM   2227 C  CG    . LYS A 1 291 ? 24.324  72.167  83.480  1.00 115.53 ? 318 LYS A CG    1 
ATOM   2228 C  CD    . LYS A 1 291 ? 25.173  72.773  82.371  1.00 129.57 ? 318 LYS A CD    1 
ATOM   2229 C  CE    . LYS A 1 291 ? 25.276  74.285  82.512  1.00 145.83 ? 318 LYS A CE    1 
ATOM   2230 N  NZ    . LYS A 1 291 ? 23.944  74.953  82.441  1.00 149.08 ? 318 LYS A NZ    1 
ATOM   2231 N  N     . HIS A 1 292 ? 23.342  67.565  84.785  1.00 101.72 ? 319 HIS A N     1 
ATOM   2232 C  CA    . HIS A 1 292 ? 23.130  66.162  84.472  1.00 96.58  ? 319 HIS A CA    1 
ATOM   2233 C  C     . HIS A 1 292 ? 22.437  65.475  85.638  1.00 102.28 ? 319 HIS A C     1 
ATOM   2234 O  O     . HIS A 1 292 ? 22.507  65.946  86.779  1.00 93.80  ? 319 HIS A O     1 
ATOM   2235 C  CB    . HIS A 1 292 ? 24.459  65.453  84.167  1.00 88.74  ? 319 HIS A CB    1 
ATOM   2236 C  CG    . HIS A 1 292 ? 25.344  66.202  83.218  1.00 102.82 ? 319 HIS A CG    1 
ATOM   2237 N  ND1   . HIS A 1 292 ? 26.306  67.094  83.643  1.00 111.13 ? 319 HIS A ND1   1 
ATOM   2238 C  CD2   . HIS A 1 292 ? 25.413  66.192  81.865  1.00 112.48 ? 319 HIS A CD2   1 
ATOM   2239 C  CE1   . HIS A 1 292 ? 26.929  67.601  82.594  1.00 106.72 ? 319 HIS A CE1   1 
ATOM   2240 N  NE2   . HIS A 1 292 ? 26.406  67.071  81.503  1.00 116.05 ? 319 HIS A NE2   1 
ATOM   2241 N  N     . PRO A 1 293 ? 21.746  64.366  85.384  1.00 98.61  ? 320 PRO A N     1 
ATOM   2242 C  CA    . PRO A 1 293 ? 21.206  63.558  86.483  1.00 89.14  ? 320 PRO A CA    1 
ATOM   2243 C  C     . PRO A 1 293 ? 22.329  63.022  87.351  1.00 99.48  ? 320 PRO A C     1 
ATOM   2244 O  O     . PRO A 1 293 ? 23.498  63.026  86.935  1.00 103.69 ? 320 PRO A O     1 
ATOM   2245 C  CB    . PRO A 1 293 ? 20.468  62.422  85.755  1.00 92.82  ? 320 PRO A CB    1 
ATOM   2246 C  CG    . PRO A 1 293 ? 20.157  62.975  84.412  1.00 92.02  ? 320 PRO A CG    1 
ATOM   2247 C  CD    . PRO A 1 293 ? 21.318  63.861  84.069  1.00 90.19  ? 320 PRO A CD    1 
ATOM   2248 N  N     . PRO A 1 294 ? 22.024  62.556  88.562  1.00 99.62  ? 321 PRO A N     1 
ATOM   2249 C  CA    . PRO A 1 294 ? 23.091  62.073  89.447  1.00 104.24 ? 321 PRO A CA    1 
ATOM   2250 C  C     . PRO A 1 294 ? 23.799  60.858  88.865  1.00 98.34  ? 321 PRO A C     1 
ATOM   2251 O  O     . PRO A 1 294 ? 23.182  59.997  88.232  1.00 101.96 ? 321 PRO A O     1 
ATOM   2252 C  CB    . PRO A 1 294 ? 22.349  61.730  90.744  1.00 103.31 ? 321 PRO A CB    1 
ATOM   2253 C  CG    . PRO A 1 294 ? 20.929  61.521  90.328  1.00 111.97 ? 321 PRO A CG    1 
ATOM   2254 C  CD    . PRO A 1 294 ? 20.699  62.478  89.201  1.00 106.87 ? 321 PRO A CD    1 
ATOM   2255 N  N     . ALA A 1 295 ? 25.113  60.803  89.076  1.00 95.35  ? 322 ALA A N     1 
ATOM   2256 C  CA    . ALA A 1 295 ? 25.927  59.677  88.629  1.00 78.92  ? 322 ALA A CA    1 
ATOM   2257 C  C     . ALA A 1 295 ? 25.731  58.514  89.594  1.00 96.62  ? 322 ALA A C     1 
ATOM   2258 O  O     . ALA A 1 295 ? 26.189  58.562  90.741  1.00 93.14  ? 322 ALA A O     1 
ATOM   2259 C  CB    . ALA A 1 295 ? 27.396  60.079  88.539  1.00 76.76  ? 322 ALA A CB    1 
ATOM   2260 N  N     . GLU A 1 296 ? 25.050  57.470  89.134  1.00 90.26  ? 323 GLU A N     1 
ATOM   2261 C  CA    . GLU A 1 296 ? 24.749  56.343  89.997  1.00 95.63  ? 323 GLU A CA    1 
ATOM   2262 C  C     . GLU A 1 296 ? 25.987  55.476  90.208  1.00 102.26 ? 323 GLU A C     1 
ATOM   2263 O  O     . GLU A 1 296 ? 26.834  55.361  89.318  1.00 94.12  ? 323 GLU A O     1 
ATOM   2264 C  CB    . GLU A 1 296 ? 23.634  55.494  89.396  1.00 101.94 ? 323 GLU A CB    1 
ATOM   2265 C  CG    . GLU A 1 296 ? 22.444  56.289  88.897  1.00 110.72 ? 323 GLU A CG    1 
ATOM   2266 C  CD    . GLU A 1 296 ? 21.730  57.034  90.006  1.00 126.49 ? 323 GLU A CD    1 
ATOM   2267 O  OE1   . GLU A 1 296 ? 21.814  56.593  91.173  1.00 129.80 ? 323 GLU A OE1   1 
ATOM   2268 O  OE2   . GLU A 1 296 ? 21.084  58.062  89.709  1.00 132.32 ? 323 GLU A OE2   1 
ATOM   2269 N  N     . PRO A 1 297 ? 26.115  54.862  91.379  1.00 100.54 ? 324 PRO A N     1 
ATOM   2270 C  CA    . PRO A 1 297 ? 27.194  53.900  91.602  1.00 87.32  ? 324 PRO A CA    1 
ATOM   2271 C  C     . PRO A 1 297 ? 26.843  52.545  91.002  1.00 92.34  ? 324 PRO A C     1 
ATOM   2272 O  O     . PRO A 1 297 ? 25.717  52.295  90.570  1.00 100.40 ? 324 PRO A O     1 
ATOM   2273 C  CB    . PRO A 1 297 ? 27.280  53.824  93.127  1.00 92.49  ? 324 PRO A CB    1 
ATOM   2274 C  CG    . PRO A 1 297 ? 25.878  54.063  93.565  1.00 85.43  ? 324 PRO A CG    1 
ATOM   2275 C  CD    . PRO A 1 297 ? 25.296  55.058  92.587  1.00 90.34  ? 324 PRO A CD    1 
ATOM   2276 N  N     . SER A 1 298 ? 27.841  51.665  90.982  1.00 92.62  ? 325 SER A N     1 
ATOM   2277 C  CA    . SER A 1 298 ? 27.638  50.317  90.468  1.00 101.67 ? 325 SER A CA    1 
ATOM   2278 C  C     . SER A 1 298 ? 26.565  49.593  91.270  1.00 101.48 ? 325 SER A C     1 
ATOM   2279 O  O     . SER A 1 298 ? 26.513  49.690  92.498  1.00 99.94  ? 325 SER A O     1 
ATOM   2280 C  CB    . SER A 1 298 ? 28.945  49.526  90.518  1.00 103.66 ? 325 SER A CB    1 
ATOM   2281 O  OG    . SER A 1 298 ? 28.717  48.153  90.245  1.00 92.05  ? 325 SER A OG    1 
ATOM   2282 N  N     . ARG A 1 299 ? 25.710  48.856  90.566  1.00 106.49 ? 326 ARG A N     1 
ATOM   2283 C  CA    . ARG A 1 299 ? 24.670  48.092  91.248  1.00 110.50 ? 326 ARG A CA    1 
ATOM   2284 C  C     . ARG A 1 299 ? 25.212  46.855  91.946  1.00 111.44 ? 326 ARG A C     1 
ATOM   2285 O  O     . ARG A 1 299 ? 24.427  46.053  92.473  1.00 117.23 ? 326 ARG A O     1 
ATOM   2286 C  CB    . ARG A 1 299 ? 23.572  47.696  90.257  1.00 116.37 ? 326 ARG A CB    1 
ATOM   2287 C  CG    . ARG A 1 299 ? 24.009  46.712  89.190  1.00 114.50 ? 326 ARG A CG    1 
ATOM   2288 C  CD    . ARG A 1 299 ? 22.865  46.402  88.238  1.00 120.33 ? 326 ARG A CD    1 
ATOM   2289 N  NE    . ARG A 1 299 ? 23.066  45.143  87.532  1.00 127.44 ? 326 ARG A NE    1 
ATOM   2290 C  CZ    . ARG A 1 299 ? 22.702  43.958  88.003  1.00 133.96 ? 326 ARG A CZ    1 
ATOM   2291 N  NH1   . ARG A 1 299 ? 22.122  43.833  89.186  1.00 133.00 ? 326 ARG A NH1   1 
ATOM   2292 N  NH2   . ARG A 1 299 ? 22.929  42.870  87.272  1.00 138.73 ? 326 ARG A NH2   1 
ATOM   2293 N  N     . PHE A 1 300 ? 26.536  46.692  91.956  1.00 110.57 ? 327 PHE A N     1 
ATOM   2294 C  CA    . PHE A 1 300 ? 27.195  45.600  92.656  1.00 100.85 ? 327 PHE A CA    1 
ATOM   2295 C  C     . PHE A 1 300 ? 28.018  46.075  93.845  1.00 106.93 ? 327 PHE A C     1 
ATOM   2296 O  O     . PHE A 1 300 ? 28.574  45.243  94.569  1.00 108.17 ? 327 PHE A O     1 
ATOM   2297 C  CB    . PHE A 1 300 ? 28.094  44.816  91.693  1.00 97.18  ? 327 PHE A CB    1 
ATOM   2298 C  CG    . PHE A 1 300 ? 27.400  44.374  90.433  1.00 110.96 ? 327 PHE A CG    1 
ATOM   2299 C  CD1   . PHE A 1 300 ? 26.375  43.441  90.478  1.00 108.18 ? 327 PHE A CD1   1 
ATOM   2300 C  CD2   . PHE A 1 300 ? 27.783  44.882  89.200  1.00 110.21 ? 327 PHE A CD2   1 
ATOM   2301 C  CE1   . PHE A 1 300 ? 25.739  43.030  89.320  1.00 105.71 ? 327 PHE A CE1   1 
ATOM   2302 C  CE2   . PHE A 1 300 ? 27.151  44.473  88.037  1.00 107.68 ? 327 PHE A CE2   1 
ATOM   2303 C  CZ    . PHE A 1 300 ? 26.128  43.545  88.098  1.00 108.89 ? 327 PHE A CZ    1 
ATOM   2304 N  N     . ILE A 1 301 ? 28.120  47.383  94.063  1.00 103.16 ? 328 ILE A N     1 
ATOM   2305 C  CA    . ILE A 1 301 ? 28.855  47.947  95.187  1.00 100.71 ? 328 ILE A CA    1 
ATOM   2306 C  C     . ILE A 1 301 ? 27.888  48.767  96.024  1.00 122.20 ? 328 ILE A C     1 
ATOM   2307 O  O     . ILE A 1 301 ? 27.174  49.626  95.494  1.00 130.07 ? 328 ILE A O     1 
ATOM   2308 C  CB    . ILE A 1 301 ? 30.033  48.822  94.723  1.00 107.53 ? 328 ILE A CB    1 
ATOM   2309 C  CG1   . ILE A 1 301 ? 30.927  48.056  93.756  1.00 104.95 ? 328 ILE A CG1   1 
ATOM   2310 C  CG2   . ILE A 1 301 ? 30.846  49.292  95.917  1.00 111.86 ? 328 ILE A CG2   1 
ATOM   2311 C  CD1   . ILE A 1 301 ? 32.072  48.883  93.244  1.00 107.00 ? 328 ILE A CD1   1 
ATOM   2312 N  N     . SER A 1 302 ? 27.873  48.510  97.327  1.00 127.78 ? 329 SER A N     1 
ATOM   2313 C  CA    . SER A 1 302 ? 27.059  49.290  98.247  1.00 128.71 ? 329 SER A CA    1 
ATOM   2314 C  C     . SER A 1 302 ? 27.822  50.545  98.649  1.00 135.18 ? 329 SER A C     1 
ATOM   2315 O  O     . SER A 1 302 ? 28.883  50.457  99.276  1.00 135.14 ? 329 SER A O     1 
ATOM   2316 C  CB    . SER A 1 302 ? 26.697  48.454  99.472  1.00 141.29 ? 329 SER A CB    1 
ATOM   2317 O  OG    . SER A 1 302 ? 27.845  47.813  100.002 1.00 136.43 ? 329 SER A OG    1 
ATOM   2318 N  N     . ALA A 1 303 ? 27.295  51.706  98.272  1.00 154.93 ? 330 ALA A N     1 
ATOM   2319 C  CA    . ALA A 1 303 ? 27.910  52.960  98.677  1.00 155.95 ? 330 ALA A CA    1 
ATOM   2320 C  C     . ALA A 1 303 ? 27.752  53.148  100.184 1.00 153.07 ? 330 ALA A C     1 
ATOM   2321 O  O     . ALA A 1 303 ? 26.710  52.798  100.748 1.00 147.89 ? 330 ALA A O     1 
ATOM   2322 C  CB    . ALA A 1 303 ? 27.283  54.137  97.929  1.00 146.98 ? 330 ALA A CB    1 
ATOM   2323 N  N     . PRO A 1 304 ? 28.761  53.688  100.863 1.00 143.52 ? 331 PRO A N     1 
ATOM   2324 C  CA    . PRO A 1 304 ? 28.688  53.788  102.324 1.00 142.70 ? 331 PRO A CA    1 
ATOM   2325 C  C     . PRO A 1 304 ? 27.644  54.801  102.762 1.00 142.19 ? 331 PRO A C     1 
ATOM   2326 O  O     . PRO A 1 304 ? 27.370  55.789  102.075 1.00 141.89 ? 331 PRO A O     1 
ATOM   2327 C  CB    . PRO A 1 304 ? 30.100  54.236  102.719 1.00 137.72 ? 331 PRO A CB    1 
ATOM   2328 C  CG    . PRO A 1 304 ? 30.581  54.997  101.528 1.00 145.73 ? 331 PRO A CG    1 
ATOM   2329 C  CD    . PRO A 1 304 ? 29.988  54.305  100.326 1.00 135.76 ? 331 PRO A CD    1 
ATOM   2330 N  N     . THR A 1 305 ? 27.054  54.539  103.923 1.00 133.78 ? 332 THR A N     1 
ATOM   2331 C  CA    . THR A 1 305 ? 26.034  55.430  104.450 1.00 143.12 ? 332 THR A CA    1 
ATOM   2332 C  C     . THR A 1 305 ? 26.663  56.740  104.911 1.00 137.67 ? 332 THR A C     1 
ATOM   2333 O  O     . THR A 1 305 ? 27.841  56.797  105.276 1.00 127.24 ? 332 THR A O     1 
ATOM   2334 C  CB    . THR A 1 305 ? 25.288  54.765  105.606 1.00 135.02 ? 332 THR A CB    1 
ATOM   2335 O  OG1   . THR A 1 305 ? 25.135  53.367  105.331 1.00 147.18 ? 332 THR A OG1   1 
ATOM   2336 C  CG2   . THR A 1 305 ? 23.909  55.384  105.776 1.00 121.51 ? 332 THR A CG2   1 
ATOM   2337 N  N     . LYS A 1 306 ? 25.864  57.803  104.880 1.00 128.94 ? 333 LYS A N     1 
ATOM   2338 C  CA    . LYS A 1 306 ? 26.306  59.130  105.277 1.00 125.54 ? 333 LYS A CA    1 
ATOM   2339 C  C     . LYS A 1 306 ? 25.448  59.627  106.432 1.00 122.43 ? 333 LYS A C     1 
ATOM   2340 O  O     . LYS A 1 306 ? 24.222  59.477  106.415 1.00 119.08 ? 333 LYS A O     1 
ATOM   2341 C  CB    . LYS A 1 306 ? 26.229  60.108  104.100 1.00 119.08 ? 333 LYS A CB    1 
ATOM   2342 C  CG    . LYS A 1 306 ? 26.405  59.453  102.742 1.00 113.08 ? 333 LYS A CG    1 
ATOM   2343 C  CD    . LYS A 1 306 ? 26.901  60.445  101.703 1.00 113.22 ? 333 LYS A CD    1 
ATOM   2344 C  CE    . LYS A 1 306 ? 28.340  60.853  101.980 1.00 116.07 ? 333 LYS A CE    1 
ATOM   2345 N  NZ    . LYS A 1 306 ? 28.910  61.681  100.881 1.00 117.56 ? 333 LYS A NZ    1 
ATOM   2346 N  N     . THR A 1 307 ? 26.097  60.216  107.434 1.00 118.32 ? 334 THR A N     1 
ATOM   2347 C  CA    . THR A 1 307 ? 25.400  60.769  108.591 1.00 126.35 ? 334 THR A CA    1 
ATOM   2348 C  C     . THR A 1 307 ? 25.376  62.289  108.504 1.00 115.39 ? 334 THR A C     1 
ATOM   2349 O  O     . THR A 1 307 ? 26.426  62.931  108.668 1.00 101.62 ? 334 THR A O     1 
ATOM   2350 C  CB    . THR A 1 307 ? 26.065  60.321  109.895 1.00 120.12 ? 334 THR A CB    1 
ATOM   2351 O  OG1   . THR A 1 307 ? 27.480  60.208  109.698 1.00 133.63 ? 334 THR A OG1   1 
ATOM   2352 C  CG2   . THR A 1 307 ? 25.504  58.979  110.353 1.00 100.86 ? 334 THR A CG2   1 
ATOM   2353 N  N     . PRO A 1 308 ? 24.223  62.905  108.243 1.00 116.19 ? 335 PRO A N     1 
ATOM   2354 C  CA    . PRO A 1 308 ? 24.164  64.367  108.140 1.00 120.90 ? 335 PRO A CA    1 
ATOM   2355 C  C     . PRO A 1 308 ? 23.956  65.045  109.485 1.00 122.04 ? 335 PRO A C     1 
ATOM   2356 O  O     . PRO A 1 308 ? 23.175  64.600  110.329 1.00 126.00 ? 335 PRO A O     1 
ATOM   2357 C  CB    . PRO A 1 308 ? 22.949  64.603  107.227 1.00 125.62 ? 335 PRO A CB    1 
ATOM   2358 C  CG    . PRO A 1 308 ? 22.513  63.234  106.744 1.00 127.28 ? 335 PRO A CG    1 
ATOM   2359 C  CD    . PRO A 1 308 ? 22.978  62.276  107.783 1.00 113.72 ? 335 PRO A CD    1 
ATOM   2360 N  N     . ASP A 1 309 ? 24.667  66.151  109.670 1.00 120.08 ? 336 ASP A N     1 
ATOM   2361 C  CA    . ASP A 1 309 ? 24.491  67.041  110.808 1.00 106.39 ? 336 ASP A CA    1 
ATOM   2362 C  C     . ASP A 1 309 ? 23.897  68.363  110.334 1.00 108.78 ? 336 ASP A C     1 
ATOM   2363 O  O     . ASP A 1 309 ? 23.624  68.562  109.147 1.00 109.44 ? 336 ASP A O     1 
ATOM   2364 C  CB    . ASP A 1 309 ? 25.822  67.258  111.533 1.00 101.01 ? 336 ASP A CB    1 
ATOM   2365 C  CG    . ASP A 1 309 ? 26.953  67.634  110.589 1.00 115.82 ? 336 ASP A CG    1 
ATOM   2366 O  OD1   . ASP A 1 309 ? 26.672  67.989  109.425 1.00 122.96 ? 336 ASP A OD1   1 
ATOM   2367 O  OD2   . ASP A 1 309 ? 28.127  67.567  111.008 1.00 109.50 ? 336 ASP A OD2   1 
ATOM   2368 N  N     . LYS A 1 310 ? 23.697  69.276  111.281 1.00 115.50 ? 337 LYS A N     1 
ATOM   2369 C  CA    . LYS A 1 310 ? 23.245  70.625  110.975 1.00 113.59 ? 337 LYS A CA    1 
ATOM   2370 C  C     . LYS A 1 310 ? 24.405  71.611  110.881 1.00 105.23 ? 337 LYS A C     1 
ATOM   2371 O  O     . LYS A 1 310 ? 24.173  72.823  110.851 1.00 94.26  ? 337 LYS A O     1 
ATOM   2372 C  CB    . LYS A 1 310 ? 22.234  71.099  112.023 1.00 117.90 ? 337 LYS A CB    1 
ATOM   2373 C  CG    . LYS A 1 310 ? 20.961  70.262  112.087 1.00 124.13 ? 337 LYS A CG    1 
ATOM   2374 C  CD    . LYS A 1 310 ? 20.139  70.387  110.810 1.00 123.52 ? 337 LYS A CD    1 
ATOM   2375 C  CE    . LYS A 1 310 ? 18.831  69.604  110.894 1.00 126.10 ? 337 LYS A CE    1 
ATOM   2376 N  NZ    . LYS A 1 310 ? 17.895  70.144  111.917 1.00 120.77 ? 337 LYS A NZ    1 
ATOM   2377 N  N     . MET A 1 311 ? 25.646  71.115  110.849 1.00 97.14  ? 338 MET A N     1 
ATOM   2378 C  CA    . MET A 1 311 ? 26.833  71.956  110.707 1.00 92.60  ? 338 MET A CA    1 
ATOM   2379 C  C     . MET A 1 311 ? 26.967  72.936  111.869 1.00 97.42  ? 338 MET A C     1 
ATOM   2380 O  O     . MET A 1 311 ? 27.578  74.001  111.738 1.00 98.89  ? 338 MET A O     1 
ATOM   2381 C  CB    . MET A 1 311 ? 26.825  72.708  109.373 1.00 96.87  ? 338 MET A CB    1 
ATOM   2382 C  CG    . MET A 1 311 ? 27.182  71.873  108.176 1.00 103.05 ? 338 MET A CG    1 
ATOM   2383 S  SD    . MET A 1 311 ? 27.189  72.889  106.695 1.00 96.65  ? 338 MET A SD    1 
ATOM   2384 C  CE    . MET A 1 311 ? 25.586  73.658  106.858 1.00 96.53  ? 338 MET A CE    1 
ATOM   2385 N  N     . GLY A 1 312 ? 26.391  72.580  113.016 1.00 97.40  ? 339 GLY A N     1 
ATOM   2386 C  CA    . GLY A 1 312 ? 26.464  73.399  114.203 1.00 83.11  ? 339 GLY A CA    1 
ATOM   2387 C  C     . GLY A 1 312 ? 25.458  74.526  114.276 1.00 89.02  ? 339 GLY A C     1 
ATOM   2388 O  O     . GLY A 1 312 ? 25.335  75.154  115.336 1.00 113.70 ? 339 GLY A O     1 
ATOM   2389 N  N     . PHE A 1 313 ? 24.743  74.812  113.192 1.00 100.10 ? 340 PHE A N     1 
ATOM   2390 C  CA    . PHE A 1 313 ? 23.698  75.821  113.238 1.00 104.15 ? 340 PHE A CA    1 
ATOM   2391 C  C     . PHE A 1 313 ? 22.524  75.328  114.078 1.00 105.68 ? 340 PHE A C     1 
ATOM   2392 O  O     . PHE A 1 313 ? 22.323  74.125  114.271 1.00 110.73 ? 340 PHE A O     1 
ATOM   2393 C  CB    . PHE A 1 313 ? 23.215  76.169  111.831 1.00 96.36  ? 340 PHE A CB    1 
ATOM   2394 C  CG    . PHE A 1 313 ? 24.267  76.787  110.962 1.00 96.21  ? 340 PHE A CG    1 
ATOM   2395 C  CD1   . PHE A 1 313 ? 24.586  78.127  111.090 1.00 95.53  ? 340 PHE A CD1   1 
ATOM   2396 C  CD2   . PHE A 1 313 ? 24.930  76.031  110.010 1.00 99.28  ? 340 PHE A CD2   1 
ATOM   2397 C  CE1   . PHE A 1 313 ? 25.555  78.703  110.287 1.00 104.16 ? 340 PHE A CE1   1 
ATOM   2398 C  CE2   . PHE A 1 313 ? 25.900  76.601  109.203 1.00 96.10  ? 340 PHE A CE2   1 
ATOM   2399 C  CZ    . PHE A 1 313 ? 26.213  77.940  109.343 1.00 94.03  ? 340 PHE A CZ    1 
ATOM   2400 N  N     . ASP A 1 314 ? 21.741  76.281  114.588 1.00 101.15 ? 341 ASP A N     1 
ATOM   2401 C  CA    . ASP A 1 314 ? 20.543  75.912  115.333 1.00 107.42 ? 341 ASP A CA    1 
ATOM   2402 C  C     . ASP A 1 314 ? 19.454  75.354  114.425 1.00 108.71 ? 341 ASP A C     1 
ATOM   2403 O  O     . ASP A 1 314 ? 18.549  74.668  114.914 1.00 108.26 ? 341 ASP A O     1 
ATOM   2404 C  CB    . ASP A 1 314 ? 20.010  77.114  116.118 1.00 103.48 ? 341 ASP A CB    1 
ATOM   2405 C  CG    . ASP A 1 314 ? 20.970  77.582  117.199 1.00 108.58 ? 341 ASP A CG    1 
ATOM   2406 O  OD1   . ASP A 1 314 ? 22.178  77.278  117.107 1.00 113.86 ? 341 ASP A OD1   1 
ATOM   2407 O  OD2   . ASP A 1 314 ? 20.512  78.248  118.152 1.00 130.34 ? 341 ASP A OD2   1 
ATOM   2408 N  N     . GLU A 1 315 ? 19.525  75.628  113.124 1.00 110.91 ? 342 GLU A N     1 
ATOM   2409 C  CA    . GLU A 1 315 ? 18.597  75.089  112.137 1.00 118.11 ? 342 GLU A CA    1 
ATOM   2410 C  C     . GLU A 1 315 ? 19.138  75.403  110.750 1.00 113.09 ? 342 GLU A C     1 
ATOM   2411 O  O     . GLU A 1 315 ? 19.846  76.395  110.558 1.00 113.67 ? 342 GLU A O     1 
ATOM   2412 C  CB    . GLU A 1 315 ? 17.182  75.667  112.305 1.00 114.35 ? 342 GLU A CB    1 
ATOM   2413 C  CG    . GLU A 1 315 ? 16.127  75.118  111.336 1.00 112.70 ? 342 GLU A CG    1 
ATOM   2414 C  CD    . GLU A 1 315 ? 15.752  73.665  111.601 1.00 118.10 ? 342 GLU A CD    1 
ATOM   2415 O  OE1   . GLU A 1 315 ? 16.584  72.770  111.344 1.00 119.10 ? 342 GLU A OE1   1 
ATOM   2416 O  OE2   . GLU A 1 315 ? 14.618  73.419  112.065 1.00 130.19 ? 342 GLU A OE2   1 
ATOM   2417 N  N     . VAL A 1 316 ? 18.811  74.539  109.794 1.00 112.37 ? 343 VAL A N     1 
ATOM   2418 C  CA    . VAL A 1 316 ? 19.140  74.745  108.389 1.00 109.98 ? 343 VAL A CA    1 
ATOM   2419 C  C     . VAL A 1 316 ? 17.839  74.640  107.603 1.00 110.63 ? 343 VAL A C     1 
ATOM   2420 O  O     . VAL A 1 316 ? 17.239  73.561  107.529 1.00 111.09 ? 343 VAL A O     1 
ATOM   2421 C  CB    . VAL A 1 316 ? 20.179  73.736  107.876 1.00 101.55 ? 343 VAL A CB    1 
ATOM   2422 C  CG1   . VAL A 1 316 ? 20.348  73.867  106.374 1.00 102.46 ? 343 VAL A CG1   1 
ATOM   2423 C  CG2   . VAL A 1 316 ? 21.511  73.950  108.576 1.00 98.83  ? 343 VAL A CG2   1 
ATOM   2424 N  N     . PHE A 1 317 ? 17.395  75.757  107.035 1.00 108.35 ? 344 PHE A N     1 
ATOM   2425 C  CA    . PHE A 1 317 ? 16.177  75.806  106.243 1.00 105.94 ? 344 PHE A CA    1 
ATOM   2426 C  C     . PHE A 1 317 ? 16.499  75.654  104.762 1.00 109.20 ? 344 PHE A C     1 
ATOM   2427 O  O     . PHE A 1 317 ? 17.595  75.989  104.307 1.00 106.02 ? 344 PHE A O     1 
ATOM   2428 C  CB    . PHE A 1 317 ? 15.428  77.123  106.461 1.00 107.51 ? 344 PHE A CB    1 
ATOM   2429 C  CG    . PHE A 1 317 ? 14.926  77.319  107.862 1.00 107.83 ? 344 PHE A CG    1 
ATOM   2430 C  CD1   . PHE A 1 317 ? 13.742  76.732  108.276 1.00 110.55 ? 344 PHE A CD1   1 
ATOM   2431 C  CD2   . PHE A 1 317 ? 15.626  78.109  108.759 1.00 106.46 ? 344 PHE A CD2   1 
ATOM   2432 C  CE1   . PHE A 1 317 ? 13.271  76.918  109.562 1.00 110.63 ? 344 PHE A CE1   1 
ATOM   2433 C  CE2   . PHE A 1 317 ? 15.159  78.301  110.047 1.00 109.96 ? 344 PHE A CE2   1 
ATOM   2434 C  CZ    . PHE A 1 317 ? 13.979  77.705  110.448 1.00 110.15 ? 344 PHE A CZ    1 
ATOM   2435 N  N     . MET A 1 318 ? 15.525  75.150  104.009 1.00 115.63 ? 345 MET A N     1 
ATOM   2436 C  CA    . MET A 1 318 ? 15.612  75.113  102.552 1.00 118.25 ? 345 MET A CA    1 
ATOM   2437 C  C     . MET A 1 318 ? 14.265  75.539  101.988 1.00 118.84 ? 345 MET A C     1 
ATOM   2438 O  O     . MET A 1 318 ? 13.274  74.818  102.137 1.00 123.63 ? 345 MET A O     1 
ATOM   2439 C  CB    . MET A 1 318 ? 15.996  73.727  102.041 1.00 125.54 ? 345 MET A CB    1 
ATOM   2440 C  CG    . MET A 1 318 ? 15.929  73.615  100.528 1.00 119.84 ? 345 MET A CG    1 
ATOM   2441 S  SD    . MET A 1 318 ? 16.132  71.929  99.940  1.00 131.45 ? 345 MET A SD    1 
ATOM   2442 C  CE    . MET A 1 318 ? 15.098  71.970  98.478  1.00 136.42 ? 345 MET A CE    1 
ATOM   2443 N  N     . ILE A 1 319 ? 14.229  76.701  101.347 1.00 114.41 ? 346 ILE A N     1 
ATOM   2444 C  CA    . ILE A 1 319 ? 13.008  77.185  100.717 1.00 124.39 ? 346 ILE A CA    1 
ATOM   2445 C  C     . ILE A 1 319 ? 12.840  76.507  99.366  1.00 134.01 ? 346 ILE A C     1 
ATOM   2446 O  O     . ILE A 1 319 ? 13.805  76.344  98.607  1.00 131.26 ? 346 ILE A O     1 
ATOM   2447 C  CB    . ILE A 1 319 ? 13.044  78.716  100.572 1.00 122.03 ? 346 ILE A CB    1 
ATOM   2448 C  CG1   . ILE A 1 319 ? 13.456  79.363  101.894 1.00 127.11 ? 346 ILE A CG1   1 
ATOM   2449 C  CG2   . ILE A 1 319 ? 11.695  79.238  100.117 1.00 112.91 ? 346 ILE A CG2   1 
ATOM   2450 C  CD1   . ILE A 1 319 ? 13.547  80.868  101.835 1.00 117.68 ? 346 ILE A CD1   1 
ATOM   2451 N  N     . ASN A 1 320 ? 11.605  76.111  99.057  1.00 130.47 ? 347 ASN A N     1 
ATOM   2452 C  CA    . ASN A 1 320 ? 11.323  75.441  97.793  1.00 138.17 ? 347 ASN A CA    1 
ATOM   2453 C  C     . ASN A 1 320 ? 9.831   75.429  97.486  1.00 144.46 ? 347 ASN A C     1 
ATOM   2454 O  O     . ASN A 1 320 ? 9.023   75.083  98.352  1.00 144.58 ? 347 ASN A O     1 
ATOM   2455 C  CB    . ASN A 1 320 ? 11.870  74.010  97.816  1.00 138.84 ? 347 ASN A CB    1 
ATOM   2456 C  CG    . ASN A 1 320 ? 11.462  73.209  96.593  1.00 141.42 ? 347 ASN A CG    1 
ATOM   2457 O  OD1   . ASN A 1 320 ? 10.727  72.225  96.697  1.00 145.82 ? 347 ASN A OD1   1 
ATOM   2458 N  ND2   . ASN A 1 320 ? 11.936  73.628  95.426  1.00 139.77 ? 347 ASN A ND2   1 
ATOM   2459 N  N     . LEU A 1 321 ? 9.454   75.833  96.275  1.00 143.38 ? 348 LEU A N     1 
ATOM   2460 C  CA    . LEU A 1 321 ? 8.067   75.695  95.854  1.00 152.50 ? 348 LEU A CA    1 
ATOM   2461 C  C     . LEU A 1 321 ? 7.691   74.220  95.795  1.00 157.33 ? 348 LEU A C     1 
ATOM   2462 O  O     . LEU A 1 321 ? 8.457   73.387  95.302  1.00 149.86 ? 348 LEU A O     1 
ATOM   2463 C  CB    . LEU A 1 321 ? 7.852   76.345  94.486  1.00 156.93 ? 348 LEU A CB    1 
ATOM   2464 C  CG    . LEU A 1 321 ? 7.823   77.871  94.406  1.00 158.99 ? 348 LEU A CG    1 
ATOM   2465 C  CD1   . LEU A 1 321 ? 8.641   78.354  93.221  1.00 163.07 ? 348 LEU A CD1   1 
ATOM   2466 C  CD2   . LEU A 1 321 ? 6.392   78.375  94.305  1.00 156.38 ? 348 LEU A CD2   1 
ATOM   2467 N  N     . ARG A 1 322 ? 6.506   73.895  96.316  1.00 166.52 ? 349 ARG A N     1 
ATOM   2468 C  CA    . ARG A 1 322 ? 6.046   72.512  96.275  1.00 167.57 ? 349 ARG A CA    1 
ATOM   2469 C  C     . ARG A 1 322 ? 5.853   72.022  94.846  1.00 170.81 ? 349 ARG A C     1 
ATOM   2470 O  O     . ARG A 1 322 ? 5.880   70.810  94.607  1.00 169.80 ? 349 ARG A O     1 
ATOM   2471 C  CB    . ARG A 1 322 ? 4.746   72.368  97.070  1.00 170.61 ? 349 ARG A CB    1 
ATOM   2472 C  CG    . ARG A 1 322 ? 4.334   70.928  97.336  1.00 167.99 ? 349 ARG A CG    1 
ATOM   2473 C  CD    . ARG A 1 322 ? 2.957   70.861  97.972  1.00 179.28 ? 349 ARG A CD    1 
ATOM   2474 N  NE    . ARG A 1 322 ? 2.010   71.735  97.291  1.00 190.26 ? 349 ARG A NE    1 
ATOM   2475 C  CZ    . ARG A 1 322 ? 1.423   71.452  96.135  1.00 194.67 ? 349 ARG A CZ    1 
ATOM   2476 N  NH1   . ARG A 1 322 ? 1.670   70.322  95.493  1.00 191.24 ? 349 ARG A NH1   1 
ATOM   2477 N  NH2   . ARG A 1 322 ? 0.571   72.328  95.609  1.00 189.79 ? 349 ARG A NH2   1 
ATOM   2478 N  N     . ARG A 1 323 ? 5.674   72.937  93.889  1.00 168.11 ? 350 ARG A N     1 
ATOM   2479 C  CA    . ARG A 1 323 ? 5.563   72.552  92.489  1.00 157.44 ? 350 ARG A CA    1 
ATOM   2480 C  C     . ARG A 1 323 ? 6.916   72.266  91.849  1.00 155.38 ? 350 ARG A C     1 
ATOM   2481 O  O     . ARG A 1 323 ? 6.973   71.523  90.863  1.00 159.31 ? 350 ARG A O     1 
ATOM   2482 C  CB    . ARG A 1 323 ? 4.836   73.643  91.692  1.00 155.50 ? 350 ARG A CB    1 
ATOM   2483 C  CG    . ARG A 1 323 ? 5.549   74.989  91.650  1.00 163.07 ? 350 ARG A CG    1 
ATOM   2484 C  CD    . ARG A 1 323 ? 5.040   75.845  90.493  1.00 160.29 ? 350 ARG A CD    1 
ATOM   2485 N  NE    . ARG A 1 323 ? 5.798   77.082  90.342  1.00 162.44 ? 350 ARG A NE    1 
ATOM   2486 C  CZ    . ARG A 1 323 ? 5.318   78.293  90.590  1.00 166.39 ? 350 ARG A CZ    1 
ATOM   2487 N  NH1   . ARG A 1 323 ? 4.066   78.473  90.978  1.00 162.78 ? 350 ARG A NH1   1 
ATOM   2488 N  NH2   . ARG A 1 323 ? 6.113   79.349  90.440  1.00 168.63 ? 350 ARG A NH2   1 
ATOM   2489 N  N     . ARG A 1 324 ? 8.001   72.829  92.383  1.00 147.98 ? 351 ARG A N     1 
ATOM   2490 C  CA    . ARG A 1 324 ? 9.339   72.613  91.828  1.00 143.06 ? 351 ARG A CA    1 
ATOM   2491 C  C     . ARG A 1 324 ? 9.936   71.332  92.414  1.00 137.00 ? 351 ARG A C     1 
ATOM   2492 O  O     . ARG A 1 324 ? 10.849  71.344  93.241  1.00 131.63 ? 351 ARG A O     1 
ATOM   2493 C  CB    . ARG A 1 324 ? 10.233  73.817  92.098  1.00 139.50 ? 351 ARG A CB    1 
ATOM   2494 C  CG    . ARG A 1 324 ? 9.678   75.147  91.619  1.00 125.10 ? 351 ARG A CG    1 
ATOM   2495 C  CD    . ARG A 1 324 ? 9.341   75.125  90.137  1.00 145.80 ? 351 ARG A CD    1 
ATOM   2496 N  NE    . ARG A 1 324 ? 8.821   76.413  89.689  1.00 156.50 ? 351 ARG A NE    1 
ATOM   2497 C  CZ    . ARG A 1 324 ? 8.302   76.641  88.490  1.00 146.49 ? 351 ARG A CZ    1 
ATOM   2498 N  NH1   . ARG A 1 324 ? 8.206   75.682  87.583  1.00 134.71 ? 351 ARG A NH1   1 
ATOM   2499 N  NH2   . ARG A 1 324 ? 7.866   77.863  88.194  1.00 138.29 ? 351 ARG A NH2   1 
ATOM   2500 N  N     . GLN A 1 325 ? 9.394   70.201  91.956  1.00 148.12 ? 352 GLN A N     1 
ATOM   2501 C  CA    . GLN A 1 325 ? 9.886   68.910  92.423  1.00 151.31 ? 352 GLN A CA    1 
ATOM   2502 C  C     . GLN A 1 325 ? 11.274  68.611  91.876  1.00 145.02 ? 352 GLN A C     1 
ATOM   2503 O  O     . GLN A 1 325 ? 12.079  67.964  92.555  1.00 147.38 ? 352 GLN A O     1 
ATOM   2504 C  CB    . GLN A 1 325 ? 8.911   67.800  92.033  1.00 158.59 ? 352 GLN A CB    1 
ATOM   2505 C  CG    . GLN A 1 325 ? 7.512   67.982  92.599  1.00 171.21 ? 352 GLN A CG    1 
ATOM   2506 C  CD    . GLN A 1 325 ? 6.617   66.794  92.322  1.00 185.05 ? 352 GLN A CD    1 
ATOM   2507 O  OE1   . GLN A 1 325 ? 7.064   65.778  91.788  1.00 191.64 ? 352 GLN A OE1   1 
ATOM   2508 N  NE2   . GLN A 1 325 ? 5.344   66.912  92.686  1.00 172.56 ? 352 GLN A NE2   1 
ATOM   2509 N  N     . ASP A 1 326 ? 11.570  69.075  90.659  1.00 135.72 ? 353 ASP A N     1 
ATOM   2510 C  CA    . ASP A 1 326 ? 12.891  68.860  90.077  1.00 121.44 ? 353 ASP A CA    1 
ATOM   2511 C  C     . ASP A 1 326 ? 13.974  69.524  90.917  1.00 125.55 ? 353 ASP A C     1 
ATOM   2512 O  O     . ASP A 1 326 ? 15.016  68.920  91.200  1.00 121.17 ? 353 ASP A O     1 
ATOM   2513 C  CB    . ASP A 1 326 ? 12.919  69.392  88.644  1.00 113.38 ? 353 ASP A CB    1 
ATOM   2514 C  CG    . ASP A 1 326 ? 12.443  70.832  88.548  1.00 143.19 ? 353 ASP A CG    1 
ATOM   2515 O  OD1   . ASP A 1 326 ? 11.375  71.153  89.117  1.00 137.13 ? 353 ASP A OD1   1 
ATOM   2516 O  OD2   . ASP A 1 326 ? 13.151  71.645  87.916  1.00 144.19 ? 353 ASP A OD2   1 
ATOM   2517 N  N     . ARG A 1 327 ? 13.745  70.774  91.325  1.00 132.95 ? 354 ARG A N     1 
ATOM   2518 C  CA    . ARG A 1 327 ? 14.717  71.477  92.155  1.00 119.56 ? 354 ARG A CA    1 
ATOM   2519 C  C     . ARG A 1 327 ? 14.830  70.844  93.535  1.00 120.47 ? 354 ARG A C     1 
ATOM   2520 O  O     . ARG A 1 327 ? 15.920  70.806  94.117  1.00 124.68 ? 354 ARG A O     1 
ATOM   2521 C  CB    . ARG A 1 327 ? 14.333  72.951  92.277  1.00 113.73 ? 354 ARG A CB    1 
ATOM   2522 C  CG    . ARG A 1 327 ? 14.463  73.746  90.992  1.00 113.57 ? 354 ARG A CG    1 
ATOM   2523 C  CD    . ARG A 1 327 ? 14.020  75.179  91.215  1.00 123.54 ? 354 ARG A CD    1 
ATOM   2524 N  NE    . ARG A 1 327 ? 14.512  76.077  90.178  1.00 132.87 ? 354 ARG A NE    1 
ATOM   2525 C  CZ    . ARG A 1 327 ? 14.314  77.388  90.170  1.00 124.17 ? 354 ARG A CZ    1 
ATOM   2526 N  NH1   . ARG A 1 327 ? 13.623  77.989  91.125  1.00 116.40 ? 354 ARG A NH1   1 
ATOM   2527 N  NH2   . ARG A 1 327 ? 14.824  78.115  89.180  1.00 127.75 ? 354 ARG A NH2   1 
ATOM   2528 N  N     . ARG A 1 328 ? 13.716  70.348  94.077  1.00 122.78 ? 355 ARG A N     1 
ATOM   2529 C  CA    . ARG A 1 328 ? 13.744  69.749  95.408  1.00 124.57 ? 355 ARG A CA    1 
ATOM   2530 C  C     . ARG A 1 328 ? 14.600  68.489  95.425  1.00 126.00 ? 355 ARG A C     1 
ATOM   2531 O  O     . ARG A 1 328 ? 15.450  68.317  96.306  1.00 129.69 ? 355 ARG A O     1 
ATOM   2532 C  CB    . ARG A 1 328 ? 12.323  69.436  95.881  1.00 135.26 ? 355 ARG A CB    1 
ATOM   2533 C  CG    . ARG A 1 328 ? 12.241  68.981  97.332  1.00 129.18 ? 355 ARG A CG    1 
ATOM   2534 C  CD    . ARG A 1 328 ? 10.905  68.319  97.652  1.00 132.80 ? 355 ARG A CD    1 
ATOM   2535 N  NE    . ARG A 1 328 ? 9.765   69.119  97.219  1.00 147.55 ? 355 ARG A NE    1 
ATOM   2536 C  CZ    . ARG A 1 328 ? 8.984   68.817  96.191  1.00 148.50 ? 355 ARG A CZ    1 
ATOM   2537 N  NH1   . ARG A 1 328 ? 9.181   67.725  95.470  1.00 149.17 ? 355 ARG A NH1   1 
ATOM   2538 N  NH2   . ARG A 1 328 ? 7.977   69.629  95.880  1.00 152.92 ? 355 ARG A NH2   1 
ATOM   2539 N  N     . GLU A 1 329 ? 14.392  67.596  94.455  1.00 123.83 ? 356 GLU A N     1 
ATOM   2540 C  CA    . GLU A 1 329 ? 15.156  66.353  94.424  1.00 122.65 ? 356 GLU A CA    1 
ATOM   2541 C  C     . GLU A 1 329 ? 16.641  66.610  94.202  1.00 120.43 ? 356 GLU A C     1 
ATOM   2542 O  O     . GLU A 1 329 ? 17.482  65.871  94.728  1.00 115.23 ? 356 GLU A O     1 
ATOM   2543 C  CB    . GLU A 1 329 ? 14.609  65.424  93.340  1.00 126.74 ? 356 GLU A CB    1 
ATOM   2544 C  CG    . GLU A 1 329 ? 13.138  65.076  93.508  1.00 139.51 ? 356 GLU A CG    1 
ATOM   2545 C  CD    . GLU A 1 329 ? 12.631  64.135  92.431  1.00 140.28 ? 356 GLU A CD    1 
ATOM   2546 O  OE1   . GLU A 1 329 ? 13.436  63.329  91.920  1.00 141.09 ? 356 GLU A OE1   1 
ATOM   2547 O  OE2   . GLU A 1 329 ? 11.430  64.205  92.093  1.00 151.32 ? 356 GLU A OE2   1 
ATOM   2548 N  N     . ARG A 1 330 ? 16.986  67.650  93.439  1.00 115.63 ? 357 ARG A N     1 
ATOM   2549 C  CA    . ARG A 1 330 ? 18.395  67.942  93.192  1.00 104.91 ? 357 ARG A CA    1 
ATOM   2550 C  C     . ARG A 1 330 ? 19.077  68.472  94.446  1.00 109.21 ? 357 ARG A C     1 
ATOM   2551 O  O     . ARG A 1 330 ? 20.216  68.095  94.747  1.00 108.40 ? 357 ARG A O     1 
ATOM   2552 C  CB    . ARG A 1 330 ? 18.539  68.944  92.048  1.00 105.05 ? 357 ARG A CB    1 
ATOM   2553 C  CG    . ARG A 1 330 ? 19.948  69.011  91.471  1.00 95.16  ? 357 ARG A CG    1 
ATOM   2554 C  CD    . ARG A 1 330 ? 20.165  70.265  90.635  1.00 95.49  ? 357 ARG A CD    1 
ATOM   2555 N  NE    . ARG A 1 330 ? 20.410  71.436  91.469  1.00 109.48 ? 357 ARG A NE    1 
ATOM   2556 C  CZ    . ARG A 1 330 ? 21.611  71.835  91.868  1.00 97.64  ? 357 ARG A CZ    1 
ATOM   2557 N  NH1   . ARG A 1 330 ? 22.708  71.185  91.516  1.00 91.25  ? 357 ARG A NH1   1 
ATOM   2558 N  NH2   . ARG A 1 330 ? 21.713  72.911  92.643  1.00 102.43 ? 357 ARG A NH2   1 
ATOM   2559 N  N     . MET A 1 331 ? 18.400  69.351  95.188  1.00 108.80 ? 358 MET A N     1 
ATOM   2560 C  CA    . MET A 1 331 ? 18.999  69.903  96.398  1.00 107.16 ? 358 MET A CA    1 
ATOM   2561 C  C     . MET A 1 331 ? 19.119  68.846  97.488  1.00 111.07 ? 358 MET A C     1 
ATOM   2562 O  O     . MET A 1 331 ? 20.150  68.760  98.164  1.00 112.64 ? 358 MET A O     1 
ATOM   2563 C  CB    . MET A 1 331 ? 18.184  71.096  96.892  1.00 117.08 ? 358 MET A CB    1 
ATOM   2564 C  CG    . MET A 1 331 ? 18.154  72.280  95.935  1.00 120.05 ? 358 MET A CG    1 
ATOM   2565 S  SD    . MET A 1 331 ? 19.773  73.033  95.673  1.00 114.32 ? 358 MET A SD    1 
ATOM   2566 C  CE    . MET A 1 331 ? 20.304  73.316  97.363  1.00 97.53  ? 358 MET A CE    1 
ATOM   2567 N  N     . LEU A 1 332 ? 18.078  68.028  97.667  1.00 118.64 ? 359 LEU A N     1 
ATOM   2568 C  CA    . LEU A 1 332 ? 18.116  66.977  98.679  1.00 123.24 ? 359 LEU A CA    1 
ATOM   2569 C  C     . LEU A 1 332 ? 19.204  65.948  98.403  1.00 120.47 ? 359 LEU A C     1 
ATOM   2570 O  O     . LEU A 1 332 ? 19.635  65.252  99.329  1.00 119.22 ? 359 LEU A O     1 
ATOM   2571 C  CB    . LEU A 1 332 ? 16.751  66.289  98.772  1.00 125.96 ? 359 LEU A CB    1 
ATOM   2572 C  CG    . LEU A 1 332 ? 15.581  67.152  99.246  1.00 124.07 ? 359 LEU A CG    1 
ATOM   2573 C  CD1   . LEU A 1 332 ? 14.277  66.374  99.181  1.00 127.54 ? 359 LEU A CD1   1 
ATOM   2574 C  CD2   . LEU A 1 332 ? 15.830  67.673  100.651 1.00 147.65 ? 359 LEU A CD2   1 
ATOM   2575 N  N     . ARG A 1 333 ? 19.655  65.839  97.154  1.00 112.62 ? 360 ARG A N     1 
ATOM   2576 C  CA    . ARG A 1 333 ? 20.772  64.961  96.827  1.00 106.66 ? 360 ARG A CA    1 
ATOM   2577 C  C     . ARG A 1 333 ? 22.112  65.628  97.108  1.00 108.24 ? 360 ARG A C     1 
ATOM   2578 O  O     . ARG A 1 333 ? 23.018  64.992  97.660  1.00 102.64 ? 360 ARG A O     1 
ATOM   2579 C  CB    . ARG A 1 333 ? 20.684  64.530  95.363  1.00 104.89 ? 360 ARG A CB    1 
ATOM   2580 C  CG    . ARG A 1 333 ? 19.583  63.527  95.085  1.00 112.60 ? 360 ARG A CG    1 
ATOM   2581 C  CD    . ARG A 1 333 ? 19.436  63.272  93.596  1.00 131.99 ? 360 ARG A CD    1 
ATOM   2582 N  NE    . ARG A 1 333 ? 18.694  62.047  93.325  1.00 143.11 ? 360 ARG A NE    1 
ATOM   2583 C  CZ    . ARG A 1 333 ? 19.236  60.837  93.300  1.00 148.11 ? 360 ARG A CZ    1 
ATOM   2584 N  NH1   . ARG A 1 333 ? 20.526  60.652  93.537  1.00 128.42 ? 360 ARG A NH1   1 
ATOM   2585 N  NH2   . ARG A 1 333 ? 18.467  59.786  93.029  1.00 149.07 ? 360 ARG A NH2   1 
ATOM   2586 N  N     . ALA A 1 334 ? 22.260  66.901  96.735  1.00 109.12 ? 361 ALA A N     1 
ATOM   2587 C  CA    . ALA A 1 334 ? 23.508  67.605  97.016  1.00 106.88 ? 361 ALA A CA    1 
ATOM   2588 C  C     . ALA A 1 334 ? 23.721  67.765  98.515  1.00 101.76 ? 361 ALA A C     1 
ATOM   2589 O  O     . ALA A 1 334 ? 24.847  67.633  99.009  1.00 98.26  ? 361 ALA A O     1 
ATOM   2590 C  CB    . ALA A 1 334 ? 23.518  68.969  96.325  1.00 87.83  ? 361 ALA A CB    1 
ATOM   2591 N  N     . LEU A 1 335 ? 22.649  68.046  99.257  1.00 100.98 ? 362 LEU A N     1 
ATOM   2592 C  CA    . LEU A 1 335 ? 22.757  68.148  100.707 1.00 99.53  ? 362 LEU A CA    1 
ATOM   2593 C  C     . LEU A 1 335 ? 23.127  66.804  101.321 1.00 100.74 ? 362 LEU A C     1 
ATOM   2594 O  O     . LEU A 1 335 ? 24.070  66.713  102.114 1.00 97.12  ? 362 LEU A O     1 
ATOM   2595 C  CB    . LEU A 1 335 ? 21.445  68.675  101.290 1.00 109.90 ? 362 LEU A CB    1 
ATOM   2596 C  CG    . LEU A 1 335 ? 21.085  70.114  100.913 1.00 104.59 ? 362 LEU A CG    1 
ATOM   2597 C  CD1   . LEU A 1 335 ? 19.657  70.448  101.314 1.00 102.79 ? 362 LEU A CD1   1 
ATOM   2598 C  CD2   . LEU A 1 335 ? 22.066  71.084  101.551 1.00 103.11 ? 362 LEU A CD2   1 
ATOM   2599 N  N     . GLN A 1 336 ? 22.402  65.744  100.951 1.00 107.73 ? 363 GLN A N     1 
ATOM   2600 C  CA    . GLN A 1 336 ? 22.695  64.422  101.495 1.00 112.41 ? 363 GLN A CA    1 
ATOM   2601 C  C     . GLN A 1 336 ? 24.100  63.964  101.121 1.00 106.13 ? 363 GLN A C     1 
ATOM   2602 O  O     . GLN A 1 336 ? 24.779  63.306  101.918 1.00 116.80 ? 363 GLN A O     1 
ATOM   2603 C  CB    . GLN A 1 336 ? 21.652  63.413  101.010 1.00 116.50 ? 363 GLN A CB    1 
ATOM   2604 C  CG    . GLN A 1 336 ? 21.934  61.968  101.414 1.00 139.92 ? 363 GLN A CG    1 
ATOM   2605 C  CD    . GLN A 1 336 ? 21.973  61.764  102.926 1.00 155.20 ? 363 GLN A CD    1 
ATOM   2606 O  OE1   . GLN A 1 336 ? 21.435  62.566  103.692 1.00 150.26 ? 363 GLN A OE1   1 
ATOM   2607 N  NE2   . GLN A 1 336 ? 22.611  60.681  103.358 1.00 144.13 ? 363 GLN A NE2   1 
ATOM   2608 N  N     . ALA A 1 337 ? 24.558  64.309  99.915  1.00 105.91 ? 364 ALA A N     1 
ATOM   2609 C  CA    . ALA A 1 337 ? 25.911  63.948  99.507  1.00 95.14  ? 364 ALA A CA    1 
ATOM   2610 C  C     . ALA A 1 337 ? 26.959  64.620  100.382 1.00 98.48  ? 364 ALA A C     1 
ATOM   2611 O  O     . ALA A 1 337 ? 28.007  64.027  100.658 1.00 96.69  ? 364 ALA A O     1 
ATOM   2612 C  CB    . ALA A 1 337 ? 26.128  64.309  98.038  1.00 89.49  ? 364 ALA A CB    1 
ATOM   2613 N  N     . GLN A 1 338 ? 26.698  65.847  100.827 1.00 106.52 ? 365 GLN A N     1 
ATOM   2614 C  CA    . GLN A 1 338 ? 27.621  66.591  101.672 1.00 101.97 ? 365 GLN A CA    1 
ATOM   2615 C  C     . GLN A 1 338 ? 27.408  66.329  103.157 1.00 103.26 ? 365 GLN A C     1 
ATOM   2616 O  O     . GLN A 1 338 ? 27.977  67.051  103.983 1.00 107.95 ? 365 GLN A O     1 
ATOM   2617 C  CB    . GLN A 1 338 ? 27.497  68.091  101.395 1.00 91.89  ? 365 GLN A CB    1 
ATOM   2618 C  CG    . GLN A 1 338 ? 27.822  68.489  99.969  1.00 79.65  ? 365 GLN A CG    1 
ATOM   2619 C  CD    . GLN A 1 338 ? 27.697  69.982  99.747  1.00 81.80  ? 365 GLN A CD    1 
ATOM   2620 O  OE1   . GLN A 1 338 ? 28.664  70.726  99.904  1.00 89.22  ? 365 GLN A OE1   1 
ATOM   2621 N  NE2   . GLN A 1 338 ? 26.500  70.429  99.379  1.00 83.07  ? 365 GLN A NE2   1 
ATOM   2622 N  N     . GLU A 1 339 ? 26.617  65.313  103.509 1.00 107.76 ? 366 GLU A N     1 
ATOM   2623 C  CA    . GLU A 1 339 ? 26.275  65.020  104.903 1.00 112.08 ? 366 GLU A CA    1 
ATOM   2624 C  C     . GLU A 1 339 ? 25.701  66.254  105.598 1.00 108.47 ? 366 GLU A C     1 
ATOM   2625 O  O     . GLU A 1 339 ? 26.058  66.585  106.731 1.00 109.46 ? 366 GLU A O     1 
ATOM   2626 C  CB    . GLU A 1 339 ? 27.480  64.462  105.665 1.00 106.84 ? 366 GLU A CB    1 
ATOM   2627 C  CG    . GLU A 1 339 ? 27.952  63.105  105.161 1.00 107.98 ? 366 GLU A CG    1 
ATOM   2628 C  CD    . GLU A 1 339 ? 28.835  62.378  106.162 1.00 121.10 ? 366 GLU A CD    1 
ATOM   2629 O  OE1   . GLU A 1 339 ? 29.431  63.046  107.034 1.00 125.03 ? 366 GLU A OE1   1 
ATOM   2630 O  OE2   . GLU A 1 339 ? 28.926  61.134  106.082 1.00 119.86 ? 366 GLU A OE2   1 
ATOM   2631 N  N     . ILE A 1 340 ? 24.803  66.944  104.899 1.00 97.10  ? 367 ILE A N     1 
ATOM   2632 C  CA    . ILE A 1 340 ? 24.116  68.120  105.415 1.00 99.95  ? 367 ILE A CA    1 
ATOM   2633 C  C     . ILE A 1 340 ? 22.631  67.798  105.517 1.00 114.67 ? 367 ILE A C     1 
ATOM   2634 O  O     . ILE A 1 340 ? 22.059  67.158  104.627 1.00 103.38 ? 367 ILE A O     1 
ATOM   2635 C  CB    . ILE A 1 340 ? 24.356  69.358  104.523 1.00 99.30  ? 367 ILE A CB    1 
ATOM   2636 C  CG1   . ILE A 1 340 ? 25.849  69.691  104.467 1.00 96.56  ? 367 ILE A CG1   1 
ATOM   2637 C  CG2   . ILE A 1 340 ? 23.561  70.557  105.026 1.00 89.83  ? 367 ILE A CG2   1 
ATOM   2638 C  CD1   . ILE A 1 340 ? 26.174  70.934  103.660 1.00 84.04  ? 367 ILE A CD1   1 
ATOM   2639 N  N     . GLU A 1 341 ? 22.015  68.230  106.615 1.00 113.26 ? 368 GLU A N     1 
ATOM   2640 C  CA    . GLU A 1 341 ? 20.611  67.978  106.896 1.00 114.17 ? 368 GLU A CA    1 
ATOM   2641 C  C     . GLU A 1 341 ? 19.870  69.305  106.983 1.00 120.57 ? 368 GLU A C     1 
ATOM   2642 O  O     . GLU A 1 341 ? 20.363  70.260  107.590 1.00 122.67 ? 368 GLU A O     1 
ATOM   2643 C  CB    . GLU A 1 341 ? 20.456  67.194  108.201 1.00 122.16 ? 368 GLU A CB    1 
ATOM   2644 C  CG    . GLU A 1 341 ? 19.032  66.817  108.553 1.00 135.39 ? 368 GLU A CG    1 
ATOM   2645 C  CD    . GLU A 1 341 ? 18.936  66.162  109.919 1.00 144.99 ? 368 GLU A CD    1 
ATOM   2646 O  OE1   . GLU A 1 341 ? 19.996  65.863  110.511 1.00 132.82 ? 368 GLU A OE1   1 
ATOM   2647 O  OE2   . GLU A 1 341 ? 17.802  65.951  110.402 1.00 152.67 ? 368 GLU A OE2   1 
ATOM   2648 N  N     . CYS A 1 342 ? 18.688  69.366  106.373 1.00 128.54 ? 369 CYS A N     1 
ATOM   2649 C  CA    . CYS A 1 342 ? 17.914  70.597  106.333 1.00 120.78 ? 369 CYS A CA    1 
ATOM   2650 C  C     . CYS A 1 342 ? 16.459  70.303  106.658 1.00 127.53 ? 369 CYS A C     1 
ATOM   2651 O  O     . CYS A 1 342 ? 15.972  69.188  106.454 1.00 141.38 ? 369 CYS A O     1 
ATOM   2652 C  CB    . CYS A 1 342 ? 17.990  71.278  104.960 1.00 124.14 ? 369 CYS A CB    1 
ATOM   2653 S  SG    . CYS A 1 342 ? 16.847  70.578  103.735 1.00 124.33 ? 369 CYS A SG    1 
ATOM   2654 N  N     . ARG A 1 343 ? 15.766  71.321  107.161 1.00 118.22 ? 370 ARG A N     1 
ATOM   2655 C  CA    . ARG A 1 343 ? 14.323  71.271  107.346 1.00 113.55 ? 370 ARG A CA    1 
ATOM   2656 C  C     . ARG A 1 343 ? 13.657  71.946  106.153 1.00 122.95 ? 370 ARG A C     1 
ATOM   2657 O  O     . ARG A 1 343 ? 13.879  73.137  105.904 1.00 121.04 ? 370 ARG A O     1 
ATOM   2658 C  CB    . ARG A 1 343 ? 13.898  71.951  108.645 1.00 120.49 ? 370 ARG A CB    1 
ATOM   2659 C  CG    . ARG A 1 343 ? 12.394  72.019  108.789 1.00 116.39 ? 370 ARG A CG    1 
ATOM   2660 C  CD    . ARG A 1 343 ? 11.965  72.883  109.946 1.00 115.27 ? 370 ARG A CD    1 
ATOM   2661 N  NE    . ARG A 1 343 ? 10.593  73.333  109.758 1.00 117.59 ? 370 ARG A NE    1 
ATOM   2662 C  CZ    . ARG A 1 343 ? 9.876   73.954  110.682 1.00 144.52 ? 370 ARG A CZ    1 
ATOM   2663 N  NH1   . ARG A 1 343 ? 10.364  74.193  111.889 1.00 148.85 ? 370 ARG A NH1   1 
ATOM   2664 N  NH2   . ARG A 1 343 ? 8.639   74.343  110.389 1.00 153.26 ? 370 ARG A NH2   1 
ATOM   2665 N  N     . LEU A 1 344 ? 12.842  71.189  105.427 1.00 123.21 ? 371 LEU A N     1 
ATOM   2666 C  CA    . LEU A 1 344 ? 12.228  71.683  104.204 1.00 117.08 ? 371 LEU A CA    1 
ATOM   2667 C  C     . LEU A 1 344 ? 11.101  72.650  104.544 1.00 123.38 ? 371 LEU A C     1 
ATOM   2668 O  O     . LEU A 1 344 ? 10.158  72.291  105.258 1.00 125.78 ? 371 LEU A O     1 
ATOM   2669 C  CB    . LEU A 1 344 ? 11.707  70.518  103.369 1.00 123.00 ? 371 LEU A CB    1 
ATOM   2670 C  CG    . LEU A 1 344 ? 11.293  70.854  101.938 1.00 131.67 ? 371 LEU A CG    1 
ATOM   2671 C  CD1   . LEU A 1 344 ? 12.447  71.511  101.194 1.00 126.53 ? 371 LEU A CD1   1 
ATOM   2672 C  CD2   . LEU A 1 344 ? 10.836  69.598  101.217 1.00 139.47 ? 371 LEU A CD2   1 
ATOM   2673 N  N     . VAL A 1 345 ? 11.200  73.875  104.037 1.00 118.03 ? 372 VAL A N     1 
ATOM   2674 C  CA    . VAL A 1 345 ? 10.159  74.884  104.181 1.00 119.64 ? 372 VAL A CA    1 
ATOM   2675 C  C     . VAL A 1 345 ? 9.513   75.083  102.818 1.00 131.41 ? 372 VAL A C     1 
ATOM   2676 O  O     . VAL A 1 345 ? 10.195  75.424  101.843 1.00 134.70 ? 372 VAL A O     1 
ATOM   2677 C  CB    . VAL A 1 345 ? 10.718  76.206  104.728 1.00 118.05 ? 372 VAL A CB    1 
ATOM   2678 C  CG1   . VAL A 1 345 ? 9.728   77.337  104.500 1.00 113.27 ? 372 VAL A CG1   1 
ATOM   2679 C  CG2   . VAL A 1 345 ? 11.030  76.069  106.205 1.00 114.83 ? 372 VAL A CG2   1 
ATOM   2680 N  N     . GLU A 1 346 ? 8.202   74.864  102.746 1.00 131.61 ? 373 GLU A N     1 
ATOM   2681 C  CA    . GLU A 1 346 ? 7.465   75.044  101.502 1.00 136.52 ? 373 GLU A CA    1 
ATOM   2682 C  C     . GLU A 1 346 ? 7.264   76.532  101.244 1.00 139.20 ? 373 GLU A C     1 
ATOM   2683 O  O     . GLU A 1 346 ? 6.718   77.248  102.091 1.00 136.29 ? 373 GLU A O     1 
ATOM   2684 C  CB    . GLU A 1 346 ? 6.124   74.317  101.566 1.00 146.26 ? 373 GLU A CB    1 
ATOM   2685 C  CG    . GLU A 1 346 ? 5.263   74.496  100.326 1.00 155.19 ? 373 GLU A CG    1 
ATOM   2686 C  CD    . GLU A 1 346 ? 3.950   73.742  100.414 1.00 165.02 ? 373 GLU A CD    1 
ATOM   2687 O  OE1   . GLU A 1 346 ? 3.900   72.714  101.122 1.00 168.28 ? 373 GLU A OE1   1 
ATOM   2688 O  OE2   . GLU A 1 346 ? 2.967   74.180  99.780  1.00 162.92 ? 373 GLU A OE2   1 
ATOM   2689 N  N     . ALA A 1 347 ? 7.705   76.996  100.078 1.00 142.79 ? 374 ALA A N     1 
ATOM   2690 C  CA    . ALA A 1 347 ? 7.618   78.409  99.749  1.00 144.17 ? 374 ALA A CA    1 
ATOM   2691 C  C     . ALA A 1 347 ? 6.171   78.822  99.497  1.00 154.60 ? 374 ALA A C     1 
ATOM   2692 O  O     . ALA A 1 347 ? 5.297   77.997  99.213  1.00 158.77 ? 374 ALA A O     1 
ATOM   2693 C  CB    . ALA A 1 347 ? 8.472   78.728  98.522  1.00 146.25 ? 374 ALA A CB    1 
ATOM   2694 N  N     . VAL A 1 348 ? 5.925   80.124  99.605  1.00 147.08 ? 375 VAL A N     1 
ATOM   2695 C  CA    . VAL A 1 348 ? 4.608   80.695  99.347  1.00 141.73 ? 375 VAL A CA    1 
ATOM   2696 C  C     . VAL A 1 348 ? 4.539   81.097  97.880  1.00 141.92 ? 375 VAL A C     1 
ATOM   2697 O  O     . VAL A 1 348 ? 5.274   81.985  97.437  1.00 146.80 ? 375 VAL A O     1 
ATOM   2698 C  CB    . VAL A 1 348 ? 4.335   81.900  100.260 1.00 139.19 ? 375 VAL A CB    1 
ATOM   2699 C  CG1   . VAL A 1 348 ? 2.965   82.491  99.964  1.00 138.92 ? 375 VAL A CG1   1 
ATOM   2700 C  CG2   . VAL A 1 348 ? 4.445   81.500  101.724 1.00 129.19 ? 375 VAL A CG2   1 
ATOM   2701 N  N     . ASP A 1 349 ? 3.658   80.442  97.123  1.00 136.13 ? 376 ASP A N     1 
ATOM   2702 C  CA    . ASP A 1 349 ? 3.488   80.768  95.711  1.00 141.47 ? 376 ASP A CA    1 
ATOM   2703 C  C     . ASP A 1 349 ? 2.793   82.116  95.563  1.00 154.28 ? 376 ASP A C     1 
ATOM   2704 O  O     . ASP A 1 349 ? 1.561   82.182  95.500  1.00 148.18 ? 376 ASP A O     1 
ATOM   2705 C  CB    . ASP A 1 349 ? 2.696   79.670  94.995  1.00 136.50 ? 376 ASP A CB    1 
ATOM   2706 C  CG    . ASP A 1 349 ? 2.701   79.832  93.485  1.00 148.90 ? 376 ASP A CG    1 
ATOM   2707 O  OD1   . ASP A 1 349 ? 3.432   80.710  92.977  1.00 151.71 ? 376 ASP A OD1   1 
ATOM   2708 O  OD2   . ASP A 1 349 ? 1.976   79.077  92.803  1.00 150.98 ? 376 ASP A OD2   1 
ATOM   2709 N  N     . GLY A 1 350 ? 3.576   83.195  95.507  1.00 162.27 ? 377 GLY A N     1 
ATOM   2710 C  CA    . GLY A 1 350 ? 3.022   84.532  95.362  1.00 163.08 ? 377 GLY A CA    1 
ATOM   2711 C  C     . GLY A 1 350 ? 2.306   84.771  94.051  1.00 161.27 ? 377 GLY A C     1 
ATOM   2712 O  O     . GLY A 1 350 ? 1.701   85.836  93.879  1.00 162.70 ? 377 GLY A O     1 
ATOM   2713 N  N     . LYS A 1 351 ? 2.362   83.814  93.126  1.00 163.24 ? 378 LYS A N     1 
ATOM   2714 C  CA    . LYS A 1 351 ? 1.636   83.909  91.869  1.00 169.41 ? 378 LYS A CA    1 
ATOM   2715 C  C     . LYS A 1 351 ? 0.240   83.308  91.960  1.00 168.86 ? 378 LYS A C     1 
ATOM   2716 O  O     . LYS A 1 351 ? -0.654  83.720  91.211  1.00 169.76 ? 378 LYS A O     1 
ATOM   2717 C  CB    . LYS A 1 351 ? 2.434   83.218  90.759  1.00 164.90 ? 378 LYS A CB    1 
ATOM   2718 C  CG    . LYS A 1 351 ? 3.896   83.645  90.717  1.00 163.08 ? 378 LYS A CG    1 
ATOM   2719 C  CD    . LYS A 1 351 ? 4.721   82.770  89.788  1.00 159.01 ? 378 LYS A CD    1 
ATOM   2720 C  CE    . LYS A 1 351 ? 6.192   83.159  89.837  1.00 152.32 ? 378 LYS A CE    1 
ATOM   2721 N  NZ    . LYS A 1 351 ? 7.035   82.309  88.949  1.00 158.15 ? 378 LYS A NZ    1 
ATOM   2722 N  N     . ALA A 1 352 ? 0.031   82.355  92.867  1.00 165.26 ? 379 ALA A N     1 
ATOM   2723 C  CA    . ALA A 1 352 ? -1.269  81.730  93.073  1.00 161.48 ? 379 ALA A CA    1 
ATOM   2724 C  C     . ALA A 1 352 ? -2.148  82.505  94.047  1.00 164.72 ? 379 ALA A C     1 
ATOM   2725 O  O     . ALA A 1 352 ? -3.198  81.998  94.455  1.00 160.05 ? 379 ALA A O     1 
ATOM   2726 C  CB    . ALA A 1 352 ? -1.089  80.292  93.567  1.00 148.78 ? 379 ALA A CB    1 
ATOM   2727 N  N     . MET A 1 353 ? -1.745  83.715  94.427  1.00 177.43 ? 380 MET A N     1 
ATOM   2728 C  CA    . MET A 1 353 ? -2.512  84.552  95.341  1.00 180.61 ? 380 MET A CA    1 
ATOM   2729 C  C     . MET A 1 353 ? -3.329  85.551  94.534  1.00 178.61 ? 380 MET A C     1 
ATOM   2730 O  O     . MET A 1 353 ? -2.774  86.303  93.725  1.00 179.12 ? 380 MET A O     1 
ATOM   2731 C  CB    . MET A 1 353 ? -1.591  85.286  96.316  1.00 187.52 ? 380 MET A CB    1 
ATOM   2732 C  CG    . MET A 1 353 ? -0.825  84.384  97.266  1.00 185.06 ? 380 MET A CG    1 
ATOM   2733 S  SD    . MET A 1 353 ? 0.313   85.315  98.313  1.00 170.82 ? 380 MET A SD    1 
ATOM   2734 C  CE    . MET A 1 353 ? -0.812  86.465  99.100  1.00 171.08 ? 380 MET A CE    1 
ATOM   2735 N  N     . ASN A 1 354 ? -4.640  85.558  94.754  1.00 166.42 ? 381 ASN A N     1 
ATOM   2736 C  CA    . ASN A 1 354 ? -5.493  86.547  94.118  1.00 173.75 ? 381 ASN A CA    1 
ATOM   2737 C  C     . ASN A 1 354 ? -5.319  87.907  94.795  1.00 181.06 ? 381 ASN A C     1 
ATOM   2738 O  O     . ASN A 1 354 ? -4.626  88.048  95.808  1.00 175.50 ? 381 ASN A O     1 
ATOM   2739 C  CB    . ASN A 1 354 ? -6.955  86.099  94.156  1.00 169.84 ? 381 ASN A CB    1 
ATOM   2740 C  CG    . ASN A 1 354 ? -7.351  85.507  95.495  1.00 163.19 ? 381 ASN A CG    1 
ATOM   2741 O  OD1   . ASN A 1 354 ? -7.855  86.207  96.372  1.00 160.64 ? 381 ASN A OD1   1 
ATOM   2742 N  ND2   . ASN A 1 354 ? -7.126  84.207  95.657  1.00 153.97 ? 381 ASN A ND2   1 
ATOM   2743 N  N     . THR A 1 355 ? -5.960  88.925  94.214  1.00 191.36 ? 382 THR A N     1 
ATOM   2744 C  CA    . THR A 1 355 ? -5.837  90.281  94.738  1.00 195.92 ? 382 THR A CA    1 
ATOM   2745 C  C     . THR A 1 355 ? -6.435  90.417  96.134  1.00 200.68 ? 382 THR A C     1 
ATOM   2746 O  O     . THR A 1 355 ? -6.083  91.354  96.860  1.00 200.00 ? 382 THR A O     1 
ATOM   2747 C  CB    . THR A 1 355 ? -6.503  91.273  93.780  1.00 194.94 ? 382 THR A CB    1 
ATOM   2748 O  OG1   . THR A 1 355 ? -6.206  90.902  92.429  1.00 198.86 ? 382 THR A OG1   1 
ATOM   2749 C  CG2   . THR A 1 355 ? -5.990  92.686  94.025  1.00 193.29 ? 382 THR A CG2   1 
ATOM   2750 N  N     . SER A 1 356 ? -7.320  89.499  96.531  1.00 197.14 ? 383 SER A N     1 
ATOM   2751 C  CA    . SER A 1 356 ? -7.931  89.573  97.854  1.00 191.59 ? 383 SER A CA    1 
ATOM   2752 C  C     . SER A 1 356 ? -6.977  89.100  98.946  1.00 189.68 ? 383 SER A C     1 
ATOM   2753 O  O     . SER A 1 356 ? -6.876  89.735  100.001 1.00 185.03 ? 383 SER A O     1 
ATOM   2754 C  CB    . SER A 1 356 ? -9.221  88.753  97.880  1.00 190.35 ? 383 SER A CB    1 
ATOM   2755 O  OG    . SER A 1 356 ? -10.138 89.213  96.902  1.00 192.80 ? 383 SER A OG    1 
ATOM   2756 N  N     . GLN A 1 357 ? -6.274  87.988  98.716  1.00 186.06 ? 384 GLN A N     1 
ATOM   2757 C  CA    . GLN A 1 357 ? -5.352  87.470  99.720  1.00 174.00 ? 384 GLN A CA    1 
ATOM   2758 C  C     . GLN A 1 357 ? -4.109  88.338  99.874  1.00 176.65 ? 384 GLN A C     1 
ATOM   2759 O  O     . GLN A 1 357 ? -3.486  88.317  100.941 1.00 168.36 ? 384 GLN A O     1 
ATOM   2760 C  CB    . GLN A 1 357 ? -4.954  86.034  99.374  1.00 162.02 ? 384 GLN A CB    1 
ATOM   2761 C  CG    . GLN A 1 357 ? -6.088  85.032  99.521  1.00 159.49 ? 384 GLN A CG    1 
ATOM   2762 C  CD    . GLN A 1 357 ? -5.696  83.638  99.076  1.00 151.47 ? 384 GLN A CD    1 
ATOM   2763 O  OE1   . GLN A 1 357 ? -4.828  83.469  98.222  1.00 157.23 ? 384 GLN A OE1   1 
ATOM   2764 N  NE2   . GLN A 1 357 ? -6.335  82.630  99.658  1.00 144.98 ? 384 GLN A NE2   1 
ATOM   2765 N  N     . VAL A 1 358 ? -3.734  89.093  98.838  1.00 183.77 ? 385 VAL A N     1 
ATOM   2766 C  CA    . VAL A 1 358 ? -2.620  90.032  98.962  1.00 178.94 ? 385 VAL A CA    1 
ATOM   2767 C  C     . VAL A 1 358 ? -2.950  91.107  99.989  1.00 179.65 ? 385 VAL A C     1 
ATOM   2768 O  O     . VAL A 1 358 ? -2.138  91.429  100.865 1.00 168.03 ? 385 VAL A O     1 
ATOM   2769 C  CB    . VAL A 1 358 ? -2.279  90.648  97.592  1.00 173.31 ? 385 VAL A CB    1 
ATOM   2770 C  CG1   . VAL A 1 358 ? -1.315  91.815  97.758  1.00 165.23 ? 385 VAL A CG1   1 
ATOM   2771 C  CG2   . VAL A 1 358 ? -1.691  89.595  96.668  1.00 177.07 ? 385 VAL A CG2   1 
ATOM   2772 N  N     . GLU A 1 359 ? -4.153  91.679  99.894  1.00 190.57 ? 386 GLU A N     1 
ATOM   2773 C  CA    . GLU A 1 359 ? -4.596  92.665  100.871 1.00 188.32 ? 386 GLU A CA    1 
ATOM   2774 C  C     . GLU A 1 359 ? -4.895  92.040  102.227 1.00 184.46 ? 386 GLU A C     1 
ATOM   2775 O  O     . GLU A 1 359 ? -4.909  92.756  103.233 1.00 178.73 ? 386 GLU A O     1 
ATOM   2776 C  CB    . GLU A 1 359 ? -5.838  93.394  100.356 1.00 191.79 ? 386 GLU A CB    1 
ATOM   2777 C  CG    . GLU A 1 359 ? -5.656  94.063  99.006  1.00 192.03 ? 386 GLU A CG    1 
ATOM   2778 C  CD    . GLU A 1 359 ? -6.956  94.607  98.450  1.00 195.24 ? 386 GLU A CD    1 
ATOM   2779 O  OE1   . GLU A 1 359 ? -8.018  94.349  99.056  1.00 192.68 ? 386 GLU A OE1   1 
ATOM   2780 O  OE2   . GLU A 1 359 ? -6.916  95.291  97.407  1.00 205.35 ? 386 GLU A OE2   1 
ATOM   2781 N  N     . ALA A 1 360 ? -5.139  90.727  102.276 1.00 183.84 ? 387 ALA A N     1 
ATOM   2782 C  CA    . ALA A 1 360 ? -5.432  90.068  103.543 1.00 179.67 ? 387 ALA A CA    1 
ATOM   2783 C  C     . ALA A 1 360 ? -4.239  90.086  104.487 1.00 172.03 ? 387 ALA A C     1 
ATOM   2784 O  O     . ALA A 1 360 ? -4.420  89.968  105.704 1.00 163.07 ? 387 ALA A O     1 
ATOM   2785 C  CB    . ALA A 1 360 ? -5.879  88.625  103.295 1.00 175.62 ? 387 ALA A CB    1 
ATOM   2786 N  N     . LEU A 1 361 ? -3.029  90.233  103.955 1.00 171.14 ? 388 LEU A N     1 
ATOM   2787 C  CA    . LEU A 1 361 ? -1.814  90.251  104.753 1.00 168.04 ? 388 LEU A CA    1 
ATOM   2788 C  C     . LEU A 1 361 ? -1.319  91.661  105.042 1.00 171.74 ? 388 LEU A C     1 
ATOM   2789 O  O     . LEU A 1 361 ? -0.341  91.821  105.780 1.00 173.34 ? 388 LEU A O     1 
ATOM   2790 C  CB    . LEU A 1 361 ? -0.717  89.451  104.043 1.00 163.84 ? 388 LEU A CB    1 
ATOM   2791 C  CG    . LEU A 1 361 ? -1.182  88.175  103.335 1.00 158.74 ? 388 LEU A CG    1 
ATOM   2792 C  CD1   . LEU A 1 361 ? -0.024  87.522  102.604 1.00 154.12 ? 388 LEU A CD1   1 
ATOM   2793 C  CD2   . LEU A 1 361 ? -1.826  87.196  104.309 1.00 149.12 ? 388 LEU A CD2   1 
ATOM   2794 N  N     . GLY A 1 362 ? -1.967  92.682  104.484 1.00 171.76 ? 389 GLY A N     1 
ATOM   2795 C  CA    . GLY A 1 362 ? -1.530  94.052  104.666 1.00 171.74 ? 389 GLY A CA    1 
ATOM   2796 C  C     . GLY A 1 362 ? -0.259  94.351  103.901 1.00 174.83 ? 389 GLY A C     1 
ATOM   2797 O  O     . GLY A 1 362 ? 0.732   94.808  104.480 1.00 172.88 ? 389 GLY A O     1 
ATOM   2798 N  N     . ILE A 1 363 ? -0.277  94.097  102.595 1.00 172.13 ? 390 ILE A N     1 
ATOM   2799 C  CA    . ILE A 1 363 ? 0.903   94.214  101.746 1.00 173.34 ? 390 ILE A CA    1 
ATOM   2800 C  C     . ILE A 1 363 ? 0.681   95.358  100.765 1.00 173.38 ? 390 ILE A C     1 
ATOM   2801 O  O     . ILE A 1 363 ? -0.311  95.371  100.026 1.00 169.19 ? 390 ILE A O     1 
ATOM   2802 C  CB    . ILE A 1 363 ? 1.200   92.902  101.005 1.00 166.18 ? 390 ILE A CB    1 
ATOM   2803 C  CG1   . ILE A 1 363 ? 1.453   91.774  102.007 1.00 156.93 ? 390 ILE A CG1   1 
ATOM   2804 C  CG2   . ILE A 1 363 ? 2.394   93.072  100.079 1.00 165.25 ? 390 ILE A CG2   1 
ATOM   2805 C  CD1   . ILE A 1 363 ? 1.790   90.453  101.362 1.00 151.17 ? 390 ILE A CD1   1 
ATOM   2806 N  N     . GLN A 1 364 ? 1.607   96.315  100.762 1.00 181.17 ? 391 GLN A N     1 
ATOM   2807 C  CA    . GLN A 1 364 ? 1.601   97.429  99.824  1.00 185.47 ? 391 GLN A CA    1 
ATOM   2808 C  C     . GLN A 1 364 ? 3.011   97.626  99.290  1.00 181.07 ? 391 GLN A C     1 
ATOM   2809 O  O     . GLN A 1 364 ? 3.970   97.671  100.068 1.00 175.16 ? 391 GLN A O     1 
ATOM   2810 C  CB    . GLN A 1 364 ? 1.101   98.719  100.483 1.00 173.15 ? 391 GLN A CB    1 
ATOM   2811 C  CG    . GLN A 1 364 ? 1.347   99.963  99.645  1.00 173.39 ? 391 GLN A CG    1 
ATOM   2812 C  CD    . GLN A 1 364 ? 1.012   101.239 100.384 1.00 183.87 ? 391 GLN A CD    1 
ATOM   2813 O  OE1   . GLN A 1 364 ? 0.085   101.277 101.191 1.00 185.01 ? 391 GLN A OE1   1 
ATOM   2814 N  NE2   . GLN A 1 364 ? 1.773   102.295 100.115 1.00 193.36 ? 391 GLN A NE2   1 
ATOM   2815 N  N     . MET A 1 365 ? 3.135   97.734  97.969  1.00 174.88 ? 392 MET A N     1 
ATOM   2816 C  CA    . MET A 1 365 ? 4.440   97.949  97.360  1.00 171.51 ? 392 MET A CA    1 
ATOM   2817 C  C     . MET A 1 365 ? 5.008   99.292  97.799  1.00 173.43 ? 392 MET A C     1 
ATOM   2818 O  O     . MET A 1 365 ? 4.273   100.271 97.963  1.00 175.12 ? 392 MET A O     1 
ATOM   2819 C  CB    . MET A 1 365 ? 4.334   97.898  95.835  1.00 161.08 ? 392 MET A CB    1 
ATOM   2820 C  CG    . MET A 1 365 ? 5.678   97.892  95.122  1.00 174.98 ? 392 MET A CG    1 
ATOM   2821 S  SD    . MET A 1 365 ? 5.551   98.263  93.361  1.00 177.38 ? 392 MET A SD    1 
ATOM   2822 C  CE    . MET A 1 365 ? 5.054   99.983  93.413  1.00 173.02 ? 392 MET A CE    1 
ATOM   2823 N  N     . LEU A 1 366 ? 6.321   99.330  98.006  1.00 163.66 ? 393 LEU A N     1 
ATOM   2824 C  CA    . LEU A 1 366 ? 7.001   100.575 98.330  1.00 161.83 ? 393 LEU A CA    1 
ATOM   2825 C  C     . LEU A 1 366 ? 6.722   101.595 97.231  1.00 173.27 ? 393 LEU A C     1 
ATOM   2826 O  O     . LEU A 1 366 ? 6.968   101.303 96.050  1.00 174.38 ? 393 LEU A O     1 
ATOM   2827 C  CB    . LEU A 1 366 ? 8.505   100.346 98.488  1.00 158.15 ? 393 LEU A CB    1 
ATOM   2828 C  CG    . LEU A 1 366 ? 9.371   101.515 98.971  1.00 159.66 ? 393 LEU A CG    1 
ATOM   2829 C  CD1   . LEU A 1 366 ? 10.521  101.002 99.818  1.00 149.11 ? 393 LEU A CD1   1 
ATOM   2830 C  CD2   . LEU A 1 366 ? 9.909   102.326 97.802  1.00 167.03 ? 393 LEU A CD2   1 
ATOM   2831 N  N     . PRO A 1 367 ? 6.199   102.774 97.561  1.00 175.80 ? 394 PRO A N     1 
ATOM   2832 C  CA    . PRO A 1 367 ? 5.824   103.742 96.518  1.00 177.56 ? 394 PRO A CA    1 
ATOM   2833 C  C     . PRO A 1 367 ? 7.028   104.169 95.693  1.00 183.02 ? 394 PRO A C     1 
ATOM   2834 O  O     . PRO A 1 367 ? 8.019   104.679 96.221  1.00 182.12 ? 394 PRO A O     1 
ATOM   2835 C  CB    . PRO A 1 367 ? 5.239   104.912 97.319  1.00 173.10 ? 394 PRO A CB    1 
ATOM   2836 C  CG    . PRO A 1 367 ? 4.833   104.316 98.629  1.00 171.17 ? 394 PRO A CG    1 
ATOM   2837 C  CD    . PRO A 1 367 ? 5.841   103.245 98.910  1.00 165.48 ? 394 PRO A CD    1 
ATOM   2838 N  N     . GLY A 1 368 ? 6.937   103.946 94.383  1.00 182.30 ? 395 GLY A N     1 
ATOM   2839 C  CA    . GLY A 1 368 ? 7.951   104.387 93.450  1.00 178.90 ? 395 GLY A CA    1 
ATOM   2840 C  C     . GLY A 1 368 ? 8.945   103.332 93.017  1.00 181.66 ? 395 GLY A C     1 
ATOM   2841 O  O     . GLY A 1 368 ? 9.864   103.655 92.254  1.00 181.14 ? 395 GLY A O     1 
ATOM   2842 N  N     . TYR A 1 369 ? 8.801   102.090 93.472  1.00 186.92 ? 396 TYR A N     1 
ATOM   2843 C  CA    . TYR A 1 369 ? 9.766   101.064 93.104  1.00 177.75 ? 396 TYR A CA    1 
ATOM   2844 C  C     . TYR A 1 369 ? 9.547   100.608 91.668  1.00 181.00 ? 396 TYR A C     1 
ATOM   2845 O  O     . TYR A 1 369 ? 8.412   100.398 91.228  1.00 183.18 ? 396 TYR A O     1 
ATOM   2846 C  CB    . TYR A 1 369 ? 9.680   99.857  94.038  1.00 178.07 ? 396 TYR A CB    1 
ATOM   2847 C  CG    . TYR A 1 369 ? 10.399  98.648  93.474  1.00 177.97 ? 396 TYR A CG    1 
ATOM   2848 C  CD1   . TYR A 1 369 ? 11.788  98.583  93.467  1.00 175.53 ? 396 TYR A CD1   1 
ATOM   2849 C  CD2   . TYR A 1 369 ? 9.690   97.586  92.923  1.00 179.91 ? 396 TYR A CD2   1 
ATOM   2850 C  CE1   . TYR A 1 369 ? 12.448  97.490  92.941  1.00 174.95 ? 396 TYR A CE1   1 
ATOM   2851 C  CE2   . TYR A 1 369 ? 10.343  96.491  92.395  1.00 178.58 ? 396 TYR A CE2   1 
ATOM   2852 C  CZ    . TYR A 1 369 ? 11.721  96.449  92.405  1.00 176.13 ? 396 TYR A CZ    1 
ATOM   2853 O  OH    . TYR A 1 369 ? 12.376  95.361  91.880  1.00 173.24 ? 396 TYR A OH    1 
ATOM   2854 N  N     . ARG A 1 370 ? 10.649  100.458 90.939  1.00 169.19 ? 397 ARG A N     1 
ATOM   2855 C  CA    . ARG A 1 370 ? 10.645  99.839  89.623  1.00 169.08 ? 397 ARG A CA    1 
ATOM   2856 C  C     . ARG A 1 370 ? 11.923  99.028  89.468  1.00 168.64 ? 397 ARG A C     1 
ATOM   2857 O  O     . ARG A 1 370 ? 12.931  99.289  90.129  1.00 166.35 ? 397 ARG A O     1 
ATOM   2858 C  CB    . ARG A 1 370 ? 10.529  100.875 88.497  1.00 161.41 ? 397 ARG A CB    1 
ATOM   2859 C  CG    . ARG A 1 370 ? 9.153   101.502 88.357  1.00 154.01 ? 397 ARG A CG    1 
ATOM   2860 C  CD    . ARG A 1 370 ? 9.126   102.521 87.233  1.00 158.57 ? 397 ARG A CD    1 
ATOM   2861 N  NE    . ARG A 1 370 ? 8.074   103.514 87.418  1.00 162.54 ? 397 ARG A NE    1 
ATOM   2862 C  CZ    . ARG A 1 370 ? 7.979   104.638 86.721  1.00 166.99 ? 397 ARG A CZ    1 
ATOM   2863 N  NH1   . ARG A 1 370 ? 8.852   104.939 85.774  1.00 168.13 ? 397 ARG A NH1   1 
ATOM   2864 N  NH2   . ARG A 1 370 ? 6.987   105.484 86.985  1.00 170.70 ? 397 ARG A NH2   1 
ATOM   2865 N  N     . ASP A 1 371 ? 11.869  98.045  88.576  1.00 193.24 ? 398 ASP A N     1 
ATOM   2866 C  CA    . ASP A 1 371 ? 13.014  97.175  88.344  1.00 192.92 ? 398 ASP A CA    1 
ATOM   2867 C  C     . ASP A 1 371 ? 14.161  97.964  87.723  1.00 193.59 ? 398 ASP A C     1 
ATOM   2868 O  O     . ASP A 1 371 ? 13.949  98.704  86.749  1.00 195.77 ? 398 ASP A O     1 
ATOM   2869 C  CB    . ASP A 1 371 ? 12.617  96.013  87.441  1.00 194.08 ? 398 ASP A CB    1 
ATOM   2870 C  CG    . ASP A 1 371 ? 13.806  95.199  86.980  1.00 195.95 ? 398 ASP A CG    1 
ATOM   2871 O  OD1   . ASP A 1 371 ? 14.514  94.630  87.836  1.00 200.89 ? 398 ASP A OD1   1 
ATOM   2872 O  OD2   . ASP A 1 371 ? 14.030  95.129  85.755  1.00 199.29 ? 398 ASP A OD2   1 
ATOM   2873 N  N     . PRO A 1 372 ? 15.379  97.837  88.251  1.00 183.73 ? 399 PRO A N     1 
ATOM   2874 C  CA    . PRO A 1 372 ? 16.533  98.539  87.677  1.00 184.57 ? 399 PRO A CA    1 
ATOM   2875 C  C     . PRO A 1 372 ? 17.028  97.981  86.351  1.00 189.27 ? 399 PRO A C     1 
ATOM   2876 O  O     . PRO A 1 372 ? 18.101  98.390  85.897  1.00 181.54 ? 399 PRO A O     1 
ATOM   2877 C  CB    . PRO A 1 372 ? 17.613  98.370  88.759  1.00 181.20 ? 399 PRO A CB    1 
ATOM   2878 C  CG    . PRO A 1 372 ? 16.872  97.940  90.005  1.00 169.06 ? 399 PRO A CG    1 
ATOM   2879 C  CD    . PRO A 1 372 ? 15.696  97.176  89.527  1.00 173.48 ? 399 PRO A CD    1 
ATOM   2880 N  N     . TYR A 1 373 ? 16.292  97.072  85.711  1.00 201.43 ? 400 TYR A N     1 
ATOM   2881 C  CA    . TYR A 1 373 ? 16.749  96.463  84.465  1.00 201.60 ? 400 TYR A CA    1 
ATOM   2882 C  C     . TYR A 1 373 ? 15.761  96.681  83.326  1.00 199.33 ? 400 TYR A C     1 
ATOM   2883 O  O     . TYR A 1 373 ? 16.137  97.254  82.299  1.00 195.52 ? 400 TYR A O     1 
ATOM   2884 C  CB    . TYR A 1 373 ? 17.020  94.967  84.672  1.00 200.12 ? 400 TYR A CB    1 
ATOM   2885 C  CG    . TYR A 1 373 ? 18.110  94.688  85.686  1.00 199.57 ? 400 TYR A CG    1 
ATOM   2886 C  CD1   . TYR A 1 373 ? 19.443  94.967  85.399  1.00 196.39 ? 400 TYR A CD1   1 
ATOM   2887 C  CD2   . TYR A 1 373 ? 17.809  94.144  86.928  1.00 196.11 ? 400 TYR A CD2   1 
ATOM   2888 C  CE1   . TYR A 1 373 ? 20.443  94.715  86.322  1.00 193.08 ? 400 TYR A CE1   1 
ATOM   2889 C  CE2   . TYR A 1 373 ? 18.803  93.887  87.857  1.00 193.76 ? 400 TYR A CE2   1 
ATOM   2890 C  CZ    . TYR A 1 373 ? 20.118  94.175  87.549  1.00 197.40 ? 400 TYR A CZ    1 
ATOM   2891 O  OH    . TYR A 1 373 ? 21.118  93.926  88.462  1.00 195.93 ? 400 TYR A OH    1 
ATOM   2892 N  N     . HIS A 1 374 ? 14.507  96.239  83.468  1.00 196.68 ? 401 HIS A N     1 
ATOM   2893 C  CA    . HIS A 1 374 ? 13.484  96.475  82.452  1.00 190.98 ? 401 HIS A CA    1 
ATOM   2894 C  C     . HIS A 1 374 ? 12.351  97.361  82.966  1.00 189.72 ? 401 HIS A C     1 
ATOM   2895 O  O     . HIS A 1 374 ? 11.289  97.429  82.339  1.00 187.51 ? 401 HIS A O     1 
ATOM   2896 C  CB    . HIS A 1 374 ? 12.929  95.154  81.906  1.00 187.33 ? 401 HIS A CB    1 
ATOM   2897 C  CG    . HIS A 1 374 ? 12.826  94.059  82.924  1.00 187.71 ? 401 HIS A CG    1 
ATOM   2898 N  ND1   . HIS A 1 374 ? 12.046  94.161  84.056  1.00 187.45 ? 401 HIS A ND1   1 
ATOM   2899 C  CD2   . HIS A 1 374 ? 13.392  92.830  82.967  1.00 180.24 ? 401 HIS A CD2   1 
ATOM   2900 C  CE1   . HIS A 1 374 ? 12.141  93.044  84.755  1.00 178.06 ? 401 HIS A CE1   1 
ATOM   2901 N  NE2   . HIS A 1 374 ? 12.953  92.221  84.117  1.00 181.65 ? 401 HIS A NE2   1 
ATOM   2902 N  N     . GLY A 1 375 ? 12.554  98.039  84.094  1.00 198.42 ? 402 GLY A N     1 
ATOM   2903 C  CA    . GLY A 1 375 ? 11.626  99.063  84.538  1.00 197.45 ? 402 GLY A CA    1 
ATOM   2904 C  C     . GLY A 1 375 ? 10.271  98.581  85.005  1.00 192.36 ? 402 GLY A C     1 
ATOM   2905 O  O     . GLY A 1 375 ? 9.311   99.357  84.983  1.00 189.14 ? 402 GLY A O     1 
ATOM   2906 N  N     . ARG A 1 376 ? 10.161  97.325  85.440  1.00 184.20 ? 403 ARG A N     1 
ATOM   2907 C  CA    . ARG A 1 376 ? 8.843   96.892  85.878  1.00 178.94 ? 403 ARG A CA    1 
ATOM   2908 C  C     . ARG A 1 376 ? 8.692   97.056  87.387  1.00 176.85 ? 403 ARG A C     1 
ATOM   2909 O  O     . ARG A 1 376 ? 9.677   96.983  88.129  1.00 179.42 ? 403 ARG A O     1 
ATOM   2910 C  CB    . ARG A 1 376 ? 8.610   95.431  85.502  1.00 172.78 ? 403 ARG A CB    1 
ATOM   2911 C  CG    . ARG A 1 376 ? 8.745   95.143  84.018  1.00 177.38 ? 403 ARG A CG    1 
ATOM   2912 C  CD    . ARG A 1 376 ? 8.826   93.649  83.755  1.00 178.56 ? 403 ARG A CD    1 
ATOM   2913 N  NE    . ARG A 1 376 ? 9.260   93.363  82.393  1.00 184.51 ? 403 ARG A NE    1 
ATOM   2914 C  CZ    . ARG A 1 376 ? 9.758   92.200  81.994  1.00 180.98 ? 403 ARG A CZ    1 
ATOM   2915 N  NH1   . ARG A 1 376 ? 9.908   91.188  82.834  1.00 177.85 ? 403 ARG A NH1   1 
ATOM   2916 N  NH2   . ARG A 1 376 ? 10.121  92.051  80.724  1.00 180.39 ? 403 ARG A NH2   1 
ATOM   2917 N  N     . PRO A 1 377 ? 7.469   97.285  87.871  1.00 165.59 ? 404 PRO A N     1 
ATOM   2918 C  CA    . PRO A 1 377 ? 7.247   97.316  89.323  1.00 169.40 ? 404 PRO A CA    1 
ATOM   2919 C  C     . PRO A 1 377 ? 7.433   95.948  89.964  1.00 175.22 ? 404 PRO A C     1 
ATOM   2920 O  O     . PRO A 1 377 ? 7.869   94.999  89.303  1.00 172.55 ? 404 PRO A O     1 
ATOM   2921 C  CB    . PRO A 1 377 ? 5.797   97.803  89.447  1.00 163.33 ? 404 PRO A CB    1 
ATOM   2922 C  CG    . PRO A 1 377 ? 5.505   98.483  88.147  1.00 161.86 ? 404 PRO A CG    1 
ATOM   2923 C  CD    . PRO A 1 377 ? 6.279   97.717  87.121  1.00 164.56 ? 404 PRO A CD    1 
ATOM   2924 N  N     . LEU A 1 378 ? 7.104   95.836  91.250  1.00 176.44 ? 405 LEU A N     1 
ATOM   2925 C  CA    . LEU A 1 378 ? 7.247   94.566  91.950  1.00 173.94 ? 405 LEU A CA    1 
ATOM   2926 C  C     . LEU A 1 378 ? 6.325   93.515  91.341  1.00 173.54 ? 405 LEU A C     1 
ATOM   2927 O  O     . LEU A 1 378 ? 5.169   93.794  91.013  1.00 166.89 ? 405 LEU A O     1 
ATOM   2928 C  CB    . LEU A 1 378 ? 6.935   94.745  93.437  1.00 174.19 ? 405 LEU A CB    1 
ATOM   2929 C  CG    . LEU A 1 378 ? 7.160   93.531  94.341  1.00 170.41 ? 405 LEU A CG    1 
ATOM   2930 C  CD1   . LEU A 1 378 ? 8.643   93.247  94.504  1.00 165.79 ? 405 LEU A CD1   1 
ATOM   2931 C  CD2   . LEU A 1 378 ? 6.501   93.738  95.692  1.00 168.37 ? 405 LEU A CD2   1 
ATOM   2932 N  N     . THR A 1 379 ? 6.845   92.301  91.190  1.00 172.47 ? 406 THR A N     1 
ATOM   2933 C  CA    . THR A 1 379 ? 6.126   91.212  90.544  1.00 170.00 ? 406 THR A CA    1 
ATOM   2934 C  C     . THR A 1 379 ? 5.517   90.273  91.581  1.00 155.54 ? 406 THR A C     1 
ATOM   2935 O  O     . THR A 1 379 ? 5.890   90.276  92.756  1.00 153.13 ? 406 THR A O     1 
ATOM   2936 C  CB    . THR A 1 379 ? 7.052   90.425  89.611  1.00 162.56 ? 406 THR A CB    1 
ATOM   2937 O  OG1   . THR A 1 379 ? 7.981   89.662  90.389  1.00 157.23 ? 406 THR A OG1   1 
ATOM   2938 C  CG2   . THR A 1 379 ? 7.824   91.371  88.701  1.00 158.19 ? 406 THR A CG2   1 
ATOM   2939 N  N     . LYS A 1 380 ? 4.564   89.457  91.119  1.00 143.39 ? 407 LYS A N     1 
ATOM   2940 C  CA    . LYS A 1 380 ? 3.917   88.497  92.008  1.00 140.66 ? 407 LYS A CA    1 
ATOM   2941 C  C     . LYS A 1 380 ? 4.883   87.414  92.468  1.00 148.38 ? 407 LYS A C     1 
ATOM   2942 O  O     . LYS A 1 380 ? 4.767   86.921  93.596  1.00 148.89 ? 407 LYS A O     1 
ATOM   2943 C  CB    . LYS A 1 380 ? 2.710   87.866  91.320  1.00 136.35 ? 407 LYS A CB    1 
ATOM   2944 C  CG    . LYS A 1 380 ? 1.419   88.638  91.510  1.00 138.15 ? 407 LYS A CG    1 
ATOM   2945 C  CD    . LYS A 1 380 ? 0.243   87.873  90.933  1.00 139.47 ? 407 LYS A CD    1 
ATOM   2946 C  CE    . LYS A 1 380 ? -1.071  88.542  91.285  1.00 142.50 ? 407 LYS A CE    1 
ATOM   2947 N  NZ    . LYS A 1 380 ? -2.229  87.806  90.708  1.00 157.03 ? 407 LYS A NZ    1 
ATOM   2948 N  N     . GLY A 1 381 ? 5.829   87.021  91.613  1.00 158.50 ? 408 GLY A N     1 
ATOM   2949 C  CA    . GLY A 1 381 ? 6.842   86.070  92.042  1.00 158.40 ? 408 GLY A CA    1 
ATOM   2950 C  C     . GLY A 1 381 ? 7.728   86.630  93.138  1.00 156.02 ? 408 GLY A C     1 
ATOM   2951 O  O     . GLY A 1 381 ? 8.032   85.944  94.117  1.00 153.71 ? 408 GLY A O     1 
ATOM   2952 N  N     . GLU A 1 382 ? 8.145   87.890  92.993  1.00 156.14 ? 409 GLU A N     1 
ATOM   2953 C  CA    . GLU A 1 382 ? 8.921   88.559  94.030  1.00 153.04 ? 409 GLU A CA    1 
ATOM   2954 C  C     . GLU A 1 382 ? 8.106   88.832  95.286  1.00 160.57 ? 409 GLU A C     1 
ATOM   2955 O  O     . GLU A 1 382 ? 8.685   89.215  96.308  1.00 159.93 ? 409 GLU A O     1 
ATOM   2956 C  CB    . GLU A 1 382 ? 9.498   89.871  93.491  1.00 151.94 ? 409 GLU A CB    1 
ATOM   2957 C  CG    . GLU A 1 382 ? 10.536  89.692  92.393  1.00 150.14 ? 409 GLU A CG    1 
ATOM   2958 C  CD    . GLU A 1 382 ? 10.994  91.010  91.795  1.00 150.73 ? 409 GLU A CD    1 
ATOM   2959 O  OE1   . GLU A 1 382 ? 10.224  91.993  91.852  1.00 160.09 ? 409 GLU A OE1   1 
ATOM   2960 O  OE2   . GLU A 1 382 ? 12.126  91.061  91.270  1.00 138.56 ? 409 GLU A OE2   1 
ATOM   2961 N  N     . LEU A 1 383 ? 6.786   88.648  95.233  1.00 161.55 ? 410 LEU A N     1 
ATOM   2962 C  CA    . LEU A 1 383 ? 5.949   88.817  96.416  1.00 164.38 ? 410 LEU A CA    1 
ATOM   2963 C  C     . LEU A 1 383 ? 6.030   87.594  97.326  1.00 160.93 ? 410 LEU A C     1 
ATOM   2964 O  O     . LEU A 1 383 ? 6.410   87.699  98.498  1.00 154.27 ? 410 LEU A O     1 
ATOM   2965 C  CB    . LEU A 1 383 ? 4.500   89.086  95.993  1.00 162.85 ? 410 LEU A CB    1 
ATOM   2966 C  CG    . LEU A 1 383 ? 3.411   88.918  97.057  1.00 158.62 ? 410 LEU A CG    1 
ATOM   2967 C  CD1   . LEU A 1 383 ? 3.556   89.958  98.153  1.00 157.52 ? 410 LEU A CD1   1 
ATOM   2968 C  CD2   . LEU A 1 383 ? 2.020   88.975  96.437  1.00 150.66 ? 410 LEU A CD2   1 
ATOM   2969 N  N     . GLY A 1 384 ? 5.679   86.419  96.795  1.00 161.92 ? 411 GLY A N     1 
ATOM   2970 C  CA    . GLY A 1 384 ? 5.686   85.212  97.603  1.00 151.95 ? 411 GLY A CA    1 
ATOM   2971 C  C     . GLY A 1 384 ? 7.068   84.795  98.061  1.00 158.04 ? 411 GLY A C     1 
ATOM   2972 O  O     . GLY A 1 384 ? 7.206   84.124  99.088  1.00 160.03 ? 411 GLY A O     1 
ATOM   2973 N  N     . CYS A 1 385 ? 8.107   85.173  97.312  1.00 156.41 ? 412 CYS A N     1 
ATOM   2974 C  CA    . CYS A 1 385 ? 9.464   84.838  97.735  1.00 155.84 ? 412 CYS A CA    1 
ATOM   2975 C  C     . CYS A 1 385 ? 9.863   85.639  98.968  1.00 151.77 ? 412 CYS A C     1 
ATOM   2976 O  O     . CYS A 1 385 ? 10.520  85.112  99.874  1.00 144.41 ? 412 CYS A O     1 
ATOM   2977 C  CB    . CYS A 1 385 ? 10.455  85.072  96.595  1.00 162.09 ? 412 CYS A CB    1 
ATOM   2978 S  SG    . CYS A 1 385 ? 12.068  84.304  96.876  1.00 160.44 ? 412 CYS A SG    1 
ATOM   2979 N  N     . PHE A 1 386 ? 9.467   86.914  99.024  1.00 154.75 ? 413 PHE A N     1 
ATOM   2980 C  CA    . PHE A 1 386 ? 9.676   87.698  100.236 1.00 148.94 ? 413 PHE A CA    1 
ATOM   2981 C  C     . PHE A 1 386 ? 8.915   87.095  101.409 1.00 146.73 ? 413 PHE A C     1 
ATOM   2982 O  O     . PHE A 1 386 ? 9.421   87.061  102.537 1.00 140.76 ? 413 PHE A O     1 
ATOM   2983 C  CB    . PHE A 1 386 ? 9.248   89.149  100.005 1.00 149.04 ? 413 PHE A CB    1 
ATOM   2984 C  CG    . PHE A 1 386 ? 9.624   90.081  101.127 1.00 148.06 ? 413 PHE A CG    1 
ATOM   2985 C  CD1   . PHE A 1 386 ? 8.835   90.182  102.263 1.00 140.35 ? 413 PHE A CD1   1 
ATOM   2986 C  CD2   . PHE A 1 386 ? 10.762  90.864  101.040 1.00 150.81 ? 413 PHE A CD2   1 
ATOM   2987 C  CE1   . PHE A 1 386 ? 9.182   91.036  103.293 1.00 142.07 ? 413 PHE A CE1   1 
ATOM   2988 C  CE2   . PHE A 1 386 ? 11.115  91.720  102.065 1.00 147.99 ? 413 PHE A CE2   1 
ATOM   2989 C  CZ    . PHE A 1 386 ? 10.323  91.807  103.192 1.00 145.87 ? 413 PHE A CZ    1 
ATOM   2990 N  N     . LEU A 1 387 ? 7.696   86.609  101.159 1.00 147.28 ? 414 LEU A N     1 
ATOM   2991 C  CA    . LEU A 1 387 ? 6.881   86.047  102.231 1.00 140.22 ? 414 LEU A CA    1 
ATOM   2992 C  C     . LEU A 1 387 ? 7.478   84.750  102.764 1.00 133.93 ? 414 LEU A C     1 
ATOM   2993 O  O     . LEU A 1 387 ? 7.383   84.465  103.964 1.00 128.23 ? 414 LEU A O     1 
ATOM   2994 C  CB    . LEU A 1 387 ? 5.452   85.820  101.739 1.00 136.86 ? 414 LEU A CB    1 
ATOM   2995 C  CG    . LEU A 1 387 ? 4.695   87.067  101.274 1.00 141.47 ? 414 LEU A CG    1 
ATOM   2996 C  CD1   . LEU A 1 387 ? 3.306   86.705  100.771 1.00 139.08 ? 414 LEU A CD1   1 
ATOM   2997 C  CD2   . LEU A 1 387 ? 4.612   88.093  102.394 1.00 134.80 ? 414 LEU A CD2   1 
ATOM   2998 N  N     . SER A 1 388 ? 8.093   83.948  101.889 1.00 143.19 ? 415 SER A N     1 
ATOM   2999 C  CA    . SER A 1 388 ? 8.733   82.718  102.344 1.00 136.86 ? 415 SER A CA    1 
ATOM   3000 C  C     . SER A 1 388 ? 9.913   83.021  103.259 1.00 135.88 ? 415 SER A C     1 
ATOM   3001 O  O     . SER A 1 388 ? 10.082  82.376  104.300 1.00 131.13 ? 415 SER A O     1 
ATOM   3002 C  CB    . SER A 1 388 ? 9.180   81.882  101.146 1.00 130.17 ? 415 SER A CB    1 
ATOM   3003 O  OG    . SER A 1 388 ? 8.073   81.543  100.329 1.00 134.48 ? 415 SER A OG    1 
ATOM   3004 N  N     . HIS A 1 389 ? 10.740  84.000  102.886 1.00 142.21 ? 416 HIS A N     1 
ATOM   3005 C  CA    . HIS A 1 389 ? 11.784  84.466  103.792 1.00 135.08 ? 416 HIS A CA    1 
ATOM   3006 C  C     . HIS A 1 389 ? 11.181  85.159  105.008 1.00 142.91 ? 416 HIS A C     1 
ATOM   3007 O  O     . HIS A 1 389 ? 11.700  85.030  106.123 1.00 138.65 ? 416 HIS A O     1 
ATOM   3008 C  CB    . HIS A 1 389 ? 12.742  85.404  103.056 1.00 132.77 ? 416 HIS A CB    1 
ATOM   3009 C  CG    . HIS A 1 389 ? 13.612  84.714  102.050 1.00 138.24 ? 416 HIS A CG    1 
ATOM   3010 N  ND1   . HIS A 1 389 ? 14.878  84.257  102.349 1.00 126.95 ? 416 HIS A ND1   1 
ATOM   3011 C  CD2   . HIS A 1 389 ? 13.400  84.406  100.748 1.00 136.95 ? 416 HIS A CD2   1 
ATOM   3012 C  CE1   . HIS A 1 389 ? 15.407  83.697  101.277 1.00 118.64 ? 416 HIS A CE1   1 
ATOM   3013 N  NE2   . HIS A 1 389 ? 14.531  83.773  100.291 1.00 127.91 ? 416 HIS A NE2   1 
ATOM   3014 N  N     . TYR A 1 390 ? 10.081  85.894  104.814 1.00 138.79 ? 417 TYR A N     1 
ATOM   3015 C  CA    . TYR A 1 390 ? 9.421   86.554  105.936 1.00 136.58 ? 417 TYR A CA    1 
ATOM   3016 C  C     . TYR A 1 390 ? 8.920   85.538  106.954 1.00 139.02 ? 417 TYR A C     1 
ATOM   3017 O  O     . TYR A 1 390 ? 9.044   85.751  108.165 1.00 145.42 ? 417 TYR A O     1 
ATOM   3018 C  CB    . TYR A 1 390 ? 8.269   87.423  105.428 1.00 146.20 ? 417 TYR A CB    1 
ATOM   3019 C  CG    . TYR A 1 390 ? 7.590   88.263  106.489 1.00 147.44 ? 417 TYR A CG    1 
ATOM   3020 C  CD1   . TYR A 1 390 ? 8.086   89.515  106.835 1.00 157.02 ? 417 TYR A CD1   1 
ATOM   3021 C  CD2   . TYR A 1 390 ? 6.443   87.814  107.131 1.00 152.96 ? 417 TYR A CD2   1 
ATOM   3022 C  CE1   . TYR A 1 390 ? 7.464   90.291  107.800 1.00 162.70 ? 417 TYR A CE1   1 
ATOM   3023 C  CE2   . TYR A 1 390 ? 5.814   88.584  108.097 1.00 158.88 ? 417 TYR A CE2   1 
ATOM   3024 C  CZ    . TYR A 1 390 ? 6.329   89.820  108.427 1.00 162.14 ? 417 TYR A CZ    1 
ATOM   3025 O  OH    . TYR A 1 390 ? 5.705   90.586  109.387 1.00 150.64 ? 417 TYR A OH    1 
ATOM   3026 N  N     . ASN A 1 391 ? 8.359   84.421  106.482 1.00 141.44 ? 418 ASN A N     1 
ATOM   3027 C  CA    . ASN A 1 391 ? 7.871   83.395  107.398 1.00 139.88 ? 418 ASN A CA    1 
ATOM   3028 C  C     . ASN A 1 391 ? 9.012   82.696  108.126 1.00 132.33 ? 418 ASN A C     1 
ATOM   3029 O  O     . ASN A 1 391 ? 8.834   82.245  109.263 1.00 127.28 ? 418 ASN A O     1 
ATOM   3030 C  CB    . ASN A 1 391 ? 7.021   82.372  106.644 1.00 134.61 ? 418 ASN A CB    1 
ATOM   3031 C  CG    . ASN A 1 391 ? 5.684   82.933  106.209 1.00 137.03 ? 418 ASN A CG    1 
ATOM   3032 O  OD1   . ASN A 1 391 ? 5.068   83.726  106.923 1.00 139.40 ? 418 ASN A OD1   1 
ATOM   3033 N  ND2   . ASN A 1 391 ? 5.227   82.523  105.033 1.00 142.94 ? 418 ASN A ND2   1 
ATOM   3034 N  N     . ILE A 1 392 ? 10.183  82.593  107.493 1.00 121.24 ? 419 ILE A N     1 
ATOM   3035 C  CA    . ILE A 1 392 ? 11.326  81.975  108.156 1.00 114.52 ? 419 ILE A CA    1 
ATOM   3036 C  C     . ILE A 1 392 ? 11.899  82.911  109.213 1.00 123.67 ? 419 ILE A C     1 
ATOM   3037 O  O     . ILE A 1 392 ? 12.290  82.474  110.303 1.00 122.14 ? 419 ILE A O     1 
ATOM   3038 C  CB    . ILE A 1 392 ? 12.385  81.557  107.120 1.00 112.29 ? 419 ILE A CB    1 
ATOM   3039 C  CG1   . ILE A 1 392 ? 11.865  80.394  106.271 1.00 120.08 ? 419 ILE A CG1   1 
ATOM   3040 C  CG2   . ILE A 1 392 ? 13.691  81.179  107.804 1.00 107.82 ? 419 ILE A CG2   1 
ATOM   3041 C  CD1   . ILE A 1 392 ? 12.933  79.693  105.457 1.00 101.77 ? 419 ILE A CD1   1 
ATOM   3042 N  N     . TRP A 1 393 ? 11.952  84.214  108.914 1.00 131.19 ? 420 TRP A N     1 
ATOM   3043 C  CA    . TRP A 1 393 ? 12.357  85.190  109.921 1.00 125.67 ? 420 TRP A CA    1 
ATOM   3044 C  C     . TRP A 1 393 ? 11.481  85.099  111.162 1.00 133.29 ? 420 TRP A C     1 
ATOM   3045 O  O     . TRP A 1 393 ? 11.965  85.300  112.281 1.00 140.96 ? 420 TRP A O     1 
ATOM   3046 C  CB    . TRP A 1 393 ? 12.297  86.608  109.346 1.00 130.45 ? 420 TRP A CB    1 
ATOM   3047 C  CG    . TRP A 1 393 ? 13.109  86.814  108.101 1.00 123.47 ? 420 TRP A CG    1 
ATOM   3048 C  CD1   . TRP A 1 393 ? 14.145  86.044  107.658 1.00 113.38 ? 420 TRP A CD1   1 
ATOM   3049 C  CD2   . TRP A 1 393 ? 12.940  87.856  107.130 1.00 130.10 ? 420 TRP A CD2   1 
ATOM   3050 N  NE1   . TRP A 1 393 ? 14.634  86.543  106.475 1.00 122.36 ? 420 TRP A NE1   1 
ATOM   3051 C  CE2   . TRP A 1 393 ? 13.913  87.656  106.129 1.00 129.51 ? 420 TRP A CE2   1 
ATOM   3052 C  CE3   . TRP A 1 393 ? 12.063  88.939  107.011 1.00 127.93 ? 420 TRP A CE3   1 
ATOM   3053 C  CZ2   . TRP A 1 393 ? 14.034  88.499  105.024 1.00 119.86 ? 420 TRP A CZ2   1 
ATOM   3054 C  CZ3   . TRP A 1 393 ? 12.185  89.776  105.914 1.00 129.93 ? 420 TRP A CZ3   1 
ATOM   3055 C  CH2   . TRP A 1 393 ? 13.163  89.550  104.935 1.00 132.69 ? 420 TRP A CH2   1 
ATOM   3056 N  N     . LYS A 1 394 ? 10.192  84.794  110.982 1.00 143.20 ? 421 LYS A N     1 
ATOM   3057 C  CA    . LYS A 1 394 ? 9.290   84.653  112.121 1.00 142.52 ? 421 LYS A CA    1 
ATOM   3058 C  C     . LYS A 1 394 ? 9.599   83.392  112.919 1.00 135.64 ? 421 LYS A C     1 
ATOM   3059 O  O     . LYS A 1 394 ? 9.625   83.424  114.155 1.00 138.75 ? 421 LYS A O     1 
ATOM   3060 C  CB    . LYS A 1 394 ? 7.838   84.642  111.640 1.00 141.70 ? 421 LYS A CB    1 
ATOM   3061 C  CG    . LYS A 1 394 ? 7.433   85.881  110.853 1.00 139.50 ? 421 LYS A CG    1 
ATOM   3062 C  CD    . LYS A 1 394 ? 6.229   85.608  109.961 1.00 143.38 ? 421 LYS A CD    1 
ATOM   3063 C  CE    . LYS A 1 394 ? 4.918   85.796  110.704 1.00 146.70 ? 421 LYS A CE    1 
ATOM   3064 N  NZ    . LYS A 1 394 ? 4.677   87.227  111.040 1.00 156.77 ? 421 LYS A NZ    1 
ATOM   3065 N  N     . GLU A 1 395 ? 9.835   82.270  112.231 1.00 131.15 ? 422 GLU A N     1 
ATOM   3066 C  CA    . GLU A 1 395 ? 10.123  81.025  112.935 1.00 131.70 ? 422 GLU A CA    1 
ATOM   3067 C  C     . GLU A 1 395 ? 11.415  81.117  113.734 1.00 134.45 ? 422 GLU A C     1 
ATOM   3068 O  O     . GLU A 1 395 ? 11.534  80.493  114.796 1.00 137.15 ? 422 GLU A O     1 
ATOM   3069 C  CB    . GLU A 1 395 ? 10.193  79.861  111.946 1.00 126.69 ? 422 GLU A CB    1 
ATOM   3070 C  CG    . GLU A 1 395 ? 10.494  78.529  112.607 1.00 127.36 ? 422 GLU A CG    1 
ATOM   3071 C  CD    . GLU A 1 395 ? 10.476  77.366  111.641 1.00 134.48 ? 422 GLU A CD    1 
ATOM   3072 O  OE1   . GLU A 1 395 ? 9.755   77.442  110.623 1.00 135.49 ? 422 GLU A OE1   1 
ATOM   3073 O  OE2   . GLU A 1 395 ? 11.189  76.373  111.902 1.00 136.61 ? 422 GLU A OE2   1 
ATOM   3074 N  N     . VAL A 1 396 ? 12.388  81.890  113.249 1.00 130.72 ? 423 VAL A N     1 
ATOM   3075 C  CA    . VAL A 1 396 ? 13.626  82.082  114.000 1.00 134.00 ? 423 VAL A CA    1 
ATOM   3076 C  C     . VAL A 1 396 ? 13.335  82.757  115.334 1.00 130.42 ? 423 VAL A C     1 
ATOM   3077 O  O     . VAL A 1 396 ? 13.753  82.280  116.396 1.00 133.58 ? 423 VAL A O     1 
ATOM   3078 C  CB    . VAL A 1 396 ? 14.642  82.887  113.171 1.00 123.61 ? 423 VAL A CB    1 
ATOM   3079 C  CG1   . VAL A 1 396 ? 15.831  83.280  114.033 1.00 126.86 ? 423 VAL A CG1   1 
ATOM   3080 C  CG2   . VAL A 1 396 ? 15.101  82.077  111.972 1.00 123.51 ? 423 VAL A CG2   1 
ATOM   3081 N  N     . VAL A 1 397 ? 12.609  83.877  115.299 1.00 118.04 ? 424 VAL A N     1 
ATOM   3082 C  CA    . VAL A 1 397 ? 12.264  84.562  116.539 1.00 127.76 ? 424 VAL A CA    1 
ATOM   3083 C  C     . VAL A 1 397 ? 11.323  83.706  117.375 1.00 125.15 ? 424 VAL A C     1 
ATOM   3084 O  O     . VAL A 1 397 ? 11.397  83.715  118.609 1.00 131.83 ? 424 VAL A O     1 
ATOM   3085 C  CB    . VAL A 1 397 ? 11.657  85.947  116.243 1.00 123.20 ? 424 VAL A CB    1 
ATOM   3086 C  CG1   . VAL A 1 397 ? 11.499  86.739  117.527 1.00 116.62 ? 424 VAL A CG1   1 
ATOM   3087 C  CG2   . VAL A 1 397 ? 12.518  86.708  115.242 1.00 116.03 ? 424 VAL A CG2   1 
ATOM   3088 N  N     . ASP A 1 398 ? 10.433  82.948  116.728 1.00 133.16 ? 425 ASP A N     1 
ATOM   3089 C  CA    . ASP A 1 398 ? 9.502   82.099  117.466 1.00 140.29 ? 425 ASP A CA    1 
ATOM   3090 C  C     . ASP A 1 398 ? 10.239  80.989  118.206 1.00 137.57 ? 425 ASP A C     1 
ATOM   3091 O  O     . ASP A 1 398 ? 10.044  80.794  119.412 1.00 142.90 ? 425 ASP A O     1 
ATOM   3092 C  CB    . ASP A 1 398 ? 8.456   81.513  116.515 1.00 141.75 ? 425 ASP A CB    1 
ATOM   3093 C  CG    . ASP A 1 398 ? 7.423   80.660  117.233 1.00 149.32 ? 425 ASP A CG    1 
ATOM   3094 O  OD1   . ASP A 1 398 ? 6.516   81.232  117.875 1.00 141.10 ? 425 ASP A OD1   1 
ATOM   3095 O  OD2   . ASP A 1 398 ? 7.519   79.418  117.152 1.00 150.32 ? 425 ASP A OD2   1 
ATOM   3096 N  N     . ARG A 1 399 ? 11.098  80.253  117.501 1.00 133.61 ? 426 ARG A N     1 
ATOM   3097 C  CA    . ARG A 1 399 ? 11.878  79.191  118.123 1.00 131.11 ? 426 ARG A CA    1 
ATOM   3098 C  C     . ARG A 1 399 ? 13.121  79.704  118.839 1.00 132.10 ? 426 ARG A C     1 
ATOM   3099 O  O     . ARG A 1 399 ? 13.789  78.919  119.521 1.00 138.75 ? 426 ARG A O     1 
ATOM   3100 C  CB    . ARG A 1 399 ? 12.285  78.151  117.073 1.00 134.00 ? 426 ARG A CB    1 
ATOM   3101 C  CG    . ARG A 1 399 ? 11.124  77.341  116.510 1.00 130.78 ? 426 ARG A CG    1 
ATOM   3102 C  CD    . ARG A 1 399 ? 11.549  76.510  115.306 1.00 131.53 ? 426 ARG A CD    1 
ATOM   3103 N  NE    . ARG A 1 399 ? 12.446  75.415  115.658 1.00 144.09 ? 426 ARG A NE    1 
ATOM   3104 C  CZ    . ARG A 1 399 ? 13.090  74.663  114.775 1.00 130.55 ? 426 ARG A CZ    1 
ATOM   3105 N  NH1   . ARG A 1 399 ? 12.980  74.876  113.474 1.00 120.62 ? 426 ARG A NH1   1 
ATOM   3106 N  NH2   . ARG A 1 399 ? 13.867  73.675  115.208 1.00 133.68 ? 426 ARG A NH2   1 
ATOM   3107 N  N     . GLY A 1 400 ? 13.441  80.987  118.708 1.00 126.87 ? 427 GLY A N     1 
ATOM   3108 C  CA    . GLY A 1 400 ? 14.632  81.533  119.340 1.00 123.13 ? 427 GLY A CA    1 
ATOM   3109 C  C     . GLY A 1 400 ? 15.930  80.972  118.798 1.00 133.57 ? 427 GLY A C     1 
ATOM   3110 O  O     . GLY A 1 400 ? 16.867  80.729  119.570 1.00 139.75 ? 427 GLY A O     1 
ATOM   3111 N  N     . LEU A 1 401 ? 16.010  80.759  117.487 1.00 132.26 ? 428 LEU A N     1 
ATOM   3112 C  CA    . LEU A 1 401 ? 17.200  80.171  116.883 1.00 121.76 ? 428 LEU A CA    1 
ATOM   3113 C  C     . LEU A 1 401 ? 18.331  81.193  116.854 1.00 128.20 ? 428 LEU A C     1 
ATOM   3114 O  O     . LEU A 1 401 ? 18.231  82.221  116.177 1.00 134.79 ? 428 LEU A O     1 
ATOM   3115 C  CB    . LEU A 1 401 ? 16.880  79.680  115.474 1.00 116.66 ? 428 LEU A CB    1 
ATOM   3116 C  CG    . LEU A 1 401 ? 15.682  78.733  115.386 1.00 127.24 ? 428 LEU A CG    1 
ATOM   3117 C  CD1   . LEU A 1 401 ? 15.317  78.445  113.937 1.00 134.97 ? 428 LEU A CD1   1 
ATOM   3118 C  CD2   . LEU A 1 401 ? 15.966  77.442  116.137 1.00 120.05 ? 428 LEU A CD2   1 
ATOM   3119 N  N     . GLN A 1 402 ? 19.410  80.905  117.588 1.00 127.59 ? 429 GLN A N     1 
ATOM   3120 C  CA    . GLN A 1 402 ? 20.527  81.841  117.670 1.00 115.39 ? 429 GLN A CA    1 
ATOM   3121 C  C     . GLN A 1 402 ? 21.178  82.041  116.306 1.00 119.61 ? 429 GLN A C     1 
ATOM   3122 O  O     . GLN A 1 402 ? 21.297  83.172  115.824 1.00 119.96 ? 429 GLN A O     1 
ATOM   3123 C  CB    . GLN A 1 402 ? 21.549  81.346  118.692 1.00 117.85 ? 429 GLN A CB    1 
ATOM   3124 C  CG    . GLN A 1 402 ? 20.957  81.058  120.064 1.00 120.61 ? 429 GLN A CG    1 
ATOM   3125 C  CD    . GLN A 1 402 ? 20.265  82.267  120.663 1.00 144.01 ? 429 GLN A CD    1 
ATOM   3126 O  OE1   . GLN A 1 402 ? 20.833  83.358  120.715 1.00 138.66 ? 429 GLN A OE1   1 
ATOM   3127 N  NE2   . GLN A 1 402 ? 19.027  82.082  121.110 1.00 144.95 ? 429 GLN A NE2   1 
ATOM   3128 N  N     . LYS A 1 403 ? 21.606  80.952  115.667 1.00 121.20 ? 430 LYS A N     1 
ATOM   3129 C  CA    . LYS A 1 403 ? 22.210  81.008  114.341 1.00 111.13 ? 430 LYS A CA    1 
ATOM   3130 C  C     . LYS A 1 403 ? 21.535  79.985  113.440 1.00 111.22 ? 430 LYS A C     1 
ATOM   3131 O  O     . LYS A 1 403 ? 21.411  78.813  113.809 1.00 102.54 ? 430 LYS A O     1 
ATOM   3132 C  CB    . LYS A 1 403 ? 23.724  80.759  114.399 1.00 100.21 ? 430 LYS A CB    1 
ATOM   3133 C  CG    . LYS A 1 403 ? 24.141  79.537  115.204 1.00 115.97 ? 430 LYS A CG    1 
ATOM   3134 C  CD    . LYS A 1 403 ? 25.643  79.298  115.108 1.00 116.03 ? 430 LYS A CD    1 
ATOM   3135 C  CE    . LYS A 1 403 ? 26.099  78.193  116.052 1.00 126.68 ? 430 LYS A CE    1 
ATOM   3136 N  NZ    . LYS A 1 403 ? 27.565  77.934  115.947 1.00 107.08 ? 430 LYS A NZ    1 
ATOM   3137 N  N     . SER A 1 404 ? 21.099  80.432  112.263 1.00 117.44 ? 431 SER A N     1 
ATOM   3138 C  CA    . SER A 1 404 ? 20.406  79.580  111.308 1.00 105.99 ? 431 SER A CA    1 
ATOM   3139 C  C     . SER A 1 404 ? 20.956  79.821  109.912 1.00 107.79 ? 431 SER A C     1 
ATOM   3140 O  O     . SER A 1 404 ? 21.326  80.948  109.568 1.00 114.08 ? 431 SER A O     1 
ATOM   3141 C  CB    . SER A 1 404 ? 18.892  79.838  111.313 1.00 109.68 ? 431 SER A CB    1 
ATOM   3142 O  OG    . SER A 1 404 ? 18.329  79.559  112.581 1.00 119.96 ? 431 SER A OG    1 
ATOM   3143 N  N     . LEU A 1 405 ? 21.012  78.756  109.118 1.00 108.79 ? 432 LEU A N     1 
ATOM   3144 C  CA    . LEU A 1 405 ? 21.385  78.823  107.712 1.00 97.85  ? 432 LEU A CA    1 
ATOM   3145 C  C     . LEU A 1 405 ? 20.131  78.648  106.865 1.00 108.96 ? 432 LEU A C     1 
ATOM   3146 O  O     . LEU A 1 405 ? 19.323  77.750  107.126 1.00 104.18 ? 432 LEU A O     1 
ATOM   3147 C  CB    . LEU A 1 405 ? 22.419  77.749  107.365 1.00 100.85 ? 432 LEU A CB    1 
ATOM   3148 C  CG    . LEU A 1 405 ? 22.828  77.617  105.894 1.00 102.20 ? 432 LEU A CG    1 
ATOM   3149 C  CD1   . LEU A 1 405 ? 23.676  78.796  105.439 1.00 99.36  ? 432 LEU A CD1   1 
ATOM   3150 C  CD2   . LEU A 1 405 ? 23.565  76.312  105.667 1.00 82.57  ? 432 LEU A CD2   1 
ATOM   3151 N  N     . VAL A 1 406 ? 19.967  79.506  105.861 1.00 107.17 ? 433 VAL A N     1 
ATOM   3152 C  CA    . VAL A 1 406 ? 18.786  79.508  105.006 1.00 94.67  ? 433 VAL A CA    1 
ATOM   3153 C  C     . VAL A 1 406 ? 19.221  79.215  103.577 1.00 99.03  ? 433 VAL A C     1 
ATOM   3154 O  O     . VAL A 1 406 ? 20.103  79.893  103.039 1.00 93.71  ? 433 VAL A O     1 
ATOM   3155 C  CB    . VAL A 1 406 ? 18.030  80.846  105.088 1.00 95.73  ? 433 VAL A CB    1 
ATOM   3156 C  CG1   . VAL A 1 406 ? 16.777  80.801  104.229 1.00 97.65  ? 433 VAL A CG1   1 
ATOM   3157 C  CG2   . VAL A 1 406 ? 17.679  81.163  106.533 1.00 101.18 ? 433 VAL A CG2   1 
ATOM   3158 N  N     . PHE A 1 407 ? 18.600  78.210  102.968 1.00 102.34 ? 434 PHE A N     1 
ATOM   3159 C  CA    . PHE A 1 407 ? 18.918  77.781  101.615 1.00 95.87  ? 434 PHE A CA    1 
ATOM   3160 C  C     . PHE A 1 407 ? 17.779  78.113  100.662 1.00 98.93  ? 434 PHE A C     1 
ATOM   3161 O  O     . PHE A 1 407 ? 16.655  78.414  101.074 1.00 112.64 ? 434 PHE A O     1 
ATOM   3162 C  CB    . PHE A 1 407 ? 19.188  76.272  101.563 1.00 102.97 ? 434 PHE A CB    1 
ATOM   3163 C  CG    . PHE A 1 407 ? 20.607  75.889  101.869 1.00 99.44  ? 434 PHE A CG    1 
ATOM   3164 C  CD1   . PHE A 1 407 ? 21.663  76.683  101.453 1.00 91.77  ? 434 PHE A CD1   1 
ATOM   3165 C  CD2   . PHE A 1 407 ? 20.885  74.724  102.568 1.00 100.93 ? 434 PHE A CD2   1 
ATOM   3166 C  CE1   . PHE A 1 407 ? 22.969  76.323  101.732 1.00 94.81  ? 434 PHE A CE1   1 
ATOM   3167 C  CE2   . PHE A 1 407 ? 22.189  74.361  102.851 1.00 96.96  ? 434 PHE A CE2   1 
ATOM   3168 C  CZ    . PHE A 1 407 ? 23.233  75.159  102.430 1.00 96.96  ? 434 PHE A CZ    1 
ATOM   3169 N  N     . GLU A 1 408 ? 18.093  78.053  99.370  1.00 98.34  ? 435 GLU A N     1 
ATOM   3170 C  CA    . GLU A 1 408 ? 17.073  78.060  98.331  1.00 112.64 ? 435 GLU A CA    1 
ATOM   3171 C  C     . GLU A 1 408 ? 17.192  76.773  97.521  1.00 117.39 ? 435 GLU A C     1 
ATOM   3172 O  O     . GLU A 1 408 ? 17.718  75.775  98.027  1.00 117.01 ? 435 GLU A O     1 
ATOM   3173 C  CB    . GLU A 1 408 ? 17.194  79.311  97.460  1.00 112.14 ? 435 GLU A CB    1 
ATOM   3174 C  CG    . GLU A 1 408 ? 16.696  80.570  98.171  1.00 113.99 ? 435 GLU A CG    1 
ATOM   3175 C  CD    . GLU A 1 408 ? 16.714  81.802  97.290  1.00 122.08 ? 435 GLU A CD    1 
ATOM   3176 O  OE1   . GLU A 1 408 ? 17.521  81.845  96.340  1.00 135.20 ? 435 GLU A OE1   1 
ATOM   3177 O  OE2   . GLU A 1 408 ? 15.917  82.730  97.548  1.00 129.54 ? 435 GLU A OE2   1 
ATOM   3178 N  N     . ASP A 1 409 ? 16.713  76.764  96.275  1.00 120.57 ? 436 ASP A N     1 
ATOM   3179 C  CA    . ASP A 1 409 ? 16.601  75.515  95.527  1.00 124.05 ? 436 ASP A CA    1 
ATOM   3180 C  C     . ASP A 1 409 ? 17.296  75.555  94.167  1.00 127.52 ? 436 ASP A C     1 
ATOM   3181 O  O     . ASP A 1 409 ? 17.043  74.687  93.326  1.00 137.32 ? 436 ASP A O     1 
ATOM   3182 C  CB    . ASP A 1 409 ? 15.129  75.129  95.359  1.00 125.43 ? 436 ASP A CB    1 
ATOM   3183 C  CG    . ASP A 1 409 ? 14.299  76.232  94.733  1.00 126.52 ? 436 ASP A CG    1 
ATOM   3184 O  OD1   . ASP A 1 409 ? 14.842  77.326  94.482  1.00 133.48 ? 436 ASP A OD1   1 
ATOM   3185 O  OD2   . ASP A 1 409 ? 13.095  76.001  94.493  1.00 135.41 ? 436 ASP A OD2   1 
ATOM   3186 N  N     . ASP A 1 410 ? 18.181  76.532  93.930  1.00 124.81 ? 437 ASP A N     1 
ATOM   3187 C  CA    . ASP A 1 410 ? 18.972  76.592  92.698  1.00 121.51 ? 437 ASP A CA    1 
ATOM   3188 C  C     . ASP A 1 410 ? 20.375  77.089  93.055  1.00 119.59 ? 437 ASP A C     1 
ATOM   3189 O  O     . ASP A 1 410 ? 20.796  78.189  92.698  1.00 124.58 ? 437 ASP A O     1 
ATOM   3190 C  CB    . ASP A 1 410 ? 18.307  77.478  91.639  1.00 128.05 ? 437 ASP A CB    1 
ATOM   3191 C  CG    . ASP A 1 410 ? 17.821  78.805  92.199  1.00 159.28 ? 437 ASP A CG    1 
ATOM   3192 O  OD1   . ASP A 1 410 ? 17.950  79.025  93.424  1.00 160.00 ? 437 ASP A OD1   1 
ATOM   3193 O  OD2   . ASP A 1 410 ? 17.305  79.629  91.411  1.00 165.03 ? 437 ASP A OD2   1 
ATOM   3194 N  N     . LEU A 1 411 ? 21.124  76.250  93.767  1.00 103.92 ? 438 LEU A N     1 
ATOM   3195 C  CA    . LEU A 1 411 ? 22.419  76.625  94.315  1.00 106.67 ? 438 LEU A CA    1 
ATOM   3196 C  C     . LEU A 1 411 ? 23.505  75.686  93.810  1.00 105.66 ? 438 LEU A C     1 
ATOM   3197 O  O     . LEU A 1 411 ? 23.270  74.491  93.598  1.00 101.07 ? 438 LEU A O     1 
ATOM   3198 C  CB    . LEU A 1 411 ? 22.396  76.597  95.849  1.00 96.42  ? 438 LEU A CB    1 
ATOM   3199 C  CG    . LEU A 1 411 ? 21.135  77.143  96.519  1.00 104.28 ? 438 LEU A CG    1 
ATOM   3200 C  CD1   . LEU A 1 411 ? 21.218  76.948  98.020  1.00 102.44 ? 438 LEU A CD1   1 
ATOM   3201 C  CD2   . LEU A 1 411 ? 20.923  78.611  96.172  1.00 116.68 ? 438 LEU A CD2   1 
ATOM   3202 N  N     . ARG A 1 412 ? 24.703  76.239  93.629  1.00 105.43 ? 439 ARG A N     1 
ATOM   3203 C  CA    . ARG A 1 412 ? 25.895  75.478  93.267  1.00 88.71  ? 439 ARG A CA    1 
ATOM   3204 C  C     . ARG A 1 412 ? 26.872  75.558  94.434  1.00 92.06  ? 439 ARG A C     1 
ATOM   3205 O  O     . ARG A 1 412 ? 27.383  76.639  94.748  1.00 103.56 ? 439 ARG A O     1 
ATOM   3206 C  CB    . ARG A 1 412 ? 26.524  76.021  91.984  1.00 86.11  ? 439 ARG A CB    1 
ATOM   3207 C  CG    . ARG A 1 412 ? 27.903  75.455  91.691  1.00 93.82  ? 439 ARG A CG    1 
ATOM   3208 C  CD    . ARG A 1 412 ? 28.582  76.218  90.574  1.00 103.82 ? 439 ARG A CD    1 
ATOM   3209 N  NE    . ARG A 1 412 ? 27.966  75.960  89.279  1.00 120.84 ? 439 ARG A NE    1 
ATOM   3210 C  CZ    . ARG A 1 412 ? 28.565  75.330  88.278  1.00 126.45 ? 439 ARG A CZ    1 
ATOM   3211 N  NH1   . ARG A 1 412 ? 29.816  74.909  88.377  1.00 104.93 ? 439 ARG A NH1   1 
ATOM   3212 N  NH2   . ARG A 1 412 ? 27.896  75.125  87.146  1.00 137.50 ? 439 ARG A NH2   1 
ATOM   3213 N  N     . PHE A 1 413 ? 27.129  74.418  95.074  1.00 89.17  ? 440 PHE A N     1 
ATOM   3214 C  CA    . PHE A 1 413 ? 27.982  74.381  96.255  1.00 85.95  ? 440 PHE A CA    1 
ATOM   3215 C  C     . PHE A 1 413 ? 29.454  74.389  95.859  1.00 81.10  ? 440 PHE A C     1 
ATOM   3216 O  O     . PHE A 1 413 ? 29.871  73.631  94.979  1.00 97.11  ? 440 PHE A O     1 
ATOM   3217 C  CB    . PHE A 1 413 ? 27.678  73.141  97.095  1.00 80.92  ? 440 PHE A CB    1 
ATOM   3218 C  CG    . PHE A 1 413 ? 26.340  73.176  97.772  1.00 86.47  ? 440 PHE A CG    1 
ATOM   3219 C  CD1   . PHE A 1 413 ? 25.190  72.813  97.086  1.00 89.04  ? 440 PHE A CD1   1 
ATOM   3220 C  CD2   . PHE A 1 413 ? 26.231  73.562  99.099  1.00 91.75  ? 440 PHE A CD2   1 
ATOM   3221 C  CE1   . PHE A 1 413 ? 23.954  72.842  97.708  1.00 98.84  ? 440 PHE A CE1   1 
ATOM   3222 C  CE2   . PHE A 1 413 ? 25.000  73.591  99.730  1.00 92.10  ? 440 PHE A CE2   1 
ATOM   3223 C  CZ    . PHE A 1 413 ? 23.859  73.231  99.033  1.00 106.40 ? 440 PHE A CZ    1 
ATOM   3224 N  N     . GLU A 1 414 ? 30.240  75.242  96.513  1.00 78.30  ? 441 GLU A N     1 
ATOM   3225 C  CA    . GLU A 1 414 ? 31.676  75.275  96.287  1.00 74.58  ? 441 GLU A CA    1 
ATOM   3226 C  C     . GLU A 1 414 ? 32.345  74.045  96.893  1.00 88.56  ? 441 GLU A C     1 
ATOM   3227 O  O     . GLU A 1 414 ? 31.766  73.324  97.713  1.00 87.80  ? 441 GLU A O     1 
ATOM   3228 C  CB    . GLU A 1 414 ? 32.289  76.545  96.877  1.00 82.78  ? 441 GLU A CB    1 
ATOM   3229 C  CG    . GLU A 1 414 ? 32.437  77.695  95.891  1.00 99.73  ? 441 GLU A CG    1 
ATOM   3230 C  CD    . GLU A 1 414 ? 33.628  77.528  94.959  1.00 108.21 ? 441 GLU A CD    1 
ATOM   3231 O  OE1   . GLU A 1 414 ? 34.434  76.592  95.171  1.00 97.41  ? 441 GLU A OE1   1 
ATOM   3232 O  OE2   . GLU A 1 414 ? 33.753  78.338  94.014  1.00 97.97  ? 441 GLU A OE2   1 
ATOM   3233 N  N     . ILE A 1 415 ? 33.592  73.810  96.479  1.00 85.47  ? 442 ILE A N     1 
ATOM   3234 C  CA    . ILE A 1 415 ? 34.342  72.674  96.995  1.00 88.09  ? 442 ILE A CA    1 
ATOM   3235 C  C     . ILE A 1 415 ? 34.681  72.911  98.462  1.00 87.79  ? 442 ILE A C     1 
ATOM   3236 O  O     . ILE A 1 415 ? 35.006  74.035  98.872  1.00 91.88  ? 442 ILE A O     1 
ATOM   3237 C  CB    . ILE A 1 415 ? 35.605  72.431  96.149  1.00 86.43  ? 442 ILE A CB    1 
ATOM   3238 C  CG1   . ILE A 1 415 ? 36.301  71.139  96.584  1.00 86.37  ? 442 ILE A CG1   1 
ATOM   3239 C  CG2   . ILE A 1 415 ? 36.554  73.623  96.227  1.00 84.04  ? 442 ILE A CG2   1 
ATOM   3240 C  CD1   . ILE A 1 415 ? 37.464  70.744  95.705  1.00 74.31  ? 442 ILE A CD1   1 
ATOM   3241 N  N     . PHE A 1 416 ? 34.579  71.850  99.267  1.00 86.57  ? 443 PHE A N     1 
ATOM   3242 C  CA    . PHE A 1 416 ? 34.827  71.918  100.710 1.00 88.08  ? 443 PHE A CA    1 
ATOM   3243 C  C     . PHE A 1 416 ? 33.859  72.879  101.395 1.00 91.42  ? 443 PHE A C     1 
ATOM   3244 O  O     . PHE A 1 416 ? 34.234  73.614  102.310 1.00 94.61  ? 443 PHE A O     1 
ATOM   3245 C  CB    . PHE A 1 416 ? 36.274  72.316  101.009 1.00 81.74  ? 443 PHE A CB    1 
ATOM   3246 C  CG    . PHE A 1 416 ? 37.291  71.485  100.291 1.00 94.77  ? 443 PHE A CG    1 
ATOM   3247 C  CD1   . PHE A 1 416 ? 37.155  70.108  100.218 1.00 87.26  ? 443 PHE A CD1   1 
ATOM   3248 C  CD2   . PHE A 1 416 ? 38.381  72.081  99.681  1.00 89.14  ? 443 PHE A CD2   1 
ATOM   3249 C  CE1   . PHE A 1 416 ? 38.092  69.342  99.555  1.00 87.23  ? 443 PHE A CE1   1 
ATOM   3250 C  CE2   . PHE A 1 416 ? 39.320  71.321  99.018  1.00 81.95  ? 443 PHE A CE2   1 
ATOM   3251 C  CZ    . PHE A 1 416 ? 39.178  69.950  98.955  1.00 80.56  ? 443 PHE A CZ    1 
ATOM   3252 N  N     . PHE A 1 417 ? 32.598  72.871  100.949 1.00 85.95  ? 444 PHE A N     1 
ATOM   3253 C  CA    . PHE A 1 417 ? 31.610  73.801  101.489 1.00 79.46  ? 444 PHE A CA    1 
ATOM   3254 C  C     . PHE A 1 417 ? 31.440  73.623  102.993 1.00 87.78  ? 444 PHE A C     1 
ATOM   3255 O  O     . PHE A 1 417 ? 31.517  74.591  103.758 1.00 90.27  ? 444 PHE A O     1 
ATOM   3256 C  CB    . PHE A 1 417 ? 30.268  73.616  100.776 1.00 79.48  ? 444 PHE A CB    1 
ATOM   3257 C  CG    . PHE A 1 417 ? 29.150  74.436  101.362 1.00 82.61  ? 444 PHE A CG    1 
ATOM   3258 C  CD1   . PHE A 1 417 ? 28.929  75.735  100.933 1.00 74.96  ? 444 PHE A CD1   1 
ATOM   3259 C  CD2   . PHE A 1 417 ? 28.319  73.909  102.344 1.00 87.91  ? 444 PHE A CD2   1 
ATOM   3260 C  CE1   . PHE A 1 417 ? 27.903  76.495  101.473 1.00 90.45  ? 444 PHE A CE1   1 
ATOM   3261 C  CE2   . PHE A 1 417 ? 27.292  74.663  102.888 1.00 83.72  ? 444 PHE A CE2   1 
ATOM   3262 C  CZ    . PHE A 1 417 ? 27.082  75.958  102.451 1.00 78.87  ? 444 PHE A CZ    1 
ATOM   3263 N  N     . LYS A 1 418 ? 31.206  72.386  103.434 1.00 88.73  ? 445 LYS A N     1 
ATOM   3264 C  CA    . LYS A 1 418 ? 30.849  72.149  104.829 1.00 84.89  ? 445 LYS A CA    1 
ATOM   3265 C  C     . LYS A 1 418 ? 31.955  72.607  105.773 1.00 81.55  ? 445 LYS A C     1 
ATOM   3266 O  O     . LYS A 1 418 ? 31.695  73.301  106.763 1.00 91.67  ? 445 LYS A O     1 
ATOM   3267 C  CB    . LYS A 1 418 ? 30.534  70.667  105.035 1.00 97.12  ? 445 LYS A CB    1 
ATOM   3268 C  CG    . LYS A 1 418 ? 30.068  70.303  106.436 1.00 86.10  ? 445 LYS A CG    1 
ATOM   3269 C  CD    . LYS A 1 418 ? 29.633  68.849  106.491 1.00 91.55  ? 445 LYS A CD    1 
ATOM   3270 C  CE    . LYS A 1 418 ? 29.345  68.405  107.907 1.00 97.06  ? 445 LYS A CE    1 
ATOM   3271 N  NZ    . LYS A 1 418 ? 28.846  67.003  107.944 1.00 102.69 ? 445 LYS A NZ    1 
ATOM   3272 N  N     . ARG A 1 419 ? 33.204  72.241  105.477 1.00 87.96  ? 446 ARG A N     1 
ATOM   3273 C  CA    . ARG A 1 419 ? 34.299  72.609  106.368 1.00 89.46  ? 446 ARG A CA    1 
ATOM   3274 C  C     . ARG A 1 419 ? 34.591  74.103  106.308 1.00 93.29  ? 446 ARG A C     1 
ATOM   3275 O  O     . ARG A 1 419 ? 34.836  74.731  107.344 1.00 92.70  ? 446 ARG A O     1 
ATOM   3276 C  CB    . ARG A 1 419 ? 35.551  71.802  106.029 1.00 89.77  ? 446 ARG A CB    1 
ATOM   3277 C  CG    . ARG A 1 419 ? 35.413  70.310  106.296 1.00 98.03  ? 446 ARG A CG    1 
ATOM   3278 C  CD    . ARG A 1 419 ? 36.741  69.592  106.124 1.00 93.62  ? 446 ARG A CD    1 
ATOM   3279 N  NE    . ARG A 1 419 ? 37.344  69.874  104.827 1.00 102.90 ? 446 ARG A NE    1 
ATOM   3280 C  CZ    . ARG A 1 419 ? 38.467  69.325  104.390 1.00 108.36 ? 446 ARG A CZ    1 
ATOM   3281 N  NH1   . ARG A 1 419 ? 39.133  68.443  105.117 1.00 107.18 ? 446 ARG A NH1   1 
ATOM   3282 N  NH2   . ARG A 1 419 ? 38.934  69.666  103.192 1.00 119.54 ? 446 ARG A NH2   1 
ATOM   3283 N  N     . ARG A 1 420 ? 34.563  74.694  105.111 1.00 89.69  ? 447 ARG A N     1 
ATOM   3284 C  CA    . ARG A 1 420 ? 34.888  76.112  104.990 1.00 89.51  ? 447 ARG A CA    1 
ATOM   3285 C  C     . ARG A 1 420 ? 33.851  76.981  105.691 1.00 88.04  ? 447 ARG A C     1 
ATOM   3286 O  O     . ARG A 1 420 ? 34.200  78.002  106.298 1.00 83.39  ? 447 ARG A O     1 
ATOM   3287 C  CB    . ARG A 1 420 ? 35.018  76.500  103.518 1.00 88.32  ? 447 ARG A CB    1 
ATOM   3288 C  CG    . ARG A 1 420 ? 36.306  76.015  102.875 1.00 80.07  ? 447 ARG A CG    1 
ATOM   3289 C  CD    . ARG A 1 420 ? 36.216  76.010  101.360 1.00 85.85  ? 447 ARG A CD    1 
ATOM   3290 N  NE    . ARG A 1 420 ? 36.138  77.353  100.800 1.00 99.76  ? 447 ARG A NE    1 
ATOM   3291 C  CZ    . ARG A 1 420 ? 36.065  77.611  99.502  1.00 99.80  ? 447 ARG A CZ    1 
ATOM   3292 N  NH1   . ARG A 1 420 ? 36.053  76.639  98.606  1.00 81.86  ? 447 ARG A NH1   1 
ATOM   3293 N  NH2   . ARG A 1 420 ? 36.002  78.876  99.094  1.00 101.17 ? 447 ARG A NH2   1 
ATOM   3294 N  N     . LEU A 1 421 ? 32.575  76.590  105.630 1.00 84.65  ? 448 LEU A N     1 
ATOM   3295 C  CA    . LEU A 1 421 ? 31.533  77.372  106.289 1.00 78.35  ? 448 LEU A CA    1 
ATOM   3296 C  C     . LEU A 1 421 ? 31.591  77.203  107.800 1.00 86.92  ? 448 LEU A C     1 
ATOM   3297 O  O     . LEU A 1 421 ? 31.436  78.178  108.546 1.00 96.63  ? 448 LEU A O     1 
ATOM   3298 C  CB    . LEU A 1 421 ? 30.152  76.975  105.763 1.00 89.20  ? 448 LEU A CB    1 
ATOM   3299 C  CG    . LEU A 1 421 ? 28.954  77.692  106.399 1.00 89.36  ? 448 LEU A CG    1 
ATOM   3300 C  CD1   . LEU A 1 421 ? 29.087  79.198  106.247 1.00 75.94  ? 448 LEU A CD1   1 
ATOM   3301 C  CD2   . LEU A 1 421 ? 27.635  77.204  105.806 1.00 91.09  ? 448 LEU A CD2   1 
ATOM   3302 N  N     . MET A 1 422 ? 31.808  75.974  108.271 1.00 88.08  ? 449 MET A N     1 
ATOM   3303 C  CA    . MET A 1 422 ? 31.916  75.751  109.707 1.00 86.41  ? 449 MET A CA    1 
ATOM   3304 C  C     . MET A 1 422 ? 33.141  76.452  110.283 1.00 85.81  ? 449 MET A C     1 
ATOM   3305 O  O     . MET A 1 422 ? 33.077  77.017  111.382 1.00 81.59  ? 449 MET A O     1 
ATOM   3306 C  CB    . MET A 1 422 ? 31.950  74.252  110.005 1.00 82.83  ? 449 MET A CB    1 
ATOM   3307 C  CG    . MET A 1 422 ? 30.632  73.547  109.732 1.00 77.56  ? 449 MET A CG    1 
ATOM   3308 S  SD    . MET A 1 422 ? 30.628  71.838  110.302 1.00 98.80  ? 449 MET A SD    1 
ATOM   3309 C  CE    . MET A 1 422 ? 30.788  72.073  112.071 1.00 95.85  ? 449 MET A CE    1 
ATOM   3310 N  N     . ASN A 1 423 ? 34.261  76.434  109.554 1.00 83.63  ? 450 ASN A N     1 
ATOM   3311 C  CA    . ASN A 1 423 ? 35.452  77.144  110.012 1.00 85.45  ? 450 ASN A CA    1 
ATOM   3312 C  C     . ASN A 1 423 ? 35.189  78.638  110.142 1.00 93.83  ? 450 ASN A C     1 
ATOM   3313 O  O     . ASN A 1 423 ? 35.695  79.288  111.065 1.00 100.03 ? 450 ASN A O     1 
ATOM   3314 C  CB    . ASN A 1 423 ? 36.617  76.893  109.054 1.00 74.57  ? 450 ASN A CB    1 
ATOM   3315 C  CG    . ASN A 1 423 ? 37.113  75.461  109.092 1.00 88.80  ? 450 ASN A CG    1 
ATOM   3316 O  OD1   . ASN A 1 423 ? 36.597  74.634  109.843 1.00 99.55  ? 450 ASN A OD1   1 
ATOM   3317 N  ND2   . ASN A 1 423 ? 38.106  75.155  108.265 1.00 103.56 ? 450 ASN A ND2   1 
ATOM   3318 N  N     . LEU A 1 424 ? 34.390  79.198  109.232 1.00 90.57  ? 451 LEU A N     1 
ATOM   3319 C  CA    . LEU A 1 424 ? 34.058  80.616  109.311 1.00 93.85  ? 451 LEU A CA    1 
ATOM   3320 C  C     . LEU A 1 424 ? 33.233  80.919  110.555 1.00 93.70  ? 451 LEU A C     1 
ATOM   3321 O  O     . LEU A 1 424 ? 33.588  81.801  111.346 1.00 103.36 ? 451 LEU A O     1 
ATOM   3322 C  CB    . LEU A 1 424 ? 33.307  81.053  108.054 1.00 84.45  ? 451 LEU A CB    1 
ATOM   3323 C  CG    . LEU A 1 424 ? 32.784  82.484  108.141 1.00 93.75  ? 451 LEU A CG    1 
ATOM   3324 C  CD1   . LEU A 1 424 ? 33.923  83.478  107.962 1.00 104.36 ? 451 LEU A CD1   1 
ATOM   3325 C  CD2   . LEU A 1 424 ? 31.678  82.719  107.131 1.00 92.70  ? 451 LEU A CD2   1 
ATOM   3326 N  N     . MET A 1 425 ? 32.119  80.203  110.741 1.00 90.37  ? 452 MET A N     1 
ATOM   3327 C  CA    . MET A 1 425 ? 31.288  80.429  111.919 1.00 94.76  ? 452 MET A CA    1 
ATOM   3328 C  C     . MET A 1 425 ? 32.070  80.203  113.206 1.00 94.78  ? 452 MET A C     1 
ATOM   3329 O  O     . MET A 1 425 ? 31.811  80.869  114.215 1.00 113.18 ? 452 MET A O     1 
ATOM   3330 C  CB    . MET A 1 425 ? 30.057  79.522  111.879 1.00 88.29  ? 452 MET A CB    1 
ATOM   3331 C  CG    . MET A 1 425 ? 29.160  79.719  110.664 1.00 84.74  ? 452 MET A CG    1 
ATOM   3332 S  SD    . MET A 1 425 ? 28.494  81.389  110.521 1.00 113.84 ? 452 MET A SD    1 
ATOM   3333 C  CE    . MET A 1 425 ? 27.677  81.574  112.104 1.00 96.02  ? 452 MET A CE    1 
ATOM   3334 N  N     . ARG A 1 426 ? 33.031  79.279  113.191 1.00 100.16 ? 453 ARG A N     1 
ATOM   3335 C  CA    . ARG A 1 426 ? 33.864  79.063  114.369 1.00 95.97  ? 453 ARG A CA    1 
ATOM   3336 C  C     . ARG A 1 426 ? 34.834  80.220  114.573 1.00 100.60 ? 453 ARG A C     1 
ATOM   3337 O  O     . ARG A 1 426 ? 35.095  80.625  115.711 1.00 102.03 ? 453 ARG A O     1 
ATOM   3338 C  CB    . ARG A 1 426 ? 34.619  77.741  114.240 1.00 103.78 ? 453 ARG A CB    1 
ATOM   3339 C  CG    . ARG A 1 426 ? 35.393  77.342  115.481 1.00 101.25 ? 453 ARG A CG    1 
ATOM   3340 C  CD    . ARG A 1 426 ? 34.462  77.128  116.662 1.00 122.66 ? 453 ARG A CD    1 
ATOM   3341 N  NE    . ARG A 1 426 ? 35.128  76.420  117.747 1.00 117.40 ? 453 ARG A NE    1 
ATOM   3342 C  CZ    . ARG A 1 426 ? 35.310  75.107  117.775 1.00 123.00 ? 453 ARG A CZ    1 
ATOM   3343 N  NH1   . ARG A 1 426 ? 34.887  74.330  116.791 1.00 128.42 ? 453 ARG A NH1   1 
ATOM   3344 N  NH2   . ARG A 1 426 ? 35.937  74.561  118.813 1.00 130.95 ? 453 ARG A NH2   1 
ATOM   3345 N  N     . ASP A 1 427 ? 35.387  80.760  113.482 1.00 111.71 ? 454 ASP A N     1 
ATOM   3346 C  CA    . ASP A 1 427 ? 36.201  81.966  113.590 1.00 110.08 ? 454 ASP A CA    1 
ATOM   3347 C  C     . ASP A 1 427 ? 35.369  83.161  114.037 1.00 110.54 ? 454 ASP A C     1 
ATOM   3348 O  O     . ASP A 1 427 ? 35.886  84.058  114.713 1.00 110.61 ? 454 ASP A O     1 
ATOM   3349 C  CB    . ASP A 1 427 ? 36.886  82.266  112.256 1.00 114.26 ? 454 ASP A CB    1 
ATOM   3350 C  CG    . ASP A 1 427 ? 38.167  81.473  112.065 1.00 125.39 ? 454 ASP A CG    1 
ATOM   3351 O  OD1   . ASP A 1 427 ? 38.512  80.672  112.960 1.00 122.68 ? 454 ASP A OD1   1 
ATOM   3352 O  OD2   . ASP A 1 427 ? 38.831  81.659  111.021 1.00 119.15 ? 454 ASP A OD2   1 
ATOM   3353 N  N     . VAL A 1 428 ? 34.083  83.185  113.682 1.00 102.99 ? 455 VAL A N     1 
ATOM   3354 C  CA    . VAL A 1 428 ? 33.219  84.293  114.078 1.00 103.01 ? 455 VAL A CA    1 
ATOM   3355 C  C     . VAL A 1 428 ? 32.890  84.215  115.566 1.00 108.92 ? 455 VAL A C     1 
ATOM   3356 O  O     . VAL A 1 428 ? 33.062  85.189  116.307 1.00 114.89 ? 455 VAL A O     1 
ATOM   3357 C  CB    . VAL A 1 428 ? 31.941  84.310  113.220 1.00 105.25 ? 455 VAL A CB    1 
ATOM   3358 C  CG1   . VAL A 1 428 ? 30.900  85.231  113.843 1.00 94.50  ? 455 VAL A CG1   1 
ATOM   3359 C  CG2   . VAL A 1 428 ? 32.263  84.742  111.793 1.00 97.89  ? 455 VAL A CG2   1 
ATOM   3360 N  N     . GLU A 1 429 ? 32.410  83.056  116.027 1.00 114.72 ? 456 GLU A N     1 
ATOM   3361 C  CA    . GLU A 1 429 ? 31.970  82.947  117.414 1.00 116.60 ? 456 GLU A CA    1 
ATOM   3362 C  C     . GLU A 1 429 ? 33.141  83.020  118.388 1.00 118.99 ? 456 GLU A C     1 
ATOM   3363 O  O     . GLU A 1 429 ? 32.987  83.542  119.498 1.00 134.97 ? 456 GLU A O     1 
ATOM   3364 C  CB    . GLU A 1 429 ? 31.171  81.658  117.620 1.00 126.41 ? 456 GLU A CB    1 
ATOM   3365 C  CG    . GLU A 1 429 ? 31.977  80.374  117.504 1.00 141.08 ? 456 GLU A CG    1 
ATOM   3366 C  CD    . GLU A 1 429 ? 31.117  79.133  117.655 1.00 154.64 ? 456 GLU A CD    1 
ATOM   3367 O  OE1   . GLU A 1 429 ? 30.038  79.076  117.025 1.00 157.30 ? 456 GLU A OE1   1 
ATOM   3368 O  OE2   . GLU A 1 429 ? 31.514  78.220  118.410 1.00 159.50 ? 456 GLU A OE2   1 
ATOM   3369 N  N     . ARG A 1 430 ? 34.313  82.514  117.997 1.00 119.49 ? 457 ARG A N     1 
ATOM   3370 C  CA    . ARG A 1 430 ? 35.507  82.668  118.821 1.00 116.78 ? 457 ARG A CA    1 
ATOM   3371 C  C     . ARG A 1 430 ? 35.986  84.115  118.871 1.00 114.23 ? 457 ARG A C     1 
ATOM   3372 O  O     . ARG A 1 430 ? 36.791  84.458  119.743 1.00 124.31 ? 457 ARG A O     1 
ATOM   3373 C  CB    . ARG A 1 430 ? 36.617  81.735  118.304 1.00 112.93 ? 457 ARG A CB    1 
ATOM   3374 C  CG    . ARG A 1 430 ? 37.922  81.748  119.104 1.00 89.17  ? 457 ARG A CG    1 
ATOM   3375 C  CD    . ARG A 1 430 ? 38.800  80.518  118.845 1.00 87.53  ? 457 ARG A CD    1 
ATOM   3376 N  NE    . ARG A 1 430 ? 38.892  80.148  117.437 1.00 104.47 ? 457 ARG A NE    1 
ATOM   3377 C  CZ    . ARG A 1 430 ? 38.415  79.020  116.924 1.00 107.57 ? 457 ARG A CZ    1 
ATOM   3378 N  NH1   . ARG A 1 430 ? 37.810  78.118  117.680 1.00 101.89 ? 457 ARG A NH1   1 
ATOM   3379 N  NH2   . ARG A 1 430 ? 38.558  78.788  115.622 1.00 96.14  ? 457 ARG A NH2   1 
ATOM   3380 N  N     . GLU A 1 431 ? 35.490  84.977  117.981 1.00 127.86 ? 458 GLU A N     1 
ATOM   3381 C  CA    . GLU A 1 431 ? 35.854  86.386  117.973 1.00 135.64 ? 458 GLU A CA    1 
ATOM   3382 C  C     . GLU A 1 431 ? 34.771  87.302  118.524 1.00 138.30 ? 458 GLU A C     1 
ATOM   3383 O  O     . GLU A 1 431 ? 35.047  88.485  118.756 1.00 140.42 ? 458 GLU A O     1 
ATOM   3384 C  CB    . GLU A 1 431 ? 36.215  86.833  116.549 1.00 138.87 ? 458 GLU A CB    1 
ATOM   3385 C  CG    . GLU A 1 431 ? 37.617  86.433  116.115 1.00 144.82 ? 458 GLU A CG    1 
ATOM   3386 C  CD    . GLU A 1 431 ? 38.694  87.228  116.828 1.00 154.44 ? 458 GLU A CD    1 
ATOM   3387 O  OE1   . GLU A 1 431 ? 38.365  88.276  117.425 1.00 145.88 ? 458 GLU A OE1   1 
ATOM   3388 O  OE2   . GLU A 1 431 ? 39.870  86.807  116.791 1.00 160.48 ? 458 GLU A OE2   1 
ATOM   3389 N  N     . GLY A 1 432 ? 33.556  86.799  118.736 1.00 130.00 ? 459 GLY A N     1 
ATOM   3390 C  CA    . GLY A 1 432 ? 32.498  87.592  119.333 1.00 136.30 ? 459 GLY A CA    1 
ATOM   3391 C  C     . GLY A 1 432 ? 32.084  88.793  118.508 1.00 128.32 ? 459 GLY A C     1 
ATOM   3392 O  O     . GLY A 1 432 ? 31.956  89.904  119.032 1.00 135.88 ? 459 GLY A O     1 
ATOM   3393 N  N     . LEU A 1 433 ? 31.871  88.580  117.214 1.00 114.72 ? 460 LEU A N     1 
ATOM   3394 C  CA    . LEU A 1 433 ? 31.473  89.658  116.321 1.00 115.55 ? 460 LEU A CA    1 
ATOM   3395 C  C     . LEU A 1 433 ? 29.972  89.901  116.426 1.00 119.96 ? 460 LEU A C     1 
ATOM   3396 O  O     . LEU A 1 433 ? 29.181  88.953  116.426 1.00 120.88 ? 460 LEU A O     1 
ATOM   3397 C  CB    . LEU A 1 433 ? 31.855  89.315  114.881 1.00 105.46 ? 460 LEU A CB    1 
ATOM   3398 C  CG    . LEU A 1 433 ? 31.496  90.328  113.793 1.00 112.07 ? 460 LEU A CG    1 
ATOM   3399 C  CD1   . LEU A 1 433 ? 32.409  91.543  113.860 1.00 117.63 ? 460 LEU A CD1   1 
ATOM   3400 C  CD2   . LEU A 1 433 ? 31.560  89.676  112.421 1.00 106.50 ? 460 LEU A CD2   1 
ATOM   3401 N  N     . ASP A 1 434 ? 29.581  91.171  116.521 1.00 127.43 ? 461 ASP A N     1 
ATOM   3402 C  CA    . ASP A 1 434 ? 28.165  91.536  116.501 1.00 131.84 ? 461 ASP A CA    1 
ATOM   3403 C  C     . ASP A 1 434 ? 27.696  91.454  115.056 1.00 124.67 ? 461 ASP A C     1 
ATOM   3404 O  O     . ASP A 1 434 ? 27.742  92.430  114.305 1.00 127.71 ? 461 ASP A O     1 
ATOM   3405 C  CB    . ASP A 1 434 ? 27.943  92.927  117.086 1.00 135.28 ? 461 ASP A CB    1 
ATOM   3406 C  CG    . ASP A 1 434 ? 26.475  93.332  117.095 1.00 147.94 ? 461 ASP A CG    1 
ATOM   3407 O  OD1   . ASP A 1 434 ? 25.610  92.460  116.862 1.00 137.88 ? 461 ASP A OD1   1 
ATOM   3408 O  OD2   . ASP A 1 434 ? 26.187  94.527  117.332 1.00 158.60 ? 461 ASP A OD2   1 
ATOM   3409 N  N     . TRP A 1 435 ? 27.245  90.269  114.658 1.00 120.11 ? 462 TRP A N     1 
ATOM   3410 C  CA    . TRP A 1 435 ? 26.791  90.024  113.299 1.00 125.72 ? 462 TRP A CA    1 
ATOM   3411 C  C     . TRP A 1 435 ? 25.299  89.728  113.289 1.00 114.48 ? 462 TRP A C     1 
ATOM   3412 O  O     . TRP A 1 435 ? 24.755  89.144  114.231 1.00 113.36 ? 462 TRP A O     1 
ATOM   3413 C  CB    . TRP A 1 435 ? 27.554  88.861  112.651 1.00 120.11 ? 462 TRP A CB    1 
ATOM   3414 C  CG    . TRP A 1 435 ? 27.253  87.519  113.250 1.00 106.22 ? 462 TRP A CG    1 
ATOM   3415 C  CD1   . TRP A 1 435 ? 27.897  86.925  114.295 1.00 106.40 ? 462 TRP A CD1   1 
ATOM   3416 C  CD2   . TRP A 1 435 ? 26.234  86.600  112.833 1.00 101.90 ? 462 TRP A CD2   1 
ATOM   3417 N  NE1   . TRP A 1 435 ? 27.342  85.697  114.559 1.00 105.19 ? 462 TRP A NE1   1 
ATOM   3418 C  CE2   . TRP A 1 435 ? 26.319  85.473  113.676 1.00 105.63 ? 462 TRP A CE2   1 
ATOM   3419 C  CE3   . TRP A 1 435 ? 25.257  86.622  111.832 1.00 112.15 ? 462 TRP A CE3   1 
ATOM   3420 C  CZ2   . TRP A 1 435 ? 25.465  84.380  113.548 1.00 107.48 ? 462 TRP A CZ2   1 
ATOM   3421 C  CZ3   . TRP A 1 435 ? 24.411  85.535  111.705 1.00 108.81 ? 462 TRP A CZ3   1 
ATOM   3422 C  CH2   . TRP A 1 435 ? 24.520  84.430  112.560 1.00 113.62 ? 462 TRP A CH2   1 
ATOM   3423 N  N     . ASP A 1 436 ? 24.647  90.140  112.209 1.00 116.87 ? 463 ASP A N     1 
ATOM   3424 C  CA    . ASP A 1 436 ? 23.228  89.894  111.991 1.00 124.11 ? 463 ASP A CA    1 
ATOM   3425 C  C     . ASP A 1 436 ? 22.953  89.106  110.721 1.00 113.96 ? 463 ASP A C     1 
ATOM   3426 O  O     . ASP A 1 436 ? 22.038  88.278  110.700 1.00 113.07 ? 463 ASP A O     1 
ATOM   3427 C  CB    . ASP A 1 436 ? 22.461  91.228  111.944 1.00 131.17 ? 463 ASP A CB    1 
ATOM   3428 C  CG    . ASP A 1 436 ? 22.506  91.982  113.265 1.00 133.76 ? 463 ASP A CG    1 
ATOM   3429 O  OD1   . ASP A 1 436 ? 22.452  91.332  114.331 1.00 134.98 ? 463 ASP A OD1   1 
ATOM   3430 O  OD2   . ASP A 1 436 ? 22.595  93.228  113.234 1.00 135.74 ? 463 ASP A OD2   1 
ATOM   3431 N  N     . LEU A 1 437 ? 23.728  89.333  109.661 1.00 108.21 ? 464 LEU A N     1 
ATOM   3432 C  CA    . LEU A 1 437 ? 23.529  88.662  108.385 1.00 110.75 ? 464 LEU A CA    1 
ATOM   3433 C  C     . LEU A 1 437 ? 24.882  88.334  107.770 1.00 111.00 ? 464 LEU A C     1 
ATOM   3434 O  O     . LEU A 1 437 ? 25.795  89.163  107.786 1.00 118.31 ? 464 LEU A O     1 
ATOM   3435 C  CB    . LEU A 1 437 ? 22.713  89.533  107.419 1.00 100.01 ? 464 LEU A CB    1 
ATOM   3436 C  CG    . LEU A 1 437 ? 22.425  88.949  106.035 1.00 110.61 ? 464 LEU A CG    1 
ATOM   3437 C  CD1   . LEU A 1 437 ? 21.401  87.832  106.133 1.00 104.61 ? 464 LEU A CD1   1 
ATOM   3438 C  CD2   . LEU A 1 437 ? 21.960  90.031  105.071 1.00 112.21 ? 464 LEU A CD2   1 
ATOM   3439 N  N     . ILE A 1 438 ? 25.013  87.123  107.234 1.00 107.55 ? 465 ILE A N     1 
ATOM   3440 C  CA    . ILE A 1 438 ? 26.235  86.686  106.568 1.00 99.42  ? 465 ILE A CA    1 
ATOM   3441 C  C     . ILE A 1 438 ? 25.835  86.024  105.260 1.00 97.05  ? 465 ILE A C     1 
ATOM   3442 O  O     . ILE A 1 438 ? 25.284  84.917  105.266 1.00 104.92 ? 465 ILE A O     1 
ATOM   3443 C  CB    . ILE A 1 438 ? 27.064  85.722  107.428 1.00 99.37  ? 465 ILE A CB    1 
ATOM   3444 C  CG1   . ILE A 1 438 ? 27.460  86.376  108.751 1.00 98.24  ? 465 ILE A CG1   1 
ATOM   3445 C  CG2   . ILE A 1 438 ? 28.306  85.287  106.673 1.00 91.05  ? 465 ILE A CG2   1 
ATOM   3446 C  CD1   . ILE A 1 438 ? 28.349  85.511  109.608 1.00 90.78  ? 465 ILE A CD1   1 
ATOM   3447 N  N     . TYR A 1 439 ? 26.110  86.694  104.144 1.00 102.94 ? 466 TYR A N     1 
ATOM   3448 C  CA    . TYR A 1 439 ? 25.853  86.104  102.839 1.00 93.81  ? 466 TYR A CA    1 
ATOM   3449 C  C     . TYR A 1 439 ? 26.774  84.916  102.604 1.00 93.41  ? 466 TYR A C     1 
ATOM   3450 O  O     . TYR A 1 439 ? 27.943  84.929  102.999 1.00 98.14  ? 466 TYR A O     1 
ATOM   3451 C  CB    . TYR A 1 439 ? 26.055  87.137  101.729 1.00 99.11  ? 466 TYR A CB    1 
ATOM   3452 C  CG    . TYR A 1 439 ? 24.935  88.141  101.562 1.00 105.60 ? 466 TYR A CG    1 
ATOM   3453 C  CD1   . TYR A 1 439 ? 23.786  87.819  100.849 1.00 107.10 ? 466 TYR A CD1   1 
ATOM   3454 C  CD2   . TYR A 1 439 ? 25.038  89.422  102.094 1.00 109.12 ? 466 TYR A CD2   1 
ATOM   3455 C  CE1   . TYR A 1 439 ? 22.764  88.739  100.682 1.00 108.11 ? 466 TYR A CE1   1 
ATOM   3456 C  CE2   . TYR A 1 439 ? 24.021  90.349  101.932 1.00 112.71 ? 466 TYR A CE2   1 
ATOM   3457 C  CZ    . TYR A 1 439 ? 22.888  90.002  101.225 1.00 114.62 ? 466 TYR A CZ    1 
ATOM   3458 O  OH    . TYR A 1 439 ? 21.877  90.921  101.061 1.00 121.85 ? 466 TYR A OH    1 
ATOM   3459 N  N     . VAL A 1 440 ? 26.236  83.881  101.962 1.00 108.04 ? 467 VAL A N     1 
ATOM   3460 C  CA    . VAL A 1 440 ? 27.024  82.731  101.531 1.00 106.48 ? 467 VAL A CA    1 
ATOM   3461 C  C     . VAL A 1 440 ? 26.936  82.663  100.013 1.00 113.92 ? 467 VAL A C     1 
ATOM   3462 O  O     . VAL A 1 440 ? 27.863  82.199  99.339  1.00 116.14 ? 467 VAL A O     1 
ATOM   3463 C  CB    . VAL A 1 440 ? 26.534  81.428  102.188 1.00 108.53 ? 467 VAL A CB    1 
ATOM   3464 C  CG1   . VAL A 1 440 ? 27.412  80.256  101.777 1.00 106.98 ? 467 VAL A CG1   1 
ATOM   3465 C  CG2   . VAL A 1 440 ? 26.508  81.574  103.707 1.00 103.27 ? 467 VAL A CG2   1 
ATOM   3466 N  N     . GLY A 1 441 ? 25.815  83.132  99.471  1.00 111.07 ? 468 GLY A N     1 
ATOM   3467 C  CA    . GLY A 1 441 ? 25.645  83.293  98.042  1.00 104.95 ? 468 GLY A CA    1 
ATOM   3468 C  C     . GLY A 1 441 ? 24.972  84.614  97.738  1.00 111.65 ? 468 GLY A C     1 
ATOM   3469 O  O     . GLY A 1 441 ? 23.948  84.942  98.345  1.00 115.42 ? 468 GLY A O     1 
ATOM   3470 N  N     . ARG A 1 442 ? 25.536  85.385  96.813  1.00 107.67 ? 469 ARG A N     1 
ATOM   3471 C  CA    . ARG A 1 442 ? 25.030  86.716  96.499  1.00 116.77 ? 469 ARG A CA    1 
ATOM   3472 C  C     . ARG A 1 442 ? 25.714  87.201  95.230  1.00 120.23 ? 469 ARG A C     1 
ATOM   3473 O  O     . ARG A 1 442 ? 26.613  86.546  94.697  1.00 114.95 ? 469 ARG A O     1 
ATOM   3474 C  CB    . ARG A 1 442 ? 25.279  87.698  97.646  1.00 117.41 ? 469 ARG A CB    1 
ATOM   3475 C  CG    . ARG A 1 442 ? 26.734  87.750  98.085  1.00 110.42 ? 469 ARG A CG    1 
ATOM   3476 C  CD    . ARG A 1 442 ? 27.143  89.146  98.515  1.00 109.17 ? 469 ARG A CD    1 
ATOM   3477 N  NE    . ARG A 1 442 ? 28.568  89.226  98.813  1.00 113.64 ? 469 ARG A NE    1 
ATOM   3478 C  CZ    . ARG A 1 442 ? 29.225  90.356  99.036  1.00 121.29 ? 469 ARG A CZ    1 
ATOM   3479 N  NH1   . ARG A 1 442 ? 28.615  91.530  98.992  1.00 128.36 ? 469 ARG A NH1   1 
ATOM   3480 N  NH2   . ARG A 1 442 ? 30.527  90.308  99.305  1.00 111.63 ? 469 ARG A NH2   1 
ATOM   3481 N  N     . LYS A 1 443 ? 25.276  88.366  94.753  1.00 129.35 ? 470 LYS A N     1 
ATOM   3482 C  CA    . LYS A 1 443 ? 25.925  89.057  93.643  1.00 130.65 ? 470 LYS A CA    1 
ATOM   3483 C  C     . LYS A 1 443 ? 26.552  90.334  94.189  1.00 127.07 ? 470 LYS A C     1 
ATOM   3484 O  O     . LYS A 1 443 ? 25.842  91.239  94.641  1.00 127.13 ? 470 LYS A O     1 
ATOM   3485 C  CB    . LYS A 1 443 ? 24.944  89.365  92.513  1.00 124.02 ? 470 LYS A CB    1 
ATOM   3486 C  CG    . LYS A 1 443 ? 25.630  89.823  91.229  1.00 125.18 ? 470 LYS A CG    1 
ATOM   3487 C  CD    . LYS A 1 443 ? 24.641  90.058  90.099  1.00 137.89 ? 470 LYS A CD    1 
ATOM   3488 C  CE    . LYS A 1 443 ? 25.357  90.214  88.762  1.00 137.94 ? 470 LYS A CE    1 
ATOM   3489 N  NZ    . LYS A 1 443 ? 26.381  91.295  88.801  1.00 146.88 ? 470 LYS A NZ    1 
ATOM   3490 N  N     . ARG A 1 444 ? 27.878  90.397  94.151  1.00 117.22 ? 471 ARG A N     1 
ATOM   3491 C  CA    . ARG A 1 444 ? 28.614  91.551  94.648  1.00 121.18 ? 471 ARG A CA    1 
ATOM   3492 C  C     . ARG A 1 444 ? 28.557  92.674  93.618  1.00 124.34 ? 471 ARG A C     1 
ATOM   3493 O  O     . ARG A 1 444 ? 29.055  92.521  92.498  1.00 127.35 ? 471 ARG A O     1 
ATOM   3494 C  CB    . ARG A 1 444 ? 30.059  91.154  94.950  1.00 108.76 ? 471 ARG A CB    1 
ATOM   3495 C  CG    . ARG A 1 444 ? 30.989  92.312  95.251  1.00 117.00 ? 471 ARG A CG    1 
ATOM   3496 C  CD    . ARG A 1 444 ? 32.418  91.821  95.403  1.00 114.03 ? 471 ARG A CD    1 
ATOM   3497 N  NE    . ARG A 1 444 ? 33.389  92.896  95.241  1.00 123.62 ? 471 ARG A NE    1 
ATOM   3498 C  CZ    . ARG A 1 444 ? 34.700  92.716  95.161  1.00 127.75 ? 471 ARG A CZ    1 
ATOM   3499 N  NH1   . ARG A 1 444 ? 35.238  91.510  95.237  1.00 126.03 ? 471 ARG A NH1   1 
ATOM   3500 N  NH2   . ARG A 1 444 ? 35.491  93.772  94.997  1.00 125.28 ? 471 ARG A NH2   1 
ATOM   3501 N  N     . MET A 1 445 ? 27.944  93.797  93.993  1.00 124.41 ? 472 MET A N     1 
ATOM   3502 C  CA    . MET A 1 445 ? 27.809  94.928  93.085  1.00 123.15 ? 472 MET A CA    1 
ATOM   3503 C  C     . MET A 1 445 ? 28.967  95.912  93.178  1.00 124.04 ? 472 MET A C     1 
ATOM   3504 O  O     . MET A 1 445 ? 29.224  96.636  92.209  1.00 138.01 ? 472 MET A O     1 
ATOM   3505 C  CB    . MET A 1 445 ? 26.491  95.663  93.349  1.00 135.22 ? 472 MET A CB    1 
ATOM   3506 C  CG    . MET A 1 445 ? 25.260  94.769  93.266  1.00 143.32 ? 472 MET A CG    1 
ATOM   3507 S  SD    . MET A 1 445 ? 25.003  94.055  91.627  1.00 133.02 ? 472 MET A SD    1 
ATOM   3508 C  CE    . MET A 1 445 ? 24.527  95.513  90.701  1.00 130.85 ? 472 MET A CE    1 
ATOM   3509 N  N     . GLN A 1 446 ? 29.665  95.962  94.311  1.00 120.39 ? 473 GLN A N     1 
ATOM   3510 C  CA    . GLN A 1 446 ? 30.870  96.778  94.443  1.00 127.33 ? 473 GLN A CA    1 
ATOM   3511 C  C     . GLN A 1 446 ? 32.047  95.963  93.920  1.00 133.39 ? 473 GLN A C     1 
ATOM   3512 O  O     . GLN A 1 446 ? 32.578  95.095  94.618  1.00 135.80 ? 473 GLN A O     1 
ATOM   3513 C  CB    . GLN A 1 446 ? 31.075  97.207  95.892  1.00 127.22 ? 473 GLN A CB    1 
ATOM   3514 C  CG    . GLN A 1 446 ? 32.441  97.818  96.191  1.00 128.84 ? 473 GLN A CG    1 
ATOM   3515 C  CD    . GLN A 1 446 ? 32.798  98.952  95.251  1.00 145.70 ? 473 GLN A CD    1 
ATOM   3516 O  OE1   . GLN A 1 446 ? 33.619  98.787  94.347  1.00 148.74 ? 473 GLN A OE1   1 
ATOM   3517 N  NE2   . GLN A 1 446 ? 32.187  100.114 95.462  1.00 157.84 ? 473 GLN A NE2   1 
ATOM   3518 N  N     . VAL A 1 447 ? 32.452  96.233  92.681  1.00 132.32 ? 474 VAL A N     1 
ATOM   3519 C  CA    . VAL A 1 447 ? 33.520  95.479  92.034  1.00 134.38 ? 474 VAL A CA    1 
ATOM   3520 C  C     . VAL A 1 447 ? 34.734  96.330  91.694  1.00 139.03 ? 474 VAL A C     1 
ATOM   3521 O  O     . VAL A 1 447 ? 35.765  95.769  91.294  1.00 139.23 ? 474 VAL A O     1 
ATOM   3522 C  CB    . VAL A 1 447 ? 33.016  94.757  90.765  1.00 132.06 ? 474 VAL A CB    1 
ATOM   3523 C  CG1   . VAL A 1 447 ? 31.999  93.686  91.133  1.00 121.60 ? 474 VAL A CG1   1 
ATOM   3524 C  CG2   . VAL A 1 447 ? 32.418  95.755  89.786  1.00 136.23 ? 474 VAL A CG2   1 
ATOM   3525 N  N     . GLU A 1 448 ? 34.656  97.655  91.826  1.00 139.55 ? 475 GLU A N     1 
ATOM   3526 C  CA    . GLU A 1 448 ? 35.828  98.496  91.612  1.00 139.78 ? 475 GLU A CA    1 
ATOM   3527 C  C     . GLU A 1 448 ? 36.908  98.153  92.629  1.00 143.16 ? 475 GLU A C     1 
ATOM   3528 O  O     . GLU A 1 448 ? 37.975  97.646  92.269  1.00 142.03 ? 475 GLU A O     1 
ATOM   3529 C  CB    . GLU A 1 448 ? 35.467  99.978  91.708  1.00 131.76 ? 475 GLU A CB    1 
ATOM   3530 C  CG    . GLU A 1 448 ? 34.654  100.502 90.546  1.00 140.86 ? 475 GLU A CG    1 
ATOM   3531 C  CD    . GLU A 1 448 ? 34.469  102.005 90.606  1.00 150.67 ? 475 GLU A CD    1 
ATOM   3532 O  OE1   . GLU A 1 448 ? 35.370  102.699 91.127  1.00 142.74 ? 475 GLU A OE1   1 
ATOM   3533 O  OE2   . GLU A 1 448 ? 33.419  102.490 90.139  1.00 155.72 ? 475 GLU A OE2   1 
ATOM   3534 N  N     . HIS A 1 449 ? 36.632  98.422  93.903  1.00 146.20 ? 476 HIS A N     1 
ATOM   3535 C  CA    . HIS A 1 449 ? 37.558  98.120  94.978  1.00 144.61 ? 476 HIS A CA    1 
ATOM   3536 C  C     . HIS A 1 449 ? 37.018  96.989  95.847  1.00 139.51 ? 476 HIS A C     1 
ATOM   3537 O  O     . HIS A 1 449 ? 35.802  96.850  96.014  1.00 136.49 ? 476 HIS A O     1 
ATOM   3538 C  CB    . HIS A 1 449 ? 37.823  99.355  95.851  1.00 148.89 ? 476 HIS A CB    1 
ATOM   3539 C  CG    . HIS A 1 449 ? 36.588  99.962  96.446  1.00 145.77 ? 476 HIS A CG    1 
ATOM   3540 N  ND1   . HIS A 1 449 ? 35.989  99.469  97.585  1.00 147.63 ? 476 HIS A ND1   1 
ATOM   3541 C  CD2   . HIS A 1 449 ? 35.849  101.032 96.066  1.00 150.50 ? 476 HIS A CD2   1 
ATOM   3542 C  CE1   . HIS A 1 449 ? 34.931  100.204 97.878  1.00 156.55 ? 476 HIS A CE1   1 
ATOM   3543 N  NE2   . HIS A 1 449 ? 34.824  101.160 96.971  1.00 158.74 ? 476 HIS A NE2   1 
ATOM   3544 N  N     . PRO A 1 450 ? 37.898  96.152  96.398  1.00 130.36 ? 477 PRO A N     1 
ATOM   3545 C  CA    . PRO A 1 450 ? 37.442  95.107  97.321  1.00 125.08 ? 477 PRO A CA    1 
ATOM   3546 C  C     . PRO A 1 450 ? 36.757  95.701  98.543  1.00 126.75 ? 477 PRO A C     1 
ATOM   3547 O  O     . PRO A 1 450 ? 37.056  96.818  98.973  1.00 139.10 ? 477 PRO A O     1 
ATOM   3548 C  CB    . PRO A 1 450 ? 38.735  94.373  97.699  1.00 114.61 ? 477 PRO A CB    1 
ATOM   3549 C  CG    . PRO A 1 450 ? 39.848  95.303  97.310  1.00 117.23 ? 477 PRO A CG    1 
ATOM   3550 C  CD    . PRO A 1 450 ? 39.342  96.062  96.128  1.00 121.64 ? 477 PRO A CD    1 
ATOM   3551 N  N     . GLU A 1 451 ? 35.822  94.937  99.099  1.00 126.50 ? 478 GLU A N     1 
ATOM   3552 C  CA    . GLU A 1 451 ? 35.021  95.402  100.220 1.00 138.91 ? 478 GLU A CA    1 
ATOM   3553 C  C     . GLU A 1 451 ? 35.808  95.297  101.524 1.00 129.94 ? 478 GLU A C     1 
ATOM   3554 O  O     . GLU A 1 451 ? 36.770  94.534  101.641 1.00 130.12 ? 478 GLU A O     1 
ATOM   3555 C  CB    . GLU A 1 451 ? 33.719  94.605  100.302 1.00 132.14 ? 478 GLU A CB    1 
ATOM   3556 C  CG    . GLU A 1 451 ? 32.872  94.728  99.043  1.00 135.04 ? 478 GLU A CG    1 
ATOM   3557 C  CD    . GLU A 1 451 ? 31.760  93.704  98.971  1.00 129.75 ? 478 GLU A CD    1 
ATOM   3558 O  OE1   . GLU A 1 451 ? 31.842  92.685  99.686  1.00 133.80 ? 478 GLU A OE1   1 
ATOM   3559 O  OE2   . GLU A 1 451 ? 30.805  93.918  98.194  1.00 133.68 ? 478 GLU A OE2   1 
ATOM   3560 N  N     . LYS A 1 452 ? 35.383  96.082  102.514 1.00 123.47 ? 479 LYS A N     1 
ATOM   3561 C  CA    . LYS A 1 452 ? 36.145  96.217  103.752 1.00 128.36 ? 479 LYS A CA    1 
ATOM   3562 C  C     . LYS A 1 452 ? 36.160  94.898  104.515 1.00 127.38 ? 479 LYS A C     1 
ATOM   3563 O  O     . LYS A 1 452 ? 35.103  94.359  104.863 1.00 129.53 ? 479 LYS A O     1 
ATOM   3564 C  CB    . LYS A 1 452 ? 35.564  97.327  104.623 1.00 127.65 ? 479 LYS A CB    1 
ATOM   3565 C  CG    . LYS A 1 452 ? 36.416  97.633  105.850 1.00 125.85 ? 479 LYS A CG    1 
ATOM   3566 C  CD    . LYS A 1 452 ? 35.733  98.606  106.798 1.00 135.19 ? 479 LYS A CD    1 
ATOM   3567 C  CE    . LYS A 1 452 ? 36.595  98.857  108.027 1.00 133.14 ? 479 LYS A CE    1 
ATOM   3568 N  NZ    . LYS A 1 452 ? 35.875  99.631  109.076 1.00 139.76 ? 479 LYS A NZ    1 
ATOM   3569 N  N     . ALA A 1 453 ? 37.358  94.387  104.782 1.00 117.43 ? 480 ALA A N     1 
ATOM   3570 C  CA    . ALA A 1 453 ? 37.502  93.130  105.497 1.00 109.91 ? 480 ALA A CA    1 
ATOM   3571 C  C     . ALA A 1 453 ? 37.198  93.316  106.981 1.00 119.74 ? 480 ALA A C     1 
ATOM   3572 O  O     . ALA A 1 453 ? 37.253  94.423  107.524 1.00 120.27 ? 480 ALA A O     1 
ATOM   3573 C  CB    . ALA A 1 453 ? 38.911  92.567  105.319 1.00 96.24  ? 480 ALA A CB    1 
ATOM   3574 N  N     . VAL A 1 454 ? 36.876  92.207  107.634 1.00 117.40 ? 481 VAL A N     1 
ATOM   3575 C  CA    . VAL A 1 454 ? 36.586  92.182  109.064 1.00 113.60 ? 481 VAL A CA    1 
ATOM   3576 C  C     . VAL A 1 454 ? 37.852  91.730  109.788 1.00 115.21 ? 481 VAL A C     1 
ATOM   3577 O  O     . VAL A 1 454 ? 38.285  90.586  109.588 1.00 123.88 ? 481 VAL A O     1 
ATOM   3578 C  CB    . VAL A 1 454 ? 35.408  91.251  109.385 1.00 114.91 ? 481 VAL A CB    1 
ATOM   3579 C  CG1   . VAL A 1 454 ? 35.090  91.292  110.869 1.00 110.33 ? 481 VAL A CG1   1 
ATOM   3580 C  CG2   . VAL A 1 454 ? 34.194  91.636  108.555 1.00 112.29 ? 481 VAL A CG2   1 
ATOM   3581 N  N     . PRO A 1 455 ? 38.468  92.577  110.609 1.00 127.96 ? 482 PRO A N     1 
ATOM   3582 C  CA    . PRO A 1 455 ? 39.718  92.182  111.268 1.00 133.46 ? 482 PRO A CA    1 
ATOM   3583 C  C     . PRO A 1 455 ? 39.526  90.957  112.150 1.00 129.87 ? 482 PRO A C     1 
ATOM   3584 O  O     . PRO A 1 455 ? 38.466  90.752  112.746 1.00 129.48 ? 482 PRO A O     1 
ATOM   3585 C  CB    . PRO A 1 455 ? 40.087  93.417  112.099 1.00 136.48 ? 482 PRO A CB    1 
ATOM   3586 C  CG    . PRO A 1 455 ? 39.372  94.550  111.436 1.00 139.77 ? 482 PRO A CG    1 
ATOM   3587 C  CD    . PRO A 1 455 ? 38.092  93.966  110.917 1.00 132.88 ? 482 PRO A CD    1 
ATOM   3588 N  N     . ARG A 1 456 ? 40.572  90.131  112.208 1.00 127.73 ? 483 ARG A N     1 
ATOM   3589 C  CA    . ARG A 1 456 ? 40.696  88.946  113.053 1.00 119.65 ? 483 ARG A CA    1 
ATOM   3590 C  C     . ARG A 1 456 ? 39.768  87.803  112.648 1.00 112.78 ? 483 ARG A C     1 
ATOM   3591 O  O     . ARG A 1 456 ? 39.743  86.777  113.341 1.00 113.94 ? 483 ARG A O     1 
ATOM   3592 C  CB    . ARG A 1 456 ? 40.466  89.268  114.539 1.00 125.06 ? 483 ARG A CB    1 
ATOM   3593 C  CG    . ARG A 1 456 ? 41.564  90.118  115.171 1.00 120.25 ? 483 ARG A CG    1 
ATOM   3594 C  CD    . ARG A 1 456 ? 41.158  90.653  116.541 1.00 123.82 ? 483 ARG A CD    1 
ATOM   3595 N  NE    . ARG A 1 456 ? 40.214  91.761  116.447 1.00 133.69 ? 483 ARG A NE    1 
ATOM   3596 C  CZ    . ARG A 1 456 ? 38.905  91.655  116.633 1.00 138.96 ? 483 ARG A CZ    1 
ATOM   3597 N  NH1   . ARG A 1 456 ? 38.340  90.498  116.939 1.00 131.43 ? 483 ARG A NH1   1 
ATOM   3598 N  NH2   . ARG A 1 456 ? 38.143  92.738  116.510 1.00 140.32 ? 483 ARG A NH2   1 
ATOM   3599 N  N     . VAL A 1 457 ? 39.015  87.932  111.557 1.00 109.80 ? 484 VAL A N     1 
ATOM   3600 C  CA    . VAL A 1 457 ? 38.145  86.867  111.064 1.00 105.12 ? 484 VAL A CA    1 
ATOM   3601 C  C     . VAL A 1 457 ? 38.458  86.672  109.588 1.00 108.73 ? 484 VAL A C     1 
ATOM   3602 O  O     . VAL A 1 457 ? 38.070  87.497  108.752 1.00 110.40 ? 484 VAL A O     1 
ATOM   3603 C  CB    . VAL A 1 457 ? 36.655  87.177  111.272 1.00 110.29 ? 484 VAL A CB    1 
ATOM   3604 C  CG1   . VAL A 1 457 ? 35.796  86.099  110.633 1.00 104.03 ? 484 VAL A CG1   1 
ATOM   3605 C  CG2   . VAL A 1 457 ? 36.338  87.289  112.754 1.00 98.28  ? 484 VAL A CG2   1 
ATOM   3606 N  N     . ARG A 1 458 ? 39.148  85.583  109.266 1.00 113.25 ? 485 ARG A N     1 
ATOM   3607 C  CA    . ARG A 1 458 ? 39.575  85.342  107.897 1.00 109.20 ? 485 ARG A CA    1 
ATOM   3608 C  C     . ARG A 1 458 ? 38.384  85.014  107.003 1.00 112.25 ? 485 ARG A C     1 
ATOM   3609 O  O     . ARG A 1 458 ? 37.379  84.450  107.446 1.00 109.72 ? 485 ARG A O     1 
ATOM   3610 C  CB    . ARG A 1 458 ? 40.602  84.209  107.854 1.00 110.55 ? 485 ARG A CB    1 
ATOM   3611 C  CG    . ARG A 1 458 ? 41.998  84.634  108.280 1.00 116.88 ? 485 ARG A CG    1 
ATOM   3612 C  CD    . ARG A 1 458 ? 42.959  83.454  108.381 1.00 126.22 ? 485 ARG A CD    1 
ATOM   3613 N  NE    . ARG A 1 458 ? 42.867  82.778  109.671 1.00 134.49 ? 485 ARG A NE    1 
ATOM   3614 C  CZ    . ARG A 1 458 ? 42.224  81.637  109.878 1.00 144.51 ? 485 ARG A CZ    1 
ATOM   3615 N  NH1   . ARG A 1 458 ? 41.615  80.998  108.892 1.00 155.13 ? 485 ARG A NH1   1 
ATOM   3616 N  NH2   . ARG A 1 458 ? 42.195  81.122  111.104 1.00 141.49 ? 485 ARG A NH2   1 
ATOM   3617 N  N     . ASN A 1 459 ? 38.505  85.399  105.731 1.00 107.11 ? 486 ASN A N     1 
ATOM   3618 C  CA    . ASN A 1 459 ? 37.525  85.076  104.692 1.00 111.58 ? 486 ASN A CA    1 
ATOM   3619 C  C     . ASN A 1 459 ? 36.158  85.706  104.965 1.00 107.81 ? 486 ASN A C     1 
ATOM   3620 O  O     . ASN A 1 459 ? 35.129  85.211  104.494 1.00 106.96 ? 486 ASN A O     1 
ATOM   3621 C  CB    . ASN A 1 459 ? 37.381  83.560  104.510 1.00 118.12 ? 486 ASN A CB    1 
ATOM   3622 C  CG    . ASN A 1 459 ? 38.665  82.899  104.053 1.00 112.74 ? 486 ASN A CG    1 
ATOM   3623 O  OD1   . ASN A 1 459 ? 39.583  83.564  103.578 1.00 124.34 ? 486 ASN A OD1   1 
ATOM   3624 N  ND2   . ASN A 1 459 ? 38.731  81.578  104.184 1.00 111.30 ? 486 ASN A ND2   1 
ATOM   3625 N  N     . LEU A 1 460 ? 36.119  86.802  105.719 1.00 105.41 ? 487 LEU A N     1 
ATOM   3626 C  CA    . LEU A 1 460 ? 34.873  87.507  105.995 1.00 103.32 ? 487 LEU A CA    1 
ATOM   3627 C  C     . LEU A 1 460 ? 35.046  88.987  105.689 1.00 107.71 ? 487 LEU A C     1 
ATOM   3628 O  O     . LEU A 1 460 ? 36.048  89.593  106.083 1.00 106.59 ? 487 LEU A O     1 
ATOM   3629 C  CB    . LEU A 1 460 ? 34.430  87.323  107.449 1.00 100.18 ? 487 LEU A CB    1 
ATOM   3630 C  CG    . LEU A 1 460 ? 33.045  87.900  107.753 1.00 102.03 ? 487 LEU A CG    1 
ATOM   3631 C  CD1   . LEU A 1 460 ? 31.950  87.060  107.105 1.00 85.21  ? 487 LEU A CD1   1 
ATOM   3632 C  CD2   . LEU A 1 460 ? 32.820  88.030  109.249 1.00 108.41 ? 487 LEU A CD2   1 
ATOM   3633 N  N     . VAL A 1 461 ? 34.065  89.565  104.990 1.00 104.48 ? 488 VAL A N     1 
ATOM   3634 C  CA    . VAL A 1 461 ? 34.090  90.972  104.616 1.00 110.90 ? 488 VAL A CA    1 
ATOM   3635 C  C     . VAL A 1 461 ? 32.751  91.608  104.959 1.00 118.22 ? 488 VAL A C     1 
ATOM   3636 O  O     . VAL A 1 461 ? 31.725  90.934  105.070 1.00 108.86 ? 488 VAL A O     1 
ATOM   3637 C  CB    . VAL A 1 461 ? 34.403  91.181  103.118 1.00 103.12 ? 488 VAL A CB    1 
ATOM   3638 C  CG1   . VAL A 1 461 ? 35.825  90.742  102.803 1.00 118.12 ? 488 VAL A CG1   1 
ATOM   3639 C  CG2   . VAL A 1 461 ? 33.394  90.432  102.250 1.00 99.44  ? 488 VAL A CG2   1 
ATOM   3640 N  N     . GLU A 1 462 ? 32.777  92.929  105.126 1.00 120.74 ? 489 GLU A N     1 
ATOM   3641 C  CA    . GLU A 1 462 ? 31.555  93.690  105.346 1.00 114.13 ? 489 GLU A CA    1 
ATOM   3642 C  C     . GLU A 1 462 ? 30.775  93.803  104.042 1.00 122.83 ? 489 GLU A C     1 
ATOM   3643 O  O     . GLU A 1 462 ? 31.311  94.243  103.019 1.00 128.58 ? 489 GLU A O     1 
ATOM   3644 C  CB    . GLU A 1 462 ? 31.882  95.082  105.892 1.00 122.60 ? 489 GLU A CB    1 
ATOM   3645 C  CG    . GLU A 1 462 ? 32.683  95.080  107.185 1.00 130.17 ? 489 GLU A CG    1 
ATOM   3646 C  CD    . GLU A 1 462 ? 32.960  96.482  107.705 1.00 135.24 ? 489 GLU A CD    1 
ATOM   3647 O  OE1   . GLU A 1 462 ? 32.403  97.447  107.139 1.00 128.31 ? 489 GLU A OE1   1 
ATOM   3648 O  OE2   . GLU A 1 462 ? 33.735  96.617  108.677 1.00 128.03 ? 489 GLU A OE2   1 
ATOM   3649 N  N     . ALA A 1 463 ? 29.506  93.408  104.082 1.00 124.27 ? 490 ALA A N     1 
ATOM   3650 C  CA    . ALA A 1 463 ? 28.704  93.331  102.868 1.00 127.48 ? 490 ALA A CA    1 
ATOM   3651 C  C     . ALA A 1 463 ? 28.367  94.729  102.360 1.00 135.47 ? 490 ALA A C     1 
ATOM   3652 O  O     . ALA A 1 463 ? 27.686  95.499  103.046 1.00 133.08 ? 490 ALA A O     1 
ATOM   3653 C  CB    . ALA A 1 463 ? 27.427  92.534  103.127 1.00 122.30 ? 490 ALA A CB    1 
ATOM   3654 N  N     . ASP A 1 464 ? 28.853  95.059  101.162 1.00 137.48 ? 491 ASP A N     1 
ATOM   3655 C  CA    . ASP A 1 464 ? 28.437  96.280  100.483 1.00 144.01 ? 491 ASP A CA    1 
ATOM   3656 C  C     . ASP A 1 464 ? 27.172  95.995  99.684  1.00 135.72 ? 491 ASP A C     1 
ATOM   3657 O  O     . ASP A 1 464 ? 26.384  95.123  100.062 1.00 133.19 ? 491 ASP A O     1 
ATOM   3658 C  CB    . ASP A 1 464 ? 29.550  96.817  99.577  1.00 142.69 ? 491 ASP A CB    1 
ATOM   3659 C  CG    . ASP A 1 464 ? 30.744  97.337  100.359 1.00 148.17 ? 491 ASP A CG    1 
ATOM   3660 O  OD1   . ASP A 1 464 ? 30.740  97.224  101.605 1.00 150.06 ? 491 ASP A OD1   1 
ATOM   3661 O  OD2   . ASP A 1 464 ? 31.685  97.862  99.725  1.00 131.91 ? 491 ASP A OD2   1 
ATOM   3662 N  N     . TYR A 1 465 ? 26.966  96.711  98.581  1.00 133.20 ? 492 TYR A N     1 
ATOM   3663 C  CA    . TYR A 1 465 ? 25.756  96.504  97.795  1.00 134.56 ? 492 TYR A CA    1 
ATOM   3664 C  C     . TYR A 1 465 ? 25.719  95.090  97.231  1.00 137.48 ? 492 TYR A C     1 
ATOM   3665 O  O     . TYR A 1 465 ? 26.571  94.715  96.420  1.00 133.09 ? 492 TYR A O     1 
ATOM   3666 C  CB    . TYR A 1 465 ? 25.654  97.528  96.662  1.00 132.69 ? 492 TYR A CB    1 
ATOM   3667 C  CG    . TYR A 1 465 ? 24.284  97.570  96.021  1.00 144.03 ? 492 TYR A CG    1 
ATOM   3668 C  CD1   . TYR A 1 465 ? 23.147  97.229  96.744  1.00 145.85 ? 492 TYR A CD1   1 
ATOM   3669 C  CD2   . TYR A 1 465 ? 24.126  97.939  94.690  1.00 151.58 ? 492 TYR A CD2   1 
ATOM   3670 C  CE1   . TYR A 1 465 ? 21.890  97.265  96.164  1.00 148.44 ? 492 TYR A CE1   1 
ATOM   3671 C  CE2   . TYR A 1 465 ? 22.874  97.973  94.100  1.00 149.82 ? 492 TYR A CE2   1 
ATOM   3672 C  CZ    . TYR A 1 465 ? 21.759  97.636  94.841  1.00 147.84 ? 492 TYR A CZ    1 
ATOM   3673 O  OH    . TYR A 1 465 ? 20.513  97.671  94.258  1.00 142.64 ? 492 TYR A OH    1 
ATOM   3674 N  N     . SER A 1 466 ? 24.748  94.295  97.668  1.00 139.94 ? 493 SER A N     1 
ATOM   3675 C  CA    . SER A 1 466 ? 24.549  92.939  97.179  1.00 140.61 ? 493 SER A CA    1 
ATOM   3676 C  C     . SER A 1 466 ? 23.172  92.843  96.535  1.00 142.02 ? 493 SER A C     1 
ATOM   3677 O  O     . SER A 1 466 ? 22.336  93.738  96.670  1.00 139.44 ? 493 SER A O     1 
ATOM   3678 C  CB    . SER A 1 466 ? 24.691  91.916  98.311  1.00 137.88 ? 493 SER A CB    1 
ATOM   3679 O  OG    . SER A 1 466 ? 25.940  92.062  98.966  1.00 133.36 ? 493 SER A OG    1 
ATOM   3680 N  N     . TYR A 1 467 ? 22.927  91.738  95.827  1.00 153.24 ? 494 TYR A N     1 
ATOM   3681 C  CA    . TYR A 1 467 ? 21.705  91.680  95.032  1.00 158.39 ? 494 TYR A CA    1 
ATOM   3682 C  C     . TYR A 1 467 ? 21.040  90.307  94.958  1.00 152.38 ? 494 TYR A C     1 
ATOM   3683 O  O     . TYR A 1 467 ? 20.131  90.139  94.137  1.00 155.54 ? 494 TYR A O     1 
ATOM   3684 C  CB    . TYR A 1 467 ? 22.007  92.182  93.607  1.00 168.74 ? 494 TYR A CB    1 
ATOM   3685 C  CG    . TYR A 1 467 ? 20.870  92.936  92.957  1.00 168.63 ? 494 TYR A CG    1 
ATOM   3686 C  CD1   . TYR A 1 467 ? 20.625  94.268  93.268  1.00 168.16 ? 494 TYR A CD1   1 
ATOM   3687 C  CD2   . TYR A 1 467 ? 20.049  92.320  92.023  1.00 171.01 ? 494 TYR A CD2   1 
ATOM   3688 C  CE1   . TYR A 1 467 ? 19.588  94.963  92.671  1.00 177.64 ? 494 TYR A CE1   1 
ATOM   3689 C  CE2   . TYR A 1 467 ? 19.011  93.003  91.422  1.00 181.00 ? 494 TYR A CE2   1 
ATOM   3690 C  CZ    . TYR A 1 467 ? 18.784  94.325  91.748  1.00 187.27 ? 494 TYR A CZ    1 
ATOM   3691 O  OH    . TYR A 1 467 ? 17.751  95.009  91.149  1.00 192.33 ? 494 TYR A OH    1 
ATOM   3692 N  N     . TRP A 1 468 ? 21.422  89.330  95.773  1.00 125.55 ? 495 TRP A N     1 
ATOM   3693 C  CA    . TRP A 1 468 ? 20.788  88.019  95.727  1.00 122.27 ? 495 TRP A CA    1 
ATOM   3694 C  C     . TRP A 1 468 ? 20.425  87.557  97.134  1.00 132.60 ? 495 TRP A C     1 
ATOM   3695 O  O     . TRP A 1 468 ? 20.745  88.207  98.134  1.00 129.91 ? 495 TRP A O     1 
ATOM   3696 C  CB    . TRP A 1 468 ? 21.690  86.980  95.045  1.00 120.83 ? 495 TRP A CB    1 
ATOM   3697 C  CG    . TRP A 1 468 ? 21.645  87.035  93.547  1.00 127.24 ? 495 TRP A CG    1 
ATOM   3698 C  CD1   . TRP A 1 468 ? 20.653  87.567  92.775  1.00 119.17 ? 495 TRP A CD1   1 
ATOM   3699 C  CD2   . TRP A 1 468 ? 22.638  86.541  92.638  1.00 121.48 ? 495 TRP A CD2   1 
ATOM   3700 N  NE1   . TRP A 1 468 ? 20.966  87.434  91.443  1.00 112.56 ? 495 TRP A NE1   1 
ATOM   3701 C  CE2   . TRP A 1 468 ? 22.179  86.807  91.333  1.00 117.50 ? 495 TRP A CE2   1 
ATOM   3702 C  CE3   . TRP A 1 468 ? 23.869  85.897  92.803  1.00 114.30 ? 495 TRP A CE3   1 
ATOM   3703 C  CZ2   . TRP A 1 468 ? 22.908  86.453  90.197  1.00 120.50 ? 495 TRP A CZ2   1 
ATOM   3704 C  CZ3   . TRP A 1 468 ? 24.592  85.548  91.673  1.00 120.21 ? 495 TRP A CZ3   1 
ATOM   3705 C  CH2   . TRP A 1 468 ? 24.108  85.826  90.388  1.00 122.05 ? 495 TRP A CH2   1 
ATOM   3706 N  N     . THR A 1 469 ? 19.744  86.415  97.197  1.00 126.41 ? 496 THR A N     1 
ATOM   3707 C  CA    . THR A 1 469 ? 19.400  85.760  98.454  1.00 117.88 ? 496 THR A CA    1 
ATOM   3708 C  C     . THR A 1 469 ? 19.530  84.251  98.311  1.00 114.26 ? 496 THR A C     1 
ATOM   3709 O  O     . THR A 1 469 ? 18.697  83.489  98.813  1.00 111.56 ? 496 THR A O     1 
ATOM   3710 C  CB    . THR A 1 469 ? 17.989  86.134  98.913  1.00 109.62 ? 496 THR A CB    1 
ATOM   3711 O  OG1   . THR A 1 469 ? 17.105  86.153  97.785  1.00 136.10 ? 496 THR A OG1   1 
ATOM   3712 C  CG2   . THR A 1 469 ? 17.983  87.498  99.584  1.00 122.13 ? 496 THR A CG2   1 
ATOM   3713 N  N     . LEU A 1 470 ? 20.584  83.805  97.621  1.00 115.24 ? 497 LEU A N     1 
ATOM   3714 C  CA    . LEU A 1 470 ? 20.779  82.378  97.375  1.00 107.60 ? 497 LEU A CA    1 
ATOM   3715 C  C     . LEU A 1 470 ? 20.856  81.597  98.680  1.00 106.98 ? 497 LEU A C     1 
ATOM   3716 O  O     . LEU A 1 470 ? 20.141  80.605  98.867  1.00 105.66 ? 497 LEU A O     1 
ATOM   3717 C  CB    . LEU A 1 470 ? 22.046  82.161  96.548  1.00 106.37 ? 497 LEU A CB    1 
ATOM   3718 C  CG    . LEU A 1 470 ? 22.060  82.723  95.127  1.00 103.14 ? 497 LEU A CG    1 
ATOM   3719 C  CD1   . LEU A 1 470 ? 23.481  82.768  94.599  1.00 105.96 ? 497 LEU A CD1   1 
ATOM   3720 C  CD2   . LEU A 1 470 ? 21.179  81.884  94.220  1.00 111.07 ? 497 LEU A CD2   1 
ATOM   3721 N  N     . ALA A 1 471 ? 21.721  82.032  99.594  1.00 106.55 ? 498 ALA A N     1 
ATOM   3722 C  CA    . ALA A 1 471 ? 21.869  81.394  100.893 1.00 99.81  ? 498 ALA A CA    1 
ATOM   3723 C  C     . ALA A 1 471 ? 22.594  82.355  101.822 1.00 105.08 ? 498 ALA A C     1 
ATOM   3724 O  O     . ALA A 1 471 ? 23.483  83.092  101.386 1.00 101.96 ? 498 ALA A O     1 
ATOM   3725 C  CB    . ALA A 1 471 ? 22.635  80.070  100.789 1.00 93.80  ? 498 ALA A CB    1 
ATOM   3726 N  N     . TYR A 1 472 ? 22.210  82.341  103.097 1.00 99.92  ? 499 TYR A N     1 
ATOM   3727 C  CA    . TYR A 1 472 ? 22.774  83.275  104.061 1.00 100.11 ? 499 TYR A CA    1 
ATOM   3728 C  C     . TYR A 1 472 ? 22.591  82.727  105.468 1.00 105.38 ? 499 TYR A C     1 
ATOM   3729 O  O     . TYR A 1 472 ? 21.718  81.894  105.725 1.00 106.51 ? 499 TYR A O     1 
ATOM   3730 C  CB    . TYR A 1 472 ? 22.128  84.661  103.944 1.00 98.96  ? 499 TYR A CB    1 
ATOM   3731 C  CG    . TYR A 1 472 ? 20.622  84.656  104.096 1.00 99.14  ? 499 TYR A CG    1 
ATOM   3732 C  CD1   . TYR A 1 472 ? 20.026  84.737  105.350 1.00 100.77 ? 499 TYR A CD1   1 
ATOM   3733 C  CD2   . TYR A 1 472 ? 19.794  84.578  102.984 1.00 101.18 ? 499 TYR A CD2   1 
ATOM   3734 C  CE1   . TYR A 1 472 ? 18.652  84.735  105.492 1.00 93.75  ? 499 TYR A CE1   1 
ATOM   3735 C  CE2   . TYR A 1 472 ? 18.416  84.577  103.117 1.00 100.13 ? 499 TYR A CE2   1 
ATOM   3736 C  CZ    . TYR A 1 472 ? 17.853  84.654  104.372 1.00 101.81 ? 499 TYR A CZ    1 
ATOM   3737 O  OH    . TYR A 1 472 ? 16.484  84.652  104.503 1.00 111.02 ? 499 TYR A OH    1 
ATOM   3738 N  N     . VAL A 1 473 ? 23.432  83.214  106.375 1.00 114.33 ? 500 VAL A N     1 
ATOM   3739 C  CA    . VAL A 1 473 ? 23.313  82.939  107.801 1.00 113.62 ? 500 VAL A CA    1 
ATOM   3740 C  C     . VAL A 1 473 ? 22.648  84.139  108.458 1.00 115.24 ? 500 VAL A C     1 
ATOM   3741 O  O     . VAL A 1 473 ? 22.936  85.291  108.106 1.00 119.04 ? 500 VAL A O     1 
ATOM   3742 C  CB    . VAL A 1 473 ? 24.689  82.651  108.432 1.00 112.15 ? 500 VAL A CB    1 
ATOM   3743 C  CG1   . VAL A 1 473 ? 24.531  82.219  109.881 1.00 109.20 ? 500 VAL A CG1   1 
ATOM   3744 C  CG2   . VAL A 1 473 ? 25.425  81.588  107.633 1.00 105.83 ? 500 VAL A CG2   1 
ATOM   3745 N  N     . ILE A 1 474 ? 21.754  83.879  109.407 1.00 116.83 ? 501 ILE A N     1 
ATOM   3746 C  CA    . ILE A 1 474 ? 20.981  84.934  110.055 1.00 117.85 ? 501 ILE A CA    1 
ATOM   3747 C  C     . ILE A 1 474 ? 20.905  84.641  111.547 1.00 111.85 ? 501 ILE A C     1 
ATOM   3748 O  O     . ILE A 1 474 ? 20.638  83.505  111.953 1.00 115.82 ? 501 ILE A O     1 
ATOM   3749 C  CB    . ILE A 1 474 ? 19.574  85.068  109.437 1.00 116.93 ? 501 ILE A CB    1 
ATOM   3750 C  CG1   . ILE A 1 474 ? 18.756  86.126  110.178 1.00 121.56 ? 501 ILE A CG1   1 
ATOM   3751 C  CG2   . ILE A 1 474 ? 18.859  83.723  109.409 1.00 110.93 ? 501 ILE A CG2   1 
ATOM   3752 C  CD1   . ILE A 1 474 ? 17.476  86.508  109.467 1.00 115.29 ? 501 ILE A CD1   1 
ATOM   3753 N  N     . SER A 1 475 ? 21.147  85.662  112.363 1.00 113.49 ? 502 SER A N     1 
ATOM   3754 C  CA    . SER A 1 475 ? 21.120  85.531  113.811 1.00 119.39 ? 502 SER A CA    1 
ATOM   3755 C  C     . SER A 1 475 ? 19.763  85.958  114.363 1.00 121.14 ? 502 SER A C     1 
ATOM   3756 O  O     . SER A 1 475 ? 18.919  86.517  113.660 1.00 122.74 ? 502 SER A O     1 
ATOM   3757 C  CB    . SER A 1 475 ? 22.241  86.356  114.452 1.00 106.09 ? 502 SER A CB    1 
ATOM   3758 O  OG    . SER A 1 475 ? 22.088  87.735  114.169 1.00 111.05 ? 502 SER A OG    1 
ATOM   3759 N  N     . LEU A 1 476 ? 19.562  85.680  115.653 1.00 111.57 ? 503 LEU A N     1 
ATOM   3760 C  CA    . LEU A 1 476 ? 18.315  86.069  116.301 1.00 117.08 ? 503 LEU A CA    1 
ATOM   3761 C  C     . LEU A 1 476 ? 18.209  87.585  116.425 1.00 125.91 ? 503 LEU A C     1 
ATOM   3762 O  O     . LEU A 1 476 ? 17.134  88.156  116.211 1.00 129.74 ? 503 LEU A O     1 
ATOM   3763 C  CB    . LEU A 1 476 ? 18.207  85.399  117.670 1.00 124.32 ? 503 LEU A CB    1 
ATOM   3764 C  CG    . LEU A 1 476 ? 16.904  85.618  118.440 1.00 129.23 ? 503 LEU A CG    1 
ATOM   3765 C  CD1   . LEU A 1 476 ? 15.706  85.314  117.554 1.00 129.62 ? 503 LEU A CD1   1 
ATOM   3766 C  CD2   . LEU A 1 476 ? 16.873  84.761  119.698 1.00 116.76 ? 503 LEU A CD2   1 
ATOM   3767 N  N     . GLN A 1 477 ? 19.316  88.252  116.768 1.00 125.93 ? 504 GLN A N     1 
ATOM   3768 C  CA    . GLN A 1 477 ? 19.321  89.711  116.810 1.00 135.02 ? 504 GLN A CA    1 
ATOM   3769 C  C     . GLN A 1 477 ? 18.975  90.301  115.449 1.00 135.45 ? 504 GLN A C     1 
ATOM   3770 O  O     . GLN A 1 477 ? 18.226  91.281  115.358 1.00 131.87 ? 504 GLN A O     1 
ATOM   3771 C  CB    . GLN A 1 477 ? 20.686  90.216  117.282 1.00 135.62 ? 504 GLN A CB    1 
ATOM   3772 C  CG    . GLN A 1 477 ? 20.847  91.729  117.237 1.00 147.75 ? 504 GLN A CG    1 
ATOM   3773 C  CD    . GLN A 1 477 ? 22.270  92.172  117.515 1.00 155.83 ? 504 GLN A CD    1 
ATOM   3774 O  OE1   . GLN A 1 477 ? 23.168  91.345  117.668 1.00 152.84 ? 504 GLN A OE1   1 
ATOM   3775 N  NE2   . GLN A 1 477 ? 22.483  93.483  117.581 1.00 160.52 ? 504 GLN A NE2   1 
ATOM   3776 N  N     . GLY A 1 478 ? 19.510  89.713  114.377 1.00 133.28 ? 505 GLY A N     1 
ATOM   3777 C  CA    . GLY A 1 478 ? 19.200  90.195  113.043 1.00 128.69 ? 505 GLY A CA    1 
ATOM   3778 C  C     . GLY A 1 478 ? 17.805  89.828  112.583 1.00 130.25 ? 505 GLY A C     1 
ATOM   3779 O  O     . GLY A 1 478 ? 17.184  90.576  111.824 1.00 130.55 ? 505 GLY A O     1 
ATOM   3780 N  N     . ALA A 1 479 ? 17.295  88.676  113.026 1.00 125.00 ? 506 ALA A N     1 
ATOM   3781 C  CA    . ALA A 1 479 ? 15.929  88.298  112.683 1.00 121.19 ? 506 ALA A CA    1 
ATOM   3782 C  C     . ALA A 1 479 ? 14.918  89.260  113.291 1.00 135.47 ? 506 ALA A C     1 
ATOM   3783 O  O     . ALA A 1 479 ? 13.837  89.466  112.727 1.00 133.67 ? 506 ALA A O     1 
ATOM   3784 C  CB    . ALA A 1 479 ? 15.650  86.866  113.139 1.00 123.20 ? 506 ALA A CB    1 
ATOM   3785 N  N     . ARG A 1 480 ? 15.250  89.858  114.438 1.00 136.23 ? 507 ARG A N     1 
ATOM   3786 C  CA    . ARG A 1 480 ? 14.376  90.867  115.028 1.00 128.14 ? 507 ARG A CA    1 
ATOM   3787 C  C     . ARG A 1 480 ? 14.461  92.184  114.266 1.00 140.94 ? 507 ARG A C     1 
ATOM   3788 O  O     . ARG A 1 480 ? 13.442  92.854  114.059 1.00 147.20 ? 507 ARG A O     1 
ATOM   3789 C  CB    . ARG A 1 480 ? 14.738  91.087  116.496 1.00 128.31 ? 507 ARG A CB    1 
ATOM   3790 C  CG    . ARG A 1 480 ? 14.577  89.874  117.397 1.00 131.45 ? 507 ARG A CG    1 
ATOM   3791 C  CD    . ARG A 1 480 ? 14.869  90.261  118.842 1.00 141.76 ? 507 ARG A CD    1 
ATOM   3792 N  NE    . ARG A 1 480 ? 14.594  89.190  119.792 1.00 148.26 ? 507 ARG A NE    1 
ATOM   3793 C  CZ    . ARG A 1 480 ? 15.523  88.425  120.351 1.00 143.44 ? 507 ARG A CZ    1 
ATOM   3794 N  NH1   . ARG A 1 480 ? 16.805  88.569  120.058 1.00 134.90 ? 507 ARG A NH1   1 
ATOM   3795 N  NH2   . ARG A 1 480 ? 15.156  87.498  121.232 1.00 131.02 ? 507 ARG A NH2   1 
ATOM   3796 N  N     . LYS A 1 481 ? 15.670  92.573  113.846 1.00 136.67 ? 508 LYS A N     1 
ATOM   3797 C  CA    . LYS A 1 481 ? 15.858  93.874  113.209 1.00 137.98 ? 508 LYS A CA    1 
ATOM   3798 C  C     . LYS A 1 481 ? 15.049  93.991  111.922 1.00 142.34 ? 508 LYS A C     1 
ATOM   3799 O  O     . LYS A 1 481 ? 14.488  95.055  111.628 1.00 142.67 ? 508 LYS A O     1 
ATOM   3800 C  CB    . LYS A 1 481 ? 17.343  94.113  112.929 1.00 131.59 ? 508 LYS A CB    1 
ATOM   3801 C  CG    . LYS A 1 481 ? 18.200  94.340  114.167 1.00 121.81 ? 508 LYS A CG    1 
ATOM   3802 C  CD    . LYS A 1 481 ? 19.631  94.690  113.779 1.00 125.91 ? 508 LYS A CD    1 
ATOM   3803 C  CE    . LYS A 1 481 ? 20.504  94.931  115.002 1.00 134.00 ? 508 LYS A CE    1 
ATOM   3804 N  NZ    . LYS A 1 481 ? 21.925  95.192  114.625 1.00 132.12 ? 508 LYS A NZ    1 
ATOM   3805 N  N     . LEU A 1 482 ? 14.979  92.911  111.139 1.00 135.25 ? 509 LEU A N     1 
ATOM   3806 C  CA    . LEU A 1 482 ? 14.220  92.946  109.892 1.00 130.72 ? 509 LEU A CA    1 
ATOM   3807 C  C     . LEU A 1 482 ? 12.733  93.147  110.160 1.00 142.96 ? 509 LEU A C     1 
ATOM   3808 O  O     . LEU A 1 482 ? 12.083  93.985  109.524 1.00 149.87 ? 509 LEU A O     1 
ATOM   3809 C  CB    . LEU A 1 482 ? 14.452  91.660  109.096 1.00 123.65 ? 509 LEU A CB    1 
ATOM   3810 C  CG    . LEU A 1 482 ? 15.867  91.386  108.583 1.00 120.65 ? 509 LEU A CG    1 
ATOM   3811 C  CD1   . LEU A 1 482 ? 15.907  90.077  107.814 1.00 100.87 ? 509 LEU A CD1   1 
ATOM   3812 C  CD2   . LEU A 1 482 ? 16.364  92.533  107.717 1.00 122.48 ? 509 LEU A CD2   1 
ATOM   3813 N  N     . LEU A 1 483 ? 12.178  92.386  111.105 1.00 140.04 ? 510 LEU A N     1 
ATOM   3814 C  CA    . LEU A 1 483 ? 10.758  92.494  111.415 1.00 136.68 ? 510 LEU A CA    1 
ATOM   3815 C  C     . LEU A 1 483 ? 10.410  93.811  112.096 1.00 135.35 ? 510 LEU A C     1 
ATOM   3816 O  O     . LEU A 1 483 ? 9.260   94.253  112.009 1.00 144.05 ? 510 LEU A O     1 
ATOM   3817 C  CB    . LEU A 1 483 ? 10.332  91.317  112.294 1.00 126.28 ? 510 LEU A CB    1 
ATOM   3818 C  CG    . LEU A 1 483 ? 10.674  89.939  111.723 1.00 122.42 ? 510 LEU A CG    1 
ATOM   3819 C  CD1   . LEU A 1 483 ? 10.454  88.853  112.762 1.00 123.82 ? 510 LEU A CD1   1 
ATOM   3820 C  CD2   . LEU A 1 483 ? 9.856   89.659  110.471 1.00 117.50 ? 510 LEU A CD2   1 
ATOM   3821 N  N     . ALA A 1 484 ? 11.375  94.446  112.769 1.00 147.97 ? 511 ALA A N     1 
ATOM   3822 C  CA    . ALA A 1 484 ? 11.108  95.727  113.416 1.00 152.43 ? 511 ALA A CA    1 
ATOM   3823 C  C     . ALA A 1 484 ? 10.860  96.831  112.397 1.00 161.46 ? 511 ALA A C     1 
ATOM   3824 O  O     . ALA A 1 484 ? 10.100  97.767  112.673 1.00 160.04 ? 511 ALA A O     1 
ATOM   3825 C  CB    . ALA A 1 484 ? 12.268  96.103  114.337 1.00 145.73 ? 511 ALA A CB    1 
ATOM   3826 N  N     . ALA A 1 485 ? 11.487  96.744  111.221 1.00 164.62 ? 512 ALA A N     1 
ATOM   3827 C  CA    . ALA A 1 485 ? 11.227  97.713  110.164 1.00 166.38 ? 512 ALA A CA    1 
ATOM   3828 C  C     . ALA A 1 485 ? 9.808   97.610  109.625 1.00 170.87 ? 512 ALA A C     1 
ATOM   3829 O  O     . ALA A 1 485 ? 9.320   98.572  109.020 1.00 174.64 ? 512 ALA A O     1 
ATOM   3830 C  CB    . ALA A 1 485 ? 12.231  97.536  109.024 1.00 158.29 ? 512 ALA A CB    1 
ATOM   3831 N  N     . GLU A 1 486 ? 9.139   96.470  109.837 1.00 166.24 ? 513 GLU A N     1 
ATOM   3832 C  CA    . GLU A 1 486 ? 7.772   96.226  109.390 1.00 167.01 ? 513 GLU A CA    1 
ATOM   3833 C  C     . GLU A 1 486 ? 7.668   96.479  107.890 1.00 169.64 ? 513 GLU A C     1 
ATOM   3834 O  O     . GLU A 1 486 ? 7.102   97.497  107.464 1.00 169.40 ? 513 GLU A O     1 
ATOM   3835 C  CB    . GLU A 1 486 ? 6.792   97.101  110.172 1.00 166.60 ? 513 GLU A CB    1 
ATOM   3836 C  CG    . GLU A 1 486 ? 6.913   96.938  111.682 1.00 167.52 ? 513 GLU A CG    1 
ATOM   3837 C  CD    . GLU A 1 486 ? 6.026   97.895  112.453 1.00 190.39 ? 513 GLU A CD    1 
ATOM   3838 O  OE1   . GLU A 1 486 ? 5.159   98.541  111.827 1.00 205.99 ? 513 GLU A OE1   1 
ATOM   3839 O  OE2   . GLU A 1 486 ? 6.197   98.004  113.685 1.00 196.78 ? 513 GLU A OE2   1 
ATOM   3840 N  N     . PRO A 1 487 ? 8.202   95.580  107.064 1.00 165.42 ? 514 PRO A N     1 
ATOM   3841 C  CA    . PRO A 1 487 ? 8.332   95.848  105.626 1.00 165.84 ? 514 PRO A CA    1 
ATOM   3842 C  C     . PRO A 1 487 ? 7.111   95.511  104.781 1.00 168.75 ? 514 PRO A C     1 
ATOM   3843 O  O     . PRO A 1 487 ? 7.137   95.772  103.573 1.00 171.38 ? 514 PRO A O     1 
ATOM   3844 C  CB    . PRO A 1 487 ? 9.512   94.944  105.243 1.00 159.01 ? 514 PRO A CB    1 
ATOM   3845 C  CG    . PRO A 1 487 ? 9.356   93.759  106.142 1.00 152.44 ? 514 PRO A CG    1 
ATOM   3846 C  CD    . PRO A 1 487 ? 8.798   94.285  107.444 1.00 159.44 ? 514 PRO A CD    1 
ATOM   3847 N  N     . LEU A 1 488 ? 6.055   94.937  105.365 1.00 173.72 ? 515 LEU A N     1 
ATOM   3848 C  CA    . LEU A 1 488 ? 4.904   94.536  104.561 1.00 179.76 ? 515 LEU A CA    1 
ATOM   3849 C  C     . LEU A 1 488 ? 4.177   95.735  103.962 1.00 184.28 ? 515 LEU A C     1 
ATOM   3850 O  O     . LEU A 1 488 ? 3.539   95.606  102.911 1.00 180.89 ? 515 LEU A O     1 
ATOM   3851 C  CB    . LEU A 1 488 ? 3.944   93.697  105.406 1.00 180.73 ? 515 LEU A CB    1 
ATOM   3852 C  CG    . LEU A 1 488 ? 4.518   92.394  105.962 1.00 162.16 ? 515 LEU A CG    1 
ATOM   3853 C  CD1   . LEU A 1 488 ? 3.497   91.677  106.829 1.00 166.75 ? 515 LEU A CD1   1 
ATOM   3854 C  CD2   . LEU A 1 488 ? 4.989   91.496  104.831 1.00 158.36 ? 515 LEU A CD2   1 
ATOM   3855 N  N     . SER A 1 489 ? 4.266   96.903  104.600 1.00 172.51 ? 516 SER A N     1 
ATOM   3856 C  CA    . SER A 1 489 ? 3.604   98.095  104.084 1.00 171.56 ? 516 SER A CA    1 
ATOM   3857 C  C     . SER A 1 489 ? 4.408   98.798  102.997 1.00 174.82 ? 516 SER A C     1 
ATOM   3858 O  O     . SER A 1 489 ? 3.855   99.643  102.284 1.00 179.19 ? 516 SER A O     1 
ATOM   3859 C  CB    . SER A 1 489 ? 3.327   99.074  105.227 1.00 171.63 ? 516 SER A CB    1 
ATOM   3860 O  OG    . SER A 1 489 ? 4.528   99.431  105.888 1.00 178.32 ? 516 SER A OG    1 
ATOM   3861 N  N     . LYS A 1 490 ? 5.696   98.463  102.849 1.00 170.82 ? 517 LYS A N     1 
ATOM   3862 C  CA    . LYS A 1 490 ? 6.600   99.126  101.912 1.00 171.79 ? 517 LYS A CA    1 
ATOM   3863 C  C     . LYS A 1 490 ? 7.536   98.061  101.328 1.00 167.03 ? 517 LYS A C     1 
ATOM   3864 O  O     . LYS A 1 490 ? 8.723   97.992  101.640 1.00 155.95 ? 517 LYS A O     1 
ATOM   3865 C  CB    . LYS A 1 490 ? 7.377   100.248 102.605 1.00 167.17 ? 517 LYS A CB    1 
ATOM   3866 C  CG    . LYS A 1 490 ? 7.749   99.914  104.045 1.00 165.50 ? 517 LYS A CG    1 
ATOM   3867 C  CD    . LYS A 1 490 ? 8.454   101.063 104.743 1.00 164.70 ? 517 LYS A CD    1 
ATOM   3868 C  CE    . LYS A 1 490 ? 8.735   100.717 106.199 1.00 161.60 ? 517 LYS A CE    1 
ATOM   3869 N  NZ    . LYS A 1 490 ? 9.496   101.786 106.903 1.00 167.30 ? 517 LYS A NZ    1 
ATOM   3870 N  N     . MET A 1 491 ? 6.991   97.220  100.451 1.00 174.25 ? 518 MET A N     1 
ATOM   3871 C  CA    . MET A 1 491 ? 7.674   96.008  100.015 1.00 183.29 ? 518 MET A CA    1 
ATOM   3872 C  C     . MET A 1 491 ? 8.503   96.248  98.756  1.00 191.46 ? 518 MET A C     1 
ATOM   3873 O  O     . MET A 1 491 ? 8.000   96.774  97.757  1.00 198.10 ? 518 MET A O     1 
ATOM   3874 C  CB    . MET A 1 491 ? 6.668   94.882  99.768  1.00 182.52 ? 518 MET A CB    1 
ATOM   3875 C  CG    . MET A 1 491 ? 7.302   93.602  99.235  1.00 184.78 ? 518 MET A CG    1 
ATOM   3876 S  SD    . MET A 1 491 ? 6.163   92.210  99.083  1.00 169.68 ? 518 MET A SD    1 
ATOM   3877 C  CE    . MET A 1 491 ? 5.884   91.807  100.805 1.00 170.42 ? 518 MET A CE    1 
ATOM   3878 N  N     . LEU A 1 492 ? 9.776   95.854  98.820  1.00 169.26 ? 519 LEU A N     1 
ATOM   3879 C  CA    . LEU A 1 492 ? 10.693  95.737  97.694  1.00 148.75 ? 519 LEU A CA    1 
ATOM   3880 C  C     . LEU A 1 492 ? 10.934  94.249  97.471  1.00 156.22 ? 519 LEU A C     1 
ATOM   3881 O  O     . LEU A 1 492 ? 10.396  93.427  98.222  1.00 157.03 ? 519 LEU A O     1 
ATOM   3882 C  CB    . LEU A 1 492 ? 12.010  96.465  97.982  1.00 146.48 ? 519 LEU A CB    1 
ATOM   3883 C  CG    . LEU A 1 492 ? 11.999  97.964  98.279  1.00 157.53 ? 519 LEU A CG    1 
ATOM   3884 C  CD1   . LEU A 1 492 ? 13.299  98.372  98.958  1.00 142.09 ? 519 LEU A CD1   1 
ATOM   3885 C  CD2   . LEU A 1 492 ? 11.788  98.764  97.003  1.00 164.03 ? 519 LEU A CD2   1 
ATOM   3886 N  N     . PRO A 1 493 ? 11.710  93.849  96.465  1.00 163.70 ? 520 PRO A N     1 
ATOM   3887 C  CA    . PRO A 1 493 ? 12.209  92.471  96.455  1.00 157.46 ? 520 PRO A CA    1 
ATOM   3888 C  C     . PRO A 1 493 ? 13.128  92.237  97.645  1.00 153.54 ? 520 PRO A C     1 
ATOM   3889 O  O     . PRO A 1 493 ? 13.769  93.160  98.152  1.00 160.20 ? 520 PRO A O     1 
ATOM   3890 C  CB    . PRO A 1 493 ? 12.963  92.373  95.125  1.00 155.41 ? 520 PRO A CB    1 
ATOM   3891 C  CG    . PRO A 1 493 ? 12.342  93.405  94.269  1.00 162.27 ? 520 PRO A CG    1 
ATOM   3892 C  CD    . PRO A 1 493 ? 11.983  94.534  95.190  1.00 164.24 ? 520 PRO A CD    1 
ATOM   3893 N  N     . VAL A 1 494 ? 13.181  90.981  98.099  1.00 150.91 ? 521 VAL A N     1 
ATOM   3894 C  CA    . VAL A 1 494 ? 13.909  90.679  99.330  1.00 144.75 ? 521 VAL A CA    1 
ATOM   3895 C  C     . VAL A 1 494 ? 15.408  90.901  99.153  1.00 141.41 ? 521 VAL A C     1 
ATOM   3896 O  O     . VAL A 1 494 ? 16.115  91.197  100.125 1.00 136.79 ? 521 VAL A O     1 
ATOM   3897 C  CB    . VAL A 1 494 ? 13.599  89.246  99.807  1.00 138.59 ? 521 VAL A CB    1 
ATOM   3898 C  CG1   . VAL A 1 494 ? 14.339  88.214  98.964  1.00 127.61 ? 521 VAL A CG1   1 
ATOM   3899 C  CG2   . VAL A 1 494 ? 13.932  89.092  101.286 1.00 131.34 ? 521 VAL A CG2   1 
ATOM   3900 N  N     . ASP A 1 495 ? 15.918  90.777  97.926  1.00 133.69 ? 522 ASP A N     1 
ATOM   3901 C  CA    . ASP A 1 495 ? 17.328  91.033  97.668  1.00 129.47 ? 522 ASP A CA    1 
ATOM   3902 C  C     . ASP A 1 495 ? 17.659  92.518  97.616  1.00 138.09 ? 522 ASP A C     1 
ATOM   3903 O  O     . ASP A 1 495 ? 18.844  92.869  97.616  1.00 140.74 ? 522 ASP A O     1 
ATOM   3904 C  CB    . ASP A 1 495 ? 17.758  90.361  96.360  1.00 132.51 ? 522 ASP A CB    1 
ATOM   3905 C  CG    . ASP A 1 495 ? 16.941  90.823  95.172  1.00 136.44 ? 522 ASP A CG    1 
ATOM   3906 O  OD1   . ASP A 1 495 ? 15.776  91.212  95.375  1.00 137.24 ? 522 ASP A OD1   1 
ATOM   3907 O  OD2   . ASP A 1 495 ? 17.460  90.797  94.037  1.00 141.46 ? 522 ASP A OD2   1 
ATOM   3908 N  N     . GLU A 1 496 ? 16.650  93.390  97.561  1.00 145.50 ? 523 GLU A N     1 
ATOM   3909 C  CA    . GLU A 1 496 ? 16.850  94.827  97.697  1.00 141.73 ? 523 GLU A CA    1 
ATOM   3910 C  C     . GLU A 1 496 ? 16.491  95.347  99.081  1.00 144.89 ? 523 GLU A C     1 
ATOM   3911 O  O     . GLU A 1 496 ? 16.975  96.416  99.469  1.00 143.81 ? 523 GLU A O     1 
ATOM   3912 C  CB    . GLU A 1 496 ? 16.025  95.591  96.653  1.00 146.19 ? 523 GLU A CB    1 
ATOM   3913 C  CG    . GLU A 1 496 ? 16.407  95.313  95.208  1.00 148.28 ? 523 GLU A CG    1 
ATOM   3914 C  CD    . GLU A 1 496 ? 15.662  96.203  94.232  1.00 159.66 ? 523 GLU A CD    1 
ATOM   3915 O  OE1   . GLU A 1 496 ? 15.358  97.360  94.591  1.00 160.99 ? 523 GLU A OE1   1 
ATOM   3916 O  OE2   . GLU A 1 496 ? 15.374  95.743  93.107  1.00 162.76 ? 523 GLU A OE2   1 
ATOM   3917 N  N     . PHE A 1 497 ? 15.654  94.621  99.827  1.00 148.19 ? 524 PHE A N     1 
ATOM   3918 C  CA    . PHE A 1 497 ? 15.288  95.050  101.173 1.00 140.69 ? 524 PHE A CA    1 
ATOM   3919 C  C     . PHE A 1 497 ? 16.465  94.933  102.132 1.00 139.71 ? 524 PHE A C     1 
ATOM   3920 O  O     . PHE A 1 497 ? 16.655  95.794  103.000 1.00 142.13 ? 524 PHE A O     1 
ATOM   3921 C  CB    . PHE A 1 497 ? 14.102  94.229  101.678 1.00 140.01 ? 524 PHE A CB    1 
ATOM   3922 C  CG    . PHE A 1 497 ? 13.865  94.346  103.158 1.00 149.36 ? 524 PHE A CG    1 
ATOM   3923 C  CD1   . PHE A 1 497 ? 13.459  95.546  103.718 1.00 156.29 ? 524 PHE A CD1   1 
ATOM   3924 C  CD2   . PHE A 1 497 ? 14.035  93.250  103.988 1.00 145.16 ? 524 PHE A CD2   1 
ATOM   3925 C  CE1   . PHE A 1 497 ? 13.234  95.653  105.081 1.00 150.57 ? 524 PHE A CE1   1 
ATOM   3926 C  CE2   . PHE A 1 497 ? 13.810  93.351  105.351 1.00 141.46 ? 524 PHE A CE2   1 
ATOM   3927 C  CZ    . PHE A 1 497 ? 13.410  94.553  105.897 1.00 133.64 ? 524 PHE A CZ    1 
ATOM   3928 N  N     . LEU A 1 498 ? 17.262  93.875  101.995 1.00 127.16 ? 525 LEU A N     1 
ATOM   3929 C  CA    . LEU A 1 498 ? 18.418  93.709  102.873 1.00 130.89 ? 525 LEU A CA    1 
ATOM   3930 C  C     . LEU A 1 498 ? 19.460  94.804  102.675 1.00 135.50 ? 525 LEU A C     1 
ATOM   3931 O  O     . LEU A 1 498 ? 19.911  95.377  103.682 1.00 138.09 ? 525 LEU A O     1 
ATOM   3932 C  CB    . LEU A 1 498 ? 19.014  92.308  102.684 1.00 121.42 ? 525 LEU A CB    1 
ATOM   3933 C  CG    . LEU A 1 498 ? 18.026  91.137  102.694 1.00 110.50 ? 525 LEU A CG    1 
ATOM   3934 C  CD1   . LEU A 1 498 ? 18.762  89.810  102.596 1.00 103.28 ? 525 LEU A CD1   1 
ATOM   3935 C  CD2   . LEU A 1 498 ? 17.133  91.167  103.926 1.00 109.90 ? 525 LEU A CD2   1 
ATOM   3936 N  N     . PRO A 1 499 ? 19.878  95.156  101.451 1.00 137.39 ? 526 PRO A N     1 
ATOM   3937 C  CA    . PRO A 1 499 ? 20.808  96.291  101.301 1.00 146.71 ? 526 PRO A CA    1 
ATOM   3938 C  C     . PRO A 1 499 ? 20.255  97.609  101.808 1.00 146.79 ? 526 PRO A C     1 
ATOM   3939 O  O     . PRO A 1 499 ? 21.040  98.521  102.096 1.00 147.12 ? 526 PRO A O     1 
ATOM   3940 C  CB    . PRO A 1 499 ? 21.069  96.336  99.790  1.00 139.57 ? 526 PRO A CB    1 
ATOM   3941 C  CG    . PRO A 1 499 ? 20.827  94.950  99.336  1.00 139.98 ? 526 PRO A CG    1 
ATOM   3942 C  CD    . PRO A 1 499 ? 19.676  94.466  100.165 1.00 131.40 ? 526 PRO A CD    1 
ATOM   3943 N  N     . VAL A 1 500 ? 18.933  97.749  101.920 1.00 139.77 ? 527 VAL A N     1 
ATOM   3944 C  CA    . VAL A 1 500 ? 18.385  98.920  102.593 1.00 148.24 ? 527 VAL A CA    1 
ATOM   3945 C  C     . VAL A 1 500 ? 18.670  98.848  104.088 1.00 145.36 ? 527 VAL A C     1 
ATOM   3946 O  O     . VAL A 1 500 ? 19.061  99.843  104.707 1.00 150.40 ? 527 VAL A O     1 
ATOM   3947 C  CB    . VAL A 1 500 ? 16.878  99.051  102.305 1.00 145.97 ? 527 VAL A CB    1 
ATOM   3948 C  CG1   . VAL A 1 500 ? 16.279  100.174 103.134 1.00 140.95 ? 527 VAL A CG1   1 
ATOM   3949 C  CG2   . VAL A 1 500 ? 16.641  99.312  100.824 1.00 152.98 ? 527 VAL A CG2   1 
ATOM   3950 N  N     . MET A 1 501 ? 18.513  97.665  104.685 1.00 144.58 ? 528 MET A N     1 
ATOM   3951 C  CA    . MET A 1 501 ? 18.660  97.534  106.130 1.00 141.86 ? 528 MET A CA    1 
ATOM   3952 C  C     . MET A 1 501 ? 20.108  97.630  106.597 1.00 142.40 ? 528 MET A C     1 
ATOM   3953 O  O     . MET A 1 501 ? 20.339  97.996  107.753 1.00 146.08 ? 528 MET A O     1 
ATOM   3954 C  CB    . MET A 1 501 ? 18.032  96.226  106.609 1.00 138.24 ? 528 MET A CB    1 
ATOM   3955 C  CG    . MET A 1 501 ? 16.521  96.163  106.398 1.00 137.29 ? 528 MET A CG    1 
ATOM   3956 S  SD    . MET A 1 501 ? 15.646  97.590  107.082 1.00 158.48 ? 528 MET A SD    1 
ATOM   3957 C  CE    . MET A 1 501 ? 15.907  97.353  108.838 1.00 143.78 ? 528 MET A CE    1 
ATOM   3958 N  N     . PHE A 1 502 ? 21.090  97.317  105.750 1.00 144.87 ? 529 PHE A N     1 
ATOM   3959 C  CA    . PHE A 1 502 ? 22.475  97.639  106.076 1.00 152.30 ? 529 PHE A CA    1 
ATOM   3960 C  C     . PHE A 1 502 ? 22.993  98.823  105.261 1.00 158.27 ? 529 PHE A C     1 
ATOM   3961 O  O     . PHE A 1 502 ? 24.209  99.028  105.168 1.00 161.09 ? 529 PHE A O     1 
ATOM   3962 C  CB    . PHE A 1 502 ? 23.397  96.419  105.942 1.00 143.43 ? 529 PHE A CB    1 
ATOM   3963 C  CG    . PHE A 1 502 ? 23.475  95.816  104.560 1.00 152.95 ? 529 PHE A CG    1 
ATOM   3964 C  CD1   . PHE A 1 502 ? 24.304  96.356  103.587 1.00 151.67 ? 529 PHE A CD1   1 
ATOM   3965 C  CD2   . PHE A 1 502 ? 22.781  94.654  104.264 1.00 142.08 ? 529 PHE A CD2   1 
ATOM   3966 C  CE1   . PHE A 1 502 ? 24.395  95.778  102.332 1.00 146.17 ? 529 PHE A CE1   1 
ATOM   3967 C  CE2   . PHE A 1 502 ? 22.871  94.070  103.014 1.00 138.88 ? 529 PHE A CE2   1 
ATOM   3968 C  CZ    . PHE A 1 502 ? 23.680  94.632  102.047 1.00 143.81 ? 529 PHE A CZ    1 
ATOM   3969 N  N     . ASP A 1 503 ? 22.083  99.603  104.671 1.00 154.71 ? 530 ASP A N     1 
ATOM   3970 C  CA    . ASP A 1 503 ? 22.359  100.968 104.211 1.00 157.11 ? 530 ASP A CA    1 
ATOM   3971 C  C     . ASP A 1 503 ? 23.405  101.005 103.097 1.00 158.37 ? 530 ASP A C     1 
ATOM   3972 O  O     . ASP A 1 503 ? 24.332  101.818 103.111 1.00 159.48 ? 530 ASP A O     1 
ATOM   3973 C  CB    . ASP A 1 503 ? 22.780  101.858 105.384 1.00 162.98 ? 530 ASP A CB    1 
ATOM   3974 C  CG    . ASP A 1 503 ? 22.250  103.273 105.263 1.00 163.10 ? 530 ASP A CG    1 
ATOM   3975 O  OD1   . ASP A 1 503 ? 21.438  103.532 104.351 1.00 165.93 ? 530 ASP A OD1   1 
ATOM   3976 O  OD2   . ASP A 1 503 ? 22.643  104.129 106.084 1.00 160.46 ? 530 ASP A OD2   1 
ATOM   3977 N  N     . LYS A 1 504 ? 23.244  100.122 102.113 1.00 155.95 ? 531 LYS A N     1 
ATOM   3978 C  CA    . LYS A 1 504 ? 24.080  100.138 100.922 1.00 147.64 ? 531 LYS A CA    1 
ATOM   3979 C  C     . LYS A 1 504 ? 23.276  100.247 99.634  1.00 146.40 ? 531 LYS A C     1 
ATOM   3980 O  O     . LYS A 1 504 ? 23.866  100.200 98.548  1.00 154.01 ? 531 LYS A O     1 
ATOM   3981 C  CB    . LYS A 1 504 ? 24.972  98.889  100.868 1.00 142.88 ? 531 LYS A CB    1 
ATOM   3982 C  CG    . LYS A 1 504 ? 26.131  98.905  101.857 1.00 141.09 ? 531 LYS A CG    1 
ATOM   3983 C  CD    . LYS A 1 504 ? 27.126  100.007 101.531 1.00 142.88 ? 531 LYS A CD    1 
ATOM   3984 C  CE    . LYS A 1 504 ? 28.345  99.943  102.439 1.00 137.15 ? 531 LYS A CE    1 
ATOM   3985 N  NZ    . LYS A 1 504 ? 29.345  100.994 102.095 1.00 131.29 ? 531 LYS A NZ    1 
ATOM   3986 N  N     . HIS A 1 505 ? 21.962  100.395 99.721  1.00 143.49 ? 532 HIS A N     1 
ATOM   3987 C  CA    . HIS A 1 505 ? 21.142  100.580 98.530  1.00 153.21 ? 532 HIS A CA    1 
ATOM   3988 C  C     . HIS A 1 505 ? 21.427  101.953 97.933  1.00 155.74 ? 532 HIS A C     1 
ATOM   3989 O  O     . HIS A 1 505 ? 21.246  102.966 98.622  1.00 145.10 ? 532 HIS A O     1 
ATOM   3990 C  CB    . HIS A 1 505 ? 19.662  100.440 98.879  1.00 150.47 ? 532 HIS A CB    1 
ATOM   3991 C  CG    . HIS A 1 505 ? 18.801  100.034 97.723  1.00 149.46 ? 532 HIS A CG    1 
ATOM   3992 N  ND1   . HIS A 1 505 ? 18.750  100.747 96.545  1.00 150.69 ? 532 HIS A ND1   1 
ATOM   3993 C  CD2   . HIS A 1 505 ? 17.951  98.991  97.568  1.00 142.05 ? 532 HIS A CD2   1 
ATOM   3994 C  CE1   . HIS A 1 505 ? 17.910  100.158 95.712  1.00 143.96 ? 532 HIS A CE1   1 
ATOM   3995 N  NE2   . HIS A 1 505 ? 17.410  99.091  96.309  1.00 141.97 ? 532 HIS A NE2   1 
ATOM   3996 N  N     . PRO A 1 506 ? 21.870  102.042 96.675  1.00 160.88 ? 533 PRO A N     1 
ATOM   3997 C  CA    . PRO A 1 506 ? 22.237  103.351 96.110  1.00 163.37 ? 533 PRO A CA    1 
ATOM   3998 C  C     . PRO A 1 506 ? 21.066  104.305 95.941  1.00 164.73 ? 533 PRO A C     1 
ATOM   3999 O  O     . PRO A 1 506 ? 21.299  105.502 95.726  1.00 164.67 ? 533 PRO A O     1 
ATOM   4000 C  CB    . PRO A 1 506 ? 22.851  102.986 94.752  1.00 173.08 ? 533 PRO A CB    1 
ATOM   4001 C  CG    . PRO A 1 506 ? 22.240  101.667 94.407  1.00 165.58 ? 533 PRO A CG    1 
ATOM   4002 C  CD    . PRO A 1 506 ? 22.065  100.946 95.712  1.00 158.51 ? 533 PRO A CD    1 
ATOM   4003 N  N     . VAL A 1 507 ? 19.829  103.827 96.031  1.00 161.17 ? 534 VAL A N     1 
ATOM   4004 C  CA    . VAL A 1 507 ? 18.653  104.677 95.887  1.00 157.58 ? 534 VAL A CA    1 
ATOM   4005 C  C     . VAL A 1 507 ? 18.282  105.208 97.267  1.00 159.39 ? 534 VAL A C     1 
ATOM   4006 O  O     . VAL A 1 507 ? 17.790  104.463 98.119  1.00 163.69 ? 534 VAL A O     1 
ATOM   4007 C  CB    . VAL A 1 507 ? 17.483  103.916 95.252  1.00 154.42 ? 534 VAL A CB    1 
ATOM   4008 C  CG1   . VAL A 1 507 ? 16.282  104.835 95.087  1.00 161.31 ? 534 VAL A CG1   1 
ATOM   4009 C  CG2   . VAL A 1 507 ? 17.900  103.321 93.916  1.00 148.68 ? 534 VAL A CG2   1 
ATOM   4010 N  N     . SER A 1 508 ? 18.520  106.502 97.492  1.00 156.14 ? 535 SER A N     1 
ATOM   4011 C  CA    . SER A 1 508 ? 18.111  107.132 98.741  1.00 154.08 ? 535 SER A CA    1 
ATOM   4012 C  C     . SER A 1 508 ? 16.603  107.321 98.834  1.00 162.41 ? 535 SER A C     1 
ATOM   4013 O  O     . SER A 1 508 ? 16.097  107.592 99.928  1.00 159.31 ? 535 SER A O     1 
ATOM   4014 C  CB    . SER A 1 508 ? 18.815  108.480 98.910  1.00 147.93 ? 535 SER A CB    1 
ATOM   4015 O  OG    . SER A 1 508 ? 20.200  108.302 99.151  1.00 151.16 ? 535 SER A OG    1 
ATOM   4016 N  N     . GLU A 1 509 ? 15.880  107.192 97.719  1.00 172.44 ? 536 GLU A N     1 
ATOM   4017 C  CA    . GLU A 1 509 ? 14.423  107.235 97.771  1.00 176.43 ? 536 GLU A CA    1 
ATOM   4018 C  C     . GLU A 1 509 ? 13.860  106.000 98.464  1.00 179.71 ? 536 GLU A C     1 
ATOM   4019 O  O     . GLU A 1 509 ? 12.849  106.084 99.171  1.00 180.00 ? 536 GLU A O     1 
ATOM   4020 C  CB    . GLU A 1 509 ? 13.852  107.366 96.359  1.00 177.32 ? 536 GLU A CB    1 
ATOM   4021 C  CG    . GLU A 1 509 ? 14.091  108.720 95.713  1.00 184.64 ? 536 GLU A CG    1 
ATOM   4022 C  CD    . GLU A 1 509 ? 13.199  109.803 96.290  1.00 201.03 ? 536 GLU A CD    1 
ATOM   4023 O  OE1   . GLU A 1 509 ? 12.164  109.459 96.899  1.00 199.39 ? 536 GLU A OE1   1 
ATOM   4024 O  OE2   . GLU A 1 509 ? 13.531  110.997 96.136  1.00 196.85 ? 536 GLU A OE2   1 
ATOM   4025 N  N     . TYR A 1 510 ? 14.502  104.845 98.275  1.00 176.99 ? 537 TYR A N     1 
ATOM   4026 C  CA    . TYR A 1 510 ? 14.046  103.620 98.924  1.00 173.40 ? 537 TYR A CA    1 
ATOM   4027 C  C     . TYR A 1 510 ? 14.451  103.591 100.392 1.00 170.98 ? 537 TYR A C     1 
ATOM   4028 O  O     . TYR A 1 510 ? 13.633  103.275 101.264 1.00 169.59 ? 537 TYR A O     1 
ATOM   4029 C  CB    . TYR A 1 510 ? 14.605  102.393 98.198  1.00 163.36 ? 537 TYR A CB    1 
ATOM   4030 C  CG    . TYR A 1 510 ? 14.142  102.240 96.766  1.00 167.68 ? 537 TYR A CG    1 
ATOM   4031 C  CD1   . TYR A 1 510 ? 13.025  102.917 96.296  1.00 173.68 ? 537 TYR A CD1   1 
ATOM   4032 C  CD2   . TYR A 1 510 ? 14.822  101.410 95.884  1.00 173.14 ? 537 TYR A CD2   1 
ATOM   4033 C  CE1   . TYR A 1 510 ? 12.602  102.777 94.988  1.00 175.21 ? 537 TYR A CE1   1 
ATOM   4034 C  CE2   . TYR A 1 510 ? 14.406  101.263 94.574  1.00 173.27 ? 537 TYR A CE2   1 
ATOM   4035 C  CZ    . TYR A 1 510 ? 13.296  101.949 94.132  1.00 173.99 ? 537 TYR A CZ    1 
ATOM   4036 O  OH    . TYR A 1 510 ? 12.880  101.806 92.829  1.00 178.85 ? 537 TYR A OH    1 
ATOM   4037 N  N     . LYS A 1 511 ? 15.715  103.917 100.682 1.00 166.92 ? 538 LYS A N     1 
ATOM   4038 C  CA    . LYS A 1 511 ? 16.189  103.900 102.062 1.00 161.96 ? 538 LYS A CA    1 
ATOM   4039 C  C     . LYS A 1 511 ? 15.441  104.904 102.928 1.00 167.70 ? 538 LYS A C     1 
ATOM   4040 O  O     . LYS A 1 511 ? 15.333  104.713 104.144 1.00 167.94 ? 538 LYS A O     1 
ATOM   4041 C  CB    . LYS A 1 511 ? 17.689  104.188 102.113 1.00 153.32 ? 538 LYS A CB    1 
ATOM   4042 C  CG    . LYS A 1 511 ? 18.549  103.248 101.293 1.00 146.63 ? 538 LYS A CG    1 
ATOM   4043 C  CD    . LYS A 1 511 ? 20.015  103.608 101.454 1.00 149.51 ? 538 LYS A CD    1 
ATOM   4044 C  CE    . LYS A 1 511 ? 20.263  105.067 101.098 1.00 148.83 ? 538 LYS A CE    1 
ATOM   4045 N  NZ    . LYS A 1 511 ? 21.665  105.487 101.373 1.00 143.59 ? 538 LYS A NZ    1 
ATOM   4046 N  N     . ALA A 1 512 ? 14.922  105.977 102.324 1.00 167.74 ? 539 ALA A N     1 
ATOM   4047 C  CA    . ALA A 1 512 ? 14.196  106.986 103.087 1.00 163.85 ? 539 ALA A CA    1 
ATOM   4048 C  C     . ALA A 1 512 ? 12.897  106.449 103.677 1.00 174.11 ? 539 ALA A C     1 
ATOM   4049 O  O     . ALA A 1 512 ? 12.329  107.087 104.570 1.00 168.29 ? 539 ALA A O     1 
ATOM   4050 C  CB    . ALA A 1 512 ? 13.904  108.202 102.208 1.00 158.27 ? 539 ALA A CB    1 
ATOM   4051 N  N     . HIS A 1 513 ? 12.416  105.298 103.205 1.00 180.24 ? 540 HIS A N     1 
ATOM   4052 C  CA    . HIS A 1 513 ? 11.189  104.710 103.727 1.00 177.02 ? 540 HIS A CA    1 
ATOM   4053 C  C     . HIS A 1 513 ? 11.405  103.891 104.995 1.00 172.47 ? 540 HIS A C     1 
ATOM   4054 O  O     . HIS A 1 513 ? 10.421  103.533 105.652 1.00 170.99 ? 540 HIS A O     1 
ATOM   4055 C  CB    . HIS A 1 513 ? 10.527  103.825 102.664 1.00 176.45 ? 540 HIS A CB    1 
ATOM   4056 C  CG    . HIS A 1 513 ? 9.841   104.591 101.575 1.00 180.74 ? 540 HIS A CG    1 
ATOM   4057 N  ND1   . HIS A 1 513 ? 10.453  104.893 100.377 1.00 184.68 ? 540 HIS A ND1   1 
ATOM   4058 C  CD2   . HIS A 1 513 ? 8.592   105.110 101.500 1.00 178.57 ? 540 HIS A CD2   1 
ATOM   4059 C  CE1   . HIS A 1 513 ? 9.611   105.567 99.613  1.00 182.73 ? 540 HIS A CE1   1 
ATOM   4060 N  NE2   . HIS A 1 513 ? 8.476   105.712 100.271 1.00 179.55 ? 540 HIS A NE2   1 
ATOM   4061 N  N     . PHE A 1 514 ? 12.652  103.592 105.360 1.00 160.99 ? 541 PHE A N     1 
ATOM   4062 C  CA    . PHE A 1 514 ? 12.962  102.737 106.504 1.00 156.36 ? 541 PHE A CA    1 
ATOM   4063 C  C     . PHE A 1 514 ? 13.803  103.534 107.494 1.00 160.15 ? 541 PHE A C     1 
ATOM   4064 O  O     . PHE A 1 514 ? 14.955  103.874 107.205 1.00 160.20 ? 541 PHE A O     1 
ATOM   4065 C  CB    . PHE A 1 514 ? 13.679  101.469 106.047 1.00 154.85 ? 541 PHE A CB    1 
ATOM   4066 C  CG    . PHE A 1 514 ? 12.882  100.651 105.071 1.00 154.45 ? 541 PHE A CG    1 
ATOM   4067 C  CD1   . PHE A 1 514 ? 12.926  100.930 103.715 1.00 153.47 ? 541 PHE A CD1   1 
ATOM   4068 C  CD2   . PHE A 1 514 ? 12.076  99.614  105.510 1.00 156.35 ? 541 PHE A CD2   1 
ATOM   4069 C  CE1   . PHE A 1 514 ? 12.190  100.186 102.815 1.00 155.45 ? 541 PHE A CE1   1 
ATOM   4070 C  CE2   . PHE A 1 514 ? 11.336  98.866  104.614 1.00 150.50 ? 541 PHE A CE2   1 
ATOM   4071 C  CZ    . PHE A 1 514 ? 11.393  99.153  103.265 1.00 152.94 ? 541 PHE A CZ    1 
ATOM   4072 N  N     . SER A 1 515 ? 13.228  103.810 108.669 1.00 177.36 ? 542 SER A N     1 
ATOM   4073 C  CA    . SER A 1 515 ? 13.812  104.791 109.581 1.00 171.27 ? 542 SER A CA    1 
ATOM   4074 C  C     . SER A 1 515 ? 15.074  104.276 110.262 1.00 162.97 ? 542 SER A C     1 
ATOM   4075 O  O     . SER A 1 515 ? 15.971  105.070 110.569 1.00 160.33 ? 542 SER A O     1 
ATOM   4076 C  CB    . SER A 1 515 ? 12.784  105.207 110.633 1.00 160.41 ? 542 SER A CB    1 
ATOM   4077 O  OG    . SER A 1 515 ? 12.418  104.109 111.451 1.00 163.56 ? 542 SER A OG    1 
ATOM   4078 N  N     . LEU A 1 516 ? 15.165  102.974 110.518 1.00 149.56 ? 543 LEU A N     1 
ATOM   4079 C  CA    . LEU A 1 516 ? 16.309  102.398 111.224 1.00 148.23 ? 543 LEU A CA    1 
ATOM   4080 C  C     . LEU A 1 516 ? 16.944  101.329 110.342 1.00 152.43 ? 543 LEU A C     1 
ATOM   4081 O  O     . LEU A 1 516 ? 16.417  100.219 110.217 1.00 153.30 ? 543 LEU A O     1 
ATOM   4082 C  CB    . LEU A 1 516 ? 15.894  101.830 112.578 1.00 137.71 ? 543 LEU A CB    1 
ATOM   4083 C  CG    . LEU A 1 516 ? 17.060  101.388 113.465 1.00 140.75 ? 543 LEU A CG    1 
ATOM   4084 C  CD1   . LEU A 1 516 ? 18.055  102.527 113.645 1.00 142.71 ? 543 LEU A CD1   1 
ATOM   4085 C  CD2   . LEU A 1 516 ? 16.559  100.894 114.813 1.00 128.28 ? 543 LEU A CD2   1 
ATOM   4086 N  N     . ARG A 1 517 ? 18.081  101.664 109.742 1.00 155.28 ? 544 ARG A N     1 
ATOM   4087 C  CA    . ARG A 1 517 ? 18.825  100.755 108.881 1.00 143.36 ? 544 ARG A CA    1 
ATOM   4088 C  C     . ARG A 1 517 ? 20.123  100.367 109.585 1.00 145.73 ? 544 ARG A C     1 
ATOM   4089 O  O     . ARG A 1 517 ? 21.227  100.708 109.155 1.00 147.61 ? 544 ARG A O     1 
ATOM   4090 C  CB    . ARG A 1 517 ? 19.075  101.416 107.516 1.00 139.84 ? 544 ARG A CB    1 
ATOM   4091 C  CG    . ARG A 1 517 ? 17.830  102.099 106.948 1.00 149.04 ? 544 ARG A CG    1 
ATOM   4092 C  CD    . ARG A 1 517 ? 18.034  102.622 105.531 1.00 157.82 ? 544 ARG A CD    1 
ATOM   4093 N  NE    . ARG A 1 517 ? 18.996  103.716 105.459 1.00 166.60 ? 544 ARG A NE    1 
ATOM   4094 C  CZ    . ARG A 1 517 ? 18.674  105.002 105.510 1.00 169.41 ? 544 ARG A CZ    1 
ATOM   4095 N  NH1   . ARG A 1 517 ? 17.418  105.395 105.653 1.00 168.95 ? 544 ARG A NH1   1 
ATOM   4096 N  NH2   . ARG A 1 517 ? 19.635  105.916 105.413 1.00 173.92 ? 544 ARG A NH2   1 
ATOM   4097 N  N     . ASN A 1 518 ? 19.972  99.631  110.689 1.00 146.42 ? 545 ASN A N     1 
ATOM   4098 C  CA    . ASN A 1 518 ? 21.064  99.332  111.607 1.00 148.43 ? 545 ASN A CA    1 
ATOM   4099 C  C     . ASN A 1 518 ? 21.577  97.901  111.475 1.00 145.80 ? 545 ASN A C     1 
ATOM   4100 O  O     . ASN A 1 518 ? 22.270  97.413  112.376 1.00 135.43 ? 545 ASN A O     1 
ATOM   4101 C  CB    . ASN A 1 518 ? 20.617  99.591  113.046 1.00 146.92 ? 545 ASN A CB    1 
ATOM   4102 C  CG    . ASN A 1 518 ? 19.500  98.657  113.487 1.00 147.41 ? 545 ASN A CG    1 
ATOM   4103 O  OD1   . ASN A 1 518 ? 18.761  98.117  112.660 1.00 139.64 ? 545 ASN A OD1   1 
ATOM   4104 N  ND2   . ASN A 1 518 ? 19.371  98.464  114.795 1.00 140.38 ? 545 ASN A ND2   1 
ATOM   4105 N  N     . LEU A 1 519 ? 21.254  97.219  110.381 1.00 144.52 ? 546 LEU A N     1 
ATOM   4106 C  CA    . LEU A 1 519 ? 21.650  95.827  110.235 1.00 130.35 ? 546 LEU A CA    1 
ATOM   4107 C  C     . LEU A 1 519 ? 23.151  95.720  110.004 1.00 130.11 ? 546 LEU A C     1 
ATOM   4108 O  O     . LEU A 1 519 ? 23.745  96.521  109.278 1.00 141.26 ? 546 LEU A O     1 
ATOM   4109 C  CB    . LEU A 1 519 ? 20.891  95.175  109.081 1.00 127.12 ? 546 LEU A CB    1 
ATOM   4110 C  CG    . LEU A 1 519 ? 20.796  93.649  109.113 1.00 129.64 ? 546 LEU A CG    1 
ATOM   4111 C  CD1   . LEU A 1 519 ? 19.958  93.196  110.297 1.00 123.91 ? 546 LEU A CD1   1 
ATOM   4112 C  CD2   . LEU A 1 519 ? 20.223  93.116  107.807 1.00 118.54 ? 546 LEU A CD2   1 
ATOM   4113 N  N     . HIS A 1 520 ? 23.766  94.725  110.635 1.00 134.37 ? 547 HIS A N     1 
ATOM   4114 C  CA    . HIS A 1 520 ? 25.195  94.453  110.502 1.00 139.39 ? 547 HIS A CA    1 
ATOM   4115 C  C     . HIS A 1 520 ? 25.340  93.197  109.645 1.00 136.58 ? 547 HIS A C     1 
ATOM   4116 O  O     . HIS A 1 520 ? 25.192  92.077  110.141 1.00 137.20 ? 547 HIS A O     1 
ATOM   4117 C  CB    . HIS A 1 520 ? 25.841  94.288  111.874 1.00 129.48 ? 547 HIS A CB    1 
ATOM   4118 C  CG    . HIS A 1 520 ? 25.573  95.429  112.808 1.00 137.58 ? 547 HIS A CG    1 
ATOM   4119 N  ND1   . HIS A 1 520 ? 25.122  95.245  114.098 1.00 138.31 ? 547 HIS A ND1   1 
ATOM   4120 C  CD2   . HIS A 1 520 ? 25.690  96.767  112.638 1.00 128.20 ? 547 HIS A CD2   1 
ATOM   4121 C  CE1   . HIS A 1 520 ? 24.974  96.421  114.683 1.00 143.74 ? 547 HIS A CE1   1 
ATOM   4122 N  NE2   . HIS A 1 520 ? 25.312  97.361  113.819 1.00 142.64 ? 547 HIS A NE2   1 
ATOM   4123 N  N     . ALA A 1 521 ? 25.627  93.387  108.359 1.00 127.47 ? 548 ALA A N     1 
ATOM   4124 C  CA    . ALA A 1 521 ? 25.648  92.302  107.389 1.00 121.33 ? 548 ALA A CA    1 
ATOM   4125 C  C     . ALA A 1 521 ? 27.059  92.059  106.869 1.00 124.18 ? 548 ALA A C     1 
ATOM   4126 O  O     . ALA A 1 521 ? 27.850  92.991  106.702 1.00 120.63 ? 548 ALA A O     1 
ATOM   4127 C  CB    . ALA A 1 521 ? 24.711  92.595  106.215 1.00 119.77 ? 548 ALA A CB    1 
ATOM   4128 N  N     . PHE A 1 522 ? 27.355  90.788  106.597 1.00 120.61 ? 549 PHE A N     1 
ATOM   4129 C  CA    . PHE A 1 522 ? 28.670  90.345  106.154 1.00 106.99 ? 549 PHE A CA    1 
ATOM   4130 C  C     . PHE A 1 522 ? 28.504  89.368  104.998 1.00 108.55 ? 549 PHE A C     1 
ATOM   4131 O  O     . PHE A 1 522 ? 27.392  89.109  104.529 1.00 113.16 ? 549 PHE A O     1 
ATOM   4132 C  CB    . PHE A 1 522 ? 29.453  89.700  107.304 1.00 101.12 ? 549 PHE A CB    1 
ATOM   4133 C  CG    . PHE A 1 522 ? 29.615  90.594  108.495 1.00 113.54 ? 549 PHE A CG    1 
ATOM   4134 C  CD1   . PHE A 1 522 ? 28.682  90.583  109.522 1.00 124.10 ? 549 PHE A CD1   1 
ATOM   4135 C  CD2   . PHE A 1 522 ? 30.694  91.459  108.585 1.00 113.59 ? 549 PHE A CD2   1 
ATOM   4136 C  CE1   . PHE A 1 522 ? 28.830  91.412  110.617 1.00 127.45 ? 549 PHE A CE1   1 
ATOM   4137 C  CE2   . PHE A 1 522 ? 30.844  92.288  109.679 1.00 117.25 ? 549 PHE A CE2   1 
ATOM   4138 C  CZ    . PHE A 1 522 ? 29.911  92.264  110.695 1.00 125.65 ? 549 PHE A CZ    1 
ATOM   4139 N  N     . SER A 1 523 ? 29.625  88.819  104.540 1.00 101.20 ? 550 SER A N     1 
ATOM   4140 C  CA    . SER A 1 523 ? 29.599  87.836  103.469 1.00 96.55  ? 550 SER A CA    1 
ATOM   4141 C  C     . SER A 1 523 ? 30.899  87.049  103.480 1.00 102.81 ? 550 SER A C     1 
ATOM   4142 O  O     . SER A 1 523 ? 31.954  87.572  103.848 1.00 106.30 ? 550 SER A O     1 
ATOM   4143 C  CB    . SER A 1 523 ? 29.394  88.490  102.100 1.00 99.40  ? 550 SER A CB    1 
ATOM   4144 O  OG    . SER A 1 523 ? 29.585  87.543  101.062 1.00 112.19 ? 550 SER A OG    1 
ATOM   4145 N  N     . VAL A 1 524 ? 30.805  85.782  103.074 1.00 100.78 ? 551 VAL A N     1 
ATOM   4146 C  CA    . VAL A 1 524 ? 31.994  84.958  102.918 1.00 102.91 ? 551 VAL A CA    1 
ATOM   4147 C  C     . VAL A 1 524 ? 32.781  85.442  101.710 1.00 103.44 ? 551 VAL A C     1 
ATOM   4148 O  O     . VAL A 1 524 ? 32.206  85.809  100.676 1.00 102.48 ? 551 VAL A O     1 
ATOM   4149 C  CB    . VAL A 1 524 ? 31.608  83.477  102.768 1.00 107.99 ? 551 VAL A CB    1 
ATOM   4150 C  CG1   . VAL A 1 524 ? 32.832  82.588  102.926 1.00 106.74 ? 551 VAL A CG1   1 
ATOM   4151 C  CG2   . VAL A 1 524 ? 30.528  83.104  103.768 1.00 101.72 ? 551 VAL A CG2   1 
ATOM   4152 N  N     . GLU A 1 525 ? 34.102  85.455  101.837 1.00 109.83 ? 552 GLU A N     1 
ATOM   4153 C  CA    . GLU A 1 525 ? 34.985  85.886  100.755 1.00 97.67  ? 552 GLU A CA    1 
ATOM   4154 C  C     . GLU A 1 525 ? 36.067  84.836  100.547 1.00 94.39  ? 552 GLU A C     1 
ATOM   4155 O  O     . GLU A 1 525 ? 36.926  84.652  101.435 1.00 98.25  ? 552 GLU A O     1 
ATOM   4156 C  CB    . GLU A 1 525 ? 35.596  87.251  101.054 1.00 100.13 ? 552 GLU A CB    1 
ATOM   4157 C  CG    . GLU A 1 525 ? 36.347  87.839  99.881  1.00 113.42 ? 552 GLU A CG    1 
ATOM   4158 C  CD    . GLU A 1 525 ? 35.490  87.925  98.631  1.00 120.72 ? 552 GLU A CD    1 
ATOM   4159 O  OE1   . GLU A 1 525 ? 34.303  88.302  98.748  1.00 116.25 ? 552 GLU A OE1   1 
ATOM   4160 O  OE2   . GLU A 1 525 ? 36.003  87.608  97.535  1.00 113.12 ? 552 GLU A OE2   1 
ATOM   4161 N  N     . PRO A 1 526 ? 36.067  84.123  99.417  1.00 92.96  ? 553 PRO A N     1 
ATOM   4162 C  CA    . PRO A 1 526 ? 35.102  84.208  98.313  1.00 98.25  ? 553 PRO A CA    1 
ATOM   4163 C  C     . PRO A 1 526 ? 33.766  83.560  98.661  1.00 95.62  ? 553 PRO A C     1 
ATOM   4164 O  O     . PRO A 1 526 ? 33.573  83.052  99.764  1.00 90.91  ? 553 PRO A O     1 
ATOM   4165 C  CB    . PRO A 1 526 ? 35.820  83.469  97.177  1.00 88.46  ? 553 PRO A CB    1 
ATOM   4166 C  CG    . PRO A 1 526 ? 36.658  82.448  97.887  1.00 82.12  ? 553 PRO A CG    1 
ATOM   4167 C  CD    . PRO A 1 526 ? 37.127  83.137  99.143  1.00 83.10  ? 553 PRO A CD    1 
ATOM   4168 N  N     . LEU A 1 527 ? 32.823  83.578  97.724  1.00 99.13  ? 554 LEU A N     1 
ATOM   4169 C  CA    . LEU A 1 527 ? 31.518  82.983  97.963  1.00 94.08  ? 554 LEU A CA    1 
ATOM   4170 C  C     . LEU A 1 527 ? 31.615  81.464  97.966  1.00 92.71  ? 554 LEU A C     1 
ATOM   4171 O  O     . LEU A 1 527 ? 32.419  80.866  97.246  1.00 98.08  ? 554 LEU A O     1 
ATOM   4172 C  CB    . LEU A 1 527 ? 30.520  83.437  96.899  1.00 84.64  ? 554 LEU A CB    1 
ATOM   4173 C  CG    . LEU A 1 527 ? 30.247  84.938  96.848  1.00 100.18 ? 554 LEU A CG    1 
ATOM   4174 C  CD1   . LEU A 1 527 ? 29.503  85.296  95.575  1.00 95.29  ? 554 LEU A CD1   1 
ATOM   4175 C  CD2   . LEU A 1 527 ? 29.470  85.389  98.087  1.00 87.02  ? 554 LEU A CD2   1 
ATOM   4176 N  N     . LEU A 1 528 ? 30.779  80.840  98.791  1.00 89.99  ? 555 LEU A N     1 
ATOM   4177 C  CA    . LEU A 1 528 ? 30.689  79.389  98.837  1.00 87.32  ? 555 LEU A CA    1 
ATOM   4178 C  C     . LEU A 1 528 ? 29.516  78.845  98.033  1.00 94.56  ? 555 LEU A C     1 
ATOM   4179 O  O     . LEU A 1 528 ? 29.429  77.626  97.844  1.00 92.31  ? 555 LEU A O     1 
ATOM   4180 C  CB    . LEU A 1 528 ? 30.581  78.908  100.289 1.00 87.44  ? 555 LEU A CB    1 
ATOM   4181 C  CG    . LEU A 1 528 ? 31.630  79.448  101.266 1.00 95.97  ? 555 LEU A CG    1 
ATOM   4182 C  CD1   . LEU A 1 528 ? 31.532  78.736  102.606 1.00 82.75  ? 555 LEU A CD1   1 
ATOM   4183 C  CD2   . LEU A 1 528 ? 33.042  79.341  100.695 1.00 92.60  ? 555 LEU A CD2   1 
ATOM   4184 N  N     . ILE A 1 529 ? 28.624  79.708  97.550  1.00 92.60  ? 556 ILE A N     1 
ATOM   4185 C  CA    . ILE A 1 529 ? 27.446  79.280  96.805  1.00 99.68  ? 556 ILE A CA    1 
ATOM   4186 C  C     . ILE A 1 529 ? 27.228  80.224  95.630  1.00 104.20 ? 556 ILE A C     1 
ATOM   4187 O  O     . ILE A 1 529 ? 27.370  81.445  95.763  1.00 105.76 ? 556 ILE A O     1 
ATOM   4188 C  CB    . ILE A 1 529 ? 26.202  79.214  97.717  1.00 99.22  ? 556 ILE A CB    1 
ATOM   4189 C  CG1   . ILE A 1 529 ? 26.291  77.984  98.621  1.00 96.85  ? 556 ILE A CG1   1 
ATOM   4190 C  CG2   . ILE A 1 529 ? 24.915  79.187  96.901  1.00 90.40  ? 556 ILE A CG2   1 
ATOM   4191 C  CD1   . ILE A 1 529 ? 25.218  77.917  99.660  1.00 101.28 ? 556 ILE A CD1   1 
ATOM   4192 N  N     . TYR A 1 530 ? 26.897  79.652  94.480  1.00 94.67  ? 557 TYR A N     1 
ATOM   4193 C  CA    . TYR A 1 530 ? 26.582  80.359  93.251  1.00 96.33  ? 557 TYR A CA    1 
ATOM   4194 C  C     . TYR A 1 530 ? 25.307  79.768  92.668  1.00 106.27 ? 557 TYR A C     1 
ATOM   4195 O  O     . TYR A 1 530 ? 24.891  78.672  93.057  1.00 109.31 ? 557 TYR A O     1 
ATOM   4196 C  CB    . TYR A 1 530 ? 27.734  80.245  92.238  1.00 99.97  ? 557 TYR A CB    1 
ATOM   4197 C  CG    . TYR A 1 530 ? 29.059  80.780  92.736  1.00 94.31  ? 557 TYR A CG    1 
ATOM   4198 C  CD1   . TYR A 1 530 ? 29.417  82.108  92.536  1.00 91.81  ? 557 TYR A CD1   1 
ATOM   4199 C  CD2   . TYR A 1 530 ? 29.955  79.954  93.405  1.00 102.88 ? 557 TYR A CD2   1 
ATOM   4200 C  CE1   . TYR A 1 530 ? 30.631  82.600  92.991  1.00 96.91  ? 557 TYR A CE1   1 
ATOM   4201 C  CE2   . TYR A 1 530 ? 31.168  80.436  93.865  1.00 106.06 ? 557 TYR A CE2   1 
ATOM   4202 C  CZ    . TYR A 1 530 ? 31.502  81.759  93.656  1.00 106.16 ? 557 TYR A CZ    1 
ATOM   4203 O  OH    . TYR A 1 530 ? 32.711  82.237  94.114  1.00 100.19 ? 557 TYR A OH    1 
ATOM   4204 N  N     . PRO A 1 531 ? 24.652  80.471  91.745  1.00 113.37 ? 558 PRO A N     1 
ATOM   4205 C  CA    . PRO A 1 531 ? 23.448  79.913  91.117  1.00 116.79 ? 558 PRO A CA    1 
ATOM   4206 C  C     . PRO A 1 531 ? 23.777  78.771  90.167  1.00 120.71 ? 558 PRO A C     1 
ATOM   4207 O  O     . PRO A 1 531 ? 24.903  78.625  89.685  1.00 115.85 ? 558 PRO A O     1 
ATOM   4208 C  CB    . PRO A 1 531 ? 22.852  81.103  90.355  1.00 119.32 ? 558 PRO A CB    1 
ATOM   4209 C  CG    . PRO A 1 531 ? 23.496  82.309  90.950  1.00 121.09 ? 558 PRO A CG    1 
ATOM   4210 C  CD    . PRO A 1 531 ? 24.864  81.874  91.358  1.00 117.08 ? 558 PRO A CD    1 
ATOM   4211 N  N     . THR A 1 532 ? 22.755  77.955  89.894  1.00 115.09 ? 559 THR A N     1 
ATOM   4212 C  CA    . THR A 1 532 ? 22.918  76.849  88.955  1.00 111.43 ? 559 THR A CA    1 
ATOM   4213 C  C     . THR A 1 532 ? 23.137  77.362  87.538  1.00 125.30 ? 559 THR A C     1 
ATOM   4214 O  O     . THR A 1 532 ? 24.007  76.866  86.815  1.00 129.50 ? 559 THR A O     1 
ATOM   4215 C  CB    . THR A 1 532 ? 21.699  75.928  89.007  1.00 111.46 ? 559 THR A CB    1 
ATOM   4216 O  OG1   . THR A 1 532 ? 20.509  76.694  88.773  1.00 123.29 ? 559 THR A OG1   1 
ATOM   4217 C  CG2   . THR A 1 532 ? 21.603  75.252  90.359  1.00 107.30 ? 559 THR A CG2   1 
ATOM   4218 N  N     . HIS A 1 533 ? 22.351  78.353  87.123  1.00 139.79 ? 560 HIS A N     1 
ATOM   4219 C  CA    . HIS A 1 533 ? 22.475  78.969  85.808  1.00 143.97 ? 560 HIS A CA    1 
ATOM   4220 C  C     . HIS A 1 533 ? 22.726  80.457  85.998  1.00 159.06 ? 560 HIS A C     1 
ATOM   4221 O  O     . HIS A 1 533 ? 21.859  81.172  86.513  1.00 168.82 ? 560 HIS A O     1 
ATOM   4222 C  CB    . HIS A 1 533 ? 21.218  78.730  84.968  1.00 154.38 ? 560 HIS A CB    1 
ATOM   4223 C  CG    . HIS A 1 533 ? 20.854  77.284  84.828  1.00 164.73 ? 560 HIS A CG    1 
ATOM   4224 N  ND1   . HIS A 1 533 ? 20.074  76.619  85.750  1.00 156.78 ? 560 HIS A ND1   1 
ATOM   4225 C  CD2   . HIS A 1 533 ? 21.169  76.372  83.877  1.00 162.26 ? 560 HIS A CD2   1 
ATOM   4226 C  CE1   . HIS A 1 533 ? 19.922  75.362  85.372  1.00 151.26 ? 560 HIS A CE1   1 
ATOM   4227 N  NE2   . HIS A 1 533 ? 20.577  75.187  84.238  1.00 154.37 ? 560 HIS A NE2   1 
ATOM   4228 N  N     . TYR A 1 534 ? 23.906  80.917  85.591  1.00 189.63 ? 561 TYR A N     1 
ATOM   4229 C  CA    . TYR A 1 534 ? 24.294  82.312  85.787  1.00 197.98 ? 561 TYR A CA    1 
ATOM   4230 C  C     . TYR A 1 534 ? 23.458  83.238  84.910  1.00 196.42 ? 561 TYR A C     1 
ATOM   4231 O  O     . TYR A 1 534 ? 22.901  84.228  85.388  1.00 191.89 ? 561 TYR A O     1 
ATOM   4232 C  CB    . TYR A 1 534 ? 25.786  82.518  85.490  1.00 192.10 ? 561 TYR A CB    1 
ATOM   4233 C  CG    . TYR A 1 534 ? 26.741  81.961  86.532  1.00 188.77 ? 561 TYR A CG    1 
ATOM   4234 C  CD1   . TYR A 1 534 ? 26.363  80.930  87.385  1.00 176.58 ? 561 TYR A CD1   1 
ATOM   4235 C  CD2   . TYR A 1 534 ? 28.026  82.476  86.663  1.00 186.03 ? 561 TYR A CD2   1 
ATOM   4236 C  CE1   . TYR A 1 534 ? 27.237  80.424  88.331  1.00 162.66 ? 561 TYR A CE1   1 
ATOM   4237 C  CE2   . TYR A 1 534 ? 28.905  81.977  87.608  1.00 178.62 ? 561 TYR A CE2   1 
ATOM   4238 C  CZ    . TYR A 1 534 ? 28.506  80.952  88.439  1.00 172.08 ? 561 TYR A CZ    1 
ATOM   4239 O  OH    . TYR A 1 534 ? 29.379  80.454  89.379  1.00 162.99 ? 561 TYR A OH    1 
ATOM   4240 N  N     . ARG B 1 15  ? 46.484  69.083  62.604  1.00 93.96  ? 42  ARG B N     1 
ATOM   4241 C  CA    . ARG B 1 15  ? 47.786  68.593  62.169  1.00 91.88  ? 42  ARG B CA    1 
ATOM   4242 C  C     . ARG B 1 15  ? 47.680  67.156  61.702  1.00 94.97  ? 42  ARG B C     1 
ATOM   4243 O  O     . ARG B 1 15  ? 47.253  66.280  62.455  1.00 95.94  ? 42  ARG B O     1 
ATOM   4244 C  CB    . ARG B 1 15  ? 48.821  68.693  63.295  1.00 109.98 ? 42  ARG B CB    1 
ATOM   4245 C  CG    . ARG B 1 15  ? 49.306  70.109  63.599  1.00 140.18 ? 42  ARG B CG    1 
ATOM   4246 C  CD    . ARG B 1 15  ? 50.458  70.537  62.687  1.00 135.93 ? 42  ARG B CD    1 
ATOM   4247 N  NE    . ARG B 1 15  ? 51.539  69.556  62.664  1.00 145.85 ? 42  ARG B NE    1 
ATOM   4248 C  CZ    . ARG B 1 15  ? 52.768  69.802  62.230  1.00 132.56 ? 42  ARG B CZ    1 
ATOM   4249 N  NH1   . ARG B 1 15  ? 53.126  71.004  61.807  1.00 108.86 ? 42  ARG B NH1   1 
ATOM   4250 N  NH2   . ARG B 1 15  ? 53.663  68.816  62.225  1.00 119.23 ? 42  ARG B NH2   1 
ATOM   4251 N  N     . TRP B 1 16  ? 48.073  66.909  60.457  1.00 96.68  ? 43  TRP B N     1 
ATOM   4252 C  CA    . TRP B 1 16  ? 48.069  65.553  59.937  1.00 89.80  ? 43  TRP B CA    1 
ATOM   4253 C  C     . TRP B 1 16  ? 49.262  64.776  60.474  1.00 85.37  ? 43  TRP B C     1 
ATOM   4254 O  O     . TRP B 1 16  ? 50.384  65.288  60.525  1.00 86.05  ? 43  TRP B O     1 
ATOM   4255 C  CB    . TRP B 1 16  ? 48.098  65.542  58.410  1.00 75.84  ? 43  TRP B CB    1 
ATOM   4256 C  CG    . TRP B 1 16  ? 48.267  64.147  57.880  1.00 84.71  ? 43  TRP B CG    1 
ATOM   4257 C  CD1   . TRP B 1 16  ? 47.334  63.152  57.886  1.00 80.89  ? 43  TRP B CD1   1 
ATOM   4258 C  CD2   . TRP B 1 16  ? 49.450  63.583  57.296  1.00 81.59  ? 43  TRP B CD2   1 
ATOM   4259 N  NE1   . TRP B 1 16  ? 47.857  62.009  57.331  1.00 79.61  ? 43  TRP B NE1   1 
ATOM   4260 C  CE2   . TRP B 1 16  ? 49.154  62.247  56.961  1.00 83.68  ? 43  TRP B CE2   1 
ATOM   4261 C  CE3   . TRP B 1 16  ? 50.727  64.080  57.018  1.00 78.20  ? 43  TRP B CE3   1 
ATOM   4262 C  CZ2   . TRP B 1 16  ? 50.088  61.401  56.364  1.00 75.33  ? 43  TRP B CZ2   1 
ATOM   4263 C  CZ3   . TRP B 1 16  ? 51.651  63.242  56.424  1.00 82.54  ? 43  TRP B CZ3   1 
ATOM   4264 C  CH2   . TRP B 1 16  ? 51.328  61.917  56.104  1.00 86.88  ? 43  TRP B CH2   1 
ATOM   4265 N  N     . SER B 1 17  ? 49.010  63.536  60.873  1.00 76.60  ? 44  SER B N     1 
ATOM   4266 C  CA    . SER B 1 17  ? 50.050  62.649  61.364  1.00 71.90  ? 44  SER B CA    1 
ATOM   4267 C  C     . SER B 1 17  ? 49.737  61.233  60.897  1.00 69.73  ? 44  SER B C     1 
ATOM   4268 O  O     . SER B 1 17  ? 48.653  60.708  61.181  1.00 88.26  ? 44  SER B O     1 
ATOM   4269 C  CB    . SER B 1 17  ? 50.149  62.722  62.888  1.00 79.66  ? 44  SER B CB    1 
ATOM   4270 O  OG    . SER B 1 17  ? 51.359  62.158  63.357  1.00 94.60  ? 44  SER B OG    1 
ATOM   4271 N  N     . PRO B 1 18  ? 50.648  60.590  60.172  1.00 64.85  ? 45  PRO B N     1 
ATOM   4272 C  CA    . PRO B 1 18  ? 50.351  59.260  59.623  1.00 69.31  ? 45  PRO B CA    1 
ATOM   4273 C  C     . PRO B 1 18  ? 50.362  58.193  60.709  1.00 68.91  ? 45  PRO B C     1 
ATOM   4274 O  O     . PRO B 1 18  ? 51.283  58.126  61.523  1.00 86.66  ? 45  PRO B O     1 
ATOM   4275 C  CB    . PRO B 1 18  ? 51.476  59.040  58.607  1.00 73.19  ? 45  PRO B CB    1 
ATOM   4276 C  CG    . PRO B 1 18  ? 52.608  59.884  59.123  1.00 65.71  ? 45  PRO B CG    1 
ATOM   4277 C  CD    . PRO B 1 18  ? 51.970  61.087  59.754  1.00 72.08  ? 45  PRO B CD    1 
ATOM   4278 N  N     . GLU B 1 19  ? 49.331  57.354  60.715  1.00 70.66  ? 46  GLU B N     1 
ATOM   4279 C  CA    . GLU B 1 19  ? 49.321  56.192  61.592  1.00 67.35  ? 46  GLU B CA    1 
ATOM   4280 C  C     . GLU B 1 19  ? 50.230  55.114  61.020  1.00 55.96  ? 46  GLU B C     1 
ATOM   4281 O  O     . GLU B 1 19  ? 50.329  54.951  59.802  1.00 82.49  ? 46  GLU B O     1 
ATOM   4282 C  CB    . GLU B 1 19  ? 47.900  55.642  61.755  1.00 56.09  ? 46  GLU B CB    1 
ATOM   4283 C  CG    . GLU B 1 19  ? 46.944  56.583  62.463  1.00 63.79  ? 46  GLU B CG    1 
ATOM   4284 C  CD    . GLU B 1 19  ? 47.324  56.831  63.909  1.00 76.82  ? 46  GLU B CD    1 
ATOM   4285 O  OE1   . GLU B 1 19  ? 47.424  55.846  64.671  1.00 80.16  ? 46  GLU B OE1   1 
ATOM   4286 O  OE2   . GLU B 1 19  ? 47.523  58.007  64.284  1.00 77.61  ? 46  GLU B OE2   1 
ATOM   4287 N  N     . SER B 1 20  ? 50.902  54.381  61.905  1.00 67.22  ? 47  SER B N     1 
ATOM   4288 C  CA    . SER B 1 20  ? 51.760  53.287  61.485  1.00 57.06  ? 47  SER B CA    1 
ATOM   4289 C  C     . SER B 1 20  ? 50.888  52.171  60.916  1.00 52.34  ? 47  SER B C     1 
ATOM   4290 O  O     . SER B 1 20  ? 49.663  52.200  61.056  1.00 59.45  ? 47  SER B O     1 
ATOM   4291 C  CB    . SER B 1 20  ? 52.613  52.811  62.666  1.00 62.25  ? 47  SER B CB    1 
ATOM   4292 O  OG    . SER B 1 20  ? 51.819  52.514  63.804  1.00 69.02  ? 47  SER B OG    1 
ATOM   4293 N  N     . PRO B 1 21  ? 51.478  51.181  60.246  1.00 57.18  ? 48  PRO B N     1 
ATOM   4294 C  CA    . PRO B 1 21  ? 50.663  50.085  59.709  1.00 63.49  ? 48  PRO B CA    1 
ATOM   4295 C  C     . PRO B 1 21  ? 50.097  49.220  60.820  1.00 59.47  ? 48  PRO B C     1 
ATOM   4296 O  O     . PRO B 1 21  ? 50.656  49.126  61.914  1.00 65.36  ? 48  PRO B O     1 
ATOM   4297 C  CB    . PRO B 1 21  ? 51.647  49.289  58.843  1.00 49.56  ? 48  PRO B CB    1 
ATOM   4298 C  CG    . PRO B 1 21  ? 52.774  50.195  58.596  1.00 51.09  ? 48  PRO B CG    1 
ATOM   4299 C  CD    . PRO B 1 21  ? 52.879  51.067  59.813  1.00 60.49  ? 48  PRO B CD    1 
ATOM   4300 N  N     . LEU B 1 22  ? 48.962  48.592  60.528  1.00 68.29  ? 49  LEU B N     1 
ATOM   4301 C  CA    . LEU B 1 22  ? 48.414  47.596  61.436  1.00 66.03  ? 49  LEU B CA    1 
ATOM   4302 C  C     . LEU B 1 22  ? 49.287  46.349  61.429  1.00 65.02  ? 49  LEU B C     1 
ATOM   4303 O  O     . LEU B 1 22  ? 49.836  45.958  60.394  1.00 69.22  ? 49  LEU B O     1 
ATOM   4304 C  CB    . LEU B 1 22  ? 46.989  47.226  61.031  1.00 48.30  ? 49  LEU B CB    1 
ATOM   4305 C  CG    . LEU B 1 22  ? 46.001  48.383  60.917  1.00 51.04  ? 49  LEU B CG    1 
ATOM   4306 C  CD1   . LEU B 1 22  ? 44.685  47.895  60.338  1.00 50.11  ? 49  LEU B CD1   1 
ATOM   4307 C  CD2   . LEU B 1 22  ? 45.795  49.028  62.272  1.00 53.57  ? 49  LEU B CD2   1 
ATOM   4308 N  N     . GLN B 1 23  ? 49.417  45.723  62.592  1.00 61.80  ? 50  GLN B N     1 
ATOM   4309 C  CA    . GLN B 1 23  ? 50.080  44.435  62.644  1.00 59.70  ? 50  GLN B CA    1 
ATOM   4310 C  C     . GLN B 1 23  ? 49.228  43.385  61.933  1.00 65.69  ? 50  GLN B C     1 
ATOM   4311 O  O     . GLN B 1 23  ? 48.017  43.548  61.752  1.00 66.70  ? 50  GLN B O     1 
ATOM   4312 C  CB    . GLN B 1 23  ? 50.344  44.031  64.093  1.00 61.85  ? 50  GLN B CB    1 
ATOM   4313 C  CG    . GLN B 1 23  ? 51.172  45.039  64.866  1.00 69.93  ? 50  GLN B CG    1 
ATOM   4314 C  CD    . GLN B 1 23  ? 51.723  44.469  66.156  1.00 78.51  ? 50  GLN B CD    1 
ATOM   4315 O  OE1   . GLN B 1 23  ? 52.724  43.753  66.148  1.00 83.67  ? 50  GLN B OE1   1 
ATOM   4316 N  NE2   . GLN B 1 23  ? 51.072  44.783  67.276  1.00 64.30  ? 50  GLN B NE2   1 
ATOM   4317 N  N     . ALA B 1 24  ? 49.881  42.299  61.509  1.00 56.67  ? 51  ALA B N     1 
ATOM   4318 C  CA    . ALA B 1 24  ? 49.170  41.242  60.806  1.00 65.99  ? 51  ALA B CA    1 
ATOM   4319 C  C     . ALA B 1 24  ? 48.106  40.621  61.713  1.00 70.85  ? 51  ALA B C     1 
ATOM   4320 O  O     . ALA B 1 24  ? 48.193  40.709  62.942  1.00 63.26  ? 51  ALA B O     1 
ATOM   4321 C  CB    . ALA B 1 24  ? 50.146  40.169  60.322  1.00 57.32  ? 51  ALA B CB    1 
ATOM   4322 N  N     . PRO B 1 25  ? 47.081  40.004  61.124  1.00 70.90  ? 52  PRO B N     1 
ATOM   4323 C  CA    . PRO B 1 25  ? 46.077  39.306  61.934  1.00 61.61  ? 52  PRO B CA    1 
ATOM   4324 C  C     . PRO B 1 25  ? 46.705  38.238  62.818  1.00 73.06  ? 52  PRO B C     1 
ATOM   4325 O  O     . PRO B 1 25  ? 47.787  37.712  62.543  1.00 72.65  ? 52  PRO B O     1 
ATOM   4326 C  CB    . PRO B 1 25  ? 45.150  38.683  60.885  1.00 61.50  ? 52  PRO B CB    1 
ATOM   4327 C  CG    . PRO B 1 25  ? 45.267  39.585  59.710  1.00 47.74  ? 52  PRO B CG    1 
ATOM   4328 C  CD    . PRO B 1 25  ? 46.705  40.043  59.700  1.00 67.08  ? 52  PRO B CD    1 
ATOM   4329 N  N     . ARG B 1 26  ? 46.000  37.916  63.900  1.00 76.94  ? 53  ARG B N     1 
ATOM   4330 C  CA    . ARG B 1 26  ? 46.477  36.961  64.895  1.00 72.62  ? 53  ARG B CA    1 
ATOM   4331 C  C     . ARG B 1 26  ? 45.864  35.596  64.604  1.00 62.90  ? 53  ARG B C     1 
ATOM   4332 O  O     . ARG B 1 26  ? 44.656  35.403  64.768  1.00 67.41  ? 53  ARG B O     1 
ATOM   4333 C  CB    . ARG B 1 26  ? 46.134  37.444  66.299  1.00 63.38  ? 53  ARG B CB    1 
ATOM   4334 C  CG    . ARG B 1 26  ? 46.921  38.681  66.702  1.00 65.58  ? 53  ARG B CG    1 
ATOM   4335 C  CD    . ARG B 1 26  ? 46.103  39.595  67.587  1.00 67.66  ? 53  ARG B CD    1 
ATOM   4336 N  NE    . ARG B 1 26  ? 45.047  40.259  66.837  1.00 64.07  ? 53  ARG B NE    1 
ATOM   4337 C  CZ    . ARG B 1 26  ? 44.356  41.300  67.278  1.00 67.51  ? 53  ARG B CZ    1 
ATOM   4338 N  NH1   . ARG B 1 26  ? 44.547  41.794  68.492  1.00 77.83  ? 53  ARG B NH1   1 
ATOM   4339 N  NH2   . ARG B 1 26  ? 43.463  41.868  66.478  1.00 74.27  ? 53  ARG B NH2   1 
ATOM   4340 N  N     . VAL B 1 27  ? 46.705  34.653  64.184  1.00 63.56  ? 54  VAL B N     1 
ATOM   4341 C  CA    . VAL B 1 27  ? 46.276  33.342  63.709  1.00 66.51  ? 54  VAL B CA    1 
ATOM   4342 C  C     . VAL B 1 27  ? 46.712  32.276  64.706  1.00 65.22  ? 54  VAL B C     1 
ATOM   4343 O  O     . VAL B 1 27  ? 47.883  32.227  65.102  1.00 74.83  ? 54  VAL B O     1 
ATOM   4344 C  CB    . VAL B 1 27  ? 46.857  33.046  62.316  1.00 64.83  ? 54  VAL B CB    1 
ATOM   4345 C  CG1   . VAL B 1 27  ? 46.430  31.671  61.842  1.00 60.72  ? 54  VAL B CG1   1 
ATOM   4346 C  CG2   . VAL B 1 27  ? 46.444  34.126  61.325  1.00 65.28  ? 54  VAL B CG2   1 
ATOM   4347 N  N     . LEU B 1 28  ? 45.774  31.424  65.110  1.00 62.94  ? 55  LEU B N     1 
ATOM   4348 C  CA    . LEU B 1 28  ? 46.092  30.197  65.830  1.00 62.85  ? 55  LEU B CA    1 
ATOM   4349 C  C     . LEU B 1 28  ? 46.110  29.046  64.833  1.00 68.93  ? 55  LEU B C     1 
ATOM   4350 O  O     . LEU B 1 28  ? 45.122  28.815  64.125  1.00 57.05  ? 55  LEU B O     1 
ATOM   4351 C  CB    . LEU B 1 28  ? 45.083  29.916  66.943  1.00 62.96  ? 55  LEU B CB    1 
ATOM   4352 C  CG    . LEU B 1 28  ? 45.362  28.613  67.705  1.00 60.90  ? 55  LEU B CG    1 
ATOM   4353 C  CD1   . LEU B 1 28  ? 46.644  28.733  68.508  1.00 75.27  ? 55  LEU B CD1   1 
ATOM   4354 C  CD2   . LEU B 1 28  ? 44.216  28.220  68.610  1.00 62.72  ? 55  LEU B CD2   1 
ATOM   4355 N  N     . ILE B 1 29  ? 47.231  28.337  64.769  1.00 64.97  ? 56  ILE B N     1 
ATOM   4356 C  CA    . ILE B 1 29  ? 47.369  27.161  63.920  1.00 55.21  ? 56  ILE B CA    1 
ATOM   4357 C  C     . ILE B 1 29  ? 47.142  25.944  64.802  1.00 69.17  ? 56  ILE B C     1 
ATOM   4358 O  O     . ILE B 1 29  ? 47.973  25.627  65.661  1.00 69.14  ? 56  ILE B O     1 
ATOM   4359 C  CB    . ILE B 1 29  ? 48.737  27.109  63.233  1.00 56.61  ? 56  ILE B CB    1 
ATOM   4360 C  CG1   . ILE B 1 29  ? 48.935  28.357  62.367  1.00 57.43  ? 56  ILE B CG1   1 
ATOM   4361 C  CG2   . ILE B 1 29  ? 48.852  25.849  62.389  1.00 56.00  ? 56  ILE B CG2   1 
ATOM   4362 C  CD1   . ILE B 1 29  ? 50.216  28.343  61.559  1.00 50.58  ? 56  ILE B CD1   1 
ATOM   4363 N  N     . ALA B 1 30  ? 46.006  25.275  64.608  1.00 70.15  ? 57  ALA B N     1 
ATOM   4364 C  CA    . ALA B 1 30  ? 45.625  24.115  65.403  1.00 67.91  ? 57  ALA B CA    1 
ATOM   4365 C  C     . ALA B 1 30  ? 45.999  22.854  64.639  1.00 64.02  ? 57  ALA B C     1 
ATOM   4366 O  O     . ALA B 1 30  ? 45.570  22.668  63.495  1.00 63.75  ? 57  ALA B O     1 
ATOM   4367 C  CB    . ALA B 1 30  ? 44.129  24.130  65.719  1.00 62.14  ? 57  ALA B CB    1 
ATOM   4368 N  N     . LEU B 1 31  ? 46.786  21.988  65.275  1.00 66.97  ? 58  LEU B N     1 
ATOM   4369 C  CA    . LEU B 1 31  ? 47.334  20.798  64.633  1.00 70.48  ? 58  LEU B CA    1 
ATOM   4370 C  C     . LEU B 1 31  ? 47.001  19.569  65.468  1.00 65.48  ? 58  LEU B C     1 
ATOM   4371 O  O     . LEU B 1 31  ? 47.553  19.389  66.559  1.00 68.08  ? 58  LEU B O     1 
ATOM   4372 C  CB    . LEU B 1 31  ? 48.846  20.935  64.452  1.00 80.70  ? 58  LEU B CB    1 
ATOM   4373 C  CG    . LEU B 1 31  ? 49.593  19.683  63.993  1.00 88.09  ? 58  LEU B CG    1 
ATOM   4374 C  CD1   . LEU B 1 31  ? 49.134  19.253  62.607  1.00 81.04  ? 58  LEU B CD1   1 
ATOM   4375 C  CD2   . LEU B 1 31  ? 51.095  19.920  64.024  1.00 81.58  ? 58  LEU B CD2   1 
ATOM   4376 N  N     . LEU B 1 32  ? 46.104  18.727  64.961  1.00 72.25  ? 59  LEU B N     1 
ATOM   4377 C  CA    . LEU B 1 32  ? 45.848  17.414  65.545  1.00 63.94  ? 59  LEU B CA    1 
ATOM   4378 C  C     . LEU B 1 32  ? 46.708  16.380  64.830  1.00 69.93  ? 59  LEU B C     1 
ATOM   4379 O  O     . LEU B 1 32  ? 46.671  16.278  63.599  1.00 77.42  ? 59  LEU B O     1 
ATOM   4380 C  CB    . LEU B 1 32  ? 44.371  17.034  65.432  1.00 55.17  ? 59  LEU B CB    1 
ATOM   4381 C  CG    . LEU B 1 32  ? 43.310  17.720  66.303  1.00 69.83  ? 59  LEU B CG    1 
ATOM   4382 C  CD1   . LEU B 1 32  ? 43.164  19.198  66.008  1.00 54.40  ? 59  LEU B CD1   1 
ATOM   4383 C  CD2   . LEU B 1 32  ? 41.975  17.025  66.125  1.00 78.00  ? 59  LEU B CD2   1 
ATOM   4384 N  N     . ALA B 1 33  ? 47.481  15.614  65.596  1.00 65.86  ? 60  ALA B N     1 
ATOM   4385 C  CA    . ALA B 1 33  ? 48.437  14.672  65.026  1.00 73.65  ? 60  ALA B CA    1 
ATOM   4386 C  C     . ALA B 1 33  ? 48.247  13.293  65.644  1.00 77.90  ? 60  ALA B C     1 
ATOM   4387 O  O     . ALA B 1 33  ? 48.317  13.140  66.869  1.00 73.80  ? 60  ALA B O     1 
ATOM   4388 C  CB    . ALA B 1 33  ? 49.872  15.164  65.234  1.00 71.05  ? 60  ALA B CB    1 
ATOM   4389 N  N     . ARG B 1 34  ? 48.006  12.294  64.795  1.00 70.78  ? 61  ARG B N     1 
ATOM   4390 C  CA    . ARG B 1 34  ? 48.022  10.892  65.193  1.00 74.89  ? 61  ARG B CA    1 
ATOM   4391 C  C     . ARG B 1 34  ? 48.705  10.099  64.094  1.00 86.10  ? 61  ARG B C     1 
ATOM   4392 O  O     . ARG B 1 34  ? 48.290  10.176  62.933  1.00 89.14  ? 61  ARG B O     1 
ATOM   4393 C  CB    . ARG B 1 34  ? 46.613  10.333  65.428  1.00 69.76  ? 61  ARG B CB    1 
ATOM   4394 C  CG    . ARG B 1 34  ? 46.628  8.881   65.887  1.00 76.84  ? 61  ARG B CG    1 
ATOM   4395 C  CD    . ARG B 1 34  ? 45.258  8.219   65.852  1.00 67.08  ? 61  ARG B CD    1 
ATOM   4396 N  NE    . ARG B 1 34  ? 45.350  6.818   66.245  1.00 74.08  ? 61  ARG B NE    1 
ATOM   4397 C  CZ    . ARG B 1 34  ? 44.382  5.923   66.094  1.00 78.60  ? 61  ARG B CZ    1 
ATOM   4398 N  NH1   . ARG B 1 34  ? 43.209  6.252   65.583  1.00 82.01  ? 61  ARG B NH1   1 
ATOM   4399 N  NH2   . ARG B 1 34  ? 44.603  4.663   66.456  1.00 76.76  ? 61  ARG B NH2   1 
ATOM   4400 N  N     . ASN B 1 35  ? 49.743  9.343   64.462  1.00 87.20  ? 62  ASN B N     1 
ATOM   4401 C  CA    . ASN B 1 35  ? 50.482  8.503   63.520  1.00 72.16  ? 62  ASN B CA    1 
ATOM   4402 C  C     . ASN B 1 35  ? 50.940  9.312   62.309  1.00 72.60  ? 62  ASN B C     1 
ATOM   4403 O  O     . ASN B 1 35  ? 50.687  8.956   61.156  1.00 76.60  ? 62  ASN B O     1 
ATOM   4404 C  CB    . ASN B 1 35  ? 49.639  7.304   63.089  1.00 66.56  ? 62  ASN B CB    1 
ATOM   4405 C  CG    . ASN B 1 35  ? 49.402  6.330   64.215  1.00 82.14  ? 62  ASN B CG    1 
ATOM   4406 O  OD1   . ASN B 1 35  ? 50.323  5.991   64.960  1.00 90.45  ? 62  ASN B OD1   1 
ATOM   4407 N  ND2   . ASN B 1 35  ? 48.162  5.868   64.349  1.00 85.85  ? 62  ASN B ND2   1 
ATOM   4408 N  N     . ALA B 1 36  ? 51.615  10.427  62.585  1.00 81.67  ? 63  ALA B N     1 
ATOM   4409 C  CA    . ALA B 1 36  ? 51.977  11.390  61.553  1.00 72.98  ? 63  ALA B CA    1 
ATOM   4410 C  C     . ALA B 1 36  ? 53.479  11.568  61.398  1.00 76.88  ? 63  ALA B C     1 
ATOM   4411 O  O     . ALA B 1 36  ? 53.907  12.445  60.637  1.00 69.22  ? 63  ALA B O     1 
ATOM   4412 C  CB    . ALA B 1 36  ? 51.336  12.746  61.847  1.00 65.53  ? 63  ALA B CB    1 
ATOM   4413 N  N     . ALA B 1 37  ? 54.290  10.765  62.094  1.00 74.92  ? 64  ALA B N     1 
ATOM   4414 C  CA    . ALA B 1 37  ? 55.736  10.928  62.025  1.00 70.01  ? 64  ALA B CA    1 
ATOM   4415 C  C     . ALA B 1 37  ? 56.256  10.849  60.597  1.00 73.93  ? 64  ALA B C     1 
ATOM   4416 O  O     . ALA B 1 37  ? 57.297  11.440  60.292  1.00 84.41  ? 64  ALA B O     1 
ATOM   4417 C  CB    . ALA B 1 37  ? 56.425  9.879   62.897  1.00 70.04  ? 64  ALA B CB    1 
ATOM   4418 N  N     . HIS B 1 38  ? 55.544  10.151  59.710  1.00 76.49  ? 65  HIS B N     1 
ATOM   4419 C  CA    . HIS B 1 38  ? 55.968  10.085  58.318  1.00 71.24  ? 65  HIS B CA    1 
ATOM   4420 C  C     . HIS B 1 38  ? 55.868  11.449  57.642  1.00 87.24  ? 65  HIS B C     1 
ATOM   4421 O  O     . HIS B 1 38  ? 56.739  11.815  56.844  1.00 90.07  ? 65  HIS B O     1 
ATOM   4422 C  CB    . HIS B 1 38  ? 55.134  9.043   57.567  1.00 68.57  ? 65  HIS B CB    1 
ATOM   4423 C  CG    . HIS B 1 38  ? 53.670  9.359   57.513  1.00 72.78  ? 65  HIS B CG    1 
ATOM   4424 N  ND1   . HIS B 1 38  ? 52.805  9.061   58.544  1.00 81.38  ? 65  HIS B ND1   1 
ATOM   4425 C  CD2   . HIS B 1 38  ? 52.918  9.941   56.549  1.00 82.85  ? 65  HIS B CD2   1 
ATOM   4426 C  CE1   . HIS B 1 38  ? 51.584  9.450   58.220  1.00 72.66  ? 65  HIS B CE1   1 
ATOM   4427 N  NE2   . HIS B 1 38  ? 51.624  9.987   57.014  1.00 81.47  ? 65  HIS B NE2   1 
ATOM   4428 N  N     . ALA B 1 39  ? 54.829  12.222  57.960  1.00 78.73  ? 66  ALA B N     1 
ATOM   4429 C  CA    . ALA B 1 39  ? 54.549  13.469  57.258  1.00 72.15  ? 66  ALA B CA    1 
ATOM   4430 C  C     . ALA B 1 39  ? 55.103  14.706  57.951  1.00 77.54  ? 66  ALA B C     1 
ATOM   4431 O  O     . ALA B 1 39  ? 55.360  15.710  57.278  1.00 82.22  ? 66  ALA B O     1 
ATOM   4432 C  CB    . ALA B 1 39  ? 53.038  13.645  57.074  1.00 76.01  ? 66  ALA B CB    1 
ATOM   4433 N  N     . LEU B 1 40  ? 55.302  14.661  59.269  1.00 80.74  ? 67  LEU B N     1 
ATOM   4434 C  CA    . LEU B 1 40  ? 55.636  15.875  60.013  1.00 78.67  ? 67  LEU B CA    1 
ATOM   4435 C  C     . LEU B 1 40  ? 56.887  16.602  59.525  1.00 71.51  ? 67  LEU B C     1 
ATOM   4436 O  O     . LEU B 1 40  ? 56.846  17.843  59.460  1.00 80.32  ? 67  LEU B O     1 
ATOM   4437 C  CB    . LEU B 1 40  ? 55.753  15.549  61.507  1.00 70.63  ? 67  LEU B CB    1 
ATOM   4438 C  CG    . LEU B 1 40  ? 54.427  15.192  62.179  1.00 69.47  ? 67  LEU B CG    1 
ATOM   4439 C  CD1   . LEU B 1 40  ? 54.639  14.876  63.650  1.00 66.56  ? 67  LEU B CD1   1 
ATOM   4440 C  CD2   . LEU B 1 40  ? 53.425  16.323  61.998  1.00 65.48  ? 67  LEU B CD2   1 
ATOM   4441 N  N     . PRO B 1 41  ? 58.006  15.942  59.193  1.00 87.45  ? 68  PRO B N     1 
ATOM   4442 C  CA    . PRO B 1 41  ? 59.169  16.712  58.706  1.00 75.89  ? 68  PRO B CA    1 
ATOM   4443 C  C     . PRO B 1 41  ? 58.832  17.616  57.533  1.00 79.70  ? 68  PRO B C     1 
ATOM   4444 O  O     . PRO B 1 41  ? 59.180  18.802  57.537  1.00 87.60  ? 68  PRO B O     1 
ATOM   4445 C  CB    . PRO B 1 41  ? 60.172  15.618  58.314  1.00 71.11  ? 68  PRO B CB    1 
ATOM   4446 C  CG    . PRO B 1 41  ? 59.786  14.437  59.120  1.00 64.89  ? 68  PRO B CG    1 
ATOM   4447 C  CD    . PRO B 1 41  ? 58.298  14.495  59.256  1.00 73.32  ? 68  PRO B CD    1 
ATOM   4448 N  N     . THR B 1 42  ? 58.139  17.079  56.529  1.00 84.21  ? 69  THR B N     1 
ATOM   4449 C  CA    . THR B 1 42  ? 57.710  17.890  55.397  1.00 81.45  ? 69  THR B CA    1 
ATOM   4450 C  C     . THR B 1 42  ? 56.557  18.810  55.783  1.00 87.87  ? 69  THR B C     1 
ATOM   4451 O  O     . THR B 1 42  ? 56.524  19.981  55.386  1.00 81.08  ? 69  THR B O     1 
ATOM   4452 C  CB    . THR B 1 42  ? 57.301  16.978  54.240  1.00 82.22  ? 69  THR B CB    1 
ATOM   4453 O  OG1   . THR B 1 42  ? 58.315  15.987  54.036  1.00 92.73  ? 69  THR B OG1   1 
ATOM   4454 C  CG2   . THR B 1 42  ? 57.132  17.774  52.964  1.00 97.74  ? 69  THR B CG2   1 
ATOM   4455 N  N     . THR B 1 43  ? 55.608  18.297  56.565  1.00 85.45  ? 70  THR B N     1 
ATOM   4456 C  CA    . THR B 1 43  ? 54.425  19.074  56.912  1.00 71.98  ? 70  THR B CA    1 
ATOM   4457 C  C     . THR B 1 43  ? 54.768  20.247  57.826  1.00 79.03  ? 70  THR B C     1 
ATOM   4458 O  O     . THR B 1 43  ? 54.320  21.376  57.595  1.00 69.82  ? 70  THR B O     1 
ATOM   4459 C  CB    . THR B 1 43  ? 53.390  18.164  57.565  1.00 60.07  ? 70  THR B CB    1 
ATOM   4460 O  OG1   . THR B 1 43  ? 52.642  17.501  56.538  1.00 83.10  ? 70  THR B OG1   1 
ATOM   4461 C  CG2   . THR B 1 43  ? 52.450  18.961  58.445  1.00 84.79  ? 70  THR B CG2   1 
ATOM   4462 N  N     . LEU B 1 44  ? 55.552  19.998  58.876  1.00 87.68  ? 71  LEU B N     1 
ATOM   4463 C  CA    . LEU B 1 44  ? 55.860  21.069  59.818  1.00 73.99  ? 71  LEU B CA    1 
ATOM   4464 C  C     . LEU B 1 44  ? 56.831  22.079  59.228  1.00 73.57  ? 71  LEU B C     1 
ATOM   4465 O  O     . LEU B 1 44  ? 56.744  23.271  59.540  1.00 73.99  ? 71  LEU B O     1 
ATOM   4466 C  CB    . LEU B 1 44  ? 56.418  20.490  61.116  1.00 65.00  ? 71  LEU B CB    1 
ATOM   4467 C  CG    . LEU B 1 44  ? 55.397  19.702  61.932  1.00 76.48  ? 71  LEU B CG    1 
ATOM   4468 C  CD1   . LEU B 1 44  ? 55.943  19.376  63.313  1.00 76.83  ? 71  LEU B CD1   1 
ATOM   4469 C  CD2   . LEU B 1 44  ? 54.089  20.471  62.029  1.00 70.71  ? 71  LEU B CD2   1 
ATOM   4470 N  N     . GLY B 1 45  ? 57.760  21.629  58.385  1.00 73.65  ? 72  GLY B N     1 
ATOM   4471 C  CA    . GLY B 1 45  ? 58.631  22.569  57.702  1.00 78.24  ? 72  GLY B CA    1 
ATOM   4472 C  C     . GLY B 1 45  ? 57.854  23.561  56.859  1.00 78.26  ? 72  GLY B C     1 
ATOM   4473 O  O     . GLY B 1 45  ? 58.187  24.747  56.813  1.00 79.44  ? 72  GLY B O     1 
ATOM   4474 N  N     . ALA B 1 46  ? 56.796  23.090  56.194  1.00 74.68  ? 73  ALA B N     1 
ATOM   4475 C  CA    . ALA B 1 46  ? 55.948  23.990  55.423  1.00 64.78  ? 73  ALA B CA    1 
ATOM   4476 C  C     . ALA B 1 46  ? 55.281  25.026  56.322  1.00 70.83  ? 73  ALA B C     1 
ATOM   4477 O  O     . ALA B 1 46  ? 55.158  26.198  55.945  1.00 81.06  ? 73  ALA B O     1 
ATOM   4478 C  CB    . ALA B 1 46  ? 54.903  23.187  54.649  1.00 54.08  ? 73  ALA B CB    1 
ATOM   4479 N  N     . LEU B 1 47  ? 54.859  24.616  57.521  1.00 76.79  ? 74  LEU B N     1 
ATOM   4480 C  CA    . LEU B 1 47  ? 54.193  25.543  58.432  1.00 70.26  ? 74  LEU B CA    1 
ATOM   4481 C  C     . LEU B 1 47  ? 55.163  26.588  58.973  1.00 73.11  ? 74  LEU B C     1 
ATOM   4482 O  O     . LEU B 1 47  ? 54.794  27.761  59.112  1.00 73.62  ? 74  LEU B O     1 
ATOM   4483 C  CB    . LEU B 1 47  ? 53.534  24.774  59.578  1.00 69.89  ? 74  LEU B CB    1 
ATOM   4484 C  CG    . LEU B 1 47  ? 52.345  23.869  59.230  1.00 73.47  ? 74  LEU B CG    1 
ATOM   4485 C  CD1   . LEU B 1 47  ? 51.767  23.253  60.483  1.00 68.63  ? 74  LEU B CD1   1 
ATOM   4486 C  CD2   . LEU B 1 47  ? 51.264  24.625  58.479  1.00 60.20  ? 74  LEU B CD2   1 
ATOM   4487 N  N     . GLU B 1 48  ? 56.401  26.185  59.289  1.00 75.15  ? 75  GLU B N     1 
ATOM   4488 C  CA    . GLU B 1 48  ? 57.410  27.143  59.743  1.00 77.58  ? 75  GLU B CA    1 
ATOM   4489 C  C     . GLU B 1 48  ? 57.581  28.277  58.744  1.00 70.48  ? 75  GLU B C     1 
ATOM   4490 O  O     . GLU B 1 48  ? 57.670  29.451  59.117  1.00 82.18  ? 75  GLU B O     1 
ATOM   4491 C  CB    . GLU B 1 48  ? 58.762  26.459  59.940  1.00 73.67  ? 75  GLU B CB    1 
ATOM   4492 C  CG    . GLU B 1 48  ? 58.817  25.326  60.922  1.00 92.76  ? 75  GLU B CG    1 
ATOM   4493 C  CD    . GLU B 1 48  ? 60.143  24.591  60.834  1.00 102.46 ? 75  GLU B CD    1 
ATOM   4494 O  OE1   . GLU B 1 48  ? 60.873  24.800  59.837  1.00 86.79  ? 75  GLU B OE1   1 
ATOM   4495 O  OE2   . GLU B 1 48  ? 60.459  23.812  61.758  1.00 106.49 ? 75  GLU B OE2   1 
ATOM   4496 N  N     . ARG B 1 49  ? 57.652  27.933  57.464  1.00 74.24  ? 76  ARG B N     1 
ATOM   4497 C  CA    . ARG B 1 49  ? 57.993  28.875  56.416  1.00 68.77  ? 76  ARG B CA    1 
ATOM   4498 C  C     . ARG B 1 49  ? 56.777  29.594  55.848  1.00 80.03  ? 76  ARG B C     1 
ATOM   4499 O  O     . ARG B 1 49  ? 56.881  30.218  54.786  1.00 71.67  ? 76  ARG B O     1 
ATOM   4500 C  CB    . ARG B 1 49  ? 58.757  28.147  55.310  1.00 63.95  ? 76  ARG B CB    1 
ATOM   4501 C  CG    . ARG B 1 49  ? 59.993  27.425  55.830  1.00 72.81  ? 76  ARG B CG    1 
ATOM   4502 C  CD    . ARG B 1 49  ? 60.834  26.852  54.704  1.00 72.76  ? 76  ARG B CD    1 
ATOM   4503 N  NE    . ARG B 1 49  ? 60.230  25.663  54.118  1.00 73.23  ? 76  ARG B NE    1 
ATOM   4504 C  CZ    . ARG B 1 49  ? 60.469  24.425  54.532  1.00 84.09  ? 76  ARG B CZ    1 
ATOM   4505 N  NH1   . ARG B 1 49  ? 61.287  24.179  55.543  1.00 72.72  ? 76  ARG B NH1   1 
ATOM   4506 N  NH2   . ARG B 1 49  ? 59.872  23.409  53.916  1.00 90.71  ? 76  ARG B NH2   1 
ATOM   4507 N  N     . LEU B 1 50  ? 55.629  29.509  56.517  1.00 70.90  ? 77  LEU B N     1 
ATOM   4508 C  CA    . LEU B 1 50  ? 54.500  30.354  56.160  1.00 69.50  ? 77  LEU B CA    1 
ATOM   4509 C  C     . LEU B 1 50  ? 54.898  31.816  56.283  1.00 73.34  ? 77  LEU B C     1 
ATOM   4510 O  O     . LEU B 1 50  ? 55.518  32.221  57.272  1.00 76.02  ? 77  LEU B O     1 
ATOM   4511 C  CB    . LEU B 1 50  ? 53.309  30.061  57.067  1.00 66.38  ? 77  LEU B CB    1 
ATOM   4512 C  CG    . LEU B 1 50  ? 52.459  28.822  56.818  1.00 66.18  ? 77  LEU B CG    1 
ATOM   4513 C  CD1   . LEU B 1 50  ? 51.440  28.691  57.934  1.00 69.40  ? 77  LEU B CD1   1 
ATOM   4514 C  CD2   . LEU B 1 50  ? 51.768  28.919  55.471  1.00 54.21  ? 77  LEU B CD2   1 
ATOM   4515 N  N     . ARG B 1 51  ? 54.554  32.610  55.272  1.00 65.22  ? 78  ARG B N     1 
ATOM   4516 C  CA    . ARG B 1 51  ? 54.883  34.034  55.301  1.00 74.50  ? 78  ARG B CA    1 
ATOM   4517 C  C     . ARG B 1 51  ? 53.758  34.759  56.029  1.00 76.29  ? 78  ARG B C     1 
ATOM   4518 O  O     . ARG B 1 51  ? 52.897  35.416  55.437  1.00 65.83  ? 78  ARG B O     1 
ATOM   4519 C  CB    . ARG B 1 51  ? 55.126  34.575  53.898  1.00 75.96  ? 78  ARG B CB    1 
ATOM   4520 C  CG    . ARG B 1 51  ? 56.579  34.402  53.447  1.00 87.06  ? 78  ARG B CG    1 
ATOM   4521 C  CD    . ARG B 1 51  ? 56.860  35.095  52.131  1.00 70.94  ? 78  ARG B CD    1 
ATOM   4522 N  NE    . ARG B 1 51  ? 56.247  34.397  51.009  1.00 75.01  ? 78  ARG B NE    1 
ATOM   4523 C  CZ    . ARG B 1 51  ? 56.867  33.497  50.260  1.00 75.02  ? 78  ARG B CZ    1 
ATOM   4524 N  NH1   . ARG B 1 51  ? 58.131  33.173  50.475  1.00 81.45  ? 78  ARG B NH1   1 
ATOM   4525 N  NH2   . ARG B 1 51  ? 56.201  32.905  49.272  1.00 74.93  ? 78  ARG B NH2   1 
ATOM   4526 N  N     . HIS B 1 52  ? 53.774  34.610  57.357  1.00 67.00  ? 79  HIS B N     1 
ATOM   4527 C  CA    . HIS B 1 52  ? 52.897  35.297  58.280  1.00 62.36  ? 79  HIS B CA    1 
ATOM   4528 C  C     . HIS B 1 52  ? 53.737  35.487  59.534  1.00 71.27  ? 79  HIS B C     1 
ATOM   4529 O  O     . HIS B 1 52  ? 54.420  34.539  59.950  1.00 80.10  ? 79  HIS B O     1 
ATOM   4530 C  CB    . HIS B 1 52  ? 51.622  34.521  58.603  1.00 67.15  ? 79  HIS B CB    1 
ATOM   4531 C  CG    . HIS B 1 52  ? 50.661  35.273  59.467  1.00 66.87  ? 79  HIS B CG    1 
ATOM   4532 N  ND1   . HIS B 1 52  ? 49.873  36.296  58.987  1.00 75.91  ? 79  HIS B ND1   1 
ATOM   4533 C  CD2   . HIS B 1 52  ? 50.370  35.159  60.784  1.00 75.27  ? 79  HIS B CD2   1 
ATOM   4534 C  CE1   . HIS B 1 52  ? 49.132  36.776  59.970  1.00 73.91  ? 79  HIS B CE1   1 
ATOM   4535 N  NE2   . HIS B 1 52  ? 49.415  36.104  61.071  1.00 76.61  ? 79  HIS B NE2   1 
ATOM   4536 N  N     . PRO B 1 53  ? 53.726  36.676  60.130  1.00 71.34  ? 80  PRO B N     1 
ATOM   4537 C  CA    . PRO B 1 53  ? 54.601  36.942  61.280  1.00 72.10  ? 80  PRO B CA    1 
ATOM   4538 C  C     . PRO B 1 53  ? 54.374  35.948  62.411  1.00 80.20  ? 80  PRO B C     1 
ATOM   4539 O  O     . PRO B 1 53  ? 53.252  35.766  62.890  1.00 86.00  ? 80  PRO B O     1 
ATOM   4540 C  CB    . PRO B 1 53  ? 54.215  38.369  61.688  1.00 64.21  ? 80  PRO B CB    1 
ATOM   4541 C  CG    . PRO B 1 53  ? 53.706  38.986  60.427  1.00 55.94  ? 80  PRO B CG    1 
ATOM   4542 C  CD    . PRO B 1 53  ? 53.003  37.882  59.692  1.00 66.65  ? 80  PRO B CD    1 
ATOM   4543 N  N     . ARG B 1 54  ? 55.460  35.306  62.839  1.00 72.21  ? 81  ARG B N     1 
ATOM   4544 C  CA    . ARG B 1 54  ? 55.346  34.276  63.864  1.00 73.76  ? 81  ARG B CA    1 
ATOM   4545 C  C     . ARG B 1 54  ? 54.924  34.854  65.209  1.00 71.67  ? 81  ARG B C     1 
ATOM   4546 O  O     . ARG B 1 54  ? 54.324  34.145  66.024  1.00 77.46  ? 81  ARG B O     1 
ATOM   4547 C  CB    . ARG B 1 54  ? 56.668  33.524  63.992  1.00 78.88  ? 81  ARG B CB    1 
ATOM   4548 C  CG    . ARG B 1 54  ? 56.965  32.602  62.825  1.00 69.02  ? 81  ARG B CG    1 
ATOM   4549 C  CD    . ARG B 1 54  ? 58.435  32.225  62.788  1.00 93.40  ? 81  ARG B CD    1 
ATOM   4550 N  NE    . ARG B 1 54  ? 58.689  31.101  61.893  1.00 100.39 ? 81  ARG B NE    1 
ATOM   4551 C  CZ    . ARG B 1 54  ? 59.889  30.758  61.443  1.00 111.13 ? 81  ARG B CZ    1 
ATOM   4552 N  NH1   . ARG B 1 54  ? 60.971  31.455  61.755  1.00 103.31 ? 81  ARG B NH1   1 
ATOM   4553 N  NH2   . ARG B 1 54  ? 60.006  29.690  60.658  1.00 108.02 ? 81  ARG B NH2   1 
ATOM   4554 N  N     . GLU B 1 55  ? 55.225  36.126  65.470  1.00 77.34  ? 82  GLU B N     1 
ATOM   4555 C  CA    . GLU B 1 55  ? 54.763  36.726  66.714  1.00 71.69  ? 82  GLU B CA    1 
ATOM   4556 C  C     . GLU B 1 55  ? 53.265  36.991  66.686  1.00 73.47  ? 82  GLU B C     1 
ATOM   4557 O  O     . GLU B 1 55  ? 52.648  37.102  67.750  1.00 80.97  ? 82  GLU B O     1 
ATOM   4558 C  CB    . GLU B 1 55  ? 55.528  38.020  67.013  1.00 72.95  ? 82  GLU B CB    1 
ATOM   4559 C  CG    . GLU B 1 55  ? 55.092  39.233  66.207  1.00 69.65  ? 82  GLU B CG    1 
ATOM   4560 C  CD    . GLU B 1 55  ? 55.817  39.357  64.880  1.00 95.62  ? 82  GLU B CD    1 
ATOM   4561 O  OE1   . GLU B 1 55  ? 56.445  38.365  64.443  1.00 99.85  ? 82  GLU B OE1   1 
ATOM   4562 O  OE2   . GLU B 1 55  ? 55.764  40.453  64.278  1.00 88.04  ? 82  GLU B OE2   1 
ATOM   4563 N  N     . ARG B 1 56  ? 52.672  37.096  65.496  1.00 73.10  ? 83  ARG B N     1 
ATOM   4564 C  CA    . ARG B 1 56  ? 51.227  37.136  65.335  1.00 64.12  ? 83  ARG B CA    1 
ATOM   4565 C  C     . ARG B 1 56  ? 50.643  35.755  65.077  1.00 72.45  ? 83  ARG B C     1 
ATOM   4566 O  O     . ARG B 1 56  ? 49.498  35.647  64.625  1.00 75.63  ? 83  ARG B O     1 
ATOM   4567 C  CB    . ARG B 1 56  ? 50.848  38.078  64.194  1.00 67.06  ? 83  ARG B CB    1 
ATOM   4568 C  CG    . ARG B 1 56  ? 51.576  39.394  64.236  1.00 75.62  ? 83  ARG B CG    1 
ATOM   4569 C  CD    . ARG B 1 56  ? 51.158  40.219  65.428  1.00 64.45  ? 83  ARG B CD    1 
ATOM   4570 N  NE    . ARG B 1 56  ? 49.809  40.749  65.282  1.00 63.12  ? 83  ARG B NE    1 
ATOM   4571 C  CZ    . ARG B 1 56  ? 49.216  41.529  66.177  1.00 75.26  ? 83  ARG B CZ    1 
ATOM   4572 N  NH1   . ARG B 1 56  ? 49.831  41.897  67.289  1.00 53.91  ? 83  ARG B NH1   1 
ATOM   4573 N  NH2   . ARG B 1 56  ? 47.975  41.952  65.948  1.00 77.49  ? 83  ARG B NH2   1 
ATOM   4574 N  N     . THR B 1 57  ? 51.413  34.704  65.334  1.00 72.37  ? 84  THR B N     1 
ATOM   4575 C  CA    . THR B 1 57  ? 50.965  33.332  65.172  1.00 63.83  ? 84  THR B CA    1 
ATOM   4576 C  C     . THR B 1 57  ? 51.106  32.600  66.498  1.00 62.24  ? 84  THR B C     1 
ATOM   4577 O  O     . THR B 1 57  ? 52.072  32.814  67.236  1.00 61.88  ? 84  THR B O     1 
ATOM   4578 C  CB    . THR B 1 57  ? 51.774  32.616  64.093  1.00 72.36  ? 84  THR B CB    1 
ATOM   4579 O  OG1   . THR B 1 57  ? 51.799  33.421  62.908  1.00 76.35  ? 84  THR B OG1   1 
ATOM   4580 C  CG2   . THR B 1 57  ? 51.160  31.256  63.771  1.00 73.04  ? 84  THR B CG2   1 
ATOM   4581 N  N     . ALA B 1 58  ? 50.133  31.753  66.807  1.00 66.20  ? 85  ALA B N     1 
ATOM   4582 C  CA    . ALA B 1 58  ? 50.204  30.883  67.968  1.00 73.17  ? 85  ALA B CA    1 
ATOM   4583 C  C     . ALA B 1 58  ? 50.029  29.441  67.519  1.00 74.69  ? 85  ALA B C     1 
ATOM   4584 O  O     . ALA B 1 58  ? 49.482  29.163  66.448  1.00 69.16  ? 85  ALA B O     1 
ATOM   4585 C  CB    . ALA B 1 58  ? 49.148  31.247  69.019  1.00 61.98  ? 85  ALA B CB    1 
ATOM   4586 N  N     . LEU B 1 59  ? 50.511  28.525  68.351  1.00 73.13  ? 86  LEU B N     1 
ATOM   4587 C  CA    . LEU B 1 59  ? 50.506  27.104  68.042  1.00 61.34  ? 86  LEU B CA    1 
ATOM   4588 C  C     . LEU B 1 59  ? 49.653  26.362  69.053  1.00 70.03  ? 86  LEU B C     1 
ATOM   4589 O  O     . LEU B 1 59  ? 49.766  26.596  70.261  1.00 82.88  ? 86  LEU B O     1 
ATOM   4590 C  CB    . LEU B 1 59  ? 51.925  26.541  68.038  1.00 64.72  ? 86  LEU B CB    1 
ATOM   4591 C  CG    . LEU B 1 59  ? 52.768  27.017  66.861  1.00 75.15  ? 86  LEU B CG    1 
ATOM   4592 C  CD1   . LEU B 1 59  ? 54.210  26.561  67.020  1.00 72.48  ? 86  LEU B CD1   1 
ATOM   4593 C  CD2   . LEU B 1 59  ? 52.160  26.504  65.570  1.00 58.49  ? 86  LEU B CD2   1 
ATOM   4594 N  N     . TRP B 1 60  ? 48.804  25.471  68.553  1.00 67.60  ? 87  TRP B N     1 
ATOM   4595 C  CA    . TRP B 1 60  ? 47.992  24.588  69.379  1.00 73.25  ? 87  TRP B CA    1 
ATOM   4596 C  C     . TRP B 1 60  ? 48.146  23.181  68.822  1.00 73.38  ? 87  TRP B C     1 
ATOM   4597 O  O     . TRP B 1 60  ? 47.784  22.927  67.669  1.00 76.72  ? 87  TRP B O     1 
ATOM   4598 C  CB    . TRP B 1 60  ? 46.529  25.036  69.374  1.00 66.13  ? 87  TRP B CB    1 
ATOM   4599 C  CG    . TRP B 1 60  ? 45.644  24.318  70.345  1.00 68.87  ? 87  TRP B CG    1 
ATOM   4600 C  CD1   . TRP B 1 60  ? 45.219  24.778  71.558  1.00 69.25  ? 87  TRP B CD1   1 
ATOM   4601 C  CD2   . TRP B 1 60  ? 45.055  23.022  70.178  1.00 72.93  ? 87  TRP B CD2   1 
ATOM   4602 N  NE1   . TRP B 1 60  ? 44.406  23.848  72.159  1.00 66.66  ? 87  TRP B NE1   1 
ATOM   4603 C  CE2   . TRP B 1 60  ? 44.289  22.761  71.332  1.00 69.53  ? 87  TRP B CE2   1 
ATOM   4604 C  CE3   . TRP B 1 60  ? 45.101  22.057  69.165  1.00 74.30  ? 87  TRP B CE3   1 
ATOM   4605 C  CZ2   . TRP B 1 60  ? 43.580  21.574  71.504  1.00 65.33  ? 87  TRP B CZ2   1 
ATOM   4606 C  CZ3   . TRP B 1 60  ? 44.394  20.881  69.336  1.00 73.73  ? 87  TRP B CZ3   1 
ATOM   4607 C  CH2   . TRP B 1 60  ? 43.646  20.648  70.499  1.00 66.08  ? 87  TRP B CH2   1 
ATOM   4608 N  N     . VAL B 1 61  ? 48.694  22.277  69.630  1.00 74.44  ? 88  VAL B N     1 
ATOM   4609 C  CA    . VAL B 1 61  ? 49.069  20.941  69.182  1.00 71.83  ? 88  VAL B CA    1 
ATOM   4610 C  C     . VAL B 1 61  ? 48.498  19.914  70.147  1.00 73.20  ? 88  VAL B C     1 
ATOM   4611 O  O     . VAL B 1 61  ? 48.643  20.053  71.367  1.00 79.29  ? 88  VAL B O     1 
ATOM   4612 C  CB    . VAL B 1 61  ? 50.597  20.782  69.088  1.00 66.91  ? 88  VAL B CB    1 
ATOM   4613 C  CG1   . VAL B 1 61  ? 50.955  19.350  68.736  1.00 67.62  ? 88  VAL B CG1   1 
ATOM   4614 C  CG2   . VAL B 1 61  ? 51.171  21.750  68.074  1.00 65.78  ? 88  VAL B CG2   1 
ATOM   4615 N  N     . ALA B 1 62  ? 47.867  18.878  69.602  1.00 63.83  ? 89  ALA B N     1 
ATOM   4616 C  CA    . ALA B 1 62  ? 47.345  17.780  70.402  1.00 72.16  ? 89  ALA B CA    1 
ATOM   4617 C  C     . ALA B 1 62  ? 47.659  16.474  69.693  1.00 74.94  ? 89  ALA B C     1 
ATOM   4618 O  O     . ALA B 1 62  ? 47.396  16.340  68.494  1.00 75.32  ? 89  ALA B O     1 
ATOM   4619 C  CB    . ALA B 1 62  ? 45.836  17.915  70.625  1.00 69.32  ? 89  ALA B CB    1 
ATOM   4620 N  N     . THR B 1 63  ? 48.223  15.519  70.431  1.00 72.81  ? 90  THR B N     1 
ATOM   4621 C  CA    . THR B 1 63  ? 48.580  14.224  69.871  1.00 78.05  ? 90  THR B CA    1 
ATOM   4622 C  C     . THR B 1 63  ? 48.273  13.133  70.888  1.00 77.10  ? 90  THR B C     1 
ATOM   4623 O  O     . THR B 1 63  ? 48.405  13.335  72.099  1.00 77.81  ? 90  THR B O     1 
ATOM   4624 C  CB    . THR B 1 63  ? 50.062  14.181  69.452  1.00 77.34  ? 90  THR B CB    1 
ATOM   4625 O  OG1   . THR B 1 63  ? 50.357  12.922  68.833  1.00 79.70  ? 90  THR B OG1   1 
ATOM   4626 C  CG2   . THR B 1 63  ? 50.975  14.388  70.652  1.00 69.40  ? 90  THR B CG2   1 
ATOM   4627 N  N     . ASP B 1 64  ? 47.852  11.975  70.382  1.00 77.25  ? 91  ASP B N     1 
ATOM   4628 C  CA    . ASP B 1 64  ? 47.445  10.854  71.221  1.00 69.57  ? 91  ASP B CA    1 
ATOM   4629 C  C     . ASP B 1 64  ? 47.190  9.648   70.329  1.00 74.67  ? 91  ASP B C     1 
ATOM   4630 O  O     . ASP B 1 64  ? 47.068  9.774   69.107  1.00 72.69  ? 91  ASP B O     1 
ATOM   4631 C  CB    . ASP B 1 64  ? 46.196  11.183  72.043  1.00 77.01  ? 91  ASP B CB    1 
ATOM   4632 C  CG    . ASP B 1 64  ? 45.104  11.829  71.208  1.00 81.76  ? 91  ASP B CG    1 
ATOM   4633 O  OD1   . ASP B 1 64  ? 44.407  11.088  70.475  1.00 76.57  ? 91  ASP B OD1   1 
ATOM   4634 O  OD2   . ASP B 1 64  ? 44.957  13.075  71.276  1.00 70.56  ? 91  ASP B OD2   1 
ATOM   4635 N  N     . HIS B 1 65  ? 47.100  8.476   70.964  1.00 82.46  ? 92  HIS B N     1 
ATOM   4636 C  CA    . HIS B 1 65  ? 46.862  7.210   70.266  1.00 85.06  ? 92  HIS B CA    1 
ATOM   4637 C  C     . HIS B 1 65  ? 47.909  6.980   69.178  1.00 86.65  ? 92  HIS B C     1 
ATOM   4638 O  O     . HIS B 1 65  ? 47.587  6.712   68.019  1.00 89.86  ? 92  HIS B O     1 
ATOM   4639 C  CB    . HIS B 1 65  ? 45.447  7.155   69.679  1.00 78.45  ? 92  HIS B CB    1 
ATOM   4640 C  CG    . HIS B 1 65  ? 44.361  7.300   70.699  1.00 76.61  ? 92  HIS B CG    1 
ATOM   4641 N  ND1   . HIS B 1 65  ? 43.898  8.525   71.128  1.00 73.88  ? 92  HIS B ND1   1 
ATOM   4642 C  CD2   . HIS B 1 65  ? 43.647  6.371   71.378  1.00 82.77  ? 92  HIS B CD2   1 
ATOM   4643 C  CE1   . HIS B 1 65  ? 42.947  8.345   72.026  1.00 77.70  ? 92  HIS B CE1   1 
ATOM   4644 N  NE2   . HIS B 1 65  ? 42.774  7.046   72.195  1.00 74.40  ? 92  HIS B NE2   1 
ATOM   4645 N  N     . ASN B 1 66  ? 49.177  7.083   69.561  1.00 87.32  ? 93  ASN B N     1 
ATOM   4646 C  CA    . ASN B 1 66  ? 50.278  7.009   68.612  1.00 83.68  ? 93  ASN B CA    1 
ATOM   4647 C  C     . ASN B 1 66  ? 50.926  5.635   68.656  1.00 92.31  ? 93  ASN B C     1 
ATOM   4648 O  O     . ASN B 1 66  ? 51.253  5.127   69.733  1.00 87.86  ? 93  ASN B O     1 
ATOM   4649 C  CB    . ASN B 1 66  ? 51.322  8.085   68.900  1.00 87.76  ? 93  ASN B CB    1 
ATOM   4650 C  CG    . ASN B 1 66  ? 50.820  9.470   68.591  1.00 82.41  ? 93  ASN B CG    1 
ATOM   4651 O  OD1   . ASN B 1 66  ? 50.585  9.807   67.432  1.00 86.60  ? 93  ASN B OD1   1 
ATOM   4652 N  ND2   . ASN B 1 66  ? 50.650  10.286  69.626  1.00 83.75  ? 93  ASN B ND2   1 
ATOM   4653 N  N     . MET B 1 67  ? 51.106  5.042   67.479  1.00 94.97  ? 94  MET B N     1 
ATOM   4654 C  CA    . MET B 1 67  ? 51.916  3.844   67.324  1.00 92.67  ? 94  MET B CA    1 
ATOM   4655 C  C     . MET B 1 67  ? 53.337  4.153   66.880  1.00 88.66  ? 94  MET B C     1 
ATOM   4656 O  O     . MET B 1 67  ? 54.255  3.395   67.209  1.00 91.66  ? 94  MET B O     1 
ATOM   4657 C  CB    . MET B 1 67  ? 51.262  2.889   66.321  1.00 80.30  ? 94  MET B CB    1 
ATOM   4658 C  CG    . MET B 1 67  ? 50.108  2.091   66.900  1.00 87.15  ? 94  MET B CG    1 
ATOM   4659 S  SD    . MET B 1 67  ? 50.667  0.787   68.019  1.00 104.16 ? 94  MET B SD    1 
ATOM   4660 C  CE    . MET B 1 67  ? 49.098  0.116   68.565  1.00 105.32 ? 94  MET B CE    1 
ATOM   4661 N  N     . ASP B 1 68  ? 53.541  5.246   66.146  1.00 82.87  ? 95  ASP B N     1 
ATOM   4662 C  CA    . ASP B 1 68  ? 54.876  5.710   65.810  1.00 92.67  ? 95  ASP B CA    1 
ATOM   4663 C  C     . ASP B 1 68  ? 55.317  6.766   66.822  1.00 89.60  ? 95  ASP B C     1 
ATOM   4664 O  O     . ASP B 1 68  ? 54.593  7.102   67.764  1.00 93.11  ? 95  ASP B O     1 
ATOM   4665 C  CB    . ASP B 1 68  ? 54.916  6.250   64.380  1.00 71.33  ? 95  ASP B CB    1 
ATOM   4666 C  CG    . ASP B 1 68  ? 53.945  7.392   64.158  1.00 85.33  ? 95  ASP B CG    1 
ATOM   4667 O  OD1   . ASP B 1 68  ? 53.251  7.787   65.118  1.00 85.62  ? 95  ASP B OD1   1 
ATOM   4668 O  OD2   . ASP B 1 68  ? 53.874  7.898   63.016  1.00 88.91  ? 95  ASP B OD2   1 
ATOM   4669 N  N     . ASN B 1 69  ? 56.516  7.305   66.630  1.00 84.32  ? 96  ASN B N     1 
ATOM   4670 C  CA    . ASN B 1 69  ? 57.038  8.321   67.543  1.00 91.50  ? 96  ASN B CA    1 
ATOM   4671 C  C     . ASN B 1 69  ? 56.598  9.721   67.123  1.00 88.60  ? 96  ASN B C     1 
ATOM   4672 O  O     . ASN B 1 69  ? 57.397  10.649  67.012  1.00 89.34  ? 96  ASN B O     1 
ATOM   4673 C  CB    . ASN B 1 69  ? 58.556  8.215   67.628  1.00 84.54  ? 96  ASN B CB    1 
ATOM   4674 C  CG    . ASN B 1 69  ? 59.234  8.470   66.301  1.00 89.75  ? 96  ASN B CG    1 
ATOM   4675 O  OD1   . ASN B 1 69  ? 58.584  8.501   65.254  1.00 86.70  ? 96  ASN B OD1   1 
ATOM   4676 N  ND2   . ASN B 1 69  ? 60.547  8.658   66.335  1.00 97.90  ? 96  ASN B ND2   1 
ATOM   4677 N  N     . THR B 1 70  ? 55.293  9.873   66.889  1.00 89.14  ? 97  THR B N     1 
ATOM   4678 C  CA    . THR B 1 70  ? 54.757  11.163  66.467  1.00 79.13  ? 97  THR B CA    1 
ATOM   4679 C  C     . THR B 1 70  ? 54.964  12.222  67.544  1.00 76.21  ? 97  THR B C     1 
ATOM   4680 O  O     . THR B 1 70  ? 55.410  13.338  67.255  1.00 81.78  ? 97  THR B O     1 
ATOM   4681 C  CB    . THR B 1 70  ? 53.272  11.026  66.121  1.00 83.78  ? 97  THR B CB    1 
ATOM   4682 O  OG1   . THR B 1 70  ? 53.115  10.145  65.001  1.00 79.72  ? 97  THR B OG1   1 
ATOM   4683 C  CG2   . THR B 1 70  ? 52.667  12.380  65.780  1.00 72.25  ? 97  THR B CG2   1 
ATOM   4684 N  N     . SER B 1 71  ? 54.653  11.886  68.800  1.00 72.70  ? 98  SER B N     1 
ATOM   4685 C  CA    . SER B 1 71  ? 54.769  12.873  69.872  1.00 80.99  ? 98  SER B CA    1 
ATOM   4686 C  C     . SER B 1 71  ? 56.220  13.264  70.123  1.00 83.39  ? 98  SER B C     1 
ATOM   4687 O  O     . SER B 1 71  ? 56.492  14.393  70.546  1.00 87.16  ? 98  SER B O     1 
ATOM   4688 C  CB    . SER B 1 71  ? 54.135  12.345  71.159  1.00 78.28  ? 98  SER B CB    1 
ATOM   4689 O  OG    . SER B 1 71  ? 55.104  11.750  72.004  1.00 94.46  ? 98  SER B OG    1 
ATOM   4690 N  N     . THR B 1 72  ? 57.161  12.352  69.874  1.00 82.34  ? 99  THR B N     1 
ATOM   4691 C  CA    . THR B 1 72  ? 58.569  12.697  70.027  1.00 77.10  ? 99  THR B CA    1 
ATOM   4692 C  C     . THR B 1 72  ? 58.999  13.704  68.969  1.00 80.29  ? 99  THR B C     1 
ATOM   4693 O  O     . THR B 1 72  ? 59.683  14.687  69.281  1.00 83.47  ? 99  THR B O     1 
ATOM   4694 C  CB    . THR B 1 72  ? 59.431  11.440  69.948  1.00 88.76  ? 99  THR B CB    1 
ATOM   4695 O  OG1   . THR B 1 72  ? 58.765  10.362  70.620  1.00 88.79  ? 99  THR B OG1   1 
ATOM   4696 C  CG2   . THR B 1 72  ? 60.777  11.685  70.608  1.00 78.56  ? 99  THR B CG2   1 
ATOM   4697 N  N     . VAL B 1 73  ? 58.597  13.480  67.715  1.00 77.89  ? 100 VAL B N     1 
ATOM   4698 C  CA    . VAL B 1 73  ? 58.915  14.423  66.644  1.00 73.57  ? 100 VAL B CA    1 
ATOM   4699 C  C     . VAL B 1 73  ? 58.302  15.787  66.937  1.00 79.60  ? 100 VAL B C     1 
ATOM   4700 O  O     . VAL B 1 73  ? 58.959  16.826  66.798  1.00 85.87  ? 100 VAL B O     1 
ATOM   4701 C  CB    . VAL B 1 73  ? 58.441  13.871  65.288  1.00 70.08  ? 100 VAL B CB    1 
ATOM   4702 C  CG1   . VAL B 1 73  ? 58.720  14.869  64.183  1.00 80.80  ? 100 VAL B CG1   1 
ATOM   4703 C  CG2   . VAL B 1 73  ? 59.109  12.540  64.991  1.00 69.22  ? 100 VAL B CG2   1 
ATOM   4704 N  N     . LEU B 1 74  ? 57.030  15.800  67.349  1.00 77.53  ? 101 LEU B N     1 
ATOM   4705 C  CA    . LEU B 1 74  ? 56.367  17.058  67.679  1.00 81.92  ? 101 LEU B CA    1 
ATOM   4706 C  C     . LEU B 1 74  ? 57.056  17.760  68.841  1.00 86.12  ? 101 LEU B C     1 
ATOM   4707 O  O     . LEU B 1 74  ? 57.272  18.977  68.800  1.00 82.58  ? 101 LEU B O     1 
ATOM   4708 C  CB    . LEU B 1 74  ? 54.896  16.809  68.015  1.00 77.20  ? 101 LEU B CB    1 
ATOM   4709 C  CG    . LEU B 1 74  ? 53.918  16.591  66.864  1.00 74.22  ? 101 LEU B CG    1 
ATOM   4710 C  CD1   . LEU B 1 74  ? 52.529  16.356  67.410  1.00 80.78  ? 101 LEU B CD1   1 
ATOM   4711 C  CD2   . LEU B 1 74  ? 53.925  17.782  65.927  1.00 73.67  ? 101 LEU B CD2   1 
ATOM   4712 N  N     . ARG B 1 75  ? 57.404  17.009  69.889  1.00 80.82  ? 102 ARG B N     1 
ATOM   4713 C  CA    . ARG B 1 75  ? 58.023  17.618  71.061  1.00 85.01  ? 102 ARG B CA    1 
ATOM   4714 C  C     . ARG B 1 75  ? 59.335  18.303  70.697  1.00 88.35  ? 102 ARG B C     1 
ATOM   4715 O  O     . ARG B 1 75  ? 59.589  19.437  71.118  1.00 86.34  ? 102 ARG B O     1 
ATOM   4716 C  CB    . ARG B 1 75  ? 58.241  16.561  72.145  1.00 79.59  ? 102 ARG B CB    1 
ATOM   4717 C  CG    . ARG B 1 75  ? 58.425  17.129  73.538  1.00 86.66  ? 102 ARG B CG    1 
ATOM   4718 C  CD    . ARG B 1 75  ? 58.330  16.048  74.608  1.00 106.74 ? 102 ARG B CD    1 
ATOM   4719 N  NE    . ARG B 1 75  ? 57.006  15.436  74.678  1.00 120.86 ? 102 ARG B NE    1 
ATOM   4720 C  CZ    . ARG B 1 75  ? 56.718  14.215  74.245  1.00 122.16 ? 102 ARG B CZ    1 
ATOM   4721 N  NH1   . ARG B 1 75  ? 57.639  13.441  73.691  1.00 109.14 ? 102 ARG B NH1   1 
ATOM   4722 N  NH2   . ARG B 1 75  ? 55.476  13.756  74.376  1.00 116.75 ? 102 ARG B NH2   1 
ATOM   4723 N  N     . GLU B 1 76  ? 60.171  17.638  69.893  1.00 84.11  ? 103 GLU B N     1 
ATOM   4724 C  CA    . GLU B 1 76  ? 61.425  18.248  69.461  1.00 83.13  ? 103 GLU B CA    1 
ATOM   4725 C  C     . GLU B 1 76  ? 61.179  19.496  68.625  1.00 91.02  ? 103 GLU B C     1 
ATOM   4726 O  O     . GLU B 1 76  ? 61.853  20.517  68.804  1.00 88.92  ? 103 GLU B O     1 
ATOM   4727 C  CB    . GLU B 1 76  ? 62.254  17.247  68.662  1.00 82.95  ? 103 GLU B CB    1 
ATOM   4728 C  CG    . GLU B 1 76  ? 62.947  16.193  69.495  1.00 111.42 ? 103 GLU B CG    1 
ATOM   4729 C  CD    . GLU B 1 76  ? 63.968  15.419  68.688  1.00 118.89 ? 103 GLU B CD    1 
ATOM   4730 O  OE1   . GLU B 1 76  ? 64.486  15.977  67.692  1.00 92.52  ? 103 GLU B OE1   1 
ATOM   4731 O  OE2   . GLU B 1 76  ? 64.244  14.253  69.046  1.00 120.35 ? 103 GLU B OE2   1 
ATOM   4732 N  N     . TRP B 1 77  ? 60.228  19.426  67.694  1.00 80.65  ? 104 TRP B N     1 
ATOM   4733 C  CA    . TRP B 1 77  ? 59.964  20.565  66.825  1.00 85.21  ? 104 TRP B CA    1 
ATOM   4734 C  C     . TRP B 1 77  ? 59.413  21.746  67.613  1.00 83.80  ? 104 TRP B C     1 
ATOM   4735 O  O     . TRP B 1 77  ? 59.796  22.895  67.367  1.00 85.72  ? 104 TRP B O     1 
ATOM   4736 C  CB    . TRP B 1 77  ? 58.997  20.160  65.715  1.00 91.36  ? 104 TRP B CB    1 
ATOM   4737 C  CG    . TRP B 1 77  ? 58.651  21.271  64.780  1.00 79.38  ? 104 TRP B CG    1 
ATOM   4738 C  CD1   . TRP B 1 77  ? 59.396  21.717  63.732  1.00 83.68  ? 104 TRP B CD1   1 
ATOM   4739 C  CD2   . TRP B 1 77  ? 57.464  22.073  64.802  1.00 84.21  ? 104 TRP B CD2   1 
ATOM   4740 N  NE1   . TRP B 1 77  ? 58.749  22.752  63.099  1.00 89.66  ? 104 TRP B NE1   1 
ATOM   4741 C  CE2   . TRP B 1 77  ? 57.561  22.989  63.738  1.00 77.90  ? 104 TRP B CE2   1 
ATOM   4742 C  CE3   . TRP B 1 77  ? 56.329  22.104  65.618  1.00 80.55  ? 104 TRP B CE3   1 
ATOM   4743 C  CZ2   . TRP B 1 77  ? 56.569  23.927  63.469  1.00 78.79  ? 104 TRP B CZ2   1 
ATOM   4744 C  CZ3   . TRP B 1 77  ? 55.343  23.034  65.347  1.00 78.87  ? 104 TRP B CZ3   1 
ATOM   4745 C  CH2   . TRP B 1 77  ? 55.470  23.933  64.283  1.00 78.86  ? 104 TRP B CH2   1 
ATOM   4746 N  N     . LEU B 1 78  ? 58.517  21.483  68.565  1.00 83.19  ? 105 LEU B N     1 
ATOM   4747 C  CA    . LEU B 1 78  ? 57.955  22.563  69.370  1.00 84.72  ? 105 LEU B CA    1 
ATOM   4748 C  C     . LEU B 1 78  ? 59.033  23.253  70.191  1.00 86.32  ? 105 LEU B C     1 
ATOM   4749 O  O     . LEU B 1 78  ? 59.091  24.486  70.246  1.00 89.04  ? 105 LEU B O     1 
ATOM   4750 C  CB    . LEU B 1 78  ? 56.851  22.023  70.278  1.00 80.18  ? 105 LEU B CB    1 
ATOM   4751 C  CG    . LEU B 1 78  ? 55.515  21.767  69.586  1.00 75.67  ? 105 LEU B CG    1 
ATOM   4752 C  CD1   . LEU B 1 78  ? 54.515  21.236  70.581  1.00 78.10  ? 105 LEU B CD1   1 
ATOM   4753 C  CD2   . LEU B 1 78  ? 55.009  23.041  68.939  1.00 62.76  ? 105 LEU B CD2   1 
ATOM   4754 N  N     . VAL B 1 79  ? 59.895  22.470  70.845  1.00 89.45  ? 106 VAL B N     1 
ATOM   4755 C  CA    . VAL B 1 79  ? 60.996  23.047  71.610  1.00 89.59  ? 106 VAL B CA    1 
ATOM   4756 C  C     . VAL B 1 79  ? 61.845  23.945  70.722  1.00 81.47  ? 106 VAL B C     1 
ATOM   4757 O  O     . VAL B 1 79  ? 62.293  25.018  71.144  1.00 91.06  ? 106 VAL B O     1 
ATOM   4758 C  CB    . VAL B 1 79  ? 61.838  21.930  72.256  1.00 79.64  ? 106 VAL B CB    1 
ATOM   4759 C  CG1   . VAL B 1 79  ? 63.144  22.494  72.801  1.00 66.99  ? 106 VAL B CG1   1 
ATOM   4760 C  CG2   . VAL B 1 79  ? 61.050  21.243  73.356  1.00 75.98  ? 106 VAL B CG2   1 
ATOM   4761 N  N     . ALA B 1 80  ? 62.052  23.537  69.470  1.00 76.42  ? 107 ALA B N     1 
ATOM   4762 C  CA    . ALA B 1 80  ? 62.920  24.299  68.581  1.00 83.06  ? 107 ALA B CA    1 
ATOM   4763 C  C     . ALA B 1 80  ? 62.278  25.604  68.127  1.00 78.89  ? 107 ALA B C     1 
ATOM   4764 O  O     . ALA B 1 80  ? 62.993  26.569  67.840  1.00 87.94  ? 107 ALA B O     1 
ATOM   4765 C  CB    . ALA B 1 80  ? 63.304  23.454  67.369  1.00 81.96  ? 107 ALA B CB    1 
ATOM   4766 N  N     . VAL B 1 81  ? 60.950  25.661  68.045  1.00 74.27  ? 108 VAL B N     1 
ATOM   4767 C  CA    . VAL B 1 81  ? 60.267  26.825  67.493  1.00 84.79  ? 108 VAL B CA    1 
ATOM   4768 C  C     . VAL B 1 81  ? 59.429  27.547  68.539  1.00 81.24  ? 108 VAL B C     1 
ATOM   4769 O  O     . VAL B 1 81  ? 58.719  28.500  68.203  1.00 89.38  ? 108 VAL B O     1 
ATOM   4770 C  CB    . VAL B 1 81  ? 59.406  26.446  66.275  1.00 81.46  ? 108 VAL B CB    1 
ATOM   4771 C  CG1   . VAL B 1 81  ? 60.217  25.633  65.280  1.00 78.23  ? 108 VAL B CG1   1 
ATOM   4772 C  CG2   . VAL B 1 81  ? 58.163  25.682  66.708  1.00 83.74  ? 108 VAL B CG2   1 
ATOM   4773 N  N     . LYS B 1 82  ? 59.507  27.129  69.806  1.00 79.07  ? 109 LYS B N     1 
ATOM   4774 C  CA    . LYS B 1 82  ? 58.626  27.684  70.831  1.00 79.43  ? 109 LYS B CA    1 
ATOM   4775 C  C     . LYS B 1 82  ? 58.830  29.186  70.996  1.00 81.71  ? 109 LYS B C     1 
ATOM   4776 O  O     . LYS B 1 82  ? 57.857  29.948  71.059  1.00 88.69  ? 109 LYS B O     1 
ATOM   4777 C  CB    . LYS B 1 82  ? 58.849  26.961  72.163  1.00 73.64  ? 109 LYS B CB    1 
ATOM   4778 C  CG    . LYS B 1 82  ? 57.840  27.294  73.254  1.00 76.33  ? 109 LYS B CG    1 
ATOM   4779 C  CD    . LYS B 1 82  ? 58.084  26.438  74.497  1.00 102.34 ? 109 LYS B CD    1 
ATOM   4780 C  CE    . LYS B 1 82  ? 56.965  26.585  75.528  1.00 101.52 ? 109 LYS B CE    1 
ATOM   4781 N  NZ    . LYS B 1 82  ? 56.918  27.942  76.150  1.00 98.60  ? 109 LYS B NZ    1 
ATOM   4782 N  N     . SER B 1 83  ? 60.086  29.635  71.051  1.00 82.78  ? 110 SER B N     1 
ATOM   4783 C  CA    . SER B 1 83  ? 60.364  31.038  71.337  1.00 80.71  ? 110 SER B CA    1 
ATOM   4784 C  C     . SER B 1 83  ? 59.992  31.964  70.185  1.00 89.23  ? 110 SER B C     1 
ATOM   4785 O  O     . SER B 1 83  ? 59.916  33.180  70.389  1.00 100.59 ? 110 SER B O     1 
ATOM   4786 C  CB    . SER B 1 83  ? 61.841  31.225  71.684  1.00 92.29  ? 110 SER B CB    1 
ATOM   4787 O  OG    . SER B 1 83  ? 62.651  31.124  70.525  1.00 111.42 ? 110 SER B OG    1 
ATOM   4788 N  N     . LEU B 1 84  ? 59.764  31.431  68.986  1.00 88.15  ? 111 LEU B N     1 
ATOM   4789 C  CA    . LEU B 1 84  ? 59.437  32.279  67.848  1.00 84.80  ? 111 LEU B CA    1 
ATOM   4790 C  C     . LEU B 1 84  ? 57.966  32.666  67.788  1.00 89.15  ? 111 LEU B C     1 
ATOM   4791 O  O     . LEU B 1 84  ? 57.610  33.544  66.995  1.00 93.24  ? 111 LEU B O     1 
ATOM   4792 C  CB    . LEU B 1 84  ? 59.818  31.585  66.538  1.00 86.97  ? 111 LEU B CB    1 
ATOM   4793 C  CG    . LEU B 1 84  ? 61.217  30.976  66.462  1.00 96.80  ? 111 LEU B CG    1 
ATOM   4794 C  CD1   . LEU B 1 84  ? 61.457  30.384  65.084  1.00 91.90  ? 111 LEU B CD1   1 
ATOM   4795 C  CD2   . LEU B 1 84  ? 62.269  32.015  66.801  1.00 105.15 ? 111 LEU B CD2   1 
ATOM   4796 N  N     . TYR B 1 85  ? 57.108  32.051  68.597  1.00 81.90  ? 112 TYR B N     1 
ATOM   4797 C  CA    . TYR B 1 85  ? 55.670  32.201  68.450  1.00 75.31  ? 112 TYR B CA    1 
ATOM   4798 C  C     . TYR B 1 85  ? 55.068  32.895  69.664  1.00 74.82  ? 112 TYR B C     1 
ATOM   4799 O  O     . TYR B 1 85  ? 55.656  32.925  70.749  1.00 90.56  ? 112 TYR B O     1 
ATOM   4800 C  CB    . TYR B 1 85  ? 55.003  30.838  68.220  1.00 74.49  ? 112 TYR B CB    1 
ATOM   4801 C  CG    . TYR B 1 85  ? 55.236  30.314  66.824  1.00 72.48  ? 112 TYR B CG    1 
ATOM   4802 C  CD1   . TYR B 1 85  ? 56.447  29.731  66.473  1.00 72.54  ? 112 TYR B CD1   1 
ATOM   4803 C  CD2   . TYR B 1 85  ? 54.254  30.425  65.850  1.00 76.82  ? 112 TYR B CD2   1 
ATOM   4804 C  CE1   . TYR B 1 85  ? 56.670  29.266  65.192  1.00 79.14  ? 112 TYR B CE1   1 
ATOM   4805 C  CE2   . TYR B 1 85  ? 54.465  29.962  64.567  1.00 73.99  ? 112 TYR B CE2   1 
ATOM   4806 C  CZ    . TYR B 1 85  ? 55.673  29.383  64.241  1.00 81.58  ? 112 TYR B CZ    1 
ATOM   4807 O  OH    . TYR B 1 85  ? 55.883  28.925  62.959  1.00 69.38  ? 112 TYR B OH    1 
ATOM   4808 N  N     . HIS B 1 86  ? 53.875  33.465  69.455  1.00 71.97  ? 113 HIS B N     1 
ATOM   4809 C  CA    . HIS B 1 86  ? 53.192  34.206  70.513  1.00 68.57  ? 113 HIS B CA    1 
ATOM   4810 C  C     . HIS B 1 86  ? 52.893  33.314  71.709  1.00 75.28  ? 113 HIS B C     1 
ATOM   4811 O  O     . HIS B 1 86  ? 52.983  33.756  72.859  1.00 71.29  ? 113 HIS B O     1 
ATOM   4812 C  CB    . HIS B 1 86  ? 51.907  34.822  69.961  1.00 67.83  ? 113 HIS B CB    1 
ATOM   4813 C  CG    . HIS B 1 86  ? 51.000  35.392  71.007  1.00 68.27  ? 113 HIS B CG    1 
ATOM   4814 N  ND1   . HIS B 1 86  ? 51.059  36.709  71.408  1.00 77.21  ? 113 HIS B ND1   1 
ATOM   4815 C  CD2   . HIS B 1 86  ? 49.991  34.830  71.715  1.00 70.99  ? 113 HIS B CD2   1 
ATOM   4816 C  CE1   . HIS B 1 86  ? 50.135  36.931  72.326  1.00 77.64  ? 113 HIS B CE1   1 
ATOM   4817 N  NE2   . HIS B 1 86  ? 49.474  35.805  72.533  1.00 72.21  ? 113 HIS B NE2   1 
ATOM   4818 N  N     . SER B 1 87  ? 52.534  32.059  71.457  1.00 74.63  ? 114 SER B N     1 
ATOM   4819 C  CA    . SER B 1 87  ? 52.316  31.081  72.513  1.00 74.44  ? 114 SER B CA    1 
ATOM   4820 C  C     . SER B 1 87  ? 52.256  29.704  71.872  1.00 82.92  ? 114 SER B C     1 
ATOM   4821 O  O     . SER B 1 87  ? 52.114  29.575  70.652  1.00 73.79  ? 114 SER B O     1 
ATOM   4822 C  CB    . SER B 1 87  ? 51.034  31.364  73.304  1.00 71.06  ? 114 SER B CB    1 
ATOM   4823 O  OG    . SER B 1 87  ? 49.886  31.204  72.494  1.00 76.32  ? 114 SER B OG    1 
ATOM   4824 N  N     . VAL B 1 88  ? 52.373  28.679  72.712  1.00 85.90  ? 115 VAL B N     1 
ATOM   4825 C  CA    . VAL B 1 88  ? 52.328  27.287  72.277  1.00 72.39  ? 115 VAL B CA    1 
ATOM   4826 C  C     . VAL B 1 88  ? 51.583  26.480  73.330  1.00 64.23  ? 115 VAL B C     1 
ATOM   4827 O  O     . VAL B 1 88  ? 51.932  26.528  74.513  1.00 81.69  ? 115 VAL B O     1 
ATOM   4828 C  CB    . VAL B 1 88  ? 53.739  26.705  72.056  1.00 71.75  ? 115 VAL B CB    1 
ATOM   4829 C  CG1   . VAL B 1 88  ? 53.674  25.187  71.934  1.00 76.92  ? 115 VAL B CG1   1 
ATOM   4830 C  CG2   . VAL B 1 88  ? 54.388  27.318  70.818  1.00 61.61  ? 115 VAL B CG2   1 
ATOM   4831 N  N     . GLU B 1 89  ? 50.551  25.755  72.906  1.00 71.66  ? 116 GLU B N     1 
ATOM   4832 C  CA    . GLU B 1 89  ? 49.853  24.806  73.761  1.00 76.87  ? 116 GLU B CA    1 
ATOM   4833 C  C     . GLU B 1 89  ? 50.161  23.385  73.299  1.00 79.76  ? 116 GLU B C     1 
ATOM   4834 O  O     . GLU B 1 89  ? 50.241  23.114  72.097  1.00 76.83  ? 116 GLU B O     1 
ATOM   4835 C  CB    . GLU B 1 89  ? 48.343  25.055  73.758  1.00 65.19  ? 116 GLU B CB    1 
ATOM   4836 C  CG    . GLU B 1 89  ? 47.590  24.179  74.750  1.00 86.74  ? 116 GLU B CG    1 
ATOM   4837 C  CD    . GLU B 1 89  ? 46.262  24.773  75.178  1.00 102.10 ? 116 GLU B CD    1 
ATOM   4838 O  OE1   . GLU B 1 89  ? 46.015  25.959  74.858  1.00 96.20  ? 116 GLU B OE1   1 
ATOM   4839 O  OE2   . GLU B 1 89  ? 45.473  24.052  75.836  1.00 97.91  ? 116 GLU B OE2   1 
ATOM   4840 N  N     . TRP B 1 90  ? 50.328  22.481  74.261  1.00 75.57  ? 117 TRP B N     1 
ATOM   4841 C  CA    . TRP B 1 90  ? 50.883  21.155  74.002  1.00 75.20  ? 117 TRP B CA    1 
ATOM   4842 C  C     . TRP B 1 90  ? 50.089  20.142  74.812  1.00 79.11  ? 117 TRP B C     1 
ATOM   4843 O  O     . TRP B 1 90  ? 50.139  20.155  76.047  1.00 80.48  ? 117 TRP B O     1 
ATOM   4844 C  CB    . TRP B 1 90  ? 52.369  21.134  74.363  1.00 80.01  ? 117 TRP B CB    1 
ATOM   4845 C  CG    . TRP B 1 90  ? 53.042  19.800  74.372  1.00 85.56  ? 117 TRP B CG    1 
ATOM   4846 C  CD1   . TRP B 1 90  ? 53.749  19.256  75.402  1.00 90.59  ? 117 TRP B CD1   1 
ATOM   4847 C  CD2   . TRP B 1 90  ? 53.105  18.853  73.298  1.00 85.93  ? 117 TRP B CD2   1 
ATOM   4848 N  NE1   . TRP B 1 90  ? 54.241  18.027  75.042  1.00 100.81 ? 117 TRP B NE1   1 
ATOM   4849 C  CE2   . TRP B 1 90  ? 53.858  17.754  73.756  1.00 81.84  ? 117 TRP B CE2   1 
ATOM   4850 C  CE3   . TRP B 1 90  ? 52.587  18.820  72.001  1.00 81.96  ? 117 TRP B CE3   1 
ATOM   4851 C  CZ2   . TRP B 1 90  ? 54.111  16.639  72.964  1.00 85.17  ? 117 TRP B CZ2   1 
ATOM   4852 C  CZ3   . TRP B 1 90  ? 52.842  17.709  71.213  1.00 85.18  ? 117 TRP B CZ3   1 
ATOM   4853 C  CH2   . TRP B 1 90  ? 53.596  16.634  71.698  1.00 82.98  ? 117 TRP B CH2   1 
ATOM   4854 N  N     . ARG B 1 91  ? 49.351  19.272  74.124  1.00 79.38  ? 118 ARG B N     1 
ATOM   4855 C  CA    . ARG B 1 91  ? 48.454  18.307  74.764  1.00 89.63  ? 118 ARG B CA    1 
ATOM   4856 C  C     . ARG B 1 91  ? 48.766  16.901  74.267  1.00 82.17  ? 118 ARG B C     1 
ATOM   4857 O  O     . ARG B 1 91  ? 48.094  16.383  73.365  1.00 87.19  ? 118 ARG B O     1 
ATOM   4858 C  CB    . ARG B 1 91  ? 46.990  18.669  74.506  1.00 87.74  ? 118 ARG B CB    1 
ATOM   4859 C  CG    . ARG B 1 91  ? 46.576  20.012  75.095  1.00 101.23 ? 118 ARG B CG    1 
ATOM   4860 C  CD    . ARG B 1 91  ? 45.101  20.296  74.856  1.00 98.49  ? 118 ARG B CD    1 
ATOM   4861 N  NE    . ARG B 1 91  ? 44.271  19.130  75.141  1.00 112.15 ? 118 ARG B NE    1 
ATOM   4862 C  CZ    . ARG B 1 91  ? 42.949  19.156  75.233  1.00 108.55 ? 118 ARG B CZ    1 
ATOM   4863 N  NH1   . ARG B 1 91  ? 42.269  20.284  75.093  1.00 90.45  ? 118 ARG B NH1   1 
ATOM   4864 N  NH2   . ARG B 1 91  ? 42.291  18.023  75.475  1.00 80.11  ? 118 ARG B NH2   1 
ATOM   4865 N  N     . PRO B 1 92  ? 49.779  16.254  74.834  1.00 84.27  ? 119 PRO B N     1 
ATOM   4866 C  CA    . PRO B 1 92  ? 50.083  14.871  74.465  1.00 88.52  ? 119 PRO B CA    1 
ATOM   4867 C  C     . PRO B 1 92  ? 49.388  13.864  75.374  1.00 79.53  ? 119 PRO B C     1 
ATOM   4868 O  O     . PRO B 1 92  ? 48.949  14.175  76.482  1.00 82.49  ? 119 PRO B O     1 
ATOM   4869 C  CB    . PRO B 1 92  ? 51.606  14.805  74.642  1.00 83.59  ? 119 PRO B CB    1 
ATOM   4870 C  CG    . PRO B 1 92  ? 51.862  15.735  75.785  1.00 83.57  ? 119 PRO B CG    1 
ATOM   4871 C  CD    . PRO B 1 92  ? 50.827  16.835  75.693  1.00 86.10  ? 119 PRO B CD    1 
ATOM   4872 N  N     . ALA B 1 93  ? 49.300  12.631  74.877  1.00 80.99  ? 120 ALA B N     1 
ATOM   4873 C  CA    . ALA B 1 93  ? 48.704  11.538  75.645  1.00 85.79  ? 120 ALA B CA    1 
ATOM   4874 C  C     . ALA B 1 93  ? 49.311  10.239  75.125  1.00 91.65  ? 120 ALA B C     1 
ATOM   4875 O  O     . ALA B 1 93  ? 48.880  9.720   74.090  1.00 97.68  ? 120 ALA B O     1 
ATOM   4876 C  CB    . ALA B 1 93  ? 47.186  11.540  75.525  1.00 78.70  ? 120 ALA B CB    1 
ATOM   4877 N  N     . GLU B 1 94  ? 50.304  9.722   75.851  1.00 93.77  ? 121 GLU B N     1 
ATOM   4878 C  CA    . GLU B 1 94  ? 51.072  8.583   75.358  1.00 96.70  ? 121 GLU B CA    1 
ATOM   4879 C  C     . GLU B 1 94  ? 50.209  7.333   75.254  1.00 92.19  ? 121 GLU B C     1 
ATOM   4880 O  O     . GLU B 1 94  ? 50.183  6.672   74.209  1.00 104.06 ? 121 GLU B O     1 
ATOM   4881 C  CB    . GLU B 1 94  ? 52.278  8.335   76.264  1.00 92.07  ? 121 GLU B CB    1 
ATOM   4882 C  CG    . GLU B 1 94  ? 53.207  9.534   76.378  1.00 114.83 ? 121 GLU B CG    1 
ATOM   4883 C  CD    . GLU B 1 94  ? 53.767  9.962   75.034  1.00 115.89 ? 121 GLU B CD    1 
ATOM   4884 O  OE1   . GLU B 1 94  ? 54.266  9.083   74.296  1.00 108.92 ? 121 GLU B OE1   1 
ATOM   4885 O  OE2   . GLU B 1 94  ? 53.697  11.171  74.713  1.00 99.84  ? 121 GLU B OE2   1 
ATOM   4886 N  N     . GLU B 1 95  ? 49.500  6.990   76.322  1.00 91.78  ? 122 GLU B N     1 
ATOM   4887 C  CA    . GLU B 1 95  ? 48.684  5.789   76.326  1.00 96.60  ? 122 GLU B CA    1 
ATOM   4888 C  C     . GLU B 1 95  ? 47.203  6.150   76.417  1.00 92.48  ? 122 GLU B C     1 
ATOM   4889 O  O     . GLU B 1 95  ? 46.849  7.198   76.968  1.00 94.86  ? 122 GLU B O     1 
ATOM   4890 C  CB    . GLU B 1 95  ? 49.055  4.868   77.494  1.00 97.43  ? 122 GLU B CB    1 
ATOM   4891 C  CG    . GLU B 1 95  ? 50.430  4.218   77.368  1.00 110.63 ? 122 GLU B CG    1 
ATOM   4892 C  CD    . GLU B 1 95  ? 50.432  2.990   76.468  1.00 120.76 ? 122 GLU B CD    1 
ATOM   4893 O  OE1   . GLU B 1 95  ? 49.385  2.310   76.376  1.00 120.36 ? 122 GLU B OE1   1 
ATOM   4894 O  OE2   . GLU B 1 95  ? 51.483  2.702   75.854  1.00 121.49 ? 122 GLU B OE2   1 
ATOM   4895 N  N     . PRO B 1 96  ? 46.309  5.320   75.857  1.00 90.82  ? 123 PRO B N     1 
ATOM   4896 C  CA    . PRO B 1 96  ? 46.565  4.100   75.081  1.00 89.18  ? 123 PRO B CA    1 
ATOM   4897 C  C     . PRO B 1 96  ? 46.998  4.429   73.661  1.00 94.57  ? 123 PRO B C     1 
ATOM   4898 O  O     . PRO B 1 96  ? 46.709  5.515   73.158  1.00 101.74 ? 123 PRO B O     1 
ATOM   4899 C  CB    . PRO B 1 96  ? 45.209  3.390   75.115  1.00 78.59  ? 123 PRO B CB    1 
ATOM   4900 C  CG    . PRO B 1 96  ? 44.231  4.528   75.095  1.00 90.39  ? 123 PRO B CG    1 
ATOM   4901 C  CD    . PRO B 1 96  ? 44.865  5.600   75.954  1.00 77.43  ? 123 PRO B CD    1 
ATOM   4902 N  N     . ARG B 1 97  ? 47.687  3.513   72.987  1.00 82.75  ? 124 ARG B N     1 
ATOM   4903 C  CA    . ARG B 1 97  ? 48.153  3.784   71.635  1.00 99.57  ? 124 ARG B CA    1 
ATOM   4904 C  C     . ARG B 1 97  ? 47.078  3.560   70.579  1.00 90.66  ? 124 ARG B C     1 
ATOM   4905 O  O     . ARG B 1 97  ? 47.241  4.018   69.442  1.00 92.29  ? 124 ARG B O     1 
ATOM   4906 C  CB    . ARG B 1 97  ? 49.389  2.932   71.340  1.00 90.54  ? 124 ARG B CB    1 
ATOM   4907 C  CG    . ARG B 1 97  ? 50.562  3.268   72.253  1.00 87.57  ? 124 ARG B CG    1 
ATOM   4908 C  CD    . ARG B 1 97  ? 51.811  2.524   71.845  1.00 88.30  ? 124 ARG B CD    1 
ATOM   4909 N  NE    . ARG B 1 97  ? 51.690  1.097   72.111  1.00 112.16 ? 124 ARG B NE    1 
ATOM   4910 C  CZ    . ARG B 1 97  ? 52.471  0.170   71.574  1.00 120.03 ? 124 ARG B CZ    1 
ATOM   4911 N  NH1   . ARG B 1 97  ? 53.432  0.487   70.721  1.00 120.48 ? 124 ARG B NH1   1 
ATOM   4912 N  NH2   . ARG B 1 97  ? 52.278  -1.106  71.896  1.00 113.61 ? 124 ARG B NH2   1 
ATOM   4913 N  N     . SER B 1 98  ? 45.985  2.889   70.928  1.00 92.63  ? 125 SER B N     1 
ATOM   4914 C  CA    . SER B 1 98  ? 44.887  2.667   70.000  1.00 88.71  ? 125 SER B CA    1 
ATOM   4915 C  C     . SER B 1 98  ? 43.577  2.698   70.775  1.00 85.33  ? 125 SER B C     1 
ATOM   4916 O  O     . SER B 1 98  ? 43.552  2.508   71.994  1.00 92.63  ? 125 SER B O     1 
ATOM   4917 C  CB    . SER B 1 98  ? 45.055  1.343   69.247  1.00 89.29  ? 125 SER B CB    1 
ATOM   4918 O  OG    . SER B 1 98  ? 45.454  0.308   70.128  1.00 110.07 ? 125 SER B OG    1 
ATOM   4919 N  N     . TYR B 1 99  ? 42.479  2.951   70.049  1.00 82.60  ? 126 TYR B N     1 
ATOM   4920 C  CA    . TYR B 1 99  ? 41.176  3.066   70.696  1.00 89.13  ? 126 TYR B CA    1 
ATOM   4921 C  C     . TYR B 1 99  ? 40.626  1.684   71.052  1.00 94.34  ? 126 TYR B C     1 
ATOM   4922 O  O     . TYR B 1 99  ? 40.801  0.729   70.292  1.00 96.56  ? 126 TYR B O     1 
ATOM   4923 C  CB    . TYR B 1 99  ? 40.186  3.797   69.793  1.00 81.20  ? 126 TYR B CB    1 
ATOM   4924 C  CG    . TYR B 1 99  ? 40.444  5.283   69.671  1.00 86.10  ? 126 TYR B CG    1 
ATOM   4925 C  CD1   . TYR B 1 99  ? 41.319  5.782   68.710  1.00 86.91  ? 126 TYR B CD1   1 
ATOM   4926 C  CD2   . TYR B 1 99  ? 39.812  6.188   70.512  1.00 82.42  ? 126 TYR B CD2   1 
ATOM   4927 C  CE1   . TYR B 1 99  ? 41.556  7.140   68.593  1.00 77.74  ? 126 TYR B CE1   1 
ATOM   4928 C  CE2   . TYR B 1 99  ? 40.045  7.548   70.401  1.00 79.17  ? 126 TYR B CE2   1 
ATOM   4929 C  CZ    . TYR B 1 99  ? 40.916  8.016   69.442  1.00 76.93  ? 126 TYR B CZ    1 
ATOM   4930 O  OH    . TYR B 1 99  ? 41.143  9.366   69.336  1.00 82.65  ? 126 TYR B OH    1 
ATOM   4931 N  N     . PRO B 1 100 ? 39.961  1.551   72.203  1.00 92.97  ? 127 PRO B N     1 
ATOM   4932 C  CA    . PRO B 1 100 ? 39.403  0.242   72.580  1.00 93.81  ? 127 PRO B CA    1 
ATOM   4933 C  C     . PRO B 1 100 ? 38.284  -0.239  71.673  1.00 96.76  ? 127 PRO B C     1 
ATOM   4934 O  O     . PRO B 1 100 ? 37.947  -1.429  71.720  1.00 99.01  ? 127 PRO B O     1 
ATOM   4935 C  CB    . PRO B 1 100 ? 38.895  0.473   74.010  1.00 85.70  ? 127 PRO B CB    1 
ATOM   4936 C  CG    . PRO B 1 100 ? 39.666  1.668   74.501  1.00 97.16  ? 127 PRO B CG    1 
ATOM   4937 C  CD    . PRO B 1 100 ? 39.855  2.534   73.295  1.00 96.01  ? 127 PRO B CD    1 
ATOM   4938 N  N     . ASP B 1 101 ? 37.695  0.632   70.853  1.00 95.02  ? 128 ASP B N     1 
ATOM   4939 C  CA    . ASP B 1 101 ? 36.599  0.246   69.973  1.00 99.55  ? 128 ASP B CA    1 
ATOM   4940 C  C     . ASP B 1 101 ? 36.985  0.307   68.499  1.00 106.11 ? 128 ASP B C     1 
ATOM   4941 O  O     . ASP B 1 101 ? 36.105  0.313   67.632  1.00 105.25 ? 128 ASP B O     1 
ATOM   4942 C  CB    . ASP B 1 101 ? 35.372  1.123   70.237  1.00 102.68 ? 128 ASP B CB    1 
ATOM   4943 C  CG    . ASP B 1 101 ? 35.551  2.548   69.738  1.00 109.29 ? 128 ASP B CG    1 
ATOM   4944 O  OD1   . ASP B 1 101 ? 36.708  3.017   69.661  1.00 95.90  ? 128 ASP B OD1   1 
ATOM   4945 O  OD2   . ASP B 1 101 ? 34.527  3.198   69.427  1.00 109.97 ? 128 ASP B OD2   1 
ATOM   4946 N  N     . GLU B 1 102 ? 38.280  0.355   68.197  1.00 104.59 ? 129 GLU B N     1 
ATOM   4947 C  CA    . GLU B 1 102 ? 38.765  0.467   66.831  1.00 84.93  ? 129 GLU B CA    1 
ATOM   4948 C  C     . GLU B 1 102 ? 39.149  -0.900  66.278  1.00 90.04  ? 129 GLU B C     1 
ATOM   4949 O  O     . GLU B 1 102 ? 39.440  -1.842  67.021  1.00 100.16 ? 129 GLU B O     1 
ATOM   4950 C  CB    . GLU B 1 102 ? 39.973  1.404   66.756  1.00 93.37  ? 129 GLU B CB    1 
ATOM   4951 C  CG    . GLU B 1 102 ? 41.304  0.709   66.995  1.00 86.22  ? 129 GLU B CG    1 
ATOM   4952 C  CD    . GLU B 1 102 ? 42.493  1.600   66.679  1.00 95.91  ? 129 GLU B CD    1 
ATOM   4953 O  OE1   . GLU B 1 102 ? 42.343  2.843   66.761  1.00 90.69  ? 129 GLU B OE1   1 
ATOM   4954 O  OE2   . GLU B 1 102 ? 43.571  1.052   66.339  1.00 90.11  ? 129 GLU B OE2   1 
ATOM   4955 N  N     . GLU B 1 103 ? 39.143  -0.995  64.950  1.00 94.69  ? 130 GLU B N     1 
ATOM   4956 C  CA    . GLU B 1 103 ? 39.570  -2.194  64.242  1.00 88.35  ? 130 GLU B CA    1 
ATOM   4957 C  C     . GLU B 1 103 ? 40.969  -2.062  63.661  1.00 97.47  ? 130 GLU B C     1 
ATOM   4958 O  O     . GLU B 1 103 ? 41.531  -3.061  63.195  1.00 99.81  ? 130 GLU B O     1 
ATOM   4959 C  CB    . GLU B 1 103 ? 38.579  -2.524  63.121  1.00 86.75  ? 130 GLU B CB    1 
ATOM   4960 C  CG    . GLU B 1 103 ? 37.171  -2.812  63.611  1.00 89.87  ? 130 GLU B CG    1 
ATOM   4961 C  CD    . GLU B 1 103 ? 36.149  -2.799  62.490  1.00 99.03  ? 130 GLU B CD    1 
ATOM   4962 O  OE1   . GLU B 1 103 ? 36.445  -2.229  61.417  1.00 91.61  ? 130 GLU B OE1   1 
ATOM   4963 O  OE2   . GLU B 1 103 ? 35.050  -3.360  62.682  1.00 104.29 ? 130 GLU B OE2   1 
ATOM   4964 N  N     . GLY B 1 104 ? 41.537  -0.863  63.682  1.00 89.06  ? 131 GLY B N     1 
ATOM   4965 C  CA    . GLY B 1 104 ? 42.861  -0.622  63.171  1.00 88.90  ? 131 GLY B CA    1 
ATOM   4966 C  C     . GLY B 1 104 ? 43.193  0.848   63.269  1.00 82.83  ? 131 GLY B C     1 
ATOM   4967 O  O     . GLY B 1 104 ? 42.328  1.682   63.554  1.00 89.67  ? 131 GLY B O     1 
ATOM   4968 N  N     . PRO B 1 105 ? 44.456  1.199   63.029  1.00 81.75  ? 132 PRO B N     1 
ATOM   4969 C  CA    . PRO B 1 105 ? 44.856  2.611   63.146  1.00 75.00  ? 132 PRO B CA    1 
ATOM   4970 C  C     . PRO B 1 105 ? 44.163  3.527   62.150  1.00 80.41  ? 132 PRO B C     1 
ATOM   4971 O  O     . PRO B 1 105 ? 44.045  4.730   62.415  1.00 79.24  ? 132 PRO B O     1 
ATOM   4972 C  CB    . PRO B 1 105 ? 46.371  2.563   62.908  1.00 75.72  ? 132 PRO B CB    1 
ATOM   4973 C  CG    . PRO B 1 105 ? 46.577  1.336   62.085  1.00 92.04  ? 132 PRO B CG    1 
ATOM   4974 C  CD    . PRO B 1 105 ? 45.561  0.341   62.572  1.00 81.93  ? 132 PRO B CD    1 
ATOM   4975 N  N     . LYS B 1 106 ? 43.702  3.002   61.017  1.00 81.18  ? 133 LYS B N     1 
ATOM   4976 C  CA    . LYS B 1 106 ? 43.026  3.797   60.001  1.00 87.21  ? 133 LYS B CA    1 
ATOM   4977 C  C     . LYS B 1 106 ? 41.510  3.659   60.056  1.00 90.44  ? 133 LYS B C     1 
ATOM   4978 O  O     . LYS B 1 106 ? 40.819  4.135   59.148  1.00 88.65  ? 133 LYS B O     1 
ATOM   4979 C  CB    . LYS B 1 106 ? 43.539  3.423   58.607  1.00 80.73  ? 133 LYS B CB    1 
ATOM   4980 C  CG    . LYS B 1 106 ? 45.002  3.768   58.392  1.00 81.18  ? 133 LYS B CG    1 
ATOM   4981 C  CD    . LYS B 1 106 ? 45.246  5.255   58.607  1.00 74.67  ? 133 LYS B CD    1 
ATOM   4982 C  CE    . LYS B 1 106 ? 46.716  5.545   58.830  1.00 85.72  ? 133 LYS B CE    1 
ATOM   4983 N  NZ    . LYS B 1 106 ? 46.976  6.994   59.044  1.00 70.89  ? 133 LYS B NZ    1 
ATOM   4984 N  N     . HIS B 1 107 ? 40.978  3.023   61.096  1.00 88.95  ? 134 HIS B N     1 
ATOM   4985 C  CA    . HIS B 1 107 ? 39.539  2.900   61.278  1.00 92.56  ? 134 HIS B CA    1 
ATOM   4986 C  C     . HIS B 1 107 ? 39.018  4.088   62.077  1.00 94.90  ? 134 HIS B C     1 
ATOM   4987 O  O     . HIS B 1 107 ? 39.543  4.397   63.153  1.00 87.90  ? 134 HIS B O     1 
ATOM   4988 C  CB    . HIS B 1 107 ? 39.192  1.591   61.989  1.00 91.30  ? 134 HIS B CB    1 
ATOM   4989 C  CG    . HIS B 1 107 ? 37.735  1.442   62.307  1.00 94.94  ? 134 HIS B CG    1 
ATOM   4990 N  ND1   . HIS B 1 107 ? 37.278  0.673   63.356  1.00 93.15  ? 134 HIS B ND1   1 
ATOM   4991 C  CD2   . HIS B 1 107 ? 36.633  1.958   61.711  1.00 91.76  ? 134 HIS B CD2   1 
ATOM   4992 C  CE1   . HIS B 1 107 ? 35.959  0.724   63.395  1.00 89.58  ? 134 HIS B CE1   1 
ATOM   4993 N  NE2   . HIS B 1 107 ? 35.542  1.497   62.408  1.00 89.55  ? 134 HIS B NE2   1 
ATOM   4994 N  N     . TRP B 1 108 ? 37.986  4.750   61.550  1.00 89.71  ? 135 TRP B N     1 
ATOM   4995 C  CA    . TRP B 1 108 ? 37.357  5.871   62.249  1.00 83.67  ? 135 TRP B CA    1 
ATOM   4996 C  C     . TRP B 1 108 ? 36.156  5.346   63.028  1.00 91.17  ? 135 TRP B C     1 
ATOM   4997 O  O     . TRP B 1 108 ? 35.012  5.362   62.569  1.00 93.30  ? 135 TRP B O     1 
ATOM   4998 C  CB    . TRP B 1 108 ? 36.961  6.972   61.274  1.00 77.72  ? 135 TRP B CB    1 
ATOM   4999 C  CG    . TRP B 1 108 ? 38.109  7.826   60.863  1.00 75.49  ? 135 TRP B CG    1 
ATOM   5000 C  CD1   . TRP B 1 108 ? 38.950  7.609   59.819  1.00 80.28  ? 135 TRP B CD1   1 
ATOM   5001 C  CD2   . TRP B 1 108 ? 38.551  9.035   61.493  1.00 77.66  ? 135 TRP B CD2   1 
ATOM   5002 N  NE1   . TRP B 1 108 ? 39.890  8.606   59.754  1.00 87.19  ? 135 TRP B NE1   1 
ATOM   5003 C  CE2   . TRP B 1 108 ? 39.666  9.496   60.771  1.00 80.66  ? 135 TRP B CE2   1 
ATOM   5004 C  CE3   . TRP B 1 108 ? 38.109  9.775   62.593  1.00 77.91  ? 135 TRP B CE3   1 
ATOM   5005 C  CZ2   . TRP B 1 108 ? 40.349  10.663  61.111  1.00 74.10  ? 135 TRP B CZ2   1 
ATOM   5006 C  CZ3   . TRP B 1 108 ? 38.788  10.935  62.928  1.00 73.85  ? 135 TRP B CZ3   1 
ATOM   5007 C  CH2   . TRP B 1 108 ? 39.896  11.364  62.191  1.00 71.26  ? 135 TRP B CH2   1 
ATOM   5008 N  N     . SER B 1 109 ? 36.436  4.873   64.240  1.00 84.21  ? 136 SER B N     1 
ATOM   5009 C  CA    . SER B 1 109 ? 35.386  4.430   65.142  1.00 85.20  ? 136 SER B CA    1 
ATOM   5010 C  C     . SER B 1 109 ? 34.652  5.639   65.720  1.00 96.28  ? 136 SER B C     1 
ATOM   5011 O  O     . SER B 1 109 ? 34.992  6.797   65.457  1.00 90.86  ? 136 SER B O     1 
ATOM   5012 C  CB    . SER B 1 109 ? 35.974  3.571   66.258  1.00 89.17  ? 136 SER B CB    1 
ATOM   5013 O  OG    . SER B 1 109 ? 36.749  4.360   67.144  1.00 95.05  ? 136 SER B OG    1 
ATOM   5014 N  N     . ASP B 1 110 ? 33.629  5.365   66.530  1.00 88.77  ? 137 ASP B N     1 
ATOM   5015 C  CA    . ASP B 1 110 ? 32.866  6.457   67.127  1.00 91.39  ? 137 ASP B CA    1 
ATOM   5016 C  C     . ASP B 1 110 ? 33.666  7.165   68.213  1.00 94.64  ? 137 ASP B C     1 
ATOM   5017 O  O     . ASP B 1 110 ? 33.601  8.395   68.335  1.00 93.89  ? 137 ASP B O     1 
ATOM   5018 C  CB    . ASP B 1 110 ? 31.542  5.936   67.679  1.00 88.78  ? 137 ASP B CB    1 
ATOM   5019 C  CG    . ASP B 1 110 ? 30.500  5.749   66.595  1.00 105.36 ? 137 ASP B CG    1 
ATOM   5020 O  OD1   . ASP B 1 110 ? 30.739  6.216   65.457  1.00 97.17  ? 137 ASP B OD1   1 
ATOM   5021 O  OD2   . ASP B 1 110 ? 29.448  5.136   66.878  1.00 112.63 ? 137 ASP B OD2   1 
ATOM   5022 N  N     . SER B 1 111 ? 34.429  6.410   69.008  1.00 87.45  ? 138 SER B N     1 
ATOM   5023 C  CA    . SER B 1 111 ? 35.254  7.032   70.036  1.00 83.28  ? 138 SER B CA    1 
ATOM   5024 C  C     . SER B 1 111 ? 36.348  7.899   69.427  1.00 93.76  ? 138 SER B C     1 
ATOM   5025 O  O     . SER B 1 111 ? 36.750  8.900   70.031  1.00 97.55  ? 138 SER B O     1 
ATOM   5026 C  CB    . SER B 1 111 ? 35.854  5.961   70.940  1.00 81.92  ? 138 SER B CB    1 
ATOM   5027 O  OG    . SER B 1 111 ? 34.825  5.221   71.573  1.00 107.81 ? 138 SER B OG    1 
ATOM   5028 N  N     . ARG B 1 112 ? 36.835  7.538   68.237  1.00 91.62  ? 139 ARG B N     1 
ATOM   5029 C  CA    . ARG B 1 112 ? 37.810  8.380   67.552  1.00 84.98  ? 139 ARG B CA    1 
ATOM   5030 C  C     . ARG B 1 112 ? 37.142  9.606   66.938  1.00 83.27  ? 139 ARG B C     1 
ATOM   5031 O  O     . ARG B 1 112 ? 37.718  10.700  66.935  1.00 76.50  ? 139 ARG B O     1 
ATOM   5032 C  CB    . ARG B 1 112 ? 38.539  7.566   66.482  1.00 82.98  ? 139 ARG B CB    1 
ATOM   5033 C  CG    . ARG B 1 112 ? 39.671  8.307   65.784  1.00 68.32  ? 139 ARG B CG    1 
ATOM   5034 C  CD    . ARG B 1 112 ? 40.102  7.571   64.525  1.00 81.64  ? 139 ARG B CD    1 
ATOM   5035 N  NE    . ARG B 1 112 ? 41.345  8.097   63.975  1.00 82.00  ? 139 ARG B NE    1 
ATOM   5036 C  CZ    . ARG B 1 112 ? 41.960  7.611   62.905  1.00 76.21  ? 139 ARG B CZ    1 
ATOM   5037 N  NH1   . ARG B 1 112 ? 41.459  6.594   62.222  1.00 87.03  ? 139 ARG B NH1   1 
ATOM   5038 N  NH2   . ARG B 1 112 ? 43.105  8.160   62.511  1.00 77.31  ? 139 ARG B NH2   1 
ATOM   5039 N  N     . TYR B 1 113 ? 35.927  9.439   66.405  1.00 93.25  ? 140 TYR B N     1 
ATOM   5040 C  CA    . TYR B 1 113 ? 35.161  10.582  65.920  1.00 78.86  ? 140 TYR B CA    1 
ATOM   5041 C  C     . TYR B 1 113 ? 34.879  11.560  67.050  1.00 80.30  ? 140 TYR B C     1 
ATOM   5042 O  O     . TYR B 1 113 ? 35.064  12.772  66.900  1.00 77.26  ? 140 TYR B O     1 
ATOM   5043 C  CB    . TYR B 1 113 ? 33.852  10.107  65.290  1.00 79.04  ? 140 TYR B CB    1 
ATOM   5044 C  CG    . TYR B 1 113 ? 33.936  9.784   63.814  1.00 83.59  ? 140 TYR B CG    1 
ATOM   5045 C  CD1   . TYR B 1 113 ? 34.482  10.687  62.912  1.00 76.07  ? 140 TYR B CD1   1 
ATOM   5046 C  CD2   . TYR B 1 113 ? 33.468  8.571   63.324  1.00 82.80  ? 140 TYR B CD2   1 
ATOM   5047 C  CE1   . TYR B 1 113 ? 34.555  10.391  61.561  1.00 83.07  ? 140 TYR B CE1   1 
ATOM   5048 C  CE2   . TYR B 1 113 ? 33.537  8.267   61.977  1.00 82.62  ? 140 TYR B CE2   1 
ATOM   5049 C  CZ    . TYR B 1 113 ? 34.078  9.179   61.100  1.00 81.65  ? 140 TYR B CZ    1 
ATOM   5050 O  OH    . TYR B 1 113 ? 34.145  8.871   59.761  1.00 94.57  ? 140 TYR B OH    1 
ATOM   5051 N  N     . GLU B 1 114 ? 34.431  11.046  68.196  1.00 77.79  ? 141 GLU B N     1 
ATOM   5052 C  CA    . GLU B 1 114 ? 34.117  11.916  69.324  1.00 74.66  ? 141 GLU B CA    1 
ATOM   5053 C  C     . GLU B 1 114 ? 35.355  12.646  69.828  1.00 77.90  ? 141 GLU B C     1 
ATOM   5054 O  O     . GLU B 1 114 ? 35.304  13.848  70.107  1.00 81.64  ? 141 GLU B O     1 
ATOM   5055 C  CB    . GLU B 1 114 ? 33.484  11.103  70.449  1.00 78.67  ? 141 GLU B CB    1 
ATOM   5056 C  CG    . GLU B 1 114 ? 33.308  11.890  71.726  1.00 86.77  ? 141 GLU B CG    1 
ATOM   5057 C  CD    . GLU B 1 114 ? 32.885  11.024  72.886  1.00 90.87  ? 141 GLU B CD    1 
ATOM   5058 O  OE1   . GLU B 1 114 ? 31.791  10.426  72.815  1.00 94.63  ? 141 GLU B OE1   1 
ATOM   5059 O  OE2   . GLU B 1 114 ? 33.656  10.936  73.865  1.00 107.11 ? 141 GLU B OE2   1 
ATOM   5060 N  N     . HIS B 1 115 ? 36.478  11.938  69.950  1.00 77.21  ? 142 HIS B N     1 
ATOM   5061 C  CA    . HIS B 1 115 ? 37.682  12.559  70.494  1.00 74.16  ? 142 HIS B CA    1 
ATOM   5062 C  C     . HIS B 1 115 ? 38.186  13.673  69.584  1.00 71.24  ? 142 HIS B C     1 
ATOM   5063 O  O     . HIS B 1 115 ? 38.505  14.773  70.049  1.00 72.14  ? 142 HIS B O     1 
ATOM   5064 C  CB    . HIS B 1 115 ? 38.767  11.500  70.710  1.00 82.78  ? 142 HIS B CB    1 
ATOM   5065 C  CG    . HIS B 1 115 ? 40.032  12.045  71.298  1.00 82.62  ? 142 HIS B CG    1 
ATOM   5066 N  ND1   . HIS B 1 115 ? 40.089  12.588  72.565  1.00 73.22  ? 142 HIS B ND1   1 
ATOM   5067 C  CD2   . HIS B 1 115 ? 41.282  12.147  70.788  1.00 76.66  ? 142 HIS B CD2   1 
ATOM   5068 C  CE1   . HIS B 1 115 ? 41.322  12.995  72.811  1.00 73.85  ? 142 HIS B CE1   1 
ATOM   5069 N  NE2   . HIS B 1 115 ? 42.065  12.742  71.748  1.00 75.21  ? 142 HIS B NE2   1 
ATOM   5070 N  N     . VAL B 1 116 ? 38.277  13.403  68.280  1.00 76.87  ? 143 VAL B N     1 
ATOM   5071 C  CA    . VAL B 1 116 ? 38.782  14.407  67.350  1.00 68.79  ? 143 VAL B CA    1 
ATOM   5072 C  C     . VAL B 1 116 ? 37.842  15.606  67.296  1.00 75.80  ? 143 VAL B C     1 
ATOM   5073 O  O     . VAL B 1 116 ? 38.286  16.757  67.199  1.00 82.25  ? 143 VAL B O     1 
ATOM   5074 C  CB    . VAL B 1 116 ? 39.001  13.781  65.960  1.00 77.64  ? 143 VAL B CB    1 
ATOM   5075 C  CG1   . VAL B 1 116 ? 39.362  14.845  64.943  1.00 63.91  ? 143 VAL B CG1   1 
ATOM   5076 C  CG2   . VAL B 1 116 ? 40.089  12.711  66.027  1.00 75.82  ? 143 VAL B CG2   1 
ATOM   5077 N  N     . MET B 1 117 ? 36.531  15.362  67.374  1.00 74.37  ? 144 MET B N     1 
ATOM   5078 C  CA    . MET B 1 117 ? 35.582  16.471  67.451  1.00 71.69  ? 144 MET B CA    1 
ATOM   5079 C  C     . MET B 1 117 ? 35.836  17.315  68.692  1.00 70.30  ? 144 MET B C     1 
ATOM   5080 O  O     . MET B 1 117 ? 35.952  18.544  68.607  1.00 69.77  ? 144 MET B O     1 
ATOM   5081 C  CB    . MET B 1 117 ? 34.145  15.945  67.444  1.00 77.25  ? 144 MET B CB    1 
ATOM   5082 C  CG    . MET B 1 117 ? 33.662  15.534  66.070  1.00 73.52  ? 144 MET B CG    1 
ATOM   5083 S  SD    . MET B 1 117 ? 31.887  15.273  65.963  1.00 84.61  ? 144 MET B SD    1 
ATOM   5084 C  CE    . MET B 1 117 ? 31.781  13.506  66.229  1.00 83.87  ? 144 MET B CE    1 
ATOM   5085 N  N     . LYS B 1 118 ? 35.932  16.666  69.856  1.00 70.50  ? 145 LYS B N     1 
ATOM   5086 C  CA    . LYS B 1 118 ? 36.228  17.386  71.091  1.00 64.51  ? 145 LYS B CA    1 
ATOM   5087 C  C     . LYS B 1 118 ? 37.520  18.185  70.969  1.00 74.90  ? 145 LYS B C     1 
ATOM   5088 O  O     . LYS B 1 118 ? 37.590  19.337  71.415  1.00 80.71  ? 145 LYS B O     1 
ATOM   5089 C  CB    . LYS B 1 118 ? 36.310  16.409  72.267  1.00 61.89  ? 145 LYS B CB    1 
ATOM   5090 C  CG    . LYS B 1 118 ? 34.999  15.714  72.632  1.00 64.61  ? 145 LYS B CG    1 
ATOM   5091 C  CD    . LYS B 1 118 ? 34.860  15.603  74.147  1.00 71.89  ? 145 LYS B CD    1 
ATOM   5092 C  CE    . LYS B 1 118 ? 33.681  14.735  74.570  1.00 73.18  ? 145 LYS B CE    1 
ATOM   5093 N  NZ    . LYS B 1 118 ? 34.065  13.306  74.728  1.00 88.13  ? 145 LYS B NZ    1 
ATOM   5094 N  N     . LEU B 1 119 ? 38.548  17.599  70.349  1.00 65.64  ? 146 LEU B N     1 
ATOM   5095 C  CA    . LEU B 1 119 ? 39.833  18.283  70.224  1.00 74.84  ? 146 LEU B CA    1 
ATOM   5096 C  C     . LEU B 1 119 ? 39.709  19.555  69.394  1.00 75.05  ? 146 LEU B C     1 
ATOM   5097 O  O     . LEU B 1 119 ? 40.121  20.636  69.833  1.00 76.93  ? 146 LEU B O     1 
ATOM   5098 C  CB    . LEU B 1 119 ? 40.877  17.345  69.619  1.00 78.39  ? 146 LEU B CB    1 
ATOM   5099 C  CG    . LEU B 1 119 ? 41.493  16.334  70.587  1.00 82.33  ? 146 LEU B CG    1 
ATOM   5100 C  CD1   . LEU B 1 119 ? 42.567  15.518  69.894  1.00 80.74  ? 146 LEU B CD1   1 
ATOM   5101 C  CD2   . LEU B 1 119 ? 42.055  17.043  71.808  1.00 75.89  ? 146 LEU B CD2   1 
ATOM   5102 N  N     . ARG B 1 120 ? 39.149  19.448  68.184  1.00 72.98  ? 147 ARG B N     1 
ATOM   5103 C  CA    . ARG B 1 120 ? 38.968  20.641  67.359  1.00 72.69  ? 147 ARG B CA    1 
ATOM   5104 C  C     . ARG B 1 120 ? 38.162  21.699  68.097  1.00 68.46  ? 147 ARG B C     1 
ATOM   5105 O  O     . ARG B 1 120 ? 38.440  22.898  67.980  1.00 65.95  ? 147 ARG B O     1 
ATOM   5106 C  CB    . ARG B 1 120 ? 38.288  20.280  66.039  1.00 73.11  ? 147 ARG B CB    1 
ATOM   5107 C  CG    . ARG B 1 120 ? 39.085  19.319  65.184  1.00 71.62  ? 147 ARG B CG    1 
ATOM   5108 C  CD    . ARG B 1 120 ? 38.853  19.557  63.703  1.00 67.35  ? 147 ARG B CD    1 
ATOM   5109 N  NE    . ARG B 1 120 ? 39.612  18.611  62.892  1.00 74.19  ? 147 ARG B NE    1 
ATOM   5110 C  CZ    . ARG B 1 120 ? 39.147  17.438  62.489  1.00 73.48  ? 147 ARG B CZ    1 
ATOM   5111 N  NH1   . ARG B 1 120 ? 37.912  17.052  62.768  1.00 89.67  ? 147 ARG B NH1   1 
ATOM   5112 N  NH2   . ARG B 1 120 ? 39.941  16.628  61.797  1.00 81.47  ? 147 ARG B NH2   1 
ATOM   5113 N  N     . GLN B 1 121 ? 37.172  21.269  68.882  1.00 71.28  ? 148 GLN B N     1 
ATOM   5114 C  CA    . GLN B 1 121 ? 36.425  22.204  69.713  1.00 68.51  ? 148 GLN B CA    1 
ATOM   5115 C  C     . GLN B 1 121 ? 37.330  22.868  70.741  1.00 65.99  ? 148 GLN B C     1 
ATOM   5116 O  O     . GLN B 1 121 ? 37.241  24.080  70.968  1.00 69.99  ? 148 GLN B O     1 
ATOM   5117 C  CB    . GLN B 1 121 ? 35.276  21.476  70.406  1.00 64.21  ? 148 GLN B CB    1 
ATOM   5118 C  CG    . GLN B 1 121 ? 34.461  22.367  71.305  1.00 53.94  ? 148 GLN B CG    1 
ATOM   5119 C  CD    . GLN B 1 121 ? 33.745  23.435  70.531  1.00 65.39  ? 148 GLN B CD    1 
ATOM   5120 O  OE1   . GLN B 1 121 ? 33.366  23.230  69.376  1.00 77.51  ? 148 GLN B OE1   1 
ATOM   5121 N  NE2   . GLN B 1 121 ? 33.562  24.592  71.151  1.00 63.94  ? 148 GLN B NE2   1 
ATOM   5122 N  N     . ALA B 1 122 ? 38.204  22.086  71.379  1.00 74.14  ? 149 ALA B N     1 
ATOM   5123 C  CA    . ALA B 1 122 ? 39.127  22.647  72.359  1.00 66.10  ? 149 ALA B CA    1 
ATOM   5124 C  C     . ALA B 1 122 ? 40.031  23.692  71.722  1.00 66.46  ? 149 ALA B C     1 
ATOM   5125 O  O     . ALA B 1 122 ? 40.251  24.766  72.295  1.00 72.40  ? 149 ALA B O     1 
ATOM   5126 C  CB    . ALA B 1 122 ? 39.958  21.531  72.993  1.00 58.62  ? 149 ALA B CB    1 
ATOM   5127 N  N     . ALA B 1 123 ? 40.558  23.396  70.531  1.00 64.98  ? 150 ALA B N     1 
ATOM   5128 C  CA    . ALA B 1 123 ? 41.362  24.375  69.809  1.00 71.53  ? 150 ALA B CA    1 
ATOM   5129 C  C     . ALA B 1 123 ? 40.537  25.602  69.444  1.00 70.73  ? 150 ALA B C     1 
ATOM   5130 O  O     . ALA B 1 123 ? 41.019  26.736  69.541  1.00 65.11  ? 150 ALA B O     1 
ATOM   5131 C  CB    . ALA B 1 123 ? 41.959  23.736  68.556  1.00 59.58  ? 150 ALA B CB    1 
ATOM   5132 N  N     . LEU B 1 124 ? 39.290  25.393  69.017  1.00 72.53  ? 151 LEU B N     1 
ATOM   5133 C  CA    . LEU B 1 124 ? 38.402  26.513  68.721  1.00 64.60  ? 151 LEU B CA    1 
ATOM   5134 C  C     . LEU B 1 124 ? 38.199  27.391  69.951  1.00 74.87  ? 151 LEU B C     1 
ATOM   5135 O  O     . LEU B 1 124 ? 38.292  28.622  69.873  1.00 69.37  ? 151 LEU B O     1 
ATOM   5136 C  CB    . LEU B 1 124 ? 37.061  25.989  68.202  1.00 66.09  ? 151 LEU B CB    1 
ATOM   5137 C  CG    . LEU B 1 124 ? 36.023  27.057  67.858  1.00 65.79  ? 151 LEU B CG    1 
ATOM   5138 C  CD1   . LEU B 1 124 ? 36.541  27.944  66.743  1.00 58.72  ? 151 LEU B CD1   1 
ATOM   5139 C  CD2   . LEU B 1 124 ? 34.700  26.430  67.474  1.00 69.94  ? 151 LEU B CD2   1 
ATOM   5140 N  N     . LYS B 1 125 ? 37.913  26.771  71.098  1.00 67.69  ? 152 LYS B N     1 
ATOM   5141 C  CA    . LYS B 1 125 ? 37.772  27.536  72.332  1.00 66.68  ? 152 LYS B CA    1 
ATOM   5142 C  C     . LYS B 1 125 ? 39.074  28.231  72.696  1.00 67.81  ? 152 LYS B C     1 
ATOM   5143 O  O     . LYS B 1 125 ? 39.071  29.404  73.086  1.00 74.73  ? 152 LYS B O     1 
ATOM   5144 C  CB    . LYS B 1 125 ? 37.320  26.621  73.470  1.00 63.63  ? 152 LYS B CB    1 
ATOM   5145 C  CG    . LYS B 1 125 ? 37.276  27.291  74.840  1.00 59.47  ? 152 LYS B CG    1 
ATOM   5146 C  CD    . LYS B 1 125 ? 36.828  26.303  75.912  1.00 67.62  ? 152 LYS B CD    1 
ATOM   5147 C  CE    . LYS B 1 125 ? 37.131  26.814  77.309  1.00 58.80  ? 152 LYS B CE    1 
ATOM   5148 N  NZ    . LYS B 1 125 ? 36.403  28.077  77.617  1.00 99.29  ? 152 LYS B NZ    1 
ATOM   5149 N  N     . SER B 1 126 ? 40.199  27.524  72.567  1.00 69.08  ? 153 SER B N     1 
ATOM   5150 C  CA    . SER B 1 126 ? 41.486  28.112  72.916  1.00 67.22  ? 153 SER B CA    1 
ATOM   5151 C  C     . SER B 1 126 ? 41.769  29.348  72.073  1.00 68.67  ? 153 SER B C     1 
ATOM   5152 O  O     . SER B 1 126 ? 42.289  30.349  72.580  1.00 69.91  ? 153 SER B O     1 
ATOM   5153 C  CB    . SER B 1 126 ? 42.595  27.071  72.754  1.00 64.03  ? 153 SER B CB    1 
ATOM   5154 O  OG    . SER B 1 126 ? 43.800  27.504  73.361  1.00 94.64  ? 153 SER B OG    1 
ATOM   5155 N  N     . ALA B 1 127 ? 41.429  29.299  70.783  1.00 65.99  ? 154 ALA B N     1 
ATOM   5156 C  CA    . ALA B 1 127 ? 41.576  30.477  69.937  1.00 61.41  ? 154 ALA B CA    1 
ATOM   5157 C  C     . ALA B 1 127 ? 40.692  31.616  70.425  1.00 69.87  ? 154 ALA B C     1 
ATOM   5158 O  O     . ALA B 1 127 ? 41.135  32.768  70.492  1.00 74.63  ? 154 ALA B O     1 
ATOM   5159 C  CB    . ALA B 1 127 ? 41.248  30.126  68.487  1.00 64.73  ? 154 ALA B CB    1 
ATOM   5160 N  N     . ARG B 1 128 ? 39.441  31.311  70.783  1.00 69.66  ? 155 ARG B N     1 
ATOM   5161 C  CA    . ARG B 1 128 ? 38.543  32.350  71.279  1.00 61.20  ? 155 ARG B CA    1 
ATOM   5162 C  C     . ARG B 1 128 ? 39.073  32.974  72.564  1.00 69.98  ? 155 ARG B C     1 
ATOM   5163 O  O     . ARG B 1 128 ? 39.015  34.197  72.739  1.00 85.29  ? 155 ARG B O     1 
ATOM   5164 C  CB    . ARG B 1 128 ? 37.144  31.780  71.510  1.00 58.97  ? 155 ARG B CB    1 
ATOM   5165 C  CG    . ARG B 1 128 ? 36.403  31.353  70.256  1.00 60.49  ? 155 ARG B CG    1 
ATOM   5166 C  CD    . ARG B 1 128 ? 34.915  31.253  70.547  1.00 61.31  ? 155 ARG B CD    1 
ATOM   5167 N  NE    . ARG B 1 128 ? 34.143  30.806  69.394  1.00 77.90  ? 155 ARG B NE    1 
ATOM   5168 C  CZ    . ARG B 1 128 ? 33.514  29.641  69.321  1.00 74.03  ? 155 ARG B CZ    1 
ATOM   5169 N  NH1   . ARG B 1 128 ? 33.547  28.774  70.321  1.00 74.08  ? 155 ARG B NH1   1 
ATOM   5170 N  NH2   . ARG B 1 128 ? 32.826  29.342  68.221  1.00 72.72  ? 155 ARG B NH2   1 
ATOM   5171 N  N     . ASP B 1 129 ? 39.591  32.151  73.478  1.00 68.66  ? 156 ASP B N     1 
ATOM   5172 C  CA    . ASP B 1 129 ? 40.019  32.670  74.772  1.00 72.49  ? 156 ASP B CA    1 
ATOM   5173 C  C     . ASP B 1 129 ? 41.249  33.562  74.650  1.00 69.02  ? 156 ASP B C     1 
ATOM   5174 O  O     . ASP B 1 129 ? 41.392  34.520  75.420  1.00 71.59  ? 156 ASP B O     1 
ATOM   5175 C  CB    . ASP B 1 129 ? 40.290  31.513  75.732  1.00 73.40  ? 156 ASP B CB    1 
ATOM   5176 C  CG    . ASP B 1 129 ? 39.046  30.690  76.022  1.00 79.39  ? 156 ASP B CG    1 
ATOM   5177 O  OD1   . ASP B 1 129 ? 37.941  31.116  75.613  1.00 83.93  ? 156 ASP B OD1   1 
ATOM   5178 O  OD2   . ASP B 1 129 ? 39.175  29.616  76.651  1.00 81.27  ? 156 ASP B OD2   1 
ATOM   5179 N  N     . MET B 1 130 ? 42.141  33.275  73.699  1.00 72.47  ? 157 MET B N     1 
ATOM   5180 C  CA    . MET B 1 130 ? 43.355  34.055  73.502  1.00 64.72  ? 157 MET B CA    1 
ATOM   5181 C  C     . MET B 1 130 ? 43.150  35.230  72.554  1.00 66.52  ? 157 MET B C     1 
ATOM   5182 O  O     . MET B 1 130 ? 44.126  35.902  72.203  1.00 72.71  ? 157 MET B O     1 
ATOM   5183 C  CB    . MET B 1 130 ? 44.483  33.160  72.979  1.00 69.71  ? 157 MET B CB    1 
ATOM   5184 C  CG    . MET B 1 130 ? 44.332  32.728  71.535  1.00 63.72  ? 157 MET B CG    1 
ATOM   5185 S  SD    . MET B 1 130 ? 45.731  31.737  70.988  1.00 81.24  ? 157 MET B SD    1 
ATOM   5186 C  CE    . MET B 1 130 ? 47.074  32.584  71.811  1.00 78.20  ? 157 MET B CE    1 
ATOM   5187 N  N     . TRP B 1 131 ? 41.908  35.472  72.123  1.00 62.74  ? 158 TRP B N     1 
ATOM   5188 C  CA    . TRP B 1 131 ? 41.538  36.657  71.346  1.00 66.64  ? 158 TRP B CA    1 
ATOM   5189 C  C     . TRP B 1 131 ? 42.228  36.685  69.985  1.00 69.33  ? 158 TRP B C     1 
ATOM   5190 O  O     . TRP B 1 131 ? 42.676  37.733  69.518  1.00 75.48  ? 158 TRP B O     1 
ATOM   5191 C  CB    . TRP B 1 131 ? 41.823  37.941  72.128  1.00 63.08  ? 158 TRP B CB    1 
ATOM   5192 C  CG    . TRP B 1 131 ? 40.620  38.490  72.835  1.00 70.63  ? 158 TRP B CG    1 
ATOM   5193 C  CD1   . TRP B 1 131 ? 39.329  38.060  72.714  1.00 62.82  ? 158 TRP B CD1   1 
ATOM   5194 C  CD2   . TRP B 1 131 ? 40.594  39.581  73.764  1.00 70.85  ? 158 TRP B CD2   1 
ATOM   5195 N  NE1   . TRP B 1 131 ? 38.504  38.812  73.516  1.00 69.99  ? 158 TRP B NE1   1 
ATOM   5196 C  CE2   . TRP B 1 131 ? 39.257  39.751  74.172  1.00 66.86  ? 158 TRP B CE2   1 
ATOM   5197 C  CE3   . TRP B 1 131 ? 41.573  40.430  74.292  1.00 67.51  ? 158 TRP B CE3   1 
ATOM   5198 C  CZ2   . TRP B 1 131 ? 38.874  40.734  75.080  1.00 73.45  ? 158 TRP B CZ2   1 
ATOM   5199 C  CZ3   . TRP B 1 131 ? 41.193  41.400  75.199  1.00 69.04  ? 158 TRP B CZ3   1 
ATOM   5200 C  CH2   . TRP B 1 131 ? 39.856  41.545  75.583  1.00 78.66  ? 158 TRP B CH2   1 
ATOM   5201 N  N     . ALA B 1 132 ? 42.301  35.530  69.334  1.00 69.87  ? 159 ALA B N     1 
ATOM   5202 C  CA    . ALA B 1 132 ? 42.855  35.464  67.992  1.00 66.98  ? 159 ALA B CA    1 
ATOM   5203 C  C     . ALA B 1 132 ? 41.825  35.912  66.960  1.00 71.27  ? 159 ALA B C     1 
ATOM   5204 O  O     . ALA B 1 132 ? 40.612  35.790  67.161  1.00 68.87  ? 159 ALA B O     1 
ATOM   5205 C  CB    . ALA B 1 132 ? 43.329  34.045  67.674  1.00 56.81  ? 159 ALA B CB    1 
ATOM   5206 N  N     . ASP B 1 133 ? 42.327  36.450  65.849  1.00 68.71  ? 160 ASP B N     1 
ATOM   5207 C  CA    . ASP B 1 133 ? 41.460  36.810  64.733  1.00 66.54  ? 160 ASP B CA    1 
ATOM   5208 C  C     . ASP B 1 133 ? 41.001  35.580  63.965  1.00 70.89  ? 160 ASP B C     1 
ATOM   5209 O  O     . ASP B 1 133 ? 39.821  35.470  63.610  1.00 68.70  ? 160 ASP B O     1 
ATOM   5210 C  CB    . ASP B 1 133 ? 42.191  37.759  63.787  1.00 64.38  ? 160 ASP B CB    1 
ATOM   5211 C  CG    . ASP B 1 133 ? 42.578  39.053  64.450  1.00 72.09  ? 160 ASP B CG    1 
ATOM   5212 O  OD1   . ASP B 1 133 ? 41.743  39.612  65.201  1.00 64.02  ? 160 ASP B OD1   1 
ATOM   5213 O  OD2   . ASP B 1 133 ? 43.722  39.500  64.220  1.00 74.66  ? 160 ASP B OD2   1 
ATOM   5214 N  N     . TYR B 1 134 ? 41.925  34.659  63.693  1.00 66.15  ? 161 TYR B N     1 
ATOM   5215 C  CA    . TYR B 1 134 ? 41.663  33.479  62.889  1.00 68.63  ? 161 TYR B CA    1 
ATOM   5216 C  C     . TYR B 1 134 ? 42.185  32.244  63.601  1.00 72.37  ? 161 TYR B C     1 
ATOM   5217 O  O     . TYR B 1 134 ? 43.117  32.320  64.407  1.00 68.61  ? 161 TYR B O     1 
ATOM   5218 C  CB    . TYR B 1 134 ? 42.331  33.571  61.511  1.00 69.02  ? 161 TYR B CB    1 
ATOM   5219 C  CG    . TYR B 1 134 ? 41.866  34.729  60.662  1.00 72.39  ? 161 TYR B CG    1 
ATOM   5220 C  CD1   . TYR B 1 134 ? 40.783  34.594  59.802  1.00 71.31  ? 161 TYR B CD1   1 
ATOM   5221 C  CD2   . TYR B 1 134 ? 42.516  35.953  60.711  1.00 58.91  ? 161 TYR B CD2   1 
ATOM   5222 C  CE1   . TYR B 1 134 ? 40.355  35.651  59.019  1.00 77.22  ? 161 TYR B CE1   1 
ATOM   5223 C  CE2   . TYR B 1 134 ? 42.096  37.015  59.931  1.00 73.12  ? 161 TYR B CE2   1 
ATOM   5224 C  CZ    . TYR B 1 134 ? 41.015  36.859  59.088  1.00 74.21  ? 161 TYR B CZ    1 
ATOM   5225 O  OH    . TYR B 1 134 ? 40.592  37.914  58.312  1.00 81.31  ? 161 TYR B OH    1 
ATOM   5226 N  N     . ILE B 1 135 ? 41.573  31.102  63.290  1.00 72.62  ? 162 ILE B N     1 
ATOM   5227 C  CA    . ILE B 1 135 ? 42.112  29.792  63.634  1.00 63.32  ? 162 ILE B CA    1 
ATOM   5228 C  C     . ILE B 1 135 ? 42.275  29.008  62.341  1.00 67.27  ? 162 ILE B C     1 
ATOM   5229 O  O     . ILE B 1 135 ? 41.371  28.994  61.496  1.00 64.75  ? 162 ILE B O     1 
ATOM   5230 C  CB    . ILE B 1 135 ? 41.227  29.034  64.641  1.00 69.79  ? 162 ILE B CB    1 
ATOM   5231 C  CG1   . ILE B 1 135 ? 41.796  27.638  64.903  1.00 60.99  ? 162 ILE B CG1   1 
ATOM   5232 C  CG2   . ILE B 1 135 ? 39.792  28.942  64.157  1.00 54.76  ? 162 ILE B CG2   1 
ATOM   5233 C  CD1   . ILE B 1 135 ? 41.263  26.995  66.165  1.00 61.73  ? 162 ILE B CD1   1 
ATOM   5234 N  N     . LEU B 1 136 ? 43.440  28.388  62.174  1.00 70.05  ? 163 LEU B N     1 
ATOM   5235 C  CA    . LEU B 1 136 ? 43.786  27.648  60.965  1.00 64.90  ? 163 LEU B CA    1 
ATOM   5236 C  C     . LEU B 1 136 ? 44.034  26.197  61.347  1.00 63.79  ? 163 LEU B C     1 
ATOM   5237 O  O     . LEU B 1 136 ? 44.996  25.892  62.062  1.00 62.62  ? 163 LEU B O     1 
ATOM   5238 C  CB    . LEU B 1 136 ? 45.018  28.247  60.288  1.00 58.04  ? 163 LEU B CB    1 
ATOM   5239 C  CG    . LEU B 1 136 ? 45.579  27.426  59.129  1.00 69.23  ? 163 LEU B CG    1 
ATOM   5240 C  CD1   . LEU B 1 136 ? 44.735  27.626  57.885  1.00 55.28  ? 163 LEU B CD1   1 
ATOM   5241 C  CD2   . LEU B 1 136 ? 47.036  27.777  58.873  1.00 62.79  ? 163 LEU B CD2   1 
ATOM   5242 N  N     . PHE B 1 137 ? 43.163  25.306  60.885  1.00 73.01  ? 164 PHE B N     1 
ATOM   5243 C  CA    . PHE B 1 137 ? 43.362  23.878  61.074  1.00 57.17  ? 164 PHE B CA    1 
ATOM   5244 C  C     . PHE B 1 137 ? 44.168  23.341  59.903  1.00 58.62  ? 164 PHE B C     1 
ATOM   5245 O  O     . PHE B 1 137 ? 43.849  23.618  58.745  1.00 71.24  ? 164 PHE B O     1 
ATOM   5246 C  CB    . PHE B 1 137 ? 42.026  23.143  61.180  1.00 57.83  ? 164 PHE B CB    1 
ATOM   5247 C  CG    . PHE B 1 137 ? 41.267  23.439  62.444  1.00 59.57  ? 164 PHE B CG    1 
ATOM   5248 C  CD1   . PHE B 1 137 ? 41.465  22.676  63.580  1.00 47.76  ? 164 PHE B CD1   1 
ATOM   5249 C  CD2   . PHE B 1 137 ? 40.353  24.475  62.490  1.00 64.76  ? 164 PHE B CD2   1 
ATOM   5250 C  CE1   . PHE B 1 137 ? 40.769  22.940  64.735  1.00 65.26  ? 164 PHE B CE1   1 
ATOM   5251 C  CE2   . PHE B 1 137 ? 39.649  24.747  63.647  1.00 65.90  ? 164 PHE B CE2   1 
ATOM   5252 C  CZ    . PHE B 1 137 ? 39.857  23.979  64.772  1.00 68.79  ? 164 PHE B CZ    1 
ATOM   5253 N  N     . VAL B 1 138 ? 45.233  22.606  60.208  1.00 72.50  ? 165 VAL B N     1 
ATOM   5254 C  CA    . VAL B 1 138 ? 46.029  21.917  59.200  1.00 59.44  ? 165 VAL B CA    1 
ATOM   5255 C  C     . VAL B 1 138 ? 46.170  20.468  59.641  1.00 71.72  ? 165 VAL B C     1 
ATOM   5256 O  O     . VAL B 1 138 ? 46.732  20.196  60.709  1.00 77.32  ? 165 VAL B O     1 
ATOM   5257 C  CB    . VAL B 1 138 ? 47.409  22.565  59.005  1.00 62.63  ? 165 VAL B CB    1 
ATOM   5258 C  CG1   . VAL B 1 138 ? 48.087  21.997  57.774  1.00 63.61  ? 165 VAL B CG1   1 
ATOM   5259 C  CG2   . VAL B 1 138 ? 47.277  24.076  58.894  1.00 70.36  ? 165 VAL B CG2   1 
ATOM   5260 N  N     . ASP B 1 139 ? 45.629  19.546  58.844  1.00 71.15  ? 166 ASP B N     1 
ATOM   5261 C  CA    . ASP B 1 139 ? 45.818  18.128  59.124  1.00 76.62  ? 166 ASP B CA    1 
ATOM   5262 C  C     . ASP B 1 139 ? 47.294  17.776  59.047  1.00 70.87  ? 166 ASP B C     1 
ATOM   5263 O  O     . ASP B 1 139 ? 48.031  18.310  58.214  1.00 76.61  ? 166 ASP B O     1 
ATOM   5264 C  CB    . ASP B 1 139 ? 45.027  17.272  58.141  1.00 87.74  ? 166 ASP B CB    1 
ATOM   5265 C  CG    . ASP B 1 139 ? 43.575  17.117  58.539  1.00 97.25  ? 166 ASP B CG    1 
ATOM   5266 O  OD1   . ASP B 1 139 ? 43.154  17.720  59.550  1.00 87.10  ? 166 ASP B OD1   1 
ATOM   5267 O  OD2   . ASP B 1 139 ? 42.857  16.381  57.827  1.00 108.65 ? 166 ASP B OD2   1 
ATOM   5268 N  N     . ALA B 1 140 ? 47.723  16.864  59.922  1.00 71.71  ? 167 ALA B N     1 
ATOM   5269 C  CA    . ALA B 1 140 ? 49.150  16.599  60.067  1.00 74.98  ? 167 ALA B CA    1 
ATOM   5270 C  C     . ALA B 1 140 ? 49.777  16.100  58.771  1.00 66.64  ? 167 ALA B C     1 
ATOM   5271 O  O     . ALA B 1 140 ? 50.983  16.265  58.569  1.00 76.59  ? 167 ALA B O     1 
ATOM   5272 C  CB    . ALA B 1 140 ? 49.381  15.590  61.194  1.00 73.52  ? 167 ALA B CB    1 
ATOM   5273 N  N     . ASP B 1 141 ? 48.991  15.484  57.887  1.00 67.97  ? 168 ASP B N     1 
ATOM   5274 C  CA    . ASP B 1 141 ? 49.501  15.005  56.609  1.00 73.90  ? 168 ASP B CA    1 
ATOM   5275 C  C     . ASP B 1 141 ? 49.190  15.958  55.458  1.00 81.51  ? 168 ASP B C     1 
ATOM   5276 O  O     . ASP B 1 141 ? 49.267  15.554  54.294  1.00 84.68  ? 168 ASP B O     1 
ATOM   5277 C  CB    . ASP B 1 141 ? 48.972  13.596  56.308  1.00 69.00  ? 168 ASP B CB    1 
ATOM   5278 C  CG    . ASP B 1 141 ? 47.451  13.532  56.195  1.00 70.88  ? 168 ASP B CG    1 
ATOM   5279 O  OD1   . ASP B 1 141 ? 46.770  14.538  56.465  1.00 103.76 ? 168 ASP B OD1   1 
ATOM   5280 O  OD2   . ASP B 1 141 ? 46.923  12.464  55.833  1.00 84.72  ? 168 ASP B OD2   1 
ATOM   5281 N  N     . ASN B 1 142 ? 48.861  17.215  55.758  1.00 79.13  ? 169 ASN B N     1 
ATOM   5282 C  CA    . ASN B 1 142 ? 48.549  18.216  54.742  1.00 76.64  ? 169 ASN B CA    1 
ATOM   5283 C  C     . ASN B 1 142 ? 49.750  19.129  54.534  1.00 80.46  ? 169 ASN B C     1 
ATOM   5284 O  O     . ASN B 1 142 ? 50.196  19.806  55.469  1.00 80.91  ? 169 ASN B O     1 
ATOM   5285 C  CB    . ASN B 1 142 ? 47.320  19.035  55.136  1.00 75.70  ? 169 ASN B CB    1 
ATOM   5286 C  CG    . ASN B 1 142 ? 46.043  18.232  55.061  1.00 79.20  ? 169 ASN B CG    1 
ATOM   5287 O  OD1   . ASN B 1 142 ? 46.072  17.006  55.090  1.00 96.70  ? 169 ASN B OD1   1 
ATOM   5288 N  ND2   . ASN B 1 142 ? 44.913  18.918  54.971  1.00 71.59  ? 169 ASN B ND2   1 
ATOM   5289 N  N     . LEU B 1 143 ? 50.249  19.163  53.303  1.00 76.12  ? 170 LEU B N     1 
ATOM   5290 C  CA    . LEU B 1 143 ? 51.467  19.889  52.956  1.00 73.29  ? 170 LEU B CA    1 
ATOM   5291 C  C     . LEU B 1 143 ? 51.079  21.241  52.367  1.00 70.01  ? 170 LEU B C     1 
ATOM   5292 O  O     . LEU B 1 143 ? 50.660  21.329  51.212  1.00 72.71  ? 170 LEU B O     1 
ATOM   5293 C  CB    . LEU B 1 143 ? 52.303  19.079  51.974  1.00 60.38  ? 170 LEU B CB    1 
ATOM   5294 C  CG    . LEU B 1 143 ? 53.603  19.726  51.509  1.00 74.56  ? 170 LEU B CG    1 
ATOM   5295 C  CD1   . LEU B 1 143 ? 54.480  20.063  52.711  1.00 73.72  ? 170 LEU B CD1   1 
ATOM   5296 C  CD2   . LEU B 1 143 ? 54.329  18.806  50.543  1.00 82.32  ? 170 LEU B CD2   1 
ATOM   5297 N  N     . ILE B 1 144 ? 51.233  22.303  53.156  1.00 70.13  ? 171 ILE B N     1 
ATOM   5298 C  CA    . ILE B 1 144 ? 50.888  23.657  52.706  1.00 70.04  ? 171 ILE B CA    1 
ATOM   5299 C  C     . ILE B 1 144 ? 52.122  24.198  51.990  1.00 68.56  ? 171 ILE B C     1 
ATOM   5300 O  O     . ILE B 1 144 ? 52.971  24.870  52.579  1.00 72.21  ? 171 ILE B O     1 
ATOM   5301 C  CB    . ILE B 1 144 ? 50.437  24.547  53.862  1.00 70.57  ? 171 ILE B CB    1 
ATOM   5302 C  CG1   . ILE B 1 144 ? 49.355  23.836  54.684  1.00 72.49  ? 171 ILE B CG1   1 
ATOM   5303 C  CG2   . ILE B 1 144 ? 49.925  25.880  53.342  1.00 69.88  ? 171 ILE B CG2   1 
ATOM   5304 C  CD1   . ILE B 1 144 ? 48.157  23.367  53.869  1.00 61.74  ? 171 ILE B CD1   1 
ATOM   5305 N  N     . LEU B 1 145 ? 52.218  23.897  50.691  1.00 82.34  ? 172 LEU B N     1 
ATOM   5306 C  CA    . LEU B 1 145 ? 53.440  24.181  49.941  1.00 81.51  ? 172 LEU B CA    1 
ATOM   5307 C  C     . LEU B 1 145 ? 53.617  25.676  49.698  1.00 76.12  ? 172 LEU B C     1 
ATOM   5308 O  O     . LEU B 1 145 ? 54.725  26.204  49.842  1.00 83.23  ? 172 LEU B O     1 
ATOM   5309 C  CB    . LEU B 1 145 ? 53.425  23.422  48.614  1.00 78.50  ? 172 LEU B CB    1 
ATOM   5310 C  CG    . LEU B 1 145 ? 54.774  23.153  47.948  1.00 84.28  ? 172 LEU B CG    1 
ATOM   5311 C  CD1   . LEU B 1 145 ? 55.588  22.185  48.788  1.00 77.92  ? 172 LEU B CD1   1 
ATOM   5312 C  CD2   . LEU B 1 145 ? 54.589  22.619  46.533  1.00 80.20  ? 172 LEU B CD2   1 
ATOM   5313 N  N     . ASN B 1 146 ? 52.550  26.366  49.327  1.00 71.22  ? 173 ASN B N     1 
ATOM   5314 C  CA    . ASN B 1 146 ? 52.583  27.801  49.071  1.00 59.10  ? 173 ASN B CA    1 
ATOM   5315 C  C     . ASN B 1 146 ? 52.731  28.569  50.379  1.00 67.52  ? 173 ASN B C     1 
ATOM   5316 O  O     . ASN B 1 146 ? 51.790  28.577  51.185  1.00 72.90  ? 173 ASN B O     1 
ATOM   5317 C  CB    . ASN B 1 146 ? 51.300  28.216  48.343  1.00 77.91  ? 173 ASN B CB    1 
ATOM   5318 C  CG    . ASN B 1 146 ? 51.299  29.676  47.919  1.00 76.93  ? 173 ASN B CG    1 
ATOM   5319 O  OD1   . ASN B 1 146 ? 52.079  30.488  48.418  1.00 84.84  ? 173 ASN B OD1   1 
ATOM   5320 N  ND2   . ASN B 1 146 ? 50.406  30.018  46.993  1.00 78.24  ? 173 ASN B ND2   1 
ATOM   5321 N  N     . PRO B 1 147 ? 53.857  29.245  50.625  1.00 67.72  ? 174 PRO B N     1 
ATOM   5322 C  CA    . PRO B 1 147 ? 54.014  29.969  51.896  1.00 67.14  ? 174 PRO B CA    1 
ATOM   5323 C  C     . PRO B 1 147 ? 53.060  31.140  52.052  1.00 68.11  ? 174 PRO B C     1 
ATOM   5324 O  O     . PRO B 1 147 ? 52.988  31.712  53.148  1.00 75.04  ? 174 PRO B O     1 
ATOM   5325 C  CB    . PRO B 1 147 ? 55.473  30.453  51.853  1.00 74.26  ? 174 PRO B CB    1 
ATOM   5326 C  CG    . PRO B 1 147 ? 56.121  29.706  50.720  1.00 52.58  ? 174 PRO B CG    1 
ATOM   5327 C  CD    . PRO B 1 147 ? 55.020  29.426  49.745  1.00 65.51  ? 174 PRO B CD    1 
ATOM   5328 N  N     . ASP B 1 148 ? 52.335  31.515  50.999  1.00 71.73  ? 175 ASP B N     1 
ATOM   5329 C  CA    . ASP B 1 148 ? 51.398  32.629  51.036  1.00 80.78  ? 175 ASP B CA    1 
ATOM   5330 C  C     . ASP B 1 148 ? 49.957  32.182  51.226  1.00 79.39  ? 175 ASP B C     1 
ATOM   5331 O  O     . ASP B 1 148 ? 49.052  33.021  51.174  1.00 68.45  ? 175 ASP B O     1 
ATOM   5332 C  CB    . ASP B 1 148 ? 51.513  33.455  49.753  1.00 72.79  ? 175 ASP B CB    1 
ATOM   5333 C  CG    . ASP B 1 148 ? 52.869  34.111  49.607  1.00 85.02  ? 175 ASP B CG    1 
ATOM   5334 O  OD1   . ASP B 1 148 ? 53.399  34.610  50.624  1.00 87.30  ? 175 ASP B OD1   1 
ATOM   5335 O  OD2   . ASP B 1 148 ? 53.406  34.119  48.479  1.00 81.31  ? 175 ASP B OD2   1 
ATOM   5336 N  N     . THR B 1 149 ? 49.727  30.884  51.444  1.00 78.00  ? 176 THR B N     1 
ATOM   5337 C  CA    . THR B 1 149 ? 48.363  30.368  51.531  1.00 68.99  ? 176 THR B CA    1 
ATOM   5338 C  C     . THR B 1 149 ? 47.583  31.057  52.644  1.00 68.12  ? 176 THR B C     1 
ATOM   5339 O  O     . THR B 1 149 ? 46.445  31.493  52.442  1.00 68.06  ? 176 THR B O     1 
ATOM   5340 C  CB    . THR B 1 149 ? 48.388  28.855  51.753  1.00 72.77  ? 176 THR B CB    1 
ATOM   5341 O  OG1   . THR B 1 149 ? 49.310  28.252  50.838  1.00 79.57  ? 176 THR B OG1   1 
ATOM   5342 C  CG2   . THR B 1 149 ? 47.009  28.263  51.524  1.00 70.57  ? 176 THR B CG2   1 
ATOM   5343 N  N     . LEU B 1 150 ? 48.188  31.177  53.827  1.00 72.56  ? 177 LEU B N     1 
ATOM   5344 C  CA    . LEU B 1 150 ? 47.487  31.785  54.953  1.00 64.66  ? 177 LEU B CA    1 
ATOM   5345 C  C     . LEU B 1 150 ? 47.133  33.237  54.663  1.00 71.63  ? 177 LEU B C     1 
ATOM   5346 O  O     . LEU B 1 150 ? 46.008  33.675  54.933  1.00 75.99  ? 177 LEU B O     1 
ATOM   5347 C  CB    . LEU B 1 150 ? 48.336  31.668  56.220  1.00 54.04  ? 177 LEU B CB    1 
ATOM   5348 C  CG    . LEU B 1 150 ? 47.847  32.351  57.496  1.00 62.70  ? 177 LEU B CG    1 
ATOM   5349 C  CD1   . LEU B 1 150 ? 46.421  31.942  57.819  1.00 69.58  ? 177 LEU B CD1   1 
ATOM   5350 C  CD2   . LEU B 1 150 ? 48.779  32.029  58.651  1.00 60.99  ? 177 LEU B CD2   1 
ATOM   5351 N  N     . SER B 1 151 ? 48.077  33.999  54.106  1.00 73.67  ? 178 SER B N     1 
ATOM   5352 C  CA    . SER B 1 151 ? 47.782  35.379  53.734  1.00 62.38  ? 178 SER B CA    1 
ATOM   5353 C  C     . SER B 1 151 ? 46.680  35.438  52.686  1.00 68.77  ? 178 SER B C     1 
ATOM   5354 O  O     . SER B 1 151 ? 45.783  36.287  52.763  1.00 72.69  ? 178 SER B O     1 
ATOM   5355 C  CB    . SER B 1 151 ? 49.045  36.070  53.220  1.00 53.66  ? 178 SER B CB    1 
ATOM   5356 O  OG    . SER B 1 151 ? 49.989  36.240  54.262  1.00 72.48  ? 178 SER B OG    1 
ATOM   5357 N  N     . LEU B 1 152 ? 46.722  34.533  51.708  1.00 75.93  ? 179 LEU B N     1 
ATOM   5358 C  CA    . LEU B 1 152 ? 45.722  34.538  50.647  1.00 67.91  ? 179 LEU B CA    1 
ATOM   5359 C  C     . LEU B 1 152 ? 44.337  34.189  51.178  1.00 72.18  ? 179 LEU B C     1 
ATOM   5360 O  O     . LEU B 1 152 ? 43.334  34.730  50.701  1.00 79.78  ? 179 LEU B O     1 
ATOM   5361 C  CB    . LEU B 1 152 ? 46.143  33.570  49.543  1.00 70.51  ? 179 LEU B CB    1 
ATOM   5362 C  CG    . LEU B 1 152 ? 47.368  34.031  48.746  1.00 72.62  ? 179 LEU B CG    1 
ATOM   5363 C  CD1   . LEU B 1 152 ? 48.039  32.862  48.056  1.00 66.02  ? 179 LEU B CD1   1 
ATOM   5364 C  CD2   . LEU B 1 152 ? 46.974  35.095  47.741  1.00 50.91  ? 179 LEU B CD2   1 
ATOM   5365 N  N     . LEU B 1 153 ? 44.259  33.290  52.163  1.00 73.17  ? 180 LEU B N     1 
ATOM   5366 C  CA    . LEU B 1 153 ? 42.961  32.926  52.723  1.00 70.91  ? 180 LEU B CA    1 
ATOM   5367 C  C     . LEU B 1 153 ? 42.376  34.067  53.547  1.00 74.38  ? 180 LEU B C     1 
ATOM   5368 O  O     . LEU B 1 153 ? 41.162  34.297  53.524  1.00 71.87  ? 180 LEU B O     1 
ATOM   5369 C  CB    . LEU B 1 153 ? 43.091  31.656  53.564  1.00 66.68  ? 180 LEU B CB    1 
ATOM   5370 C  CG    . LEU B 1 153 ? 43.493  30.380  52.812  1.00 72.51  ? 180 LEU B CG    1 
ATOM   5371 C  CD1   . LEU B 1 153 ? 43.808  29.248  53.781  1.00 59.37  ? 180 LEU B CD1   1 
ATOM   5372 C  CD2   . LEU B 1 153 ? 42.409  29.960  51.830  1.00 66.30  ? 180 LEU B CD2   1 
ATOM   5373 N  N     . ILE B 1 154 ? 43.223  34.790  54.284  1.00 72.86  ? 181 ILE B N     1 
ATOM   5374 C  CA    . ILE B 1 154 ? 42.756  35.970  55.003  1.00 66.79  ? 181 ILE B CA    1 
ATOM   5375 C  C     . ILE B 1 154 ? 42.273  37.032  54.029  1.00 67.16  ? 181 ILE B C     1 
ATOM   5376 O  O     . ILE B 1 154 ? 41.345  37.792  54.332  1.00 65.07  ? 181 ILE B O     1 
ATOM   5377 C  CB    . ILE B 1 154 ? 43.870  36.519  55.916  1.00 66.65  ? 181 ILE B CB    1 
ATOM   5378 C  CG1   . ILE B 1 154 ? 44.271  35.486  56.967  1.00 67.67  ? 181 ILE B CG1   1 
ATOM   5379 C  CG2   . ILE B 1 154 ? 43.423  37.796  56.595  1.00 64.29  ? 181 ILE B CG2   1 
ATOM   5380 C  CD1   . ILE B 1 154 ? 45.275  36.016  57.976  1.00 62.82  ? 181 ILE B CD1   1 
ATOM   5381 N  N     . ALA B 1 155 ? 42.879  37.098  52.843  1.00 74.91  ? 182 ALA B N     1 
ATOM   5382 C  CA    . ALA B 1 155 ? 42.529  38.137  51.884  1.00 71.62  ? 182 ALA B CA    1 
ATOM   5383 C  C     . ALA B 1 155 ? 41.103  38.001  51.359  1.00 71.88  ? 182 ALA B C     1 
ATOM   5384 O  O     . ALA B 1 155 ? 40.562  38.969  50.815  1.00 79.51  ? 182 ALA B O     1 
ATOM   5385 C  CB    . ALA B 1 155 ? 43.518  38.127  50.719  1.00 70.45  ? 182 ALA B CB    1 
ATOM   5386 N  N     . GLU B 1 156 ? 40.479  36.836  51.513  1.00 69.50  ? 183 GLU B N     1 
ATOM   5387 C  CA    . GLU B 1 156 ? 39.161  36.620  50.934  1.00 69.38  ? 183 GLU B CA    1 
ATOM   5388 C  C     . GLU B 1 156 ? 38.028  37.137  51.808  1.00 64.00  ? 183 GLU B C     1 
ATOM   5389 O  O     . GLU B 1 156 ? 36.894  37.233  51.325  1.00 76.83  ? 183 GLU B O     1 
ATOM   5390 C  CB    . GLU B 1 156 ? 38.959  35.131  50.650  1.00 75.51  ? 183 GLU B CB    1 
ATOM   5391 C  CG    . GLU B 1 156 ? 39.829  34.615  49.519  1.00 76.46  ? 183 GLU B CG    1 
ATOM   5392 C  CD    . GLU B 1 156 ? 39.463  35.231  48.177  1.00 84.85  ? 183 GLU B CD    1 
ATOM   5393 O  OE1   . GLU B 1 156 ? 38.287  35.620  47.996  1.00 83.54  ? 183 GLU B OE1   1 
ATOM   5394 O  OE2   . GLU B 1 156 ? 40.350  35.317  47.299  1.00 81.54  ? 183 GLU B OE2   1 
ATOM   5395 N  N     . ASN B 1 157 ? 38.305  37.471  53.065  1.00 75.34  ? 184 ASN B N     1 
ATOM   5396 C  CA    . ASN B 1 157 ? 37.301  37.972  54.002  1.00 75.59  ? 184 ASN B CA    1 
ATOM   5397 C  C     . ASN B 1 157 ? 36.062  37.075  54.027  1.00 78.02  ? 184 ASN B C     1 
ATOM   5398 O  O     . ASN B 1 157 ? 34.924  37.535  53.910  1.00 80.25  ? 184 ASN B O     1 
ATOM   5399 C  CB    . ASN B 1 157 ? 36.927  39.419  53.680  1.00 70.34  ? 184 ASN B CB    1 
ATOM   5400 C  CG    . ASN B 1 157 ? 36.215  40.101  54.828  1.00 68.79  ? 184 ASN B CG    1 
ATOM   5401 O  OD1   . ASN B 1 157 ? 36.068  39.524  55.906  1.00 81.17  ? 184 ASN B OD1   1 
ATOM   5402 N  ND2   . ASN B 1 157 ? 35.774  41.337  54.607  1.00 71.96  ? 184 ASN B ND2   1 
ATOM   5403 N  N     . LYS B 1 158 ? 36.296  35.774  54.168  1.00 75.09  ? 185 LYS B N     1 
ATOM   5404 C  CA    . LYS B 1 158 ? 35.232  34.809  54.395  1.00 72.03  ? 185 LYS B CA    1 
ATOM   5405 C  C     . LYS B 1 158 ? 35.270  34.350  55.847  1.00 70.08  ? 185 LYS B C     1 
ATOM   5406 O  O     . LYS B 1 158 ? 36.257  34.552  56.560  1.00 89.51  ? 185 LYS B O     1 
ATOM   5407 C  CB    . LYS B 1 158 ? 35.358  33.607  53.452  1.00 70.41  ? 185 LYS B CB    1 
ATOM   5408 C  CG    . LYS B 1 158 ? 35.424  33.973  51.975  1.00 71.22  ? 185 LYS B CG    1 
ATOM   5409 C  CD    . LYS B 1 158 ? 34.154  34.653  51.508  1.00 75.69  ? 185 LYS B CD    1 
ATOM   5410 C  CE    . LYS B 1 158 ? 34.310  35.195  50.098  1.00 81.59  ? 185 LYS B CE    1 
ATOM   5411 N  NZ    . LYS B 1 158 ? 33.202  36.132  49.746  1.00 92.28  ? 185 LYS B NZ    1 
ATOM   5412 N  N     . THR B 1 159 ? 34.174  33.735  56.291  1.00 76.32  ? 186 THR B N     1 
ATOM   5413 C  CA    . THR B 1 159 ? 34.105  33.279  57.675  1.00 68.78  ? 186 THR B CA    1 
ATOM   5414 C  C     . THR B 1 159 ? 34.672  31.873  57.838  1.00 70.85  ? 186 THR B C     1 
ATOM   5415 O  O     . THR B 1 159 ? 35.370  31.596  58.818  1.00 74.77  ? 186 THR B O     1 
ATOM   5416 C  CB    . THR B 1 159 ? 32.660  33.344  58.181  1.00 68.13  ? 186 THR B CB    1 
ATOM   5417 O  OG1   . THR B 1 159 ? 32.155  34.674  58.000  1.00 80.03  ? 186 THR B OG1   1 
ATOM   5418 C  CG2   . THR B 1 159 ? 32.587  32.995  59.655  1.00 62.55  ? 186 THR B CG2   1 
ATOM   5419 N  N     . VAL B 1 160 ? 34.393  30.981  56.892  1.00 71.76  ? 187 VAL B N     1 
ATOM   5420 C  CA    . VAL B 1 160 ? 35.045  29.678  56.801  1.00 64.54  ? 187 VAL B CA    1 
ATOM   5421 C  C     . VAL B 1 160 ? 35.503  29.518  55.359  1.00 72.70  ? 187 VAL B C     1 
ATOM   5422 O  O     . VAL B 1 160 ? 34.672  29.384  54.452  1.00 78.30  ? 187 VAL B O     1 
ATOM   5423 C  CB    . VAL B 1 160 ? 34.125  28.518  57.211  1.00 69.48  ? 187 VAL B CB    1 
ATOM   5424 C  CG1   . VAL B 1 160 ? 34.819  27.185  56.963  1.00 53.78  ? 187 VAL B CG1   1 
ATOM   5425 C  CG2   . VAL B 1 160 ? 33.711  28.643  58.674  1.00 60.42  ? 187 VAL B CG2   1 
ATOM   5426 N  N     . VAL B 1 161 ? 36.813  29.542  55.139  1.00 71.37  ? 188 VAL B N     1 
ATOM   5427 C  CA    . VAL B 1 161 ? 37.374  29.376  53.807  1.00 74.09  ? 188 VAL B CA    1 
ATOM   5428 C  C     . VAL B 1 161 ? 38.417  28.268  53.860  1.00 66.41  ? 188 VAL B C     1 
ATOM   5429 O  O     . VAL B 1 161 ? 39.064  28.048  54.889  1.00 73.05  ? 188 VAL B O     1 
ATOM   5430 C  CB    . VAL B 1 161 ? 37.980  30.697  53.272  1.00 60.98  ? 188 VAL B CB    1 
ATOM   5431 C  CG1   . VAL B 1 161 ? 39.294  31.007  53.969  1.00 75.27  ? 188 VAL B CG1   1 
ATOM   5432 C  CG2   . VAL B 1 161 ? 38.163  30.633  51.767  1.00 57.52  ? 188 VAL B CG2   1 
ATOM   5433 N  N     . ALA B 1 162 ? 38.565  27.552  52.744  1.00 68.07  ? 189 ALA B N     1 
ATOM   5434 C  CA    . ALA B 1 162 ? 39.493  26.438  52.648  1.00 69.68  ? 189 ALA B CA    1 
ATOM   5435 C  C     . ALA B 1 162 ? 40.254  26.507  51.331  1.00 69.04  ? 189 ALA B C     1 
ATOM   5436 O  O     . ALA B 1 162 ? 39.652  26.771  50.281  1.00 66.48  ? 189 ALA B O     1 
ATOM   5437 C  CB    . ALA B 1 162 ? 38.761  25.094  52.749  1.00 65.28  ? 189 ALA B CB    1 
ATOM   5438 N  N     . PRO B 1 163 ? 41.566  26.285  51.354  1.00 68.45  ? 190 PRO B N     1 
ATOM   5439 C  CA    . PRO B 1 163 ? 42.336  26.281  50.104  1.00 68.67  ? 190 PRO B CA    1 
ATOM   5440 C  C     . PRO B 1 163 ? 42.286  24.925  49.425  1.00 77.48  ? 190 PRO B C     1 
ATOM   5441 O  O     . PRO B 1 163 ? 42.602  23.922  50.067  1.00 74.69  ? 190 PRO B O     1 
ATOM   5442 C  CB    . PRO B 1 163 ? 43.754  26.630  50.578  1.00 74.22  ? 190 PRO B CB    1 
ATOM   5443 C  CG    . PRO B 1 163 ? 43.831  26.036  51.959  1.00 70.64  ? 190 PRO B CG    1 
ATOM   5444 C  CD    . PRO B 1 163 ? 42.428  26.099  52.536  1.00 73.37  ? 190 PRO B CD    1 
ATOM   5445 N  N     . MET B 1 164 ? 41.891  24.856  48.153  1.00 75.74  ? 191 MET B N     1 
ATOM   5446 C  CA    . MET B 1 164 ? 41.764  23.559  47.486  1.00 72.42  ? 191 MET B CA    1 
ATOM   5447 C  C     . MET B 1 164 ? 43.136  22.908  47.359  1.00 84.45  ? 191 MET B C     1 
ATOM   5448 O  O     . MET B 1 164 ? 43.999  23.394  46.621  1.00 80.81  ? 191 MET B O     1 
ATOM   5449 C  CB    . MET B 1 164 ? 41.116  23.694  46.112  1.00 75.14  ? 191 MET B CB    1 
ATOM   5450 C  CG    . MET B 1 164 ? 40.929  22.340  45.421  1.00 75.40  ? 191 MET B CG    1 
ATOM   5451 S  SD    . MET B 1 164 ? 40.515  22.440  43.671  1.00 85.04  ? 191 MET B SD    1 
ATOM   5452 C  CE    . MET B 1 164 ? 42.107  22.870  42.974  1.00 89.05  ? 191 MET B CE    1 
ATOM   5453 N  N     . LEU B 1 165 ? 43.337  21.805  48.074  1.00 80.27  ? 192 LEU B N     1 
ATOM   5454 C  CA    . LEU B 1 165 ? 44.588  21.069  48.010  1.00 73.01  ? 192 LEU B CA    1 
ATOM   5455 C  C     . LEU B 1 165 ? 44.488  19.977  46.956  1.00 81.60  ? 192 LEU B C     1 
ATOM   5456 O  O     . LEU B 1 165 ? 43.428  19.371  46.769  1.00 89.43  ? 192 LEU B O     1 
ATOM   5457 C  CB    . LEU B 1 165 ? 44.927  20.469  49.372  1.00 74.12  ? 192 LEU B CB    1 
ATOM   5458 C  CG    . LEU B 1 165 ? 45.022  21.476  50.521  1.00 75.76  ? 192 LEU B CG    1 
ATOM   5459 C  CD1   . LEU B 1 165 ? 45.336  20.771  51.827  1.00 69.56  ? 192 LEU B CD1   1 
ATOM   5460 C  CD2   . LEU B 1 165 ? 46.064  22.543  50.219  1.00 66.56  ? 192 LEU B CD2   1 
ATOM   5461 N  N     . ASP B 1 166 ? 45.596  19.739  46.260  1.00 87.67  ? 193 ASP B N     1 
ATOM   5462 C  CA    . ASP B 1 166 ? 45.636  18.764  45.179  1.00 78.58  ? 193 ASP B CA    1 
ATOM   5463 C  C     . ASP B 1 166 ? 45.967  17.383  45.725  1.00 82.44  ? 193 ASP B C     1 
ATOM   5464 O  O     . ASP B 1 166 ? 46.792  17.240  46.631  1.00 87.73  ? 193 ASP B O     1 
ATOM   5465 C  CB    . ASP B 1 166 ? 46.673  19.167  44.129  1.00 83.89  ? 193 ASP B CB    1 
ATOM   5466 C  CG    . ASP B 1 166 ? 46.285  20.426  43.373  1.00 102.57 ? 193 ASP B CG    1 
ATOM   5467 O  OD1   . ASP B 1 166 ? 45.129  20.511  42.904  1.00 104.61 ? 193 ASP B OD1   1 
ATOM   5468 O  OD2   . ASP B 1 166 ? 47.136  21.333  43.249  1.00 103.47 ? 193 ASP B OD2   1 
ATOM   5469 N  N     . SER B 1 167 ? 45.317  16.368  45.168  1.00 77.52  ? 194 SER B N     1 
ATOM   5470 C  CA    . SER B 1 167 ? 45.599  14.974  45.478  1.00 84.89  ? 194 SER B CA    1 
ATOM   5471 C  C     . SER B 1 167 ? 46.010  14.252  44.200  1.00 81.92  ? 194 SER B C     1 
ATOM   5472 O  O     . SER B 1 167 ? 46.009  14.823  43.109  1.00 85.76  ? 194 SER B O     1 
ATOM   5473 C  CB    . SER B 1 167 ? 44.384  14.300  46.124  1.00 88.80  ? 194 SER B CB    1 
ATOM   5474 O  OG    . SER B 1 167 ? 43.301  14.206  45.214  1.00 82.42  ? 194 SER B OG    1 
ATOM   5475 N  N     . ARG B 1 168 ? 46.357  12.972  44.339  1.00 84.58  ? 195 ARG B N     1 
ATOM   5476 C  CA    . ARG B 1 168 ? 46.679  12.176  43.161  1.00 86.69  ? 195 ARG B CA    1 
ATOM   5477 C  C     . ARG B 1 168 ? 45.450  11.890  42.308  1.00 87.58  ? 195 ARG B C     1 
ATOM   5478 O  O     . ARG B 1 168 ? 45.594  11.524  41.139  1.00 104.21 ? 195 ARG B O     1 
ATOM   5479 C  CB    . ARG B 1 168 ? 47.335  10.859  43.576  1.00 91.16  ? 195 ARG B CB    1 
ATOM   5480 C  CG    . ARG B 1 168 ? 46.376  9.907   44.266  1.00 87.36  ? 195 ARG B CG    1 
ATOM   5481 C  CD    . ARG B 1 168 ? 47.081  8.698   44.832  1.00 91.22  ? 195 ARG B CD    1 
ATOM   5482 N  NE    . ARG B 1 168 ? 46.203  7.980   45.747  1.00 104.47 ? 195 ARG B NE    1 
ATOM   5483 C  CZ    . ARG B 1 168 ? 45.349  7.033   45.381  1.00 101.68 ? 195 ARG B CZ    1 
ATOM   5484 N  NH1   . ARG B 1 168 ? 45.247  6.645   44.120  1.00 104.37 ? 195 ARG B NH1   1 
ATOM   5485 N  NH2   . ARG B 1 168 ? 44.578  6.464   46.303  1.00 96.64  ? 195 ARG B NH2   1 
ATOM   5486 N  N     . ALA B 1 169 ? 44.252  12.042  42.867  1.00 86.64  ? 196 ALA B N     1 
ATOM   5487 C  CA    . ALA B 1 169 ? 43.016  11.751  42.152  1.00 82.95  ? 196 ALA B CA    1 
ATOM   5488 C  C     . ALA B 1 169 ? 42.040  12.913  42.220  1.00 90.68  ? 196 ALA B C     1 
ATOM   5489 O  O     . ALA B 1 169 ? 42.433  14.029  42.556  1.00 91.39  ? 196 ALA B O     1 
ATOM   5490 C  CB    . ALA B 1 169 ? 42.354  10.501  42.710  1.00 89.27  ? 196 ALA B CB    1 
ATOM   5491 N  N     . ALA B 1 170 ? 40.779  12.675  41.858  1.00 90.82  ? 197 ALA B N     1 
ATOM   5492 C  CA    . ALA B 1 170 ? 39.764  13.720  41.928  1.00 85.45  ? 197 ALA B CA    1 
ATOM   5493 C  C     . ALA B 1 170 ? 39.471  14.156  43.357  1.00 96.42  ? 197 ALA B C     1 
ATOM   5494 O  O     . ALA B 1 170 ? 38.842  15.202  43.548  1.00 101.69 ? 197 ALA B O     1 
ATOM   5495 C  CB    . ALA B 1 170 ? 38.477  13.241  41.254  1.00 85.89  ? 197 ALA B CB    1 
ATOM   5496 N  N     . TYR B 1 171 ? 39.907  13.387  44.357  1.00 96.44  ? 198 TYR B N     1 
ATOM   5497 C  CA    . TYR B 1 171 ? 39.645  13.745  45.744  1.00 79.89  ? 198 TYR B CA    1 
ATOM   5498 C  C     . TYR B 1 171 ? 40.303  15.073  46.092  1.00 92.07  ? 198 TYR B C     1 
ATOM   5499 O  O     . TYR B 1 171 ? 41.419  15.370  45.658  1.00 96.39  ? 198 TYR B O     1 
ATOM   5500 C  CB    . TYR B 1 171 ? 40.150  12.652  46.688  1.00 80.00  ? 198 TYR B CB    1 
ATOM   5501 C  CG    . TYR B 1 171 ? 40.082  13.022  48.155  1.00 87.30  ? 198 TYR B CG    1 
ATOM   5502 C  CD1   . TYR B 1 171 ? 38.947  12.752  48.908  1.00 75.10  ? 198 TYR B CD1   1 
ATOM   5503 C  CD2   . TYR B 1 171 ? 41.157  13.638  48.789  1.00 88.44  ? 198 TYR B CD2   1 
ATOM   5504 C  CE1   . TYR B 1 171 ? 38.882  13.090  50.248  1.00 84.35  ? 198 TYR B CE1   1 
ATOM   5505 C  CE2   . TYR B 1 171 ? 41.100  13.980  50.126  1.00 87.16  ? 198 TYR B CE2   1 
ATOM   5506 C  CZ    . TYR B 1 171 ? 39.962  13.703  50.854  1.00 90.83  ? 198 TYR B CZ    1 
ATOM   5507 O  OH    . TYR B 1 171 ? 39.906  14.041  52.190  1.00 85.40  ? 198 TYR B OH    1 
ATOM   5508 N  N     . SER B 1 172 ? 39.595  15.874  46.879  1.00 87.13  ? 199 SER B N     1 
ATOM   5509 C  CA    . SER B 1 172 ? 40.143  17.091  47.452  1.00 75.82  ? 199 SER B CA    1 
ATOM   5510 C  C     . SER B 1 172 ? 39.409  17.348  48.760  1.00 89.47  ? 199 SER B C     1 
ATOM   5511 O  O     . SER B 1 172 ? 38.518  16.588  49.153  1.00 86.76  ? 199 SER B O     1 
ATOM   5512 C  CB    . SER B 1 172 ? 40.027  18.265  46.476  1.00 80.75  ? 199 SER B CB    1 
ATOM   5513 O  OG    . SER B 1 172 ? 40.684  19.416  46.973  1.00 82.24  ? 199 SER B OG    1 
ATOM   5514 N  N     . ASN B 1 173 ? 39.785  18.430  49.437  1.00 83.10  ? 200 ASN B N     1 
ATOM   5515 C  CA    . ASN B 1 173 ? 39.223  18.752  50.748  1.00 77.03  ? 200 ASN B CA    1 
ATOM   5516 C  C     . ASN B 1 173 ? 37.931  19.557  50.654  1.00 80.63  ? 200 ASN B C     1 
ATOM   5517 O  O     . ASN B 1 173 ? 37.726  20.503  51.422  1.00 81.63  ? 200 ASN B O     1 
ATOM   5518 C  CB    . ASN B 1 173 ? 40.267  19.486  51.583  1.00 73.55  ? 200 ASN B CB    1 
ATOM   5519 C  CG    . ASN B 1 173 ? 40.849  20.692  50.867  1.00 86.13  ? 200 ASN B CG    1 
ATOM   5520 O  OD1   . ASN B 1 173 ? 41.079  20.663  49.657  1.00 78.64  ? 200 ASN B OD1   1 
ATOM   5521 N  ND2   . ASN B 1 173 ? 41.091  21.763  51.616  1.00 84.02  ? 200 ASN B ND2   1 
ATOM   5522 N  N     . PHE B 1 174 ? 37.034  19.202  49.737  1.00 81.68  ? 201 PHE B N     1 
ATOM   5523 C  CA    . PHE B 1 174 ? 35.747  19.877  49.638  1.00 80.85  ? 201 PHE B CA    1 
ATOM   5524 C  C     . PHE B 1 174 ? 34.770  18.987  48.884  1.00 88.42  ? 201 PHE B C     1 
ATOM   5525 O  O     . PHE B 1 174 ? 35.163  18.210  48.009  1.00 85.95  ? 201 PHE B O     1 
ATOM   5526 C  CB    . PHE B 1 174 ? 35.873  21.233  48.935  1.00 76.45  ? 201 PHE B CB    1 
ATOM   5527 C  CG    . PHE B 1 174 ? 36.086  21.126  47.453  1.00 75.39  ? 201 PHE B CG    1 
ATOM   5528 C  CD1   . PHE B 1 174 ? 37.317  20.747  46.942  1.00 76.26  ? 201 PHE B CD1   1 
ATOM   5529 C  CD2   . PHE B 1 174 ? 35.054  21.397  46.571  1.00 78.38  ? 201 PHE B CD2   1 
ATOM   5530 C  CE1   . PHE B 1 174 ? 37.515  20.643  45.580  1.00 83.19  ? 201 PHE B CE1   1 
ATOM   5531 C  CE2   . PHE B 1 174 ? 35.245  21.293  45.205  1.00 85.97  ? 201 PHE B CE2   1 
ATOM   5532 C  CZ    . PHE B 1 174 ? 36.477  20.919  44.709  1.00 87.72  ? 201 PHE B CZ    1 
ATOM   5533 N  N     . TRP B 1 175 ? 33.494  19.106  49.240  1.00 84.08  ? 202 TRP B N     1 
ATOM   5534 C  CA    . TRP B 1 175 ? 32.408  18.495  48.490  1.00 84.56  ? 202 TRP B CA    1 
ATOM   5535 C  C     . TRP B 1 175 ? 31.666  19.578  47.721  1.00 97.45  ? 202 TRP B C     1 
ATOM   5536 O  O     . TRP B 1 175 ? 31.578  20.727  48.164  1.00 93.09  ? 202 TRP B O     1 
ATOM   5537 C  CB    . TRP B 1 175 ? 31.422  17.763  49.405  1.00 88.68  ? 202 TRP B CB    1 
ATOM   5538 C  CG    . TRP B 1 175 ? 32.016  16.694  50.269  1.00 95.06  ? 202 TRP B CG    1 
ATOM   5539 C  CD1   . TRP B 1 175 ? 33.306  16.250  50.266  1.00 93.17  ? 202 TRP B CD1   1 
ATOM   5540 C  CD2   . TRP B 1 175 ? 31.331  15.933  51.273  1.00 97.18  ? 202 TRP B CD2   1 
ATOM   5541 N  NE1   . TRP B 1 175 ? 33.467  15.259  51.205  1.00 100.55 ? 202 TRP B NE1   1 
ATOM   5542 C  CE2   . TRP B 1 175 ? 32.269  15.046  51.836  1.00 94.66  ? 202 TRP B CE2   1 
ATOM   5543 C  CE3   . TRP B 1 175 ? 30.016  15.916  51.748  1.00 93.39  ? 202 TRP B CE3   1 
ATOM   5544 C  CZ2   . TRP B 1 175 ? 31.933  14.152  52.851  1.00 101.91 ? 202 TRP B CZ2   1 
ATOM   5545 C  CZ3   . TRP B 1 175 ? 29.685  15.029  52.754  1.00 95.92  ? 202 TRP B CZ3   1 
ATOM   5546 C  CH2   . TRP B 1 175 ? 30.639  14.159  53.295  1.00 106.38 ? 202 TRP B CH2   1 
ATOM   5547 N  N     . CYS B 1 176 ? 31.126  19.204  46.563  1.00 97.14  ? 203 CYS B N     1 
ATOM   5548 C  CA    . CYS B 1 176 ? 30.337  20.138  45.776  1.00 98.94  ? 203 CYS B CA    1 
ATOM   5549 C  C     . CYS B 1 176 ? 28.837  19.959  45.956  1.00 108.82 ? 203 CYS B C     1 
ATOM   5550 O  O     . CYS B 1 176 ? 28.083  20.899  45.682  1.00 116.55 ? 203 CYS B O     1 
ATOM   5551 C  CB    . CYS B 1 176 ? 30.692  20.017  44.292  1.00 105.18 ? 203 CYS B CB    1 
ATOM   5552 S  SG    . CYS B 1 176 ? 31.758  21.354  43.698  1.00 132.15 ? 203 CYS B SG    1 
ATOM   5553 N  N     . GLY B 1 177 ? 28.391  18.797  46.415  1.00 115.20 ? 204 GLY B N     1 
ATOM   5554 C  CA    . GLY B 1 177 ? 26.984  18.582  46.695  1.00 111.73 ? 204 GLY B CA    1 
ATOM   5555 C  C     . GLY B 1 177 ? 26.798  17.744  47.941  1.00 116.19 ? 204 GLY B C     1 
ATOM   5556 O  O     . GLY B 1 177 ? 27.654  16.936  48.309  1.00 116.38 ? 204 GLY B O     1 
ATOM   5557 N  N     . MET B 1 178 ? 25.656  17.948  48.595  1.00 114.31 ? 205 MET B N     1 
ATOM   5558 C  CA    . MET B 1 178 ? 25.259  17.159  49.751  1.00 105.95 ? 205 MET B CA    1 
ATOM   5559 C  C     . MET B 1 178 ? 23.849  16.628  49.521  1.00 120.07 ? 205 MET B C     1 
ATOM   5560 O  O     . MET B 1 178 ? 23.083  17.162  48.713  1.00 132.92 ? 205 MET B O     1 
ATOM   5561 C  CB    . MET B 1 178 ? 25.332  17.978  51.047  1.00 97.30  ? 205 MET B CB    1 
ATOM   5562 C  CG    . MET B 1 178 ? 25.641  17.163  52.298  1.00 94.24  ? 205 MET B CG    1 
ATOM   5563 S  SD    . MET B 1 178 ? 25.779  18.177  53.787  1.00 106.38 ? 205 MET B SD    1 
ATOM   5564 C  CE    . MET B 1 178 ? 27.557  18.270  53.986  1.00 97.17  ? 205 MET B CE    1 
ATOM   5565 N  N     . THR B 1 179 ? 23.511  15.571  50.257  1.00 125.72 ? 206 THR B N     1 
ATOM   5566 C  CA    . THR B 1 179 ? 22.347  14.745  49.964  1.00 133.32 ? 206 THR B CA    1 
ATOM   5567 C  C     . THR B 1 179 ? 21.159  15.014  50.874  1.00 139.99 ? 206 THR B C     1 
ATOM   5568 O  O     . THR B 1 179 ? 20.186  14.251  50.839  1.00 151.81 ? 206 THR B O     1 
ATOM   5569 C  CB    . THR B 1 179 ? 22.721  13.270  50.064  1.00 133.60 ? 206 THR B CB    1 
ATOM   5570 O  OG1   . THR B 1 179 ? 23.231  13.003  51.374  1.00 128.77 ? 206 THR B OG1   1 
ATOM   5571 C  CG2   . THR B 1 179 ? 23.784  12.928  49.040  1.00 144.06 ? 206 THR B CG2   1 
ATOM   5572 N  N     . SER B 1 180 ? 21.216  16.066  51.690  1.00 126.02 ? 207 SER B N     1 
ATOM   5573 C  CA    . SER B 1 180 ? 20.148  16.395  52.631  1.00 136.19 ? 207 SER B CA    1 
ATOM   5574 C  C     . SER B 1 180 ? 20.046  15.308  53.697  1.00 132.25 ? 207 SER B C     1 
ATOM   5575 O  O     . SER B 1 180 ? 19.226  15.393  54.615  1.00 116.55 ? 207 SER B O     1 
ATOM   5576 C  CB    . SER B 1 180 ? 18.813  16.610  51.902  1.00 146.70 ? 207 SER B CB    1 
ATOM   5577 O  OG    . SER B 1 180 ? 18.250  15.395  51.427  1.00 152.58 ? 207 SER B OG    1 
ATOM   5578 N  N     . GLN B 1 181 ? 20.888  14.280  53.571  1.00 132.73 ? 208 GLN B N     1 
ATOM   5579 C  CA    . GLN B 1 181 ? 21.140  13.319  54.629  1.00 120.54 ? 208 GLN B CA    1 
ATOM   5580 C  C     . GLN B 1 181 ? 22.559  13.395  55.177  1.00 114.89 ? 208 GLN B C     1 
ATOM   5581 O  O     . GLN B 1 181 ? 22.834  12.784  56.216  1.00 111.65 ? 208 GLN B O     1 
ATOM   5582 C  CB    . GLN B 1 181 ? 20.878  11.890  54.133  1.00 120.95 ? 208 GLN B CB    1 
ATOM   5583 C  CG    . GLN B 1 181 ? 19.452  11.641  53.689  1.00 140.00 ? 208 GLN B CG    1 
ATOM   5584 C  CD    . GLN B 1 181 ? 19.228  10.206  53.262  1.00 159.06 ? 208 GLN B CD    1 
ATOM   5585 O  OE1   . GLN B 1 181 ? 20.137  9.377   53.329  1.00 159.62 ? 208 GLN B OE1   1 
ATOM   5586 N  NE2   . GLN B 1 181 ? 18.014  9.904   52.817  1.00 163.66 ? 208 GLN B NE2   1 
ATOM   5587 N  N     . GLY B 1 182 ? 23.461  14.125  54.516  1.00 112.18 ? 209 GLY B N     1 
ATOM   5588 C  CA    . GLY B 1 182 ? 24.835  14.276  54.952  1.00 108.65 ? 209 GLY B CA    1 
ATOM   5589 C  C     . GLY B 1 182 ? 25.855  13.553  54.102  1.00 113.81 ? 209 GLY B C     1 
ATOM   5590 O  O     . GLY B 1 182 ? 27.058  13.712  54.343  1.00 107.81 ? 209 GLY B O     1 
ATOM   5591 N  N     . TYR B 1 183 ? 25.427  12.780  53.113  1.00 114.87 ? 210 TYR B N     1 
ATOM   5592 C  CA    . TYR B 1 183 ? 26.339  11.956  52.337  1.00 120.22 ? 210 TYR B CA    1 
ATOM   5593 C  C     . TYR B 1 183 ? 26.928  12.742  51.167  1.00 115.76 ? 210 TYR B C     1 
ATOM   5594 O  O     . TYR B 1 183 ? 26.387  13.761  50.732  1.00 111.24 ? 210 TYR B O     1 
ATOM   5595 C  CB    . TYR B 1 183 ? 25.617  10.704  51.833  1.00 127.71 ? 210 TYR B CB    1 
ATOM   5596 C  CG    . TYR B 1 183 ? 24.977  9.889   52.939  1.00 127.00 ? 210 TYR B CG    1 
ATOM   5597 C  CD1   . TYR B 1 183 ? 25.622  9.704   54.157  1.00 126.15 ? 210 TYR B CD1   1 
ATOM   5598 C  CD2   . TYR B 1 183 ? 23.724  9.314   52.767  1.00 131.17 ? 210 TYR B CD2   1 
ATOM   5599 C  CE1   . TYR B 1 183 ? 25.040  8.964   55.170  1.00 129.02 ? 210 TYR B CE1   1 
ATOM   5600 C  CE2   . TYR B 1 183 ? 23.133  8.573   53.773  1.00 134.54 ? 210 TYR B CE2   1 
ATOM   5601 C  CZ    . TYR B 1 183 ? 23.794  8.401   54.972  1.00 138.90 ? 210 TYR B CZ    1 
ATOM   5602 O  OH    . TYR B 1 183 ? 23.205  7.662   55.974  1.00 137.80 ? 210 TYR B OH    1 
ATOM   5603 N  N     . TYR B 1 184 ? 28.056  12.249  50.664  1.00 115.96 ? 211 TYR B N     1 
ATOM   5604 C  CA    . TYR B 1 184 ? 28.718  12.888  49.536  1.00 109.64 ? 211 TYR B CA    1 
ATOM   5605 C  C     . TYR B 1 184 ? 27.827  12.841  48.299  1.00 113.11 ? 211 TYR B C     1 
ATOM   5606 O  O     . TYR B 1 184 ? 26.976  11.961  48.151  1.00 121.07 ? 211 TYR B O     1 
ATOM   5607 C  CB    . TYR B 1 184 ? 30.056  12.207  49.254  1.00 106.51 ? 211 TYR B CB    1 
ATOM   5608 C  CG    . TYR B 1 184 ? 30.809  12.809  48.094  1.00 110.67 ? 211 TYR B CG    1 
ATOM   5609 C  CD1   . TYR B 1 184 ? 31.533  13.982  48.250  1.00 105.19 ? 211 TYR B CD1   1 
ATOM   5610 C  CD2   . TYR B 1 184 ? 30.791  12.209  46.841  1.00 103.29 ? 211 TYR B CD2   1 
ATOM   5611 C  CE1   . TYR B 1 184 ? 32.219  14.542  47.196  1.00 103.71 ? 211 TYR B CE1   1 
ATOM   5612 C  CE2   . TYR B 1 184 ? 31.475  12.761  45.783  1.00 109.80 ? 211 TYR B CE2   1 
ATOM   5613 C  CZ    . TYR B 1 184 ? 32.187  13.929  45.966  1.00 114.70 ? 211 TYR B CZ    1 
ATOM   5614 O  OH    . TYR B 1 184 ? 32.874  14.492  44.917  1.00 127.74 ? 211 TYR B OH    1 
ATOM   5615 N  N     . LYS B 1 185 ? 28.033  13.801  47.400  1.00 108.79 ? 212 LYS B N     1 
ATOM   5616 C  CA    . LYS B 1 185 ? 27.176  13.930  46.224  1.00 109.73 ? 212 LYS B CA    1 
ATOM   5617 C  C     . LYS B 1 185 ? 27.951  14.632  45.122  1.00 109.85 ? 212 LYS B C     1 
ATOM   5618 O  O     . LYS B 1 185 ? 28.391  15.771  45.306  1.00 121.16 ? 212 LYS B O     1 
ATOM   5619 C  CB    . LYS B 1 185 ? 25.904  14.703  46.575  1.00 117.28 ? 212 LYS B CB    1 
ATOM   5620 C  CG    . LYS B 1 185 ? 24.957  14.954  45.415  1.00 126.57 ? 212 LYS B CG    1 
ATOM   5621 C  CD    . LYS B 1 185 ? 23.727  15.711  45.896  1.00 126.39 ? 212 LYS B CD    1 
ATOM   5622 C  CE    . LYS B 1 185 ? 22.728  15.948  44.777  1.00 131.53 ? 212 LYS B CE    1 
ATOM   5623 N  NZ    . LYS B 1 185 ? 21.517  16.653  45.284  1.00 122.47 ? 212 LYS B NZ    1 
ATOM   5624 N  N     . ARG B 1 186 ? 28.122  13.957  43.988  1.00 115.82 ? 213 ARG B N     1 
ATOM   5625 C  CA    . ARG B 1 186 ? 28.740  14.583  42.828  1.00 118.67 ? 213 ARG B CA    1 
ATOM   5626 C  C     . ARG B 1 186 ? 27.783  15.588  42.199  1.00 128.33 ? 213 ARG B C     1 
ATOM   5627 O  O     . ARG B 1 186 ? 26.576  15.348  42.107  1.00 143.67 ? 213 ARG B O     1 
ATOM   5628 C  CB    . ARG B 1 186 ? 29.132  13.528  41.790  1.00 136.60 ? 213 ARG B CB    1 
ATOM   5629 C  CG    . ARG B 1 186 ? 30.154  12.506  42.262  1.00 140.39 ? 213 ARG B CG    1 
ATOM   5630 C  CD    . ARG B 1 186 ? 31.536  13.121  42.413  1.00 143.55 ? 213 ARG B CD    1 
ATOM   5631 N  NE    . ARG B 1 186 ? 32.424  12.803  41.300  1.00 163.70 ? 213 ARG B NE    1 
ATOM   5632 C  CZ    . ARG B 1 186 ? 33.745  12.922  41.341  1.00 153.33 ? 213 ARG B CZ    1 
ATOM   5633 N  NH1   . ARG B 1 186 ? 34.368  13.335  42.434  1.00 131.60 ? 213 ARG B NH1   1 
ATOM   5634 N  NH2   . ARG B 1 186 ? 34.458  12.613  40.261  1.00 142.59 ? 213 ARG B NH2   1 
ATOM   5635 N  N     . THR B 1 187 ? 28.326  16.719  41.774  1.00 116.68 ? 214 THR B N     1 
ATOM   5636 C  CA    . THR B 1 187 ? 27.614  17.720  40.998  1.00 110.27 ? 214 THR B CA    1 
ATOM   5637 C  C     . THR B 1 187 ? 28.475  18.085  39.800  1.00 114.82 ? 214 THR B C     1 
ATOM   5638 O  O     . THR B 1 187 ? 29.701  17.932  39.840  1.00 107.28 ? 214 THR B O     1 
ATOM   5639 C  CB    . THR B 1 187 ? 27.302  18.979  41.824  1.00 113.23 ? 214 THR B CB    1 
ATOM   5640 O  OG1   . THR B 1 187 ? 28.521  19.639  42.176  1.00 118.10 ? 214 THR B OG1   1 
ATOM   5641 C  CG2   . THR B 1 187 ? 26.530  18.622  43.088  1.00 118.30 ? 214 THR B CG2   1 
ATOM   5642 N  N     . PRO B 1 188 ? 27.863  18.563  38.711  1.00 120.37 ? 215 PRO B N     1 
ATOM   5643 C  CA    . PRO B 1 188 ? 28.645  18.831  37.489  1.00 119.04 ? 215 PRO B CA    1 
ATOM   5644 C  C     . PRO B 1 188 ? 29.796  19.802  37.684  1.00 114.94 ? 215 PRO B C     1 
ATOM   5645 O  O     . PRO B 1 188 ? 30.754  19.762  36.901  1.00 111.86 ? 215 PRO B O     1 
ATOM   5646 C  CB    . PRO B 1 188 ? 27.598  19.399  36.520  1.00 113.02 ? 215 PRO B CB    1 
ATOM   5647 C  CG    . PRO B 1 188 ? 26.303  18.840  37.000  1.00 113.69 ? 215 PRO B CG    1 
ATOM   5648 C  CD    . PRO B 1 188 ? 26.419  18.768  38.495  1.00 113.51 ? 215 PRO B CD    1 
ATOM   5649 N  N     . ALA B 1 189 ? 29.748  20.657  38.700  1.00 105.08 ? 216 ALA B N     1 
ATOM   5650 C  CA    . ALA B 1 189 ? 30.743  21.704  38.868  1.00 98.31  ? 216 ALA B CA    1 
ATOM   5651 C  C     . ALA B 1 189 ? 31.987  21.246  39.617  1.00 99.88  ? 216 ALA B C     1 
ATOM   5652 O  O     . ALA B 1 189 ? 32.928  22.034  39.752  1.00 99.83  ? 216 ALA B O     1 
ATOM   5653 C  CB    . ALA B 1 189 ? 30.120  22.900  39.592  1.00 94.90  ? 216 ALA B CB    1 
ATOM   5654 N  N     . TYR B 1 190 ? 32.027  20.004  40.102  1.00 95.48  ? 217 TYR B N     1 
ATOM   5655 C  CA    . TYR B 1 190 ? 33.176  19.567  40.891  1.00 95.18  ? 217 TYR B CA    1 
ATOM   5656 C  C     . TYR B 1 190 ? 34.428  19.446  40.029  1.00 100.78 ? 217 TYR B C     1 
ATOM   5657 O  O     . TYR B 1 190 ? 35.475  20.026  40.347  1.00 90.60  ? 217 TYR B O     1 
ATOM   5658 C  CB    . TYR B 1 190 ? 32.874  18.240  41.588  1.00 85.32  ? 217 TYR B CB    1 
ATOM   5659 C  CG    . TYR B 1 190 ? 34.013  17.767  42.466  1.00 88.04  ? 217 TYR B CG    1 
ATOM   5660 C  CD1   . TYR B 1 190 ? 34.101  18.165  43.791  1.00 94.03  ? 217 TYR B CD1   1 
ATOM   5661 C  CD2   . TYR B 1 190 ? 35.005  16.933  41.966  1.00 97.15  ? 217 TYR B CD2   1 
ATOM   5662 C  CE1   . TYR B 1 190 ? 35.142  17.743  44.597  1.00 93.79  ? 217 TYR B CE1   1 
ATOM   5663 C  CE2   . TYR B 1 190 ? 36.050  16.506  42.763  1.00 96.32  ? 217 TYR B CE2   1 
ATOM   5664 C  CZ    . TYR B 1 190 ? 36.114  16.914  44.079  1.00 93.80  ? 217 TYR B CZ    1 
ATOM   5665 O  OH    . TYR B 1 190 ? 37.151  16.492  44.879  1.00 93.13  ? 217 TYR B OH    1 
ATOM   5666 N  N     . ILE B 1 191 ? 34.352  18.672  38.942  1.00 99.70  ? 218 ILE B N     1 
ATOM   5667 C  CA    . ILE B 1 191 ? 35.522  18.475  38.081  1.00 97.27  ? 218 ILE B CA    1 
ATOM   5668 C  C     . ILE B 1 191 ? 36.065  19.800  37.552  1.00 95.42  ? 218 ILE B C     1 
ATOM   5669 O  O     . ILE B 1 191 ? 37.292  19.967  37.519  1.00 102.33 ? 218 ILE B O     1 
ATOM   5670 C  CB    . ILE B 1 191 ? 35.213  17.462  36.980  1.00 101.64 ? 218 ILE B CB    1 
ATOM   5671 C  CG1   . ILE B 1 191 ? 34.930  16.086  37.585  1.00 99.02  ? 218 ILE B CG1   1 
ATOM   5672 C  CG2   . ILE B 1 191 ? 36.377  17.350  36.003  1.00 107.10 ? 218 ILE B CG2   1 
ATOM   5673 C  CD1   . ILE B 1 191 ? 36.107  15.511  38.354  1.00 106.35 ? 218 ILE B CD1   1 
ATOM   5674 N  N     . PRO B 1 192 ? 35.241  20.769  37.128  1.00 100.52 ? 219 PRO B N     1 
ATOM   5675 C  CA    . PRO B 1 192 ? 35.818  22.073  36.737  1.00 102.46 ? 219 PRO B CA    1 
ATOM   5676 C  C     . PRO B 1 192 ? 36.587  22.759  37.855  1.00 94.83  ? 219 PRO B C     1 
ATOM   5677 O  O     . PRO B 1 192 ? 37.700  23.253  37.626  1.00 91.80  ? 219 PRO B O     1 
ATOM   5678 C  CB    . PRO B 1 192 ? 34.584  22.876  36.308  1.00 101.41 ? 219 PRO B CB    1 
ATOM   5679 C  CG    . PRO B 1 192 ? 33.628  21.847  35.831  1.00 108.84 ? 219 PRO B CG    1 
ATOM   5680 C  CD    . PRO B 1 192 ? 33.821  20.671  36.741  1.00 101.68 ? 219 PRO B CD    1 
ATOM   5681 N  N     . ILE B 1 193 ? 36.019  22.813  39.062  1.00 93.41  ? 220 ILE B N     1 
ATOM   5682 C  CA    . ILE B 1 193 ? 36.727  23.405  40.195  1.00 86.20  ? 220 ILE B CA    1 
ATOM   5683 C  C     . ILE B 1 193 ? 37.983  22.606  40.514  1.00 96.65  ? 220 ILE B C     1 
ATOM   5684 O  O     . ILE B 1 193 ? 39.055  23.172  40.764  1.00 92.04  ? 220 ILE B O     1 
ATOM   5685 C  CB    . ILE B 1 193 ? 35.798  23.493  41.418  1.00 85.72  ? 220 ILE B CB    1 
ATOM   5686 C  CG1   . ILE B 1 193 ? 34.602  24.398  41.124  1.00 94.57  ? 220 ILE B CG1   1 
ATOM   5687 C  CG2   . ILE B 1 193 ? 36.566  23.978  42.638  1.00 81.56  ? 220 ILE B CG2   1 
ATOM   5688 C  CD1   . ILE B 1 193 ? 33.536  24.355  42.198  1.00 101.56 ? 220 ILE B CD1   1 
ATOM   5689 N  N     . ARG B 1 194 ? 37.867  21.275  40.511  1.00 99.10  ? 221 ARG B N     1 
ATOM   5690 C  CA    . ARG B 1 194 ? 38.996  20.423  40.867  1.00 83.39  ? 221 ARG B CA    1 
ATOM   5691 C  C     . ARG B 1 194 ? 40.170  20.632  39.918  1.00 88.33  ? 221 ARG B C     1 
ATOM   5692 O  O     . ARG B 1 194 ? 41.331  20.617  40.344  1.00 92.77  ? 221 ARG B O     1 
ATOM   5693 C  CB    . ARG B 1 194 ? 38.554  18.959  40.871  1.00 87.83  ? 221 ARG B CB    1 
ATOM   5694 C  CG    . ARG B 1 194 ? 39.655  17.962  41.188  1.00 89.20  ? 221 ARG B CG    1 
ATOM   5695 C  CD    . ARG B 1 194 ? 40.218  18.165  42.584  1.00 83.15  ? 221 ARG B CD    1 
ATOM   5696 N  NE    . ARG B 1 194 ? 41.299  17.227  42.859  1.00 85.40  ? 221 ARG B NE    1 
ATOM   5697 C  CZ    . ARG B 1 194 ? 42.575  17.453  42.575  1.00 87.84  ? 221 ARG B CZ    1 
ATOM   5698 N  NH1   . ARG B 1 194 ? 42.970  18.589  42.024  1.00 89.39  ? 221 ARG B NH1   1 
ATOM   5699 N  NH2   . ARG B 1 194 ? 43.477  16.515  42.849  1.00 81.44  ? 221 ARG B NH2   1 
ATOM   5700 N  N     . LYS B 1 195 ? 39.889  20.846  38.633  1.00 89.95  ? 222 LYS B N     1 
ATOM   5701 C  CA    . LYS B 1 195 ? 40.927  21.013  37.625  1.00 86.26  ? 222 LYS B CA    1 
ATOM   5702 C  C     . LYS B 1 195 ? 41.326  22.468  37.413  1.00 93.27  ? 222 LYS B C     1 
ATOM   5703 O  O     . LYS B 1 195 ? 42.098  22.755  36.492  1.00 104.75 ? 222 LYS B O     1 
ATOM   5704 C  CB    . LYS B 1 195 ? 40.479  20.395  36.296  1.00 84.56  ? 222 LYS B CB    1 
ATOM   5705 C  CG    . LYS B 1 195 ? 40.325  18.881  36.344  1.00 101.65 ? 222 LYS B CG    1 
ATOM   5706 C  CD    . LYS B 1 195 ? 40.288  18.267  34.951  1.00 104.16 ? 222 LYS B CD    1 
ATOM   5707 C  CE    . LYS B 1 195 ? 40.272  16.744  35.027  1.00 118.04 ? 222 LYS B CE    1 
ATOM   5708 N  NZ    . LYS B 1 195 ? 40.390  16.106  33.684  1.00 138.72 ? 222 LYS B NZ    1 
ATOM   5709 N  N     . ARG B 1 196 ? 40.826  23.385  38.242  1.00 95.18  ? 223 ARG B N     1 
ATOM   5710 C  CA    . ARG B 1 196 ? 41.129  24.814  38.160  1.00 92.20  ? 223 ARG B CA    1 
ATOM   5711 C  C     . ARG B 1 196 ? 40.778  25.416  36.801  1.00 99.62  ? 223 ARG B C     1 
ATOM   5712 O  O     . ARG B 1 196 ? 41.336  26.449  36.413  1.00 95.70  ? 223 ARG B O     1 
ATOM   5713 C  CB    . ARG B 1 196 ? 42.599  25.098  38.496  1.00 87.83  ? 223 ARG B CB    1 
ATOM   5714 C  CG    . ARG B 1 196 ? 42.948  24.911  39.964  1.00 83.24  ? 223 ARG B CG    1 
ATOM   5715 C  CD    . ARG B 1 196 ? 44.371  25.359  40.263  1.00 81.37  ? 223 ARG B CD    1 
ATOM   5716 N  NE    . ARG B 1 196 ? 44.761  25.050  41.634  1.00 103.62 ? 223 ARG B NE    1 
ATOM   5717 C  CZ    . ARG B 1 196 ? 45.348  23.921  42.013  1.00 97.80  ? 223 ARG B CZ    1 
ATOM   5718 N  NH1   . ARG B 1 196 ? 45.642  22.969  41.144  1.00 85.97  ? 223 ARG B NH1   1 
ATOM   5719 N  NH2   . ARG B 1 196 ? 45.645  23.743  43.298  1.00 103.53 ? 223 ARG B NH2   1 
ATOM   5720 N  N     . ASP B 1 197 ? 39.864  24.788  36.056  1.00 93.73  ? 224 ASP B N     1 
ATOM   5721 C  CA    . ASP B 1 197 ? 39.326  25.439  34.867  1.00 88.76  ? 224 ASP B CA    1 
ATOM   5722 C  C     . ASP B 1 197 ? 38.493  26.654  35.252  1.00 97.46  ? 224 ASP B C     1 
ATOM   5723 O  O     . ASP B 1 197 ? 38.554  27.694  34.587  1.00 109.60 ? 224 ASP B O     1 
ATOM   5724 C  CB    . ASP B 1 197 ? 38.496  24.451  34.052  1.00 97.74  ? 224 ASP B CB    1 
ATOM   5725 C  CG    . ASP B 1 197 ? 39.337  23.344  33.447  1.00 113.80 ? 224 ASP B CG    1 
ATOM   5726 O  OD1   . ASP B 1 197 ? 40.543  23.574  33.215  1.00 114.17 ? 224 ASP B OD1   1 
ATOM   5727 O  OD2   . ASP B 1 197 ? 38.792  22.245  33.205  1.00 112.37 ? 224 ASP B OD2   1 
ATOM   5728 N  N     . ARG B 1 198 ? 37.711  26.537  36.320  1.00 92.22  ? 225 ARG B N     1 
ATOM   5729 C  CA    . ARG B 1 198 ? 37.044  27.670  36.942  1.00 91.79  ? 225 ARG B CA    1 
ATOM   5730 C  C     . ARG B 1 198 ? 37.827  28.055  38.192  1.00 95.67  ? 225 ARG B C     1 
ATOM   5731 O  O     . ARG B 1 198 ? 37.922  27.264  39.136  1.00 101.04 ? 225 ARG B O     1 
ATOM   5732 C  CB    . ARG B 1 198 ? 35.596  27.331  37.296  1.00 97.24  ? 225 ARG B CB    1 
ATOM   5733 C  CG    . ARG B 1 198 ? 34.644  27.293  36.114  1.00 113.20 ? 225 ARG B CG    1 
ATOM   5734 C  CD    . ARG B 1 198 ? 33.251  26.880  36.566  1.00 130.38 ? 225 ARG B CD    1 
ATOM   5735 N  NE    . ARG B 1 198 ? 32.823  27.628  37.743  1.00 120.94 ? 225 ARG B NE    1 
ATOM   5736 C  CZ    . ARG B 1 198 ? 31.693  27.410  38.404  1.00 126.55 ? 225 ARG B CZ    1 
ATOM   5737 N  NH1   . ARG B 1 198 ? 30.845  26.466  38.029  1.00 138.63 ? 225 ARG B NH1   1 
ATOM   5738 N  NH2   . ARG B 1 198 ? 31.409  28.156  39.467  1.00 126.34 ? 225 ARG B NH2   1 
ATOM   5739 N  N     . ARG B 1 199 ? 38.392  29.257  38.192  1.00 98.57  ? 226 ARG B N     1 
ATOM   5740 C  CA    . ARG B 1 199 ? 39.112  29.777  39.344  1.00 96.06  ? 226 ARG B CA    1 
ATOM   5741 C  C     . ARG B 1 199 ? 38.212  30.705  40.155  1.00 92.87  ? 226 ARG B C     1 
ATOM   5742 O  O     . ARG B 1 199 ? 37.189  31.199  39.674  1.00 85.59  ? 226 ARG B O     1 
ATOM   5743 C  CB    . ARG B 1 199 ? 40.379  30.520  38.909  1.00 99.77  ? 226 ARG B CB    1 
ATOM   5744 C  CG    . ARG B 1 199 ? 41.420  29.654  38.218  1.00 97.35  ? 226 ARG B CG    1 
ATOM   5745 C  CD    . ARG B 1 199 ? 42.566  30.508  37.689  1.00 118.30 ? 226 ARG B CD    1 
ATOM   5746 N  NE    . ARG B 1 199 ? 43.493  29.740  36.866  1.00 135.61 ? 226 ARG B NE    1 
ATOM   5747 C  CZ    . ARG B 1 199 ? 44.596  29.160  37.320  1.00 141.52 ? 226 ARG B CZ    1 
ATOM   5748 N  NH1   . ARG B 1 199 ? 44.947  29.245  38.593  1.00 136.57 ? 226 ARG B NH1   1 
ATOM   5749 N  NH2   . ARG B 1 199 ? 45.366  28.479  36.475  1.00 132.93 ? 226 ARG B NH2   1 
ATOM   5750 N  N     . GLY B 1 200 ? 38.609  30.935  41.404  1.00 87.78  ? 227 GLY B N     1 
ATOM   5751 C  CA    . GLY B 1 200 ? 37.892  31.816  42.296  1.00 90.76  ? 227 GLY B CA    1 
ATOM   5752 C  C     . GLY B 1 200 ? 37.645  31.140  43.622  1.00 81.48  ? 227 GLY B C     1 
ATOM   5753 O  O     . GLY B 1 200 ? 38.329  30.177  43.988  1.00 87.40  ? 227 GLY B O     1 
ATOM   5754 N  N     . CYS B 1 201 ? 36.664  31.657  44.355  1.00 84.04  ? 228 CYS B N     1 
ATOM   5755 C  CA    . CYS B 1 201 ? 36.204  31.056  45.600  1.00 85.61  ? 228 CYS B CA    1 
ATOM   5756 C  C     . CYS B 1 201 ? 34.722  30.752  45.464  1.00 87.11  ? 228 CYS B C     1 
ATOM   5757 O  O     . CYS B 1 201 ? 33.936  31.630  45.093  1.00 104.91 ? 228 CYS B O     1 
ATOM   5758 C  CB    . CYS B 1 201 ? 36.457  31.974  46.798  1.00 73.50  ? 228 CYS B CB    1 
ATOM   5759 S  SG    . CYS B 1 201 ? 38.198  32.404  47.054  1.00 98.41  ? 228 CYS B SG    1 
ATOM   5760 N  N     . PHE B 1 202 ? 34.346  29.514  45.759  1.00 90.14  ? 229 PHE B N     1 
ATOM   5761 C  CA    . PHE B 1 202 ? 33.008  29.021  45.476  1.00 89.06  ? 229 PHE B CA    1 
ATOM   5762 C  C     . PHE B 1 202 ? 32.311  28.611  46.764  1.00 86.64  ? 229 PHE B C     1 
ATOM   5763 O  O     . PHE B 1 202 ? 32.941  28.079  47.683  1.00 83.19  ? 229 PHE B O     1 
ATOM   5764 C  CB    . PHE B 1 202 ? 33.066  27.841  44.502  1.00 87.52  ? 229 PHE B CB    1 
ATOM   5765 C  CG    . PHE B 1 202 ? 33.914  28.108  43.294  1.00 83.39  ? 229 PHE B CG    1 
ATOM   5766 C  CD1   . PHE B 1 202 ? 33.394  28.787  42.205  1.00 80.55  ? 229 PHE B CD1   1 
ATOM   5767 C  CD2   . PHE B 1 202 ? 35.235  27.698  43.255  1.00 85.33  ? 229 PHE B CD2   1 
ATOM   5768 C  CE1   . PHE B 1 202 ? 34.173  29.045  41.098  1.00 87.72  ? 229 PHE B CE1   1 
ATOM   5769 C  CE2   . PHE B 1 202 ? 36.022  27.952  42.148  1.00 89.75  ? 229 PHE B CE2   1 
ATOM   5770 C  CZ    . PHE B 1 202 ? 35.490  28.627  41.068  1.00 95.60  ? 229 PHE B CZ    1 
ATOM   5771 N  N     . ALA B 1 203 ? 31.012  28.878  46.828  1.00 85.99  ? 230 ALA B N     1 
ATOM   5772 C  CA    . ALA B 1 203 ? 30.205  28.433  47.954  1.00 93.91  ? 230 ALA B CA    1 
ATOM   5773 C  C     . ALA B 1 203 ? 29.978  26.931  47.843  1.00 92.84  ? 230 ALA B C     1 
ATOM   5774 O  O     . ALA B 1 203 ? 29.472  26.446  46.826  1.00 85.73  ? 230 ALA B O     1 
ATOM   5775 C  CB    . ALA B 1 203 ? 28.876  29.185  47.983  1.00 74.53  ? 230 ALA B CB    1 
ATOM   5776 N  N     . VAL B 1 204 ? 30.368  26.192  48.876  1.00 80.85  ? 231 VAL B N     1 
ATOM   5777 C  CA    . VAL B 1 204 ? 30.217  24.739  48.877  1.00 83.16  ? 231 VAL B CA    1 
ATOM   5778 C  C     . VAL B 1 204 ? 29.642  24.312  50.219  1.00 91.80  ? 231 VAL B C     1 
ATOM   5779 O  O     . VAL B 1 204 ? 29.788  25.016  51.232  1.00 92.28  ? 231 VAL B O     1 
ATOM   5780 C  CB    . VAL B 1 204 ? 31.559  24.023  48.599  1.00 78.54  ? 231 VAL B CB    1 
ATOM   5781 C  CG1   . VAL B 1 204 ? 32.049  24.343  47.201  1.00 73.22  ? 231 VAL B CG1   1 
ATOM   5782 C  CG2   . VAL B 1 204 ? 32.593  24.415  49.641  1.00 77.74  ? 231 VAL B CG2   1 
ATOM   5783 N  N     . PRO B 1 205 ? 28.967  23.160  50.259  1.00 86.38  ? 232 PRO B N     1 
ATOM   5784 C  CA    . PRO B 1 205 ? 28.394  22.678  51.520  1.00 85.73  ? 232 PRO B CA    1 
ATOM   5785 C  C     . PRO B 1 205 ? 29.375  21.954  52.428  1.00 82.57  ? 232 PRO B C     1 
ATOM   5786 O  O     . PRO B 1 205 ? 28.989  21.587  53.543  1.00 97.68  ? 232 PRO B O     1 
ATOM   5787 C  CB    . PRO B 1 205 ? 27.290  21.722  51.046  1.00 95.58  ? 232 PRO B CB    1 
ATOM   5788 C  CG    . PRO B 1 205 ? 27.794  21.201  49.748  1.00 97.88  ? 232 PRO B CG    1 
ATOM   5789 C  CD    . PRO B 1 205 ? 28.532  22.346  49.108  1.00 93.19  ? 232 PRO B CD    1 
ATOM   5790 N  N     . MET B 1 206 ? 30.621  21.735  52.006  1.00 86.62  ? 233 MET B N     1 
ATOM   5791 C  CA    . MET B 1 206 ? 31.555  20.964  52.822  1.00 89.53  ? 233 MET B CA    1 
ATOM   5792 C  C     . MET B 1 206 ? 32.992  21.333  52.485  1.00 79.95  ? 233 MET B C     1 
ATOM   5793 O  O     . MET B 1 206 ? 33.379  21.325  51.312  1.00 79.03  ? 233 MET B O     1 
ATOM   5794 C  CB    . MET B 1 206 ? 31.346  19.458  52.620  1.00 81.82  ? 233 MET B CB    1 
ATOM   5795 C  CG    . MET B 1 206 ? 32.432  18.600  53.252  1.00 78.28  ? 233 MET B CG    1 
ATOM   5796 S  SD    . MET B 1 206 ? 32.394  18.614  55.058  1.00 87.07  ? 233 MET B SD    1 
ATOM   5797 C  CE    . MET B 1 206 ? 30.946  17.613  55.385  1.00 92.87  ? 233 MET B CE    1 
ATOM   5798 N  N     . VAL B 1 207 ? 33.773  21.652  53.518  1.00 79.41  ? 234 VAL B N     1 
ATOM   5799 C  CA    . VAL B 1 207 ? 35.226  21.738  53.430  1.00 79.04  ? 234 VAL B CA    1 
ATOM   5800 C  C     . VAL B 1 207 ? 35.801  21.075  54.672  1.00 73.00  ? 234 VAL B C     1 
ATOM   5801 O  O     . VAL B 1 207 ? 35.169  21.045  55.732  1.00 85.40  ? 234 VAL B O     1 
ATOM   5802 C  CB    . VAL B 1 207 ? 35.753  23.189  53.310  1.00 70.14  ? 234 VAL B CB    1 
ATOM   5803 C  CG1   . VAL B 1 207 ? 35.168  23.887  52.095  1.00 75.09  ? 234 VAL B CG1   1 
ATOM   5804 C  CG2   . VAL B 1 207 ? 35.464  23.970  54.574  1.00 70.21  ? 234 VAL B CG2   1 
ATOM   5805 N  N     . HIS B 1 208 ? 37.009  20.534  54.537  1.00 77.09  ? 235 HIS B N     1 
ATOM   5806 C  CA    . HIS B 1 208 ? 37.658  19.843  55.641  1.00 69.36  ? 235 HIS B CA    1 
ATOM   5807 C  C     . HIS B 1 208 ? 39.167  19.889  55.436  1.00 72.69  ? 235 HIS B C     1 
ATOM   5808 O  O     . HIS B 1 208 ? 39.664  20.511  54.493  1.00 80.56  ? 235 HIS B O     1 
ATOM   5809 C  CB    . HIS B 1 208 ? 37.141  18.405  55.764  1.00 79.92  ? 235 HIS B CB    1 
ATOM   5810 C  CG    . HIS B 1 208 ? 37.156  17.639  54.475  1.00 73.91  ? 235 HIS B CG    1 
ATOM   5811 N  ND1   . HIS B 1 208 ? 38.224  16.859  54.086  1.00 69.48  ? 235 HIS B ND1   1 
ATOM   5812 C  CD2   . HIS B 1 208 ? 36.231  17.528  53.492  1.00 74.50  ? 235 HIS B CD2   1 
ATOM   5813 C  CE1   . HIS B 1 208 ? 37.958  16.304  52.916  1.00 76.29  ? 235 HIS B CE1   1 
ATOM   5814 N  NE2   . HIS B 1 208 ? 36.755  16.694  52.534  1.00 71.85  ? 235 HIS B NE2   1 
ATOM   5815 N  N     . SER B 1 209 ? 39.889  19.241  56.358  1.00 76.53  ? 236 SER B N     1 
ATOM   5816 C  CA    . SER B 1 209 ? 41.331  19.004  56.287  1.00 75.53  ? 236 SER B CA    1 
ATOM   5817 C  C     . SER B 1 209 ? 42.145  20.247  56.639  1.00 81.88  ? 236 SER B C     1 
ATOM   5818 O  O     . SER B 1 209 ? 42.861  20.253  57.647  1.00 75.00  ? 236 SER B O     1 
ATOM   5819 C  CB    . SER B 1 209 ? 41.715  18.466  54.907  1.00 73.11  ? 236 SER B CB    1 
ATOM   5820 O  OG    . SER B 1 209 ? 40.985  17.285  54.616  1.00 88.36  ? 236 SER B OG    1 
ATOM   5821 N  N     . THR B 1 210 ? 42.062  21.291  55.815  1.00 79.69  ? 237 THR B N     1 
ATOM   5822 C  CA    . THR B 1 210 ? 42.642  22.591  56.129  1.00 73.00  ? 237 THR B CA    1 
ATOM   5823 C  C     . THR B 1 210 ? 41.625  23.669  55.809  1.00 75.19  ? 237 THR B C     1 
ATOM   5824 O  O     . THR B 1 210 ? 41.097  23.717  54.694  1.00 84.91  ? 237 THR B O     1 
ATOM   5825 C  CB    . THR B 1 210 ? 43.931  22.872  55.346  1.00 62.81  ? 237 THR B CB    1 
ATOM   5826 O  OG1   . THR B 1 210 ? 43.713  22.617  53.956  1.00 107.19 ? 237 THR B OG1   1 
ATOM   5827 C  CG2   . THR B 1 210 ? 45.072  22.013  55.838  1.00 64.89  ? 237 THR B CG2   1 
ATOM   5828 N  N     . PHE B 1 211 ? 41.357  24.535  56.777  1.00 77.01  ? 238 PHE B N     1 
ATOM   5829 C  CA    . PHE B 1 211 ? 40.494  25.677  56.528  1.00 76.40  ? 238 PHE B CA    1 
ATOM   5830 C  C     . PHE B 1 211 ? 40.794  26.750  57.561  1.00 74.74  ? 238 PHE B C     1 
ATOM   5831 O  O     . PHE B 1 211 ? 41.453  26.503  58.575  1.00 73.76  ? 238 PHE B O     1 
ATOM   5832 C  CB    . PHE B 1 211 ? 39.014  25.279  56.540  1.00 66.28  ? 238 PHE B CB    1 
ATOM   5833 C  CG    . PHE B 1 211 ? 38.602  24.478  57.740  1.00 79.52  ? 238 PHE B CG    1 
ATOM   5834 C  CD1   . PHE B 1 211 ? 38.153  25.105  58.891  1.00 74.75  ? 238 PHE B CD1   1 
ATOM   5835 C  CD2   . PHE B 1 211 ? 38.644  23.094  57.710  1.00 71.72  ? 238 PHE B CD2   1 
ATOM   5836 C  CE1   . PHE B 1 211 ? 37.762  24.366  59.993  1.00 76.87  ? 238 PHE B CE1   1 
ATOM   5837 C  CE2   . PHE B 1 211 ? 38.261  22.352  58.806  1.00 61.14  ? 238 PHE B CE2   1 
ATOM   5838 C  CZ    . PHE B 1 211 ? 37.819  22.987  59.950  1.00 72.53  ? 238 PHE B CZ    1 
ATOM   5839 N  N     . LEU B 1 212 ? 40.300  27.951  57.280  1.00 72.74  ? 239 LEU B N     1 
ATOM   5840 C  CA    . LEU B 1 212 ? 40.504  29.125  58.113  1.00 59.53  ? 239 LEU B CA    1 
ATOM   5841 C  C     . LEU B 1 212 ? 39.148  29.601  58.606  1.00 72.42  ? 239 LEU B C     1 
ATOM   5842 O  O     . LEU B 1 212 ? 38.211  29.737  57.811  1.00 77.29  ? 239 LEU B O     1 
ATOM   5843 C  CB    . LEU B 1 212 ? 41.201  30.231  57.318  1.00 60.75  ? 239 LEU B CB    1 
ATOM   5844 C  CG    . LEU B 1 212 ? 41.762  31.425  58.086  1.00 71.75  ? 239 LEU B CG    1 
ATOM   5845 C  CD1   . LEU B 1 212 ? 42.897  30.993  59.011  1.00 64.14  ? 239 LEU B CD1   1 
ATOM   5846 C  CD2   . LEU B 1 212 ? 42.237  32.487  57.108  1.00 69.30  ? 239 LEU B CD2   1 
ATOM   5847 N  N     . ILE B 1 213 ? 39.037  29.841  59.910  1.00 62.50  ? 240 ILE B N     1 
ATOM   5848 C  CA    . ILE B 1 213 ? 37.819  30.375  60.508  1.00 53.71  ? 240 ILE B CA    1 
ATOM   5849 C  C     . ILE B 1 213 ? 38.085  31.808  60.941  1.00 73.95  ? 240 ILE B C     1 
ATOM   5850 O  O     . ILE B 1 213 ? 39.092  32.088  61.604  1.00 71.88  ? 240 ILE B O     1 
ATOM   5851 C  CB    . ILE B 1 213 ? 37.339  29.529  61.697  1.00 66.66  ? 240 ILE B CB    1 
ATOM   5852 C  CG1   . ILE B 1 213 ? 37.296  28.049  61.326  1.00 61.57  ? 240 ILE B CG1   1 
ATOM   5853 C  CG2   . ILE B 1 213 ? 35.970  30.008  62.160  1.00 61.69  ? 240 ILE B CG2   1 
ATOM   5854 C  CD1   . ILE B 1 213 ? 36.774  27.166  62.449  1.00 69.21  ? 240 ILE B CD1   1 
ATOM   5855 N  N     . ASP B 1 214 ? 37.181  32.711  60.568  1.00 80.40  ? 241 ASP B N     1 
ATOM   5856 C  CA    . ASP B 1 214 ? 37.305  34.132  60.885  1.00 65.32  ? 241 ASP B CA    1 
ATOM   5857 C  C     . ASP B 1 214 ? 36.600  34.384  62.212  1.00 74.77  ? 241 ASP B C     1 
ATOM   5858 O  O     . ASP B 1 214 ? 35.376  34.529  62.260  1.00 74.19  ? 241 ASP B O     1 
ATOM   5859 C  CB    . ASP B 1 214 ? 36.712  34.978  59.765  1.00 62.00  ? 241 ASP B CB    1 
ATOM   5860 C  CG    . ASP B 1 214 ? 37.159  36.425  59.824  1.00 73.02  ? 241 ASP B CG    1 
ATOM   5861 O  OD1   . ASP B 1 214 ? 37.399  36.938  60.940  1.00 66.68  ? 241 ASP B OD1   1 
ATOM   5862 O  OD2   . ASP B 1 214 ? 37.276  37.047  58.745  1.00 76.66  ? 241 ASP B OD2   1 
ATOM   5863 N  N     . LEU B 1 215 ? 37.375  34.435  63.296  1.00 74.79  ? 242 LEU B N     1 
ATOM   5864 C  CA    . LEU B 1 215 ? 36.812  34.693  64.615  1.00 66.16  ? 242 LEU B CA    1 
ATOM   5865 C  C     . LEU B 1 215 ? 36.525  36.166  64.856  1.00 69.44  ? 242 LEU B C     1 
ATOM   5866 O  O     . LEU B 1 215 ? 36.021  36.516  65.929  1.00 67.10  ? 242 LEU B O     1 
ATOM   5867 C  CB    . LEU B 1 215 ? 37.745  34.163  65.704  1.00 63.73  ? 242 LEU B CB    1 
ATOM   5868 C  CG    . LEU B 1 215 ? 38.051  32.669  65.609  1.00 71.12  ? 242 LEU B CG    1 
ATOM   5869 C  CD1   . LEU B 1 215 ? 38.889  32.222  66.791  1.00 69.39  ? 242 LEU B CD1   1 
ATOM   5870 C  CD2   . LEU B 1 215 ? 36.766  31.860  65.516  1.00 68.22  ? 242 LEU B CD2   1 
ATOM   5871 N  N     . ARG B 1 216 ? 36.846  37.039  63.900  1.00 71.75  ? 243 ARG B N     1 
ATOM   5872 C  CA    . ARG B 1 216 ? 36.330  38.400  63.967  1.00 65.78  ? 243 ARG B CA    1 
ATOM   5873 C  C     . ARG B 1 216 ? 34.849  38.440  63.619  1.00 72.01  ? 243 ARG B C     1 
ATOM   5874 O  O     . ARG B 1 216 ? 34.101  39.240  64.189  1.00 66.39  ? 243 ARG B O     1 
ATOM   5875 C  CB    . ARG B 1 216 ? 37.110  39.308  63.022  1.00 67.99  ? 243 ARG B CB    1 
ATOM   5876 C  CG    . ARG B 1 216 ? 38.614  39.169  63.105  1.00 67.77  ? 243 ARG B CG    1 
ATOM   5877 C  CD    . ARG B 1 216 ? 39.242  39.891  61.934  1.00 70.82  ? 243 ARG B CD    1 
ATOM   5878 N  NE    . ARG B 1 216 ? 38.565  39.556  60.687  1.00 73.54  ? 243 ARG B NE    1 
ATOM   5879 C  CZ    . ARG B 1 216 ? 38.572  40.319  59.602  1.00 75.20  ? 243 ARG B CZ    1 
ATOM   5880 N  NH1   . ARG B 1 216 ? 39.217  41.473  59.573  1.00 84.62  ? 243 ARG B NH1   1 
ATOM   5881 N  NH2   . ARG B 1 216 ? 37.910  39.915  58.522  1.00 67.00  ? 243 ARG B NH2   1 
ATOM   5882 N  N     . LYS B 1 217 ? 34.413  37.579  62.699  1.00 74.80  ? 244 LYS B N     1 
ATOM   5883 C  CA    . LYS B 1 217 ? 33.018  37.544  62.285  1.00 68.51  ? 244 LYS B CA    1 
ATOM   5884 C  C     . LYS B 1 217 ? 32.123  37.151  63.451  1.00 69.76  ? 244 LYS B C     1 
ATOM   5885 O  O     . LYS B 1 217 ? 32.410  36.192  64.174  1.00 73.31  ? 244 LYS B O     1 
ATOM   5886 C  CB    . LYS B 1 217 ? 32.840  36.558  61.133  1.00 68.71  ? 244 LYS B CB    1 
ATOM   5887 C  CG    . LYS B 1 217 ? 33.594  36.928  59.877  1.00 64.33  ? 244 LYS B CG    1 
ATOM   5888 C  CD    . LYS B 1 217 ? 33.265  38.337  59.436  1.00 62.55  ? 244 LYS B CD    1 
ATOM   5889 C  CE    . LYS B 1 217 ? 33.737  38.584  58.012  1.00 79.93  ? 244 LYS B CE    1 
ATOM   5890 N  NZ    . LYS B 1 217 ? 35.167  38.216  57.815  1.00 71.39  ? 244 LYS B NZ    1 
ATOM   5891 N  N     . ALA B 1 218 ? 31.031  37.898  63.629  1.00 69.72  ? 245 ALA B N     1 
ATOM   5892 C  CA    . ALA B 1 218 ? 30.118  37.620  64.732  1.00 62.66  ? 245 ALA B CA    1 
ATOM   5893 C  C     . ALA B 1 218 ? 29.427  36.274  64.569  1.00 74.05  ? 245 ALA B C     1 
ATOM   5894 O  O     . ALA B 1 218 ? 29.038  35.656  65.566  1.00 72.31  ? 245 ALA B O     1 
ATOM   5895 C  CB    . ALA B 1 218 ? 29.078  38.731  64.849  1.00 64.80  ? 245 ALA B CB    1 
ATOM   5896 N  N     . ALA B 1 219 ? 29.255  35.810  63.329  1.00 70.93  ? 246 ALA B N     1 
ATOM   5897 C  CA    . ALA B 1 219 ? 28.578  34.538  63.120  1.00 65.07  ? 246 ALA B CA    1 
ATOM   5898 C  C     . ALA B 1 219 ? 29.427  33.371  63.602  1.00 69.17  ? 246 ALA B C     1 
ATOM   5899 O  O     . ALA B 1 219 ? 28.885  32.316  63.948  1.00 79.17  ? 246 ALA B O     1 
ATOM   5900 C  CB    . ALA B 1 219 ? 28.224  34.366  61.640  1.00 81.21  ? 246 ALA B CB    1 
ATOM   5901 N  N     . SER B 1 220 ? 30.753  33.539  63.632  1.00 72.17  ? 247 SER B N     1 
ATOM   5902 C  CA    . SER B 1 220 ? 31.631  32.456  64.060  1.00 80.59  ? 247 SER B CA    1 
ATOM   5903 C  C     . SER B 1 220 ? 31.403  32.071  65.516  1.00 81.90  ? 247 SER B C     1 
ATOM   5904 O  O     . SER B 1 220 ? 31.732  30.944  65.904  1.00 72.48  ? 247 SER B O     1 
ATOM   5905 C  CB    . SER B 1 220 ? 33.094  32.850  63.840  1.00 74.79  ? 247 SER B CB    1 
ATOM   5906 O  OG    . SER B 1 220 ? 33.486  33.883  64.724  1.00 71.25  ? 247 SER B OG    1 
ATOM   5907 N  N     . ARG B 1 221 ? 30.838  32.973  66.324  1.00 74.14  ? 248 ARG B N     1 
ATOM   5908 C  CA    . ARG B 1 221 ? 30.584  32.665  67.727  1.00 76.86  ? 248 ARG B CA    1 
ATOM   5909 C  C     . ARG B 1 221 ? 29.628  31.495  67.900  1.00 79.77  ? 248 ARG B C     1 
ATOM   5910 O  O     . ARG B 1 221 ? 29.641  30.856  68.958  1.00 75.11  ? 248 ARG B O     1 
ATOM   5911 C  CB    . ARG B 1 221 ? 30.035  33.896  68.448  1.00 62.32  ? 248 ARG B CB    1 
ATOM   5912 C  CG    . ARG B 1 221 ? 31.018  35.058  68.515  1.00 71.14  ? 248 ARG B CG    1 
ATOM   5913 C  CD    . ARG B 1 221 ? 30.472  36.223  69.320  1.00 76.12  ? 248 ARG B CD    1 
ATOM   5914 N  NE    . ARG B 1 221 ? 30.176  35.856  70.700  1.00 104.16 ? 248 ARG B NE    1 
ATOM   5915 C  CZ    . ARG B 1 221 ? 31.073  35.818  71.677  1.00 109.39 ? 248 ARG B CZ    1 
ATOM   5916 N  NH1   . ARG B 1 221 ? 32.348  36.096  71.457  1.00 104.37 ? 248 ARG B NH1   1 
ATOM   5917 N  NH2   . ARG B 1 221 ? 30.681  35.490  72.905  1.00 106.34 ? 248 ARG B NH2   1 
ATOM   5918 N  N     . ASN B 1 222 ? 28.815  31.193  66.887  1.00 82.24  ? 249 ASN B N     1 
ATOM   5919 C  CA    . ASN B 1 222 ? 27.863  30.090  66.941  1.00 67.79  ? 249 ASN B CA    1 
ATOM   5920 C  C     . ASN B 1 222 ? 28.405  28.793  66.353  1.00 75.28  ? 249 ASN B C     1 
ATOM   5921 O  O     . ASN B 1 222 ? 27.721  27.765  66.425  1.00 72.42  ? 249 ASN B O     1 
ATOM   5922 C  CB    . ASN B 1 222 ? 26.576  30.477  66.209  1.00 68.67  ? 249 ASN B CB    1 
ATOM   5923 C  CG    . ASN B 1 222 ? 25.878  31.651  66.851  1.00 81.13  ? 249 ASN B CG    1 
ATOM   5924 O  OD1   . ASN B 1 222 ? 25.761  31.720  68.073  1.00 83.99  ? 249 ASN B OD1   1 
ATOM   5925 N  ND2   . ASN B 1 222 ? 25.415  32.590  66.031  1.00 90.90  ? 249 ASN B ND2   1 
ATOM   5926 N  N     . LEU B 1 223 ? 29.600  28.811  65.770  1.00 77.31  ? 250 LEU B N     1 
ATOM   5927 C  CA    . LEU B 1 223 ? 30.183  27.590  65.236  1.00 72.50  ? 250 LEU B CA    1 
ATOM   5928 C  C     . LEU B 1 223 ? 30.667  26.692  66.369  1.00 71.74  ? 250 LEU B C     1 
ATOM   5929 O  O     . LEU B 1 223 ? 31.082  27.162  67.431  1.00 77.04  ? 250 LEU B O     1 
ATOM   5930 C  CB    . LEU B 1 223 ? 31.338  27.917  64.291  1.00 70.28  ? 250 LEU B CB    1 
ATOM   5931 C  CG    . LEU B 1 223 ? 30.968  28.732  63.051  1.00 70.82  ? 250 LEU B CG    1 
ATOM   5932 C  CD1   . LEU B 1 223 ? 32.213  29.189  62.314  1.00 60.26  ? 250 LEU B CD1   1 
ATOM   5933 C  CD2   . LEU B 1 223 ? 30.074  27.922  62.135  1.00 69.14  ? 250 LEU B CD2   1 
ATOM   5934 N  N     . ALA B 1 224 ? 30.613  25.383  66.131  1.00 72.22  ? 251 ALA B N     1 
ATOM   5935 C  CA    . ALA B 1 224 ? 30.955  24.414  67.163  1.00 68.79  ? 251 ALA B CA    1 
ATOM   5936 C  C     . ALA B 1 224 ? 31.308  23.085  66.514  1.00 74.82  ? 251 ALA B C     1 
ATOM   5937 O  O     . ALA B 1 224 ? 30.550  22.578  65.681  1.00 76.89  ? 251 ALA B O     1 
ATOM   5938 C  CB    . ALA B 1 224 ? 29.795  24.233  68.147  1.00 62.99  ? 251 ALA B CB    1 
ATOM   5939 N  N     . PHE B 1 225 ? 32.454  22.523  66.903  1.00 77.71  ? 252 PHE B N     1 
ATOM   5940 C  CA    . PHE B 1 225 ? 32.841  21.207  66.411  1.00 70.47  ? 252 PHE B CA    1 
ATOM   5941 C  C     . PHE B 1 225 ? 32.173  20.089  67.196  1.00 71.33  ? 252 PHE B C     1 
ATOM   5942 O  O     . PHE B 1 225 ? 31.891  19.025  66.633  1.00 76.92  ? 252 PHE B O     1 
ATOM   5943 C  CB    . PHE B 1 225 ? 34.360  21.046  66.467  1.00 63.58  ? 252 PHE B CB    1 
ATOM   5944 C  CG    . PHE B 1 225 ? 35.097  21.919  65.498  1.00 63.29  ? 252 PHE B CG    1 
ATOM   5945 C  CD1   . PHE B 1 225 ? 35.281  21.516  64.191  1.00 56.79  ? 252 PHE B CD1   1 
ATOM   5946 C  CD2   . PHE B 1 225 ? 35.606  23.143  65.894  1.00 65.65  ? 252 PHE B CD2   1 
ATOM   5947 C  CE1   . PHE B 1 225 ? 35.962  22.311  63.296  1.00 58.96  ? 252 PHE B CE1   1 
ATOM   5948 C  CE2   . PHE B 1 225 ? 36.286  23.943  65.004  1.00 67.52  ? 252 PHE B CE2   1 
ATOM   5949 C  CZ    . PHE B 1 225 ? 36.464  23.526  63.701  1.00 67.62  ? 252 PHE B CZ    1 
ATOM   5950 N  N     . TYR B 1 226 ? 31.915  20.311  68.487  1.00 66.29  ? 253 TYR B N     1 
ATOM   5951 C  CA    . TYR B 1 226 ? 31.286  19.339  69.363  1.00 73.20  ? 253 TYR B CA    1 
ATOM   5952 C  C     . TYR B 1 226 ? 30.571  20.090  70.477  1.00 81.44  ? 253 TYR B C     1 
ATOM   5953 O  O     . TYR B 1 226 ? 31.063  21.142  70.914  1.00 86.04  ? 253 TYR B O     1 
ATOM   5954 C  CB    . TYR B 1 226 ? 32.314  18.373  69.958  1.00 75.59  ? 253 TYR B CB    1 
ATOM   5955 C  CG    . TYR B 1 226 ? 31.712  17.178  70.660  1.00 77.96  ? 253 TYR B CG    1 
ATOM   5956 C  CD1   . TYR B 1 226 ? 31.330  16.049  69.944  1.00 77.57  ? 253 TYR B CD1   1 
ATOM   5957 C  CD2   . TYR B 1 226 ? 31.527  17.175  72.036  1.00 72.43  ? 253 TYR B CD2   1 
ATOM   5958 C  CE1   . TYR B 1 226 ? 30.786  14.947  70.579  1.00 84.66  ? 253 TYR B CE1   1 
ATOM   5959 C  CE2   . TYR B 1 226 ? 30.977  16.078  72.681  1.00 87.07  ? 253 TYR B CE2   1 
ATOM   5960 C  CZ    . TYR B 1 226 ? 30.611  14.966  71.947  1.00 89.47  ? 253 TYR B CZ    1 
ATOM   5961 O  OH    . TYR B 1 226 ? 30.068  13.870  72.581  1.00 92.97  ? 253 TYR B OH    1 
ATOM   5962 N  N     . PRO B 1 227 ? 29.409  19.605  70.939  1.00 77.91  ? 254 PRO B N     1 
ATOM   5963 C  CA    . PRO B 1 227 ? 28.640  18.453  70.445  1.00 79.26  ? 254 PRO B CA    1 
ATOM   5964 C  C     . PRO B 1 227 ? 27.876  18.807  69.179  1.00 78.14  ? 254 PRO B C     1 
ATOM   5965 O  O     . PRO B 1 227 ? 27.883  19.962  68.766  1.00 80.48  ? 254 PRO B O     1 
ATOM   5966 C  CB    . PRO B 1 227 ? 27.712  18.139  71.623  1.00 59.36  ? 254 PRO B CB    1 
ATOM   5967 C  CG    . PRO B 1 227 ? 27.459  19.475  72.240  1.00 59.66  ? 254 PRO B CG    1 
ATOM   5968 C  CD    . PRO B 1 227 ? 28.772  20.211  72.122  1.00 74.87  ? 254 PRO B CD    1 
ATOM   5969 N  N     . PRO B 1 228 ? 27.229  17.845  68.524  1.00 81.65  ? 255 PRO B N     1 
ATOM   5970 C  CA    . PRO B 1 228 ? 26.392  18.189  67.371  1.00 90.84  ? 255 PRO B CA    1 
ATOM   5971 C  C     . PRO B 1 228 ? 25.306  19.182  67.756  1.00 82.28  ? 255 PRO B C     1 
ATOM   5972 O  O     . PRO B 1 228 ? 24.859  19.238  68.904  1.00 91.22  ? 255 PRO B O     1 
ATOM   5973 C  CB    . PRO B 1 228 ? 25.795  16.840  66.950  1.00 83.87  ? 255 PRO B CB    1 
ATOM   5974 C  CG    . PRO B 1 228 ? 26.797  15.839  67.410  1.00 81.99  ? 255 PRO B CG    1 
ATOM   5975 C  CD    . PRO B 1 228 ? 27.359  16.388  68.692  1.00 77.14  ? 255 PRO B CD    1 
ATOM   5976 N  N     . HIS B 1 229 ? 24.894  19.982  66.775  1.00 83.43  ? 256 HIS B N     1 
ATOM   5977 C  CA    . HIS B 1 229 ? 23.825  20.956  66.946  1.00 82.53  ? 256 HIS B CA    1 
ATOM   5978 C  C     . HIS B 1 229 ? 22.571  20.258  67.449  1.00 84.27  ? 256 HIS B C     1 
ATOM   5979 O  O     . HIS B 1 229 ? 22.342  19.094  67.104  1.00 89.58  ? 256 HIS B O     1 
ATOM   5980 C  CB    . HIS B 1 229 ? 23.563  21.678  65.621  1.00 77.32  ? 256 HIS B CB    1 
ATOM   5981 C  CG    . HIS B 1 229 ? 22.732  22.917  65.753  1.00 90.69  ? 256 HIS B CG    1 
ATOM   5982 N  ND1   . HIS B 1 229 ? 21.353  22.899  65.735  1.00 89.60  ? 256 HIS B ND1   1 
ATOM   5983 C  CD2   . HIS B 1 229 ? 23.087  24.214  65.909  1.00 87.11  ? 256 HIS B CD2   1 
ATOM   5984 C  CE1   . HIS B 1 229 ? 20.895  24.131  65.869  1.00 94.18  ? 256 HIS B CE1   1 
ATOM   5985 N  NE2   . HIS B 1 229 ? 21.927  24.948  65.976  1.00 94.19  ? 256 HIS B NE2   1 
ATOM   5986 N  N     . PRO B 1 230 ? 21.750  20.914  68.271  1.00 81.82  ? 257 PRO B N     1 
ATOM   5987 C  CA    . PRO B 1 230 ? 20.538  20.248  68.779  1.00 84.82  ? 257 PRO B CA    1 
ATOM   5988 C  C     . PRO B 1 230 ? 19.626  19.698  67.695  1.00 86.82  ? 257 PRO B C     1 
ATOM   5989 O  O     . PRO B 1 230 ? 18.875  18.750  67.954  1.00 91.82  ? 257 PRO B O     1 
ATOM   5990 C  CB    . PRO B 1 230 ? 19.854  21.360  69.583  1.00 89.18  ? 257 PRO B CB    1 
ATOM   5991 C  CG    . PRO B 1 230 ? 20.977  22.226  70.037  1.00 75.63  ? 257 PRO B CG    1 
ATOM   5992 C  CD    . PRO B 1 230 ? 21.981  22.215  68.924  1.00 76.22  ? 257 PRO B CD    1 
ATOM   5993 N  N     . ASP B 1 231 ? 19.671  20.256  66.486  1.00 90.22  ? 258 ASP B N     1 
ATOM   5994 C  CA    . ASP B 1 231 ? 18.856  19.782  65.375  1.00 89.21  ? 258 ASP B CA    1 
ATOM   5995 C  C     . ASP B 1 231 ? 19.563  18.736  64.522  1.00 94.06  ? 258 ASP B C     1 
ATOM   5996 O  O     . ASP B 1 231 ? 18.959  18.221  63.574  1.00 98.97  ? 258 ASP B O     1 
ATOM   5997 C  CB    . ASP B 1 231 ? 18.436  20.964  64.497  1.00 78.98  ? 258 ASP B CB    1 
ATOM   5998 C  CG    . ASP B 1 231 ? 17.624  21.996  65.257  1.00 98.58  ? 258 ASP B CG    1 
ATOM   5999 O  OD1   . ASP B 1 231 ? 16.820  21.595  66.128  1.00 93.48  ? 258 ASP B OD1   1 
ATOM   6000 O  OD2   . ASP B 1 231 ? 17.788  23.206  64.986  1.00 103.62 ? 258 ASP B OD2   1 
ATOM   6001 N  N     . TYR B 1 232 ? 20.813  18.405  64.842  1.00 93.90  ? 259 TYR B N     1 
ATOM   6002 C  CA    . TYR B 1 232 ? 21.592  17.479  64.029  1.00 92.30  ? 259 TYR B CA    1 
ATOM   6003 C  C     . TYR B 1 232 ? 21.038  16.063  64.138  1.00 91.40  ? 259 TYR B C     1 
ATOM   6004 O  O     . TYR B 1 232 ? 20.878  15.528  65.240  1.00 95.05  ? 259 TYR B O     1 
ATOM   6005 C  CB    . TYR B 1 232 ? 23.052  17.512  64.467  1.00 83.36  ? 259 TYR B CB    1 
ATOM   6006 C  CG    . TYR B 1 232 ? 23.980  16.657  63.638  1.00 87.11  ? 259 TYR B CG    1 
ATOM   6007 C  CD1   . TYR B 1 232 ? 24.527  17.139  62.459  1.00 89.13  ? 259 TYR B CD1   1 
ATOM   6008 C  CD2   . TYR B 1 232 ? 24.327  15.376  64.046  1.00 83.22  ? 259 TYR B CD2   1 
ATOM   6009 C  CE1   . TYR B 1 232 ? 25.386  16.368  61.704  1.00 92.73  ? 259 TYR B CE1   1 
ATOM   6010 C  CE2   . TYR B 1 232 ? 25.182  14.598  63.296  1.00 83.92  ? 259 TYR B CE2   1 
ATOM   6011 C  CZ    . TYR B 1 232 ? 25.709  15.100  62.128  1.00 90.72  ? 259 TYR B CZ    1 
ATOM   6012 O  OH    . TYR B 1 232 ? 26.563  14.332  61.375  1.00 100.07 ? 259 TYR B OH    1 
ATOM   6013 N  N     . THR B 1 233 ? 20.752  15.453  62.990  1.00 86.54  ? 260 THR B N     1 
ATOM   6014 C  CA    . THR B 1 233 ? 20.160  14.120  62.937  1.00 94.05  ? 260 THR B CA    1 
ATOM   6015 C  C     . THR B 1 233 ? 20.846  13.270  61.875  1.00 98.91  ? 260 THR B C     1 
ATOM   6016 O  O     . THR B 1 233 ? 20.213  12.443  61.210  1.00 111.67 ? 260 THR B O     1 
ATOM   6017 C  CB    . THR B 1 233 ? 18.659  14.201  62.670  1.00 92.90  ? 260 THR B CB    1 
ATOM   6018 O  OG1   . THR B 1 233 ? 18.428  14.989  61.496  1.00 96.46  ? 260 THR B OG1   1 
ATOM   6019 C  CG2   . THR B 1 233 ? 17.941  14.839  63.852  1.00 94.11  ? 260 THR B CG2   1 
ATOM   6020 N  N     . TRP B 1 234 ? 22.149  13.458  61.702  1.00 105.35 ? 261 TRP B N     1 
ATOM   6021 C  CA    . TRP B 1 234 ? 22.923  12.784  60.671  1.00 99.90  ? 261 TRP B CA    1 
ATOM   6022 C  C     . TRP B 1 234 ? 23.921  11.817  61.312  1.00 103.64 ? 261 TRP B C     1 
ATOM   6023 O  O     . TRP B 1 234 ? 23.902  11.581  62.526  1.00 102.97 ? 261 TRP B O     1 
ATOM   6024 C  CB    . TRP B 1 234 ? 23.620  13.818  59.779  1.00 92.22  ? 261 TRP B CB    1 
ATOM   6025 C  CG    . TRP B 1 234 ? 22.677  14.614  58.926  1.00 102.23 ? 261 TRP B CG    1 
ATOM   6026 C  CD1   . TRP B 1 234 ? 21.349  14.366  58.718  1.00 112.40 ? 261 TRP B CD1   1 
ATOM   6027 C  CD2   . TRP B 1 234 ? 22.988  15.789  58.166  1.00 101.54 ? 261 TRP B CD2   1 
ATOM   6028 N  NE1   . TRP B 1 234 ? 20.817  15.312  57.874  1.00 114.57 ? 261 TRP B NE1   1 
ATOM   6029 C  CE2   . TRP B 1 234 ? 21.803  16.197  57.522  1.00 107.94 ? 261 TRP B CE2   1 
ATOM   6030 C  CE3   . TRP B 1 234 ? 24.153  16.535  57.968  1.00 100.41 ? 261 TRP B CE3   1 
ATOM   6031 C  CZ2   . TRP B 1 234 ? 21.751  17.317  56.696  1.00 110.99 ? 261 TRP B CZ2   1 
ATOM   6032 C  CZ3   . TRP B 1 234 ? 24.102  17.647  57.146  1.00 96.43  ? 261 TRP B CZ3   1 
ATOM   6033 C  CH2   . TRP B 1 234 ? 22.908  18.028  56.521  1.00 104.49 ? 261 TRP B CH2   1 
ATOM   6034 N  N     . SER B 1 235 ? 24.795  11.253  60.483  1.00 99.48  ? 262 SER B N     1 
ATOM   6035 C  CA    . SER B 1 235 ? 25.772  10.285  60.957  1.00 97.37  ? 262 SER B CA    1 
ATOM   6036 C  C     . SER B 1 235 ? 26.764  10.939  61.911  1.00 91.89  ? 262 SER B C     1 
ATOM   6037 O  O     . SER B 1 235 ? 27.027  12.141  61.842  1.00 93.97  ? 262 SER B O     1 
ATOM   6038 C  CB    . SER B 1 235 ? 26.522  9.658   59.782  1.00 103.00 ? 262 SER B CB    1 
ATOM   6039 O  OG    . SER B 1 235 ? 25.648  8.913   58.951  1.00 133.51 ? 262 SER B OG    1 
ATOM   6040 N  N     . PHE B 1 236 ? 27.322  10.127  62.810  1.00 89.21  ? 263 PHE B N     1 
ATOM   6041 C  CA    . PHE B 1 236 ? 28.312  10.605  63.775  1.00 87.90  ? 263 PHE B CA    1 
ATOM   6042 C  C     . PHE B 1 236 ? 29.661  10.744  63.068  1.00 90.56  ? 263 PHE B C     1 
ATOM   6043 O  O     . PHE B 1 236 ? 30.600  9.971   63.270  1.00 94.70  ? 263 PHE B O     1 
ATOM   6044 C  CB    . PHE B 1 236 ? 28.384  9.663   64.970  1.00 93.17  ? 263 PHE B CB    1 
ATOM   6045 C  CG    . PHE B 1 236 ? 29.060  10.256  66.176  1.00 81.14  ? 263 PHE B CG    1 
ATOM   6046 C  CD1   . PHE B 1 236 ? 28.443  11.255  66.910  1.00 82.99  ? 263 PHE B CD1   1 
ATOM   6047 C  CD2   . PHE B 1 236 ? 30.301  9.803   66.585  1.00 85.22  ? 263 PHE B CD2   1 
ATOM   6048 C  CE1   . PHE B 1 236 ? 29.057  11.801  68.022  1.00 84.14  ? 263 PHE B CE1   1 
ATOM   6049 C  CE2   . PHE B 1 236 ? 30.921  10.346  67.696  1.00 94.47  ? 263 PHE B CE2   1 
ATOM   6050 C  CZ    . PHE B 1 236 ? 30.294  11.346  68.417  1.00 82.22  ? 263 PHE B CZ    1 
ATOM   6051 N  N     . ASP B 1 237 ? 29.739  11.760  62.209  1.00 85.98  ? 264 ASP B N     1 
ATOM   6052 C  CA    . ASP B 1 237 ? 30.925  12.056  61.417  1.00 75.72  ? 264 ASP B CA    1 
ATOM   6053 C  C     . ASP B 1 237 ? 31.396  13.459  61.766  1.00 81.29  ? 264 ASP B C     1 
ATOM   6054 O  O     . ASP B 1 237 ? 30.585  14.389  61.826  1.00 82.89  ? 264 ASP B O     1 
ATOM   6055 C  CB    . ASP B 1 237 ? 30.624  11.936  59.918  1.00 86.89  ? 264 ASP B CB    1 
ATOM   6056 C  CG    . ASP B 1 237 ? 31.878  11.826  59.067  1.00 99.76  ? 264 ASP B CG    1 
ATOM   6057 O  OD1   . ASP B 1 237 ? 32.815  12.627  59.271  1.00 101.35 ? 264 ASP B OD1   1 
ATOM   6058 O  OD2   . ASP B 1 237 ? 31.922  10.935  58.190  1.00 102.83 ? 264 ASP B OD2   1 
ATOM   6059 N  N     . ASP B 1 238 ? 32.705  13.609  61.996  1.00 84.61  ? 265 ASP B N     1 
ATOM   6060 C  CA    . ASP B 1 238 ? 33.227  14.881  62.489  1.00 73.16  ? 265 ASP B CA    1 
ATOM   6061 C  C     . ASP B 1 238 ? 33.043  15.997  61.467  1.00 80.64  ? 265 ASP B C     1 
ATOM   6062 O  O     . ASP B 1 238 ? 32.620  17.105  61.821  1.00 80.86  ? 265 ASP B O     1 
ATOM   6063 C  CB    . ASP B 1 238 ? 34.701  14.738  62.877  1.00 74.13  ? 265 ASP B CB    1 
ATOM   6064 C  CG    . ASP B 1 238 ? 35.575  14.275  61.730  1.00 74.73  ? 265 ASP B CG    1 
ATOM   6065 O  OD1   . ASP B 1 238 ? 35.035  13.848  60.689  1.00 80.05  ? 265 ASP B OD1   1 
ATOM   6066 O  OD2   . ASP B 1 238 ? 36.811  14.341  61.876  1.00 81.81  ? 265 ASP B OD2   1 
ATOM   6067 N  N     . ILE B 1 239 ? 33.342  15.726  60.195  1.00 78.35  ? 266 ILE B N     1 
ATOM   6068 C  CA    . ILE B 1 239 ? 33.226  16.773  59.186  1.00 73.22  ? 266 ILE B CA    1 
ATOM   6069 C  C     . ILE B 1 239 ? 31.765  17.101  58.913  1.00 80.29  ? 266 ILE B C     1 
ATOM   6070 O  O     . ILE B 1 239 ? 31.432  18.241  58.570  1.00 95.94  ? 266 ILE B O     1 
ATOM   6071 C  CB    . ILE B 1 239 ? 33.965  16.369  57.897  1.00 85.90  ? 266 ILE B CB    1 
ATOM   6072 C  CG1   . ILE B 1 239 ? 33.282  15.180  57.219  1.00 75.20  ? 266 ILE B CG1   1 
ATOM   6073 C  CG2   . ILE B 1 239 ? 35.412  16.038  58.203  1.00 61.85  ? 266 ILE B CG2   1 
ATOM   6074 C  CD1   . ILE B 1 239 ? 33.806  14.901  55.831  1.00 71.16  ? 266 ILE B CD1   1 
ATOM   6075 N  N     . ILE B 1 240 ? 30.872  16.123  59.061  1.00 82.60  ? 267 ILE B N     1 
ATOM   6076 C  CA    . ILE B 1 240 ? 29.457  16.385  58.837  1.00 73.82  ? 267 ILE B CA    1 
ATOM   6077 C  C     . ILE B 1 240 ? 28.883  17.209  59.981  1.00 79.86  ? 267 ILE B C     1 
ATOM   6078 O  O     . ILE B 1 240 ? 28.081  18.125  59.763  1.00 78.19  ? 267 ILE B O     1 
ATOM   6079 C  CB    . ILE B 1 240 ? 28.700  15.059  58.648  1.00 86.24  ? 267 ILE B CB    1 
ATOM   6080 C  CG1   . ILE B 1 240 ? 29.274  14.284  57.468  1.00 91.69  ? 267 ILE B CG1   1 
ATOM   6081 C  CG2   . ILE B 1 240 ? 27.237  15.311  58.404  1.00 88.90  ? 267 ILE B CG2   1 
ATOM   6082 C  CD1   . ILE B 1 240 ? 28.512  13.022  57.158  1.00 100.60 ? 267 ILE B CD1   1 
ATOM   6083 N  N     . VAL B 1 241 ? 29.293  16.908  61.216  1.00 85.04  ? 268 VAL B N     1 
ATOM   6084 C  CA    . VAL B 1 241 ? 28.804  17.662  62.368  1.00 79.07  ? 268 VAL B CA    1 
ATOM   6085 C  C     . VAL B 1 241 ? 29.171  19.132  62.235  1.00 76.29  ? 268 VAL B C     1 
ATOM   6086 O  O     . VAL B 1 241 ? 28.361  20.020  62.530  1.00 83.34  ? 268 VAL B O     1 
ATOM   6087 C  CB    . VAL B 1 241 ? 29.348  17.055  63.674  1.00 80.46  ? 268 VAL B CB    1 
ATOM   6088 C  CG1   . VAL B 1 241 ? 29.230  18.047  64.821  1.00 67.80  ? 268 VAL B CG1   1 
ATOM   6089 C  CG2   . VAL B 1 241 ? 28.600  15.775  64.008  1.00 84.29  ? 268 VAL B CG2   1 
ATOM   6090 N  N     . PHE B 1 242 ? 30.388  19.415  61.768  1.00 83.82  ? 269 PHE B N     1 
ATOM   6091 C  CA    . PHE B 1 242 ? 30.816  20.803  61.637  1.00 78.75  ? 269 PHE B CA    1 
ATOM   6092 C  C     . PHE B 1 242 ? 30.113  21.492  60.475  1.00 78.10  ? 269 PHE B C     1 
ATOM   6093 O  O     . PHE B 1 242 ? 29.645  22.627  60.614  1.00 81.26  ? 269 PHE B O     1 
ATOM   6094 C  CB    . PHE B 1 242 ? 32.335  20.878  61.474  1.00 67.99  ? 269 PHE B CB    1 
ATOM   6095 C  CG    . PHE B 1 242 ? 32.866  22.281  61.454  1.00 71.01  ? 269 PHE B CG    1 
ATOM   6096 C  CD1   . PHE B 1 242 ? 32.676  23.120  62.539  1.00 80.71  ? 269 PHE B CD1   1 
ATOM   6097 C  CD2   . PHE B 1 242 ? 33.547  22.766  60.352  1.00 82.60  ? 269 PHE B CD2   1 
ATOM   6098 C  CE1   . PHE B 1 242 ? 33.155  24.418  62.521  1.00 85.71  ? 269 PHE B CE1   1 
ATOM   6099 C  CE2   . PHE B 1 242 ? 34.031  24.060  60.331  1.00 79.09  ? 269 PHE B CE2   1 
ATOM   6100 C  CZ    . PHE B 1 242 ? 33.836  24.886  61.416  1.00 76.40  ? 269 PHE B CZ    1 
ATOM   6101 N  N     . ALA B 1 243 ? 30.023  20.821  59.321  1.00 78.02  ? 270 ALA B N     1 
ATOM   6102 C  CA    . ALA B 1 243 ? 29.350  21.414  58.168  1.00 80.65  ? 270 ALA B CA    1 
ATOM   6103 C  C     . ALA B 1 243 ? 27.907  21.775  58.496  1.00 79.60  ? 270 ALA B C     1 
ATOM   6104 O  O     . ALA B 1 243 ? 27.400  22.812  58.050  1.00 85.44  ? 270 ALA B O     1 
ATOM   6105 C  CB    . ALA B 1 243 ? 29.404  20.457  56.978  1.00 77.46  ? 270 ALA B CB    1 
ATOM   6106 N  N     . PHE B 1 244 ? 27.232  20.930  59.276  1.00 71.61  ? 271 PHE B N     1 
ATOM   6107 C  CA    . PHE B 1 244 ? 25.884  21.254  59.727  1.00 79.77  ? 271 PHE B CA    1 
ATOM   6108 C  C     . PHE B 1 244 ? 25.885  22.439  60.685  1.00 83.16  ? 271 PHE B C     1 
ATOM   6109 O  O     . PHE B 1 244 ? 24.899  23.181  60.751  1.00 87.22  ? 271 PHE B O     1 
ATOM   6110 C  CB    . PHE B 1 244 ? 25.252  20.030  60.392  1.00 76.02  ? 271 PHE B CB    1 
ATOM   6111 C  CG    . PHE B 1 244 ? 23.803  20.205  60.724  1.00 83.51  ? 271 PHE B CG    1 
ATOM   6112 C  CD1   . PHE B 1 244 ? 22.829  19.938  59.778  1.00 88.31  ? 271 PHE B CD1   1 
ATOM   6113 C  CD2   . PHE B 1 244 ? 23.411  20.631  61.983  1.00 87.63  ? 271 PHE B CD2   1 
ATOM   6114 C  CE1   . PHE B 1 244 ? 21.492  20.096  60.077  1.00 80.49  ? 271 PHE B CE1   1 
ATOM   6115 C  CE2   . PHE B 1 244 ? 22.074  20.789  62.290  1.00 87.80  ? 271 PHE B CE2   1 
ATOM   6116 C  CZ    . PHE B 1 244 ? 21.114  20.521  61.335  1.00 85.13  ? 271 PHE B CZ    1 
ATOM   6117 N  N     . SER B 1 245 ? 26.976  22.630  61.431  1.00 79.67  ? 272 SER B N     1 
ATOM   6118 C  CA    . SER B 1 245 ? 27.062  23.768  62.339  1.00 72.78  ? 272 SER B CA    1 
ATOM   6119 C  C     . SER B 1 245 ? 27.174  25.083  61.579  1.00 83.56  ? 272 SER B C     1 
ATOM   6120 O  O     . SER B 1 245 ? 26.706  26.120  62.064  1.00 92.06  ? 272 SER B O     1 
ATOM   6121 C  CB    . SER B 1 245 ? 28.252  23.596  63.282  1.00 65.81  ? 272 SER B CB    1 
ATOM   6122 O  OG    . SER B 1 245 ? 28.284  24.623  64.253  1.00 72.45  ? 272 SER B OG    1 
ATOM   6123 N  N     . CYS B 1 246 ? 27.790  25.061  60.395  1.00 87.61  ? 273 CYS B N     1 
ATOM   6124 C  CA    . CYS B 1 246 ? 27.876  26.269  59.583  1.00 70.90  ? 273 CYS B CA    1 
ATOM   6125 C  C     . CYS B 1 246 ? 26.523  26.617  58.974  1.00 87.19  ? 273 CYS B C     1 
ATOM   6126 O  O     . CYS B 1 246 ? 26.193  27.799  58.821  1.00 95.01  ? 273 CYS B O     1 
ATOM   6127 C  CB    . CYS B 1 246 ? 28.933  26.099  58.489  1.00 75.46  ? 273 CYS B CB    1 
ATOM   6128 S  SG    . CYS B 1 246 ? 30.601  25.672  59.080  1.00 75.77  ? 273 CYS B SG    1 
ATOM   6129 N  N     . LYS B 1 247 ? 25.724  25.604  58.620  1.00 79.67  ? 274 LYS B N     1 
ATOM   6130 C  CA    . LYS B 1 247 ? 24.395  25.870  58.075  1.00 88.53  ? 274 LYS B CA    1 
ATOM   6131 C  C     . LYS B 1 247 ? 23.505  26.557  59.102  1.00 89.04  ? 274 LYS B C     1 
ATOM   6132 O  O     . LYS B 1 247 ? 22.775  27.501  58.772  1.00 86.22  ? 274 LYS B O     1 
ATOM   6133 C  CB    . LYS B 1 247 ? 23.746  24.570  57.595  1.00 87.01  ? 274 LYS B CB    1 
ATOM   6134 C  CG    . LYS B 1 247 ? 24.160  24.129  56.199  1.00 110.19 ? 274 LYS B CG    1 
ATOM   6135 C  CD    . LYS B 1 247 ? 23.345  22.917  55.753  1.00 125.14 ? 274 LYS B CD    1 
ATOM   6136 C  CE    . LYS B 1 247 ? 23.621  22.547  54.301  1.00 125.80 ? 274 LYS B CE    1 
ATOM   6137 N  NZ    . LYS B 1 247 ? 22.712  21.467  53.815  1.00 106.76 ? 274 LYS B NZ    1 
ATOM   6138 N  N     . GLN B 1 248 ? 23.553  26.099  60.356  1.00 83.98  ? 275 GLN B N     1 
ATOM   6139 C  CA    . GLN B 1 248 ? 22.723  26.695  61.398  1.00 81.13  ? 275 GLN B CA    1 
ATOM   6140 C  C     . GLN B 1 248 ? 23.161  28.121  61.708  1.00 86.49  ? 275 GLN B C     1 
ATOM   6141 O  O     . GLN B 1 248 ? 22.320  29.018  61.844  1.00 114.77 ? 275 GLN B O     1 
ATOM   6142 C  CB    . GLN B 1 248 ? 22.759  25.830  62.656  1.00 91.38  ? 275 GLN B CB    1 
ATOM   6143 C  CG    . GLN B 1 248 ? 22.308  24.397  62.425  1.00 94.56  ? 275 GLN B CG    1 
ATOM   6144 C  CD    . GLN B 1 248 ? 20.904  24.311  61.852  1.00 97.85  ? 275 GLN B CD    1 
ATOM   6145 O  OE1   . GLN B 1 248 ? 20.702  23.799  60.750  1.00 98.25  ? 275 GLN B OE1   1 
ATOM   6146 N  NE2   . GLN B 1 248 ? 19.927  24.813  62.598  1.00 99.79  ? 275 GLN B NE2   1 
ATOM   6147 N  N     . ALA B 1 249 ? 24.468  28.350  61.825  1.00 87.46  ? 276 ALA B N     1 
ATOM   6148 C  CA    . ALA B 1 249 ? 24.982  29.704  61.987  1.00 86.11  ? 276 ALA B CA    1 
ATOM   6149 C  C     . ALA B 1 249 ? 24.893  30.520  60.704  1.00 89.13  ? 276 ALA B C     1 
ATOM   6150 O  O     . ALA B 1 249 ? 25.278  31.695  60.714  1.00 84.92  ? 276 ALA B O     1 
ATOM   6151 C  CB    . ALA B 1 249 ? 26.430  29.658  62.477  1.00 72.36  ? 276 ALA B CB    1 
ATOM   6152 N  N     . GLU B 1 250 ? 24.387  29.926  59.621  1.00 89.13  ? 277 GLU B N     1 
ATOM   6153 C  CA    . GLU B 1 250 ? 24.289  30.579  58.317  1.00 89.97  ? 277 GLU B CA    1 
ATOM   6154 C  C     . GLU B 1 250 ? 25.647  31.108  57.866  1.00 83.68  ? 277 GLU B C     1 
ATOM   6155 O  O     . GLU B 1 250 ? 25.765  32.202  57.308  1.00 99.48  ? 277 GLU B O     1 
ATOM   6156 C  CB    . GLU B 1 250 ? 23.225  31.678  58.328  1.00 92.47  ? 277 GLU B CB    1 
ATOM   6157 C  CG    . GLU B 1 250 ? 21.817  31.124  58.151  1.00 98.89  ? 277 GLU B CG    1 
ATOM   6158 C  CD    . GLU B 1 250 ? 20.740  32.074  58.623  1.00 125.13 ? 277 GLU B CD    1 
ATOM   6159 O  OE1   . GLU B 1 250 ? 21.018  33.286  58.731  1.00 131.66 ? 277 GLU B OE1   1 
ATOM   6160 O  OE2   . GLU B 1 250 ? 19.612  31.603  58.890  1.00 144.05 ? 277 GLU B OE2   1 
ATOM   6161 N  N     . VAL B 1 251 ? 26.682  30.310  58.108  1.00 84.72  ? 278 VAL B N     1 
ATOM   6162 C  CA    . VAL B 1 251 ? 28.034  30.595  57.649  1.00 84.47  ? 278 VAL B CA    1 
ATOM   6163 C  C     . VAL B 1 251 ? 28.270  29.808  56.369  1.00 80.45  ? 278 VAL B C     1 
ATOM   6164 O  O     . VAL B 1 251 ? 28.243  28.572  56.377  1.00 88.59  ? 278 VAL B O     1 
ATOM   6165 C  CB    . VAL B 1 251 ? 29.080  30.237  58.716  1.00 77.03  ? 278 VAL B CB    1 
ATOM   6166 C  CG1   . VAL B 1 251 ? 30.478  30.376  58.145  1.00 75.84  ? 278 VAL B CG1   1 
ATOM   6167 C  CG2   . VAL B 1 251 ? 28.911  31.117  59.946  1.00 84.33  ? 278 VAL B CG2   1 
ATOM   6168 N  N     . GLN B 1 252 ? 28.495  30.517  55.269  1.00 82.09  ? 279 GLN B N     1 
ATOM   6169 C  CA    . GLN B 1 252 ? 28.771  29.870  53.995  1.00 79.28  ? 279 GLN B CA    1 
ATOM   6170 C  C     . GLN B 1 252 ? 30.232  29.441  53.950  1.00 83.80  ? 279 GLN B C     1 
ATOM   6171 O  O     . GLN B 1 252 ? 31.134  30.277  54.078  1.00 91.65  ? 279 GLN B O     1 
ATOM   6172 C  CB    . GLN B 1 252 ? 28.448  30.810  52.837  1.00 89.06  ? 279 GLN B CB    1 
ATOM   6173 C  CG    . GLN B 1 252 ? 28.627  30.181  51.467  1.00 88.82  ? 279 GLN B CG    1 
ATOM   6174 C  CD    . GLN B 1 252 ? 27.787  28.927  51.286  1.00 102.51 ? 279 GLN B CD    1 
ATOM   6175 O  OE1   . GLN B 1 252 ? 26.558  28.993  51.209  1.00 105.72 ? 279 GLN B OE1   1 
ATOM   6176 N  NE2   . GLN B 1 252 ? 28.449  27.774  51.221  1.00 91.34  ? 279 GLN B NE2   1 
ATOM   6177 N  N     . MET B 1 253 ? 30.464  28.142  53.784  1.00 85.32  ? 280 MET B N     1 
ATOM   6178 C  CA    . MET B 1 253 ? 31.808  27.631  53.560  1.00 75.27  ? 280 MET B CA    1 
ATOM   6179 C  C     . MET B 1 253 ? 32.231  27.885  52.121  1.00 73.23  ? 280 MET B C     1 
ATOM   6180 O  O     . MET B 1 253 ? 31.444  27.707  51.186  1.00 77.00  ? 280 MET B O     1 
ATOM   6181 C  CB    . MET B 1 253 ? 31.870  26.133  53.856  1.00 73.03  ? 280 MET B CB    1 
ATOM   6182 C  CG    . MET B 1 253 ? 31.886  25.783  55.325  1.00 88.73  ? 280 MET B CG    1 
ATOM   6183 S  SD    . MET B 1 253 ? 31.320  24.097  55.606  1.00 113.54 ? 280 MET B SD    1 
ATOM   6184 C  CE    . MET B 1 253 ? 29.597  24.274  55.143  1.00 109.13 ? 280 MET B CE    1 
ATOM   6185 N  N     . TYR B 1 254 ? 33.482  28.300  51.945  1.00 64.21  ? 281 TYR B N     1 
ATOM   6186 C  CA    . TYR B 1 254 ? 34.043  28.551  50.627  1.00 85.60  ? 281 TYR B CA    1 
ATOM   6187 C  C     . TYR B 1 254 ? 35.303  27.718  50.417  1.00 85.24  ? 281 TYR B C     1 
ATOM   6188 O  O     . TYR B 1 254 ? 36.053  27.444  51.359  1.00 85.18  ? 281 TYR B O     1 
ATOM   6189 C  CB    . TYR B 1 254 ? 34.377  30.037  50.429  1.00 69.61  ? 281 TYR B CB    1 
ATOM   6190 C  CG    . TYR B 1 254 ? 33.177  30.960  50.387  1.00 85.72  ? 281 TYR B CG    1 
ATOM   6191 C  CD1   . TYR B 1 254 ? 32.593  31.429  51.560  1.00 84.01  ? 281 TYR B CD1   1 
ATOM   6192 C  CD2   . TYR B 1 254 ? 32.643  31.385  49.173  1.00 89.40  ? 281 TYR B CD2   1 
ATOM   6193 C  CE1   . TYR B 1 254 ? 31.505  32.280  51.527  1.00 82.01  ? 281 TYR B CE1   1 
ATOM   6194 C  CE2   . TYR B 1 254 ? 31.553  32.239  49.130  1.00 83.68  ? 281 TYR B CE2   1 
ATOM   6195 C  CZ    . TYR B 1 254 ? 30.989  32.683  50.311  1.00 95.40  ? 281 TYR B CZ    1 
ATOM   6196 O  OH    . TYR B 1 254 ? 29.905  33.531  50.277  1.00 109.55 ? 281 TYR B OH    1 
ATOM   6197 N  N     . VAL B 1 255 ? 35.522  27.311  49.168  1.00 73.85  ? 282 VAL B N     1 
ATOM   6198 C  CA    . VAL B 1 255 ? 36.785  26.732  48.724  1.00 74.95  ? 282 VAL B CA    1 
ATOM   6199 C  C     . VAL B 1 255 ? 37.348  27.629  47.629  1.00 80.45  ? 282 VAL B C     1 
ATOM   6200 O  O     . VAL B 1 255 ? 36.612  28.059  46.733  1.00 77.84  ? 282 VAL B O     1 
ATOM   6201 C  CB    . VAL B 1 255 ? 36.616  25.281  48.227  1.00 86.13  ? 282 VAL B CB    1 
ATOM   6202 C  CG1   . VAL B 1 255 ? 35.532  25.187  47.160  1.00 85.87  ? 282 VAL B CG1   1 
ATOM   6203 C  CG2   . VAL B 1 255 ? 37.940  24.728  47.691  1.00 66.38  ? 282 VAL B CG2   1 
ATOM   6204 N  N     . CYS B 1 256 ? 38.644  27.926  47.711  1.00 77.47  ? 283 CYS B N     1 
ATOM   6205 C  CA    . CYS B 1 256 ? 39.328  28.744  46.720  1.00 75.05  ? 283 CYS B CA    1 
ATOM   6206 C  C     . CYS B 1 256 ? 40.374  27.911  45.998  1.00 80.43  ? 283 CYS B C     1 
ATOM   6207 O  O     . CYS B 1 256 ? 41.091  27.120  46.621  1.00 83.27  ? 283 CYS B O     1 
ATOM   6208 C  CB    . CYS B 1 256 ? 40.001  29.959  47.359  1.00 67.00  ? 283 CYS B CB    1 
ATOM   6209 S  SG    . CYS B 1 256 ? 38.909  30.999  48.338  1.00 103.53 ? 283 CYS B SG    1 
ATOM   6210 N  N     . ASN B 1 257 ? 40.459  28.097  44.679  1.00 71.53  ? 284 ASN B N     1 
ATOM   6211 C  CA    . ASN B 1 257 ? 41.453  27.427  43.851  1.00 77.73  ? 284 ASN B CA    1 
ATOM   6212 C  C     . ASN B 1 257 ? 42.144  28.419  42.923  1.00 86.61  ? 284 ASN B C     1 
ATOM   6213 O  O     . ASN B 1 257 ? 42.599  28.047  41.836  1.00 84.13  ? 284 ASN B O     1 
ATOM   6214 C  CB    . ASN B 1 257 ? 40.820  26.291  43.048  1.00 79.56  ? 284 ASN B CB    1 
ATOM   6215 C  CG    . ASN B 1 257 ? 39.881  26.794  41.960  1.00 89.75  ? 284 ASN B CG    1 
ATOM   6216 O  OD1   . ASN B 1 257 ? 39.358  27.907  42.034  1.00 81.08  ? 284 ASN B OD1   1 
ATOM   6217 N  ND2   . ASN B 1 257 ? 39.668  25.970  40.939  1.00 97.55  ? 284 ASN B ND2   1 
ATOM   6218 N  N     . LYS B 1 258 ? 42.231  29.687  43.342  1.00 73.10  ? 285 LYS B N     1 
ATOM   6219 C  CA    . LYS B 1 258 ? 42.793  30.719  42.476  1.00 76.03  ? 285 LYS B CA    1 
ATOM   6220 C  C     . LYS B 1 258 ? 44.240  30.423  42.111  1.00 91.51  ? 285 LYS B C     1 
ATOM   6221 O  O     . LYS B 1 258 ? 44.709  30.839  41.044  1.00 93.36  ? 285 LYS B O     1 
ATOM   6222 C  CB    . LYS B 1 258 ? 42.676  32.087  43.144  1.00 71.72  ? 285 LYS B CB    1 
ATOM   6223 C  CG    . LYS B 1 258 ? 41.244  32.542  43.368  1.00 78.49  ? 285 LYS B CG    1 
ATOM   6224 C  CD    . LYS B 1 258 ? 41.185  33.952  43.948  1.00 67.36  ? 285 LYS B CD    1 
ATOM   6225 C  CE    . LYS B 1 258 ? 39.752  34.375  44.238  1.00 71.14  ? 285 LYS B CE    1 
ATOM   6226 N  NZ    . LYS B 1 258 ? 39.688  35.752  44.789  1.00 82.74  ? 285 LYS B NZ    1 
ATOM   6227 N  N     . GLU B 1 259 ? 44.959  29.709  42.971  1.00 78.76  ? 286 GLU B N     1 
ATOM   6228 C  CA    . GLU B 1 259 ? 46.287  29.223  42.627  1.00 89.43  ? 286 GLU B CA    1 
ATOM   6229 C  C     . GLU B 1 259 ? 46.588  28.003  43.483  1.00 82.64  ? 286 GLU B C     1 
ATOM   6230 O  O     . GLU B 1 259 ? 45.810  27.629  44.363  1.00 82.44  ? 286 GLU B O     1 
ATOM   6231 C  CB    . GLU B 1 259 ? 47.352  30.309  42.806  1.00 89.50  ? 286 GLU B CB    1 
ATOM   6232 C  CG    . GLU B 1 259 ? 47.400  30.925  44.184  1.00 85.62  ? 286 GLU B CG    1 
ATOM   6233 C  CD    . GLU B 1 259 ? 48.415  32.047  44.269  1.00 107.20 ? 286 GLU B CD    1 
ATOM   6234 O  OE1   . GLU B 1 259 ? 49.540  31.867  43.757  1.00 114.10 ? 286 GLU B OE1   1 
ATOM   6235 O  OE2   . GLU B 1 259 ? 48.086  33.112  44.832  1.00 116.86 ? 286 GLU B OE2   1 
ATOM   6236 N  N     . GLU B 1 260 ? 47.730  27.382  43.204  1.00 81.96  ? 287 GLU B N     1 
ATOM   6237 C  CA    . GLU B 1 260 ? 48.126  26.183  43.928  1.00 75.71  ? 287 GLU B CA    1 
ATOM   6238 C  C     . GLU B 1 260 ? 48.478  26.533  45.365  1.00 81.98  ? 287 GLU B C     1 
ATOM   6239 O  O     . GLU B 1 260 ? 49.177  27.519  45.622  1.00 89.90  ? 287 GLU B O     1 
ATOM   6240 C  CB    . GLU B 1 260 ? 49.313  25.518  43.236  1.00 66.21  ? 287 GLU B CB    1 
ATOM   6241 C  CG    . GLU B 1 260 ? 49.531  24.074  43.621  1.00 91.59  ? 287 GLU B CG    1 
ATOM   6242 C  CD    . GLU B 1 260 ? 50.485  23.367  42.681  1.00 105.17 ? 287 GLU B CD    1 
ATOM   6243 O  OE1   . GLU B 1 260 ? 51.591  23.900  42.454  1.00 106.95 ? 287 GLU B OE1   1 
ATOM   6244 O  OE2   . GLU B 1 260 ? 50.123  22.291  42.155  1.00 102.79 ? 287 GLU B OE2   1 
ATOM   6245 N  N     . TYR B 1 261 ? 47.984  25.734  46.304  1.00 85.49  ? 288 TYR B N     1 
ATOM   6246 C  CA    . TYR B 1 261 ? 48.244  25.970  47.718  1.00 80.13  ? 288 TYR B CA    1 
ATOM   6247 C  C     . TYR B 1 261 ? 49.032  24.842  48.357  1.00 74.08  ? 288 TYR B C     1 
ATOM   6248 O  O     . TYR B 1 261 ? 50.002  25.101  49.078  1.00 80.04  ? 288 TYR B O     1 
ATOM   6249 C  CB    . TYR B 1 261 ? 46.924  26.169  48.468  1.00 72.68  ? 288 TYR B CB    1 
ATOM   6250 C  CG    . TYR B 1 261 ? 46.070  27.275  47.905  1.00 69.63  ? 288 TYR B CG    1 
ATOM   6251 C  CD1   . TYR B 1 261 ? 46.515  28.587  47.904  1.00 68.24  ? 288 TYR B CD1   1 
ATOM   6252 C  CD2   . TYR B 1 261 ? 44.810  27.008  47.390  1.00 73.79  ? 288 TYR B CD2   1 
ATOM   6253 C  CE1   . TYR B 1 261 ? 45.729  29.602  47.398  1.00 78.51  ? 288 TYR B CE1   1 
ATOM   6254 C  CE2   . TYR B 1 261 ? 44.018  28.013  46.885  1.00 71.29  ? 288 TYR B CE2   1 
ATOM   6255 C  CZ    . TYR B 1 261 ? 44.482  29.308  46.886  1.00 83.28  ? 288 TYR B CZ    1 
ATOM   6256 O  OH    . TYR B 1 261 ? 43.693  30.317  46.378  1.00 93.17  ? 288 TYR B OH    1 
ATOM   6257 N  N     . GLY B 1 262 ? 48.646  23.599  48.111  1.00 77.19  ? 289 GLY B N     1 
ATOM   6258 C  CA    . GLY B 1 262 ? 49.345  22.483  48.709  1.00 72.52  ? 289 GLY B CA    1 
ATOM   6259 C  C     . GLY B 1 262 ? 48.764  21.171  48.237  1.00 79.23  ? 289 GLY B C     1 
ATOM   6260 O  O     . GLY B 1 262 ? 47.917  21.127  47.340  1.00 86.70  ? 289 GLY B O     1 
ATOM   6261 N  N     . PHE B 1 263 ? 49.236  20.094  48.861  1.00 82.44  ? 290 PHE B N     1 
ATOM   6262 C  CA    . PHE B 1 263 ? 48.873  18.737  48.486  1.00 77.17  ? 290 PHE B CA    1 
ATOM   6263 C  C     . PHE B 1 263 ? 48.504  17.952  49.735  1.00 75.05  ? 290 PHE B C     1 
ATOM   6264 O  O     . PHE B 1 263 ? 48.829  18.343  50.859  1.00 72.46  ? 290 PHE B O     1 
ATOM   6265 C  CB    . PHE B 1 263 ? 50.017  18.029  47.741  1.00 79.56  ? 290 PHE B CB    1 
ATOM   6266 C  CG    . PHE B 1 263 ? 50.502  18.769  46.530  1.00 86.37  ? 290 PHE B CG    1 
ATOM   6267 C  CD1   . PHE B 1 263 ? 51.389  19.829  46.655  1.00 88.22  ? 290 PHE B CD1   1 
ATOM   6268 C  CD2   . PHE B 1 263 ? 50.073  18.405  45.264  1.00 89.53  ? 290 PHE B CD2   1 
ATOM   6269 C  CE1   . PHE B 1 263 ? 51.836  20.516  45.542  1.00 89.18  ? 290 PHE B CE1   1 
ATOM   6270 C  CE2   . PHE B 1 263 ? 50.517  19.086  44.145  1.00 97.69  ? 290 PHE B CE2   1 
ATOM   6271 C  CZ    . PHE B 1 263 ? 51.400  20.144  44.285  1.00 98.54  ? 290 PHE B CZ    1 
ATOM   6272 N  N     . LEU B 1 264 ? 47.823  16.827  49.521  1.00 75.30  ? 291 LEU B N     1 
ATOM   6273 C  CA    . LEU B 1 264 ? 47.383  15.975  50.617  1.00 79.31  ? 291 LEU B CA    1 
ATOM   6274 C  C     . LEU B 1 264 ? 47.183  14.565  50.084  1.00 81.83  ? 291 LEU B C     1 
ATOM   6275 O  O     . LEU B 1 264 ? 46.833  14.393  48.910  1.00 83.48  ? 291 LEU B O     1 
ATOM   6276 C  CB    . LEU B 1 264 ? 46.088  16.508  51.254  1.00 75.71  ? 291 LEU B CB    1 
ATOM   6277 C  CG    . LEU B 1 264 ? 44.718  16.345  50.584  1.00 74.49  ? 291 LEU B CG    1 
ATOM   6278 C  CD1   . LEU B 1 264 ? 43.670  17.057  51.420  1.00 65.89  ? 291 LEU B CD1   1 
ATOM   6279 C  CD2   . LEU B 1 264 ? 44.686  16.855  49.153  1.00 78.29  ? 291 LEU B CD2   1 
ATOM   6280 N  N     . PRO B 1 265 ? 47.420  13.544  50.900  1.00 83.10  ? 292 PRO B N     1 
ATOM   6281 C  CA    . PRO B 1 265 ? 47.196  12.172  50.445  1.00 71.88  ? 292 PRO B CA    1 
ATOM   6282 C  C     . PRO B 1 265 ? 45.722  11.800  50.478  1.00 68.66  ? 292 PRO B C     1 
ATOM   6283 O  O     . PRO B 1 265 ? 44.936  12.323  51.270  1.00 85.42  ? 292 PRO B O     1 
ATOM   6284 C  CB    . PRO B 1 265 ? 48.002  11.337  51.447  1.00 74.86  ? 292 PRO B CB    1 
ATOM   6285 C  CG    . PRO B 1 265 ? 47.986  12.150  52.692  1.00 80.82  ? 292 PRO B CG    1 
ATOM   6286 C  CD    . PRO B 1 265 ? 48.018  13.590  52.246  1.00 80.80  ? 292 PRO B CD    1 
ATOM   6287 N  N     . VAL B 1 266 ? 45.355  10.882  49.597  1.00 79.46  ? 293 VAL B N     1 
ATOM   6288 C  CA    . VAL B 1 266 ? 43.978  10.379  49.583  1.00 83.88  ? 293 VAL B CA    1 
ATOM   6289 C  C     . VAL B 1 266 ? 43.785  9.422   50.757  1.00 79.03  ? 293 VAL B C     1 
ATOM   6290 O  O     . VAL B 1 266 ? 44.615  8.517   50.961  1.00 83.38  ? 293 VAL B O     1 
ATOM   6291 C  CB    . VAL B 1 266 ? 43.676  9.696   48.250  1.00 80.06  ? 293 VAL B CB    1 
ATOM   6292 C  CG1   . VAL B 1 266 ? 42.224  9.252   48.198  1.00 69.12  ? 293 VAL B CG1   1 
ATOM   6293 C  CG2   . VAL B 1 266 ? 43.989  10.637  47.095  1.00 74.58  ? 293 VAL B CG2   1 
ATOM   6294 N  N     . PRO B 1 267 ? 42.737  9.594   51.563  1.00 85.79  ? 294 PRO B N     1 
ATOM   6295 C  CA    . PRO B 1 267 ? 42.536  8.710   52.717  1.00 83.06  ? 294 PRO B CA    1 
ATOM   6296 C  C     . PRO B 1 267 ? 42.430  7.241   52.326  1.00 90.25  ? 294 PRO B C     1 
ATOM   6297 O  O     . PRO B 1 267 ? 41.960  6.888   51.241  1.00 88.76  ? 294 PRO B O     1 
ATOM   6298 C  CB    . PRO B 1 267 ? 41.225  9.219   53.321  1.00 78.36  ? 294 PRO B CB    1 
ATOM   6299 C  CG    . PRO B 1 267 ? 41.207  10.667  52.960  1.00 75.06  ? 294 PRO B CG    1 
ATOM   6300 C  CD    . PRO B 1 267 ? 41.821  10.749  51.588  1.00 83.65  ? 294 PRO B CD    1 
ATOM   6301 N  N     . LEU B 1 268 ? 42.867  6.383   53.244  1.00 83.50  ? 295 LEU B N     1 
ATOM   6302 C  CA    . LEU B 1 268 ? 42.886  4.943   53.058  1.00 85.10  ? 295 LEU B CA    1 
ATOM   6303 C  C     . LEU B 1 268 ? 41.626  4.315   53.646  1.00 91.68  ? 295 LEU B C     1 
ATOM   6304 O  O     . LEU B 1 268 ? 40.787  4.985   54.252  1.00 87.12  ? 295 LEU B O     1 
ATOM   6305 C  CB    . LEU B 1 268 ? 44.136  4.346   53.702  1.00 81.30  ? 295 LEU B CB    1 
ATOM   6306 C  CG    . LEU B 1 268 ? 45.460  4.932   53.228  1.00 75.82  ? 295 LEU B CG    1 
ATOM   6307 C  CD1   . LEU B 1 268 ? 46.577  4.508   54.161  1.00 75.45  ? 295 LEU B CD1   1 
ATOM   6308 C  CD2   . LEU B 1 268 ? 45.747  4.484   51.809  1.00 67.35  ? 295 LEU B CD2   1 
ATOM   6309 N  N     . ARG B 1 269 ? 41.503  3.001   53.472  1.00 86.41  ? 296 ARG B N     1 
ATOM   6310 C  CA    . ARG B 1 269 ? 40.363  2.267   53.992  1.00 83.81  ? 296 ARG B CA    1 
ATOM   6311 C  C     . ARG B 1 269 ? 40.561  1.957   55.476  1.00 87.78  ? 296 ARG B C     1 
ATOM   6312 O  O     . ARG B 1 269 ? 41.654  2.103   56.030  1.00 103.15 ? 296 ARG B O     1 
ATOM   6313 C  CB    . ARG B 1 269 ? 40.152  0.984   53.192  1.00 112.95 ? 296 ARG B CB    1 
ATOM   6314 C  CG    . ARG B 1 269 ? 40.067  1.210   51.693  1.00 111.78 ? 296 ARG B CG    1 
ATOM   6315 C  CD    . ARG B 1 269 ? 39.945  -0.099  50.931  1.00 123.29 ? 296 ARG B CD    1 
ATOM   6316 N  NE    . ARG B 1 269 ? 40.051  0.114   49.492  1.00 138.90 ? 296 ARG B NE    1 
ATOM   6317 C  CZ    . ARG B 1 269 ? 39.904  -0.835  48.578  1.00 152.94 ? 296 ARG B CZ    1 
ATOM   6318 N  NH1   . ARG B 1 269 ? 39.629  -2.085  48.917  1.00 160.10 ? 296 ARG B NH1   1 
ATOM   6319 N  NH2   . ARG B 1 269 ? 40.035  -0.522  47.292  1.00 146.90 ? 296 ARG B NH2   1 
ATOM   6320 N  N     . ALA B 1 270 ? 39.474  1.523   56.122  1.00 74.36  ? 297 ALA B N     1 
ATOM   6321 C  CA    . ALA B 1 270 ? 39.513  1.272   57.561  1.00 87.52  ? 297 ALA B CA    1 
ATOM   6322 C  C     . ALA B 1 270 ? 40.527  0.190   57.912  1.00 103.58 ? 297 ALA B C     1 
ATOM   6323 O  O     . ALA B 1 270 ? 41.307  0.341   58.861  1.00 102.27 ? 297 ALA B O     1 
ATOM   6324 C  CB    . ALA B 1 270 ? 38.122  0.886   58.061  1.00 73.96  ? 297 ALA B CB    1 
ATOM   6325 N  N     . HIS B 1 271 ? 40.538  -0.905  57.154  1.00 105.78 ? 298 HIS B N     1 
ATOM   6326 C  CA    . HIS B 1 271 ? 41.452  -2.011  57.403  1.00 97.65  ? 298 HIS B CA    1 
ATOM   6327 C  C     . HIS B 1 271 ? 42.775  -1.853  56.662  1.00 101.83 ? 298 HIS B C     1 
ATOM   6328 O  O     . HIS B 1 271 ? 43.359  -2.848  56.215  1.00 105.35 ? 298 HIS B O     1 
ATOM   6329 C  CB    . HIS B 1 271 ? 40.777  -3.332  57.044  1.00 110.22 ? 298 HIS B CB    1 
ATOM   6330 C  CG    . HIS B 1 271 ? 39.647  -3.697  57.956  1.00 126.14 ? 298 HIS B CG    1 
ATOM   6331 N  ND1   . HIS B 1 271 ? 38.597  -4.498  57.561  1.00 148.59 ? 298 HIS B ND1   1 
ATOM   6332 C  CD2   . HIS B 1 271 ? 39.404  -3.368  59.247  1.00 106.66 ? 298 HIS B CD2   1 
ATOM   6333 C  CE1   . HIS B 1 271 ? 37.758  -4.649  58.569  1.00 151.98 ? 298 HIS B CE1   1 
ATOM   6334 N  NE2   . HIS B 1 271 ? 38.224  -3.974  59.604  1.00 129.61 ? 298 HIS B NE2   1 
ATOM   6335 N  N     . SER B 1 272 ? 43.267  -0.624  56.529  1.00 90.89  ? 299 SER B N     1 
ATOM   6336 C  CA    . SER B 1 272 ? 44.585  -0.349  55.982  1.00 97.77  ? 299 SER B CA    1 
ATOM   6337 C  C     . SER B 1 272 ? 45.612  -0.320  57.110  1.00 106.01 ? 299 SER B C     1 
ATOM   6338 O  O     . SER B 1 272 ? 45.284  -0.475  58.291  1.00 116.15 ? 299 SER B O     1 
ATOM   6339 C  CB    . SER B 1 272 ? 44.588  0.968   55.207  1.00 94.15  ? 299 SER B CB    1 
ATOM   6340 O  OG    . SER B 1 272 ? 43.683  0.919   54.118  1.00 100.26 ? 299 SER B OG    1 
ATOM   6341 N  N     . THR B 1 273 ? 46.873  -0.106  56.749  1.00 83.39  ? 300 THR B N     1 
ATOM   6342 C  CA    . THR B 1 273 ? 47.970  -0.161  57.702  1.00 92.45  ? 300 THR B CA    1 
ATOM   6343 C  C     . THR B 1 273 ? 48.744  1.147   57.688  1.00 89.95  ? 300 THR B C     1 
ATOM   6344 O  O     . THR B 1 273 ? 48.571  1.992   56.807  1.00 93.65  ? 300 THR B O     1 
ATOM   6345 C  CB    . THR B 1 273 ? 48.918  -1.325  57.395  1.00 106.69 ? 300 THR B CB    1 
ATOM   6346 O  OG1   . THR B 1 273 ? 49.873  -1.450  58.456  1.00 123.92 ? 300 THR B OG1   1 
ATOM   6347 C  CG2   . THR B 1 273 ? 49.654  -1.072  56.094  1.00 86.99  ? 300 THR B CG2   1 
ATOM   6348 N  N     . LEU B 1 274 ? 49.614  1.305   58.689  1.00 90.67  ? 301 LEU B N     1 
ATOM   6349 C  CA    . LEU B 1 274 ? 50.434  2.508   58.759  1.00 80.67  ? 301 LEU B CA    1 
ATOM   6350 C  C     . LEU B 1 274 ? 51.415  2.584   57.598  1.00 83.06  ? 301 LEU B C     1 
ATOM   6351 O  O     . LEU B 1 274 ? 51.736  3.683   57.133  1.00 82.90  ? 301 LEU B O     1 
ATOM   6352 C  CB    . LEU B 1 274 ? 51.186  2.567   60.087  1.00 71.06  ? 301 LEU B CB    1 
ATOM   6353 C  CG    . LEU B 1 274 ? 50.347  2.756   61.350  1.00 74.41  ? 301 LEU B CG    1 
ATOM   6354 C  CD1   . LEU B 1 274 ? 51.255  2.975   62.549  1.00 74.26  ? 301 LEU B CD1   1 
ATOM   6355 C  CD2   . LEU B 1 274 ? 49.388  3.916   61.184  1.00 82.38  ? 301 LEU B CD2   1 
ATOM   6356 N  N     . GLN B 1 275 ? 51.901  1.435   57.119  1.00 94.80  ? 302 GLN B N     1 
ATOM   6357 C  CA    . GLN B 1 275 ? 52.813  1.445   55.981  1.00 82.08  ? 302 GLN B CA    1 
ATOM   6358 C  C     . GLN B 1 275 ? 52.127  1.988   54.738  1.00 91.83  ? 302 GLN B C     1 
ATOM   6359 O  O     . GLN B 1 275 ? 52.726  2.753   53.972  1.00 91.95  ? 302 GLN B O     1 
ATOM   6360 C  CB    . GLN B 1 275 ? 53.353  0.043   55.720  1.00 95.52  ? 302 GLN B CB    1 
ATOM   6361 C  CG    . GLN B 1 275 ? 54.382  0.001   54.610  1.00 91.66  ? 302 GLN B CG    1 
ATOM   6362 C  CD    . GLN B 1 275 ? 54.638  -1.402  54.109  1.00 102.65 ? 302 GLN B CD    1 
ATOM   6363 O  OE1   . GLN B 1 275 ? 54.009  -2.361  54.559  1.00 104.08 ? 302 GLN B OE1   1 
ATOM   6364 N  NE2   . GLN B 1 275 ? 55.565  -1.530  53.167  1.00 101.02 ? 302 GLN B NE2   1 
ATOM   6365 N  N     . ASP B 1 276 ? 50.868  1.597   54.518  1.00 84.35  ? 303 ASP B N     1 
ATOM   6366 C  CA    . ASP B 1 276 ? 50.078  2.212   53.457  1.00 86.31  ? 303 ASP B CA    1 
ATOM   6367 C  C     . ASP B 1 276 ? 50.085  3.731   53.576  1.00 82.42  ? 303 ASP B C     1 
ATOM   6368 O  O     . ASP B 1 276 ? 50.267  4.439   52.580  1.00 84.95  ? 303 ASP B O     1 
ATOM   6369 C  CB    . ASP B 1 276 ? 48.642  1.690   53.492  1.00 88.36  ? 303 ASP B CB    1 
ATOM   6370 C  CG    . ASP B 1 276 ? 48.549  0.218   53.188  1.00 88.02  ? 303 ASP B CG    1 
ATOM   6371 O  OD1   . ASP B 1 276 ? 49.421  -0.298  52.458  1.00 106.20 ? 303 ASP B OD1   1 
ATOM   6372 O  OD2   . ASP B 1 276 ? 47.600  -0.425  53.682  1.00 101.98 ? 303 ASP B OD2   1 
ATOM   6373 N  N     . GLU B 1 277 ? 49.903  4.252   54.793  1.00 85.33  ? 304 GLU B N     1 
ATOM   6374 C  CA    . GLU B 1 277 ? 49.840  5.699   54.973  1.00 81.63  ? 304 GLU B CA    1 
ATOM   6375 C  C     . GLU B 1 277 ? 51.195  6.354   54.740  1.00 80.76  ? 304 GLU B C     1 
ATOM   6376 O  O     . GLU B 1 277 ? 51.276  7.411   54.104  1.00 84.59  ? 304 GLU B O     1 
ATOM   6377 C  CB    . GLU B 1 277 ? 49.322  6.039   56.367  1.00 81.98  ? 304 GLU B CB    1 
ATOM   6378 C  CG    . GLU B 1 277 ? 49.118  7.526   56.590  1.00 85.53  ? 304 GLU B CG    1 
ATOM   6379 C  CD    . GLU B 1 277 ? 47.870  8.055   55.909  1.00 85.71  ? 304 GLU B CD    1 
ATOM   6380 O  OE1   . GLU B 1 277 ? 46.798  7.434   56.077  1.00 73.71  ? 304 GLU B OE1   1 
ATOM   6381 O  OE2   . GLU B 1 277 ? 47.961  9.091   55.212  1.00 96.00  ? 304 GLU B OE2   1 
ATOM   6382 N  N     . ALA B 1 278 ? 52.271  5.753   55.254  1.00 83.62  ? 305 ALA B N     1 
ATOM   6383 C  CA    . ALA B 1 278 ? 53.594  6.334   55.045  1.00 84.62  ? 305 ALA B CA    1 
ATOM   6384 C  C     . ALA B 1 278 ? 53.959  6.340   53.566  1.00 84.30  ? 305 ALA B C     1 
ATOM   6385 O  O     . ALA B 1 278 ? 54.531  7.314   53.062  1.00 91.38  ? 305 ALA B O     1 
ATOM   6386 C  CB    . ALA B 1 278 ? 54.644  5.578   55.859  1.00 67.79  ? 305 ALA B CB    1 
ATOM   6387 N  N     . GLU B 1 279 ? 53.621  5.267   52.848  1.00 81.18  ? 306 GLU B N     1 
ATOM   6388 C  CA    . GLU B 1 279 ? 53.890  5.246   51.415  1.00 90.06  ? 306 GLU B CA    1 
ATOM   6389 C  C     . GLU B 1 279 ? 52.930  6.153   50.653  1.00 82.75  ? 306 GLU B C     1 
ATOM   6390 O  O     . GLU B 1 279 ? 53.305  6.716   49.618  1.00 91.30  ? 306 GLU B O     1 
ATOM   6391 C  CB    . GLU B 1 279 ? 53.825  3.809   50.892  1.00 77.49  ? 306 GLU B CB    1 
ATOM   6392 C  CG    . GLU B 1 279 ? 54.892  2.907   51.499  1.00 86.36  ? 306 GLU B CG    1 
ATOM   6393 C  CD    . GLU B 1 279 ? 54.905  1.506   50.917  1.00 90.94  ? 306 GLU B CD    1 
ATOM   6394 O  OE1   . GLU B 1 279 ? 54.116  1.228   49.990  1.00 89.08  ? 306 GLU B OE1   1 
ATOM   6395 O  OE2   . GLU B 1 279 ? 55.714  0.683   51.394  1.00 89.48  ? 306 GLU B OE2   1 
ATOM   6396 N  N     . SER B 1 280 ? 51.699  6.317   51.149  1.00 80.61  ? 307 SER B N     1 
ATOM   6397 C  CA    . SER B 1 280 ? 50.748  7.213   50.497  1.00 75.25  ? 307 SER B CA    1 
ATOM   6398 C  C     . SER B 1 280 ? 51.228  8.660   50.549  1.00 88.14  ? 307 SER B C     1 
ATOM   6399 O  O     . SER B 1 280 ? 51.114  9.392   49.559  1.00 86.68  ? 307 SER B O     1 
ATOM   6400 C  CB    . SER B 1 280 ? 49.368  7.079   51.143  1.00 78.01  ? 307 SER B CB    1 
ATOM   6401 O  OG    . SER B 1 280 ? 48.394  7.837   50.445  1.00 82.79  ? 307 SER B OG    1 
ATOM   6402 N  N     . PHE B 1 281 ? 51.765  9.093   51.692  1.00 79.38  ? 308 PHE B N     1 
ATOM   6403 C  CA    . PHE B 1 281 ? 52.301  10.447  51.769  1.00 77.74  ? 308 PHE B CA    1 
ATOM   6404 C  C     . PHE B 1 281 ? 53.585  10.583  50.961  1.00 86.20  ? 308 PHE B C     1 
ATOM   6405 O  O     . PHE B 1 281 ? 53.906  11.680  50.485  1.00 85.90  ? 308 PHE B O     1 
ATOM   6406 C  CB    . PHE B 1 281 ? 52.546  10.845  53.225  1.00 75.39  ? 308 PHE B CB    1 
ATOM   6407 C  CG    . PHE B 1 281 ? 53.038  12.257  53.390  1.00 72.54  ? 308 PHE B CG    1 
ATOM   6408 C  CD1   . PHE B 1 281 ? 52.149  13.318  53.388  1.00 71.32  ? 308 PHE B CD1   1 
ATOM   6409 C  CD2   . PHE B 1 281 ? 54.391  12.523  53.536  1.00 79.37  ? 308 PHE B CD2   1 
ATOM   6410 C  CE1   . PHE B 1 281 ? 52.598  14.617  53.529  1.00 60.97  ? 308 PHE B CE1   1 
ATOM   6411 C  CE2   . PHE B 1 281 ? 54.844  13.819  53.678  1.00 76.61  ? 308 PHE B CE2   1 
ATOM   6412 C  CZ    . PHE B 1 281 ? 53.944  14.867  53.672  1.00 69.37  ? 308 PHE B CZ    1 
ATOM   6413 N  N     . MET B 1 282 ? 54.332  9.490   50.801  1.00 85.03  ? 309 MET B N     1 
ATOM   6414 C  CA    . MET B 1 282 ? 55.532  9.542   49.975  1.00 75.54  ? 309 MET B CA    1 
ATOM   6415 C  C     . MET B 1 282 ? 55.181  9.789   48.512  1.00 78.98  ? 309 MET B C     1 
ATOM   6416 O  O     . MET B 1 282 ? 55.935  10.455  47.794  1.00 83.15  ? 309 MET B O     1 
ATOM   6417 C  CB    . MET B 1 282 ? 56.329  8.250   50.132  1.00 77.70  ? 309 MET B CB    1 
ATOM   6418 C  CG    . MET B 1 282 ? 57.617  8.196   49.315  1.00 90.85  ? 309 MET B CG    1 
ATOM   6419 S  SD    . MET B 1 282 ? 57.408  7.474   47.670  1.00 101.89 ? 309 MET B SD    1 
ATOM   6420 C  CE    . MET B 1 282 ? 56.675  5.887   48.080  1.00 85.56  ? 309 MET B CE    1 
ATOM   6421 N  N     . HIS B 1 283 ? 54.042  9.268   48.050  1.00 81.75  ? 310 HIS B N     1 
ATOM   6422 C  CA    . HIS B 1 283 ? 53.620  9.568   46.687  1.00 84.84  ? 310 HIS B CA    1 
ATOM   6423 C  C     . HIS B 1 283 ? 53.264  11.042  46.534  1.00 90.16  ? 310 HIS B C     1 
ATOM   6424 O  O     . HIS B 1 283 ? 53.482  11.623  45.465  1.00 86.28  ? 310 HIS B O     1 
ATOM   6425 C  CB    . HIS B 1 283 ? 52.442  8.682   46.286  1.00 73.87  ? 310 HIS B CB    1 
ATOM   6426 C  CG    . HIS B 1 283 ? 52.126  8.727   44.824  1.00 82.39  ? 310 HIS B CG    1 
ATOM   6427 N  ND1   . HIS B 1 283 ? 51.003  9.348   44.321  1.00 82.15  ? 310 HIS B ND1   1 
ATOM   6428 C  CD2   . HIS B 1 283 ? 52.796  8.238   43.753  1.00 84.46  ? 310 HIS B CD2   1 
ATOM   6429 C  CE1   . HIS B 1 283 ? 50.991  9.234   43.004  1.00 102.51 ? 310 HIS B CE1   1 
ATOM   6430 N  NE2   . HIS B 1 283 ? 52.069  8.564   42.633  1.00 87.18  ? 310 HIS B NE2   1 
ATOM   6431 N  N     . VAL B 1 284 ? 52.723  11.658  47.589  1.00 86.54  ? 311 VAL B N     1 
ATOM   6432 C  CA    . VAL B 1 284 ? 52.478  13.098  47.568  1.00 79.50  ? 311 VAL B CA    1 
ATOM   6433 C  C     . VAL B 1 284 ? 53.776  13.853  47.314  1.00 81.70  ? 311 VAL B C     1 
ATOM   6434 O  O     . VAL B 1 284 ? 53.823  14.774  46.490  1.00 85.32  ? 311 VAL B O     1 
ATOM   6435 C  CB    . VAL B 1 284 ? 51.808  13.550  48.880  1.00 76.74  ? 311 VAL B CB    1 
ATOM   6436 C  CG1   . VAL B 1 284 ? 51.740  15.064  48.945  1.00 67.92  ? 311 VAL B CG1   1 
ATOM   6437 C  CG2   . VAL B 1 284 ? 50.417  12.958  48.993  1.00 86.36  ? 311 VAL B CG2   1 
ATOM   6438 N  N     . GLN B 1 285 ? 54.851  13.472  48.013  1.00 79.66  ? 312 GLN B N     1 
ATOM   6439 C  CA    . GLN B 1 285 ? 56.157  14.070  47.745  1.00 81.33  ? 312 GLN B CA    1 
ATOM   6440 C  C     . GLN B 1 285 ? 56.571  13.868  46.291  1.00 86.94  ? 312 GLN B C     1 
ATOM   6441 O  O     . GLN B 1 285 ? 57.152  14.769  45.672  1.00 78.83  ? 312 GLN B O     1 
ATOM   6442 C  CB    . GLN B 1 285 ? 57.206  13.488  48.694  1.00 69.49  ? 312 GLN B CB    1 
ATOM   6443 C  CG    . GLN B 1 285 ? 57.209  14.127  50.076  1.00 80.83  ? 312 GLN B CG    1 
ATOM   6444 C  CD    . GLN B 1 285 ? 57.682  13.182  51.163  1.00 87.88  ? 312 GLN B CD    1 
ATOM   6445 O  OE1   . GLN B 1 285 ? 57.169  12.071  51.299  1.00 96.82  ? 312 GLN B OE1   1 
ATOM   6446 N  NE2   . GLN B 1 285 ? 58.662  13.620  51.950  1.00 66.69  ? 312 GLN B NE2   1 
ATOM   6447 N  N     . LEU B 1 286 ? 56.266  12.694  45.727  1.00 84.35  ? 313 LEU B N     1 
ATOM   6448 C  CA    . LEU B 1 286 ? 56.559  12.438  44.320  1.00 76.97  ? 313 LEU B CA    1 
ATOM   6449 C  C     . LEU B 1 286 ? 55.772  13.376  43.414  1.00 82.00  ? 313 LEU B C     1 
ATOM   6450 O  O     . LEU B 1 286 ? 56.330  13.984  42.492  1.00 85.17  ? 313 LEU B O     1 
ATOM   6451 C  CB    . LEU B 1 286 ? 56.247  10.982  43.975  1.00 81.08  ? 313 LEU B CB    1 
ATOM   6452 C  CG    . LEU B 1 286 ? 57.128  9.890   44.577  1.00 78.33  ? 313 LEU B CG    1 
ATOM   6453 C  CD1   . LEU B 1 286 ? 56.623  8.521   44.160  1.00 81.17  ? 313 LEU B CD1   1 
ATOM   6454 C  CD2   . LEU B 1 286 ? 58.568  10.077  44.147  1.00 78.92  ? 313 LEU B CD2   1 
ATOM   6455 N  N     . GLU B 1 287 ? 54.465  13.499  43.658  1.00 83.77  ? 314 GLU B N     1 
ATOM   6456 C  CA    . GLU B 1 287 ? 53.633  14.369  42.833  1.00 84.27  ? 314 GLU B CA    1 
ATOM   6457 C  C     . GLU B 1 287 ? 54.129  15.811  42.864  1.00 95.92  ? 314 GLU B C     1 
ATOM   6458 O  O     . GLU B 1 287 ? 54.079  16.512  41.847  1.00 99.36  ? 314 GLU B O     1 
ATOM   6459 C  CB    . GLU B 1 287 ? 52.178  14.287  43.295  1.00 73.47  ? 314 GLU B CB    1 
ATOM   6460 C  CG    . GLU B 1 287 ? 51.537  12.925  43.072  1.00 72.48  ? 314 GLU B CG    1 
ATOM   6461 C  CD    . GLU B 1 287 ? 51.431  12.568  41.597  1.00 99.86  ? 314 GLU B CD    1 
ATOM   6462 O  OE1   . GLU B 1 287 ? 50.538  13.117  40.914  1.00 99.79  ? 314 GLU B OE1   1 
ATOM   6463 O  OE2   . GLU B 1 287 ? 52.243  11.742  41.118  1.00 104.75 ? 314 GLU B OE2   1 
ATOM   6464 N  N     . VAL B 1 288 ? 54.625  16.265  44.018  1.00 84.82  ? 315 VAL B N     1 
ATOM   6465 C  CA    . VAL B 1 288 ? 55.186  17.610  44.106  1.00 81.12  ? 315 VAL B CA    1 
ATOM   6466 C  C     . VAL B 1 288 ? 56.409  17.734  43.209  1.00 88.47  ? 315 VAL B C     1 
ATOM   6467 O  O     . VAL B 1 288 ? 56.604  18.754  42.537  1.00 92.57  ? 315 VAL B O     1 
ATOM   6468 C  CB    . VAL B 1 288 ? 55.519  17.959  45.569  1.00 82.14  ? 315 VAL B CB    1 
ATOM   6469 C  CG1   . VAL B 1 288 ? 56.186  19.324  45.652  1.00 84.62  ? 315 VAL B CG1   1 
ATOM   6470 C  CG2   . VAL B 1 288 ? 54.265  17.935  46.418  1.00 78.35  ? 315 VAL B CG2   1 
ATOM   6471 N  N     . MET B 1 289 ? 57.246  16.693  43.171  1.00 77.39  ? 316 MET B N     1 
ATOM   6472 C  CA    . MET B 1 289 ? 58.493  16.748  42.419  1.00 88.47  ? 316 MET B CA    1 
ATOM   6473 C  C     . MET B 1 289 ? 58.293  16.637  40.914  1.00 91.34  ? 316 MET B C     1 
ATOM   6474 O  O     . MET B 1 289 ? 59.271  16.763  40.169  1.00 84.98  ? 316 MET B O     1 
ATOM   6475 C  CB    . MET B 1 289 ? 59.443  15.651  42.896  1.00 80.81  ? 316 MET B CB    1 
ATOM   6476 C  CG    . MET B 1 289 ? 60.076  15.947  44.240  1.00 83.23  ? 316 MET B CG    1 
ATOM   6477 S  SD    . MET B 1 289 ? 61.177  14.635  44.790  1.00 105.06 ? 316 MET B SD    1 
ATOM   6478 C  CE    . MET B 1 289 ? 60.002  13.323  45.092  1.00 74.87  ? 316 MET B CE    1 
ATOM   6479 N  N     . VAL B 1 290 ? 57.061  16.407  40.454  1.00 85.53  ? 317 VAL B N     1 
ATOM   6480 C  CA    . VAL B 1 290 ? 56.792  16.398  39.019  1.00 95.23  ? 317 VAL B CA    1 
ATOM   6481 C  C     . VAL B 1 290 ? 56.990  17.791  38.430  1.00 94.83  ? 317 VAL B C     1 
ATOM   6482 O  O     . VAL B 1 290 ? 57.652  17.961  37.399  1.00 97.52  ? 317 VAL B O     1 
ATOM   6483 C  CB    . VAL B 1 290 ? 55.373  15.864  38.744  1.00 91.15  ? 317 VAL B CB    1 
ATOM   6484 C  CG1   . VAL B 1 290 ? 55.011  16.037  37.282  1.00 93.13  ? 317 VAL B CG1   1 
ATOM   6485 C  CG2   . VAL B 1 290 ? 55.274  14.408  39.142  1.00 99.64  ? 317 VAL B CG2   1 
ATOM   6486 N  N     . LYS B 1 291 ? 56.432  18.810  39.083  1.00 98.13  ? 318 LYS B N     1 
ATOM   6487 C  CA    . LYS B 1 291 ? 56.471  20.172  38.573  1.00 93.13  ? 318 LYS B CA    1 
ATOM   6488 C  C     . LYS B 1 291 ? 57.110  21.170  39.529  1.00 94.55  ? 318 LYS B C     1 
ATOM   6489 O  O     . LYS B 1 291 ? 57.137  22.366  39.217  1.00 105.95 ? 318 LYS B O     1 
ATOM   6490 C  CB    . LYS B 1 291 ? 55.055  20.650  38.225  1.00 114.18 ? 318 LYS B CB    1 
ATOM   6491 C  CG    . LYS B 1 291 ? 54.525  20.159  36.886  1.00 120.31 ? 318 LYS B CG    1 
ATOM   6492 C  CD    . LYS B 1 291 ? 53.151  20.757  36.610  1.00 143.53 ? 318 LYS B CD    1 
ATOM   6493 C  CE    . LYS B 1 291 ? 52.884  20.897  35.119  1.00 144.69 ? 318 LYS B CE    1 
ATOM   6494 N  NZ    . LYS B 1 291 ? 51.687  21.748  34.856  1.00 131.64 ? 318 LYS B NZ    1 
ATOM   6495 N  N     . HIS B 1 292 ? 57.613  20.729  40.674  1.00 97.47  ? 319 HIS B N     1 
ATOM   6496 C  CA    . HIS B 1 292 ? 58.227  21.602  41.660  1.00 86.37  ? 319 HIS B CA    1 
ATOM   6497 C  C     . HIS B 1 292 ? 59.545  21.003  42.118  1.00 82.71  ? 319 HIS B C     1 
ATOM   6498 O  O     . HIS B 1 292 ? 59.815  19.821  41.880  1.00 91.54  ? 319 HIS B O     1 
ATOM   6499 C  CB    . HIS B 1 292 ? 57.323  21.806  42.885  1.00 80.55  ? 319 HIS B CB    1 
ATOM   6500 C  CG    . HIS B 1 292 ? 55.918  22.192  42.550  1.00 87.77  ? 319 HIS B CG    1 
ATOM   6501 N  ND1   . HIS B 1 292 ? 55.020  21.312  41.986  1.00 98.92  ? 319 HIS B ND1   1 
ATOM   6502 C  CD2   . HIS B 1 292 ? 55.253  23.359  42.712  1.00 80.61  ? 319 HIS B CD2   1 
ATOM   6503 C  CE1   . HIS B 1 292 ? 53.865  21.925  41.804  1.00 101.25 ? 319 HIS B CE1   1 
ATOM   6504 N  NE2   . HIS B 1 292 ? 53.979  23.167  42.237  1.00 92.17  ? 319 HIS B NE2   1 
ATOM   6505 N  N     . PRO B 1 293 ? 60.393  21.797  42.765  1.00 84.59  ? 320 PRO B N     1 
ATOM   6506 C  CA    . PRO B 1 293 ? 61.484  21.223  43.553  1.00 77.14  ? 320 PRO B CA    1 
ATOM   6507 C  C     . PRO B 1 293 ? 60.920  20.389  44.686  1.00 82.65  ? 320 PRO B C     1 
ATOM   6508 O  O     . PRO B 1 293 ? 59.760  20.578  45.086  1.00 82.47  ? 320 PRO B O     1 
ATOM   6509 C  CB    . PRO B 1 293 ? 62.227  22.458  44.088  1.00 78.02  ? 320 PRO B CB    1 
ATOM   6510 C  CG    . PRO B 1 293 ? 61.865  23.554  43.154  1.00 79.63  ? 320 PRO B CG    1 
ATOM   6511 C  CD    . PRO B 1 293 ? 60.474  23.267  42.694  1.00 79.42  ? 320 PRO B CD    1 
ATOM   6512 N  N     . PRO B 1 294 ? 61.695  19.451  45.223  1.00 86.25  ? 321 PRO B N     1 
ATOM   6513 C  CA    . PRO B 1 294 ? 61.189  18.639  46.334  1.00 78.40  ? 321 PRO B CA    1 
ATOM   6514 C  C     . PRO B 1 294 ? 60.868  19.505  47.542  1.00 73.84  ? 321 PRO B C     1 
ATOM   6515 O  O     . PRO B 1 294 ? 61.605  20.433  47.880  1.00 91.11  ? 321 PRO B O     1 
ATOM   6516 C  CB    . PRO B 1 294 ? 62.341  17.670  46.618  1.00 76.44  ? 321 PRO B CB    1 
ATOM   6517 C  CG    . PRO B 1 294 ? 63.552  18.359  46.088  1.00 91.81  ? 321 PRO B CG    1 
ATOM   6518 C  CD    . PRO B 1 294 ? 63.084  19.108  44.877  1.00 85.11  ? 321 PRO B CD    1 
ATOM   6519 N  N     . ALA B 1 295 ? 59.740  19.206  48.178  1.00 89.38  ? 322 ALA B N     1 
ATOM   6520 C  CA    . ALA B 1 295 ? 59.327  19.938  49.367  1.00 72.86  ? 322 ALA B CA    1 
ATOM   6521 C  C     . ALA B 1 295 ? 60.299  19.652  50.507  1.00 75.39  ? 322 ALA B C     1 
ATOM   6522 O  O     . ALA B 1 295 ? 60.425  18.506  50.958  1.00 83.85  ? 322 ALA B O     1 
ATOM   6523 C  CB    . ALA B 1 295 ? 57.903  19.554  49.761  1.00 72.19  ? 322 ALA B CB    1 
ATOM   6524 N  N     . GLU B 1 296 ? 60.987  20.693  50.969  1.00 79.68  ? 323 GLU B N     1 
ATOM   6525 C  CA    . GLU B 1 296 ? 62.029  20.543  51.971  1.00 78.79  ? 323 GLU B CA    1 
ATOM   6526 C  C     . GLU B 1 296 ? 61.434  20.299  53.358  1.00 89.09  ? 323 GLU B C     1 
ATOM   6527 O  O     . GLU B 1 296 ? 60.315  20.734  53.653  1.00 82.44  ? 323 GLU B O     1 
ATOM   6528 C  CB    . GLU B 1 296 ? 62.912  21.785  52.004  1.00 90.92  ? 323 GLU B CB    1 
ATOM   6529 C  CG    . GLU B 1 296 ? 63.526  22.144  50.657  1.00 112.80 ? 323 GLU B CG    1 
ATOM   6530 C  CD    . GLU B 1 296 ? 64.472  21.075  50.134  1.00 113.53 ? 323 GLU B CD    1 
ATOM   6531 O  OE1   . GLU B 1 296 ? 65.055  20.333  50.956  1.00 97.30  ? 323 GLU B OE1   1 
ATOM   6532 O  OE2   . GLU B 1 296 ? 64.628  20.977  48.897  1.00 113.76 ? 323 GLU B OE2   1 
ATOM   6533 N  N     . PRO B 1 297 ? 62.155  19.593  54.219  1.00 82.03  ? 324 PRO B N     1 
ATOM   6534 C  CA    . PRO B 1 297 ? 61.695  19.382  55.592  1.00 82.57  ? 324 PRO B CA    1 
ATOM   6535 C  C     . PRO B 1 297 ? 62.040  20.586  56.461  1.00 83.79  ? 324 PRO B C     1 
ATOM   6536 O  O     . PRO B 1 297 ? 62.611  21.573  56.004  1.00 95.00  ? 324 PRO B O     1 
ATOM   6537 C  CB    . PRO B 1 297 ? 62.468  18.135  56.025  1.00 83.84  ? 324 PRO B CB    1 
ATOM   6538 C  CG    . PRO B 1 297 ? 63.736  18.214  55.258  1.00 72.38  ? 324 PRO B CG    1 
ATOM   6539 C  CD    . PRO B 1 297 ? 63.375  18.822  53.923  1.00 78.27  ? 324 PRO B CD    1 
ATOM   6540 N  N     . SER B 1 298 ? 61.679  20.485  57.737  1.00 82.40  ? 325 SER B N     1 
ATOM   6541 C  CA    . SER B 1 298 ? 62.040  21.513  58.700  1.00 89.26  ? 325 SER B CA    1 
ATOM   6542 C  C     . SER B 1 298 ? 63.539  21.486  58.972  1.00 97.56  ? 325 SER B C     1 
ATOM   6543 O  O     . SER B 1 298 ? 64.181  20.433  58.937  1.00 102.08 ? 325 SER B O     1 
ATOM   6544 C  CB    . SER B 1 298 ? 61.272  21.309  60.004  1.00 83.02  ? 325 SER B CB    1 
ATOM   6545 O  OG    . SER B 1 298 ? 61.911  21.974  61.077  1.00 92.56  ? 325 SER B OG    1 
ATOM   6546 N  N     . ARG B 1 299 ? 64.104  22.662  59.244  1.00 95.89  ? 326 ARG B N     1 
ATOM   6547 C  CA    . ARG B 1 299 ? 65.504  22.719  59.646  1.00 94.52  ? 326 ARG B CA    1 
ATOM   6548 C  C     . ARG B 1 299 ? 65.714  22.259  61.082  1.00 96.84  ? 326 ARG B C     1 
ATOM   6549 O  O     . ARG B 1 299 ? 66.840  22.333  61.582  1.00 107.82 ? 326 ARG B O     1 
ATOM   6550 C  CB    . ARG B 1 299 ? 66.063  24.133  59.458  1.00 99.46  ? 326 ARG B CB    1 
ATOM   6551 C  CG    . ARG B 1 299 ? 65.233  25.231  60.098  1.00 118.12 ? 326 ARG B CG    1 
ATOM   6552 C  CD    . ARG B 1 299 ? 65.670  26.603  59.603  1.00 135.12 ? 326 ARG B CD    1 
ATOM   6553 N  NE    . ARG B 1 299 ? 64.759  27.663  60.024  1.00 149.83 ? 326 ARG B NE    1 
ATOM   6554 C  CZ    . ARG B 1 299 ? 63.637  27.987  59.393  1.00 143.23 ? 326 ARG B CZ    1 
ATOM   6555 N  NH1   . ARG B 1 299 ? 63.236  27.334  58.314  1.00 129.35 ? 326 ARG B NH1   1 
ATOM   6556 N  NH2   . ARG B 1 299 ? 62.898  28.992  59.858  1.00 114.54 ? 326 ARG B NH2   1 
ATOM   6557 N  N     . PHE B 1 300 ? 64.659  21.784  61.748  1.00 86.65  ? 327 PHE B N     1 
ATOM   6558 C  CA    . PHE B 1 300 ? 64.761  21.225  63.086  1.00 90.10  ? 327 PHE B CA    1 
ATOM   6559 C  C     . PHE B 1 300 ? 64.306  19.777  63.177  1.00 95.53  ? 327 PHE B C     1 
ATOM   6560 O  O     . PHE B 1 300 ? 64.604  19.119  64.180  1.00 96.25  ? 327 PHE B O     1 
ATOM   6561 C  CB    . PHE B 1 300 ? 63.948  22.066  64.082  1.00 87.79  ? 327 PHE B CB    1 
ATOM   6562 C  CG    . PHE B 1 300 ? 64.182  23.544  63.954  1.00 91.35  ? 327 PHE B CG    1 
ATOM   6563 C  CD1   . PHE B 1 300 ? 65.419  24.092  64.252  1.00 98.72  ? 327 PHE B CD1   1 
ATOM   6564 C  CD2   . PHE B 1 300 ? 63.164  24.386  63.537  1.00 97.35  ? 327 PHE B CD2   1 
ATOM   6565 C  CE1   . PHE B 1 300 ? 65.639  25.455  64.133  1.00 88.88  ? 327 PHE B CE1   1 
ATOM   6566 C  CE2   . PHE B 1 300 ? 63.376  25.749  63.417  1.00 93.24  ? 327 PHE B CE2   1 
ATOM   6567 C  CZ    . PHE B 1 300 ? 64.614  26.283  63.716  1.00 95.95  ? 327 PHE B CZ    1 
ATOM   6568 N  N     . ILE B 1 301 ? 63.597  19.266  62.174  1.00 93.19  ? 328 ILE B N     1 
ATOM   6569 C  CA    . ILE B 1 301 ? 63.211  17.863  62.097  1.00 89.05  ? 328 ILE B CA    1 
ATOM   6570 C  C     . ILE B 1 301 ? 64.011  17.210  60.979  1.00 96.38  ? 328 ILE B C     1 
ATOM   6571 O  O     . ILE B 1 301 ? 64.196  17.798  59.906  1.00 88.73  ? 328 ILE B O     1 
ATOM   6572 C  CB    . ILE B 1 301 ? 61.699  17.694  61.846  1.00 89.41  ? 328 ILE B CB    1 
ATOM   6573 C  CG1   . ILE B 1 301 ? 60.878  18.490  62.854  1.00 87.25  ? 328 ILE B CG1   1 
ATOM   6574 C  CG2   . ILE B 1 301 ? 61.301  16.232  61.915  1.00 96.75  ? 328 ILE B CG2   1 
ATOM   6575 C  CD1   . ILE B 1 301 ? 59.392  18.377  62.611  1.00 92.78  ? 328 ILE B CD1   1 
ATOM   6576 N  N     . SER B 1 302 ? 64.481  15.993  61.226  1.00 113.11 ? 329 SER B N     1 
ATOM   6577 C  CA    . SER B 1 302 ? 65.210  15.220  60.230  1.00 112.92 ? 329 SER B CA    1 
ATOM   6578 C  C     . SER B 1 302 ? 64.415  13.962  59.915  1.00 114.31 ? 329 SER B C     1 
ATOM   6579 O  O     . SER B 1 302 ? 64.090  13.186  60.821  1.00 121.99 ? 329 SER B O     1 
ATOM   6580 C  CB    . SER B 1 302 ? 66.615  14.872  60.725  1.00 128.02 ? 329 SER B CB    1 
ATOM   6581 O  OG    . SER B 1 302 ? 67.363  16.045  60.997  1.00 123.20 ? 329 SER B OG    1 
ATOM   6582 N  N     . ALA B 1 303 ? 64.093  13.771  58.639  1.00 110.06 ? 330 ALA B N     1 
ATOM   6583 C  CA    . ALA B 1 303 ? 63.402  12.565  58.220  1.00 122.61 ? 330 ALA B CA    1 
ATOM   6584 C  C     . ALA B 1 303 ? 64.341  11.361  58.313  1.00 116.84 ? 330 ALA B C     1 
ATOM   6585 O  O     . ALA B 1 303 ? 65.553  11.494  58.127  1.00 111.44 ? 330 ALA B O     1 
ATOM   6586 C  CB    . ALA B 1 303 ? 62.882  12.716  56.793  1.00 123.12 ? 330 ALA B CB    1 
ATOM   6587 N  N     . PRO B 1 304 ? 63.805  10.175  58.603  1.00 124.79 ? 331 PRO B N     1 
ATOM   6588 C  CA    . PRO B 1 304 ? 64.670  9.000   58.772  1.00 138.63 ? 331 PRO B CA    1 
ATOM   6589 C  C     . PRO B 1 304 ? 65.387  8.625   57.482  1.00 134.69 ? 331 PRO B C     1 
ATOM   6590 O  O     . PRO B 1 304 ? 64.864  8.791   56.378  1.00 130.06 ? 331 PRO B O     1 
ATOM   6591 C  CB    . PRO B 1 304 ? 63.695  7.901   59.211  1.00 124.17 ? 331 PRO B CB    1 
ATOM   6592 C  CG    . PRO B 1 304 ? 62.359  8.361   58.729  1.00 127.52 ? 331 PRO B CG    1 
ATOM   6593 C  CD    . PRO B 1 304 ? 62.386  9.856   58.833  1.00 122.19 ? 331 PRO B CD    1 
ATOM   6594 N  N     . THR B 1 305 ? 66.607  8.114   57.637  1.00 133.06 ? 332 THR B N     1 
ATOM   6595 C  CA    . THR B 1 305 ? 67.418  7.736   56.487  1.00 139.32 ? 332 THR B CA    1 
ATOM   6596 C  C     . THR B 1 305 ? 66.857  6.478   55.838  1.00 140.24 ? 332 THR B C     1 
ATOM   6597 O  O     . THR B 1 305 ? 66.593  5.479   56.515  1.00 145.21 ? 332 THR B O     1 
ATOM   6598 C  CB    . THR B 1 305 ? 68.871  7.508   56.908  1.00 146.32 ? 332 THR B CB    1 
ATOM   6599 O  OG1   . THR B 1 305 ? 69.461  8.753   57.300  1.00 146.96 ? 332 THR B OG1   1 
ATOM   6600 C  CG2   . THR B 1 305 ? 69.679  6.904   55.761  1.00 134.87 ? 332 THR B CG2   1 
ATOM   6601 N  N     . LYS B 1 306 ? 66.679  6.525   54.522  1.00 125.27 ? 333 LYS B N     1 
ATOM   6602 C  CA    . LYS B 1 306 ? 66.171  5.385   53.779  1.00 122.08 ? 333 LYS B CA    1 
ATOM   6603 C  C     . LYS B 1 306 ? 67.312  4.551   53.209  1.00 123.65 ? 333 LYS B C     1 
ATOM   6604 O  O     . LYS B 1 306 ? 68.408  5.052   52.946  1.00 123.18 ? 333 LYS B O     1 
ATOM   6605 C  CB    . LYS B 1 306 ? 65.242  5.847   52.658  1.00 115.74 ? 333 LYS B CB    1 
ATOM   6606 C  CG    . LYS B 1 306 ? 65.615  7.184   52.048  1.00 96.28  ? 333 LYS B CG    1 
ATOM   6607 C  CD    . LYS B 1 306 ? 64.458  7.732   51.235  1.00 98.46  ? 333 LYS B CD    1 
ATOM   6608 C  CE    . LYS B 1 306 ? 63.178  7.755   52.060  1.00 104.31 ? 333 LYS B CE    1 
ATOM   6609 N  NZ    . LYS B 1 306 ? 62.025  8.329   51.313  1.00 105.30 ? 333 LYS B NZ    1 
ATOM   6610 N  N     . THR B 1 307 ? 67.042  3.261   53.031  1.00 121.08 ? 334 THR B N     1 
ATOM   6611 C  CA    . THR B 1 307 ? 67.996  2.317   52.460  1.00 124.81 ? 334 THR B CA    1 
ATOM   6612 C  C     . THR B 1 307 ? 67.355  1.661   51.242  1.00 114.58 ? 334 THR B C     1 
ATOM   6613 O  O     . THR B 1 307 ? 66.341  0.953   51.387  1.00 118.57 ? 334 THR B O     1 
ATOM   6614 C  CB    . THR B 1 307 ? 68.413  1.264   53.494  1.00 124.21 ? 334 THR B CB    1 
ATOM   6615 O  OG1   . THR B 1 307 ? 67.246  0.660   54.062  1.00 125.18 ? 334 THR B OG1   1 
ATOM   6616 C  CG2   . THR B 1 307 ? 69.237  1.896   54.600  1.00 112.06 ? 334 THR B CG2   1 
ATOM   6617 N  N     . PRO B 1 308 ? 67.883  1.860   50.039  1.00 111.54 ? 335 PRO B N     1 
ATOM   6618 C  CA    . PRO B 1 308 ? 67.242  1.323   48.838  1.00 112.62 ? 335 PRO B CA    1 
ATOM   6619 C  C     . PRO B 1 308 ? 67.745  -0.070  48.471  1.00 117.69 ? 335 PRO B C     1 
ATOM   6620 O  O     . PRO B 1 308 ? 68.663  -0.618  49.085  1.00 125.68 ? 335 PRO B O     1 
ATOM   6621 C  CB    . PRO B 1 308 ? 67.640  2.339   47.763  1.00 109.50 ? 335 PRO B CB    1 
ATOM   6622 C  CG    . PRO B 1 308 ? 69.004  2.771   48.188  1.00 102.28 ? 335 PRO B CG    1 
ATOM   6623 C  CD    . PRO B 1 308 ? 69.000  2.762   49.705  1.00 111.64 ? 335 PRO B CD    1 
ATOM   6624 N  N     . ASP B 1 309 ? 67.118  -0.631  47.440  1.00 117.80 ? 336 ASP B N     1 
ATOM   6625 C  CA    . ASP B 1 309 ? 67.509  -1.919  46.885  1.00 126.38 ? 336 ASP B CA    1 
ATOM   6626 C  C     . ASP B 1 309 ? 67.196  -1.909  45.394  1.00 122.47 ? 336 ASP B C     1 
ATOM   6627 O  O     . ASP B 1 309 ? 66.706  -0.916  44.848  1.00 111.83 ? 336 ASP B O     1 
ATOM   6628 C  CB    . ASP B 1 309 ? 66.800  -3.076  47.602  1.00 119.89 ? 336 ASP B CB    1 
ATOM   6629 C  CG    . ASP B 1 309 ? 65.295  -2.875  47.699  1.00 109.65 ? 336 ASP B CG    1 
ATOM   6630 O  OD1   . ASP B 1 309 ? 64.646  -2.637  46.660  1.00 116.09 ? 336 ASP B OD1   1 
ATOM   6631 O  OD2   . ASP B 1 309 ? 64.756  -2.962  48.820  1.00 115.73 ? 336 ASP B OD2   1 
ATOM   6632 N  N     . LYS B 1 310 ? 67.483  -3.029  44.732  1.00 127.92 ? 337 LYS B N     1 
ATOM   6633 C  CA    . LYS B 1 310 ? 67.120  -3.216  43.335  1.00 125.30 ? 337 LYS B CA    1 
ATOM   6634 C  C     . LYS B 1 310 ? 65.742  -3.853  43.173  1.00 121.74 ? 337 LYS B C     1 
ATOM   6635 O  O     . LYS B 1 310 ? 65.425  -4.354  42.088  1.00 120.47 ? 337 LYS B O     1 
ATOM   6636 C  CB    . LYS B 1 310 ? 68.178  -4.059  42.618  1.00 128.98 ? 337 LYS B CB    1 
ATOM   6637 C  CG    . LYS B 1 310 ? 69.571  -3.448  42.610  1.00 123.13 ? 337 LYS B CG    1 
ATOM   6638 C  CD    . LYS B 1 310 ? 69.592  -2.106  41.901  1.00 117.86 ? 337 LYS B CD    1 
ATOM   6639 C  CE    . LYS B 1 310 ? 71.008  -1.559  41.800  1.00 120.35 ? 337 LYS B CE    1 
ATOM   6640 N  NZ    . LYS B 1 310 ? 71.887  -2.435  40.981  1.00 117.94 ? 337 LYS B NZ    1 
ATOM   6641 N  N     . MET B 1 311 ? 64.923  -3.841  44.230  1.00 115.07 ? 338 MET B N     1 
ATOM   6642 C  CA    . MET B 1 311 ? 63.584  -4.434  44.222  1.00 112.23 ? 338 MET B CA    1 
ATOM   6643 C  C     . MET B 1 311 ? 63.613  -5.906  43.824  1.00 113.97 ? 338 MET B C     1 
ATOM   6644 O  O     . MET B 1 311 ? 62.660  -6.420  43.235  1.00 117.80 ? 338 MET B O     1 
ATOM   6645 C  CB    . MET B 1 311 ? 62.631  -3.662  43.306  1.00 115.85 ? 338 MET B CB    1 
ATOM   6646 C  CG    . MET B 1 311 ? 62.357  -2.240  43.745  1.00 109.86 ? 338 MET B CG    1 
ATOM   6647 S  SD    . MET B 1 311 ? 61.073  -1.480  42.733  1.00 115.65 ? 338 MET B SD    1 
ATOM   6648 C  CE    . MET B 1 311 ? 61.740  -1.742  41.098  1.00 114.08 ? 338 MET B CE    1 
ATOM   6649 N  N     . GLY B 1 312 ? 64.702  -6.599  44.142  1.00 106.58 ? 339 GLY B N     1 
ATOM   6650 C  CA    . GLY B 1 312 ? 64.829  -7.989  43.766  1.00 99.59  ? 339 GLY B CA    1 
ATOM   6651 C  C     . GLY B 1 312 ? 65.183  -8.234  42.318  1.00 99.88  ? 339 GLY B C     1 
ATOM   6652 O  O     . GLY B 1 312 ? 65.173  -9.391  41.886  1.00 125.02 ? 339 GLY B O     1 
ATOM   6653 N  N     . PHE B 1 313 ? 65.489  -7.192  41.555  1.00 110.83 ? 340 PHE B N     1 
ATOM   6654 C  CA    . PHE B 1 313 ? 65.916  -7.350  40.174  1.00 119.62 ? 340 PHE B CA    1 
ATOM   6655 C  C     . PHE B 1 313 ? 67.415  -7.618  40.106  1.00 115.21 ? 340 PHE B C     1 
ATOM   6656 O  O     . PHE B 1 313 ? 68.162  -7.370  41.055  1.00 118.79 ? 340 PHE B O     1 
ATOM   6657 C  CB    . PHE B 1 313 ? 65.578  -6.107  39.350  1.00 112.47 ? 340 PHE B CB    1 
ATOM   6658 C  CG    . PHE B 1 313 ? 64.114  -5.951  39.058  1.00 111.79 ? 340 PHE B CG    1 
ATOM   6659 C  CD1   . PHE B 1 313 ? 63.532  -6.628  37.999  1.00 109.98 ? 340 PHE B CD1   1 
ATOM   6660 C  CD2   . PHE B 1 313 ? 63.322  -5.120  39.834  1.00 111.56 ? 340 PHE B CD2   1 
ATOM   6661 C  CE1   . PHE B 1 313 ? 62.185  -6.486  37.724  1.00 102.43 ? 340 PHE B CE1   1 
ATOM   6662 C  CE2   . PHE B 1 313 ? 61.974  -4.973  39.563  1.00 106.24 ? 340 PHE B CE2   1 
ATOM   6663 C  CZ    . PHE B 1 313 ? 61.405  -5.659  38.506  1.00 107.99 ? 340 PHE B CZ    1 
ATOM   6664 N  N     . ASP B 1 314 ? 67.850  -8.137  38.959  1.00 101.53 ? 341 ASP B N     1 
ATOM   6665 C  CA    . ASP B 1 314 ? 69.281  -8.282  38.733  1.00 117.42 ? 341 ASP B CA    1 
ATOM   6666 C  C     . ASP B 1 314 ? 69.925  -6.936  38.426  1.00 119.35 ? 341 ASP B C     1 
ATOM   6667 O  O     . ASP B 1 314 ? 71.109  -6.733  38.719  1.00 111.13 ? 341 ASP B O     1 
ATOM   6668 C  CB    . ASP B 1 314 ? 69.535  -9.286  37.607  1.00 117.84 ? 341 ASP B CB    1 
ATOM   6669 C  CG    . ASP B 1 314 ? 69.213  -10.716 38.015  1.00 125.73 ? 341 ASP B CG    1 
ATOM   6670 O  OD1   . ASP B 1 314 ? 68.110  -10.950 38.555  1.00 118.73 ? 341 ASP B OD1   1 
ATOM   6671 O  OD2   . ASP B 1 314 ? 70.060  -11.607 37.794  1.00 140.73 ? 341 ASP B OD2   1 
ATOM   6672 N  N     . GLU B 1 315 ? 69.162  -6.008  37.855  1.00 128.84 ? 342 GLU B N     1 
ATOM   6673 C  CA    . GLU B 1 315 ? 69.621  -4.648  37.608  1.00 123.84 ? 342 GLU B CA    1 
ATOM   6674 C  C     . GLU B 1 315 ? 68.413  -3.787  37.280  1.00 112.55 ? 342 GLU B C     1 
ATOM   6675 O  O     . GLU B 1 315 ? 67.433  -4.265  36.701  1.00 108.18 ? 342 GLU B O     1 
ATOM   6676 C  CB    . GLU B 1 315 ? 70.645  -4.589  36.465  1.00 112.04 ? 342 GLU B CB    1 
ATOM   6677 C  CG    . GLU B 1 315 ? 71.276  -3.215  36.240  1.00 112.06 ? 342 GLU B CG    1 
ATOM   6678 C  CD    . GLU B 1 315 ? 72.144  -2.754  37.402  1.00 123.68 ? 342 GLU B CD    1 
ATOM   6679 O  OE1   . GLU B 1 315 ? 71.590  -2.298  38.426  1.00 125.14 ? 342 GLU B OE1   1 
ATOM   6680 O  OE2   . GLU B 1 315 ? 73.386  -2.848  37.290  1.00 125.09 ? 342 GLU B OE2   1 
ATOM   6681 N  N     . VAL B 1 316 ? 68.490  -2.520  37.670  1.00 105.82 ? 343 VAL B N     1 
ATOM   6682 C  CA    . VAL B 1 316 ? 67.477  -1.525  37.348  1.00 104.04 ? 343 VAL B CA    1 
ATOM   6683 C  C     . VAL B 1 316 ? 68.174  -0.419  36.569  1.00 112.01 ? 343 VAL B C     1 
ATOM   6684 O  O     . VAL B 1 316 ? 68.994  0.321   37.128  1.00 113.86 ? 343 VAL B O     1 
ATOM   6685 C  CB    . VAL B 1 316 ? 66.788  -0.973  38.603  1.00 105.45 ? 343 VAL B CB    1 
ATOM   6686 C  CG1   . VAL B 1 316 ? 65.770  0.097   38.222  1.00 108.47 ? 343 VAL B CG1   1 
ATOM   6687 C  CG2   . VAL B 1 316 ? 66.127  -2.101  39.387  1.00 88.70  ? 343 VAL B CG2   1 
ATOM   6688 N  N     . PHE B 1 317 ? 67.865  -0.311  35.281  1.00 104.14 ? 344 PHE B N     1 
ATOM   6689 C  CA    . PHE B 1 317 ? 68.477  0.693   34.426  1.00 101.23 ? 344 PHE B CA    1 
ATOM   6690 C  C     . PHE B 1 317 ? 67.624  1.959   34.375  1.00 106.75 ? 344 PHE B C     1 
ATOM   6691 O  O     . PHE B 1 317 ? 66.415  1.937   34.614  1.00 102.62 ? 344 PHE B O     1 
ATOM   6692 C  CB    . PHE B 1 317 ? 68.677  0.149   33.009  1.00 106.57 ? 344 PHE B CB    1 
ATOM   6693 C  CG    . PHE B 1 317 ? 69.571  -1.058  32.933  1.00 112.00 ? 344 PHE B CG    1 
ATOM   6694 C  CD1   . PHE B 1 317 ? 70.950  -0.917  32.883  1.00 113.44 ? 344 PHE B CD1   1 
ATOM   6695 C  CD2   . PHE B 1 317 ? 69.032  -2.334  32.889  1.00 113.67 ? 344 PHE B CD2   1 
ATOM   6696 C  CE1   . PHE B 1 317 ? 71.775  -2.026  32.805  1.00 112.12 ? 344 PHE B CE1   1 
ATOM   6697 C  CE2   . PHE B 1 317 ? 69.850  -3.447  32.809  1.00 110.91 ? 344 PHE B CE2   1 
ATOM   6698 C  CZ    . PHE B 1 317 ? 71.224  -3.293  32.766  1.00 115.10 ? 344 PHE B CZ    1 
ATOM   6699 N  N     . MET B 1 318 ? 68.278  3.075   34.052  1.00 108.60 ? 345 MET B N     1 
ATOM   6700 C  CA    . MET B 1 318 ? 67.598  4.347   33.814  1.00 99.09  ? 345 MET B CA    1 
ATOM   6701 C  C     . MET B 1 318 ? 68.336  5.079   32.702  1.00 105.64 ? 345 MET B C     1 
ATOM   6702 O  O     . MET B 1 318 ? 69.460  5.548   32.909  1.00 107.41 ? 345 MET B O     1 
ATOM   6703 C  CB    . MET B 1 318 ? 67.544  5.203   35.078  1.00 100.75 ? 345 MET B CB    1 
ATOM   6704 C  CG    . MET B 1 318 ? 66.947  6.579   34.837  1.00 89.96  ? 345 MET B CG    1 
ATOM   6705 S  SD    . MET B 1 318 ? 67.266  7.734   36.175  1.00 118.77 ? 345 MET B SD    1 
ATOM   6706 C  CE    . MET B 1 318 ? 67.553  9.235   35.239  1.00 95.84  ? 345 MET B CE    1 
ATOM   6707 N  N     . ILE B 1 319 ? 67.707  5.181   31.530  1.00 102.24 ? 346 ILE B N     1 
ATOM   6708 C  CA    . ILE B 1 319 ? 68.303  5.876   30.394  1.00 109.33 ? 346 ILE B CA    1 
ATOM   6709 C  C     . ILE B 1 319 ? 68.151  7.378   30.589  1.00 102.57 ? 346 ILE B C     1 
ATOM   6710 O  O     . ILE B 1 319 ? 67.096  7.861   31.018  1.00 100.39 ? 346 ILE B O     1 
ATOM   6711 C  CB    . ILE B 1 319 ? 67.653  5.422   29.074  1.00 105.66 ? 346 ILE B CB    1 
ATOM   6712 C  CG1   . ILE B 1 319 ? 67.379  3.921   29.093  1.00 102.64 ? 346 ILE B CG1   1 
ATOM   6713 C  CG2   . ILE B 1 319 ? 68.546  5.769   27.890  1.00 98.22  ? 346 ILE B CG2   1 
ATOM   6714 C  CD1   . ILE B 1 319 ? 66.716  3.411   27.835  1.00 95.14  ? 346 ILE B CD1   1 
ATOM   6715 N  N     . ASN B 1 320 ? 69.203  8.129   30.268  1.00 99.16  ? 347 ASN B N     1 
ATOM   6716 C  CA    . ASN B 1 320 ? 69.158  9.578   30.419  1.00 100.73 ? 347 ASN B CA    1 
ATOM   6717 C  C     . ASN B 1 320 ? 70.184  10.220  29.499  1.00 96.33  ? 347 ASN B C     1 
ATOM   6718 O  O     . ASN B 1 320 ? 71.326  9.758   29.425  1.00 99.48  ? 347 ASN B O     1 
ATOM   6719 C  CB    . ASN B 1 320 ? 69.417  9.986   31.871  1.00 102.25 ? 347 ASN B CB    1 
ATOM   6720 C  CG    . ASN B 1 320 ? 69.519  11.484  32.040  1.00 102.07 ? 347 ASN B CG    1 
ATOM   6721 O  OD1   . ASN B 1 320 ? 70.605  12.023  32.259  1.00 107.90 ? 347 ASN B OD1   1 
ATOM   6722 N  ND2   . ASN B 1 320 ? 68.387  12.170  31.919  1.00 99.74  ? 347 ASN B ND2   1 
ATOM   6723 N  N     . LEU B 1 321 ? 69.775  11.275  28.800  1.00 105.17 ? 348 LEU B N     1 
ATOM   6724 C  CA    . LEU B 1 321 ? 70.708  12.076  28.021  1.00 101.62 ? 348 LEU B CA    1 
ATOM   6725 C  C     . LEU B 1 321 ? 71.372  13.095  28.940  1.00 110.91 ? 348 LEU B C     1 
ATOM   6726 O  O     . LEU B 1 321 ? 70.693  13.775  29.718  1.00 109.38 ? 348 LEU B O     1 
ATOM   6727 C  CB    . LEU B 1 321 ? 69.983  12.769  26.869  1.00 101.74 ? 348 LEU B CB    1 
ATOM   6728 C  CG    . LEU B 1 321 ? 70.646  12.671  25.492  1.00 105.55 ? 348 LEU B CG    1 
ATOM   6729 C  CD1   . LEU B 1 321 ? 69.698  13.160  24.409  1.00 99.65  ? 348 LEU B CD1   1 
ATOM   6730 C  CD2   . LEU B 1 321 ? 71.950  13.456  25.458  1.00 116.20 ? 348 LEU B CD2   1 
ATOM   6731 N  N     . ARG B 1 322 ? 72.703  13.194  28.855  1.00 112.97 ? 349 ARG B N     1 
ATOM   6732 C  CA    . ARG B 1 322 ? 73.454  13.978  29.833  1.00 117.78 ? 349 ARG B CA    1 
ATOM   6733 C  C     . ARG B 1 322 ? 73.040  15.443  29.832  1.00 121.22 ? 349 ARG B C     1 
ATOM   6734 O  O     . ARG B 1 322 ? 73.051  16.090  30.887  1.00 126.08 ? 349 ARG B O     1 
ATOM   6735 C  CB    . ARG B 1 322 ? 74.958  13.850  29.575  1.00 125.69 ? 349 ARG B CB    1 
ATOM   6736 C  CG    . ARG B 1 322 ? 75.826  14.514  30.641  1.00 135.60 ? 349 ARG B CG    1 
ATOM   6737 C  CD    . ARG B 1 322 ? 77.314  14.218  30.463  1.00 143.54 ? 349 ARG B CD    1 
ATOM   6738 N  NE    . ARG B 1 322 ? 77.853  14.753  29.217  1.00 161.34 ? 349 ARG B NE    1 
ATOM   6739 C  CZ    . ARG B 1 322 ? 78.271  14.011  28.200  1.00 157.57 ? 349 ARG B CZ    1 
ATOM   6740 N  NH1   . ARG B 1 322 ? 78.240  12.690  28.251  1.00 155.97 ? 349 ARG B NH1   1 
ATOM   6741 N  NH2   . ARG B 1 322 ? 78.738  14.610  27.108  1.00 143.57 ? 349 ARG B NH2   1 
ATOM   6742 N  N     . ARG B 1 323 ? 72.660  15.984  28.672  1.00 122.86 ? 350 ARG B N     1 
ATOM   6743 C  CA    . ARG B 1 323 ? 72.274  17.388  28.611  1.00 122.42 ? 350 ARG B CA    1 
ATOM   6744 C  C     . ARG B 1 323 ? 70.937  17.653  29.291  1.00 119.82 ? 350 ARG B C     1 
ATOM   6745 O  O     . ARG B 1 323 ? 70.637  18.809  29.612  1.00 121.75 ? 350 ARG B O     1 
ATOM   6746 C  CB    . ARG B 1 323 ? 72.220  17.865  27.160  1.00 116.49 ? 350 ARG B CB    1 
ATOM   6747 C  CG    . ARG B 1 323 ? 71.004  17.392  26.395  1.00 114.98 ? 350 ARG B CG    1 
ATOM   6748 C  CD    . ARG B 1 323 ? 70.820  18.210  25.131  1.00 116.67 ? 350 ARG B CD    1 
ATOM   6749 N  NE    . ARG B 1 323 ? 69.546  17.935  24.480  1.00 115.47 ? 350 ARG B NE    1 
ATOM   6750 C  CZ    . ARG B 1 323 ? 69.368  17.002  23.555  1.00 109.46 ? 350 ARG B CZ    1 
ATOM   6751 N  NH1   . ARG B 1 323 ? 70.363  16.231  23.151  1.00 119.06 ? 350 ARG B NH1   1 
ATOM   6752 N  NH2   . ARG B 1 323 ? 68.160  16.841  23.022  1.00 102.95 ? 350 ARG B NH2   1 
ATOM   6753 N  N     . ARG B 1 324 ? 70.130  16.616  29.515  1.00 113.62 ? 351 ARG B N     1 
ATOM   6754 C  CA    . ARG B 1 324 ? 68.871  16.752  30.248  1.00 111.43 ? 351 ARG B CA    1 
ATOM   6755 C  C     . ARG B 1 324 ? 69.137  16.564  31.742  1.00 109.87 ? 351 ARG B C     1 
ATOM   6756 O  O     . ARG B 1 324 ? 68.747  15.576  32.367  1.00 103.31 ? 351 ARG B O     1 
ATOM   6757 C  CB    . ARG B 1 324 ? 67.845  15.756  29.729  1.00 105.57 ? 351 ARG B CB    1 
ATOM   6758 C  CG    . ARG B 1 324 ? 67.468  15.961  28.279  1.00 98.28  ? 351 ARG B CG    1 
ATOM   6759 C  CD    . ARG B 1 324 ? 66.217  15.176  27.944  1.00 110.36 ? 351 ARG B CD    1 
ATOM   6760 N  NE    . ARG B 1 324 ? 65.726  15.471  26.605  1.00 118.61 ? 351 ARG B NE    1 
ATOM   6761 C  CZ    . ARG B 1 324 ? 65.851  14.658  25.566  1.00 115.44 ? 351 ARG B CZ    1 
ATOM   6762 N  NH1   . ARG B 1 324 ? 66.436  13.477  25.679  1.00 128.56 ? 351 ARG B NH1   1 
ATOM   6763 N  NH2   . ARG B 1 324 ? 65.371  15.037  24.384  1.00 107.35 ? 351 ARG B NH2   1 
ATOM   6764 N  N     . GLN B 1 325 ? 69.821  17.559  32.311  1.00 110.70 ? 352 GLN B N     1 
ATOM   6765 C  CA    . GLN B 1 325 ? 70.257  17.472  33.701  1.00 107.08 ? 352 GLN B CA    1 
ATOM   6766 C  C     . GLN B 1 325 ? 69.086  17.516  34.675  1.00 108.15 ? 352 GLN B C     1 
ATOM   6767 O  O     . GLN B 1 325 ? 69.133  16.862  35.724  1.00 117.86 ? 352 GLN B O     1 
ATOM   6768 C  CB    . GLN B 1 325 ? 71.245  18.596  34.003  1.00 121.89 ? 352 GLN B CB    1 
ATOM   6769 C  CG    . GLN B 1 325 ? 71.727  18.634  35.440  1.00 131.31 ? 352 GLN B CG    1 
ATOM   6770 C  CD    . GLN B 1 325 ? 72.775  19.703  35.663  1.00 141.09 ? 352 GLN B CD    1 
ATOM   6771 O  OE1   . GLN B 1 325 ? 73.085  20.484  34.761  1.00 143.77 ? 352 GLN B OE1   1 
ATOM   6772 N  NE2   . GLN B 1 325 ? 73.331  19.743  36.868  1.00 150.44 ? 352 GLN B NE2   1 
ATOM   6773 N  N     . ASP B 1 326 ? 68.034  18.271  34.356  1.00 101.29 ? 353 ASP B N     1 
ATOM   6774 C  CA    . ASP B 1 326 ? 66.908  18.385  35.277  1.00 99.19  ? 353 ASP B CA    1 
ATOM   6775 C  C     . ASP B 1 326 ? 66.035  17.136  35.278  1.00 92.15  ? 353 ASP B C     1 
ATOM   6776 O  O     . ASP B 1 326 ? 65.445  16.801  36.311  1.00 93.73  ? 353 ASP B O     1 
ATOM   6777 C  CB    . ASP B 1 326 ? 66.079  19.626  34.945  1.00 85.78  ? 353 ASP B CB    1 
ATOM   6778 C  CG    . ASP B 1 326 ? 66.833  20.917  35.225  1.00 119.87 ? 353 ASP B CG    1 
ATOM   6779 O  OD1   . ASP B 1 326 ? 67.705  20.910  36.126  1.00 121.97 ? 353 ASP B OD1   1 
ATOM   6780 O  OD2   . ASP B 1 326 ? 66.557  21.935  34.551  1.00 119.47 ? 353 ASP B OD2   1 
ATOM   6781 N  N     . ARG B 1 327 ? 65.938  16.438  34.142  1.00 98.20  ? 354 ARG B N     1 
ATOM   6782 C  CA    . ARG B 1 327 ? 65.298  15.126  34.136  1.00 89.09  ? 354 ARG B CA    1 
ATOM   6783 C  C     . ARG B 1 327 ? 66.072  14.124  34.981  1.00 101.86 ? 354 ARG B C     1 
ATOM   6784 O  O     . ARG B 1 327 ? 65.474  13.218  35.575  1.00 98.84  ? 354 ARG B O     1 
ATOM   6785 C  CB    . ARG B 1 327 ? 65.175  14.595  32.709  1.00 91.81  ? 354 ARG B CB    1 
ATOM   6786 C  CG    . ARG B 1 327 ? 64.062  15.196  31.893  1.00 92.18  ? 354 ARG B CG    1 
ATOM   6787 C  CD    . ARG B 1 327 ? 63.896  14.417  30.605  1.00 83.97  ? 354 ARG B CD    1 
ATOM   6788 N  NE    . ARG B 1 327 ? 63.024  15.102  29.661  1.00 112.65 ? 354 ARG B NE    1 
ATOM   6789 C  CZ    . ARG B 1 327 ? 62.767  14.672  28.434  1.00 115.26 ? 354 ARG B CZ    1 
ATOM   6790 N  NH1   . ARG B 1 327 ? 63.298  13.552  27.969  1.00 104.50 ? 354 ARG B NH1   1 
ATOM   6791 N  NH2   . ARG B 1 327 ? 61.960  15.384  27.652  1.00 129.69 ? 354 ARG B NH2   1 
ATOM   6792 N  N     . ARG B 1 328 ? 67.400  14.263  35.034  1.00 94.12  ? 355 ARG B N     1 
ATOM   6793 C  CA    . ARG B 1 328 ? 68.225  13.325  35.787  1.00 94.35  ? 355 ARG B CA    1 
ATOM   6794 C  C     . ARG B 1 328 ? 68.042  13.507  37.289  1.00 96.07  ? 355 ARG B C     1 
ATOM   6795 O  O     . ARG B 1 328 ? 67.823  12.532  38.017  1.00 85.80  ? 355 ARG B O     1 
ATOM   6796 C  CB    . ARG B 1 328 ? 69.692  13.492  35.394  1.00 87.24  ? 355 ARG B CB    1 
ATOM   6797 C  CG    . ARG B 1 328 ? 70.621  12.466  36.013  1.00 88.07  ? 355 ARG B CG    1 
ATOM   6798 C  CD    . ARG B 1 328 ? 72.011  12.537  35.407  1.00 86.95  ? 355 ARG B CD    1 
ATOM   6799 N  NE    . ARG B 1 328 ? 72.630  13.848  35.573  1.00 104.36 ? 355 ARG B NE    1 
ATOM   6800 C  CZ    . ARG B 1 328 ? 72.778  14.740  34.601  1.00 109.63 ? 355 ARG B CZ    1 
ATOM   6801 N  NH1   . ARG B 1 328 ? 72.352  14.503  33.371  1.00 99.05  ? 355 ARG B NH1   1 
ATOM   6802 N  NH2   . ARG B 1 328 ? 73.372  15.899  34.870  1.00 115.23 ? 355 ARG B NH2   1 
ATOM   6803 N  N     . GLU B 1 329 ? 68.127  14.748  37.774  1.00 91.15  ? 356 GLU B N     1 
ATOM   6804 C  CA    . GLU B 1 329 ? 67.987  14.982  39.207  1.00 98.97  ? 356 GLU B CA    1 
ATOM   6805 C  C     . GLU B 1 329 ? 66.582  14.646  39.691  1.00 98.17  ? 356 GLU B C     1 
ATOM   6806 O  O     . GLU B 1 329 ? 66.407  14.156  40.813  1.00 100.39 ? 356 GLU B O     1 
ATOM   6807 C  CB    . GLU B 1 329 ? 68.331  16.432  39.537  1.00 107.22 ? 356 GLU B CB    1 
ATOM   6808 C  CG    . GLU B 1 329 ? 69.729  16.845  39.123  1.00 113.67 ? 356 GLU B CG    1 
ATOM   6809 C  CD    . GLU B 1 329 ? 70.026  18.289  39.467  1.00 130.73 ? 356 GLU B CD    1 
ATOM   6810 O  OE1   . GLU B 1 329 ? 69.221  18.900  40.207  1.00 116.83 ? 356 GLU B OE1   1 
ATOM   6811 O  OE2   . GLU B 1 329 ? 71.060  18.809  38.995  1.00 124.58 ? 356 GLU B OE2   1 
ATOM   6812 N  N     . ARG B 1 330 ? 65.569  14.895  38.857  1.00 95.61  ? 357 ARG B N     1 
ATOM   6813 C  CA    . ARG B 1 330 ? 64.197  14.585  39.244  1.00 87.45  ? 357 ARG B CA    1 
ATOM   6814 C  C     . ARG B 1 330 ? 64.004  13.086  39.426  1.00 95.46  ? 357 ARG B C     1 
ATOM   6815 O  O     . ARG B 1 330 ? 63.395  12.646  40.407  1.00 94.28  ? 357 ARG B O     1 
ATOM   6816 C  CB    . ARG B 1 330 ? 63.222  15.127  38.200  1.00 83.14  ? 357 ARG B CB    1 
ATOM   6817 C  CG    . ARG B 1 330 ? 61.789  15.227  38.706  1.00 92.80  ? 357 ARG B CG    1 
ATOM   6818 C  CD    . ARG B 1 330 ? 60.783  15.358  37.572  1.00 85.92  ? 357 ARG B CD    1 
ATOM   6819 N  NE    . ARG B 1 330 ? 60.448  14.062  36.993  1.00 112.46 ? 357 ARG B NE    1 
ATOM   6820 C  CZ    . ARG B 1 330 ? 59.451  13.290  37.407  1.00 111.75 ? 357 ARG B CZ    1 
ATOM   6821 N  NH1   . ARG B 1 330 ? 58.653  13.660  38.396  1.00 107.85 ? 357 ARG B NH1   1 
ATOM   6822 N  NH2   . ARG B 1 330 ? 59.251  12.115  36.815  1.00 94.07  ? 357 ARG B NH2   1 
ATOM   6823 N  N     . MET B 1 331 ? 64.512  12.285  38.482  1.00 95.28  ? 358 MET B N     1 
ATOM   6824 C  CA    . MET B 1 331 ? 64.364  10.835  38.576  1.00 91.93  ? 358 MET B CA    1 
ATOM   6825 C  C     . MET B 1 331 ? 65.169  10.265  39.737  1.00 97.57  ? 358 MET B C     1 
ATOM   6826 O  O     . MET B 1 331 ? 64.728  9.315   40.397  1.00 91.64  ? 358 MET B O     1 
ATOM   6827 C  CB    . MET B 1 331 ? 64.788  10.177  37.265  1.00 96.19  ? 358 MET B CB    1 
ATOM   6828 C  CG    . MET B 1 331 ? 63.854  10.433  36.096  1.00 97.24  ? 358 MET B CG    1 
ATOM   6829 S  SD    . MET B 1 331 ? 62.268  9.601   36.287  1.00 101.50 ? 358 MET B SD    1 
ATOM   6830 C  CE    . MET B 1 331 ? 62.797  7.890   36.419  1.00 92.30  ? 358 MET B CE    1 
ATOM   6831 N  N     . LEU B 1 332 ? 66.354  10.822  40.000  1.00 102.63 ? 359 LEU B N     1 
ATOM   6832 C  CA    . LEU B 1 332 ? 67.159  10.335  41.115  1.00 96.08  ? 359 LEU B CA    1 
ATOM   6833 C  C     . LEU B 1 332 ? 66.498  10.653  42.450  1.00 98.60  ? 359 LEU B C     1 
ATOM   6834 O  O     . LEU B 1 332 ? 66.570  9.852   43.387  1.00 93.43  ? 359 LEU B O     1 
ATOM   6835 C  CB    . LEU B 1 332 ? 68.565  10.929  41.053  1.00 94.21  ? 359 LEU B CB    1 
ATOM   6836 C  CG    . LEU B 1 332 ? 69.401  10.508  39.843  1.00 87.94  ? 359 LEU B CG    1 
ATOM   6837 C  CD1   . LEU B 1 332 ? 70.739  11.235  39.827  1.00 101.78 ? 359 LEU B CD1   1 
ATOM   6838 C  CD2   . LEU B 1 332 ? 69.599  9.007   39.818  1.00 121.77 ? 359 LEU B CD2   1 
ATOM   6839 N  N     . ARG B 1 333 ? 65.845  11.814  42.555  1.00 85.42  ? 360 ARG B N     1 
ATOM   6840 C  CA    . ARG B 1 333 ? 65.101  12.122  43.771  1.00 95.00  ? 360 ARG B CA    1 
ATOM   6841 C  C     . ARG B 1 333 ? 63.866  11.239  43.913  1.00 102.49 ? 360 ARG B C     1 
ATOM   6842 O  O     . ARG B 1 333 ? 63.487  10.876  45.033  1.00 94.81  ? 360 ARG B O     1 
ATOM   6843 C  CB    . ARG B 1 333 ? 64.698  13.595  43.788  1.00 82.36  ? 360 ARG B CB    1 
ATOM   6844 C  CG    . ARG B 1 333 ? 65.861  14.568  43.869  1.00 91.20  ? 360 ARG B CG    1 
ATOM   6845 C  CD    . ARG B 1 333 ? 65.361  15.959  44.220  1.00 103.00 ? 360 ARG B CD    1 
ATOM   6846 N  NE    . ARG B 1 333 ? 66.280  17.008  43.797  1.00 114.21 ? 360 ARG B NE    1 
ATOM   6847 C  CZ    . ARG B 1 333 ? 66.141  17.717  42.685  1.00 125.58 ? 360 ARG B CZ    1 
ATOM   6848 N  NH1   . ARG B 1 333 ? 65.120  17.523  41.865  1.00 107.35 ? 360 ARG B NH1   1 
ATOM   6849 N  NH2   . ARG B 1 333 ? 67.048  18.644  42.389  1.00 134.35 ? 360 ARG B NH2   1 
ATOM   6850 N  N     . ALA B 1 334 ? 63.233  10.878  42.795  1.00 98.31  ? 361 ALA B N     1 
ATOM   6851 C  CA    . ALA B 1 334 ? 62.041  10.040  42.862  1.00 89.83  ? 361 ALA B CA    1 
ATOM   6852 C  C     . ALA B 1 334 ? 62.398  8.600   43.199  1.00 96.57  ? 361 ALA B C     1 
ATOM   6853 O  O     . ALA B 1 334 ? 61.747  7.973   44.043  1.00 93.79  ? 361 ALA B O     1 
ATOM   6854 C  CB    . ALA B 1 334 ? 61.274  10.108  41.543  1.00 92.23  ? 361 ALA B CB    1 
ATOM   6855 N  N     . LEU B 1 335 ? 63.425  8.055   42.543  1.00 102.30 ? 362 LEU B N     1 
ATOM   6856 C  CA    . LEU B 1 335 ? 63.852  6.692   42.844  1.00 102.31 ? 362 LEU B CA    1 
ATOM   6857 C  C     . LEU B 1 335 ? 64.397  6.585   44.264  1.00 104.73 ? 362 LEU B C     1 
ATOM   6858 O  O     . LEU B 1 335 ? 64.142  5.596   44.963  1.00 104.51 ? 362 LEU B O     1 
ATOM   6859 C  CB    . LEU B 1 335 ? 64.897  6.235   41.827  1.00 97.06  ? 362 LEU B CB    1 
ATOM   6860 C  CG    . LEU B 1 335 ? 64.373  6.053   40.403  1.00 98.24  ? 362 LEU B CG    1 
ATOM   6861 C  CD1   . LEU B 1 335 ? 65.512  5.774   39.431  1.00 103.68 ? 362 LEU B CD1   1 
ATOM   6862 C  CD2   . LEU B 1 335 ? 63.338  4.937   40.366  1.00 99.21  ? 362 LEU B CD2   1 
ATOM   6863 N  N     . GLN B 1 336 ? 65.144  7.598   44.708  1.00 101.73 ? 363 GLN B N     1 
ATOM   6864 C  CA    . GLN B 1 336 ? 65.639  7.619   46.080  1.00 94.69  ? 363 GLN B CA    1 
ATOM   6865 C  C     . GLN B 1 336 ? 64.489  7.622   47.080  1.00 95.24  ? 363 GLN B C     1 
ATOM   6866 O  O     . GLN B 1 336 ? 64.504  6.870   48.061  1.00 98.31  ? 363 GLN B O     1 
ATOM   6867 C  CB    . GLN B 1 336 ? 66.535  8.841   46.285  1.00 99.11  ? 363 GLN B CB    1 
ATOM   6868 C  CG    . GLN B 1 336 ? 66.763  9.228   47.733  1.00 112.63 ? 363 GLN B CG    1 
ATOM   6869 C  CD    . GLN B 1 336 ? 67.446  10.575  47.869  1.00 117.33 ? 363 GLN B CD    1 
ATOM   6870 O  OE1   . GLN B 1 336 ? 66.997  11.574  47.302  1.00 109.44 ? 363 GLN B OE1   1 
ATOM   6871 N  NE2   . GLN B 1 336 ? 68.550  10.605  48.608  1.00 117.81 ? 363 GLN B NE2   1 
ATOM   6872 N  N     . ALA B 1 337 ? 63.475  8.459   46.838  1.00 95.13  ? 364 ALA B N     1 
ATOM   6873 C  CA    . ALA B 1 337 ? 62.347  8.554   47.759  1.00 89.81  ? 364 ALA B CA    1 
ATOM   6874 C  C     . ALA B 1 337 ? 61.571  7.246   47.842  1.00 95.44  ? 364 ALA B C     1 
ATOM   6875 O  O     . ALA B 1 337 ? 61.024  6.919   48.902  1.00 92.12  ? 364 ALA B O     1 
ATOM   6876 C  CB    . ALA B 1 337 ? 61.421  9.696   47.337  1.00 76.36  ? 364 ALA B CB    1 
ATOM   6877 N  N     . GLN B 1 338 ? 61.504  6.493   46.746  1.00 98.15  ? 365 GLN B N     1 
ATOM   6878 C  CA    . GLN B 1 338 ? 60.833  5.200   46.724  1.00 79.23  ? 365 GLN B CA    1 
ATOM   6879 C  C     . GLN B 1 338 ? 61.747  4.061   47.146  1.00 92.58  ? 365 GLN B C     1 
ATOM   6880 O  O     . GLN B 1 338 ? 61.338  2.898   47.068  1.00 103.84 ? 365 GLN B O     1 
ATOM   6881 C  CB    . GLN B 1 338 ? 60.271  4.922   45.328  1.00 91.11  ? 365 GLN B CB    1 
ATOM   6882 C  CG    . GLN B 1 338 ? 59.166  5.880   44.909  1.00 91.10  ? 365 GLN B CG    1 
ATOM   6883 C  CD    . GLN B 1 338 ? 58.721  5.665   43.477  1.00 94.46  ? 365 GLN B CD    1 
ATOM   6884 O  OE1   . GLN B 1 338 ? 57.591  5.244   43.222  1.00 100.46 ? 365 GLN B OE1   1 
ATOM   6885 N  NE2   . GLN B 1 338 ? 59.609  5.957   42.530  1.00 81.21  ? 365 GLN B NE2   1 
ATOM   6886 N  N     . GLU B 1 339 ? 62.966  4.372   47.594  1.00 99.70  ? 366 GLU B N     1 
ATOM   6887 C  CA    . GLU B 1 339 ? 63.962  3.377   47.991  1.00 97.33  ? 366 GLU B CA    1 
ATOM   6888 C  C     . GLU B 1 339 ? 64.231  2.392   46.853  1.00 92.10  ? 366 GLU B C     1 
ATOM   6889 O  O     . GLU B 1 339 ? 64.075  1.177   46.987  1.00 98.00  ? 366 GLU B O     1 
ATOM   6890 C  CB    . GLU B 1 339 ? 63.533  2.649   49.269  1.00 96.51  ? 366 GLU B CB    1 
ATOM   6891 C  CG    . GLU B 1 339 ? 63.460  3.549   50.490  1.00 100.56 ? 366 GLU B CG    1 
ATOM   6892 C  CD    . GLU B 1 339 ? 63.198  2.774   51.762  1.00 118.25 ? 366 GLU B CD    1 
ATOM   6893 O  OE1   . GLU B 1 339 ? 62.144  2.111   51.848  1.00 131.84 ? 366 GLU B OE1   1 
ATOM   6894 O  OE2   . GLU B 1 339 ? 64.055  2.814   52.670  1.00 125.95 ? 366 GLU B OE2   1 
ATOM   6895 N  N     . ILE B 1 340 ? 64.636  2.951   45.714  1.00 100.93 ? 367 ILE B N     1 
ATOM   6896 C  CA    . ILE B 1 340 ? 64.953  2.188   44.513  1.00 107.15 ? 367 ILE B CA    1 
ATOM   6897 C  C     . ILE B 1 340 ? 66.294  2.677   43.984  1.00 106.22 ? 367 ILE B C     1 
ATOM   6898 O  O     . ILE B 1 340 ? 66.514  3.888   43.862  1.00 99.85  ? 367 ILE B O     1 
ATOM   6899 C  CB    . ILE B 1 340 ? 63.858  2.327   43.436  1.00 97.96  ? 367 ILE B CB    1 
ATOM   6900 C  CG1   . ILE B 1 340 ? 62.495  1.908   43.996  1.00 94.46  ? 367 ILE B CG1   1 
ATOM   6901 C  CG2   . ILE B 1 340 ? 64.208  1.500   42.208  1.00 93.34  ? 367 ILE B CG2   1 
ATOM   6902 C  CD1   . ILE B 1 340 ? 61.345  2.100   43.033  1.00 95.41  ? 367 ILE B CD1   1 
ATOM   6903 N  N     . GLU B 1 341 ? 67.189  1.740   43.680  1.00 104.63 ? 368 GLU B N     1 
ATOM   6904 C  CA    . GLU B 1 341 ? 68.525  2.041   43.191  1.00 113.01 ? 368 GLU B CA    1 
ATOM   6905 C  C     . GLU B 1 341 ? 68.614  1.710   41.705  1.00 119.29 ? 368 GLU B C     1 
ATOM   6906 O  O     . GLU B 1 341 ? 67.996  0.753   41.230  1.00 114.33 ? 368 GLU B O     1 
ATOM   6907 C  CB    . GLU B 1 341 ? 69.580  1.254   43.975  1.00 115.08 ? 368 GLU B CB    1 
ATOM   6908 C  CG    . GLU B 1 341 ? 70.988  1.818   43.889  1.00 129.18 ? 368 GLU B CG    1 
ATOM   6909 C  CD    . GLU B 1 341 ? 71.972  1.041   44.747  1.00 139.85 ? 368 GLU B CD    1 
ATOM   6910 O  OE1   . GLU B 1 341 ? 71.537  0.101   45.448  1.00 128.51 ? 368 GLU B OE1   1 
ATOM   6911 O  OE2   . GLU B 1 341 ? 73.178  1.369   44.720  1.00 147.84 ? 368 GLU B OE2   1 
ATOM   6912 N  N     . CYS B 1 342 ? 69.387  2.511   40.970  1.00 126.09 ? 369 CYS B N     1 
ATOM   6913 C  CA    . CYS B 1 342 ? 69.451  2.382   39.522  1.00 127.37 ? 369 CYS B CA    1 
ATOM   6914 C  C     . CYS B 1 342 ? 70.893  2.467   39.042  1.00 125.53 ? 369 CYS B C     1 
ATOM   6915 O  O     . CYS B 1 342 ? 71.766  3.025   39.710  1.00 143.47 ? 369 CYS B O     1 
ATOM   6916 C  CB    . CYS B 1 342 ? 68.612  3.464   38.816  1.00 127.75 ? 369 CYS B CB    1 
ATOM   6917 S  SG    . CYS B 1 342 ? 69.391  5.114   38.728  1.00 104.23 ? 369 CYS B SG    1 
ATOM   6918 N  N     . ARG B 1 343 ? 71.129  1.894   37.865  1.00 112.31 ? 370 ARG B N     1 
ATOM   6919 C  CA    . ARG B 1 343 ? 72.351  2.121   37.106  1.00 110.04 ? 370 ARG B CA    1 
ATOM   6920 C  C     . ARG B 1 343 ? 72.035  3.129   36.007  1.00 115.62 ? 370 ARG B C     1 
ATOM   6921 O  O     . ARG B 1 343 ? 71.156  2.888   35.172  1.00 109.47 ? 370 ARG B O     1 
ATOM   6922 C  CB    . ARG B 1 343 ? 72.890  0.822   36.506  1.00 108.88 ? 370 ARG B CB    1 
ATOM   6923 C  CG    . ARG B 1 343 ? 74.195  0.993   35.743  1.00 98.78  ? 370 ARG B CG    1 
ATOM   6924 C  CD    . ARG B 1 343 ? 74.674  -0.315  35.131  1.00 118.43 ? 370 ARG B CD    1 
ATOM   6925 N  NE    . ARG B 1 343 ? 76.024  -0.196  34.592  1.00 131.85 ? 370 ARG B NE    1 
ATOM   6926 C  CZ    . ARG B 1 343 ? 76.309  0.081   33.326  1.00 135.88 ? 370 ARG B CZ    1 
ATOM   6927 N  NH1   . ARG B 1 343 ? 75.356  0.258   32.426  1.00 135.02 ? 370 ARG B NH1   1 
ATOM   6928 N  NH2   . ARG B 1 343 ? 77.582  0.184   32.955  1.00 139.55 ? 370 ARG B NH2   1 
ATOM   6929 N  N     . LEU B 1 344 ? 72.734  4.259   36.020  1.00 103.46 ? 371 LEU B N     1 
ATOM   6930 C  CA    . LEU B 1 344 ? 72.497  5.303   35.033  1.00 102.68 ? 371 LEU B CA    1 
ATOM   6931 C  C     . LEU B 1 344 ? 73.148  4.906   33.713  1.00 106.05 ? 371 LEU B C     1 
ATOM   6932 O  O     . LEU B 1 344 ? 74.355  4.643   33.663  1.00 112.14 ? 371 LEU B O     1 
ATOM   6933 C  CB    . LEU B 1 344 ? 73.043  6.638   35.532  1.00 109.01 ? 371 LEU B CB    1 
ATOM   6934 C  CG    . LEU B 1 344 ? 72.508  7.888   34.837  1.00 111.46 ? 371 LEU B CG    1 
ATOM   6935 C  CD1   . LEU B 1 344 ? 71.026  8.058   35.131  1.00 115.95 ? 371 LEU B CD1   1 
ATOM   6936 C  CD2   . LEU B 1 344 ? 73.290  9.117   35.272  1.00 114.80 ? 371 LEU B CD2   1 
ATOM   6937 N  N     . VAL B 1 345 ? 72.351  4.851   32.650  1.00 103.38 ? 372 VAL B N     1 
ATOM   6938 C  CA    . VAL B 1 345 ? 72.834  4.520   31.314  1.00 112.31 ? 372 VAL B CA    1 
ATOM   6939 C  C     . VAL B 1 345 ? 72.816  5.793   30.479  1.00 116.82 ? 372 VAL B C     1 
ATOM   6940 O  O     . VAL B 1 345 ? 71.769  6.439   30.339  1.00 112.18 ? 372 VAL B O     1 
ATOM   6941 C  CB    . VAL B 1 345 ? 71.988  3.416   30.659  1.00 102.60 ? 372 VAL B CB    1 
ATOM   6942 C  CG1   . VAL B 1 345 ? 72.475  3.141   29.245  1.00 92.37  ? 372 VAL B CG1   1 
ATOM   6943 C  CG2   . VAL B 1 345 ? 72.036  2.148   31.493  1.00 100.37 ? 372 VAL B CG2   1 
ATOM   6944 N  N     . GLU B 1 346 ? 73.973  6.156   29.931  1.00 115.83 ? 373 GLU B N     1 
ATOM   6945 C  CA    . GLU B 1 346 ? 74.075  7.348   29.099  1.00 104.20 ? 373 GLU B CA    1 
ATOM   6946 C  C     . GLU B 1 346 ? 73.347  7.124   27.780  1.00 101.25 ? 373 GLU B C     1 
ATOM   6947 O  O     . GLU B 1 346 ? 73.641  6.167   27.057  1.00 115.48 ? 373 GLU B O     1 
ATOM   6948 C  CB    . GLU B 1 346 ? 75.541  7.696   28.855  1.00 115.82 ? 373 GLU B CB    1 
ATOM   6949 C  CG    . GLU B 1 346 ? 76.268  8.214   30.091  1.00 130.94 ? 373 GLU B CG    1 
ATOM   6950 C  CD    . GLU B 1 346 ? 76.800  9.623   29.902  1.00 143.43 ? 373 GLU B CD    1 
ATOM   6951 O  OE1   . GLU B 1 346 ? 76.968  10.043  28.737  1.00 149.55 ? 373 GLU B OE1   1 
ATOM   6952 O  OE2   . GLU B 1 346 ? 77.044  10.313  30.916  1.00 143.56 ? 373 GLU B OE2   1 
ATOM   6953 N  N     . ALA B 1 347 ? 72.400  8.004   27.468  1.00 106.17 ? 374 ALA B N     1 
ATOM   6954 C  CA    . ALA B 1 347 ? 71.603  7.852   26.259  1.00 107.14 ? 374 ALA B CA    1 
ATOM   6955 C  C     . ALA B 1 347 ? 72.421  8.202   25.022  1.00 105.22 ? 374 ALA B C     1 
ATOM   6956 O  O     . ALA B 1 347 ? 73.260  9.107   25.046  1.00 110.90 ? 374 ALA B O     1 
ATOM   6957 C  CB    . ALA B 1 347 ? 70.357  8.733   26.330  1.00 100.09 ? 374 ALA B CB    1 
ATOM   6958 N  N     . VAL B 1 348 ? 72.169  7.475   23.936  1.00 105.85 ? 375 VAL B N     1 
ATOM   6959 C  CA    . VAL B 1 348 ? 72.847  7.724   22.667  1.00 114.85 ? 375 VAL B CA    1 
ATOM   6960 C  C     . VAL B 1 348 ? 72.258  8.992   22.054  1.00 117.98 ? 375 VAL B C     1 
ATOM   6961 O  O     . VAL B 1 348 ? 71.085  9.021   21.673  1.00 114.20 ? 375 VAL B O     1 
ATOM   6962 C  CB    . VAL B 1 348 ? 72.716  6.531   21.714  1.00 110.23 ? 375 VAL B CB    1 
ATOM   6963 C  CG1   . VAL B 1 348 ? 73.220  6.898   20.329  1.00 109.13 ? 375 VAL B CG1   1 
ATOM   6964 C  CG2   . VAL B 1 348 ? 73.477  5.329   22.255  1.00 110.42 ? 375 VAL B CG2   1 
ATOM   6965 N  N     . ASP B 1 349 ? 73.070  10.041  21.959  1.00 115.63 ? 376 ASP B N     1 
ATOM   6966 C  CA    . ASP B 1 349 ? 72.638  11.295  21.346  1.00 125.00 ? 376 ASP B CA    1 
ATOM   6967 C  C     . ASP B 1 349 ? 72.537  11.084  19.841  1.00 136.43 ? 376 ASP B C     1 
ATOM   6968 O  O     . ASP B 1 349 ? 73.546  11.084  19.131  1.00 127.60 ? 376 ASP B O     1 
ATOM   6969 C  CB    . ASP B 1 349 ? 73.610  12.419  21.689  1.00 128.73 ? 376 ASP B CB    1 
ATOM   6970 C  CG    . ASP B 1 349 ? 72.979  13.796  21.565  1.00 135.86 ? 376 ASP B CG    1 
ATOM   6971 O  OD1   . ASP B 1 349 ? 72.133  13.991  20.666  1.00 135.94 ? 376 ASP B OD1   1 
ATOM   6972 O  OD2   . ASP B 1 349 ? 73.326  14.682  22.375  1.00 138.31 ? 376 ASP B OD2   1 
ATOM   6973 N  N     . GLY B 1 350 ? 71.308  10.905  19.348  1.00 143.39 ? 377 GLY B N     1 
ATOM   6974 C  CA    . GLY B 1 350 ? 71.119  10.576  17.946  1.00 150.24 ? 377 GLY B CA    1 
ATOM   6975 C  C     . GLY B 1 350 ? 71.489  11.696  16.995  1.00 159.36 ? 377 GLY B C     1 
ATOM   6976 O  O     . GLY B 1 350 ? 71.883  11.438  15.853  1.00 159.21 ? 377 GLY B O     1 
ATOM   6977 N  N     . LYS B 1 351 ? 71.370  12.947  17.440  1.00 149.20 ? 378 LYS B N     1 
ATOM   6978 C  CA    . LYS B 1 351 ? 71.690  14.080  16.580  1.00 150.92 ? 378 LYS B CA    1 
ATOM   6979 C  C     . LYS B 1 351 ? 73.190  14.309  16.441  1.00 144.17 ? 378 LYS B C     1 
ATOM   6980 O  O     . LYS B 1 351 ? 73.622  14.893  15.443  1.00 139.24 ? 378 LYS B O     1 
ATOM   6981 C  CB    . LYS B 1 351 ? 71.025  15.356  17.107  1.00 149.60 ? 378 LYS B CB    1 
ATOM   6982 C  CG    . LYS B 1 351 ? 69.542  15.502  16.765  1.00 141.30 ? 378 LYS B CG    1 
ATOM   6983 C  CD    . LYS B 1 351 ? 68.666  14.569  17.591  1.00 140.14 ? 378 LYS B CD    1 
ATOM   6984 C  CE    . LYS B 1 351 ? 67.189  14.796  17.310  1.00 134.18 ? 378 LYS B CE    1 
ATOM   6985 N  NZ    . LYS B 1 351 ? 66.752  16.162  17.709  1.00 117.95 ? 378 LYS B NZ    1 
ATOM   6986 N  N     . ALA B 1 352 ? 73.990  13.860  17.406  1.00 149.55 ? 379 ALA B N     1 
ATOM   6987 C  CA    . ALA B 1 352 ? 75.434  14.057  17.364  1.00 152.71 ? 379 ALA B CA    1 
ATOM   6988 C  C     . ALA B 1 352 ? 76.153  13.043  16.482  1.00 155.32 ? 379 ALA B C     1 
ATOM   6989 O  O     . ALA B 1 352 ? 77.388  13.051  16.440  1.00 155.29 ? 379 ALA B O     1 
ATOM   6990 C  CB    . ALA B 1 352 ? 76.012  14.008  18.781  1.00 148.69 ? 379 ALA B CB    1 
ATOM   6991 N  N     . MET B 1 353 ? 75.424  12.180  15.779  1.00 155.25 ? 380 MET B N     1 
ATOM   6992 C  CA    . MET B 1 353 ? 76.019  11.160  14.925  1.00 150.30 ? 380 MET B CA    1 
ATOM   6993 C  C     . MET B 1 353 ? 75.941  11.612  13.473  1.00 158.78 ? 380 MET B C     1 
ATOM   6994 O  O     . MET B 1 353 ? 74.844  11.797  12.935  1.00 157.10 ? 380 MET B O     1 
ATOM   6995 C  CB    . MET B 1 353 ? 75.308  9.817   15.097  1.00 143.29 ? 380 MET B CB    1 
ATOM   6996 C  CG    . MET B 1 353 ? 75.374  9.233   16.497  1.00 143.70 ? 380 MET B CG    1 
ATOM   6997 S  SD    . MET B 1 353 ? 74.336  7.765   16.673  1.00 147.39 ? 380 MET B SD    1 
ATOM   6998 C  CE    . MET B 1 353 ? 75.034  6.696   15.415  1.00 141.56 ? 380 MET B CE    1 
ATOM   6999 N  N     . ASN B 1 354 ? 77.099  11.786  12.842  1.00 169.51 ? 381 ASN B N     1 
ATOM   7000 C  CA    . ASN B 1 354 ? 77.120  12.073  11.418  1.00 178.31 ? 381 ASN B CA    1 
ATOM   7001 C  C     . ASN B 1 354 ? 76.763  10.815  10.623  1.00 179.80 ? 381 ASN B C     1 
ATOM   7002 O  O     . ASN B 1 354 ? 76.570  9.728   11.177  1.00 170.08 ? 381 ASN B O     1 
ATOM   7003 C  CB    . ASN B 1 354 ? 78.485  12.619  10.997  1.00 174.44 ? 381 ASN B CB    1 
ATOM   7004 C  CG    . ASN B 1 354 ? 79.636  11.849  11.611  1.00 174.36 ? 381 ASN B CG    1 
ATOM   7005 O  OD1   . ASN B 1 354 ? 79.863  10.684  11.284  1.00 179.15 ? 381 ASN B OD1   1 
ATOM   7006 N  ND2   . ASN B 1 354 ? 80.376  12.499  12.501  1.00 174.81 ? 381 ASN B ND2   1 
ATOM   7007 N  N     . THR B 1 355 ? 76.676  10.975  9.300   1.00 182.05 ? 382 THR B N     1 
ATOM   7008 C  CA    . THR B 1 355 ? 76.243  9.869   8.450   1.00 176.83 ? 382 THR B CA    1 
ATOM   7009 C  C     . THR B 1 355 ? 77.257  8.732   8.430   1.00 175.11 ? 382 THR B C     1 
ATOM   7010 O  O     . THR B 1 355 ? 76.887  7.578   8.187   1.00 170.86 ? 382 THR B O     1 
ATOM   7011 C  CB    . THR B 1 355 ? 75.990  10.363  7.027   1.00 171.50 ? 382 THR B CB    1 
ATOM   7012 O  OG1   . THR B 1 355 ? 77.215  10.855  6.471   1.00 177.17 ? 382 THR B OG1   1 
ATOM   7013 C  CG2   . THR B 1 355 ? 74.958  11.476  7.027   1.00 172.39 ? 382 THR B CG2   1 
ATOM   7014 N  N     . SER B 1 356 ? 78.533  9.034   8.674   1.00 177.14 ? 383 SER B N     1 
ATOM   7015 C  CA    . SER B 1 356 ? 79.551  7.988   8.685   1.00 174.25 ? 383 SER B CA    1 
ATOM   7016 C  C     . SER B 1 356 ? 79.360  7.046   9.867   1.00 179.03 ? 383 SER B C     1 
ATOM   7017 O  O     . SER B 1 356 ? 79.405  5.820   9.710   1.00 176.21 ? 383 SER B O     1 
ATOM   7018 C  CB    . SER B 1 356 ? 80.947  8.612   8.712   1.00 166.91 ? 383 SER B CB    1 
ATOM   7019 O  OG    . SER B 1 356 ? 81.173  9.303   9.928   1.00 164.68 ? 383 SER B OG    1 
ATOM   7020 N  N     . GLN B 1 357 ? 79.150  7.600   11.064  1.00 178.43 ? 384 GLN B N     1 
ATOM   7021 C  CA    . GLN B 1 357 ? 78.993  6.754   12.242  1.00 169.23 ? 384 GLN B CA    1 
ATOM   7022 C  C     . GLN B 1 357 ? 77.698  5.952   12.186  1.00 163.67 ? 384 GLN B C     1 
ATOM   7023 O  O     . GLN B 1 357 ? 77.594  4.894   12.817  1.00 160.62 ? 384 GLN B O     1 
ATOM   7024 C  CB    . GLN B 1 357 ? 79.048  7.613   13.504  1.00 172.36 ? 384 GLN B CB    1 
ATOM   7025 C  CG    . GLN B 1 357 ? 80.321  8.438   13.625  1.00 171.82 ? 384 GLN B CG    1 
ATOM   7026 C  CD    . GLN B 1 357 ? 80.137  9.683   14.467  1.00 176.47 ? 384 GLN B CD    1 
ATOM   7027 O  OE1   . GLN B 1 357 ? 79.026  9.999   14.893  1.00 169.97 ? 384 GLN B OE1   1 
ATOM   7028 N  NE2   . GLN B 1 357 ? 81.230  10.399  14.711  1.00 178.33 ? 384 GLN B NE2   1 
ATOM   7029 N  N     . VAL B 1 358 ? 76.706  6.432   11.433  1.00 152.89 ? 385 VAL B N     1 
ATOM   7030 C  CA    . VAL B 1 358 ? 75.478  5.670   11.241  1.00 147.36 ? 385 VAL B CA    1 
ATOM   7031 C  C     . VAL B 1 358 ? 75.755  4.417   10.415  1.00 154.79 ? 385 VAL B C     1 
ATOM   7032 O  O     . VAL B 1 358 ? 75.285  3.322   10.746  1.00 152.35 ? 385 VAL B O     1 
ATOM   7033 C  CB    . VAL B 1 358 ? 74.402  6.563   10.595  1.00 135.18 ? 385 VAL B CB    1 
ATOM   7034 C  CG1   . VAL B 1 358 ? 73.154  5.754   10.285  1.00 130.86 ? 385 VAL B CG1   1 
ATOM   7035 C  CG2   . VAL B 1 358 ? 74.066  7.729   11.508  1.00 121.11 ? 385 VAL B CG2   1 
ATOM   7036 N  N     . GLU B 1 359 ? 76.528  4.552   9.333   1.00 162.90 ? 386 GLU B N     1 
ATOM   7037 C  CA    . GLU B 1 359 ? 76.856  3.389   8.514   1.00 161.76 ? 386 GLU B CA    1 
ATOM   7038 C  C     . GLU B 1 359 ? 77.796  2.432   9.237   1.00 166.09 ? 386 GLU B C     1 
ATOM   7039 O  O     . GLU B 1 359 ? 77.786  1.228   8.957   1.00 168.56 ? 386 GLU B O     1 
ATOM   7040 C  CB    . GLU B 1 359 ? 77.481  3.832   7.191   1.00 167.00 ? 386 GLU B CB    1 
ATOM   7041 C  CG    . GLU B 1 359 ? 76.623  4.782   6.371   1.00 168.63 ? 386 GLU B CG    1 
ATOM   7042 C  CD    . GLU B 1 359 ? 77.283  5.168   5.060   1.00 175.09 ? 386 GLU B CD    1 
ATOM   7043 O  OE1   . GLU B 1 359 ? 78.266  4.503   4.668   1.00 166.83 ? 386 GLU B OE1   1 
ATOM   7044 O  OE2   . GLU B 1 359 ? 76.822  6.137   4.421   1.00 184.40 ? 386 GLU B OE2   1 
ATOM   7045 N  N     . ALA B 1 360 ? 78.607  2.942   10.168  1.00 172.24 ? 387 ALA B N     1 
ATOM   7046 C  CA    . ALA B 1 360 ? 79.601  2.125   10.858  1.00 168.95 ? 387 ALA B CA    1 
ATOM   7047 C  C     . ALA B 1 360 ? 78.987  1.044   11.739  1.00 168.38 ? 387 ALA B C     1 
ATOM   7048 O  O     . ALA B 1 360 ? 79.723  0.182   12.231  1.00 165.74 ? 387 ALA B O     1 
ATOM   7049 C  CB    . ALA B 1 360 ? 80.517  3.017   11.699  1.00 165.30 ? 387 ALA B CB    1 
ATOM   7050 N  N     . LEU B 1 361 ? 77.670  1.066   11.954  1.00 164.37 ? 388 LEU B N     1 
ATOM   7051 C  CA    . LEU B 1 361 ? 76.986  0.045   12.738  1.00 162.38 ? 388 LEU B CA    1 
ATOM   7052 C  C     . LEU B 1 361 ? 75.932  -0.688  11.917  1.00 160.29 ? 388 LEU B C     1 
ATOM   7053 O  O     . LEU B 1 361 ? 75.066  -1.361  12.485  1.00 156.01 ? 388 LEU B O     1 
ATOM   7054 C  CB    . LEU B 1 361 ? 76.356  0.664   13.987  1.00 155.14 ? 388 LEU B CB    1 
ATOM   7055 C  CG    . LEU B 1 361 ? 77.331  1.408   14.903  1.00 146.63 ? 388 LEU B CG    1 
ATOM   7056 C  CD1   . LEU B 1 361 ? 76.599  1.987   16.098  1.00 132.47 ? 388 LEU B CD1   1 
ATOM   7057 C  CD2   . LEU B 1 361 ? 78.454  0.485   15.348  1.00 147.54 ? 388 LEU B CD2   1 
ATOM   7058 N  N     . GLY B 1 362 ? 75.990  -0.573  10.594  1.00 145.17 ? 389 GLY B N     1 
ATOM   7059 C  CA    . GLY B 1 362 ? 75.024  -1.243  9.739   1.00 140.34 ? 389 GLY B CA    1 
ATOM   7060 C  C     . GLY B 1 362 ? 73.607  -0.750  9.923   1.00 148.63 ? 389 GLY B C     1 
ATOM   7061 O  O     . GLY B 1 362 ? 72.660  -1.542  9.842   1.00 151.83 ? 389 GLY B O     1 
ATOM   7062 N  N     . ILE B 1 363 ? 73.439  0.544   10.166  1.00 156.01 ? 390 ILE B N     1 
ATOM   7063 C  CA    . ILE B 1 363 ? 72.132  1.117   10.460  1.00 162.02 ? 390 ILE B CA    1 
ATOM   7064 C  C     . ILE B 1 363 ? 71.449  1.490   9.150   1.00 155.50 ? 390 ILE B C     1 
ATOM   7065 O  O     . ILE B 1 363 ? 71.986  2.270   8.356   1.00 148.91 ? 390 ILE B O     1 
ATOM   7066 C  CB    . ILE B 1 363 ? 72.258  2.333   11.388  1.00 155.80 ? 390 ILE B CB    1 
ATOM   7067 C  CG1   . ILE B 1 363 ? 72.802  1.907   12.756  1.00 144.59 ? 390 ILE B CG1   1 
ATOM   7068 C  CG2   . ILE B 1 363 ? 70.912  3.031   11.535  1.00 149.79 ? 390 ILE B CG2   1 
ATOM   7069 C  CD1   . ILE B 1 363 ? 72.967  3.049   13.729  1.00 141.30 ? 390 ILE B CD1   1 
ATOM   7070 N  N     . GLN B 1 364 ? 70.263  0.926   8.927   1.00 148.98 ? 391 GLN B N     1 
ATOM   7071 C  CA    . GLN B 1 364 ? 69.450  1.205   7.750   1.00 143.28 ? 391 GLN B CA    1 
ATOM   7072 C  C     . GLN B 1 364 ? 67.987  1.185   8.160   1.00 145.55 ? 391 GLN B C     1 
ATOM   7073 O  O     . GLN B 1 364 ? 67.537  0.227   8.796   1.00 154.28 ? 391 GLN B O     1 
ATOM   7074 C  CB    . GLN B 1 364 ? 69.696  0.174   6.642   1.00 148.90 ? 391 GLN B CB    1 
ATOM   7075 C  CG    . GLN B 1 364 ? 71.110  0.152   6.092   1.00 147.58 ? 391 GLN B CG    1 
ATOM   7076 C  CD    . GLN B 1 364 ? 71.455  -1.175  5.448   1.00 151.60 ? 391 GLN B CD    1 
ATOM   7077 O  OE1   . GLN B 1 364 ? 70.799  -2.187  5.696   1.00 153.00 ? 391 GLN B OE1   1 
ATOM   7078 N  NE2   . GLN B 1 364 ? 72.489  -1.178  4.615   1.00 144.23 ? 391 GLN B NE2   1 
ATOM   7079 N  N     . MET B 1 365 ? 67.250  2.234   7.800   1.00 138.62 ? 392 MET B N     1 
ATOM   7080 C  CA    . MET B 1 365 ? 65.834  2.301   8.139   1.00 146.04 ? 392 MET B CA    1 
ATOM   7081 C  C     . MET B 1 365 ? 65.066  1.178   7.449   1.00 156.25 ? 392 MET B C     1 
ATOM   7082 O  O     . MET B 1 365 ? 65.463  0.679   6.392   1.00 153.58 ? 392 MET B O     1 
ATOM   7083 C  CB    . MET B 1 365 ? 65.249  3.660   7.740   1.00 136.66 ? 392 MET B CB    1 
ATOM   7084 C  CG    . MET B 1 365 ? 63.840  3.916   8.265   1.00 142.41 ? 392 MET B CG    1 
ATOM   7085 S  SD    . MET B 1 365 ? 62.973  5.244   7.405   1.00 142.22 ? 392 MET B SD    1 
ATOM   7086 C  CE    . MET B 1 365 ? 62.864  4.573   5.748   1.00 148.72 ? 392 MET B CE    1 
ATOM   7087 N  N     . LEU B 1 366 ? 63.962  0.772   8.068   1.00 169.72 ? 393 LEU B N     1 
ATOM   7088 C  CA    . LEU B 1 366 ? 63.101  -0.235  7.468   1.00 178.65 ? 393 LEU B CA    1 
ATOM   7089 C  C     . LEU B 1 366 ? 62.535  0.295   6.154   1.00 191.69 ? 393 LEU B C     1 
ATOM   7090 O  O     . LEU B 1 366 ? 61.950  1.388   6.133   1.00 190.89 ? 393 LEU B O     1 
ATOM   7091 C  CB    . LEU B 1 366 ? 61.972  -0.609  8.428   1.00 178.49 ? 393 LEU B CB    1 
ATOM   7092 C  CG    . LEU B 1 366 ? 61.027  -1.736  8.002   1.00 186.89 ? 393 LEU B CG    1 
ATOM   7093 C  CD1   . LEU B 1 366 ? 60.675  -2.604  9.197   1.00 178.54 ? 393 LEU B CD1   1 
ATOM   7094 C  CD2   . LEU B 1 366 ? 59.764  -1.175  7.366   1.00 196.34 ? 393 LEU B CD2   1 
ATOM   7095 N  N     . PRO B 1 367 ? 62.697  -0.431  5.041   1.00 195.89 ? 394 PRO B N     1 
ATOM   7096 C  CA    . PRO B 1 367 ? 62.204  0.067   3.748   1.00 192.04 ? 394 PRO B CA    1 
ATOM   7097 C  C     . PRO B 1 367 ? 60.703  0.308   3.732   1.00 197.24 ? 394 PRO B C     1 
ATOM   7098 O  O     . PRO B 1 367 ? 59.908  -0.634  3.802   1.00 196.47 ? 394 PRO B O     1 
ATOM   7099 C  CB    . PRO B 1 367 ? 62.602  -1.048  2.771   1.00 193.68 ? 394 PRO B CB    1 
ATOM   7100 C  CG    . PRO B 1 367 ? 63.745  -1.743  3.434   1.00 181.03 ? 394 PRO B CG    1 
ATOM   7101 C  CD    . PRO B 1 367 ? 63.442  -1.694  4.901   1.00 190.66 ? 394 PRO B CD    1 
ATOM   7102 N  N     . GLY B 1 368 ? 60.312  1.573   3.642   1.00 202.88 ? 395 GLY B N     1 
ATOM   7103 C  CA    . GLY B 1 368 ? 58.921  1.947   3.576   1.00 211.26 ? 395 GLY B CA    1 
ATOM   7104 C  C     . GLY B 1 368 ? 58.282  2.358   4.882   1.00 210.23 ? 395 GLY B C     1 
ATOM   7105 O  O     . GLY B 1 368 ? 57.063  2.213   5.023   1.00 212.77 ? 395 GLY B O     1 
ATOM   7106 N  N     . TYR B 1 369 ? 59.055  2.867   5.839   1.00 202.10 ? 396 TYR B N     1 
ATOM   7107 C  CA    . TYR B 1 369 ? 58.492  3.292   7.113   1.00 200.88 ? 396 TYR B CA    1 
ATOM   7108 C  C     . TYR B 1 369 ? 57.966  4.718   7.022   1.00 204.46 ? 396 TYR B C     1 
ATOM   7109 O  O     . TYR B 1 369 ? 58.626  5.606   6.474   1.00 198.95 ? 396 TYR B O     1 
ATOM   7110 C  CB    . TYR B 1 369 ? 59.531  3.199   8.230   1.00 193.58 ? 396 TYR B CB    1 
ATOM   7111 C  CG    . TYR B 1 369 ? 59.057  3.837   9.517   1.00 191.50 ? 396 TYR B CG    1 
ATOM   7112 C  CD1   . TYR B 1 369 ? 57.921  3.368   10.163  1.00 192.98 ? 396 TYR B CD1   1 
ATOM   7113 C  CD2   . TYR B 1 369 ? 59.733  4.913   10.079  1.00 182.34 ? 396 TYR B CD2   1 
ATOM   7114 C  CE1   . TYR B 1 369 ? 57.474  3.943   11.335  1.00 183.91 ? 396 TYR B CE1   1 
ATOM   7115 C  CE2   . TYR B 1 369 ? 59.292  5.498   11.254  1.00 186.17 ? 396 TYR B CE2   1 
ATOM   7116 C  CZ    . TYR B 1 369 ? 58.160  5.007   11.877  1.00 183.91 ? 396 TYR B CZ    1 
ATOM   7117 O  OH    . TYR B 1 369 ? 57.710  5.579   13.045  1.00 177.81 ? 396 TYR B OH    1 
ATOM   7118 N  N     . ARG B 1 370 ? 56.770  4.934   7.567   1.00 203.96 ? 397 ARG B N     1 
ATOM   7119 C  CA    . ARG B 1 370 ? 56.151  6.250   7.593   1.00 205.98 ? 397 ARG B CA    1 
ATOM   7120 C  C     . ARG B 1 370 ? 55.492  6.468   8.947   1.00 204.33 ? 397 ARG B C     1 
ATOM   7121 O  O     . ARG B 1 370 ? 54.865  5.555   9.494   1.00 200.34 ? 397 ARG B O     1 
ATOM   7122 C  CB    . ARG B 1 370 ? 55.124  6.413   6.462   1.00 204.68 ? 397 ARG B CB    1 
ATOM   7123 C  CG    . ARG B 1 370 ? 55.752  6.486   5.077   1.00 193.61 ? 397 ARG B CG    1 
ATOM   7124 C  CD    . ARG B 1 370 ? 54.723  6.757   3.993   1.00 186.65 ? 397 ARG B CD    1 
ATOM   7125 N  NE    . ARG B 1 370 ? 55.355  6.974   2.697   1.00 185.70 ? 397 ARG B NE    1 
ATOM   7126 C  CZ    . ARG B 1 370 ? 54.702  7.276   1.583   1.00 187.91 ? 397 ARG B CZ    1 
ATOM   7127 N  NH1   . ARG B 1 370 ? 53.385  7.398   1.566   1.00 185.97 ? 397 ARG B NH1   1 
ATOM   7128 N  NH2   . ARG B 1 370 ? 55.387  7.462   0.459   1.00 189.36 ? 397 ARG B NH2   1 
ATOM   7129 N  N     . ASP B 1 371 ? 55.647  7.679   9.477   1.00 218.41 ? 398 ASP B N     1 
ATOM   7130 C  CA    . ASP B 1 371 ? 55.102  8.033   10.779  1.00 217.45 ? 398 ASP B CA    1 
ATOM   7131 C  C     . ASP B 1 371 ? 53.592  7.786   10.804  1.00 219.79 ? 398 ASP B C     1 
ATOM   7132 O  O     . ASP B 1 371 ? 52.891  8.175   9.859   1.00 224.68 ? 398 ASP B O     1 
ATOM   7133 C  CB    . ASP B 1 371 ? 55.412  9.504   11.074  1.00 220.32 ? 398 ASP B CB    1 
ATOM   7134 C  CG    . ASP B 1 371 ? 55.334  9.848   12.550  1.00 220.15 ? 398 ASP B CG    1 
ATOM   7135 O  OD1   . ASP B 1 371 ? 54.420  9.358   13.242  1.00 222.40 ? 398 ASP B OD1   1 
ATOM   7136 O  OD2   . ASP B 1 371 ? 56.192  10.623  13.017  1.00 215.68 ? 398 ASP B OD2   1 
ATOM   7137 N  N     . PRO B 1 372 ? 53.061  7.127   11.838  1.00 201.79 ? 399 PRO B N     1 
ATOM   7138 C  CA    . PRO B 1 372 ? 51.608  6.889   11.885  1.00 197.24 ? 399 PRO B CA    1 
ATOM   7139 C  C     . PRO B 1 372 ? 50.766  8.155   11.893  1.00 201.28 ? 399 PRO B C     1 
ATOM   7140 O  O     . PRO B 1 372 ? 49.573  8.082   11.576  1.00 190.00 ? 399 PRO B O     1 
ATOM   7141 C  CB    . PRO B 1 372 ? 51.426  6.098   13.187  1.00 189.82 ? 399 PRO B CB    1 
ATOM   7142 C  CG    . PRO B 1 372 ? 52.725  5.431   13.402  1.00 185.16 ? 399 PRO B CG    1 
ATOM   7143 C  CD    . PRO B 1 372 ? 53.775  6.374   12.887  1.00 192.84 ? 399 PRO B CD    1 
ATOM   7144 N  N     . TYR B 1 373 ? 51.335  9.308   12.249  1.00 219.91 ? 400 TYR B N     1 
ATOM   7145 C  CA    . TYR B 1 373 ? 50.559  10.535  12.351  1.00 219.79 ? 400 TYR B CA    1 
ATOM   7146 C  C     . TYR B 1 373 ? 51.115  11.683  11.521  1.00 221.46 ? 400 TYR B C     1 
ATOM   7147 O  O     . TYR B 1 373 ? 50.517  12.765  11.516  1.00 219.64 ? 400 TYR B O     1 
ATOM   7148 C  CB    . TYR B 1 373 ? 50.444  10.968  13.821  1.00 215.72 ? 400 TYR B CB    1 
ATOM   7149 C  CG    . TYR B 1 373 ? 49.924  9.869   14.721  1.00 214.77 ? 400 TYR B CG    1 
ATOM   7150 C  CD1   . TYR B 1 373 ? 48.560  9.633   14.848  1.00 210.84 ? 400 TYR B CD1   1 
ATOM   7151 C  CD2   . TYR B 1 373 ? 50.797  9.057   15.432  1.00 209.72 ? 400 TYR B CD2   1 
ATOM   7152 C  CE1   . TYR B 1 373 ? 48.082  8.624   15.664  1.00 207.26 ? 400 TYR B CE1   1 
ATOM   7153 C  CE2   . TYR B 1 373 ? 50.328  8.048   16.250  1.00 208.62 ? 400 TYR B CE2   1 
ATOM   7154 C  CZ    . TYR B 1 373 ? 48.971  7.835   16.363  1.00 207.88 ? 400 TYR B CZ    1 
ATOM   7155 O  OH    . TYR B 1 373 ? 48.504  6.829   17.177  1.00 206.09 ? 400 TYR B OH    1 
ATOM   7156 N  N     . HIS B 1 374 ? 52.233  11.484  10.822  1.00 224.80 ? 401 HIS B N     1 
ATOM   7157 C  CA    . HIS B 1 374 ? 52.751  12.485  9.896   1.00 223.83 ? 401 HIS B CA    1 
ATOM   7158 C  C     . HIS B 1 374 ? 53.397  11.894  8.649   1.00 224.67 ? 401 HIS B C     1 
ATOM   7159 O  O     . HIS B 1 374 ? 53.706  12.656  7.728   1.00 226.53 ? 401 HIS B O     1 
ATOM   7160 C  CB    . HIS B 1 374 ? 53.762  13.403  10.600  1.00 216.24 ? 401 HIS B CB    1 
ATOM   7161 C  CG    . HIS B 1 374 ? 53.140  14.349  11.582  1.00 207.45 ? 401 HIS B CG    1 
ATOM   7162 N  ND1   . HIS B 1 374 ? 52.276  15.354  11.202  1.00 197.09 ? 401 HIS B ND1   1 
ATOM   7163 C  CD2   . HIS B 1 374 ? 53.261  14.448  12.927  1.00 202.89 ? 401 HIS B CD2   1 
ATOM   7164 C  CE1   . HIS B 1 374 ? 51.889  16.028  12.270  1.00 193.20 ? 401 HIS B CE1   1 
ATOM   7165 N  NE2   . HIS B 1 374 ? 52.473  15.499  13.330  1.00 193.57 ? 401 HIS B NE2   1 
ATOM   7166 N  N     . GLY B 1 375 ? 53.615  10.580  8.581   1.00 230.67 ? 402 GLY B N     1 
ATOM   7167 C  CA    . GLY B 1 375 ? 54.118  9.950   7.374   1.00 230.41 ? 402 GLY B CA    1 
ATOM   7168 C  C     . GLY B 1 375 ? 55.586  10.165  7.084   1.00 228.64 ? 402 GLY B C     1 
ATOM   7169 O  O     . GLY B 1 375 ? 56.000  10.050  5.927   1.00 227.88 ? 402 GLY B O     1 
ATOM   7170 N  N     . ARG B 1 376 ? 56.394  10.458  8.106   1.00 219.50 ? 403 ARG B N     1 
ATOM   7171 C  CA    . ARG B 1 376 ? 57.802  10.791  7.964   1.00 206.36 ? 403 ARG B CA    1 
ATOM   7172 C  C     . ARG B 1 376 ? 58.684  9.580   8.246   1.00 199.96 ? 403 ARG B C     1 
ATOM   7173 O  O     . ARG B 1 376 ? 58.296  8.681   8.998   1.00 202.19 ? 403 ARG B O     1 
ATOM   7174 C  CB    . ARG B 1 376 ? 58.179  11.924  8.922   1.00 202.81 ? 403 ARG B CB    1 
ATOM   7175 C  CG    . ARG B 1 376 ? 57.303  13.160  8.791   1.00 204.41 ? 403 ARG B CG    1 
ATOM   7176 C  CD    . ARG B 1 376 ? 57.362  14.032  10.038  1.00 195.15 ? 403 ARG B CD    1 
ATOM   7177 N  NE    . ARG B 1 376 ? 58.712  14.499  10.328  1.00 189.42 ? 403 ARG B NE    1 
ATOM   7178 C  CZ    . ARG B 1 376 ? 59.520  13.947  11.223  1.00 194.87 ? 403 ARG B CZ    1 
ATOM   7179 N  NH1   . ARG B 1 376 ? 59.145  12.901  11.941  1.00 193.35 ? 403 ARG B NH1   1 
ATOM   7180 N  NH2   . ARG B 1 376 ? 60.736  14.457  11.400  1.00 198.21 ? 403 ARG B NH2   1 
ATOM   7181 N  N     . PRO B 1 377 ? 59.880  9.527   7.649   1.00 192.88 ? 404 PRO B N     1 
ATOM   7182 C  CA    . PRO B 1 377 ? 60.810  8.430   7.953   1.00 183.60 ? 404 PRO B CA    1 
ATOM   7183 C  C     . PRO B 1 377 ? 61.336  8.485   9.380   1.00 180.81 ? 404 PRO B C     1 
ATOM   7184 O  O     . PRO B 1 377 ? 60.942  9.355   10.164  1.00 183.81 ? 404 PRO B O     1 
ATOM   7185 C  CB    . PRO B 1 377 ? 61.940  8.633   6.933   1.00 179.01 ? 404 PRO B CB    1 
ATOM   7186 C  CG    . PRO B 1 377 ? 61.335  9.462   5.845   1.00 181.85 ? 404 PRO B CG    1 
ATOM   7187 C  CD    . PRO B 1 377 ? 60.359  10.362  6.535   1.00 190.75 ? 404 PRO B CD    1 
ATOM   7188 N  N     . LEU B 1 378 ? 62.230  7.562   9.723   1.00 165.94 ? 405 LEU B N     1 
ATOM   7189 C  CA    . LEU B 1 378 ? 62.785  7.515   11.069  1.00 154.28 ? 405 LEU B CA    1 
ATOM   7190 C  C     . LEU B 1 378 ? 63.705  8.707   11.312  1.00 151.44 ? 405 LEU B C     1 
ATOM   7191 O  O     . LEU B 1 378 ? 64.500  9.089   10.448  1.00 139.37 ? 405 LEU B O     1 
ATOM   7192 C  CB    . LEU B 1 378 ? 63.540  6.203   11.283  1.00 137.87 ? 405 LEU B CB    1 
ATOM   7193 C  CG    . LEU B 1 378 ? 64.088  5.928   12.684  1.00 133.85 ? 405 LEU B CG    1 
ATOM   7194 C  CD1   . LEU B 1 378 ? 63.778  4.506   13.095  1.00 136.40 ? 405 LEU B CD1   1 
ATOM   7195 C  CD2   . LEU B 1 378 ? 65.585  6.173   12.731  1.00 127.82 ? 405 LEU B CD2   1 
ATOM   7196 N  N     . THR B 1 379 ? 63.596  9.292   12.500  1.00 155.33 ? 406 THR B N     1 
ATOM   7197 C  CA    . THR B 1 379 ? 64.313  10.508  12.855  1.00 149.67 ? 406 THR B CA    1 
ATOM   7198 C  C     . THR B 1 379 ? 65.616  10.184  13.578  1.00 144.88 ? 406 THR B C     1 
ATOM   7199 O  O     . THR B 1 379 ? 65.806  9.087   14.108  1.00 145.54 ? 406 THR B O     1 
ATOM   7200 C  CB    . THR B 1 379 ? 63.444  11.409  13.738  1.00 151.58 ? 406 THR B CB    1 
ATOM   7201 O  OG1   . THR B 1 379 ? 63.382  10.868  15.062  1.00 141.65 ? 406 THR B OG1   1 
ATOM   7202 C  CG2   . THR B 1 379 ? 62.032  11.501  13.174  1.00 157.84 ? 406 THR B CG2   1 
ATOM   7203 N  N     . LYS B 1 380 ? 66.518  11.170  13.595  1.00 151.31 ? 407 LYS B N     1 
ATOM   7204 C  CA    . LYS B 1 380 ? 67.762  11.018  14.343  1.00 144.02 ? 407 LYS B CA    1 
ATOM   7205 C  C     . LYS B 1 380 ? 67.499  10.878  15.836  1.00 134.64 ? 407 LYS B C     1 
ATOM   7206 O  O     . LYS B 1 380 ? 68.271  10.221  16.542  1.00 136.87 ? 407 LYS B O     1 
ATOM   7207 C  CB    . LYS B 1 380 ? 68.690  12.203  14.071  1.00 142.15 ? 407 LYS B CB    1 
ATOM   7208 C  CG    . LYS B 1 380 ? 69.247  12.245  12.655  1.00 138.79 ? 407 LYS B CG    1 
ATOM   7209 C  CD    . LYS B 1 380 ? 70.069  11.001  12.351  1.00 147.55 ? 407 LYS B CD    1 
ATOM   7210 C  CE    . LYS B 1 380 ? 70.649  11.040  10.946  1.00 154.99 ? 407 LYS B CE    1 
ATOM   7211 N  NZ    . LYS B 1 380 ? 71.415  9.800   10.627  1.00 147.15 ? 407 LYS B NZ    1 
ATOM   7212 N  N     . GLY B 1 381 ? 66.420  11.485  16.334  1.00 123.74 ? 408 GLY B N     1 
ATOM   7213 C  CA    . GLY B 1 381 ? 66.057  11.290  17.728  1.00 125.28 ? 408 GLY B CA    1 
ATOM   7214 C  C     . GLY B 1 381 ? 65.618  9.867   18.012  1.00 121.21 ? 408 GLY B C     1 
ATOM   7215 O  O     . GLY B 1 381 ? 66.092  9.235   18.960  1.00 120.79 ? 408 GLY B O     1 
ATOM   7216 N  N     . GLU B 1 382 ? 64.708  9.341   17.188  1.00 126.20 ? 409 GLU B N     1 
ATOM   7217 C  CA    . GLU B 1 382 ? 64.287  7.951   17.336  1.00 120.26 ? 409 GLU B CA    1 
ATOM   7218 C  C     . GLU B 1 382 ? 65.436  6.986   17.085  1.00 127.35 ? 409 GLU B C     1 
ATOM   7219 O  O     . GLU B 1 382 ? 65.440  5.874   17.626  1.00 122.11 ? 409 GLU B O     1 
ATOM   7220 C  CB    . GLU B 1 382 ? 63.129  7.650   16.385  1.00 123.88 ? 409 GLU B CB    1 
ATOM   7221 C  CG    . GLU B 1 382 ? 61.868  8.442   16.672  1.00 126.29 ? 409 GLU B CG    1 
ATOM   7222 C  CD    . GLU B 1 382 ? 60.800  8.229   15.619  1.00 138.38 ? 409 GLU B CD    1 
ATOM   7223 O  OE1   . GLU B 1 382 ? 61.152  7.863   14.477  1.00 140.60 ? 409 GLU B OE1   1 
ATOM   7224 O  OE2   . GLU B 1 382 ? 59.608  8.427   15.937  1.00 131.09 ? 409 GLU B OE2   1 
ATOM   7225 N  N     . LEU B 1 383 ? 66.409  7.387   16.263  1.00 137.39 ? 410 LEU B N     1 
ATOM   7226 C  CA    . LEU B 1 383 ? 67.593  6.562   16.040  1.00 137.62 ? 410 LEU B CA    1 
ATOM   7227 C  C     . LEU B 1 383 ? 68.421  6.425   17.309  1.00 132.43 ? 410 LEU B C     1 
ATOM   7228 O  O     . LEU B 1 383 ? 68.769  5.310   17.714  1.00 134.88 ? 410 LEU B O     1 
ATOM   7229 C  CB    . LEU B 1 383 ? 68.436  7.151   14.910  1.00 140.86 ? 410 LEU B CB    1 
ATOM   7230 C  CG    . LEU B 1 383 ? 69.809  6.521   14.664  1.00 140.98 ? 410 LEU B CG    1 
ATOM   7231 C  CD1   . LEU B 1 383 ? 69.681  5.034   14.353  1.00 148.39 ? 410 LEU B CD1   1 
ATOM   7232 C  CD2   . LEU B 1 383 ? 70.540  7.241   13.542  1.00 137.11 ? 410 LEU B CD2   1 
ATOM   7233 N  N     . GLY B 1 384 ? 68.756  7.549   17.940  1.00 127.69 ? 411 GLY B N     1 
ATOM   7234 C  CA    . GLY B 1 384 ? 69.513  7.497   19.175  1.00 120.77 ? 411 GLY B CA    1 
ATOM   7235 C  C     . GLY B 1 384 ? 68.744  6.862   20.312  1.00 117.45 ? 411 GLY B C     1 
ATOM   7236 O  O     . GLY B 1 384 ? 69.343  6.295   21.227  1.00 113.97 ? 411 GLY B O     1 
ATOM   7237 N  N     . CYS B 1 385 ? 67.412  6.938   20.267  1.00 120.85 ? 412 CYS B N     1 
ATOM   7238 C  CA    . CYS B 1 385 ? 66.596  6.295   21.287  1.00 124.23 ? 412 CYS B CA    1 
ATOM   7239 C  C     . CYS B 1 385 ? 66.615  4.781   21.127  1.00 124.87 ? 412 CYS B C     1 
ATOM   7240 O  O     . CYS B 1 385 ? 66.658  4.051   22.122  1.00 124.03 ? 412 CYS B O     1 
ATOM   7241 C  CB    . CYS B 1 385 ? 65.167  6.838   21.223  1.00 115.08 ? 412 CYS B CB    1 
ATOM   7242 S  SG    . CYS B 1 385 ? 64.145  6.407   22.659  1.00 127.34 ? 412 CYS B SG    1 
ATOM   7243 N  N     . PHE B 1 386 ? 66.580  4.291   19.885  1.00 126.77 ? 413 PHE B N     1 
ATOM   7244 C  CA    . PHE B 1 386 ? 66.658  2.851   19.659  1.00 121.13 ? 413 PHE B CA    1 
ATOM   7245 C  C     . PHE B 1 386 ? 68.007  2.298   20.101  1.00 124.02 ? 413 PHE B C     1 
ATOM   7246 O  O     . PHE B 1 386 ? 68.079  1.216   20.695  1.00 122.83 ? 413 PHE B O     1 
ATOM   7247 C  CB    . PHE B 1 386 ? 66.410  2.534   18.183  1.00 123.49 ? 413 PHE B CB    1 
ATOM   7248 C  CG    . PHE B 1 386 ? 66.303  1.062   17.888  1.00 122.32 ? 413 PHE B CG    1 
ATOM   7249 C  CD1   . PHE B 1 386 ? 67.436  0.302   17.638  1.00 125.32 ? 413 PHE B CD1   1 
ATOM   7250 C  CD2   . PHE B 1 386 ? 65.069  0.438   17.862  1.00 124.52 ? 413 PHE B CD2   1 
ATOM   7251 C  CE1   . PHE B 1 386 ? 67.335  -1.049  17.373  1.00 134.02 ? 413 PHE B CE1   1 
ATOM   7252 C  CE2   . PHE B 1 386 ? 64.962  -0.911  17.598  1.00 125.37 ? 413 PHE B CE2   1 
ATOM   7253 C  CZ    . PHE B 1 386 ? 66.095  -1.654  17.353  1.00 131.63 ? 413 PHE B CZ    1 
ATOM   7254 N  N     . LEU B 1 387 ? 69.090  3.024   19.812  1.00 120.10 ? 414 LEU B N     1 
ATOM   7255 C  CA    . LEU B 1 387 ? 70.422  2.566   20.186  1.00 121.74 ? 414 LEU B CA    1 
ATOM   7256 C  C     . LEU B 1 387 ? 70.642  2.582   21.693  1.00 122.65 ? 414 LEU B C     1 
ATOM   7257 O  O     . LEU B 1 387 ? 71.484  1.827   22.190  1.00 123.12 ? 414 LEU B O     1 
ATOM   7258 C  CB    . LEU B 1 387 ? 71.481  3.420   19.489  1.00 119.66 ? 414 LEU B CB    1 
ATOM   7259 C  CG    . LEU B 1 387 ? 71.524  3.285   17.967  1.00 124.36 ? 414 LEU B CG    1 
ATOM   7260 C  CD1   . LEU B 1 387 ? 72.420  4.351   17.361  1.00 133.57 ? 414 LEU B CD1   1 
ATOM   7261 C  CD2   . LEU B 1 387 ? 71.996  1.893   17.569  1.00 117.21 ? 414 LEU B CD2   1 
ATOM   7262 N  N     . SER B 1 388 ? 69.908  3.421   22.428  1.00 131.05 ? 415 SER B N     1 
ATOM   7263 C  CA    . SER B 1 388 ? 70.012  3.411   23.884  1.00 125.77 ? 415 SER B CA    1 
ATOM   7264 C  C     . SER B 1 388 ? 69.456  2.114   24.460  1.00 119.22 ? 415 SER B C     1 
ATOM   7265 O  O     . SER B 1 388 ? 70.124  1.438   25.252  1.00 119.46 ? 415 SER B O     1 
ATOM   7266 C  CB    . SER B 1 388 ? 69.285  4.621   24.472  1.00 121.05 ? 415 SER B CB    1 
ATOM   7267 O  OG    . SER B 1 388 ? 69.881  5.833   24.043  1.00 120.75 ? 415 SER B OG    1 
ATOM   7268 N  N     . HIS B 1 389 ? 68.229  1.752   24.074  1.00 114.36 ? 416 HIS B N     1 
ATOM   7269 C  CA    . HIS B 1 389 ? 67.688  0.455   24.464  1.00 108.20 ? 416 HIS B CA    1 
ATOM   7270 C  C     . HIS B 1 389 ? 68.509  -0.685  23.879  1.00 120.95 ? 416 HIS B C     1 
ATOM   7271 O  O     . HIS B 1 389 ? 68.622  -1.749  24.499  1.00 121.42 ? 416 HIS B O     1 
ATOM   7272 C  CB    . HIS B 1 389 ? 66.229  0.335   24.023  1.00 111.43 ? 416 HIS B CB    1 
ATOM   7273 C  CG    . HIS B 1 389 ? 65.297  1.255   24.749  1.00 107.11 ? 416 HIS B CG    1 
ATOM   7274 N  ND1   . HIS B 1 389 ? 64.721  0.929   25.958  1.00 108.45 ? 416 HIS B ND1   1 
ATOM   7275 C  CD2   . HIS B 1 389 ? 64.830  2.485   24.431  1.00 110.90 ? 416 HIS B CD2   1 
ATOM   7276 C  CE1   . HIS B 1 389 ? 63.946  1.921   26.357  1.00 109.54 ? 416 HIS B CE1   1 
ATOM   7277 N  NE2   . HIS B 1 389 ? 63.994  2.878   25.447  1.00 108.68 ? 416 HIS B NE2   1 
ATOM   7278 N  N     . TYR B 1 390 ? 69.090  -0.482  22.693  1.00 120.73 ? 417 TYR B N     1 
ATOM   7279 C  CA    . TYR B 1 390 ? 69.927  -1.512  22.083  1.00 118.94 ? 417 TYR B CA    1 
ATOM   7280 C  C     . TYR B 1 390 ? 71.167  -1.784  22.927  1.00 115.46 ? 417 TYR B C     1 
ATOM   7281 O  O     . TYR B 1 390 ? 71.609  -2.933  23.042  1.00 115.18 ? 417 TYR B O     1 
ATOM   7282 C  CB    . TYR B 1 390 ? 70.310  -1.089  20.662  1.00 126.18 ? 417 TYR B CB    1 
ATOM   7283 C  CG    . TYR B 1 390 ? 71.276  -2.012  19.947  1.00 126.91 ? 417 TYR B CG    1 
ATOM   7284 C  CD1   . TYR B 1 390 ? 70.860  -3.244  19.456  1.00 122.04 ? 417 TYR B CD1   1 
ATOM   7285 C  CD2   . TYR B 1 390 ? 72.598  -1.637  19.740  1.00 126.84 ? 417 TYR B CD2   1 
ATOM   7286 C  CE1   . TYR B 1 390 ? 71.740  -4.083  18.794  1.00 127.64 ? 417 TYR B CE1   1 
ATOM   7287 C  CE2   . TYR B 1 390 ? 73.483  -2.469  19.079  1.00 131.86 ? 417 TYR B CE2   1 
ATOM   7288 C  CZ    . TYR B 1 390 ? 73.050  -3.691  18.608  1.00 136.35 ? 417 TYR B CZ    1 
ATOM   7289 O  OH    . TYR B 1 390 ? 73.930  -4.522  17.948  1.00 133.19 ? 417 TYR B OH    1 
ATOM   7290 N  N     . ASN B 1 391 ? 71.737  -0.739  23.532  1.00 112.66 ? 418 ASN B N     1 
ATOM   7291 C  CA    . ASN B 1 391 ? 72.893  -0.931  24.403  1.00 117.25 ? 418 ASN B CA    1 
ATOM   7292 C  C     . ASN B 1 391 ? 72.515  -1.705  25.659  1.00 115.17 ? 418 ASN B C     1 
ATOM   7293 O  O     . ASN B 1 391 ? 73.282  -2.557  26.124  1.00 111.97 ? 418 ASN B O     1 
ATOM   7294 C  CB    . ASN B 1 391 ? 73.502  0.421   24.772  1.00 115.96 ? 418 ASN B CB    1 
ATOM   7295 C  CG    . ASN B 1 391 ? 74.153  1.103   23.591  1.00 122.59 ? 418 ASN B CG    1 
ATOM   7296 O  OD1   . ASN B 1 391 ? 74.100  0.604   22.467  1.00 118.61 ? 418 ASN B OD1   1 
ATOM   7297 N  ND2   . ASN B 1 391 ? 74.768  2.255   23.836  1.00 134.96 ? 418 ASN B ND2   1 
ATOM   7298 N  N     . ILE B 1 392 ? 71.339  -1.419  26.222  1.00 108.73 ? 419 ILE B N     1 
ATOM   7299 C  CA    . ILE B 1 392 ? 70.902  -2.120  27.424  1.00 106.45 ? 419 ILE B CA    1 
ATOM   7300 C  C     . ILE B 1 392 ? 70.671  -3.595  27.127  1.00 108.78 ? 419 ILE B C     1 
ATOM   7301 O  O     . ILE B 1 392 ? 71.032  -4.464  27.929  1.00 117.48 ? 419 ILE B O     1 
ATOM   7302 C  CB    . ILE B 1 392 ? 69.643  -1.450  28.007  1.00 108.71 ? 419 ILE B CB    1 
ATOM   7303 C  CG1   . ILE B 1 392 ? 69.924  0.017   28.333  1.00 91.10  ? 419 ILE B CG1   1 
ATOM   7304 C  CG2   . ILE B 1 392 ? 69.171  -2.183  29.255  1.00 100.04 ? 419 ILE B CG2   1 
ATOM   7305 C  CD1   . ILE B 1 392 ? 68.827  0.675   29.124  1.00 89.40  ? 419 ILE B CD1   1 
ATOM   7306 N  N     . TRP B 1 393 ? 70.070  -3.902  25.973  1.00 111.19 ? 420 TRP B N     1 
ATOM   7307 C  CA    . TRP B 1 393 ? 69.943  -5.296  25.555  1.00 110.49 ? 420 TRP B CA    1 
ATOM   7308 C  C     . TRP B 1 393 ? 71.308  -5.965  25.478  1.00 120.36 ? 420 TRP B C     1 
ATOM   7309 O  O     . TRP B 1 393 ? 71.466  -7.124  25.881  1.00 120.08 ? 420 TRP B O     1 
ATOM   7310 C  CB    . TRP B 1 393 ? 69.235  -5.386  24.202  1.00 117.37 ? 420 TRP B CB    1 
ATOM   7311 C  CG    . TRP B 1 393 ? 67.909  -4.689  24.140  1.00 119.52 ? 420 TRP B CG    1 
ATOM   7312 C  CD1   . TRP B 1 393 ? 67.100  -4.361  25.190  1.00 111.51 ? 420 TRP B CD1   1 
ATOM   7313 C  CD2   . TRP B 1 393 ? 67.243  -4.223  22.959  1.00 120.26 ? 420 TRP B CD2   1 
ATOM   7314 N  NE1   . TRP B 1 393 ? 65.971  -3.722  24.735  1.00 113.85 ? 420 TRP B NE1   1 
ATOM   7315 C  CE2   . TRP B 1 393 ? 66.035  -3.625  23.370  1.00 120.27 ? 420 TRP B CE2   1 
ATOM   7316 C  CE3   . TRP B 1 393 ? 67.552  -4.254  21.595  1.00 110.90 ? 420 TRP B CE3   1 
ATOM   7317 C  CZ2   . TRP B 1 393 ? 65.134  -3.064  22.465  1.00 118.61 ? 420 TRP B CZ2   1 
ATOM   7318 C  CZ3   . TRP B 1 393 ? 66.657  -3.697  20.699  1.00 116.38 ? 420 TRP B CZ3   1 
ATOM   7319 C  CH2   . TRP B 1 393 ? 65.462  -3.110  21.137  1.00 121.85 ? 420 TRP B CH2   1 
ATOM   7320 N  N     . LYS B 1 394 ? 72.310  -5.245  24.964  1.00 128.52 ? 421 LYS B N     1 
ATOM   7321 C  CA    . LYS B 1 394 ? 73.668  -5.777  24.925  1.00 125.48 ? 421 LYS B CA    1 
ATOM   7322 C  C     . LYS B 1 394 ? 74.223  -5.977  26.330  1.00 126.88 ? 421 LYS B C     1 
ATOM   7323 O  O     . LYS B 1 394 ? 74.914  -6.967  26.596  1.00 127.78 ? 421 LYS B O     1 
ATOM   7324 C  CB    . LYS B 1 394 ? 74.576  -4.847  24.121  1.00 129.60 ? 421 LYS B CB    1 
ATOM   7325 C  CG    . LYS B 1 394 ? 74.492  -5.020  22.613  1.00 122.05 ? 421 LYS B CG    1 
ATOM   7326 C  CD    . LYS B 1 394 ? 75.567  -4.189  21.926  1.00 133.69 ? 421 LYS B CD    1 
ATOM   7327 C  CE    . LYS B 1 394 ? 75.810  -4.654  20.502  1.00 143.55 ? 421 LYS B CE    1 
ATOM   7328 N  NZ    . LYS B 1 394 ? 76.955  -3.948  19.860  1.00 144.80 ? 421 LYS B NZ    1 
ATOM   7329 N  N     . GLU B 1 395 ? 73.935  -5.046  27.245  1.00 127.70 ? 422 GLU B N     1 
ATOM   7330 C  CA    . GLU B 1 395 ? 74.398  -5.204  28.620  1.00 116.02 ? 422 GLU B CA    1 
ATOM   7331 C  C     . GLU B 1 395 ? 73.727  -6.387  29.306  1.00 116.85 ? 422 GLU B C     1 
ATOM   7332 O  O     . GLU B 1 395 ? 74.355  -7.062  30.130  1.00 119.62 ? 422 GLU B O     1 
ATOM   7333 C  CB    . GLU B 1 395 ? 74.154  -3.921  29.413  1.00 108.72 ? 422 GLU B CB    1 
ATOM   7334 C  CG    . GLU B 1 395 ? 74.458  -4.051  30.899  1.00 111.48 ? 422 GLU B CG    1 
ATOM   7335 C  CD    . GLU B 1 395 ? 75.230  -2.871  31.445  1.00 119.18 ? 422 GLU B CD    1 
ATOM   7336 O  OE1   . GLU B 1 395 ? 75.451  -1.904  30.688  1.00 132.92 ? 422 GLU B OE1   1 
ATOM   7337 O  OE2   . GLU B 1 395 ? 75.622  -2.913  32.630  1.00 110.93 ? 422 GLU B OE2   1 
ATOM   7338 N  N     . VAL B 1 396 ? 72.464  -6.661  28.972  1.00 114.46 ? 423 VAL B N     1 
ATOM   7339 C  CA    . VAL B 1 396 ? 71.759  -7.777  29.596  1.00 121.48 ? 423 VAL B CA    1 
ATOM   7340 C  C     . VAL B 1 396 ? 72.371  -9.106  29.171  1.00 119.23 ? 423 VAL B C     1 
ATOM   7341 O  O     . VAL B 1 396 ? 72.590  -9.998  29.999  1.00 120.19 ? 423 VAL B O     1 
ATOM   7342 C  CB    . VAL B 1 396 ? 70.256  -7.715  29.264  1.00 113.56 ? 423 VAL B CB    1 
ATOM   7343 C  CG1   . VAL B 1 396 ? 69.561  -8.984  29.734  1.00 124.50 ? 423 VAL B CG1   1 
ATOM   7344 C  CG2   . VAL B 1 396 ? 69.615  -6.492  29.905  1.00 98.62  ? 423 VAL B CG2   1 
ATOM   7345 N  N     . VAL B 1 397 ? 72.660  -9.260  27.878  1.00 119.96 ? 424 VAL B N     1 
ATOM   7346 C  CA    . VAL B 1 397 ? 73.207  -10.521 27.386  1.00 119.87 ? 424 VAL B CA    1 
ATOM   7347 C  C     . VAL B 1 397 ? 74.630  -10.726 27.893  1.00 127.82 ? 424 VAL B C     1 
ATOM   7348 O  O     . VAL B 1 397 ? 74.991  -11.823 28.337  1.00 129.93 ? 424 VAL B O     1 
ATOM   7349 C  CB    . VAL B 1 397 ? 73.133  -10.570 25.849  1.00 109.48 ? 424 VAL B CB    1 
ATOM   7350 C  CG1   . VAL B 1 397 ? 73.996  -11.693 25.311  1.00 113.44 ? 424 VAL B CG1   1 
ATOM   7351 C  CG2   . VAL B 1 397 ? 71.690  -10.746 25.397  1.00 108.52 ? 424 VAL B CG2   1 
ATOM   7352 N  N     . ASP B 1 398 ? 75.456  -9.676  27.850  1.00 147.13 ? 425 ASP B N     1 
ATOM   7353 C  CA    . ASP B 1 398 ? 76.844  -9.797  28.292  1.00 148.24 ? 425 ASP B CA    1 
ATOM   7354 C  C     . ASP B 1 398 ? 76.925  -10.219 29.753  1.00 150.41 ? 425 ASP B C     1 
ATOM   7355 O  O     . ASP B 1 398 ? 77.593  -11.202 30.094  1.00 169.50 ? 425 ASP B O     1 
ATOM   7356 C  CB    . ASP B 1 398 ? 77.582  -8.474  28.083  1.00 144.71 ? 425 ASP B CB    1 
ATOM   7357 C  CG    . ASP B 1 398 ? 77.685  -8.086  26.624  1.00 166.70 ? 425 ASP B CG    1 
ATOM   7358 O  OD1   . ASP B 1 398 ? 77.375  -8.932  25.758  1.00 168.24 ? 425 ASP B OD1   1 
ATOM   7359 O  OD2   . ASP B 1 398 ? 78.068  -6.930  26.344  1.00 169.80 ? 425 ASP B OD2   1 
ATOM   7360 N  N     . ARG B 1 399 ? 76.249  -9.485  30.633  1.00 145.07 ? 426 ARG B N     1 
ATOM   7361 C  CA    . ARG B 1 399 ? 76.302  -9.770  32.060  1.00 142.96 ? 426 ARG B CA    1 
ATOM   7362 C  C     . ARG B 1 399 ? 75.387  -10.916 32.475  1.00 137.35 ? 426 ARG B C     1 
ATOM   7363 O  O     . ARG B 1 399 ? 75.441  -11.337 33.636  1.00 130.66 ? 426 ARG B O     1 
ATOM   7364 C  CB    . ARG B 1 399 ? 75.960  -8.505  32.849  1.00 124.92 ? 426 ARG B CB    1 
ATOM   7365 C  CG    . ARG B 1 399 ? 76.999  -7.403  32.695  1.00 124.51 ? 426 ARG B CG    1 
ATOM   7366 C  CD    . ARG B 1 399 ? 76.481  -6.071  33.200  1.00 118.18 ? 426 ARG B CD    1 
ATOM   7367 N  NE    . ARG B 1 399 ? 75.868  -6.191  34.516  1.00 120.81 ? 426 ARG B NE    1 
ATOM   7368 C  CZ    . ARG B 1 399 ? 75.295  -5.188  35.165  1.00 129.82 ? 426 ARG B CZ    1 
ATOM   7369 N  NH1   . ARG B 1 399 ? 75.249  -3.970  34.653  1.00 131.68 ? 426 ARG B NH1   1 
ATOM   7370 N  NH2   . ARG B 1 399 ? 74.753  -5.414  36.358  1.00 126.36 ? 426 ARG B NH2   1 
ATOM   7371 N  N     . GLY B 1 400 ? 74.561  -11.429 31.566  1.00 128.43 ? 427 GLY B N     1 
ATOM   7372 C  CA    . GLY B 1 400 ? 73.710  -12.564 31.874  1.00 126.51 ? 427 GLY B CA    1 
ATOM   7373 C  C     . GLY B 1 400 ? 72.631  -12.296 32.900  1.00 135.60 ? 427 GLY B C     1 
ATOM   7374 O  O     . GLY B 1 400 ? 72.243  -13.213 33.632  1.00 136.17 ? 427 GLY B O     1 
ATOM   7375 N  N     . LEU B 1 401 ? 72.134  -11.064 32.976  1.00 143.47 ? 428 LEU B N     1 
ATOM   7376 C  CA    . LEU B 1 401 ? 71.088  -10.730 33.933  1.00 139.12 ? 428 LEU B CA    1 
ATOM   7377 C  C     . LEU B 1 401 ? 69.781  -11.405 33.537  1.00 136.94 ? 428 LEU B C     1 
ATOM   7378 O  O     . LEU B 1 401 ? 69.311  -11.255 32.406  1.00 147.34 ? 428 LEU B O     1 
ATOM   7379 C  CB    . LEU B 1 401 ? 70.909  -9.214  34.002  1.00 136.59 ? 428 LEU B CB    1 
ATOM   7380 C  CG    . LEU B 1 401 ? 72.197  -8.432  34.271  1.00 134.06 ? 428 LEU B CG    1 
ATOM   7381 C  CD1   . LEU B 1 401 ? 71.995  -6.948  34.023  1.00 134.49 ? 428 LEU B CD1   1 
ATOM   7382 C  CD2   . LEU B 1 401 ? 72.679  -8.679  35.691  1.00 140.19 ? 428 LEU B CD2   1 
ATOM   7383 N  N     . GLN B 1 402 ? 69.190  -12.151 34.473  1.00 134.55 ? 429 GLN B N     1 
ATOM   7384 C  CA    . GLN B 1 402 ? 68.001  -12.931 34.145  1.00 132.23 ? 429 GLN B CA    1 
ATOM   7385 C  C     . GLN B 1 402 ? 66.756  -12.056 34.043  1.00 126.48 ? 429 GLN B C     1 
ATOM   7386 O  O     . GLN B 1 402 ? 65.901  -12.293 33.183  1.00 115.32 ? 429 GLN B O     1 
ATOM   7387 C  CB    . GLN B 1 402 ? 67.800  -14.040 35.181  1.00 121.09 ? 429 GLN B CB    1 
ATOM   7388 C  CG    . GLN B 1 402 ? 69.048  -14.876 35.454  1.00 130.07 ? 429 GLN B CG    1 
ATOM   7389 C  CD    . GLN B 1 402 ? 69.522  -15.661 34.239  1.00 143.60 ? 429 GLN B CD    1 
ATOM   7390 O  OE1   . GLN B 1 402 ? 68.772  -15.870 33.286  1.00 153.38 ? 429 GLN B OE1   1 
ATOM   7391 N  NE2   . GLN B 1 402 ? 70.777  -16.101 34.273  1.00 141.91 ? 429 GLN B NE2   1 
ATOM   7392 N  N     . LYS B 1 403 ? 66.634  -11.047 34.905  1.00 124.99 ? 430 LYS B N     1 
ATOM   7393 C  CA    . LYS B 1 403 ? 65.500  -10.129 34.869  1.00 132.94 ? 430 LYS B CA    1 
ATOM   7394 C  C     . LYS B 1 403 ? 65.965  -8.729  35.238  1.00 125.89 ? 430 LYS B C     1 
ATOM   7395 O  O     . LYS B 1 403 ? 66.665  -8.544  36.238  1.00 121.62 ? 430 LYS B O     1 
ATOM   7396 C  CB    . LYS B 1 403 ? 64.380  -10.582 35.815  1.00 129.26 ? 430 LYS B CB    1 
ATOM   7397 C  CG    . LYS B 1 403 ? 64.850  -10.957 37.208  1.00 134.37 ? 430 LYS B CG    1 
ATOM   7398 C  CD    . LYS B 1 403 ? 63.743  -10.761 38.228  1.00 135.22 ? 430 LYS B CD    1 
ATOM   7399 C  CE    . LYS B 1 403 ? 64.159  -11.263 39.599  1.00 140.73 ? 430 LYS B CE    1 
ATOM   7400 N  NZ    . LYS B 1 403 ? 63.186  -10.856 40.653  1.00 129.85 ? 430 LYS B NZ    1 
ATOM   7401 N  N     . SER B 1 404 ? 65.564  -7.746  34.434  1.00 115.19 ? 431 SER B N     1 
ATOM   7402 C  CA    . SER B 1 404 ? 65.998  -6.370  34.608  1.00 110.69 ? 431 SER B CA    1 
ATOM   7403 C  C     . SER B 1 404 ? 64.826  -5.434  34.362  1.00 106.98 ? 431 SER B C     1 
ATOM   7404 O  O     . SER B 1 404 ? 63.941  -5.722  33.553  1.00 104.57 ? 431 SER B O     1 
ATOM   7405 C  CB    . SER B 1 404 ? 67.151  -6.020  33.656  1.00 113.53 ? 431 SER B CB    1 
ATOM   7406 O  OG    . SER B 1 404 ? 68.186  -6.986  33.731  1.00 130.23 ? 431 SER B OG    1 
ATOM   7407 N  N     . LEU B 1 405 ? 64.829  -4.308  35.070  1.00 103.58 ? 432 LEU B N     1 
ATOM   7408 C  CA    . LEU B 1 405 ? 63.848  -3.249  34.879  1.00 99.94  ? 432 LEU B CA    1 
ATOM   7409 C  C     . LEU B 1 405 ? 64.529  -2.062  34.213  1.00 100.52 ? 432 LEU B C     1 
ATOM   7410 O  O     . LEU B 1 405 ? 65.630  -1.671  34.613  1.00 98.39  ? 432 LEU B O     1 
ATOM   7411 C  CB    . LEU B 1 405 ? 63.225  -2.831  36.211  1.00 100.64 ? 432 LEU B CB    1 
ATOM   7412 C  CG    . LEU B 1 405 ? 62.136  -1.760  36.143  1.00 99.24  ? 432 LEU B CG    1 
ATOM   7413 C  CD1   . LEU B 1 405 ? 61.018  -2.194  35.214  1.00 89.59  ? 432 LEU B CD1   1 
ATOM   7414 C  CD2   . LEU B 1 405 ? 61.592  -1.477  37.529  1.00 91.25  ? 432 LEU B CD2   1 
ATOM   7415 N  N     . VAL B 1 406 ? 63.878  -1.496  33.198  1.00 105.54 ? 433 VAL B N     1 
ATOM   7416 C  CA    . VAL B 1 406 ? 64.440  -0.411  32.401  1.00 109.50 ? 433 VAL B CA    1 
ATOM   7417 C  C     . VAL B 1 406 ? 63.550  0.817   32.551  1.00 110.06 ? 433 VAL B C     1 
ATOM   7418 O  O     . VAL B 1 406 ? 62.326  0.722   32.407  1.00 104.08 ? 433 VAL B O     1 
ATOM   7419 C  CB    . VAL B 1 406 ? 64.578  -0.811  30.920  1.00 109.89 ? 433 VAL B CB    1 
ATOM   7420 C  CG1   . VAL B 1 406 ? 65.188  0.329   30.110  1.00 101.73 ? 433 VAL B CG1   1 
ATOM   7421 C  CG2   . VAL B 1 406 ? 65.415  -2.077  30.790  1.00 109.82 ? 433 VAL B CG2   1 
ATOM   7422 N  N     . PHE B 1 407 ? 64.168  1.964   32.838  1.00 106.28 ? 434 PHE B N     1 
ATOM   7423 C  CA    . PHE B 1 407 ? 63.471  3.229   33.015  1.00 96.16  ? 434 PHE B CA    1 
ATOM   7424 C  C     . PHE B 1 407 ? 63.952  4.246   31.990  1.00 101.84 ? 434 PHE B C     1 
ATOM   7425 O  O     . PHE B 1 407 ? 65.082  4.168   31.498  1.00 98.09  ? 434 PHE B O     1 
ATOM   7426 C  CB    . PHE B 1 407 ? 63.699  3.807   34.423  1.00 91.85  ? 434 PHE B CB    1 
ATOM   7427 C  CG    . PHE B 1 407 ? 62.854  3.180   35.494  1.00 100.63 ? 434 PHE B CG    1 
ATOM   7428 C  CD1   . PHE B 1 407 ? 61.589  2.690   35.207  1.00 113.73 ? 434 PHE B CD1   1 
ATOM   7429 C  CD2   . PHE B 1 407 ? 63.325  3.087   36.796  1.00 97.06  ? 434 PHE B CD2   1 
ATOM   7430 C  CE1   . PHE B 1 407 ? 60.812  2.114   36.201  1.00 110.64 ? 434 PHE B CE1   1 
ATOM   7431 C  CE2   . PHE B 1 407 ? 62.551  2.513   37.792  1.00 102.24 ? 434 PHE B CE2   1 
ATOM   7432 C  CZ    . PHE B 1 407 ? 61.293  2.030   37.494  1.00 104.79 ? 434 PHE B CZ    1 
ATOM   7433 N  N     . GLU B 1 408 ? 63.087  5.203   31.676  1.00 106.51 ? 435 GLU B N     1 
ATOM   7434 C  CA    . GLU B 1 408 ? 63.472  6.381   30.917  1.00 102.80 ? 435 GLU B CA    1 
ATOM   7435 C  C     . GLU B 1 408 ? 63.610  7.561   31.889  1.00 102.22 ? 435 GLU B C     1 
ATOM   7436 O  O     . GLU B 1 408 ? 63.711  7.366   33.106  1.00 112.49 ? 435 GLU B O     1 
ATOM   7437 C  CB    . GLU B 1 408 ? 62.462  6.615   29.785  1.00 111.34 ? 435 GLU B CB    1 
ATOM   7438 C  CG    . GLU B 1 408 ? 62.574  5.588   28.656  1.00 106.18 ? 435 GLU B CG    1 
ATOM   7439 C  CD    . GLU B 1 408 ? 61.732  5.936   27.437  1.00 120.45 ? 435 GLU B CD    1 
ATOM   7440 O  OE1   . GLU B 1 408 ? 60.639  6.516   27.605  1.00 141.65 ? 435 GLU B OE1   1 
ATOM   7441 O  OE2   . GLU B 1 408 ? 62.166  5.628   26.305  1.00 123.62 ? 435 GLU B OE2   1 
ATOM   7442 N  N     . ASP B 1 409 ? 63.622  8.789   31.370  1.00 103.61 ? 436 ASP B N     1 
ATOM   7443 C  CA    . ASP B 1 409 ? 63.957  9.948   32.187  1.00 94.95  ? 436 ASP B CA    1 
ATOM   7444 C  C     . ASP B 1 409 ? 62.782  10.877  32.468  1.00 101.16 ? 436 ASP B C     1 
ATOM   7445 O  O     . ASP B 1 409 ? 62.940  11.825  33.245  1.00 109.56 ? 436 ASP B O     1 
ATOM   7446 C  CB    . ASP B 1 409 ? 65.101  10.743  31.537  1.00 91.79  ? 436 ASP B CB    1 
ATOM   7447 C  CG    . ASP B 1 409 ? 64.839  11.074  30.082  1.00 99.87  ? 436 ASP B CG    1 
ATOM   7448 O  OD1   . ASP B 1 409 ? 63.809  10.626  29.537  1.00 107.77 ? 436 ASP B OD1   1 
ATOM   7449 O  OD2   . ASP B 1 409 ? 65.679  11.784  29.481  1.00 109.40 ? 436 ASP B OD2   1 
ATOM   7450 N  N     . ASP B 1 410 ? 61.610  10.642  31.871  1.00 104.59 ? 437 ASP B N     1 
ATOM   7451 C  CA    . ASP B 1 410 ? 60.438  11.499  32.093  1.00 102.64 ? 437 ASP B CA    1 
ATOM   7452 C  C     . ASP B 1 410 ? 59.225  10.599  32.317  1.00 99.58  ? 437 ASP B C     1 
ATOM   7453 O  O     . ASP B 1 410 ? 58.505  10.257  31.376  1.00 117.95 ? 437 ASP B O     1 
ATOM   7454 C  CB    . ASP B 1 410 ? 60.222  12.468  30.934  1.00 123.13 ? 437 ASP B CB    1 
ATOM   7455 C  CG    . ASP B 1 410 ? 60.337  11.799  29.569  1.00 153.00 ? 437 ASP B CG    1 
ATOM   7456 O  OD1   . ASP B 1 410 ? 60.630  10.581  29.510  1.00 150.06 ? 437 ASP B OD1   1 
ATOM   7457 O  OD2   . ASP B 1 410 ? 60.131  12.500  28.553  1.00 156.52 ? 437 ASP B OD2   1 
ATOM   7458 N  N     . LEU B 1 411 ? 58.997  10.229  33.574  1.00 103.29 ? 438 LEU B N     1 
ATOM   7459 C  CA    . LEU B 1 411 ? 57.891  9.348   33.915  1.00 110.78 ? 438 LEU B CA    1 
ATOM   7460 C  C     . LEU B 1 411 ? 57.527  9.547   35.381  1.00 95.72  ? 438 LEU B C     1 
ATOM   7461 O  O     . LEU B 1 411 ? 58.404  9.791   36.213  1.00 106.20 ? 438 LEU B O     1 
ATOM   7462 C  CB    . LEU B 1 411 ? 58.256  7.886   33.629  1.00 106.15 ? 438 LEU B CB    1 
ATOM   7463 C  CG    . LEU B 1 411 ? 59.591  7.382   34.185  1.00 105.66 ? 438 LEU B CG    1 
ATOM   7464 C  CD1   . LEU B 1 411 ? 59.388  6.647   35.501  1.00 108.24 ? 438 LEU B CD1   1 
ATOM   7465 C  CD2   . LEU B 1 411 ? 60.304  6.497   33.175  1.00 110.21 ? 438 LEU B CD2   1 
ATOM   7466 N  N     . ARG B 1 412 ? 56.234  9.454   35.685  1.00 96.88  ? 439 ARG B N     1 
ATOM   7467 C  CA    . ARG B 1 412 ? 55.727  9.587   37.044  1.00 99.34  ? 439 ARG B CA    1 
ATOM   7468 C  C     . ARG B 1 412 ? 55.277  8.230   37.570  1.00 96.95  ? 439 ARG B C     1 
ATOM   7469 O  O     . ARG B 1 412 ? 54.846  7.362   36.806  1.00 106.93 ? 439 ARG B O     1 
ATOM   7470 C  CB    . ARG B 1 412 ? 54.563  10.580  37.114  1.00 104.18 ? 439 ARG B CB    1 
ATOM   7471 C  CG    . ARG B 1 412 ? 53.397  10.242  36.208  1.00 108.56 ? 439 ARG B CG    1 
ATOM   7472 C  CD    . ARG B 1 412 ? 52.130  10.917  36.693  1.00 105.94 ? 439 ARG B CD    1 
ATOM   7473 N  NE    . ARG B 1 412 ? 52.391  12.276  37.152  1.00 101.44 ? 439 ARG B NE    1 
ATOM   7474 C  CZ    . ARG B 1 412 ? 51.473  13.082  37.668  1.00 121.21 ? 439 ARG B CZ    1 
ATOM   7475 N  NH1   . ARG B 1 412 ? 50.214  12.699  37.807  1.00 116.39 ? 439 ARG B NH1   1 
ATOM   7476 N  NH2   . ARG B 1 412 ? 51.828  14.304  38.053  1.00 131.10 ? 439 ARG B NH2   1 
ATOM   7477 N  N     . PHE B 1 413 ? 55.370  8.062   38.886  1.00 98.66  ? 440 PHE B N     1 
ATOM   7478 C  CA    . PHE B 1 413 ? 55.158  6.775   39.530  1.00 91.00  ? 440 PHE B CA    1 
ATOM   7479 C  C     . PHE B 1 413 ? 53.788  6.701   40.192  1.00 88.09  ? 440 PHE B C     1 
ATOM   7480 O  O     . PHE B 1 413 ? 53.268  7.693   40.711  1.00 91.46  ? 440 PHE B O     1 
ATOM   7481 C  CB    . PHE B 1 413 ? 56.245  6.508   40.572  1.00 84.33  ? 440 PHE B CB    1 
ATOM   7482 C  CG    . PHE B 1 413 ? 57.617  6.346   39.988  1.00 89.14  ? 440 PHE B CG    1 
ATOM   7483 C  CD1   . PHE B 1 413 ? 58.380  7.454   39.658  1.00 84.34  ? 440 PHE B CD1   1 
ATOM   7484 C  CD2   . PHE B 1 413 ? 58.144  5.084   39.773  1.00 90.57  ? 440 PHE B CD2   1 
ATOM   7485 C  CE1   . PHE B 1 413 ? 59.643  7.307   39.118  1.00 93.44  ? 440 PHE B CE1   1 
ATOM   7486 C  CE2   . PHE B 1 413 ? 59.409  4.928   39.238  1.00 99.68  ? 440 PHE B CE2   1 
ATOM   7487 C  CZ    . PHE B 1 413 ? 60.160  6.041   38.910  1.00 109.86 ? 440 PHE B CZ    1 
ATOM   7488 N  N     . GLU B 1 414 ? 53.208  5.504   40.164  1.00 92.19  ? 441 GLU B N     1 
ATOM   7489 C  CA    . GLU B 1 414 ? 51.952  5.250   40.847  1.00 91.05  ? 441 GLU B CA    1 
ATOM   7490 C  C     . GLU B 1 414 ? 52.198  4.966   42.325  1.00 91.59  ? 441 GLU B C     1 
ATOM   7491 O  O     . GLU B 1 414 ? 53.305  4.615   42.747  1.00 89.13  ? 441 GLU B O     1 
ATOM   7492 C  CB    . GLU B 1 414 ? 51.209  4.078   40.204  1.00 88.77  ? 441 GLU B CB    1 
ATOM   7493 C  CG    . GLU B 1 414 ? 50.313  4.470   39.036  1.00 101.26 ? 441 GLU B CG    1 
ATOM   7494 C  CD    . GLU B 1 414 ? 48.975  5.025   39.491  1.00 111.76 ? 441 GLU B CD    1 
ATOM   7495 O  OE1   . GLU B 1 414 ? 48.557  4.708   40.626  1.00 110.02 ? 441 GLU B OE1   1 
ATOM   7496 O  OE2   . GLU B 1 414 ? 48.342  5.777   38.718  1.00 105.33 ? 441 GLU B OE2   1 
ATOM   7497 N  N     . ILE B 1 415 ? 51.136  5.134   43.117  1.00 88.82  ? 442 ILE B N     1 
ATOM   7498 C  CA    . ILE B 1 415 ? 51.230  4.889   44.549  1.00 92.46  ? 442 ILE B CA    1 
ATOM   7499 C  C     . ILE B 1 415 ? 51.542  3.417   44.798  1.00 99.35  ? 442 ILE B C     1 
ATOM   7500 O  O     . ILE B 1 415 ? 51.049  2.527   44.092  1.00 97.56  ? 442 ILE B O     1 
ATOM   7501 C  CB    . ILE B 1 415 ? 49.929  5.330   45.242  1.00 97.93  ? 442 ILE B CB    1 
ATOM   7502 C  CG1   . ILE B 1 415 ? 50.057  5.236   46.763  1.00 90.63  ? 442 ILE B CG1   1 
ATOM   7503 C  CG2   . ILE B 1 415 ? 48.736  4.514   44.741  1.00 90.44  ? 442 ILE B CG2   1 
ATOM   7504 C  CD1   . ILE B 1 415 ? 48.916  5.894   47.494  1.00 93.49  ? 442 ILE B CD1   1 
ATOM   7505 N  N     . PHE B 1 416 ? 52.389  3.161   45.800  1.00 89.64  ? 443 PHE B N     1 
ATOM   7506 C  CA    . PHE B 1 416 ? 52.855  1.810   46.129  1.00 92.42  ? 443 PHE B CA    1 
ATOM   7507 C  C     . PHE B 1 416 ? 53.544  1.147   44.938  1.00 97.45  ? 443 PHE B C     1 
ATOM   7508 O  O     . PHE B 1 416 ? 53.368  -0.047  44.691  1.00 100.12 ? 443 PHE B O     1 
ATOM   7509 C  CB    . PHE B 1 416 ? 51.714  0.922   46.632  1.00 87.89  ? 443 PHE B CB    1 
ATOM   7510 C  CG    . PHE B 1 416 ? 50.810  1.589   47.620  1.00 87.03  ? 443 PHE B CG    1 
ATOM   7511 C  CD1   . PHE B 1 416 ? 51.303  2.061   48.824  1.00 92.82  ? 443 PHE B CD1   1 
ATOM   7512 C  CD2   . PHE B 1 416 ? 49.459  1.726   47.353  1.00 88.48  ? 443 PHE B CD2   1 
ATOM   7513 C  CE1   . PHE B 1 416 ? 50.472  2.674   49.735  1.00 89.30  ? 443 PHE B CE1   1 
ATOM   7514 C  CE2   . PHE B 1 416 ? 48.620  2.334   48.263  1.00 89.60  ? 443 PHE B CE2   1 
ATOM   7515 C  CZ    . PHE B 1 416 ? 49.126  2.810   49.456  1.00 89.26  ? 443 PHE B CZ    1 
ATOM   7516 N  N     . PHE B 1 417 ? 54.333  1.922   44.190  1.00 97.46  ? 444 PHE B N     1 
ATOM   7517 C  CA    . PHE B 1 417 ? 54.969  1.372   42.997  1.00 88.04  ? 444 PHE B CA    1 
ATOM   7518 C  C     . PHE B 1 417 ? 55.871  0.193   43.339  1.00 91.95  ? 444 PHE B C     1 
ATOM   7519 O  O     . PHE B 1 417 ? 55.858  -0.829  42.644  1.00 102.36 ? 444 PHE B O     1 
ATOM   7520 C  CB    . PHE B 1 417 ? 55.769  2.452   42.266  1.00 92.12  ? 444 PHE B CB    1 
ATOM   7521 C  CG    . PHE B 1 417 ? 56.598  1.917   41.126  1.00 93.41  ? 444 PHE B CG    1 
ATOM   7522 C  CD1   . PHE B 1 417 ? 56.019  1.656   39.893  1.00 99.96  ? 444 PHE B CD1   1 
ATOM   7523 C  CD2   . PHE B 1 417 ? 57.950  1.660   41.292  1.00 82.78  ? 444 PHE B CD2   1 
ATOM   7524 C  CE1   . PHE B 1 417 ? 56.774  1.157   38.846  1.00 87.75  ? 444 PHE B CE1   1 
ATOM   7525 C  CE2   . PHE B 1 417 ? 58.708  1.161   40.251  1.00 89.99  ? 444 PHE B CE2   1 
ATOM   7526 C  CZ    . PHE B 1 417 ? 58.119  0.911   39.025  1.00 92.44  ? 444 PHE B CZ    1 
ATOM   7527 N  N     . LYS B 1 418 ? 56.653  0.312   44.414  1.00 91.10  ? 445 LYS B N     1 
ATOM   7528 C  CA    . LYS B 1 418 ? 57.640  -0.716  44.728  1.00 83.69  ? 445 LYS B CA    1 
ATOM   7529 C  C     . LYS B 1 418 ? 56.972  -2.018  45.157  1.00 94.55  ? 445 LYS B C     1 
ATOM   7530 O  O     . LYS B 1 418 ? 57.316  -3.096  44.658  1.00 96.92  ? 445 LYS B O     1 
ATOM   7531 C  CB    . LYS B 1 418 ? 58.592  -0.208  45.809  1.00 92.01  ? 445 LYS B CB    1 
ATOM   7532 C  CG    . LYS B 1 418 ? 59.741  -1.144  46.114  1.00 96.71  ? 445 LYS B CG    1 
ATOM   7533 C  CD    . LYS B 1 418 ? 60.660  -0.553  47.168  1.00 96.14  ? 445 LYS B CD    1 
ATOM   7534 C  CE    . LYS B 1 418 ? 61.782  -1.513  47.513  1.00 93.46  ? 445 LYS B CE    1 
ATOM   7535 N  NZ    . LYS B 1 418 ? 62.676  -0.956  48.561  1.00 103.74 ? 445 LYS B NZ    1 
ATOM   7536 N  N     . ARG B 1 419 ? 56.013  -1.941  46.083  1.00 98.33  ? 446 ARG B N     1 
ATOM   7537 C  CA    . ARG B 1 419 ? 55.336  -3.153  46.537  1.00 92.59  ? 446 ARG B CA    1 
ATOM   7538 C  C     . ARG B 1 419 ? 54.514  -3.784  45.419  1.00 96.21  ? 446 ARG B C     1 
ATOM   7539 O  O     . ARG B 1 419 ? 54.435  -5.013  45.319  1.00 106.83 ? 446 ARG B O     1 
ATOM   7540 C  CB    . ARG B 1 419 ? 54.443  -2.850  47.744  1.00 92.41  ? 446 ARG B CB    1 
ATOM   7541 C  CG    . ARG B 1 419 ? 55.111  -3.032  49.101  1.00 89.21  ? 446 ARG B CG    1 
ATOM   7542 C  CD    . ARG B 1 419 ? 54.082  -3.031  50.228  1.00 90.60  ? 446 ARG B CD    1 
ATOM   7543 N  NE    . ARG B 1 419 ? 53.422  -1.740  50.376  1.00 93.14  ? 446 ARG B NE    1 
ATOM   7544 C  CZ    . ARG B 1 419 ? 52.396  -1.504  51.184  1.00 97.46  ? 446 ARG B CZ    1 
ATOM   7545 N  NH1   . ARG B 1 419 ? 51.862  -2.462  51.925  1.00 103.62 ? 446 ARG B NH1   1 
ATOM   7546 N  NH2   . ARG B 1 419 ? 51.893  -0.274  51.250  1.00 93.74  ? 446 ARG B NH2   1 
ATOM   7547 N  N     . ARG B 1 420 ? 53.902  -2.962  44.562  1.00 92.88  ? 447 ARG B N     1 
ATOM   7548 C  CA    . ARG B 1 420 ? 52.979  -3.497  43.564  1.00 99.98  ? 447 ARG B CA    1 
ATOM   7549 C  C     . ARG B 1 420 ? 53.713  -4.274  42.478  1.00 104.32 ? 447 ARG B C     1 
ATOM   7550 O  O     . ARG B 1 420 ? 53.263  -5.353  42.073  1.00 104.87 ? 447 ARG B O     1 
ATOM   7551 C  CB    . ARG B 1 420 ? 52.142  -2.369  42.959  1.00 98.38  ? 447 ARG B CB    1 
ATOM   7552 C  CG    . ARG B 1 420 ? 51.007  -1.908  43.866  1.00 92.01  ? 447 ARG B CG    1 
ATOM   7553 C  CD    . ARG B 1 420 ? 50.425  -0.580  43.423  1.00 90.23  ? 447 ARG B CD    1 
ATOM   7554 N  NE    . ARG B 1 420 ? 49.566  -0.713  42.254  1.00 103.30 ? 447 ARG B NE    1 
ATOM   7555 C  CZ    . ARG B 1 420 ? 48.849  0.276   41.737  1.00 109.77 ? 447 ARG B CZ    1 
ATOM   7556 N  NH1   . ARG B 1 420 ? 48.871  1.493   42.259  1.00 95.49  ? 447 ARG B NH1   1 
ATOM   7557 N  NH2   . ARG B 1 420 ? 48.089  0.038   40.671  1.00 120.26 ? 447 ARG B NH2   1 
ATOM   7558 N  N     . LEU B 1 421 ? 54.843  -3.751  41.996  1.00 103.40 ? 448 LEU B N     1 
ATOM   7559 C  CA    . LEU B 1 421 ? 55.594  -4.470  40.971  1.00 105.43 ? 448 LEU B CA    1 
ATOM   7560 C  C     . LEU B 1 421 ? 56.289  -5.696  41.553  1.00 105.57 ? 448 LEU B C     1 
ATOM   7561 O  O     . LEU B 1 421 ? 56.352  -6.746  40.903  1.00 101.92 ? 448 LEU B O     1 
ATOM   7562 C  CB    . LEU B 1 421 ? 56.611  -3.543  40.302  1.00 99.61  ? 448 LEU B CB    1 
ATOM   7563 C  CG    . LEU B 1 421 ? 57.366  -4.155  39.113  1.00 100.45 ? 448 LEU B CG    1 
ATOM   7564 C  CD1   . LEU B 1 421 ? 56.398  -4.629  38.037  1.00 92.83  ? 448 LEU B CD1   1 
ATOM   7565 C  CD2   . LEU B 1 421 ? 58.381  -3.179  38.528  1.00 89.94  ? 448 LEU B CD2   1 
ATOM   7566 N  N     . MET B 1 422 ? 56.811  -5.585  42.779  1.00 104.32 ? 449 MET B N     1 
ATOM   7567 C  CA    . MET B 1 422 ? 57.502  -6.716  43.392  1.00 106.77 ? 449 MET B CA    1 
ATOM   7568 C  C     . MET B 1 422 ? 56.556  -7.882  43.644  1.00 114.38 ? 449 MET B C     1 
ATOM   7569 O  O     . MET B 1 422 ? 56.967  -9.045  43.554  1.00 119.27 ? 449 MET B O     1 
ATOM   7570 C  CB    . MET B 1 422 ? 58.174  -6.286  44.696  1.00 97.55  ? 449 MET B CB    1 
ATOM   7571 C  CG    . MET B 1 422 ? 59.515  -5.595  44.496  1.00 98.37  ? 449 MET B CG    1 
ATOM   7572 S  SD    . MET B 1 422 ? 60.387  -5.296  46.043  1.00 119.55 ? 449 MET B SD    1 
ATOM   7573 C  CE    . MET B 1 422 ? 60.403  -6.941  46.756  1.00 129.34 ? 449 MET B CE    1 
ATOM   7574 N  N     . ASN B 1 423 ? 55.292  -7.594  43.957  1.00 117.32 ? 450 ASN B N     1 
ATOM   7575 C  CA    . ASN B 1 423 ? 54.305  -8.649  44.140  1.00 122.24 ? 450 ASN B CA    1 
ATOM   7576 C  C     . ASN B 1 423 ? 53.830  -9.237  42.819  1.00 125.48 ? 450 ASN B C     1 
ATOM   7577 O  O     . ASN B 1 423 ? 53.304  -10.355 42.807  1.00 131.92 ? 450 ASN B O     1 
ATOM   7578 C  CB    . ASN B 1 423 ? 53.116  -8.121  44.944  1.00 113.98 ? 450 ASN B CB    1 
ATOM   7579 C  CG    . ASN B 1 423 ? 53.513  -7.671  46.335  1.00 107.53 ? 450 ASN B CG    1 
ATOM   7580 O  OD1   . ASN B 1 423 ? 54.585  -8.020  46.828  1.00 112.49 ? 450 ASN B OD1   1 
ATOM   7581 N  ND2   . ASN B 1 423 ? 52.653  -6.887  46.974  1.00 105.41 ? 450 ASN B ND2   1 
ATOM   7582 N  N     . LEU B 1 424 ? 53.999  -8.516  41.710  1.00 114.70 ? 451 LEU B N     1 
ATOM   7583 C  CA    . LEU B 1 424 ? 53.777  -9.129  40.406  1.00 115.47 ? 451 LEU B CA    1 
ATOM   7584 C  C     . LEU B 1 424 ? 54.937  -10.040 40.030  1.00 116.88 ? 451 LEU B C     1 
ATOM   7585 O  O     . LEU B 1 424 ? 54.725  -11.128 39.485  1.00 115.98 ? 451 LEU B O     1 
ATOM   7586 C  CB    . LEU B 1 424 ? 53.580  -8.056  39.336  1.00 98.71  ? 451 LEU B CB    1 
ATOM   7587 C  CG    . LEU B 1 424 ? 53.262  -8.607  37.944  1.00 100.52 ? 451 LEU B CG    1 
ATOM   7588 C  CD1   . LEU B 1 424 ? 51.855  -9.180  37.904  1.00 103.15 ? 451 LEU B CD1   1 
ATOM   7589 C  CD2   . LEU B 1 424 ? 53.438  -7.542  36.885  1.00 108.49 ? 451 LEU B CD2   1 
ATOM   7590 N  N     . MET B 1 425 ? 56.167  -9.615  40.329  1.00 110.74 ? 452 MET B N     1 
ATOM   7591 C  CA    . MET B 1 425 ? 57.334  -10.426 40.001  1.00 113.66 ? 452 MET B CA    1 
ATOM   7592 C  C     . MET B 1 425 ? 57.401  -11.693 40.848  1.00 125.56 ? 452 MET B C     1 
ATOM   7593 O  O     . MET B 1 425 ? 57.936  -12.712 40.394  1.00 106.90 ? 452 MET B O     1 
ATOM   7594 C  CB    . MET B 1 425 ? 58.608  -9.598  40.166  1.00 98.94  ? 452 MET B CB    1 
ATOM   7595 C  CG    . MET B 1 425 ? 58.650  -8.368  39.277  1.00 113.17 ? 452 MET B CG    1 
ATOM   7596 S  SD    . MET B 1 425 ? 58.454  -8.742  37.520  1.00 121.84 ? 452 MET B SD    1 
ATOM   7597 C  CE    . MET B 1 425 ? 60.040  -9.480  37.141  1.00 99.77  ? 452 MET B CE    1 
ATOM   7598 N  N     . ARG B 1 426 ? 56.871  -11.656 42.073  1.00 124.53 ? 453 ARG B N     1 
ATOM   7599 C  CA    . ARG B 1 426 ? 56.758  -12.878 42.854  1.00 129.26 ? 453 ARG B CA    1 
ATOM   7600 C  C     . ARG B 1 426 ? 55.568  -13.722 42.416  1.00 130.52 ? 453 ARG B C     1 
ATOM   7601 O  O     . ARG B 1 426 ? 55.527  -14.918 42.720  1.00 130.10 ? 453 ARG B O     1 
ATOM   7602 C  CB    . ARG B 1 426 ? 56.653  -12.550 44.347  1.00 127.08 ? 453 ARG B CB    1 
ATOM   7603 C  CG    . ARG B 1 426 ? 57.440  -13.507 45.237  1.00 133.90 ? 453 ARG B CG    1 
ATOM   7604 C  CD    . ARG B 1 426 ? 57.615  -12.969 46.655  1.00 139.04 ? 453 ARG B CD    1 
ATOM   7605 N  NE    . ARG B 1 426 ? 58.132  -11.604 46.677  1.00 149.19 ? 453 ARG B NE    1 
ATOM   7606 C  CZ    . ARG B 1 426 ? 57.507  -10.570 47.227  1.00 148.21 ? 453 ARG B CZ    1 
ATOM   7607 N  NH1   . ARG B 1 426 ? 56.348  -10.713 47.852  1.00 131.44 ? 453 ARG B NH1   1 
ATOM   7608 N  NH2   . ARG B 1 426 ? 58.064  -9.363  47.157  1.00 128.51 ? 453 ARG B NH2   1 
ATOM   7609 N  N     . ASP B 1 427 ? 54.605  -13.130 41.701  1.00 124.80 ? 454 ASP B N     1 
ATOM   7610 C  CA    . ASP B 1 427 ? 53.506  -13.907 41.134  1.00 121.35 ? 454 ASP B CA    1 
ATOM   7611 C  C     . ASP B 1 427 ? 53.881  -14.503 39.783  1.00 121.80 ? 454 ASP B C     1 
ATOM   7612 O  O     . ASP B 1 427 ? 53.555  -15.660 39.502  1.00 131.44 ? 454 ASP B O     1 
ATOM   7613 C  CB    . ASP B 1 427 ? 52.255  -13.037 40.996  1.00 120.88 ? 454 ASP B CB    1 
ATOM   7614 C  CG    . ASP B 1 427 ? 51.487  -12.904 42.295  1.00 134.67 ? 454 ASP B CG    1 
ATOM   7615 O  OD1   . ASP B 1 427 ? 51.994  -13.372 43.337  1.00 137.64 ? 454 ASP B OD1   1 
ATOM   7616 O  OD2   . ASP B 1 427 ? 50.372  -12.340 42.270  1.00 126.86 ? 454 ASP B OD2   1 
ATOM   7617 N  N     . VAL B 1 428 ? 54.563  -13.728 38.936  1.00 124.89 ? 455 VAL B N     1 
ATOM   7618 C  CA    . VAL B 1 428 ? 55.016  -14.248 37.649  1.00 117.62 ? 455 VAL B CA    1 
ATOM   7619 C  C     . VAL B 1 428 ? 55.998  -15.395 37.856  1.00 133.98 ? 455 VAL B C     1 
ATOM   7620 O  O     . VAL B 1 428 ? 55.974  -16.395 37.127  1.00 139.75 ? 455 VAL B O     1 
ATOM   7621 C  CB    . VAL B 1 428 ? 55.634  -13.116 36.804  1.00 110.81 ? 455 VAL B CB    1 
ATOM   7622 C  CG1   . VAL B 1 428 ? 56.261  -13.676 35.546  1.00 115.64 ? 455 VAL B CG1   1 
ATOM   7623 C  CG2   . VAL B 1 428 ? 54.583  -12.080 36.444  1.00 108.90 ? 455 VAL B CG2   1 
ATOM   7624 N  N     . GLU B 1 429 ? 56.868  -15.275 38.863  1.00 137.32 ? 456 GLU B N     1 
ATOM   7625 C  CA    . GLU B 1 429 ? 57.856  -16.317 39.124  1.00 138.01 ? 456 GLU B CA    1 
ATOM   7626 C  C     . GLU B 1 429 ? 57.203  -17.590 39.647  1.00 145.63 ? 456 GLU B C     1 
ATOM   7627 O  O     . GLU B 1 429 ? 57.562  -18.697 39.227  1.00 147.77 ? 456 GLU B O     1 
ATOM   7628 C  CB    . GLU B 1 429 ? 58.895  -15.812 40.122  1.00 136.27 ? 456 GLU B CB    1 
ATOM   7629 C  CG    . GLU B 1 429 ? 59.932  -16.848 40.514  1.00 151.92 ? 456 GLU B CG    1 
ATOM   7630 C  CD    . GLU B 1 429 ? 60.707  -16.451 41.752  1.00 164.75 ? 456 GLU B CD    1 
ATOM   7631 O  OE1   . GLU B 1 429 ? 60.070  -16.018 42.736  1.00 177.12 ? 456 GLU B OE1   1 
ATOM   7632 O  OE2   . GLU B 1 429 ? 61.951  -16.565 41.739  1.00 169.60 ? 456 GLU B OE2   1 
ATOM   7633 N  N     . ARG B 1 430 ? 56.245  -17.458 40.566  1.00 144.62 ? 457 ARG B N     1 
ATOM   7634 C  CA    . ARG B 1 430 ? 55.637  -18.633 41.177  1.00 143.13 ? 457 ARG B CA    1 
ATOM   7635 C  C     . ARG B 1 430 ? 54.808  -19.441 40.183  1.00 151.10 ? 457 ARG B C     1 
ATOM   7636 O  O     . ARG B 1 430 ? 54.442  -20.581 40.492  1.00 165.71 ? 457 ARG B O     1 
ATOM   7637 C  CB    . ARG B 1 430 ? 54.781  -18.204 42.376  1.00 147.74 ? 457 ARG B CB    1 
ATOM   7638 C  CG    . ARG B 1 430 ? 54.469  -19.321 43.366  1.00 142.49 ? 457 ARG B CG    1 
ATOM   7639 C  CD    . ARG B 1 430 ? 53.708  -18.811 44.588  1.00 127.55 ? 457 ARG B CD    1 
ATOM   7640 N  NE    . ARG B 1 430 ? 54.517  -17.939 45.435  1.00 136.95 ? 457 ARG B NE    1 
ATOM   7641 C  CZ    . ARG B 1 430 ? 54.364  -16.624 45.528  1.00 148.57 ? 457 ARG B CZ    1 
ATOM   7642 N  NH1   . ARG B 1 430 ? 53.434  -15.984 44.838  1.00 147.79 ? 457 ARG B NH1   1 
ATOM   7643 N  NH2   . ARG B 1 430 ? 55.160  -15.933 46.342  1.00 122.65 ? 457 ARG B NH2   1 
ATOM   7644 N  N     . GLU B 1 431 ? 54.521  -18.895 38.999  1.00 153.76 ? 458 GLU B N     1 
ATOM   7645 C  CA    . GLU B 1 431 ? 53.737  -19.589 37.986  1.00 155.29 ? 458 GLU B CA    1 
ATOM   7646 C  C     . GLU B 1 431 ? 54.571  -20.088 36.815  1.00 147.59 ? 458 GLU B C     1 
ATOM   7647 O  O     . GLU B 1 431 ? 54.017  -20.716 35.906  1.00 159.72 ? 458 GLU B O     1 
ATOM   7648 C  CB    . GLU B 1 431 ? 52.617  -18.678 37.471  1.00 155.40 ? 458 GLU B CB    1 
ATOM   7649 C  CG    . GLU B 1 431 ? 51.716  -18.144 38.569  1.00 163.62 ? 458 GLU B CG    1 
ATOM   7650 C  CD    . GLU B 1 431 ? 51.199  -19.241 39.478  1.00 169.63 ? 458 GLU B CD    1 
ATOM   7651 O  OE1   . GLU B 1 431 ? 50.624  -20.222 38.961  1.00 163.40 ? 458 GLU B OE1   1 
ATOM   7652 O  OE2   . GLU B 1 431 ? 51.377  -19.125 40.708  1.00 175.75 ? 458 GLU B OE2   1 
ATOM   7653 N  N     . GLY B 1 432 ? 55.876  -19.829 36.808  1.00 139.18 ? 459 GLY B N     1 
ATOM   7654 C  CA    . GLY B 1 432 ? 56.731  -20.316 35.734  1.00 149.39 ? 459 GLY B CA    1 
ATOM   7655 C  C     . GLY B 1 432 ? 56.358  -19.792 34.365  1.00 153.70 ? 459 GLY B C     1 
ATOM   7656 O  O     . GLY B 1 432 ? 56.427  -20.533 33.375  1.00 146.63 ? 459 GLY B O     1 
ATOM   7657 N  N     . LEU B 1 433 ? 55.963  -18.524 34.284  1.00 142.43 ? 460 LEU B N     1 
ATOM   7658 C  CA    . LEU B 1 433 ? 55.502  -17.959 33.025  1.00 136.79 ? 460 LEU B CA    1 
ATOM   7659 C  C     . LEU B 1 433 ? 56.678  -17.729 32.082  1.00 143.34 ? 460 LEU B C     1 
ATOM   7660 O  O     . LEU B 1 433 ? 57.673  -17.099 32.454  1.00 142.78 ? 460 LEU B O     1 
ATOM   7661 C  CB    . LEU B 1 433 ? 54.757  -16.650 33.284  1.00 137.87 ? 460 LEU B CB    1 
ATOM   7662 C  CG    . LEU B 1 433 ? 53.962  -16.038 32.128  1.00 142.49 ? 460 LEU B CG    1 
ATOM   7663 C  CD1   . LEU B 1 433 ? 52.893  -17.006 31.637  1.00 138.07 ? 460 LEU B CD1   1 
ATOM   7664 C  CD2   . LEU B 1 433 ? 53.341  -14.711 32.548  1.00 134.87 ? 460 LEU B CD2   1 
ATOM   7665 N  N     . ASP B 1 434 ? 56.565  -18.252 30.862  1.00 146.75 ? 461 ASP B N     1 
ATOM   7666 C  CA    . ASP B 1 434 ? 57.563  -18.043 29.812  1.00 151.95 ? 461 ASP B CA    1 
ATOM   7667 C  C     . ASP B 1 434 ? 57.334  -16.655 29.224  1.00 156.52 ? 461 ASP B C     1 
ATOM   7668 O  O     . ASP B 1 434 ? 56.559  -16.474 28.283  1.00 166.50 ? 461 ASP B O     1 
ATOM   7669 C  CB    . ASP B 1 434 ? 57.460  -19.134 28.750  1.00 153.39 ? 461 ASP B CB    1 
ATOM   7670 C  CG    . ASP B 1 434 ? 58.527  -19.017 27.672  1.00 158.77 ? 461 ASP B CG    1 
ATOM   7671 O  OD1   . ASP B 1 434 ? 59.502  -18.261 27.869  1.00 160.35 ? 461 ASP B OD1   1 
ATOM   7672 O  OD2   . ASP B 1 434 ? 58.388  -19.683 26.622  1.00 159.12 ? 461 ASP B OD2   1 
ATOM   7673 N  N     . TRP B 1 435 ? 58.014  -15.657 29.788  1.00 145.58 ? 462 TRP B N     1 
ATOM   7674 C  CA    . TRP B 1 435 ? 57.816  -14.266 29.410  1.00 143.30 ? 462 TRP B CA    1 
ATOM   7675 C  C     . TRP B 1 435 ? 59.129  -13.640 28.957  1.00 135.34 ? 462 TRP B C     1 
ATOM   7676 O  O     . TRP B 1 435 ? 60.214  -14.050 29.379  1.00 126.45 ? 462 TRP B O     1 
ATOM   7677 C  CB    . TRP B 1 435 ? 57.230  -13.448 30.575  1.00 137.76 ? 462 TRP B CB    1 
ATOM   7678 C  CG    . TRP B 1 435 ? 58.163  -13.304 31.737  1.00 132.39 ? 462 TRP B CG    1 
ATOM   7679 C  CD1   . TRP B 1 435 ? 58.273  -14.140 32.809  1.00 123.88 ? 462 TRP B CD1   1 
ATOM   7680 C  CD2   . TRP B 1 435 ? 59.123  -12.259 31.942  1.00 127.17 ? 462 TRP B CD2   1 
ATOM   7681 N  NE1   . TRP B 1 435 ? 59.241  -13.682 33.669  1.00 114.29 ? 462 TRP B NE1   1 
ATOM   7682 C  CE2   . TRP B 1 435 ? 59.779  -12.530 33.159  1.00 112.30 ? 462 TRP B CE2   1 
ATOM   7683 C  CE3   . TRP B 1 435 ? 59.491  -11.122 31.213  1.00 126.29 ? 462 TRP B CE3   1 
ATOM   7684 C  CZ2   . TRP B 1 435 ? 60.782  -11.706 33.664  1.00 112.22 ? 462 TRP B CZ2   1 
ATOM   7685 C  CZ3   . TRP B 1 435 ? 60.486  -10.306 31.716  1.00 118.03 ? 462 TRP B CZ3   1 
ATOM   7686 C  CH2   . TRP B 1 435 ? 61.120  -10.602 32.930  1.00 127.27 ? 462 TRP B CH2   1 
ATOM   7687 N  N     . ASP B 1 436 ? 59.013  -12.631 28.096  1.00 133.91 ? 463 ASP B N     1 
ATOM   7688 C  CA    . ASP B 1 436 ? 60.150  -11.886 27.567  1.00 121.84 ? 463 ASP B CA    1 
ATOM   7689 C  C     . ASP B 1 436 ? 60.107  -10.406 27.907  1.00 119.71 ? 463 ASP B C     1 
ATOM   7690 O  O     . ASP B 1 436 ? 61.149  -9.815  28.201  1.00 114.70 ? 463 ASP B O     1 
ATOM   7691 C  CB    . ASP B 1 436 ? 60.227  -12.042 26.037  1.00 125.87 ? 463 ASP B CB    1 
ATOM   7692 C  CG    . ASP B 1 436 ? 60.378  -13.485 25.599  1.00 138.35 ? 463 ASP B CG    1 
ATOM   7693 O  OD1   . ASP B 1 436 ? 61.068  -14.253 26.300  1.00 141.94 ? 463 ASP B OD1   1 
ATOM   7694 O  OD2   . ASP B 1 436 ? 59.806  -13.851 24.550  1.00 148.64 ? 463 ASP B OD2   1 
ATOM   7695 N  N     . LEU B 1 437 ? 58.926  -9.791  27.877  1.00 119.65 ? 464 LEU B N     1 
ATOM   7696 C  CA    . LEU B 1 437 ? 58.793  -8.345  28.014  1.00 114.32 ? 464 LEU B CA    1 
ATOM   7697 C  C     . LEU B 1 437 ? 57.534  -8.041  28.812  1.00 122.87 ? 464 LEU B C     1 
ATOM   7698 O  O     . LEU B 1 437 ? 56.426  -8.335  28.355  1.00 129.56 ? 464 LEU B O     1 
ATOM   7699 C  CB    . LEU B 1 437 ? 58.732  -7.677  26.636  1.00 110.04 ? 464 LEU B CB    1 
ATOM   7700 C  CG    . LEU B 1 437 ? 58.815  -6.152  26.550  1.00 126.35 ? 464 LEU B CG    1 
ATOM   7701 C  CD1   . LEU B 1 437 ? 60.216  -5.681  26.883  1.00 116.19 ? 464 LEU B CD1   1 
ATOM   7702 C  CD2   . LEU B 1 437 ? 58.401  -5.668  25.165  1.00 131.76 ? 464 LEU B CD2   1 
ATOM   7703 N  N     . ILE B 1 438 ? 57.696  -7.454  29.993  1.00 118.47 ? 465 ILE B N     1 
ATOM   7704 C  CA    . ILE B 1 438 ? 56.570  -7.068  30.838  1.00 115.66 ? 465 ILE B CA    1 
ATOM   7705 C  C     . ILE B 1 438 ? 56.511  -5.547  30.866  1.00 115.89 ? 465 ILE B C     1 
ATOM   7706 O  O     . ILE B 1 438 ? 57.413  -4.888  31.397  1.00 110.03 ? 465 ILE B O     1 
ATOM   7707 C  CB    . ILE B 1 438 ? 56.682  -7.652  32.251  1.00 117.77 ? 465 ILE B CB    1 
ATOM   7708 C  CG1   . ILE B 1 438 ? 56.560  -9.177  32.197  1.00 120.32 ? 465 ILE B CG1   1 
ATOM   7709 C  CG2   . ILE B 1 438 ? 55.611  -7.058  33.157  1.00 111.63 ? 465 ILE B CG2   1 
ATOM   7710 C  CD1   . ILE B 1 438 ? 56.425  -9.831  33.551  1.00 117.36 ? 465 ILE B CD1   1 
ATOM   7711 N  N     . TYR B 1 439 ? 55.444  -4.991  30.294  1.00 123.96 ? 466 TYR B N     1 
ATOM   7712 C  CA    . TYR B 1 439 ? 55.277  -3.546  30.225  1.00 110.53 ? 466 TYR B CA    1 
ATOM   7713 C  C     . TYR B 1 439 ? 54.886  -2.992  31.589  1.00 114.65 ? 466 TYR B C     1 
ATOM   7714 O  O     . TYR B 1 439 ? 53.862  -3.387  32.157  1.00 115.86 ? 466 TYR B O     1 
ATOM   7715 C  CB    . TYR B 1 439 ? 54.212  -3.186  29.192  1.00 116.99 ? 466 TYR B CB    1 
ATOM   7716 C  CG    . TYR B 1 439 ? 54.700  -3.123  27.762  1.00 123.78 ? 466 TYR B CG    1 
ATOM   7717 C  CD1   . TYR B 1 439 ? 55.266  -1.962  27.252  1.00 120.48 ? 466 TYR B CD1   1 
ATOM   7718 C  CD2   . TYR B 1 439 ? 54.575  -4.216  26.915  1.00 124.07 ? 466 TYR B CD2   1 
ATOM   7719 C  CE1   . TYR B 1 439 ? 55.703  -1.894  25.943  1.00 123.05 ? 466 TYR B CE1   1 
ATOM   7720 C  CE2   . TYR B 1 439 ? 55.011  -4.157  25.604  1.00 129.58 ? 466 TYR B CE2   1 
ATOM   7721 C  CZ    . TYR B 1 439 ? 55.573  -2.994  25.124  1.00 120.90 ? 466 TYR B CZ    1 
ATOM   7722 O  OH    . TYR B 1 439 ? 56.006  -2.930  23.820  1.00 130.01 ? 466 TYR B OH    1 
ATOM   7723 N  N     . VAL B 1 440 ? 55.697  -2.069  32.111  1.00 113.83 ? 467 VAL B N     1 
ATOM   7724 C  CA    . VAL B 1 440 ? 55.317  -1.314  33.301  1.00 105.86 ? 467 VAL B CA    1 
ATOM   7725 C  C     . VAL B 1 440 ? 54.622  -0.003  32.938  1.00 107.28 ? 467 VAL B C     1 
ATOM   7726 O  O     . VAL B 1 440 ? 53.854  0.529   33.753  1.00 102.02 ? 467 VAL B O     1 
ATOM   7727 C  CB    . VAL B 1 440 ? 56.548  -1.048  34.190  1.00 93.48  ? 467 VAL B CB    1 
ATOM   7728 C  CG1   . VAL B 1 440 ? 56.131  -0.526  35.555  1.00 106.62 ? 467 VAL B CG1   1 
ATOM   7729 C  CG2   . VAL B 1 440 ? 57.378  -2.315  34.342  1.00 94.30  ? 467 VAL B CG2   1 
ATOM   7730 N  N     . GLY B 1 441 ? 54.854  0.520   31.734  1.00 106.77 ? 468 GLY B N     1 
ATOM   7731 C  CA    . GLY B 1 441 ? 54.200  1.727   31.266  1.00 105.91 ? 468 GLY B CA    1 
ATOM   7732 C  C     . GLY B 1 441 ? 54.221  1.852   29.755  1.00 119.20 ? 468 GLY B C     1 
ATOM   7733 O  O     . GLY B 1 441 ? 55.296  1.877   29.147  1.00 130.86 ? 468 GLY B O     1 
ATOM   7734 N  N     . ARG B 1 442 ? 53.046  1.936   29.136  1.00 120.16 ? 469 ARG B N     1 
ATOM   7735 C  CA    . ARG B 1 442 ? 52.927  1.947   27.682  1.00 124.67 ? 469 ARG B CA    1 
ATOM   7736 C  C     . ARG B 1 442 ? 51.698  2.763   27.298  1.00 133.54 ? 469 ARG B C     1 
ATOM   7737 O  O     . ARG B 1 442 ? 51.058  3.392   28.146  1.00 136.11 ? 469 ARG B O     1 
ATOM   7738 C  CB    . ARG B 1 442 ? 52.843  0.515   27.139  1.00 125.70 ? 469 ARG B CB    1 
ATOM   7739 C  CG    . ARG B 1 442 ? 51.900  -0.366  27.940  1.00 120.31 ? 469 ARG B CG    1 
ATOM   7740 C  CD    . ARG B 1 442 ? 51.109  -1.314  27.063  1.00 118.77 ? 469 ARG B CD    1 
ATOM   7741 N  NE    . ARG B 1 442 ? 50.063  -1.986  27.824  1.00 129.71 ? 469 ARG B NE    1 
ATOM   7742 C  CZ    . ARG B 1 442 ? 49.128  -2.764  27.295  1.00 137.12 ? 469 ARG B CZ    1 
ATOM   7743 N  NH1   . ARG B 1 442 ? 49.077  -2.996  25.994  1.00 144.57 ? 469 ARG B NH1   1 
ATOM   7744 N  NH2   . ARG B 1 442 ? 48.220  -3.320  28.092  1.00 140.46 ? 469 ARG B NH2   1 
ATOM   7745 N  N     . LYS B 1 443 ? 51.367  2.750   26.007  1.00 139.69 ? 470 LYS B N     1 
ATOM   7746 C  CA    . LYS B 1 443 ? 50.140  3.353   25.487  1.00 143.09 ? 470 LYS B CA    1 
ATOM   7747 C  C     . LYS B 1 443 ? 49.339  2.245   24.810  1.00 148.51 ? 470 LYS B C     1 
ATOM   7748 O  O     . LYS B 1 443 ? 49.599  1.899   23.654  1.00 153.05 ? 470 LYS B O     1 
ATOM   7749 C  CB    . LYS B 1 443 ? 50.439  4.495   24.518  1.00 143.32 ? 470 LYS B CB    1 
ATOM   7750 C  CG    . LYS B 1 443 ? 49.203  5.278   24.089  1.00 142.88 ? 470 LYS B CG    1 
ATOM   7751 C  CD    . LYS B 1 443 ? 49.562  6.427   23.157  1.00 143.51 ? 470 LYS B CD    1 
ATOM   7752 C  CE    . LYS B 1 443 ? 48.366  7.329   22.897  1.00 131.41 ? 470 LYS B CE    1 
ATOM   7753 N  NZ    . LYS B 1 443 ? 48.723  8.483   22.028  1.00 130.96 ? 470 LYS B NZ    1 
ATOM   7754 N  N     . ARG B 1 444 ? 48.372  1.690   25.536  1.00 149.98 ? 471 ARG B N     1 
ATOM   7755 C  CA    . ARG B 1 444 ? 47.546  0.611   25.009  1.00 152.02 ? 471 ARG B CA    1 
ATOM   7756 C  C     . ARG B 1 444 ? 46.718  1.106   23.829  1.00 153.55 ? 471 ARG B C     1 
ATOM   7757 O  O     . ARG B 1 444 ? 45.897  2.017   23.972  1.00 157.66 ? 471 ARG B O     1 
ATOM   7758 C  CB    . ARG B 1 444 ? 46.642  0.072   26.117  1.00 151.20 ? 471 ARG B CB    1 
ATOM   7759 C  CG    . ARG B 1 444 ? 45.646  -0.983  25.682  1.00 154.55 ? 471 ARG B CG    1 
ATOM   7760 C  CD    . ARG B 1 444 ? 44.798  -1.420  26.865  1.00 150.87 ? 471 ARG B CD    1 
ATOM   7761 N  NE    . ARG B 1 444 ? 43.694  -2.285  26.468  1.00 156.14 ? 471 ARG B NE    1 
ATOM   7762 C  CZ    . ARG B 1 444 ? 42.782  -2.762  27.304  1.00 156.81 ? 471 ARG B CZ    1 
ATOM   7763 N  NH1   . ARG B 1 444 ? 42.817  -2.484  28.597  1.00 158.39 ? 471 ARG B NH1   1 
ATOM   7764 N  NH2   . ARG B 1 444 ? 41.811  -3.537  26.832  1.00 165.72 ? 471 ARG B NH2   1 
ATOM   7765 N  N     . MET B 1 445 ? 46.940  0.506   22.658  1.00 155.17 ? 472 MET B N     1 
ATOM   7766 C  CA    . MET B 1 445 ? 46.275  0.924   21.431  1.00 150.93 ? 472 MET B CA    1 
ATOM   7767 C  C     . MET B 1 445 ? 45.082  0.052   21.065  1.00 151.99 ? 472 MET B C     1 
ATOM   7768 O  O     . MET B 1 445 ? 44.356  0.390   20.125  1.00 154.52 ? 472 MET B O     1 
ATOM   7769 C  CB    . MET B 1 445 ? 47.270  0.928   20.262  1.00 148.89 ? 472 MET B CB    1 
ATOM   7770 C  CG    . MET B 1 445 ? 48.547  1.720   20.522  1.00 161.14 ? 472 MET B CG    1 
ATOM   7771 S  SD    . MET B 1 445 ? 48.368  3.506   20.331  1.00 153.00 ? 472 MET B SD    1 
ATOM   7772 C  CE    . MET B 1 445 ? 48.325  3.658   18.547  1.00 150.65 ? 472 MET B CE    1 
ATOM   7773 N  N     . GLN B 1 446 ? 44.862  -1.053  21.773  1.00 163.79 ? 473 GLN B N     1 
ATOM   7774 C  CA    . GLN B 1 446 ? 43.765  -1.978  21.495  1.00 172.12 ? 473 GLN B CA    1 
ATOM   7775 C  C     . GLN B 1 446 ? 42.836  -1.968  22.707  1.00 175.60 ? 473 GLN B C     1 
ATOM   7776 O  O     . GLN B 1 446 ? 42.999  -2.763  23.635  1.00 177.75 ? 473 GLN B O     1 
ATOM   7777 C  CB    . GLN B 1 446 ? 44.306  -3.382  21.189  1.00 170.84 ? 473 GLN B CB    1 
ATOM   7778 C  CG    . GLN B 1 446 ? 43.311  -4.316  20.521  1.00 171.66 ? 473 GLN B CG    1 
ATOM   7779 C  CD    . GLN B 1 446 ? 42.350  -4.946  21.504  1.00 178.03 ? 473 GLN B CD    1 
ATOM   7780 O  OE1   . GLN B 1 446 ? 41.154  -5.052  21.238  1.00 186.70 ? 473 GLN B OE1   1 
ATOM   7781 N  NE2   . GLN B 1 446 ? 42.869  -5.374  22.649  1.00 174.51 ? 473 GLN B NE2   1 
ATOM   7782 N  N     . VAL B 1 447 ? 41.857  -1.063  22.694  1.00 178.51 ? 474 VAL B N     1 
ATOM   7783 C  CA    . VAL B 1 447 ? 40.945  -0.872  23.817  1.00 180.57 ? 474 VAL B CA    1 
ATOM   7784 C  C     . VAL B 1 447 ? 39.514  -1.261  23.486  1.00 190.32 ? 474 VAL B C     1 
ATOM   7785 O  O     . VAL B 1 447 ? 38.634  -1.121  24.349  1.00 183.28 ? 474 VAL B O     1 
ATOM   7786 C  CB    . VAL B 1 447 ? 40.991  0.577   24.338  1.00 164.61 ? 474 VAL B CB    1 
ATOM   7787 C  CG1   . VAL B 1 447 ? 42.414  0.962   24.709  1.00 161.08 ? 474 VAL B CG1   1 
ATOM   7788 C  CG2   . VAL B 1 447 ? 40.422  1.534   23.301  1.00 167.66 ? 474 VAL B CG2   1 
ATOM   7789 N  N     . GLU B 1 448 ? 39.246  -1.740  22.270  1.00 201.89 ? 475 GLU B N     1 
ATOM   7790 C  CA    . GLU B 1 448 ? 37.901  -2.172  21.907  1.00 201.32 ? 475 GLU B CA    1 
ATOM   7791 C  C     . GLU B 1 448 ? 37.514  -3.415  22.700  1.00 199.24 ? 475 GLU B C     1 
ATOM   7792 O  O     . GLU B 1 448 ? 36.658  -3.350  23.588  1.00 198.69 ? 475 GLU B O     1 
ATOM   7793 C  CB    . GLU B 1 448 ? 37.802  -2.437  20.402  1.00 200.93 ? 475 GLU B CB    1 
ATOM   7794 C  CG    . GLU B 1 448 ? 37.590  -1.184  19.559  1.00 203.79 ? 475 GLU B CG    1 
ATOM   7795 C  CD    . GLU B 1 448 ? 38.772  -0.234  19.604  1.00 210.59 ? 475 GLU B CD    1 
ATOM   7796 O  OE1   . GLU B 1 448 ? 39.924  -0.713  19.537  1.00 212.33 ? 475 GLU B OE1   1 
ATOM   7797 O  OE2   . GLU B 1 448 ? 38.549  0.990   19.714  1.00 212.01 ? 475 GLU B OE2   1 
ATOM   7798 N  N     . HIS B 1 449 ? 38.133  -4.550  22.383  1.00 196.58 ? 476 HIS B N     1 
ATOM   7799 C  CA    . HIS B 1 449 ? 37.908  -5.676  23.279  1.00 195.02 ? 476 HIS B CA    1 
ATOM   7800 C  C     . HIS B 1 449 ? 39.073  -5.812  24.252  1.00 190.96 ? 476 HIS B C     1 
ATOM   7801 O  O     . HIS B 1 449 ? 40.228  -5.588  23.870  1.00 187.50 ? 476 HIS B O     1 
ATOM   7802 C  CB    . HIS B 1 449 ? 37.731  -6.979  22.493  1.00 191.50 ? 476 HIS B CB    1 
ATOM   7803 C  CG    . HIS B 1 449 ? 38.816  -7.244  21.495  1.00 187.52 ? 476 HIS B CG    1 
ATOM   7804 N  ND1   . HIS B 1 449 ? 39.980  -7.908  21.818  1.00 185.17 ? 476 HIS B ND1   1 
ATOM   7805 C  CD2   . HIS B 1 449 ? 38.907  -6.947  20.176  1.00 185.63 ? 476 HIS B CD2   1 
ATOM   7806 C  CE1   . HIS B 1 449 ? 40.744  -8.003  20.744  1.00 180.04 ? 476 HIS B CE1   1 
ATOM   7807 N  NE2   . HIS B 1 449 ? 40.116  -7.427  19.735  1.00 181.05 ? 476 HIS B NE2   1 
ATOM   7808 N  N     . PRO B 1 450 ? 38.804  -6.161  25.510  1.00 185.73 ? 477 PRO B N     1 
ATOM   7809 C  CA    . PRO B 1 450 ? 39.873  -6.171  26.517  1.00 179.54 ? 477 PRO B CA    1 
ATOM   7810 C  C     . PRO B 1 450 ? 40.966  -7.174  26.176  1.00 183.58 ? 477 PRO B C     1 
ATOM   7811 O  O     . PRO B 1 450 ? 40.703  -8.245  25.624  1.00 188.68 ? 477 PRO B O     1 
ATOM   7812 C  CB    . PRO B 1 450 ? 39.140  -6.549  27.810  1.00 181.85 ? 477 PRO B CB    1 
ATOM   7813 C  CG    . PRO B 1 450 ? 37.894  -7.242  27.355  1.00 174.98 ? 477 PRO B CG    1 
ATOM   7814 C  CD    . PRO B 1 450 ? 37.506  -6.571  26.074  1.00 177.21 ? 477 PRO B CD    1 
ATOM   7815 N  N     . GLU B 1 451 ? 42.203  -6.809  26.505  1.00 177.78 ? 478 GLU B N     1 
ATOM   7816 C  CA    . GLU B 1 451 ? 43.344  -7.670  26.226  1.00 171.51 ? 478 GLU B CA    1 
ATOM   7817 C  C     . GLU B 1 451 ? 43.286  -8.932  27.080  1.00 168.10 ? 478 GLU B C     1 
ATOM   7818 O  O     . GLU B 1 451 ? 42.840  -8.911  28.230  1.00 174.98 ? 478 GLU B O     1 
ATOM   7819 C  CB    . GLU B 1 451 ? 44.652  -6.916  26.471  1.00 168.68 ? 478 GLU B CB    1 
ATOM   7820 C  CG    . GLU B 1 451 ? 44.859  -5.726  25.539  1.00 170.79 ? 478 GLU B CG    1 
ATOM   7821 C  CD    . GLU B 1 451 ? 46.099  -4.918  25.877  1.00 166.17 ? 478 GLU B CD    1 
ATOM   7822 O  OE1   . GLU B 1 451 ? 46.635  -5.077  26.995  1.00 159.98 ? 478 GLU B OE1   1 
ATOM   7823 O  OE2   . GLU B 1 451 ? 46.538  -4.120  25.021  1.00 162.85 ? 478 GLU B OE2   1 
ATOM   7824 N  N     . LYS B 1 452 ? 43.745  -10.040 26.499  1.00 167.01 ? 479 LYS B N     1 
ATOM   7825 C  CA    . LYS B 1 452 ? 43.587  -11.352 27.115  1.00 159.07 ? 479 LYS B CA    1 
ATOM   7826 C  C     . LYS B 1 452 ? 44.357  -11.433 28.428  1.00 151.09 ? 479 LYS B C     1 
ATOM   7827 O  O     . LYS B 1 452 ? 45.585  -11.303 28.448  1.00 150.08 ? 479 LYS B O     1 
ATOM   7828 C  CB    . LYS B 1 452 ? 44.056  -12.436 26.145  1.00 157.32 ? 479 LYS B CB    1 
ATOM   7829 C  CG    . LYS B 1 452 ? 43.577  -13.842 26.483  1.00 157.37 ? 479 LYS B CG    1 
ATOM   7830 C  CD    . LYS B 1 452 ? 43.876  -14.807 25.343  1.00 150.15 ? 479 LYS B CD    1 
ATOM   7831 C  CE    . LYS B 1 452 ? 43.366  -16.204 25.645  1.00 152.79 ? 479 LYS B CE    1 
ATOM   7832 N  NZ    . LYS B 1 452 ? 43.569  -17.135 24.498  1.00 160.04 ? 479 LYS B NZ    1 
ATOM   7833 N  N     . ALA B 1 453 ? 43.631  -11.657 29.522  1.00 150.69 ? 480 ALA B N     1 
ATOM   7834 C  CA    . ALA B 1 453 ? 44.249  -11.710 30.840  1.00 146.09 ? 480 ALA B CA    1 
ATOM   7835 C  C     . ALA B 1 453 ? 45.116  -12.956 30.982  1.00 149.41 ? 480 ALA B C     1 
ATOM   7836 O  O     . ALA B 1 453 ? 44.784  -14.027 30.466  1.00 160.94 ? 480 ALA B O     1 
ATOM   7837 C  CB    . ALA B 1 453 ? 43.178  -11.690 31.931  1.00 144.48 ? 480 ALA B CB    1 
ATOM   7838 N  N     . VAL B 1 454 ? 46.231  -12.810 31.690  1.00 146.05 ? 481 VAL B N     1 
ATOM   7839 C  CA    . VAL B 1 454 ? 47.162  -13.913 31.923  1.00 143.49 ? 481 VAL B CA    1 
ATOM   7840 C  C     . VAL B 1 454 ? 46.671  -14.737 33.107  1.00 148.41 ? 481 VAL B C     1 
ATOM   7841 O  O     . VAL B 1 454 ? 46.558  -14.210 34.224  1.00 151.96 ? 481 VAL B O     1 
ATOM   7842 C  CB    . VAL B 1 454 ? 48.590  -13.398 32.164  1.00 142.82 ? 481 VAL B CB    1 
ATOM   7843 C  CG1   . VAL B 1 454 ? 49.506  -14.543 32.576  1.00 124.39 ? 481 VAL B CG1   1 
ATOM   7844 C  CG2   . VAL B 1 454 ? 49.117  -12.700 30.919  1.00 136.00 ? 481 VAL B CG2   1 
ATOM   7845 N  N     . PRO B 1 455 ? 46.367  -16.019 32.915  1.00 151.05 ? 482 PRO B N     1 
ATOM   7846 C  CA    . PRO B 1 455 ? 45.855  -16.829 34.024  1.00 152.50 ? 482 PRO B CA    1 
ATOM   7847 C  C     . PRO B 1 455 ? 46.911  -17.069 35.091  1.00 152.93 ? 482 PRO B C     1 
ATOM   7848 O  O     . PRO B 1 455 ? 48.109  -17.163 34.809  1.00 152.73 ? 482 PRO B O     1 
ATOM   7849 C  CB    . PRO B 1 455 ? 45.446  -18.144 33.347  1.00 140.79 ? 482 PRO B CB    1 
ATOM   7850 C  CG    . PRO B 1 455 ? 45.311  -17.810 31.896  1.00 141.70 ? 482 PRO B CG    1 
ATOM   7851 C  CD    . PRO B 1 455 ? 46.334  -16.750 31.639  1.00 146.74 ? 482 PRO B CD    1 
ATOM   7852 N  N     . ARG B 1 456 ? 46.442  -17.162 36.336  1.00 153.89 ? 483 ARG B N     1 
ATOM   7853 C  CA    . ARG B 1 456 ? 47.213  -17.468 37.539  1.00 154.21 ? 483 ARG B CA    1 
ATOM   7854 C  C     . ARG B 1 456 ? 48.193  -16.365 37.932  1.00 152.05 ? 483 ARG B C     1 
ATOM   7855 O  O     . ARG B 1 456 ? 48.900  -16.520 38.934  1.00 151.60 ? 483 ARG B O     1 
ATOM   7856 C  CB    . ARG B 1 456 ? 47.970  -18.800 37.422  1.00 152.17 ? 483 ARG B CB    1 
ATOM   7857 C  CG    . ARG B 1 456 ? 47.069  -20.028 37.485  1.00 147.37 ? 483 ARG B CG    1 
ATOM   7858 C  CD    . ARG B 1 456 ? 47.845  -21.315 37.239  1.00 151.32 ? 483 ARG B CD    1 
ATOM   7859 N  NE    . ARG B 1 456 ? 47.685  -21.808 35.876  1.00 158.95 ? 483 ARG B NE    1 
ATOM   7860 C  CZ    . ARG B 1 456 ? 48.435  -21.435 34.847  1.00 170.39 ? 483 ARG B CZ    1 
ATOM   7861 N  NH1   . ARG B 1 456 ? 49.406  -20.545 34.984  1.00 159.19 ? 483 ARG B NH1   1 
ATOM   7862 N  NH2   . ARG B 1 456 ? 48.205  -21.968 33.650  1.00 168.36 ? 483 ARG B NH2   1 
ATOM   7863 N  N     . VAL B 1 457 ? 48.260  -15.261 37.191  1.00 145.81 ? 484 VAL B N     1 
ATOM   7864 C  CA    . VAL B 1 457 ? 49.076  -14.106 37.556  1.00 131.70 ? 484 VAL B CA    1 
ATOM   7865 C  C     . VAL B 1 457 ? 48.158  -12.892 37.570  1.00 134.77 ? 484 VAL B C     1 
ATOM   7866 O  O     . VAL B 1 457 ? 47.748  -12.405 36.508  1.00 128.09 ? 484 VAL B O     1 
ATOM   7867 C  CB    . VAL B 1 457 ? 50.254  -13.885 36.599  1.00 134.34 ? 484 VAL B CB    1 
ATOM   7868 C  CG1   . VAL B 1 457 ? 51.116  -12.738 37.103  1.00 121.98 ? 484 VAL B CG1   1 
ATOM   7869 C  CG2   . VAL B 1 457 ? 51.079  -15.156 36.452  1.00 128.29 ? 484 VAL B CG2   1 
ATOM   7870 N  N     . ARG B 1 458 ? 47.843  -12.399 38.764  1.00 133.57 ? 485 ARG B N     1 
ATOM   7871 C  CA    . ARG B 1 458 ? 46.908  -11.292 38.896  1.00 121.86 ? 485 ARG B CA    1 
ATOM   7872 C  C     . ARG B 1 458 ? 47.541  -9.991  38.415  1.00 115.85 ? 485 ARG B C     1 
ATOM   7873 O  O     . ARG B 1 458 ? 48.753  -9.788  38.519  1.00 112.11 ? 485 ARG B O     1 
ATOM   7874 C  CB    . ARG B 1 458 ? 46.463  -11.153 40.348  1.00 119.18 ? 485 ARG B CB    1 
ATOM   7875 C  CG    . ARG B 1 458 ? 45.198  -10.349 40.553  1.00 134.80 ? 485 ARG B CG    1 
ATOM   7876 C  CD    . ARG B 1 458 ? 44.882  -10.265 42.032  1.00 147.55 ? 485 ARG B CD    1 
ATOM   7877 N  NE    . ARG B 1 458 ? 45.194  -11.522 42.702  1.00 157.02 ? 485 ARG B NE    1 
ATOM   7878 C  CZ    . ARG B 1 458 ? 45.128  -11.713 44.013  1.00 164.71 ? 485 ARG B CZ    1 
ATOM   7879 N  NH1   . ARG B 1 458 ? 44.752  -10.746 44.834  1.00 174.07 ? 485 ARG B NH1   1 
ATOM   7880 N  NH2   . ARG B 1 458 ? 45.450  -12.904 44.511  1.00 147.28 ? 485 ARG B NH2   1 
ATOM   7881 N  N     . ASN B 1 459 ? 46.696  -9.110  37.871  1.00 109.79 ? 486 ASN B N     1 
ATOM   7882 C  CA    . ASN B 1 459 ? 47.116  -7.790  37.398  1.00 120.78 ? 486 ASN B CA    1 
ATOM   7883 C  C     . ASN B 1 459 ? 48.169  -7.890  36.294  1.00 120.65 ? 486 ASN B C     1 
ATOM   7884 O  O     . ASN B 1 459 ? 49.147  -7.140  36.272  1.00 121.22 ? 486 ASN B O     1 
ATOM   7885 C  CB    . ASN B 1 459 ? 47.618  -6.921  38.554  1.00 113.79 ? 486 ASN B CB    1 
ATOM   7886 C  CG    . ASN B 1 459 ? 46.522  -6.584  39.544  1.00 111.46 ? 486 ASN B CG    1 
ATOM   7887 O  OD1   . ASN B 1 459 ? 46.375  -7.244  40.573  1.00 123.51 ? 486 ASN B OD1   1 
ATOM   7888 N  ND2   . ASN B 1 459 ? 45.741  -5.555  39.234  1.00 103.93 ? 486 ASN B ND2   1 
ATOM   7889 N  N     . LEU B 1 460 ? 47.964  -8.821  35.365  1.00 123.41 ? 487 LEU B N     1 
ATOM   7890 C  CA    . LEU B 1 460 ? 48.868  -8.994  34.236  1.00 123.21 ? 487 LEU B CA    1 
ATOM   7891 C  C     . LEU B 1 460 ? 48.060  -9.477  33.042  1.00 126.01 ? 487 LEU B C     1 
ATOM   7892 O  O     . LEU B 1 460 ? 47.259  -10.408 33.171  1.00 124.22 ? 487 LEU B O     1 
ATOM   7893 C  CB    . LEU B 1 460 ? 49.986  -9.990  34.565  1.00 123.11 ? 487 LEU B CB    1 
ATOM   7894 C  CG    . LEU B 1 460 ? 51.074  -10.185 33.507  1.00 110.62 ? 487 LEU B CG    1 
ATOM   7895 C  CD1   . LEU B 1 460 ? 51.895  -8.918  33.340  1.00 115.44 ? 487 LEU B CD1   1 
ATOM   7896 C  CD2   . LEU B 1 460 ? 51.970  -11.359 33.861  1.00 115.29 ? 487 LEU B CD2   1 
ATOM   7897 N  N     . VAL B 1 461 ? 48.265  -8.838  31.889  1.00 125.53 ? 488 VAL B N     1 
ATOM   7898 C  CA    . VAL B 1 461 ? 47.568  -9.194  30.661  1.00 129.41 ? 488 VAL B CA    1 
ATOM   7899 C  C     . VAL B 1 461 ? 48.591  -9.399  29.554  1.00 131.50 ? 488 VAL B C     1 
ATOM   7900 O  O     . VAL B 1 461 ? 49.740  -8.963  29.646  1.00 136.32 ? 488 VAL B O     1 
ATOM   7901 C  CB    . VAL B 1 461 ? 46.535  -8.127  30.237  1.00 122.38 ? 488 VAL B CB    1 
ATOM   7902 C  CG1   . VAL B 1 461 ? 45.457  -7.974  31.298  1.00 125.84 ? 488 VAL B CG1   1 
ATOM   7903 C  CG2   . VAL B 1 461 ? 47.227  -6.799  29.967  1.00 127.07 ? 488 VAL B CG2   1 
ATOM   7904 N  N     . GLU B 1 462 ? 48.153  -10.075 28.495  1.00 130.19 ? 489 GLU B N     1 
ATOM   7905 C  CA    . GLU B 1 462 ? 48.981  -10.261 27.311  1.00 128.04 ? 489 GLU B CA    1 
ATOM   7906 C  C     . GLU B 1 462 ? 49.019  -8.957  26.525  1.00 132.17 ? 489 GLU B C     1 
ATOM   7907 O  O     . GLU B 1 462 ? 47.973  -8.433  26.128  1.00 138.11 ? 489 GLU B O     1 
ATOM   7908 C  CB    . GLU B 1 462 ? 48.440  -11.400 26.452  1.00 132.39 ? 489 GLU B CB    1 
ATOM   7909 C  CG    . GLU B 1 462 ? 48.291  -12.710 27.203  1.00 141.43 ? 489 GLU B CG    1 
ATOM   7910 C  CD    . GLU B 1 462 ? 47.760  -13.826 26.328  1.00 140.91 ? 489 GLU B CD    1 
ATOM   7911 O  OE1   . GLU B 1 462 ? 48.183  -13.916 25.156  1.00 135.40 ? 489 GLU B OE1   1 
ATOM   7912 O  OE2   . GLU B 1 462 ? 46.913  -14.607 26.811  1.00 151.18 ? 489 GLU B OE2   1 
ATOM   7913 N  N     . ALA B 1 463 ? 50.222  -8.434  26.308  1.00 138.35 ? 490 ALA B N     1 
ATOM   7914 C  CA    . ALA B 1 463 ? 50.376  -7.134  25.671  1.00 146.34 ? 490 ALA B CA    1 
ATOM   7915 C  C     . ALA B 1 463 ? 49.957  -7.206  24.208  1.00 153.57 ? 490 ALA B C     1 
ATOM   7916 O  O     . ALA B 1 463 ? 50.565  -7.931  23.414  1.00 149.96 ? 490 ALA B O     1 
ATOM   7917 C  CB    . ALA B 1 463 ? 51.822  -6.656  25.792  1.00 137.22 ? 490 ALA B CB    1 
ATOM   7918 N  N     . ASP B 1 464 ? 48.910  -6.460  23.856  1.00 169.82 ? 491 ASP B N     1 
ATOM   7919 C  CA    . ASP B 1 464 ? 48.548  -6.278  22.457  1.00 171.57 ? 491 ASP B CA    1 
ATOM   7920 C  C     . ASP B 1 464 ? 49.338  -5.102  21.899  1.00 169.63 ? 491 ASP B C     1 
ATOM   7921 O  O     . ASP B 1 464 ? 50.410  -4.780  22.419  1.00 167.19 ? 491 ASP B O     1 
ATOM   7922 C  CB    . ASP B 1 464 ? 47.041  -6.066  22.299  1.00 177.65 ? 491 ASP B CB    1 
ATOM   7923 C  CG    . ASP B 1 464 ? 46.240  -7.317  22.612  1.00 183.60 ? 491 ASP B CG    1 
ATOM   7924 O  OD1   . ASP B 1 464 ? 46.848  -8.343  22.980  1.00 180.58 ? 491 ASP B OD1   1 
ATOM   7925 O  OD2   . ASP B 1 464 ? 44.999  -7.276  22.490  1.00 187.62 ? 491 ASP B OD2   1 
ATOM   7926 N  N     . TYR B 1 465 ? 48.830  -4.451  20.856  1.00 144.28 ? 492 TYR B N     1 
ATOM   7927 C  CA    . TYR B 1 465 ? 49.587  -3.375  20.227  1.00 145.27 ? 492 TYR B CA    1 
ATOM   7928 C  C     . TYR B 1 465 ? 49.789  -2.221  21.203  1.00 148.85 ? 492 TYR B C     1 
ATOM   7929 O  O     . TYR B 1 465 ? 48.824  -1.585  21.641  1.00 148.47 ? 492 TYR B O     1 
ATOM   7930 C  CB    . TYR B 1 465 ? 48.880  -2.891  18.962  1.00 147.06 ? 492 TYR B CB    1 
ATOM   7931 C  CG    . TYR B 1 465 ? 49.675  -1.857  18.193  1.00 154.95 ? 492 TYR B CG    1 
ATOM   7932 C  CD1   . TYR B 1 465 ? 51.029  -2.045  17.937  1.00 144.22 ? 492 TYR B CD1   1 
ATOM   7933 C  CD2   . TYR B 1 465 ? 49.075  -0.698  17.718  1.00 157.36 ? 492 TYR B CD2   1 
ATOM   7934 C  CE1   . TYR B 1 465 ? 51.763  -1.104  17.238  1.00 143.93 ? 492 TYR B CE1   1 
ATOM   7935 C  CE2   . TYR B 1 465 ? 49.801  0.249   17.015  1.00 154.02 ? 492 TYR B CE2   1 
ATOM   7936 C  CZ    . TYR B 1 465 ? 51.145  0.042   16.777  1.00 149.32 ? 492 TYR B CZ    1 
ATOM   7937 O  OH    . TYR B 1 465 ? 51.869  0.981   16.077  1.00 147.79 ? 492 TYR B OH    1 
ATOM   7938 N  N     . SER B 1 466 ? 51.047  -1.969  21.554  1.00 144.54 ? 493 SER B N     1 
ATOM   7939 C  CA    . SER B 1 466 ? 51.453  -0.869  22.416  1.00 145.71 ? 493 SER B CA    1 
ATOM   7940 C  C     . SER B 1 466 ? 52.110  0.213   21.565  1.00 150.76 ? 493 SER B C     1 
ATOM   7941 O  O     . SER B 1 466 ? 52.184  0.108   20.338  1.00 151.52 ? 493 SER B O     1 
ATOM   7942 C  CB    . SER B 1 466 ? 52.394  -1.370  23.513  1.00 145.60 ? 493 SER B CB    1 
ATOM   7943 O  OG    . SER B 1 466 ? 51.838  -2.490  24.180  1.00 135.19 ? 493 SER B OG    1 
ATOM   7944 N  N     . TYR B 1 467 ? 52.601  1.266   22.222  1.00 157.45 ? 494 TYR B N     1 
ATOM   7945 C  CA    . TYR B 1 467 ? 53.124  2.391   21.455  1.00 162.90 ? 494 TYR B CA    1 
ATOM   7946 C  C     . TYR B 1 467 ? 54.254  3.141   22.154  1.00 158.81 ? 494 TYR B C     1 
ATOM   7947 O  O     . TYR B 1 467 ? 54.843  4.052   21.564  1.00 165.67 ? 494 TYR B O     1 
ATOM   7948 C  CB    . TYR B 1 467 ? 51.986  3.362   21.119  1.00 169.80 ? 494 TYR B CB    1 
ATOM   7949 C  CG    . TYR B 1 467 ? 52.257  4.223   19.905  1.00 175.92 ? 494 TYR B CG    1 
ATOM   7950 C  CD1   . TYR B 1 467 ? 52.186  3.690   18.625  1.00 174.61 ? 494 TYR B CD1   1 
ATOM   7951 C  CD2   . TYR B 1 467 ? 52.581  5.569   20.039  1.00 175.00 ? 494 TYR B CD2   1 
ATOM   7952 C  CE1   . TYR B 1 467 ? 52.434  4.469   17.512  1.00 183.39 ? 494 TYR B CE1   1 
ATOM   7953 C  CE2   . TYR B 1 467 ? 52.830  6.356   18.930  1.00 184.33 ? 494 TYR B CE2   1 
ATOM   7954 C  CZ    . TYR B 1 467 ? 52.755  5.801   17.670  1.00 190.97 ? 494 TYR B CZ    1 
ATOM   7955 O  OH    . TYR B 1 467 ? 53.002  6.578   16.563  1.00 196.29 ? 494 TYR B OH    1 
ATOM   7956 N  N     . TRP B 1 468 ? 54.577  2.779   23.394  1.00 148.14 ? 495 TRP B N     1 
ATOM   7957 C  CA    . TRP B 1 468 ? 55.631  3.453   24.141  1.00 143.07 ? 495 TRP B CA    1 
ATOM   7958 C  C     . TRP B 1 468 ? 56.576  2.432   24.758  1.00 138.52 ? 495 TRP B C     1 
ATOM   7959 O  O     . TRP B 1 468 ? 56.283  1.234   24.824  1.00 153.73 ? 495 TRP B O     1 
ATOM   7960 C  CB    . TRP B 1 468 ? 55.059  4.357   25.244  1.00 147.30 ? 495 TRP B CB    1 
ATOM   7961 C  CG    . TRP B 1 468 ? 54.362  5.585   24.740  1.00 151.61 ? 495 TRP B CG    1 
ATOM   7962 C  CD1   . TRP B 1 468 ? 54.583  6.230   23.558  1.00 152.58 ? 495 TRP B CD1   1 
ATOM   7963 C  CD2   . TRP B 1 468 ? 53.322  6.312   25.405  1.00 149.08 ? 495 TRP B CD2   1 
ATOM   7964 N  NE1   . TRP B 1 468 ? 53.747  7.315   23.447  1.00 149.99 ? 495 TRP B NE1   1 
ATOM   7965 C  CE2   . TRP B 1 468 ? 52.962  7.387   24.568  1.00 150.42 ? 495 TRP B CE2   1 
ATOM   7966 C  CE3   . TRP B 1 468 ? 52.661  6.158   26.628  1.00 141.30 ? 495 TRP B CE3   1 
ATOM   7967 C  CZ2   . TRP B 1 468 ? 51.972  8.303   24.913  1.00 151.64 ? 495 TRP B CZ2   1 
ATOM   7968 C  CZ3   . TRP B 1 468 ? 51.676  7.067   26.968  1.00 137.86 ? 495 TRP B CZ3   1 
ATOM   7969 C  CH2   . TRP B 1 468 ? 51.342  8.126   26.115  1.00 148.12 ? 495 TRP B CH2   1 
ATOM   7970 N  N     . THR B 1 469 ? 57.728  2.926   25.211  1.00 121.66 ? 496 THR B N     1 
ATOM   7971 C  CA    . THR B 1 469 ? 58.702  2.143   25.968  1.00 128.71 ? 496 THR B CA    1 
ATOM   7972 C  C     . THR B 1 469 ? 59.172  2.936   27.185  1.00 120.10 ? 496 THR B C     1 
ATOM   7973 O  O     . THR B 1 469 ? 60.368  3.139   27.410  1.00 101.57 ? 496 THR B O     1 
ATOM   7974 C  CB    . THR B 1 469 ? 59.894  1.732   25.100  1.00 120.52 ? 496 THR B CB    1 
ATOM   7975 O  OG1   . THR B 1 469 ? 60.564  2.901   24.611  1.00 124.47 ? 496 THR B OG1   1 
ATOM   7976 C  CG2   . THR B 1 469 ? 59.438  0.883   23.918  1.00 121.13 ? 496 THR B CG2   1 
ATOM   7977 N  N     . LEU B 1 470 ? 58.212  3.396   27.994  1.00 120.76 ? 497 LEU B N     1 
ATOM   7978 C  CA    . LEU B 1 470 ? 58.538  4.215   29.161  1.00 112.28 ? 497 LEU B CA    1 
ATOM   7979 C  C     . LEU B 1 470 ? 59.250  3.398   30.231  1.00 111.45 ? 497 LEU B C     1 
ATOM   7980 O  O     . LEU B 1 470 ? 60.315  3.791   30.723  1.00 96.59  ? 497 LEU B O     1 
ATOM   7981 C  CB    . LEU B 1 470 ? 57.267  4.840   29.735  1.00 106.17 ? 497 LEU B CB    1 
ATOM   7982 C  CG    . LEU B 1 470 ? 56.562  5.901   28.894  1.00 127.44 ? 497 LEU B CG    1 
ATOM   7983 C  CD1   . LEU B 1 470 ? 55.186  6.180   29.466  1.00 125.88 ? 497 LEU B CD1   1 
ATOM   7984 C  CD2   . LEU B 1 470 ? 57.391  7.174   28.839  1.00 121.26 ? 497 LEU B CD2   1 
ATOM   7985 N  N     . ALA B 1 471 ? 58.661  2.271   30.620  1.00 106.40 ? 498 ALA B N     1 
ATOM   7986 C  CA    . ALA B 1 471 ? 59.243  1.389   31.619  1.00 94.17  ? 498 ALA B CA    1 
ATOM   7987 C  C     . ALA B 1 471 ? 58.775  -0.027  31.329  1.00 100.57 ? 498 ALA B C     1 
ATOM   7988 O  O     . ALA B 1 471 ? 57.600  -0.247  31.025  1.00 106.23 ? 498 ALA B O     1 
ATOM   7989 C  CB    . ALA B 1 471 ? 58.848  1.799   33.042  1.00 98.29  ? 498 ALA B CB    1 
ATOM   7990 N  N     . TYR B 1 472 ? 59.700  -0.978  31.415  1.00 106.46 ? 499 TYR B N     1 
ATOM   7991 C  CA    . TYR B 1 472 ? 59.366  -2.370  31.159  1.00 97.86  ? 499 TYR B CA    1 
ATOM   7992 C  C     . TYR B 1 472 ? 60.380  -3.261  31.855  1.00 100.75 ? 499 TYR B C     1 
ATOM   7993 O  O     . TYR B 1 472 ? 61.508  -2.848  32.140  1.00 96.91  ? 499 TYR B O     1 
ATOM   7994 C  CB    . TYR B 1 472 ? 59.328  -2.677  29.657  1.00 93.83  ? 499 TYR B CB    1 
ATOM   7995 C  CG    . TYR B 1 472 ? 60.620  -2.372  28.932  1.00 93.21  ? 499 TYR B CG    1 
ATOM   7996 C  CD1   . TYR B 1 472 ? 61.648  -3.310  28.875  1.00 101.53 ? 499 TYR B CD1   1 
ATOM   7997 C  CD2   . TYR B 1 472 ? 60.813  -1.150  28.299  1.00 104.23 ? 499 TYR B CD2   1 
ATOM   7998 C  CE1   . TYR B 1 472 ? 62.831  -3.040  28.211  1.00 98.33  ? 499 TYR B CE1   1 
ATOM   7999 C  CE2   . TYR B 1 472 ? 61.995  -0.868  27.631  1.00 109.66 ? 499 TYR B CE2   1 
ATOM   8000 C  CZ    . TYR B 1 472 ? 63.000  -1.818  27.592  1.00 109.78 ? 499 TYR B CZ    1 
ATOM   8001 O  OH    . TYR B 1 472 ? 64.177  -1.545  26.932  1.00 105.28 ? 499 TYR B OH    1 
ATOM   8002 N  N     . VAL B 1 473 ? 59.958  -4.492  32.122  1.00 104.03 ? 500 VAL B N     1 
ATOM   8003 C  CA    . VAL B 1 473 ? 60.846  -5.553  32.575  1.00 94.33  ? 500 VAL B CA    1 
ATOM   8004 C  C     . VAL B 1 473 ? 61.218  -6.401  31.369  1.00 101.45 ? 500 VAL B C     1 
ATOM   8005 O  O     . VAL B 1 473 ? 60.374  -6.679  30.507  1.00 106.40 ? 500 VAL B O     1 
ATOM   8006 C  CB    . VAL B 1 473 ? 60.180  -6.408  33.668  1.00 95.55  ? 500 VAL B CB    1 
ATOM   8007 C  CG1   . VAL B 1 473 ? 61.193  -7.358  34.287  1.00 102.13 ? 500 VAL B CG1   1 
ATOM   8008 C  CG2   . VAL B 1 473 ? 59.547  -5.517  34.724  1.00 93.45  ? 500 VAL B CG2   1 
ATOM   8009 N  N     . ILE B 1 474 ? 62.482  -6.804  31.293  1.00 98.65  ? 501 ILE B N     1 
ATOM   8010 C  CA    . ILE B 1 474 ? 62.961  -7.660  30.217  1.00 104.38 ? 501 ILE B CA    1 
ATOM   8011 C  C     . ILE B 1 474 ? 63.760  -8.805  30.826  1.00 111.48 ? 501 ILE B C     1 
ATOM   8012 O  O     . ILE B 1 474 ? 64.522  -8.608  31.779  1.00 115.40 ? 501 ILE B O     1 
ATOM   8013 C  CB    . ILE B 1 474 ? 63.806  -6.870  29.192  1.00 103.21 ? 501 ILE B CB    1 
ATOM   8014 C  CG1   . ILE B 1 474 ? 64.165  -7.751  27.994  1.00 112.42 ? 501 ILE B CG1   1 
ATOM   8015 C  CG2   . ILE B 1 474 ? 65.057  -6.291  29.841  1.00 103.85 ? 501 ILE B CG2   1 
ATOM   8016 C  CD1   . ILE B 1 474 ? 64.907  -7.016  26.892  1.00 112.98 ? 501 ILE B CD1   1 
ATOM   8017 N  N     . SER B 1 475 ? 63.565  -10.005 30.294  1.00 110.66 ? 502 SER B N     1 
ATOM   8018 C  CA    . SER B 1 475 ? 64.315  -11.171 30.734  1.00 112.66 ? 502 SER B CA    1 
ATOM   8019 C  C     . SER B 1 475 ? 65.485  -11.430 29.792  1.00 125.27 ? 502 SER B C     1 
ATOM   8020 O  O     . SER B 1 475 ? 65.538  -10.917 28.671  1.00 126.48 ? 502 SER B O     1 
ATOM   8021 C  CB    . SER B 1 475 ? 63.414  -12.408 30.815  1.00 113.13 ? 502 SER B CB    1 
ATOM   8022 O  OG    . SER B 1 475 ? 62.982  -12.831 29.533  1.00 114.77 ? 502 SER B OG    1 
ATOM   8023 N  N     . LEU B 1 476 ? 66.439  -12.232 30.274  1.00 132.57 ? 503 LEU B N     1 
ATOM   8024 C  CA    . LEU B 1 476 ? 67.581  -12.601 29.443  1.00 122.97 ? 503 LEU B CA    1 
ATOM   8025 C  C     . LEU B 1 476 ? 67.135  -13.315 28.176  1.00 128.71 ? 503 LEU B C     1 
ATOM   8026 O  O     . LEU B 1 476 ? 67.773  -13.175 27.126  1.00 132.97 ? 503 LEU B O     1 
ATOM   8027 C  CB    . LEU B 1 476 ? 68.547  -13.476 30.243  1.00 125.00 ? 503 LEU B CB    1 
ATOM   8028 C  CG    . LEU B 1 476 ? 69.820  -13.960 29.545  1.00 134.12 ? 503 LEU B CG    1 
ATOM   8029 C  CD1   . LEU B 1 476 ? 70.701  -12.786 29.148  1.00 130.78 ? 503 LEU B CD1   1 
ATOM   8030 C  CD2   . LEU B 1 476 ? 70.577  -14.929 30.440  1.00 127.43 ? 503 LEU B CD2   1 
ATOM   8031 N  N     . GLN B 1 477 ? 66.042  -14.079 28.253  1.00 140.25 ? 504 GLN B N     1 
ATOM   8032 C  CA    . GLN B 1 477 ? 65.495  -14.716 27.060  1.00 146.18 ? 504 GLN B CA    1 
ATOM   8033 C  C     . GLN B 1 477 ? 65.040  -13.676 26.043  1.00 144.38 ? 504 GLN B C     1 
ATOM   8034 O  O     . GLN B 1 477 ? 65.324  -13.802 24.846  1.00 147.07 ? 504 GLN B O     1 
ATOM   8035 C  CB    . GLN B 1 477 ? 64.335  -15.637 27.446  1.00 141.84 ? 504 GLN B CB    1 
ATOM   8036 C  CG    . GLN B 1 477 ? 63.582  -16.227 26.265  1.00 149.47 ? 504 GLN B CG    1 
ATOM   8037 C  CD    . GLN B 1 477 ? 62.391  -17.065 26.691  1.00 152.32 ? 504 GLN B CD    1 
ATOM   8038 O  OE1   . GLN B 1 477 ? 62.478  -17.853 27.633  1.00 155.81 ? 504 GLN B OE1   1 
ATOM   8039 N  NE2   . GLN B 1 477 ? 61.270  -16.897 25.998  1.00 154.04 ? 504 GLN B NE2   1 
ATOM   8040 N  N     . GLY B 1 478 ? 64.341  -12.636 26.504  1.00 129.13 ? 505 GLY B N     1 
ATOM   8041 C  CA    . GLY B 1 478 ? 63.847  -11.619 25.593  1.00 120.72 ? 505 GLY B CA    1 
ATOM   8042 C  C     . GLY B 1 478 ? 64.937  -10.729 25.031  1.00 129.92 ? 505 GLY B C     1 
ATOM   8043 O  O     . GLY B 1 478 ? 64.806  -10.215 23.916  1.00 135.05 ? 505 GLY B O     1 
ATOM   8044 N  N     . ALA B 1 479 ? 66.020  -10.531 25.785  1.00 128.35 ? 506 ALA B N     1 
ATOM   8045 C  CA    . ALA B 1 479 ? 67.114  -9.698  25.294  1.00 123.29 ? 506 ALA B CA    1 
ATOM   8046 C  C     . ALA B 1 479 ? 67.807  -10.344 24.102  1.00 136.81 ? 506 ALA B C     1 
ATOM   8047 O  O     . ALA B 1 479 ? 68.200  -9.651  23.155  1.00 134.09 ? 506 ALA B O     1 
ATOM   8048 C  CB    . ALA B 1 479 ? 68.113  -9.423  26.416  1.00 108.62 ? 506 ALA B CB    1 
ATOM   8049 N  N     . ARG B 1 480 ? 67.964  -11.671 24.127  1.00 140.72 ? 507 ARG B N     1 
ATOM   8050 C  CA    . ARG B 1 480 ? 68.564  -12.362 22.991  1.00 139.49 ? 507 ARG B CA    1 
ATOM   8051 C  C     . ARG B 1 480 ? 67.647  -12.327 21.775  1.00 142.54 ? 507 ARG B C     1 
ATOM   8052 O  O     . ARG B 1 480 ? 68.117  -12.156 20.644  1.00 144.53 ? 507 ARG B O     1 
ATOM   8053 C  CB    . ARG B 1 480 ? 68.893  -13.808 23.359  1.00 145.67 ? 507 ARG B CB    1 
ATOM   8054 C  CG    . ARG B 1 480 ? 69.868  -13.976 24.510  1.00 145.48 ? 507 ARG B CG    1 
ATOM   8055 C  CD    . ARG B 1 480 ? 70.490  -15.367 24.471  1.00 156.77 ? 507 ARG B CD    1 
ATOM   8056 N  NE    . ARG B 1 480 ? 71.202  -15.702 25.699  1.00 160.86 ? 507 ARG B NE    1 
ATOM   8057 C  CZ    . ARG B 1 480 ? 70.700  -16.446 26.675  1.00 158.97 ? 507 ARG B CZ    1 
ATOM   8058 N  NH1   . ARG B 1 480 ? 69.477  -16.947 26.604  1.00 154.43 ? 507 ARG B NH1   1 
ATOM   8059 N  NH2   . ARG B 1 480 ? 71.445  -16.699 27.748  1.00 154.48 ? 507 ARG B NH2   1 
ATOM   8060 N  N     . LYS B 1 481 ? 66.337  -12.492 21.987  1.00 138.43 ? 508 LYS B N     1 
ATOM   8061 C  CA    . LYS B 1 481 ? 65.394  -12.492 20.871  1.00 142.02 ? 508 LYS B CA    1 
ATOM   8062 C  C     . LYS B 1 481 ? 65.415  -11.163 20.126  1.00 136.68 ? 508 LYS B C     1 
ATOM   8063 O  O     . LYS B 1 481 ? 65.336  -11.134 18.891  1.00 132.52 ? 508 LYS B O     1 
ATOM   8064 C  CB    . LYS B 1 481 ? 63.979  -12.797 21.368  1.00 132.33 ? 508 LYS B CB    1 
ATOM   8065 C  CG    . LYS B 1 481 ? 63.720  -14.249 21.735  1.00 129.76 ? 508 LYS B CG    1 
ATOM   8066 C  CD    . LYS B 1 481 ? 62.249  -14.461 22.070  1.00 130.45 ? 508 LYS B CD    1 
ATOM   8067 C  CE    . LYS B 1 481 ? 61.980  -15.867 22.588  1.00 134.57 ? 508 LYS B CE    1 
ATOM   8068 N  NZ    . LYS B 1 481 ? 60.559  -16.045 23.008  1.00 135.75 ? 508 LYS B NZ    1 
ATOM   8069 N  N     . LEU B 1 482 ? 65.515  -10.051 20.858  1.00 132.40 ? 509 LEU B N     1 
ATOM   8070 C  CA    . LEU B 1 482 ? 65.552  -8.745  20.208  1.00 133.26 ? 509 LEU B CA    1 
ATOM   8071 C  C     . LEU B 1 482 ? 66.856  -8.546  19.443  1.00 137.88 ? 509 LEU B C     1 
ATOM   8072 O  O     . LEU B 1 482 ? 66.848  -8.034  18.317  1.00 139.89 ? 509 LEU B O     1 
ATOM   8073 C  CB    . LEU B 1 482 ? 65.358  -7.638  21.244  1.00 124.12 ? 509 LEU B CB    1 
ATOM   8074 C  CG    . LEU B 1 482 ? 64.013  -7.627  21.975  1.00 113.26 ? 509 LEU B CG    1 
ATOM   8075 C  CD1   . LEU B 1 482 ? 63.943  -6.469  22.955  1.00 108.22 ? 509 LEU B CD1   1 
ATOM   8076 C  CD2   . LEU B 1 482 ? 62.868  -7.559  20.980  1.00 119.72 ? 509 LEU B CD2   1 
ATOM   8077 N  N     . LEU B 1 483 ? 67.984  -8.950  20.032  1.00 137.78 ? 510 LEU B N     1 
ATOM   8078 C  CA    . LEU B 1 483 ? 69.268  -8.786  19.359  1.00 136.58 ? 510 LEU B CA    1 
ATOM   8079 C  C     . LEU B 1 483 ? 69.406  -9.730  18.169  1.00 141.08 ? 510 LEU B C     1 
ATOM   8080 O  O     . LEU B 1 483 ? 70.044  -9.374  17.170  1.00 140.76 ? 510 LEU B O     1 
ATOM   8081 C  CB    . LEU B 1 483 ? 70.413  -9.006  20.348  1.00 127.22 ? 510 LEU B CB    1 
ATOM   8082 C  CG    . LEU B 1 483 ? 70.506  -8.023  21.519  1.00 121.78 ? 510 LEU B CG    1 
ATOM   8083 C  CD1   . LEU B 1 483 ? 71.560  -8.472  22.515  1.00 117.00 ? 510 LEU B CD1   1 
ATOM   8084 C  CD2   . LEU B 1 483 ? 70.806  -6.619  21.021  1.00 115.33 ? 510 LEU B CD2   1 
ATOM   8085 N  N     . ALA B 1 484 ? 68.813  -10.924 18.248  1.00 144.48 ? 511 ALA B N     1 
ATOM   8086 C  CA    . ALA B 1 484 ? 68.939  -11.899 17.170  1.00 148.79 ? 511 ALA B CA    1 
ATOM   8087 C  C     . ALA B 1 484 ? 68.159  -11.500 15.924  1.00 151.22 ? 511 ALA B C     1 
ATOM   8088 O  O     . ALA B 1 484 ? 68.417  -12.046 14.846  1.00 152.87 ? 511 ALA B O     1 
ATOM   8089 C  CB    . ALA B 1 484 ? 68.479  -13.276 17.649  1.00 141.72 ? 511 ALA B CB    1 
ATOM   8090 N  N     . ALA B 1 485 ? 67.216  -10.567 16.041  1.00 144.95 ? 512 ALA B N     1 
ATOM   8091 C  CA    . ALA B 1 485 ? 66.440  -10.114 14.894  1.00 147.11 ? 512 ALA B CA    1 
ATOM   8092 C  C     . ALA B 1 485 ? 67.179  -9.093  14.039  1.00 156.79 ? 512 ALA B C     1 
ATOM   8093 O  O     . ALA B 1 485 ? 66.597  -8.595  13.068  1.00 162.17 ? 512 ALA B O     1 
ATOM   8094 C  CB    . ALA B 1 485 ? 65.107  -9.525  15.362  1.00 148.78 ? 512 ALA B CB    1 
ATOM   8095 N  N     . GLU B 1 486 ? 68.450  -8.799  14.360  1.00 157.91 ? 513 GLU B N     1 
ATOM   8096 C  CA    . GLU B 1 486 ? 69.298  -7.773  13.751  1.00 161.81 ? 513 GLU B CA    1 
ATOM   8097 C  C     . GLU B 1 486 ? 68.488  -6.561  13.301  1.00 158.19 ? 513 GLU B C     1 
ATOM   8098 O  O     . GLU B 1 486 ? 68.359  -6.306  12.096  1.00 154.50 ? 513 GLU B O     1 
ATOM   8099 C  CB    . GLU B 1 486 ? 70.103  -8.346  12.578  1.00 153.65 ? 513 GLU B CB    1 
ATOM   8100 C  CG    . GLU B 1 486 ? 69.325  -9.193  11.583  1.00 166.55 ? 513 GLU B CG    1 
ATOM   8101 C  CD    . GLU B 1 486 ? 70.181  -9.657  10.426  1.00 172.24 ? 513 GLU B CD    1 
ATOM   8102 O  OE1   . GLU B 1 486 ? 71.391  -9.345  10.420  1.00 173.44 ? 513 GLU B OE1   1 
ATOM   8103 O  OE2   . GLU B 1 486 ? 69.644  -10.331 9.523   1.00 184.91 ? 513 GLU B OE2   1 
ATOM   8104 N  N     . PRO B 1 487 ? 67.934  -5.785  14.238  1.00 146.35 ? 514 PRO B N     1 
ATOM   8105 C  CA    . PRO B 1 487 ? 67.095  -4.644  13.852  1.00 152.89 ? 514 PRO B CA    1 
ATOM   8106 C  C     . PRO B 1 487 ? 67.874  -3.417  13.409  1.00 150.81 ? 514 PRO B C     1 
ATOM   8107 O  O     . PRO B 1 487 ? 67.253  -2.455  12.937  1.00 152.39 ? 514 PRO B O     1 
ATOM   8108 C  CB    . PRO B 1 487 ? 66.306  -4.354  15.132  1.00 142.93 ? 514 PRO B CB    1 
ATOM   8109 C  CG    . PRO B 1 487 ? 67.242  -4.751  16.222  1.00 144.63 ? 514 PRO B CG    1 
ATOM   8110 C  CD    . PRO B 1 487 ? 68.024  -5.933  15.702  1.00 146.99 ? 514 PRO B CD    1 
ATOM   8111 N  N     . LEU B 1 488 ? 69.202  -3.411  13.549  1.00 145.21 ? 515 LEU B N     1 
ATOM   8112 C  CA    . LEU B 1 488 ? 69.977  -2.248  13.129  1.00 145.50 ? 515 LEU B CA    1 
ATOM   8113 C  C     . LEU B 1 488 ? 69.874  -2.032  11.625  1.00 151.00 ? 515 LEU B C     1 
ATOM   8114 O  O     . LEU B 1 488 ? 69.751  -0.893  11.161  1.00 155.33 ? 515 LEU B O     1 
ATOM   8115 C  CB    . LEU B 1 488 ? 71.438  -2.400  13.554  1.00 143.48 ? 515 LEU B CB    1 
ATOM   8116 C  CG    . LEU B 1 488 ? 71.719  -2.405  15.060  1.00 127.15 ? 515 LEU B CG    1 
ATOM   8117 C  CD1   . LEU B 1 488 ? 73.216  -2.356  15.323  1.00 129.70 ? 515 LEU B CD1   1 
ATOM   8118 C  CD2   . LEU B 1 488 ? 71.011  -1.251  15.754  1.00 116.87 ? 515 LEU B CD2   1 
ATOM   8119 N  N     . SER B 1 489 ? 69.910  -3.114  10.845  1.00 152.07 ? 516 SER B N     1 
ATOM   8120 C  CA    . SER B 1 489 ? 69.735  -3.011  9.402   1.00 157.77 ? 516 SER B CA    1 
ATOM   8121 C  C     . SER B 1 489 ? 68.281  -2.798  8.995   1.00 158.65 ? 516 SER B C     1 
ATOM   8122 O  O     . SER B 1 489 ? 68.023  -2.453  7.837   1.00 156.11 ? 516 SER B O     1 
ATOM   8123 C  CB    . SER B 1 489 ? 70.287  -4.262  8.711   1.00 154.70 ? 516 SER B CB    1 
ATOM   8124 O  OG    . SER B 1 489 ? 69.665  -5.439  9.195   1.00 155.91 ? 516 SER B OG    1 
ATOM   8125 N  N     . LYS B 1 490 ? 67.332  -2.994  9.911   1.00 159.62 ? 517 LYS B N     1 
ATOM   8126 C  CA    . LYS B 1 490 ? 65.921  -2.761  9.631   1.00 156.25 ? 517 LYS B CA    1 
ATOM   8127 C  C     . LYS B 1 490 ? 65.376  -1.723  10.603  1.00 156.65 ? 517 LYS B C     1 
ATOM   8128 O  O     . LYS B 1 490 ? 64.388  -1.976  11.300  1.00 158.53 ? 517 LYS B O     1 
ATOM   8129 C  CB    . LYS B 1 490 ? 65.130  -4.066  9.741   1.00 155.21 ? 517 LYS B CB    1 
ATOM   8130 C  CG    . LYS B 1 490 ? 65.900  -5.295  9.287   1.00 150.37 ? 517 LYS B CG    1 
ATOM   8131 C  CD    . LYS B 1 490 ? 65.366  -6.555  9.946   1.00 148.80 ? 517 LYS B CD    1 
ATOM   8132 C  CE    . LYS B 1 490 ? 66.327  -7.718  9.772   1.00 157.03 ? 517 LYS B CE    1 
ATOM   8133 N  NZ    . LYS B 1 490 ? 65.907  -8.909  10.560  1.00 159.64 ? 517 LYS B NZ    1 
ATOM   8134 N  N     . MET B 1 491 ? 66.014  -0.554  10.651  1.00 165.45 ? 518 MET B N     1 
ATOM   8135 C  CA    . MET B 1 491 ? 65.758  0.413   11.713  1.00 161.40 ? 518 MET B CA    1 
ATOM   8136 C  C     . MET B 1 491 ? 64.312  0.897   11.682  1.00 154.51 ? 518 MET B C     1 
ATOM   8137 O  O     . MET B 1 491 ? 63.839  1.432   10.675  1.00 154.57 ? 518 MET B O     1 
ATOM   8138 C  CB    . MET B 1 491 ? 66.728  1.590   11.594  1.00 166.46 ? 518 MET B CB    1 
ATOM   8139 C  CG    . MET B 1 491 ? 66.730  2.540   12.790  1.00 163.69 ? 518 MET B CG    1 
ATOM   8140 S  SD    . MET B 1 491 ? 67.184  1.775   14.364  1.00 154.09 ? 518 MET B SD    1 
ATOM   8141 C  CE    . MET B 1 491 ? 68.887  1.316   14.057  1.00 151.76 ? 518 MET B CE    1 
ATOM   8142 N  N     . LEU B 1 492 ? 63.620  0.695   12.801  1.00 145.63 ? 519 LEU B N     1 
ATOM   8143 C  CA    . LEU B 1 492 ? 62.242  1.067   13.045  1.00 137.75 ? 519 LEU B CA    1 
ATOM   8144 C  C     . LEU B 1 492 ? 62.227  1.593   14.474  1.00 135.20 ? 519 LEU B C     1 
ATOM   8145 O  O     . LEU B 1 492 ? 62.973  1.075   15.320  1.00 131.72 ? 519 LEU B O     1 
ATOM   8146 C  CB    . LEU B 1 492 ? 61.303  -0.141  12.893  1.00 138.28 ? 519 LEU B CB    1 
ATOM   8147 C  CG    . LEU B 1 492 ? 59.791  -0.025  13.087  1.00 138.26 ? 519 LEU B CG    1 
ATOM   8148 C  CD1   . LEU B 1 492 ? 59.150  0.677   11.911  1.00 152.40 ? 519 LEU B CD1   1 
ATOM   8149 C  CD2   . LEU B 1 492 ? 59.184  -1.405  13.276  1.00 140.10 ? 519 LEU B CD2   1 
ATOM   8150 N  N     . PRO B 1 493 ? 61.433  2.624   14.774  1.00 131.22 ? 520 PRO B N     1 
ATOM   8151 C  CA    . PRO B 1 493 ? 61.436  3.179   16.134  1.00 124.88 ? 520 PRO B CA    1 
ATOM   8152 C  C     . PRO B 1 493 ? 61.173  2.100   17.176  1.00 125.78 ? 520 PRO B C     1 
ATOM   8153 O  O     . PRO B 1 493 ? 60.390  1.174   16.953  1.00 134.23 ? 520 PRO B O     1 
ATOM   8154 C  CB    . PRO B 1 493 ? 60.314  4.221   16.091  1.00 122.57 ? 520 PRO B CB    1 
ATOM   8155 C  CG    . PRO B 1 493 ? 60.270  4.640   14.664  1.00 125.13 ? 520 PRO B CG    1 
ATOM   8156 C  CD    . PRO B 1 493 ? 60.546  3.386   13.878  1.00 136.39 ? 520 PRO B CD    1 
ATOM   8157 N  N     . VAL B 1 494 ? 61.853  2.223   18.321  1.00 124.23 ? 521 VAL B N     1 
ATOM   8158 C  CA    . VAL B 1 494 ? 61.897  1.133   19.295  1.00 131.47 ? 521 VAL B CA    1 
ATOM   8159 C  C     . VAL B 1 494 ? 60.510  0.816   19.840  1.00 141.19 ? 521 VAL B C     1 
ATOM   8160 O  O     . VAL B 1 494 ? 60.206  -0.344  20.148  1.00 141.25 ? 521 VAL B O     1 
ATOM   8161 C  CB    . VAL B 1 494 ? 62.895  1.468   20.426  1.00 124.77 ? 521 VAL B CB    1 
ATOM   8162 C  CG1   . VAL B 1 494 ? 62.454  2.703   21.202  1.00 124.09 ? 521 VAL B CG1   1 
ATOM   8163 C  CG2   . VAL B 1 494 ? 63.077  0.274   21.354  1.00 122.36 ? 521 VAL B CG2   1 
ATOM   8164 N  N     . ASP B 1 495 ? 59.643  1.822   19.952  1.00 141.06 ? 522 ASP B N     1 
ATOM   8165 C  CA    . ASP B 1 495 ? 58.285  1.593   20.428  1.00 140.09 ? 522 ASP B CA    1 
ATOM   8166 C  C     . ASP B 1 495 ? 57.391  0.939   19.382  1.00 142.39 ? 522 ASP B C     1 
ATOM   8167 O  O     . ASP B 1 495 ? 56.254  0.579   19.704  1.00 149.62 ? 522 ASP B O     1 
ATOM   8168 C  CB    . ASP B 1 495 ? 57.667  2.911   20.896  1.00 142.48 ? 522 ASP B CB    1 
ATOM   8169 C  CG    . ASP B 1 495 ? 57.890  4.042   19.914  1.00 146.62 ? 522 ASP B CG    1 
ATOM   8170 O  OD1   . ASP B 1 495 ? 58.968  4.082   19.287  1.00 147.64 ? 522 ASP B OD1   1 
ATOM   8171 O  OD2   . ASP B 1 495 ? 56.987  4.894   19.770  1.00 161.50 ? 522 ASP B OD2   1 
ATOM   8172 N  N     . GLU B 1 496 ? 57.868  0.789   18.145  1.00 150.80 ? 523 GLU B N     1 
ATOM   8173 C  CA    . GLU B 1 496 ? 57.192  -0.003  17.125  1.00 151.67 ? 523 GLU B CA    1 
ATOM   8174 C  C     . GLU B 1 496 ? 57.908  -1.302  16.799  1.00 150.33 ? 523 GLU B C     1 
ATOM   8175 O  O     . GLU B 1 496 ? 57.260  -2.259  16.372  1.00 148.19 ? 523 GLU B O     1 
ATOM   8176 C  CB    . GLU B 1 496 ? 57.029  0.803   15.830  1.00 141.36 ? 523 GLU B CB    1 
ATOM   8177 C  CG    . GLU B 1 496 ? 55.918  1.829   15.875  1.00 149.79 ? 523 GLU B CG    1 
ATOM   8178 C  CD    . GLU B 1 496 ? 55.589  2.379   14.505  1.00 159.66 ? 523 GLU B CD    1 
ATOM   8179 O  OE1   . GLU B 1 496 ? 56.134  1.861   13.508  1.00 168.11 ? 523 GLU B OE1   1 
ATOM   8180 O  OE2   . GLU B 1 496 ? 54.786  3.329   14.426  1.00 165.34 ? 523 GLU B OE2   1 
ATOM   8181 N  N     . PHE B 1 497 ? 59.229  -1.353  16.987  1.00 145.02 ? 524 PHE B N     1 
ATOM   8182 C  CA    . PHE B 1 497 ? 59.961  -2.597  16.787  1.00 138.49 ? 524 PHE B CA    1 
ATOM   8183 C  C     . PHE B 1 497 ? 59.569  -3.652  17.815  1.00 151.11 ? 524 PHE B C     1 
ATOM   8184 O  O     . PHE B 1 497 ? 59.591  -4.850  17.508  1.00 155.84 ? 524 PHE B O     1 
ATOM   8185 C  CB    . PHE B 1 497 ? 61.465  -2.327  16.836  1.00 131.76 ? 524 PHE B CB    1 
ATOM   8186 C  CG    . PHE B 1 497 ? 62.299  -3.556  17.057  1.00 134.56 ? 524 PHE B CG    1 
ATOM   8187 C  CD1   . PHE B 1 497 ? 62.447  -4.501  16.054  1.00 136.30 ? 524 PHE B CD1   1 
ATOM   8188 C  CD2   . PHE B 1 497 ? 62.943  -3.761  18.267  1.00 123.97 ? 524 PHE B CD2   1 
ATOM   8189 C  CE1   . PHE B 1 497 ? 63.216  -5.630  16.258  1.00 129.47 ? 524 PHE B CE1   1 
ATOM   8190 C  CE2   . PHE B 1 497 ? 63.714  -4.887  18.474  1.00 124.18 ? 524 PHE B CE2   1 
ATOM   8191 C  CZ    . PHE B 1 497 ? 63.851  -5.823  17.468  1.00 128.46 ? 524 PHE B CZ    1 
ATOM   8192 N  N     . LEU B 1 498 ? 59.204  -3.232  19.034  1.00 147.94 ? 525 LEU B N     1 
ATOM   8193 C  CA    . LEU B 1 498 ? 58.752  -4.205  20.027  1.00 144.55 ? 525 LEU B CA    1 
ATOM   8194 C  C     . LEU B 1 498 ? 57.390  -4.793  19.672  1.00 152.58 ? 525 LEU B C     1 
ATOM   8195 O  O     . LEU B 1 498 ? 57.240  -6.025  19.745  1.00 151.34 ? 525 LEU B O     1 
ATOM   8196 C  CB    . LEU B 1 498 ? 58.765  -3.576  21.424  1.00 126.59 ? 525 LEU B CB    1 
ATOM   8197 C  CG    . LEU B 1 498 ? 60.137  -3.220  21.996  1.00 125.73 ? 525 LEU B CG    1 
ATOM   8198 C  CD1   . LEU B 1 498 ? 59.999  -2.699  23.418  1.00 112.41 ? 525 LEU B CD1   1 
ATOM   8199 C  CD2   . LEU B 1 498 ? 61.066  -4.423  21.951  1.00 123.53 ? 525 LEU B CD2   1 
ATOM   8200 N  N     . PRO B 1 499 ? 56.371  -4.009  19.292  1.00 158.20 ? 526 PRO B N     1 
ATOM   8201 C  CA    . PRO B 1 499 ? 55.130  -4.627  18.793  1.00 164.13 ? 526 PRO B CA    1 
ATOM   8202 C  C     . PRO B 1 499 ? 55.325  -5.481  17.553  1.00 165.26 ? 526 PRO B C     1 
ATOM   8203 O  O     . PRO B 1 499 ? 54.509  -6.376  17.302  1.00 161.91 ? 526 PRO B O     1 
ATOM   8204 C  CB    . PRO B 1 499 ? 54.228  -3.420  18.506  1.00 161.84 ? 526 PRO B CB    1 
ATOM   8205 C  CG    . PRO B 1 499 ? 54.710  -2.376  19.434  1.00 154.71 ? 526 PRO B CG    1 
ATOM   8206 C  CD    . PRO B 1 499 ? 56.198  -2.559  19.496  1.00 151.79 ? 526 PRO B CD    1 
ATOM   8207 N  N     . VAL B 1 500 ? 56.370  -5.229  16.762  1.00 174.75 ? 527 VAL B N     1 
ATOM   8208 C  CA    . VAL B 1 500 ? 56.683  -6.126  15.656  1.00 173.12 ? 527 VAL B CA    1 
ATOM   8209 C  C     . VAL B 1 500 ? 57.192  -7.463  16.184  1.00 174.79 ? 527 VAL B C     1 
ATOM   8210 O  O     . VAL B 1 500 ? 56.941  -8.514  15.582  1.00 175.46 ? 527 VAL B O     1 
ATOM   8211 C  CB    . VAL B 1 500 ? 57.694  -5.458  14.701  1.00 171.84 ? 527 VAL B CB    1 
ATOM   8212 C  CG1   . VAL B 1 500 ? 58.274  -6.467  13.723  1.00 174.83 ? 527 VAL B CG1   1 
ATOM   8213 C  CG2   . VAL B 1 500 ? 57.029  -4.321  13.943  1.00 169.15 ? 527 VAL B CG2   1 
ATOM   8214 N  N     . MET B 1 501 ? 57.873  -7.458  17.333  1.00 172.25 ? 528 MET B N     1 
ATOM   8215 C  CA    . MET B 1 501 ? 58.505  -8.679  17.819  1.00 170.43 ? 528 MET B CA    1 
ATOM   8216 C  C     . MET B 1 501 ? 57.534  -9.610  18.538  1.00 168.00 ? 528 MET B C     1 
ATOM   8217 O  O     . MET B 1 501 ? 57.722  -10.830 18.492  1.00 164.62 ? 528 MET B O     1 
ATOM   8218 C  CB    . MET B 1 501 ? 59.686  -8.337  18.727  1.00 171.41 ? 528 MET B CB    1 
ATOM   8219 C  CG    . MET B 1 501 ? 60.911  -7.860  17.961  1.00 170.29 ? 528 MET B CG    1 
ATOM   8220 S  SD    . MET B 1 501 ? 61.400  -8.997  16.641  1.00 160.84 ? 528 MET B SD    1 
ATOM   8221 C  CE    . MET B 1 501 ? 61.791  -10.470 17.581  1.00 163.13 ? 528 MET B CE    1 
ATOM   8222 N  N     . PHE B 1 502 ? 56.505  -9.085  19.208  1.00 164.39 ? 529 PHE B N     1 
ATOM   8223 C  CA    . PHE B 1 502 ? 55.460  -9.950  19.741  1.00 160.51 ? 529 PHE B CA    1 
ATOM   8224 C  C     . PHE B 1 502 ? 54.237  -10.008 18.828  1.00 158.71 ? 529 PHE B C     1 
ATOM   8225 O  O     . PHE B 1 502 ? 53.164  -10.444 19.260  1.00 155.63 ? 529 PHE B O     1 
ATOM   8226 C  CB    . PHE B 1 502 ? 55.080  -9.554  21.176  1.00 148.35 ? 529 PHE B CB    1 
ATOM   8227 C  CG    . PHE B 1 502 ? 54.484  -8.177  21.327  1.00 153.17 ? 529 PHE B CG    1 
ATOM   8228 C  CD1   . PHE B 1 502 ? 53.127  -7.967  21.139  1.00 153.09 ? 529 PHE B CD1   1 
ATOM   8229 C  CD2   . PHE B 1 502 ? 55.268  -7.109  21.733  1.00 148.84 ? 529 PHE B CD2   1 
ATOM   8230 C  CE1   . PHE B 1 502 ? 52.576  -6.711  21.306  1.00 144.54 ? 529 PHE B CE1   1 
ATOM   8231 C  CE2   . PHE B 1 502 ? 54.720  -5.853  21.910  1.00 139.07 ? 529 PHE B CE2   1 
ATOM   8232 C  CZ    . PHE B 1 502 ? 53.373  -5.653  21.692  1.00 138.54 ? 529 PHE B CZ    1 
ATOM   8233 N  N     . ASP B 1 503 ? 54.388  -9.571  17.575  1.00 161.62 ? 530 ASP B N     1 
ATOM   8234 C  CA    . ASP B 1 503 ? 53.481  -9.920  16.479  1.00 166.38 ? 530 ASP B CA    1 
ATOM   8235 C  C     . ASP B 1 503 ? 52.081  -9.334  16.671  1.00 164.50 ? 530 ASP B C     1 
ATOM   8236 O  O     . ASP B 1 503 ? 51.076  -10.014 16.460  1.00 163.79 ? 530 ASP B O     1 
ATOM   8237 C  CB    . ASP B 1 503 ? 53.414  -11.439 16.294  1.00 161.59 ? 530 ASP B CB    1 
ATOM   8238 C  CG    . ASP B 1 503 ? 53.053  -11.839 14.880  1.00 157.93 ? 530 ASP B CG    1 
ATOM   8239 O  OD1   . ASP B 1 503 ? 52.786  -10.940 14.054  1.00 160.63 ? 530 ASP B OD1   1 
ATOM   8240 O  OD2   . ASP B 1 503 ? 53.044  -13.054 14.593  1.00 166.08 ? 530 ASP B OD2   1 
ATOM   8241 N  N     . LYS B 1 504 ? 52.013  -8.058  17.059  1.00 167.80 ? 531 LYS B N     1 
ATOM   8242 C  CA    . LYS B 1 504 ? 50.740  -7.356  17.175  1.00 163.61 ? 531 LYS B CA    1 
ATOM   8243 C  C     . LYS B 1 504 ? 50.772  -6.004  16.469  1.00 161.49 ? 531 LYS B C     1 
ATOM   8244 O  O     . LYS B 1 504 ? 49.956  -5.131  16.778  1.00 165.64 ? 531 LYS B O     1 
ATOM   8245 C  CB    . LYS B 1 504 ? 50.346  -7.174  18.644  1.00 161.39 ? 531 LYS B CB    1 
ATOM   8246 C  CG    . LYS B 1 504 ? 49.983  -8.463  19.370  1.00 151.96 ? 531 LYS B CG    1 
ATOM   8247 C  CD    . LYS B 1 504 ? 48.636  -9.003  18.916  1.00 153.83 ? 531 LYS B CD    1 
ATOM   8248 C  CE    . LYS B 1 504 ? 48.229  -10.214 19.738  1.00 149.72 ? 531 LYS B CE    1 
ATOM   8249 N  NZ    . LYS B 1 504 ? 48.154  -9.884  21.189  1.00 159.66 ? 531 LYS B NZ    1 
ATOM   8250 N  N     . HIS B 1 505 ? 51.701  -5.812  15.523  1.00 158.15 ? 532 HIS B N     1 
ATOM   8251 C  CA    . HIS B 1 505 ? 51.773  -4.558  14.784  1.00 153.14 ? 532 HIS B CA    1 
ATOM   8252 C  C     . HIS B 1 505 ? 50.673  -4.511  13.724  1.00 157.02 ? 532 HIS B C     1 
ATOM   8253 O  O     . HIS B 1 505 ? 50.421  -5.511  13.045  1.00 153.59 ? 532 HIS B O     1 
ATOM   8254 C  CB    . HIS B 1 505 ? 53.141  -4.398  14.121  1.00 151.46 ? 532 HIS B CB    1 
ATOM   8255 C  CG    . HIS B 1 505 ? 53.443  -2.995  13.693  1.00 153.18 ? 532 HIS B CG    1 
ATOM   8256 N  ND1   . HIS B 1 505 ? 53.967  -2.052  14.551  1.00 151.02 ? 532 HIS B ND1   1 
ATOM   8257 C  CD2   . HIS B 1 505 ? 53.286  -2.372  12.501  1.00 154.26 ? 532 HIS B CD2   1 
ATOM   8258 C  CE1   . HIS B 1 505 ? 54.124  -0.911  13.906  1.00 148.24 ? 532 HIS B CE1   1 
ATOM   8259 N  NE2   . HIS B 1 505 ? 53.717  -1.077  12.661  1.00 150.76 ? 532 HIS B NE2   1 
ATOM   8260 N  N     . PRO B 1 506 ? 50.003  -3.365  13.561  1.00 165.51 ? 533 PRO B N     1 
ATOM   8261 C  CA    . PRO B 1 506 ? 48.882  -3.317  12.607  1.00 165.14 ? 533 PRO B CA    1 
ATOM   8262 C  C     . PRO B 1 506 ? 49.317  -3.438  11.157  1.00 157.01 ? 533 PRO B C     1 
ATOM   8263 O  O     . PRO B 1 506 ? 48.695  -4.186  10.393  1.00 156.16 ? 533 PRO B O     1 
ATOM   8264 C  CB    . PRO B 1 506 ? 48.236  -1.956  12.902  1.00 161.34 ? 533 PRO B CB    1 
ATOM   8265 C  CG    . PRO B 1 506 ? 49.345  -1.130  13.470  1.00 149.04 ? 533 PRO B CG    1 
ATOM   8266 C  CD    . PRO B 1 506 ? 50.201  -2.080  14.255  1.00 152.83 ? 533 PRO B CD    1 
ATOM   8267 N  N     . VAL B 1 507 ? 50.363  -2.724  10.755  1.00 160.92 ? 534 VAL B N     1 
ATOM   8268 C  CA    . VAL B 1 507 ? 50.827  -2.757  9.372   1.00 163.04 ? 534 VAL B CA    1 
ATOM   8269 C  C     . VAL B 1 507 ? 51.601  -4.047  9.139   1.00 170.08 ? 534 VAL B C     1 
ATOM   8270 O  O     . VAL B 1 507 ? 52.491  -4.402  9.920   1.00 172.25 ? 534 VAL B O     1 
ATOM   8271 C  CB    . VAL B 1 507 ? 51.691  -1.526  9.058   1.00 164.09 ? 534 VAL B CB    1 
ATOM   8272 C  CG1   . VAL B 1 507 ? 52.009  -1.464  7.570   1.00 172.00 ? 534 VAL B CG1   1 
ATOM   8273 C  CG2   . VAL B 1 507 ? 50.994  -0.255  9.519   1.00 159.85 ? 534 VAL B CG2   1 
ATOM   8274 N  N     . SER B 1 508 ? 51.262  -4.755  8.062   1.00 177.35 ? 535 SER B N     1 
ATOM   8275 C  CA    . SER B 1 508 ? 51.948  -5.991  7.709   1.00 180.78 ? 535 SER B CA    1 
ATOM   8276 C  C     . SER B 1 508 ? 53.146  -5.771  6.796   1.00 185.33 ? 535 SER B C     1 
ATOM   8277 O  O     . SER B 1 508 ? 53.955  -6.691  6.633   1.00 177.67 ? 535 SER B O     1 
ATOM   8278 C  CB    . SER B 1 508 ? 50.972  -6.971  7.047   1.00 174.22 ? 535 SER B CB    1 
ATOM   8279 O  OG    . SER B 1 508 ? 50.049  -7.484  7.992   1.00 174.29 ? 535 SER B OG    1 
ATOM   8280 N  N     . GLU B 1 509 ? 53.282  -4.585  6.197   1.00 191.78 ? 536 GLU B N     1 
ATOM   8281 C  CA    . GLU B 1 509 ? 54.490  -4.280  5.440   1.00 193.65 ? 536 GLU B CA    1 
ATOM   8282 C  C     . GLU B 1 509 ? 55.706  -4.136  6.348   1.00 195.33 ? 536 GLU B C     1 
ATOM   8283 O  O     . GLU B 1 509 ? 56.839  -4.262  5.872   1.00 201.18 ? 536 GLU B O     1 
ATOM   8284 C  CB    . GLU B 1 509 ? 54.296  -3.005  4.615   1.00 193.79 ? 536 GLU B CB    1 
ATOM   8285 C  CG    . GLU B 1 509 ? 55.367  -2.788  3.552   1.00 203.62 ? 536 GLU B CG    1 
ATOM   8286 C  CD    . GLU B 1 509 ? 55.333  -1.395  2.959   1.00 216.36 ? 536 GLU B CD    1 
ATOM   8287 O  OE1   . GLU B 1 509 ? 54.498  -0.579  3.402   1.00 211.74 ? 536 GLU B OE1   1 
ATOM   8288 O  OE2   . GLU B 1 509 ? 56.145  -1.115  2.051   1.00 217.23 ? 536 GLU B OE2   1 
ATOM   8289 N  N     . TYR B 1 510 ? 55.494  -3.883  7.641   1.00 189.16 ? 537 TYR B N     1 
ATOM   8290 C  CA    . TYR B 1 510 ? 56.585  -3.805  8.607   1.00 185.10 ? 537 TYR B CA    1 
ATOM   8291 C  C     . TYR B 1 510 ? 56.913  -5.169  9.204   1.00 183.34 ? 537 TYR B C     1 
ATOM   8292 O  O     . TYR B 1 510 ? 58.090  -5.523  9.330   1.00 179.20 ? 537 TYR B O     1 
ATOM   8293 C  CB    . TYR B 1 510 ? 56.244  -2.825  9.735   1.00 175.53 ? 537 TYR B CB    1 
ATOM   8294 C  CG    . TYR B 1 510 ? 56.006  -1.393  9.301   1.00 176.15 ? 537 TYR B CG    1 
ATOM   8295 C  CD1   . TYR B 1 510 ? 56.284  -0.971  8.006   1.00 188.91 ? 537 TYR B CD1   1 
ATOM   8296 C  CD2   . TYR B 1 510 ? 55.512  -0.456  10.199  1.00 170.38 ? 537 TYR B CD2   1 
ATOM   8297 C  CE1   . TYR B 1 510 ? 56.067  0.336   7.619   1.00 193.04 ? 537 TYR B CE1   1 
ATOM   8298 C  CE2   . TYR B 1 510 ? 55.292  0.854   9.821   1.00 177.40 ? 537 TYR B CE2   1 
ATOM   8299 C  CZ    . TYR B 1 510 ? 55.572  1.244   8.531   1.00 186.21 ? 537 TYR B CZ    1 
ATOM   8300 O  OH    . TYR B 1 510 ? 55.355  2.547   8.151   1.00 189.69 ? 537 TYR B OH    1 
ATOM   8301 N  N     . LYS B 1 511 ? 55.891  -5.944  9.576   1.00 182.96 ? 538 LYS B N     1 
ATOM   8302 C  CA    . LYS B 1 511 ? 56.106  -7.285  10.107  1.00 178.14 ? 538 LYS B CA    1 
ATOM   8303 C  C     . LYS B 1 511 ? 56.666  -8.248  9.069   1.00 174.37 ? 538 LYS B C     1 
ATOM   8304 O  O     . LYS B 1 511 ? 57.078  -9.353  9.436   1.00 164.25 ? 538 LYS B O     1 
ATOM   8305 C  CB    . LYS B 1 511 ? 54.802  -7.852  10.675  1.00 171.93 ? 538 LYS B CB    1 
ATOM   8306 C  CG    . LYS B 1 511 ? 54.345  -7.206  11.977  1.00 169.20 ? 538 LYS B CG    1 
ATOM   8307 C  CD    . LYS B 1 511 ? 53.135  -7.925  12.567  1.00 162.35 ? 538 LYS B CD    1 
ATOM   8308 C  CE    . LYS B 1 511 ? 51.956  -7.920  11.605  1.00 158.94 ? 538 LYS B CE    1 
ATOM   8309 N  NZ    . LYS B 1 511 ? 50.718  -8.447  12.245  1.00 155.20 ? 538 LYS B NZ    1 
ATOM   8310 N  N     . ALA B 1 512 ? 56.687  -7.861  7.793   1.00 182.95 ? 539 ALA B N     1 
ATOM   8311 C  CA    . ALA B 1 512 ? 57.250  -8.718  6.757   1.00 186.87 ? 539 ALA B CA    1 
ATOM   8312 C  C     . ALA B 1 512 ? 58.772  -8.667  6.738   1.00 186.09 ? 539 ALA B C     1 
ATOM   8313 O  O     . ALA B 1 512 ? 59.417  -9.681  6.445   1.00 181.64 ? 539 ALA B O     1 
ATOM   8314 C  CB    . ALA B 1 512 ? 56.696  -8.326  5.389   1.00 187.13 ? 539 ALA B CB    1 
ATOM   8315 N  N     . HIS B 1 513 ? 59.362  -7.511  7.055   1.00 189.72 ? 540 HIS B N     1 
ATOM   8316 C  CA    . HIS B 1 513 ? 60.817  -7.391  7.008   1.00 187.55 ? 540 HIS B CA    1 
ATOM   8317 C  C     . HIS B 1 513 ? 61.479  -8.193  8.124   1.00 181.62 ? 540 HIS B C     1 
ATOM   8318 O  O     . HIS B 1 513 ? 62.569  -8.746  7.934   1.00 177.96 ? 540 HIS B O     1 
ATOM   8319 C  CB    . HIS B 1 513 ? 61.226  -5.918  7.074   1.00 196.24 ? 540 HIS B CB    1 
ATOM   8320 C  CG    . HIS B 1 513 ? 60.861  -5.133  5.851   1.00 200.61 ? 540 HIS B CG    1 
ATOM   8321 N  ND1   . HIS B 1 513 ? 59.641  -4.508  5.701   1.00 207.04 ? 540 HIS B ND1   1 
ATOM   8322 C  CD2   . HIS B 1 513 ? 61.557  -4.872  4.719   1.00 186.42 ? 540 HIS B CD2   1 
ATOM   8323 C  CE1   . HIS B 1 513 ? 59.602  -3.897  4.530   1.00 193.21 ? 540 HIS B CE1   1 
ATOM   8324 N  NE2   . HIS B 1 513 ? 60.751  -4.103  3.914   1.00 178.62 ? 540 HIS B NE2   1 
ATOM   8325 N  N     . PHE B 1 514 ? 60.835  -8.277  9.288   1.00 176.67 ? 541 PHE B N     1 
ATOM   8326 C  CA    . PHE B 1 514 ? 61.332  -9.088  10.392  1.00 166.86 ? 541 PHE B CA    1 
ATOM   8327 C  C     . PHE B 1 514 ? 60.744  -10.492 10.299  1.00 171.89 ? 541 PHE B C     1 
ATOM   8328 O  O     . PHE B 1 514 ? 59.525  -10.653 10.197  1.00 177.53 ? 541 PHE B O     1 
ATOM   8329 C  CB    . PHE B 1 514 ? 60.979  -8.449  11.735  1.00 152.40 ? 541 PHE B CB    1 
ATOM   8330 C  CG    . PHE B 1 514 ? 61.682  -7.147  11.992  1.00 146.73 ? 541 PHE B CG    1 
ATOM   8331 C  CD1   . PHE B 1 514 ? 61.113  -5.946  11.604  1.00 153.24 ? 541 PHE B CD1   1 
ATOM   8332 C  CD2   . PHE B 1 514 ? 62.913  -7.125  12.624  1.00 150.70 ? 541 PHE B CD2   1 
ATOM   8333 C  CE1   . PHE B 1 514 ? 61.759  -4.747  11.843  1.00 155.60 ? 541 PHE B CE1   1 
ATOM   8334 C  CE2   . PHE B 1 514 ? 63.564  -5.930  12.865  1.00 152.15 ? 541 PHE B CE2   1 
ATOM   8335 C  CZ    . PHE B 1 514 ? 62.986  -4.740  12.474  1.00 153.09 ? 541 PHE B CZ    1 
ATOM   8336 N  N     . SER B 1 515 ? 61.614  -11.504 10.339  1.00 171.63 ? 542 SER B N     1 
ATOM   8337 C  CA    . SER B 1 515 ? 61.168  -12.886 10.147  1.00 167.78 ? 542 SER B CA    1 
ATOM   8338 C  C     . SER B 1 515 ? 60.619  -13.487 11.440  1.00 172.59 ? 542 SER B C     1 
ATOM   8339 O  O     . SER B 1 515 ? 59.405  -13.651 11.595  1.00 179.96 ? 542 SER B O     1 
ATOM   8340 C  CB    . SER B 1 515 ? 62.313  -13.737 9.584   1.00 160.34 ? 542 SER B CB    1 
ATOM   8341 O  OG    . SER B 1 515 ? 63.413  -13.788 10.477  1.00 164.07 ? 542 SER B OG    1 
ATOM   8342 N  N     . LEU B 1 516 ? 61.502  -13.824 12.380  1.00 163.04 ? 543 LEU B N     1 
ATOM   8343 C  CA    . LEU B 1 516 ? 61.089  -14.475 13.619  1.00 154.09 ? 543 LEU B CA    1 
ATOM   8344 C  C     . LEU B 1 516 ? 60.587  -13.431 14.612  1.00 159.66 ? 543 LEU B C     1 
ATOM   8345 O  O     . LEU B 1 516 ? 61.335  -12.532 15.011  1.00 153.95 ? 543 LEU B O     1 
ATOM   8346 C  CB    . LEU B 1 516 ? 62.245  -15.276 14.215  1.00 140.83 ? 543 LEU B CB    1 
ATOM   8347 C  CG    . LEU B 1 516 ? 61.935  -16.014 15.520  1.00 147.80 ? 543 LEU B CG    1 
ATOM   8348 C  CD1   . LEU B 1 516 ? 60.760  -16.962 15.332  1.00 142.88 ? 543 LEU B CD1   1 
ATOM   8349 C  CD2   . LEU B 1 516 ? 63.156  -16.765 16.029  1.00 144.74 ? 543 LEU B CD2   1 
ATOM   8350 N  N     . ARG B 1 517 ? 59.316  -13.556 15.015  1.00 160.14 ? 544 ARG B N     1 
ATOM   8351 C  CA    . ARG B 1 517 ? 58.667  -12.619 15.934  1.00 166.59 ? 544 ARG B CA    1 
ATOM   8352 C  C     . ARG B 1 517 ? 57.959  -13.424 17.030  1.00 164.55 ? 544 ARG B C     1 
ATOM   8353 O  O     . ARG B 1 517 ? 56.729  -13.440 17.113  1.00 160.38 ? 544 ARG B O     1 
ATOM   8354 C  CB    . ARG B 1 517 ? 57.686  -11.705 15.190  1.00 169.06 ? 544 ARG B CB    1 
ATOM   8355 C  CG    . ARG B 1 517 ? 58.193  -11.181 13.851  1.00 172.29 ? 544 ARG B CG    1 
ATOM   8356 C  CD    . ARG B 1 517 ? 57.110  -10.412 13.104  1.00 172.24 ? 544 ARG B CD    1 
ATOM   8357 N  NE    . ARG B 1 517 ? 55.889  -11.194 12.949  1.00 172.54 ? 544 ARG B NE    1 
ATOM   8358 C  CZ    . ARG B 1 517 ? 55.607  -11.943 11.892  1.00 161.68 ? 544 ARG B CZ    1 
ATOM   8359 N  NH1   . ARG B 1 517 ? 56.438  -12.031 10.866  1.00 162.60 ? 544 ARG B NH1   1 
ATOM   8360 N  NH2   . ARG B 1 517 ? 54.463  -12.621 11.863  1.00 156.57 ? 544 ARG B NH2   1 
ATOM   8361 N  N     . ASN B 1 518 ? 58.743  -14.084 17.881  1.00 165.23 ? 545 ASN B N     1 
ATOM   8362 C  CA    . ASN B 1 518 ? 58.219  -14.959 18.926  1.00 161.18 ? 545 ASN B CA    1 
ATOM   8363 C  C     . ASN B 1 518 ? 58.462  -14.386 20.320  1.00 154.30 ? 545 ASN B C     1 
ATOM   8364 O  O     . ASN B 1 518 ? 58.831  -15.105 21.251  1.00 156.72 ? 545 ASN B O     1 
ATOM   8365 C  CB    . ASN B 1 518 ? 58.825  -16.357 18.812  1.00 160.72 ? 545 ASN B CB    1 
ATOM   8366 C  CG    . ASN B 1 518 ? 60.330  -16.362 19.007  1.00 154.95 ? 545 ASN B CG    1 
ATOM   8367 O  OD1   . ASN B 1 518 ? 60.998  -15.345 18.816  1.00 156.38 ? 545 ASN B OD1   1 
ATOM   8368 N  ND2   . ASN B 1 518 ? 60.870  -17.512 19.391  1.00 150.60 ? 545 ASN B ND2   1 
ATOM   8369 N  N     . LEU B 1 519 ? 58.245  -13.084 20.481  1.00 154.23 ? 546 LEU B N     1 
ATOM   8370 C  CA    . LEU B 1 519 ? 58.470  -12.430 21.762  1.00 146.15 ? 546 LEU B CA    1 
ATOM   8371 C  C     . LEU B 1 519 ? 57.249  -12.600 22.659  1.00 148.88 ? 546 LEU B C     1 
ATOM   8372 O  O     . LEU B 1 519 ? 56.114  -12.384 22.225  1.00 147.38 ? 546 LEU B O     1 
ATOM   8373 C  CB    . LEU B 1 519 ? 58.776  -10.948 21.557  1.00 135.97 ? 546 LEU B CB    1 
ATOM   8374 C  CG    . LEU B 1 519 ? 59.630  -10.287 22.639  1.00 129.52 ? 546 LEU B CG    1 
ATOM   8375 C  CD1   . LEU B 1 519 ? 61.034  -10.871 22.627  1.00 118.78 ? 546 LEU B CD1   1 
ATOM   8376 C  CD2   . LEU B 1 519 ? 59.663  -8.778  22.449  1.00 131.48 ? 546 LEU B CD2   1 
ATOM   8377 N  N     . HIS B 1 520 ? 57.486  -12.990 23.910  1.00 172.71 ? 547 HIS B N     1 
ATOM   8378 C  CA    . HIS B 1 520 ? 56.415  -13.173 24.888  1.00 170.68 ? 547 HIS B CA    1 
ATOM   8379 C  C     . HIS B 1 520 ? 56.286  -11.877 25.677  1.00 167.89 ? 547 HIS B C     1 
ATOM   8380 O  O     . HIS B 1 520 ? 56.983  -11.655 26.668  1.00 164.90 ? 547 HIS B O     1 
ATOM   8381 C  CB    . HIS B 1 520 ? 56.703  -14.362 25.797  1.00 179.51 ? 547 HIS B CB    1 
ATOM   8382 C  CG    . HIS B 1 520 ? 56.796  -15.674 25.078  1.00 182.03 ? 547 HIS B CG    1 
ATOM   8383 N  ND1   . HIS B 1 520 ? 56.315  -16.849 25.615  1.00 193.27 ? 547 HIS B ND1   1 
ATOM   8384 C  CD2   . HIS B 1 520 ? 57.323  -16.001 23.874  1.00 175.05 ? 547 HIS B CD2   1 
ATOM   8385 C  CE1   . HIS B 1 520 ? 56.534  -17.841 24.770  1.00 195.82 ? 547 HIS B CE1   1 
ATOM   8386 N  NE2   . HIS B 1 520 ? 57.145  -17.354 23.706  1.00 191.15 ? 547 HIS B NE2   1 
ATOM   8387 N  N     . ALA B 1 521 ? 55.383  -11.006 25.231  1.00 145.19 ? 548 ALA B N     1 
ATOM   8388 C  CA    . ALA B 1 521 ? 55.198  -9.693  25.832  1.00 143.89 ? 548 ALA B CA    1 
ATOM   8389 C  C     . ALA B 1 521 ? 53.930  -9.659  26.673  1.00 142.09 ? 548 ALA B C     1 
ATOM   8390 O  O     . ALA B 1 521 ? 52.879  -10.151 26.253  1.00 143.76 ? 548 ALA B O     1 
ATOM   8391 C  CB    . ALA B 1 521 ? 55.135  -8.598  24.768  1.00 136.69 ? 548 ALA B CB    1 
ATOM   8392 N  N     . PHE B 1 522 ? 54.039  -9.071  27.860  1.00 140.63 ? 549 PHE B N     1 
ATOM   8393 C  CA    . PHE B 1 522 ? 52.910  -8.874  28.753  1.00 133.99 ? 549 PHE B CA    1 
ATOM   8394 C  C     . PHE B 1 522 ? 52.935  -7.444  29.270  1.00 133.25 ? 549 PHE B C     1 
ATOM   8395 O  O     . PHE B 1 522 ? 53.895  -6.700  29.059  1.00 132.23 ? 549 PHE B O     1 
ATOM   8396 C  CB    . PHE B 1 522 ? 52.931  -9.878  29.914  1.00 122.04 ? 549 PHE B CB    1 
ATOM   8397 C  CG    . PHE B 1 522 ? 52.909  -11.309 29.469  1.00 136.41 ? 549 PHE B CG    1 
ATOM   8398 C  CD1   . PHE B 1 522 ? 51.789  -11.835 28.848  1.00 134.68 ? 549 PHE B CD1   1 
ATOM   8399 C  CD2   . PHE B 1 522 ? 54.007  -12.128 29.663  1.00 140.82 ? 549 PHE B CD2   1 
ATOM   8400 C  CE1   . PHE B 1 522 ? 51.762  -13.151 28.431  1.00 135.23 ? 549 PHE B CE1   1 
ATOM   8401 C  CE2   . PHE B 1 522 ? 53.986  -13.449 29.248  1.00 140.46 ? 549 PHE B CE2   1 
ATOM   8402 C  CZ    . PHE B 1 522 ? 52.862  -13.960 28.632  1.00 135.11 ? 549 PHE B CZ    1 
ATOM   8403 N  N     . SER B 1 523 ? 51.860  -7.056  29.949  1.00 133.16 ? 550 SER B N     1 
ATOM   8404 C  CA    . SER B 1 523 ? 51.732  -5.700  30.456  1.00 128.86 ? 550 SER B CA    1 
ATOM   8405 C  C     . SER B 1 523 ? 51.079  -5.727  31.829  1.00 134.41 ? 550 SER B C     1 
ATOM   8406 O  O     . SER B 1 523 ? 50.118  -6.469  32.055  1.00 131.56 ? 550 SER B O     1 
ATOM   8407 C  CB    . SER B 1 523 ? 50.910  -4.823  29.508  1.00 128.61 ? 550 SER B CB    1 
ATOM   8408 O  OG    . SER B 1 523 ? 50.609  -3.575  30.107  1.00 129.28 ? 550 SER B OG    1 
ATOM   8409 N  N     . VAL B 1 524 ? 51.614  -4.918  32.744  1.00 129.94 ? 551 VAL B N     1 
ATOM   8410 C  CA    . VAL B 1 524 ? 50.984  -4.749  34.043  1.00 123.35 ? 551 VAL B CA    1 
ATOM   8411 C  C     . VAL B 1 524 ? 49.645  -4.052  33.860  1.00 126.91 ? 551 VAL B C     1 
ATOM   8412 O  O     . VAL B 1 524 ? 49.523  -3.081  33.104  1.00 118.27 ? 551 VAL B O     1 
ATOM   8413 C  CB    . VAL B 1 524 ? 51.898  -3.959  34.995  1.00 128.31 ? 551 VAL B CB    1 
ATOM   8414 C  CG1   . VAL B 1 524 ? 51.305  -3.929  36.392  1.00 131.15 ? 551 VAL B CG1   1 
ATOM   8415 C  CG2   . VAL B 1 524 ? 53.293  -4.549  35.015  1.00 117.69 ? 551 VAL B CG2   1 
ATOM   8416 N  N     . GLU B 1 525 ? 48.628  -4.556  34.540  1.00 132.60 ? 552 GLU B N     1 
ATOM   8417 C  CA    . GLU B 1 525 ? 47.292  -3.975  34.452  1.00 134.31 ? 552 GLU B CA    1 
ATOM   8418 C  C     . GLU B 1 525 ? 46.690  -3.862  35.847  1.00 133.57 ? 552 GLU B C     1 
ATOM   8419 O  O     . GLU B 1 525 ? 46.392  -4.884  36.473  1.00 140.99 ? 552 GLU B O     1 
ATOM   8420 C  CB    . GLU B 1 525 ? 46.397  -4.817  33.543  1.00 137.72 ? 552 GLU B CB    1 
ATOM   8421 C  CG    . GLU B 1 525 ? 45.028  -4.202  33.275  1.00 133.61 ? 552 GLU B CG    1 
ATOM   8422 C  CD    . GLU B 1 525 ? 45.109  -2.929  32.452  1.00 150.88 ? 552 GLU B CD    1 
ATOM   8423 O  OE1   . GLU B 1 525 ? 46.120  -2.732  31.743  1.00 151.59 ? 552 GLU B OE1   1 
ATOM   8424 O  OE2   . GLU B 1 525 ? 44.158  -2.121  32.516  1.00 153.51 ? 552 GLU B OE2   1 
ATOM   8425 N  N     . PRO B 1 526 ? 46.474  -2.645  36.366  1.00 128.65 ? 553 PRO B N     1 
ATOM   8426 C  CA    . PRO B 1 526 ? 46.682  -1.336  35.731  1.00 124.43 ? 553 PRO B CA    1 
ATOM   8427 C  C     . PRO B 1 526 ? 48.151  -0.957  35.572  1.00 122.53 ? 553 PRO B C     1 
ATOM   8428 O  O     . PRO B 1 526 ? 49.025  -1.505  36.236  1.00 121.23 ? 553 PRO B O     1 
ATOM   8429 C  CB    . PRO B 1 526 ? 45.964  -0.383  36.698  1.00 122.51 ? 553 PRO B CB    1 
ATOM   8430 C  CG    . PRO B 1 526 ? 46.120  -1.039  38.035  1.00 118.35 ? 553 PRO B CG    1 
ATOM   8431 C  CD    . PRO B 1 526 ? 45.976  -2.509  37.748  1.00 113.52 ? 553 PRO B CD    1 
ATOM   8432 N  N     . LEU B 1 527 ? 48.437  -0.020  34.672  1.00 111.16 ? 554 LEU B N     1 
ATOM   8433 C  CA    . LEU B 1 527 ? 49.807  0.414   34.449  1.00 107.31 ? 554 LEU B CA    1 
ATOM   8434 C  C     . LEU B 1 527 ? 50.344  1.127   35.683  1.00 104.08 ? 554 LEU B C     1 
ATOM   8435 O  O     . LEU B 1 527 ? 49.628  1.886   36.342  1.00 110.55 ? 554 LEU B O     1 
ATOM   8436 C  CB    . LEU B 1 527 ? 49.877  1.334   33.230  1.00 103.44 ? 554 LEU B CB    1 
ATOM   8437 C  CG    . LEU B 1 527 ? 49.516  0.687   31.889  1.00 120.88 ? 554 LEU B CG    1 
ATOM   8438 C  CD1   . LEU B 1 527 ? 49.385  1.738   30.798  1.00 124.65 ? 554 LEU B CD1   1 
ATOM   8439 C  CD2   . LEU B 1 527 ? 50.549  -0.361  31.500  1.00 118.29 ? 554 LEU B CD2   1 
ATOM   8440 N  N     . LEU B 1 528 ? 51.614  0.876   35.997  1.00 103.32 ? 555 LEU B N     1 
ATOM   8441 C  CA    . LEU B 1 528 ? 52.231  1.432   37.193  1.00 101.38 ? 555 LEU B CA    1 
ATOM   8442 C  C     . LEU B 1 528 ? 52.965  2.742   36.942  1.00 99.89  ? 555 LEU B C     1 
ATOM   8443 O  O     . LEU B 1 528 ? 53.305  3.435   37.906  1.00 92.51  ? 555 LEU B O     1 
ATOM   8444 C  CB    . LEU B 1 528 ? 53.201  0.417   37.806  1.00 96.51  ? 555 LEU B CB    1 
ATOM   8445 C  CG    . LEU B 1 528 ? 52.569  -0.881  38.313  1.00 106.42 ? 555 LEU B CG    1 
ATOM   8446 C  CD1   . LEU B 1 528 ? 53.640  -1.877  38.730  1.00 99.07  ? 555 LEU B CD1   1 
ATOM   8447 C  CD2   . LEU B 1 528 ? 51.617  -0.596  39.468  1.00 97.13  ? 555 LEU B CD2   1 
ATOM   8448 N  N     . ILE B 1 529 ? 53.215  3.102   35.685  1.00 96.88  ? 556 ILE B N     1 
ATOM   8449 C  CA    . ILE B 1 529 ? 53.967  4.308   35.356  1.00 92.94  ? 556 ILE B CA    1 
ATOM   8450 C  C     . ILE B 1 529 ? 53.314  4.992   34.162  1.00 87.87  ? 556 ILE B C     1 
ATOM   8451 O  O     . ILE B 1 529 ? 52.954  4.335   33.180  1.00 94.33  ? 556 ILE B O     1 
ATOM   8452 C  CB    . ILE B 1 529 ? 55.448  3.992   35.067  1.00 95.94  ? 556 ILE B CB    1 
ATOM   8453 C  CG1   . ILE B 1 529 ? 56.176  3.642   36.366  1.00 99.65  ? 556 ILE B CG1   1 
ATOM   8454 C  CG2   . ILE B 1 529 ? 56.126  5.160   34.382  1.00 88.35  ? 556 ILE B CG2   1 
ATOM   8455 C  CD1   . ILE B 1 529 ? 57.654  3.439   36.196  1.00 102.00 ? 556 ILE B CD1   1 
ATOM   8456 N  N     . TYR B 1 530 ? 53.156  6.312   34.251  1.00 93.57  ? 557 TYR B N     1 
ATOM   8457 C  CA    . TYR B 1 530 ? 52.579  7.127   33.190  1.00 98.97  ? 557 TYR B CA    1 
ATOM   8458 C  C     . TYR B 1 530 ? 53.574  8.215   32.798  1.00 104.44 ? 557 TYR B C     1 
ATOM   8459 O  O     . TYR B 1 530 ? 54.571  8.419   33.502  1.00 105.81 ? 557 TYR B O     1 
ATOM   8460 C  CB    . TYR B 1 530 ? 51.250  7.739   33.647  1.00 104.93 ? 557 TYR B CB    1 
ATOM   8461 C  CG    . TYR B 1 530 ? 50.171  6.727   33.975  1.00 103.67 ? 557 TYR B CG    1 
ATOM   8462 C  CD1   . TYR B 1 530 ? 49.383  6.175   32.975  1.00 106.86 ? 557 TYR B CD1   1 
ATOM   8463 C  CD2   . TYR B 1 530 ? 49.930  6.337   35.287  1.00 101.05 ? 557 TYR B CD2   1 
ATOM   8464 C  CE1   . TYR B 1 530 ? 48.392  5.256   33.269  1.00 108.10 ? 557 TYR B CE1   1 
ATOM   8465 C  CE2   . TYR B 1 530 ? 48.940  5.418   35.591  1.00 109.40 ? 557 TYR B CE2   1 
ATOM   8466 C  CZ    . TYR B 1 530 ? 48.174  4.881   34.578  1.00 112.74 ? 557 TYR B CZ    1 
ATOM   8467 O  OH    . TYR B 1 530 ? 47.188  3.967   34.875  1.00 114.06 ? 557 TYR B OH    1 
ATOM   8468 N  N     . PRO B 1 531 ? 53.366  8.912   31.682  1.00 114.23 ? 558 PRO B N     1 
ATOM   8469 C  CA    . PRO B 1 531 ? 54.239  10.045  31.352  1.00 107.36 ? 558 PRO B CA    1 
ATOM   8470 C  C     . PRO B 1 531 ? 53.992  11.238  32.264  1.00 109.18 ? 558 PRO B C     1 
ATOM   8471 O  O     . PRO B 1 531 ? 52.951  11.363  32.914  1.00 112.88 ? 558 PRO B O     1 
ATOM   8472 C  CB    . PRO B 1 531 ? 53.865  10.376  29.902  1.00 114.01 ? 558 PRO B CB    1 
ATOM   8473 C  CG    . PRO B 1 531 ? 53.202  9.147   29.380  1.00 116.43 ? 558 PRO B CG    1 
ATOM   8474 C  CD    . PRO B 1 531 ? 52.499  8.541   30.551  1.00 116.73 ? 558 PRO B CD    1 
ATOM   8475 N  N     . THR B 1 532 ? 54.984  12.131  32.304  1.00 110.45 ? 559 THR B N     1 
ATOM   8476 C  CA    . THR B 1 532 ? 54.860  13.360  33.091  1.00 113.44 ? 559 THR B CA    1 
ATOM   8477 C  C     . THR B 1 532 ? 53.924  14.351  32.407  1.00 123.18 ? 559 THR B C     1 
ATOM   8478 O  O     . THR B 1 532 ? 52.844  14.659  32.919  1.00 116.16 ? 559 THR B O     1 
ATOM   8479 C  CB    . THR B 1 532 ? 56.236  13.995  33.320  1.00 108.94 ? 559 THR B CB    1 
ATOM   8480 O  OG1   . THR B 1 532 ? 56.882  14.216  32.059  1.00 128.42 ? 559 THR B OG1   1 
ATOM   8481 C  CG2   . THR B 1 532 ? 57.104  13.100  34.187  1.00 87.67  ? 559 THR B CG2   1 
ATOM   8482 N  N     . HIS B 1 533 ? 54.334  14.867  31.248  1.00 131.81 ? 560 HIS B N     1 
ATOM   8483 C  CA    . HIS B 1 533 ? 53.539  15.835  30.507  1.00 142.22 ? 560 HIS B CA    1 
ATOM   8484 C  C     . HIS B 1 533 ? 52.609  15.181  29.491  1.00 141.54 ? 560 HIS B C     1 
ATOM   8485 O  O     . HIS B 1 533 ? 52.181  15.852  28.545  1.00 153.71 ? 560 HIS B O     1 
ATOM   8486 C  CB    . HIS B 1 533 ? 54.454  16.855  29.824  1.00 129.86 ? 560 HIS B CB    1 
ATOM   8487 C  CG    . HIS B 1 533 ? 55.031  17.862  30.769  1.00 127.34 ? 560 HIS B CG    1 
ATOM   8488 N  ND1   . HIS B 1 533 ? 55.910  17.519  31.775  1.00 111.04 ? 560 HIS B ND1   1 
ATOM   8489 C  CD2   . HIS B 1 533 ? 54.833  19.197  30.880  1.00 133.28 ? 560 HIS B CD2   1 
ATOM   8490 C  CE1   . HIS B 1 533 ? 56.234  18.601  32.460  1.00 136.37 ? 560 HIS B CE1   1 
ATOM   8491 N  NE2   . HIS B 1 533 ? 55.596  19.633  31.935  1.00 142.00 ? 560 HIS B NE2   1 
ATOM   8492 N  N     . TYR B 1 534 ? 52.276  13.903  29.684  1.00 137.39 ? 561 TYR B N     1 
ATOM   8493 C  CA    . TYR B 1 534 ? 51.369  13.146  28.812  1.00 151.52 ? 561 TYR B CA    1 
ATOM   8494 C  C     . TYR B 1 534 ? 51.538  13.455  27.324  1.00 149.52 ? 561 TYR B C     1 
ATOM   8495 O  O     . TYR B 1 534 ? 50.581  13.833  26.648  1.00 142.37 ? 561 TYR B O     1 
ATOM   8496 C  CB    . TYR B 1 534 ? 49.911  13.385  29.226  1.00 162.46 ? 561 TYR B CB    1 
ATOM   8497 C  CG    . TYR B 1 534 ? 49.361  12.337  30.174  1.00 163.75 ? 561 TYR B CG    1 
ATOM   8498 C  CD1   . TYR B 1 534 ? 50.190  11.687  31.080  1.00 160.77 ? 561 TYR B CD1   1 
ATOM   8499 C  CD2   . TYR B 1 534 ? 48.015  11.985  30.150  1.00 161.98 ? 561 TYR B CD2   1 
ATOM   8500 C  CE1   . TYR B 1 534 ? 49.694  10.726  31.943  1.00 159.87 ? 561 TYR B CE1   1 
ATOM   8501 C  CE2   . TYR B 1 534 ? 47.509  11.021  31.010  1.00 159.41 ? 561 TYR B CE2   1 
ATOM   8502 C  CZ    . TYR B 1 534 ? 48.354  10.395  31.904  1.00 163.92 ? 561 TYR B CZ    1 
ATOM   8503 O  OH    . TYR B 1 534 ? 47.863  9.438   32.762  1.00 162.00 ? 561 TYR B OH    1 
HETATM 8504 HG HG    . HG  C 2 .   ? 52.362  59.601  75.511  0.67 166.84 ? 701 HG  A HG    1 
HETATM 8505 HG HG    . HG  D 2 .   ? 47.095  72.428  70.885  0.68 314.94 ? 702 HG  A HG    1 
HETATM 8506 HG HG    . HG  E 2 .   ? 14.334  84.262  95.962  0.72 308.83 ? 703 HG  A HG    1 
HETATM 8507 HG HG    . HG  F 2 .   ? 31.629  74.683  92.572  0.50 163.51 ? 704 HG  A HG    1 
HETATM 8508 HG HG    . HG  G 2 .   ? 16.314  68.043  103.897 0.93 351.21 ? 705 HG  A HG    1 
HETATM 8509 CL CL    . CL  H 3 .   ? 38.874  37.871  91.417  1.00 107.36 ? 706 CL  A CL    1 
HETATM 8510 CL CL    . CL  I 3 .   ? 37.499  76.891  82.893  1.00 116.53 ? 707 CL  A CL    1 
HETATM 8511 CL CL    . CL  J 3 .   ? 49.790  70.869  85.561  1.00 108.91 ? 708 CL  A CL    1 
HETATM 8512 CL CL    . CL  K 3 .   ? 18.787  66.715  103.377 1.00 101.04 ? 709 CL  A CL    1 
HETATM 8513 N  N1    . GDU L 4 .   ? 47.813  54.913  92.234  1.00 62.34  ? 710 GDU A N1    1 
HETATM 8514 C  C2    . GDU L 4 .   ? 47.979  53.474  92.658  1.00 71.96  ? 710 GDU A C2    1 
HETATM 8515 N  N3    . GDU L 4 .   ? 49.064  53.069  93.606  1.00 53.84  ? 710 GDU A N3    1 
HETATM 8516 C  C4    . GDU L 4 .   ? 49.981  54.094  94.105  1.00 85.62  ? 710 GDU A C4    1 
HETATM 8517 C  C5    . GDU L 4 .   ? 49.823  55.512  93.669  1.00 75.37  ? 710 GDU A C5    1 
HETATM 8518 C  C6    . GDU L 4 .   ? 48.740  55.912  92.726  1.00 56.79  ? 710 GDU A C6    1 
HETATM 8519 O  O2    . GDU L 4 .   ? 47.236  52.626  92.262  1.00 82.16  ? 710 GDU A O2    1 
HETATM 8520 O  O4    . GDU L 4 .   ? 50.851  53.786  94.863  1.00 82.57  ? 710 GDU A O4    1 
HETATM 8521 C  C1D   . GDU L 4 .   ? 46.757  55.275  91.275  1.00 75.90  ? 710 GDU A C1D   1 
HETATM 8522 C  C2D   . GDU L 4 .   ? 45.510  56.036  91.833  1.00 78.67  ? 710 GDU A C2D   1 
HETATM 8523 O  O2D   . GDU L 4 .   ? 44.609  55.201  92.417  1.00 70.20  ? 710 GDU A O2D   1 
HETATM 8524 C  C3D   . GDU L 4 .   ? 44.923  56.627  90.553  1.00 73.68  ? 710 GDU A C3D   1 
HETATM 8525 C  C4D   . GDU L 4 .   ? 45.964  56.842  89.739  1.00 64.36  ? 710 GDU A C4D   1 
HETATM 8526 O  O4D   . GDU L 4 .   ? 47.238  56.123  90.403  1.00 76.43  ? 710 GDU A O4D   1 
HETATM 8527 O  O3D   . GDU L 4 .   ? 43.992  55.674  89.888  1.00 66.76  ? 710 GDU A O3D   1 
HETATM 8528 C  C5D   . GDU L 4 .   ? 46.241  58.325  89.651  1.00 80.93  ? 710 GDU A C5D   1 
HETATM 8529 O  O5D   . GDU L 4 .   ? 46.688  58.750  90.965  1.00 94.66  ? 710 GDU A O5D   1 
HETATM 8530 P  PA    . GDU L 4 .   ? 45.885  59.981  91.722  1.00 71.55  ? 710 GDU A PA    1 
HETATM 8531 O  O1A   . GDU L 4 .   ? 44.549  60.234  91.076  1.00 75.10  ? 710 GDU A O1A   1 
HETATM 8532 O  O2A   . GDU L 4 .   ? 45.701  59.660  93.188  1.00 74.38  ? 710 GDU A O2A   1 
HETATM 8533 O  O3A   . GDU L 4 .   ? 46.873  61.295  91.544  1.00 68.12  ? 710 GDU A O3A   1 
HETATM 8534 P  PB    . GDU L 4 .   ? 46.442  62.633  90.683  1.00 72.52  ? 710 GDU A PB    1 
HETATM 8535 O  O1B   . GDU L 4 .   ? 44.975  62.941  90.989  1.00 73.60  ? 710 GDU A O1B   1 
HETATM 8536 O  O2B   . GDU L 4 .   ? 47.358  63.778  91.132  1.00 74.64  ? 710 GDU A O2B   1 
HETATM 8537 O  O3B   . GDU L 4 .   ? 46.600  62.433  89.029  1.00 95.89  ? 710 GDU A O3B   1 
HETATM 8538 C  "C1'" . GDU L 4 .   ? 47.632  61.780  88.413  1.00 76.41  ? 710 GDU A "C1'" 1 
HETATM 8539 C  "C2'" . GDU L 4 .   ? 49.011  62.169  88.946  1.00 79.27  ? 710 GDU A "C2'" 1 
HETATM 8540 C  "C3'" . GDU L 4 .   ? 50.111  61.860  87.985  1.00 78.83  ? 710 GDU A "C3'" 1 
HETATM 8541 C  "C4'" . GDU L 4 .   ? 49.746  60.868  86.925  1.00 91.52  ? 710 GDU A "C4'" 1 
HETATM 8542 C  "C5'" . GDU L 4 .   ? 48.500  61.329  86.134  1.00 93.46  ? 710 GDU A "C5'" 1 
HETATM 8543 C  "C6'" . GDU L 4 .   ? 47.807  60.159  85.519  1.00 90.89  ? 710 GDU A "C6'" 1 
HETATM 8544 O  "O2'" . GDU L 4 .   ? 49.015  63.586  89.157  1.00 103.93 ? 710 GDU A "O2'" 1 
HETATM 8545 O  "O3'" . GDU L 4 .   ? 51.285  61.366  88.707  1.00 69.17  ? 710 GDU A "O3'" 1 
HETATM 8546 O  "O4'" . GDU L 4 .   ? 49.567  59.558  87.481  1.00 64.68  ? 710 GDU A "O4'" 1 
HETATM 8547 O  "O5'" . GDU L 4 .   ? 47.553  62.113  86.955  1.00 76.93  ? 710 GDU A "O5'" 1 
HETATM 8548 O  "O6'" . GDU L 4 .   ? 47.111  59.423  86.508  1.00 86.84  ? 710 GDU A "O6'" 1 
HETATM 8549 O  O1    . MES M 5 .   ? 51.087  66.040  105.870 1.00 101.27 ? 711 MES A O1    1 
HETATM 8550 C  C2    . MES M 5 .   ? 51.266  64.679  106.244 1.00 100.61 ? 711 MES A C2    1 
HETATM 8551 C  C3    . MES M 5 .   ? 50.153  63.831  105.646 1.00 105.51 ? 711 MES A C3    1 
HETATM 8552 N  N4    . MES M 5 .   ? 48.864  64.437  105.954 1.00 93.40  ? 711 MES A N4    1 
HETATM 8553 C  C5    . MES M 5 .   ? 48.670  65.882  105.876 1.00 96.75  ? 711 MES A C5    1 
HETATM 8554 C  C6    . MES M 5 .   ? 49.900  66.571  106.448 1.00 99.87  ? 711 MES A C6    1 
HETATM 8555 C  C7    . MES M 5 .   ? 47.713  63.636  105.572 1.00 100.41 ? 711 MES A C7    1 
HETATM 8556 C  C8    . MES M 5 .   ? 47.177  63.013  106.851 1.00 107.38 ? 711 MES A C8    1 
HETATM 8557 S  S     . MES M 5 .   ? 46.206  61.738  106.410 1.00 126.91 ? 711 MES A S     1 
HETATM 8558 O  O1S   . MES M 5 .   ? 47.010  60.723  105.693 1.00 118.66 ? 711 MES A O1S   1 
HETATM 8559 O  O2S   . MES M 5 .   ? 45.124  62.222  105.524 1.00 100.29 ? 711 MES A O2S   1 
HETATM 8560 O  O3S   . MES M 5 .   ? 45.622  61.124  107.624 1.00 151.09 ? 711 MES A O3S   1 
HETATM 8561 O  O1    . MES N 5 .   ? 44.023  70.600  100.591 1.00 126.28 ? 712 MES A O1    1 
HETATM 8562 C  C2    . MES N 5 .   ? 44.745  71.374  101.547 1.00 141.70 ? 712 MES A C2    1 
HETATM 8563 C  C3    . MES N 5 .   ? 43.847  71.673  102.745 1.00 150.52 ? 712 MES A C3    1 
HETATM 8564 N  N4    . MES N 5 .   ? 42.490  71.811  102.229 1.00 144.99 ? 712 MES A N4    1 
HETATM 8565 C  C5    . MES N 5 .   ? 42.280  72.309  100.877 1.00 128.39 ? 712 MES A C5    1 
HETATM 8566 C  C6    . MES N 5 .   ? 42.987  71.336  99.937  1.00 122.02 ? 712 MES A C6    1 
HETATM 8567 C  C7    . MES N 5 .   ? 41.384  71.877  103.177 1.00 135.40 ? 712 MES A C7    1 
HETATM 8568 C  C8    . MES N 5 .   ? 40.860  73.311  103.125 1.00 147.08 ? 712 MES A C8    1 
HETATM 8569 S  S     . MES N 5 .   ? 39.568  73.466  104.163 1.00 172.51 ? 712 MES A S     1 
HETATM 8570 O  O1S   . MES N 5 .   ? 39.727  72.508  105.281 1.00 161.11 ? 712 MES A O1S   1 
HETATM 8571 O  O2S   . MES N 5 .   ? 38.306  73.173  103.446 1.00 142.49 ? 712 MES A O2S   1 
HETATM 8572 O  O3S   . MES N 5 .   ? 39.514  74.851  104.688 1.00 157.04 ? 712 MES A O3S   1 
HETATM 8573 CA CA    . CA  O 6 .   ? 43.116  61.955  90.357  1.00 109.51 ? 713 CA  A CA    1 
HETATM 8574 HG HG    . HG  P 2 .   ? 31.945  23.777  58.060  0.43 211.34 ? 701 HG  B HG    1 
HETATM 8575 HG HG    . HG  Q 2 .   ? 30.268  23.978  43.587  0.67 188.19 ? 702 HG  B HG    1 
HETATM 8576 HG HG    . HG  R 2 .   ? 70.419  5.991   40.851  0.87 339.41 ? 703 HG  B HG    1 
HETATM 8577 HG HG    . HG  S 2 .   ? 38.880  -6.127  56.118  0.77 185.39 ? 704 HG  B HG    1 
HETATM 8578 CL CL    . CL  T 3 .   ? 38.412  -5.077  53.413  1.00 123.69 ? 705 CL  B CL    1 
HETATM 8579 CL CL    . CL  U 3 .   ? 36.683  -7.941  57.192  1.00 137.01 ? 706 CL  B CL    1 
HETATM 8580 CL CL    . CL  V 3 .   ? 68.843  5.918   42.937  1.00 141.33 ? 707 CL  B CL    1 
HETATM 8581 N  N1    . GDU W 4 .   ? 44.108  12.651  64.515  1.00 72.26  ? 708 GDU B N1    1 
HETATM 8582 C  C2    . GDU W 4 .   ? 44.411  12.749  65.986  1.00 70.39  ? 708 GDU B C2    1 
HETATM 8583 N  N3    . GDU W 4 .   ? 43.863  11.754  66.956  1.00 55.66  ? 708 GDU B N3    1 
HETATM 8584 C  C4    . GDU W 4 .   ? 43.006  10.685  66.444  1.00 84.13  ? 708 GDU B C4    1 
HETATM 8585 C  C5    . GDU W 4 .   ? 42.703  10.605  64.990  1.00 73.87  ? 708 GDU B C5    1 
HETATM 8586 C  C6    . GDU W 4 .   ? 43.248  11.596  64.028  1.00 65.13  ? 708 GDU B C6    1 
HETATM 8587 O  O2    . GDU W 4 .   ? 45.110  13.623  66.403  1.00 76.20  ? 708 GDU B O2    1 
HETATM 8588 O  O4    . GDU W 4 .   ? 42.553  9.874   67.196  1.00 85.71  ? 708 GDU B O4    1 
HETATM 8589 C  C1D   . GDU W 4 .   ? 44.641  13.671  63.604  1.00 80.75  ? 708 GDU B C1D   1 
HETATM 8590 C  C2D   . GDU W 4 .   ? 45.474  13.155  62.384  1.00 76.98  ? 708 GDU B C2D   1 
HETATM 8591 O  O2D   . GDU W 4 .   ? 46.811  13.228  62.639  1.00 81.29  ? 708 GDU B O2D   1 
HETATM 8592 C  C3D   . GDU W 4 .   ? 45.125  14.157  61.297  1.00 77.07  ? 708 GDU B C3D   1 
HETATM 8593 C  C4D   . GDU W 4 .   ? 43.835  14.408  61.508  1.00 70.57  ? 708 GDU B C4D   1 
HETATM 8594 O  O4D   . GDU W 4 .   ? 43.614  14.303  63.091  1.00 81.60  ? 708 GDU B O4D   1 
HETATM 8595 O  O3D   . GDU W 4 .   ? 45.911  15.414  61.448  1.00 84.66  ? 708 GDU B O3D   1 
HETATM 8596 C  C5D   . GDU W 4 .   ? 43.023  13.356  60.799  1.00 74.12  ? 708 GDU B C5D   1 
HETATM 8597 O  O5D   . GDU W 4 .   ? 43.678  13.177  59.518  1.00 99.46  ? 708 GDU B O5D   1 
HETATM 8598 P  PA    . GDU W 4 .   ? 43.888  11.650  58.928  1.00 67.55  ? 708 GDU B PA    1 
HETATM 8599 O  O1A   . GDU W 4 .   ? 44.898  11.727  57.813  1.00 89.30  ? 708 GDU B O1A   1 
HETATM 8600 O  O2A   . GDU W 4 .   ? 44.419  10.746  60.022  1.00 74.06  ? 708 GDU B O2A   1 
HETATM 8601 O  O3A   . GDU W 4 .   ? 42.403  11.147  58.373  1.00 61.80  ? 708 GDU B O3A   1 
HETATM 8602 P  PB    . GDU W 4 .   ? 41.975  11.143  56.767  1.00 69.56  ? 708 GDU B PB    1 
HETATM 8603 O  O1B   . GDU W 4 .   ? 41.511  9.726   56.426  1.00 90.85  ? 708 GDU B O1B   1 
HETATM 8604 O  O2B   . GDU W 4 .   ? 43.164  11.533  55.872  1.00 86.71  ? 708 GDU B O2B   1 
HETATM 8605 O  O3B   . GDU W 4 .   ? 40.729  12.205  56.444  1.00 88.85  ? 708 GDU B O3B   1 
HETATM 8606 C  "C1'" . GDU W 4 .   ? 40.117  12.851  57.466  1.00 80.63  ? 708 GDU B "C1'" 1 
HETATM 8607 C  "C2'" . GDU W 4 .   ? 39.048  11.944  58.083  1.00 87.78  ? 708 GDU B "C2'" 1 
HETATM 8608 C  "C3'" . GDU W 4 .   ? 37.821  12.719  58.417  1.00 83.64  ? 708 GDU B "C3'" 1 
HETATM 8609 C  "C4'" . GDU W 4 .   ? 38.161  14.039  59.032  1.00 96.56  ? 708 GDU B "C4'" 1 
HETATM 8610 C  "C5'" . GDU W 4 .   ? 38.976  14.899  58.053  1.00 85.76  ? 708 GDU B "C5'" 1 
HETATM 8611 C  "C6'" . GDU W 4 .   ? 40.133  15.446  58.793  1.00 81.28  ? 708 GDU B "C6'" 1 
HETATM 8612 O  "O2'" . GDU W 4 .   ? 38.699  10.931  57.128  1.00 125.90 ? 708 GDU B "O2'" 1 
HETATM 8613 O  "O3'" . GDU W 4 .   ? 36.962  11.954  59.325  1.00 74.51  ? 708 GDU B "O3'" 1 
HETATM 8614 O  "O4'" . GDU W 4 .   ? 38.914  13.847  60.235  1.00 70.88  ? 708 GDU B "O4'" 1 
HETATM 8615 O  "O5'" . GDU W 4 .   ? 39.497  14.101  56.930  1.00 71.82  ? 708 GDU B "O5'" 1 
HETATM 8616 O  "O6'" . GDU W 4 .   ? 40.429  16.725  58.270  1.00 103.93 ? 708 GDU B "O6'" 1 
HETATM 8617 CA CA    . CA  X 6 .   ? 44.811  13.057  55.680  1.00 185.50 ? 709 CA  B CA    1 
HETATM 8618 O  O     . HOH Y 7 .   ? 48.849  50.835  93.253  1.00 64.10  ? 801 HOH A O     1 
HETATM 8619 O  O     . HOH Y 7 .   ? 44.105  62.674  87.606  1.00 135.06 ? 802 HOH A O     1 
HETATM 8620 O  O     . HOH Z 7 .   ? 44.924  13.392  68.672  1.00 58.33  ? 801 HOH B O     1 
HETATM 8621 O  O     . HOH Z 7 .   ? 49.208  -1.551  61.130  1.00 76.63  ? 802 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  ? 1.7356 1.7769 1.8341 -0.0433 -0.2496 -0.4824 44  SER A N   
2    C CA  . SER A 17  ? 1.8537 1.8940 2.0047 -0.0471 -0.2196 -0.4592 44  SER A CA  
3    C C   . SER A 17  ? 1.9530 1.9735 2.0621 -0.0247 -0.2109 -0.4185 44  SER A C   
4    O O   . SER A 17  ? 1.9459 1.9311 1.9898 -0.0160 -0.2060 -0.4046 44  SER A O   
5    C CB  . SER A 17  ? 1.7864 1.7932 1.9643 -0.0686 -0.1831 -0.4638 44  SER A CB  
6    O OG  . SER A 17  ? 1.7518 1.7582 1.9796 -0.0731 -0.1551 -0.4421 44  SER A OG  
7    N N   . PRO A 18  ? 1.6999 1.7440 1.8474 -0.0165 -0.2081 -0.4010 45  PRO A N   
8    C CA  . PRO A 18  ? 1.5863 1.6134 1.6950 0.0051  -0.2033 -0.3651 45  PRO A CA  
9    C C   . PRO A 18  ? 1.3937 1.3895 1.5105 0.0006  -0.1641 -0.3390 45  PRO A C   
10   O O   . PRO A 18  ? 1.4118 1.4155 1.5866 -0.0131 -0.1421 -0.3403 45  PRO A O   
11   C CB  . PRO A 18  ? 1.4498 1.5225 1.5976 0.0179  -0.2234 -0.3645 45  PRO A CB  
12   C CG  . PRO A 18  ? 1.5914 1.6992 1.8211 -0.0039 -0.2152 -0.3889 45  PRO A CG  
13   C CD  . PRO A 18  ? 1.5542 1.6465 1.7803 -0.0255 -0.2131 -0.4163 45  PRO A CD  
14   N N   . GLU A 19  ? 1.0828 1.0434 1.1410 0.0119  -0.1552 -0.3150 46  GLU A N   
15   C CA  . GLU A 19  ? 1.0654 1.0000 1.1277 0.0113  -0.1221 -0.2891 46  GLU A CA  
16   C C   . GLU A 19  ? 0.9736 0.9271 1.0665 0.0214  -0.1179 -0.2695 46  GLU A C   
17   O O   . GLU A 19  ? 1.2829 1.2545 1.3632 0.0372  -0.1405 -0.2651 46  GLU A O   
18   C CB  . GLU A 19  ? 0.9905 0.8893 0.9849 0.0203  -0.1160 -0.2708 46  GLU A CB  
19   C CG  . GLU A 19  ? 1.2760 1.1532 1.2421 0.0101  -0.1111 -0.2883 46  GLU A CG  
20   C CD  . GLU A 19  ? 1.1517 1.0138 1.1571 -0.0046 -0.0820 -0.2943 46  GLU A CD  
21   O OE1 . GLU A 19  ? 1.1349 0.9827 1.1521 -0.0018 -0.0581 -0.2714 46  GLU A OE1 
22   O OE2 . GLU A 19  ? 1.0105 0.8732 1.0335 -0.0183 -0.0840 -0.3221 46  GLU A OE2 
23   N N   . SER A 20  ? 0.9455 0.8929 1.0766 0.0133  -0.0886 -0.2580 47  SER A N   
24   C CA  . SER A 20  ? 0.8639 0.8280 1.0228 0.0219  -0.0804 -0.2399 47  SER A CA  
25   C C   . SER A 20  ? 0.8090 0.7526 0.9160 0.0409  -0.0814 -0.2128 47  SER A C   
26   O O   . SER A 20  ? 0.9151 0.8289 0.9713 0.0435  -0.0803 -0.2052 47  SER A O   
27   C CB  . SER A 20  ? 0.9947 0.9518 1.1988 0.0079  -0.0470 -0.2326 47  SER A CB  
28   O OG  . SER A 20  ? 0.9970 0.9135 1.1711 0.0068  -0.0256 -0.2171 47  SER A OG  
29   N N   . PRO A 21  ? 0.7916 0.7513 0.9109 0.0538  -0.0828 -0.1993 48  PRO A N   
30   C CA  . PRO A 21  ? 0.9676 0.9044 1.0400 0.0699  -0.0815 -0.1742 48  PRO A CA  
31   C C   . PRO A 21  ? 0.9148 0.8214 0.9745 0.0642  -0.0526 -0.1558 48  PRO A C   
32   O O   . PRO A 21  ? 0.9322 0.8380 1.0277 0.0521  -0.0303 -0.1565 48  PRO A O   
33   C CB  . PRO A 21  ? 0.7689 0.7321 0.8700 0.0827  -0.0847 -0.1679 48  PRO A CB  
34   C CG  . PRO A 21  ? 0.7756 0.7803 0.9274 0.0778  -0.0991 -0.1926 48  PRO A CG  
35   C CD  . PRO A 21  ? 0.7826 0.7844 0.9581 0.0550  -0.0880 -0.2091 48  PRO A CD  
36   N N   . LEU A 22  ? 0.8442 0.7252 0.8520 0.0730  -0.0536 -0.1392 49  LEU A N   
37   C CA  . LEU A 22  ? 0.8804 0.7389 0.8770 0.0714  -0.0293 -0.1205 49  LEU A CA  
38   C C   . LEU A 22  ? 0.7926 0.6605 0.8154 0.0775  -0.0154 -0.1057 49  LEU A C   
39   O O   . LEU A 22  ? 0.9971 0.8837 1.0307 0.0873  -0.0264 -0.1058 49  LEU A O   
40   C CB  . LEU A 22  ? 0.8404 0.6745 0.7786 0.0778  -0.0346 -0.1080 49  LEU A CB  
41   C CG  . LEU A 22  ? 0.8661 0.6884 0.7694 0.0720  -0.0453 -0.1205 49  LEU A CG  
42   C CD1 . LEU A 22  ? 0.7990 0.5984 0.6472 0.0761  -0.0462 -0.1058 49  LEU A CD1 
43   C CD2 . LEU A 22  ? 0.9574 0.7755 0.8818 0.0591  -0.0289 -0.1324 49  LEU A CD2 
44   N N   . GLN A 23  ? 0.9034 0.7585 0.9356 0.0732  0.0090  -0.0932 50  GLN A N   
45   C CA  . GLN A 23  ? 0.8098 0.6697 0.8559 0.0797  0.0236  -0.0769 50  GLN A CA  
46   C C   . GLN A 23  ? 0.7987 0.6472 0.8021 0.0932  0.0163  -0.0615 50  GLN A C   
47   O O   . GLN A 23  ? 0.9615 0.7940 0.9248 0.0948  0.0054  -0.0605 50  GLN A O   
48   C CB  . GLN A 23  ? 0.7229 0.5689 0.7853 0.0727  0.0502  -0.0665 50  GLN A CB  
49   C CG  . GLN A 23  ? 0.9055 0.7567 1.0119 0.0576  0.0609  -0.0803 50  GLN A CG  
50   C CD  . GLN A 23  ? 0.9542 0.7874 1.0755 0.0532  0.0885  -0.0661 50  GLN A CD  
51   O OE1 . GLN A 23  ? 0.9459 0.7819 1.0727 0.0585  0.1019  -0.0500 50  GLN A OE1 
52   N NE2 . GLN A 23  ? 0.8995 0.7116 1.0241 0.0448  0.0970  -0.0718 50  GLN A NE2 
53   N N   . ALA A 24  ? 0.7678 0.6238 0.7791 0.1019  0.0236  -0.0504 51  ALA A N   
54   C CA  . ALA A 24  ? 0.8205 0.6636 0.7929 0.1137  0.0176  -0.0373 51  ALA A CA  
55   C C   . ALA A 24  ? 0.9973 0.8192 0.9436 0.1109  0.0300  -0.0238 51  ALA A C   
56   O O   . ALA A 24  ? 0.9622 0.7812 0.9259 0.1043  0.0470  -0.0205 51  ALA A O   
57   C CB  . ALA A 24  ? 0.8591 0.7161 0.8466 0.1241  0.0236  -0.0311 51  ALA A CB  
58   N N   . PRO A 25  ? 0.9421 0.7488 0.8476 0.1158  0.0215  -0.0163 52  PRO A N   
59   C CA  . PRO A 25  ? 0.9267 0.7196 0.8109 0.1130  0.0316  -0.0056 52  PRO A CA  
60   C C   . PRO A 25  ? 1.0021 0.7984 0.8997 0.1175  0.0493  0.0074  52  PRO A C   
61   O O   . PRO A 25  ? 0.9437 0.7481 0.8509 0.1247  0.0522  0.0113  52  PRO A O   
62   C CB  . PRO A 25  ? 0.9123 0.6908 0.7538 0.1161  0.0181  -0.0015 52  PRO A CB  
63   C CG  . PRO A 25  ? 0.8583 0.6362 0.6925 0.1183  -0.0009 -0.0122 52  PRO A CG  
64   C CD  . PRO A 25  ? 0.9427 0.7423 0.8189 0.1227  0.0006  -0.0193 52  PRO A CD  
65   N N   . ARG A 26  ? 0.9468 0.7370 0.8432 0.1146  0.0610  0.0138  53  ARG A N   
66   C CA  . ARG A 26  ? 0.9705 0.7609 0.8745 0.1201  0.0769  0.0277  53  ARG A CA  
67   C C   . ARG A 26  ? 0.9746 0.7626 0.8484 0.1273  0.0725  0.0374  53  ARG A C   
68   O O   . ARG A 26  ? 1.0384 0.8215 0.8890 0.1248  0.0658  0.0374  53  ARG A O   
69   C CB  . ARG A 26  ? 1.0627 0.8463 0.9767 0.1172  0.0887  0.0302  53  ARG A CB  
70   C CG  . ARG A 26  ? 1.0158 0.7977 0.9614 0.1090  0.0955  0.0199  53  ARG A CG  
71   C CD  . ARG A 26  ? 0.9735 0.7468 0.9178 0.1041  0.0964  0.0117  53  ARG A CD  
72   N NE  . ARG A 26  ? 1.0182 0.7942 0.9427 0.0988  0.0806  -0.0012 53  ARG A NE  
73   C CZ  . ARG A 26  ? 0.8552 0.6267 0.7778 0.0923  0.0790  -0.0140 53  ARG A CZ  
74   N NH1 . ARG A 26  ? 0.9093 0.6727 0.8506 0.0911  0.0918  -0.0172 53  ARG A NH1 
75   N NH2 . ARG A 26  ? 1.0837 0.8565 0.9826 0.0876  0.0647  -0.0239 53  ARG A NH2 
76   N N   . VAL A 27  ? 0.9524 0.7449 0.8267 0.1352  0.0771  0.0444  54  VAL A N   
77   C CA  . VAL A 27  ? 0.8900 0.6796 0.7356 0.1422  0.0726  0.0513  54  VAL A CA  
78   C C   . VAL A 27  ? 1.0507 0.8431 0.8971 0.1495  0.0871  0.0649  54  VAL A C   
79   O O   . VAL A 27  ? 1.0387 0.8354 0.9046 0.1522  0.1004  0.0693  54  VAL A O   
80   C CB  . VAL A 27  ? 0.9807 0.7707 0.8184 0.1478  0.0630  0.0456  54  VAL A CB  
81   C CG1 . VAL A 27  ? 0.9268 0.7101 0.7334 0.1543  0.0588  0.0507  54  VAL A CG1 
82   C CG2 . VAL A 27  ? 1.1546 0.9389 0.9869 0.1430  0.0468  0.0341  54  VAL A CG2 
83   N N   . LEU A 28  ? 1.0325 0.8232 0.8573 0.1523  0.0847  0.0715  55  LEU A N   
84   C CA  . LEU A 28  ? 1.0069 0.8000 0.8222 0.1619  0.0937  0.0846  55  LEU A CA  
85   C C   . LEU A 28  ? 1.0264 0.8199 0.8145 0.1672  0.0856  0.0834  55  LEU A C   
86   O O   . LEU A 28  ? 1.0629 0.8532 0.8318 0.1629  0.0720  0.0768  55  LEU A O   
87   C CB  . LEU A 28  ? 0.8937 0.6887 0.7047 0.1640  0.0943  0.0913  55  LEU A CB  
88   C CG  . LEU A 28  ? 1.0182 0.8167 0.8118 0.1761  0.0984  0.1047  55  LEU A CG  
89   C CD1 . LEU A 28  ? 1.0653 0.8572 0.8689 0.1828  0.1162  0.1173  55  LEU A CD1 
90   C CD2 . LEU A 28  ? 1.0159 0.8218 0.8051 0.1798  0.0935  0.1083  55  LEU A CD2 
91   N N   . ILE A 29  ? 0.9804 0.7762 0.7659 0.1756  0.0950  0.0888  56  ILE A N   
92   C CA  . ILE A 29  ? 1.0431 0.8379 0.8022 0.1823  0.0891  0.0861  56  ILE A CA  
93   C C   . ILE A 29  ? 1.0404 0.8381 0.7762 0.1897  0.0912  0.0964  56  ILE A C   
94   O O   . ILE A 29  ? 1.0763 0.8764 0.8149 0.1965  0.1054  0.1090  56  ILE A O   
95   C CB  . ILE A 29  ? 1.0548 0.8537 0.8241 0.1883  0.0986  0.0834  56  ILE A CB  
96   C CG1 . ILE A 29  ? 0.9532 0.7534 0.7474 0.1826  0.0929  0.0717  56  ILE A CG1 
97   C CG2 . ILE A 29  ? 0.9441 0.7399 0.6840 0.1971  0.0935  0.0791  56  ILE A CG2 
98   C CD1 . ILE A 29  ? 0.9540 0.7645 0.7642 0.1895  0.1004  0.0661  56  ILE A CD1 
99   N N   . ALA A 30  ? 1.1139 0.9108 0.8260 0.1879  0.0768  0.0913  57  ALA A N   
100  C CA  . ALA A 30  ? 0.9985 0.8027 0.6890 0.1944  0.0740  0.0981  57  ALA A CA  
101  C C   . ALA A 30  ? 1.0263 0.8278 0.6877 0.2017  0.0715  0.0941  57  ALA A C   
102  O O   . ALA A 30  ? 1.1973 0.9897 0.8471 0.1972  0.0615  0.0815  57  ALA A O   
103  C CB  . ALA A 30  ? 1.0021 0.8126 0.6892 0.1858  0.0599  0.0926  57  ALA A CB  
104  N N   . LEU A 31  ? 1.1414 0.9477 0.7880 0.2135  0.0808  0.1049  58  LEU A N   
105  C CA  . LEU A 31  ? 1.1973 1.0015 0.8151 0.2223  0.0825  0.1013  58  LEU A CA  
106  C C   . LEU A 31  ? 1.1827 0.9952 0.7705 0.2311  0.0777  0.1084  58  LEU A C   
107  O O   . LEU A 31  ? 1.1043 0.9202 0.6879 0.2407  0.0892  0.1246  58  LEU A O   
108  C CB  . LEU A 31  ? 1.1335 0.9365 0.7617 0.2287  0.1030  0.1067  58  LEU A CB  
109  C CG  . LEU A 31  ? 1.2933 1.0968 0.8912 0.2402  0.1103  0.1050  58  LEU A CG  
110  C CD1 . LEU A 31  ? 1.4527 1.2483 1.0353 0.2395  0.0966  0.0855  58  LEU A CD1 
111  C CD2 . LEU A 31  ? 1.4405 1.2476 1.0540 0.2447  0.1347  0.1124  58  LEU A CD2 
112  N N   . LEU A 32  ? 1.1844 0.9990 0.7503 0.2278  0.0601  0.0962  59  LEU A N   
113  C CA  . LEU A 32  ? 1.1637 0.9883 0.6967 0.2369  0.0526  0.0982  59  LEU A CA  
114  C C   . LEU A 32  ? 1.2027 1.0194 0.7048 0.2459  0.0587  0.0923  59  LEU A C   
115  O O   . LEU A 32  ? 1.2124 1.0167 0.7121 0.2411  0.0560  0.0771  59  LEU A O   
116  C CB  . LEU A 32  ? 1.0781 0.9122 0.6052 0.2268  0.0306  0.0852  59  LEU A CB  
117  C CG  . LEU A 32  ? 1.1665 1.0186 0.7164 0.2216  0.0223  0.0897  59  LEU A CG  
118  C CD1 . LEU A 32  ? 0.9191 0.7643 0.5042 0.2093  0.0275  0.0891  59  LEU A CD1 
119  C CD2 . LEU A 32  ? 1.2853 1.1531 0.8235 0.2132  0.0018  0.0754  59  LEU A CD2 
120  N N   . ALA A 33  ? 1.1051 0.9272 0.5812 0.2600  0.0673  0.1044  60  ALA A N   
121  C CA  . ALA A 33  ? 1.1747 0.9909 0.6198 0.2697  0.0771  0.0995  60  ALA A CA  
122  C C   . ALA A 33  ? 1.3440 1.1688 0.7443 0.2811  0.0688  0.1021  60  ALA A C   
123  O O   . ALA A 33  ? 1.2210 1.0527 0.6118 0.2906  0.0732  0.1214  60  ALA A O   
124  C CB  . ALA A 33  ? 1.2633 1.0757 0.7216 0.2755  0.1045  0.1131  60  ALA A CB  
125  N N   . ARG A 34  ? 1.2968 1.1193 0.6679 0.2807  0.0558  0.0825  61  ARG A N   
126  C CA  . ARG A 34  ? 1.2776 1.1078 0.6005 0.2921  0.0479  0.0806  61  ARG A CA  
127  C C   . ARG A 34  ? 1.3575 1.1754 0.6505 0.2973  0.0550  0.0637  61  ARG A C   
128  O O   . ARG A 34  ? 1.2747 1.0800 0.5754 0.2881  0.0470  0.0430  61  ARG A O   
129  C CB  . ARG A 34  ? 1.2114 1.0559 0.5277 0.2849  0.0193  0.0687  61  ARG A CB  
130  C CG  . ARG A 34  ? 1.2713 1.1272 0.5373 0.2972  0.0077  0.0649  61  ARG A CG  
131  C CD  . ARG A 34  ? 1.1442 1.0162 0.4062 0.2867  -0.0219 0.0455  61  ARG A CD  
132  N NE  . ARG A 34  ? 1.3759 1.2619 0.5893 0.2996  -0.0349 0.0414  61  ARG A NE  
133  C CZ  . ARG A 34  ? 1.3909 1.2930 0.5905 0.2923  -0.0609 0.0207  61  ARG A CZ  
134  N NH1 . ARG A 34  ? 1.3619 1.2672 0.5928 0.2706  -0.0752 0.0028  61  ARG A NH1 
135  N NH2 . ARG A 34  ? 1.3947 1.3100 0.5468 0.3063  -0.0724 0.0174  61  ARG A NH2 
136  N N   . ASN A 35  ? 1.3211 1.1405 0.5780 0.3125  0.0705  0.0727  62  ASN A N   
137  C CA  . ASN A 35  ? 1.3481 1.1585 0.5721 0.3205  0.0801  0.0567  62  ASN A CA  
138  C C   . ASN A 35  ? 1.3920 1.1892 0.6493 0.3149  0.0906  0.0435  62  ASN A C   
139  O O   . ASN A 35  ? 1.3630 1.1470 0.6131 0.3118  0.0799  0.0197  62  ASN A O   
140  C CB  . ASN A 35  ? 1.2530 1.0634 0.4362 0.3206  0.0560  0.0344  62  ASN A CB  
141  C CG  . ASN A 35  ? 1.4548 1.2818 0.5995 0.3303  0.0449  0.0457  62  ASN A CG  
142  O OD1 . ASN A 35  ? 1.5234 1.3532 0.6378 0.3450  0.0617  0.0633  62  ASN A OD1 
143  N ND2 . ASN A 35  ? 1.5322 1.3710 0.6774 0.3222  0.0164  0.0361  62  ASN A ND2 
144  N N   . ALA A 36  ? 1.3785 1.1784 0.6730 0.3139  0.1111  0.0594  63  ALA A N   
145  C CA  . ALA A 36  ? 1.3627 1.1553 0.6961 0.3093  0.1188  0.0491  63  ALA A CA  
146  C C   . ALA A 36  ? 1.3486 1.1489 0.6939 0.3178  0.1499  0.0570  63  ALA A C   
147  O O   . ALA A 36  ? 1.4740 1.2753 0.8600 0.3147  0.1581  0.0522  63  ALA A O   
148  C CB  . ALA A 36  ? 1.2264 1.0182 0.6063 0.2949  0.1086  0.0553  63  ALA A CB  
149  N N   . ALA A 37  ? 1.3424 1.1496 0.6525 0.3281  0.1677  0.0686  64  ALA A N   
150  C CA  . ALA A 37  ? 1.3229 1.1396 0.6443 0.3338  0.2009  0.0768  64  ALA A CA  
151  C C   . ALA A 37  ? 1.4368 1.2549 0.7703 0.3400  0.2085  0.0528  64  ALA A C   
152  O O   . ALA A 37  ? 1.5043 1.3350 0.8741 0.3402  0.2310  0.0543  64  ALA A O   
153  C CB  . ALA A 37  ? 1.4265 1.2462 0.6965 0.3442  0.2181  0.0923  64  ALA A CB  
154  N N   . HIS A 38  ? 1.4317 1.2373 0.7370 0.3454  0.1899  0.0294  65  HIS A N   
155  C CA  . HIS A 38  ? 1.3268 1.1293 0.6417 0.3544  0.1950  0.0053  65  HIS A CA  
156  C C   . HIS A 38  ? 1.4586 1.2604 0.8317 0.3479  0.1889  0.0005  65  HIS A C   
157  O O   . HIS A 38  ? 1.4732 1.2814 0.8699 0.3570  0.2002  -0.0129 65  HIS A O   
158  C CB  . HIS A 38  ? 1.2983 1.0801 0.5701 0.3596  0.1733  -0.0189 65  HIS A CB  
159  C CG  . HIS A 38  ? 1.4286 1.1927 0.7052 0.3458  0.1412  -0.0231 65  HIS A CG  
160  N ND1 . HIS A 38  ? 1.6115 1.3767 0.8640 0.3375  0.1248  -0.0136 65  HIS A ND1 
161  C CD2 . HIS A 38  ? 1.4790 1.2250 0.7821 0.3386  0.1235  -0.0352 65  HIS A CD2 
162  C CE1 . HIS A 38  ? 1.4802 1.2314 0.7470 0.3241  0.1000  -0.0209 65  HIS A CE1 
163  N NE2 . HIS A 38  ? 1.4805 1.2173 0.7753 0.3239  0.0993  -0.0330 65  HIS A NE2 
164  N N   . ALA A 39  ? 1.3887 1.1845 0.7849 0.3335  0.1709  0.0108  66  ALA A N   
165  C CA  . ALA A 39  ? 1.3392 1.1312 0.7827 0.3269  0.1610  0.0057  66  ALA A CA  
166  C C   . ALA A 39  ? 1.3528 1.1623 0.8425 0.3173  0.1733  0.0247  66  ALA A C   
167  O O   . ALA A 39  ? 1.3451 1.1599 0.8773 0.3157  0.1728  0.0192  66  ALA A O   
168  C CB  . ALA A 39  ? 1.2800 1.0481 0.7144 0.3163  0.1301  -0.0013 66  ALA A CB  
169  N N   . LEU A 40  ? 1.3784 1.1957 0.8597 0.3118  0.1835  0.0460  67  LEU A N   
170  C CA  . LEU A 40  ? 1.3330 1.1604 0.8562 0.3007  0.1931  0.0634  67  LEU A CA  
171  C C   . LEU A 40  ? 1.3108 1.1579 0.8780 0.3016  0.2159  0.0611  67  LEU A C   
172  O O   . LEU A 40  ? 1.2701 1.1225 0.8823 0.2920  0.2122  0.0624  67  LEU A O   
173  C CB  . LEU A 40  ? 1.3036 1.1314 0.8042 0.2983  0.2028  0.0872  67  LEU A CB  
174  C CG  . LEU A 40  ? 1.2597 1.0757 0.7380 0.2938  0.1776  0.0922  67  LEU A CG  
175  C CD1 . LEU A 40  ? 1.3071 1.1238 0.7668 0.2952  0.1872  0.1170  67  LEU A CD1 
176  C CD2 . LEU A 40  ? 1.1403 0.9517 0.6562 0.2814  0.1593  0.0875  67  LEU A CD2 
177  N N   . PRO A 41  ? 1.3423 1.2035 0.9015 0.3119  0.2397  0.0567  68  PRO A N   
178  C CA  . PRO A 41  ? 1.3084 1.1946 0.9182 0.3116  0.2601  0.0512  68  PRO A CA  
179  C C   . PRO A 41  ? 1.2904 1.1787 0.9383 0.3136  0.2404  0.0321  68  PRO A C   
180  O O   . PRO A 41  ? 1.3570 1.2598 1.0548 0.3047  0.2420  0.0335  68  PRO A O   
181  C CB  . PRO A 41  ? 1.2206 1.1200 0.8060 0.3254  0.2848  0.0441  68  PRO A CB  
182  C CG  . PRO A 41  ? 1.3005 1.1836 0.8252 0.3275  0.2864  0.0580  68  PRO A CG  
183  C CD  . PRO A 41  ? 1.2895 1.1484 0.7952 0.3233  0.2516  0.0571  68  PRO A CD  
184  N N   . THR A 42  ? 1.3327 1.2040 0.9558 0.3251  0.2205  0.0143  69  THR A N   
185  C CA  . THR A 42  ? 1.2284 1.0949 0.8802 0.3294  0.2001  -0.0022 69  THR A CA  
186  C C   . THR A 42  ? 1.2918 1.1413 0.9539 0.3144  0.1763  0.0056  69  THR A C   
187  O O   . THR A 42  ? 1.2202 1.0760 0.9213 0.3116  0.1671  0.0011  69  THR A O   
188  C CB  . THR A 42  ? 1.2136 1.0590 0.8306 0.3459  0.1872  -0.0224 69  THR A CB  
189  O OG1 . THR A 42  ? 1.2550 1.1222 0.8780 0.3625  0.2095  -0.0347 69  THR A OG1 
190  C CG2 . THR A 42  ? 1.3578 1.1833 0.9889 0.3488  0.1601  -0.0347 69  THR A CG2 
191  N N   . THR A 43  ? 1.3997 1.2304 1.0277 0.3052  0.1664  0.0167  70  THR A N   
192  C CA  . THR A 43  ? 1.1004 0.9164 0.7361 0.2912  0.1454  0.0228  70  THR A CA  
193  C C   . THR A 43  ? 1.1599 0.9931 0.8363 0.2789  0.1559  0.0369  70  THR A C   
194  O O   . THR A 43  ? 1.2140 1.0471 0.9206 0.2720  0.1442  0.0339  70  THR A O   
195  C CB  . THR A 43  ? 1.0557 0.8532 0.6479 0.2855  0.1329  0.0287  70  THR A CB  
196  O OG1 . THR A 43  ? 1.2272 1.0013 0.7898 0.2906  0.1144  0.0121  70  THR A OG1 
197  C CG2 . THR A 43  ? 1.3388 1.1323 0.9445 0.2698  0.1214  0.0404  70  THR A CG2 
198  N N   . LEU A 44  ? 1.2170 1.0622 0.8918 0.2759  0.1779  0.0524  71  LEU A N   
199  C CA  . LEU A 44  ? 1.2668 1.1229 0.9785 0.2632  0.1895  0.0657  71  LEU A CA  
200  C C   . LEU A 44  ? 1.2874 1.1665 1.0503 0.2622  0.1991  0.0561  71  LEU A C   
201  O O   . LEU A 44  ? 1.1834 1.0683 0.9828 0.2504  0.1972  0.0587  71  LEU A O   
202  C CB  . LEU A 44  ? 1.1705 1.0286 0.8648 0.2616  0.2125  0.0855  71  LEU A CB  
203  C CG  . LEU A 44  ? 1.2116 1.0513 0.8608 0.2628  0.2001  0.0964  71  LEU A CG  
204  C CD1 . LEU A 44  ? 1.1321 0.9713 0.7548 0.2663  0.2219  0.1162  71  LEU A CD1 
205  C CD2 . LEU A 44  ? 1.1267 0.9568 0.7917 0.2515  0.1821  0.1009  71  LEU A CD2 
206  N N   . GLY A 45  ? 1.1477 1.0423 0.9155 0.2749  0.2089  0.0432  72  GLY A N   
207  C CA  . GLY A 45  ? 1.1302 1.0522 0.9505 0.2761  0.2144  0.0307  72  GLY A CA  
208  C C   . GLY A 45  ? 1.1566 1.0713 0.9954 0.2760  0.1855  0.0189  72  GLY A C   
209  O O   . GLY A 45  ? 1.2047 1.1376 1.0889 0.2686  0.1840  0.0151  72  GLY A O   
210  N N   . ALA A 46  ? 1.0937 0.9802 0.8956 0.2832  0.1621  0.0130  73  ALA A N   
211  C CA  . ALA A 46  ? 1.0506 0.9236 0.8611 0.2830  0.1350  0.0044  73  ALA A CA  
212  C C   . ALA A 46  ? 1.0446 0.9127 0.8686 0.2645  0.1276  0.0149  73  ALA A C   
213  O O   . ALA A 46  ? 1.0864 0.9581 0.9358 0.2615  0.1133  0.0085  73  ALA A O   
214  C CB  . ALA A 46  ? 1.0559 0.8939 0.8196 0.2911  0.1145  -0.0021 73  ALA A CB  
215  N N   . LEU A 47  ? 1.0714 0.9311 0.8771 0.2536  0.1363  0.0304  74  LEU A N   
216  C CA  . LEU A 47  ? 1.0783 0.9318 0.8952 0.2379  0.1301  0.0393  74  LEU A CA  
217  C C   . LEU A 47  ? 1.1021 0.9793 0.9673 0.2287  0.1455  0.0412  74  LEU A C   
218  O O   . LEU A 47  ? 1.0739 0.9529 0.9634 0.2198  0.1346  0.0371  74  LEU A O   
219  C CB  . LEU A 47  ? 1.0099 0.8483 0.7939 0.2323  0.1334  0.0542  74  LEU A CB  
220  C CG  . LEU A 47  ? 1.1118 0.9278 0.8515 0.2362  0.1154  0.0511  74  LEU A CG  
221  C CD1 . LEU A 47  ? 0.9834 0.7924 0.6991 0.2305  0.1168  0.0649  74  LEU A CD1 
222  C CD2 . LEU A 47  ? 1.0471 0.8479 0.7868 0.2320  0.0922  0.0413  74  LEU A CD2 
223  N N   . GLU A 48  ? 1.1461 1.0412 1.0249 0.2294  0.1715  0.0468  75  GLU A N   
224  C CA  . GLU A 48  ? 1.1850 1.1015 1.1113 0.2174  0.1887  0.0482  75  GLU A CA  
225  C C   . GLU A 48  ? 1.0692 1.0113 1.0399 0.2193  0.1794  0.0294  75  GLU A C   
226  O O   . GLU A 48  ? 1.2682 1.2289 1.2828 0.2067  0.1874  0.0266  75  GLU A O   
227  C CB  . GLU A 48  ? 0.9887 0.9174 0.9168 0.2169  0.2211  0.0587  75  GLU A CB  
228  C CG  . GLU A 48  ? 1.0784 1.0295 1.0099 0.2311  0.2315  0.0473  75  GLU A CG  
229  C CD  . GLU A 48  ? 1.2612 1.2238 1.1905 0.2289  0.2665  0.0588  75  GLU A CD  
230  O OE1 . GLU A 48  ? 1.2885 1.2304 1.1898 0.2225  0.2778  0.0787  75  GLU A OE1 
231  O OE2 . GLU A 48  ? 1.3305 1.3231 1.2856 0.2341  0.2832  0.0483  75  GLU A OE2 
232  N N   . ARG A 49  ? 1.0013 0.9434 0.9615 0.2350  0.1614  0.0160  76  ARG A N   
233  C CA  . ARG A 49  ? 0.9880 0.9536 0.9866 0.2415  0.1480  -0.0019 76  ARG A CA  
234  C C   . ARG A 49  ? 1.1013 1.0450 1.0851 0.2425  0.1160  -0.0073 76  ARG A C   
235  O O   . ARG A 49  ? 1.0421 0.9964 1.0424 0.2538  0.0984  -0.0214 76  ARG A O   
236  C CB  . ARG A 49  ? 0.7742 0.7569 0.7751 0.2619  0.1526  -0.0140 76  ARG A CB  
237  C CG  . ARG A 49  ? 1.0651 1.0757 1.0855 0.2601  0.1871  -0.0107 76  ARG A CG  
238  C CD  . ARG A 49  ? 0.9365 0.9745 0.9732 0.2806  0.1927  -0.0273 76  ARG A CD  
239  N NE  . ARG A 49  ? 1.1736 1.1864 1.1580 0.2972  0.1911  -0.0272 76  ARG A NE  
240  C CZ  . ARG A 49  ? 1.2913 1.3032 1.2498 0.2985  0.2160  -0.0192 76  ARG A CZ  
241  N NH1 . ARG A 49  ? 1.2015 1.2325 1.1781 0.2841  0.2458  -0.0078 76  ARG A NH1 
242  N NH2 . ARG A 49  ? 1.2246 1.2138 1.1355 0.3141  0.2109  -0.0230 76  ARG A NH2 
243  N N   . LEU A 50  ? 0.9734 0.8874 0.9259 0.2318  0.1084  0.0040  77  LEU A N   
244  C CA  . LEU A 50  ? 0.9681 0.8617 0.9059 0.2293  0.0818  0.0002  77  LEU A CA  
245  C C   . LEU A 50  ? 1.0016 0.9164 0.9822 0.2202  0.0759  -0.0081 77  LEU A C   
246  O O   . LEU A 50  ? 1.1074 1.0356 1.1158 0.2057  0.0919  -0.0041 77  LEU A O   
247  C CB  . LEU A 50  ? 0.9724 0.8363 0.8730 0.2183  0.0791  0.0132  77  LEU A CB  
248  C CG  . LEU A 50  ? 1.1222 0.9601 0.9743 0.2246  0.0748  0.0186  77  LEU A CG  
249  C CD1 . LEU A 50  ? 0.9660 0.7895 0.7975 0.2120  0.0785  0.0316  77  LEU A CD1 
250  C CD2 . LEU A 50  ? 0.9451 0.7600 0.7719 0.2325  0.0506  0.0101  77  LEU A CD2 
251  N N   . ARG A 51  ? 0.9938 0.9095 0.9780 0.2289  0.0521  -0.0200 78  ARG A N   
252  C CA  . ARG A 51  ? 0.9684 0.9043 0.9889 0.2207  0.0423  -0.0299 78  ARG A CA  
253  C C   . ARG A 51  ? 1.0099 0.9220 1.0101 0.2042  0.0359  -0.0231 78  ARG A C   
254  O O   . ARG A 51  ? 1.0704 0.9640 1.0466 0.2060  0.0135  -0.0262 78  ARG A O   
255  C CB  . ARG A 51  ? 1.0988 1.0435 1.1260 0.2380  0.0167  -0.0442 78  ARG A CB  
256  C CG  . ARG A 51  ? 0.9873 0.9746 1.0608 0.2517  0.0240  -0.0572 78  ARG A CG  
257  C CD  . ARG A 51  ? 0.9687 0.9661 1.0510 0.2710  -0.0048 -0.0717 78  ARG A CD  
258  N NE  . ARG A 51  ? 1.1344 1.0981 1.1716 0.2924  -0.0189 -0.0694 78  ARG A NE  
259  C CZ  . ARG A 51  ? 1.2484 1.2238 1.2936 0.3137  -0.0146 -0.0763 78  ARG A CZ  
260  N NH1 . ARG A 51  ? 1.1066 1.1304 1.2037 0.3165  0.0046  -0.0857 78  ARG A NH1 
261  N NH2 . ARG A 51  ? 1.3252 1.2618 1.3252 0.3318  -0.0285 -0.0745 78  ARG A NH2 
262  N N   . HIS A 52  ? 0.9087 0.8193 0.9161 0.1892  0.0561  -0.0135 79  HIS A N   
263  C CA  . HIS A 52  ? 1.0195 0.9106 1.0129 0.1745  0.0542  -0.0079 79  HIS A CA  
264  C C   . HIS A 52  ? 1.0559 0.9588 1.0818 0.1610  0.0789  -0.0029 79  HIS A C   
265  O O   . HIS A 52  ? 1.0922 0.9977 1.1184 0.1632  0.0993  0.0073  79  HIS A O   
266  C CB  . HIS A 52  ? 0.9211 0.7800 0.8647 0.1752  0.0508  0.0043  79  HIS A CB  
267  C CG  . HIS A 52  ? 1.0264 0.8702 0.9593 0.1617  0.0490  0.0078  79  HIS A CG  
268  N ND1 . HIS A 52  ? 1.2123 1.0481 1.1354 0.1573  0.0307  -0.0004 79  HIS A ND1 
269  C CD2 . HIS A 52  ? 1.0308 0.8663 0.9604 0.1533  0.0635  0.0182  79  HIS A CD2 
270  C CE1 . HIS A 52  ? 1.0876 0.9127 1.0036 0.1459  0.0357  0.0035  79  HIS A CE1 
271  N NE2 . HIS A 52  ? 0.9969 0.8218 0.9184 0.1441  0.0549  0.0146  79  HIS A NE2 
272  N N   . PRO A 53  ? 0.9208 0.8273 0.9700 0.1471  0.0781  -0.0094 80  PRO A N   
273  C CA  . PRO A 53  ? 1.0272 0.9420 1.1115 0.1332  0.1017  -0.0065 80  PRO A CA  
274  C C   . PRO A 53  ? 1.1441 1.0375 1.2056 0.1325  0.1222  0.0136  80  PRO A C   
275  O O   . PRO A 53  ? 1.2421 1.1116 1.2697 0.1338  0.1168  0.0222  80  PRO A O   
276  C CB  . PRO A 53  ? 0.8727 0.7829 0.9702 0.1197  0.0922  -0.0173 80  PRO A CB  
277  C CG  . PRO A 53  ? 0.8689 0.7830 0.9517 0.1275  0.0633  -0.0300 80  PRO A CG  
278  C CD  . PRO A 53  ? 0.8675 0.7671 0.9084 0.1431  0.0556  -0.0202 80  PRO A CD  
279  N N   . ARG A 54  ? 1.0586 0.9622 1.1390 0.1308  0.1461  0.0212  81  ARG A N   
280  C CA  . ARG A 54  ? 1.1041 0.9871 1.1607 0.1319  0.1655  0.0417  81  ARG A CA  
281  C C   . ARG A 54  ? 1.0599 0.9197 1.1173 0.1210  0.1714  0.0483  81  ARG A C   
282  O O   . ARG A 54  ? 1.1402 0.9780 1.1665 0.1263  0.1752  0.0635  81  ARG A O   
283  C CB  . ARG A 54  ? 1.1508 1.0483 1.2262 0.1309  0.1920  0.0487  81  ARG A CB  
284  C CG  . ARG A 54  ? 1.0827 0.9974 1.1455 0.1461  0.1907  0.0462  81  ARG A CG  
285  C CD  . ARG A 54  ? 1.2397 1.1622 1.3077 0.1455  0.2212  0.0580  81  ARG A CD  
286  N NE  . ARG A 54  ? 1.2164 1.1527 1.2668 0.1616  0.2221  0.0556  81  ARG A NE  
287  C CZ  . ARG A 54  ? 1.2020 1.1715 1.2848 0.1647  0.2296  0.0427  81  ARG A CZ  
288  N NH1 . ARG A 54  ? 1.2428 1.2391 1.3799 0.1518  0.2355  0.0305  81  ARG A NH1 
289  N NH2 . ARG A 54  ? 1.2409 1.2189 1.3028 0.1814  0.2311  0.0404  81  ARG A NH2 
290  N N   . GLU A 55  ? 1.1238 0.9887 1.2168 0.1068  0.1714  0.0357  82  GLU A N   
291  C CA  . GLU A 55  ? 1.0871 0.9270 1.1804 0.0977  0.1762  0.0392  82  GLU A CA  
292  C C   . GLU A 55  ? 1.0855 0.9115 1.1467 0.1037  0.1557  0.0368  82  GLU A C   
293  O O   . GLU A 55  ? 1.2735 1.0775 1.3254 0.1019  0.1602  0.0430  82  GLU A O   
294  C CB  . GLU A 55  ? 1.0112 0.8594 1.1502 0.0797  0.1804  0.0229  82  GLU A CB  
295  C CG  . GLU A 55  ? 1.1463 1.0129 1.2971 0.0769  0.1548  -0.0004 82  GLU A CG  
296  C CD  . GLU A 55  ? 1.2399 1.1435 1.4180 0.0789  0.1479  -0.0133 82  GLU A CD  
297  O OE1 . GLU A 55  ? 1.3240 1.2396 1.5042 0.0857  0.1610  -0.0041 82  GLU A OE1 
298  O OE2 . GLU A 55  ? 1.2134 1.1354 1.4106 0.0749  0.1289  -0.0335 82  GLU A OE2 
299  N N   . ARG A 56  ? 1.1290 0.9661 1.1730 0.1111  0.1344  0.0282  83  ARG A N   
300  C CA  . ARG A 56  ? 0.9610 0.7853 0.9707 0.1157  0.1171  0.0275  83  ARG A CA  
301  C C   . ARG A 56  ? 1.0633 0.8813 1.0360 0.1280  0.1151  0.0410  83  ARG A C   
302  O O   . ARG A 56  ? 1.1263 0.9378 1.0704 0.1311  0.0998  0.0391  83  ARG A O   
303  C CB  . ARG A 56  ? 0.9983 0.8325 1.0074 0.1142  0.0945  0.0099  83  ARG A CB  
304  C CG  . ARG A 56  ? 1.0792 0.9256 1.1261 0.1025  0.0930  -0.0068 83  ARG A CG  
305  C CD  . ARG A 56  ? 0.7089 0.5385 0.7630 0.0919  0.1017  -0.0086 83  ARG A CD  
306  N NE  . ARG A 56  ? 0.8993 0.7166 0.9234 0.0925  0.0872  -0.0135 83  ARG A NE  
307  C CZ  . ARG A 56  ? 0.9493 0.7519 0.9731 0.0860  0.0919  -0.0175 83  ARG A CZ  
308  N NH1 . ARG A 56  ? 1.0126 0.8059 1.0632 0.0789  0.1094  -0.0167 83  ARG A NH1 
309  N NH2 . ARG A 56  ? 0.9728 0.7680 0.9681 0.0866  0.0800  -0.0226 83  ARG A NH2 
310  N N   . THR A 57  ? 1.1389 0.9585 1.1103 0.1339  0.1308  0.0538  84  THR A N   
311  C CA  . THR A 57  ? 0.8975 0.7128 0.8341 0.1455  0.1292  0.0649  84  THR A CA  
312  C C   . THR A 57  ? 1.0288 0.8328 0.9567 0.1490  0.1468  0.0831  84  THR A C   
313  O O   . THR A 57  ? 1.0432 0.8451 0.9926 0.1446  0.1657  0.0895  84  THR A O   
314  C CB  . THR A 57  ? 1.1280 0.9576 1.0638 0.1533  0.1290  0.0616  84  THR A CB  
315  O OG1 . THR A 57  ? 1.2273 1.0669 1.1747 0.1523  0.1122  0.0451  84  THR A OG1 
316  C CG2 . THR A 57  ? 1.1206 0.9433 1.0163 0.1646  0.1238  0.0690  84  THR A CG2 
317  N N   . ALA A 58  ? 1.0574 0.8537 0.9536 0.1567  0.1402  0.0914  85  ALA A N   
318  C CA  . ALA A 58  ? 0.9673 0.7540 0.8485 0.1643  0.1525  0.1094  85  ALA A CA  
319  C C   . ALA A 58  ? 1.0317 0.8228 0.8780 0.1754  0.1464  0.1150  85  ALA A C   
320  O O   . ALA A 58  ? 1.0074 0.8040 0.8392 0.1759  0.1305  0.1047  85  ALA A O   
321  C CB  . ALA A 58  ? 1.0959 0.8715 0.9762 0.1643  0.1497  0.1131  85  ALA A CB  
322  N N   . LEU A 59  ? 1.0291 0.8147 0.8590 0.1843  0.1589  0.1315  86  LEU A N   
323  C CA  . LEU A 59  ? 0.9187 0.7088 0.7141 0.1952  0.1555  0.1367  86  LEU A CA  
324  C C   . LEU A 59  ? 1.0872 0.8727 0.8577 0.2047  0.1499  0.1487  86  LEU A C   
325  O O   . LEU A 59  ? 1.1230 0.8979 0.9002 0.2076  0.1588  0.1612  86  LEU A O   
326  C CB  . LEU A 59  ? 0.9979 0.7895 0.7908 0.1991  0.1757  0.1450  86  LEU A CB  
327  C CG  . LEU A 59  ? 1.1269 0.9298 0.9506 0.1912  0.1827  0.1322  86  LEU A CG  
328  C CD1 . LEU A 59  ? 1.0956 0.9028 0.9204 0.1935  0.2073  0.1414  86  LEU A CD1 
329  C CD2 . LEU A 59  ? 1.0450 0.8575 0.8618 0.1931  0.1634  0.1147  86  LEU A CD2 
330  N N   . TRP A 60  ? 1.0815 0.8749 0.8242 0.2101  0.1345  0.1441  87  TRP A N   
331  C CA  . TRP A 60  ? 1.0702 0.8668 0.7898 0.2198  0.1256  0.1525  87  TRP A CA  
332  C C   . TRP A 60  ? 1.0442 0.8469 0.7280 0.2280  0.1200  0.1519  87  TRP A C   
333  O O   . TRP A 60  ? 1.1284 0.9361 0.8033 0.2230  0.1072  0.1370  87  TRP A O   
334  C CB  . TRP A 60  ? 0.9755 0.7801 0.7042 0.2134  0.1085  0.1417  87  TRP A CB  
335  C CG  . TRP A 60  ? 1.0630 0.8771 0.7791 0.2232  0.0993  0.1485  87  TRP A CG  
336  C CD1 . TRP A 60  ? 1.0275 0.8405 0.7586 0.2291  0.1017  0.1565  87  TRP A CD1 
337  C CD2 . TRP A 60  ? 1.1781 1.0064 0.8665 0.2292  0.0848  0.1461  87  TRP A CD2 
338  N NE1 . TRP A 60  ? 1.0383 0.8671 0.7545 0.2399  0.0891  0.1597  87  TRP A NE1 
339  C CE2 . TRP A 60  ? 1.1459 0.9855 0.8362 0.2390  0.0781  0.1530  87  TRP A CE2 
340  C CE3 . TRP A 60  ? 1.0247 0.8571 0.6876 0.2275  0.0762  0.1372  87  TRP A CE3 
341  C CZ2 . TRP A 60  ? 1.0994 0.9587 0.7690 0.2463  0.0621  0.1510  87  TRP A CZ2 
342  C CZ3 . TRP A 60  ? 0.9753 0.8231 0.6153 0.2332  0.0612  0.1347  87  TRP A CZ3 
343  C CH2 . TRP A 60  ? 1.1108 0.9741 0.7553 0.2420  0.0537  0.1414  87  TRP A CH2 
344  N N   . VAL A 61  ? 1.0498 0.8490 0.7100 0.2406  0.1295  0.1679  88  VAL A N   
345  C CA  . VAL A 61  ? 1.0835 0.8869 0.7067 0.2491  0.1280  0.1674  88  VAL A CA  
346  C C   . VAL A 61  ? 1.1632 0.9720 0.7554 0.2628  0.1178  0.1781  88  VAL A C   
347  O O   . VAL A 61  ? 1.1859 0.9870 0.7757 0.2721  0.1257  0.1967  88  VAL A O   
348  C CB  . VAL A 61  ? 0.9732 0.7691 0.5918 0.2520  0.1520  0.1759  88  VAL A CB  
349  C CG1 . VAL A 61  ? 1.1967 0.9969 0.7729 0.2624  0.1514  0.1746  88  VAL A CG1 
350  C CG2 . VAL A 61  ? 1.0886 0.8858 0.7418 0.2399  0.1593  0.1629  88  VAL A CG2 
351  N N   . ALA A 62  ? 1.0713 0.8923 0.6392 0.2643  0.0994  0.1659  89  ALA A N   
352  C CA  . ALA A 62  ? 1.2046 1.0367 0.7421 0.2774  0.0859  0.1721  89  ALA A CA  
353  C C   . ALA A 62  ? 1.2963 1.1314 0.7931 0.2826  0.0815  0.1642  89  ALA A C   
354  O O   . ALA A 62  ? 1.2655 1.1007 0.7622 0.2728  0.0756  0.1452  89  ALA A O   
355  C CB  . ALA A 62  ? 0.9898 0.8402 0.5432 0.2719  0.0638  0.1611  89  ALA A CB  
356  N N   . THR A 63  ? 1.2140 1.0491 0.6735 0.2989  0.0843  0.1787  90  THR A N   
357  C CA  . THR A 63  ? 1.2848 1.1221 0.7001 0.3057  0.0817  0.1715  90  THR A CA  
358  C C   . THR A 63  ? 1.2665 1.1142 0.6423 0.3230  0.0685  0.1822  90  THR A C   
359  O O   . THR A 63  ? 1.3587 1.2015 0.7317 0.3350  0.0738  0.2045  90  THR A O   
360  C CB  . THR A 63  ? 1.2623 1.0845 0.6664 0.3081  0.1092  0.1785  90  THR A CB  
361  O OG1 . THR A 63  ? 1.3610 1.1856 0.7163 0.3177  0.1078  0.1726  90  THR A OG1 
362  C CG2 . THR A 63  ? 1.2395 1.0482 0.6467 0.3152  0.1310  0.2061  90  THR A CG2 
363  N N   . ASP A 64  ? 1.2194 1.0799 0.5638 0.3247  0.0504  0.1655  91  ASP A N   
364  C CA  . ASP A 64  ? 1.2865 1.1622 0.5917 0.3408  0.0323  0.1706  91  ASP A CA  
365  C C   . ASP A 64  ? 1.4194 1.3029 0.6887 0.3386  0.0186  0.1474  91  ASP A C   
366  O O   . ASP A 64  ? 1.3436 1.2203 0.6245 0.3239  0.0200  0.1267  91  ASP A O   
367  C CB  . ASP A 64  ? 1.3159 1.2141 0.6482 0.3416  0.0101  0.1705  91  ASP A CB  
368  C CG  . ASP A 64  ? 1.3225 1.2314 0.6979 0.3195  -0.0010 0.1476  91  ASP A CG  
369  O OD1 . ASP A 64  ? 1.4270 1.3449 0.7916 0.3090  -0.0157 0.1245  91  ASP A OD1 
370  O OD2 . ASP A 64  ? 1.2395 1.1454 0.6575 0.3120  0.0058  0.1525  91  ASP A OD2 
371  N N   . HIS A 65  ? 1.5510 1.4467 0.7744 0.3545  0.0046  0.1507  92  HIS A N   
372  C CA  . HIS A 65  ? 1.5564 1.4610 0.7407 0.3538  -0.0116 0.1273  92  HIS A CA  
373  C C   . HIS A 65  ? 1.5730 1.4554 0.7365 0.3506  0.0098  0.1180  92  HIS A C   
374  O O   . HIS A 65  ? 1.4889 1.3683 0.6514 0.3389  0.0023  0.0915  92  HIS A O   
375  C CB  . HIS A 65  ? 1.3899 1.3141 0.6022 0.3359  -0.0381 0.1002  92  HIS A CB  
376  C CG  . HIS A 65  ? 1.5059 1.4590 0.7433 0.3390  -0.0589 0.1058  92  HIS A CG  
377  N ND1 . HIS A 65  ? 1.3483 1.3046 0.6388 0.3304  -0.0549 0.1129  92  HIS A ND1 
378  C CD2 . HIS A 65  ? 1.4923 1.4750 0.7096 0.3513  -0.0841 0.1042  92  HIS A CD2 
379  C CE1 . HIS A 65  ? 1.3484 1.3351 0.6524 0.3376  -0.0753 0.1152  92  HIS A CE1 
380  N NE2 . HIS A 65  ? 1.4234 1.4279 0.6851 0.3506  -0.0942 0.1102  92  HIS A NE2 
381  N N   . ASN A 66  ? 1.5851 1.4519 0.7362 0.3602  0.0374  0.1392  93  ASN A N   
382  C CA  . ASN A 66  ? 1.4201 1.2701 0.5579 0.3590  0.0622  0.1328  93  ASN A CA  
383  C C   . ASN A 66  ? 1.5792 1.4319 0.6728 0.3673  0.0639  0.1284  93  ASN A C   
384  O O   . ASN A 66  ? 1.5309 1.3862 0.6083 0.3766  0.0671  0.1481  93  ASN A O   
385  C CB  . ASN A 66  ? 1.3433 1.1784 0.5074 0.3585  0.0942  0.1556  93  ASN A CB  
386  C CG  . ASN A 66  ? 1.4813 1.3149 0.7101 0.3417  0.0933  0.1505  93  ASN A CG  
387  O OD1 . ASN A 66  ? 1.5830 1.4192 0.8320 0.3295  0.0788  0.1269  93  ASN A OD1 
388  N ND2 . ASN A 66  ? 1.4279 1.2547 0.6869 0.3406  0.1088  0.1726  93  ASN A ND2 
389  N N   . MET A 67  ? 1.6399 1.4894 0.7126 0.3644  0.0617  0.1023  94  MET A N   
390  C CA  . MET A 67  ? 1.4889 1.3382 0.5196 0.3718  0.0687  0.0964  94  MET A CA  
391  C C   . MET A 67  ? 1.4889 1.3251 0.5178 0.3752  0.1055  0.1036  94  MET A C   
392  O O   . MET A 67  ? 1.7056 1.5416 0.7014 0.3821  0.1184  0.1072  94  MET A O   
393  C CB  . MET A 67  ? 1.4314 1.2838 0.4391 0.3671  0.0465  0.0620  94  MET A CB  
394  C CG  . MET A 67  ? 1.9941 1.8535 0.9548 0.3745  0.0410  0.0553  94  MET A CG  
395  S SD  . MET A 67  ? 1.8484 1.7302 0.7931 0.3813  0.0144  0.0708  94  MET A SD  
396  C CE  . MET A 67  ? 1.7946 1.6933 0.7620 0.3682  -0.0239 0.0453  94  MET A CE  
397  N N   . ASP A 68  ? 1.4768 1.3042 0.5406 0.3702  0.1229  0.1055  95  ASP A N   
398  C CA  . ASP A 68  ? 1.5668 1.3874 0.6390 0.3723  0.1590  0.1125  95  ASP A CA  
399  C C   . ASP A 68  ? 1.5948 1.4119 0.6960 0.3700  0.1788  0.1441  95  ASP A C   
400  O O   . ASP A 68  ? 1.5568 1.3744 0.6684 0.3690  0.1640  0.1602  95  ASP A O   
401  C CB  . ASP A 68  ? 1.3726 1.1870 0.4640 0.3694  0.1643  0.0885  95  ASP A CB  
402  C CG  . ASP A 68  ? 1.5127 1.3257 0.6623 0.3549  0.1490  0.0870  95  ASP A CG  
403  O OD1 . ASP A 68  ? 1.5999 1.4168 0.7604 0.3511  0.1348  0.1025  95  ASP A OD1 
404  O OD2 . ASP A 68  ? 1.5676 1.3758 0.7531 0.3479  0.1508  0.0700  95  ASP A OD2 
405  N N   . ASN A 69  ? 1.5518 1.3657 0.6692 0.3687  0.2129  0.1517  96  ASN A N   
406  C CA  . ASN A 69  ? 1.6217 1.4295 0.7689 0.3637  0.2353  0.1797  96  ASN A CA  
407  C C   . ASN A 69  ? 1.6108 1.4188 0.8186 0.3516  0.2311  0.1757  96  ASN A C   
408  O O   . ASN A 69  ? 1.6085 1.4166 0.8575 0.3429  0.2551  0.1837  96  ASN A O   
409  C CB  . ASN A 69  ? 1.5770 1.3856 0.7224 0.3630  0.2737  0.1882  96  ASN A CB  
410  C CG  . ASN A 69  ? 1.6421 1.4605 0.8066 0.3626  0.2908  0.1649  96  ASN A CG  
411  O OD1 . ASN A 69  ? 1.7131 1.5344 0.8749 0.3657  0.2708  0.1382  96  ASN A OD1 
412  N ND2 . ASN A 69  ? 1.5997 1.4241 0.7898 0.3576  0.3266  0.1733  96  ASN A ND2 
413  N N   . THR A 70  ? 1.4697 1.2804 0.6935 0.3467  0.1984  0.1606  97  THR A N   
414  C CA  . THR A 70  ? 1.4199 1.2312 0.7057 0.3323  0.1904  0.1554  97  THR A CA  
415  C C   . THR A 70  ? 1.3992 1.2045 0.7122 0.3278  0.2020  0.1820  97  THR A C   
416  O O   . THR A 70  ? 1.4628 1.2676 0.8252 0.3167  0.2146  0.1831  97  THR A O   
417  C CB  . THR A 70  ? 1.4106 1.2247 0.7007 0.3273  0.1550  0.1378  97  THR A CB  
418  O OG1 . THR A 70  ? 1.4314 1.2447 0.7071 0.3277  0.1462  0.1104  97  THR A OG1 
419  C CG2 . THR A 70  ? 1.2948 1.1084 0.6416 0.3132  0.1468  0.1377  97  THR A CG2 
420  N N   . SER A 71  ? 1.5355 1.3351 0.8156 0.3374  0.1971  0.2030  98  SER A N   
421  C CA  . SER A 71  ? 1.4966 1.2849 0.7986 0.3353  0.2064  0.2284  98  SER A CA  
422  C C   . SER A 71  ? 1.5226 1.3007 0.8394 0.3297  0.2440  0.2437  98  SER A C   
423  O O   . SER A 71  ? 1.4589 1.2281 0.8171 0.3198  0.2542  0.2545  98  SER A O   
424  C CB  . SER A 71  ? 1.6608 1.4431 0.9171 0.3514  0.1942  0.2486  98  SER A CB  
425  O OG  . SER A 71  ? 1.8851 1.6507 1.1591 0.3518  0.2046  0.2742  98  SER A OG  
426  N N   . THR A 72  ? 1.6253 1.4054 0.9099 0.3347  0.2657  0.2433  99  THR A N   
427  C CA  . THR A 72  ? 1.4595 1.2333 0.7576 0.3277  0.3044  0.2578  99  THR A CA  
428  C C   . THR A 72  ? 1.4184 1.2072 0.7795 0.3124  0.3146  0.2381  99  THR A C   
429  O O   . THR A 72  ? 1.5756 1.3609 0.9746 0.3002  0.3384  0.2485  99  THR A O   
430  C CB  . THR A 72  ? 1.5120 1.2868 0.7576 0.3369  0.3241  0.2621  99  THR A CB  
431  O OG1 . THR A 72  ? 1.6481 1.4159 0.8518 0.3473  0.3018  0.2707  99  THR A OG1 
432  C CG2 . THR A 72  ? 1.4527 1.2203 0.7139 0.3265  0.3639  0.2799  99  THR A CG2 
433  N N   . VAL A 73  ? 1.4273 1.2316 0.8000 0.3131  0.2962  0.2095  100 VAL A N   
434  C CA  . VAL A 73  ? 1.4425 1.2613 0.8731 0.3020  0.3015  0.1902  100 VAL A CA  
435  C C   . VAL A 73  ? 1.4497 1.2641 0.9319 0.2889  0.2893  0.1926  100 VAL A C   
436  O O   . VAL A 73  ? 1.4168 1.2385 0.9486 0.2770  0.3043  0.1905  100 VAL A O   
437  C CB  . VAL A 73  ? 1.3885 1.2177 0.8123 0.3085  0.2825  0.1606  100 VAL A CB  
438  C CG1 . VAL A 73  ? 1.2870 1.1298 0.7690 0.3004  0.2840  0.1415  100 VAL A CG1 
439  C CG2 . VAL A 73  ? 1.2976 1.1308 0.6701 0.3218  0.2970  0.1559  100 VAL A CG2 
440  N N   . LEU A 74  ? 1.3797 1.1847 0.8517 0.2908  0.2621  0.1956  101 LEU A N   
441  C CA  . LEU A 74  ? 1.3284 1.1289 0.8447 0.2796  0.2508  0.1972  101 LEU A CA  
442  C C   . LEU A 74  ? 1.4309 1.2182 0.9646 0.2730  0.2745  0.2206  101 LEU A C   
443  O O   . LEU A 74  ? 1.4284 1.2168 1.0114 0.2596  0.2814  0.2175  101 LEU A O   
444  C CB  . LEU A 74  ? 1.3636 1.1601 0.8630 0.2840  0.2195  0.1956  101 LEU A CB  
445  C CG  . LEU A 74  ? 1.3912 1.1966 0.8866 0.2837  0.1932  0.1705  101 LEU A CG  
446  C CD1 . LEU A 74  ? 1.1936 0.9989 0.6643 0.2885  0.1670  0.1716  101 LEU A CD1 
447  C CD2 . LEU A 74  ? 1.1933 1.0023 0.7385 0.2708  0.1867  0.1549  101 LEU A CD2 
448  N N   . ARG A 75  ? 1.4672 1.2393 0.9584 0.2825  0.2867  0.2443  102 ARG A N   
449  C CA  . ARG A 75  ? 1.4831 1.2343 0.9850 0.2766  0.3098  0.2690  102 ARG A CA  
450  C C   . ARG A 75  ? 1.5378 1.2955 1.0718 0.2625  0.3432  0.2679  102 ARG A C   
451  O O   . ARG A 75  ? 1.4949 1.2444 1.0716 0.2480  0.3563  0.2729  102 ARG A O   
452  C CB  . ARG A 75  ? 1.5783 1.3088 1.0202 0.2921  0.3155  0.2960  102 ARG A CB  
453  C CG  . ARG A 75  ? 1.6660 1.3652 1.1130 0.2890  0.3331  0.3240  102 ARG A CG  
454  C CD  . ARG A 75  ? 1.7428 1.4189 1.1250 0.3072  0.3372  0.3521  102 ARG A CD  
455  N NE  . ARG A 75  ? 1.9763 1.6633 1.3308 0.3241  0.3000  0.3450  102 ARG A NE  
456  C CZ  . ARG A 75  ? 2.0327 1.7373 1.3474 0.3344  0.2863  0.3344  102 ARG A CZ  
457  N NH1 . ARG A 75  ? 1.9072 1.6192 1.2015 0.3319  0.3062  0.3297  102 ARG A NH1 
458  N NH2 . ARG A 75  ? 1.8642 1.5806 1.1609 0.3470  0.2523  0.3269  102 ARG A NH2 
459  N N   . GLU A 76  ? 1.5592 1.3335 1.0751 0.2664  0.3576  0.2595  103 GLU A N   
460  C CA  . GLU A 76  ? 1.5686 1.3583 1.1210 0.2533  0.3889  0.2541  103 GLU A CA  
461  C C   . GLU A 76  ? 1.4871 1.2951 1.1082 0.2395  0.3788  0.2320  103 GLU A C   
462  O O   . GLU A 76  ? 1.4710 1.2854 1.1377 0.2234  0.4007  0.2325  103 GLU A O   
463  C CB  . GLU A 76  ? 1.5393 1.3488 1.0622 0.2632  0.4008  0.2427  103 GLU A CB  
464  C CG  . GLU A 76  ? 1.7136 1.5471 1.2761 0.2518  0.4338  0.2341  103 GLU A CG  
465  C CD  . GLU A 76  ? 1.9360 1.7925 1.4747 0.2642  0.4413  0.2166  103 GLU A CD  
466  O OE1 . GLU A 76  ? 2.0385 1.8946 1.5452 0.2789  0.4140  0.2029  103 GLU A OE1 
467  O OE2 . GLU A 76  ? 1.9382 1.8135 1.4913 0.2587  0.4754  0.2154  103 GLU A OE2 
468  N N   . TRP A 77  ? 1.3857 1.2016 1.0137 0.2446  0.3455  0.2125  104 TRP A N   
469  C CA  . TRP A 77  ? 1.3676 1.1995 1.0530 0.2339  0.3330  0.1915  104 TRP A CA  
470  C C   . TRP A 77  ? 1.3979 1.2139 1.1133 0.2221  0.3257  0.1992  104 TRP A C   
471  O O   . TRP A 77  ? 1.3177 1.1428 1.0841 0.2074  0.3338  0.1918  104 TRP A O   
472  C CB  . TRP A 77  ? 1.2057 1.0467 0.8812 0.2436  0.3021  0.1693  104 TRP A CB  
473  C CG  . TRP A 77  ? 1.2775 1.1321 1.0027 0.2358  0.2866  0.1485  104 TRP A CG  
474  C CD1 . TRP A 77  ? 1.3114 1.1902 1.0777 0.2321  0.2961  0.1326  104 TRP A CD1 
475  C CD2 . TRP A 77  ? 1.2382 1.0844 0.9750 0.2318  0.2580  0.1412  104 TRP A CD2 
476  N NE1 . TRP A 77  ? 1.2747 1.1586 1.0748 0.2272  0.2734  0.1167  104 TRP A NE1 
477  C CE2 . TRP A 77  ? 1.1387 1.0015 0.9196 0.2261  0.2510  0.1221  104 TRP A CE2 
478  C CE3 . TRP A 77  ? 1.2652 1.0939 0.9800 0.2329  0.2382  0.1485  104 TRP A CE3 
479  C CZ2 . TRP A 77  ? 1.2204 1.0785 1.0178 0.2210  0.2258  0.1118  104 TRP A CZ2 
480  C CZ3 . TRP A 77  ? 1.1609 0.9878 0.8964 0.2265  0.2152  0.1370  104 TRP A CZ3 
481  C CH2 . TRP A 77  ? 1.1078 0.9472 0.8813 0.2204  0.2096  0.1196  104 TRP A CH2 
482  N N   . LEU A 78  ? 1.4636 1.2578 1.1492 0.2288  0.3100  0.2124  105 LEU A N   
483  C CA  . LEU A 78  ? 1.3261 1.1043 1.0379 0.2201  0.3025  0.2181  105 LEU A CA  
484  C C   . LEU A 78  ? 1.4426 1.2056 1.1772 0.2073  0.3325  0.2341  105 LEU A C   
485  O O   . LEU A 78  ? 1.4239 1.1845 1.2030 0.1929  0.3332  0.2277  105 LEU A O   
486  C CB  . LEU A 78  ? 1.2527 1.0137 0.9275 0.2327  0.2826  0.2300  105 LEU A CB  
487  C CG  . LEU A 78  ? 1.1513 0.9244 0.8170 0.2388  0.2498  0.2124  105 LEU A CG  
488  C CD1 . LEU A 78  ? 1.1891 0.9499 0.8285 0.2493  0.2334  0.2246  105 LEU A CD1 
489  C CD2 . LEU A 78  ? 1.2195 1.0029 0.9313 0.2261  0.2373  0.1919  105 LEU A CD2 
490  N N   . VAL A 79  ? 1.4110 1.1617 1.1133 0.2112  0.3580  0.2549  106 VAL A N   
491  C CA  . VAL A 79  ? 1.4439 1.1755 1.1645 0.1968  0.3899  0.2719  106 VAL A CA  
492  C C   . VAL A 79  ? 1.3184 1.0764 1.0983 0.1771  0.4057  0.2532  106 VAL A C   
493  O O   . VAL A 79  ? 1.4309 1.1780 1.2492 0.1590  0.4212  0.2561  106 VAL A O   
494  C CB  . VAL A 79  ? 1.3570 1.0700 1.0244 0.2052  0.4156  0.2984  106 VAL A CB  
495  C CG1 . VAL A 79  ? 1.4692 1.1618 1.1561 0.1868  0.4532  0.3156  106 VAL A CG1 
496  C CG2 . VAL A 79  ? 1.3624 1.0483 0.9753 0.2253  0.3978  0.3181  106 VAL A CG2 
497  N N   . ALA A 80  ? 1.2660 1.0595 1.0562 0.1807  0.4005  0.2322  107 ALA A N   
498  C CA  . ALA A 80  ? 1.2845 1.1101 1.1327 0.1654  0.4132  0.2126  107 ALA A CA  
499  C C   . ALA A 80  ? 1.3269 1.1641 1.2239 0.1568  0.3882  0.1910  107 ALA A C   
500  O O   . ALA A 80  ? 1.3674 1.2255 1.3188 0.1405  0.3985  0.1778  107 ALA A O   
501  C CB  . ALA A 80  ? 1.2604 1.1192 1.1008 0.1761  0.4168  0.1977  107 ALA A CB  
502  N N   . VAL A 81  ? 1.2620 1.0880 1.1410 0.1668  0.3561  0.1865  108 VAL A N   
503  C CA  . VAL A 81  ? 1.1814 1.0175 1.0978 0.1604  0.3312  0.1661  108 VAL A CA  
504  C C   . VAL A 81  ? 1.2070 1.0140 1.1230 0.1557  0.3204  0.1743  108 VAL A C   
505  O O   . VAL A 81  ? 1.2722 1.0845 1.2148 0.1499  0.3008  0.1583  108 VAL A O   
506  C CB  . VAL A 81  ? 1.2666 1.1185 1.1677 0.1745  0.3022  0.1484  108 VAL A CB  
507  C CG1 . VAL A 81  ? 1.0599 0.9403 0.9649 0.1814  0.3122  0.1371  108 VAL A CG1 
508  C CG2 . VAL A 81  ? 1.1115 0.9420 0.9589 0.1889  0.2853  0.1594  108 VAL A CG2 
509  N N   . LYS A 82  ? 1.2877 1.0637 1.1721 0.1598  0.3323  0.1985  109 LYS A N   
510  C CA  . LYS A 82  ? 1.3040 1.0519 1.1877 0.1588  0.3222  0.2059  109 LYS A CA  
511  C C   . LYS A 82  ? 1.1823 0.9287 1.1187 0.1387  0.3272  0.1938  109 LYS A C   
512  O O   . LYS A 82  ? 1.3240 1.0665 1.2742 0.1367  0.3074  0.1824  109 LYS A O   
513  C CB  . LYS A 82  ? 1.3532 1.0665 1.1982 0.1673  0.3382  0.2354  109 LYS A CB  
514  C CG  . LYS A 82  ? 1.4558 1.1395 1.2961 0.1719  0.3268  0.2439  109 LYS A CG  
515  C CD  . LYS A 82  ? 1.6262 1.2767 1.4209 0.1865  0.3378  0.2740  109 LYS A CD  
516  C CE  . LYS A 82  ? 1.6608 1.2828 1.4544 0.1941  0.3264  0.2815  109 LYS A CE  
517  N NZ  . LYS A 82  ? 1.6616 1.3041 1.4524 0.2048  0.2938  0.2657  109 LYS A NZ  
518  N N   . SER A 83  ? 1.3369 1.0887 1.3039 0.1226  0.3539  0.1944  110 SER A N   
519  C CA  . SER A 83  ? 1.2883 1.0383 1.3067 0.1009  0.3610  0.1825  110 SER A CA  
520  C C   . SER A 83  ? 1.2894 1.0737 1.3460 0.0952  0.3376  0.1522  110 SER A C   
521  O O   . SER A 83  ? 1.4085 1.1915 1.5039 0.0791  0.3357  0.1388  110 SER A O   
522  C CB  . SER A 83  ? 1.1679 0.9197 1.2110 0.0830  0.3970  0.1898  110 SER A CB  
523  O OG  . SER A 83  ? 1.3440 1.1373 1.3984 0.0843  0.4031  0.1791  110 SER A OG  
524  N N   . LEU A 84  ? 1.1796 0.9917 1.2240 0.1083  0.3194  0.1410  111 LEU A N   
525  C CA  . LEU A 84  ? 1.1407 0.9836 1.2170 0.1053  0.2973  0.1143  111 LEU A CA  
526  C C   . LEU A 84  ? 1.2319 1.0651 1.2897 0.1134  0.2661  0.1064  111 LEU A C   
527  O O   . LEU A 84  ? 1.1937 1.0450 1.2745 0.1097  0.2469  0.0858  111 LEU A O   
528  C CB  . LEU A 84  ? 1.1788 1.0557 1.2549 0.1155  0.2960  0.1051  111 LEU A CB  
529  C CG  . LEU A 84  ? 1.2155 1.1054 1.3005 0.1112  0.3289  0.1141  111 LEU A CG  
530  C CD1 . LEU A 84  ? 1.2151 1.1385 1.2979 0.1250  0.3246  0.1021  111 LEU A CD1 
531  C CD2 . LEU A 84  ? 1.3188 1.2203 1.4597 0.0872  0.3497  0.1075  111 LEU A CD2 
532  N N   . TYR A 85  ? 1.1805 0.9874 1.1974 0.1243  0.2607  0.1219  112 TYR A N   
533  C CA  . TYR A 85  ? 1.1210 0.9227 1.1177 0.1321  0.2335  0.1150  112 TYR A CA  
534  C C   . TYR A 85  ? 1.1553 0.9301 1.1522 0.1281  0.2332  0.1206  112 TYR A C   
535  O O   . TYR A 85  ? 1.1312 0.8836 1.1307 0.1245  0.2531  0.1355  112 TYR A O   
536  C CB  . TYR A 85  ? 1.0652 0.8663 1.0158 0.1495  0.2235  0.1237  112 TYR A CB  
537  C CG  . TYR A 85  ? 1.1068 0.9320 1.0549 0.1557  0.2164  0.1121  112 TYR A CG  
538  C CD1 . TYR A 85  ? 1.1289 0.9660 1.0770 0.1588  0.2357  0.1173  112 TYR A CD1 
539  C CD2 . TYR A 85  ? 1.1642 0.9983 1.1090 0.1588  0.1914  0.0959  112 TYR A CD2 
540  C CE1 . TYR A 85  ? 1.1832 1.0420 1.1305 0.1668  0.2296  0.1049  112 TYR A CE1 
541  C CE2 . TYR A 85  ? 1.1377 0.9890 1.0794 0.1666  0.1842  0.0853  112 TYR A CE2 
542  C CZ  . TYR A 85  ? 1.0527 0.9171 0.9971 0.1715  0.2030  0.0889  112 TYR A CZ  
543  O OH  . TYR A 85  ? 1.1079 0.9892 1.0504 0.1816  0.1960  0.0766  112 TYR A OH  
544  N N   . HIS A 86  ? 1.0912 0.8665 1.0837 0.1293  0.2109  0.1086  113 HIS A N   
545  C CA  . HIS A 86  ? 0.9885 0.7419 0.9833 0.1268  0.2093  0.1096  113 HIS A CA  
546  C C   . HIS A 86  ? 1.0805 0.8115 1.0460 0.1399  0.2174  0.1320  113 HIS A C   
547  O O   . HIS A 86  ? 1.1338 0.8397 1.1065 0.1384  0.2288  0.1402  113 HIS A O   
548  C CB  . HIS A 86  ? 1.0554 0.8168 1.0443 0.1270  0.1850  0.0932  113 HIS A CB  
549  C CG  . HIS A 86  ? 0.9935 0.7364 0.9824 0.1267  0.1829  0.0922  113 HIS A CG  
550  N ND1 . HIS A 86  ? 1.0380 0.7755 1.0000 0.1388  0.1751  0.1001  113 HIS A ND1 
551  C CD2 . HIS A 86  ? 0.9930 0.7231 1.0068 0.1162  0.1876  0.0823  113 HIS A CD2 
552  C CE1 . HIS A 86  ? 0.9747 0.6978 0.9458 0.1373  0.1760  0.0956  113 HIS A CE1 
553  N NE2 . HIS A 86  ? 1.0964 0.8124 1.0969 0.1238  0.1837  0.0847  113 HIS A NE2 
554  N N   . SER A 87  ? 1.1222 0.8609 1.0540 0.1536  0.2106  0.1414  114 SER A N   
555  C CA  . SER A 87  ? 1.0294 0.7516 0.9311 0.1683  0.2150  0.1621  114 SER A CA  
556  C C   . SER A 87  ? 1.1157 0.8512 0.9842 0.1796  0.2114  0.1696  114 SER A C   
557  O O   . SER A 87  ? 1.1066 0.8622 0.9733 0.1777  0.2009  0.1566  114 SER A O   
558  C CB  . SER A 87  ? 0.9206 0.6381 0.8150 0.1755  0.1995  0.1593  114 SER A CB  
559  O OG  . SER A 87  ? 1.1622 0.9001 1.0351 0.1816  0.1797  0.1523  114 SER A OG  
560  N N   . VAL A 88  ? 1.1039 0.8257 0.9438 0.1927  0.2194  0.1905  115 VAL A N   
561  C CA  . VAL A 88  ? 1.0726 0.8045 0.8750 0.2051  0.2158  0.1983  115 VAL A CA  
562  C C   . VAL A 88  ? 1.2008 0.9233 0.9728 0.2221  0.2075  0.2135  115 VAL A C   
563  O O   . VAL A 88  ? 1.4599 1.1587 1.2257 0.2288  0.2205  0.2324  115 VAL A O   
564  C CB  . VAL A 88  ? 1.1415 0.8700 0.9365 0.2038  0.2396  0.2098  115 VAL A CB  
565  C CG1 . VAL A 88  ? 1.1951 0.9271 0.9427 0.2198  0.2372  0.2215  115 VAL A CG1 
566  C CG2 . VAL A 88  ? 1.0679 0.8166 0.8924 0.1906  0.2438  0.1916  115 VAL A CG2 
567  N N   . GLU A 89  ? 1.1286 0.8692 0.8827 0.2291  0.1855  0.2051  116 GLU A N   
568  C CA  . GLU A 89  ? 1.0490 0.7902 0.7737 0.2465  0.1745  0.2170  116 GLU A CA  
569  C C   . GLU A 89  ? 1.3318 1.0838 1.0179 0.2552  0.1710  0.2207  116 GLU A C   
570  O O   . GLU A 89  ? 1.2502 1.0162 0.9342 0.2480  0.1658  0.2058  116 GLU A O   
571  C CB  . GLU A 89  ? 1.0194 0.7769 0.7543 0.2468  0.1527  0.2032  116 GLU A CB  
572  C CG  . GLU A 89  ? 1.2273 0.9884 0.9435 0.2656  0.1419  0.2149  116 GLU A CG  
573  C CD  . GLU A 89  ? 1.4483 1.2294 1.1819 0.2643  0.1238  0.2002  116 GLU A CD  
574  O OE1 . GLU A 89  ? 1.4043 1.1867 1.1655 0.2496  0.1241  0.1852  116 GLU A OE1 
575  O OE2 . GLU A 89  ? 1.4988 1.2965 1.2182 0.2780  0.1094  0.2031  116 GLU A OE2 
576  N N   . TRP A 90  ? 1.3288 1.0720 0.9820 0.2720  0.1733  0.2404  117 TRP A N   
577  C CA  . TRP A 90  ? 1.1940 0.9419 0.8055 0.2811  0.1754  0.2470  117 TRP A CA  
578  C C   . TRP A 90  ? 1.2998 1.0539 0.8771 0.3007  0.1579  0.2569  117 TRP A C   
579  O O   . TRP A 90  ? 1.4842 1.2213 1.0534 0.3140  0.1619  0.2766  117 TRP A O   
580  C CB  . TRP A 90  ? 1.3024 1.0287 0.9053 0.2799  0.2049  0.2648  117 TRP A CB  
581  C CG  . TRP A 90  ? 1.3967 1.1208 0.9499 0.2923  0.2127  0.2782  117 TRP A CG  
582  C CD1 . TRP A 90  ? 1.3483 1.0486 0.8691 0.3042  0.2286  0.3052  117 TRP A CD1 
583  C CD2 . TRP A 90  ? 1.4346 1.1780 0.9615 0.2942  0.2062  0.2653  117 TRP A CD2 
584  N NE1 . TRP A 90  ? 1.4460 1.1521 0.9202 0.3133  0.2324  0.3100  117 TRP A NE1 
585  C CE2 . TRP A 90  ? 1.4652 1.1981 0.9434 0.3075  0.2188  0.2846  117 TRP A CE2 
586  C CE3 . TRP A 90  ? 1.3351 1.1000 0.8720 0.2865  0.1912  0.2396  117 TRP A CE3 
587  C CZ2 . TRP A 90  ? 1.3739 1.1200 0.8144 0.3133  0.2170  0.2766  117 TRP A CZ2 
588  C CZ3 . TRP A 90  ? 1.3891 1.1640 0.8903 0.2925  0.1892  0.2321  117 TRP A CZ3 
589  C CH2 . TRP A 90  ? 1.4509 1.2178 0.9051 0.3057  0.2020  0.2494  117 TRP A CH2 
590  N N   . ARG A 91  ? 1.2126 0.9907 0.7711 0.3029  0.1374  0.2424  118 ARG A N   
591  C CA  . ARG A 91  ? 1.2115 1.0044 0.7423 0.3198  0.1161  0.2463  118 ARG A CA  
592  C C   . ARG A 91  ? 1.3716 1.1723 0.8551 0.3273  0.1119  0.2453  118 ARG A C   
593  O O   . ARG A 91  ? 1.3764 1.1961 0.8547 0.3201  0.0966  0.2243  118 ARG A O   
594  C CB  . ARG A 91  ? 1.2283 1.0469 0.7854 0.3129  0.0927  0.2260  118 ARG A CB  
595  C CG  . ARG A 91  ? 1.3814 1.1954 0.9781 0.3112  0.0943  0.2280  118 ARG A CG  
596  C CD  . ARG A 91  ? 1.3797 1.2215 1.0021 0.3020  0.0745  0.2068  118 ARG A CD  
597  N NE  . ARG A 91  ? 1.5379 1.4080 1.1410 0.3126  0.0520  0.2022  118 ARG A NE  
598  C CZ  . ARG A 91  ? 1.5680 1.4667 1.1925 0.3094  0.0348  0.1882  118 ARG A CZ  
599  N NH1 . ARG A 91  ? 1.2068 1.1079 0.8692 0.2975  0.0382  0.1785  118 ARG A NH1 
600  N NH2 . ARG A 91  ? 1.2828 1.2107 0.8907 0.3178  0.0141  0.1826  118 ARG A NH2 
601  N N   . PRO A 92  ? 1.4208 1.2044 0.8661 0.3413  0.1260  0.2673  119 PRO A N   
602  C CA  . PRO A 92  ? 1.4196 1.2109 0.8138 0.3505  0.1216  0.2661  119 PRO A CA  
603  C C   . PRO A 92  ? 1.4148 1.2188 0.7728 0.3715  0.0985  0.2740  119 PRO A C   
604  O O   . PRO A 92  ? 1.4110 1.2093 0.7750 0.3845  0.0933  0.2902  119 PRO A O   
605  C CB  . PRO A 92  ? 1.5219 1.2871 0.8947 0.3522  0.1536  0.2861  119 PRO A CB  
606  C CG  . PRO A 92  ? 1.2461 0.9869 0.6393 0.3555  0.1662  0.3084  119 PRO A CG  
607  C CD  . PRO A 92  ? 1.3860 1.1381 0.8331 0.3450  0.1519  0.2926  119 PRO A CD  
608  N N   . ALA A 93  ? 1.4701 1.2915 0.7902 0.3761  0.0836  0.2617  120 ALA A N   
609  C CA  . ALA A 93  ? 1.4538 1.2941 0.7474 0.3917  0.0593  0.2624  120 ALA A CA  
610  C C   . ALA A 93  ? 1.4882 1.3325 0.7368 0.3930  0.0591  0.2536  120 ALA A C   
611  O O   . ALA A 93  ? 1.5536 1.4126 0.7921 0.3855  0.0477  0.2307  120 ALA A O   
612  C CB  . ALA A 93  ? 1.3352 1.2071 0.6472 0.3922  0.0285  0.2456  120 ALA A CB  
613  N N   . GLU A 94  ? 1.4517 1.2807 0.6719 0.4025  0.0719  0.2713  121 GLU A N   
614  C CA  . GLU A 94  ? 1.7341 1.5643 0.9099 0.4041  0.0756  0.2646  121 GLU A CA  
615  C C   . GLU A 94  ? 1.6580 1.5167 0.8079 0.4122  0.0422  0.2485  121 GLU A C   
616  O O   . GLU A 94  ? 1.7767 1.6469 0.9058 0.4066  0.0345  0.2267  121 GLU A O   
617  C CB  . GLU A 94  ? 1.5956 1.4002 0.7464 0.4110  0.1001  0.2896  121 GLU A CB  
618  C CG  . GLU A 94  ? 1.6887 1.4659 0.8661 0.4009  0.1346  0.3051  121 GLU A CG  
619  C CD  . GLU A 94  ? 2.1103 1.8891 1.2990 0.3865  0.1521  0.2893  121 GLU A CD  
620  O OE1 . GLU A 94  ? 2.1362 1.9242 1.2945 0.3866  0.1523  0.2750  121 GLU A OE1 
621  O OE2 . GLU A 94  ? 2.0339 1.8048 1.2618 0.3760  0.1653  0.2904  121 GLU A OE2 
622  N N   . GLU A 95  ? 1.6861 1.5567 0.8377 0.4257  0.0218  0.2577  122 GLU A N   
623  C CA  . GLU A 95  ? 1.5873 1.4886 0.7161 0.4337  -0.0106 0.2426  122 GLU A CA  
624  C C   . GLU A 95  ? 1.6350 1.5680 0.7994 0.4305  -0.0380 0.2258  122 GLU A C   
625  O O   . GLU A 95  ? 1.7040 1.6360 0.9055 0.4329  -0.0367 0.2361  122 GLU A O   
626  C CB  . GLU A 95  ? 1.8188 1.7173 0.9193 0.4536  -0.0182 0.2626  122 GLU A CB  
627  C CG  . GLU A 95  ? 1.8036 1.6719 0.8622 0.4572  0.0076  0.2802  122 GLU A CG  
628  C CD  . GLU A 95  ? 1.9707 1.8472 0.9888 0.4524  0.0056  0.2616  122 GLU A CD  
629  O OE1 . GLU A 95  ? 2.1227 2.0285 1.1380 0.4496  -0.0214 0.2364  122 GLU A OE1 
630  O OE2 . GLU A 95  ? 1.8465 1.7002 0.8358 0.4507  0.0318  0.2712  122 GLU A OE2 
631  N N   . PRO A 96  ? 1.5706 1.5320 0.7253 0.4240  -0.0623 0.1988  123 PRO A N   
632  C CA  . PRO A 96  ? 1.4489 1.4117 0.5619 0.4195  -0.0657 0.1815  123 PRO A CA  
633  C C   . PRO A 96  ? 1.6955 1.6392 0.8095 0.4027  -0.0458 0.1677  123 PRO A C   
634  O O   . PRO A 96  ? 1.7421 1.6763 0.8900 0.3931  -0.0344 0.1685  123 PRO A O   
635  C CB  . PRO A 96  ? 1.4362 1.4399 0.5506 0.4182  -0.1032 0.1571  123 PRO A CB  
636  C CG  . PRO A 96  ? 1.5106 1.5303 0.6741 0.4103  -0.1116 0.1514  123 PRO A CG  
637  C CD  . PRO A 96  ? 1.5708 1.5678 0.7578 0.4200  -0.0901 0.1815  123 PRO A CD  
638  N N   . ARG A 97  ? 1.5430 1.4808 0.6200 0.3998  -0.0417 0.1539  124 ARG A N   
639  C CA  . ARG A 97  ? 1.5528 1.4730 0.6290 0.3867  -0.0241 0.1384  124 ARG A CA  
640  C C   . ARG A 97  ? 1.5742 1.5084 0.6544 0.3729  -0.0467 0.1050  124 ARG A C   
641  O O   . ARG A 97  ? 1.6426 1.5601 0.7220 0.3628  -0.0351 0.0893  124 ARG A O   
642  C CB  . ARG A 97  ? 1.5123 1.4161 0.5474 0.3919  -0.0037 0.1409  124 ARG A CB  
643  C CG  . ARG A 97  ? 1.5678 1.4539 0.5961 0.4026  0.0214  0.1737  124 ARG A CG  
644  C CD  . ARG A 97  ? 1.7377 1.6060 0.7349 0.4033  0.0498  0.1754  124 ARG A CD  
645  N NE  . ARG A 97  ? 1.9964 1.8742 0.9476 0.4074  0.0367  0.1583  124 ARG A NE  
646  C CZ  . ARG A 97  ? 2.0885 1.9557 1.0059 0.4093  0.0572  0.1555  124 ARG A CZ  
647  N NH1 . ARG A 97  ? 2.0446 1.8939 0.9700 0.4072  0.0923  0.1687  124 ARG A NH1 
648  N NH2 . ARG A 97  ? 2.0670 1.9436 0.9423 0.4128  0.0425  0.1382  124 ARG A NH2 
649  N N   . SER A 98  ? 1.6034 1.5673 0.6889 0.3720  -0.0783 0.0931  125 SER A N   
650  C CA  . SER A 98  ? 1.4856 1.4630 0.5763 0.3559  -0.1006 0.0606  125 SER A CA  
651  C C   . SER A 98  ? 1.5356 1.5510 0.6515 0.3553  -0.1305 0.0561  125 SER A C   
652  O O   . SER A 98  ? 1.4694 1.5035 0.5864 0.3708  -0.1393 0.0733  125 SER A O   
653  C CB  . SER A 98  ? 1.4075 1.3830 0.4568 0.3527  -0.1085 0.0367  125 SER A CB  
654  O OG  . SER A 98  ? 1.5079 1.4975 0.5280 0.3674  -0.1165 0.0469  125 SER A OG  
655  N N   . TYR A 99  ? 1.4646 1.4912 0.6011 0.3374  -0.1459 0.0320  126 TYR A N   
656  C CA  . TYR A 99  ? 1.4871 1.5548 0.6622 0.3309  -0.1716 0.0239  126 TYR A CA  
657  C C   . TYR A 99  ? 1.4371 1.5396 0.5858 0.3349  -0.2025 0.0052  126 TYR A C   
658  O O   . TYR A 99  ? 1.6699 1.7616 0.7873 0.3262  -0.2064 -0.0159 126 TYR A O   
659  C CB  . TYR A 99  ? 1.4422 1.5081 0.6686 0.2989  -0.1713 0.0029  126 TYR A CB  
660  C CG  . TYR A 99  ? 1.4420 1.4832 0.7091 0.2925  -0.1453 0.0205  126 TYR A CG  
661  C CD1 . TYR A 99  ? 1.4226 1.4218 0.6814 0.2872  -0.1206 0.0229  126 TYR A CD1 
662  C CD2 . TYR A 99  ? 1.2114 1.2735 0.5261 0.2926  -0.1462 0.0329  126 TYR A CD2 
663  C CE1 . TYR A 99  ? 1.2867 1.2663 0.5828 0.2813  -0.0993 0.0371  126 TYR A CE1 
664  C CE2 . TYR A 99  ? 1.2880 1.3275 0.6374 0.2863  -0.1235 0.0467  126 TYR A CE2 
665  C CZ  . TYR A 99  ? 1.2437 1.2424 0.5833 0.2802  -0.1010 0.0487  126 TYR A CZ  
666  O OH  . TYR A 99  ? 1.2860 1.2652 0.6601 0.2740  -0.0808 0.0608  126 TYR A OH  
667  N N   . PRO A 100 ? 1.4285 1.5727 0.5976 0.3459  -0.2238 0.0112  127 PRO A N   
668  C CA  . PRO A 100 ? 1.5483 1.7288 0.7029 0.3473  -0.2534 -0.0070 127 PRO A CA  
669  C C   . PRO A 100 ? 1.5137 1.7175 0.6789 0.3203  -0.2762 -0.0470 127 PRO A C   
670  O O   . PRO A 100 ? 1.5957 1.8257 0.7465 0.3174  -0.2997 -0.0663 127 PRO A O   
671  C CB  . PRO A 100 ? 1.4368 1.6564 0.6203 0.3670  -0.2687 0.0105  127 PRO A CB  
672  C CG  . PRO A 100 ? 1.4108 1.5999 0.6068 0.3812  -0.2407 0.0445  127 PRO A CG  
673  C CD  . PRO A 100 ? 1.4336 1.5905 0.6369 0.3616  -0.2198 0.0376  127 PRO A CD  
674  N N   . ASP A 101 ? 1.4562 1.6479 0.6519 0.2966  -0.2679 -0.0600 128 ASP A N   
675  C CA  . ASP A 101 ? 1.4592 1.6643 0.6754 0.2633  -0.2839 -0.0970 128 ASP A CA  
676  C C   . ASP A 101 ? 1.5664 1.7169 0.7649 0.2428  -0.2649 -0.1114 128 ASP A C   
677  O O   . ASP A 101 ? 1.5057 1.6521 0.7273 0.2115  -0.2703 -0.1376 128 ASP A O   
678  C CB  . ASP A 101 ? 1.5878 1.8267 0.8756 0.2430  -0.2886 -0.1018 128 ASP A CB  
679  C CG  . ASP A 101 ? 1.4781 1.6807 0.8007 0.2323  -0.2580 -0.0848 128 ASP A CG  
680  O OD1 . ASP A 101 ? 1.4844 1.6455 0.7831 0.2480  -0.2345 -0.0622 128 ASP A OD1 
681  O OD2 . ASP A 101 ? 1.5107 1.7280 0.8847 0.2073  -0.2573 -0.0948 128 ASP A OD2 
682  N N   . GLU A 102 ? 1.5565 1.6647 0.7149 0.2601  -0.2422 -0.0948 129 GLU A N   
683  C CA  . GLU A 102 ? 1.4357 1.4928 0.5785 0.2460  -0.2233 -0.1069 129 GLU A CA  
684  C C   . GLU A 102 ? 1.5488 1.5957 0.6341 0.2477  -0.2355 -0.1329 129 GLU A C   
685  O O   . GLU A 102 ? 1.5541 1.6259 0.6159 0.2607  -0.2485 -0.1317 129 GLU A O   
686  C CB  . GLU A 102 ? 1.4819 1.5026 0.6183 0.2627  -0.1906 -0.0778 129 GLU A CB  
687  C CG  . GLU A 102 ? 1.4867 1.4976 0.5641 0.2909  -0.1820 -0.0648 129 GLU A CG  
688  C CD  . GLU A 102 ? 1.5662 1.5407 0.6399 0.3023  -0.1474 -0.0410 129 GLU A CD  
689  O OE1 . GLU A 102 ? 1.5692 1.5380 0.6892 0.2970  -0.1332 -0.0237 129 GLU A OE1 
690  O OE2 . GLU A 102 ? 1.5563 1.5107 0.5982 0.3105  -0.1319 -0.0404 129 GLU A OE2 
691  N N   . GLU A 103 ? 1.6362 1.6425 0.7148 0.2291  -0.2267 -0.1543 130 GLU A N   
692  C CA  . GLU A 103 ? 1.4828 1.4684 0.5116 0.2288  -0.2316 -0.1797 130 GLU A CA  
693  C C   . GLU A 103 ? 1.4930 1.4347 0.4951 0.2439  -0.2011 -0.1682 130 GLU A C   
694  O O   . GLU A 103 ? 1.5484 1.4703 0.5180 0.2433  -0.1986 -0.1866 130 GLU A O   
695  C CB  . GLU A 103 ? 1.6422 1.6117 0.6803 0.1967  -0.2461 -0.2170 130 GLU A CB  
696  C CG  . GLU A 103 ? 1.5044 1.5210 0.5811 0.1744  -0.2735 -0.2316 130 GLU A CG  
697  C CD  . GLU A 103 ? 1.7221 1.7142 0.8246 0.1361  -0.2776 -0.2599 130 GLU A CD  
698  O OE1 . GLU A 103 ? 1.7278 1.6637 0.8102 0.1300  -0.2628 -0.2700 130 GLU A OE1 
699  O OE2 . GLU A 103 ? 1.8230 1.8512 0.9662 0.1124  -0.2946 -0.2716 130 GLU A OE2 
700  N N   . GLY A 104 ? 1.4745 1.4031 0.4918 0.2568  -0.1777 -0.1397 131 GLY A N   
701  C CA  . GLY A 104 ? 1.4573 1.3502 0.4582 0.2699  -0.1477 -0.1290 131 GLY A CA  
702  C C   . GLY A 104 ? 1.5177 1.4006 0.5578 0.2729  -0.1260 -0.1015 131 GLY A C   
703  O O   . GLY A 104 ? 1.5438 1.4441 0.6306 0.2608  -0.1328 -0.0920 131 GLY A O   
704  N N   . PRO A 105 ? 1.5637 1.4216 0.5936 0.2867  -0.0980 -0.0888 132 PRO A N   
705  C CA  . PRO A 105 ? 1.4867 1.3369 0.5621 0.2867  -0.0764 -0.0636 132 PRO A CA  
706  C C   . PRO A 105 ? 1.4730 1.3020 0.5925 0.2644  -0.0770 -0.0746 132 PRO A C   
707  O O   . PRO A 105 ? 1.3740 1.2051 0.5370 0.2594  -0.0679 -0.0562 132 PRO A O   
708  C CB  . PRO A 105 ? 1.3654 1.1975 0.4150 0.3059  -0.0476 -0.0533 132 PRO A CB  
709  C CG  . PRO A 105 ? 1.5048 1.3214 0.5082 0.3086  -0.0526 -0.0822 132 PRO A CG  
710  C CD  . PRO A 105 ? 1.5324 1.3729 0.5222 0.2994  -0.0832 -0.0972 132 PRO A CD  
711  N N   . LYS A 106 ? 1.5219 1.3276 0.6289 0.2510  -0.0873 -0.1037 133 LYS A N   
712  C CA  . LYS A 106 ? 1.5158 1.2951 0.6572 0.2298  -0.0886 -0.1134 133 LYS A CA  
713  C C   . LYS A 106 ? 1.3840 1.1773 0.5440 0.2043  -0.1126 -0.1275 133 LYS A C   
714  O O   . LYS A 106 ? 1.5999 1.3677 0.7805 0.1835  -0.1153 -0.1382 133 LYS A O   
715  C CB  . LYS A 106 ? 1.4296 1.1655 0.5475 0.2316  -0.0814 -0.1349 133 LYS A CB  
716  C CG  . LYS A 106 ? 1.4035 1.1283 0.5147 0.2547  -0.0549 -0.1224 133 LYS A CG  
717  C CD  . LYS A 106 ? 1.3233 1.0560 0.4810 0.2556  -0.0397 -0.0949 133 LYS A CD  
718  C CE  . LYS A 106 ? 1.5973 1.3335 0.7512 0.2777  -0.0130 -0.0789 133 LYS A CE  
719  N NZ  . LYS A 106 ? 1.4064 1.1505 0.6073 0.2767  0.0011  -0.0543 133 LYS A NZ  
720  N N   . HIS A 107 ? 1.4735 1.3072 0.6267 0.2055  -0.1299 -0.1274 134 HIS A N   
721  C CA  . HIS A 107 ? 1.3673 1.2250 0.5454 0.1814  -0.1519 -0.1404 134 HIS A CA  
722  C C   . HIS A 107 ? 1.4320 1.3171 0.6592 0.1783  -0.1480 -0.1167 134 HIS A C   
723  O O   . HIS A 107 ? 1.4703 1.3781 0.7000 0.1993  -0.1412 -0.0928 134 HIS A O   
724  C CB  . HIS A 107 ? 1.5600 1.4531 0.7087 0.1853  -0.1757 -0.1558 134 HIS A CB  
725  C CG  . HIS A 107 ? 1.5854 1.5140 0.7658 0.1613  -0.1986 -0.1696 134 HIS A CG  
726  N ND1 . HIS A 107 ? 1.5489 1.5297 0.7266 0.1686  -0.2203 -0.1714 134 HIS A ND1 
727  C CD2 . HIS A 107 ? 1.5493 1.4704 0.7655 0.1300  -0.2028 -0.1824 134 HIS A CD2 
728  C CE1 . HIS A 107 ? 1.6057 1.6142 0.8210 0.1425  -0.2366 -0.1864 134 HIS A CE1 
729  N NE2 . HIS A 107 ? 1.4778 1.4498 0.7161 0.1176  -0.2251 -0.1929 134 HIS A NE2 
730  N N   . TRP A 108 ? 1.5255 1.4056 0.7892 0.1521  -0.1511 -0.1234 135 TRP A N   
731  C CA  . TRP A 108 ? 1.4727 1.3767 0.7841 0.1464  -0.1465 -0.1048 135 TRP A CA  
732  C C   . TRP A 108 ? 1.5026 1.4567 0.8351 0.1338  -0.1683 -0.1153 135 TRP A C   
733  O O   . TRP A 108 ? 1.4989 1.4555 0.8521 0.1050  -0.1768 -0.1330 135 TRP A O   
734  C CB  . TRP A 108 ? 1.3964 1.2647 0.7327 0.1266  -0.1342 -0.1043 135 TRP A CB  
735  C CG  . TRP A 108 ? 1.3097 1.1453 0.6429 0.1430  -0.1126 -0.0868 135 TRP A CG  
736  C CD1 . TRP A 108 ? 1.3666 1.1621 0.6710 0.1517  -0.1038 -0.0934 135 TRP A CD1 
737  C CD2 . TRP A 108 ? 1.3953 1.2384 0.7581 0.1529  -0.0973 -0.0618 135 TRP A CD2 
738  N NE1 . TRP A 108 ? 1.4512 1.2328 0.7684 0.1659  -0.0843 -0.0741 135 TRP A NE1 
739  C CE2 . TRP A 108 ? 1.3590 1.1679 0.7110 0.1658  -0.0802 -0.0547 135 TRP A CE2 
740  C CE3 . TRP A 108 ? 1.1934 1.0692 0.5919 0.1524  -0.0963 -0.0464 135 TRP A CE3 
741  C CZ2 . TRP A 108 ? 1.3381 1.1455 0.7143 0.1758  -0.0631 -0.0333 135 TRP A CZ2 
742  C CZ3 . TRP A 108 ? 1.2504 1.1198 0.6696 0.1631  -0.0789 -0.0251 135 TRP A CZ3 
743  C CH2 . TRP A 108 ? 1.3053 1.1413 0.7137 0.1735  -0.0629 -0.0189 135 TRP A CH2 
744  N N   . SER A 109 ? 1.3337 1.3286 0.6614 0.1557  -0.1769 -0.1039 136 SER A N   
745  C CA  . SER A 109 ? 1.3784 1.4284 0.7309 0.1489  -0.1987 -0.1124 136 SER A CA  
746  C C   . SER A 109 ? 1.4312 1.5027 0.8381 0.1416  -0.1909 -0.0980 136 SER A C   
747  O O   . SER A 109 ? 1.3847 1.4283 0.8058 0.1438  -0.1698 -0.0803 136 SER A O   
748  C CB  . SER A 109 ? 1.4474 1.5315 0.7722 0.1787  -0.2125 -0.1041 136 SER A CB  
749  O OG  . SER A 109 ? 1.3944 1.4859 0.7310 0.2035  -0.1997 -0.0725 136 SER A OG  
750  N N   . ASP A 110 ? 1.3639 1.4885 0.8027 0.1330  -0.2087 -0.1077 137 ASP A N   
751  C CA  . ASP A 110 ? 1.3319 1.4820 0.8229 0.1273  -0.2013 -0.0966 137 ASP A CA  
752  C C   . ASP A 110 ? 1.3854 1.5406 0.8806 0.1603  -0.1906 -0.0661 137 ASP A C   
753  O O   . ASP A 110 ? 1.2917 1.4396 0.8179 0.1586  -0.1740 -0.0518 137 ASP A O   
754  C CB  . ASP A 110 ? 1.3752 1.5871 0.9026 0.1120  -0.2226 -0.1160 137 ASP A CB  
755  C CG  . ASP A 110 ? 1.3995 1.6033 0.9346 0.0715  -0.2275 -0.1449 137 ASP A CG  
756  O OD1 . ASP A 110 ? 1.4737 1.6196 0.9827 0.0580  -0.2154 -0.1487 137 ASP A OD1 
757  O OD2 . ASP A 110 ? 1.3737 1.6284 0.9417 0.0533  -0.2433 -0.1641 137 ASP A OD2 
758  N N   . SER A 111 ? 1.3680 1.5324 0.8294 0.1897  -0.1993 -0.0558 138 SER A N   
759  C CA  . SER A 111 ? 1.2546 1.4134 0.7135 0.2202  -0.1867 -0.0250 138 SER A CA  
760  C C   . SER A 111 ? 1.2915 1.3953 0.7395 0.2207  -0.1587 -0.0095 138 SER A C   
761  O O   . SER A 111 ? 1.2967 1.3914 0.7664 0.2303  -0.1423 0.0113  138 SER A O   
762  C CB  . SER A 111 ? 1.2461 1.4196 0.6622 0.2505  -0.2009 -0.0164 138 SER A CB  
763  O OG  . SER A 111 ? 1.4563 1.6869 0.8872 0.2543  -0.2290 -0.0291 138 SER A OG  
764  N N   . ARG A 112 ? 1.3252 1.3926 0.7413 0.2107  -0.1534 -0.0211 139 ARG A N   
765  C CA  . ARG A 112 ? 1.2985 1.3183 0.7082 0.2108  -0.1286 -0.0097 139 ARG A CA  
766  C C   . ARG A 112 ? 1.2563 1.2642 0.7073 0.1881  -0.1183 -0.0119 139 ARG A C   
767  O O   . ARG A 112 ? 1.2360 1.2260 0.7038 0.1936  -0.0998 0.0055  139 ARG A O   
768  C CB  . ARG A 112 ? 1.2706 1.2578 0.6370 0.2080  -0.1272 -0.0242 139 ARG A CB  
769  C CG  . ARG A 112 ? 1.2933 1.2369 0.6510 0.2136  -0.1026 -0.0130 139 ARG A CG  
770  C CD  . ARG A 112 ? 1.3506 1.2637 0.6694 0.2109  -0.1021 -0.0313 139 ARG A CD  
771  N NE  . ARG A 112 ? 1.2427 1.1207 0.5564 0.2189  -0.0791 -0.0218 139 ARG A NE  
772  C CZ  . ARG A 112 ? 1.3017 1.1526 0.5828 0.2239  -0.0730 -0.0334 139 ARG A CZ  
773  N NH1 . ARG A 112 ? 1.3602 1.2097 0.6066 0.2212  -0.0878 -0.0555 139 ARG A NH1 
774  N NH2 . ARG A 112 ? 1.4122 1.2386 0.6968 0.2323  -0.0517 -0.0242 139 ARG A NH2 
775  N N   . TYR A 113 ? 1.2414 1.2583 0.7075 0.1615  -0.1296 -0.0337 140 TYR A N   
776  C CA  . TYR A 113 ? 1.1768 1.1860 0.6793 0.1390  -0.1206 -0.0354 140 TYR A CA  
777  C C   . TYR A 113 ? 1.2060 1.2448 0.7468 0.1486  -0.1149 -0.0189 140 TYR A C   
778  O O   . TYR A 113 ? 1.1940 1.2133 0.7533 0.1467  -0.0983 -0.0071 140 TYR A O   
779  C CB  . TYR A 113 ? 1.1987 1.2202 0.7113 0.1083  -0.1343 -0.0606 140 TYR A CB  
780  C CG  . TYR A 113 ? 1.2984 1.2726 0.7832 0.0899  -0.1329 -0.0765 140 TYR A CG  
781  C CD1 . TYR A 113 ? 1.1982 1.1227 0.6723 0.0914  -0.1161 -0.0676 140 TYR A CD1 
782  C CD2 . TYR A 113 ? 1.2505 1.2296 0.7210 0.0715  -0.1495 -0.1015 140 TYR A CD2 
783  C CE1 . TYR A 113 ? 1.2824 1.1612 0.7309 0.0777  -0.1158 -0.0819 140 TYR A CE1 
784  C CE2 . TYR A 113 ? 1.2256 1.1559 0.6695 0.0554  -0.1481 -0.1165 140 TYR A CE2 
785  C CZ  . TYR A 113 ? 1.3617 1.2409 0.7940 0.0599  -0.1313 -0.1060 140 TYR A CZ  
786  O OH  . TYR A 113 ? 1.4267 1.2549 0.8319 0.0469  -0.1310 -0.1208 140 TYR A OH  
787  N N   . GLU A 114 ? 1.2215 1.3076 0.7744 0.1601  -0.1297 -0.0190 141 GLU A N   
788  C CA  . GLU A 114 ? 1.1195 1.2348 0.7099 0.1715  -0.1257 -0.0054 141 GLU A CA  
789  C C   . GLU A 114 ? 1.1000 1.1881 0.6828 0.1957  -0.1081 0.0207  141 GLU A C   
790  O O   . GLU A 114 ? 1.1507 1.2325 0.7619 0.1949  -0.0940 0.0306  141 GLU A O   
791  C CB  . GLU A 114 ? 1.1395 1.3106 0.7406 0.1847  -0.1475 -0.0104 141 GLU A CB  
792  C CG  . GLU A 114 ? 1.2690 1.4681 0.9040 0.2049  -0.1445 0.0054  141 GLU A CG  
793  C CD  . GLU A 114 ? 1.1852 1.4403 0.8292 0.2228  -0.1686 0.0010  141 GLU A CD  
794  O OE1 . GLU A 114 ? 1.2341 1.5230 0.8830 0.2065  -0.1874 -0.0221 141 GLU A OE1 
795  O OE2 . GLU A 114 ? 1.3082 1.5722 0.9539 0.2535  -0.1693 0.0205  141 GLU A OE2 
796  N N   . HIS A 115 ? 1.0860 1.1575 0.6299 0.2162  -0.1077 0.0313  142 HIS A N   
797  C CA  . HIS A 115 ? 1.1506 1.1963 0.6873 0.2371  -0.0893 0.0563  142 HIS A CA  
798  C C   . HIS A 115 ? 1.1308 1.1368 0.6756 0.2238  -0.0685 0.0588  142 HIS A C   
799  O O   . HIS A 115 ? 1.1485 1.1427 0.7136 0.2298  -0.0532 0.0738  142 HIS A O   
800  C CB  . HIS A 115 ? 1.2549 1.2906 0.7445 0.2590  -0.0910 0.0665  142 HIS A CB  
801  C CG  . HIS A 115 ? 1.1599 1.1694 0.6408 0.2787  -0.0705 0.0929  142 HIS A CG  
802  N ND1 . HIS A 115 ? 1.1248 1.1440 0.6217 0.2972  -0.0679 0.1124  142 HIS A ND1 
803  C CD2 . HIS A 115 ? 1.1729 1.1466 0.6330 0.2816  -0.0506 0.1025  142 HIS A CD2 
804  C CE1 . HIS A 115 ? 1.2707 1.2579 0.7550 0.3088  -0.0469 0.1333  142 HIS A CE1 
805  N NE2 . HIS A 115 ? 1.2705 1.2328 0.7343 0.2990  -0.0358 0.1274  142 HIS A NE2 
806  N N   . VAL A 116 ? 1.2303 1.2147 0.7593 0.2064  -0.0689 0.0432  143 VAL A N   
807  C CA  . VAL A 116 ? 1.2644 1.2121 0.7993 0.1961  -0.0522 0.0446  143 VAL A CA  
808  C C   . VAL A 116 ? 1.1891 1.1414 0.7626 0.1798  -0.0479 0.0428  143 VAL A C   
809  O O   . VAL A 116 ? 1.1377 1.0709 0.7262 0.1806  -0.0329 0.0527  143 VAL A O   
810  C CB  . VAL A 116 ? 1.2046 1.1266 0.7117 0.1840  -0.0559 0.0277  143 VAL A CB  
811  C CG1 . VAL A 116 ? 0.9556 0.8441 0.4734 0.1716  -0.0437 0.0261  143 VAL A CG1 
812  C CG2 . VAL A 116 ? 1.1308 1.0424 0.5990 0.2030  -0.0532 0.0317  143 VAL A CG2 
813  N N   . MET A 117 ? 1.1884 1.1679 0.7786 0.1642  -0.0604 0.0292  144 MET A N   
814  C CA  . MET A 117 ? 1.0719 1.0602 0.6974 0.1494  -0.0547 0.0274  144 MET A CA  
815  C C   . MET A 117 ? 0.9653 0.9684 0.6158 0.1676  -0.0462 0.0439  144 MET A C   
816  O O   . MET A 117 ? 1.0946 1.0862 0.7657 0.1623  -0.0337 0.0482  144 MET A O   
817  C CB  . MET A 117 ? 1.1345 1.1555 0.7753 0.1290  -0.0681 0.0093  144 MET A CB  
818  C CG  . MET A 117 ? 1.1299 1.1274 0.7519 0.1034  -0.0728 -0.0079 144 MET A CG  
819  S SD  . MET A 117 ? 1.1343 1.1693 0.7822 0.0730  -0.0830 -0.0286 144 MET A SD  
820  C CE  . MET A 117 ? 1.1968 1.2406 0.8162 0.0691  -0.1037 -0.0466 144 MET A CE  
821  N N   . LYS A 118 ? 1.1400 1.1659 0.7864 0.1901  -0.0532 0.0529  145 LYS A N   
822  C CA  . LYS A 118 ? 1.1684 1.2019 0.8356 0.2096  -0.0452 0.0696  145 LYS A CA  
823  C C   . LYS A 118 ? 1.0727 1.0663 0.7320 0.2179  -0.0261 0.0856  145 LYS A C   
824  O O   . LYS A 118 ? 0.9796 0.9662 0.6630 0.2208  -0.0142 0.0935  145 LYS A O   
825  C CB  . LYS A 118 ? 0.9114 0.9737 0.5702 0.2341  -0.0587 0.0773  145 LYS A CB  
826  C CG  . LYS A 118 ? 0.8532 0.9650 0.5303 0.2276  -0.0786 0.0604  145 LYS A CG  
827  C CD  . LYS A 118 ? 1.0547 1.1997 0.7348 0.2562  -0.0920 0.0698  145 LYS A CD  
828  C CE  . LYS A 118 ? 0.9284 1.1309 0.6382 0.2488  -0.1114 0.0505  145 LYS A CE  
829  N NZ  . LYS A 118 ? 1.1701 1.4087 0.8913 0.2800  -0.1251 0.0597  145 LYS A NZ  
830  N N   . LEU A 119 ? 1.0084 0.9771 0.6360 0.2207  -0.0225 0.0887  146 LEU A N   
831  C CA  . LEU A 119 ? 1.0784 1.0144 0.7024 0.2268  -0.0037 0.1021  146 LEU A CA  
832  C C   . LEU A 119 ? 1.1491 1.0672 0.7941 0.2084  0.0055  0.0948  146 LEU A C   
833  O O   . LEU A 119 ? 1.1036 1.0076 0.7661 0.2115  0.0194  0.1042  146 LEU A O   
834  C CB  . LEU A 119 ? 1.1675 1.0861 0.7542 0.2337  -0.0011 0.1044  146 LEU A CB  
835  C CG  . LEU A 119 ? 1.0936 1.0215 0.6521 0.2559  -0.0050 0.1173  146 LEU A CG  
836  C CD1 . LEU A 119 ? 1.1887 1.1003 0.7084 0.2600  -0.0011 0.1157  146 LEU A CD1 
837  C CD2 . LEU A 119 ? 1.0216 0.9408 0.5905 0.2724  0.0088  0.1400  146 LEU A CD2 
838  N N   . ARG A 120 ? 0.9999 0.9164 0.6417 0.1890  -0.0025 0.0781  147 ARG A N   
839  C CA  . ARG A 120 ? 0.9840 0.8817 0.6402 0.1729  0.0045  0.0723  147 ARG A CA  
840  C C   . ARG A 120 ? 1.0749 0.9878 0.7626 0.1679  0.0081  0.0727  147 ARG A C   
841  O O   . ARG A 120 ? 1.1579 1.0557 0.8604 0.1646  0.0186  0.0755  147 ARG A O   
842  C CB  . ARG A 120 ? 1.0242 0.9107 0.6643 0.1539  -0.0046 0.0564  147 ARG A CB  
843  C CG  . ARG A 120 ? 1.1563 1.0205 0.7664 0.1593  -0.0055 0.0539  147 ARG A CG  
844  C CD  . ARG A 120 ? 0.9841 0.8229 0.5807 0.1421  -0.0106 0.0403  147 ARG A CD  
845  N NE  . ARG A 120 ? 1.0876 0.9030 0.6591 0.1510  -0.0093 0.0377  147 ARG A NE  
846  C CZ  . ARG A 120 ? 1.1034 0.9121 0.6476 0.1495  -0.0186 0.0265  147 ARG A CZ  
847  N NH1 . ARG A 120 ? 1.1703 0.9934 0.7092 0.1366  -0.0313 0.0159  147 ARG A NH1 
848  N NH2 . ARG A 120 ? 1.2212 1.0100 0.7443 0.1608  -0.0148 0.0242  147 ARG A NH2 
849  N N   . GLN A 121 ? 1.0357 0.9809 0.7350 0.1678  -0.0009 0.0683  148 GLN A N   
850  C CA  . GLN A 121 ? 0.8529 0.8169 0.5839 0.1676  0.0037  0.0683  148 GLN A CA  
851  C C   . GLN A 121 ? 1.0070 0.9608 0.7495 0.1873  0.0153  0.0840  148 GLN A C   
852  O O   . GLN A 121 ? 0.9629 0.9098 0.7263 0.1843  0.0254  0.0841  148 GLN A O   
853  C CB  . GLN A 121 ? 0.8796 0.8861 0.6234 0.1684  -0.0087 0.0607  148 GLN A CB  
854  C CG  . GLN A 121 ? 0.8290 0.8602 0.6078 0.1691  -0.0037 0.0580  148 GLN A CG  
855  C CD  . GLN A 121 ? 0.8691 0.8956 0.6576 0.1435  0.0031  0.0456  148 GLN A CD  
856  O OE1 . GLN A 121 ? 0.8875 0.9005 0.6581 0.1233  -0.0003 0.0372  148 GLN A OE1 
857  N NE2 . GLN A 121 ? 0.8901 0.9247 0.7042 0.1446  0.0132  0.0446  148 GLN A NE2 
858  N N   . ALA A 122 ? 1.0232 0.9735 0.7499 0.2069  0.0147  0.0972  149 ALA A N   
859  C CA  . ALA A 122 ? 0.9007 0.8351 0.6349 0.2245  0.0273  0.1140  149 ALA A CA  
860  C C   . ALA A 122 ? 0.9430 0.8453 0.6803 0.2161  0.0422  0.1162  149 ALA A C   
861  O O   . ALA A 122 ? 1.0408 0.9309 0.7977 0.2197  0.0538  0.1220  149 ALA A O   
862  C CB  . ALA A 122 ? 0.8931 0.8264 0.6020 0.2455  0.0244  0.1291  149 ALA A CB  
863  N N   . ALA A 123 ? 0.9394 0.8282 0.6589 0.2056  0.0414  0.1103  150 ALA A N   
864  C CA  . ALA A 123 ? 1.1052 0.9695 0.8311 0.1979  0.0529  0.1098  150 ALA A CA  
865  C C   . ALA A 123 ? 1.0820 0.9456 0.8293 0.1830  0.0536  0.0989  150 ALA A C   
866  O O   . ALA A 123 ? 1.0110 0.8605 0.7746 0.1811  0.0638  0.1004  150 ALA A O   
867  C CB  . ALA A 123 ? 0.9554 0.8080 0.6581 0.1930  0.0500  0.1044  150 ALA A CB  
868  N N   . LEU A 124 ? 1.0055 0.8843 0.7519 0.1711  0.0434  0.0873  151 LEU A N   
869  C CA  . LEU A 124 ? 0.8903 0.7689 0.6520 0.1566  0.0454  0.0775  151 LEU A CA  
870  C C   . LEU A 124 ? 1.0173 0.9047 0.8051 0.1647  0.0537  0.0807  151 LEU A C   
871  O O   . LEU A 124 ? 0.9491 0.8251 0.7500 0.1588  0.0612  0.0768  151 LEU A O   
872  C CB  . LEU A 124 ? 0.8921 0.7859 0.6462 0.1408  0.0353  0.0655  151 LEU A CB  
873  C CG  . LEU A 124 ? 0.8858 0.7800 0.6486 0.1233  0.0381  0.0553  151 LEU A CG  
874  C CD1 . LEU A 124 ? 0.8679 0.7313 0.6198 0.1153  0.0408  0.0535  151 LEU A CD1 
875  C CD2 . LEU A 124 ? 0.9161 0.8268 0.6715 0.1066  0.0303  0.0451  151 LEU A CD2 
876  N N   . LYS A 125 ? 0.9059 0.8128 0.7007 0.1796  0.0515  0.0872  152 LYS A N   
877  C CA  . LYS A 125 ? 0.9080 0.8193 0.7271 0.1912  0.0593  0.0908  152 LYS A CA  
878  C C   . LYS A 125 ? 1.0445 0.9256 0.8682 0.1987  0.0723  0.1012  152 LYS A C   
879  O O   . LYS A 125 ? 0.9403 0.8120 0.7833 0.1980  0.0813  0.0980  152 LYS A O   
880  C CB  . LYS A 125 ? 0.8809 0.8180 0.7044 0.2096  0.0521  0.0970  152 LYS A CB  
881  C CG  . LYS A 125 ? 0.7832 0.7209 0.6302 0.2271  0.0596  0.1025  152 LYS A CG  
882  C CD  . LYS A 125 ? 0.7448 0.7115 0.5957 0.2479  0.0490  0.1081  152 LYS A CD  
883  C CE  . LYS A 125 ? 0.7605 0.7207 0.6314 0.2699  0.0562  0.1160  152 LYS A CE  
884  N NZ  . LYS A 125 ? 1.0520 1.0260 0.9525 0.2633  0.0622  0.1001  152 LYS A NZ  
885  N N   . SER A 126 ? 0.9550 0.8210 0.7614 0.2046  0.0744  0.1123  153 SER A N   
886  C CA  . SER A 126 ? 0.9676 0.8066 0.7802 0.2079  0.0885  0.1215  153 SER A CA  
887  C C   . SER A 126 ? 1.0026 0.8298 0.8277 0.1910  0.0929  0.1093  153 SER A C   
888  O O   . SER A 126 ? 1.0453 0.8590 0.8898 0.1900  0.1028  0.1083  153 SER A O   
889  C CB  . SER A 126 ? 0.9609 0.7904 0.7514 0.2144  0.0913  0.1335  153 SER A CB  
890  O OG  . SER A 126 ? 1.2106 1.0461 0.9872 0.2328  0.0888  0.1475  153 SER A OG  
891  N N   . ALA A 127 ? 0.9421 0.7726 0.7547 0.1782  0.0846  0.0994  154 ALA A N   
892  C CA  . ALA A 127 ? 1.0029 0.8232 0.8232 0.1641  0.0854  0.0880  154 ALA A CA  
893  C C   . ALA A 127 ? 0.9503 0.7742 0.7869 0.1583  0.0874  0.0785  154 ALA A C   
894  O O   . ALA A 127 ? 0.9733 0.7852 0.8241 0.1531  0.0935  0.0728  154 ALA A O   
895  C CB  . ALA A 127 ? 0.8937 0.7146 0.6933 0.1538  0.0741  0.0801  154 ALA A CB  
896  N N   . ARG A 128 ? 0.9604 0.8033 0.7966 0.1591  0.0828  0.0751  155 ARG A N   
897  C CA  . ARG A 128 ? 0.8308 0.6802 0.6825 0.1548  0.0868  0.0648  155 ARG A CA  
898  C C   . ARG A 128 ? 0.9652 0.8044 0.8385 0.1676  0.0980  0.0696  155 ARG A C   
899  O O   . ARG A 128 ? 0.9516 0.7808 0.8377 0.1624  0.1044  0.0603  155 ARG A O   
900  C CB  . ARG A 128 ? 0.7843 0.6618 0.6348 0.1529  0.0808  0.0595  155 ARG A CB  
901  C CG  . ARG A 128 ? 0.7938 0.6764 0.6237 0.1351  0.0720  0.0518  155 ARG A CG  
902  C CD  . ARG A 128 ? 0.9592 0.8726 0.7901 0.1335  0.0660  0.0487  155 ARG A CD  
903  N NE  . ARG A 128 ? 0.8674 0.7830 0.6806 0.1127  0.0605  0.0399  155 ARG A NE  
904  C CZ  . ARG A 128 ? 1.0059 0.9444 0.8158 0.1054  0.0537  0.0359  155 ARG A CZ  
905  N NH1 . ARG A 128 ? 0.9326 0.8976 0.7552 0.1190  0.0490  0.0393  155 ARG A NH1 
906  N NH2 . ARG A 128 ? 0.9079 0.8417 0.7006 0.0838  0.0512  0.0283  155 ARG A NH2 
907  N N   . ASP A 129 ? 0.9759 0.8144 0.8508 0.1848  0.1003  0.0841  156 ASP A N   
908  C CA  . ASP A 129 ? 0.9480 0.7713 0.8407 0.1985  0.1111  0.0905  156 ASP A CA  
909  C C   . ASP A 129 ? 0.8977 0.6912 0.7986 0.1921  0.1220  0.0916  156 ASP A C   
910  O O   . ASP A 129 ? 1.1043 0.8812 1.0228 0.1948  0.1315  0.0884  156 ASP A O   
911  C CB  . ASP A 129 ? 0.9041 0.7300 0.7904 0.2195  0.1098  0.1083  156 ASP A CB  
912  C CG  . ASP A 129 ? 1.0817 0.9418 0.9688 0.2282  0.0987  0.1048  156 ASP A CG  
913  O OD1 . ASP A 129 ? 1.1364 1.0165 1.0336 0.2177  0.0960  0.0887  156 ASP A OD1 
914  O OD2 . ASP A 129 ? 1.0686 0.9374 0.9461 0.2449  0.0927  0.1176  156 ASP A OD2 
915  N N   . MET A 130 ? 0.9030 0.6905 0.7935 0.1834  0.1209  0.0943  157 MET A N   
916  C CA  . MET A 130 ? 0.7806 0.5472 0.6835 0.1753  0.1304  0.0931  157 MET A CA  
917  C C   . MET A 130 ? 1.0231 0.7918 0.9320 0.1584  0.1255  0.0741  157 MET A C   
918  O O   . MET A 130 ? 1.0681 0.8263 0.9886 0.1500  0.1299  0.0699  157 MET A O   
919  C CB  . MET A 130 ? 0.8076 0.5702 0.6995 0.1765  0.1334  0.1053  157 MET A CB  
920  C CG  . MET A 130 ? 0.8508 0.6281 0.7261 0.1689  0.1215  0.0988  157 MET A CG  
921  S SD  . MET A 130 ? 1.0650 0.8401 0.9258 0.1750  0.1268  0.1128  157 MET A SD  
922  C CE  . MET A 130 ? 1.1392 0.8953 1.0271 0.1697  0.1459  0.1163  157 MET A CE  
923  N N   . TRP A 131 ? 0.9302 0.7137 0.8310 0.1532  0.1164  0.0627  158 TRP A N   
924  C CA  . TRP A 131 ? 0.9682 0.7514 0.8689 0.1387  0.1116  0.0454  158 TRP A CA  
925  C C   . TRP A 131 ? 1.0659 0.8472 0.9574 0.1302  0.1038  0.0433  158 TRP A C   
926  O O   . TRP A 131 ? 0.9867 0.7621 0.8857 0.1214  0.1019  0.0322  158 TRP A O   
927  C CB  . TRP A 131 ? 0.8627 0.6313 0.7848 0.1363  0.1208  0.0356  158 TRP A CB  
928  C CG  . TRP A 131 ? 0.9105 0.6846 0.8364 0.1395  0.1240  0.0264  158 TRP A CG  
929  C CD1 . TRP A 131 ? 0.9993 0.7940 0.9138 0.1411  0.1194  0.0244  158 TRP A CD1 
930  C CD2 . TRP A 131 ? 0.9305 0.6904 0.8745 0.1409  0.1336  0.0159  158 TRP A CD2 
931  N NE1 . TRP A 131 ? 0.9541 0.7517 0.8798 0.1446  0.1263  0.0136  158 TRP A NE1 
932  C CE2 . TRP A 131 ? 0.9033 0.6778 0.8457 0.1456  0.1347  0.0080  158 TRP A CE2 
933  C CE3 . TRP A 131 ? 0.7976 0.5340 0.7604 0.1378  0.1419  0.0111  158 TRP A CE3 
934  C CZ2 . TRP A 131 ? 0.8938 0.6592 0.8508 0.1496  0.1438  -0.0048 158 TRP A CZ2 
935  C CZ3 . TRP A 131 ? 0.9131 0.6368 0.8893 0.1404  0.1502  -0.0015 158 TRP A CZ3 
936  C CH2 . TRP A 131 ? 1.0068 0.7445 0.9791 0.1475  0.1510  -0.0095 158 TRP A CH2 
937  N N   . ALA A 132 ? 0.9202 0.7075 0.7955 0.1341  0.0984  0.0527  159 ALA A N   
938  C CA  . ALA A 132 ? 0.9078 0.6938 0.7728 0.1290  0.0900  0.0499  159 ALA A CA  
939  C C   . ALA A 132 ? 0.9745 0.7616 0.8197 0.1191  0.0774  0.0389  159 ALA A C   
940  O O   . ALA A 132 ? 0.9423 0.7351 0.7759 0.1156  0.0756  0.0365  159 ALA A O   
941  C CB  . ALA A 132 ? 0.8174 0.6071 0.6684 0.1372  0.0886  0.0617  159 ALA A CB  
942  N N   . ASP A 133 ? 0.9772 0.7590 0.8184 0.1147  0.0692  0.0324  160 ASP A N   
943  C CA  . ASP A 133 ? 1.0247 0.8013 0.8400 0.1068  0.0565  0.0249  160 ASP A CA  
944  C C   . ASP A 133 ? 1.0060 0.7796 0.7953 0.1081  0.0491  0.0314  160 ASP A C   
945  O O   . ASP A 133 ? 0.9972 0.7665 0.7628 0.1000  0.0437  0.0293  160 ASP A O   
946  C CB  . ASP A 133 ? 1.0852 0.8567 0.9040 0.1044  0.0476  0.0156  160 ASP A CB  
947  C CG  . ASP A 133 ? 1.0876 0.8616 0.9312 0.1004  0.0532  0.0057  160 ASP A CG  
948  O OD1 . ASP A 133 ? 1.0168 0.7905 0.8596 0.0960  0.0592  0.0015  160 ASP A OD1 
949  O OD2 . ASP A 133 ? 1.0219 0.7994 0.8873 0.1013  0.0521  0.0007  160 ASP A OD2 
950  N N   . TYR A 134 ? 1.0565 0.8312 0.8490 0.1170  0.0501  0.0384  161 TYR A N   
951  C CA  . TYR A 134 ? 1.0259 0.7951 0.7936 0.1191  0.0428  0.0423  161 TYR A CA  
952  C C   . TYR A 134 ? 0.9984 0.7768 0.7712 0.1286  0.0505  0.0519  161 TYR A C   
953  O O   . TYR A 134 ? 0.9648 0.7495 0.7592 0.1354  0.0613  0.0572  161 TYR A O   
954  C CB  . TYR A 134 ? 0.9627 0.7203 0.7209 0.1228  0.0327  0.0384  161 TYR A CB  
955  C CG  . TYR A 134 ? 1.1019 0.8464 0.8447 0.1156  0.0212  0.0307  161 TYR A CG  
956  C CD1 . TYR A 134 ? 0.9756 0.7025 0.6841 0.1083  0.0123  0.0306  161 TYR A CD1 
957  C CD2 . TYR A 134 ? 1.0253 0.7737 0.7858 0.1155  0.0191  0.0235  161 TYR A CD2 
958  C CE1 . TYR A 134 ? 1.1542 0.8650 0.8421 0.1024  0.0022  0.0258  161 TYR A CE1 
959  C CE2 . TYR A 134 ? 1.1112 0.8472 0.8524 0.1105  0.0069  0.0168  161 TYR A CE2 
960  C CZ  . TYR A 134 ? 1.1373 0.8532 0.8401 0.1046  -0.0012 0.0192  161 TYR A CZ  
961  O OH  . TYR A 134 ? 1.1735 0.8729 0.8506 0.1001  -0.0129 0.0149  161 TYR A OH  
962  N N   . ILE A 135 ? 0.9539 0.7311 0.7042 0.1284  0.0449  0.0540  162 ILE A N   
963  C CA  . ILE A 135 ? 0.9127 0.6959 0.6582 0.1386  0.0484  0.0614  162 ILE A CA  
964  C C   . ILE A 135 ? 1.0411 0.8111 0.7626 0.1401  0.0392  0.0575  162 ILE A C   
965  O O   . ILE A 135 ? 1.0210 0.7791 0.7216 0.1310  0.0292  0.0519  162 ILE A O   
966  C CB  . ILE A 135 ? 0.9304 0.7280 0.6727 0.1390  0.0493  0.0658  162 ILE A CB  
967  C CG1 . ILE A 135 ? 0.8703 0.6729 0.6010 0.1506  0.0505  0.0730  162 ILE A CG1 
968  C CG2 . ILE A 135 ? 0.9152 0.7132 0.6419 0.1255  0.0401  0.0584  162 ILE A CG2 
969  C CD1 . ILE A 135 ? 0.9022 0.7226 0.6352 0.1564  0.0517  0.0795  162 ILE A CD1 
970  N N   . LEU A 136 ? 1.0333 0.8034 0.7575 0.1514  0.0439  0.0600  163 LEU A N   
971  C CA  . LEU A 136 ? 0.9472 0.7046 0.6509 0.1565  0.0368  0.0551  163 LEU A CA  
972  C C   . LEU A 136 ? 1.0757 0.8393 0.7641 0.1643  0.0402  0.0593  163 LEU A C   
973  O O   . LEU A 136 ? 1.0574 0.8321 0.7559 0.1739  0.0521  0.0667  163 LEU A O   
974  C CB  . LEU A 136 ? 0.9526 0.7093 0.6727 0.1647  0.0396  0.0518  163 LEU A CB  
975  C CG  . LEU A 136 ? 1.1131 0.8580 0.8159 0.1744  0.0337  0.0456  163 LEU A CG  
976  C CD1 . LEU A 136 ? 1.0865 0.8064 0.7657 0.1686  0.0173  0.0385  163 LEU A CD1 
977  C CD2 . LEU A 136 ? 0.9310 0.6879 0.6595 0.1851  0.0414  0.0431  163 LEU A CD2 
978  N N   . PHE A 137 ? 1.0974 0.8528 0.7598 0.1592  0.0301  0.0546  164 PHE A N   
979  C CA  . PHE A 137 ? 0.9954 0.7552 0.6379 0.1663  0.0299  0.0552  164 PHE A CA  
980  C C   . PHE A 137 ? 1.0618 0.8064 0.6890 0.1757  0.0287  0.0484  164 PHE A C   
981  O O   . PHE A 137 ? 1.1892 0.9126 0.8068 0.1723  0.0198  0.0402  164 PHE A O   
982  C CB  . PHE A 137 ? 1.0718 0.8324 0.6964 0.1547  0.0189  0.0502  164 PHE A CB  
983  C CG  . PHE A 137 ? 1.0503 0.8347 0.6902 0.1510  0.0211  0.0564  164 PHE A CG  
984  C CD1 . PHE A 137 ? 0.9453 0.7485 0.5820 0.1612  0.0232  0.0630  164 PHE A CD1 
985  C CD2 . PHE A 137 ? 1.0286 0.8164 0.6844 0.1391  0.0208  0.0555  164 PHE A CD2 
986  C CE1 . PHE A 137 ? 1.0266 0.8520 0.6784 0.1614  0.0237  0.0686  164 PHE A CE1 
987  C CE2 . PHE A 137 ? 0.9472 0.7585 0.6195 0.1380  0.0232  0.0596  164 PHE A CE2 
988  C CZ  . PHE A 137 ? 1.0836 0.9138 0.7554 0.1501  0.0240  0.0663  164 PHE A CZ  
989  N N   . VAL A 138 ? 1.0965 0.8506 0.7200 0.1889  0.0385  0.0522  165 VAL A N   
990  C CA  . VAL A 138 ? 1.1490 0.8929 0.7584 0.2003  0.0401  0.0446  165 VAL A CA  
991  C C   . VAL A 138 ? 1.1352 0.8854 0.7181 0.2078  0.0425  0.0451  165 VAL A C   
992  O O   . VAL A 138 ? 1.1608 0.9283 0.7474 0.2139  0.0539  0.0564  165 VAL A O   
993  C CB  . VAL A 138 ? 1.0643 0.8176 0.7003 0.2101  0.0537  0.0471  165 VAL A CB  
994  C CG1 . VAL A 138 ? 0.9199 0.6652 0.5436 0.2234  0.0552  0.0367  165 VAL A CG1 
995  C CG2 . VAL A 138 ? 1.0172 0.7689 0.6805 0.2027  0.0499  0.0464  165 VAL A CG2 
996  N N   . ASP A 139 ? 1.0107 0.7443 0.5642 0.2072  0.0316  0.0328  166 ASP A N   
997  C CA  . ASP A 139 ? 1.1337 0.8723 0.6581 0.2152  0.0324  0.0299  166 ASP A CA  
998  C C   . ASP A 139 ? 1.1695 0.9155 0.6934 0.2322  0.0495  0.0325  166 ASP A C   
999  O O   . ASP A 139 ? 1.2218 0.9619 0.7608 0.2386  0.0556  0.0279  166 ASP A O   
1000 C CB  . ASP A 139 ? 1.3015 1.0166 0.7956 0.2099  0.0175  0.0129  166 ASP A CB  
1001 C CG  . ASP A 139 ? 1.4256 1.1430 0.9129 0.1923  0.0033  0.0103  166 ASP A CG  
1002 O OD1 . ASP A 139 ? 1.1242 0.8643 0.6305 0.1872  0.0049  0.0215  166 ASP A OD1 
1003 O OD2 . ASP A 139 ? 1.4475 1.1442 0.9121 0.1835  -0.0088 -0.0039 166 ASP A OD2 
1004 N N   . ALA A 140 ? 1.0948 0.8554 0.6006 0.2402  0.0573  0.0398  167 ALA A N   
1005 C CA  . ALA A 140 ? 1.1457 0.9161 0.6507 0.2544  0.0780  0.0458  167 ALA A CA  
1006 C C   . ALA A 140 ? 1.2302 0.9893 0.7229 0.2649  0.0816  0.0296  167 ALA A C   
1007 O O   . ALA A 140 ? 1.3292 1.0988 0.8326 0.2752  0.1007  0.0320  167 ALA A O   
1008 C CB  . ALA A 140 ? 1.2180 1.0009 0.6947 0.2615  0.0837  0.0568  167 ALA A CB  
1009 N N   . ASP A 141 ? 1.2422 0.9798 0.7139 0.2624  0.0648  0.0126  168 ASP A N   
1010 C CA  . ASP A 141 ? 1.2482 0.9704 0.7075 0.2745  0.0666  -0.0045 168 ASP A CA  
1011 C C   . ASP A 141 ? 1.3074 1.0080 0.7856 0.2716  0.0554  -0.0135 168 ASP A C   
1012 O O   . ASP A 141 ? 1.3501 1.0268 0.8114 0.2794  0.0488  -0.0298 168 ASP A O   
1013 C CB  . ASP A 141 ? 1.1825 0.8908 0.5956 0.2776  0.0576  -0.0190 168 ASP A CB  
1014 C CG  . ASP A 141 ? 1.3303 1.0203 0.7294 0.2604  0.0346  -0.0261 168 ASP A CG  
1015 O OD1 . ASP A 141 ? 1.3785 1.0694 0.8012 0.2464  0.0272  -0.0176 168 ASP A OD1 
1016 O OD2 . ASP A 141 ? 1.4438 1.1189 0.8079 0.2599  0.0247  -0.0415 168 ASP A OD2 
1017 N N   . ASN A 142 ? 1.2898 0.9961 0.8003 0.2617  0.0529  -0.0032 169 ASN A N   
1018 C CA  . ASN A 142 ? 1.2459 0.9327 0.7723 0.2597  0.0419  -0.0091 169 ASN A CA  
1019 C C   . ASN A 142 ? 1.2110 0.9176 0.7752 0.2708  0.0545  -0.0068 169 ASN A C   
1020 O O   . ASN A 142 ? 1.2122 0.9439 0.8048 0.2659  0.0657  0.0057  169 ASN A O   
1021 C CB  . ASN A 142 ? 1.2352 0.9151 0.7688 0.2403  0.0293  -0.0016 169 ASN A CB  
1022 C CG  . ASN A 142 ? 1.2520 0.9102 0.7529 0.2272  0.0146  -0.0081 169 ASN A CG  
1023 O OD1 . ASN A 142 ? 1.2553 0.8996 0.7567 0.2116  0.0036  -0.0067 169 ASN A OD1 
1024 N ND2 . ASN A 142 ? 1.2512 0.9073 0.7233 0.2324  0.0151  -0.0162 169 ASN A ND2 
1025 N N   . LEU A 143 ? 1.1735 0.8690 0.7395 0.2859  0.0523  -0.0199 170 LEU A N   
1026 C CA  . LEU A 143 ? 1.2101 0.9303 0.8143 0.2988  0.0641  -0.0218 170 LEU A CA  
1027 C C   . LEU A 143 ? 1.1896 0.9019 0.8179 0.2959  0.0492  -0.0220 170 LEU A C   
1028 O O   . LEU A 143 ? 1.3122 0.9977 0.9295 0.3053  0.0342  -0.0323 170 LEU A O   
1029 C CB  . LEU A 143 ? 1.2120 0.9304 0.8067 0.3204  0.0710  -0.0375 170 LEU A CB  
1030 C CG  . LEU A 143 ? 1.2649 1.0128 0.9023 0.3361  0.0827  -0.0437 170 LEU A CG  
1031 C CD1 . LEU A 143 ? 1.1973 0.9858 0.8691 0.3273  0.1043  -0.0304 170 LEU A CD1 
1032 C CD2 . LEU A 143 ? 1.3488 1.0960 0.9731 0.3584  0.0915  -0.0605 170 LEU A CD2 
1033 N N   . ILE A 144 ? 1.1703 0.9036 0.8290 0.2838  0.0530  -0.0108 171 ILE A N   
1034 C CA  . ILE A 144 ? 1.1333 0.8631 0.8140 0.2802  0.0392  -0.0109 171 ILE A CA  
1035 C C   . ILE A 144 ? 1.1613 0.9162 0.8801 0.2967  0.0437  -0.0199 171 ILE A C   
1036 O O   . ILE A 144 ? 1.1791 0.9667 0.9380 0.2920  0.0541  -0.0163 171 ILE A O   
1037 C CB  . ILE A 144 ? 1.0908 0.8332 0.7883 0.2609  0.0416  0.0020  171 ILE A CB  
1038 C CG1 . ILE A 144 ? 1.0266 0.7555 0.6931 0.2471  0.0409  0.0102  171 ILE A CG1 
1039 C CG2 . ILE A 144 ? 1.0479 0.7800 0.7558 0.2556  0.0245  0.0008  171 ILE A CG2 
1040 C CD1 . ILE A 144 ? 1.0358 0.7273 0.6636 0.2431  0.0229  0.0045  171 ILE A CD1 
1041 N N   . LEU A 145 ? 1.2262 0.9662 0.9344 0.3162  0.0357  -0.0330 172 LEU A N   
1042 C CA  . LEU A 145 ? 1.1554 0.9241 0.9021 0.3353  0.0399  -0.0441 172 LEU A CA  
1043 C C   . LEU A 145 ? 1.2280 1.0133 1.0112 0.3321  0.0281  -0.0435 172 LEU A C   
1044 O O   . LEU A 145 ? 1.2925 1.1206 1.1232 0.3351  0.0390  -0.0474 172 LEU A O   
1045 C CB  . LEU A 145 ? 1.1906 0.9333 0.9160 0.3591  0.0290  -0.0588 172 LEU A CB  
1046 C CG  . LEU A 145 ? 1.4384 1.1898 1.1548 0.3750  0.0467  -0.0694 172 LEU A CG  
1047 C CD1 . LEU A 145 ? 1.3358 1.0729 1.0518 0.4035  0.0354  -0.0868 172 LEU A CD1 
1048 C CD2 . LEU A 145 ? 1.3343 1.1389 1.0894 0.3728  0.0747  -0.0669 172 LEU A CD2 
1049 N N   . ASN A 146 ? 1.1742 0.9269 0.9353 0.3250  0.0062  -0.0394 173 ASN A N   
1050 C CA  . ASN A 146 ? 1.1092 0.8729 0.8967 0.3250  -0.0090 -0.0408 173 ASN A CA  
1051 C C   . ASN A 146 ? 1.1254 0.9189 0.9428 0.3036  0.0023  -0.0324 173 ASN A C   
1052 O O   . ASN A 146 ? 1.1907 0.9670 0.9858 0.2847  0.0038  -0.0214 173 ASN A O   
1053 C CB  . ASN A 146 ? 1.2314 0.9465 0.9782 0.3235  -0.0340 -0.0376 173 ASN A CB  
1054 C CG  . ASN A 146 ? 1.2569 0.9798 1.0230 0.3288  -0.0532 -0.0404 173 ASN A CG  
1055 O OD1 . ASN A 146 ? 1.2743 1.0380 1.0829 0.3226  -0.0481 -0.0421 173 ASN A OD1 
1056 N ND2 . ASN A 146 ? 1.2586 0.9398 0.9909 0.3399  -0.0759 -0.0410 173 ASN A ND2 
1057 N N   . PRO A 147 ? 1.1079 0.9455 0.9768 0.3055  0.0101  -0.0384 174 PRO A N   
1058 C CA  . PRO A 147 ? 1.1385 0.9996 1.0356 0.2841  0.0222  -0.0314 174 PRO A CA  
1059 C C   . PRO A 147 ? 1.1026 0.9454 0.9879 0.2707  0.0042  -0.0272 174 PRO A C   
1060 O O   . PRO A 147 ? 1.2240 1.0755 1.1218 0.2521  0.0137  -0.0206 174 PRO A O   
1061 C CB  . PRO A 147 ? 1.0804 0.9914 1.0369 0.2901  0.0318  -0.0426 174 PRO A CB  
1062 C CG  . PRO A 147 ? 1.0370 0.9554 0.9956 0.3154  0.0314  -0.0539 174 PRO A CG  
1063 C CD  . PRO A 147 ? 0.8819 0.7507 0.7881 0.3269  0.0085  -0.0532 174 PRO A CD  
1064 N N   . ASP A 148 ? 1.1214 0.9369 0.9807 0.2801  -0.0204 -0.0307 175 ASP A N   
1065 C CA  . ASP A 148 ? 1.1732 0.9705 1.0163 0.2684  -0.0374 -0.0272 175 ASP A CA  
1066 C C   . ASP A 148 ? 1.1778 0.9309 0.9682 0.2566  -0.0409 -0.0162 175 ASP A C   
1067 O O   . ASP A 148 ? 1.0788 0.8137 0.8497 0.2461  -0.0530 -0.0127 175 ASP A O   
1068 C CB  . ASP A 148 ? 1.0130 0.8071 0.8575 0.2855  -0.0630 -0.0364 175 ASP A CB  
1069 C CG  . ASP A 148 ? 1.1810 1.0263 1.0843 0.2952  -0.0623 -0.0498 175 ASP A CG  
1070 O OD1 . ASP A 148 ? 1.2904 1.1698 1.2326 0.2803  -0.0442 -0.0507 175 ASP A OD1 
1071 O OD2 . ASP A 148 ? 1.2925 1.1441 1.2044 0.3176  -0.0798 -0.0597 175 ASP A OD2 
1072 N N   . THR A 149 ? 1.2092 0.9471 0.9767 0.2573  -0.0303 -0.0118 176 THR A N   
1073 C CA  . THR A 149 ? 1.2207 0.9204 0.9418 0.2451  -0.0341 -0.0038 176 THR A CA  
1074 C C   . THR A 149 ? 1.1197 0.8236 0.8416 0.2232  -0.0296 0.0040  176 THR A C   
1075 O O   . THR A 149 ? 1.1560 0.8327 0.8474 0.2126  -0.0399 0.0079  176 THR A O   
1076 C CB  . THR A 149 ? 1.1893 0.8832 0.8941 0.2474  -0.0214 -0.0024 176 THR A CB  
1077 O OG1 . THR A 149 ? 1.2543 0.9443 0.9586 0.2692  -0.0242 -0.0117 176 THR A OG1 
1078 C CG2 . THR A 149 ? 1.1640 0.8214 0.8243 0.2338  -0.0269 0.0032  176 THR A CG2 
1079 N N   . LEU A 150 ? 1.0831 0.8194 0.8391 0.2163  -0.0131 0.0063  177 LEU A N   
1080 C CA  . LEU A 150 ? 0.9849 0.7255 0.7448 0.1981  -0.0078 0.0123  177 LEU A CA  
1081 C C   . LEU A 150 ? 1.1050 0.8413 0.8660 0.1932  -0.0225 0.0079  177 LEU A C   
1082 O O   . LEU A 150 ? 1.1260 0.8434 0.8615 0.1811  -0.0280 0.0116  177 LEU A O   
1083 C CB  . LEU A 150 ? 0.9296 0.7009 0.7264 0.1943  0.0125  0.0154  177 LEU A CB  
1084 C CG  . LEU A 150 ? 0.9638 0.7400 0.7696 0.1785  0.0205  0.0211  177 LEU A CG  
1085 C CD1 . LEU A 150 ? 0.9895 0.7440 0.7593 0.1695  0.0161  0.0271  177 LEU A CD1 
1086 C CD2 . LEU A 150 ? 0.9325 0.7291 0.7651 0.1775  0.0422  0.0274  177 LEU A CD2 
1087 N N   . SER A 151 ? 1.1067 0.8629 0.8974 0.2026  -0.0288 -0.0009 178 SER A N   
1088 C CA  . SER A 151 ? 0.9832 0.7371 0.7728 0.2002  -0.0456 -0.0067 178 SER A CA  
1089 C C   . SER A 151 ? 1.1635 0.8770 0.9024 0.2025  -0.0638 -0.0032 178 SER A C   
1090 O O   . SER A 151 ? 1.1745 0.8731 0.8911 0.1909  -0.0706 -0.0012 178 SER A O   
1091 C CB  . SER A 151 ? 1.0856 0.8697 0.9149 0.2133  -0.0530 -0.0186 178 SER A CB  
1092 O OG  . SER A 151 ? 1.1191 0.9383 0.9949 0.2096  -0.0331 -0.0211 178 SER A OG  
1093 N N   . LEU A 152 ? 1.1456 0.8384 0.8636 0.2168  -0.0704 -0.0026 179 LEU A N   
1094 C CA  . LEU A 152 ? 1.0045 0.6519 0.6721 0.2190  -0.0869 0.0017  179 LEU A CA  
1095 C C   . LEU A 152 ? 1.1299 0.7527 0.7634 0.1976  -0.0794 0.0108  179 LEU A C   
1096 O O   . LEU A 152 ? 1.2031 0.7993 0.8030 0.1886  -0.0888 0.0148  179 LEU A O   
1097 C CB  . LEU A 152 ? 1.1953 0.8228 0.8493 0.2388  -0.0929 -0.0006 179 LEU A CB  
1098 C CG  . LEU A 152 ? 1.1840 0.8353 0.8703 0.2633  -0.1027 -0.0111 179 LEU A CG  
1099 C CD1 . LEU A 152 ? 1.1917 0.8278 0.8693 0.2827  -0.1024 -0.0148 179 LEU A CD1 
1100 C CD2 . LEU A 152 ? 0.9338 0.5731 0.6069 0.2725  -0.1271 -0.0132 179 LEU A CD2 
1101 N N   . LEU A 153 ? 1.1228 0.7561 0.7643 0.1893  -0.0625 0.0140  180 LEU A N   
1102 C CA  . LEU A 153 ? 1.1037 0.7220 0.7201 0.1694  -0.0555 0.0207  180 LEU A CA  
1103 C C   . LEU A 153 ? 1.2014 0.8319 0.8242 0.1543  -0.0524 0.0218  180 LEU A C   
1104 O O   . LEU A 153 ? 1.2113 0.8203 0.8033 0.1401  -0.0546 0.0256  180 LEU A O   
1105 C CB  . LEU A 153 ? 1.1719 0.8067 0.8006 0.1665  -0.0399 0.0227  180 LEU A CB  
1106 C CG  . LEU A 153 ? 1.2851 0.9018 0.8959 0.1770  -0.0415 0.0208  180 LEU A CG  
1107 C CD1 . LEU A 153 ? 1.0667 0.7083 0.6943 0.1775  -0.0262 0.0220  180 LEU A CD1 
1108 C CD2 . LEU A 153 ? 1.1647 0.7392 0.7305 0.1663  -0.0499 0.0228  180 LEU A CD2 
1109 N N   . ILE A 154 ? 1.0342 0.6981 0.6967 0.1562  -0.0459 0.0176  181 ILE A N   
1110 C CA  . ILE A 154 ? 1.0698 0.7440 0.7390 0.1434  -0.0432 0.0160  181 ILE A CA  
1111 C C   . ILE A 154 ? 1.1343 0.7870 0.7742 0.1429  -0.0602 0.0136  181 ILE A C   
1112 O O   . ILE A 154 ? 1.1659 0.8126 0.7890 0.1294  -0.0589 0.0140  181 ILE A O   
1113 C CB  . ILE A 154 ? 1.0738 0.7831 0.7915 0.1458  -0.0340 0.0103  181 ILE A CB  
1114 C CG1 . ILE A 154 ? 1.0916 0.8174 0.8316 0.1470  -0.0163 0.0155  181 ILE A CG1 
1115 C CG2 . ILE A 154 ? 1.0083 0.7250 0.7320 0.1331  -0.0311 0.0063  181 ILE A CG2 
1116 C CD1 . ILE A 154 ? 1.0129 0.7668 0.7972 0.1460  -0.0038 0.0123  181 ILE A CD1 
1117 N N   . ALA A 155 ? 1.1658 0.8064 0.7972 0.1590  -0.0765 0.0112  182 ALA A N   
1118 C CA  . ALA A 155 ? 1.1516 0.7731 0.7548 0.1622  -0.0952 0.0095  182 ALA A CA  
1119 C C   . ALA A 155 ? 1.2046 0.7830 0.7514 0.1505  -0.0982 0.0189  182 ALA A C   
1120 O O   . ALA A 155 ? 1.2442 0.8079 0.7624 0.1450  -0.1068 0.0196  182 ALA A O   
1121 C CB  . ALA A 155 ? 1.1716 0.7918 0.7812 0.1858  -0.1132 0.0048  182 ALA A CB  
1122 N N   . GLU A 156 ? 1.2505 0.8082 0.7796 0.1452  -0.0906 0.0255  183 GLU A N   
1123 C CA  . GLU A 156 ? 1.2801 0.7950 0.7569 0.1316  -0.0923 0.0340  183 GLU A CA  
1124 C C   . GLU A 156 ? 1.1273 0.6509 0.5971 0.1079  -0.0784 0.0356  183 GLU A C   
1125 O O   . GLU A 156 ? 1.4273 0.9186 0.8542 0.0935  -0.0776 0.0422  183 GLU A O   
1126 C CB  . GLU A 156 ? 1.2602 0.7513 0.7228 0.1311  -0.0886 0.0378  183 GLU A CB  
1127 C CG  . GLU A 156 ? 1.2450 0.7252 0.7123 0.1559  -0.1008 0.0348  183 GLU A CG  
1128 C CD  . GLU A 156 ? 1.4768 0.9173 0.9071 0.1699  -0.1216 0.0381  183 GLU A CD  
1129 O OE1 . GLU A 156 ? 1.4084 0.8197 0.7983 0.1576  -0.1257 0.0453  183 GLU A OE1 
1130 O OE2 . GLU A 156 ? 1.2809 0.7194 0.7215 0.1945  -0.1336 0.0337  183 GLU A OE2 
1131 N N   . ASN A 157 ? 1.0699 0.6346 0.5802 0.1039  -0.0667 0.0296  184 ASN A N   
1132 C CA  . ASN A 157 ? 1.1528 0.7308 0.6628 0.0849  -0.0528 0.0287  184 ASN A CA  
1133 C C   . ASN A 157 ? 1.2691 0.8311 0.7549 0.0669  -0.0424 0.0349  184 ASN A C   
1134 O O   . ASN A 157 ? 1.2274 0.7740 0.6820 0.0506  -0.0380 0.0375  184 ASN A O   
1135 C CB  . ASN A 157 ? 1.0128 0.5823 0.4990 0.0814  -0.0603 0.0258  184 ASN A CB  
1136 C CG  . ASN A 157 ? 1.1973 0.7871 0.6907 0.0650  -0.0445 0.0213  184 ASN A CG  
1137 O OD1 . ASN A 157 ? 1.3042 0.9206 0.8306 0.0601  -0.0295 0.0192  184 ASN A OD1 
1138 N ND2 . ASN A 157 ? 1.2949 0.8716 0.7553 0.0579  -0.0481 0.0196  184 ASN A ND2 
1139 N N   . LYS A 158 ? 1.2217 0.7890 0.7220 0.0692  -0.0381 0.0364  185 LYS A N   
1140 C CA  . LYS A 158 ? 1.2093 0.7708 0.6970 0.0519  -0.0285 0.0393  185 LYS A CA  
1141 C C   . LYS A 158 ? 1.1896 0.7941 0.7180 0.0493  -0.0148 0.0358  185 LYS A C   
1142 O O   . LYS A 158 ? 1.2566 0.8870 0.8198 0.0631  -0.0129 0.0333  185 LYS A O   
1143 C CB  . LYS A 158 ? 1.3291 0.8599 0.7964 0.0562  -0.0362 0.0421  185 LYS A CB  
1144 C CG  . LYS A 158 ? 1.1676 0.6501 0.5926 0.0622  -0.0509 0.0467  185 LYS A CG  
1145 C CD  . LYS A 158 ? 1.3284 0.7817 0.7114 0.0407  -0.0476 0.0525  185 LYS A CD  
1146 C CE  . LYS A 158 ? 1.3370 0.7329 0.6704 0.0467  -0.0623 0.0599  185 LYS A CE  
1147 N NZ  . LYS A 158 ? 1.7847 1.1498 1.0725 0.0248  -0.0570 0.0674  185 LYS A NZ  
1148 N N   . THR A 159 ? 1.0859 0.6976 0.6099 0.0315  -0.0051 0.0359  186 THR A N   
1149 C CA  . THR A 159 ? 1.0767 0.7294 0.6376 0.0312  0.0059  0.0330  186 THR A CA  
1150 C C   . THR A 159 ? 1.1693 0.8286 0.7412 0.0398  0.0033  0.0338  186 THR A C   
1151 O O   . THR A 159 ? 1.1261 0.8137 0.7290 0.0516  0.0077  0.0338  186 THR A O   
1152 C CB  . THR A 159 ? 1.0966 0.7633 0.6546 0.0101  0.0171  0.0306  186 THR A CB  
1153 O OG1 . THR A 159 ? 1.1204 0.7817 0.6654 0.0030  0.0212  0.0291  186 THR A OG1 
1154 C CG2 . THR A 159 ? 1.0729 0.7838 0.6707 0.0138  0.0264  0.0274  186 THR A CG2 
1155 N N   . VAL A 160 ? 1.1348 0.7656 0.6790 0.0342  -0.0036 0.0345  187 VAL A N   
1156 C CA  . VAL A 160 ? 1.1464 0.7778 0.6940 0.0435  -0.0077 0.0333  187 VAL A CA  
1157 C C   . VAL A 160 ? 1.2211 0.8087 0.7382 0.0507  -0.0191 0.0340  187 VAL A C   
1158 O O   . VAL A 160 ? 1.1704 0.7231 0.6545 0.0367  -0.0230 0.0342  187 VAL A O   
1159 C CB  . VAL A 160 ? 1.2402 0.8856 0.7879 0.0278  -0.0043 0.0296  187 VAL A CB  
1160 C CG1 . VAL A 160 ? 0.9608 0.6048 0.5070 0.0384  -0.0099 0.0269  187 VAL A CG1 
1161 C CG2 . VAL A 160 ? 1.1296 0.8204 0.7096 0.0243  0.0057  0.0285  187 VAL A CG2 
1162 N N   . VAL A 161 ? 1.1683 0.7570 0.6971 0.0725  -0.0236 0.0340  188 VAL A N   
1163 C CA  . VAL A 161 ? 1.2607 0.8125 0.7662 0.0848  -0.0349 0.0333  188 VAL A CA  
1164 C C   . VAL A 161 ? 1.2194 0.7832 0.7398 0.1028  -0.0346 0.0297  188 VAL A C   
1165 O O   . VAL A 161 ? 1.1293 0.7295 0.6808 0.1106  -0.0264 0.0301  188 VAL A O   
1166 C CB  . VAL A 161 ? 1.1253 0.6669 0.6293 0.0954  -0.0424 0.0353  188 VAL A CB  
1167 C CG1 . VAL A 161 ? 1.0913 0.6715 0.6367 0.1103  -0.0379 0.0334  188 VAL A CG1 
1168 C CG2 . VAL A 161 ? 1.1017 0.6007 0.5767 0.1083  -0.0561 0.0351  188 VAL A CG2 
1169 N N   . ALA A 162 ? 1.2148 0.7448 0.7100 0.1094  -0.0426 0.0261  189 ALA A N   
1170 C CA  . ALA A 162 ? 1.2443 0.7823 0.7475 0.1263  -0.0414 0.0209  189 ALA A CA  
1171 C C   . ALA A 162 ? 1.2711 0.7798 0.7622 0.1464  -0.0512 0.0175  189 ALA A C   
1172 O O   . ALA A 162 ? 1.2330 0.6999 0.6947 0.1438  -0.0614 0.0187  189 ALA A O   
1173 C CB  . ALA A 162 ? 1.1236 0.6536 0.6089 0.1151  -0.0407 0.0157  189 ALA A CB  
1174 N N   . PRO A 163 ? 1.1635 0.6929 0.6763 0.1673  -0.0477 0.0135  190 PRO A N   
1175 C CA  . PRO A 163 ? 1.1452 0.6510 0.6498 0.1891  -0.0566 0.0078  190 PRO A CA  
1176 C C   . PRO A 163 ? 1.3372 0.8137 0.8141 0.1930  -0.0585 -0.0003 190 PRO A C   
1177 O O   . PRO A 163 ? 1.2475 0.7430 0.7277 0.1896  -0.0498 -0.0037 190 PRO A O   
1178 C CB  . PRO A 163 ? 1.2260 0.7755 0.7721 0.2068  -0.0482 0.0058  190 PRO A CB  
1179 C CG  . PRO A 163 ? 1.0731 0.6575 0.6362 0.1965  -0.0333 0.0094  190 PRO A CG  
1180 C CD  . PRO A 163 ? 1.1834 0.7600 0.7315 0.1724  -0.0344 0.0150  190 PRO A CD  
1181 N N   . MET A 164 ? 1.2827 0.7102 0.7295 0.2004  -0.0708 -0.0035 191 MET A N   
1182 C CA  . MET A 164 ? 1.2546 0.6477 0.6732 0.2047  -0.0733 -0.0133 191 MET A CA  
1183 C C   . MET A 164 ? 1.4506 0.8676 0.8888 0.2308  -0.0672 -0.0229 191 MET A C   
1184 O O   . MET A 164 ? 1.4763 0.8975 0.9301 0.2540  -0.0712 -0.0254 191 MET A O   
1185 C CB  . MET A 164 ? 1.2549 0.5830 0.6346 0.2073  -0.0875 -0.0134 191 MET A CB  
1186 C CG  . MET A 164 ? 1.3679 0.6530 0.7147 0.2059  -0.0896 -0.0247 191 MET A CG  
1187 S SD  . MET A 164 ? 1.5159 0.7150 0.8150 0.2144  -0.1056 -0.0252 191 MET A SD  
1188 C CE  . MET A 164 ? 1.4659 0.6770 0.7877 0.2591  -0.1123 -0.0307 191 MET A CE  
1189 N N   . LEU A 165 ? 1.4107 0.8454 0.8478 0.2272  -0.0577 -0.0290 192 LEU A N   
1190 C CA  . LEU A 165 ? 1.2756 0.7331 0.7256 0.2494  -0.0488 -0.0383 192 LEU A CA  
1191 C C   . LEU A 165 ? 1.4440 0.8563 0.8602 0.2608  -0.0550 -0.0529 192 LEU A C   
1192 O O   . LEU A 165 ? 1.4562 0.8327 0.8396 0.2440  -0.0609 -0.0570 192 LEU A O   
1193 C CB  . LEU A 165 ? 1.2686 0.7703 0.7320 0.2413  -0.0346 -0.0358 192 LEU A CB  
1194 C CG  . LEU A 165 ? 1.3631 0.9054 0.8596 0.2308  -0.0276 -0.0219 192 LEU A CG  
1195 C CD1 . LEU A 165 ? 1.1974 0.7786 0.7041 0.2270  -0.0139 -0.0180 192 LEU A CD1 
1196 C CD2 . LEU A 165 ? 1.1417 0.7024 0.6709 0.2467  -0.0257 -0.0195 192 LEU A CD2 
1197 N N   . ASP A 166 ? 1.4332 0.8476 0.8592 0.2891  -0.0532 -0.0619 193 ASP A N   
1198 C CA  . ASP A 166 ? 1.3842 0.7562 0.7805 0.3047  -0.0580 -0.0779 193 ASP A CA  
1199 C C   . ASP A 166 ? 1.5258 0.9151 0.9110 0.3042  -0.0462 -0.0889 193 ASP A C   
1200 O O   . ASP A 166 ? 1.4002 0.8410 0.8087 0.3053  -0.0317 -0.0851 193 ASP A O   
1201 C CB  . ASP A 166 ? 1.4787 0.8507 0.8928 0.3383  -0.0605 -0.0850 193 ASP A CB  
1202 C CG  . ASP A 166 ? 1.7398 1.0929 1.1602 0.3423  -0.0755 -0.0751 193 ASP A CG  
1203 O OD1 . ASP A 166 ? 1.8734 1.1713 1.2587 0.3305  -0.0889 -0.0706 193 ASP A OD1 
1204 O OD2 . ASP A 166 ? 1.7673 1.1607 1.2266 0.3566  -0.0739 -0.0719 193 ASP A OD2 
1205 N N   . SER A 167 ? 1.5990 0.9419 0.9455 0.3019  -0.0526 -0.1027 194 SER A N   
1206 C CA  . SER A 167 ? 1.5188 0.8701 0.8469 0.3043  -0.0444 -0.1173 194 SER A CA  
1207 C C   . SER A 167 ? 1.5238 0.8272 0.8251 0.3262  -0.0490 -0.1375 194 SER A C   
1208 O O   . SER A 167 ? 1.6984 0.9593 0.9943 0.3379  -0.0597 -0.1383 194 SER A O   
1209 C CB  . SER A 167 ? 1.5059 0.8529 0.8118 0.2731  -0.0485 -0.1169 194 SER A CB  
1210 O OG  . SER A 167 ? 1.5507 0.8356 0.8226 0.2595  -0.0620 -0.1256 194 SER A OG  
1211 N N   . ARG A 168 ? 1.6369 0.9455 0.9190 0.3333  -0.0412 -0.1542 195 ARG A N   
1212 C CA  . ARG A 168 ? 1.6486 0.9112 0.9035 0.3548  -0.0441 -0.1765 195 ARG A CA  
1213 C C   . ARG A 168 ? 1.6326 0.8218 0.8480 0.3378  -0.0607 -0.1843 195 ARG A C   
1214 O O   . ARG A 168 ? 1.7307 0.8672 0.9232 0.3560  -0.0663 -0.2004 195 ARG A O   
1215 C CB  . ARG A 168 ? 1.6099 0.8977 0.8500 0.3649  -0.0306 -0.1935 195 ARG A CB  
1216 C CG  . ARG A 168 ? 1.5064 0.7982 0.7198 0.3366  -0.0338 -0.1965 195 ARG A CG  
1217 C CD  . ARG A 168 ? 1.5933 0.9075 0.7854 0.3484  -0.0220 -0.2137 195 ARG A CD  
1218 N NE  . ARG A 168 ? 1.6692 0.9937 0.8379 0.3224  -0.0278 -0.2158 195 ARG A NE  
1219 C CZ  . ARG A 168 ? 1.7244 1.0053 0.8576 0.3059  -0.0415 -0.2335 195 ARG A CZ  
1220 N NH1 . ARG A 168 ? 1.9465 1.1636 1.0591 0.3123  -0.0498 -0.2501 195 ARG A NH1 
1221 N NH2 . ARG A 168 ? 1.7174 1.0186 0.8362 0.2825  -0.0477 -0.2351 195 ARG A NH2 
1222 N N   . ALA A 169 ? 1.6976 0.8818 0.9053 0.3032  -0.0677 -0.1739 196 ALA A N   
1223 C CA  . ALA A 169 ? 1.6657 0.7824 0.8374 0.2810  -0.0809 -0.1807 196 ALA A CA  
1224 C C   . ALA A 169 ? 1.7727 0.8773 0.9527 0.2570  -0.0883 -0.1592 196 ALA A C   
1225 O O   . ALA A 169 ? 1.7020 0.8437 0.9138 0.2631  -0.0851 -0.1410 196 ALA A O   
1226 C CB  . ALA A 169 ? 1.5810 0.7020 0.7292 0.2577  -0.0815 -0.1960 196 ALA A CB  
1227 N N   . ALA A 170 ? 1.7361 0.7890 0.8870 0.2283  -0.0971 -0.1620 197 ALA A N   
1228 C CA  . ALA A 170 ? 1.7341 0.7721 0.8874 0.2031  -0.1020 -0.1424 197 ALA A CA  
1229 C C   . ALA A 170 ? 1.8026 0.9108 0.9881 0.1827  -0.0954 -0.1279 197 ALA A C   
1230 O O   . ALA A 170 ? 1.8184 0.9275 1.0132 0.1672  -0.0967 -0.1102 197 ALA A O   
1231 C CB  . ALA A 170 ? 1.6124 0.5810 0.7274 0.1734  -0.1096 -0.1501 197 ALA A CB  
1232 N N   . TYR A 171 ? 1.6041 0.7685 0.8041 0.1836  -0.0885 -0.1349 198 TYR A N   
1233 C CA  . TYR A 171 ? 1.5989 0.8273 0.8286 0.1673  -0.0829 -0.1214 198 TYR A CA  
1234 C C   . TYR A 171 ? 1.5916 0.8516 0.8541 0.1811  -0.0775 -0.1015 198 TYR A C   
1235 O O   . TYR A 171 ? 1.7233 0.9890 0.9972 0.2104  -0.0741 -0.1014 198 TYR A O   
1236 C CB  . TYR A 171 ? 1.5535 0.8323 0.7885 0.1733  -0.0769 -0.1311 198 TYR A CB  
1237 C CG  . TYR A 171 ? 1.5463 0.8884 0.8097 0.1596  -0.0720 -0.1173 198 TYR A CG  
1238 C CD1 . TYR A 171 ? 1.4641 0.8522 0.7596 0.1757  -0.0620 -0.1014 198 TYR A CD1 
1239 C CD2 . TYR A 171 ? 1.3793 0.7355 0.6391 0.1310  -0.0775 -0.1214 198 TYR A CD2 
1240 C CE1 . TYR A 171 ? 1.2889 0.7291 0.6088 0.1651  -0.0575 -0.0889 198 TYR A CE1 
1241 C CE2 . TYR A 171 ? 1.4130 0.8267 0.6997 0.1220  -0.0740 -0.1094 198 TYR A CE2 
1242 C CZ  . TYR A 171 ? 1.3141 0.7669 0.6291 0.1399  -0.0639 -0.0926 198 TYR A CZ  
1243 O OH  . TYR A 171 ? 1.2756 0.7802 0.6157 0.1327  -0.0603 -0.0807 198 TYR A OH  
1244 N N   . SER A 172 ? 1.4753 0.7579 0.7548 0.1593  -0.0768 -0.0865 199 SER A N   
1245 C CA  . SER A 172 ? 1.3643 0.6859 0.6774 0.1680  -0.0712 -0.0693 199 SER A CA  
1246 C C   . SER A 172 ? 1.3532 0.7195 0.6861 0.1440  -0.0668 -0.0601 199 SER A C   
1247 O O   . SER A 172 ? 1.4843 0.8531 0.8066 0.1222  -0.0692 -0.0671 199 SER A O   
1248 C CB  . SER A 172 ? 1.6961 0.9777 1.0029 0.1726  -0.0779 -0.0599 199 SER A CB  
1249 O OG  . SER A 172 ? 1.5107 0.8314 0.8507 0.1837  -0.0736 -0.0468 199 SER A OG  
1250 N N   . ASN A 173 ? 1.3563 0.7594 0.7199 0.1484  -0.0610 -0.0457 200 ASN A N   
1251 C CA  . ASN A 173 ? 1.3351 0.7829 0.7210 0.1305  -0.0558 -0.0370 200 ASN A CA  
1252 C C   . ASN A 173 ? 1.3616 0.7927 0.7437 0.1053  -0.0588 -0.0296 200 ASN A C   
1253 O O   . ASN A 173 ? 1.2627 0.7241 0.6685 0.0998  -0.0538 -0.0186 200 ASN A O   
1254 C CB  . ASN A 173 ? 1.3119 0.8069 0.7325 0.1473  -0.0461 -0.0267 200 ASN A CB  
1255 C CG  . ASN A 173 ? 1.2941 0.7785 0.7270 0.1599  -0.0468 -0.0193 200 ASN A CG  
1256 O OD1 . ASN A 173 ? 1.3377 0.7834 0.7535 0.1713  -0.0537 -0.0241 200 ASN A OD1 
1257 N ND2 . ASN A 173 ? 1.3284 0.8470 0.7911 0.1589  -0.0406 -0.0084 200 ASN A ND2 
1258 N N   . PHE A 174 ? 1.3085 0.6901 0.6596 0.0887  -0.0657 -0.0358 201 PHE A N   
1259 C CA  . PHE A 174 ? 1.4502 0.8147 0.7935 0.0611  -0.0658 -0.0290 201 PHE A CA  
1260 C C   . PHE A 174 ? 1.5021 0.8202 0.8131 0.0385  -0.0709 -0.0401 201 PHE A C   
1261 O O   . PHE A 174 ? 1.5609 0.8448 0.8499 0.0486  -0.0765 -0.0518 201 PHE A O   
1262 C CB  . PHE A 174 ? 1.5441 0.8808 0.8809 0.0689  -0.0677 -0.0166 201 PHE A CB  
1263 C CG  . PHE A 174 ? 1.3773 0.6476 0.6789 0.0804  -0.0767 -0.0194 201 PHE A CG  
1264 C CD1 . PHE A 174 ? 1.5637 0.8280 0.8675 0.1126  -0.0807 -0.0245 201 PHE A CD1 
1265 C CD2 . PHE A 174 ? 1.5336 0.7462 0.7996 0.0595  -0.0803 -0.0167 201 PHE A CD2 
1266 C CE1 . PHE A 174 ? 1.6278 0.8308 0.9006 0.1266  -0.0898 -0.0278 201 PHE A CE1 
1267 C CE2 . PHE A 174 ? 1.6505 0.7958 0.8813 0.0723  -0.0893 -0.0180 201 PHE A CE2 
1268 C CZ  . PHE A 174 ? 1.6583 0.7993 0.8932 0.1074  -0.0950 -0.0240 201 PHE A CZ  
1269 N N   . TRP A 175 ? 1.5350 0.8526 0.8442 0.0068  -0.0678 -0.0373 202 TRP A N   
1270 C CA  . TRP A 175 ? 1.5502 0.8182 0.8291 -0.0211 -0.0705 -0.0455 202 TRP A CA  
1271 C C   . TRP A 175 ? 1.6569 0.8782 0.9130 -0.0351 -0.0680 -0.0318 202 TRP A C   
1272 O O   . TRP A 175 ? 1.6985 0.9447 0.9696 -0.0343 -0.0626 -0.0185 202 TRP A O   
1273 C CB  . TRP A 175 ? 1.6128 0.9208 0.9087 -0.0514 -0.0676 -0.0555 202 TRP A CB  
1274 C CG  . TRP A 175 ? 1.6129 0.9702 0.9281 -0.0400 -0.0714 -0.0681 202 TRP A CG  
1275 C CD1 . TRP A 175 ? 1.5239 0.8912 0.8400 -0.0077 -0.0744 -0.0711 202 TRP A CD1 
1276 C CD2 . TRP A 175 ? 1.5620 0.9671 0.8968 -0.0605 -0.0725 -0.0793 202 TRP A CD2 
1277 N NE1 . TRP A 175 ? 1.6240 1.0383 0.9538 -0.0068 -0.0772 -0.0819 202 TRP A NE1 
1278 C CE2 . TRP A 175 ? 1.4666 0.9057 0.8087 -0.0379 -0.0777 -0.0874 202 TRP A CE2 
1279 C CE3 . TRP A 175 ? 1.6357 1.0608 0.9834 -0.0957 -0.0695 -0.0836 202 TRP A CE3 
1280 C CZ2 . TRP A 175 ? 1.5381 1.0282 0.8970 -0.0473 -0.0826 -0.0990 202 TRP A CZ2 
1281 C CZ3 . TRP A 175 ? 1.6103 1.0906 0.9807 -0.1054 -0.0742 -0.0969 202 TRP A CZ3 
1282 C CH2 . TRP A 175 ? 1.4946 1.0060 0.8691 -0.0803 -0.0820 -0.1041 202 TRP A CH2 
1283 N N   . CYS A 176 ? 1.8537 1.0040 1.0703 -0.0481 -0.0717 -0.0350 203 CYS A N   
1284 C CA  . CYS A 176 ? 1.8345 0.9345 1.0220 -0.0652 -0.0684 -0.0208 203 CYS A CA  
1285 C C   . CYS A 176 ? 1.9470 1.0470 1.1314 -0.1105 -0.0586 -0.0230 203 CYS A C   
1286 O O   . CYS A 176 ? 1.9989 1.0793 1.1679 -0.1283 -0.0510 -0.0092 203 CYS A O   
1287 C CB  . CYS A 176 ? 1.9807 0.9940 1.1222 -0.0512 -0.0774 -0.0192 203 CYS A CB  
1288 S SG  . CYS A 176 ? 2.2114 1.2055 1.3428 -0.0124 -0.0850 -0.0013 203 CYS A SG  
1289 N N   . GLY A 177 ? 1.9474 1.0715 1.1463 -0.1297 -0.0584 -0.0406 204 GLY A N   
1290 C CA  . GLY A 177 ? 1.8824 1.0173 1.0870 -0.1737 -0.0490 -0.0456 204 GLY A CA  
1291 C C   . GLY A 177 ? 1.7924 1.0078 1.0414 -0.1815 -0.0494 -0.0612 204 GLY A C   
1292 O O   . GLY A 177 ? 1.8145 1.0623 1.0793 -0.1554 -0.0579 -0.0698 204 GLY A O   
1293 N N   . MET A 178 ? 1.7655 1.0137 1.0339 -0.2177 -0.0397 -0.0646 205 MET A N   
1294 C CA  . MET A 178 ? 1.7766 1.1029 1.0882 -0.2278 -0.0412 -0.0801 205 MET A CA  
1295 C C   . MET A 178 ? 1.8113 1.1390 1.1281 -0.2763 -0.0333 -0.0912 205 MET A C   
1296 O O   . MET A 178 ? 1.8456 1.1510 1.1517 -0.3011 -0.0194 -0.0802 205 MET A O   
1297 C CB  . MET A 178 ? 1.6061 1.0074 0.9584 -0.2099 -0.0364 -0.0703 205 MET A CB  
1298 C CG  . MET A 178 ? 1.7744 1.2573 1.1711 -0.2146 -0.0399 -0.0846 205 MET A CG  
1299 S SD  . MET A 178 ? 1.6756 1.2372 1.1172 -0.1898 -0.0344 -0.0725 205 MET A SD  
1300 C CE  . MET A 178 ? 1.5245 1.0647 0.9508 -0.1418 -0.0424 -0.0619 205 MET A CE  
1301 N N   . THR A 179 ? 1.8848 1.2397 1.2174 -0.2905 -0.0418 -0.1135 206 THR A N   
1302 C CA  . THR A 179 ? 1.9366 1.2996 1.2804 -0.3387 -0.0351 -0.1278 206 THR A CA  
1303 C C   . THR A 179 ? 2.0311 1.4787 1.4244 -0.3532 -0.0244 -0.1263 206 THR A C   
1304 O O   . THR A 179 ? 1.9734 1.4734 1.3922 -0.3243 -0.0243 -0.1161 206 THR A O   
1305 C CB  . THR A 179 ? 1.9277 1.3002 1.2760 -0.3488 -0.0498 -0.1550 206 THR A CB  
1306 O OG1 . THR A 179 ? 1.9359 1.4030 1.3310 -0.3366 -0.0583 -0.1655 206 THR A OG1 
1307 C CG2 . THR A 179 ? 2.0034 1.3134 1.3113 -0.3188 -0.0626 -0.1581 206 THR A CG2 
1308 N N   . SER A 180 ? 2.3430 1.8038 1.7514 -0.3990 -0.0146 -0.1377 207 SER A N   
1309 C CA  . SER A 180 ? 2.2819 1.8279 1.7418 -0.4156 -0.0039 -0.1407 207 SER A CA  
1310 C C   . SER A 180 ? 2.1752 1.8113 1.6832 -0.3969 -0.0194 -0.1567 207 SER A C   
1311 O O   . SER A 180 ? 2.1305 1.8441 1.6858 -0.4032 -0.0131 -0.1600 207 SER A O   
1312 C CB  . SER A 180 ? 2.2752 1.8138 1.7409 -0.4718 0.0114  -0.1512 207 SER A CB  
1313 O OG  . SER A 180 ? 2.4142 1.9214 1.8676 -0.4951 0.0006  -0.1725 207 SER A OG  
1314 N N   . GLN A 181 ? 1.9717 1.5990 1.4671 -0.3728 -0.0392 -0.1666 208 GLN A N   
1315 C CA  . GLN A 181 ? 1.8955 1.6011 1.4270 -0.3511 -0.0557 -0.1795 208 GLN A CA  
1316 C C   . GLN A 181 ? 1.8058 1.5115 1.3254 -0.2993 -0.0649 -0.1656 208 GLN A C   
1317 O O   . GLN A 181 ? 1.7000 1.4649 1.2431 -0.2766 -0.0780 -0.1724 208 GLN A O   
1318 C CB  . GLN A 181 ? 1.7938 1.5012 1.3233 -0.3716 -0.0718 -0.2076 208 GLN A CB  
1319 C CG  . GLN A 181 ? 1.9534 1.6737 1.5043 -0.4260 -0.0633 -0.2250 208 GLN A CG  
1320 C CD  . GLN A 181 ? 2.0468 1.7265 1.5756 -0.4523 -0.0752 -0.2500 208 GLN A CD  
1321 O OE1 . GLN A 181 ? 2.2042 1.8424 1.6981 -0.4283 -0.0896 -0.2546 208 GLN A OE1 
1322 N NE2 . GLN A 181 ? 2.0383 1.7296 1.5878 -0.5028 -0.0682 -0.2677 208 GLN A NE2 
1323 N N   . GLY A 182 ? 1.8367 1.4789 1.3207 -0.2803 -0.0583 -0.1466 209 GLY A N   
1324 C CA  . GLY A 182 ? 1.6127 1.2572 1.0899 -0.2343 -0.0635 -0.1328 209 GLY A CA  
1325 C C   . GLY A 182 ? 1.7435 1.3414 1.1844 -0.2121 -0.0758 -0.1385 209 GLY A C   
1326 O O   . GLY A 182 ? 1.7341 1.3537 1.1774 -0.1761 -0.0820 -0.1330 209 GLY A O   
1327 N N   . TYR A 183 ? 1.8931 1.4263 1.2999 -0.2322 -0.0783 -0.1493 210 TYR A N   
1328 C CA  . TYR A 183 ? 1.8748 1.3607 1.2460 -0.2116 -0.0891 -0.1577 210 TYR A CA  
1329 C C   . TYR A 183 ? 1.7966 1.2064 1.1316 -0.1953 -0.0827 -0.1414 210 TYR A C   
1330 O O   . TYR A 183 ? 1.7299 1.1093 1.0581 -0.2096 -0.0715 -0.1270 210 TYR A O   
1331 C CB  . TYR A 183 ? 1.9833 1.4444 1.3394 -0.2419 -0.0980 -0.1840 210 TYR A CB  
1332 C CG  . TYR A 183 ? 1.9701 1.5080 1.3638 -0.2618 -0.1065 -0.2030 210 TYR A CG  
1333 C CD1 . TYR A 183 ? 2.0238 1.6392 1.4477 -0.2356 -0.1138 -0.2008 210 TYR A CD1 
1334 C CD2 . TYR A 183 ? 1.9675 1.5006 1.3671 -0.3067 -0.1075 -0.2231 210 TYR A CD2 
1335 C CE1 . TYR A 183 ? 2.0121 1.6999 1.4706 -0.2504 -0.1242 -0.2181 210 TYR A CE1 
1336 C CE2 . TYR A 183 ? 1.9978 1.6072 1.4360 -0.3244 -0.1171 -0.2425 210 TYR A CE2 
1337 C CZ  . TYR A 183 ? 2.0408 1.7285 1.5083 -0.2945 -0.1265 -0.2398 210 TYR A CZ  
1338 O OH  . TYR A 183 ? 2.0910 1.8568 1.5971 -0.3089 -0.1385 -0.2590 210 TYR A OH  
1339 N N   . TYR A 184 ? 1.8515 1.2328 1.1626 -0.1637 -0.0902 -0.1441 211 TYR A N   
1340 C CA  . TYR A 184 ? 1.7528 1.0641 1.0312 -0.1445 -0.0871 -0.1317 211 TYR A CA  
1341 C C   . TYR A 184 ? 1.9097 1.1421 1.1540 -0.1743 -0.0850 -0.1362 211 TYR A C   
1342 O O   . TYR A 184 ? 2.0016 1.2230 1.2404 -0.2048 -0.0886 -0.1552 211 TYR A O   
1343 C CB  . TYR A 184 ? 1.7047 1.0037 0.9663 -0.1071 -0.0948 -0.1385 211 TYR A CB  
1344 C CG  . TYR A 184 ? 1.8693 1.0955 1.0982 -0.0864 -0.0938 -0.1302 211 TYR A CG  
1345 C CD1 . TYR A 184 ? 1.8188 1.0455 1.0549 -0.0646 -0.0879 -0.1086 211 TYR A CD1 
1346 C CD2 . TYR A 184 ? 1.8870 1.0439 1.0786 -0.0882 -0.0997 -0.1453 211 TYR A CD2 
1347 C CE1 . TYR A 184 ? 1.9515 1.1160 1.1602 -0.0436 -0.0894 -0.1018 211 TYR A CE1 
1348 C CE2 . TYR A 184 ? 2.0113 1.1018 1.1741 -0.0661 -0.1001 -0.1380 211 TYR A CE2 
1349 C CZ  . TYR A 184 ? 1.9863 1.0831 1.1586 -0.0433 -0.0956 -0.1160 211 TYR A CZ  
1350 O OH  . TYR A 184 ? 1.9377 0.9728 1.0836 -0.0191 -0.0983 -0.1095 211 TYR A OH  
1351 N N   . LYS A 185 ? 1.9382 1.1140 1.1585 -0.1658 -0.0795 -0.1183 212 LYS A N   
1352 C CA  . LYS A 185 ? 2.0090 1.1017 1.1915 -0.1920 -0.0762 -0.1173 212 LYS A CA  
1353 C C   . LYS A 185 ? 2.1048 1.1284 1.2519 -0.1605 -0.0791 -0.1040 212 LYS A C   
1354 O O   . LYS A 185 ? 2.0691 1.1073 1.2238 -0.1380 -0.0762 -0.0848 212 LYS A O   
1355 C CB  . LYS A 185 ? 2.0498 1.1532 1.2426 -0.2283 -0.0630 -0.1051 212 LYS A CB  
1356 C CG  . LYS A 185 ? 2.0933 1.1090 1.2441 -0.2594 -0.0566 -0.1008 212 LYS A CG  
1357 C CD  . LYS A 185 ? 2.0727 1.1074 1.2345 -0.2931 -0.0405 -0.0872 212 LYS A CD  
1358 C CE  . LYS A 185 ? 2.2868 1.2321 1.4033 -0.3269 -0.0314 -0.0803 212 LYS A CE  
1359 N NZ  . LYS A 185 ? 2.1968 1.1630 1.3219 -0.3592 -0.0129 -0.0663 212 LYS A NZ  
1360 N N   . ARG A 186 ? 2.0980 1.0478 1.2079 -0.1580 -0.0856 -0.1157 213 ARG A N   
1361 C CA  . ARG A 186 ? 2.1194 0.9955 1.1931 -0.1299 -0.0893 -0.1038 213 ARG A CA  
1362 C C   . ARG A 186 ? 2.1525 0.9751 1.2002 -0.1517 -0.0816 -0.0828 213 ARG A C   
1363 O O   . ARG A 186 ? 2.2278 1.0373 1.2701 -0.1950 -0.0732 -0.0840 213 ARG A O   
1364 C CB  . ARG A 186 ? 2.0727 0.8794 1.1121 -0.1217 -0.0978 -0.1232 213 ARG A CB  
1365 C CG  . ARG A 186 ? 2.4138 1.2656 1.4701 -0.0979 -0.1048 -0.1448 213 ARG A CG  
1366 C CD  . ARG A 186 ? 2.4479 1.2276 1.4674 -0.0947 -0.1121 -0.1674 213 ARG A CD  
1367 N NE  . ARG A 186 ? 2.3707 1.1928 1.4014 -0.0721 -0.1178 -0.1890 213 ARG A NE  
1368 C CZ  . ARG A 186 ? 2.6812 1.4563 1.6843 -0.0649 -0.1242 -0.2133 213 ARG A CZ  
1369 N NH1 . ARG A 186 ? 2.6549 1.3355 1.6188 -0.0782 -0.1263 -0.2197 213 ARG A NH1 
1370 N NH2 . ARG A 186 ? 2.7064 1.5274 1.7185 -0.0436 -0.1280 -0.2315 213 ARG A NH2 
1371 N N   . THR A 187 ? 2.1271 0.9222 1.1590 -0.1215 -0.0843 -0.0635 214 THR A N   
1372 C CA  . THR A 187 ? 2.1644 0.8995 1.1614 -0.1336 -0.0796 -0.0416 214 THR A CA  
1373 C C   . THR A 187 ? 2.2809 0.9398 1.2390 -0.0963 -0.0911 -0.0341 214 THR A C   
1374 O O   . THR A 187 ? 2.2761 0.9509 1.2467 -0.0573 -0.1005 -0.0431 214 THR A O   
1375 C CB  . THR A 187 ? 2.1405 0.9347 1.1619 -0.1336 -0.0722 -0.0225 214 THR A CB  
1376 O OG1 . THR A 187 ? 2.0930 0.9082 1.1253 -0.0877 -0.0811 -0.0144 214 THR A OG1 
1377 C CG2 . THR A 187 ? 2.0232 0.9105 1.0947 -0.1556 -0.0636 -0.0321 214 THR A CG2 
1378 N N   . PRO A 188 ? 2.3902 0.9654 1.3001 -0.1064 -0.0901 -0.0175 215 PRO A N   
1379 C CA  . PRO A 188 ? 2.4597 0.9838 1.3425 -0.0654 -0.1023 -0.0078 215 PRO A CA  
1380 C C   . PRO A 188 ? 2.2217 0.7863 1.1236 -0.0228 -0.1109 0.0024  215 PRO A C   
1381 O O   . PRO A 188 ? 2.3540 0.9069 1.2525 0.0171  -0.1225 0.0042  215 PRO A O   
1382 C CB  . PRO A 188 ? 2.5425 1.0153 1.3882 -0.0879 -0.0960 0.0120  215 PRO A CB  
1383 C CG  . PRO A 188 ? 2.5220 0.9887 1.3664 -0.1429 -0.0811 0.0040  215 PRO A CG  
1384 C CD  . PRO A 188 ? 2.4113 0.9458 1.2947 -0.1557 -0.0770 -0.0085 215 PRO A CD  
1385 N N   . ALA A 189 ? 2.1920 0.8340 1.1306 -0.0297 -0.1042 0.0077  216 ALA A N   
1386 C CA  . ALA A 189 ? 2.2204 0.9100 1.1825 0.0057  -0.1108 0.0180  216 ALA A CA  
1387 C C   . ALA A 189 ? 2.2189 0.9806 1.2297 0.0351  -0.1140 0.0022  216 ALA A C   
1388 O O   . ALA A 189 ? 2.1935 0.9893 1.2250 0.0679  -0.1204 0.0078  216 ALA A O   
1389 C CB  . ALA A 189 ? 2.1769 0.9147 1.1536 -0.0165 -0.1005 0.0329  216 ALA A CB  
1390 N N   . TYR A 190 ? 2.2385 1.0242 1.2669 0.0237  -0.1098 -0.0176 217 TYR A N   
1391 C CA  . TYR A 190 ? 2.1167 0.9742 1.1885 0.0485  -0.1102 -0.0305 217 TYR A CA  
1392 C C   . TYR A 190 ? 2.0444 0.8787 1.1112 0.0941  -0.1207 -0.0356 217 TYR A C   
1393 O O   . TYR A 190 ? 1.8469 0.7342 0.9464 0.1227  -0.1220 -0.0334 217 TYR A O   
1394 C CB  . TYR A 190 ? 2.0084 0.8915 1.0924 0.0271  -0.1051 -0.0507 217 TYR A CB  
1395 C CG  . TYR A 190 ? 1.8141 0.7739 0.9390 0.0492  -0.1034 -0.0611 217 TYR A CG  
1396 C CD1 . TYR A 190 ? 1.8505 0.8022 0.9734 0.0820  -0.1084 -0.0748 217 TYR A CD1 
1397 C CD2 . TYR A 190 ? 1.8064 0.8447 0.9702 0.0381  -0.0958 -0.0568 217 TYR A CD2 
1398 C CE1 . TYR A 190 ? 1.8736 0.8930 1.0299 0.1009  -0.1044 -0.0826 217 TYR A CE1 
1399 C CE2 . TYR A 190 ? 1.8108 0.9132 1.0073 0.0581  -0.0934 -0.0638 217 TYR A CE2 
1400 C CZ  . TYR A 190 ? 1.7857 0.8783 0.9772 0.0884  -0.0971 -0.0760 217 TYR A CZ  
1401 O OH  . TYR A 190 ? 1.7844 0.9385 1.0044 0.1070  -0.0924 -0.0816 217 TYR A OH  
1402 N N   . ILE A 191 ? 2.0341 0.7898 1.0620 0.1012  -0.1275 -0.0437 218 ILE A N   
1403 C CA  . ILE A 191 ? 2.0111 0.7459 1.0362 0.1464  -0.1370 -0.0519 218 ILE A CA  
1404 C C   . ILE A 191 ? 2.0174 0.7515 1.0456 0.1772  -0.1461 -0.0348 218 ILE A C   
1405 O O   . ILE A 191 ? 2.0134 0.7933 1.0739 0.2122  -0.1490 -0.0401 218 ILE A O   
1406 C CB  . ILE A 191 ? 2.0444 0.7019 1.0312 0.1455  -0.1416 -0.0639 218 ILE A CB  
1407 C CG1 . ILE A 191 ? 1.9478 0.6034 0.9301 0.1181  -0.1350 -0.0862 218 ILE A CG1 
1408 C CG2 . ILE A 191 ? 1.9372 0.5994 0.9353 0.1911  -0.1493 -0.0711 218 ILE A CG2 
1409 C CD1 . ILE A 191 ? 1.9469 0.6862 0.9706 0.1342  -0.1302 -0.1017 218 ILE A CD1 
1410 N N   . PRO A 192 ? 2.1514 0.8537 1.1554 0.1644  -0.1497 -0.0149 219 PRO A N   
1411 C CA  . PRO A 192 ? 2.0588 0.7842 1.0750 0.1929  -0.1596 -0.0012 219 PRO A CA  
1412 C C   . PRO A 192 ? 1.9810 0.7753 1.0377 0.2043  -0.1574 0.0016  219 PRO A C   
1413 O O   . PRO A 192 ? 1.9279 0.7592 1.0120 0.2378  -0.1653 0.0013  219 PRO A O   
1414 C CB  . PRO A 192 ? 2.0203 0.7022 0.9983 0.1678  -0.1603 0.0183  219 PRO A CB  
1415 C CG  . PRO A 192 ? 2.1355 0.7591 1.0802 0.1372  -0.1535 0.0129  219 PRO A CG  
1416 C CD  . PRO A 192 ? 2.1328 0.7813 1.0982 0.1242  -0.1448 -0.0055 219 PRO A CD  
1417 N N   . ILE A 193 ? 1.9123 0.7548 0.9896 0.1721  -0.1441 0.0025  220 ILE A N   
1418 C CA  . ILE A 193 ? 1.8504 0.7818 0.9791 0.1775  -0.1382 0.0036  220 ILE A CA  
1419 C C   . ILE A 193 ? 1.8699 0.8496 1.0363 0.2023  -0.1350 -0.0133 220 ILE A C   
1420 O O   . ILE A 193 ? 1.9345 0.9635 1.1365 0.2276  -0.1366 -0.0135 220 ILE A O   
1421 C CB  . ILE A 193 ? 1.8035 0.7740 0.9449 0.1373  -0.1245 0.0083  220 ILE A CB  
1422 C CG1 . ILE A 193 ? 1.6859 0.6180 0.7933 0.1144  -0.1250 0.0259  220 ILE A CG1 
1423 C CG2 . ILE A 193 ? 1.7530 0.8117 0.9479 0.1434  -0.1171 0.0071  220 ILE A CG2 
1424 C CD1 . ILE A 193 ? 1.7133 0.6813 0.8324 0.0744  -0.1103 0.0288  220 ILE A CD1 
1425 N N   . ARG A 194 ? 1.8109 0.7772 0.9689 0.1944  -0.1299 -0.0284 221 ARG A N   
1426 C CA  . ARG A 194 ? 1.8050 0.8174 0.9932 0.2149  -0.1243 -0.0446 221 ARG A CA  
1427 C C   . ARG A 194 ? 1.8645 0.8667 1.0589 0.2585  -0.1325 -0.0507 221 ARG A C   
1428 O O   . ARG A 194 ? 1.8059 0.8661 1.0385 0.2797  -0.1266 -0.0577 221 ARG A O   
1429 C CB  . ARG A 194 ? 1.6810 0.6720 0.8498 0.1977  -0.1197 -0.0609 221 ARG A CB  
1430 C CG  . ARG A 194 ? 1.7131 0.7423 0.9020 0.2191  -0.1138 -0.0787 221 ARG A CG  
1431 C CD  . ARG A 194 ? 1.7287 0.8444 0.9632 0.2198  -0.1030 -0.0741 221 ARG A CD  
1432 N NE  . ARG A 194 ? 1.7849 0.9346 1.0343 0.2415  -0.0956 -0.0891 221 ARG A NE  
1433 C CZ  . ARG A 194 ? 1.8076 0.9739 1.0759 0.2758  -0.0941 -0.0934 221 ARG A CZ  
1434 N NH1 . ARG A 194 ? 1.8199 0.9754 1.0976 0.2942  -0.1019 -0.0846 221 ARG A NH1 
1435 N NH2 . ARG A 194 ? 1.6447 0.8412 0.9227 0.2921  -0.0844 -0.1074 221 ARG A NH2 
1436 N N   . LYS A 195 ? 1.8295 0.7595 0.9879 0.2727  -0.1456 -0.0480 222 LYS A N   
1437 C CA  . LYS A 195 ? 1.7328 0.6541 0.8987 0.3157  -0.1552 -0.0546 222 LYS A CA  
1438 C C   . LYS A 195 ? 1.9472 0.8984 1.1349 0.3317  -0.1650 -0.0403 222 LYS A C   
1439 O O   . LYS A 195 ? 1.9419 0.8990 1.1416 0.3604  -0.1745 -0.0436 222 LYS A O   
1440 C CB  . LYS A 195 ? 1.8975 0.7559 1.0283 0.3175  -0.1623 -0.0594 222 LYS A CB  
1441 C CG  . LYS A 195 ? 2.0343 0.8635 1.1442 0.3021  -0.1542 -0.0768 222 LYS A CG  
1442 C CD  . LYS A 195 ? 2.1835 0.9562 1.2661 0.3102  -0.1608 -0.0840 222 LYS A CD  
1443 C CE  . LYS A 195 ? 2.2828 1.0353 1.3500 0.2972  -0.1531 -0.1051 222 LYS A CE  
1444 N NZ  . LYS A 195 ? 2.3213 1.0222 1.3666 0.3091  -0.1584 -0.1149 222 LYS A NZ  
1445 N N   . ARG A 196 ? 1.8181 0.7927 1.0131 0.3128  -0.1630 -0.0261 223 ARG A N   
1446 C CA  . ARG A 196 ? 1.7397 0.7386 0.9499 0.3245  -0.1735 -0.0135 223 ARG A CA  
1447 C C   . ARG A 196 ? 1.9663 0.9196 1.1454 0.3314  -0.1887 -0.0058 223 ARG A C   
1448 O O   . ARG A 196 ? 1.8783 0.8547 1.0753 0.3554  -0.2009 -0.0039 223 ARG A O   
1449 C CB  . ARG A 196 ? 1.7396 0.8074 1.0046 0.3556  -0.1732 -0.0226 223 ARG A CB  
1450 C CG  . ARG A 196 ? 1.5866 0.7328 0.8971 0.3373  -0.1553 -0.0247 223 ARG A CG  
1451 C CD  . ARG A 196 ? 1.5864 0.7999 0.9519 0.3645  -0.1531 -0.0330 223 ARG A CD  
1452 N NE  . ARG A 196 ? 1.8089 1.0889 1.2135 0.3483  -0.1335 -0.0356 223 ARG A NE  
1453 C CZ  . ARG A 196 ? 1.7456 1.0460 1.1611 0.3498  -0.1186 -0.0468 223 ARG A CZ  
1454 N NH1 . ARG A 196 ? 1.5871 0.8505 0.9803 0.3665  -0.1202 -0.0592 223 ARG A NH1 
1455 N NH2 . ARG A 196 ? 1.9240 1.2810 1.3705 0.3349  -0.1018 -0.0455 223 ARG A NH2 
1456 N N   . ASP A 197 ? 1.9113 0.7989 1.0435 0.3106  -0.1881 -0.0019 224 ASP A N   
1457 C CA  . ASP A 197 ? 1.8321 0.6705 0.9280 0.3127  -0.2005 0.0090  224 ASP A CA  
1458 C C   . ASP A 197 ? 1.9852 0.8234 1.0646 0.2921  -0.2025 0.0274  224 ASP A C   
1459 O O   . ASP A 197 ? 2.1063 0.9464 1.1814 0.3080  -0.2157 0.0351  224 ASP A O   
1460 C CB  . ASP A 197 ? 2.1072 0.8741 1.1592 0.2961  -0.1974 0.0069  224 ASP A CB  
1461 C CG  . ASP A 197 ? 2.2497 1.0085 1.3115 0.3230  -0.1995 -0.0110 224 ASP A CG  
1462 O OD1 . ASP A 197 ? 2.1760 0.9867 1.2792 0.3546  -0.2026 -0.0211 224 ASP A OD1 
1463 O OD2 . ASP A 197 ? 2.1069 0.8087 1.1361 0.3117  -0.1972 -0.0156 224 ASP A OD2 
1464 N N   . ARG A 198 ? 2.1326 0.9687 1.2017 0.2569  -0.1895 0.0337  225 ARG A N   
1465 C CA  . ARG A 198 ? 1.9834 0.8348 1.0461 0.2372  -0.1877 0.0488  225 ARG A CA  
1466 C C   . ARG A 198 ? 1.9094 0.8320 1.0209 0.2456  -0.1839 0.0450  225 ARG A C   
1467 O O   . ARG A 198 ? 2.0501 0.9976 1.1813 0.2313  -0.1706 0.0387  225 ARG A O   
1468 C CB  . ARG A 198 ? 2.0784 0.8910 1.1051 0.1933  -0.1741 0.0577  225 ARG A CB  
1469 C CG  . ARG A 198 ? 2.3565 1.0983 1.3313 0.1786  -0.1758 0.0660  225 ARG A CG  
1470 C CD  . ARG A 198 ? 2.5965 1.3079 1.5428 0.1312  -0.1593 0.0729  225 ARG A CD  
1471 N NE  . ARG A 198 ? 2.8351 1.5685 1.7761 0.1103  -0.1527 0.0867  225 ARG A NE  
1472 C CZ  . ARG A 198 ? 2.7117 1.4269 1.6298 0.0690  -0.1372 0.0946  225 ARG A CZ  
1473 N NH1 . ARG A 198 ? 2.4790 1.1533 1.3784 0.0413  -0.1272 0.0900  225 ARG A NH1 
1474 N NH2 . ARG A 198 ? 2.1181 0.8589 1.0334 0.0542  -0.1310 0.1059  225 ARG A NH2 
1475 N N   . ARG A 199 ? 1.9334 0.8944 1.0679 0.2674  -0.1951 0.0472  226 ARG A N   
1476 C CA  . ARG A 199 ? 1.8170 0.8446 0.9983 0.2751  -0.1920 0.0442  226 ARG A CA  
1477 C C   . ARG A 199 ? 1.6885 0.7342 0.8629 0.2481  -0.1868 0.0563  226 ARG A C   
1478 O O   . ARG A 199 ? 1.7919 0.8032 0.9282 0.2421  -0.1951 0.0679  226 ARG A O   
1479 C CB  . ARG A 199 ? 1.7190 0.7879 0.9381 0.3126  -0.2062 0.0358  226 ARG A CB  
1480 C CG  . ARG A 199 ? 1.7594 0.8387 1.0044 0.3389  -0.2055 0.0197  226 ARG A CG  
1481 C CD  . ARG A 199 ? 1.7953 0.9171 1.0788 0.3744  -0.2195 0.0114  226 ARG A CD  
1482 N NE  . ARG A 199 ? 2.0476 1.1767 1.3523 0.3995  -0.2179 -0.0042 226 ARG A NE  
1483 C CZ  . ARG A 199 ? 2.1247 1.3065 1.4773 0.4137  -0.2076 -0.0174 226 ARG A CZ  
1484 N NH1 . ARG A 199 ? 2.0209 1.2529 1.4077 0.4059  -0.1982 -0.0168 226 ARG A NH1 
1485 N NH2 . ARG A 199 ? 2.0437 1.2285 1.4100 0.4357  -0.2051 -0.0317 226 ARG A NH2 
1486 N N   . GLY A 200 ? 1.7686 0.8785 0.9855 0.2294  -0.1705 0.0508  227 GLY A N   
1487 C CA  . GLY A 200 ? 1.7164 0.8532 0.9353 0.2048  -0.1631 0.0585  227 GLY A CA  
1488 C C   . GLY A 200 ? 1.6405 0.8175 0.8864 0.1762  -0.1415 0.0538  227 GLY A C   
1489 O O   . GLY A 200 ? 1.7018 0.8920 0.9674 0.1774  -0.1338 0.0444  227 GLY A O   
1490 N N   . CYS A 201 ? 1.5224 0.7195 0.7677 0.1519  -0.1325 0.0599  228 CYS A N   
1491 C CA  . CYS A 201 ? 1.5239 0.7600 0.7939 0.1252  -0.1133 0.0564  228 CYS A CA  
1492 C C   . CYS A 201 ? 1.6206 0.8136 0.8487 0.0938  -0.1052 0.0632  228 CYS A C   
1493 O O   . CYS A 201 ? 1.6790 0.8429 0.8715 0.0816  -0.1064 0.0737  228 CYS A O   
1494 C CB  . CYS A 201 ? 1.3152 0.6085 0.6199 0.1203  -0.1066 0.0558  228 CYS A CB  
1495 S SG  . CYS A 201 ? 1.7394 1.0891 1.1005 0.1507  -0.1122 0.0465  228 CYS A SG  
1496 N N   . PHE A 202 ? 1.5938 0.7841 0.8259 0.0797  -0.0965 0.0567  229 PHE A N   
1497 C CA  . PHE A 202 ? 1.5971 0.7456 0.7934 0.0486  -0.0889 0.0604  229 PHE A CA  
1498 C C   . PHE A 202 ? 1.5341 0.7336 0.7609 0.0214  -0.0721 0.0548  229 PHE A C   
1499 O O   . PHE A 202 ? 1.5340 0.7852 0.8029 0.0294  -0.0684 0.0457  229 PHE A O   
1500 C CB  . PHE A 202 ? 1.5883 0.6833 0.7595 0.0539  -0.0953 0.0551  229 PHE A CB  
1501 C CG  . PHE A 202 ? 1.7449 0.7949 0.8930 0.0870  -0.1127 0.0583  229 PHE A CG  
1502 C CD1 . PHE A 202 ? 1.6898 0.6740 0.7858 0.0868  -0.1214 0.0717  229 PHE A CD1 
1503 C CD2 . PHE A 202 ? 1.7857 0.8605 0.9641 0.1193  -0.1201 0.0482  229 PHE A CD2 
1504 C CE1 . PHE A 202 ? 1.8306 0.7747 0.9063 0.1207  -0.1397 0.0746  229 PHE A CE1 
1505 C CE2 . PHE A 202 ? 1.7638 0.8028 0.9259 0.1519  -0.1366 0.0495  229 PHE A CE2 
1506 C CZ  . PHE A 202 ? 1.8984 0.8724 1.0099 0.1539  -0.1476 0.0626  229 PHE A CZ  
1507 N N   . ALA A 203 ? 1.5461 0.7312 0.7508 -0.0101 -0.0618 0.0605  230 ALA A N   
1508 C CA  . ALA A 203 ? 1.6241 0.8580 0.8580 -0.0365 -0.0462 0.0543  230 ALA A CA  
1509 C C   . ALA A 203 ? 1.6402 0.8628 0.8740 -0.0512 -0.0445 0.0442  230 ALA A C   
1510 O O   . ALA A 203 ? 1.5742 0.7377 0.7687 -0.0676 -0.0453 0.0462  230 ALA A O   
1511 C CB  . ALA A 203 ? 1.5939 0.8209 0.8067 -0.0650 -0.0340 0.0626  230 ALA A CB  
1512 N N   . VAL A 204 ? 1.5657 0.8421 0.8409 -0.0455 -0.0426 0.0332  231 VAL A N   
1513 C CA  . VAL A 204 ? 1.4447 0.7169 0.7216 -0.0557 -0.0437 0.0208  231 VAL A CA  
1514 C C   . VAL A 204 ? 1.4821 0.8186 0.7970 -0.0748 -0.0338 0.0132  231 VAL A C   
1515 O O   . VAL A 204 ? 1.6039 0.9910 0.9492 -0.0706 -0.0273 0.0167  231 VAL A O   
1516 C CB  . VAL A 204 ? 1.4062 0.6768 0.6905 -0.0240 -0.0543 0.0135  231 VAL A CB  
1517 C CG1 . VAL A 204 ? 1.3879 0.5984 0.6385 -0.0025 -0.0651 0.0198  231 VAL A CG1 
1518 C CG2 . VAL A 204 ? 1.3717 0.7084 0.7003 -0.0028 -0.0521 0.0128  231 VAL A CG2 
1519 N N   . PRO A 205 ? 1.4313 0.7676 0.7460 -0.0955 -0.0332 0.0015  232 PRO A N   
1520 C CA  . PRO A 205 ? 1.3306 0.7320 0.6835 -0.1119 -0.0264 -0.0073 232 PRO A CA  
1521 C C   . PRO A 205 ? 1.4256 0.8779 0.8109 -0.0884 -0.0322 -0.0149 232 PRO A C   
1522 O O   . PRO A 205 ? 1.4207 0.9266 0.8362 -0.0984 -0.0294 -0.0223 232 PRO A O   
1523 C CB  . PRO A 205 ? 1.4034 0.7774 0.7387 -0.1461 -0.0250 -0.0177 232 PRO A CB  
1524 C CG  . PRO A 205 ? 1.5168 0.8243 0.8148 -0.1341 -0.0357 -0.0203 232 PRO A CG  
1525 C CD  . PRO A 205 ? 1.5589 0.8324 0.8370 -0.1079 -0.0387 -0.0049 232 PRO A CD  
1526 N N   . MET A 206 ? 1.4191 0.8577 0.7988 -0.0574 -0.0398 -0.0131 233 MET A N   
1527 C CA  . MET A 206 ? 1.3118 0.7928 0.7155 -0.0360 -0.0435 -0.0192 233 MET A CA  
1528 C C   . MET A 206 ? 1.3456 0.8163 0.7482 -0.0023 -0.0466 -0.0130 233 MET A C   
1529 O O   . MET A 206 ? 1.4596 0.8796 0.8344 0.0072  -0.0523 -0.0131 233 MET A O   
1530 C CB  . MET A 206 ? 1.3987 0.8699 0.7896 -0.0446 -0.0508 -0.0349 233 MET A CB  
1531 C CG  . MET A 206 ? 1.3681 0.8730 0.7720 -0.0200 -0.0554 -0.0409 233 MET A CG  
1532 S SD  . MET A 206 ? 1.2939 0.8802 0.7409 -0.0191 -0.0518 -0.0395 233 MET A SD  
1533 C CE  . MET A 206 ? 1.4483 1.0487 0.8962 -0.0541 -0.0567 -0.0563 233 MET A CE  
1534 N N   . VAL A 207 ? 1.2976 0.8160 0.7315 0.0156  -0.0423 -0.0079 234 VAL A N   
1535 C CA  . VAL A 207 ? 1.2688 0.7907 0.7099 0.0461  -0.0432 -0.0048 234 VAL A CA  
1536 C C   . VAL A 207 ? 1.1963 0.7696 0.6633 0.0573  -0.0394 -0.0058 234 VAL A C   
1537 O O   . VAL A 207 ? 1.3843 0.9951 0.8709 0.0461  -0.0360 -0.0048 234 VAL A O   
1538 C CB  . VAL A 207 ? 1.1982 0.7181 0.6495 0.0573  -0.0404 0.0061  234 VAL A CB  
1539 C CG1 . VAL A 207 ? 1.3374 0.8019 0.7565 0.0522  -0.0466 0.0086  234 VAL A CG1 
1540 C CG2 . VAL A 207 ? 1.1875 0.7473 0.6656 0.0470  -0.0322 0.0123  234 VAL A CG2 
1541 N N   . HIS A 208 ? 1.2716 0.8464 0.7375 0.0805  -0.0397 -0.0076 235 HIS A N   
1542 C CA  . HIS A 208 ? 1.1990 0.8160 0.6814 0.0925  -0.0357 -0.0070 235 HIS A CA  
1543 C C   . HIS A 208 ? 1.1709 0.7864 0.6547 0.1189  -0.0312 -0.0050 235 HIS A C   
1544 O O   . HIS A 208 ? 1.2732 0.8614 0.7519 0.1283  -0.0320 -0.0049 235 HIS A O   
1545 C CB  . HIS A 208 ? 1.2027 0.8265 0.6702 0.0820  -0.0425 -0.0187 235 HIS A CB  
1546 C CG  . HIS A 208 ? 1.3272 0.9077 0.7618 0.0818  -0.0497 -0.0317 235 HIS A CG  
1547 N ND1 . HIS A 208 ? 1.2920 0.8635 0.7136 0.1041  -0.0491 -0.0366 235 HIS A ND1 
1548 C CD2 . HIS A 208 ? 1.2160 0.7575 0.6274 0.0618  -0.0566 -0.0413 235 HIS A CD2 
1549 C CE1 . HIS A 208 ? 1.3447 0.8732 0.7367 0.0997  -0.0562 -0.0498 235 HIS A CE1 
1550 N NE2 . HIS A 208 ? 1.2787 0.7860 0.6634 0.0736  -0.0612 -0.0524 235 HIS A NE2 
1551 N N   . SER A 209 ? 1.3425 0.9893 0.8338 0.1313  -0.0261 -0.0032 236 SER A N   
1552 C CA  . SER A 209 ? 1.2937 0.9458 0.7869 0.1546  -0.0182 -0.0014 236 SER A CA  
1553 C C   . SER A 209 ? 1.2129 0.8770 0.7355 0.1637  -0.0086 0.0098  236 SER A C   
1554 O O   . SER A 209 ? 1.2536 0.9463 0.7945 0.1727  0.0018  0.0188  236 SER A O   
1555 C CB  . SER A 209 ? 1.2164 0.8324 0.6832 0.1633  -0.0230 -0.0140 236 SER A CB  
1556 O OG  . SER A 209 ? 1.3496 0.9561 0.7891 0.1553  -0.0310 -0.0264 236 SER A OG  
1557 N N   . THR A 210 ? 1.2956 0.9372 0.8218 0.1612  -0.0125 0.0094  237 THR A N   
1558 C CA  . THR A 210 ? 1.2514 0.9057 0.8065 0.1671  -0.0061 0.0174  237 THR A CA  
1559 C C   . THR A 210 ? 1.1400 0.7792 0.6955 0.1519  -0.0130 0.0194  237 THR A C   
1560 O O   . THR A 210 ? 1.1519 0.7566 0.6855 0.1481  -0.0227 0.0144  237 THR A O   
1561 C CB  . THR A 210 ? 1.1336 0.7807 0.6945 0.1864  -0.0035 0.0135  237 THR A CB  
1562 O OG1 . THR A 210 ? 1.1925 0.8575 0.7537 0.2000  0.0069  0.0126  237 THR A OG1 
1563 C CG2 . THR A 210 ? 0.9226 0.5846 0.5156 0.1897  0.0007  0.0192  237 THR A CG2 
1564 N N   . PHE A 211 ? 1.1878 0.8504 0.7655 0.1440  -0.0075 0.0267  238 PHE A N   
1565 C CA  . PHE A 211 ? 1.1525 0.8047 0.7300 0.1295  -0.0117 0.0284  238 PHE A CA  
1566 C C   . PHE A 211 ? 1.0531 0.7335 0.6621 0.1296  -0.0029 0.0348  238 PHE A C   
1567 O O   . PHE A 211 ? 1.1595 0.8656 0.7882 0.1371  0.0063  0.0393  238 PHE A O   
1568 C CB  . PHE A 211 ? 1.1504 0.7942 0.7088 0.1090  -0.0160 0.0257  238 PHE A CB  
1569 C CG  . PHE A 211 ? 1.2054 0.8821 0.7757 0.1049  -0.0112 0.0266  238 PHE A CG  
1570 C CD1 . PHE A 211 ? 1.1627 0.8423 0.7198 0.1089  -0.0140 0.0217  238 PHE A CD1 
1571 C CD2 . PHE A 211 ? 1.0792 0.7839 0.6727 0.0988  -0.0048 0.0315  238 PHE A CD2 
1572 C CE1 . PHE A 211 ? 1.2047 0.9163 0.7711 0.1074  -0.0123 0.0226  238 PHE A CE1 
1573 C CE2 . PHE A 211 ? 1.2588 0.9944 0.8638 0.0985  -0.0022 0.0327  238 PHE A CE2 
1574 C CZ  . PHE A 211 ? 1.0804 0.8203 0.6715 0.1032  -0.0069 0.0287  238 PHE A CZ  
1575 N N   . LEU A 212 ? 1.1480 0.8199 0.7582 0.1211  -0.0059 0.0351  239 LEU A N   
1576 C CA  . LEU A 212 ? 0.9035 0.5961 0.5411 0.1205  0.0011  0.0383  239 LEU A CA  
1577 C C   . LEU A 212 ? 1.0848 0.7809 0.7183 0.1029  0.0025  0.0384  239 LEU A C   
1578 O O   . LEU A 212 ? 1.2229 0.8962 0.8310 0.0908  -0.0040 0.0363  239 LEU A O   
1579 C CB  . LEU A 212 ? 0.9666 0.6496 0.6107 0.1281  -0.0041 0.0358  239 LEU A CB  
1580 C CG  . LEU A 212 ? 1.0735 0.7763 0.7476 0.1281  0.0020  0.0360  239 LEU A CG  
1581 C CD1 . LEU A 212 ? 1.0580 0.7858 0.7626 0.1370  0.0149  0.0397  239 LEU A CD1 
1582 C CD2 . LEU A 212 ? 1.0927 0.7855 0.7679 0.1338  -0.0079 0.0311  239 LEU A CD2 
1583 N N   . ILE A 213 ? 0.9651 0.6884 0.6226 0.1019  0.0119  0.0410  240 ILE A N   
1584 C CA  . ILE A 213 ? 0.9799 0.7131 0.6401 0.0876  0.0156  0.0395  240 ILE A CA  
1585 C C   . ILE A 213 ? 0.9960 0.7346 0.6745 0.0890  0.0204  0.0383  240 ILE A C   
1586 O O   . ILE A 213 ? 1.1228 0.8716 0.8251 0.1005  0.0255  0.0403  240 ILE A O   
1587 C CB  . ILE A 213 ? 0.9514 0.7125 0.6257 0.0869  0.0214  0.0411  240 ILE A CB  
1588 C CG1 . ILE A 213 ? 1.0648 0.8239 0.7236 0.0888  0.0156  0.0409  240 ILE A CG1 
1589 C CG2 . ILE A 213 ? 0.8512 0.6235 0.5262 0.0705  0.0248  0.0370  240 ILE A CG2 
1590 C CD1 . ILE A 213 ? 1.0632 0.8522 0.7333 0.0883  0.0174  0.0413  240 ILE A CD1 
1591 N N   . ASP A 214 ? 1.0479 0.7788 0.7139 0.0760  0.0196  0.0345  241 ASP A N   
1592 C CA  . ASP A 214 ? 0.9153 0.6486 0.5922 0.0755  0.0225  0.0306  241 ASP A CA  
1593 C C   . ASP A 214 ? 1.0340 0.7914 0.7310 0.0710  0.0342  0.0284  241 ASP A C   
1594 O O   . ASP A 214 ? 1.0902 0.8507 0.7755 0.0577  0.0375  0.0251  241 ASP A O   
1595 C CB  . ASP A 214 ? 1.0500 0.7579 0.6948 0.0660  0.0142  0.0277  241 ASP A CB  
1596 C CG  . ASP A 214 ? 1.2664 0.9742 0.9186 0.0687  0.0125  0.0221  241 ASP A CG  
1597 O OD1 . ASP A 214 ? 1.1010 0.8290 0.7832 0.0721  0.0213  0.0186  241 ASP A OD1 
1598 O OD2 . ASP A 214 ? 1.2058 0.8915 0.8321 0.0679  0.0015  0.0209  241 ASP A OD2 
1599 N N   . LEU A 215 ? 1.0266 0.8002 0.7541 0.0823  0.0415  0.0302  242 LEU A N   
1600 C CA  . LEU A 215 ? 0.9486 0.7430 0.6969 0.0824  0.0520  0.0282  242 LEU A CA  
1601 C C   . LEU A 215 ? 0.9235 0.7164 0.6769 0.0771  0.0569  0.0193  242 LEU A C   
1602 O O   . LEU A 215 ? 0.9593 0.7677 0.7308 0.0785  0.0664  0.0156  242 LEU A O   
1603 C CB  . LEU A 215 ? 0.8192 0.6251 0.5934 0.0977  0.0582  0.0353  242 LEU A CB  
1604 C CG  . LEU A 215 ? 0.9841 0.7916 0.7494 0.1042  0.0534  0.0434  242 LEU A CG  
1605 C CD1 . LEU A 215 ? 0.9737 0.7911 0.7589 0.1193  0.0607  0.0522  242 LEU A CD1 
1606 C CD2 . LEU A 215 ? 1.0633 0.8802 0.8126 0.0948  0.0486  0.0415  242 LEU A CD2 
1607 N N   . ARG A 216 ? 1.0956 0.8706 0.8330 0.0726  0.0497  0.0148  243 ARG A N   
1608 C CA  . ARG A 216 ? 1.0329 0.8056 0.7654 0.0653  0.0525  0.0046  243 ARG A CA  
1609 C C   . ARG A 216 ? 0.9832 0.7567 0.6899 0.0507  0.0556  0.0019  243 ARG A C   
1610 O O   . ARG A 216 ? 0.9643 0.7450 0.6712 0.0449  0.0638  -0.0068 243 ARG A O   
1611 C CB  . ARG A 216 ? 0.9109 0.6664 0.6318 0.0660  0.0414  0.0002  243 ARG A CB  
1612 C CG  . ARG A 216 ? 1.0057 0.7632 0.7547 0.0775  0.0391  0.0011  243 ARG A CG  
1613 C CD  . ARG A 216 ? 0.9130 0.6582 0.6493 0.0785  0.0246  -0.0039 243 ARG A CD  
1614 N NE  . ARG A 216 ? 1.1299 0.8578 0.8295 0.0763  0.0135  0.0018  243 ARG A NE  
1615 C CZ  . ARG A 216 ? 1.0935 0.8045 0.7640 0.0744  0.0000  -0.0014 243 ARG A CZ  
1616 N NH1 . ARG A 216 ? 1.0358 0.7489 0.7096 0.0743  -0.0057 -0.0117 243 ARG A NH1 
1617 N NH2 . ARG A 216 ? 1.1423 0.8316 0.7775 0.0726  -0.0084 0.0057  243 ARG A NH2 
1618 N N   . LYS A 217 ? 1.0690 0.8346 0.7533 0.0438  0.0505  0.0083  244 LYS A N   
1619 C CA  . LYS A 217 ? 0.9802 0.7430 0.6378 0.0263  0.0544  0.0066  244 LYS A CA  
1620 C C   . LYS A 217 ? 1.0351 0.8303 0.7161 0.0224  0.0674  0.0031  244 LYS A C   
1621 O O   . LYS A 217 ? 1.1328 0.9462 0.8376 0.0311  0.0676  0.0069  244 LYS A O   
1622 C CB  . LYS A 217 ? 1.0533 0.7928 0.6807 0.0192  0.0449  0.0141  244 LYS A CB  
1623 C CG  . LYS A 217 ? 1.1229 0.8310 0.7278 0.0265  0.0304  0.0174  244 LYS A CG  
1624 C CD  . LYS A 217 ? 0.9983 0.6843 0.5678 0.0173  0.0275  0.0150  244 LYS A CD  
1625 C CE  . LYS A 217 ? 0.9861 0.6510 0.5443 0.0302  0.0115  0.0156  244 LYS A CE  
1626 N NZ  . LYS A 217 ? 1.1347 0.7791 0.6823 0.0380  -0.0002 0.0229  244 LYS A NZ  
1627 N N   . ALA A 218 ? 0.8768 0.6810 0.5503 0.0104  0.0780  -0.0046 245 ALA A N   
1628 C CA  . ALA A 218 ? 1.0626 0.9028 0.7619 0.0075  0.0909  -0.0102 245 ALA A CA  
1629 C C   . ALA A 218 ? 1.1310 0.9837 0.8302 -0.0020 0.0890  -0.0058 245 ALA A C   
1630 O O   . ALA A 218 ? 1.0362 0.9231 0.7664 0.0033  0.0933  -0.0082 245 ALA A O   
1631 C CB  . ALA A 218 ? 0.9387 0.7860 0.6261 -0.0055 0.1043  -0.0205 245 ALA A CB  
1632 N N   . ALA A 219 ? 1.1214 0.9460 0.7861 -0.0154 0.0816  -0.0002 246 ALA A N   
1633 C CA  . ALA A 219 ? 1.1360 0.9688 0.7990 -0.0273 0.0794  0.0018  246 ALA A CA  
1634 C C   . ALA A 219 ? 1.1196 0.9648 0.8058 -0.0101 0.0698  0.0060  246 ALA A C   
1635 O O   . ALA A 219 ? 1.1660 1.0366 0.8668 -0.0148 0.0694  0.0038  246 ALA A O   
1636 C CB  . ALA A 219 ? 1.1430 0.9340 0.7607 -0.0443 0.0733  0.0072  246 ALA A CB  
1637 N N   . SER A 220 ? 1.0196 0.8493 0.7094 0.0091  0.0626  0.0114  247 SER A N   
1638 C CA  . SER A 220 ? 1.0253 0.8637 0.7315 0.0254  0.0554  0.0167  247 SER A CA  
1639 C C   . SER A 220 ? 1.0417 0.9206 0.7837 0.0361  0.0609  0.0147  247 SER A C   
1640 O O   . SER A 220 ? 1.0221 0.9141 0.7733 0.0459  0.0548  0.0186  247 SER A O   
1641 C CB  . SER A 220 ? 0.9215 0.7384 0.6276 0.0423  0.0503  0.0222  247 SER A CB  
1642 O OG  . SER A 220 ? 0.9538 0.7835 0.6859 0.0540  0.0579  0.0207  247 SER A OG  
1643 N N   . ARG A 221 ? 0.9411 0.8396 0.7015 0.0358  0.0718  0.0083  248 ARG A N   
1644 C CA  . ARG A 221 ? 0.9134 0.8509 0.7084 0.0478  0.0766  0.0055  248 ARG A CA  
1645 C C   . ARG A 221 ? 0.9879 0.9557 0.7897 0.0388  0.0724  0.0022  248 ARG A C   
1646 O O   . ARG A 221 ? 0.9405 0.9392 0.7677 0.0536  0.0694  0.0029  248 ARG A O   
1647 C CB  . ARG A 221 ? 0.9462 0.8989 0.7568 0.0464  0.0901  -0.0040 248 ARG A CB  
1648 C CG  . ARG A 221 ? 0.9250 0.8534 0.7353 0.0563  0.0942  -0.0042 248 ARG A CG  
1649 C CD  . ARG A 221 ? 1.0398 0.9851 0.8641 0.0546  0.1081  -0.0164 248 ARG A CD  
1650 N NE  . ARG A 221 ? 1.3115 1.2991 1.1672 0.0620  0.1133  -0.0212 248 ARG A NE  
1651 C CZ  . ARG A 221 ? 1.3204 1.3345 1.1929 0.0599  0.1264  -0.0337 248 ARG A CZ  
1652 N NH1 . ARG A 221 ? 0.9767 0.9776 0.8340 0.0497  0.1366  -0.0429 248 ARG A NH1 
1653 N NH2 . ARG A 221 ? 1.3481 1.4048 1.2532 0.0692  0.1288  -0.0381 248 ARG A NH2 
1654 N N   . ASN A 222 ? 0.9486 0.9075 0.7278 0.0147  0.0715  -0.0015 249 ASN A N   
1655 C CA  . ASN A 222 ? 0.9749 0.9628 0.7616 0.0007  0.0683  -0.0075 249 ASN A CA  
1656 C C   . ASN A 222 ? 0.9544 0.9285 0.7256 0.0026  0.0535  -0.0027 249 ASN A C   
1657 O O   . ASN A 222 ? 0.9566 0.9557 0.7351 -0.0080 0.0482  -0.0091 249 ASN A O   
1658 C CB  . ASN A 222 ? 0.8656 0.8492 0.6357 -0.0299 0.0779  -0.0146 249 ASN A CB  
1659 C CG  . ASN A 222 ? 1.1269 1.1301 0.9116 -0.0330 0.0944  -0.0218 249 ASN A CG  
1660 O OD1 . ASN A 222 ? 1.1132 1.1506 0.9325 -0.0152 0.0986  -0.0258 249 ASN A OD1 
1661 N ND2 . ASN A 222 ? 1.1527 1.1321 0.9086 -0.0543 0.1041  -0.0233 249 ASN A ND2 
1662 N N   . LEU A 223 ? 0.9662 0.9040 0.7176 0.0154  0.0469  0.0064  250 LEU A N   
1663 C CA  . LEU A 223 ? 0.9355 0.8603 0.6713 0.0201  0.0344  0.0098  250 LEU A CA  
1664 C C   . LEU A 223 ? 0.9404 0.8971 0.6988 0.0420  0.0286  0.0128  250 LEU A C   
1665 O O   . LEU A 223 ? 1.0207 0.9893 0.7994 0.0611  0.0336  0.0180  250 LEU A O   
1666 C CB  . LEU A 223 ? 0.8907 0.7698 0.6006 0.0279  0.0310  0.0175  250 LEU A CB  
1667 C CG  . LEU A 223 ? 0.9293 0.7713 0.6113 0.0107  0.0334  0.0167  250 LEU A CG  
1668 C CD1 . LEU A 223 ? 0.9737 0.7774 0.6354 0.0229  0.0273  0.0232  250 LEU A CD1 
1669 C CD2 . LEU A 223 ? 0.9432 0.7770 0.6057 -0.0145 0.0313  0.0106  250 LEU A CD2 
1670 N N   . ALA A 224 ? 0.9905 0.9584 0.7425 0.0396  0.0176  0.0093  251 ALA A N   
1671 C CA  . ALA A 224 ? 1.0056 1.0023 0.7716 0.0611  0.0095  0.0128  251 ALA A CA  
1672 C C   . ALA A 224 ? 0.9855 0.9715 0.7268 0.0597  -0.0033 0.0107  251 ALA A C   
1673 O O   . ALA A 224 ? 1.0026 0.9911 0.7353 0.0381  -0.0088 -0.0004 251 ALA A O   
1674 C CB  . ALA A 224 ? 0.7698 0.8199 0.5696 0.0610  0.0089  0.0048  251 ALA A CB  
1675 N N   . PHE A 225 ? 0.9789 0.9519 0.7081 0.0818  -0.0068 0.0206  252 PHE A N   
1676 C CA  . PHE A 225 ? 0.9826 0.9497 0.6877 0.0842  -0.0187 0.0176  252 PHE A CA  
1677 C C   . PHE A 225 ? 0.9144 0.9272 0.6322 0.0883  -0.0308 0.0110  252 PHE A C   
1678 O O   . PHE A 225 ? 1.0331 1.0493 0.7345 0.0796  -0.0426 0.0009  252 PHE A O   
1679 C CB  . PHE A 225 ? 0.9220 0.8641 0.6095 0.1063  -0.0162 0.0300  252 PHE A CB  
1680 C CG  . PHE A 225 ? 1.0112 0.9108 0.6842 0.1018  -0.0086 0.0329  252 PHE A CG  
1681 C CD1 . PHE A 225 ? 1.1109 0.9811 0.7565 0.0916  -0.0139 0.0257  252 PHE A CD1 
1682 C CD2 . PHE A 225 ? 0.9769 0.8662 0.6643 0.1085  0.0028  0.0414  252 PHE A CD2 
1683 C CE1 . PHE A 225 ? 0.9211 0.7546 0.5548 0.0907  -0.0089 0.0280  252 PHE A CE1 
1684 C CE2 . PHE A 225 ? 1.0278 0.8831 0.7042 0.1054  0.0073  0.0426  252 PHE A CE2 
1685 C CZ  . PHE A 225 ? 0.9775 0.8060 0.6274 0.0976  0.0010  0.0364  252 PHE A CZ  
1686 N N   . TYR A 226 ? 0.9183 0.9666 0.6654 0.1024  -0.0293 0.0153  253 TYR A N   
1687 C CA  . TYR A 226 ? 0.9299 1.0275 0.6939 0.1100  -0.0425 0.0091  253 TYR A CA  
1688 C C   . TYR A 226 ? 0.9325 1.0664 0.7366 0.1151  -0.0362 0.0084  253 TYR A C   
1689 O O   . TYR A 226 ? 1.0818 1.1991 0.8946 0.1263  -0.0233 0.0189  253 TYR A O   
1690 C CB  . TYR A 226 ? 1.0716 1.1711 0.8179 0.1386  -0.0518 0.0204  253 TYR A CB  
1691 C CG  . TYR A 226 ? 0.9734 1.1192 0.7249 0.1441  -0.0712 0.0111  253 TYR A CG  
1692 C CD1 . TYR A 226 ? 0.9717 1.1195 0.7025 0.1282  -0.0844 -0.0035 253 TYR A CD1 
1693 C CD2 . TYR A 226 ? 0.9900 1.1773 0.7670 0.1661  -0.0777 0.0157  253 TYR A CD2 
1694 C CE1 . TYR A 226 ? 1.0711 1.2644 0.8074 0.1324  -0.1042 -0.0144 253 TYR A CE1 
1695 C CE2 . TYR A 226 ? 1.0435 1.2775 0.8264 0.1729  -0.0983 0.0062  253 TYR A CE2 
1696 C CZ  . TYR A 226 ? 1.1505 1.3889 0.9133 0.1551  -0.1119 -0.0094 253 TYR A CZ  
1697 O OH  . TYR A 226 ? 1.2471 1.5347 1.0162 0.1608  -0.1343 -0.0212 253 TYR A OH  
1698 N N   . PRO A 227 ? 0.9386 1.1232 0.7694 0.1070  -0.0447 -0.0054 254 PRO A N   
1699 C CA  . PRO A 227 ? 1.0066 1.2163 0.8337 0.0889  -0.0599 -0.0217 254 PRO A CA  
1700 C C   . PRO A 227 ? 1.0351 1.2241 0.8550 0.0510  -0.0520 -0.0340 254 PRO A C   
1701 O O   . PRO A 227 ? 1.0476 1.2055 0.8640 0.0421  -0.0360 -0.0287 254 PRO A O   
1702 C CB  . PRO A 227 ? 0.9435 1.2211 0.8123 0.0987  -0.0693 -0.0303 254 PRO A CB  
1703 C CG  . PRO A 227 ? 0.8629 1.1470 0.7611 0.1056  -0.0524 -0.0252 254 PRO A CG  
1704 C CD  . PRO A 227 ? 0.8921 1.1185 0.7636 0.1203  -0.0407 -0.0061 254 PRO A CD  
1705 N N   . PRO A 228 ? 1.0581 1.2596 0.8726 0.0282  -0.0629 -0.0501 255 PRO A N   
1706 C CA  . PRO A 228 ? 1.1004 1.2790 0.9076 -0.0093 -0.0538 -0.0607 255 PRO A CA  
1707 C C   . PRO A 228 ? 1.0659 1.2764 0.9095 -0.0252 -0.0392 -0.0663 255 PRO A C   
1708 O O   . PRO A 228 ? 1.0343 1.3002 0.9167 -0.0121 -0.0408 -0.0697 255 PRO A O   
1709 C CB  . PRO A 228 ? 1.0846 1.2802 0.8860 -0.0283 -0.0701 -0.0787 255 PRO A CB  
1710 C CG  . PRO A 228 ? 1.0603 1.2630 0.8457 0.0018  -0.0874 -0.0740 255 PRO A CG  
1711 C CD  . PRO A 228 ? 0.9511 1.1781 0.7576 0.0354  -0.0843 -0.0586 255 PRO A CD  
1712 N N   . HIS A 229 ? 1.0252 1.1994 0.8541 -0.0524 -0.0245 -0.0670 256 HIS A N   
1713 C CA  . HIS A 229 ? 0.9332 1.1343 0.7905 -0.0716 -0.0079 -0.0733 256 HIS A CA  
1714 C C   . HIS A 229 ? 1.0104 1.2774 0.9061 -0.0900 -0.0139 -0.0929 256 HIS A C   
1715 O O   . HIS A 229 ? 1.1213 1.3914 1.0086 -0.1049 -0.0276 -0.1039 256 HIS A O   
1716 C CB  . HIS A 229 ? 1.0164 1.1626 0.8422 -0.1006 0.0070  -0.0707 256 HIS A CB  
1717 C CG  . HIS A 229 ? 1.1303 1.2932 0.9750 -0.1155 0.0276  -0.0727 256 HIS A CG  
1718 N ND1 . HIS A 229 ? 1.0142 1.2185 0.8855 -0.1457 0.0365  -0.0877 256 HIS A ND1 
1719 C CD2 . HIS A 229 ? 1.2702 1.4149 1.1102 -0.1051 0.0417  -0.0629 256 HIS A CD2 
1720 C CE1 . HIS A 229 ? 1.1834 1.3938 1.0637 -0.1525 0.0567  -0.0863 256 HIS A CE1 
1721 N NE2 . HIS A 229 ? 1.2534 1.4273 1.1139 -0.1278 0.0593  -0.0718 256 HIS A NE2 
1722 N N   . PRO A 230 ? 1.0247 1.3476 0.9648 -0.0888 -0.0045 -0.0996 257 PRO A N   
1723 C CA  . PRO A 230 ? 1.0249 1.4209 1.0096 -0.1037 -0.0113 -0.1200 257 PRO A CA  
1724 C C   . PRO A 230 ? 0.9379 1.3275 0.9158 -0.1507 -0.0075 -0.1351 257 PRO A C   
1725 O O   . PRO A 230 ? 1.1647 1.6120 1.1766 -0.1655 -0.0173 -0.1539 257 PRO A O   
1726 C CB  . PRO A 230 ? 0.9087 1.3539 0.9378 -0.0963 0.0049  -0.1233 257 PRO A CB  
1727 C CG  . PRO A 230 ? 0.8405 1.2474 0.8517 -0.0621 0.0101  -0.1037 257 PRO A CG  
1728 C CD  . PRO A 230 ? 0.8410 1.1670 0.7956 -0.0698 0.0111  -0.0903 257 PRO A CD  
1729 N N   . ASP A 231 ? 1.0811 1.4026 1.0169 -0.1744 0.0057  -0.1277 258 ASP A N   
1730 C CA  . ASP A 231 ? 1.1664 1.4675 1.0878 -0.2191 0.0099  -0.1394 258 ASP A CA  
1731 C C   . ASP A 231 ? 1.2169 1.4666 1.0964 -0.2206 -0.0081 -0.1393 258 ASP A C   
1732 O O   . ASP A 231 ? 1.2517 1.4753 1.1148 -0.2566 -0.0065 -0.1493 258 ASP A O   
1733 C CB  . ASP A 231 ? 1.2694 1.5223 1.1651 -0.2454 0.0355  -0.1311 258 ASP A CB  
1734 C CG  . ASP A 231 ? 1.2635 1.5659 1.1972 -0.2471 0.0562  -0.1337 258 ASP A CG  
1735 O OD1 . ASP A 231 ? 1.1890 1.5703 1.1766 -0.2416 0.0527  -0.1479 258 ASP A OD1 
1736 O OD2 . ASP A 231 ? 1.1502 1.4135 1.0592 -0.2528 0.0754  -0.1224 258 ASP A OD2 
1737 N N   . TYR A 232 ? 1.0473 1.2804 0.9085 -0.1831 -0.0237 -0.1287 259 TYR A N   
1738 C CA  . TYR A 232 ? 1.1321 1.3133 0.9503 -0.1808 -0.0385 -0.1281 259 TYR A CA  
1739 C C   . TYR A 232 ? 1.1807 1.4000 1.0139 -0.1981 -0.0563 -0.1505 259 TYR A C   
1740 O O   . TYR A 232 ? 1.1681 1.4545 1.0364 -0.1815 -0.0705 -0.1591 259 TYR A O   
1741 C CB  . TYR A 232 ? 1.0218 1.1856 0.8215 -0.1363 -0.0481 -0.1119 259 TYR A CB  
1742 C CG  . TYR A 232 ? 1.1101 1.2156 0.8624 -0.1301 -0.0591 -0.1095 259 TYR A CG  
1743 C CD1 . TYR A 232 ? 1.1720 1.2049 0.8844 -0.1342 -0.0494 -0.0983 259 TYR A CD1 
1744 C CD2 . TYR A 232 ? 1.1162 1.2407 0.8629 -0.1182 -0.0796 -0.1191 259 TYR A CD2 
1745 C CE1 . TYR A 232 ? 1.2630 1.2446 0.9347 -0.1262 -0.0587 -0.0975 259 TYR A CE1 
1746 C CE2 . TYR A 232 ? 1.0700 1.1420 0.7726 -0.1115 -0.0880 -0.1187 259 TYR A CE2 
1747 C CZ  . TYR A 232 ? 1.2012 1.2025 0.8683 -0.1152 -0.0769 -0.1081 259 TYR A CZ  
1748 O OH  . TYR A 232 ? 1.3522 1.3034 0.9782 -0.1065 -0.0845 -0.1091 259 TYR A OH  
1749 N N   . THR A 233 ? 1.2229 1.3979 1.0284 -0.2309 -0.0567 -0.1605 260 THR A N   
1750 C CA  . THR A 233 ? 1.2988 1.5030 1.1156 -0.2530 -0.0733 -0.1848 260 THR A CA  
1751 C C   . THR A 233 ? 1.4506 1.5918 1.2169 -0.2509 -0.0870 -0.1879 260 THR A C   
1752 O O   . THR A 233 ? 1.5953 1.7358 1.3585 -0.2788 -0.0969 -0.2090 260 THR A O   
1753 C CB  . THR A 233 ? 1.3598 1.5795 1.2002 -0.3036 -0.0593 -0.2006 260 THR A CB  
1754 O OG1 . THR A 233 ? 1.5343 1.6745 1.3346 -0.3256 -0.0395 -0.1885 260 THR A OG1 
1755 C CG2 . THR A 233 ? 1.3937 1.6938 1.2929 -0.3048 -0.0484 -0.2040 260 THR A CG2 
1756 N N   . TRP A 234 ? 1.3600 1.4497 1.0882 -0.2191 -0.0872 -0.1692 261 TRP A N   
1757 C CA  . TRP A 234 ? 1.3245 1.3513 1.0038 -0.2140 -0.0969 -0.1714 261 TRP A CA  
1758 C C   . TRP A 234 ? 1.3559 1.4104 1.0293 -0.1778 -0.1171 -0.1731 261 TRP A C   
1759 O O   . TRP A 234 ? 1.2671 1.3890 0.9738 -0.1594 -0.1256 -0.1735 261 TRP A O   
1760 C CB  . TRP A 234 ? 1.3163 1.2662 0.9571 -0.2052 -0.0823 -0.1509 261 TRP A CB  
1761 C CG  . TRP A 234 ? 1.4642 1.3769 1.0990 -0.2414 -0.0643 -0.1490 261 TRP A CG  
1762 C CD1 . TRP A 234 ? 1.5556 1.4790 1.2048 -0.2845 -0.0599 -0.1656 261 TRP A CD1 
1763 C CD2 . TRP A 234 ? 1.5487 1.4071 1.1595 -0.2385 -0.0480 -0.1292 261 TRP A CD2 
1764 N NE1 . TRP A 234 ? 1.5613 1.4367 1.1933 -0.3087 -0.0402 -0.1554 261 TRP A NE1 
1765 C CE2 . TRP A 234 ? 1.5422 1.3773 1.1491 -0.2799 -0.0339 -0.1331 261 TRP A CE2 
1766 C CE3 . TRP A 234 ? 1.5180 1.3463 1.1102 -0.2056 -0.0441 -0.1090 261 TRP A CE3 
1767 C CZ2 . TRP A 234 ? 1.5869 1.3679 1.1671 -0.2871 -0.0174 -0.1163 261 TRP A CZ2 
1768 C CZ3 . TRP A 234 ? 1.4924 1.2712 1.0626 -0.2130 -0.0294 -0.0945 261 TRP A CZ3 
1769 C CH2 . TRP A 234 ? 1.4949 1.2495 1.0568 -0.2523 -0.0168 -0.0976 261 TRP A CH2 
1770 N N   . SER A 235 ? 1.3084 1.3095 0.9368 -0.1663 -0.1245 -0.1740 262 SER A N   
1771 C CA  . SER A 235 ? 1.3119 1.3333 0.9263 -0.1341 -0.1420 -0.1762 262 SER A CA  
1772 C C   . SER A 235 ? 1.2041 1.2377 0.8226 -0.0936 -0.1360 -0.1512 262 SER A C   
1773 O O   . SER A 235 ? 1.3297 1.3396 0.9518 -0.0887 -0.1189 -0.1331 262 SER A O   
1774 C CB  . SER A 235 ? 1.5150 1.4740 1.0790 -0.1327 -0.1485 -0.1848 262 SER A CB  
1775 O OG  . SER A 235 ? 1.8600 1.7503 1.3962 -0.1267 -0.1329 -0.1688 262 SER A OG  
1776 N N   . PHE A 236 ? 1.2120 1.2814 0.8275 -0.0648 -0.1507 -0.1507 263 PHE A N   
1777 C CA  . PHE A 236 ? 1.1803 1.2655 0.8012 -0.0270 -0.1460 -0.1276 263 PHE A CA  
1778 C C   . PHE A 236 ? 1.2259 1.2516 0.8057 -0.0054 -0.1372 -0.1128 263 PHE A C   
1779 O O   . PHE A 236 ? 1.4929 1.5213 1.0517 0.0235  -0.1428 -0.1054 263 PHE A O   
1780 C CB  . PHE A 236 ? 1.1690 1.3153 0.8009 -0.0054 -0.1655 -0.1317 263 PHE A CB  
1781 C CG  . PHE A 236 ? 1.1391 1.3105 0.7869 0.0289  -0.1606 -0.1087 263 PHE A CG  
1782 C CD1 . PHE A 236 ? 1.1982 1.3800 0.8809 0.0270  -0.1449 -0.0970 263 PHE A CD1 
1783 C CD2 . PHE A 236 ? 1.0478 1.2303 0.6733 0.0627  -0.1711 -0.0992 263 PHE A CD2 
1784 C CE1 . PHE A 236 ? 1.2047 1.4054 0.9021 0.0581  -0.1403 -0.0772 263 PHE A CE1 
1785 C CE2 . PHE A 236 ? 1.1975 1.3973 0.8359 0.0934  -0.1659 -0.0770 263 PHE A CE2 
1786 C CZ  . PHE A 236 ? 1.1560 1.3641 0.8316 0.0910  -0.1508 -0.0666 263 PHE A CZ  
1787 N N   . ASP A 237 ? 1.3409 1.3132 0.9094 -0.0199 -0.1228 -0.1086 264 ASP A N   
1788 C CA  . ASP A 237 ? 1.3049 1.2211 0.8401 -0.0028 -0.1138 -0.0972 264 ASP A CA  
1789 C C   . ASP A 237 ? 1.3482 1.2578 0.9001 0.0109  -0.0972 -0.0748 264 ASP A C   
1790 O O   . ASP A 237 ? 1.3278 1.2443 0.9042 -0.0056 -0.0887 -0.0718 264 ASP A O   
1791 C CB  . ASP A 237 ? 1.3495 1.2071 0.8574 -0.0264 -0.1122 -0.1096 264 ASP A CB  
1792 C CG  . ASP A 237 ? 1.5393 1.3432 1.0127 -0.0062 -0.1062 -0.1024 264 ASP A CG  
1793 O OD1 . ASP A 237 ? 1.6783 1.4923 1.1493 0.0237  -0.1020 -0.0884 264 ASP A OD1 
1794 O OD2 . ASP A 237 ? 1.6593 1.4104 1.1086 -0.0202 -0.1051 -0.1109 264 ASP A OD2 
1795 N N   . ASP A 238 ? 1.2938 1.1898 0.8317 0.0401  -0.0917 -0.0603 265 ASP A N   
1796 C CA  . ASP A 238 ? 1.1436 1.0401 0.7006 0.0549  -0.0774 -0.0402 265 ASP A CA  
1797 C C   . ASP A 238 ? 1.1802 1.0355 0.7364 0.0402  -0.0660 -0.0368 265 ASP A C   
1798 O O   . ASP A 238 ? 1.2792 1.1448 0.8596 0.0364  -0.0568 -0.0281 265 ASP A O   
1799 C CB  . ASP A 238 ? 0.9679 0.8579 0.5097 0.0861  -0.0729 -0.0266 265 ASP A CB  
1800 C CG  . ASP A 238 ? 1.2958 1.1401 0.8028 0.0911  -0.0710 -0.0312 265 ASP A CG  
1801 O OD1 . ASP A 238 ? 1.3138 1.1327 0.8030 0.0731  -0.0777 -0.0471 265 ASP A OD1 
1802 O OD2 . ASP A 238 ? 1.2751 1.1093 0.7735 0.1133  -0.0621 -0.0194 265 ASP A OD2 
1803 N N   . ILE A 239 ? 1.2235 1.0311 0.7502 0.0328  -0.0672 -0.0439 266 ILE A N   
1804 C CA  . ILE A 239 ? 1.2501 1.0154 0.7711 0.0230  -0.0584 -0.0388 266 ILE A CA  
1805 C C   . ILE A 239 ? 1.1797 0.9450 0.7101 -0.0090 -0.0572 -0.0455 266 ILE A C   
1806 O O   . ILE A 239 ? 1.3187 1.0719 0.8567 -0.0166 -0.0478 -0.0371 266 ILE A O   
1807 C CB  . ILE A 239 ? 1.3147 1.0269 0.8009 0.0292  -0.0605 -0.0437 266 ILE A CB  
1808 C CG1 . ILE A 239 ? 1.3473 1.0475 0.8106 0.0152  -0.0721 -0.0629 266 ILE A CG1 
1809 C CG2 . ILE A 239 ? 1.0857 0.7993 0.5676 0.0603  -0.0561 -0.0347 266 ILE A CG2 
1810 C CD1 . ILE A 239 ? 1.1546 0.7977 0.5829 0.0204  -0.0740 -0.0700 266 ILE A CD1 
1811 N N   . ILE A 240 ? 1.2944 1.0738 0.8238 -0.0294 -0.0662 -0.0614 267 ILE A N   
1812 C CA  . ILE A 240 ? 1.2258 1.0085 0.7664 -0.0631 -0.0627 -0.0686 267 ILE A CA  
1813 C C   . ILE A 240 ? 1.2421 1.0789 0.8228 -0.0640 -0.0555 -0.0623 267 ILE A C   
1814 O O   . ILE A 240 ? 1.0980 0.9310 0.6882 -0.0833 -0.0448 -0.0596 267 ILE A O   
1815 C CB  . ILE A 240 ? 1.3024 1.0910 0.8362 -0.0861 -0.0743 -0.0897 267 ILE A CB  
1816 C CG1 . ILE A 240 ? 1.4994 1.2374 0.9931 -0.0785 -0.0823 -0.0975 267 ILE A CG1 
1817 C CG2 . ILE A 240 ? 1.3750 1.1524 0.9138 -0.1251 -0.0677 -0.0969 267 ILE A CG2 
1818 C CD1 . ILE A 240 ? 1.7227 1.4633 1.2071 -0.1003 -0.0949 -0.1207 267 ILE A CD1 
1819 N N   . VAL A 241 ? 1.3116 1.1975 0.9141 -0.0419 -0.0609 -0.0599 268 VAL A N   
1820 C CA  . VAL A 241 ? 1.1544 1.0903 0.7958 -0.0376 -0.0545 -0.0542 268 VAL A CA  
1821 C C   . VAL A 241 ? 1.0589 0.9722 0.7027 -0.0299 -0.0397 -0.0388 268 VAL A C   
1822 O O   . VAL A 241 ? 1.2133 1.1440 0.8784 -0.0427 -0.0295 -0.0381 268 VAL A O   
1823 C CB  . VAL A 241 ? 1.0768 1.0594 0.7341 -0.0099 -0.0642 -0.0516 268 VAL A CB  
1824 C CG1 . VAL A 241 ? 0.9140 0.9267 0.6025 0.0074  -0.0549 -0.0388 268 VAL A CG1 
1825 C CG2 . VAL A 241 ? 1.0677 1.0961 0.7396 -0.0230 -0.0787 -0.0695 268 VAL A CG2 
1826 N N   . PHE A 242 ? 1.1272 1.0037 0.7499 -0.0095 -0.0379 -0.0279 269 PHE A N   
1827 C CA  . PHE A 242 ? 1.1082 0.9621 0.7321 -0.0037 -0.0259 -0.0156 269 PHE A CA  
1828 C C   . PHE A 242 ? 1.1850 1.0010 0.7908 -0.0297 -0.0205 -0.0183 269 PHE A C   
1829 O O   . PHE A 242 ? 1.1178 0.9356 0.7333 -0.0372 -0.0102 -0.0136 269 PHE A O   
1830 C CB  . PHE A 242 ? 0.9622 0.7889 0.5709 0.0221  -0.0257 -0.0055 269 PHE A CB  
1831 C CG  . PHE A 242 ? 0.9936 0.8082 0.6110 0.0310  -0.0152 0.0058  269 PHE A CG  
1832 C CD1 . PHE A 242 ? 1.0753 0.9210 0.7216 0.0324  -0.0072 0.0098  269 PHE A CD1 
1833 C CD2 . PHE A 242 ? 1.0497 0.8233 0.6475 0.0389  -0.0141 0.0107  269 PHE A CD2 
1834 C CE1 . PHE A 242 ? 1.0092 0.8430 0.6626 0.0395  0.0016  0.0177  269 PHE A CE1 
1835 C CE2 . PHE A 242 ? 1.0280 0.7938 0.6352 0.0464  -0.0065 0.0189  269 PHE A CE2 
1836 C CZ  . PHE A 242 ? 1.0750 0.8698 0.7090 0.0457  0.0014  0.0220  269 PHE A CZ  
1837 N N   . ALA A 243 ? 1.1985 0.9772 0.7749 -0.0433 -0.0270 -0.0259 270 ALA A N   
1838 C CA  . ALA A 243 ? 1.1455 0.8793 0.6980 -0.0676 -0.0222 -0.0264 270 ALA A CA  
1839 C C   . ALA A 243 ? 1.1451 0.9071 0.7170 -0.0953 -0.0128 -0.0308 270 ALA A C   
1840 O O   . ALA A 243 ? 1.2482 0.9920 0.8128 -0.1061 -0.0022 -0.0242 270 ALA A O   
1841 C CB  . ALA A 243 ? 1.1877 0.8785 0.7078 -0.0785 -0.0312 -0.0360 270 ALA A CB  
1842 N N   . PHE A 244 ? 1.1629 0.9724 0.7599 -0.1066 -0.0165 -0.0428 271 PHE A N   
1843 C CA  . PHE A 244 ? 1.1113 0.9575 0.7339 -0.1326 -0.0064 -0.0492 271 PHE A CA  
1844 C C   . PHE A 244 ? 1.1753 1.0558 0.8257 -0.1187 0.0046  -0.0409 271 PHE A C   
1845 O O   . PHE A 244 ? 1.2002 1.0957 0.8624 -0.1387 0.0179  -0.0429 271 PHE A O   
1846 C CB  . PHE A 244 ? 1.0390 0.9364 0.6880 -0.1438 -0.0154 -0.0657 271 PHE A CB  
1847 C CG  . PHE A 244 ? 1.1656 1.1050 0.8447 -0.1738 -0.0049 -0.0756 271 PHE A CG  
1848 C CD1 . PHE A 244 ? 1.1801 1.0897 0.8422 -0.2122 0.0031  -0.0822 271 PHE A CD1 
1849 C CD2 . PHE A 244 ? 1.1517 1.1598 0.8764 -0.1636 -0.0019 -0.0786 271 PHE A CD2 
1850 C CE1 . PHE A 244 ? 1.2400 1.1913 0.9317 -0.2420 0.0156  -0.0919 271 PHE A CE1 
1851 C CE2 . PHE A 244 ? 1.1488 1.2013 0.9053 -0.1905 0.0091  -0.0895 271 PHE A CE2 
1852 C CZ  . PHE A 244 ? 1.2083 1.2343 0.9491 -0.2309 0.0188  -0.0964 271 PHE A CZ  
1853 N N   . SER A 245 ? 1.1702 1.0618 0.8302 -0.0854 0.0007  -0.0322 272 SER A N   
1854 C CA  . SER A 245 ? 1.0377 0.9563 0.7231 -0.0714 0.0110  -0.0254 272 SER A CA  
1855 C C   . SER A 245 ? 1.2139 1.0910 0.8772 -0.0775 0.0221  -0.0171 272 SER A C   
1856 O O   . SER A 245 ? 1.2311 1.1268 0.9091 -0.0845 0.0347  -0.0174 272 SER A O   
1857 C CB  . SER A 245 ? 1.0494 0.9828 0.7475 -0.0362 0.0048  -0.0175 272 SER A CB  
1858 O OG  . SER A 245 ? 0.7993 0.7523 0.5208 -0.0229 0.0149  -0.0117 272 SER A OG  
1859 N N   . CYS A 246 ? 1.1530 0.9751 0.7802 -0.0736 0.0169  -0.0106 273 CYS A N   
1860 C CA  . CYS A 246 ? 1.2032 0.9845 0.8051 -0.0789 0.0241  -0.0030 273 CYS A CA  
1861 C C   . CYS A 246 ? 1.1972 0.9629 0.7813 -0.1128 0.0333  -0.0067 273 CYS A C   
1862 O O   . CYS A 246 ? 1.2754 1.0298 0.8488 -0.1209 0.0440  -0.0022 273 CYS A O   
1863 C CB  . CYS A 246 ? 1.0555 0.7850 0.6256 -0.0640 0.0144  0.0040  273 CYS A CB  
1864 S SG  . CYS A 246 ? 1.2929 1.0389 0.8818 -0.0275 0.0069  0.0084  273 CYS A SG  
1865 N N   . LYS A 247 ? 1.2391 1.0033 0.8184 -0.1341 0.0298  -0.0152 274 LYS A N   
1866 C CA  . LYS A 247 ? 1.2829 1.0348 0.8484 -0.1703 0.0412  -0.0191 274 LYS A CA  
1867 C C   . LYS A 247 ? 1.1117 0.9183 0.7113 -0.1810 0.0569  -0.0238 274 LYS A C   
1868 O O   . LYS A 247 ? 1.3093 1.1008 0.8925 -0.1971 0.0714  -0.0197 274 LYS A O   
1869 C CB  . LYS A 247 ? 1.2268 0.9746 0.7891 -0.1919 0.0343  -0.0304 274 LYS A CB  
1870 C CG  . LYS A 247 ? 1.4902 1.2136 1.0331 -0.2330 0.0465  -0.0338 274 LYS A CG  
1871 C CD  . LYS A 247 ? 1.6834 1.3302 1.1725 -0.2378 0.0504  -0.0197 274 LYS A CD  
1872 C CE  . LYS A 247 ? 1.8915 1.5071 1.3559 -0.2805 0.0643  -0.0209 274 LYS A CE  
1873 N NZ  . LYS A 247 ? 1.9164 1.4582 1.3249 -0.2838 0.0692  -0.0045 274 LYS A NZ  
1874 N N   . GLN A 248 ? 1.1713 1.0416 0.8169 -0.1697 0.0542  -0.0324 275 GLN A N   
1875 C CA  . GLN A 248 ? 1.2142 1.1409 0.8973 -0.1745 0.0685  -0.0385 275 GLN A CA  
1876 C C   . GLN A 248 ? 1.1910 1.1092 0.8698 -0.1563 0.0774  -0.0296 275 GLN A C   
1877 O O   . GLN A 248 ? 1.1060 1.0462 0.7954 -0.1678 0.0941  -0.0330 275 GLN A O   
1878 C CB  . GLN A 248 ? 1.0493 1.0425 0.7809 -0.1589 0.0600  -0.0482 275 GLN A CB  
1879 C CG  . GLN A 248 ? 1.1433 1.1552 0.8839 -0.1787 0.0505  -0.0608 275 GLN A CG  
1880 C CD  . GLN A 248 ? 1.2290 1.2391 0.9652 -0.2218 0.0648  -0.0693 275 GLN A CD  
1881 O OE1 . GLN A 248 ? 1.2820 1.2429 0.9835 -0.2444 0.0628  -0.0691 275 GLN A OE1 
1882 N NE2 . GLN A 248 ? 1.3560 1.4187 1.1272 -0.2335 0.0808  -0.0770 275 GLN A NE2 
1883 N N   . ALA A 249 ? 1.1748 1.0633 0.8393 -0.1287 0.0672  -0.0197 276 ALA A N   
1884 C CA  . ALA A 249 ? 1.1522 1.0308 0.8128 -0.1124 0.0737  -0.0131 276 ALA A CA  
1885 C C   . ALA A 249 ? 1.1959 1.0207 0.8101 -0.1270 0.0793  -0.0060 276 ALA A C   
1886 O O   . ALA A 249 ? 1.1526 0.9696 0.7600 -0.1175 0.0849  -0.0026 276 ALA A O   
1887 C CB  . ALA A 249 ? 1.0563 0.9275 0.7236 -0.0790 0.0614  -0.0063 276 ALA A CB  
1888 N N   . GLU A 250 ? 1.2836 1.0696 0.8642 -0.1494 0.0772  -0.0041 277 GLU A N   
1889 C CA  . GLU A 250 ? 1.2332 0.9587 0.7620 -0.1609 0.0793  0.0053  277 GLU A CA  
1890 C C   . GLU A 250 ? 1.1315 0.8203 0.6404 -0.1328 0.0657  0.0145  277 GLU A C   
1891 O O   . GLU A 250 ? 1.3468 1.0000 0.8220 -0.1324 0.0669  0.0217  277 GLU A O   
1892 C CB  . GLU A 250 ? 1.2614 0.9949 0.7806 -0.1795 0.0989  0.0047  277 GLU A CB  
1893 C CG  . GLU A 250 ? 1.3518 1.1101 0.8812 -0.2143 0.1146  -0.0034 277 GLU A CG  
1894 C CD  . GLU A 250 ? 1.5020 1.2755 1.0252 -0.2318 0.1371  -0.0053 277 GLU A CD  
1895 O OE1 . GLU A 250 ? 1.8487 1.6145 1.3597 -0.2156 0.1393  -0.0014 277 GLU A OE1 
1896 O OE2 . GLU A 250 ? 1.3935 1.1883 0.9248 -0.2628 0.1532  -0.0120 277 GLU A OE2 
1897 N N   . VAL A 251 ? 0.9707 0.6697 0.4999 -0.1095 0.0528  0.0138  278 VAL A N   
1898 C CA  . VAL A 251 ? 1.1710 0.8410 0.6879 -0.0836 0.0402  0.0208  278 VAL A CA  
1899 C C   . VAL A 251 ? 1.3828 1.0034 0.8662 -0.0857 0.0285  0.0241  278 VAL A C   
1900 O O   . VAL A 251 ? 1.5156 1.1429 1.0066 -0.0903 0.0240  0.0187  278 VAL A O   
1901 C CB  . VAL A 251 ? 1.0777 0.7858 0.6348 -0.0574 0.0360  0.0188  278 VAL A CB  
1902 C CG1 . VAL A 251 ? 0.9773 0.6582 0.5248 -0.0336 0.0249  0.0247  278 VAL A CG1 
1903 C CG2 . VAL A 251 ? 1.1705 0.9206 0.7591 -0.0535 0.0475  0.0152  278 VAL A CG2 
1904 N N   . GLN A 252 ? 1.4435 1.0144 0.8890 -0.0811 0.0223  0.0319  279 GLN A N   
1905 C CA  . GLN A 252 ? 1.2987 0.8159 0.7090 -0.0802 0.0110  0.0353  279 GLN A CA  
1906 C C   . GLN A 252 ? 1.3783 0.8955 0.8017 -0.0498 -0.0020 0.0348  279 GLN A C   
1907 O O   . GLN A 252 ? 1.4733 1.0031 0.9106 -0.0290 -0.0050 0.0373  279 GLN A O   
1908 C CB  . GLN A 252 ? 1.3625 0.8242 0.7235 -0.0866 0.0092  0.0450  279 GLN A CB  
1909 C CG  . GLN A 252 ? 1.6279 1.0270 0.9488 -0.0860 -0.0020 0.0492  279 GLN A CG  
1910 C CD  . GLN A 252 ? 1.6685 1.0546 0.9809 -0.1141 0.0040  0.0440  279 GLN A CD  
1911 O OE1 . GLN A 252 ? 1.7610 1.1381 1.0568 -0.1436 0.0166  0.0460  279 GLN A OE1 
1912 N NE2 . GLN A 252 ? 1.6150 1.0015 0.9391 -0.1063 -0.0044 0.0362  279 GLN A NE2 
1913 N N   . MET A 253 ? 1.4484 0.9524 0.8675 -0.0484 -0.0087 0.0302  280 MET A N   
1914 C CA  . MET A 253 ? 1.4023 0.9037 0.8295 -0.0209 -0.0191 0.0288  280 MET A CA  
1915 C C   . MET A 253 ? 1.3724 0.8163 0.7628 -0.0093 -0.0299 0.0337  280 MET A C   
1916 O O   . MET A 253 ? 1.4770 0.8725 0.8295 -0.0250 -0.0318 0.0362  280 MET A O   
1917 C CB  . MET A 253 ? 1.2995 0.8137 0.7359 -0.0231 -0.0215 0.0199  280 MET A CB  
1918 C CG  . MET A 253 ? 1.4772 1.0524 0.9532 -0.0242 -0.0150 0.0154  280 MET A CG  
1919 S SD  . MET A 253 ? 2.1368 1.7243 1.6138 -0.0416 -0.0181 0.0032  280 MET A SD  
1920 C CE  . MET A 253 ? 1.5432 1.1058 0.9988 -0.0804 -0.0107 0.0019  280 MET A CE  
1921 N N   . TYR A 254 ? 1.3998 0.8487 0.8022 0.0185  -0.0369 0.0350  281 TYR A N   
1922 C CA  . TYR A 254 ? 1.2846 0.6865 0.6588 0.0353  -0.0492 0.0383  281 TYR A CA  
1923 C C   . TYR A 254 ? 1.3659 0.7731 0.7547 0.0604  -0.0553 0.0322  281 TYR A C   
1924 O O   . TYR A 254 ? 1.3238 0.7762 0.7475 0.0692  -0.0497 0.0283  281 TYR A O   
1925 C CB  . TYR A 254 ? 1.2849 0.6876 0.6582 0.0459  -0.0532 0.0446  281 TYR A CB  
1926 C CG  . TYR A 254 ? 1.4047 0.7850 0.7473 0.0241  -0.0492 0.0517  281 TYR A CG  
1927 C CD1 . TYR A 254 ? 1.4457 0.8635 0.8064 0.0068  -0.0360 0.0511  281 TYR A CD1 
1928 C CD2 . TYR A 254 ? 1.4369 0.7571 0.7303 0.0219  -0.0577 0.0591  281 TYR A CD2 
1929 C CE1 . TYR A 254 ? 1.3853 0.7844 0.7163 -0.0135 -0.0299 0.0568  281 TYR A CE1 
1930 C CE2 . TYR A 254 ? 1.6152 0.9126 0.8753 0.0012  -0.0522 0.0670  281 TYR A CE2 
1931 C CZ  . TYR A 254 ? 1.5520 0.8905 0.8311 -0.0172 -0.0374 0.0653  281 TYR A CZ  
1932 O OH  . TYR A 254 ? 1.6841 1.0011 0.9282 -0.0383 -0.0296 0.0725  281 TYR A OH  
1933 N N   . VAL A 255 ? 1.4915 0.8501 0.8510 0.0725  -0.0661 0.0316  282 VAL A N   
1934 C CA  . VAL A 255 ? 1.3448 0.7043 0.7151 0.1003  -0.0722 0.0253  282 VAL A CA  
1935 C C   . VAL A 255 ? 1.4822 0.8092 0.8362 0.1214  -0.0852 0.0293  282 VAL A C   
1936 O O   . VAL A 255 ? 1.4859 0.7630 0.8007 0.1142  -0.0923 0.0359  282 VAL A O   
1937 C CB  . VAL A 255 ? 1.4151 0.7485 0.7673 0.0975  -0.0733 0.0163  282 VAL A CB  
1938 C CG1 . VAL A 255 ? 1.3010 0.5667 0.6055 0.0833  -0.0797 0.0186  282 VAL A CG1 
1939 C CG2 . VAL A 255 ? 1.3277 0.6666 0.6920 0.1277  -0.0771 0.0084  282 VAL A CG2 
1940 N N   . CYS A 256 ? 1.3755 0.7320 0.7597 0.1472  -0.0881 0.0258  283 CYS A N   
1941 C CA  . CYS A 256 ? 1.4437 0.7806 0.8211 0.1709  -0.1022 0.0273  283 CYS A CA  
1942 C C   . CYS A 256 ? 1.4843 0.8139 0.8683 0.1978  -0.1070 0.0179  283 CYS A C   
1943 O O   . CYS A 256 ? 1.4230 0.7896 0.8364 0.2037  -0.0970 0.0105  283 CYS A O   
1944 C CB  . CYS A 256 ? 1.2881 0.6711 0.7007 0.1779  -0.1023 0.0289  283 CYS A CB  
1945 S SG  . CYS A 256 ? 1.7318 1.1324 1.1428 0.1487  -0.0938 0.0366  283 CYS A SG  
1946 N N   . ASN A 257 ? 1.4330 0.7128 0.7869 0.2149  -0.1219 0.0184  284 ASN A N   
1947 C CA  . ASN A 257 ? 1.4947 0.7646 0.8538 0.2443  -0.1275 0.0081  284 ASN A CA  
1948 C C   . ASN A 257 ? 1.5539 0.8190 0.9182 0.2735  -0.1444 0.0087  284 ASN A C   
1949 O O   . ASN A 257 ? 1.6152 0.8450 0.9638 0.2983  -0.1554 0.0036  284 ASN A O   
1950 C CB  . ASN A 257 ? 1.4858 0.6932 0.8016 0.2403  -0.1300 0.0044  284 ASN A CB  
1951 C CG  . ASN A 257 ? 1.7099 0.8485 0.9740 0.2304  -0.1414 0.0156  284 ASN A CG  
1952 O OD1 . ASN A 257 ? 1.6843 0.8219 0.9414 0.2283  -0.1484 0.0265  284 ASN A OD1 
1953 N ND2 . ASN A 257 ? 1.7202 0.7982 0.9450 0.2236  -0.1429 0.0128  284 ASN A ND2 
1954 N N   . LYS A 258 ? 1.4439 0.7452 0.8308 0.2720  -0.1474 0.0136  285 LYS A N   
1955 C CA  . LYS A 258 ? 1.4918 0.7916 0.8827 0.2981  -0.1664 0.0137  285 LYS A CA  
1956 C C   . LYS A 258 ? 1.4487 0.7829 0.8809 0.3301  -0.1685 0.0000  285 LYS A C   
1957 O O   . LYS A 258 ? 1.6005 0.9166 1.0271 0.3589  -0.1865 -0.0029 285 LYS A O   
1958 C CB  . LYS A 258 ? 1.5512 0.8870 0.9591 0.2867  -0.1684 0.0190  285 LYS A CB  
1959 C CG  . LYS A 258 ? 1.4394 0.7438 0.8063 0.2559  -0.1647 0.0315  285 LYS A CG  
1960 C CD  . LYS A 258 ? 1.3739 0.7115 0.7543 0.2465  -0.1668 0.0346  285 LYS A CD  
1961 C CE  . LYS A 258 ? 1.4965 0.7992 0.8310 0.2182  -0.1627 0.0467  285 LYS A CE  
1962 N NZ  . LYS A 258 ? 1.5394 0.8668 0.8778 0.2113  -0.1666 0.0488  285 LYS A NZ  
1963 N N   . GLU A 259 ? 1.4684 0.8516 0.9409 0.3265  -0.1499 -0.0082 286 GLU A N   
1964 C CA  . GLU A 259 ? 1.6192 1.0351 1.1293 0.3543  -0.1471 -0.0218 286 GLU A CA  
1965 C C   . GLU A 259 ? 1.4794 0.9159 1.0018 0.3451  -0.1248 -0.0276 286 GLU A C   
1966 O O   . GLU A 259 ? 1.3326 0.7615 0.8378 0.3185  -0.1140 -0.0214 286 GLU A O   
1967 C CB  . GLU A 259 ? 1.5163 0.9936 1.0799 0.3656  -0.1499 -0.0267 286 GLU A CB  
1968 C CG  . GLU A 259 ? 1.5326 1.0416 1.1126 0.3389  -0.1430 -0.0193 286 GLU A CG  
1969 C CD  . GLU A 259 ? 1.7144 1.2778 1.3446 0.3492  -0.1488 -0.0262 286 GLU A CD  
1970 O OE1 . GLU A 259 ? 1.5463 1.1549 1.2231 0.3632  -0.1396 -0.0372 286 GLU A OE1 
1971 O OE2 . GLU A 259 ? 1.6833 1.2452 1.3061 0.3423  -0.1620 -0.0215 286 GLU A OE2 
1972 N N   . GLU A 260 ? 1.5108 0.9747 1.0621 0.3685  -0.1183 -0.0402 287 GLU A N   
1973 C CA  . GLU A 260 ? 1.4771 0.9622 1.0376 0.3635  -0.0971 -0.0464 287 GLU A CA  
1974 C C   . GLU A 260 ? 1.4827 1.0227 1.0787 0.3432  -0.0797 -0.0405 287 GLU A C   
1975 O O   . GLU A 260 ? 1.4416 1.0266 1.0808 0.3484  -0.0777 -0.0418 287 GLU A O   
1976 C CB  . GLU A 260 ? 1.5726 1.0753 1.1552 0.3949  -0.0929 -0.0619 287 GLU A CB  
1977 C CG  . GLU A 260 ? 1.7432 1.2529 1.3193 0.3934  -0.0732 -0.0697 287 GLU A CG  
1978 C CD  . GLU A 260 ? 1.9468 1.4733 1.5429 0.4256  -0.0676 -0.0865 287 GLU A CD  
1979 O OE1 . GLU A 260 ? 1.9866 1.5679 1.6327 0.4379  -0.0606 -0.0912 287 GLU A OE1 
1980 O OE2 . GLU A 260 ? 1.9048 1.3905 1.4679 0.4381  -0.0696 -0.0965 287 GLU A OE2 
1981 N N   . TYR A 261 ? 1.5363 1.0719 1.1146 0.3202  -0.0679 -0.0347 288 TYR A N   
1982 C CA  . TYR A 261 ? 1.3164 0.8971 0.9231 0.3023  -0.0514 -0.0278 288 TYR A CA  
1983 C C   . TYR A 261 ? 1.2944 0.9035 0.9134 0.3069  -0.0312 -0.0326 288 TYR A C   
1984 O O   . TYR A 261 ? 1.3203 0.9748 0.9789 0.3111  -0.0171 -0.0330 288 TYR A O   
1985 C CB  . TYR A 261 ? 1.2874 0.8497 0.8692 0.2743  -0.0529 -0.0169 288 TYR A CB  
1986 C CG  . TYR A 261 ? 1.2465 0.7829 0.8133 0.2673  -0.0695 -0.0109 288 TYR A CG  
1987 C CD1 . TYR A 261 ? 1.2148 0.7792 0.8115 0.2679  -0.0730 -0.0085 288 TYR A CD1 
1988 C CD2 . TYR A 261 ? 1.2380 0.7205 0.7586 0.2590  -0.0811 -0.0080 288 TYR A CD2 
1989 C CE1 . TYR A 261 ? 1.2930 0.8334 0.8707 0.2623  -0.0886 -0.0033 288 TYR A CE1 
1990 C CE2 . TYR A 261 ? 1.3322 0.7884 0.8334 0.2524  -0.0947 -0.0009 288 TYR A CE2 
1991 C CZ  . TYR A 261 ? 1.3410 0.8268 0.8693 0.2550  -0.0988 0.0015  288 TYR A CZ  
1992 O OH  . TYR A 261 ? 1.4368 0.8961 0.9406 0.2491  -0.1126 0.0083  288 TYR A OH  
1993 N N   . GLY A 262 ? 1.2977 0.8797 0.8816 0.3054  -0.0293 -0.0365 289 GLY A N   
1994 C CA  . GLY A 262 ? 1.2046 0.8114 0.7923 0.3096  -0.0108 -0.0406 289 GLY A CA  
1995 C C   . GLY A 262 ? 1.3475 0.9173 0.8919 0.3120  -0.0139 -0.0497 289 GLY A C   
1996 O O   . GLY A 262 ? 1.3872 0.9096 0.9014 0.3122  -0.0297 -0.0540 289 GLY A O   
1997 N N   . PHE A 263 ? 1.3476 0.9374 0.8866 0.3131  0.0015  -0.0526 290 PHE A N   
1998 C CA  . PHE A 263 ? 1.3251 0.8862 0.8252 0.3184  0.0003  -0.0652 290 PHE A CA  
1999 C C   . PHE A 263 ? 1.3008 0.8732 0.7817 0.3006  0.0068  -0.0602 290 PHE A C   
2000 O O   . PHE A 263 ? 1.2641 0.8739 0.7654 0.2928  0.0185  -0.0480 290 PHE A O   
2001 C CB  . PHE A 263 ? 1.3312 0.9053 0.8391 0.3455  0.0118  -0.0793 290 PHE A CB  
2002 C CG  . PHE A 263 ? 1.4079 0.9682 0.9319 0.3672  0.0020  -0.0875 290 PHE A CG  
2003 C CD1 . PHE A 263 ? 1.3257 0.9198 0.8948 0.3728  0.0031  -0.0814 290 PHE A CD1 
2004 C CD2 . PHE A 263 ? 1.4826 0.9954 0.9766 0.3825  -0.0098 -0.1020 290 PHE A CD2 
2005 C CE1 . PHE A 263 ? 1.3353 0.9204 0.9201 0.3947  -0.0088 -0.0894 290 PHE A CE1 
2006 C CE2 . PHE A 263 ? 1.6012 1.1001 1.1090 0.4058  -0.0207 -0.1088 290 PHE A CE2 
2007 C CZ  . PHE A 263 ? 1.6116 1.1489 1.1653 0.4127  -0.0210 -0.1023 290 PHE A CZ  
2008 N N   . LEU A 264 ? 1.3965 0.9347 0.8376 0.2947  -0.0019 -0.0704 291 LEU A N   
2009 C CA  . LEU A 264 ? 1.2820 0.8265 0.7027 0.2756  -0.0025 -0.0674 291 LEU A CA  
2010 C C   . LEU A 264 ? 1.4678 0.9927 0.8504 0.2823  -0.0033 -0.0853 291 LEU A C   
2011 O O   . LEU A 264 ? 1.6215 1.1040 0.9834 0.2901  -0.0121 -0.0999 291 LEU A O   
2012 C CB  . LEU A 264 ? 1.2753 0.7959 0.6886 0.2512  -0.0175 -0.0615 291 LEU A CB  
2013 C CG  . LEU A 264 ? 1.3654 0.9140 0.7881 0.2296  -0.0168 -0.0488 291 LEU A CG  
2014 C CD1 . LEU A 264 ? 1.2667 0.7888 0.6837 0.2077  -0.0296 -0.0455 291 LEU A CD1 
2015 C CD2 . LEU A 264 ? 1.8037 1.3656 1.2038 0.2252  -0.0155 -0.0549 291 LEU A CD2 
2016 N N   . PRO A 265 ? 1.5443 1.0958 0.9143 0.2809  0.0050  -0.0853 292 PRO A N   
2017 C CA  . PRO A 265 ? 1.4241 0.9558 0.7532 0.2842  0.0014  -0.1042 292 PRO A CA  
2018 C C   . PRO A 265 ? 1.4338 0.9404 0.7399 0.2593  -0.0164 -0.1096 292 PRO A C   
2019 O O   . PRO A 265 ? 1.4610 0.9851 0.7808 0.2400  -0.0212 -0.0966 292 PRO A O   
2020 C CB  . PRO A 265 ? 1.2587 0.8325 0.5828 0.2921  0.0169  -0.0991 292 PRO A CB  
2021 C CG  . PRO A 265 ? 1.2753 0.8832 0.6306 0.2812  0.0217  -0.0760 292 PRO A CG  
2022 C CD  . PRO A 265 ? 1.4677 1.0664 0.8575 0.2792  0.0187  -0.0686 292 PRO A CD  
2023 N N   . VAL A 266 ? 1.3795 0.8447 0.6523 0.2596  -0.0256 -0.1303 293 VAL A N   
2024 C CA  . VAL A 266 ? 1.4555 0.8957 0.7066 0.2333  -0.0416 -0.1387 293 VAL A CA  
2025 C C   . VAL A 266 ? 1.3853 0.8637 0.6248 0.2243  -0.0426 -0.1401 293 VAL A C   
2026 O O   . VAL A 266 ? 1.5314 1.0257 0.7519 0.2409  -0.0351 -0.1483 293 VAL A O   
2027 C CB  . VAL A 266 ? 1.5008 0.8819 0.7181 0.2358  -0.0504 -0.1619 293 VAL A CB  
2028 C CG1 . VAL A 266 ? 1.4254 0.7788 0.6242 0.2043  -0.0658 -0.1704 293 VAL A CG1 
2029 C CG2 . VAL A 266 ? 1.5273 0.8713 0.7544 0.2516  -0.0500 -0.1596 293 VAL A CG2 
2030 N N   . PRO A 267 ? 1.5031 0.9990 0.7525 0.2001  -0.0516 -0.1324 294 PRO A N   
2031 C CA  . PRO A 267 ? 1.4433 0.9783 0.6829 0.1940  -0.0556 -0.1338 294 PRO A CA  
2032 C C   . PRO A 267 ? 1.5592 1.0761 0.7575 0.1937  -0.0645 -0.1599 294 PRO A C   
2033 O O   . PRO A 267 ? 1.5516 1.0203 0.7301 0.1884  -0.0712 -0.1784 294 PRO A O   
2034 C CB  . PRO A 267 ? 1.3303 0.8790 0.5912 0.1665  -0.0657 -0.1255 294 PRO A CB  
2035 C CG  . PRO A 267 ? 1.3217 0.8563 0.6107 0.1650  -0.0596 -0.1098 294 PRO A CG  
2036 C CD  . PRO A 267 ? 1.4152 0.9030 0.6889 0.1800  -0.0567 -0.1197 294 PRO A CD  
2037 N N   . LEU A 268 ? 1.3851 0.9393 0.5680 0.1999  -0.0651 -0.1613 295 LEU A N   
2038 C CA  . LEU A 268 ? 1.5462 1.0916 0.6869 0.2024  -0.0734 -0.1862 295 LEU A CA  
2039 C C   . LEU A 268 ? 1.6712 1.2391 0.8070 0.1787  -0.0928 -0.1948 295 LEU A C   
2040 O O   . LEU A 268 ? 1.6013 1.2006 0.7671 0.1653  -0.0972 -0.1790 295 LEU A O   
2041 C CB  . LEU A 268 ? 1.6893 1.2601 0.8088 0.2301  -0.0593 -0.1831 295 LEU A CB  
2042 C CG  . LEU A 268 ? 1.5817 1.1369 0.7046 0.2550  -0.0387 -0.1801 295 LEU A CG  
2043 C CD1 . LEU A 268 ? 1.6216 1.2145 0.7340 0.2769  -0.0209 -0.1679 295 LEU A CD1 
2044 C CD2 . LEU A 268 ? 1.5240 1.0305 0.6172 0.2615  -0.0415 -0.2088 295 LEU A CD2 
2045 N N   . ARG A 269 ? 1.6062 1.1595 0.7049 0.1743  -0.1047 -0.2222 296 ARG A N   
2046 C CA  . ARG A 269 ? 1.5225 1.0996 0.6160 0.1516  -0.1253 -0.2357 296 ARG A CA  
2047 C C   . ARG A 269 ? 1.5801 1.2191 0.6765 0.1629  -0.1278 -0.2200 296 ARG A C   
2048 O O   . ARG A 269 ? 1.5910 1.2477 0.6826 0.1883  -0.1126 -0.2018 296 ARG A O   
2049 C CB  . ARG A 269 ? 1.8143 1.3617 0.8645 0.1464  -0.1374 -0.2708 296 ARG A CB  
2050 C CG  . ARG A 269 ? 1.8305 1.3145 0.8766 0.1264  -0.1417 -0.2901 296 ARG A CG  
2051 C CD  . ARG A 269 ? 2.0284 1.4954 1.0379 0.1121  -0.1590 -0.3263 296 ARG A CD  
2052 N NE  . ARG A 269 ? 2.1730 1.5707 1.1529 0.1162  -0.1556 -0.3490 296 ARG A NE  
2053 C CZ  . ARG A 269 ? 2.3919 1.7666 1.3304 0.1156  -0.1650 -0.3822 296 ARG A CZ  
2054 N NH1 . ARG A 269 ? 2.3156 1.7350 1.2383 0.1108  -0.1788 -0.3961 296 ARG A NH1 
2055 N NH2 . ARG A 269 ? 2.3835 1.6949 1.3050 0.1198  -0.1596 -0.3993 296 ARG A NH2 
2056 N N   . ALA A 270 ? 1.4722 1.1438 0.5763 0.1434  -0.1473 -0.2277 297 ALA A N   
2057 C CA  . ALA A 270 ? 1.5768 1.3068 0.6849 0.1545  -0.1535 -0.2127 297 ALA A CA  
2058 C C   . ALA A 270 ? 1.7003 1.4415 0.7594 0.1803  -0.1529 -0.2182 297 ALA A C   
2059 O O   . ALA A 270 ? 1.5621 1.3394 0.6171 0.1998  -0.1488 -0.1970 297 ALA A O   
2060 C CB  . ALA A 270 ? 1.4096 1.1744 0.5371 0.1288  -0.1770 -0.2247 297 ALA A CB  
2061 N N   . HIS A 271 ? 1.5084 1.2165 0.5272 0.1812  -0.1561 -0.2461 298 HIS A N   
2062 C CA  . HIS A 271 ? 1.7570 1.4742 0.7234 0.2046  -0.1553 -0.2548 298 HIS A CA  
2063 C C   . HIS A 271 ? 1.7451 1.4286 0.6906 0.2280  -0.1295 -0.2517 298 HIS A C   
2064 O O   . HIS A 271 ? 1.7166 1.3991 0.6334 0.2387  -0.1242 -0.2635 298 HIS A O   
2065 C CB  . HIS A 271 ? 1.8197 1.5344 0.7574 0.1889  -0.1782 -0.2908 298 HIS A CB  
2066 C CG  . HIS A 271 ? 1.7543 1.5150 0.7062 0.1713  -0.2052 -0.2960 298 HIS A CG  
2067 N ND1 . HIS A 271 ? 1.8109 1.5867 0.7492 0.1546  -0.2271 -0.3246 298 HIS A ND1 
2068 C CD2 . HIS A 271 ? 1.5583 1.3597 0.5516 0.1653  -0.2112 -0.2743 298 HIS A CD2 
2069 C CE1 . HIS A 271 ? 1.8361 1.6595 0.7973 0.1422  -0.2489 -0.3238 298 HIS A CE1 
2070 N NE2 . HIS A 271 ? 1.6248 1.4645 0.6195 0.1493  -0.2394 -0.2934 298 HIS A NE2 
2071 N N   . SER A 272 ? 1.6726 1.3387 0.6543 0.2309  -0.1105 -0.2323 299 SER A N   
2072 C CA  . SER A 272 ? 1.7169 1.3643 0.6878 0.2553  -0.0847 -0.2256 299 SER A CA  
2073 C C   . SER A 272 ? 1.8000 1.4860 0.7623 0.2772  -0.0692 -0.1988 299 SER A C   
2074 O O   . SER A 272 ? 1.8691 1.5919 0.8379 0.2748  -0.0786 -0.1818 299 SER A O   
2075 C CB  . SER A 272 ? 1.7961 1.4151 0.8100 0.2512  -0.0722 -0.2150 299 SER A CB  
2076 O OG  . SER A 272 ? 1.8477 1.4190 0.8572 0.2370  -0.0819 -0.2403 299 SER A OG  
2077 N N   . THR A 273 ? 1.6985 1.3761 0.6498 0.2981  -0.0443 -0.1942 300 THR A N   
2078 C CA  . THR A 273 ? 1.6945 1.4045 0.6400 0.3152  -0.0254 -0.1693 300 THR A CA  
2079 C C   . THR A 273 ? 1.6060 1.3175 0.5818 0.3255  -0.0014 -0.1431 300 THR A C   
2080 O O   . THR A 273 ? 1.5764 1.2677 0.5918 0.3182  0.0023  -0.1443 300 THR A O   
2081 C CB  . THR A 273 ? 1.5804 1.2871 0.4944 0.3282  -0.0121 -0.1833 300 THR A CB  
2082 O OG1 . THR A 273 ? 1.6303 1.3125 0.5552 0.3402  0.0103  -0.1890 300 THR A OG1 
2083 C CG2 . THR A 273 ? 1.7487 1.4436 0.6356 0.3161  -0.0350 -0.2159 300 THR A CG2 
2084 N N   . LEU A 274 ? 1.3254 1.2027 0.7702 0.2441  0.0697  -0.0337 301 LEU A N   
2085 C CA  . LEU A 274 ? 1.3381 1.1989 0.7785 0.2337  0.0755  -0.0130 301 LEU A CA  
2086 C C   . LEU A 274 ? 1.2147 1.0768 0.6624 0.2238  0.0871  0.0000  301 LEU A C   
2087 O O   . LEU A 274 ? 1.4000 1.2601 0.8613 0.2105  0.0912  0.0084  301 LEU A O   
2088 C CB  . LEU A 274 ? 1.1601 1.0002 0.5691 0.2458  0.0733  -0.0030 301 LEU A CB  
2089 C CG  . LEU A 274 ? 1.3273 1.1628 0.7264 0.2584  0.0597  -0.0144 301 LEU A CG  
2090 C CD1 . LEU A 274 ? 1.4576 1.2662 0.8146 0.2765  0.0581  -0.0041 301 LEU A CD1 
2091 C CD2 . LEU A 274 ? 1.1623 0.9962 0.5808 0.2437  0.0587  -0.0139 301 LEU A CD2 
2092 N N   . GLN A 275 ? 1.2661 1.1333 0.7058 0.2312  0.0916  -0.0001 302 GLN A N   
2093 C CA  . GLN A 275 ? 1.2535 1.1248 0.7031 0.2231  0.1022  0.0093  302 GLN A CA  
2094 C C   . GLN A 275 ? 1.3122 1.1944 0.7871 0.2136  0.1024  0.0036  302 GLN A C   
2095 O O   . GLN A 275 ? 1.3784 1.2622 0.8653 0.2056  0.1072  0.0117  302 GLN A O   
2096 C CB  . GLN A 275 ? 1.2507 1.1252 0.6862 0.2332  0.1074  0.0084  302 GLN A CB  
2097 C CG  . GLN A 275 ? 1.3883 1.2674 0.8344 0.2254  0.1194  0.0171  302 GLN A CG  
2098 C CD  . GLN A 275 ? 1.5790 1.4642 1.0154 0.2341  0.1248  0.0132  302 GLN A CD  
2099 O OE1 . GLN A 275 ? 1.6364 1.5264 1.0624 0.2458  0.1182  0.0019  302 GLN A OE1 
2100 N NE2 . GLN A 275 ? 1.5589 1.4464 1.0010 0.2285  0.1368  0.0200  302 GLN A NE2 
2101 N N   . ASP A 276 ? 1.3356 1.2236 0.8176 0.2151  0.0979  -0.0118 303 ASP A N   
2102 C CA  . ASP A 276 ? 1.3806 1.2683 0.8785 0.2058  0.1007  -0.0164 303 ASP A CA  
2103 C C   . ASP A 276 ? 1.3331 1.2108 0.8349 0.1960  0.0987  -0.0073 303 ASP A C   
2104 O O   . ASP A 276 ? 1.2941 1.1687 0.8021 0.1910  0.1011  -0.0008 303 ASP A O   
2105 C CB  . ASP A 276 ? 1.3414 1.2332 0.8456 0.2064  0.1000  -0.0373 303 ASP A CB  
2106 C CG  . ASP A 276 ? 1.4466 1.3510 0.9521 0.2147  0.1030  -0.0494 303 ASP A CG  
2107 O OD1 . ASP A 276 ? 1.3932 1.3000 0.8969 0.2170  0.1079  -0.0405 303 ASP A OD1 
2108 O OD2 . ASP A 276 ? 1.4597 1.3738 0.9703 0.2188  0.1004  -0.0701 303 ASP A OD2 
2109 N N   . GLU A 277 ? 1.2350 1.1077 0.7323 0.1949  0.0932  -0.0081 304 GLU A N   
2110 C CA  . GLU A 277 ? 1.3266 1.1908 0.8276 0.1854  0.0913  -0.0005 304 GLU A CA  
2111 C C   . GLU A 277 ? 1.2747 1.1398 0.7779 0.1825  0.0940  0.0142  304 GLU A C   
2112 O O   . GLU A 277 ? 1.1320 0.9959 0.6435 0.1760  0.0932  0.0183  304 GLU A O   
2113 C CB  . GLU A 277 ? 1.3841 1.2434 0.8801 0.1860  0.0852  -0.0047 304 GLU A CB  
2114 C CG  . GLU A 277 ? 1.1957 1.0467 0.6967 0.1753  0.0833  0.0001  304 GLU A CG  
2115 C CD  . GLU A 277 ? 1.4062 1.2520 0.9131 0.1675  0.0849  -0.0094 304 GLU A CD  
2116 O OE1 . GLU A 277 ? 1.3319 1.1799 0.8414 0.1689  0.0866  -0.0253 304 GLU A OE1 
2117 O OE2 . GLU A 277 ? 1.6069 1.4452 1.1148 0.1603  0.0854  -0.0027 304 GLU A OE2 
2118 N N   . ALA A 278 ? 1.1586 1.0251 0.6537 0.1877  0.0981  0.0201  305 ALA A N   
2119 C CA  . ALA A 278 ? 1.2999 1.1683 0.8008 0.1825  0.1046  0.0301  305 ALA A CA  
2120 C C   . ALA A 278 ? 1.3601 1.2408 0.8767 0.1815  0.1065  0.0292  305 ALA A C   
2121 O O   . ALA A 278 ? 1.3471 1.2338 0.8781 0.1758  0.1062  0.0314  305 ALA A O   
2122 C CB  . ALA A 278 ? 1.1364 0.9976 0.6202 0.1878  0.1127  0.0357  305 ALA A CB  
2123 N N   . GLU A 279 ? 1.2241 1.1097 0.7389 0.1882  0.1078  0.0241  306 GLU A N   
2124 C CA  . GLU A 279 ? 1.2563 1.1511 0.7838 0.1897  0.1092  0.0228  306 GLU A CA  
2125 C C   . GLU A 279 ? 1.2583 1.1462 0.7886 0.1887  0.1029  0.0200  306 GLU A C   
2126 O O   . GLU A 279 ? 1.3770 1.2693 0.9162 0.1909  0.1006  0.0206  306 GLU A O   
2127 C CB  . GLU A 279 ? 1.3403 1.2404 0.8637 0.1971  0.1142  0.0182  306 GLU A CB  
2128 C CG  . GLU A 279 ? 1.4159 1.3190 0.9311 0.1994  0.1221  0.0219  306 GLU A CG  
2129 C CD  . GLU A 279 ? 1.4738 1.3835 0.9845 0.2072  0.1266  0.0165  306 GLU A CD  
2130 O OE1 . GLU A 279 ? 1.2523 1.1646 0.7681 0.2102  0.1240  0.0088  306 GLU A OE1 
2131 O OE2 . GLU A 279 ? 1.4621 1.3717 0.9623 0.2098  0.1345  0.0195  306 GLU A OE2 
2132 N N   . SER A 280 ? 1.3024 1.1780 0.8236 0.1863  0.1003  0.0155  307 SER A N   
2133 C CA  . SER A 280 ? 1.1563 1.0177 0.6732 0.1842  0.0975  0.0134  307 SER A CA  
2134 C C   . SER A 280 ? 1.2471 1.1083 0.7683 0.1806  0.0908  0.0194  307 SER A C   
2135 O O   . SER A 280 ? 1.3360 1.1897 0.8536 0.1841  0.0867  0.0201  307 SER A O   
2136 C CB  . SER A 280 ? 1.0794 0.9282 0.5880 0.1799  0.0995  0.0043  307 SER A CB  
2137 O OG  . SER A 280 ? 1.2766 1.1056 0.7761 0.1758  0.0997  0.0031  307 SER A OG  
2138 N N   . PHE A 281 ? 1.3838 1.2515 0.9105 0.1749  0.0897  0.0229  308 PHE A N   
2139 C CA  . PHE A 281 ? 1.3962 1.2675 0.9311 0.1705  0.0843  0.0259  308 PHE A CA  
2140 C C   . PHE A 281 ? 1.3480 1.2375 0.8998 0.1739  0.0839  0.0260  308 PHE A C   
2141 O O   . PHE A 281 ? 1.3111 1.2064 0.8712 0.1749  0.0765  0.0238  308 PHE A O   
2142 C CB  . PHE A 281 ? 1.2909 1.1616 0.8274 0.1626  0.0855  0.0284  308 PHE A CB  
2143 C CG  . PHE A 281 ? 1.2854 1.1619 0.8336 0.1565  0.0816  0.0292  308 PHE A CG  
2144 C CD1 . PHE A 281 ? 1.3161 1.1832 0.8589 0.1535  0.0744  0.0274  308 PHE A CD1 
2145 C CD2 . PHE A 281 ? 1.1581 1.0496 0.7234 0.1529  0.0865  0.0296  308 PHE A CD2 
2146 C CE1 . PHE A 281 ? 1.1291 1.0040 0.6836 0.1487  0.0696  0.0261  308 PHE A CE1 
2147 C CE2 . PHE A 281 ? 1.2567 1.1573 0.8374 0.1465  0.0835  0.0263  308 PHE A CE2 
2148 C CZ  . PHE A 281 ? 1.0986 0.9921 0.6740 0.1452  0.0737  0.0246  308 PHE A CZ  
2149 N N   . MET A 282 ? 1.4001 1.3002 0.9581 0.1761  0.0915  0.0263  309 MET A N   
2150 C CA  . MET A 282 ? 1.3119 1.2314 0.8895 0.1791  0.0926  0.0227  309 MET A CA  
2151 C C   . MET A 282 ? 1.3289 1.2479 0.9058 0.1901  0.0832  0.0188  309 MET A C   
2152 O O   . MET A 282 ? 1.2229 1.1572 0.8161 0.1946  0.0763  0.0130  309 MET A O   
2153 C CB  . MET A 282 ? 1.0598 0.9862 0.6393 0.1796  0.1042  0.0233  309 MET A CB  
2154 C CG  . MET A 282 ? 1.1989 1.1469 0.8013 0.1823  0.1073  0.0167  309 MET A CG  
2155 S SD  . MET A 282 ? 1.5390 1.4895 1.1363 0.1899  0.1151  0.0158  309 MET A SD  
2156 C CE  . MET A 282 ? 1.3926 1.3254 0.9714 0.1997  0.1050  0.0165  309 MET A CE  
2157 N N   . HIS A 283 ? 1.2711 1.1714 0.8284 0.1955  0.0833  0.0202  310 HIS A N   
2158 C CA  . HIS A 283 ? 1.2769 1.1660 0.8243 0.2071  0.0766  0.0180  310 HIS A CA  
2159 C C   . HIS A 283 ? 1.3477 1.2263 0.8863 0.2097  0.0654  0.0180  310 HIS A C   
2160 O O   . HIS A 283 ? 1.3561 1.2318 0.8899 0.2229  0.0559  0.0152  310 HIS A O   
2161 C CB  . HIS A 283 ? 1.2486 1.1145 0.7752 0.2091  0.0836  0.0182  310 HIS A CB  
2162 C CG  . HIS A 283 ? 1.2186 1.0638 0.7281 0.2215  0.0806  0.0172  310 HIS A CG  
2163 N ND1 . HIS A 283 ? 1.3335 1.1460 0.8157 0.2231  0.0795  0.0186  310 HIS A ND1 
2164 C CD2 . HIS A 283 ? 1.2525 1.1008 0.7646 0.2340  0.0793  0.0150  310 HIS A CD2 
2165 C CE1 . HIS A 283 ? 1.5270 1.3193 0.9914 0.2370  0.0781  0.0185  310 HIS A CE1 
2166 N NE2 . HIS A 283 ? 1.5428 1.3577 1.0264 0.2444  0.0769  0.0161  310 HIS A NE2 
2167 N N   . VAL A 284 ? 1.2881 1.1602 0.8223 0.1992  0.0654  0.0203  311 VAL A N   
2168 C CA  . VAL A 284 ? 1.3692 1.2345 0.8966 0.2007  0.0548  0.0194  311 VAL A CA  
2169 C C   . VAL A 284 ? 1.3182 1.2135 0.8723 0.2047  0.0458  0.0128  311 VAL A C   
2170 O O   . VAL A 284 ? 1.2203 1.1153 0.7697 0.2163  0.0327  0.0081  311 VAL A O   
2171 C CB  . VAL A 284 ? 1.2982 1.1534 0.8196 0.1872  0.0579  0.0219  311 VAL A CB  
2172 C CG1 . VAL A 284 ? 1.1045 0.9570 0.6220 0.1878  0.0471  0.0200  311 VAL A CG1 
2173 C CG2 . VAL A 284 ? 1.3871 1.2147 0.8853 0.1840  0.0661  0.0228  311 VAL A CG2 
2174 N N   . GLN A 285 ? 1.2712 1.1918 0.8527 0.1957  0.0535  0.0105  312 GLN A N   
2175 C CA  . GLN A 285 ? 1.1830 1.1352 0.7963 0.1967  0.0491  -0.0004 312 GLN A CA  
2176 C C   . GLN A 285 ? 1.2388 1.2037 0.8602 0.2134  0.0412  -0.0083 312 GLN A C   
2177 O O   . GLN A 285 ? 1.2389 1.2241 0.8775 0.2228  0.0284  -0.0206 312 GLN A O   
2178 C CB  . GLN A 285 ? 1.1382 1.1069 0.7741 0.1819  0.0647  -0.0013 312 GLN A CB  
2179 C CG  . GLN A 285 ? 1.3125 1.2655 0.9374 0.1681  0.0727  0.0068  312 GLN A CG  
2180 C CD  . GLN A 285 ? 1.2130 1.1751 0.8536 0.1556  0.0894  0.0061  312 GLN A CD  
2181 O OE1 . GLN A 285 ? 1.2252 1.1726 0.8499 0.1526  0.1004  0.0145  312 GLN A OE1 
2182 N NE2 . GLN A 285 ? 1.1691 1.1535 0.8392 0.1488  0.0923  -0.0054 312 GLN A NE2 
2183 N N   . LEU A 286 ? 1.2679 1.2229 0.8786 0.2184  0.0479  -0.0034 313 LEU A N   
2184 C CA  . LEU A 286 ? 1.1914 1.1540 0.8064 0.2359  0.0404  -0.0103 313 LEU A CA  
2185 C C   . LEU A 286 ? 1.2865 1.2266 0.8739 0.2542  0.0238  -0.0104 313 LEU A C   
2186 O O   . LEU A 286 ? 1.4547 1.4099 1.0520 0.2714  0.0092  -0.0214 313 LEU A O   
2187 C CB  . LEU A 286 ? 1.1725 1.1243 0.7778 0.2366  0.0523  -0.0045 313 LEU A CB  
2188 C CG  . LEU A 286 ? 1.0777 1.0452 0.7004 0.2225  0.0689  -0.0035 313 LEU A CG  
2189 C CD1 . LEU A 286 ? 1.1775 1.1327 0.7864 0.2262  0.0776  0.0008  313 LEU A CD1 
2190 C CD2 . LEU A 286 ? 1.0746 1.0777 0.7351 0.2201  0.0714  -0.0161 313 LEU A CD2 
2191 N N   . GLU A 287 ? 1.3028 1.2054 0.8539 0.2518  0.0261  0.0003  314 GLU A N   
2192 C CA  . GLU A 287 ? 1.3291 1.1999 0.8439 0.2684  0.0139  0.0019  314 GLU A CA  
2193 C C   . GLU A 287 ? 1.3231 1.2106 0.8466 0.2753  -0.0036 -0.0069 314 GLU A C   
2194 O O   . GLU A 287 ? 1.4339 1.3109 0.9382 0.2977  -0.0200 -0.0117 314 GLU A O   
2195 C CB  . GLU A 287 ? 1.3350 1.1631 0.8126 0.2592  0.0248  0.0126  314 GLU A CB  
2196 C CG  . GLU A 287 ? 1.2438 1.0471 0.7039 0.2589  0.0394  0.0173  314 GLU A CG  
2197 C CD  . GLU A 287 ? 1.5700 1.3466 1.0024 0.2814  0.0340  0.0172  314 GLU A CD  
2198 O OE1 . GLU A 287 ? 1.5567 1.3575 1.0093 0.2942  0.0263  0.0114  314 GLU A OE1 
2199 O OE2 . GLU A 287 ? 1.5679 1.2968 0.9567 0.2864  0.0388  0.0223  314 GLU A OE2 
2200 N N   . VAL A 288 ? 1.3532 1.2650 0.9035 0.2578  -0.0007 -0.0100 315 VAL A N   
2201 C CA  . VAL A 288 ? 1.3895 1.3235 0.9555 0.2623  -0.0162 -0.0219 315 VAL A CA  
2202 C C   . VAL A 288 ? 1.4299 1.4026 1.0291 0.2780  -0.0289 -0.0401 315 VAL A C   
2203 O O   . VAL A 288 ? 1.4392 1.4190 1.0343 0.2978  -0.0496 -0.0518 315 VAL A O   
2204 C CB  . VAL A 288 ? 1.2961 1.2477 0.8871 0.2382  -0.0065 -0.0225 315 VAL A CB  
2205 C CG1 . VAL A 288 ? 1.3816 1.3743 1.0112 0.2390  -0.0172 -0.0415 315 VAL A CG1 
2206 C CG2 . VAL A 288 ? 1.2657 1.1829 0.8234 0.2300  -0.0040 -0.0113 315 VAL A CG2 
2207 N N   . MET A 289 ? 1.3088 1.3069 0.9404 0.2709  -0.0173 -0.0445 316 MET A N   
2208 C CA  . MET A 289 ? 1.3221 1.3628 0.9941 0.2821  -0.0261 -0.0656 316 MET A CA  
2209 C C   . MET A 289 ? 1.4071 1.4371 1.0594 0.3120  -0.0425 -0.0694 316 MET A C   
2210 O O   . MET A 289 ? 1.3941 1.4604 1.0807 0.3243  -0.0514 -0.0890 316 MET A O   
2211 C CB  . MET A 289 ? 1.1080 1.1744 0.8171 0.2634  -0.0050 -0.0690 316 MET A CB  
2212 C CG  . MET A 289 ? 1.2346 1.3159 0.9682 0.2373  0.0102  -0.0708 316 MET A CG  
2213 S SD  . MET A 289 ? 1.4378 1.5379 1.2028 0.2171  0.0379  -0.0733 316 MET A SD  
2214 C CE  . MET A 289 ? 1.1982 1.2610 0.9219 0.2224  0.0451  -0.0510 316 MET A CE  
2215 N N   . VAL A 290 ? 1.3894 1.3692 0.9876 0.3241  -0.0454 -0.0530 317 VAL A N   
2216 C CA  . VAL A 290 ? 1.3831 1.3437 0.9540 0.3552  -0.0608 -0.0556 317 VAL A CA  
2217 C C   . VAL A 290 ? 1.4769 1.4469 1.0416 0.3803  -0.0887 -0.0709 317 VAL A C   
2218 O O   . VAL A 290 ? 1.5963 1.5986 1.1861 0.4019  -0.1062 -0.0910 317 VAL A O   
2219 C CB  . VAL A 290 ? 1.4625 1.3603 0.9743 0.3584  -0.0507 -0.0343 317 VAL A CB  
2220 C CG1 . VAL A 290 ? 1.3605 1.2287 0.8354 0.3924  -0.0656 -0.0357 317 VAL A CG1 
2221 C CG2 . VAL A 290 ? 1.2722 1.1677 0.7948 0.3367  -0.0260 -0.0242 317 VAL A CG2 
2222 N N   . LYS A 291 ? 1.5261 1.4699 1.0581 0.3788  -0.0939 -0.0636 318 LYS A N   
2223 C CA  . LYS A 291 ? 1.4246 1.3714 0.9415 0.4044  -0.1213 -0.0771 318 LYS A CA  
2224 C C   . LYS A 291 ? 1.4527 1.4416 1.0094 0.3885  -0.1260 -0.0917 318 LYS A C   
2225 O O   . LYS A 291 ? 1.6863 1.6824 1.2337 0.4083  -0.1493 -0.1053 318 LYS A O   
2226 C CB  . LYS A 291 ? 1.5250 1.4013 0.9633 0.4201  -0.1251 -0.0590 318 LYS A CB  
2227 C CG  . LYS A 291 ? 1.7233 1.5512 1.1149 0.4412  -0.1223 -0.0474 318 LYS A CG  
2228 C CD  . LYS A 291 ? 1.9538 1.7056 1.2637 0.4543  -0.1214 -0.0306 318 LYS A CD  
2229 C CE  . LYS A 291 ? 2.1946 1.8920 1.4544 0.4761  -0.1163 -0.0201 318 LYS A CE  
2230 N NZ  . LYS A 291 ? 2.2272 1.9441 1.4930 0.5140  -0.1429 -0.0361 318 LYS A NZ  
2231 N N   . HIS A 292 ? 1.4176 1.4319 1.0154 0.3551  -0.1046 -0.0900 319 HIS A N   
2232 C CA  . HIS A 292 ? 1.3279 1.3780 0.9637 0.3368  -0.1043 -0.1030 319 HIS A CA  
2233 C C   . HIS A 292 ? 1.3614 1.4620 1.0628 0.3156  -0.0884 -0.1177 319 HIS A C   
2234 O O   . HIS A 292 ? 1.2519 1.3507 0.9613 0.3082  -0.0724 -0.1101 319 HIS A O   
2235 C CB  . HIS A 292 ? 1.2495 1.2649 0.8571 0.3141  -0.0897 -0.0827 319 HIS A CB  
2236 C CG  . HIS A 292 ? 1.4704 1.4269 1.0095 0.3288  -0.0961 -0.0655 319 HIS A CG  
2237 N ND1 . HIS A 292 ? 1.6044 1.5142 1.1038 0.3263  -0.0811 -0.0447 319 HIS A ND1 
2238 C CD2 . HIS A 292 ? 1.6126 1.5470 1.1140 0.3453  -0.1137 -0.0674 319 HIS A CD2 
2239 C CE1 . HIS A 292 ? 1.5849 1.4443 1.0257 0.3390  -0.0867 -0.0346 319 HIS A CE1 
2240 N NE2 . HIS A 292 ? 1.7002 1.5714 1.1380 0.3514  -0.1067 -0.0468 319 HIS A NE2 
2241 N N   . PRO A 293 ? 1.2847 1.4293 1.0328 0.3051  -0.0906 -0.1400 320 PRO A N   
2242 C CA  . PRO A 293 ? 1.1324 1.3162 0.9382 0.2794  -0.0684 -0.1527 320 PRO A CA  
2243 C C   . PRO A 293 ? 1.2786 1.4320 1.0691 0.2509  -0.0399 -0.1270 320 PRO A C   
2244 O O   . PRO A 293 ? 1.3608 1.4724 1.1066 0.2481  -0.0390 -0.1046 320 PRO A O   
2245 C CB  . PRO A 293 ? 1.1505 1.3769 0.9993 0.2732  -0.0758 -0.1806 320 PRO A CB  
2246 C CG  . PRO A 293 ? 1.1488 1.3742 0.9731 0.3061  -0.1098 -0.1912 320 PRO A CG  
2247 C CD  . PRO A 293 ? 1.1715 1.3329 0.9225 0.3182  -0.1136 -0.1582 320 PRO A CD  
2248 N N   . PRO A 294 ? 1.2630 1.4346 1.0875 0.2302  -0.0161 -0.1307 321 PRO A N   
2249 C CA  . PRO A 294 ? 1.3386 1.4788 1.1431 0.2076  0.0088  -0.1067 321 PRO A CA  
2250 C C   . PRO A 294 ? 1.2708 1.3979 1.0677 0.1909  0.0140  -0.1002 321 PRO A C   
2251 O O   . PRO A 294 ? 1.2973 1.4517 1.1250 0.1852  0.0103  -0.1194 321 PRO A O   
2252 C CB  . PRO A 294 ? 1.3055 1.4705 1.1493 0.1915  0.0322  -0.1175 321 PRO A CB  
2253 C CG  . PRO A 294 ? 1.3808 1.5966 1.2770 0.1965  0.0234  -0.1519 321 PRO A CG  
2254 C CD  . PRO A 294 ? 1.3203 1.5397 1.2005 0.2277  -0.0100 -0.1583 321 PRO A CD  
2255 N N   . ALA A 295 ? 1.2595 1.3461 1.0172 0.1836  0.0223  -0.0752 322 ALA A N   
2256 C CA  . ALA A 295 ? 1.0602 1.1305 0.8079 0.1680  0.0284  -0.0672 322 ALA A CA  
2257 C C   . ALA A 295 ? 1.2732 1.3514 1.0465 0.1447  0.0538  -0.0698 322 ALA A C   
2258 O O   . ALA A 295 ? 1.2395 1.2995 0.9998 0.1377  0.0708  -0.0563 322 ALA A O   
2259 C CB  . ALA A 295 ? 1.0633 1.0901 0.7631 0.1696  0.0282  -0.0436 322 ALA A CB  
2260 N N   . GLU A 296 ? 1.1732 1.2759 0.9804 0.1334  0.0574  -0.0879 323 GLU A N   
2261 C CA  . GLU A 296 ? 1.2325 1.3383 1.0626 0.1106  0.0851  -0.0924 323 GLU A CA  
2262 C C   . GLU A 296 ? 1.3402 1.4067 1.1385 0.0981  0.0975  -0.0710 323 GLU A C   
2263 O O   . GLU A 296 ? 1.2498 1.3004 1.0259 0.1021  0.0840  -0.0622 323 GLU A O   
2264 C CB  . GLU A 296 ? 1.2831 1.4277 1.1625 0.1010  0.0872  -0.1220 323 GLU A CB  
2265 C CG  . GLU A 296 ? 1.3681 1.5572 1.2814 0.1179  0.0676  -0.1485 323 GLU A CG  
2266 C CD  . GLU A 296 ? 1.5577 1.7607 1.4875 0.1205  0.0781  -0.1546 323 GLU A CD  
2267 O OE1 . GLU A 296 ? 1.6051 1.7925 1.5343 0.1028  0.1068  -0.1467 323 GLU A OE1 
2268 O OE2 . GLU A 296 ? 1.6198 1.8472 1.5606 0.1416  0.0575  -0.1675 323 GLU A OE2 
2269 N N   . PRO A 297 ? 1.3263 1.3745 1.1195 0.0843  0.1233  -0.0631 324 PRO A N   
2270 C CA  . PRO A 297 ? 1.1807 1.1920 0.9450 0.0744  0.1349  -0.0458 324 PRO A CA  
2271 C C   . PRO A 297 ? 1.2343 1.2519 1.0223 0.0577  0.1453  -0.0584 324 PRO A C   
2272 O O   . PRO A 297 ? 1.3108 1.3630 1.1409 0.0513  0.1472  -0.0824 324 PRO A O   
2273 C CB  . PRO A 297 ? 1.2597 1.2480 1.0064 0.0696  0.1583  -0.0348 324 PRO A CB  
2274 C CG  . PRO A 297 ? 1.1474 1.1666 0.9319 0.0644  0.1701  -0.0546 324 PRO A CG  
2275 C CD  . PRO A 297 ? 1.1888 1.2457 0.9978 0.0789  0.1433  -0.0695 324 PRO A CD  
2276 N N   . SER A 298 ? 1.2576 1.2422 1.0196 0.0511  0.1518  -0.0440 325 SER A N   
2277 C CA  . SER A 298 ? 1.3663 1.3501 1.1464 0.0345  0.1641  -0.0538 325 SER A CA  
2278 C C   . SER A 298 ? 1.3536 1.3420 1.1600 0.0168  0.1952  -0.0679 325 SER A C   
2279 O O   . SER A 298 ? 1.3473 1.3140 1.1359 0.0151  0.2145  -0.0586 325 SER A O   
2280 C CB  . SER A 298 ? 1.4178 1.3599 1.1610 0.0324  0.1678  -0.0343 325 SER A CB  
2281 O OG  . SER A 298 ? 1.2684 1.2029 1.0261 0.0150  0.1853  -0.0425 325 SER A OG  
2282 N N   . ARG A 299 ? 1.3940 1.4096 1.2425 0.0031  0.2016  -0.0921 326 ARG A N   
2283 C CA  . ARG A 299 ? 1.4336 1.4532 1.3116 -0.0175 0.2357  -0.1100 326 ARG A CA  
2284 C C   . ARG A 299 ? 1.4734 1.4401 1.3206 -0.0325 0.2668  -0.0951 326 ARG A C   
2285 O O   . ARG A 299 ? 1.5430 1.5025 1.4088 -0.0526 0.3009  -0.1092 326 ARG A O   
2286 C CB  . ARG A 299 ? 1.4712 1.5409 1.4092 -0.0278 0.2332  -0.1457 326 ARG A CB  
2287 C CG  . ARG A 299 ? 1.4472 1.5136 1.3896 -0.0353 0.2279  -0.1494 326 ARG A CG  
2288 C CD  . ARG A 299 ? 1.4819 1.6036 1.4864 -0.0434 0.2234  -0.1887 326 ARG A CD  
2289 N NE  . ARG A 299 ? 1.5707 1.6852 1.5863 -0.0595 0.2331  -0.1968 326 ARG A NE  
2290 C CZ  . ARG A 299 ? 1.6541 1.7507 1.6851 -0.0849 0.2713  -0.2069 326 ARG A CZ  
2291 N NH1 . ARG A 299 ? 1.6459 1.7271 1.6805 -0.0981 0.3052  -0.2100 326 ARG A NH1 
2292 N NH2 . ARG A 299 ? 1.7132 1.8038 1.7539 -0.0980 0.2777  -0.2144 326 ARG A NH2 
2293 N N   . PHE A 300 ? 1.4912 1.4190 1.2908 -0.0224 0.2566  -0.0686 327 PHE A N   
2294 C CA  . PHE A 300 ? 1.3999 1.2716 1.1603 -0.0299 0.2813  -0.0515 327 PHE A CA  
2295 C C   . PHE A 300 ? 1.5084 1.3399 1.2145 -0.0146 0.2825  -0.0254 327 PHE A C   
2296 O O   . PHE A 300 ? 1.5550 1.3350 1.2201 -0.0159 0.3018  -0.0101 327 PHE A O   
2297 C CB  . PHE A 300 ? 1.3608 1.2195 1.1119 -0.0301 0.2692  -0.0458 327 PHE A CB  
2298 C CG  . PHE A 300 ? 1.5050 1.4044 1.3067 -0.0427 0.2639  -0.0716 327 PHE A CG  
2299 C CD1 . PHE A 300 ? 1.4557 1.3618 1.2926 -0.0655 0.2941  -0.0939 327 PHE A CD1 
2300 C CD2 . PHE A 300 ? 1.4819 1.4112 1.2945 -0.0319 0.2301  -0.0752 327 PHE A CD2 
2301 C CE1 . PHE A 300 ? 1.3941 1.3419 1.2806 -0.0763 0.2879  -0.1212 327 PHE A CE1 
2302 C CE2 . PHE A 300 ? 1.4229 1.3897 1.2787 -0.0410 0.2233  -0.1000 327 PHE A CE2 
2303 C CZ  . PHE A 300 ? 1.4212 1.4001 1.3162 -0.0627 0.2509  -0.1239 327 PHE A CZ  
2304 N N   . ILE A 301 ? 1.4550 1.3071 1.1577 0.0012  0.2620  -0.0209 328 ILE A N   
2305 C CA  . ILE A 301 ? 1.4498 1.2709 1.1058 0.0165  0.2612  0.0000  328 ILE A CA  
2306 C C   . ILE A 301 ? 1.7116 1.5502 1.3812 0.0157  0.2723  -0.0076 328 ILE A C   
2307 O O   . ILE A 301 ? 1.7829 1.6676 1.4915 0.0173  0.2580  -0.0231 328 ILE A O   
2308 C CB  . ILE A 301 ? 1.5404 1.3674 1.1777 0.0364  0.2274  0.0121  328 ILE A CB  
2309 C CG1 . ILE A 301 ? 1.5134 1.3296 1.1446 0.0357  0.2158  0.0156  328 ILE A CG1 
2310 C CG2 . ILE A 301 ? 1.6209 1.4172 1.2121 0.0521  0.2272  0.0302  328 ILE A CG2 
2311 C CD1 . ILE A 301 ? 1.5426 1.3643 1.1588 0.0520  0.1866  0.0237  328 ILE A CD1 
2312 N N   . SER A 302 ? 1.8068 1.6067 1.4415 0.0148  0.2972  0.0030  329 SER A N   
2313 C CA  . SER A 302 ? 1.8124 1.6238 1.4540 0.0144  0.3095  -0.0026 329 SER A CA  
2314 C C   . SER A 302 ? 1.9011 1.7169 1.5182 0.0368  0.2845  0.0112  329 SER A C   
2315 O O   . SER A 302 ? 1.9294 1.7081 1.4974 0.0501  0.2808  0.0303  329 SER A O   
2316 C CB  . SER A 302 ? 1.9986 1.7615 1.6083 0.0031  0.3501  0.0023  329 SER A CB  
2317 O OG  . SER A 302 ? 1.9764 1.6828 1.5244 0.0146  0.3522  0.0257  329 SER A OG  
2318 N N   . ALA A 303 ? 2.1247 1.9856 1.7761 0.0421  0.2668  -0.0002 330 ALA A N   
2319 C CA  . ALA A 303 ? 2.1428 2.0082 1.7745 0.0613  0.2468  0.0102  330 ALA A CA  
2320 C C   . ALA A 303 ? 2.1247 1.9647 1.7264 0.0634  0.2680  0.0178  330 ALA A C   
2321 O O   . ALA A 303 ? 2.0548 1.8939 1.6704 0.0491  0.2955  0.0075  330 ALA A O   
2322 C CB  . ALA A 303 ? 1.9994 1.9135 1.6717 0.0670  0.2257  -0.0041 330 ALA A CB  
2323 N N   . PRO A 304 ? 2.0243 1.8437 1.5852 0.0806  0.2571  0.0335  331 PRO A N   
2324 C CA  . PRO A 304 ? 2.0355 1.8262 1.5604 0.0846  0.2767  0.0414  331 PRO A CA  
2325 C C   . PRO A 304 ? 2.0089 1.8309 1.5629 0.0817  0.2827  0.0293  331 PRO A C   
2326 O O   . PRO A 304 ? 1.9794 1.8425 1.5694 0.0861  0.2624  0.0197  331 PRO A O   
2327 C CB  . PRO A 304 ? 1.9926 1.7648 1.4753 0.1064  0.2560  0.0563  331 PRO A CB  
2328 C CG  . PRO A 304 ? 2.0729 1.8798 1.5844 0.1121  0.2260  0.0515  331 PRO A CG  
2329 C CD  . PRO A 304 ? 1.9289 1.7526 1.4768 0.0970  0.2270  0.0418  331 PRO A CD  
2330 N N   . THR A 305 ? 1.9164 1.7150 1.4516 0.0749  0.3121  0.0295  332 THR A N   
2331 C CA  . THR A 305 ? 2.0163 1.8428 1.5788 0.0709  0.3213  0.0166  332 THR A CA  
2332 C C   . THR A 305 ? 1.9491 1.7857 1.4960 0.0909  0.2997  0.0241  332 THR A C   
2333 O O   . THR A 305 ? 1.8399 1.6510 1.3437 0.1063  0.2874  0.0396  332 THR A O   
2334 C CB  . THR A 305 ? 1.9317 1.7250 1.4736 0.0568  0.3623  0.0147  332 THR A CB  
2335 O OG1 . THR A 305 ? 2.0977 1.8615 1.6329 0.0409  0.3846  0.0141  332 THR A OG1 
2336 C CG2 . THR A 305 ? 1.7306 1.5633 1.3229 0.0441  0.3765  -0.0081 332 THR A CG2 
2337 N N   . LYS A 306 ? 1.8128 1.6886 1.3976 0.0911  0.2948  0.0106  333 LYS A N   
2338 C CA  . LYS A 306 ? 1.7682 1.6566 1.3450 0.1080  0.2768  0.0145  333 LYS A CA  
2339 C C   . LYS A 306 ? 1.7272 1.6187 1.3059 0.1041  0.2982  0.0075  333 LYS A C   
2340 O O   . LYS A 306 ? 1.6656 1.5772 1.2816 0.0892  0.3163  -0.0096 333 LYS A O   
2341 C CB  . LYS A 306 ? 1.6596 1.5890 1.2758 0.1154  0.2482  0.0057  333 LYS A CB  
2342 C CG  . LYS A 306 ? 1.5752 1.5121 1.2090 0.1111  0.2349  0.0033  333 LYS A CG  
2343 C CD  . LYS A 306 ? 1.5665 1.5237 1.2116 0.1247  0.2042  0.0031  333 LYS A CD  
2344 C CE  . LYS A 306 ? 1.6237 1.5575 1.2290 0.1378  0.1917  0.0185  333 LYS A CE  
2345 N NZ  . LYS A 306 ? 1.6365 1.5818 1.2486 0.1477  0.1669  0.0181  333 LYS A NZ  
2346 N N   . THR A 307 ? 1.6938 1.5674 1.2343 0.1173  0.2965  0.0180  334 THR A N   
2347 C CA  . THR A 307 ? 1.7965 1.6709 1.3335 0.1153  0.3159  0.0125  334 THR A CA  
2348 C C   . THR A 307 ? 1.6374 1.5477 1.1993 0.1275  0.2950  0.0060  334 THR A C   
2349 O O   . THR A 307 ? 1.4734 1.3776 1.0103 0.1436  0.2763  0.0155  334 THR A O   
2350 C CB  . THR A 307 ? 1.7559 1.5810 1.2271 0.1225  0.3313  0.0277  334 THR A CB  
2351 O OG1 . THR A 307 ? 1.9447 1.7518 1.3808 0.1396  0.3079  0.0418  334 THR A OG1 
2352 C CG2 . THR A 307 ? 1.5328 1.3185 0.9810 0.1060  0.3666  0.0294  334 THR A CG2 
2353 N N   . PRO A 308 ? 1.6186 1.5664 1.2298 0.1211  0.2976  -0.0119 335 PRO A N   
2354 C CA  . PRO A 308 ? 1.6612 1.6388 1.2935 0.1342  0.2784  -0.0180 335 PRO A CA  
2355 C C   . PRO A 308 ? 1.6827 1.6554 1.2990 0.1372  0.2931  -0.0189 335 PRO A C   
2356 O O   . PRO A 308 ? 1.7363 1.7005 1.3507 0.1248  0.3214  -0.0252 335 PRO A O   
2357 C CB  . PRO A 308 ? 1.6871 1.7065 1.3792 0.1283  0.2739  -0.0389 335 PRO A CB  
2358 C CG  . PRO A 308 ? 1.7059 1.7200 1.4102 0.1113  0.2884  -0.0443 335 PRO A CG  
2359 C CD  . PRO A 308 ? 1.5659 1.5339 1.2211 0.1031  0.3140  -0.0301 335 PRO A CD  
2360 N N   . ASP A 309 ? 1.6602 1.6374 1.2650 0.1531  0.2751  -0.0140 336 ASP A N   
2361 C CA  . ASP A 309 ? 1.4888 1.4688 1.0848 0.1583  0.2838  -0.0172 336 ASP A CA  
2362 C C   . ASP A 309 ? 1.4921 1.5096 1.1316 0.1652  0.2695  -0.0306 336 ASP A C   
2363 O O   . ASP A 309 ? 1.4830 1.5210 1.1543 0.1675  0.2527  -0.0367 336 ASP A O   
2364 C CB  . ASP A 309 ? 1.4460 1.3999 0.9919 0.1720  0.2762  -0.0036 336 ASP A CB  
2365 C CG  . ASP A 309 ? 1.6332 1.5900 1.1774 0.1834  0.2484  0.0022  336 ASP A CG  
2366 O OD1 . ASP A 309 ? 1.7052 1.6829 1.2838 0.1829  0.2343  -0.0031 336 ASP A OD1 
2367 O OD2 . ASP A 309 ? 1.5720 1.5093 1.0793 0.1935  0.2410  0.0104  336 ASP A OD2 
2368 N N   . LYS A 310 ? 1.5758 1.5995 1.2130 0.1701  0.2761  -0.0352 337 LYS A N   
2369 C CA  . LYS A 310 ? 1.5304 1.5838 1.2016 0.1795  0.2629  -0.0465 337 LYS A CA  
2370 C C   . LYS A 310 ? 1.4341 1.4797 1.0846 0.1950  0.2437  -0.0382 337 LYS A C   
2371 O O   . LYS A 310 ? 1.2838 1.3454 0.9523 0.2040  0.2361  -0.0458 337 LYS A O   
2372 C CB  . LYS A 310 ? 1.5746 1.6427 1.2624 0.1744  0.2831  -0.0599 337 LYS A CB  
2373 C CG  . LYS A 310 ? 1.6392 1.7200 1.3571 0.1570  0.3053  -0.0746 337 LYS A CG  
2374 C CD  . LYS A 310 ? 1.6022 1.7179 1.3731 0.1583  0.2897  -0.0905 337 LYS A CD  
2375 C CE  . LYS A 310 ? 1.6154 1.7508 1.4251 0.1399  0.3129  -0.1116 337 LYS A CE  
2376 N NZ  . LYS A 310 ? 1.5352 1.6874 1.3660 0.1339  0.3340  -0.1288 337 LYS A NZ  
2377 N N   . MET A 311 ? 1.3520 1.3729 0.9659 0.1982  0.2371  -0.0249 338 MET A N   
2378 C CA  . MET A 311 ? 1.3021 1.3166 0.8997 0.2105  0.2209  -0.0208 338 MET A CA  
2379 C C   . MET A 311 ? 1.3651 1.3830 0.9533 0.2170  0.2273  -0.0260 338 MET A C   
2380 O O   . MET A 311 ? 1.3821 1.4035 0.9718 0.2261  0.2168  -0.0292 338 MET A O   
2381 C CB  . MET A 311 ? 1.3445 1.3697 0.9666 0.2166  0.2025  -0.0240 338 MET A CB  
2382 C CG  . MET A 311 ? 1.4258 1.4427 1.0469 0.2135  0.1916  -0.0175 338 MET A CG  
2383 S SD  . MET A 311 ? 1.3374 1.3588 0.9761 0.2236  0.1715  -0.0208 338 MET A SD  
2384 C CE  . MET A 311 ? 1.3142 1.3634 0.9902 0.2277  0.1748  -0.0350 338 MET A CE  
2385 N N   . GLY A 312 ? 1.3695 1.3844 0.9468 0.2116  0.2467  -0.0277 339 GLY A N   
2386 C CA  . GLY A 312 ? 1.1916 1.2091 0.7572 0.2173  0.2544  -0.0330 339 GLY A CA  
2387 C C   . GLY A 312 ? 1.2454 1.2886 0.8485 0.2177  0.2578  -0.0459 339 GLY A C   
2388 O O   . GLY A 312 ? 1.5589 1.6058 1.1552 0.2203  0.2676  -0.0517 339 GLY A O   
2389 N N   . PHE A 313 ? 1.3671 1.4279 1.0082 0.2170  0.2489  -0.0516 340 PHE A N   
2390 C CA  . PHE A 313 ? 1.3980 1.4836 1.0757 0.2199  0.2508  -0.0655 340 PHE A CA  
2391 C C   . PHE A 313 ? 1.4090 1.5057 1.1009 0.2078  0.2740  -0.0752 340 PHE A C   
2392 O O   . PHE A 313 ? 1.4806 1.5659 1.1608 0.1957  0.2880  -0.0714 340 PHE A O   
2393 C CB  . PHE A 313 ? 1.2840 1.3832 0.9939 0.2260  0.2332  -0.0703 340 PHE A CB  
2394 C CG  . PHE A 313 ? 1.2921 1.3763 0.9873 0.2371  0.2143  -0.0624 340 PHE A CG  
2395 C CD1 . PHE A 313 ? 1.2842 1.3666 0.9790 0.2479  0.2096  -0.0661 340 PHE A CD1 
2396 C CD2 . PHE A 313 ? 1.3402 1.4100 1.0221 0.2354  0.2036  -0.0524 340 PHE A CD2 
2397 C CE1 . PHE A 313 ? 1.4045 1.4685 1.0845 0.2557  0.1969  -0.0606 340 PHE A CE1 
2398 C CE2 . PHE A 313 ? 1.3100 1.3635 0.9779 0.2436  0.1896  -0.0468 340 PHE A CE2 
2399 C CZ  . PHE A 313 ? 1.2856 1.3350 0.9519 0.2532  0.1874  -0.0512 340 PHE A CZ  
2400 N N   . ASP A 314 ? 1.3362 1.4535 1.0535 0.2104  0.2801  -0.0889 341 ASP A N   
2401 C CA  . ASP A 314 ? 1.4044 1.5354 1.1418 0.1976  0.3039  -0.1023 341 ASP A CA  
2402 C C   . ASP A 314 ? 1.3983 1.5522 1.1799 0.1904  0.3034  -0.1153 341 ASP A C   
2403 O O   . ASP A 314 ? 1.3850 1.5463 1.1821 0.1749  0.3268  -0.1269 341 ASP A O   
2404 C CB  . ASP A 314 ? 1.3423 1.4915 1.0979 0.2027  0.3102  -0.1156 341 ASP A CB  
2405 C CG  . ASP A 314 ? 1.4274 1.5573 1.1410 0.2078  0.3148  -0.1069 341 ASP A CG  
2406 O OD1 . ASP A 314 ? 1.5144 1.6213 1.1905 0.2128  0.3051  -0.0921 341 ASP A OD1 
2407 O OD2 . ASP A 314 ? 1.6977 1.8373 1.4174 0.2073  0.3280  -0.1172 341 ASP A OD2 
2408 N N   . GLU A 315 ? 1.4163 1.5804 1.2172 0.2013  0.2784  -0.1155 342 GLU A N   
2409 C CA  . GLU A 315 ? 1.4861 1.6737 1.3277 0.1978  0.2728  -0.1292 342 GLU A CA  
2410 C C   . GLU A 315 ? 1.4244 1.6083 1.2641 0.2135  0.2427  -0.1213 342 GLU A C   
2411 O O   . GLU A 315 ? 1.4418 1.6134 1.2637 0.2282  0.2279  -0.1127 342 GLU A O   
2412 C CB  . GLU A 315 ? 1.4080 1.6344 1.3025 0.1986  0.2783  -0.1565 342 GLU A CB  
2413 C CG  . GLU A 315 ? 1.3600 1.6184 1.3036 0.1962  0.2719  -0.1776 342 GLU A CG  
2414 C CD  . GLU A 315 ? 1.4277 1.6835 1.3761 0.1715  0.2978  -0.1827 342 GLU A CD  
2415 O OE1 . GLU A 315 ? 1.4619 1.6884 1.3751 0.1650  0.2984  -0.1633 342 GLU A OE1 
2416 O OE2 . GLU A 315 ? 1.5588 1.8407 1.5469 0.1581  0.3191  -0.2077 342 GLU A OE2 
2417 N N   . VAL A 316 ? 1.4070 1.5990 1.2634 0.2092  0.2358  -0.1253 343 VAL A N   
2418 C CA  . VAL A 316 ? 1.3776 1.5673 1.2339 0.2239  0.2082  -0.1207 343 VAL A CA  
2419 C C   . VAL A 316 ? 1.3564 1.5836 1.2635 0.2284  0.1988  -0.1453 343 VAL A C   
2420 O O   . VAL A 316 ? 1.3493 1.5920 1.2796 0.2130  0.2106  -0.1566 343 VAL A O   
2421 C CB  . VAL A 316 ? 1.2910 1.4533 1.1140 0.2166  0.2051  -0.1016 343 VAL A CB  
2422 C CG1 . VAL A 316 ? 1.3019 1.4635 1.1276 0.2301  0.1788  -0.0999 343 VAL A CG1 
2423 C CG2 . VAL A 316 ? 1.2832 1.4128 1.0591 0.2166  0.2096  -0.0816 343 VAL A CG2 
2424 N N   . PHE A 317 ? 1.3172 1.5584 1.2413 0.2504  0.1783  -0.1554 344 PHE A N   
2425 C CA  . PHE A 317 ? 1.2581 1.5373 1.2298 0.2613  0.1636  -0.1818 344 PHE A CA  
2426 C C   . PHE A 317 ? 1.3067 1.5764 1.2660 0.2764  0.1363  -0.1758 344 PHE A C   
2427 O O   . PHE A 317 ? 1.2936 1.5262 1.2085 0.2844  0.1259  -0.1526 344 PHE A O   
2428 C CB  . PHE A 317 ? 1.2636 1.5624 1.2589 0.2811  0.1547  -0.1983 344 PHE A CB  
2429 C CG  . PHE A 317 ? 1.2562 1.5702 1.2705 0.2671  0.1810  -0.2092 344 PHE A CG  
2430 C CD1 . PHE A 317 ? 1.2606 1.6142 1.3256 0.2529  0.1976  -0.2376 344 PHE A CD1 
2431 C CD2 . PHE A 317 ? 1.2576 1.5470 1.2403 0.2678  0.1904  -0.1936 344 PHE A CD2 
2432 C CE1 . PHE A 317 ? 1.2529 1.6175 1.3329 0.2391  0.2243  -0.2483 344 PHE A CE1 
2433 C CE2 . PHE A 317 ? 1.2928 1.5951 1.2902 0.2556  0.2146  -0.2039 344 PHE A CE2 
2434 C CZ  . PHE A 317 ? 1.2676 1.6057 1.3118 0.2412  0.2320  -0.2304 344 PHE A CZ  
2435 N N   . MET A 318 ? 1.3630 1.6673 1.3631 0.2801  0.1255  -0.1994 345 MET A N   
2436 C CA  . MET A 318 ? 1.4002 1.7007 1.3921 0.2992  0.0964  -0.1991 345 MET A CA  
2437 C C   . MET A 318 ? 1.3767 1.7217 1.4171 0.3206  0.0765  -0.2330 345 MET A C   
2438 O O   . MET A 318 ? 1.4052 1.7941 1.4982 0.3086  0.0852  -0.2614 345 MET A O   
2439 C CB  . MET A 318 ? 1.4955 1.7914 1.4828 0.2807  0.1013  -0.1928 345 MET A CB  
2440 C CG  . MET A 318 ? 1.4238 1.7217 1.4077 0.2999  0.0716  -0.1972 345 MET A CG  
2441 S SD  . MET A 318 ? 1.5666 1.8694 1.5583 0.2771  0.0784  -0.1973 345 MET A SD  
2442 C CE  . MET A 318 ? 1.6054 1.9464 1.6316 0.3031  0.0442  -0.2276 345 MET A CE  
2443 N N   . ILE A 319 ? 1.3306 1.6633 1.3531 0.3528  0.0506  -0.2318 346 ILE A N   
2444 C CA  . ILE A 319 ? 1.4308 1.8024 1.4929 0.3805  0.0258  -0.2641 346 ILE A CA  
2445 C C   . ILE A 319 ? 1.5488 1.9299 1.6132 0.3920  0.0018  -0.2728 346 ILE A C   
2446 O O   . ILE A 319 ? 1.5443 1.8841 1.5590 0.3951  -0.0069 -0.2472 346 ILE A O   
2447 C CB  . ILE A 319 ? 1.4184 1.7656 1.4527 0.4136  0.0077  -0.2583 346 ILE A CB  
2448 C CG1 . ILE A 319 ? 1.4917 1.8224 1.5154 0.3997  0.0329  -0.2450 346 ILE A CG1 
2449 C CG2 . ILE A 319 ? 1.2735 1.6644 1.3520 0.4440  -0.0173 -0.2951 346 ILE A CG2 
2450 C CD1 . ILE A 319 ? 1.3908 1.6938 1.3868 0.4292  0.0197  -0.2387 346 ILE A CD1 
2451 N N   . ASN A 320 ? 1.4651 1.9028 1.5894 0.3981  -0.0086 -0.3118 347 ASN A N   
2452 C CA  . ASN A 320 ? 1.5538 2.0086 1.6873 0.4100  -0.0325 -0.3261 347 ASN A CA  
2453 C C   . ASN A 320 ? 1.5877 2.1100 1.7910 0.4274  -0.0504 -0.3762 347 ASN A C   
2454 O O   . ASN A 320 ? 1.5541 2.1218 1.8174 0.4069  -0.0286 -0.4040 347 ASN A O   
2455 C CB  . ASN A 320 ? 1.5633 2.0142 1.6976 0.3740  -0.0107 -0.3155 347 ASN A CB  
2456 C CG  . ASN A 320 ? 1.5806 2.0578 1.7350 0.3823  -0.0323 -0.3359 347 ASN A CG  
2457 O OD1 . ASN A 320 ? 1.6020 2.1255 1.8130 0.3625  -0.0203 -0.3654 347 ASN A OD1 
2458 N ND2 . ASN A 320 ? 1.5859 2.0319 1.6927 0.4111  -0.0626 -0.3215 347 ASN A ND2 
2459 N N   . LEU A 321 ? 1.5748 2.1033 1.7696 0.4662  -0.0895 -0.3899 348 LEU A N   
2460 C CA  . LEU A 321 ? 1.6442 2.2421 1.9078 0.4850  -0.1107 -0.4420 348 LEU A CA  
2461 C C   . LEU A 321 ? 1.6725 2.3151 1.9904 0.4520  -0.0937 -0.4663 348 LEU A C   
2462 O O   . LEU A 321 ? 1.5967 2.2130 1.8845 0.4358  -0.0887 -0.4446 348 LEU A O   
2463 C CB  . LEU A 321 ? 1.7140 2.3025 1.9463 0.5364  -0.1585 -0.4492 348 LEU A CB  
2464 C CG  . LEU A 321 ? 1.7653 2.3199 1.9556 0.5784  -0.1808 -0.4393 348 LEU A CG  
2465 C CD1 . LEU A 321 ? 1.8680 2.3559 1.9720 0.6100  -0.2074 -0.4079 348 LEU A CD1 
2466 C CD2 . LEU A 321 ? 1.6909 2.3085 1.9422 0.6119  -0.2072 -0.4906 348 LEU A CD2 
2467 N N   . ARG A 322 ? 1.7390 2.4490 2.1389 0.4407  -0.0826 -0.5133 349 ARG A N   
2468 C CA  . ARG A 322 ? 1.7186 2.4726 2.1756 0.4082  -0.0629 -0.5420 349 ARG A CA  
2469 C C   . ARG A 322 ? 1.7515 2.5258 2.2129 0.4304  -0.0977 -0.5602 349 ARG A C   
2470 O O   . ARG A 322 ? 1.7253 2.5156 2.2106 0.4027  -0.0823 -0.5697 349 ARG A O   
2471 C CB  . ARG A 322 ? 1.7040 2.5275 2.2510 0.3934  -0.0435 -0.5944 349 ARG A CB  
2472 C CG  . ARG A 322 ? 1.6395 2.4991 2.2441 0.3495  -0.0085 -0.6216 349 ARG A CG  
2473 C CD  . ARG A 322 ? 1.7270 2.6595 2.4255 0.3381  0.0084  -0.6810 349 ARG A CD  
2474 N NE  . ARG A 322 ? 1.8356 2.8204 2.5732 0.3850  -0.0366 -0.7225 349 ARG A NE  
2475 C CZ  . ARG A 322 ? 1.8644 2.8956 2.6366 0.4103  -0.0720 -0.7600 349 ARG A CZ  
2476 N NH1 . ARG A 322 ? 1.8189 2.8529 2.5946 0.3918  -0.0673 -0.7618 349 ARG A NH1 
2477 N NH2 . ARG A 322 ? 1.7777 2.8533 2.5804 0.4570  -0.1142 -0.7974 349 ARG A NH2 
2478 N N   . ARG A 323 ? 1.7275 2.4978 2.1621 0.4807  -0.1436 -0.5648 350 ARG A N   
2479 C CA  . ARG A 323 ? 1.5910 2.3734 2.0177 0.5065  -0.1796 -0.5791 350 ARG A CA  
2480 C C   . ARG A 323 ? 1.6164 2.3275 1.9597 0.5016  -0.1807 -0.5274 350 ARG A C   
2481 O O   . ARG A 323 ? 1.6635 2.3840 2.0055 0.5050  -0.1963 -0.5359 350 ARG A O   
2482 C CB  . ARG A 323 ? 1.5619 2.3621 1.9843 0.5663  -0.2296 -0.6044 350 ARG A CB  
2483 C CG  . ARG A 323 ? 1.7103 2.4381 2.0476 0.5982  -0.2446 -0.5614 350 ARG A CG  
2484 C CD  . ARG A 323 ? 1.6844 2.4119 1.9942 0.6614  -0.2982 -0.5792 350 ARG A CD  
2485 N NE  . ARG A 323 ? 1.7686 2.4158 1.9876 0.6911  -0.3095 -0.5356 350 ARG A NE  
2486 C CZ  . ARG A 323 ? 1.8229 2.4646 2.0345 0.7264  -0.3259 -0.5435 350 ARG A CZ  
2487 N NH1 . ARG A 323 ? 1.7266 2.4413 2.0170 0.7394  -0.3363 -0.5944 350 ARG A NH1 
2488 N NH2 . ARG A 323 ? 1.9075 2.4680 2.0316 0.7487  -0.3307 -0.5011 350 ARG A NH2 
2489 N N   . ARG A 324 ? 1.5676 2.2104 1.8445 0.4931  -0.1640 -0.4769 351 ARG A N   
2490 C CA  . ARG A 324 ? 1.5537 2.1286 1.7532 0.4872  -0.1627 -0.4295 351 ARG A CA  
2491 C C   . ARG A 324 ? 1.4741 2.0446 1.6866 0.4358  -0.1232 -0.4149 351 ARG A C   
2492 O O   . ARG A 324 ? 1.4320 1.9591 1.6104 0.4108  -0.0946 -0.3789 351 ARG A O   
2493 C CB  . ARG A 324 ? 1.5563 2.0621 1.6818 0.5023  -0.1627 -0.3870 351 ARG A CB  
2494 C CG  . ARG A 324 ? 1.3828 1.8826 1.4879 0.5535  -0.1978 -0.3982 351 ARG A CG  
2495 C CD  . ARG A 324 ? 1.6502 2.1540 1.7354 0.5932  -0.2400 -0.4145 351 ARG A CD  
2496 N NE  . ARG A 324 ? 1.7994 2.2900 1.8568 0.6460  -0.2742 -0.4239 351 ARG A NE  
2497 C CZ  . ARG A 324 ? 1.6766 2.1732 1.7162 0.6917  -0.3164 -0.4443 351 ARG A CZ  
2498 N NH1 . ARG A 324 ? 1.5159 2.0360 1.5663 0.6909  -0.3308 -0.4595 351 ARG A NH1 
2499 N NH2 . ARG A 324 ? 1.5898 2.0668 1.5977 0.7409  -0.3452 -0.4502 351 ARG A NH2 
2500 N N   . GLN A 325 ? 1.5830 2.1995 1.8454 0.4218  -0.1227 -0.4456 352 GLN A N   
2501 C CA  . GLN A 325 ? 1.6214 2.2320 1.8957 0.3751  -0.0858 -0.4345 352 GLN A CA  
2502 C C   . GLN A 325 ? 1.5874 2.1341 1.7884 0.3694  -0.0861 -0.3885 352 GLN A C   
2503 O O   . GLN A 325 ? 1.6336 2.1495 1.8166 0.3352  -0.0538 -0.3615 352 GLN A O   
2504 C CB  . GLN A 325 ? 1.6669 2.3430 2.0159 0.3615  -0.0837 -0.4825 352 GLN A CB  
2505 C CG  . GLN A 325 ? 1.7761 2.5217 2.2076 0.3624  -0.0791 -0.5345 352 GLN A CG  
2506 C CD  . GLN A 325 ? 1.9038 2.7134 2.4138 0.3414  -0.0689 -0.5840 352 GLN A CD  
2507 O OE1 . GLN A 325 ? 1.9934 2.7928 2.4951 0.3233  -0.0621 -0.5769 352 GLN A OE1 
2508 N NE2 . GLN A 325 ? 1.6967 2.5737 2.2859 0.3429  -0.0663 -0.6370 352 GLN A NE2 
2509 N N   . ASP A 326 ? 1.4921 2.0164 1.6481 0.4034  -0.1218 -0.3801 353 ASP A N   
2510 C CA  . ASP A 326 ? 1.3550 1.8180 1.4412 0.3989  -0.1221 -0.3387 353 ASP A CA  
2511 C C   . ASP A 326 ? 1.4445 1.8487 1.4772 0.3886  -0.1016 -0.2957 353 ASP A C   
2512 O O   . ASP A 326 ? 1.4103 1.7791 1.4145 0.3615  -0.0794 -0.2666 353 ASP A O   
2513 C CB  . ASP A 326 ? 1.2728 1.7188 1.3162 0.4405  -0.1634 -0.3397 353 ASP A CB  
2514 C CG  . ASP A 326 ? 1.6601 2.0977 1.6825 0.4828  -0.1889 -0.3448 353 ASP A CG  
2515 O OD1 . ASP A 326 ? 1.5482 2.0356 1.6266 0.4902  -0.1911 -0.3771 353 ASP A OD1 
2516 O OD2 . ASP A 326 ? 1.7170 2.0956 1.6659 0.5080  -0.2047 -0.3168 353 ASP A OD2 
2517 N N   . ARG A 327 ? 1.5458 1.9402 1.5655 0.4111  -0.1094 -0.2934 354 ARG A N   
2518 C CA  . ARG A 327 ? 1.4085 1.7517 1.3824 0.4022  -0.0900 -0.2571 354 ARG A CA  
2519 C C   . ARG A 327 ? 1.4057 1.7610 1.4105 0.3630  -0.0517 -0.2534 354 ARG A C   
2520 O O   . ARG A 327 ? 1.4858 1.7989 1.4524 0.3445  -0.0313 -0.2213 354 ARG A O   
2521 C CB  . ARG A 327 ? 1.3436 1.6764 1.3012 0.4357  -0.1064 -0.2594 354 ARG A CB  
2522 C CG  . ARG A 327 ? 1.3711 1.6692 1.2749 0.4769  -0.1408 -0.2535 354 ARG A CG  
2523 C CD  . ARG A 327 ? 1.5064 1.7923 1.3953 0.5098  -0.1542 -0.2569 354 ARG A CD  
2524 N NE  . ARG A 327 ? 1.6695 1.8955 1.4836 0.5451  -0.1770 -0.2381 354 ARG A NE  
2525 C CZ  . ARG A 327 ? 1.5796 1.7766 1.3617 0.5777  -0.1894 -0.2350 354 ARG A CZ  
2526 N NH1 . ARG A 327 ? 1.4583 1.6848 1.2797 0.5807  -0.1837 -0.2503 354 ARG A NH1 
2527 N NH2 . ARG A 327 ? 1.6714 1.8047 1.3777 0.6078  -0.2062 -0.2162 354 ARG A NH2 
2528 N N   . ARG A 328 ? 1.3937 1.8052 1.4662 0.3506  -0.0408 -0.2876 355 ARG A N   
2529 C CA  . ARG A 328 ? 1.4061 1.8239 1.5030 0.3142  -0.0019 -0.2852 355 ARG A CA  
2530 C C   . ARG A 328 ? 1.4382 1.8320 1.5172 0.2835  0.0191  -0.2653 355 ARG A C   
2531 O O   . ARG A 328 ? 1.5067 1.8653 1.5557 0.2632  0.0438  -0.2381 355 ARG A O   
2532 C CB  . ARG A 328 ? 1.4943 1.9762 1.6686 0.3061  0.0078  -0.3299 355 ARG A CB  
2533 C CG  . ARG A 328 ? 1.4100 1.8936 1.6047 0.2711  0.0503  -0.3288 355 ARG A CG  
2534 C CD  . ARG A 328 ? 1.4092 1.9538 1.6827 0.2545  0.0669  -0.3758 355 ARG A CD  
2535 N NE  . ARG A 328 ? 1.5635 2.1593 1.8835 0.2842  0.0393  -0.4143 355 ARG A NE  
2536 C CZ  . ARG A 328 ? 1.5461 2.1882 1.9082 0.2998  0.0143  -0.4504 355 ARG A CZ  
2537 N NH1 . ARG A 328 ? 1.5519 2.1972 1.9185 0.2866  0.0148  -0.4536 355 ARG A NH1 
2538 N NH2 . ARG A 328 ? 1.5740 2.2613 1.9752 0.3309  -0.0127 -0.4858 355 ARG A NH2 
2539 N N   . GLU A 329 ? 1.3987 1.8111 1.4951 0.2814  0.0085  -0.2799 356 GLU A N   
2540 C CA  . GLU A 329 ? 1.3961 1.7863 1.4778 0.2530  0.0281  -0.2632 356 GLU A CA  
2541 C C   . GLU A 329 ? 1.4119 1.7414 1.4226 0.2561  0.0242  -0.2205 356 GLU A C   
2542 O O   . GLU A 329 ? 1.3628 1.6634 1.3518 0.2319  0.0472  -0.1989 356 GLU A O   
2543 C CB  . GLU A 329 ? 1.4250 1.8494 1.5411 0.2524  0.0152  -0.2899 356 GLU A CB  
2544 C CG  . GLU A 329 ? 1.5387 2.0289 1.7330 0.2469  0.0206  -0.3385 356 GLU A CG  
2545 C CD  . GLU A 329 ? 1.5242 2.0507 1.7550 0.2457  0.0081  -0.3679 356 GLU A CD  
2546 O OE1 . GLU A 329 ? 1.5533 2.0518 1.7555 0.2334  0.0113  -0.3484 356 GLU A OE1 
2547 O OE2 . GLU A 329 ? 1.6247 2.2100 1.9149 0.2576  -0.0057 -0.4126 356 GLU A OE2 
2548 N N   . ARG A 330 ? 1.3711 1.6787 1.3437 0.2860  -0.0036 -0.2095 357 ARG A N   
2549 C CA  . ARG A 330 ? 1.2758 1.5264 1.1841 0.2876  -0.0049 -0.1729 357 ARG A CA  
2550 C C   . ARG A 330 ? 1.3472 1.5697 1.2325 0.2768  0.0169  -0.1509 357 ARG A C   
2551 O O   . ARG A 330 ? 1.3598 1.5473 1.2116 0.2612  0.0308  -0.1261 357 ARG A O   
2552 C CB  . ARG A 330 ? 1.2976 1.5262 1.1676 0.3218  -0.0363 -0.1684 357 ARG A CB  
2553 C CG  . ARG A 330 ? 1.2116 1.3842 1.0197 0.3208  -0.0374 -0.1370 357 ARG A CG  
2554 C CD  . ARG A 330 ? 1.2438 1.3809 1.0036 0.3535  -0.0599 -0.1284 357 ARG A CD  
2555 N NE  . ARG A 330 ? 1.4347 1.5492 1.1758 0.3601  -0.0512 -0.1167 357 ARG A NE  
2556 C CZ  . ARG A 330 ? 1.3129 1.3830 1.0137 0.3500  -0.0357 -0.0911 357 ARG A CZ  
2557 N NH1 . ARG A 330 ? 1.2501 1.2926 0.9242 0.3337  -0.0277 -0.0742 357 ARG A NH1 
2558 N NH2 . ARG A 330 ? 1.3821 1.4375 1.0721 0.3564  -0.0280 -0.0849 357 ARG A NH2 
2559 N N   . MET A 331 ? 1.3303 1.5695 1.2342 0.2860  0.0191  -0.1615 358 MET A N   
2560 C CA  . MET A 331 ? 1.3243 1.5396 1.2075 0.2770  0.0390  -0.1430 358 MET A CA  
2561 C C   . MET A 331 ? 1.3673 1.5872 1.2657 0.2456  0.0701  -0.1404 358 MET A C   
2562 O O   . MET A 331 ? 1.4097 1.5963 1.2737 0.2341  0.0851  -0.1169 358 MET A O   
2563 C CB  . MET A 331 ? 1.4380 1.6713 1.3392 0.2951  0.0335  -0.1569 358 MET A CB  
2564 C CG  . MET A 331 ? 1.4902 1.7068 1.3644 0.3295  0.0046  -0.1557 358 MET A CG  
2565 S SD  . MET A 331 ? 1.4651 1.6133 1.2653 0.3347  0.0047  -0.1190 358 MET A SD  
2566 C CE  . MET A 331 ? 1.2556 1.3955 1.0547 0.3140  0.0345  -0.1065 358 MET A CE  
2567 N N   . LEU A 332 ? 1.4336 1.6925 1.3815 0.2322  0.0810  -0.1658 359 LEU A N   
2568 C CA  . LEU A 332 ? 1.4897 1.7460 1.4470 0.2024  0.1141  -0.1640 359 LEU A CA  
2569 C C   . LEU A 332 ? 1.4773 1.6996 1.4005 0.1879  0.1208  -0.1418 359 LEU A C   
2570 O O   . LEU A 332 ? 1.4734 1.6748 1.3814 0.1682  0.1467  -0.1299 359 LEU A O   
2571 C CB  . LEU A 332 ? 1.4877 1.7914 1.5071 0.1897  0.1264  -0.1996 359 LEU A CB  
2572 C CG  . LEU A 332 ? 1.4365 1.7792 1.4985 0.1997  0.1254  -0.2268 359 LEU A CG  
2573 C CD1 . LEU A 332 ? 1.4412 1.8345 1.5701 0.1857  0.1374  -0.2671 359 LEU A CD1 
2574 C CD2 . LEU A 332 ? 1.7480 2.0708 1.7913 0.1916  0.1484  -0.2130 359 LEU A CD2 
2575 N N   . ARG A 333 ? 1.3854 1.5999 1.2936 0.1988  0.0981  -0.1366 360 ARG A N   
2576 C CA  . ARG A 333 ? 1.3321 1.5138 1.2069 0.1872  0.1021  -0.1156 360 ARG A CA  
2577 C C   . ARG A 333 ? 1.3836 1.5230 1.2061 0.1938  0.0994  -0.0869 360 ARG A C   
2578 O O   . ARG A 333 ? 1.3304 1.4426 1.1269 0.1803  0.1143  -0.0697 360 ARG A O   
2579 C CB  . ARG A 333 ? 1.3038 1.4957 1.1857 0.1946  0.0805  -0.1241 360 ARG A CB  
2580 C CG  . ARG A 333 ? 1.3707 1.6028 1.3049 0.1819  0.0873  -0.1531 360 ARG A CG  
2581 C CD  . ARG A 333 ? 1.6092 1.8555 1.5503 0.1941  0.0613  -0.1645 360 ARG A CD  
2582 N NE  . ARG A 333 ? 1.7244 2.0025 1.7108 0.1762  0.0720  -0.1893 360 ARG A NE  
2583 C CZ  . ARG A 333 ? 1.7961 2.0562 1.7751 0.1542  0.0890  -0.1803 360 ARG A CZ  
2584 N NH1 . ARG A 333 ? 1.5789 1.7921 1.5083 0.1486  0.0955  -0.1480 360 ARG A NH1 
2585 N NH2 . ARG A 333 ? 1.7832 2.0737 1.8071 0.1380  0.1000  -0.2065 360 ARG A NH2 
2586 N N   . ALA A 334 ? 1.4026 1.5348 1.2087 0.2153  0.0810  -0.0833 361 ALA A N   
2587 C CA  . ALA A 334 ? 1.4018 1.4960 1.1631 0.2201  0.0811  -0.0606 361 ALA A CA  
2588 C C   . ALA A 334 ? 1.3406 1.4289 1.0969 0.2104  0.1025  -0.0541 361 ALA A C   
2589 O O   . ALA A 334 ? 1.3160 1.3766 1.0408 0.2043  0.1105  -0.0372 361 ALA A O   
2590 C CB  . ALA A 334 ? 1.1697 1.2536 0.9139 0.2445  0.0610  -0.0601 361 ALA A CB  
2591 N N   . LEU A 335 ? 1.3115 1.4266 1.0988 0.2097  0.1114  -0.0693 362 LEU A N   
2592 C CA  . LEU A 335 ? 1.2972 1.4064 1.0782 0.2003  0.1331  -0.0644 362 LEU A CA  
2593 C C   . LEU A 335 ? 1.3206 1.4157 1.0913 0.1797  0.1543  -0.0569 362 LEU A C   
2594 O O   . LEU A 335 ? 1.2951 1.3632 1.0319 0.1761  0.1640  -0.0409 362 LEU A O   
2595 C CB  . LEU A 335 ? 1.4046 1.5469 1.2241 0.2027  0.1395  -0.0851 362 LEU A CB  
2596 C CG  . LEU A 335 ? 1.3325 1.4840 1.1573 0.2259  0.1202  -0.0918 362 LEU A CG  
2597 C CD1 . LEU A 335 ? 1.2807 1.4723 1.1526 0.2286  0.1241  -0.1177 362 LEU A CD1 
2598 C CD2 . LEU A 335 ? 1.3358 1.4582 1.1239 0.2324  0.1225  -0.0742 362 LEU A CD2 
2599 N N   . GLN A 336 ? 1.3943 1.5061 1.1926 0.1672  0.1615  -0.0696 363 GLN A N   
2600 C CA  . GLN A 336 ? 1.4644 1.5569 1.2498 0.1479  0.1840  -0.0625 363 GLN A CA  
2601 C C   . GLN A 336 ? 1.4100 1.4684 1.1541 0.1491  0.1761  -0.0410 363 GLN A C   
2602 O O   . GLN A 336 ? 1.5647 1.5949 1.2784 0.1414  0.1915  -0.0278 363 GLN A O   
2603 C CB  . GLN A 336 ? 1.4943 1.6115 1.3206 0.1336  0.1935  -0.0832 363 GLN A CB  
2604 C CG  . GLN A 336 ? 1.8046 1.8961 1.6155 0.1133  0.2182  -0.0761 363 GLN A CG  
2605 C CD  . GLN A 336 ? 2.0149 2.0810 1.8009 0.1035  0.2477  -0.0683 363 GLN A CD  
2606 O OE1 . GLN A 336 ? 1.9449 2.0236 1.7406 0.1066  0.2545  -0.0755 363 GLN A OE1 
2607 N NE2 . GLN A 336 ? 1.8993 1.9271 1.6500 0.0930  0.2652  -0.0537 363 GLN A NE2 
2608 N N   . ALA A 337 ? 1.4082 1.4672 1.1488 0.1600  0.1523  -0.0383 364 ALA A N   
2609 C CA  . ALA A 337 ? 1.2934 1.3227 0.9987 0.1608  0.1450  -0.0209 364 ALA A CA  
2610 C C   . ALA A 337 ? 1.3549 1.3610 1.0257 0.1675  0.1470  -0.0070 364 ALA A C   
2611 O O   . ALA A 337 ? 1.3500 1.3316 0.9922 0.1643  0.1506  0.0049  364 ALA A O   
2612 C CB  . ALA A 337 ? 1.2203 1.2529 0.9270 0.1712  0.1213  -0.0225 364 ALA A CB  
2613 N N   . GLN A 338 ? 1.4528 1.4674 1.1269 0.1776  0.1442  -0.0105 365 GLN A N   
2614 C CA  . GLN A 338 ? 1.4101 1.4076 1.0565 0.1841  0.1462  -0.0014 365 GLN A CA  
2615 C C   . GLN A 338 ? 1.4304 1.4243 1.0686 0.1784  0.1663  -0.0003 365 GLN A C   
2616 O O   . GLN A 338 ? 1.4988 1.4845 1.1183 0.1851  0.1681  0.0035  365 GLN A O   
2617 C CB  . GLN A 338 ? 1.2787 1.2830 0.9298 0.1982  0.1346  -0.0057 365 GLN A CB  
2618 C CG  . GLN A 338 ? 1.1275 1.1247 0.7742 0.2065  0.1163  -0.0050 365 GLN A CG  
2619 C CD  . GLN A 338 ? 1.1565 1.1513 0.8003 0.2216  0.1078  -0.0081 365 GLN A CD  
2620 O OE1 . GLN A 338 ? 1.2646 1.2394 0.8858 0.2256  0.1082  -0.0025 365 GLN A OE1 
2621 N NE2 . GLN A 338 ? 1.1579 1.1728 0.8254 0.2306  0.1005  -0.0192 365 GLN A NE2 
2622 N N   . GLU A 339 ? 1.4822 1.4800 1.1321 0.1657  0.1829  -0.0046 366 GLU A N   
2623 C CA  . GLU A 339 ? 1.5438 1.5329 1.1820 0.1593  0.2060  -0.0041 366 GLU A CA  
2624 C C   . GLU A 339 ? 1.4879 1.4945 1.1391 0.1660  0.2082  -0.0121 366 GLU A C   
2625 O O   . GLU A 339 ? 1.5127 1.5067 1.1396 0.1693  0.2175  -0.0071 366 GLU A O   
2626 C CB  . GLU A 339 ? 1.5047 1.4594 1.0956 0.1618  0.2109  0.0110  366 GLU A CB  
2627 C CG  . GLU A 339 ? 1.5308 1.4648 1.1071 0.1545  0.2128  0.0185  366 GLU A CG  
2628 C CD  . GLU A 339 ? 1.7252 1.6228 1.2531 0.1580  0.2225  0.0309  366 GLU A CD  
2629 O OE1 . GLU A 339 ? 1.7855 1.6761 1.2891 0.1695  0.2198  0.0341  366 GLU A OE1 
2630 O OE2 . GLU A 339 ? 1.7223 1.5972 1.2348 0.1506  0.2325  0.0364  366 GLU A OE2 
2631 N N   . ILE A 340 ? 1.3215 1.3574 1.0103 0.1700  0.1984  -0.0256 367 ILE A N   
2632 C CA  . ILE A 340 ? 1.3450 1.4005 1.0523 0.1773  0.1991  -0.0358 367 ILE A CA  
2633 C C   . ILE A 340 ? 1.5077 1.5919 1.2573 0.1675  0.2124  -0.0555 367 ILE A C   
2634 O O   . ILE A 340 ? 1.3505 1.4506 1.1269 0.1623  0.2082  -0.0657 367 ILE A O   
2635 C CB  . ILE A 340 ? 1.3326 1.3952 1.0451 0.1944  0.1751  -0.0368 367 ILE A CB  
2636 C CG1 . ILE A 340 ? 1.3199 1.3547 0.9942 0.2009  0.1664  -0.0214 367 ILE A CG1 
2637 C CG2 . ILE A 340 ? 1.1992 1.2816 0.9324 0.2032  0.1758  -0.0486 367 ILE A CG2 
2638 C CD1 . ILE A 340 ? 1.1630 1.1950 0.8353 0.2158  0.1487  -0.0217 367 ILE A CD1 
2639 N N   . GLU A 341 ? 1.4845 1.5770 1.2419 0.1645  0.2292  -0.0633 368 GLU A N   
2640 C CA  . GLU A 341 ? 1.4725 1.5931 1.2722 0.1532  0.2465  -0.0856 368 GLU A CA  
2641 C C   . GLU A 341 ? 1.5334 1.6840 1.3637 0.1661  0.2370  -0.1009 368 GLU A C   
2642 O O   . GLU A 341 ? 1.5704 1.7109 1.3797 0.1761  0.2338  -0.0924 368 GLU A O   
2643 C CB  . GLU A 341 ? 1.5875 1.6869 1.3672 0.1358  0.2807  -0.0832 368 GLU A CB  
2644 C CG  . GLU A 341 ? 1.7320 1.8567 1.5553 0.1194  0.3054  -0.1086 368 GLU A CG  
2645 C CD  . GLU A 341 ? 1.8738 1.9679 1.6671 0.1029  0.3426  -0.1043 368 GLU A CD  
2646 O OE1 . GLU A 341 ? 1.7528 1.8051 1.4888 0.1063  0.3461  -0.0807 368 GLU A OE1 
2647 O OE2 . GLU A 341 ? 1.9549 2.0656 1.7803 0.0874  0.3686  -0.1259 368 GLU A OE2 
2648 N N   . CYS A 342 ? 1.6048 1.7933 1.4858 0.1667  0.2319  -0.1255 369 CYS A N   
2649 C CA  . CYS A 342 ? 1.4859 1.7046 1.3986 0.1822  0.2197  -0.1426 369 CYS A CA  
2650 C C   . CYS A 342 ? 1.5400 1.7979 1.5076 0.1705  0.2370  -0.1742 369 CYS A C   
2651 O O   . CYS A 342 ? 1.7050 1.9727 1.6943 0.1533  0.2512  -0.1865 369 CYS A O   
2652 C CB  . CYS A 342 ? 1.5230 1.7512 1.4424 0.2052  0.1850  -0.1442 369 CYS A CB  
2653 S SG  . CYS A 342 ? 1.4939 1.7635 1.4664 0.2060  0.1721  -0.1729 369 CYS A SG  
2654 N N   . ARG A 343 ? 1.4062 1.6872 1.3984 0.1794  0.2369  -0.1895 370 ARG A N   
2655 C CA  . ARG A 343 ? 1.3117 1.6379 1.3647 0.1725  0.2486  -0.2255 370 ARG A CA  
2656 C C   . ARG A 343 ? 1.4053 1.7688 1.4973 0.1971  0.2144  -0.2464 370 ARG A C   
2657 O O   . ARG A 343 ? 1.3865 1.7464 1.4661 0.2217  0.1913  -0.2399 370 ARG A O   
2658 C CB  . ARG A 343 ? 1.3959 1.7270 1.4550 0.1677  0.2698  -0.2329 370 ARG A CB  
2659 C CG  . ARG A 343 ? 1.3043 1.6863 1.4317 0.1620  0.2805  -0.2740 370 ARG A CG  
2660 C CD  . ARG A 343 ? 1.2848 1.6745 1.4205 0.1613  0.2967  -0.2827 370 ARG A CD  
2661 N NE  . ARG A 343 ? 1.2722 1.7177 1.4782 0.1672  0.2924  -0.3241 370 ARG A NE  
2662 C CZ  . ARG A 343 ? 1.5976 2.0632 1.8302 0.1636  0.3093  -0.3434 370 ARG A CZ  
2663 N NH1 . ARG A 343 ? 1.6763 2.1100 1.8695 0.1534  0.3328  -0.3247 370 ARG A NH1 
2664 N NH2 . ARG A 343 ? 1.6673 2.1876 1.9682 0.1715  0.3016  -0.3842 370 ARG A NH2 
2665 N N   . LEU A 344 ? 1.3823 1.7798 1.5194 0.1916  0.2117  -0.2726 371 LEU A N   
2666 C CA  . LEU A 344 ? 1.2819 1.7143 1.4522 0.2177  0.1763  -0.2940 371 LEU A CA  
2667 C C   . LEU A 344 ? 1.3317 1.8063 1.5499 0.2318  0.1712  -0.3255 371 LEU A C   
2668 O O   . LEU A 344 ? 1.3354 1.8424 1.6012 0.2130  0.1969  -0.3544 371 LEU A O   
2669 C CB  . LEU A 344 ? 1.3359 1.7953 1.5424 0.2069  0.1754  -0.3158 371 LEU A CB  
2670 C CG  . LEU A 344 ? 1.4290 1.9171 1.6568 0.2364  0.1346  -0.3335 371 LEU A CG  
2671 C CD1 . LEU A 344 ? 1.4002 1.8432 1.5643 0.2602  0.1063  -0.2976 371 LEU A CD1 
2672 C CD2 . LEU A 344 ? 1.5067 2.0220 1.7708 0.2218  0.1375  -0.3560 371 LEU A CD2 
2673 N N   . VAL A 345 ? 1.2696 1.7410 1.4740 0.2647  0.1399  -0.3208 372 VAL A N   
2674 C CA  . VAL A 345 ? 1.2628 1.7729 1.5101 0.2851  0.1280  -0.3508 372 VAL A CA  
2675 C C   . VAL A 345 ? 1.3924 1.9341 1.6667 0.3157  0.0894  -0.3750 372 VAL A C   
2676 O O   . VAL A 345 ? 1.4590 1.9700 1.6891 0.3387  0.0615  -0.3536 372 VAL A O   
2677 C CB  . VAL A 345 ? 1.2663 1.7447 1.4744 0.3017  0.1231  -0.3284 372 VAL A CB  
2678 C CG1 . VAL A 345 ? 1.1821 1.6948 1.4267 0.3326  0.1001  -0.3570 372 VAL A CG1 
2679 C CG2 . VAL A 345 ? 1.2352 1.6971 1.4309 0.2737  0.1611  -0.3163 372 VAL A CG2 
2680 N N   . GLU A 346 ? 1.3508 1.9532 1.6966 0.3166  0.0882  -0.4215 373 GLU A N   
2681 C CA  . GLU A 346 ? 1.3901 2.0300 1.7671 0.3487  0.0495  -0.4514 373 GLU A CA  
2682 C C   . GLU A 346 ? 1.4306 2.0656 1.7930 0.3910  0.0180  -0.4524 373 GLU A C   
2683 O O   . GLU A 346 ? 1.3790 2.0319 1.7674 0.3931  0.0278  -0.4671 373 GLU A O   
2684 C CB  . GLU A 346 ? 1.4605 2.1718 1.9247 0.3351  0.0598  -0.5061 373 GLU A CB  
2685 C CG  . GLU A 346 ? 1.5445 2.3037 2.0482 0.3710  0.0174  -0.5444 373 GLU A CG  
2686 C CD  . GLU A 346 ? 1.6126 2.4477 2.2098 0.3550  0.0297  -0.6040 373 GLU A CD  
2687 O OE1 . GLU A 346 ? 1.6443 2.4843 2.2652 0.3111  0.0723  -0.6092 373 GLU A OE1 
2688 O OE2 . GLU A 346 ? 1.5517 2.4404 2.1982 0.3869  -0.0025 -0.6472 373 GLU A OE2 
2689 N N   . ALA A 347 ? 1.7061 2.1950 1.5244 0.1809  0.0664  -0.2018 374 ALA A N   
2690 C CA  . ALA A 347 ? 1.7172 2.2047 1.5558 0.2108  0.0638  -0.1829 374 ALA A CA  
2691 C C   . ALA A 347 ? 1.8238 2.3745 1.6757 0.2273  0.0637  -0.1782 374 ALA A C   
2692 O O   . ALA A 347 ? 1.8604 2.4648 1.7072 0.2131  0.0644  -0.1844 374 ALA A O   
2693 C CB  . ALA A 347 ? 1.7454 2.2232 1.5880 0.2124  0.0626  -0.1629 374 ALA A CB  
2694 N N   . VAL A 348 ? 1.7241 2.2673 1.5972 0.2575  0.0615  -0.1660 375 VAL A N   
2695 C CA  . VAL A 348 ? 1.6281 2.2296 1.5274 0.2793  0.0600  -0.1580 375 VAL A CA  
2696 C C   . VAL A 348 ? 1.6185 2.2492 1.5246 0.2856  0.0471  -0.1313 375 VAL A C   
2697 O O   . VAL A 348 ? 1.6925 2.2855 1.5998 0.2988  0.0417  -0.1139 375 VAL A O   
2698 C CB  . VAL A 348 ? 1.5990 2.1721 1.5176 0.3107  0.0654  -0.1600 375 VAL A CB  
2699 C CG1 . VAL A 348 ? 1.5610 2.1981 1.5192 0.3365  0.0649  -0.1508 375 VAL A CG1 
2700 C CG2 . VAL A 348 ? 1.4922 2.0260 1.3904 0.3001  0.0785  -0.1866 375 VAL A CG2 
2701 N N   . ASP A 349 ? 1.5237 2.2183 1.4304 0.2733  0.0407  -0.1270 376 ASP A N   
2702 C CA  . ASP A 349 ? 1.5836 2.3043 1.4873 0.2748  0.0251  -0.1009 376 ASP A CA  
2703 C C   . ASP A 349 ? 1.7270 2.4649 1.6701 0.3107  0.0136  -0.0803 376 ASP A C   
2704 O O   . ASP A 349 ? 1.6185 2.4171 1.5944 0.3209  0.0056  -0.0756 376 ASP A O   
2705 C CB  . ASP A 349 ? 1.5059 2.2856 1.3947 0.2485  0.0171  -0.1020 376 ASP A CB  
2706 C CG  . ASP A 349 ? 1.6664 2.4585 1.5326 0.2408  0.0001  -0.0764 376 ASP A CG  
2707 O OD1 . ASP A 349 ? 1.7175 2.4702 1.5765 0.2533  -0.0023 -0.0587 376 ASP A OD1 
2708 O OD2 . ASP A 349 ? 1.6826 2.5205 1.5335 0.2196  -0.0117 -0.0734 376 ASP A OD2 
2709 N N   . GLY A 350 ? 1.8455 2.5301 1.7898 0.3300  0.0118  -0.0670 377 GLY A N   
2710 C CA  . GLY A 350 ? 1.8423 2.5318 1.8221 0.3655  -0.0003 -0.0466 377 GLY A CA  
2711 C C   . GLY A 350 ? 1.8012 2.5382 1.7881 0.3674  -0.0242 -0.0179 377 GLY A C   
2712 O O   . GLY A 350 ? 1.8036 2.5517 1.8267 0.3978  -0.0384 0.0013  377 GLY A O   
2713 N N   . LYS A 351 ? 1.8305 2.5907 1.7812 0.3351  -0.0305 -0.0140 378 LYS A N   
2714 C CA  . LYS A 351 ? 1.8958 2.6987 1.8424 0.3298  -0.0570 0.0132  378 LYS A CA  
2715 C C   . LYS A 351 ? 1.8513 2.7329 1.8318 0.3264  -0.0680 0.0094  378 LYS A C   
2716 O O   . LYS A 351 ? 1.8403 2.7652 1.8447 0.3346  -0.0956 0.0349  378 LYS A O   
2717 C CB  . LYS A 351 ? 1.8686 2.6479 1.7489 0.2942  -0.0573 0.0195  378 LYS A CB  
2718 C CG  . LYS A 351 ? 1.8790 2.5854 1.7319 0.2930  -0.0406 0.0207  378 LYS A CG  
2719 C CD  . LYS A 351 ? 1.8554 2.5395 1.6468 0.2568  -0.0298 0.0189  378 LYS A CD  
2720 C CE  . LYS A 351 ? 1.7970 2.4151 1.5752 0.2560  -0.0096 0.0194  378 LYS A CE  
2721 N NZ  . LYS A 351 ? 1.8962 2.4922 1.6207 0.2230  0.0079  0.0156  378 LYS A NZ  
2722 N N   . ALA A 352 ? 1.7976 2.6985 1.7831 0.3132  -0.0490 -0.0199 379 ALA A N   
2723 C CA  . ALA A 352 ? 1.7123 2.6893 1.7340 0.3071  -0.0555 -0.0253 379 ALA A CA  
2724 C C   . ALA A 352 ? 1.7184 2.7266 1.8134 0.3444  -0.0474 -0.0293 379 ALA A C   
2725 O O   . ALA A 352 ? 1.6247 2.6969 1.7595 0.3411  -0.0447 -0.0378 379 ALA A O   
2726 C CB  . ALA A 352 ? 1.5614 2.5419 1.5496 0.2719  -0.0381 -0.0543 379 ALA A CB  
2727 N N   . MET A 353 ? 1.8882 2.8514 2.0020 0.3789  -0.0416 -0.0240 380 MET A N   
2728 C CA  . MET A 353 ? 1.9006 2.8819 2.0799 0.4177  -0.0298 -0.0295 380 MET A CA  
2729 C C   . MET A 353 ? 1.8445 2.8635 2.0782 0.4471  -0.0587 0.0040  380 MET A C   
2730 O O   . MET A 353 ? 1.8711 2.8508 2.0840 0.4547  -0.0789 0.0285  380 MET A O   
2731 C CB  . MET A 353 ? 2.0205 2.9209 2.1836 0.4375  -0.0071 -0.0455 380 MET A CB  
2732 C CG  . MET A 353 ? 2.0185 2.8779 2.1349 0.4111  0.0182  -0.0774 380 MET A CG  
2733 S SD  . MET A 353 ? 1.8800 2.6373 1.9729 0.4305  0.0356  -0.0908 380 MET A SD  
2734 C CE  . MET A 353 ? 1.8562 2.6310 2.0130 0.4786  0.0486  -0.0945 380 MET A CE  
2735 N N   . ASN A 354 ? 1.6408 2.7358 1.9466 0.4628  -0.0611 0.0063  381 ASN A N   
2736 C CA  . ASN A 354 ? 1.6985 2.8321 2.0712 0.4953  -0.0895 0.0382  381 ASN A CA  
2737 C C   . ASN A 354 ? 1.7963 2.8804 2.2026 0.5433  -0.0749 0.0363  381 ASN A C   
2738 O O   . ASN A 354 ? 1.7556 2.7794 2.1333 0.5493  -0.0426 0.0091  381 ASN A O   
2739 C CB  . ASN A 354 ? 1.5887 2.8246 2.0400 0.4970  -0.0965 0.0421  381 ASN A CB  
2740 C CG  . ASN A 354 ? 1.4882 2.7484 1.9638 0.4962  -0.0533 0.0053  381 ASN A CG  
2741 O OD1 . ASN A 354 ? 1.4334 2.7009 1.9693 0.5336  -0.0282 -0.0061 381 ASN A OD1 
2742 N ND2 . ASN A 354 ? 1.3855 2.6541 1.8104 0.4527  -0.0432 -0.0140 381 ASN A ND2 
2743 N N   . THR A 355 ? 1.8999 3.0054 2.3657 0.5767  -0.1021 0.0667  382 THR A N   
2744 C CA  . THR A 355 ? 1.9638 3.0184 2.4620 0.6240  -0.0924 0.0678  382 THR A CA  
2745 C C   . THR A 355 ? 2.0020 3.0702 2.5529 0.6521  -0.0490 0.0349  382 THR A C   
2746 O O   . THR A 355 ? 2.0144 3.0184 2.5664 0.6841  -0.0288 0.0230  382 THR A O   
2747 C CB  . THR A 355 ? 1.9233 3.0031 2.4806 0.6536  -0.1342 0.1094  382 THR A CB  
2748 O OG1 . THR A 355 ? 1.9882 3.0725 2.4952 0.6191  -0.1752 0.1400  382 THR A OG1 
2749 C CG2 . THR A 355 ? 1.9278 2.9281 2.4881 0.6937  -0.1326 0.1162  382 THR A CG2 
2750 N N   . SER A 356 ? 1.9181 3.0644 2.5079 0.6386  -0.0329 0.0195  383 SER A N   
2751 C CA  . SER A 356 ? 1.8273 2.9886 2.4636 0.6618  0.0133  -0.0127 383 SER A CA  
2752 C C   . SER A 356 ? 1.8551 2.9427 2.4090 0.6403  0.0512  -0.0508 383 SER A C   
2753 O O   . SER A 356 ? 1.8130 2.8496 2.3675 0.6667  0.0851  -0.0742 383 SER A O   
2754 C CB  . SER A 356 ? 1.7500 3.0233 2.4593 0.6518  0.0175  -0.0136 383 SER A CB  
2755 O OG  . SER A 356 ? 1.7298 3.0727 2.5230 0.6718  -0.0220 0.0240  383 SER A OG  
2756 N N   . GLN A 357 ? 1.8372 2.9140 2.3185 0.5922  0.0450  -0.0574 384 GLN A N   
2757 C CA  . GLN A 357 ? 1.7324 2.7401 2.1386 0.5691  0.0749  -0.0904 384 GLN A CA  
2758 C C   . GLN A 357 ? 1.8194 2.7212 2.1713 0.5805  0.0724  -0.0900 384 GLN A C   
2759 O O   . GLN A 357 ? 1.7519 2.5871 2.0581 0.5754  0.0988  -0.1172 384 GLN A O   
2760 C CB  . GLN A 357 ? 1.5928 2.6191 1.9443 0.5165  0.0663  -0.0956 384 GLN A CB  
2761 C CG  . GLN A 357 ? 1.5163 2.6352 1.9086 0.4978  0.0750  -0.1036 384 GLN A CG  
2762 C CD  . GLN A 357 ? 1.4295 2.5610 1.7648 0.4461  0.0626  -0.1069 384 GLN A CD  
2763 O OE1 . GLN A 357 ? 1.5315 2.6273 1.8154 0.4278  0.0388  -0.0932 384 GLN A OE1 
2764 N NE2 . GLN A 357 ? 1.3285 2.5083 1.6717 0.4219  0.0810  -0.1258 384 GLN A NE2 
2765 N N   . VAL A 358 ? 1.9154 2.7980 2.2690 0.5928  0.0397  -0.0584 385 VAL A N   
2766 C CA  . VAL A 358 ? 1.9010 2.6859 2.2122 0.6053  0.0364  -0.0548 385 VAL A CA  
2767 C C   . VAL A 358 ? 1.9137 2.6574 2.2546 0.6481  0.0610  -0.0705 385 VAL A C   
2768 O O   . VAL A 358 ? 1.8110 2.4700 2.1033 0.6479  0.0785  -0.0903 385 VAL A O   
2769 C CB  . VAL A 358 ? 1.8325 2.6105 2.1423 0.6092  -0.0032 -0.0153 385 VAL A CB  
2770 C CG1 . VAL A 358 ? 1.7715 2.4535 2.0530 0.6285  -0.0065 -0.0088 385 VAL A CG1 
2771 C CG2 . VAL A 358 ? 1.8916 2.6859 2.1505 0.5633  -0.0205 -0.0052 385 VAL A CG2 
2772 N N   . GLU A 359 ? 2.0059 2.8067 2.4281 0.6852  0.0621  -0.0617 386 GLU A N   
2773 C CA  . GLU A 359 ? 1.9776 2.7438 2.4341 0.7288  0.0912  -0.0794 386 GLU A CA  
2774 C C   . GLU A 359 ? 1.9343 2.6991 2.3753 0.7194  0.1386  -0.1210 386 GLU A C   
2775 O O   . GLU A 359 ? 1.8841 2.5888 2.3179 0.7454  0.1692  -0.1438 386 GLU A O   
2776 C CB  . GLU A 359 ? 1.9644 2.7990 2.5237 0.7724  0.0800  -0.0575 386 GLU A CB  
2777 C CG  . GLU A 359 ? 1.9624 2.7971 2.5370 0.7819  0.0298  -0.0134 386 GLU A CG  
2778 C CD  . GLU A 359 ? 1.9407 2.8540 2.6235 0.8200  0.0120  0.0115  386 GLU A CD  
2779 O OE1 . GLU A 359 ? 1.8626 2.8426 2.6156 0.8365  0.0402  -0.0054 386 GLU A OE1 
2780 O OE2 . GLU A 359 ? 2.0647 2.9733 2.7645 0.8325  -0.0307 0.0491  386 GLU A OE2 
2781 N N   . ALA A 360 ? 1.9101 2.7345 2.3403 0.6813  0.1454  -0.1313 387 ALA A N   
2782 C CA  . ALA A 360 ? 1.8648 2.6876 2.2744 0.6672  0.1894  -0.1690 387 ALA A CA  
2783 C C   . ALA A 360 ? 1.8374 2.5476 2.1514 0.6486  0.2035  -0.1932 387 ALA A C   
2784 O O   . ALA A 360 ? 1.7433 2.4213 2.0312 0.6469  0.2421  -0.2254 387 ALA A O   
2785 C CB  . ALA A 360 ? 1.7841 2.6908 2.1980 0.6262  0.1873  -0.1711 387 ALA A CB  
2786 N N   . LEU A 361 ? 1.8641 2.5131 2.1255 0.6329  0.1730  -0.1776 388 LEU A N   
2787 C CA  . LEU A 361 ? 1.8879 2.4317 2.0653 0.6126  0.1781  -0.1952 388 LEU A CA  
2788 C C   . LEU A 361 ? 1.9694 2.4222 2.1337 0.6456  0.1762  -0.1925 388 LEU A C   
2789 O O   . LEU A 361 ? 2.0437 2.4021 2.1403 0.6309  0.1787  -0.2064 388 LEU A O   
2790 C CB  . LEU A 361 ? 1.8534 2.3865 1.9851 0.5715  0.1483  -0.1808 388 LEU A CB  
2791 C CG  . LEU A 361 ? 1.7523 2.3776 1.9016 0.5418  0.1395  -0.1742 388 LEU A CG  
2792 C CD1 . LEU A 361 ? 1.7166 2.3194 1.8200 0.5063  0.1137  -0.1610 388 LEU A CD1 
2793 C CD2 . LEU A 361 ? 1.6228 2.2795 1.7637 0.5217  0.1701  -0.2038 388 LEU A CD2 
2794 N N   . GLY A 362 ? 1.9409 2.4169 2.1684 0.6885  0.1689  -0.1738 389 GLY A N   
2795 C CA  . GLY A 362 ? 1.9732 2.3617 2.1903 0.7209  0.1639  -0.1688 389 GLY A CA  
2796 C C   . GLY A 362 ? 2.0441 2.3777 2.2209 0.7037  0.1257  -0.1425 389 GLY A C   
2797 O O   . GLY A 362 ? 2.0717 2.3069 2.1902 0.6960  0.1239  -0.1505 389 GLY A O   
2798 N N   . ILE A 363 ? 1.9797 2.3749 2.1857 0.6955  0.0950  -0.1105 390 ILE A N   
2799 C CA  . ILE A 363 ? 2.0202 2.3763 2.1895 0.6737  0.0628  -0.0846 390 ILE A CA  
2800 C C   . ILE A 363 ? 2.0076 2.3635 2.2165 0.7060  0.0357  -0.0500 390 ILE A C   
2801 O O   . ILE A 363 ? 1.9091 2.3427 2.1767 0.7232  0.0247  -0.0323 390 ILE A O   
2802 C CB  . ILE A 363 ? 1.9151 2.3303 2.0685 0.6309  0.0512  -0.0768 390 ILE A CB  
2803 C CG1 . ILE A 363 ? 1.8138 2.2220 1.9269 0.5985  0.0751  -0.1099 390 ILE A CG1 
2804 C CG2 . ILE A 363 ? 1.9274 2.3039 2.0475 0.6104  0.0238  -0.0501 390 ILE A CG2 
2805 C CD1 . ILE A 363 ? 1.7307 2.1876 1.8253 0.5569  0.0656  -0.1056 390 ILE A CD1 
2806 N N   . GLN A 364 ? 2.1466 2.4134 2.3235 0.7122  0.0221  -0.0387 391 GLN A N   
2807 C CA  . GLN A 364 ? 2.1982 2.4487 2.4000 0.7373  -0.0071 -0.0033 391 GLN A CA  
2808 C C   . GLN A 364 ? 2.1811 2.3685 2.3303 0.7085  -0.0288 0.0171  391 GLN A C   
2809 O O   . GLN A 364 ? 2.1467 2.2597 2.2490 0.6921  -0.0201 0.0010  391 GLN A O   
2810 C CB  . GLN A 364 ? 2.0515 2.2477 2.2795 0.7858  0.0021  -0.0106 391 GLN A CB  
2811 C CG  . GLN A 364 ? 2.0653 2.2180 2.3049 0.8084  -0.0307 0.0256  391 GLN A CG  
2812 C CD  . GLN A 364 ? 2.2163 2.2978 2.4722 0.8545  -0.0206 0.0153  391 GLN A CD  
2813 O OE1 . GLN A 364 ? 2.2127 2.3130 2.5037 0.8833  0.0096  -0.0116 391 GLN A OE1 
2814 N NE2 . GLN A 364 ? 2.3738 2.3702 2.6029 0.8611  -0.0436 0.0361  391 GLN A NE2 
2815 N N   . MET A 365 ? 2.0904 2.3071 2.2472 0.7005  -0.0571 0.0532  392 MET A N   
2816 C CA  . MET A 365 ? 2.0806 2.2433 2.1927 0.6730  -0.0743 0.0751  392 MET A CA  
2817 C C   . MET A 365 ? 2.1423 2.2062 2.2410 0.6940  -0.0821 0.0815  392 MET A C   
2818 O O   . MET A 365 ? 2.1588 2.2055 2.2895 0.7349  -0.0868 0.0856  392 MET A O   
2819 C CB  . MET A 365 ? 1.9310 2.1404 2.0488 0.6619  -0.1011 0.1132  392 MET A CB  
2820 C CG  . MET A 365 ? 2.1370 2.3037 2.2077 0.6268  -0.1112 0.1342  392 MET A CG  
2821 S SD  . MET A 365 ? 2.1605 2.3534 2.2256 0.6192  -0.1441 0.1830  392 MET A SD  
2822 C CE  . MET A 365 ? 2.1129 2.2517 2.2094 0.6676  -0.1682 0.2056  392 MET A CE  
2823 N N   . LEU A 366 ? 2.0553 2.0532 2.1096 0.6659  -0.0837 0.0822  393 LEU A N   
2824 C CA  . LEU A 366 ? 2.0711 1.9707 2.1069 0.6781  -0.0956 0.0921  393 LEU A CA  
2825 C C   . LEU A 366 ? 2.2107 2.1065 2.2662 0.6992  -0.1233 0.1315  393 LEU A C   
2826 O O   . LEU A 366 ? 2.2135 2.1476 2.2647 0.6777  -0.1382 0.1600  393 LEU A O   
2827 C CB  . LEU A 366 ? 2.0569 1.9012 2.0510 0.6379  -0.0980 0.0944  393 LEU A CB  
2828 C CG  . LEU A 366 ? 2.1203 1.8564 2.0896 0.6414  -0.1112 0.1022  393 LEU A CG  
2829 C CD1 . LEU A 366 ? 2.0137 1.7017 1.9501 0.6062  -0.1048 0.0846  393 LEU A CD1 
2830 C CD2 . LEU A 366 ? 2.2207 1.9358 2.1898 0.6367  -0.1364 0.1452  393 LEU A CD2 
2831 N N   . PRO A 367 ? 2.2526 2.1003 2.3267 0.7401  -0.1306 0.1343  394 PRO A N   
2832 C CA  . PRO A 367 ? 2.2682 2.1130 2.3651 0.7624  -0.1607 0.1735  394 PRO A CA  
2833 C C   . PRO A 367 ? 2.3670 2.1621 2.4250 0.7317  -0.1829 0.2077  394 PRO A C   
2834 O O   . PRO A 367 ? 2.3938 2.1061 2.4197 0.7200  -0.1832 0.2049  394 PRO A O   
2835 C CB  . PRO A 367 ? 2.2255 2.0077 2.3438 0.8110  -0.1587 0.1620  394 PRO A CB  
2836 C CG  . PRO A 367 ? 2.1980 1.9880 2.3178 0.8186  -0.1222 0.1148  394 PRO A CG  
2837 C CD  . PRO A 367 ? 2.1400 1.9333 2.2141 0.7688  -0.1104 0.1004  394 PRO A CD  
2838 N N   . GLY A 368 ? 2.3407 2.1860 2.4000 0.7162  -0.2015 0.2407  395 GLY A N   
2839 C CA  . GLY A 368 ? 2.3231 2.1275 2.3468 0.6876  -0.2206 0.2768  395 GLY A CA  
2840 C C   . GLY A 368 ? 2.3601 2.1914 2.3508 0.6371  -0.2060 0.2766  395 GLY A C   
2841 O O   . GLY A 368 ? 2.3741 2.1725 2.3358 0.6102  -0.2157 0.3054  395 GLY A O   
2842 N N   . TYR A 369 ? 2.4061 2.2944 2.4014 0.6231  -0.1816 0.2454  396 TYR A N   
2843 C CA  . TYR A 369 ? 2.2916 2.2020 2.2600 0.5775  -0.1658 0.2430  396 TYR A CA  
2844 C C   . TYR A 369 ? 2.3191 2.2855 2.2726 0.5575  -0.1743 0.2700  396 TYR A C   
2845 O O   . TYR A 369 ? 2.3220 2.3457 2.2924 0.5733  -0.1850 0.2743  396 TYR A O   
2846 C CB  . TYR A 369 ? 2.2808 2.2291 2.2558 0.5679  -0.1394 0.2020  396 TYR A CB  
2847 C CG  . TYR A 369 ? 2.2728 2.2612 2.2280 0.5255  -0.1239 0.2000  396 TYR A CG  
2848 C CD1 . TYR A 369 ? 2.2618 2.2075 2.2002 0.4948  -0.1163 0.2056  396 TYR A CD1 
2849 C CD2 . TYR A 369 ? 2.2704 2.3384 2.2269 0.5161  -0.1169 0.1933  396 TYR A CD2 
2850 C CE1 . TYR A 369 ? 2.2465 2.2277 2.1729 0.4591  -0.0986 0.2028  396 TYR A CE1 
2851 C CE2 . TYR A 369 ? 2.2507 2.3486 2.1859 0.4787  -0.1009 0.1898  396 TYR A CE2 
2852 C CZ  . TYR A 369 ? 2.2387 2.2931 2.1604 0.4519  -0.0900 0.1939  396 TYR A CZ  
2853 O OH  . TYR A 369 ? 2.1974 2.2808 2.1039 0.4175  -0.0704 0.1891  396 TYR A OH  
2854 N N   . ARG A 370 ? 2.1864 2.1343 2.1077 0.5209  -0.1692 0.2885  397 ARG A N   
2855 C CA  . ARG A 370 ? 2.1795 2.1728 2.0718 0.4927  -0.1690 0.3085  397 ARG A CA  
2856 C C   . ARG A 370 ? 2.1826 2.1720 2.0529 0.4512  -0.1410 0.3010  397 ARG A C   
2857 O O   . ARG A 370 ? 2.1672 2.1079 2.0454 0.4431  -0.1314 0.2948  397 ARG A O   
2858 C CB  . ARG A 370 ? 2.0994 2.0640 1.9694 0.4946  -0.1975 0.3534  397 ARG A CB  
2859 C CG  . ARG A 370 ? 1.9906 1.9745 1.8866 0.5331  -0.2286 0.3661  397 ARG A CG  
2860 C CD  . ARG A 370 ? 2.0692 2.0170 1.9389 0.5315  -0.2608 0.4134  397 ARG A CD  
2861 N NE  . ARG A 370 ? 2.1102 2.0468 2.0186 0.5769  -0.2930 0.4264  397 ARG A NE  
2862 C CZ  . ARG A 370 ? 2.1859 2.0763 2.0826 0.5861  -0.3265 0.4663  397 ARG A CZ  
2863 N NH1 . ARG A 370 ? 2.2319 2.0824 2.0740 0.5509  -0.3319 0.4984  397 ARG A NH1 
2864 N NH2 . ARG A 370 ? 2.2203 2.1028 2.1626 0.6317  -0.3540 0.4746  397 ARG A NH2 
2865 N N   . ASP A 371 ? 2.4862 2.5257 2.3303 0.4246  -0.1288 0.3023  398 ASP A N   
2866 C CA  . ASP A 371 ? 2.4869 2.5287 2.3145 0.3869  -0.0979 0.2935  398 ASP A CA  
2867 C C   . ASP A 371 ? 2.5200 2.5068 2.3289 0.3663  -0.0951 0.3243  398 ASP A C   
2868 O O   . ASP A 371 ? 2.5632 2.5334 2.3418 0.3642  -0.1129 0.3582  398 ASP A O   
2869 C CB  . ASP A 371 ? 2.4925 2.5932 2.2883 0.3641  -0.0855 0.2885  398 ASP A CB  
2870 C CG  . ASP A 371 ? 2.5237 2.6223 2.2990 0.3259  -0.0510 0.2834  398 ASP A CG  
2871 O OD1 . ASP A 371 ? 2.5777 2.6726 2.3825 0.3202  -0.0306 0.2582  398 ASP A OD1 
2872 O OD2 . ASP A 371 ? 2.5815 2.6801 2.3107 0.3013  -0.0441 0.3050  398 ASP A OD2 
2873 N N   . PRO A 372 ? 2.3985 2.3561 2.2262 0.3494  -0.0750 0.3157  399 PRO A N   
2874 C CA  . PRO A 372 ? 2.4284 2.3384 2.2459 0.3264  -0.0689 0.3453  399 PRO A CA  
2875 C C   . PRO A 372 ? 2.4942 2.4250 2.2721 0.2907  -0.0434 0.3608  399 PRO A C   
2876 O O   . PRO A 372 ? 2.4086 2.3064 2.1825 0.2669  -0.0290 0.3820  399 PRO A O   
2877 C CB  . PRO A 372 ? 2.3803 2.2638 2.2407 0.3187  -0.0555 0.3271  399 PRO A CB  
2878 C CG  . PRO A 372 ? 2.2133 2.1126 2.0977 0.3448  -0.0639 0.2917  399 PRO A CG  
2879 C CD  . PRO A 372 ? 2.2553 2.2166 2.1194 0.3530  -0.0625 0.2802  399 PRO A CD  
2880 N N   . TYR A 373 ? 2.6418 2.6234 2.3882 0.2844  -0.0361 0.3510  400 TYR A N   
2881 C CA  . TYR A 373 ? 2.6555 2.6508 2.3538 0.2486  -0.0081 0.3614  400 TYR A CA  
2882 C C   . TYR A 373 ? 2.6435 2.6495 2.2806 0.2459  -0.0301 0.3851  400 TYR A C   
2883 O O   . TYR A 373 ? 2.6212 2.5958 2.2117 0.2245  -0.0288 0.4175  400 TYR A O   
2884 C CB  . TYR A 373 ? 2.6189 2.6576 2.3271 0.2335  0.0265  0.3257  400 TYR A CB  
2885 C CG  . TYR A 373 ? 2.5960 2.6225 2.3644 0.2308  0.0468  0.3063  400 TYR A CG  
2886 C CD1 . TYR A 373 ? 2.5604 2.5571 2.3444 0.2075  0.0716  0.3217  400 TYR A CD1 
2887 C CD2 . TYR A 373 ? 2.5322 2.5764 2.3427 0.2495  0.0401  0.2742  400 TYR A CD2 
2888 C CE1 . TYR A 373 ? 2.5009 2.4880 2.3472 0.2040  0.0850  0.3070  400 TYR A CE1 
2889 C CE2 . TYR A 373 ? 2.4903 2.5189 2.3528 0.2447  0.0527  0.2590  400 TYR A CE2 
2890 C CZ  . TYR A 373 ? 2.5387 2.5397 2.4220 0.2224  0.0732  0.2761  400 TYR A CZ  
2891 O OH  . TYR A 373 ? 2.5052 2.4920 2.4472 0.2163  0.0810  0.2642  400 TYR A OH  
2892 N N   . HIS A 374 ? 2.5963 2.6448 2.2317 0.2646  -0.0515 0.3717  401 HIS A N   
2893 C CA  . HIS A 374 ? 2.5372 2.5972 2.1221 0.2633  -0.0811 0.3965  401 HIS A CA  
2894 C C   . HIS A 374 ? 2.5087 2.5708 2.1291 0.3045  -0.1268 0.4068  401 HIS A C   
2895 O O   . HIS A 374 ? 2.4805 2.5656 2.0784 0.3101  -0.1574 0.4229  401 HIS A O   
2896 C CB  . HIS A 374 ? 2.4865 2.5976 2.0336 0.2439  -0.0691 0.3777  401 HIS A CB  
2897 C CG  . HIS A 374 ? 2.4622 2.6159 2.0540 0.2529  -0.0498 0.3342  401 HIS A CG  
2898 N ND1 . HIS A 374 ? 2.4316 2.6094 2.0812 0.2881  -0.0697 0.3162  401 HIS A ND1 
2899 C CD2 . HIS A 374 ? 2.3633 2.5369 1.9480 0.2305  -0.0119 0.3055  401 HIS A CD2 
2900 C CE1 . HIS A 374 ? 2.2946 2.5043 1.9666 0.2846  -0.0465 0.2795  401 HIS A CE1 
2901 N NE2 . HIS A 374 ? 2.3529 2.5605 1.9885 0.2507  -0.0131 0.2727  401 HIS A NE2 
2902 N N   . GLY A 375 ? 2.6087 2.6453 2.2851 0.3332  -0.1324 0.3979  402 GLY A N   
2903 C CA  . GLY A 375 ? 2.5895 2.6140 2.2988 0.3735  -0.1711 0.4100  402 GLY A CA  
2904 C C   . GLY A 375 ? 2.4942 2.5775 2.2370 0.4013  -0.1870 0.3900  402 GLY A C   
2905 O O   . GLY A 375 ? 2.4459 2.5301 2.2104 0.4317  -0.2215 0.4071  402 GLY A O   
2906 N N   . ARG A 376 ? 2.3712 2.5041 2.1234 0.3921  -0.1626 0.3550  403 ARG A N   
2907 C CA  . ARG A 376 ? 2.2736 2.4649 2.0605 0.4167  -0.1772 0.3379  403 ARG A CA  
2908 C C   . ARG A 376 ? 2.2291 2.4160 2.0744 0.4492  -0.1686 0.3072  403 ARG A C   
2909 O O   . ARG A 376 ? 2.2713 2.4234 2.1225 0.4423  -0.1454 0.2894  403 ARG A O   
2910 C CB  . ARG A 376 ? 2.1850 2.4335 1.9462 0.3887  -0.1600 0.3178  403 ARG A CB  
2911 C CG  . ARG A 376 ? 2.2667 2.5152 1.9577 0.3524  -0.1647 0.3436  403 ARG A CG  
2912 C CD  . ARG A 376 ? 2.2789 2.5676 1.9381 0.3209  -0.1385 0.3179  403 ARG A CD  
2913 N NE  . ARG A 376 ? 2.3863 2.6577 1.9666 0.2814  -0.1317 0.3379  403 ARG A NE  
2914 C CZ  . ARG A 376 ? 2.3522 2.6341 1.8900 0.2479  -0.0992 0.3183  403 ARG A CZ  
2915 N NH1 . ARG A 376 ? 2.2928 2.6033 1.8615 0.2485  -0.0735 0.2799  403 ARG A NH1 
2916 N NH2 . ARG A 376 ? 2.3790 2.6371 1.8380 0.2125  -0.0916 0.3374  403 ARG A NH2 
2917 N N   . PRO A 377 ? 2.0608 2.2810 1.9500 0.4841  -0.1868 0.3010  404 PRO A N   
2918 C CA  . PRO A 377 ? 2.0944 2.3117 2.0304 0.5122  -0.1728 0.2675  404 PRO A CA  
2919 C C   . PRO A 377 ? 2.1559 2.4108 2.0907 0.4923  -0.1426 0.2295  404 PRO A C   
2920 O O   . PRO A 377 ? 2.1264 2.4037 2.0261 0.4573  -0.1302 0.2279  404 PRO A O   
2921 C CB  . PRO A 377 ? 1.9890 2.2436 1.9731 0.5516  -0.1968 0.2734  404 PRO A CB  
2922 C CG  . PRO A 377 ? 1.9785 2.2278 1.9438 0.5496  -0.2318 0.3179  404 PRO A CG  
2923 C CD  . PRO A 377 ? 2.0332 2.2856 1.9339 0.5013  -0.2229 0.3283  404 PRO A CD  
2924 N N   . LEU A 378 ? 2.1591 2.4164 2.1284 0.5136  -0.1298 0.1983  405 LEU A N   
2925 C CA  . LEU A 378 ? 2.1180 2.4055 2.0853 0.4949  -0.1039 0.1627  405 LEU A CA  
2926 C C   . LEU A 378 ? 2.0869 2.4539 2.0529 0.4820  -0.1063 0.1592  405 LEU A C   
2927 O O   . LEU A 378 ? 1.9798 2.3891 1.9724 0.5023  -0.1261 0.1715  405 LEU A O   
2928 C CB  . LEU A 378 ? 2.1167 2.3872 2.1145 0.5204  -0.0918 0.1322  405 LEU A CB  
2929 C CG  . LEU A 378 ? 2.0651 2.3526 2.0571 0.5007  -0.0669 0.0955  405 LEU A CG  
2930 C CD1 . LEU A 378 ? 2.0328 2.2690 1.9976 0.4715  -0.0556 0.0917  405 LEU A CD1 
2931 C CD2 . LEU A 378 ? 2.0335 2.3129 2.0508 0.5276  -0.0564 0.0677  405 LEU A CD2 
2932 N N   . THR A 379 ? 2.0766 2.4623 2.0141 0.4477  -0.0876 0.1430  406 THR A N   
2933 C CA  . THR A 379 ? 2.0276 2.4795 1.9521 0.4281  -0.0896 0.1393  406 THR A CA  
2934 C C   . THR A 379 ? 1.8223 2.3158 1.7715 0.4300  -0.0743 0.1039  406 THR A C   
2935 O O   . THR A 379 ? 1.7968 2.2614 1.7601 0.4382  -0.0575 0.0800  406 THR A O   
2936 C CB  . THR A 379 ? 1.9542 2.3970 1.8253 0.3876  -0.0770 0.1437  406 THR A CB  
2937 O OG1 . THR A 379 ? 1.8945 2.3165 1.7629 0.3715  -0.0491 0.1152  406 THR A OG1 
2938 C CG2 . THR A 379 ? 1.9249 2.3178 1.7679 0.3822  -0.0853 0.1769  406 THR A CG2 
2939 N N   . LYS A 380 ? 1.6461 2.2056 1.5964 0.4193  -0.0818 0.1021  407 LYS A N   
2940 C CA  . LYS A 380 ? 1.5897 2.1937 1.5612 0.4166  -0.0677 0.0708  407 LYS A CA  
2941 C C   . LYS A 380 ? 1.7054 2.2873 1.6451 0.3866  -0.0423 0.0440  407 LYS A C   
2942 O O   . LYS A 380 ? 1.7058 2.2909 1.6603 0.3882  -0.0266 0.0159  407 LYS A O   
2943 C CB  . LYS A 380 ? 1.5070 2.1865 1.4871 0.4078  -0.0851 0.0786  407 LYS A CB  
2944 C CG  . LYS A 380 ? 1.4948 2.2172 1.5372 0.4437  -0.1038 0.0906  407 LYS A CG  
2945 C CD  . LYS A 380 ? 1.4797 2.2820 1.5377 0.4304  -0.1219 0.0968  407 LYS A CD  
2946 C CE  . LYS A 380 ? 1.4744 2.3283 1.6115 0.4677  -0.1360 0.1054  407 LYS A CE  
2947 N NZ  . LYS A 380 ? 1.6233 2.5595 1.7837 0.4527  -0.1577 0.1148  407 LYS A NZ  
2948 N N   . GLY A 381 ? 1.8728 2.1578 1.9918 0.6680  -0.0563 0.0297  408 GLY A N   
2949 C CA  . GLY A 381 ? 1.8902 2.1597 1.9687 0.6281  -0.0429 0.0203  408 GLY A CA  
2950 C C   . GLY A 381 ? 1.8841 2.1099 1.9341 0.6258  -0.0079 0.0027  408 GLY A C   
2951 O O   . GLY A 381 ? 1.8478 2.0943 1.8984 0.6024  0.0131  -0.0104 408 GLY A O   
2952 N N   . GLU A 382 ? 1.9152 2.0787 1.9386 0.6491  -0.0024 0.0028  409 GLU A N   
2953 C CA  . GLU A 382 ? 1.8996 2.0188 1.8963 0.6485  0.0293  -0.0148 409 GLU A CA  
2954 C C   . GLU A 382 ? 1.9637 2.1280 2.0093 0.6658  0.0557  -0.0326 409 GLU A C   
2955 O O   . GLU A 382 ? 1.9716 2.1088 1.9962 0.6608  0.0838  -0.0504 409 GLU A O   
2956 C CB  . GLU A 382 ? 1.9260 1.9643 1.8827 0.6685  0.0262  -0.0090 409 GLU A CB  
2957 C CG  . GLU A 382 ? 1.9401 1.9264 1.8382 0.6477  0.0076  0.0064  409 GLU A CG  
2958 C CD  . GLU A 382 ? 1.9855 1.8947 1.8468 0.6670  0.0026  0.0158  409 GLU A CD  
2959 O OE1 . GLU A 382 ? 2.0974 1.9988 1.9865 0.7029  0.0018  0.0167  409 GLU A OE1 
2960 O OE2 . GLU A 382 ? 1.8676 1.7239 1.6731 0.6465  -0.0002 0.0228  409 GLU A OE2 
2961 N N   . LEU A 383 ? 1.9314 2.1657 2.0409 0.6852  0.0475  -0.0286 410 LEU A N   
2962 C CA  . LEU A 383 ? 1.9327 2.2203 2.0926 0.7011  0.0744  -0.0455 410 LEU A CA  
2963 C C   . LEU A 383 ? 1.8690 2.2087 2.0370 0.6648  0.0906  -0.0547 410 LEU A C   
2964 O O   . LEU A 383 ? 1.7911 2.1245 1.9457 0.6564  0.1212  -0.0733 410 LEU A O   
2965 C CB  . LEU A 383 ? 1.8694 2.2185 2.0998 0.7361  0.0595  -0.0360 410 LEU A CB  
2966 C CG  . LEU A 383 ? 1.7659 2.1981 2.0630 0.7484  0.0834  -0.0495 410 LEU A CG  
2967 C CD1 . LEU A 383 ? 1.7650 2.1652 2.0548 0.7720  0.1198  -0.0731 410 LEU A CD1 
2968 C CD2 . LEU A 383 ? 1.6172 2.1198 1.9875 0.7774  0.0618  -0.0353 410 LEU A CD2 
2969 N N   . GLY A 384 ? 1.8588 2.2477 2.0459 0.6417  0.0691  -0.0416 411 GLY A N   
2970 C CA  . GLY A 384 ? 1.7132 2.1505 1.9097 0.6067  0.0815  -0.0473 411 GLY A CA  
2971 C C   . GLY A 384 ? 1.8285 2.2137 1.9625 0.5742  0.0940  -0.0544 411 GLY A C   
2972 O O   . GLY A 384 ? 1.8442 2.2568 1.9794 0.5507  0.1139  -0.0636 411 GLY A O   
2973 N N   . CYS A 385 ? 1.8502 2.1627 1.9299 0.5717  0.0822  -0.0490 412 CYS A N   
2974 C CA  . CYS A 385 ? 1.8774 2.1430 1.9010 0.5426  0.0939  -0.0551 412 CYS A CA  
2975 C C   . CYS A 385 ? 1.8388 2.0806 1.8472 0.5487  0.1265  -0.0743 412 CYS A C   
2976 O O   . CYS A 385 ? 1.7528 1.9946 1.7394 0.5225  0.1435  -0.0831 412 CYS A O   
2977 C CB  . CYS A 385 ? 1.9959 2.1950 1.9680 0.5386  0.0746  -0.0440 412 CYS A CB  
2978 S SG  . CYS A 385 ? 2.0081 2.1666 1.9212 0.4992  0.0821  -0.0468 412 CYS A SG  
2979 N N   . PHE A 386 ? 1.8806 2.1004 1.8989 0.5832  0.1347  -0.0812 413 PHE A N   
2980 C CA  . PHE A 386 ? 1.8173 2.0176 1.8242 0.5912  0.1663  -0.1025 413 PHE A CA  
2981 C C   . PHE A 386 ? 1.7524 2.0248 1.7980 0.5841  0.1885  -0.1143 413 PHE A C   
2982 O O   . PHE A 386 ? 1.6869 1.9525 1.7087 0.5679  0.2132  -0.1297 413 PHE A O   
2983 C CB  . PHE A 386 ? 1.8281 1.9915 1.8433 0.6332  0.1693  -0.1076 413 PHE A CB  
2984 C CG  . PHE A 386 ? 1.8367 1.9612 1.8278 0.6413  0.2000  -0.1313 413 PHE A CG  
2985 C CD1 . PHE A 386 ? 1.7122 1.8840 1.7367 0.6534  0.2272  -0.1502 413 PHE A CD1 
2986 C CD2 . PHE A 386 ? 1.9184 1.9593 1.8522 0.6355  0.2018  -0.1353 413 PHE A CD2 
2987 C CE1 . PHE A 386 ? 1.7559 1.8889 1.7532 0.6602  0.2554  -0.1742 413 PHE A CE1 
2988 C CE2 . PHE A 386 ? 1.9043 1.9060 1.8127 0.6406  0.2283  -0.1583 413 PHE A CE2 
2989 C CZ  . PHE A 386 ? 1.8527 1.8987 1.7911 0.6534  0.2550  -0.1787 413 PHE A CZ  
2990 N N   . LEU A 387 ? 1.7158 2.0596 1.8204 0.5943  0.1797  -0.1062 414 LEU A N   
2991 C CA  . LEU A 387 ? 1.5877 2.0065 1.7336 0.5874  0.2015  -0.1154 414 LEU A CA  
2992 C C   . LEU A 387 ? 1.5095 1.9460 1.6334 0.5420  0.2041  -0.1122 414 LEU A C   
2993 O O   . LEU A 387 ? 1.4261 1.8936 1.5526 0.5284  0.2300  -0.1241 414 LEU A O   
2994 C CB  . LEU A 387 ? 1.4960 1.9902 1.7137 0.6070  0.1884  -0.1049 414 LEU A CB  
2995 C CG  . LEU A 387 ? 1.5457 2.0335 1.7959 0.6561  0.1856  -0.1065 414 LEU A CG  
2996 C CD1 . LEU A 387 ? 1.4625 2.0342 1.7877 0.6716  0.1695  -0.0935 414 LEU A CD1 
2997 C CD2 . LEU A 387 ? 1.4671 1.9399 1.7148 0.6805  0.2219  -0.1313 414 LEU A CD2 
2998 N N   . SER A 388 ? 1.6413 2.0572 1.7420 0.5188  0.1779  -0.0962 415 SER A N   
2999 C CA  . SER A 388 ? 1.5658 1.9904 1.6437 0.4779  0.1786  -0.0924 415 SER A CA  
3000 C C   . SER A 388 ? 1.5875 1.9633 1.6121 0.4636  0.1996  -0.1053 415 SER A C   
3001 O O   . SER A 388 ? 1.5213 1.9215 1.5393 0.4393  0.2161  -0.1101 415 SER A O   
3002 C CB  . SER A 388 ? 1.4928 1.8984 1.5546 0.4605  0.1465  -0.0748 415 SER A CB  
3003 O OG  . SER A 388 ? 1.5158 1.9688 1.6251 0.4699  0.1250  -0.0631 415 SER A OG  
3004 N N   . HIS A 389 ? 1.7036 2.0108 1.6890 0.4766  0.1983  -0.1098 416 HIS A N   
3005 C CA  . HIS A 389 ? 1.6440 1.9065 1.5819 0.4651  0.2184  -0.1238 416 HIS A CA  
3006 C C   . HIS A 389 ? 1.7315 2.0154 1.6830 0.4798  0.2492  -0.1443 416 HIS A C   
3007 O O   . HIS A 389 ? 1.6874 1.9688 1.6118 0.4603  0.2690  -0.1557 416 HIS A O   
3008 C CB  . HIS A 389 ? 1.6544 1.8398 1.5503 0.4748  0.2091  -0.1230 416 HIS A CB  
3009 C CG  . HIS A 389 ? 1.7410 1.9004 1.6111 0.4555  0.1851  -0.1061 416 HIS A CG  
3010 N ND1 . HIS A 389 ? 1.6213 1.7527 1.4497 0.4269  0.1869  -0.1053 416 HIS A ND1 
3011 C CD2 . HIS A 389 ? 1.7217 1.8803 1.6014 0.4614  0.1591  -0.0899 416 HIS A CD2 
3012 C CE1 . HIS A 389 ? 1.5262 1.6408 1.3410 0.4176  0.1651  -0.0903 416 HIS A CE1 
3013 N NE2 . HIS A 389 ? 1.6294 1.7584 1.4721 0.4372  0.1481  -0.0814 416 HIS A NE2 
3014 N N   . TYR A 390 ? 1.6581 1.9644 1.6510 0.5149  0.2534  -0.1493 417 TYR A N   
3015 C CA  . TYR A 390 ? 1.6167 1.9469 1.6259 0.5328  0.2847  -0.1706 417 TYR A CA  
3016 C C   . TYR A 390 ? 1.6163 2.0185 1.6472 0.5092  0.3016  -0.1725 417 TYR A C   
3017 O O   . TYR A 390 ? 1.7023 2.1089 1.7143 0.5023  0.3295  -0.1902 417 TYR A O   
3018 C CB  . TYR A 390 ? 1.7162 2.0642 1.7744 0.5776  0.2837  -0.1729 417 TYR A CB  
3019 C CG  . TYR A 390 ? 1.7205 2.0860 1.7956 0.6036  0.3174  -0.1974 417 TYR A CG  
3020 C CD1 . TYR A 390 ? 1.8775 2.1736 1.9151 0.6227  0.3323  -0.2169 417 TYR A CD1 
3021 C CD2 . TYR A 390 ? 1.7441 2.1954 1.8724 0.6087  0.3349  -0.2016 417 TYR A CD2 
3022 C CE1 . TYR A 390 ? 1.9413 2.2494 1.9913 0.6481  0.3642  -0.2421 417 TYR A CE1 
3023 C CE2 . TYR A 390 ? 1.8078 2.2774 1.9513 0.6342  0.3683  -0.2256 417 TYR A CE2 
3024 C CZ  . TYR A 390 ? 1.8872 2.2834 1.9902 0.6549  0.3830  -0.2468 417 TYR A CZ  
3025 O OH  . TYR A 390 ? 1.7327 2.1433 1.8477 0.6817  0.4173  -0.2733 417 TYR A OH  
3026 N N   . ASN A 391 ? 1.6163 2.0738 1.6840 0.4945  0.2844  -0.1540 418 ASN A N   
3027 C CA  . ASN A 391 ? 1.5670 2.0922 1.6555 0.4686  0.2986  -0.1524 418 ASN A CA  
3028 C C   . ASN A 391 ? 1.4978 1.9969 1.5332 0.4296  0.3033  -0.1517 418 ASN A C   
3029 O O   . ASN A 391 ? 1.4219 1.9587 1.4556 0.4108  0.3249  -0.1573 418 ASN A O   
3030 C CB  . ASN A 391 ? 1.4635 2.0482 1.6027 0.4600  0.2760  -0.1318 418 ASN A CB  
3031 C CG  . ASN A 391 ? 1.4563 2.0909 1.6594 0.4958  0.2754  -0.1323 418 ASN A CG  
3032 O OD1 . ASN A 391 ? 1.4714 2.1295 1.6957 0.5209  0.3022  -0.1489 418 ASN A OD1 
3033 N ND2 . ASN A 391 ? 1.5150 2.1669 1.7492 0.4991  0.2444  -0.1143 418 ASN A ND2 
3034 N N   . ILE A 392 ? 1.3921 1.8297 1.3847 0.4172  0.2836  -0.1438 419 ILE A N   
3035 C CA  . ILE A 392 ? 1.3315 1.7439 1.2759 0.3827  0.2864  -0.1423 419 ILE A CA  
3036 C C   . ILE A 392 ? 1.4722 1.8507 1.3761 0.3854  0.3118  -0.1637 419 ILE A C   
3037 O O   . ILE A 392 ? 1.4575 1.8470 1.3362 0.3602  0.3265  -0.1678 419 ILE A O   
3038 C CB  . ILE A 392 ? 1.3292 1.6921 1.2450 0.3703  0.2583  -0.1274 419 ILE A CB  
3039 C CG1 . ILE A 392 ? 1.4052 1.8035 1.3538 0.3597  0.2344  -0.1078 419 ILE A CG1 
3040 C CG2 . ILE A 392 ? 1.3003 1.6305 1.1656 0.3410  0.2620  -0.1276 419 ILE A CG2 
3041 C CD1 . ILE A 392 ? 1.1972 1.5544 1.1150 0.3415  0.2106  -0.0943 419 ILE A CD1 
3042 N N   . TRP A 393 ? 1.5851 1.9196 1.4799 0.4149  0.3165  -0.1773 420 TRP A N   
3043 C CA  . TRP A 393 ? 1.5388 1.8396 1.3965 0.4195  0.3415  -0.2008 420 TRP A CA  
3044 C C   . TRP A 393 ? 1.6104 1.9685 1.4856 0.4197  0.3716  -0.2154 420 TRP A C   
3045 O O   . TRP A 393 ? 1.7247 2.0705 1.5605 0.4046  0.3916  -0.2306 420 TRP A O   
3046 C CB  . TRP A 393 ? 1.6183 1.8658 1.4723 0.4554  0.3417  -0.2128 420 TRP A CB  
3047 C CG  . TRP A 393 ? 1.5550 1.7460 1.3902 0.4565  0.3142  -0.1982 420 TRP A CG  
3048 C CD1 . TRP A 393 ? 1.4423 1.6144 1.2513 0.4277  0.2949  -0.1820 420 TRP A CD1 
3049 C CD2 . TRP A 393 ? 1.6515 1.7988 1.4928 0.4885  0.3036  -0.1978 420 TRP A CD2 
3050 N NE1 . TRP A 393 ? 1.5767 1.6986 1.3739 0.4388  0.2749  -0.1724 420 TRP A NE1 
3051 C CE2 . TRP A 393 ? 1.6671 1.7716 1.4823 0.4749  0.2789  -0.1808 420 TRP A CE2 
3052 C CE3 . TRP A 393 ? 1.6183 1.7580 1.4846 0.5284  0.3128  -0.2096 420 TRP A CE3 
3053 C CZ2 . TRP A 393 ? 1.5631 1.6178 1.3731 0.4970  0.2631  -0.1739 420 TRP A CZ2 
3054 C CZ3 . TRP A 393 ? 1.6624 1.7496 1.5248 0.5517  0.2953  -0.2021 420 TRP A CZ3 
3055 C CH2 . TRP A 393 ? 1.7211 1.7664 1.5541 0.5346  0.2706  -0.1838 420 TRP A CH2 
3056 N N   . LYS A 394 ? 1.6946 2.1181 1.6284 0.4354  0.3751  -0.2106 421 LYS A N   
3057 C CA  . LYS A 394 ? 1.6576 2.1445 1.6130 0.4351  0.4054  -0.2229 421 LYS A CA  
3058 C C   . LYS A 394 ? 1.5641 2.0865 1.5030 0.3917  0.4084  -0.2114 421 LYS A C   
3059 O O   . LYS A 394 ? 1.6064 2.1446 1.5207 0.3786  0.4347  -0.2251 421 LYS A O   
3060 C CB  . LYS A 394 ? 1.6010 2.1538 1.6293 0.4628  0.4065  -0.2183 421 LYS A CB  
3061 C CG  . LYS A 394 ? 1.5764 2.0979 1.6260 0.5090  0.4025  -0.2274 421 LYS A CG  
3062 C CD  . LYS A 394 ? 1.5812 2.1630 1.7035 0.5301  0.3874  -0.2121 421 LYS A CD  
3063 C CE  . LYS A 394 ? 1.5795 2.2394 1.7552 0.5508  0.4169  -0.2245 421 LYS A CE  
3064 N NZ  . LYS A 394 ? 1.7187 2.3466 1.8911 0.5934  0.4402  -0.2509 421 LYS A NZ  
3065 N N   . GLU A 395 ? 1.5003 2.0330 1.4497 0.3688  0.3813  -0.1862 422 GLU A N   
3066 C CA  . GLU A 395 ? 1.5025 2.0642 1.4374 0.3282  0.3814  -0.1726 422 GLU A CA  
3067 C C   . GLU A 395 ? 1.5759 2.0883 1.4444 0.3054  0.3867  -0.1793 422 GLU A C   
3068 O O   . GLU A 395 ? 1.6082 2.1464 1.4566 0.2777  0.3998  -0.1772 422 GLU A O   
3069 C CB  . GLU A 395 ? 1.4292 1.9994 1.3851 0.3109  0.3493  -0.1461 422 GLU A CB  
3070 C CG  . GLU A 395 ? 1.4344 2.0284 1.3762 0.2697  0.3466  -0.1298 422 GLU A CG  
3071 C CD  . GLU A 395 ? 1.5154 2.1156 1.4787 0.2538  0.3159  -0.1058 422 GLU A CD  
3072 O OE1 . GLU A 395 ? 1.5090 2.1250 1.5139 0.2724  0.3014  -0.1013 422 GLU A OE1 
3073 O OE2 . GLU A 395 ? 1.5552 2.1428 1.4926 0.2230  0.3054  -0.0917 422 GLU A OE2 
3074 N N   . VAL A 396 ? 1.5632 2.0064 1.3970 0.3151  0.3760  -0.1860 423 VAL A N   
3075 C CA  . VAL A 396 ? 1.6402 2.0382 1.4131 0.2939  0.3801  -0.1932 423 VAL A CA  
3076 C C   . VAL A 396 ? 1.5987 2.0083 1.3485 0.2956  0.4134  -0.2177 423 VAL A C   
3077 O O   . VAL A 396 ? 1.6462 2.0672 1.3621 0.2669  0.4232  -0.2177 423 VAL A O   
3078 C CB  . VAL A 396 ? 1.5422 1.8671 1.2873 0.3049  0.3634  -0.1962 423 VAL A CB  
3079 C CG1 . VAL A 396 ? 1.6177 1.8996 1.3028 0.2847  0.3701  -0.2072 423 VAL A CG1 
3080 C CG2 . VAL A 396 ? 1.5403 1.8542 1.2981 0.2972  0.3322  -0.1719 423 VAL A CG2 
3081 N N   . VAL A 397 ? 1.4378 1.8433 1.2040 0.3302  0.4311  -0.2391 424 VAL A N   
3082 C CA  . VAL A 397 ? 1.5650 1.9804 1.3090 0.3354  0.4652  -0.2659 424 VAL A CA  
3083 C C   . VAL A 397 ? 1.4965 1.9927 1.2661 0.3212  0.4849  -0.2611 424 VAL A C   
3084 O O   . VAL A 397 ? 1.5882 2.0982 1.3227 0.3045  0.5086  -0.2741 424 VAL A O   
3085 C CB  . VAL A 397 ? 1.5102 1.9006 1.2701 0.3798  0.4795  -0.2900 424 VAL A CB  
3086 C CG1 . VAL A 397 ? 1.4402 1.8256 1.1653 0.3849  0.5148  -0.3218 424 VAL A CG1 
3087 C CG2 . VAL A 397 ? 1.4521 1.7642 1.1923 0.3923  0.4565  -0.2889 424 VAL A CG2 
3088 N N   . ASP A 398 ? 1.5598 2.1110 1.3885 0.3253  0.4750  -0.2418 425 ASP A N   
3089 C CA  . ASP A 398 ? 1.6139 2.2454 1.4712 0.3091  0.4929  -0.2345 425 ASP A CA  
3090 C C   . ASP A 398 ? 1.5909 2.2276 1.4086 0.2628  0.4871  -0.2175 425 ASP A C   
3091 O O   . ASP A 398 ? 1.6549 2.3243 1.4503 0.2447  0.5121  -0.2242 425 ASP A O   
3092 C CB  . ASP A 398 ? 1.5901 2.2758 1.5198 0.3203  0.4787  -0.2157 425 ASP A CB  
3093 C CG  . ASP A 398 ? 1.6452 2.4181 1.6101 0.3025  0.4975  -0.2070 425 ASP A CG  
3094 O OD1 . ASP A 398 ? 1.5189 2.3368 1.5055 0.3218  0.5297  -0.2255 425 ASP A OD1 
3095 O OD2 . ASP A 398 ? 1.6482 2.4440 1.6192 0.2692  0.4806  -0.1816 425 ASP A OD2 
3096 N N   . ARG A 399 ? 1.5551 2.1593 1.3624 0.2439  0.4544  -0.1951 426 ARG A N   
3097 C CA  . ARG A 399 ? 1.5359 2.1388 1.3070 0.2027  0.4451  -0.1768 426 ARG A CA  
3098 C C   . ARG A 399 ? 1.5893 2.1376 1.2924 0.1900  0.4478  -0.1889 426 ARG A C   
3099 O O   . ARG A 399 ? 1.6848 2.2333 1.3537 0.1566  0.4421  -0.1752 426 ARG A O   
3100 C CB  . ARG A 399 ? 1.5704 2.1611 1.3600 0.1896  0.4094  -0.1487 426 ARG A CB  
3101 C CG  . ARG A 399 ? 1.4898 2.1385 1.3408 0.1898  0.4031  -0.1322 426 ARG A CG  
3102 C CD  . ARG A 399 ? 1.5026 2.1268 1.3680 0.1828  0.3669  -0.1100 426 ARG A CD  
3103 N NE  . ARG A 399 ? 1.6784 2.2852 1.5112 0.1479  0.3520  -0.0905 426 ARG A NE  
3104 C CZ  . ARG A 399 ? 1.5177 2.0927 1.3497 0.1395  0.3222  -0.0732 426 ARG A CZ  
3105 N NH1 . ARG A 399 ? 1.3900 1.9460 1.2471 0.1608  0.3036  -0.0728 426 ARG A NH1 
3106 N NH2 . ARG A 399 ? 1.5715 2.1327 1.3753 0.1098  0.3109  -0.0558 426 ARG A NH2 
3107 N N   . GLY A 400 ? 1.5454 2.0468 1.2282 0.2145  0.4550  -0.2132 427 GLY A N   
3108 C CA  . GLY A 400 ? 1.5371 1.9851 1.1560 0.2008  0.4555  -0.2256 427 GLY A CA  
3109 C C   . GLY A 400 ? 1.6904 2.0972 1.2876 0.1806  0.4234  -0.2050 427 GLY A C   
3110 O O   . GLY A 400 ? 1.7897 2.1804 1.3400 0.1532  0.4200  -0.2020 427 GLY A O   
3111 N N   . LEU A 401 ? 1.6679 2.0592 1.2983 0.1938  0.3996  -0.1908 428 LEU A N   
3112 C CA  . LEU A 401 ? 1.5515 1.9081 1.1665 0.1773  0.3705  -0.1712 428 LEU A CA  
3113 C C   . LEU A 401 ? 1.6679 1.9628 1.2402 0.1798  0.3667  -0.1854 428 LEU A C   
3114 O O   . LEU A 401 ? 1.7603 2.0217 1.3392 0.2060  0.3679  -0.1992 428 LEU A O   
3115 C CB  . LEU A 401 ? 1.4710 1.8301 1.1314 0.1915  0.3486  -0.1544 428 LEU A CB  
3116 C CG  . LEU A 401 ? 1.5692 1.9887 1.2765 0.1891  0.3503  -0.1410 428 LEU A CG  
3117 C CD1 . LEU A 401 ? 1.6540 2.0713 1.4030 0.2059  0.3283  -0.1287 428 LEU A CD1 
3118 C CD2 . LEU A 401 ? 1.4740 1.9191 1.1680 0.1536  0.3455  -0.1212 428 LEU A CD2 
3119 N N   . GLN A 402 ? 1.6796 1.9597 1.2087 0.1516  0.3609  -0.1806 429 GLN A N   
3120 C CA  . GLN A 402 ? 1.5570 1.7828 1.0444 0.1484  0.3568  -0.1935 429 GLN A CA  
3121 C C   . GLN A 402 ? 1.6186 1.8056 1.1205 0.1609  0.3345  -0.1839 429 GLN A C   
3122 O O   . GLN A 402 ? 1.6390 1.7847 1.1341 0.1794  0.3371  -0.1992 429 GLN A O   
3123 C CB  . GLN A 402 ? 1.6027 1.8289 1.0462 0.1136  0.3511  -0.1860 429 GLN A CB  
3124 C CG  . GLN A 402 ? 1.6312 1.8971 1.0544 0.0974  0.3723  -0.1926 429 GLN A CG  
3125 C CD  . GLN A 402 ? 1.9359 2.1939 1.3421 0.1141  0.4015  -0.2259 429 GLN A CD  
3126 O OE1 . GLN A 402 ? 1.8943 2.1046 1.2694 0.1192  0.4040  -0.2462 429 GLN A OE1 
3127 N NE2 . GLN A 402 ? 1.9252 2.2297 1.3525 0.1226  0.4242  -0.2320 429 GLN A NE2 
3128 N N   . LYS A 403 ? 1.6292 1.8267 1.1491 0.1509  0.3128  -0.1586 430 LYS A N   
3129 C CA  . LYS A 403 ? 1.5078 1.6736 1.0409 0.1617  0.2926  -0.1482 430 LYS A CA  
3130 C C   . LYS A 403 ? 1.4852 1.6790 1.0616 0.1698  0.2803  -0.1298 430 LYS A C   
3131 O O   . LYS A 403 ? 1.3614 1.5879 0.9467 0.1528  0.2751  -0.1142 430 LYS A O   
3132 C CB  . LYS A 403 ? 1.3869 1.5290 0.8914 0.1397  0.2764  -0.1373 430 LYS A CB  
3133 C CG  . LYS A 403 ? 1.5792 1.7518 1.0752 0.1127  0.2692  -0.1198 430 LYS A CG  
3134 C CD  . LYS A 403 ? 1.5935 1.7455 1.0697 0.0958  0.2511  -0.1075 430 LYS A CD  
3135 C CE  . LYS A 403 ? 1.7233 1.9028 1.1872 0.0696  0.2436  -0.0903 430 LYS A CE  
3136 N NZ  . LYS A 403 ? 1.4844 1.6493 0.9350 0.0555  0.2251  -0.0771 430 LYS A NZ  
3137 N N   . SER A 404 ? 1.5607 1.7395 1.1618 0.1948  0.2745  -0.1312 431 SER A N   
3138 C CA  . SER A 404 ? 1.3949 1.5968 1.0354 0.2036  0.2613  -0.1162 431 SER A CA  
3139 C C   . SER A 404 ? 1.4290 1.5941 1.0725 0.2169  0.2434  -0.1097 431 SER A C   
3140 O O   . SER A 404 ? 1.5265 1.6536 1.1542 0.2297  0.2462  -0.1203 431 SER A O   
3141 C CB  . SER A 404 ? 1.4182 1.6549 1.0941 0.2231  0.2744  -0.1247 431 SER A CB  
3142 O OG  . SER A 404 ? 1.5358 1.8120 1.2101 0.2101  0.2931  -0.1300 431 SER A OG  
3143 N N   . LEU A 405 ? 1.4326 1.6072 1.0939 0.2129  0.2254  -0.0923 432 LEU A N   
3144 C CA  . LEU A 405 ? 1.3020 1.4482 0.9675 0.2256  0.2086  -0.0852 432 LEU A CA  
3145 C C   . LEU A 405 ? 1.4236 1.5908 1.1256 0.2439  0.2023  -0.0826 432 LEU A C   
3146 O O   . LEU A 405 ? 1.3416 1.5482 1.0685 0.2367  0.2010  -0.0763 432 LEU A O   
3147 C CB  . LEU A 405 ? 1.3457 1.4843 1.0018 0.2092  0.1926  -0.0694 432 LEU A CB  
3148 C CG  . LEU A 405 ? 1.3705 1.4837 1.0288 0.2202  0.1759  -0.0616 432 LEU A CG  
3149 C CD1 . LEU A 405 ? 1.3561 1.4287 0.9904 0.2283  0.1783  -0.0678 432 LEU A CD1 
3150 C CD2 . LEU A 405 ? 1.1218 1.2371 0.7783 0.2058  0.1622  -0.0471 432 LEU A CD2 
3151 N N   . VAL A 406 ? 1.4085 1.5501 1.1136 0.2660  0.1972  -0.0862 433 VAL A N   
3152 C CA  . VAL A 406 ? 1.2325 1.3929 0.9717 0.2855  0.1892  -0.0836 433 VAL A CA  
3153 C C   . VAL A 406 ? 1.2979 1.4327 1.0320 0.2905  0.1678  -0.0724 433 VAL A C   
3154 O O   . VAL A 406 ? 1.2532 1.3462 0.9610 0.2952  0.1653  -0.0729 433 VAL A O   
3155 C CB  . VAL A 406 ? 1.2444 1.3993 0.9934 0.3111  0.2018  -0.0975 433 VAL A CB  
3156 C CG1 . VAL A 406 ? 1.2465 1.4280 1.0356 0.3317  0.1914  -0.0928 433 VAL A CG1 
3157 C CG2 . VAL A 406 ? 1.3063 1.4838 1.0544 0.3063  0.2257  -0.1116 433 VAL A CG2 
3158 N N   . PHE A 407 ? 1.3237 1.4835 1.0813 0.2879  0.1529  -0.0625 434 PHE A N   
3159 C CA  . PHE A 407 ? 1.2510 1.3897 1.0020 0.2911  0.1325  -0.0531 434 PHE A CA  
3160 C C   . PHE A 407 ? 1.2771 1.4280 1.0539 0.3116  0.1208  -0.0514 434 PHE A C   
3161 O O   . PHE A 407 ? 1.4287 1.6139 1.2371 0.3215  0.1271  -0.0557 434 PHE A O   
3162 C CB  . PHE A 407 ? 1.3364 1.4872 1.0888 0.2705  0.1210  -0.0433 434 PHE A CB  
3163 C CG  . PHE A 407 ? 1.3102 1.4358 1.0322 0.2554  0.1232  -0.0404 434 PHE A CG  
3164 C CD1 . PHE A 407 ? 1.2349 1.3231 0.9289 0.2613  0.1257  -0.0425 434 PHE A CD1 
3165 C CD2 . PHE A 407 ? 1.3236 1.4644 1.0470 0.2349  0.1221  -0.0340 434 PHE A CD2 
3166 C CE1 . PHE A 407 ? 1.2864 1.3583 0.9578 0.2477  0.1273  -0.0390 434 PHE A CE1 
3167 C CE2 . PHE A 407 ? 1.2879 1.4088 0.9874 0.2232  0.1227  -0.0300 434 PHE A CE2 
3168 C CZ  . PHE A 407 ? 1.3065 1.3957 0.9818 0.2300  0.1254  -0.0328 434 PHE A CZ  
3169 N N   . GLU A 408 ? 1.2830 1.4076 1.0461 0.3179  0.1035  -0.0447 435 GLU A N   
3170 C CA  . GLU A 408 ? 1.4523 1.5903 1.2371 0.3326  0.0860  -0.0397 435 GLU A CA  
3171 C C   . GLU A 408 ? 1.5137 1.6529 1.2938 0.3186  0.0662  -0.0316 435 GLU A C   
3172 O O   . GLU A 408 ? 1.5099 1.6524 1.2834 0.2984  0.0683  -0.0303 435 GLU A O   
3173 C CB  . GLU A 408 ? 1.4631 1.5656 1.2322 0.3552  0.0821  -0.0392 435 GLU A CB  
3174 C CG  . GLU A 408 ? 1.4814 1.5857 1.2639 0.3737  0.0986  -0.0481 435 GLU A CG  
3175 C CD  . GLU A 408 ? 1.6012 1.6671 1.3700 0.3971  0.0927  -0.0456 435 GLU A CD  
3176 O OE1 . GLU A 408 ? 1.7905 1.8195 1.5268 0.3942  0.0822  -0.0381 435 GLU A OE1 
3177 O OE2 . GLU A 408 ? 1.6866 1.7589 1.4766 0.4188  0.0992  -0.0506 435 GLU A OE2 
3178 N N   . ASP A 409 ? 1.5550 1.6895 1.3366 0.3289  0.0462  -0.0263 436 ASP A N   
3179 C CA  . ASP A 409 ? 1.5985 1.7369 1.3779 0.3154  0.0265  -0.0211 436 ASP A CA  
3180 C C   . ASP A 409 ? 1.6686 1.7660 1.4106 0.3207  0.0125  -0.0179 436 ASP A C   
3181 O O   . ASP A 409 ? 1.7943 1.8917 1.5318 0.3139  -0.0066 -0.0152 436 ASP A O   
3182 C CB  . ASP A 409 ? 1.5867 1.7710 1.4080 0.3162  0.0122  -0.0180 436 ASP A CB  
3183 C CG  . ASP A 409 ? 1.5922 1.7848 1.4300 0.3413  0.0047  -0.0160 436 ASP A CG  
3184 O OD1 . ASP A 409 ? 1.6991 1.8580 1.5143 0.3580  0.0116  -0.0170 436 ASP A OD1 
3185 O OD2 . ASP A 409 ? 1.6789 1.9123 1.5537 0.3440  -0.0090 -0.0123 436 ASP A OD2 
3186 N N   . ASP A 410 ? 1.6561 1.7176 1.3687 0.3310  0.0219  -0.0183 437 ASP A N   
3187 C CA  . ASP A 410 ? 1.6403 1.6634 1.3134 0.3341  0.0126  -0.0146 437 ASP A CA  
3188 C C   . ASP A 410 ? 1.6360 1.6279 1.2798 0.3306  0.0310  -0.0164 437 ASP A C   
3189 O O   . ASP A 410 ? 1.7148 1.6798 1.3389 0.3411  0.0361  -0.0140 437 ASP A O   
3190 C CB  . ASP A 410 ? 1.7270 1.7415 1.3966 0.3532  -0.0017 -0.0087 437 ASP A CB  
3191 C CG  . ASP A 410 ? 2.1151 2.1331 1.8035 0.3709  0.0088  -0.0090 437 ASP A CG  
3192 O OD1 . ASP A 410 ? 2.1158 2.1447 1.8189 0.3673  0.0279  -0.0157 437 ASP A OD1 
3193 O OD2 . ASP A 410 ? 2.1919 2.1999 1.8785 0.3889  -0.0025 -0.0026 437 ASP A OD2 
3194 N N   . LEU A 411 ? 1.4373 1.4326 1.0784 0.3146  0.0398  -0.0193 438 LEU A N   
3195 C CA  . LEU A 411 ? 1.4853 1.4611 1.1064 0.3085  0.0568  -0.0206 438 LEU A CA  
3196 C C   . LEU A 411 ? 1.4854 1.4458 1.0835 0.2991  0.0548  -0.0192 438 LEU A C   
3197 O O   . LEU A 411 ? 1.4225 1.3916 1.0261 0.2924  0.0443  -0.0197 438 LEU A O   
3198 C CB  . LEU A 411 ? 1.3415 1.3393 0.9826 0.2988  0.0714  -0.0250 438 LEU A CB  
3199 C CG  . LEU A 411 ? 1.4221 1.4466 1.0936 0.3066  0.0748  -0.0287 438 LEU A CG  
3200 C CD1 . LEU A 411 ? 1.3873 1.4334 1.0715 0.2938  0.0902  -0.0333 438 LEU A CD1 
3201 C CD2 . LEU A 411 ? 1.5881 1.5923 1.2530 0.3251  0.0785  -0.0299 438 LEU A CD2 
3202 N N   . ARG A 412 ? 1.4985 1.4358 1.0715 0.2987  0.0653  -0.0178 439 ARG A N   
3203 C CA  . ARG A 412 ? 1.2968 1.2230 0.8507 0.2918  0.0679  -0.0169 439 ARG A CA  
3204 C C   . ARG A 412 ? 1.3356 1.2684 0.8941 0.2808  0.0829  -0.0170 439 ARG A C   
3205 O O   . ARG A 412 ? 1.4871 1.4104 1.0373 0.2802  0.0938  -0.0163 439 ARG A O   
3206 C CB  . ARG A 412 ? 1.2836 1.1831 0.8050 0.2992  0.0675  -0.0135 439 ARG A CB  
3207 C CG  . ARG A 412 ? 1.3900 1.2814 0.8933 0.2938  0.0756  -0.0131 439 ARG A CG  
3208 C CD  . ARG A 412 ? 1.5350 1.4035 1.0061 0.2990  0.0800  -0.0086 439 ARG A CD  
3209 N NE  . ARG A 412 ? 1.7613 1.6176 1.2126 0.3076  0.0661  -0.0086 439 ARG A NE  
3210 C CZ  . ARG A 412 ? 1.8444 1.6900 1.2699 0.3093  0.0657  -0.0104 439 ARG A CZ  
3211 N NH1 . ARG A 412 ? 1.5732 1.4207 0.9930 0.3051  0.0793  -0.0116 439 ARG A NH1 
3212 N NH2 . ARG A 412 ? 1.9952 1.8293 1.3999 0.3157  0.0511  -0.0112 439 ARG A NH2 
3213 N N   . PHE A 413 ? 1.2900 1.2374 0.8607 0.2713  0.0822  -0.0173 440 PHE A N   
3214 C CA  . PHE A 413 ? 1.2438 1.2016 0.8204 0.2599  0.0933  -0.0159 440 PHE A CA  
3215 C C   . PHE A 413 ? 1.1918 1.1384 0.7512 0.2586  0.1003  -0.0128 440 PHE A C   
3216 O O   . PHE A 413 ? 1.4005 1.3388 0.9506 0.2635  0.0958  -0.0123 440 PHE A O   
3217 C CB  . PHE A 413 ? 1.1674 1.1442 0.7632 0.2502  0.0883  -0.0145 440 PHE A CB  
3218 C CG  . PHE A 413 ? 1.2240 1.2207 0.8406 0.2474  0.0856  -0.0164 440 PHE A CG  
3219 C CD1 . PHE A 413 ? 1.2521 1.2525 0.8783 0.2530  0.0732  -0.0178 440 PHE A CD1 
3220 C CD2 . PHE A 413 ? 1.2817 1.2959 0.9083 0.2383  0.0957  -0.0171 440 PHE A CD2 
3221 C CE1 . PHE A 413 ? 1.3600 1.3854 1.0102 0.2502  0.0718  -0.0189 440 PHE A CE1 
3222 C CE2 . PHE A 413 ? 1.2719 1.3087 0.9186 0.2362  0.0960  -0.0194 440 PHE A CE2 
3223 C CZ  . PHE A 413 ? 1.4457 1.4901 1.1067 0.2425  0.0845  -0.0198 440 PHE A CZ  
3224 N N   . GLU A 414 ? 1.1573 1.1050 0.7128 0.2514  0.1115  -0.0113 441 GLU A N   
3225 C CA  . GLU A 414 ? 1.1143 1.0598 0.6596 0.2475  0.1189  -0.0071 441 GLU A CA  
3226 C C   . GLU A 414 ? 1.2809 1.2439 0.8402 0.2419  0.1171  -0.0038 441 GLU A C   
3227 O O   . GLU A 414 ? 1.2621 1.2372 0.8365 0.2371  0.1115  -0.0036 441 GLU A O   
3228 C CB  . GLU A 414 ? 1.2216 1.1639 0.7599 0.2381  0.1295  -0.0063 441 GLU A CB  
3229 C CG  . GLU A 414 ? 1.4514 1.3693 0.9684 0.2431  0.1337  -0.0051 441 GLU A CG  
3230 C CD  . GLU A 414 ? 1.5638 1.4796 1.0680 0.2431  0.1387  0.0006  441 GLU A CD  
3231 O OE1 . GLU A 414 ? 1.4172 1.3519 0.9321 0.2404  0.1400  0.0027  441 GLU A OE1 
3232 O OE2 . GLU A 414 ? 1.4477 1.3434 0.9314 0.2466  0.1417  0.0036  441 GLU A OE2 
3233 N N   . ILE A 415 ? 1.2426 1.2077 0.7973 0.2427  0.1223  0.0000  442 ILE A N   
3234 C CA  . ILE A 415 ? 1.2654 1.2463 0.8351 0.2407  0.1203  0.0044  442 ILE A CA  
3235 C C   . ILE A 415 ? 1.2510 1.2516 0.8331 0.2255  0.1222  0.0091  442 ILE A C   
3236 O O   . ILE A 415 ? 1.3042 1.3069 0.8800 0.2161  0.1292  0.0090  442 ILE A O   
3237 C CB  . ILE A 415 ? 1.2455 1.2281 0.8104 0.2479  0.1272  0.0069  442 ILE A CB  
3238 C CG1 . ILE A 415 ? 1.2341 1.2306 0.8171 0.2509  0.1236  0.0113  442 ILE A CG1 
3239 C CG2 . ILE A 415 ? 1.2144 1.2049 0.7737 0.2389  0.1385  0.0109  442 ILE A CG2 
3240 C CD1 . ILE A 415 ? 1.0803 1.0808 0.6622 0.2623  0.1314  0.0119  442 ILE A CD1 
3241 N N   . PHE A 416 ? 1.2267 1.2390 0.8236 0.2219  0.1149  0.0134  443 PHE A N   
3242 C CA  . PHE A 416 ? 1.2365 1.2683 0.8420 0.2065  0.1146  0.0189  443 PHE A CA  
3243 C C   . PHE A 416 ? 1.2815 1.3121 0.8802 0.1975  0.1181  0.0128  443 PHE A C   
3244 O O   . PHE A 416 ? 1.3201 1.3601 0.9147 0.1845  0.1230  0.0129  443 PHE A O   
3245 C CB  . PHE A 416 ? 1.1499 1.1977 0.7581 0.1996  0.1199  0.0252  443 PHE A CB  
3246 C CG  . PHE A 416 ? 1.3099 1.3630 0.9278 0.2113  0.1194  0.0304  443 PHE A CG  
3247 C CD1 . PHE A 416 ? 1.2123 1.2622 0.8410 0.2209  0.1109  0.0336  443 PHE A CD1 
3248 C CD2 . PHE A 416 ? 1.2366 1.2972 0.8529 0.2127  0.1283  0.0318  443 PHE A CD2 
3249 C CE1 . PHE A 416 ? 1.2080 1.2607 0.8457 0.2348  0.1119  0.0364  443 PHE A CE1 
3250 C CE2 . PHE A 416 ? 1.1390 1.2085 0.7661 0.2255  0.1304  0.0356  443 PHE A CE2 
3251 C CZ  . PHE A 416 ? 1.1194 1.1842 0.7573 0.2380  0.1225  0.0370  443 PHE A CZ  
3252 N N   . PHE A 417 ? 1.2161 1.2358 0.8140 0.2049  0.1155  0.0066  444 PHE A N   
3253 C CA  . PHE A 417 ? 1.1349 1.1546 0.7296 0.2010  0.1203  -0.0005 444 PHE A CA  
3254 C C   . PHE A 417 ? 1.2320 1.2715 0.8318 0.1857  0.1218  0.0015  444 PHE A C   
3255 O O   . PHE A 417 ? 1.2658 1.3076 0.8564 0.1770  0.1297  -0.0034 444 PHE A O   
3256 C CB  . PHE A 417 ? 1.1359 1.1484 0.7357 0.2121  0.1149  -0.0054 444 PHE A CB  
3257 C CG  . PHE A 417 ? 1.1725 1.1905 0.7756 0.2113  0.1202  -0.0125 444 PHE A CG  
3258 C CD1 . PHE A 417 ? 1.0844 1.0865 0.6773 0.2193  0.1263  -0.0191 444 PHE A CD1 
3259 C CD2 . PHE A 417 ? 1.2282 1.2671 0.8447 0.2031  0.1197  -0.0121 444 PHE A CD2 
3260 C CE1 . PHE A 417 ? 1.2774 1.2838 0.8753 0.2221  0.1321  -0.0268 444 PHE A CE1 
3261 C CE2 . PHE A 417 ? 1.1704 1.2184 0.7920 0.2043  0.1270  -0.0198 444 PHE A CE2 
3262 C CZ  . PHE A 417 ? 1.1173 1.1488 0.7305 0.2153  0.1334  -0.0279 444 PHE A CZ  
3263 N N   . LYS A 418 ? 1.2362 1.2876 0.8477 0.1813  0.1140  0.0089  445 LYS A N   
3264 C CA  . LYS A 418 ? 1.1803 1.2509 0.7941 0.1660  0.1151  0.0122  445 LYS A CA  
3265 C C   . LYS A 418 ? 1.1382 1.2184 0.7418 0.1525  0.1187  0.0156  445 LYS A C   
3266 O O   . LYS A 418 ? 1.2670 1.3556 0.8605 0.1411  0.1259  0.0104  445 LYS A O   
3267 C CB  . LYS A 418 ? 1.3288 1.4059 0.9553 0.1625  0.1044  0.0226  445 LYS A CB  
3268 C CG  . LYS A 418 ? 1.1821 1.2798 0.8095 0.1451  0.1052  0.0287  445 LYS A CG  
3269 C CD  . LYS A 418 ? 1.2468 1.3451 0.8864 0.1413  0.0938  0.0400  445 LYS A CD  
3270 C CE  . LYS A 418 ? 1.3106 1.4291 0.9480 0.1217  0.0940  0.0499  445 LYS A CE  
3271 N NZ  . LYS A 418 ? 1.3793 1.4945 1.0279 0.1158  0.0824  0.0623  445 LYS A NZ  
3272 N N   . ARG A 419 ? 1.2184 1.2990 0.8245 0.1537  0.1138  0.0238  446 ARG A N   
3273 C CA  . ARG A 419 ? 1.2349 1.3295 0.8345 0.1393  0.1144  0.0289  446 ARG A CA  
3274 C C   . ARG A 419 ? 1.2916 1.3772 0.8757 0.1348  0.1242  0.0182  446 ARG A C   
3275 O O   . ARG A 419 ? 1.2859 1.3792 0.8572 0.1187  0.1273  0.0156  446 ARG A O   
3276 C CB  . ARG A 419 ? 1.2322 1.3344 0.8443 0.1437  0.1065  0.0413  446 ARG A CB  
3277 C CG  . ARG A 419 ? 1.3307 1.4377 0.9561 0.1463  0.0952  0.0534  446 ARG A CG  
3278 C CD  . ARG A 419 ? 1.2669 1.3836 0.9065 0.1522  0.0880  0.0656  446 ARG A CD  
3279 N NE  . ARG A 419 ? 1.3861 1.4941 1.0297 0.1679  0.0937  0.0600  446 ARG A NE  
3280 C CZ  . ARG A 419 ? 1.4474 1.5642 1.1058 0.1781  0.0912  0.0674  446 ARG A CZ  
3281 N NH1 . ARG A 419 ? 1.4222 1.5551 1.0951 0.1764  0.0811  0.0817  446 ARG A NH1 
3282 N NH2 . ARG A 419 ? 1.5909 1.7012 1.2497 0.1911  0.0993  0.0611  446 ARG A NH2 
3283 N N   . ARG A 420 ? 1.2531 1.3196 0.8351 0.1478  0.1287  0.0120  447 ARG A N   
3284 C CA  . ARG A 420 ? 1.2609 1.3132 0.8271 0.1428  0.1372  0.0037  447 ARG A CA  
3285 C C   . ARG A 420 ? 1.2497 1.2924 0.8031 0.1388  0.1446  -0.0090 447 ARG A C   
3286 O O   . ARG A 420 ? 1.1986 1.2340 0.7356 0.1265  0.1502  -0.0159 447 ARG A O   
3287 C CB  . ARG A 420 ? 1.2529 1.2853 0.8176 0.1576  0.1399  0.0021  447 ARG A CB  
3288 C CG  . ARG A 420 ? 1.1421 1.1848 0.7152 0.1593  0.1377  0.0121  447 ARG A CG  
3289 C CD  . ARG A 420 ? 1.2220 1.2475 0.7925 0.1763  0.1398  0.0111  447 ARG A CD  
3290 N NE  . ARG A 420 ? 1.4117 1.4140 0.9647 0.1756  0.1472  0.0057  447 ARG A NE  
3291 C CZ  . ARG A 420 ? 1.4210 1.4055 0.9652 0.1876  0.1496  0.0057  447 ARG A CZ  
3292 N NH1 . ARG A 420 ? 1.1912 1.1783 0.7409 0.2015  0.1462  0.0084  447 ARG A NH1 
3293 N NH2 . ARG A 420 ? 1.4522 1.4128 0.9789 0.1853  0.1553  0.0029  447 ARG A NH2 
3294 N N   . LEU A 421 ? 1.2040 1.2472 0.7651 0.1489  0.1448  -0.0129 448 LEU A N   
3295 C CA  . LEU A 421 ? 1.1284 1.1672 0.6814 0.1483  0.1538  -0.0256 448 LEU A CA  
3296 C C   . LEU A 421 ? 1.2331 1.2917 0.7777 0.1297  0.1563  -0.0262 448 LEU A C   
3297 O O   . LEU A 421 ? 1.3644 1.4158 0.8914 0.1221  0.1655  -0.0382 448 LEU A O   
3298 C CB  . LEU A 421 ? 1.2599 1.3009 0.8286 0.1641  0.1530  -0.0282 448 LEU A CB  
3299 C CG  . LEU A 421 ? 1.2615 1.3048 0.8290 0.1674  0.1636  -0.0412 448 LEU A CG  
3300 C CD1 . LEU A 421 ? 1.1069 1.1215 0.6570 0.1723  0.1724  -0.0533 448 LEU A CD1 
3301 C CD2 . LEU A 421 ? 1.2729 1.3258 0.8622 0.1823  0.1607  -0.0412 448 LEU A CD2 
3302 N N   . MET A 422 ? 1.2370 1.3181 0.7914 0.1220  0.1479  -0.0134 449 MET A N   
3303 C CA  . MET A 422 ? 1.2132 1.3138 0.7562 0.1027  0.1486  -0.0110 449 MET A CA  
3304 C C   . MET A 422 ? 1.2125 1.3114 0.7366 0.0864  0.1478  -0.0118 449 MET A C   
3305 O O   . MET A 422 ? 1.1648 1.2673 0.6678 0.0713  0.1536  -0.0199 449 MET A O   
3306 C CB  . MET A 422 ? 1.1565 1.2771 0.7135 0.0982  0.1375  0.0061  449 MET A CB  
3307 C CG  . MET A 422 ? 1.0827 1.2085 0.6557 0.1070  0.1381  0.0067  449 MET A CG  
3308 S SD  . MET A 422 ? 1.3421 1.4858 0.9262 0.0966  0.1251  0.0274  449 MET A SD  
3309 C CE  . MET A 422 ? 1.3057 1.4707 0.8657 0.0717  0.1300  0.0297  449 MET A CE  
3310 N N   . ASN A 423 ? 1.1839 1.2786 0.7149 0.0884  0.1410  -0.0041 450 ASN A N   
3311 C CA  . ASN A 423 ? 1.2112 1.3073 0.7281 0.0714  0.1392  -0.0041 450 ASN A CA  
3312 C C   . ASN A 423 ? 1.3339 1.4038 0.8274 0.0669  0.1506  -0.0226 450 ASN A C   
3313 O O   . ASN A 423 ? 1.4195 1.4895 0.8916 0.0470  0.1513  -0.0284 450 ASN A O   
3314 C CB  . ASN A 423 ? 1.0668 1.1664 0.6000 0.0766  0.1325  0.0072  450 ASN A CB  
3315 C CG  . ASN A 423 ? 1.2318 1.3559 0.7865 0.0801  0.1206  0.0252  450 ASN A CG  
3316 O OD1 . ASN A 423 ? 1.3634 1.4995 0.9194 0.0766  0.1158  0.0310  450 ASN A OD1 
3317 N ND2 . ASN A 423 ? 1.4109 1.5414 0.9824 0.0875  0.1164  0.0342  450 ASN A ND2 
3318 N N   . LEU A 424 ? 1.2999 1.3453 0.7960 0.0850  0.1585  -0.0321 451 LEU A N   
3319 C CA  . LEU A 424 ? 1.3588 1.3735 0.8337 0.0843  0.1691  -0.0495 451 LEU A CA  
3320 C C   . LEU A 424 ? 1.3618 1.3791 0.8192 0.0772  0.1779  -0.0635 451 LEU A C   
3321 O O   . LEU A 424 ? 1.4973 1.5016 0.9285 0.0612  0.1823  -0.0751 451 LEU A O   
3322 C CB  . LEU A 424 ? 1.2453 1.2347 0.7288 0.1079  0.1736  -0.0539 451 LEU A CB  
3323 C CG  . LEU A 424 ? 1.3817 1.3353 0.8451 0.1116  0.1844  -0.0716 451 LEU A CG  
3324 C CD1 . LEU A 424 ? 1.5308 1.4590 0.9754 0.0967  0.1837  -0.0726 451 LEU A CD1 
3325 C CD2 . LEU A 424 ? 1.3699 1.3065 0.8456 0.1380  0.1877  -0.0750 451 LEU A CD2 
3326 N N   . MET A 425 ? 1.3095 1.3440 0.7801 0.0879  0.1811  -0.0633 452 MET A N   
3327 C CA  . MET A 425 ? 1.3675 1.4103 0.8228 0.0817  0.1922  -0.0762 452 MET A CA  
3328 C C   . MET A 425 ? 1.3693 1.4296 0.8023 0.0548  0.1881  -0.0730 452 MET A C   
3329 O O   . MET A 425 ? 1.6132 1.6684 1.0188 0.0439  0.1980  -0.0885 452 MET A O   
3330 C CB  . MET A 425 ? 1.2700 1.3367 0.7481 0.0942  0.1949  -0.0721 452 MET A CB  
3331 C CG  . MET A 425 ? 1.2217 1.2756 0.7224 0.1202  0.1972  -0.0752 452 MET A CG  
3332 S SD  . MET A 425 ? 1.6065 1.6253 1.0937 0.1355  0.2125  -0.0986 452 MET A SD  
3333 C CE  . MET A 425 ? 1.3794 1.4181 0.8507 0.1265  0.2295  -0.1145 452 MET A CE  
3334 N N   . ARG A 426 ? 1.4273 1.5078 0.8703 0.0446  0.1731  -0.0534 453 ARG A N   
3335 C CA  . ARG A 426 ? 1.3749 1.4737 0.7977 0.0188  0.1657  -0.0474 453 ARG A CA  
3336 C C   . ARG A 426 ? 1.4481 1.5271 0.8469 0.0030  0.1648  -0.0574 453 ARG A C   
3337 O O   . ARG A 426 ? 1.4757 1.5572 0.8440 -0.0184 0.1654  -0.0653 453 ARG A O   
3338 C CB  . ARG A 426 ? 1.4576 1.5833 0.9023 0.0158  0.1487  -0.0223 453 ARG A CB  
3339 C CG  . ARG A 426 ? 1.4234 1.5730 0.8507 -0.0093 0.1379  -0.0117 453 ARG A CG  
3340 C CD  . ARG A 426 ? 1.6979 1.8595 1.1031 -0.0195 0.1459  -0.0168 453 ARG A CD  
3341 N NE  . ARG A 426 ? 1.6271 1.8148 1.0188 -0.0415 0.1322  -0.0002 453 ARG A NE  
3342 C CZ  . ARG A 426 ? 1.6846 1.8928 1.0961 -0.0402 0.1188  0.0238  453 ARG A CZ  
3343 N NH1 . ARG A 426 ? 1.7434 1.9484 1.1877 -0.0193 0.1176  0.0324  453 ARG A NH1 
3344 N NH2 . ARG A 426 ? 1.7831 2.0132 1.1794 -0.0606 0.1052  0.0398  453 ARG A NH2 
3345 N N   . ASP A 427 ? 1.5920 1.6506 1.0019 0.0111  0.1629  -0.0569 454 ASP A N   
3346 C CA  . ASP A 427 ? 1.5869 1.6215 0.9741 -0.0050 0.1633  -0.0672 454 ASP A CA  
3347 C C   . ASP A 427 ? 1.6145 1.6139 0.9718 -0.0039 0.1786  -0.0931 454 ASP A C   
3348 O O   . ASP A 427 ? 1.6316 1.6130 0.9581 -0.0245 0.1792  -0.1055 454 ASP A O   
3349 C CB  . ASP A 427 ? 1.6384 1.6589 1.0442 0.0038  0.1598  -0.0594 454 ASP A CB  
3350 C CG  . ASP A 427 ? 1.7614 1.8149 1.1881 -0.0059 0.1451  -0.0379 454 ASP A CG  
3351 O OD1 . ASP A 427 ? 1.7160 1.8013 1.1438 -0.0182 0.1356  -0.0278 454 ASP A OD1 
3352 O OD2 . ASP A 427 ? 1.6789 1.7274 1.1209 -0.0007 0.1435  -0.0306 454 ASP A OD2 
3353 N N   . VAL A 428 ? 1.5190 1.5086 0.8856 0.0200  0.1907  -0.1019 455 VAL A N   
3354 C CA  . VAL A 428 ? 1.5379 1.4953 0.8807 0.0263  0.2069  -0.1271 455 VAL A CA  
3355 C C   . VAL A 428 ? 1.6169 1.5900 0.9315 0.0101  0.2138  -0.1387 455 VAL A C   
3356 O O   . VAL A 428 ? 1.7130 1.6606 0.9915 -0.0039 0.2202  -0.1582 455 VAL A O   
3357 C CB  . VAL A 428 ? 1.5612 1.5100 0.9279 0.0584  0.2166  -0.1312 455 VAL A CB  
3358 C CG1 . VAL A 428 ? 1.4388 1.3658 0.7860 0.0679  0.2348  -0.1567 455 VAL A CG1 
3359 C CG2 . VAL A 428 ? 1.4720 1.3936 0.8538 0.0725  0.2114  -0.1242 455 VAL A CG2 
3360 N N   . GLU A 429 ? 1.6726 1.6858 1.0004 0.0105  0.2126  -0.1272 456 GLU A N   
3361 C CA  . GLU A 429 ? 1.7001 1.7305 0.9996 -0.0040 0.2214  -0.1372 456 GLU A CA  
3362 C C   . GLU A 429 ? 1.7394 1.7758 1.0060 -0.0368 0.2097  -0.1345 456 GLU A C   
3363 O O   . GLU A 429 ? 1.9569 1.9874 1.1841 -0.0523 0.2184  -0.1522 456 GLU A O   
3364 C CB  . GLU A 429 ? 1.8032 1.8746 1.1254 0.0023  0.2223  -0.1223 456 GLU A CB  
3365 C CG  . GLU A 429 ? 1.9727 2.0737 1.3139 -0.0081 0.2020  -0.0932 456 GLU A CG  
3366 C CD  . GLU A 429 ? 2.1265 2.2602 1.4890 -0.0024 0.2028  -0.0787 456 GLU A CD  
3367 O OE1 . GLU A 429 ? 2.1523 2.2857 1.5385 0.0190  0.2128  -0.0835 456 GLU A OE1 
3368 O OE2 . GLU A 429 ? 2.1816 2.3414 1.5372 -0.0203 0.1924  -0.0615 456 GLU A OE2 
3369 N N   . ARG A 430 ? 1.7362 1.7857 1.0180 -0.0476 0.1900  -0.1133 457 ARG A N   
3370 C CA  . ARG A 430 ? 1.7083 1.7654 0.9635 -0.0787 0.1761  -0.1094 457 ARG A CA  
3371 C C   . ARG A 430 ? 1.7000 1.7152 0.9248 -0.0911 0.1797  -0.1312 457 ARG A C   
3372 O O   . ARG A 430 ? 1.8379 1.8544 1.0310 -0.1200 0.1706  -0.1350 457 ARG A O   
3373 C CB  . ARG A 430 ? 1.6392 1.7253 0.9263 -0.0831 0.1548  -0.0802 457 ARG A CB  
3374 C CG  . ARG A 430 ? 1.3383 1.4427 0.6070 -0.1146 0.1366  -0.0711 457 ARG A CG  
3375 C CD  . ARG A 430 ? 1.2926 1.4369 0.5963 -0.1149 0.1165  -0.0397 457 ARG A CD  
3376 N NE  . ARG A 430 ? 1.4935 1.6356 0.8405 -0.0900 0.1166  -0.0288 457 ARG A NE  
3377 C CZ  . ARG A 430 ? 1.5175 1.6748 0.8949 -0.0692 0.1155  -0.0138 457 ARG A CZ  
3378 N NH1 . ARG A 430 ? 1.4407 1.6171 0.8134 -0.0707 0.1140  -0.0056 457 ARG A NH1 
3379 N NH2 . ARG A 430 ? 1.3634 1.5152 0.7742 -0.0481 0.1159  -0.0069 457 ARG A NH2 
3380 N N   . GLU A 431 ? 1.8833 1.8595 1.1152 -0.0709 0.1916  -0.1452 458 GLU A N   
3381 C CA  . GLU A 431 ? 2.0079 1.9358 1.2101 -0.0812 0.1956  -0.1660 458 GLU A CA  
3382 C C   . GLU A 431 ? 2.0641 1.9560 1.2347 -0.0714 0.2168  -0.1972 458 GLU A C   
3383 O O   . GLU A 431 ? 2.1171 1.9639 1.2545 -0.0830 0.2204  -0.2178 458 GLU A O   
3384 C CB  . GLU A 431 ? 2.0485 1.9510 1.2772 -0.0674 0.1926  -0.1584 458 GLU A CB  
3385 C CG  . GLU A 431 ? 2.1096 2.0358 1.3572 -0.0852 0.1735  -0.1351 458 GLU A CG  
3386 C CD  . GLU A 431 ? 2.2465 2.1600 1.4614 -0.1210 0.1640  -0.1425 458 GLU A CD  
3387 O OE1 . GLU A 431 ? 2.1652 2.0372 1.3403 -0.1299 0.1731  -0.1681 458 GLU A OE1 
3388 O OE2 . GLU A 431 ? 2.3076 2.2528 1.5371 -0.1400 0.1471  -0.1233 458 GLU A OE2 
3389 N N   . GLY A 432 ? 1.9494 1.8597 1.1303 -0.0506 0.2310  -0.2014 459 GLY A N   
3390 C CA  . GLY A 432 ? 2.0467 1.9310 1.2010 -0.0392 0.2533  -0.2312 459 GLY A CA  
3391 C C   . GLY A 432 ? 1.9636 1.7924 1.1196 -0.0169 0.2635  -0.2487 459 GLY A C   
3392 O O   . GLY A 432 ? 2.0866 1.8713 1.2049 -0.0209 0.2745  -0.2760 459 GLY A O   
3393 N N   . LEU A 433 ? 1.7779 1.6056 0.9753 0.0066  0.2595  -0.2331 460 LEU A N   
3394 C CA  . LEU A 433 ? 1.8044 1.5800 1.0061 0.0293  0.2666  -0.2448 460 LEU A CA  
3395 C C   . LEU A 433 ? 1.8583 1.6307 1.0691 0.0613  0.2874  -0.2625 460 LEU A C   
3396 O O   . LEU A 433 ? 1.8447 1.6634 1.0846 0.0751  0.2916  -0.2530 460 LEU A O   
3397 C CB  . LEU A 433 ? 1.6632 1.4413 0.9025 0.0408  0.2533  -0.2200 460 LEU A CB  
3398 C CG  . LEU A 433 ? 1.7621 1.4883 1.0079 0.0641  0.2573  -0.2254 460 LEU A CG  
3399 C CD1 . LEU A 433 ? 1.8630 1.5332 1.0732 0.0432  0.2537  -0.2361 460 LEU A CD1 
3400 C CD2 . LEU A 433 ? 1.6724 1.4160 0.9579 0.0798  0.2466  -0.1998 460 LEU A CD2 
3401 N N   . ASP A 434 ? 1.9789 1.6968 1.1663 0.0730  0.3003  -0.2882 461 ASP A N   
3402 C CA  . ASP A 434 ? 2.0319 1.7442 1.2332 0.1082  0.3204  -0.3055 461 ASP A CA  
3403 C C   . ASP A 434 ? 1.9273 1.6362 1.1733 0.1380  0.3139  -0.2881 461 ASP A C   
3404 O O   . ASP A 434 ? 1.9846 1.6402 1.2275 0.1516  0.3122  -0.2924 461 ASP A O   
3405 C CB  . ASP A 434 ? 2.1096 1.7605 1.2700 0.1127  0.3359  -0.3394 461 ASP A CB  
3406 C CG  . ASP A 434 ? 2.2651 1.9128 1.4433 0.1525  0.3582  -0.3582 461 ASP A CG  
3407 O OD1 . ASP A 434 ? 2.1056 1.8080 1.3251 0.1713  0.3624  -0.3459 461 ASP A OD1 
3408 O OD2 . ASP A 434 ? 2.4278 2.0183 1.5799 0.1652  0.3711  -0.3854 461 ASP A OD2 
3409 N N   . TRP A 435 ? 1.8377 1.6024 1.1234 0.1470  0.3090  -0.2675 462 TRP A N   
3410 C CA  . TRP A 435 ? 1.8937 1.6624 1.2207 0.1727  0.3007  -0.2497 462 TRP A CA  
3411 C C   . TRP A 435 ? 1.7291 1.5308 1.0896 0.2031  0.3139  -0.2549 462 TRP A C   
3412 O O   . TRP A 435 ? 1.7004 1.5444 1.0625 0.1984  0.3255  -0.2612 462 TRP A O   
3413 C CB  . TRP A 435 ? 1.8040 1.6076 1.1520 0.1581  0.2813  -0.2202 462 TRP A CB  
3414 C CG  . TRP A 435 ? 1.6018 1.4674 0.9666 0.1495  0.2810  -0.2097 462 TRP A CG  
3415 C CD1 . TRP A 435 ? 1.6025 1.4936 0.9466 0.1207  0.2788  -0.2073 462 TRP A CD1 
3416 C CD2 . TRP A 435 ? 1.5197 1.4276 0.9244 0.1682  0.2815  -0.1986 462 TRP A CD2 
3417 N NE1 . TRP A 435 ? 1.5618 1.5057 0.9295 0.1208  0.2785  -0.1947 462 TRP A NE1 
3418 C CE2 . TRP A 435 ? 1.5510 1.5060 0.9564 0.1487  0.2804  -0.1897 462 TRP A CE2 
3419 C CE3 . TRP A 435 ? 1.6369 1.5475 1.0766 0.1982  0.2813  -0.1945 462 TRP A CE3 
3420 C CZ2 . TRP A 435 ? 1.5476 1.5492 0.9869 0.1568  0.2799  -0.1774 462 TRP A CZ2 
3421 C CZ3 . TRP A 435 ? 1.5664 1.5269 1.0408 0.2059  0.2801  -0.1831 462 TRP A CZ3 
3422 C CH2 . TRP A 435 ? 1.6131 1.6171 1.0869 0.1846  0.2798  -0.1749 462 TRP A CH2 
3423 N N   . ASP A 436 ? 1.7564 1.5403 1.1439 0.2333  0.3116  -0.2508 463 ASP A N   
3424 C CA  . ASP A 436 ? 1.8237 1.6412 1.2507 0.2642  0.3207  -0.2526 463 ASP A CA  
3425 C C   . ASP A 436 ? 1.6730 1.5163 1.1405 0.2766  0.3036  -0.2270 463 ASP A C   
3426 O O   . ASP A 436 ? 1.6330 1.5279 1.1354 0.2867  0.3055  -0.2205 463 ASP A O   
3427 C CB  . ASP A 436 ? 1.9289 1.7022 1.3529 0.2951  0.3348  -0.2747 463 ASP A CB  
3428 C CG  . ASP A 436 ? 1.9828 1.7325 1.3670 0.2870  0.3552  -0.3048 463 ASP A CG  
3429 O OD1 . ASP A 436 ? 1.9876 1.7792 1.3617 0.2688  0.3653  -0.3109 463 ASP A OD1 
3430 O OD2 . ASP A 436 ? 2.0369 1.7234 1.3970 0.2982  0.3609  -0.3226 463 ASP A OD2 
3431 N N   . LEU A 437 ? 1.6135 1.4225 1.0757 0.2742  0.2870  -0.2125 464 LEU A N   
3432 C CA  . LEU A 437 ? 1.6292 1.4560 1.1228 0.2855  0.2704  -0.1899 464 LEU A CA  
3433 C C   . LEU A 437 ? 1.6431 1.4545 1.1201 0.2627  0.2545  -0.1725 464 LEU A C   
3434 O O   . LEU A 437 ? 1.7610 1.5273 1.2071 0.2503  0.2538  -0.1767 464 LEU A O   
3435 C CB  . LEU A 437 ? 1.4976 1.2946 1.0079 0.3194  0.2685  -0.1908 464 LEU A CB  
3436 C CG  . LEU A 437 ? 1.6173 1.4292 1.1560 0.3325  0.2503  -0.1685 464 LEU A CG  
3437 C CD1 . LEU A 437 ? 1.5065 1.3832 1.0850 0.3396  0.2498  -0.1631 464 LEU A CD1 
3438 C CD2 . LEU A 437 ? 1.6512 1.4189 1.1935 0.3611  0.2454  -0.1674 464 LEU A CD2 
3439 N N   . ILE A 438 ? 1.5798 1.4289 1.0777 0.2569  0.2422  -0.1536 465 ILE A N   
3440 C CA  . ILE A 438 ? 1.4825 1.3244 0.9705 0.2392  0.2282  -0.1366 465 ILE A CA  
3441 C C   . ILE A 438 ? 1.4393 1.2950 0.9532 0.2549  0.2149  -0.1198 465 ILE A C   
3442 O O   . ILE A 438 ? 1.5166 1.4146 1.0550 0.2565  0.2108  -0.1130 465 ILE A O   
3443 C CB  . ILE A 438 ? 1.4736 1.3478 0.9543 0.2111  0.2264  -0.1315 465 ILE A CB  
3444 C CG1 . ILE A 438 ? 1.4736 1.3350 0.9242 0.1933  0.2379  -0.1486 465 ILE A CG1 
3445 C CG2 . ILE A 438 ? 1.3712 1.2411 0.8472 0.1971  0.2131  -0.1142 465 ILE A CG2 
3446 C CD1 . ILE A 438 ? 1.3723 1.2638 0.8130 0.1647  0.2336  -0.1417 465 ILE A CD1 
3447 N N   . TYR A 439 ? 1.5289 1.3474 1.0348 0.2646  0.2077  -0.1128 466 TYR A N   
3448 C CA  . TYR A 439 ? 1.4046 1.2323 0.9275 0.2771  0.1940  -0.0969 466 TYR A CA  
3449 C C   . TYR A 439 ? 1.3910 1.2436 0.9144 0.2584  0.1856  -0.0836 466 TYR A C   
3450 O O   . TYR A 439 ? 1.4590 1.3055 0.9643 0.2374  0.1874  -0.0820 466 TYR A O   
3451 C CB  . TYR A 439 ? 1.4929 1.2724 1.0003 0.2888  0.1886  -0.0910 466 TYR A CB  
3452 C CG  . TYR A 439 ? 1.5804 1.3363 1.0955 0.3160  0.1917  -0.0989 466 TYR A CG  
3453 C CD1 . TYR A 439 ? 1.5831 1.3597 1.1263 0.3398  0.1831  -0.0931 466 TYR A CD1 
3454 C CD2 . TYR A 439 ? 1.6468 1.3580 1.1413 0.3183  0.2020  -0.1122 466 TYR A CD2 
3455 C CE1 . TYR A 439 ? 1.5983 1.3565 1.1529 0.3672  0.1848  -0.0989 466 TYR A CE1 
3456 C CE2 . TYR A 439 ? 1.6975 1.3843 1.2005 0.3466  0.2048  -0.1195 466 TYR A CE2 
3457 C CZ  . TYR A 439 ? 1.7025 1.4150 1.2375 0.3720  0.1962  -0.1121 466 TYR A CZ  
3458 O OH  . TYR A 439 ? 1.7968 1.4885 1.3445 0.4025  0.1981  -0.1181 466 TYR A OH  
3459 N N   . VAL A 440 ? 1.5596 1.4405 1.1050 0.2665  0.1758  -0.0743 467 VAL A N   
3460 C CA  . VAL A 440 ? 1.5334 1.4322 1.0801 0.2543  0.1669  -0.0620 467 VAL A CA  
3461 C C   . VAL A 440 ? 1.6328 1.5172 1.1786 0.2678  0.1555  -0.0517 467 VAL A C   
3462 O O   . VAL A 440 ? 1.6654 1.5463 1.2011 0.2604  0.1504  -0.0425 467 VAL A O   
3463 C CB  . VAL A 440 ? 1.5378 1.4796 1.1063 0.2482  0.1648  -0.0608 467 VAL A CB  
3464 C CG1 . VAL A 440 ? 1.5141 1.4680 1.0827 0.2373  0.1557  -0.0490 467 VAL A CG1 
3465 C CG2 . VAL A 440 ? 1.4674 1.4235 1.0327 0.2352  0.1768  -0.0708 467 VAL A CG2 
3466 N N   . GLY A 441 ? 1.5954 1.4730 1.1517 0.2883  0.1515  -0.0533 468 GLY A N   
3467 C CA  . GLY A 441 ? 1.5259 1.3852 1.0763 0.3019  0.1399  -0.0437 468 GLY A CA  
3468 C C   . GLY A 441 ? 1.6224 1.4509 1.1690 0.3206  0.1408  -0.0463 468 GLY A C   
3469 O O   . GLY A 441 ? 1.6599 1.4996 1.2262 0.3333  0.1451  -0.0552 468 GLY A O   
3470 N N   . ARG A 442 ? 1.5932 1.3830 1.1149 0.3230  0.1374  -0.0381 469 ARG A N   
3471 C CA  . ARG A 442 ? 1.7238 1.4752 1.2377 0.3403  0.1373  -0.0384 469 ARG A CA  
3472 C C   . ARG A 442 ? 1.7895 1.5045 1.2741 0.3393  0.1299  -0.0238 469 ARG A C   
3473 O O   . ARG A 442 ? 1.7247 1.4469 1.1958 0.3248  0.1279  -0.0159 469 ARG A O   
3474 C CB  . ARG A 442 ? 1.7428 1.4705 1.2478 0.3348  0.1523  -0.0518 469 ARG A CB  
3475 C CG  . ARG A 442 ? 1.6665 1.3820 1.1470 0.3071  0.1602  -0.0520 469 ARG A CG  
3476 C CD  . ARG A 442 ? 1.6752 1.3410 1.1319 0.3026  0.1690  -0.0591 469 ARG A CD  
3477 N NE  . ARG A 442 ? 1.7424 1.3987 1.1768 0.2738  0.1740  -0.0570 469 ARG A NE  
3478 C CZ  . ARG A 442 ? 1.8629 1.4740 1.2716 0.2618  0.1795  -0.0601 469 ARG A CZ  
3479 N NH1 . ARG A 442 ? 1.9711 1.5356 1.3702 0.2773  0.1813  -0.0659 469 ARG A NH1 
3480 N NH2 . ARG A 442 ? 1.7452 1.3575 1.1387 0.2335  0.1827  -0.0569 469 ARG A NH2 
3481 N N   . LYS A 443 ? 1.9216 1.5969 1.3962 0.3554  0.1265  -0.0198 470 LYS A N   
3482 C CA  . LYS A 443 ? 1.9631 1.5962 1.4051 0.3529  0.1212  -0.0047 470 LYS A CA  
3483 C C   . LYS A 443 ? 1.9410 1.5257 1.3613 0.3440  0.1322  -0.0088 470 LYS A C   
3484 O O   . LYS A 443 ? 1.9485 1.5075 1.3745 0.3601  0.1347  -0.0167 470 LYS A O   
3485 C CB  . LYS A 443 ? 1.8827 1.5035 1.3260 0.3773  0.1047  0.0072  470 LYS A CB  
3486 C CG  . LYS A 443 ? 1.9219 1.5063 1.3280 0.3721  0.0978  0.0258  470 LYS A CG  
3487 C CD  . LYS A 443 ? 2.0864 1.6613 1.4915 0.3956  0.0787  0.0393  470 LYS A CD  
3488 C CE  . LYS A 443 ? 2.1092 1.6579 1.4738 0.3869  0.0717  0.0586  470 LYS A CE  
3489 N NZ  . LYS A 443 ? 2.2497 1.7486 1.5826 0.3717  0.0827  0.0651  470 LYS A NZ  
3490 N N   . ARG A 444 ? 1.8282 1.4011 1.2247 0.3185  0.1389  -0.0041 471 ARG A N   
3491 C CA  . ARG A 444 ? 1.9012 1.4284 1.2747 0.3037  0.1482  -0.0073 471 ARG A CA  
3492 C C   . ARG A 444 ? 1.9687 1.4395 1.3161 0.3122  0.1414  0.0078  471 ARG A C   
3493 O O   . ARG A 444 ? 2.0144 1.4811 1.3434 0.3062  0.1355  0.0253  471 ARG A O   
3494 C CB  . ARG A 444 ? 1.7426 1.2851 1.1045 0.2717  0.1564  -0.0057 471 ARG A CB  
3495 C CG  . ARG A 444 ? 1.8715 1.3675 1.2065 0.2504  0.1636  -0.0053 471 ARG A CG  
3496 C CD  . ARG A 444 ? 1.8272 1.3490 1.1565 0.2194  0.1696  -0.0005 471 ARG A CD  
3497 N NE  . ARG A 444 ? 1.9724 1.4508 1.2736 0.1965  0.1737  0.0070  471 ARG A NE  
3498 C CZ  . ARG A 444 ? 2.0212 1.5168 1.3158 0.1685  0.1786  0.0152  471 ARG A CZ  
3499 N NH1 . ARG A 444 ? 1.9740 1.5271 1.2876 0.1620  0.1803  0.0164  471 ARG A NH1 
3500 N NH2 . ARG A 444 ? 2.0121 1.4663 1.2817 0.1464  0.1817  0.0229  471 ARG A NH2 
3501 N N   . MET A 445 ? 1.9856 1.4116 1.3297 0.3268  0.1424  0.0011  472 MET A N   
3502 C CA  . MET A 445 ? 1.9979 1.3639 1.3174 0.3370  0.1346  0.0164  472 MET A CA  
3503 C C   . MET A 445 ? 2.0382 1.3516 1.3230 0.3099  0.1419  0.0209  472 MET A C   
3504 O O   . MET A 445 ? 2.2391 1.5080 1.4967 0.3081  0.1354  0.0400  472 MET A O   
3505 C CB  . MET A 445 ? 2.1537 1.4944 1.4895 0.3708  0.1305  0.0084  472 MET A CB  
3506 C CG  . MET A 445 ? 2.2252 1.6206 1.5996 0.3971  0.1225  0.0048  472 MET A CG  
3507 S SD  . MET A 445 ? 2.0886 1.5066 1.4591 0.4052  0.1024  0.0297  472 MET A SD  
3508 C CE  . MET A 445 ? 2.0925 1.4386 1.4404 0.4275  0.0895  0.0481  472 MET A CE  
3509 N N   . GLN A 446 ? 1.9911 1.3083 1.2747 0.2872  0.1541  0.0049  473 GLN A N   
3510 C CA  . GLN A 446 ? 2.1032 1.3787 1.3561 0.2555  0.1603  0.0090  473 GLN A CA  
3511 C C   . GLN A 446 ? 2.1676 1.4844 1.4160 0.2285  0.1622  0.0228  473 GLN A C   
3512 O O   . GLN A 446 ? 2.1762 1.5430 1.4407 0.2134  0.1683  0.0134  473 GLN A O   
3513 C CB  . GLN A 446 ? 2.1066 1.3686 1.3588 0.2424  0.1708  -0.0150 473 GLN A CB  
3514 C CG  . GLN A 446 ? 2.1455 1.3793 1.3705 0.2027  0.1763  -0.0128 473 GLN A CG  
3515 C CD  . GLN A 446 ? 2.3924 1.5584 1.5851 0.1953  0.1715  0.0064  473 GLN A CD  
3516 O OE1 . GLN A 446 ? 2.4318 1.6070 1.6127 0.1769  0.1697  0.0277  473 GLN A OE1 
3517 N NE2 . GLN A 446 ? 2.5745 1.6709 1.7519 0.2098  0.1701  -0.0009 473 GLN A NE2 
3518 N N   . VAL A 447 ? 2.1681 1.4649 1.3945 0.2235  0.1573  0.0456  474 VAL A N   
3519 C CA  . VAL A 447 ? 2.1825 1.5191 1.4042 0.2017  0.1608  0.0593  474 VAL A CA  
3520 C C   . VAL A 447 ? 2.2628 1.5648 1.4548 0.1693  0.1664  0.0738  474 VAL A C   
3521 O O   . VAL A 447 ? 2.2534 1.5925 1.4442 0.1481  0.1725  0.0837  474 VAL A O   
3522 C CB  . VAL A 447 ? 2.1453 1.5054 1.3671 0.2217  0.1520  0.0739  474 VAL A CB  
3523 C CG1 . VAL A 447 ? 1.9860 1.3930 1.2411 0.2465  0.1469  0.0599  474 VAL A CG1 
3524 C CG2 . VAL A 447 ? 2.2261 1.5281 1.4220 0.2369  0.1417  0.0909  474 VAL A CG2 
3525 N N   . GLU A 448 ? 2.3003 1.5329 1.4692 0.1645  0.1649  0.0757  475 GLU A N   
3526 C CA  . GLU A 448 ? 2.3239 1.5220 1.4652 0.1289  0.1700  0.0891  475 GLU A CA  
3527 C C   . GLU A 448 ? 2.3498 1.5857 1.5040 0.0966  0.1795  0.0770  475 GLU A C   
3528 O O   . GLU A 448 ? 2.3205 1.5985 1.4774 0.0731  0.1856  0.0883  475 GLU A O   
3529 C CB  . GLU A 448 ? 2.2608 1.3705 1.3751 0.1302  0.1655  0.0906  475 GLU A CB  
3530 C CG  . GLU A 448 ? 2.3972 1.4620 1.4927 0.1559  0.1545  0.1101  475 GLU A CG  
3531 C CD  . GLU A 448 ? 2.5621 1.5338 1.6287 0.1542  0.1501  0.1144  475 GLU A CD  
3532 O OE1 . GLU A 448 ? 2.4783 1.4173 1.5279 0.1203  0.1563  0.1118  475 GLU A OE1 
3533 O OE2 . GLU A 448 ? 2.6415 1.5719 1.7031 0.1868  0.1394  0.1204  475 GLU A OE2 
3534 N N   . HIS A 449 ? 2.3898 1.6132 1.5520 0.0960  0.1808  0.0538  476 HIS A N   
3535 C CA  . HIS A 449 ? 2.3545 1.6126 1.5276 0.0663  0.1871  0.0412  476 HIS A CA  
3536 C C   . HIS A 449 ? 2.2599 1.5763 1.4647 0.0838  0.1880  0.0221  476 HIS A C   
3537 O O   . HIS A 449 ? 2.2205 1.5304 1.4350 0.1161  0.1849  0.0112  476 HIS A O   
3538 C CB  . HIS A 449 ? 2.4372 1.6327 1.5874 0.0443  0.1879  0.0289  476 HIS A CB  
3539 C CG  . HIS A 449 ? 2.4162 1.5613 1.5611 0.0731  0.1856  0.0091  476 HIS A CG  
3540 N ND1 . HIS A 449 ? 2.4245 1.5970 1.5879 0.0866  0.1885  -0.0160 476 HIS A ND1 
3541 C CD2 . HIS A 449 ? 2.5084 1.5780 1.6321 0.0916  0.1814  0.0111  476 HIS A CD2 
3542 C CE1 . HIS A 449 ? 2.5578 1.6772 1.7132 0.1129  0.1880  -0.0299 476 HIS A CE1 
3543 N NE2 . HIS A 449 ? 2.6145 1.6700 1.7470 0.1176  0.1830  -0.0140 476 HIS A NE2 
3544 N N   . PRO A 450 ? 2.1181 1.4940 1.3411 0.0631  0.1918  0.0194  477 PRO A N   
3545 C CA  . PRO A 450 ? 2.0250 1.4523 1.2752 0.0760  0.1920  0.0026  477 PRO A CA  
3546 C C   . PRO A 450 ? 2.0593 1.4540 1.3028 0.0806  0.1930  -0.0212 477 PRO A C   
3547 O O   . PRO A 450 ? 2.2414 1.5832 1.4605 0.0626  0.1940  -0.0279 477 PRO A O   
3548 C CB  . PRO A 450 ? 1.8680 1.3533 1.1333 0.0471  0.1948  0.0072  477 PRO A CB  
3549 C CG  . PRO A 450 ? 1.9174 1.3747 1.1621 0.0142  0.1968  0.0205  477 PRO A CG  
3550 C CD  . PRO A 450 ? 1.9987 1.4022 1.2208 0.0283  0.1956  0.0340  477 PRO A CD  
3551 N N   . GLU A 451 ? 2.0386 1.4648 1.3031 0.1046  0.1931  -0.0347 478 GLU A N   
3552 C CA  . GLU A 451 ? 2.2056 1.6072 1.4653 0.1141  0.1966  -0.0584 478 GLU A CA  
3553 C C   . GLU A 451 ? 2.0868 1.5084 1.3419 0.0838  0.1996  -0.0722 478 GLU A C   
3554 O O   . GLU A 451 ? 2.0685 1.5398 1.3356 0.0624  0.1977  -0.0634 478 GLU A O   
3555 C CB  . GLU A 451 ? 2.1006 1.5340 1.3860 0.1491  0.1965  -0.0659 478 GLU A CB  
3556 C CG  . GLU A 451 ? 2.1419 1.5570 1.4319 0.1792  0.1908  -0.0526 478 GLU A CG  
3557 C CD  . GLU A 451 ? 2.0493 1.5105 1.3699 0.2082  0.1884  -0.0555 478 GLU A CD  
3558 O OE1 . GLU A 451 ? 2.0769 1.5907 1.4161 0.2019  0.1907  -0.0622 478 GLU A OE1 
3559 O OE2 . GLU A 451 ? 2.1028 1.5474 1.4290 0.2361  0.1829  -0.0498 478 GLU A OE2 
3560 N N   . LYS A 452 ? 2.0240 1.4062 1.2610 0.0829  0.2039  -0.0943 479 LYS A N   
3561 C CA  . LYS A 452 ? 2.0885 1.4772 1.3115 0.0507  0.2054  -0.1085 479 LYS A CA  
3562 C C   . LYS A 452 ? 2.0435 1.5060 1.2904 0.0496  0.2053  -0.1118 479 LYS A C   
3563 O O   . LYS A 452 ? 2.0590 1.5420 1.3205 0.0754  0.2093  -0.1217 479 LYS A O   
3564 C CB  . LYS A 452 ? 2.1097 1.4362 1.3042 0.0536  0.2112  -0.1344 479 LYS A CB  
3565 C CG  . LYS A 452 ? 2.0959 1.4189 1.2669 0.0161  0.2111  -0.1500 479 LYS A CG  
3566 C CD  . LYS A 452 ? 2.2438 1.5081 1.3847 0.0222  0.2189  -0.1801 479 LYS A CD  
3567 C CE  . LYS A 452 ? 2.2276 1.4901 1.3411 -0.0176 0.2172  -0.1963 479 LYS A CE  
3568 N NZ  . LYS A 452 ? 2.3383 1.5513 1.4207 -0.0101 0.2268  -0.2296 479 LYS A NZ  
3569 N N   . ALA A 453 ? 1.9021 1.4053 1.1543 0.0192  0.2004  -0.1024 480 ALA A N   
3570 C CA  . ALA A 453 ? 1.7772 1.3480 1.0511 0.0161  0.1983  -0.1022 480 ALA A CA  
3571 C C   . ALA A 453 ? 1.9090 1.4758 1.1649 0.0065  0.2016  -0.1257 480 ALA A C   
3572 O O   . ALA A 453 ? 1.9434 1.4585 1.1678 -0.0071 0.2043  -0.1422 480 ALA A O   
3573 C CB  . ALA A 453 ? 1.5845 1.2005 0.8718 -0.0115 0.1913  -0.0839 480 ALA A CB  
3574 N N   . VAL A 454 ? 1.8556 1.4758 1.1293 0.0130  0.2014  -0.1273 481 VAL A N   
3575 C CA  . VAL A 454 ? 1.8109 1.4381 1.0674 0.0034  0.2049  -0.1474 481 VAL A CA  
3576 C C   . VAL A 454 ? 1.8190 1.4855 1.0731 -0.0323 0.1950  -0.1402 481 VAL A C   
3577 O O   . VAL A 454 ? 1.9007 1.6229 1.1833 -0.0324 0.1882  -0.1220 481 VAL A O   
3578 C CB  . VAL A 454 ? 1.8092 1.4716 1.0854 0.0306  0.2108  -0.1519 481 VAL A CB  
3579 C CG1 . VAL A 454 ? 1.7566 1.4251 1.0105 0.0197  0.2167  -0.1728 481 VAL A CG1 
3580 C CG2 . VAL A 454 ? 1.7828 1.4150 1.0687 0.0666  0.2182  -0.1556 481 VAL A CG2 
3581 N N   . PRO A 455 ? 2.0004 1.6395 1.2221 -0.0624 0.1927  -0.1535 482 PRO A N   
3582 C CA  . PRO A 455 ? 2.0567 1.7364 1.2780 -0.0979 0.1805  -0.1447 482 PRO A CA  
3583 C C   . PRO A 455 ? 1.9873 1.7259 1.2211 -0.0958 0.1772  -0.1422 482 PRO A C   
3584 O O   . PRO A 455 ? 1.9858 1.7225 1.2113 -0.0786 0.1861  -0.1567 482 PRO A O   
3585 C CB  . PRO A 455 ? 2.1264 1.7559 1.3033 -0.1278 0.1797  -0.1658 482 PRO A CB  
3586 C CG  . PRO A 455 ? 2.1980 1.7548 1.3579 -0.1096 0.1901  -0.1778 482 PRO A CG  
3587 C CD  . PRO A 455 ? 2.0995 1.6664 1.2831 -0.0658 0.2000  -0.1768 482 PRO A CD  
3588 N N   . ARG A 456 ? 1.9350 1.7275 1.1907 -0.1131 0.1645  -0.1221 483 ARG A N   
3589 C CA  . ARG A 456 ? 1.8095 1.6594 1.0772 -0.1173 0.1569  -0.1142 483 ARG A CA  
3590 C C   . ARG A 456 ? 1.7036 1.5813 1.0004 -0.0837 0.1620  -0.1055 483 ARG A C   
3591 O O   . ARG A 456 ? 1.7009 1.6216 1.0068 -0.0852 0.1562  -0.0981 483 ARG A O   
3592 C CB  . ARG A 456 ? 1.8940 1.7355 1.1223 -0.1367 0.1570  -0.1346 483 ARG A CB  
3593 C CG  . ARG A 456 ? 1.8472 1.6749 1.0467 -0.1774 0.1463  -0.1409 483 ARG A CG  
3594 C CD  . ARG A 456 ? 1.9167 1.7206 1.0673 -0.1940 0.1496  -0.1673 483 ARG A CD  
3595 N NE  . ARG A 456 ? 2.0743 1.8100 1.1954 -0.1795 0.1664  -0.1941 483 ARG A NE  
3596 C CZ  . ARG A 456 ? 2.1468 1.8701 1.2628 -0.1502 0.1827  -0.2089 483 ARG A CZ  
3597 N NH1 . ARG A 456 ? 2.0286 1.8009 1.1642 -0.1346 0.1847  -0.1999 483 ARG A NH1 
3598 N NH2 . ARG A 456 ? 2.1930 1.8534 1.2850 -0.1362 0.1972  -0.2328 483 ARG A NH2 
3599 N N   . VAL A 457 ? 1.6690 1.5233 0.9797 -0.0550 0.1710  -0.1050 484 VAL A N   
3600 C CA  . VAL A 457 ? 1.5920 1.4712 0.9310 -0.0249 0.1742  -0.0965 484 VAL A CA  
3601 C C   . VAL A 457 ? 1.6289 1.5084 0.9939 -0.0100 0.1726  -0.0801 484 VAL A C   
3602 O O   . VAL A 457 ? 1.6659 1.5044 1.0243 0.0022  0.1792  -0.0849 484 VAL A O   
3603 C CB  . VAL A 457 ? 1.6696 1.5229 0.9982 -0.0021 0.1874  -0.1150 484 VAL A CB  
3604 C CG1 . VAL A 457 ? 1.5709 1.4506 0.9314 0.0262  0.1886  -0.1045 484 VAL A CG1 
3605 C CG2 . VAL A 457 ? 1.5252 1.3827 0.8261 -0.0166 0.1914  -0.1318 484 VAL A CG2 
3606 N N   . ARG A 458 ? 1.6619 1.5862 1.0550 -0.0099 0.1642  -0.0606 485 ARG A N   
3607 C CA  . ARG A 458 ? 1.6018 1.5304 1.0169 0.0024  0.1637  -0.0456 485 ARG A CA  
3608 C C   . ARG A 458 ? 1.6418 1.5562 1.0671 0.0347  0.1698  -0.0470 485 ARG A C   
3609 O O   . ARG A 458 ? 1.6056 1.5282 1.0350 0.0484  0.1715  -0.0529 485 ARG A O   
3610 C CB  . ARG A 458 ? 1.5919 1.5731 1.0352 -0.0033 0.1542  -0.0266 485 ARG A CB  
3611 C CG  . ARG A 458 ? 1.6669 1.6658 1.1084 -0.0342 0.1470  -0.0201 485 ARG A CG  
3612 C CD  . ARG A 458 ? 1.7555 1.8113 1.2289 -0.0367 0.1368  -0.0012 485 ARG A CD  
3613 N NE  . ARG A 458 ? 1.8523 1.9343 1.3233 -0.0453 0.1275  -0.0009 485 ARG A NE  
3614 C CZ  . ARG A 458 ? 1.9692 2.0685 1.4529 -0.0272 0.1251  0.0037  485 ARG A CZ  
3615 N NH1 . ARG A 458 ? 2.0997 2.1940 1.6005 0.0004  0.1305  0.0072  485 ARG A NH1 
3616 N NH2 . ARG A 458 ? 1.9261 2.0470 1.4028 -0.0390 0.1163  0.0054  485 ARG A NH2 
3617 N N   . ASN A 459 ? 1.5823 1.4765 1.0108 0.0451  0.1727  -0.0406 486 ASN A N   
3618 C CA  . ASN A 459 ? 1.6395 1.5224 1.0777 0.0743  0.1756  -0.0390 486 ASN A CA  
3619 C C   . ASN A 459 ? 1.6069 1.4570 1.0322 0.0894  0.1815  -0.0550 486 ASN A C   
3620 O O   . ASN A 459 ? 1.5911 1.4441 1.0289 0.1129  0.1819  -0.0554 486 ASN A O   
3621 C CB  . ASN A 459 ? 1.6997 1.6237 1.1645 0.0879  0.1703  -0.0291 486 ASN A CB  
3622 C CG  . ASN A 459 ? 1.6156 1.5710 1.0970 0.0803  0.1659  -0.0134 486 ASN A CG  
3623 O OD1 . ASN A 459 ? 1.7666 1.7151 1.2426 0.0679  0.1680  -0.0080 486 ASN A OD1 
3624 N ND2 . ASN A 459 ? 1.5787 1.5688 1.0815 0.0880  0.1602  -0.0057 486 ASN A ND2 
3625 N N   . LEU A 460 ? 1.5950 1.4141 0.9960 0.0766  0.1861  -0.0691 487 LEU A N   
3626 C CA  . LEU A 460 ? 1.5834 1.3697 0.9727 0.0929  0.1937  -0.0860 487 LEU A CA  
3627 C C   . LEU A 460 ? 1.6666 1.3957 1.0303 0.0878  0.1976  -0.0932 487 LEU A C   
3628 O O   . LEU A 460 ? 1.6629 1.3788 1.0084 0.0611  0.1961  -0.0944 487 LEU A O   
3629 C CB  . LEU A 460 ? 1.5410 1.3429 0.9225 0.0852  0.1979  -0.1008 487 LEU A CB  
3630 C CG  . LEU A 460 ? 1.5746 1.3522 0.9500 0.1063  0.2083  -0.1190 487 LEU A CG  
3631 C CD1 . LEU A 460 ? 1.3438 1.1451 0.7486 0.1341  0.2078  -0.1126 487 LEU A CD1 
3632 C CD2 . LEU A 460 ? 1.6593 1.4437 1.0160 0.0931  0.2154  -0.1366 487 LEU A CD2 
3633 N N   . VAL A 461 ? 1.6374 1.3322 1.0000 0.1128  0.2013  -0.0972 488 VAL A N   
3634 C CA  . VAL A 461 ? 1.7474 1.3807 1.0857 0.1124  0.2043  -0.1026 488 VAL A CA  
3635 C C   . VAL A 461 ? 1.8518 1.4546 1.1855 0.1372  0.2120  -0.1207 488 VAL A C   
3636 O O   . VAL A 461 ? 1.7164 1.3482 1.0715 0.1591  0.2142  -0.1240 488 VAL A O   
3637 C CB  . VAL A 461 ? 1.6540 1.2695 0.9944 0.1193  0.1995  -0.0837 488 VAL A CB  
3638 C CG1 . VAL A 461 ? 1.8337 1.4769 1.1772 0.0936  0.1950  -0.0675 488 VAL A CG1 
3639 C CG2 . VAL A 461 ? 1.5930 1.2285 0.9568 0.1506  0.1965  -0.0761 488 VAL A CG2 
3640 N N   . GLU A 462 ? 1.9127 1.4559 1.2191 0.1333  0.2162  -0.1324 489 GLU A N   
3641 C CA  . GLU A 462 ? 1.8426 1.3492 1.1446 0.1603  0.2243  -0.1498 489 GLU A CA  
3642 C C   . GLU A 462 ? 1.9520 1.4444 1.2707 0.1914  0.2197  -0.1366 489 GLU A C   
3643 O O   . GLU A 462 ? 2.0377 1.5007 1.3471 0.1873  0.2129  -0.1206 489 GLU A O   
3644 C CB  . GLU A 462 ? 1.9845 1.4243 1.2495 0.1467  0.2294  -0.1668 489 GLU A CB  
3645 C CG  . GLU A 462 ? 2.0847 1.5338 1.3273 0.1129  0.2320  -0.1810 489 GLU A CG  
3646 C CD  . GLU A 462 ? 2.1863 1.5633 1.3888 0.0987  0.2363  -0.2001 489 GLU A CD  
3647 O OE1 . GLU A 462 ? 2.1211 1.4392 1.3150 0.1193  0.2388  -0.2038 489 GLU A OE1 
3648 O OE2 . GLU A 462 ? 2.1028 1.4802 1.2815 0.0666  0.2359  -0.2111 489 GLU A OE2 
3649 N N   . ALA A 463 ? 1.9543 1.4698 1.2976 0.2213  0.2229  -0.1424 490 ALA A N   
3650 C CA  . ALA A 463 ? 1.9889 1.5027 1.3522 0.2507  0.2157  -0.1285 490 ALA A CA  
3651 C C   . ALA A 463 ? 2.1196 1.5628 1.4650 0.2671  0.2157  -0.1308 490 ALA A C   
3652 O O   . ALA A 463 ? 2.1010 1.5145 1.4410 0.2820  0.2250  -0.1505 490 ALA A O   
3653 C CB  . ALA A 463 ? 1.8958 1.4579 1.2931 0.2757  0.2184  -0.1342 490 ALA A CB  
3654 N N   . ASP A 464 ? 2.1579 1.5728 1.4929 0.2648  0.2057  -0.1105 491 ASP A N   
3655 C CA  . ASP A 464 ? 2.2676 1.6162 1.5880 0.2837  0.2025  -0.1068 491 ASP A CA  
3656 C C   . ASP A 464 ? 2.1470 1.5135 1.4963 0.3215  0.1951  -0.0984 491 ASP A C   
3657 O O   . ASP A 464 ? 2.0863 1.5078 1.4664 0.3355  0.1973  -0.1051 491 ASP A O   
3658 C CB  . ASP A 464 ? 2.2734 1.5821 1.5659 0.2612  0.1953  -0.0870 491 ASP A CB  
3659 C CG  . ASP A 464 ? 2.3609 1.6439 1.6248 0.2236  0.2012  -0.0957 491 ASP A CG  
3660 O OD1 . ASP A 464 ? 2.3804 1.6776 1.6437 0.2145  0.2098  -0.1172 491 ASP A OD1 
3661 O OD2 . ASP A 464 ? 2.1735 1.4237 1.4148 0.2016  0.1969  -0.0804 491 ASP A OD2 
3662 N N   . TYR A 465 ? 2.1331 1.4552 1.4728 0.3368  0.1853  -0.0823 492 TYR A N   
3663 C CA  . TYR A 465 ? 2.1358 1.4745 1.5025 0.3725  0.1755  -0.0730 492 TYR A CA  
3664 C C   . TYR A 465 ? 2.1424 1.5498 1.5314 0.3691  0.1673  -0.0603 492 TYR A C   
3665 O O   . TYR A 465 ? 2.0906 1.5018 1.4642 0.3506  0.1606  -0.0429 492 TYR A O   
3666 C CB  . TYR A 465 ? 2.1394 1.4154 1.4866 0.3866  0.1640  -0.0546 492 TYR A CB  
3667 C CG  . TYR A 465 ? 2.2706 1.5558 1.6459 0.4275  0.1531  -0.0477 492 TYR A CG  
3668 C CD1 . TYR A 465 ? 2.2674 1.5936 1.6807 0.4526  0.1591  -0.0649 492 TYR A CD1 
3669 C CD2 . TYR A 465 ? 2.3794 1.6362 1.7439 0.4399  0.1365  -0.0229 492 TYR A CD2 
3670 C CE1 . TYR A 465 ? 2.2850 1.6260 1.7291 0.4896  0.1482  -0.0578 492 TYR A CE1 
3671 C CE2 . TYR A 465 ? 2.3441 1.6127 1.7358 0.4768  0.1239  -0.0152 492 TYR A CE2 
3672 C CZ  . TYR A 465 ? 2.2905 1.6027 1.7242 0.5018  0.1295  -0.0327 492 TYR A CZ  
3673 O OH  . TYR A 465 ? 2.2081 1.5379 1.6735 0.5382  0.1160  -0.0243 492 TYR A OH  
3674 N N   . SER A 466 ? 2.1438 1.6052 1.5683 0.3859  0.1688  -0.0695 493 SER A N   
3675 C CA  . SER A 466 ? 2.1240 1.6471 1.5712 0.3845  0.1601  -0.0594 493 SER A CA  
3676 C C   . SER A 466 ? 2.1257 1.6672 1.6030 0.4183  0.1487  -0.0535 493 SER A C   
3677 O O   . SER A 466 ? 2.0986 1.6142 1.5854 0.4443  0.1500  -0.0596 493 SER A O   
3678 C CB  . SER A 466 ? 2.0660 1.6430 1.5296 0.3681  0.1704  -0.0733 493 SER A CB  
3679 O OG  . SER A 466 ? 2.0227 1.5845 1.4601 0.3376  0.1793  -0.0786 493 SER A OG  
3680 N N   . TYR A 467 ? 2.2474 1.8344 1.7408 0.4184  0.1366  -0.0419 494 TYR A N   
3681 C CA  . TYR A 467 ? 2.2988 1.9017 1.8176 0.4474  0.1215  -0.0328 494 TYR A CA  
3682 C C   . TYR A 467 ? 2.1890 1.8597 1.7410 0.4480  0.1140  -0.0320 494 TYR A C   
3683 O O   . TYR A 467 ? 2.2172 1.9046 1.7881 0.4675  0.0977  -0.0218 494 TYR A O   
3684 C CB  . TYR A 467 ? 2.4528 2.0149 1.9437 0.4514  0.1054  -0.0107 494 TYR A CB  
3685 C CG  . TYR A 467 ? 2.4525 1.9967 1.9578 0.4856  0.0917  -0.0019 494 TYR A CG  
3686 C CD1 . TYR A 467 ? 2.4662 1.9575 1.9655 0.5035  0.0971  -0.0065 494 TYR A CD1 
3687 C CD2 . TYR A 467 ? 2.4649 2.0434 1.9893 0.5000  0.0720  0.0111  494 TYR A CD2 
3688 C CE1 . TYR A 467 ? 2.5866 2.0614 2.1017 0.5375  0.0835  0.0030  494 TYR A CE1 
3689 C CE2 . TYR A 467 ? 2.5904 2.1564 2.1304 0.5318  0.0571  0.0211  494 TYR A CE2 
3690 C CZ  . TYR A 467 ? 2.6881 2.2028 2.2247 0.5517  0.0630  0.0177  494 TYR A CZ  
3691 O OH  . TYR A 467 ? 2.7503 2.2524 2.3051 0.5861  0.0471  0.0289  494 TYR A OH  
3692 N N   . TRP A 468 ? 1.8337 1.5429 1.3936 0.4273  0.1235  -0.0414 495 TRP A N   
3693 C CA  . TRP A 468 ? 1.7624 1.5310 1.3525 0.4258  0.1159  -0.0402 495 TRP A CA  
3694 C C   . TRP A 468 ? 1.8718 1.6796 1.4867 0.4198  0.1315  -0.0568 495 TRP A C   
3695 O O   . TRP A 468 ? 1.8471 1.6366 1.4521 0.4155  0.1483  -0.0702 495 TRP A O   
3696 C CB  . TRP A 468 ? 1.7473 1.5252 1.3185 0.4040  0.1077  -0.0299 495 TRP A CB  
3697 C CG  . TRP A 468 ? 1.8397 1.5999 1.3949 0.4122  0.0892  -0.0131 495 TRP A CG  
3698 C CD1 . TRP A 468 ? 1.7363 1.4897 1.3020 0.4366  0.0746  -0.0048 495 TRP A CD1 
3699 C CD2 . TRP A 468 ? 1.7809 1.5294 1.3053 0.3964  0.0833  -0.0024 495 TRP A CD2 
3700 N NE1 . TRP A 468 ? 1.6670 1.4034 1.2065 0.4351  0.0591  0.0109  495 TRP A NE1 
3701 C CE2 . TRP A 468 ? 1.7394 1.4725 1.2526 0.4107  0.0655  0.0117  495 TRP A CE2 
3702 C CE3 . TRP A 468 ? 1.6952 1.4466 1.2011 0.3724  0.0917  -0.0033 495 TRP A CE3 
3703 C CZ2 . TRP A 468 ? 1.7928 1.5125 1.2732 0.4008  0.0576  0.0235  495 TRP A CZ2 
3704 C CZ3 . TRP A 468 ? 1.7831 1.5230 1.2612 0.3647  0.0847  0.0081  495 TRP A CZ3 
3705 C CH2 . TRP A 468 ? 1.8166 1.5403 1.2803 0.3784  0.0686  0.0207  495 TRP A CH2 
3706 N N   . THR A 469 ? 1.7655 1.6268 1.4105 0.4178  0.1254  -0.0556 496 THR A N   
3707 C CA  . THR A 469 ? 1.6355 1.5403 1.3032 0.4080  0.1389  -0.0678 496 THR A CA  
3708 C C   . THR A 469 ? 1.5737 1.5173 1.2505 0.3889  0.1299  -0.0608 496 THR A C   
3709 O O   . THR A 469 ? 1.5131 1.5040 1.2217 0.3874  0.1306  -0.0635 496 THR A O   
3710 C CB  . THR A 469 ? 1.5076 1.4426 1.2148 0.4319  0.1443  -0.0760 496 THR A CB  
3711 O OG1 . THR A 469 ? 1.8323 1.7776 1.5612 0.4526  0.1248  -0.0641 496 THR A OG1 
3712 C CG2 . THR A 469 ? 1.6818 1.5800 1.3785 0.4466  0.1611  -0.0899 496 THR A CG2 
3713 N N   . LEU A 470 ? 1.6022 1.5254 1.2512 0.3740  0.1218  -0.0517 497 LEU A N   
3714 C CA  . LEU A 470 ? 1.4944 1.4456 1.1484 0.3580  0.1124  -0.0456 497 LEU A CA  
3715 C C   . LEU A 470 ? 1.4714 1.4552 1.1380 0.3403  0.1241  -0.0527 497 LEU A C   
3716 O O   . LEU A 470 ? 1.4332 1.4558 1.1255 0.3356  0.1188  -0.0511 497 LEU A O   
3717 C CB  . LEU A 470 ? 1.5003 1.4214 1.1200 0.3465  0.1068  -0.0373 497 LEU A CB  
3718 C CG  . LEU A 470 ? 1.4759 1.3662 1.0768 0.3597  0.0937  -0.0273 497 LEU A CG  
3719 C CD1 . LEU A 470 ? 1.5339 1.3937 1.0984 0.3464  0.0963  -0.0215 497 LEU A CD1 
3720 C CD2 . LEU A 470 ? 1.5632 1.4773 1.1797 0.3665  0.0743  -0.0209 497 LEU A CD2 
3721 N N   . ALA A 471 ? 1.4777 1.4457 1.1250 0.3285  0.1392  -0.0596 498 ALA A N   
3722 C CA  . ALA A 471 ? 1.3811 1.3769 1.0345 0.3108  0.1503  -0.0654 498 ALA A CA  
3723 C C   . ALA A 471 ? 1.4638 1.4351 1.0937 0.3040  0.1664  -0.0757 498 ALA A C   
3724 O O   . ALA A 471 ? 1.4460 1.3783 1.0499 0.3028  0.1662  -0.0743 498 ALA A O   
3725 C CB  . ALA A 471 ? 1.3029 1.3103 0.9508 0.2914  0.1422  -0.0563 498 ALA A CB  
3726 N N   . TYR A 472 ? 1.3882 1.3825 1.0256 0.2978  0.1803  -0.0860 499 TYR A N   
3727 C CA  . TYR A 472 ? 1.4064 1.3777 1.0195 0.2908  0.1956  -0.0987 499 TYR A CA  
3728 C C   . TYR A 472 ? 1.4605 1.4665 1.0769 0.2751  0.2077  -0.1058 499 TYR A C   
3729 O O   . TYR A 472 ? 1.4522 1.4998 1.0950 0.2753  0.2076  -0.1029 499 TYR A O   
3730 C CB  . TYR A 472 ? 1.4015 1.3445 1.0141 0.3142  0.2035  -0.1103 499 TYR A CB  
3731 C CG  . TYR A 472 ? 1.3805 1.3574 1.0289 0.3352  0.2082  -0.1160 499 TYR A CG  
3732 C CD1 . TYR A 472 ? 1.3895 1.3931 1.0462 0.3341  0.2264  -0.1304 499 TYR A CD1 
3733 C CD2 . TYR A 472 ? 1.3949 1.3803 1.0691 0.3558  0.1945  -0.1067 499 TYR A CD2 
3734 C CE1 . TYR A 472 ? 1.2758 1.3167 0.9694 0.3537  0.2326  -0.1353 499 TYR A CE1 
3735 C CE2 . TYR A 472 ? 1.3566 1.3792 1.0688 0.3749  0.1980  -0.1108 499 TYR A CE2 
3736 C CZ  . TYR A 472 ? 1.3642 1.4161 1.0880 0.3742  0.2178  -0.1251 499 TYR A CZ  
3737 O OH  . TYR A 472 ? 1.4526 1.5475 1.2181 0.3935  0.2229  -0.1288 499 TYR A OH  
3738 N N   . VAL A 473 ? 1.5894 1.5778 1.1769 0.2594  0.2176  -0.1144 500 VAL A N   
3739 C CA  . VAL A 473 ? 1.5737 1.5884 1.1549 0.2439  0.2308  -0.1232 500 VAL A CA  
3740 C C   . VAL A 473 ? 1.6012 1.6018 1.1754 0.2578  0.2491  -0.1442 500 VAL A C   
3741 O O   . VAL A 473 ? 1.6702 1.6255 1.2272 0.2681  0.2511  -0.1526 500 VAL A O   
3742 C CB  . VAL A 473 ? 1.5675 1.5743 1.1194 0.2162  0.2281  -0.1191 500 VAL A CB  
3743 C CG1 . VAL A 473 ? 1.5226 1.5601 1.0662 0.1986  0.2392  -0.1250 500 VAL A CG1 
3744 C CG2 . VAL A 473 ? 1.4825 1.4965 1.0422 0.2079  0.2106  -0.0993 500 VAL A CG2 
3745 N N   . ILE A 474 ? 1.6049 1.6427 1.1915 0.2582  0.2632  -0.1530 501 ILE A N   
3746 C CA  . ILE A 474 ? 1.6212 1.6517 1.2050 0.2750  0.2833  -0.1751 501 ILE A CA  
3747 C C   . ILE A 474 ? 1.5411 1.6001 1.1084 0.2561  0.3004  -0.1858 501 ILE A C   
3748 O O   . ILE A 474 ? 1.5712 1.6764 1.1529 0.2417  0.2991  -0.1747 501 ILE A O   
3749 C CB  . ILE A 474 ? 1.5873 1.6411 1.2142 0.3058  0.2855  -0.1758 501 ILE A CB  
3750 C CG1 . ILE A 474 ? 1.6473 1.6970 1.2745 0.3260  0.3087  -0.1999 501 ILE A CG1 
3751 C CG2 . ILE A 474 ? 1.4795 1.5936 1.1419 0.2989  0.2799  -0.1613 501 ILE A CG2 
3752 C CD1 . ILE A 474 ? 1.5481 1.6136 1.2187 0.3613  0.3094  -0.2009 501 ILE A CD1 
3753 N N   . SER A 475 ? 1.5830 1.6121 1.1172 0.2548  0.3160  -0.2073 502 SER A N   
3754 C CA  . SER A 475 ? 1.6586 1.7093 1.1683 0.2363  0.3333  -0.2202 502 SER A CA  
3755 C C   . SER A 475 ? 1.6660 1.7429 1.1940 0.2586  0.3575  -0.2391 502 SER A C   
3756 O O   . SER A 475 ? 1.6777 1.7499 1.2360 0.2899  0.3605  -0.2439 502 SER A O   
3757 C CB  . SER A 475 ? 1.5234 1.5267 0.9810 0.2181  0.3357  -0.2343 502 SER A CB  
3758 O OG  . SER A 475 ? 1.6072 1.5590 1.0534 0.2396  0.3438  -0.2538 502 SER A OG  
3759 N N   . LEU A 476 ? 1.5409 1.6481 1.0502 0.2422  0.3752  -0.2491 503 LEU A N   
3760 C CA  . LEU A 476 ? 1.5956 1.7329 1.1200 0.2618  0.4021  -0.2687 503 LEU A CA  
3761 C C   . LEU A 476 ? 1.7321 1.8170 1.2350 0.2854  0.4175  -0.2979 503 LEU A C   
3762 O O   . LEU A 476 ? 1.7673 1.8612 1.3010 0.3186  0.4319  -0.3104 503 LEU A O   
3763 C CB  . LEU A 476 ? 1.6800 1.8608 1.1827 0.2355  0.4181  -0.2718 503 LEU A CB  
3764 C CG  . LEU A 476 ? 1.7221 1.9468 1.2412 0.2518  0.4491  -0.2903 503 LEU A CG  
3765 C CD1 . LEU A 476 ? 1.6909 1.9574 1.2766 0.2792  0.4478  -0.2797 503 LEU A CD1 
3766 C CD2 . LEU A 476 ? 1.5562 1.8276 1.0525 0.2204  0.4615  -0.2866 503 LEU A CD2 
3767 N N   . GLN A 477 ? 1.7679 1.7973 1.2196 0.2687  0.4141  -0.3088 504 GLN A N   
3768 C CA  . GLN A 477 ? 1.9116 1.8795 1.3390 0.2889  0.4256  -0.3359 504 GLN A CA  
3769 C C   . GLN A 477 ? 1.9158 1.8531 1.3776 0.3218  0.4139  -0.3289 504 GLN A C   
3770 O O   . GLN A 477 ? 1.8752 1.7889 1.3465 0.3546  0.4282  -0.3481 504 GLN A O   
3771 C CB  . GLN A 477 ? 1.9573 1.8707 1.3251 0.2593  0.4182  -0.3440 504 GLN A CB  
3772 C CG  . GLN A 477 ? 2.1458 1.9841 1.4839 0.2755  0.4260  -0.3703 504 GLN A CG  
3773 C CD  . GLN A 477 ? 2.2837 2.0690 1.5680 0.2425  0.4133  -0.3737 504 GLN A CD  
3774 O OE1 . GLN A 477 ? 2.2421 2.0496 1.5155 0.2098  0.3973  -0.3548 504 GLN A OE1 
3775 N NE2 . GLN A 477 ? 2.3774 2.0923 1.6292 0.2508  0.4195  -0.3975 504 GLN A NE2 
3776 N N   . GLY A 478 ? 1.8826 1.8192 1.3623 0.3146  0.3878  -0.3013 505 GLY A N   
3777 C CA  . GLY A 478 ? 1.8236 1.7336 1.3326 0.3433  0.3746  -0.2917 505 GLY A CA  
3778 C C   . GLY A 478 ? 1.8069 1.7687 1.3734 0.3733  0.3786  -0.2857 505 GLY A C   
3779 O O   . GLY A 478 ? 1.8101 1.7503 1.3999 0.4066  0.3770  -0.2882 505 GLY A O   
3780 N N   . ALA A 479 ? 1.7093 1.7402 1.3000 0.3611  0.3826  -0.2764 506 ALA A N   
3781 C CA  . ALA A 479 ? 1.6230 1.7106 1.2709 0.3860  0.3872  -0.2710 506 ALA A CA  
3782 C C   . ALA A 479 ? 1.7989 1.8906 1.4579 0.4173  0.4148  -0.2979 506 ALA A C   
3783 O O   . ALA A 479 ? 1.7513 1.8686 1.4588 0.4499  0.4163  -0.2964 506 ALA A O   
3784 C CB  . ALA A 479 ? 1.6188 1.7765 1.2857 0.3613  0.3867  -0.2556 506 ALA A CB  
3785 N N   . ARG A 480 ? 1.8313 1.8987 1.4461 0.4086  0.4365  -0.3231 507 ARG A N   
3786 C CA  . ARG A 480 ? 1.7292 1.7911 1.3486 0.4403  0.4647  -0.3526 507 ARG A CA  
3787 C C   . ARG A 480 ? 1.9177 1.9056 1.5317 0.4719  0.4588  -0.3624 507 ARG A C   
3788 O O   . ARG A 480 ? 1.9839 1.9766 1.6324 0.5123  0.4707  -0.3737 507 ARG A O   
3789 C CB  . ARG A 480 ? 1.7513 1.8059 1.3180 0.4193  0.4895  -0.3782 507 ARG A CB  
3790 C CG  . ARG A 480 ? 1.7670 1.8933 1.3341 0.3889  0.4988  -0.3698 507 ARG A CG  
3791 C CD  . ARG A 480 ? 1.9205 2.0349 1.4307 0.3716  0.5246  -0.3978 507 ARG A CD  
3792 N NE  . ARG A 480 ? 1.9804 2.1643 1.4887 0.3446  0.5371  -0.3909 507 ARG A NE  
3793 C CZ  . ARG A 480 ? 1.9310 2.1188 1.4003 0.3026  0.5261  -0.3781 507 ARG A CZ  
3794 N NH1 . ARG A 480 ? 1.8536 1.9858 1.2861 0.2822  0.5026  -0.3708 507 ARG A NH1 
3795 N NH2 . ARG A 480 ? 1.7532 2.0036 1.2213 0.2804  0.5389  -0.3712 507 ARG A NH2 
3796 N N   . LYS A 481 ? 1.9002 1.8201 1.4726 0.4542  0.4403  -0.3570 508 LYS A N   
3797 C CA  . LYS A 481 ? 1.9477 1.7887 1.5063 0.4791  0.4351  -0.3660 508 LYS A CA  
3798 C C   . LYS A 481 ? 1.9817 1.8321 1.5945 0.5150  0.4199  -0.3479 508 LYS A C   
3799 O O   . LYS A 481 ? 1.9952 1.8072 1.6185 0.5522  0.4259  -0.3602 508 LYS A O   
3800 C CB  . LYS A 481 ? 1.9051 1.6814 1.4131 0.4475  0.4160  -0.3583 508 LYS A CB  
3801 C CG  . LYS A 481 ? 1.8099 1.5599 1.2583 0.4152  0.4289  -0.3796 508 LYS A CG  
3802 C CD  . LYS A 481 ? 1.8974 1.5840 1.3026 0.3865  0.4087  -0.3709 508 LYS A CD  
3803 C CE  . LYS A 481 ? 2.0279 1.6898 1.3739 0.3523  0.4184  -0.3916 508 LYS A CE  
3804 N NZ  . LYS A 481 ? 2.0334 1.6435 1.3430 0.3210  0.3974  -0.3806 508 LYS A NZ  
3805 N N   . LEU A 482 ? 1.8646 1.7635 1.5106 0.5047  0.3992  -0.3187 509 LEU A N   
3806 C CA  . LEU A 482 ? 1.7867 1.6983 1.4817 0.5355  0.3819  -0.3001 509 LEU A CA  
3807 C C   . LEU A 482 ? 1.9071 1.8702 1.6547 0.5735  0.4002  -0.3117 509 LEU A C   
3808 O O   . LEU A 482 ? 1.9934 1.9342 1.7667 0.6126  0.3970  -0.3130 509 LEU A O   
3809 C CB  . LEU A 482 ? 1.6760 1.6308 1.3914 0.5131  0.3571  -0.2694 509 LEU A CB  
3810 C CG  . LEU A 482 ? 1.6662 1.5777 1.3402 0.4806  0.3365  -0.2537 509 LEU A CG  
3811 C CD1 . LEU A 482 ? 1.3917 1.3502 1.0907 0.4644  0.3148  -0.2264 509 LEU A CD1 
3812 C CD2 . LEU A 482 ? 1.7234 1.5558 1.3746 0.4957  0.3245  -0.2515 509 LEU A CD2 
3813 N N   . LEU A 483 ? 1.8406 1.8745 1.6058 0.5626  0.4195  -0.3190 510 LEU A N   
3814 C CA  . LEU A 483 ? 1.7597 1.8542 1.5792 0.5963  0.4394  -0.3295 510 LEU A CA  
3815 C C   . LEU A 483 ? 1.7616 1.8145 1.5665 0.6288  0.4668  -0.3627 510 LEU A C   
3816 O O   . LEU A 483 ? 1.8453 1.9289 1.6992 0.6697  0.4789  -0.3706 510 LEU A O   
3817 C CB  . LEU A 483 ? 1.5937 1.7738 1.4308 0.5711  0.4544  -0.3276 510 LEU A CB  
3818 C CG  . LEU A 483 ? 1.5279 1.7465 1.3770 0.5373  0.4285  -0.2964 510 LEU A CG  
3819 C CD1 . LEU A 483 ? 1.5217 1.8092 1.3737 0.5069  0.4446  -0.2958 510 LEU A CD1 
3820 C CD2 . LEU A 483 ? 1.4344 1.6867 1.3433 0.5599  0.4057  -0.2742 510 LEU A CD2 
3821 N N   . ALA A 484 ? 1.9662 1.9502 1.7058 0.6117  0.4765  -0.3828 511 ALA A N   
3822 C CA  . ALA A 484 ? 2.0464 1.9802 1.7650 0.6413  0.5021  -0.4170 511 ALA A CA  
3823 C C   . ALA A 484 ? 2.1762 2.0476 1.9108 0.6828  0.4886  -0.4144 511 ALA A C   
3824 O O   . ALA A 484 ? 2.1554 2.0131 1.9122 0.7133  0.5030  -0.4341 511 ALA A O   
3825 C CB  . ALA A 484 ? 2.0083 1.8799 1.6490 0.6080  0.5116  -0.4379 511 ALA A CB  
3826 N N   . ALA A 485 ? 2.2294 2.0654 1.9600 0.6733  0.4553  -0.3866 512 ALA A N   
3827 C CA  . ALA A 485 ? 2.2651 2.0450 2.0114 0.7110  0.4393  -0.3786 512 ALA A CA  
3828 C C   . ALA A 485 ? 2.2748 2.1196 2.0979 0.7546  0.4381  -0.3690 512 ALA A C   
3829 O O   . ALA A 485 ? 2.3297 2.1339 2.1718 0.7963  0.4325  -0.3693 512 ALA A O   
3830 C CB  . ALA A 485 ? 2.1852 1.9208 1.9081 0.6870  0.4047  -0.3489 512 ALA A CB  
3831 N N   . GLU A 486 ? 2.1680 2.1124 2.0361 0.7450  0.4421  -0.3594 513 GLU A N   
3832 C CA  . GLU A 486 ? 2.1263 2.1471 2.0723 0.7806  0.4406  -0.3489 513 GLU A CA  
3833 C C   . GLU A 486 ? 2.1605 2.1551 2.1301 0.8008  0.4049  -0.3204 513 GLU A C   
3834 O O   . GLU A 486 ? 2.1615 2.1226 2.1525 0.8459  0.4034  -0.3243 513 GLU A O   
3835 C CB  . GLU A 486 ? 2.1072 2.1389 2.0841 0.8120  0.4684  -0.3762 513 GLU A CB  
3836 C CG  . GLU A 486 ? 2.1214 2.1733 2.0705 0.7849  0.5021  -0.4046 513 GLU A CG  
3837 C CD  . GLU A 486 ? 2.4017 2.4546 2.3775 0.8101  0.5284  -0.4332 513 GLU A CD  
3838 O OE1 . GLU A 486 ? 2.5810 2.6360 2.6096 0.8500  0.5212  -0.4285 513 GLU A OE1 
3839 O OE2 . GLU A 486 ? 2.4938 2.5454 2.4374 0.7900  0.5560  -0.4604 513 GLU A OE2 
3840 N N   . PRO A 487 ? 2.1045 2.1117 2.0690 0.7693  0.3758  -0.2916 514 PRO A N   
3841 C CA  . PRO A 487 ? 2.1205 2.0901 2.0905 0.7817  0.3410  -0.2647 514 PRO A CA  
3842 C C   . PRO A 487 ? 2.1101 2.1489 2.1528 0.8109  0.3233  -0.2444 514 PRO A C   
3843 O O   . PRO A 487 ? 2.1518 2.1609 2.1988 0.8236  0.2936  -0.2217 514 PRO A O   
3844 C CB  . PRO A 487 ? 2.0526 2.0091 1.9800 0.7315  0.3216  -0.2464 514 PRO A CB  
3845 C CG  . PRO A 487 ? 1.9391 1.9733 1.8796 0.7018  0.3369  -0.2516 514 PRO A CG  
3846 C CD  . PRO A 487 ? 2.0204 2.0705 1.9671 0.7193  0.3739  -0.2832 514 PRO A CD  
3847 N N   . LEU A 488 ? 2.1234 2.2549 2.2223 0.8199  0.3397  -0.2508 515 LEU A N   
3848 C CA  . LEU A 488 ? 2.1512 2.3564 2.3224 0.8430  0.3205  -0.2300 515 LEU A CA  
3849 C C   . LEU A 488 ? 2.2073 2.3838 2.4108 0.8990  0.3134  -0.2290 515 LEU A C   
3850 O O   . LEU A 488 ? 2.1396 2.3466 2.3867 0.9172  0.2849  -0.2047 515 LEU A O   
3851 C CB  . LEU A 488 ? 2.1096 2.4225 2.3349 0.8382  0.3424  -0.2378 515 LEU A CB  
3852 C CG  . LEU A 488 ? 1.8704 2.2199 2.0711 0.7836  0.3466  -0.2344 515 LEU A CG  
3853 C CD1 . LEU A 488 ? 1.8757 2.3296 2.1304 0.7806  0.3703  -0.2416 515 LEU A CD1 
3854 C CD2 . LEU A 488 ? 1.8254 2.1738 2.0177 0.7544  0.3084  -0.2042 515 LEU A CD2 
3855 N N   . SER A 489 ? 2.0856 2.2015 2.2673 0.9269  0.3375  -0.2547 516 SER A N   
3856 C CA  . SER A 489 ? 2.0758 2.1552 2.2875 0.9708  0.3284  -0.2526 516 SER A CA  
3857 C C   . SER A 489 ? 2.1660 2.1458 2.3307 0.9780  0.2996  -0.2347 516 SER A C   
3858 O O   . SER A 489 ? 2.2210 2.1742 2.4131 1.0106  0.2821  -0.2231 516 SER A O   
3859 C CB  . SER A 489 ? 2.0866 2.1379 2.2968 0.9820  0.3619  -0.2862 516 SER A CB  
3860 O OG  . SER A 489 ? 2.2247 2.1947 2.3560 0.9557  0.3770  -0.3063 516 SER A OG  
3861 N N   . LYS A 490 ? 2.1557 2.0820 2.2525 0.9379  0.2918  -0.2296 517 LYS A N   
3862 C CA  . LYS A 490 ? 2.2179 2.0465 2.2627 0.9329  0.2671  -0.2129 517 LYS A CA  
3863 C C   . LYS A 490 ? 2.1664 2.0031 2.1771 0.8809  0.2456  -0.1913 517 LYS A C   
3864 O O   . LYS A 490 ? 2.0628 1.8494 2.0133 0.8439  0.2512  -0.1975 517 LYS A O   
3865 C CB  . LYS A 490 ? 2.2126 1.9408 2.1985 0.9349  0.2879  -0.2384 517 LYS A CB  
3866 C CG  . LYS A 490 ? 2.1938 1.9395 2.1548 0.9081  0.3229  -0.2702 517 LYS A CG  
3867 C CD  . LYS A 490 ? 2.2356 1.8830 2.1395 0.9065  0.3412  -0.2967 517 LYS A CD  
3868 C CE  . LYS A 490 ? 2.1958 1.8678 2.0765 0.8781  0.3742  -0.3280 517 LYS A CE  
3869 N NZ  . LYS A 490 ? 2.3189 1.8968 2.1408 0.8669  0.3886  -0.3541 517 LYS A NZ  
3870 N N   . MET A 491 ? 2.2229 2.1243 2.2735 0.8787  0.2200  -0.1657 518 MET A N   
3871 C CA  . MET A 491 ? 2.3360 2.2633 2.3649 0.8317  0.2033  -0.1488 518 MET A CA  
3872 C C   . MET A 491 ? 2.4767 2.3367 2.4612 0.8205  0.1731  -0.1239 518 MET A C   
3873 O O   . MET A 491 ? 2.5602 2.4045 2.5620 0.8496  0.1497  -0.1049 518 MET A O   
3874 C CB  . MET A 491 ? 2.2702 2.3029 2.3618 0.8303  0.1921  -0.1362 518 MET A CB  
3875 C CG  . MET A 491 ? 2.2979 2.3543 2.3685 0.7846  0.1727  -0.1187 518 MET A CG  
3876 S SD  . MET A 491 ? 2.0438 2.2199 2.1835 0.7758  0.1610  -0.1067 518 MET A SD  
3877 C CE  . MET A 491 ? 2.0285 2.2600 2.1868 0.7641  0.2031  -0.1352 518 MET A CE  
3878 N N   . LEU A 492 ? 2.2268 2.0499 2.1543 0.7779  0.1741  -0.1235 519 LEU A N   
3879 C CA  . LEU A 492 ? 1.9973 1.7738 1.8809 0.7558  0.1486  -0.1000 519 LEU A CA  
3880 C C   . LEU A 492 ? 2.0701 1.9079 1.9576 0.7193  0.1386  -0.0898 519 LEU A C   
3881 O O   . LEU A 492 ? 2.0451 1.9536 1.9676 0.7118  0.1513  -0.1004 519 LEU A O   
3882 C CB  . LEU A 492 ? 2.0201 1.7079 1.8376 0.7353  0.1595  -0.1085 519 LEU A CB  
3883 C CG  . LEU A 492 ? 2.1919 1.8014 1.9921 0.7642  0.1706  -0.1211 519 LEU A CG  
3884 C CD1 . LEU A 492 ? 2.0387 1.5821 1.7781 0.7326  0.1873  -0.1365 519 LEU A CD1 
3885 C CD2 . LEU A 492 ? 2.2923 1.8516 2.0885 0.7904  0.1441  -0.0961 519 LEU A CD2 
3886 N N   . PRO A 493 ? 2.1846 1.9982 2.0372 0.6962  0.1170  -0.0697 520 PRO A N   
3887 C CA  . PRO A 493 ? 2.0939 1.9505 1.9385 0.6578  0.1131  -0.0657 520 PRO A CA  
3888 C C   . PRO A 493 ? 2.0574 1.9035 1.8728 0.6284  0.1391  -0.0853 520 PRO A C   
3889 O O   . PRO A 493 ? 2.1726 1.9595 1.9547 0.6287  0.1540  -0.0974 520 PRO A O   
3890 C CB  . PRO A 493 ? 2.0944 1.9111 1.8993 0.6439  0.0881  -0.0427 520 PRO A CB  
3891 C CG  . PRO A 493 ? 2.1893 1.9734 2.0027 0.6796  0.0711  -0.0288 520 PRO A CG  
3892 C CD  . PRO A 493 ? 2.2198 1.9754 2.0453 0.7072  0.0927  -0.0474 520 PRO A CD  
3893 N N   . VAL A 494 ? 2.0012 1.9043 1.8285 0.6020  0.1431  -0.0880 521 VAL A N   
3894 C CA  . VAL A 494 ? 1.9303 1.8340 1.7357 0.5754  0.1669  -0.1058 521 VAL A CA  
3895 C C   . VAL A 494 ? 1.9284 1.7695 1.6753 0.5492  0.1662  -0.1029 521 VAL A C   
3896 O O   . VAL A 494 ? 1.8869 1.7039 1.6067 0.5337  0.1852  -0.1186 521 VAL A O   
3897 C CB  . VAL A 494 ? 1.8187 1.7964 1.6506 0.5531  0.1689  -0.1058 521 VAL A CB  
3898 C CG1 . VAL A 494 ? 1.6862 1.6651 1.4974 0.5254  0.1488  -0.0885 521 VAL A CG1 
3899 C CG2 . VAL A 494 ? 1.7265 1.7161 1.5479 0.5354  0.1964  -0.1260 521 VAL A CG2 
3900 N N   . ASP A 495 ? 1.8460 1.6618 1.5720 0.5429  0.1446  -0.0830 522 ASP A N   
3901 C CA  . ASP A 495 ? 1.8284 1.5886 1.5023 0.5189  0.1442  -0.0784 522 ASP A CA  
3902 C C   . ASP A 495 ? 1.9715 1.6580 1.6172 0.5328  0.1493  -0.0819 522 ASP A C   
3903 O O   . ASP A 495 ? 2.0349 1.6744 1.6382 0.5108  0.1529  -0.0809 522 ASP A O   
3904 C CB  . ASP A 495 ? 1.8714 1.6324 1.5310 0.5071  0.1217  -0.0565 522 ASP A CB  
3905 C CG  . ASP A 495 ? 1.9199 1.6718 1.5924 0.5349  0.1006  -0.0403 522 ASP A CG  
3906 O OD1 . ASP A 495 ? 1.9103 1.6834 1.6210 0.5637  0.1005  -0.0446 522 ASP A OD1 
3907 O OD2 . ASP A 495 ? 2.0015 1.7273 1.6461 0.5284  0.0841  -0.0229 522 ASP A OD2 
3908 N N   . GLU A 496 ? 2.0612 1.7364 1.7308 0.5685  0.1491  -0.0851 523 GLU A N   
3909 C CA  . GLU A 496 ? 2.0459 1.6477 1.6913 0.5843  0.1562  -0.0920 523 GLU A CA  
3910 C C   . GLU A 496 ? 2.0834 1.6838 1.7381 0.5947  0.1821  -0.1203 523 GLU A C   
3911 O O   . GLU A 496 ? 2.1024 1.6365 1.7254 0.5962  0.1924  -0.1317 523 GLU A O   
3912 C CB  . GLU A 496 ? 2.1052 1.6830 1.7663 0.6208  0.1377  -0.0758 523 GLU A CB  
3913 C CG  . GLU A 496 ? 2.1422 1.7078 1.7839 0.6122  0.1118  -0.0474 523 GLU A CG  
3914 C CD  . GLU A 496 ? 2.2942 1.8275 1.9448 0.6476  0.0927  -0.0302 523 GLU A CD  
3915 O OE1 . GLU A 496 ? 2.3268 1.8123 1.9777 0.6728  0.1006  -0.0387 523 GLU A OE1 
3916 O OE2 . GLU A 496 ? 2.3246 1.8788 1.9807 0.6507  0.0691  -0.0083 523 GLU A OE2 
3917 N N   . PHE A 497 ? 2.0882 1.7590 1.7835 0.6006  0.1931  -0.1321 524 PHE A N   
3918 C CA  . PHE A 497 ? 1.9894 1.6647 1.6915 0.6096  0.2201  -0.1603 524 PHE A CA  
3919 C C   . PHE A 497 ? 1.9992 1.6523 1.6567 0.5722  0.2357  -0.1750 524 PHE A C   
3920 O O   . PHE A 497 ? 2.0515 1.6627 1.6860 0.5753  0.2541  -0.1970 524 PHE A O   
3921 C CB  . PHE A 497 ? 1.9331 1.6961 1.6905 0.6222  0.2280  -0.1663 524 PHE A CB  
3922 C CG  . PHE A 497 ? 2.0445 1.8265 1.8041 0.6214  0.2584  -0.1949 524 PHE A CG  
3923 C CD1 . PHE A 497 ? 2.1466 1.8882 1.9036 0.6508  0.2762  -0.2162 524 PHE A CD1 
3924 C CD2 . PHE A 497 ? 1.9716 1.8100 1.7337 0.5918  0.2693  -0.2005 524 PHE A CD2 
3925 C CE1 . PHE A 497 ? 2.0691 1.8280 1.8238 0.6500  0.3056  -0.2443 524 PHE A CE1 
3926 C CE2 . PHE A 497 ? 1.9193 1.7763 1.6792 0.5897  0.2975  -0.2260 524 PHE A CE2 
3927 C CZ  . PHE A 497 ? 1.8348 1.6531 1.5899 0.6186  0.3163  -0.2488 524 PHE A CZ  
3928 N N   . LEU A 498 ? 1.8356 1.5158 1.4801 0.5372  0.2279  -0.1635 525 LEU A N   
3929 C CA  . LEU A 498 ? 1.9013 1.5657 1.5062 0.5011  0.2397  -0.1745 525 LEU A CA  
3930 C C   . LEU A 498 ? 2.0036 1.5845 1.5602 0.4909  0.2383  -0.1757 525 LEU A C   
3931 O O   . LEU A 498 ? 2.0562 1.6059 1.5846 0.4794  0.2547  -0.1965 525 LEU A O   
3932 C CB  . LEU A 498 ? 1.7649 1.4774 1.3712 0.4698  0.2298  -0.1597 525 LEU A CB  
3933 C CG  . LEU A 498 ? 1.5849 1.3759 1.2376 0.4758  0.2267  -0.1542 525 LEU A CG  
3934 C CD1 . LEU A 498 ? 1.4842 1.3094 1.1307 0.4431  0.2179  -0.1416 525 LEU A CD1 
3935 C CD2 . LEU A 498 ? 1.5568 1.3859 1.2329 0.4868  0.2491  -0.1754 525 LEU A CD2 
3936 N N   . PRO A 499 ? 2.0454 1.5867 1.5882 0.4925  0.2198  -0.1547 526 PRO A N   
3937 C CA  . PRO A 499 ? 2.2058 1.6651 1.7033 0.4820  0.2197  -0.1555 526 PRO A CA  
3938 C C   . PRO A 499 ? 2.2275 1.6312 1.7186 0.5089  0.2317  -0.1751 526 PRO A C   
3939 O O   . PRO A 499 ? 2.2678 1.6040 1.7182 0.4948  0.2367  -0.1836 526 PRO A O   
3940 C CB  . PRO A 499 ? 2.1246 1.5627 1.6159 0.4845  0.1974  -0.1265 526 PRO A CB  
3941 C CG  . PRO A 499 ? 2.0962 1.6070 1.6156 0.4787  0.1873  -0.1130 526 PRO A CG  
3942 C CD  . PRO A 499 ? 1.9544 1.5230 1.5153 0.4970  0.1981  -0.1286 526 PRO A CD  
3943 N N   . VAL A 500 ? 2.1169 1.5461 1.6476 0.5473  0.2365  -0.1827 527 VAL A N   
3944 C CA  . VAL A 500 ? 2.2414 1.6230 1.7681 0.5747  0.2524  -0.2064 527 VAL A CA  
3945 C C   . VAL A 500 ? 2.2079 1.5989 1.7163 0.5557  0.2768  -0.2366 527 VAL A C   
3946 O O   . VAL A 500 ? 2.3057 1.6310 1.7780 0.5529  0.2885  -0.2568 527 VAL A O   
3947 C CB  . VAL A 500 ? 2.1839 1.5986 1.7638 0.6231  0.2515  -0.2059 527 VAL A CB  
3948 C CG1 . VAL A 500 ? 2.1347 1.5070 1.7137 0.6540  0.2720  -0.2343 527 VAL A CG1 
3949 C CG2 . VAL A 500 ? 2.2764 1.6695 1.8666 0.6422  0.2252  -0.1759 527 VAL A CG2 
3950 N N   . MET A 501 ? 2.1649 1.6346 1.6938 0.5401  0.2838  -0.2396 528 MET A N   
3951 C CA  . MET A 501 ? 2.1306 1.6166 1.6429 0.5235  0.3069  -0.2670 528 MET A CA  
3952 C C   . MET A 501 ? 2.1684 1.6152 1.6270 0.4794  0.3068  -0.2712 528 MET A C   
3953 O O   . MET A 501 ? 2.2301 1.6597 1.6605 0.4677  0.3246  -0.2972 528 MET A O   
3954 C CB  . MET A 501 ? 2.0403 1.6217 1.5904 0.5190  0.3133  -0.2658 528 MET A CB  
3955 C CG  . MET A 501 ? 1.9936 1.6224 1.6002 0.5610  0.3176  -0.2664 528 MET A CG  
3956 S SD  . MET A 501 ? 2.2763 1.8604 1.8849 0.6039  0.3415  -0.2981 528 MET A SD  
3957 C CE  . MET A 501 ? 2.0928 1.6985 1.6715 0.5784  0.3721  -0.3307 528 MET A CE  
3958 N N   . PHE A 502 ? 2.3140 1.4931 1.6972 0.4009  0.1962  -0.1578 529 PHE A N   
3959 C CA  . PHE A 502 ? 2.4402 1.5926 1.7537 0.3779  0.1953  -0.1529 529 PHE A CA  
3960 C C   . PHE A 502 ? 2.5431 1.6512 1.8190 0.3679  0.1642  -0.1408 529 PHE A C   
3961 O O   . PHE A 502 ? 2.6002 1.6917 1.8288 0.3444  0.1582  -0.1332 529 PHE A O   
3962 C CB  . PHE A 502 ? 2.3195 1.5117 1.6184 0.3548  0.2031  -0.1477 529 PHE A CB  
3963 C CG  . PHE A 502 ? 2.4248 1.6483 1.7382 0.3435  0.1815  -0.1346 529 PHE A CG  
3964 C CD1 . PHE A 502 ? 2.4299 1.6308 1.7020 0.3256  0.1571  -0.1194 529 PHE A CD1 
3965 C CD2 . PHE A 502 ? 2.2529 1.5267 1.6190 0.3507  0.1878  -0.1376 529 PHE A CD2 
3966 C CE1 . PHE A 502 ? 2.3513 1.5756 1.6267 0.3181  0.1392  -0.1075 529 PHE A CE1 
3967 C CE2 . PHE A 502 ? 2.2011 1.5005 1.5752 0.3425  0.1657  -0.1277 529 PHE A CE2 
3968 C CZ  . PHE A 502 ? 2.2889 1.5622 1.6131 0.3273  0.1416  -0.1126 529 PHE A CZ  
3969 N N   . ASP A 503 ? 2.4970 1.5846 1.7966 0.3860  0.1450  -0.1390 530 ASP A N   
3970 C CA  . ASP A 503 ? 2.5579 1.5896 1.8222 0.3840  0.1210  -0.1302 530 ASP A CA  
3971 C C   . ASP A 503 ? 2.5907 1.6135 1.8130 0.3586  0.1018  -0.1100 530 ASP A C   
3972 O O   . ASP A 503 ? 2.6326 1.6151 1.8118 0.3424  0.0964  -0.1023 530 ASP A O   
3973 C CB  . ASP A 503 ? 2.6571 1.6454 1.8900 0.3850  0.1327  -0.1407 530 ASP A CB  
3974 C CG  . ASP A 503 ? 2.6775 1.6125 1.9072 0.4010  0.1147  -0.1410 530 ASP A CG  
3975 O OD1 . ASP A 503 ? 2.7053 1.6384 1.9609 0.4145  0.0947  -0.1345 530 ASP A OD1 
3976 O OD2 . ASP A 503 ? 2.6678 1.5605 1.8684 0.4014  0.1182  -0.1489 530 ASP A OD2 
3977 N N   . LYS A 504 ? 2.5432 1.6022 1.7802 0.3561  0.0924  -0.1015 531 LYS A N   
3978 C CA  . LYS A 504 ? 2.4554 1.5031 1.6512 0.3371  0.0757  -0.0810 531 LYS A CA  
3979 C C   . LYS A 504 ? 2.4396 1.4797 1.6431 0.3544  0.0467  -0.0717 531 LYS A C   
3980 O O   . LYS A 504 ? 2.5535 1.5811 1.7173 0.3433  0.0335  -0.0538 531 LYS A O   
3981 C CB  . LYS A 504 ? 2.3826 1.4758 1.5702 0.3146  0.0903  -0.0780 531 LYS A CB  
3982 C CG  . LYS A 504 ? 2.3697 1.4587 1.5325 0.2925  0.1106  -0.0825 531 LYS A CG  
3983 C CD  . LYS A 504 ? 2.4242 1.4616 1.5429 0.2744  0.1019  -0.0688 531 LYS A CD  
3984 C CE  . LYS A 504 ? 2.3578 1.3939 1.4593 0.2518  0.1169  -0.0753 531 LYS A CE  
3985 N NZ  . LYS A 504 ? 2.3100 1.2978 1.3808 0.2322  0.1092  -0.0623 531 LYS A NZ  
3986 N N   . HIS A 505 ? 2.3852 1.4296 1.6373 0.3827  0.0365  -0.0840 532 HIS A N   
3987 C CA  . HIS A 505 ? 2.5098 1.5411 1.7704 0.4032  0.0027  -0.0782 532 HIS A CA  
3988 C C   . HIS A 505 ? 2.5829 1.5448 1.7896 0.4042  -0.0171 -0.0622 532 HIS A C   
3989 O O   . HIS A 505 ? 2.4591 1.3865 1.6675 0.4104  -0.0131 -0.0675 532 HIS A O   
3990 C CB  . HIS A 505 ? 2.4417 1.4956 1.7798 0.4334  -0.0029 -0.0981 532 HIS A CB  
3991 C CG  . HIS A 505 ? 2.4156 1.4811 1.7821 0.4538  -0.0376 -0.0988 532 HIS A CG  
3992 N ND1 . HIS A 505 ? 2.4621 1.4796 1.7838 0.4639  -0.0738 -0.0848 532 HIS A ND1 
3993 C CD2 . HIS A 505 ? 2.2818 1.3981 1.7174 0.4676  -0.0434 -0.1127 532 HIS A CD2 
3994 C CE1 . HIS A 505 ? 2.3585 1.3955 1.7160 0.4846  -0.1037 -0.0916 532 HIS A CE1 
3995 N NE2 . HIS A 505 ? 2.2879 1.3866 1.7196 0.4864  -0.0867 -0.1092 532 HIS A NE2 
3996 N N   . PRO A 506 ? 2.6738 1.6097 1.8293 0.3996  -0.0370 -0.0420 533 PRO A N   
3997 C CA  . PRO A 506 ? 2.7480 1.6123 1.8469 0.3989  -0.0508 -0.0234 533 PRO A CA  
3998 C C   . PRO A 506 ? 2.7715 1.5978 1.8896 0.4303  -0.0781 -0.0293 533 PRO A C   
3999 O O   . PRO A 506 ? 2.8047 1.5692 1.8828 0.4308  -0.0864 -0.0165 533 PRO A O   
4000 C CB  . PRO A 506 ? 2.8952 1.7452 1.9360 0.3913  -0.0626 -0.0010 533 PRO A CB  
4001 C CG  . PRO A 506 ? 2.7686 1.6759 1.8469 0.4030  -0.0725 -0.0130 533 PRO A CG  
4002 C CD  . PRO A 506 ? 2.6375 1.6042 1.7808 0.3960  -0.0461 -0.0350 533 PRO A CD  
4003 N N   . VAL A 507 ? 2.6936 1.5540 1.8760 0.4563  -0.0920 -0.0484 534 VAL A N   
4004 C CA  . VAL A 507 ? 2.6489 1.4778 1.8606 0.4881  -0.1194 -0.0570 534 VAL A CA  
4005 C C   . VAL A 507 ? 2.6554 1.4883 1.9124 0.4920  -0.0964 -0.0748 534 VAL A C   
4006 O O   . VAL A 507 ? 2.6715 1.5566 1.9912 0.4961  -0.0755 -0.0940 534 VAL A O   
4007 C CB  . VAL A 507 ? 2.5792 1.4417 1.8466 0.5157  -0.1485 -0.0705 534 VAL A CB  
4008 C CG1 . VAL A 507 ? 2.6663 1.4946 1.9681 0.5496  -0.1797 -0.0804 534 VAL A CG1 
4009 C CG2 . VAL A 507 ? 2.5263 1.3824 1.7403 0.5136  -0.1716 -0.0545 534 VAL A CG2 
4010 N N   . SER A 508 ? 2.6452 1.4195 1.8680 0.4917  -0.0986 -0.0680 535 SER A N   
4011 C CA  . SER A 508 ? 2.6092 1.3773 1.8677 0.5001  -0.0808 -0.0856 535 SER A CA  
4012 C C   . SER A 508 ? 2.6884 1.4646 2.0177 0.5359  -0.0973 -0.1044 535 SER A C   
4013 O O   . SER A 508 ? 2.6327 1.4160 2.0043 0.5466  -0.0770 -0.1224 535 SER A O   
4014 C CB  . SER A 508 ? 2.5721 1.2727 1.7758 0.4897  -0.0817 -0.0739 535 SER A CB  
4015 O OG  . SER A 508 ? 2.6288 1.3283 1.7864 0.4558  -0.0599 -0.0625 535 SER A OG  
4016 N N   . GLU A 509 ? 2.8121 1.5850 2.1551 0.5562  -0.1339 -0.1016 536 GLU A N   
4017 C CA  . GLU A 509 ? 2.8300 1.6185 2.2548 0.5905  -0.1518 -0.1221 536 GLU A CA  
4018 C C   . GLU A 509 ? 2.8187 1.6823 2.3273 0.5931  -0.1259 -0.1422 536 GLU A C   
4019 O O   . GLU A 509 ? 2.7903 1.6726 2.3762 0.6143  -0.1154 -0.1625 536 GLU A O   
4020 C CB  . GLU A 509 ? 2.8532 1.6160 2.2682 0.6125  -0.2031 -0.1152 536 GLU A CB  
4021 C CG  . GLU A 509 ? 2.9970 1.6779 2.3405 0.6191  -0.2300 -0.0972 536 GLU A CG  
4022 C CD  . GLU A 509 ? 3.2004 1.8517 2.5863 0.6436  -0.2374 -0.1116 536 GLU A CD  
4023 O OE1 . GLU A 509 ? 3.1346 1.8286 2.6127 0.6629  -0.2315 -0.1362 536 GLU A OE1 
4024 O OE2 . GLU A 509 ? 3.1883 1.7731 2.5182 0.6437  -0.2474 -0.0982 536 GLU A OE2 
4025 N N   . TYR A 510 ? 2.7742 1.6802 2.2703 0.5723  -0.1131 -0.1365 537 TYR A N   
4026 C CA  . TYR A 510 ? 2.6802 1.6555 2.2527 0.5727  -0.0859 -0.1534 537 TYR A CA  
4027 C C   . TYR A 510 ? 2.6451 1.6326 2.2189 0.5596  -0.0356 -0.1606 537 TYR A C   
4028 O O   . TYR A 510 ? 2.5928 1.6112 2.2397 0.5743  -0.0098 -0.1786 537 TYR A O   
4029 C CB  . TYR A 510 ? 2.5458 1.5593 2.1017 0.5558  -0.0914 -0.1451 537 TYR A CB  
4030 C CG  . TYR A 510 ? 2.6042 1.6081 2.1588 0.5727  -0.1418 -0.1413 537 TYR A CG  
4031 C CD1 . TYR A 510 ? 2.6749 1.6536 2.2704 0.6049  -0.1790 -0.1509 537 TYR A CD1 
4032 C CD2 . TYR A 510 ? 2.6837 1.7010 2.1939 0.5584  -0.1539 -0.1291 537 TYR A CD2 
4033 C CE1 . TYR A 510 ? 2.7017 1.6658 2.2897 0.6238  -0.2297 -0.1491 537 TYR A CE1 
4034 C CE2 . TYR A 510 ? 2.6940 1.6962 2.1933 0.5772  -0.2018 -0.1267 537 TYR A CE2 
4035 C CZ  . TYR A 510 ? 2.7001 1.6743 2.2366 0.6104  -0.2410 -0.1370 537 TYR A CZ  
4036 O OH  . TYR A 510 ? 2.7740 1.7276 2.2940 0.6324  -0.2931 -0.1362 537 TYR A OH  
4037 N N   . LYS A 511 ? 2.6292 1.5901 2.1229 0.5334  -0.0209 -0.1469 538 LYS A N   
4038 C CA  . LYS A 511 ? 2.5682 1.5337 2.0520 0.5226  0.0215  -0.1548 538 LYS A CA  
4039 C C   . LYS A 511 ? 2.6427 1.5769 2.1522 0.5455  0.0313  -0.1690 538 LYS A C   
4040 O O   . LYS A 511 ? 2.6360 1.5823 2.1625 0.5493  0.0686  -0.1822 538 LYS A O   
4041 C CB  . LYS A 511 ? 2.4971 1.4339 1.8945 0.4917  0.0269  -0.1391 538 LYS A CB  
4042 C CG  . LYS A 511 ? 2.4135 1.3777 1.7799 0.4678  0.0211  -0.1243 538 LYS A CG  
4043 C CD  . LYS A 511 ? 2.4839 1.4195 1.7771 0.4378  0.0299  -0.1109 538 LYS A CD  
4044 C CE  . LYS A 511 ? 2.5126 1.3796 1.7624 0.4388  0.0095  -0.0999 538 LYS A CE  
4045 N NZ  . LYS A 511 ? 2.4750 1.3132 1.6674 0.4097  0.0198  -0.0894 538 LYS A NZ  
4046 N N   . ALA A 512 ? 2.6580 1.5486 2.1666 0.5627  -0.0012 -0.1666 539 ALA A N   
4047 C CA  . ALA A 512 ? 2.6111 1.4697 2.1447 0.5858  0.0057  -0.1805 539 ALA A CA  
4048 C C   . ALA A 512 ? 2.6943 1.5954 2.3257 0.6121  0.0268  -0.2016 539 ALA A C   
4049 O O   . ALA A 512 ? 2.6188 1.5012 2.2742 0.6309  0.0462  -0.2155 539 ALA A O   
4050 C CB  . ALA A 512 ? 2.5659 1.3684 2.0791 0.5992  -0.0369 -0.1724 539 ALA A CB  
4051 N N   . HIS A 513 ? 2.7337 1.6902 2.4245 0.6141  0.0248  -0.2046 540 HIS A N   
4052 C CA  . HIS A 513 ? 2.6432 1.6436 2.4391 0.6373  0.0476  -0.2240 540 HIS A CA  
4053 C C   . HIS A 513 ? 2.5716 1.6041 2.3775 0.6296  0.1050  -0.2311 540 HIS A C   
4054 O O   . HIS A 513 ? 2.5159 1.5763 2.4045 0.6495  0.1354  -0.2464 540 HIS A O   
4055 C CB  . HIS A 513 ? 2.5983 1.6430 2.4630 0.6443  0.0178  -0.2263 540 HIS A CB  
4056 C CG  . HIS A 513 ? 2.6563 1.6716 2.5395 0.6656  -0.0369 -0.2270 540 HIS A CG  
4057 N ND1 . HIS A 513 ? 2.7412 1.7240 2.5520 0.6566  -0.0819 -0.2097 540 HIS A ND1 
4058 C CD2 . HIS A 513 ? 2.6031 1.6139 2.5677 0.6971  -0.0538 -0.2430 540 HIS A CD2 
4059 C CE1 . HIS A 513 ? 2.7155 1.6717 2.5557 0.6828  -0.1260 -0.2148 540 HIS A CE1 
4060 N NE2 . HIS A 513 ? 2.6370 1.6113 2.5737 0.7073  -0.1119 -0.2358 540 HIS A NE2 
4061 N N   . PHE A 514 ? 2.4549 1.4817 2.1804 0.6026  0.1214  -0.2205 541 PHE A N   
4062 C CA  . PHE A 514 ? 2.3885 1.4416 2.1108 0.5953  0.1722  -0.2258 541 PHE A CA  
4063 C C   . PHE A 514 ? 2.4813 1.4842 2.1197 0.5891  0.1904  -0.2261 541 PHE A C   
4064 O O   . PHE A 514 ? 2.5167 1.4930 2.0772 0.5660  0.1713  -0.2142 541 PHE A O   
4065 C CB  . PHE A 514 ? 2.3589 1.4561 2.0684 0.5701  0.1725  -0.2157 541 PHE A CB  
4066 C CG  . PHE A 514 ? 2.3110 1.4557 2.1018 0.5770  0.1511  -0.2174 541 PHE A CG  
4067 C CD1 . PHE A 514 ? 2.3056 1.4405 2.0850 0.5747  0.0993  -0.2085 541 PHE A CD1 
4068 C CD2 . PHE A 514 ? 2.2889 1.4843 2.1674 0.5873  0.1825  -0.2285 541 PHE A CD2 
4069 C CE1 . PHE A 514 ? 2.2937 1.4679 2.1448 0.5839  0.0744  -0.2129 541 PHE A CE1 
4070 C CE2 . PHE A 514 ? 2.1730 1.4115 2.1337 0.5941  0.1591  -0.2327 541 PHE A CE2 
4071 C CZ  . PHE A 514 ? 2.2124 1.4402 2.1583 0.5931  0.1025  -0.2261 541 PHE A CZ  
4072 N N   . SER A 515 ? 2.6979 1.6868 2.3542 0.6107  0.2280  -0.2406 542 SER A N   
4073 C CA  . SER A 515 ? 2.6648 1.5960 2.2466 0.6131  0.2377  -0.2453 542 SER A CA  
4074 C C   . SER A 515 ? 2.5873 1.5137 2.0912 0.5907  0.2561  -0.2416 542 SER A C   
4075 O O   . SER A 515 ? 2.5942 1.4732 2.0244 0.5809  0.2436  -0.2408 542 SER A O   
4076 C CB  . SER A 515 ? 2.5198 1.4346 2.1403 0.6465  0.2739  -0.2628 542 SER A CB  
4077 O OG  . SER A 515 ? 2.5364 1.4874 2.1906 0.6542  0.3245  -0.2689 542 SER A OG  
4078 N N   . LEU A 516 ? 2.3960 1.3688 1.9178 0.5831  0.2842  -0.2403 543 LEU A N   
4079 C CA  . LEU A 516 ? 2.4039 1.3731 1.8552 0.5649  0.3023  -0.2385 543 LEU A CA  
4080 C C   . LEU A 516 ? 2.4395 1.4566 1.8955 0.5369  0.2875  -0.2249 543 LEU A C   
4081 O O   . LEU A 516 ? 2.4148 1.4822 1.9277 0.5390  0.3064  -0.2244 543 LEU A O   
4082 C CB  . LEU A 516 ? 2.2696 1.2399 1.7231 0.5853  0.3567  -0.2505 543 LEU A CB  
4083 C CG  . LEU A 516 ? 2.3420 1.2948 1.7110 0.5726  0.3730  -0.2518 543 LEU A CG  
4084 C CD1 . LEU A 516 ? 2.4128 1.3075 1.7019 0.5635  0.3427  -0.2546 543 LEU A CD1 
4085 C CD2 . LEU A 516 ? 2.1893 1.1330 1.5519 0.5983  0.4287  -0.2628 543 LEU A CD2 
4086 N N   . ARG A 517 ? 2.5004 1.5005 1.8991 0.5110  0.2553  -0.2140 544 ARG A N   
4087 C CA  . ARG A 517 ? 2.3386 1.3774 1.7310 0.4837  0.2403  -0.2005 544 ARG A CA  
4088 C C   . ARG A 517 ? 2.3939 1.4244 1.7186 0.4636  0.2523  -0.2005 544 ARG A C   
4089 O O   . ARG A 517 ? 2.4396 1.4526 1.7165 0.4399  0.2285  -0.1918 544 ARG A O   
4090 C CB  . ARG A 517 ? 2.3012 1.3266 1.6855 0.4712  0.1954  -0.1864 544 ARG A CB  
4091 C CG  . ARG A 517 ? 2.4025 1.4188 1.8416 0.4956  0.1774  -0.1892 544 ARG A CG  
4092 C CD  . ARG A 517 ? 2.5235 1.5244 1.9487 0.4862  0.1332  -0.1737 544 ARG A CD  
4093 N NE  . ARG A 517 ? 2.6760 1.6220 2.0322 0.4717  0.1164  -0.1650 544 ARG A NE  
4094 C CZ  . ARG A 517 ? 2.7317 1.6268 2.0782 0.4853  0.1016  -0.1672 544 ARG A CZ  
4095 N NH1 . ARG A 517 ? 2.7096 1.6010 2.1087 0.5148  0.1011  -0.1786 544 ARG A NH1 
4096 N NH2 . ARG A 517 ? 2.8247 1.6714 2.1121 0.4689  0.0872  -0.1583 544 ARG A NH2 
4097 N N   . ASN A 518 ? 2.3994 1.4412 1.7226 0.4743  0.2907  -0.2105 545 ASN A N   
4098 C CA  . ASN A 518 ? 2.4529 1.4776 1.7090 0.4637  0.3036  -0.2152 545 ASN A CA  
4099 C C   . ASN A 518 ? 2.4017 1.4759 1.6620 0.4459  0.3156  -0.2089 545 ASN A C   
4100 O O   . ASN A 518 ? 2.2888 1.3544 1.5024 0.4431  0.3332  -0.2148 545 ASN A O   
4101 C CB  . ASN A 518 ? 2.4538 1.4424 1.6860 0.4921  0.3383  -0.2313 545 ASN A CB  
4102 C CG  . ASN A 518 ? 2.4298 1.4527 1.7183 0.5134  0.3816  -0.2345 545 ASN A CG  
4103 O OD1 . ASN A 518 ? 2.2910 1.3607 1.6538 0.5122  0.3801  -0.2277 545 ASN A OD1 
4104 N ND2 . ASN A 518 ? 2.3611 1.3579 1.6147 0.5342  0.4206  -0.2453 545 ASN A ND2 
4105 N N   . LEU A 519 ? 2.3519 1.4746 1.6647 0.4358  0.3045  -0.1982 546 LEU A N   
4106 C CA  . LEU A 519 ? 2.1529 1.3241 1.4758 0.4207  0.3163  -0.1931 546 LEU A CA  
4107 C C   . LEU A 519 ? 2.1714 1.3374 1.4349 0.3913  0.2963  -0.1867 546 LEU A C   
4108 O O   . LEU A 519 ? 2.3270 1.4721 1.5680 0.3763  0.2653  -0.1793 546 LEU A O   
4109 C CB  . LEU A 519 ? 2.0712 1.2922 1.4667 0.4194  0.3049  -0.1856 546 LEU A CB  
4110 C CG  . LEU A 519 ? 2.0734 1.3480 1.5044 0.4141  0.3268  -0.1843 546 LEU A CG  
4111 C CD1 . LEU A 519 ? 1.9902 1.2670 1.4508 0.4377  0.3738  -0.1943 546 LEU A CD1 
4112 C CD2 . LEU A 519 ? 1.8967 1.2151 1.3923 0.4105  0.3036  -0.1780 546 LEU A CD2 
4113 N N   . HIS A 520 ? 2.2272 1.4107 1.4674 0.3836  0.3157  -0.1894 547 HIS A N   
4114 C CA  . HIS A 520 ? 2.3062 1.4908 1.4990 0.3565  0.2998  -0.1854 547 HIS A CA  
4115 C C   . HIS A 520 ? 2.2402 1.4831 1.4661 0.3398  0.2985  -0.1752 547 HIS A C   
4116 O O   . HIS A 520 ? 2.2342 1.5061 1.4726 0.3438  0.3237  -0.1781 547 HIS A O   
4117 C CB  . HIS A 520 ? 2.2091 1.3648 1.3459 0.3624  0.3177  -0.1981 547 HIS A CB  
4118 C CG  . HIS A 520 ? 2.3427 1.4392 1.4456 0.3842  0.3214  -0.2108 547 HIS A CG  
4119 N ND1 . HIS A 520 ? 2.3686 1.4403 1.4464 0.4108  0.3539  -0.2232 547 HIS A ND1 
4120 C CD2 . HIS A 520 ? 2.2431 1.2972 1.3308 0.3845  0.2975  -0.2129 547 HIS A CD2 
4121 C CE1 . HIS A 520 ? 2.4659 1.4828 1.5128 0.4274  0.3486  -0.2338 547 HIS A CE1 
4122 N NE2 . HIS A 520 ? 2.4528 1.4592 1.5078 0.4112  0.3135  -0.2281 547 HIS A NE2 
4123 N N   . ALA A 521 ? 2.1167 1.3731 1.3535 0.3226  0.2701  -0.1629 548 ALA A N   
4124 C CA  . ALA A 521 ? 2.0111 1.3191 1.2798 0.3100  0.2646  -0.1537 548 ALA A CA  
4125 C C   . ALA A 521 ? 2.0578 1.3722 1.2882 0.2807  0.2490  -0.1453 548 ALA A C   
4126 O O   . ALA A 521 ? 2.0366 1.3161 1.2309 0.2682  0.2323  -0.1415 548 ALA A O   
4127 C CB  . ALA A 521 ? 1.9729 1.2914 1.2863 0.3186  0.2443  -0.1466 548 ALA A CB  
4128 N N   . PHE A 522 ? 1.9930 1.3527 1.2371 0.2699  0.2556  -0.1426 549 PHE A N   
4129 C CA  . PHE A 522 ? 1.8255 1.1988 1.0407 0.2431  0.2458  -0.1359 549 PHE A CA  
4130 C C   . PHE A 522 ? 1.8197 1.2395 1.0652 0.2359  0.2381  -0.1268 549 PHE A C   
4131 O O   . PHE A 522 ? 1.8574 1.2959 1.1464 0.2515  0.2361  -0.1266 549 PHE A O   
4132 C CB  . PHE A 522 ? 1.7594 1.1351 0.9477 0.2378  0.2631  -0.1461 549 PHE A CB  
4133 C CG  . PHE A 522 ? 1.9452 1.2712 1.0977 0.2485  0.2682  -0.1578 549 PHE A CG  
4134 C CD1 . PHE A 522 ? 2.0821 1.3938 1.2391 0.2748  0.2915  -0.1681 549 PHE A CD1 
4135 C CD2 . PHE A 522 ? 1.9696 1.2606 1.0855 0.2334  0.2502  -0.1592 549 PHE A CD2 
4136 C CE1 . PHE A 522 ? 2.1550 1.4160 1.2714 0.2877  0.2953  -0.1801 549 PHE A CE1 
4137 C CE2 . PHE A 522 ? 2.0435 1.2858 1.1258 0.2450  0.2506  -0.1725 549 PHE A CE2 
4138 C CZ  . PHE A 522 ? 2.1567 1.3828 1.2348 0.2731  0.2724  -0.1832 549 PHE A CZ  
4139 N N   . SER A 523 ? 1.7277 1.1653 0.9522 0.2130  0.2326  -0.1206 550 SER A N   
4140 C CA  . SER A 523 ? 1.6479 1.1274 0.8930 0.2061  0.2252  -0.1131 550 SER A CA  
4141 C C   . SER A 523 ? 1.7275 1.2284 0.9503 0.1830  0.2294  -0.1115 550 SER A C   
4142 O O   . SER A 523 ? 1.7906 1.2680 0.9805 0.1680  0.2282  -0.1116 550 SER A O   
4143 C CB  . SER A 523 ? 1.6907 1.1556 0.9305 0.2062  0.2011  -0.1001 550 SER A CB  
4144 O OG  . SER A 523 ? 1.8390 1.3384 1.0852 0.1988  0.1925  -0.0934 550 SER A OG  
4145 N N   . VAL A 524 ? 1.6790 1.2251 0.9252 0.1807  0.2328  -0.1114 551 VAL A N   
4146 C CA  . VAL A 524 ? 1.7034 1.2738 0.9329 0.1594  0.2351  -0.1095 551 VAL A CA  
4147 C C   . VAL A 524 ? 1.7221 1.2816 0.9264 0.1430  0.2192  -0.0955 551 VAL A C   
4148 O O   . VAL A 524 ? 1.7120 1.2634 0.9182 0.1507  0.2051  -0.0864 551 VAL A O   
4149 C CB  . VAL A 524 ? 1.7399 1.3599 1.0033 0.1630  0.2425  -0.1132 551 VAL A CB  
4150 C CG1 . VAL A 524 ? 1.7218 1.3653 0.9685 0.1433  0.2483  -0.1145 551 VAL A CG1 
4151 C CG2 . VAL A 524 ? 1.6471 1.2735 0.9443 0.1835  0.2612  -0.1236 551 VAL A CG2 
4152 N N   . GLU A 525 ? 1.8121 1.3683 0.9926 0.1214  0.2219  -0.0938 552 GLU A N   
4153 C CA  . GLU A 525 ? 1.6695 1.2139 0.8276 0.1039  0.2142  -0.0793 552 GLU A CA  
4154 C C   . GLU A 525 ? 1.6164 1.1960 0.7741 0.0850  0.2208  -0.0794 552 GLU A C   
4155 O O   . GLU A 525 ? 1.6645 1.2474 0.8214 0.0733  0.2273  -0.0888 552 GLU A O   
4156 C CB  . GLU A 525 ? 1.7233 1.2201 0.8610 0.0946  0.2115  -0.0760 552 GLU A CB  
4157 C CG  . GLU A 525 ? 1.9052 1.3820 1.0222 0.0790  0.2080  -0.0578 552 GLU A CG  
4158 C CD  . GLU A 525 ? 2.0032 1.4741 1.1097 0.0932  0.1983  -0.0442 552 GLU A CD  
4159 O OE1 . GLU A 525 ? 1.9478 1.4062 1.0631 0.1147  0.1891  -0.0477 552 GLU A OE1 
4160 O OE2 . GLU A 525 ? 1.9109 1.3876 0.9995 0.0845  0.1993  -0.0309 552 GLU A OE2 
4161 N N   . PRO A 526 ? 1.5902 1.1946 0.7474 0.0833  0.2175  -0.0707 553 PRO A N   
4162 C CA  . PRO A 526 ? 1.6595 1.2594 0.8140 0.0994  0.2048  -0.0618 553 PRO A CA  
4163 C C   . PRO A 526 ? 1.6062 1.2299 0.7971 0.1215  0.2008  -0.0732 553 PRO A C   
4164 O O   . PRO A 526 ? 1.5328 1.1744 0.7471 0.1244  0.2125  -0.0857 553 PRO A O   
4165 C CB  . PRO A 526 ? 1.5343 1.1545 0.6723 0.0885  0.2048  -0.0523 553 PRO A CB  
4166 C CG  . PRO A 526 ? 1.4360 1.0938 0.5902 0.0736  0.2174  -0.0626 553 PRO A CG  
4167 C CD  . PRO A 526 ? 1.4544 1.0918 0.6111 0.0656  0.2246  -0.0705 553 PRO A CD  
4168 N N   . LEU A 527 ? 1.6493 1.2708 0.8463 0.1385  0.1844  -0.0691 554 LEU A N   
4169 C CA  . LEU A 527 ? 1.5618 1.2069 0.8059 0.1595  0.1794  -0.0806 554 LEU A CA  
4170 C C   . LEU A 527 ? 1.5187 1.2138 0.7899 0.1561  0.1848  -0.0883 554 LEU A C   
4171 O O   . LEU A 527 ? 1.5888 1.2991 0.8386 0.1440  0.1823  -0.0831 554 LEU A O   
4172 C CB  . LEU A 527 ? 1.4476 1.0744 0.6940 0.1798  0.1543  -0.0762 554 LEU A CB  
4173 C CG  . LEU A 527 ? 1.6693 1.2445 0.8924 0.1868  0.1466  -0.0687 554 LEU A CG  
4174 C CD1 . LEU A 527 ? 1.6187 1.1721 0.8298 0.2059  0.1180  -0.0623 554 LEU A CD1 
4175 C CD2 . LEU A 527 ? 1.4925 1.0621 0.7518 0.1977  0.1574  -0.0801 554 LEU A CD2 
4176 N N   . LEU A 528 ? 1.4601 1.1791 0.7799 0.1675  0.1944  -0.1005 555 LEU A N   
4177 C CA  . LEU A 528 ? 1.3995 1.1645 0.7537 0.1667  0.1998  -0.1083 555 LEU A CA  
4178 C C   . LEU A 528 ? 1.4691 1.2540 0.8700 0.1856  0.1803  -0.1138 555 LEU A C   
4179 O O   . LEU A 528 ? 1.4178 1.2403 0.8493 0.1853  0.1797  -0.1202 555 LEU A O   
4180 C CB  . LEU A 528 ? 1.3885 1.1662 0.7675 0.1670  0.2267  -0.1175 555 LEU A CB  
4181 C CG  . LEU A 528 ? 1.5188 1.2727 0.8548 0.1530  0.2423  -0.1165 555 LEU A CG  
4182 C CD1 . LEU A 528 ? 1.3423 1.1077 0.6941 0.1568  0.2673  -0.1258 555 LEU A CD1 
4183 C CD2 . LEU A 528 ? 1.4886 1.2455 0.7844 0.1307  0.2363  -0.1098 555 LEU A CD2 
4184 N N   . ILE A 529 ? 1.4497 1.2094 0.8592 0.2026  0.1617  -0.1129 556 ILE A N   
4185 C CA  . ILE A 529 ? 1.5173 1.2924 0.9774 0.2233  0.1376  -0.1210 556 ILE A CA  
4186 C C   . ILE A 529 ? 1.5998 1.3371 1.0222 0.2349  0.1060  -0.1135 556 ILE A C   
4187 O O   . ILE A 529 ? 1.6448 1.3420 1.0317 0.2345  0.1074  -0.1050 556 ILE A O   
4188 C CB  . ILE A 529 ? 1.4824 1.2695 1.0180 0.2393  0.1502  -0.1327 556 ILE A CB  
4189 C CG1 . ILE A 529 ? 1.4259 1.2523 1.0017 0.2318  0.1786  -0.1398 556 ILE A CG1 
4190 C CG2 . ILE A 529 ? 1.3505 1.1423 0.9421 0.2630  0.1192  -0.1417 556 ILE A CG2 
4191 C CD1 . ILE A 529 ? 1.4570 1.2909 1.1004 0.2457  0.2022  -0.1483 556 ILE A CD1 
4192 N N   . TYR A 530 ? 1.4746 1.2211 0.9014 0.2465  0.0767  -0.1169 557 TYR A N   
4193 C CA  . TYR A 530 ? 1.5210 1.2297 0.9092 0.2631  0.0421  -0.1113 557 TYR A CA  
4194 C C   . TYR A 530 ? 1.6199 1.3464 1.0717 0.2887  0.0088  -0.1277 557 TYR A C   
4195 O O   . TYR A 530 ? 1.6206 1.3921 1.1408 0.2891  0.0143  -0.1413 557 TYR A O   
4196 C CB  . TYR A 530 ? 1.5998 1.2920 0.9067 0.2523  0.0371  -0.0976 557 TYR A CB  
4197 C CG  . TYR A 530 ? 1.5507 1.2277 0.8050 0.2258  0.0686  -0.0826 557 TYR A CG  
4198 C CD1 . TYR A 530 ? 1.5536 1.1799 0.7548 0.2233  0.0700  -0.0675 557 TYR A CD1 
4199 C CD2 . TYR A 530 ? 1.6451 1.3572 0.9067 0.2038  0.0951  -0.0844 557 TYR A CD2 
4200 C CE1 . TYR A 530 ? 1.6352 1.2481 0.7989 0.1987  0.0970  -0.0555 557 TYR A CE1 
4201 C CE2 . TYR A 530 ? 1.7031 1.4019 0.9249 0.1805  0.1198  -0.0735 557 TYR A CE2 
4202 C CZ  . TYR A 530 ? 1.7358 1.3858 0.9120 0.1776  0.1206  -0.0595 557 TYR A CZ  
4203 O OH  . TYR A 530 ? 1.6741 1.3115 0.8211 0.1539  0.1434  -0.0504 557 TYR A OH  
4204 N N   . PRO A 531 ? 1.7276 1.4179 1.1621 0.3113  -0.0274 -0.1276 558 PRO A N   
4205 C CA  . PRO A 531 ? 1.7447 1.4498 1.2428 0.3377  -0.0663 -0.1461 558 PRO A CA  
4206 C C   . PRO A 531 ? 1.7941 1.5176 1.2749 0.3403  -0.0878 -0.1517 558 PRO A C   
4207 O O   . PRO A 531 ? 1.7627 1.4747 1.1644 0.3267  -0.0789 -0.1384 558 PRO A O   
4208 C CB  . PRO A 531 ? 1.8061 1.4571 1.2704 0.3613  -0.1011 -0.1425 558 PRO A CB  
4209 C CG  . PRO A 531 ? 1.8579 1.4742 1.2688 0.3461  -0.0720 -0.1243 558 PRO A CG  
4210 C CD  . PRO A 531 ? 1.8167 1.4490 1.1827 0.3156  -0.0350 -0.1123 558 PRO A CD  
4211 N N   . THR A 532 ? 1.6866 1.4386 1.2476 0.3591  -0.1166 -0.1727 559 THR A N   
4212 C CA  . THR A 532 ? 1.6382 1.4060 1.1898 0.3660  -0.1437 -0.1820 559 THR A CA  
4213 C C   . THR A 532 ? 1.8643 1.5778 1.3188 0.3855  -0.1833 -0.1751 559 THR A C   
4214 O O   . THR A 532 ? 1.9437 1.6498 1.3269 0.3808  -0.1852 -0.1683 559 THR A O   
4215 C CB  . THR A 532 ? 1.5856 1.3937 1.2555 0.3828  -0.1686 -0.2080 559 THR A CB  
4216 O OG1 . THR A 532 ? 1.7281 1.5134 1.4429 0.4092  -0.2021 -0.2185 559 THR A OG1 
4217 C CG2 . THR A 532 ? 1.4869 1.3465 1.2433 0.3630  -0.1232 -0.2121 559 THR A CG2 
4218 N N   . HIS A 533 ? 2.0640 1.7357 1.5117 0.4093  -0.2141 -0.1764 560 HIS A N   
4219 C CA  . HIS A 533 ? 2.1709 1.7802 1.5189 0.4319  -0.2518 -0.1683 560 HIS A CA  
4220 C C   . HIS A 533 ? 2.3989 1.9576 1.6872 0.4283  -0.2358 -0.1472 560 HIS A C   
4221 O O   . HIS A 533 ? 2.5057 2.0592 1.8494 0.4377  -0.2420 -0.1532 560 HIS A O   
4222 C CB  . HIS A 533 ? 2.2914 1.8902 1.6841 0.4701  -0.3152 -0.1924 560 HIS A CB  
4223 C CG  . HIS A 533 ? 2.3807 2.0301 1.8484 0.4747  -0.3343 -0.2161 560 HIS A CG  
4224 N ND1 . HIS A 533 ? 2.2153 1.9236 1.8181 0.4683  -0.3240 -0.2348 560 HIS A ND1 
4225 C CD2 . HIS A 533 ? 2.3637 2.0112 1.7902 0.4852  -0.3615 -0.2241 560 HIS A CD2 
4226 C CE1 . HIS A 533 ? 2.1197 1.8616 1.7661 0.4736  -0.3452 -0.2532 560 HIS A CE1 
4227 N NE2 . HIS A 533 ? 2.2062 1.9126 1.7466 0.4843  -0.3699 -0.2481 560 HIS A NE2 
4228 N N   . TYR A 534 ? 2.8344 2.3561 2.0148 0.4148  -0.2139 -0.1230 561 TYR A N   
4229 C CA  . TYR A 534 ? 2.9756 2.4484 2.0982 0.4074  -0.1942 -0.1011 561 TYR A CA  
4230 C C   . TYR A 534 ? 2.9887 2.3998 2.0745 0.4422  -0.2399 -0.1010 561 TYR A C   
4231 O O   . TYR A 534 ? 2.9293 2.3211 2.0403 0.4471  -0.2408 -0.0995 561 TYR A O   
4232 C CB  . TYR A 534 ? 2.9424 2.3904 1.9660 0.3843  -0.1588 -0.0752 561 TYR A CB  
4233 C CG  . TYR A 534 ? 2.8730 2.3721 1.9272 0.3472  -0.1096 -0.0719 561 TYR A CG  
4234 C CD1 . TYR A 534 ? 2.6657 2.2302 1.8134 0.3388  -0.1019 -0.0914 561 TYR A CD1 
4235 C CD2 . TYR A 534 ? 2.8659 2.3451 1.8572 0.3215  -0.0711 -0.0493 561 TYR A CD2 
4236 C CE1 . TYR A 534 ? 2.4690 2.0743 1.6372 0.3077  -0.0597 -0.0885 561 TYR A CE1 
4237 C CE2 . TYR A 534 ? 2.7479 2.2711 1.7676 0.2898  -0.0313 -0.0483 561 TYR A CE2 
4238 C CZ  . TYR A 534 ? 2.6167 2.2013 1.7204 0.2840  -0.0269 -0.0680 561 TYR A CZ  
4239 O OH  . TYR A 534 ? 2.4816 2.1046 1.6069 0.2551  0.0102  -0.0672 561 TYR A OH  
4240 N N   . ARG B 15  ? 1.7955 0.5822 1.1923 -0.0306 0.0021  -0.0640 42  ARG B N   
4241 C CA  . ARG B 15  ? 1.7616 0.5666 1.1627 -0.0640 0.0085  -0.0560 42  ARG B CA  
4242 C C   . ARG B 15  ? 1.7736 0.6432 1.1916 -0.0600 0.0133  -0.0447 42  ARG B C   
4243 O O   . ARG B 15  ? 1.7644 0.6822 1.1987 -0.0452 0.0136  -0.0550 42  ARG B O   
4244 C CB  . ARG B 15  ? 1.9832 0.8015 1.3939 -0.0857 0.0092  -0.0772 42  ARG B CB  
4245 C CG  . ARG B 15  ? 2.3843 1.1540 1.7878 -0.0998 0.0054  -0.0865 42  ARG B CG  
4246 C CD  . ARG B 15  ? 2.3341 1.0913 1.7392 -0.1332 0.0103  -0.0714 42  ARG B CD  
4247 N NE  . ARG B 15  ? 2.4436 1.2386 1.8594 -0.1591 0.0168  -0.0711 42  ARG B NE  
4248 C CZ  . ARG B 15  ? 2.2723 1.0684 1.6959 -0.1924 0.0221  -0.0654 42  ARG B CZ  
4249 N NH1 . ARG B 15  ? 1.9852 0.7448 1.4061 -0.2056 0.0221  -0.0596 42  ARG B NH1 
4250 N NH2 . ARG B 15  ? 2.0826 0.9255 1.5223 -0.2117 0.0280  -0.0655 42  ARG B NH2 
4251 N N   . TRP B 16  ? 1.7970 0.6662 1.2100 -0.0734 0.0176  -0.0235 43  TRP B N   
4252 C CA  . TRP B 16  ? 1.6854 0.6129 1.1135 -0.0718 0.0224  -0.0133 43  TRP B CA  
4253 C C   . TRP B 16  ? 1.6063 0.5822 1.0550 -0.0951 0.0287  -0.0218 43  TRP B C   
4254 O O   . TRP B 16  ? 1.6201 0.5812 1.0681 -0.1224 0.0317  -0.0245 43  TRP B O   
4255 C CB  . TRP B 16  ? 1.5191 0.4301 0.9322 -0.0777 0.0251  0.0111  43  TRP B CB  
4256 C CG  . TRP B 16  ? 1.6067 0.5770 1.0351 -0.0799 0.0309  0.0193  43  TRP B CG  
4257 C CD1 . TRP B 16  ? 1.5407 0.5512 0.9814 -0.0567 0.0284  0.0195  43  TRP B CD1 
4258 C CD2 . TRP B 16  ? 1.5563 0.5526 0.9912 -0.1068 0.0405  0.0271  43  TRP B CD2 
4259 N NE1 . TRP B 16  ? 1.5053 0.5616 0.9578 -0.0674 0.0353  0.0269  43  TRP B NE1 
4260 C CE2 . TRP B 16  ? 1.5603 0.6096 1.0095 -0.0970 0.0429  0.0315  43  TRP B CE2 
4261 C CE3 . TRP B 16  ? 1.5199 0.5002 0.9513 -0.1383 0.0478  0.0304  43  TRP B CE3 
4262 C CZ2 . TRP B 16  ? 1.4393 0.5248 0.8982 -0.1160 0.0523  0.0383  43  TRP B CZ2 
4263 C CZ3 . TRP B 16  ? 1.5578 0.5775 1.0007 -0.1575 0.0578  0.0376  43  TRP B CZ3 
4264 C CH2 . TRP B 16  ? 1.5914 0.6624 1.0471 -0.1454 0.0599  0.0412  43  TRP B CH2 
4265 N N   . SER B 17  ? 1.4695 0.5034 0.9375 -0.0841 0.0303  -0.0259 44  SER B N   
4266 C CA  . SER B 17  ? 1.3863 0.4706 0.8751 -0.1017 0.0351  -0.0326 44  SER B CA  
4267 C C   . SER B 17  ? 1.3366 0.4730 0.8400 -0.0919 0.0392  -0.0233 44  SER B C   
4268 O O   . SER B 17  ? 1.5640 0.7177 1.0718 -0.0672 0.0365  -0.0252 44  SER B O   
4269 C CB  . SER B 17  ? 1.4774 0.5749 0.9744 -0.0980 0.0309  -0.0550 44  SER B CB  
4270 O OG  . SER B 17  ? 1.6481 0.7839 1.1622 -0.1191 0.0335  -0.0619 44  SER B OG  
4271 N N   . PRO B 18  ? 1.2633 0.4255 0.7753 -0.1107 0.0462  -0.0137 45  PRO B N   
4272 C CA  . PRO B 18  ? 1.3007 0.5077 0.8249 -0.1016 0.0500  -0.0049 45  PRO B CA  
4273 C C   . PRO B 18  ? 1.2714 0.5292 0.8178 -0.0935 0.0498  -0.0170 45  PRO B C   
4274 O O   . PRO B 18  ? 1.4865 0.7619 1.0441 -0.1070 0.0502  -0.0278 45  PRO B O   
4275 C CB  . PRO B 18  ? 1.3468 0.5620 0.8723 -0.1262 0.0586  0.0064  45  PRO B CB  
4276 C CG  . PRO B 18  ? 1.2569 0.4554 0.7843 -0.1505 0.0597  -0.0022 45  PRO B CG  
4277 C CD  . PRO B 18  ? 1.3593 0.5091 0.8704 -0.1414 0.0516  -0.0105 45  PRO B CD  
4278 N N   . GLU B 19  ? 1.2837 0.5647 0.8363 -0.0717 0.0488  -0.0146 46  GLU B N   
4279 C CA  . GLU B 19  ? 1.2190 0.5486 0.7915 -0.0644 0.0502  -0.0223 46  GLU B CA  
4280 C C   . GLU B 19  ? 1.0570 0.4245 0.6447 -0.0781 0.0566  -0.0154 46  GLU B C   
4281 O O   . GLU B 19  ? 1.3960 0.7592 0.9791 -0.0838 0.0604  -0.0030 46  GLU B O   
4282 C CB  . GLU B 19  ? 1.0711 0.4129 0.6472 -0.0381 0.0483  -0.0216 46  GLU B CB  
4283 C CG  . GLU B 19  ? 1.1822 0.4941 0.7475 -0.0212 0.0430  -0.0306 46  GLU B CG  
4284 C CD  . GLU B 19  ? 1.3449 0.6622 0.9115 -0.0228 0.0419  -0.0473 46  GLU B CD  
4285 O OE1 . GLU B 19  ? 1.3694 0.7269 0.9496 -0.0196 0.0445  -0.0520 46  GLU B OE1 
4286 O OE2 . GLU B 19  ? 1.3721 0.6520 0.9248 -0.0273 0.0381  -0.0557 46  GLU B OE2 
4287 N N   . SER B 20  ? 1.1818 0.5859 0.7864 -0.0826 0.0577  -0.0237 47  SER B N   
4288 C CA  . SER B 20  ? 1.0345 0.4772 0.6565 -0.0928 0.0635  -0.0188 47  SER B CA  
4289 C C   . SER B 20  ? 0.9655 0.4294 0.5935 -0.0770 0.0660  -0.0105 47  SER B C   
4290 O O   . SER B 20  ? 1.0605 0.5153 0.6830 -0.0585 0.0628  -0.0102 47  SER B O   
4291 C CB  . SER B 20  ? 1.0841 0.5591 0.7220 -0.0984 0.0617  -0.0299 47  SER B CB  
4292 O OG  . SER B 20  ? 1.1667 0.6512 0.8044 -0.0803 0.0576  -0.0376 47  SER B OG  
4293 N N   . PRO B 21  ? 1.0132 0.5057 0.6537 -0.0837 0.0719  -0.0045 48  PRO B N   
4294 C CA  . PRO B 21  ? 1.0846 0.5962 0.7313 -0.0697 0.0738  0.0019  48  PRO B CA  
4295 C C   . PRO B 21  ? 1.0204 0.5586 0.6807 -0.0547 0.0720  -0.0041 48  PRO B C   
4296 O O   . PRO B 21  ? 1.0876 0.6403 0.7553 -0.0572 0.0707  -0.0120 48  PRO B O   
4297 C CB  . PRO B 21  ? 0.8970 0.4321 0.5540 -0.0826 0.0811  0.0071  48  PRO B CB  
4298 C CG  . PRO B 21  ? 0.9230 0.4434 0.5747 -0.1032 0.0838  0.0068  48  PRO B CG  
4299 C CD  . PRO B 21  ? 1.0474 0.5540 0.6969 -0.1047 0.0775  -0.0033 48  PRO B CD  
4300 N N   . LEU B 22  ? 1.1291 0.6735 0.7920 -0.0393 0.0718  -0.0001 49  LEU B N   
4301 C CA  . LEU B 22  ? 1.0867 0.6583 0.7638 -0.0265 0.0725  -0.0033 49  LEU B CA  
4302 C C   . LEU B 22  ? 1.0571 0.6622 0.7513 -0.0328 0.0771  -0.0018 49  LEU B C   
4303 O O   . LEU B 22  ? 1.1074 0.7180 0.8046 -0.0413 0.0806  0.0033  49  LEU B O   
4304 C CB  . LEU B 22  ? 0.8617 0.4329 0.5406 -0.0105 0.0715  0.0005  49  LEU B CB  
4305 C CG  . LEU B 22  ? 0.9116 0.4516 0.5763 -0.0008 0.0663  -0.0003 49  LEU B CG  
4306 C CD1 . LEU B 22  ? 0.8957 0.4416 0.5668 0.0138  0.0646  0.0039  49  LEU B CD1 
4307 C CD2 . LEU B 22  ? 0.9472 0.4801 0.6081 0.0056  0.0648  -0.0100 49  LEU B CD2 
4308 N N   . GLN B 23  ? 1.0059 0.6325 0.7099 -0.0277 0.0772  -0.0061 50  GLN B N   
4309 C CA  . GLN B 23  ? 0.9633 0.6206 0.6842 -0.0296 0.0808  -0.0039 50  GLN B CA  
4310 C C   . GLN B 23  ? 1.0332 0.7001 0.7628 -0.0208 0.0842  0.0022  50  GLN B C   
4311 O O   . GLN B 23  ? 1.0509 0.7071 0.7763 -0.0109 0.0831  0.0037  50  GLN B O   
4312 C CB  . GLN B 23  ? 0.9829 0.6580 0.7089 -0.0247 0.0790  -0.0086 50  GLN B CB  
4313 C CG  . GLN B 23  ? 1.0908 0.7580 0.8082 -0.0335 0.0739  -0.0167 50  GLN B CG  
4314 C CD  . GLN B 23  ? 1.1901 0.8802 0.9127 -0.0304 0.0710  -0.0207 50  GLN B CD  
4315 O OE1 . GLN B 23  ? 1.2431 0.9562 0.9795 -0.0358 0.0709  -0.0194 50  GLN B OE1 
4316 N NE2 . GLN B 23  ? 1.0160 0.7004 0.7268 -0.0207 0.0686  -0.0257 50  GLN B NE2 
4317 N N   . ALA B 24  ? 0.9073 0.5953 0.6506 -0.0244 0.0881  0.0050  51  ALA B N   
4318 C CA  . ALA B 24  ? 1.0196 0.7160 0.7717 -0.0177 0.0911  0.0093  51  ALA B CA  
4319 C C   . ALA B 24  ? 1.0761 0.7806 0.8351 -0.0047 0.0913  0.0098  51  ALA B C   
4320 O O   . ALA B 24  ? 0.9785 0.6883 0.7368 -0.0010 0.0905  0.0074  51  ALA B O   
4321 C CB  . ALA B 24  ? 0.8984 0.6152 0.6644 -0.0231 0.0957  0.0106  51  ALA B CB  
4322 N N   . PRO B 25  ? 1.0742 0.7803 0.8395 0.0019  0.0925  0.0125  52  PRO B N   
4323 C CA  . PRO B 25  ? 0.9498 0.6661 0.7250 0.0125  0.0946  0.0135  52  PRO B CA  
4324 C C   . PRO B 25  ? 1.0851 0.8201 0.8708 0.0132  0.0983  0.0154  52  PRO B C   
4325 O O   . PRO B 25  ? 1.0751 0.8189 0.8662 0.0072  0.0992  0.0161  52  PRO B O   
4326 C CB  . PRO B 25  ? 0.9451 0.6627 0.7289 0.0154  0.0947  0.0156  52  PRO B CB  
4327 C CG  . PRO B 25  ? 0.7813 0.4815 0.5513 0.0104  0.0903  0.0151  52  PRO B CG  
4328 C CD  . PRO B 25  ? 1.0301 0.7271 0.7917 -0.0002 0.0913  0.0144  52  PRO B CD  
4329 N N   . ARG B 26  ? 1.1313 0.8725 0.9198 0.0213  0.1009  0.0167  53  ARG B N   
4330 C CA  . ARG B 26  ? 1.0697 0.8255 0.8640 0.0238  0.1040  0.0202  53  ARG B CA  
4331 C C   . ARG B 26  ? 0.9380 0.7028 0.7490 0.0270  0.1091  0.0255  53  ARG B C   
4332 O O   . ARG B 26  ? 0.9932 0.7584 0.8095 0.0322  0.1125  0.0269  53  ARG B O   
4333 C CB  . ARG B 26  ? 0.9564 0.7121 0.7396 0.0301  0.1046  0.0189  53  ARG B CB  
4334 C CG  . ARG B 26  ? 0.9926 0.7395 0.7598 0.0258  0.0987  0.0123  53  ARG B CG  
4335 C CD  . ARG B 26  ? 1.0265 0.7642 0.7801 0.0327  0.0990  0.0075  53  ARG B CD  
4336 N NE  . ARG B 26  ? 0.9852 0.7097 0.7394 0.0358  0.0991  0.0054  53  ARG B NE  
4337 C CZ  . ARG B 26  ? 1.0366 0.7485 0.7798 0.0418  0.0984  -0.0004 53  ARG B CZ  
4338 N NH1 . ARG B 26  ? 1.1725 0.8829 0.9016 0.0450  0.0983  -0.0057 53  ARG B NH1 
4339 N NH2 . ARG B 26  ? 1.1254 0.8257 0.8709 0.0456  0.0970  -0.0016 53  ARG B NH2 
4340 N N   . VAL B 27  ? 0.9408 0.7130 0.7612 0.0237  0.1100  0.0277  54  VAL B N   
4341 C CA  . VAL B 27  ? 0.9712 0.7481 0.8076 0.0251  0.1142  0.0313  54  VAL B CA  
4342 C C   . VAL B 27  ? 0.9502 0.7357 0.7923 0.0294  0.1176  0.0377  54  VAL B C   
4343 O O   . VAL B 27  ? 1.0709 0.8622 0.9101 0.0291  0.1149  0.0382  54  VAL B O   
4344 C CB  . VAL B 27  ? 0.9486 0.7243 0.7904 0.0192  0.1130  0.0280  54  VAL B CB  
4345 C CG1 . VAL B 27  ? 0.8902 0.6688 0.7480 0.0206  0.1168  0.0299  54  VAL B CG1 
4346 C CG2 . VAL B 27  ? 0.9611 0.7261 0.7931 0.0154  0.1092  0.0235  54  VAL B CG2 
4347 N N   . LEU B 28  ? 0.9181 0.7045 0.7687 0.0333  0.1231  0.0431  55  LEU B N   
4348 C CA  . LEU B 28  ? 0.9135 0.7039 0.7705 0.0370  0.1271  0.0511  55  LEU B CA  
4349 C C   . LEU B 28  ? 0.9855 0.7738 0.8596 0.0347  0.1291  0.0511  55  LEU B C   
4350 O O   . LEU B 28  ? 0.8330 0.6180 0.7167 0.0320  0.1312  0.0487  55  LEU B O   
4351 C CB  . LEU B 28  ? 0.9155 0.7064 0.7702 0.0415  0.1337  0.0581  55  LEU B CB  
4352 C CG  . LEU B 28  ? 0.8881 0.6793 0.7467 0.0453  0.1383  0.0687  55  LEU B CG  
4353 C CD1 . LEU B 28  ? 1.0731 0.8685 0.9185 0.0497  0.1327  0.0714  55  LEU B CD1 
4354 C CD2 . LEU B 28  ? 0.9114 0.7022 0.7696 0.0476  0.1476  0.0765  55  LEU B CD2 
4355 N N   . ILE B 29  ? 0.9330 0.7238 0.8117 0.0362  0.1279  0.0527  56  ILE B N   
4356 C CA  . ILE B 29  ? 0.8054 0.5926 0.6995 0.0355  0.1302  0.0518  56  ILE B CA  
4357 C C   . ILE B 29  ? 0.9816 0.7645 0.8821 0.0407  0.1351  0.0621  56  ILE B C   
4358 O O   . ILE B 29  ? 0.9817 0.7674 0.8778 0.0467  0.1337  0.0686  56  ILE B O   
4359 C CB  . ILE B 29  ? 0.8205 0.6131 0.7174 0.0351  0.1269  0.0464  56  ILE B CB  
4360 C CG1 . ILE B 29  ? 0.8331 0.6277 0.7212 0.0284  0.1235  0.0378  56  ILE B CG1 
4361 C CG2 . ILE B 29  ? 0.8094 0.5968 0.7214 0.0358  0.1300  0.0442  56  ILE B CG2 
4362 C CD1 . ILE B 29  ? 0.7428 0.5444 0.6346 0.0260  0.1226  0.0319  56  ILE B CD1 
4363 N N   . ALA B 30  ? 0.9927 0.7687 0.9038 0.0381  0.1405  0.0641  57  ALA B N   
4364 C CA  . ALA B 30  ? 0.9649 0.7334 0.8822 0.0409  0.1469  0.0750  57  ALA B CA  
4365 C C   . ALA B 30  ? 0.9136 0.6725 0.8463 0.0409  0.1479  0.0735  57  ALA B C   
4366 O O   . ALA B 30  ? 0.9076 0.6635 0.8510 0.0353  0.1475  0.0643  57  ALA B O   
4367 C CB  . ALA B 30  ? 0.8904 0.6581 0.8126 0.0367  0.1536  0.0780  57  ALA B CB  
4368 N N   . LEU B 31  ? 0.9528 0.7062 0.8856 0.0480  0.1485  0.0820  58  LEU B N   
4369 C CA  . LEU B 31  ? 0.9961 0.7389 0.9427 0.0506  0.1490  0.0802  58  LEU B CA  
4370 C C   . LEU B 31  ? 0.9367 0.6634 0.8877 0.0541  0.1549  0.0939  58  LEU B C   
4371 O O   . LEU B 31  ? 0.9733 0.6993 0.9139 0.0622  0.1541  0.1057  58  LEU B O   
4372 C CB  . LEU B 31  ? 1.1232 0.8749 1.0681 0.0580  0.1429  0.0763  58  LEU B CB  
4373 C CG  . LEU B 31  ? 1.2155 0.9574 1.1742 0.0645  0.1435  0.0751  58  LEU B CG  
4374 C CD1 . LEU B 31  ? 1.1249 0.8587 1.0957 0.0577  0.1461  0.0624  58  LEU B CD1 
4375 C CD2 . LEU B 31  ? 1.1281 0.8846 1.0869 0.0729  0.1377  0.0722  58  LEU B CD2 
4376 N N   . LEU B 32  ? 1.0223 0.7353 0.9876 0.0474  0.1604  0.0925  59  LEU B N   
4377 C CA  . LEU B 32  ? 0.9216 0.6143 0.8936 0.0491  0.1667  0.1048  59  LEU B CA  
4378 C C   . LEU B 32  ? 0.9983 0.6771 0.9817 0.0548  0.1644  0.0997  59  LEU B C   
4379 O O   . LEU B 32  ? 1.0897 0.7680 1.0840 0.0503  0.1626  0.0848  59  LEU B O   
4380 C CB  . LEU B 32  ? 0.8090 0.4941 0.7933 0.0372  0.1745  0.1057  59  LEU B CB  
4381 C CG  . LEU B 32  ? 0.9934 0.6890 0.9709 0.0320  0.1806  0.1132  59  LEU B CG  
4382 C CD1 . LEU B 32  ? 0.7934 0.5108 0.7627 0.0309  0.1752  0.1030  59  LEU B CD1 
4383 C CD2 . LEU B 32  ? 1.0932 0.7807 1.0897 0.0201  0.1891  0.1142  59  LEU B CD2 
4384 N N   . ALA B 33  ? 0.9516 0.6191 0.9316 0.0658  0.1641  0.1118  60  ALA B N   
4385 C CA  . ALA B 33  ? 1.0507 0.7061 1.0415 0.0746  0.1614  0.1072  60  ALA B CA  
4386 C C   . ALA B 33  ? 1.1129 0.7388 1.1082 0.0787  0.1666  0.1217  60  ALA B C   
4387 O O   . ALA B 33  ? 1.0670 0.6876 1.0493 0.0847  0.1677  0.1397  60  ALA B O   
4388 C CB  . ALA B 33  ? 1.0140 0.6872 0.9982 0.0873  0.1534  0.1060  60  ALA B CB  
4389 N N   . ARG B 34  ? 1.0242 0.6291 1.0359 0.0753  0.1696  0.1138  61  ARG B N   
4390 C CA  . ARG B 34  ? 1.0851 0.6573 1.1031 0.0804  0.1737  0.1254  61  ARG B CA  
4391 C C   . ARG B 34  ? 1.2263 0.7855 1.2597 0.0866  0.1713  0.1102  61  ARG B C   
4392 O O   . ARG B 34  ? 1.2606 0.8222 1.3042 0.0770  0.1718  0.0920  61  ARG B O   
4393 C CB  . ARG B 34  ? 1.0246 0.5771 1.0488 0.0653  0.1833  0.1327  61  ARG B CB  
4394 C CG  . ARG B 34  ? 1.1254 0.6396 1.1547 0.0694  0.1883  0.1465  61  ARG B CG  
4395 C CD  . ARG B 34  ? 1.0045 0.4980 1.0461 0.0516  0.1984  0.1499  61  ARG B CD  
4396 N NE  . ARG B 34  ? 1.1054 0.5582 1.1512 0.0552  0.2033  0.1631  61  ARG B NE  
4397 C CZ  . ARG B 34  ? 1.1667 0.5926 1.2272 0.0406  0.2117  0.1650  61  ARG B CZ  
4398 N NH1 . ARG B 34  ? 1.2012 0.6394 1.2755 0.0214  0.2159  0.1543  61  ARG B NH1 
4399 N NH2 . ARG B 34  ? 1.1562 0.5416 1.2188 0.0455  0.2155  0.1777  61  ARG B NH2 
4400 N N   . ASN B 35  ? 1.2444 0.7903 1.2786 0.1034  0.1683  0.1174  62  ASN B N   
4401 C CA  . ASN B 35  ? 1.0535 0.5856 1.1026 0.1124  0.1668  0.1035  62  ASN B CA  
4402 C C   . ASN B 35  ? 1.0484 0.6083 1.1019 0.1103  0.1637  0.0805  62  ASN B C   
4403 O O   . ASN B 35  ? 1.0984 0.6501 1.1619 0.1042  0.1658  0.0628  62  ASN B O   
4404 C CB  . ASN B 35  ? 0.9909 0.4855 1.0525 0.1038  0.1733  0.1010  62  ASN B CB  
4405 C CG  . ASN B 35  ? 1.2006 0.6621 1.2584 0.1079  0.1773  0.1245  62  ASN B CG  
4406 O OD1 . ASN B 35  ? 1.3099 0.7654 1.3614 0.1257  0.1733  0.1378  62  ASN B OD1 
4407 N ND2 . ASN B 35  ? 1.2532 0.6935 1.3152 0.0914  0.1851  0.1301  62  ASN B ND2 
4408 N N   . ALA B 36  ? 1.1555 0.7480 1.1997 0.1146  0.1586  0.0810  63  ALA B N   
4409 C CA  . ALA B 36  ? 1.0359 0.6563 1.0806 0.1101  0.1567  0.0623  63  ALA B CA  
4410 C C   . ALA B 36  ? 1.0768 0.7176 1.1265 0.1252  0.1523  0.0566  63  ALA B C   
4411 O O   . ALA B 36  ? 0.9718 0.6378 1.0205 0.1214  0.1516  0.0431  63  ALA B O   
4412 C CB  . ALA B 36  ? 0.9388 0.5817 0.9696 0.0980  0.1554  0.0650  63  ALA B CB  
4413 N N   . ALA B 37  ? 1.0533 0.6845 1.1089 0.1422  0.1495  0.0668  64  ALA B N   
4414 C CA  . ALA B 37  ? 0.9804 0.6352 1.0446 0.1575  0.1447  0.0616  64  ALA B CA  
4415 C C   . ALA B 37  ? 1.0229 0.6865 1.0997 0.1578  0.1489  0.0387  64  ALA B C   
4416 O O   . ALA B 37  ? 1.1434 0.8374 1.2263 0.1634  0.1471  0.0303  64  ALA B O   
4417 C CB  . ALA B 37  ? 0.9841 0.6224 1.0548 0.1775  0.1405  0.0756  64  ALA B CB  
4418 N N   . HIS B 38  ? 1.0623 0.7011 1.1428 0.1510  0.1548  0.0279  65  HIS B N   
4419 C CA  . HIS B 38  ? 0.9908 0.6369 1.0790 0.1508  0.1594  0.0051  65  HIS B CA  
4420 C C   . HIS B 38  ? 1.1871 0.8631 1.2644 0.1368  0.1602  -0.0047 65  HIS B C   
4421 O O   . HIS B 38  ? 1.2142 0.9124 1.2958 0.1400  0.1629  -0.0185 65  HIS B O   
4422 C CB  . HIS B 38  ? 0.9676 0.5784 1.0594 0.1454  0.1642  -0.0048 65  HIS B CB  
4423 C CG  . HIS B 38  ? 1.0282 0.6277 1.1093 0.1255  0.1648  -0.0023 65  HIS B CG  
4424 N ND1 . HIS B 38  ? 1.1445 0.7249 1.2227 0.1205  0.1640  0.0161  65  HIS B ND1 
4425 C CD2 . HIS B 38  ? 1.1561 0.7623 1.2296 0.1098  0.1660  -0.0158 65  HIS B CD2 
4426 C CE1 . HIS B 38  ? 1.0368 0.6149 1.1092 0.1025  0.1651  0.0130  65  HIS B CE1 
4427 N NE2 . HIS B 38  ? 1.1443 0.7376 1.2136 0.0963  0.1653  -0.0062 65  HIS B NE2 
4428 N N   . ALA B 39  ? 1.0837 0.7608 1.1470 0.1218  0.1585  0.0027  66  ALA B N   
4429 C CA  . ALA B 39  ? 0.9972 0.6957 1.0483 0.1081  0.1589  -0.0061 66  ALA B CA  
4430 C C   . ALA B 39  ? 1.0582 0.7858 1.1021 0.1074  0.1547  0.0022  66  ALA B C   
4431 O O   . ALA B 39  ? 1.1129 0.8611 1.1498 0.0998  0.1556  -0.0066 66  ALA B O   
4432 C CB  . ALA B 39  ? 1.0543 0.7378 1.0959 0.0923  0.1588  -0.0054 66  ALA B CB  
4433 N N   . LEU B 40  ? 1.0984 0.8270 1.1425 0.1147  0.1499  0.0188  67  LEU B N   
4434 C CA  . LEU B 40  ? 1.0670 0.8204 1.1018 0.1119  0.1448  0.0263  67  LEU B CA  
4435 C C   . LEU B 40  ? 0.9641 0.7483 1.0048 0.1142  0.1443  0.0163  67  LEU B C   
4436 O O   . LEU B 40  ? 1.0734 0.8748 1.1035 0.1036  0.1430  0.0148  67  LEU B O   
4437 C CB  . LEU B 40  ? 0.9676 0.7160 1.0002 0.1217  0.1392  0.0449  67  LEU B CB  
4438 C CG  . LEU B 40  ? 0.9646 0.6879 0.9871 0.1155  0.1409  0.0576  67  LEU B CG  
4439 C CD1 . LEU B 40  ? 0.9313 0.6498 0.9477 0.1259  0.1361  0.0767  67  LEU B CD1 
4440 C CD2 . LEU B 40  ? 0.9162 0.6465 0.9252 0.0993  0.1421  0.0551  67  LEU B CD2 
4441 N N   . PRO B 41  ? 1.1572 0.9500 1.2154 0.1270  0.1459  0.0094  68  PRO B N   
4442 C CA  . PRO B 41  ? 0.9971 0.8232 1.0631 0.1268  0.1470  -0.0005 68  PRO B CA  
4443 C C   . PRO B 41  ? 1.0471 0.8799 1.1014 0.1108  0.1533  -0.0126 68  PRO B C   
4444 O O   . PRO B 41  ? 1.1419 0.9963 1.1902 0.1019  0.1521  -0.0133 68  PRO B O   
4445 C CB  . PRO B 41  ? 0.9282 0.7571 1.0165 0.1436  0.1503  -0.0085 68  PRO B CB  
4446 C CG  . PRO B 41  ? 0.8579 0.6584 0.9494 0.1558  0.1463  0.0033  68  PRO B CG  
4447 C CD  . PRO B 41  ? 0.9799 0.7533 1.0528 0.1425  0.1470  0.0101  68  PRO B CD  
4448 N N   . THR B 42  ? 1.1123 0.9253 1.1620 0.1066  0.1592  -0.0221 69  THR B N   
4449 C CA  . THR B 42  ? 1.0814 0.8974 1.1158 0.0921  0.1639  -0.0325 69  THR B CA  
4450 C C   . THR B 42  ? 1.1715 0.9799 1.1872 0.0791  0.1589  -0.0237 69  THR B C   
4451 O O   . THR B 42  ? 1.0860 0.9062 1.0887 0.0682  0.1592  -0.0259 69  THR B O   
4452 C CB  . THR B 42  ? 1.0977 0.8946 1.1316 0.0927  0.1700  -0.0461 69  THR B CB  
4453 O OG1 . THR B 42  ? 1.2232 1.0236 1.2763 0.1076  0.1745  -0.0537 69  THR B OG1 
4454 C CG2 . THR B 42  ? 1.2976 1.1013 1.3148 0.0802  0.1751  -0.0579 69  THR B CG2 
4455 N N   . THR B 43  ? 1.1480 0.9363 1.1623 0.0803  0.1549  -0.0136 70  THR B N   
4456 C CA  . THR B 43  ? 0.9848 0.7663 0.9839 0.0692  0.1513  -0.0065 70  THR B CA  
4457 C C   . THR B 43  ? 1.0706 0.8698 1.0625 0.0669  0.1465  0.0025  70  THR B C   
4458 O O   . THR B 43  ? 0.9570 0.7609 0.9349 0.0565  0.1452  0.0016  70  THR B O   
4459 C CB  . THR B 43  ? 0.8407 0.5986 0.8432 0.0710  0.1501  0.0022  70  THR B CB  
4460 O OG1 . THR B 43  ? 1.1377 0.8784 1.1414 0.0661  0.1531  -0.0084 70  THR B OG1 
4461 C CG2 . THR B 43  ? 1.1577 0.9153 1.1488 0.0640  0.1464  0.0136  70  THR B CG2 
4462 N N   . LEU B 44  ? 1.1742 0.9823 1.1747 0.0769  0.1430  0.0110  71  LEU B N   
4463 C CA  . LEU B 44  ? 0.9981 0.8221 0.9909 0.0746  0.1373  0.0184  71  LEU B CA  
4464 C C   . LEU B 44  ? 0.9848 0.8324 0.9782 0.0687  0.1381  0.0097  71  LEU B C   
4465 O O   . LEU B 44  ? 0.9914 0.8468 0.9730 0.0602  0.1348  0.0117  71  LEU B O   
4466 C CB  . LEU B 44  ? 0.8810 0.7080 0.8809 0.0874  0.1317  0.0298  71  LEU B CB  
4467 C CG  . LEU B 44  ? 1.0360 0.8392 1.0307 0.0911  0.1314  0.0422  71  LEU B CG  
4468 C CD1 . LEU B 44  ? 1.0393 0.8462 1.0338 0.1030  0.1249  0.0555  71  LEU B CD1 
4469 C CD2 . LEU B 44  ? 0.9712 0.7658 0.9497 0.0789  0.1325  0.0447  71  LEU B CD2 
4470 N N   . GLY B 45  ? 0.9776 0.8361 0.9847 0.0727  0.1432  -0.0002 72  GLY B N   
4471 C CA  . GLY B 45  ? 1.0281 0.9088 1.0360 0.0649  0.1466  -0.0086 72  GLY B CA  
4472 C C   . GLY B 45  ? 1.0380 0.9102 1.0254 0.0499  0.1495  -0.0124 72  GLY B C   
4473 O O   . GLY B 45  ? 1.0515 0.9355 1.0312 0.0402  0.1489  -0.0128 72  GLY B O   
4474 N N   . ALA B 46  ? 1.0028 0.8535 0.9811 0.0479  0.1519  -0.0151 73  ALA B N   
4475 C CA  . ALA B 46  ? 0.8874 0.7288 0.8452 0.0356  0.1525  -0.0177 73  ALA B CA  
4476 C C   . ALA B 46  ? 0.9693 0.8072 0.9148 0.0301  0.1456  -0.0082 73  ALA B C   
4477 O O   . ALA B 46  ? 1.1033 0.9424 1.0342 0.0203  0.1452  -0.0090 73  ALA B O   
4478 C CB  . ALA B 46  ? 0.7603 0.5812 0.7134 0.0357  0.1541  -0.0228 73  ALA B CB  
4479 N N   . LEU B 47  ? 1.0449 0.8775 0.9951 0.0366  0.1408  0.0010  74  LEU B N   
4480 C CA  . LEU B 47  ? 0.9674 0.7967 0.9054 0.0327  0.1352  0.0090  74  LEU B CA  
4481 C C   . LEU B 47  ? 0.9984 0.8449 0.9344 0.0294  0.1320  0.0099  74  LEU B C   
4482 O O   . LEU B 47  ? 1.0107 0.8544 0.9323 0.0217  0.1292  0.0110  74  LEU B O   
4483 C CB  . LEU B 47  ? 0.9646 0.7845 0.9065 0.0405  0.1326  0.0187  74  LEU B CB  
4484 C CG  . LEU B 47  ? 1.0153 0.8166 0.9597 0.0409  0.1353  0.0191  74  LEU B CG  
4485 C CD1 . LEU B 47  ? 0.9559 0.7489 0.9027 0.0469  0.1342  0.0307  74  LEU B CD1 
4486 C CD2 . LEU B 47  ? 0.8537 0.6475 0.7860 0.0316  0.1348  0.0148  74  LEU B CD2 
4487 N N   . GLU B 48  ? 1.0134 0.8775 0.9647 0.0354  0.1317  0.0088  75  GLU B N   
4488 C CA  . GLU B 48  ? 1.0369 0.9205 0.9901 0.0310  0.1281  0.0079  75  GLU B CA  
4489 C C   . GLU B 48  ? 0.9497 0.8353 0.8930 0.0171  0.1323  0.0014  75  GLU B C   
4490 O O   . GLU B 48  ? 1.1004 0.9879 1.0340 0.0088  0.1286  0.0024  75  GLU B O   
4491 C CB  . GLU B 48  ? 0.9725 0.8786 0.9483 0.0395  0.1278  0.0055  75  GLU B CB  
4492 C CG  . GLU B 48  ? 1.2114 1.1159 1.1970 0.0547  0.1230  0.0129  75  GLU B CG  
4493 C CD  . GLU B 48  ? 1.3188 1.2451 1.3290 0.0646  0.1233  0.0087  75  GLU B CD  
4494 O OE1 . GLU B 48  ? 1.1120 1.0531 1.1324 0.0596  0.1301  -0.0012 75  GLU B OE1 
4495 O OE2 . GLU B 48  ? 1.3661 1.2951 1.3851 0.0781  0.1171  0.0156  75  GLU B OE2 
4496 N N   . ARG B 49  ? 0.9976 0.8811 0.9419 0.0146  0.1403  -0.0053 76  ARG B N   
4497 C CA  . ARG B 49  ? 0.9307 0.8171 0.8652 0.0020  0.1460  -0.0108 76  ARG B CA  
4498 C C   . ARG B 49  ? 1.0890 0.9524 0.9992 -0.0054 0.1451  -0.0090 76  ARG B C   
4499 O O   . ARG B 49  ? 0.9884 0.8484 0.8861 -0.0147 0.1504  -0.0126 76  ARG B O   
4500 C CB  . ARG B 49  ? 0.8622 0.7598 0.8079 0.0037  0.1559  -0.0194 76  ARG B CB  
4501 C CG  . ARG B 49  ? 0.9569 0.8795 0.9299 0.0130  0.1566  -0.0218 76  ARG B CG  
4502 C CD  . ARG B 49  ? 0.9477 0.8842 0.9325 0.0144  0.1680  -0.0319 76  ARG B CD  
4503 N NE  . ARG B 49  ? 0.9594 0.8799 0.9432 0.0237  0.1713  -0.0359 76  ARG B NE  
4504 C CZ  . ARG B 49  ? 1.0901 1.0122 1.0927 0.0385  0.1700  -0.0367 76  ARG B CZ  
4505 N NH1 . ARG B 49  ? 0.9333 0.8735 0.9564 0.0473  0.1647  -0.0329 76  ARG B NH1 
4506 N NH2 . ARG B 49  ? 1.1809 1.0849 1.1809 0.0448  0.1734  -0.0416 76  ARG B NH2 
4507 N N   . LEU B 50  ? 0.9810 0.8290 0.8841 -0.0010 0.1389  -0.0034 77  LEU B N   
4508 C CA  . LEU B 50  ? 0.9763 0.8056 0.8589 -0.0068 0.1361  -0.0014 77  LEU B CA  
4509 C C   . LEU B 50  ? 1.0289 0.8583 0.8995 -0.0169 0.1344  -0.0002 77  LEU B C   
4510 O O   . LEU B 50  ? 1.0572 0.8969 0.9342 -0.0174 0.1309  0.0016  77  LEU B O   
4511 C CB  . LEU B 50  ? 0.9407 0.7590 0.8225 -0.0001 0.1305  0.0044  77  LEU B CB  
4512 C CG  . LEU B 50  ? 0.9384 0.7486 0.8275 0.0065  0.1316  0.0039  77  LEU B CG  
4513 C CD1 . LEU B 50  ? 0.9812 0.7845 0.8712 0.0114  0.1276  0.0110  77  LEU B CD1 
4514 C CD2 . LEU B 50  ? 0.7942 0.5935 0.6720 0.0017  0.1328  -0.0016 77  LEU B CD2 
4515 N N   . ARG B 51  ? 0.9363 0.7531 0.7887 -0.0250 0.1362  -0.0012 78  ARG B N   
4516 C CA  . ARG B 51  ? 1.0600 0.8715 0.8993 -0.0356 0.1351  0.0005  78  ARG B CA  
4517 C C   . ARG B 51  ? 1.0925 0.8867 0.9196 -0.0330 0.1269  0.0050  78  ARG B C   
4518 O O   . ARG B 51  ? 0.9721 0.7478 0.7814 -0.0350 0.1247  0.0067  78  ARG B O   
4519 C CB  . ARG B 51  ? 1.0862 0.8905 0.9095 -0.0454 0.1415  -0.0012 78  ARG B CB  
4520 C CG  . ARG B 51  ? 1.2157 1.0410 1.0512 -0.0521 0.1511  -0.0056 78  ARG B CG  
4521 C CD  . ARG B 51  ? 1.0207 0.8380 0.8368 -0.0638 0.1591  -0.0059 78  ARG B CD  
4522 N NE  . ARG B 51  ? 1.0791 0.8880 0.8831 -0.0593 0.1622  -0.0086 78  ARG B NE  
4523 C CZ  . ARG B 51  ? 1.0718 0.8949 0.8835 -0.0575 0.1715  -0.0152 78  ARG B CZ  
4524 N NH1 . ARG B 51  ? 1.1376 0.9857 0.9714 -0.0591 0.1791  -0.0194 78  ARG B NH1 
4525 N NH2 . ARG B 51  ? 1.0788 0.8915 0.8765 -0.0535 0.1727  -0.0188 78  ARG B NH2 
4526 N N   . HIS B 52  ? 0.9693 0.7705 0.8060 -0.0272 0.1223  0.0068  79  HIS B N   
4527 C CA  . HIS B 52  ? 0.9177 0.7068 0.7449 -0.0240 0.1159  0.0099  79  HIS B CA  
4528 C C   . HIS B 52  ? 1.0236 0.8259 0.8586 -0.0238 0.1126  0.0096  79  HIS B C   
4529 O O   . HIS B 52  ? 1.1241 0.9441 0.9753 -0.0190 0.1134  0.0095  79  HIS B O   
4530 C CB  . HIS B 52  ? 0.9792 0.7629 0.8092 -0.0136 0.1142  0.0126  79  HIS B CB  
4531 C CG  . HIS B 52  ? 0.9825 0.7552 0.8029 -0.0099 0.1094  0.0149  79  HIS B CG  
4532 N ND1 . HIS B 52  ? 1.1079 0.8632 0.9131 -0.0120 0.1066  0.0148  79  HIS B ND1 
4533 C CD2 . HIS B 52  ? 1.0868 0.8633 0.9096 -0.0034 0.1072  0.0172  79  HIS B CD2 
4534 C CE1 . HIS B 52  ? 1.0859 0.8357 0.8868 -0.0065 0.1033  0.0158  79  HIS B CE1 
4535 N NE2 . HIS B 52  ? 1.1126 0.8752 0.9230 -0.0017 0.1042  0.0172  79  HIS B NE2 
4536 N N   . PRO B 53  ? 1.0311 0.8246 0.8547 -0.0286 0.1080  0.0088  80  PRO B N   
4537 C CA  . PRO B 53  ? 1.0344 0.8411 0.8637 -0.0298 0.1034  0.0068  80  PRO B CA  
4538 C C   . PRO B 53  ? 1.1308 0.9483 0.9680 -0.0174 0.1005  0.0099  80  PRO B C   
4539 O O   . PRO B 53  ? 1.2102 1.0173 1.0400 -0.0095 0.0999  0.0133  80  PRO B O   
4540 C CB  . PRO B 53  ? 0.9468 0.7347 0.7582 -0.0352 0.0987  0.0049  80  PRO B CB  
4541 C CG  . PRO B 53  ? 0.8527 0.6209 0.6518 -0.0411 0.1022  0.0060  80  PRO B CG  
4542 C CD  . PRO B 53  ? 0.9860 0.7562 0.7903 -0.0334 0.1062  0.0091  80  PRO B CD  
4543 N N   . ARG B 54  ? 1.0174 0.8563 0.8700 -0.0155 0.0991  0.0092  81  ARG B N   
4544 C CA  . ARG B 54  ? 1.0320 0.8798 0.8907 -0.0031 0.0964  0.0140  81  ARG B CA  
4545 C C   . ARG B 54  ? 1.0121 0.8548 0.8561 0.0006  0.0899  0.0150  81  ARG B C   
4546 O O   . ARG B 54  ? 1.0869 0.9284 0.9277 0.0109  0.0897  0.0208  81  ARG B O   
4547 C CB  . ARG B 54  ? 1.0821 0.9543 0.9608 -0.0006 0.0948  0.0129  81  ARG B CB  
4548 C CG  . ARG B 54  ? 0.9503 0.8280 0.8443 0.0005  0.1025  0.0122  81  ARG B CG  
4549 C CD  . ARG B 54  ? 1.2430 1.1472 1.1584 0.0006  0.1015  0.0084  81  ARG B CD  
4550 N NE  . ARG B 54  ? 1.3245 1.2344 1.2553 0.0061  0.1088  0.0075  81  ARG B NE  
4551 C CZ  . ARG B 54  ? 1.4463 1.3787 1.3976 0.0057  0.1116  0.0025  81  ARG B CZ  
4552 N NH1 . ARG B 54  ? 1.3368 1.2904 1.2983 -0.0013 0.1077  -0.0020 81  ARG B NH1 
4553 N NH2 . ARG B 54  ? 1.4021 1.3366 1.3655 0.0125  0.1187  0.0008  81  ARG B NH2 
4554 N N   . GLU B 55  ? 1.0888 0.9273 0.9226 -0.0080 0.0854  0.0092  82  GLU B N   
4555 C CA  . GLU B 55  ? 1.0251 0.8566 0.8421 -0.0042 0.0797  0.0082  82  GLU B CA  
4556 C C   . GLU B 55  ? 1.0594 0.8700 0.8623 0.0006  0.0840  0.0106  82  GLU B C   
4557 O O   . GLU B 55  ? 1.1599 0.9664 0.9503 0.0077  0.0824  0.0117  82  GLU B O   
4558 C CB  . GLU B 55  ? 1.0434 0.8745 0.8540 -0.0152 0.0730  -0.0005 82  GLU B CB  
4559 C CG  . GLU B 55  ? 1.0127 0.8213 0.8126 -0.0253 0.0756  -0.0044 82  GLU B CG  
4560 C CD  . GLU B 55  ? 1.3365 1.1483 1.1481 -0.0369 0.0805  -0.0053 82  GLU B CD  
4561 O OE1 . GLU B 55  ? 1.3778 1.2088 1.2072 -0.0353 0.0837  -0.0030 82  GLU B OE1 
4562 O OE2 . GLU B 55  ? 1.2496 1.0437 1.0518 -0.0475 0.0815  -0.0082 82  GLU B OE2 
4563 N N   . ARG B 56  ? 1.0580 0.8568 0.8626 -0.0028 0.0893  0.0113  83  ARG B N   
4564 C CA  . ARG B 56  ? 0.9518 0.7355 0.7490 0.0030  0.0930  0.0139  83  ARG B CA  
4565 C C   . ARG B 56  ? 1.0512 0.8408 0.8607 0.0102  0.0984  0.0204  83  ARG B C   
4566 O O   . ARG B 56  ? 1.0946 0.8750 0.9040 0.0131  0.1018  0.0220  83  ARG B O   
4567 C CB  . ARG B 56  ? 0.9970 0.7635 0.7875 -0.0040 0.0937  0.0110  83  ARG B CB  
4568 C CG  . ARG B 56  ? 1.1117 0.8695 0.8920 -0.0139 0.0893  0.0051  83  ARG B CG  
4569 C CD  . ARG B 56  ? 0.9781 0.7268 0.7440 -0.0098 0.0850  0.0011  83  ARG B CD  
4570 N NE  . ARG B 56  ? 0.9707 0.7009 0.7267 -0.0033 0.0864  0.0013  83  ARG B NE  
4571 C CZ  . ARG B 56  ? 1.1325 0.8517 0.8752 0.0020  0.0843  -0.0031 83  ARG B CZ  
4572 N NH1 . ARG B 56  ? 0.8635 0.5866 0.5983 0.0010  0.0801  -0.0084 83  ARG B NH1 
4573 N NH2 . ARG B 56  ? 1.1673 0.8722 0.9047 0.0092  0.0859  -0.0031 83  ARG B NH2 
4574 N N   . THR B 57  ? 1.0414 0.8457 0.8628 0.0132  0.0987  0.0237  84  THR B N   
4575 C CA  . THR B 57  ? 0.9282 0.7356 0.7616 0.0197  0.1036  0.0297  84  THR B CA  
4576 C C   . THR B 57  ? 0.9058 0.7209 0.7383 0.0283  0.1026  0.0362  84  THR B C   
4577 O O   . THR B 57  ? 0.8988 0.7240 0.7281 0.0290  0.0968  0.0353  84  THR B O   
4578 C CB  . THR B 57  ? 1.0287 0.8433 0.8772 0.0167  0.1058  0.0282  84  THR B CB  
4579 O OG1 . THR B 57  ? 1.0829 0.8906 0.9275 0.0078  0.1066  0.0226  84  THR B OG1 
4580 C CG2 . THR B 57  ? 1.0342 0.8466 0.8944 0.0225  0.1109  0.0328  84  THR B CG2 
4581 N N   . ALA B 58  ? 0.9567 0.7670 0.7915 0.0345  0.1080  0.0430  85  ALA B N   
4582 C CA  . ALA B 58  ? 1.0442 0.8589 0.8769 0.0428  0.1086  0.0517  85  ALA B CA  
4583 C C   . ALA B 58  ? 1.0589 0.8713 0.9076 0.0461  0.1139  0.0581  85  ALA B C   
4584 O O   . ALA B 58  ? 0.9873 0.7938 0.8465 0.0422  0.1179  0.0552  85  ALA B O   
4585 C CB  . ALA B 58  ? 0.9096 0.7187 0.7267 0.0467  0.1119  0.0552  85  ALA B CB  
4586 N N   . LEU B 59  ? 1.0378 0.8538 0.8872 0.0537  0.1130  0.0666  86  LEU B N   
4587 C CA  . LEU B 59  ? 0.8851 0.6962 0.7492 0.0579  0.1173  0.0731  86  LEU B CA  
4588 C C   . LEU B 59  ? 1.0005 0.8028 0.8577 0.0632  0.1231  0.0853  86  LEU B C   
4589 O O   . LEU B 59  ? 1.1679 0.9731 1.0083 0.0682  0.1209  0.0914  86  LEU B O   
4590 C CB  . LEU B 59  ? 0.9215 0.7427 0.7949 0.0635  0.1114  0.0735  86  LEU B CB  
4591 C CG  . LEU B 59  ? 1.0466 0.8772 0.9316 0.0574  0.1089  0.0619  86  LEU B CG  
4592 C CD1 . LEU B 59  ? 1.0039 0.8497 0.9001 0.0637  0.1029  0.0616  86  LEU B CD1 
4593 C CD2 . LEU B 59  ? 0.8349 0.6557 0.7316 0.0530  0.1158  0.0576  86  LEU B CD2 
4594 N N   . TRP B 60  ? 0.9692 0.7608 0.8386 0.0614  0.1308  0.0887  87  TRP B N   
4595 C CA  . TRP B 60  ? 1.0449 0.8266 0.9117 0.0645  0.1385  0.1014  87  TRP B CA  
4596 C C   . TRP B 60  ? 1.0443 0.8150 0.9288 0.0662  0.1414  0.1057  87  TRP B C   
4597 O O   . TRP B 60  ? 1.0827 0.8493 0.9830 0.0603  0.1436  0.0978  87  TRP B O   
4598 C CB  . TRP B 60  ? 0.9557 0.7351 0.8219 0.0584  0.1463  0.1001  87  TRP B CB  
4599 C CG  . TRP B 60  ? 0.9941 0.7664 0.8561 0.0600  0.1562  0.1131  87  TRP B CG  
4600 C CD1 . TRP B 60  ? 1.0045 0.7799 0.8470 0.0630  0.1603  0.1195  87  TRP B CD1 
4601 C CD2 . TRP B 60  ? 1.0446 0.8046 0.9216 0.0576  0.1643  0.1213  87  TRP B CD2 
4602 N NE1 . TRP B 60  ? 0.9739 0.7410 0.8179 0.0624  0.1716  0.1322  87  TRP B NE1 
4603 C CE2 . TRP B 60  ? 1.0064 0.7631 0.8724 0.0585  0.1740  0.1337  87  TRP B CE2 
4604 C CE3 . TRP B 60  ? 1.0582 0.8086 0.9561 0.0543  0.1647  0.1186  87  TRP B CE3 
4605 C CZ2 . TRP B 60  ? 0.9538 0.6978 0.8305 0.0550  0.1844  0.1448  87  TRP B CZ2 
4606 C CZ3 . TRP B 60  ? 1.0521 0.7886 0.9608 0.0513  0.1738  0.1282  87  TRP B CZ3 
4607 C CH2 . TRP B 60  ? 0.9596 0.6928 0.8583 0.0511  0.1837  0.1417  87  TRP B CH2 
4608 N N   . VAL B 61  ? 1.0611 0.8257 0.9416 0.0748  0.1408  0.1177  88  VAL B N   
4609 C CA  . VAL B 61  ? 1.0269 0.7789 0.9232 0.0788  0.1421  0.1217  88  VAL B CA  
4610 C C   . VAL B 61  ? 1.0520 0.7869 0.9423 0.0823  0.1493  0.1390  88  VAL B C   
4611 O O   . VAL B 61  ? 1.1353 0.8718 1.0057 0.0884  0.1483  0.1502  88  VAL B O   
4612 C CB  . VAL B 61  ? 0.9605 0.7214 0.8606 0.0882  0.1325  0.1191  88  VAL B CB  
4613 C CG1 . VAL B 61  ? 0.9695 0.7148 0.8850 0.0948  0.1343  0.1238  88  VAL B CG1 
4614 C CG2 . VAL B 61  ? 0.9384 0.7156 0.8454 0.0828  0.1276  0.1027  88  VAL B CG2 
4615 N N   . ALA B 62  ? 0.9337 0.6514 0.8401 0.0781  0.1566  0.1411  89  ALA B N   
4616 C CA  . ALA B 62  ? 1.0471 0.7445 0.9503 0.0798  0.1648  0.1583  89  ALA B CA  
4617 C C   . ALA B 62  ? 1.0826 0.7601 1.0048 0.0821  0.1655  0.1584  89  ALA B C   
4618 O O   . ALA B 62  ? 1.0818 0.7577 1.0226 0.0750  0.1663  0.1447  89  ALA B O   
4619 C CB  . ALA B 62  ? 1.0117 0.7066 0.9158 0.0682  0.1766  0.1614  89  ALA B CB  
4620 N N   . THR B 63  ? 1.0631 0.7242 0.9790 0.0927  0.1647  0.1735  90  THR B N   
4621 C CA  . THR B 63  ? 1.1316 0.7699 1.0642 0.0972  0.1652  0.1746  90  THR B CA  
4622 C C   . THR B 63  ? 1.1319 0.7427 1.0551 0.1013  0.1717  0.1968  90  THR B C   
4623 O O   . THR B 63  ? 1.1478 0.7607 1.0478 0.1077  0.1710  0.2122  90  THR B O   
4624 C CB  . THR B 63  ? 1.1172 0.7651 1.0561 0.1108  0.1538  0.1667  90  THR B CB  
4625 O OG1 . THR B 63  ? 1.1492 0.7737 1.1055 0.1159  0.1551  0.1656  90  THR B OG1 
4626 C CG2 . THR B 63  ? 1.0202 0.6769 0.9396 0.1250  0.1452  0.1796  90  THR B CG2 
4627 N N   . ASP B 64  ? 1.1373 0.7208 1.0771 0.0970  0.1782  0.1984  91  ASP B N   
4628 C CA  . ASP B 64  ? 1.0528 0.6047 0.9858 0.0981  0.1864  0.2200  91  ASP B CA  
4629 C C   . ASP B 64  ? 1.1192 0.6417 1.0761 0.0932  0.1908  0.2149  91  ASP B C   
4630 O O   . ASP B 64  ? 1.0852 0.6145 1.0621 0.0863  0.1892  0.1943  91  ASP B O   
4631 C CB  . ASP B 64  ? 1.1506 0.7042 1.0712 0.0854  0.1986  0.2316  91  ASP B CB  
4632 C CG  . ASP B 64  ? 1.1995 0.7695 1.1375 0.0679  0.2044  0.2148  91  ASP B CG  
4633 O OD1 . ASP B 64  ? 1.1318 0.6855 1.0920 0.0567  0.2107  0.2094  91  ASP B OD1 
4634 O OD2 . ASP B 64  ? 1.0508 0.6495 0.9807 0.0659  0.2018  0.2065  91  ASP B OD2 
4635 N N   . HIS B 65  ? 1.2309 0.7188 1.1835 0.0968  0.1964  0.2340  92  HIS B N   
4636 C CA  . HIS B 65  ? 1.2685 0.7215 1.2420 0.0926  0.2010  0.2313  92  HIS B CA  
4637 C C   . HIS B 65  ? 1.2826 0.7372 1.2725 0.1040  0.1907  0.2123  92  HIS B C   
4638 O O   . HIS B 65  ? 1.3179 0.7675 1.3288 0.0951  0.1921  0.1936  92  HIS B O   
4639 C CB  . HIS B 65  ? 1.1797 0.6300 1.1711 0.0693  0.2120  0.2226  92  HIS B CB  
4640 C CG  . HIS B 65  ? 1.1605 0.6102 1.1402 0.0572  0.2247  0.2405  92  HIS B CG  
4641 N ND1 . HIS B 65  ? 1.1184 0.6021 1.0865 0.0523  0.2264  0.2392  92  HIS B ND1 
4642 C CD2 . HIS B 65  ? 1.2492 0.6683 1.2272 0.0489  0.2373  0.2601  92  HIS B CD2 
4643 C CE1 . HIS B 65  ? 1.1720 0.6483 1.1320 0.0422  0.2401  0.2564  92  HIS B CE1 
4644 N NE2 . HIS B 65  ? 1.1412 0.5788 1.1068 0.0392  0.2473  0.2699  92  HIS B NE2 
4645 N N   . ASN B 66  ? 1.2915 0.7545 1.2716 0.1242  0.1801  0.2165  93  ASN B N   
4646 C CA  . ASN B 66  ? 1.2374 0.7094 1.2328 0.1366  0.1710  0.1983  93  ASN B CA  
4647 C C   . ASN B 66  ? 1.3565 0.7918 1.3592 0.1521  0.1692  0.2061  93  ASN B C   
4648 O O   . ASN B 66  ? 1.3111 0.7286 1.2986 0.1644  0.1672  0.2287  93  ASN B O   
4649 C CB  . ASN B 66  ? 1.2794 0.7901 1.2650 0.1485  0.1599  0.1946  93  ASN B CB  
4650 C CG  . ASN B 66  ? 1.2014 0.7467 1.1830 0.1343  0.1606  0.1820  93  ASN B CG  
4651 O OD1 . ASN B 66  ? 1.2462 0.8018 1.2423 0.1247  0.1619  0.1619  93  ASN B OD1 
4652 N ND2 . ASN B 66  ? 1.2200 0.7818 1.1803 0.1334  0.1593  0.1937  93  ASN B ND2 
4653 N N   . MET B 67  ? 1.3870 0.8100 1.4115 0.1523  0.1698  0.1873  94  MET B N   
4654 C CA  . MET B 67  ? 1.3647 0.7569 1.3994 0.1703  0.1666  0.1890  94  MET B CA  
4655 C C   . MET B 67  ? 1.3019 0.7213 1.3453 0.1901  0.1562  0.1756  94  MET B C   
4656 O O   . MET B 67  ? 1.3441 0.7479 1.3906 0.2114  0.1503  0.1834  94  MET B O   
4657 C CB  . MET B 67  ? 1.2130 0.5714 1.2667 0.1593  0.1742  0.1755  94  MET B CB  
4658 C CG  . MET B 67  ? 1.3144 0.6329 1.3641 0.1450  0.1843  0.1932  94  MET B CG  
4659 S SD  . MET B 67  ? 1.5495 0.8196 1.5885 0.1650  0.1833  0.2225  94  MET B SD  
4660 C CE  . MET B 67  ? 1.5787 0.8094 1.6137 0.1401  0.1986  0.2410  94  MET B CE  
4661 N N   . ASP B 68  ? 1.2137 0.6733 1.2617 0.1836  0.1539  0.1560  95  ASP B N   
4662 C CA  . ASP B 68  ? 1.3243 0.8164 1.3805 0.1997  0.1453  0.1442  95  ASP B CA  
4663 C C   . ASP B 68  ? 1.2796 0.8056 1.3192 0.2039  0.1374  0.1560  95  ASP B C   
4664 O O   . ASP B 68  ? 1.3317 0.8543 1.3518 0.1955  0.1390  0.1728  95  ASP B O   
4665 C CB  . ASP B 68  ? 1.0421 0.5561 1.1119 0.1901  0.1483  0.1162  95  ASP B CB  
4666 C CG  . ASP B 68  ? 1.2158 0.7508 1.2755 0.1678  0.1518  0.1108  95  ASP B CG  
4667 O OD1 . ASP B 68  ? 1.2248 0.7595 1.2687 0.1600  0.1526  0.1275  95  ASP B OD1 
4668 O OD2 . ASP B 68  ? 1.2534 0.8049 1.3200 0.1588  0.1539  0.0899  95  ASP B OD2 
4669 N N   . ASN B 69  ? 1.1986 0.7587 1.2466 0.2163  0.1290  0.1463  96  ASN B N   
4670 C CA  . ASN B 69  ? 1.2829 0.8767 1.3171 0.2202  0.1199  0.1547  96  ASN B CA  
4671 C C   . ASN B 69  ? 1.2376 0.8630 1.2659 0.2011  0.1223  0.1421  96  ASN B C   
4672 O O   . ASN B 69  ? 1.2336 0.8956 1.2652 0.2031  0.1159  0.1329  96  ASN B O   
4673 C CB  . ASN B 69  ? 1.1824 0.7989 1.2308 0.2426  0.1088  0.1513  96  ASN B CB  
4674 C CG  . ASN B 69  ? 1.2324 0.8729 1.3048 0.2425  0.1113  0.1256  96  ASN B CG  
4675 O OD1 . ASN B 69  ? 1.1948 0.8274 1.2722 0.2281  0.1210  0.1108  96  ASN B OD1 
4676 N ND2 . ASN B 69  ? 1.3203 0.9918 1.4076 0.2586  0.1026  0.1200  96  ASN B ND2 
4677 N N   . THR B 70  ? 1.2519 0.8626 1.2725 0.1821  0.1315  0.1417  97  THR B N   
4678 C CA  . THR B 70  ? 1.1185 0.7549 1.1331 0.1647  0.1337  0.1304  97  THR B CA  
4679 C C   . THR B 70  ? 1.0796 0.7406 1.0753 0.1652  0.1269  0.1402  97  THR B C   
4680 O O   . THR B 70  ? 1.1398 0.8321 1.1354 0.1609  0.1228  0.1289  97  THR B O   
4681 C CB  . THR B 70  ? 1.1853 0.8009 1.1971 0.1463  0.1437  0.1297  97  THR B CB  
4682 O OG1 . THR B 70  ? 1.1347 0.7300 1.1640 0.1444  0.1488  0.1165  97  THR B OG1 
4683 C CG2 . THR B 70  ? 1.0334 0.6742 1.0376 0.1303  0.1450  0.1200  97  THR B CG2 
4684 N N   . SER B 71  ? 1.0462 0.6921 1.0241 0.1700  0.1257  0.1613  98  SER B N   
4685 C CA  . SER B 71  ? 1.1511 0.8184 1.1076 0.1702  0.1194  0.1699  98  SER B CA  
4686 C C   . SER B 71  ? 1.1706 0.8665 1.1315 0.1849  0.1059  0.1662  98  SER B C   
4687 O O   . SER B 71  ? 1.2129 0.9359 1.1630 0.1814  0.0996  0.1630  98  SER B O   
4688 C CB  . SER B 71  ? 1.1323 0.7758 1.0661 0.1730  0.1221  0.1938  98  SER B CB  
4689 O OG  . SER B 71  ? 1.3407 0.9802 1.2679 0.1929  0.1119  0.2077  98  SER B OG  
4690 N N   . THR B 72  ? 1.1532 0.8440 1.1314 0.2013  0.1011  0.1657  99  THR B N   
4691 C CA  . THR B 72  ? 1.0728 0.7953 1.0612 0.2152  0.0883  0.1603  99  THR B CA  
4692 C C   . THR B 72  ? 1.0971 0.8521 1.1015 0.2048  0.0894  0.1376  99  THR B C   
4693 O O   . THR B 72  ? 1.1270 0.9146 1.1298 0.2042  0.0809  0.1328  99  THR B O   
4694 C CB  . THR B 72  ? 1.2189 0.9282 1.2251 0.2366  0.0838  0.1643  99  THR B CB  
4695 O OG1 . THR B 72  ? 1.2379 0.9056 1.2301 0.2422  0.0873  0.1845  99  THR B OG1 
4696 C CG2 . THR B 72  ? 1.0778 0.8180 1.0892 0.2542  0.0677  0.1664  99  THR B CG2 
4697 N N   . VAL B 73  ? 1.0651 0.8109 1.0836 0.1959  0.0998  0.1237  100 VAL B N   
4698 C CA  . VAL B 73  ? 0.9976 0.7706 1.0273 0.1848  0.1026  0.1035  100 VAL B CA  
4699 C C   . VAL B 73  ? 1.0755 0.8626 1.0864 0.1681  0.1024  0.1027  100 VAL B C   
4700 O O   . VAL B 73  ? 1.1439 0.9612 1.1575 0.1637  0.0978  0.0934  100 VAL B O   
4701 C CB  . VAL B 73  ? 0.9548 0.7107 0.9972 0.1781  0.1138  0.0900  100 VAL B CB  
4702 C CG1 . VAL B 73  ? 1.0797 0.8616 1.1288 0.1662  0.1174  0.0709  100 VAL B CG1 
4703 C CG2 . VAL B 73  ? 0.9425 0.6834 1.0040 0.1958  0.1141  0.0888  100 VAL B CG2 
4704 N N   . LEU B 74  ? 1.0627 0.8278 1.0553 0.1587  0.1078  0.1121  101 LEU B N   
4705 C CA  . LEU B 74  ? 1.1207 0.8967 1.0951 0.1447  0.1080  0.1114  101 LEU B CA  
4706 C C   . LEU B 74  ? 1.1714 0.9681 1.1328 0.1508  0.0968  0.1182  101 LEU B C   
4707 O O   . LEU B 74  ? 1.1208 0.9396 1.0773 0.1423  0.0933  0.1095  101 LEU B O   
4708 C CB  . LEU B 74  ? 1.0742 0.8244 1.0344 0.1358  0.1164  0.1212  101 LEU B CB  
4709 C CG  . LEU B 74  ? 1.0384 0.7739 1.0077 0.1234  0.1264  0.1114  101 LEU B CG  
4710 C CD1 . LEU B 74  ? 1.1322 0.8471 1.0901 0.1153  0.1338  0.1226  101 LEU B CD1 
4711 C CD2 . LEU B 74  ? 1.0241 0.7799 0.9950 0.1118  0.1266  0.0949  101 LEU B CD2 
4712 N N   . ARG B 75  ? 1.1093 0.8978 1.0637 0.1655  0.0905  0.1336  102 ARG B N   
4713 C CA  . ARG B 75  ? 1.1612 0.9686 1.1002 0.1720  0.0782  0.1403  102 ARG B CA  
4714 C C   . ARG B 75  ? 1.1858 1.0287 1.1424 0.1743  0.0686  0.1262  102 ARG B C   
4715 O O   . ARG B 75  ? 1.1565 1.0208 1.1034 0.1678  0.0619  0.1212  102 ARG B O   
4716 C CB  . ARG B 75  ? 1.1017 0.8925 1.0300 0.1894  0.0723  0.1600  102 ARG B CB  
4717 C CG  . ARG B 75  ? 1.1967 0.9982 1.0979 0.1941  0.0616  0.1706  102 ARG B CG  
4718 C CD  . ARG B 75  ? 1.4651 1.2423 1.3483 0.2093  0.0586  0.1934  102 ARG B CD  
4719 N NE  . ARG B 75  ? 1.6596 1.4021 1.5304 0.2017  0.0737  0.2052  102 ARG B NE  
4720 C CZ  . ARG B 75  ? 1.6818 1.3952 1.5647 0.2058  0.0814  0.2121  102 ARG B CZ  
4721 N NH1 . ARG B 75  ? 1.5090 1.2218 1.4159 0.2191  0.0760  0.2083  102 ARG B NH1 
4722 N NH2 . ARG B 75  ? 1.6266 1.3109 1.4986 0.1963  0.0952  0.2225  102 ARG B NH2 
4723 N N   . GLU B 76  ? 1.1207 0.9705 1.1045 0.1829  0.0686  0.1187  103 GLU B N   
4724 C CA  . GLU B 76  ? 1.0890 0.9754 1.0941 0.1840  0.0617  0.1045  103 GLU B CA  
4725 C C   . GLU B 76  ? 1.1842 1.0845 1.1896 0.1639  0.0681  0.0893  103 GLU B C   
4726 O O   . GLU B 76  ? 1.1476 1.0758 1.1551 0.1582  0.0609  0.0818  103 GLU B O   
4727 C CB  . GLU B 76  ? 1.0756 0.9655 1.1106 0.1971  0.0636  0.0983  103 GLU B CB  
4728 C CG  . GLU B 76  ? 1.4355 1.3218 1.4761 0.2203  0.0530  0.1111  103 GLU B CG  
4729 C CD  . GLU B 76  ? 1.5149 1.4131 1.5893 0.2343  0.0537  0.1013  103 GLU B CD  
4730 O OE1 . GLU B 76  ? 1.1659 1.0893 1.2602 0.2260  0.0591  0.0836  103 GLU B OE1 
4731 O OE2 . GLU B 76  ? 1.5369 1.4184 1.6173 0.2538  0.0496  0.1115  103 GLU B OE2 
4732 N N   . TRP B 77  ? 1.0602 0.9405 1.0636 0.1529  0.0808  0.0845  104 TRP B N   
4733 C CA  . TRP B 77  ? 1.1152 1.0053 1.1171 0.1350  0.0867  0.0712  104 TRP B CA  
4734 C C   . TRP B 77  ? 1.1045 0.9969 1.0826 0.1246  0.0826  0.0744  104 TRP B C   
4735 O O   . TRP B 77  ? 1.1225 1.0338 1.1007 0.1140  0.0804  0.0647  104 TRP B O   
4736 C CB  . TRP B 77  ? 1.2005 1.0675 1.2032 0.1272  0.0993  0.0664  104 TRP B CB  
4737 C CG  . TRP B 77  ? 1.0481 0.9216 1.0463 0.1101  0.1049  0.0544  104 TRP B CG  
4738 C CD1 . TRP B 77  ? 1.0921 0.9839 1.1036 0.1044  0.1083  0.0409  104 TRP B CD1 
4739 C CD2 . TRP B 77  ? 1.1202 0.9810 1.0986 0.0973  0.1079  0.0557  104 TRP B CD2 
4740 N NE1 . TRP B 77  ? 1.1731 1.0619 1.1718 0.0886  0.1128  0.0348  104 TRP B NE1 
4741 C CE2 . TRP B 77  ? 1.0367 0.9069 1.0161 0.0848  0.1119  0.0433  104 TRP B CE2 
4742 C CE3 . TRP B 77  ? 1.0857 0.9287 1.0459 0.0955  0.1083  0.0662  104 TRP B CE3 
4743 C CZ2 . TRP B 77  ? 1.0565 0.9175 1.0195 0.0721  0.1146  0.0414  104 TRP B CZ2 
4744 C CZ3 . TRP B 77  ? 1.0710 0.9080 1.0177 0.0829  0.1118  0.0629  104 TRP B CZ3 
4745 C CH2 . TRP B 77  ? 1.0677 0.9128 1.0158 0.0720  0.1140  0.0507  104 TRP B CH2 
4746 N N   . LEU B 78  ? 1.1103 0.9829 1.0677 0.1274  0.0822  0.0876  105 LEU B N   
4747 C CA  . LEU B 78  ? 1.1372 1.0111 1.0707 0.1193  0.0791  0.0899  105 LEU B CA  
4748 C C   . LEU B 78  ? 1.1497 1.0495 1.0808 0.1229  0.0656  0.0878  105 LEU B C   
4749 O O   . LEU B 78  ? 1.1828 1.0942 1.1060 0.1119  0.0627  0.0794  105 LEU B O   
4750 C CB  . LEU B 78  ? 1.0948 0.9443 1.0073 0.1229  0.0829  0.1051  105 LEU B CB  
4751 C CG  . LEU B 78  ? 1.0456 0.8724 0.9572 0.1138  0.0959  0.1051  105 LEU B CG  
4752 C CD1 . LEU B 78  ? 1.0892 0.8958 0.9825 0.1168  0.1005  0.1208  105 LEU B CD1 
4753 C CD2 . LEU B 78  ? 0.8814 0.7143 0.7888 0.0990  0.0991  0.0930  105 LEU B CD2 
4754 N N   . VAL B 79  ? 1.1842 1.0925 1.1221 0.1384  0.0563  0.0951  106 VAL B N   
4755 C CA  . VAL B 79  ? 1.1763 1.1127 1.1151 0.1427  0.0412  0.0922  106 VAL B CA  
4756 C C   . VAL B 79  ? 1.0571 1.0205 1.0178 0.1315  0.0405  0.0749  106 VAL B C   
4757 O O   . VAL B 79  ? 1.1740 1.1560 1.1297 0.1238  0.0321  0.0679  106 VAL B O   
4758 C CB  . VAL B 79  ? 1.0453 0.9875 0.9930 0.1633  0.0309  0.1024  106 VAL B CB  
4759 C CG1 . VAL B 79  ? 0.8697 0.8479 0.8276 0.1676  0.0141  0.0958  106 VAL B CG1 
4760 C CG2 . VAL B 79  ? 1.0173 0.9331 0.9367 0.1729  0.0303  0.1213  106 VAL B CG2 
4761 N N   . ALA B 80  ? 0.9850 0.9496 0.9689 0.1294  0.0501  0.0675  107 ALA B N   
4762 C CA  . ALA B 80  ? 1.0533 1.0441 1.0585 0.1189  0.0515  0.0522  107 ALA B CA  
4763 C C   . ALA B 80  ? 1.0075 0.9921 0.9980 0.0989  0.0575  0.0446  107 ALA B C   
4764 O O   . ALA B 80  ? 1.1119 1.1179 1.1116 0.0879  0.0550  0.0341  107 ALA B O   
4765 C CB  . ALA B 80  ? 1.0301 1.0231 1.0611 0.1233  0.0613  0.0464  107 ALA B CB  
4766 N N   . VAL B 81  ? 0.9657 0.9214 0.9348 0.0939  0.0652  0.0496  108 VAL B N   
4767 C CA  . VAL B 81  ? 1.1062 1.0532 1.0624 0.0771  0.0712  0.0428  108 VAL B CA  
4768 C C   . VAL B 81  ? 1.0748 1.0091 1.0030 0.0742  0.0669  0.0478  108 VAL B C   
4769 O O   . VAL B 81  ? 1.1859 1.1091 1.1012 0.0624  0.0713  0.0432  108 VAL B O   
4770 C CB  . VAL B 81  ? 1.0701 0.9972 1.0278 0.0723  0.0843  0.0410  108 VAL B CB  
4771 C CG1 . VAL B 81  ? 1.0171 0.9553 1.0001 0.0770  0.0894  0.0352  108 VAL B CG1 
4772 C CG2 . VAL B 81  ? 1.1124 1.0133 1.0560 0.0786  0.0882  0.0519  108 VAL B CG2 
4773 N N   . LYS B 82  ? 1.0506 0.9858 0.9679 0.0855  0.0583  0.0570  109 LYS B N   
4774 C CA  . LYS B 82  ? 1.0693 0.9910 0.9575 0.0844  0.0563  0.0621  109 LYS B CA  
4775 C C   . LYS B 82  ? 1.0986 1.0287 0.9772 0.0719  0.0510  0.0511  109 LYS B C   
4776 O O   . LYS B 82  ? 1.1985 1.1126 1.0587 0.0647  0.0557  0.0495  109 LYS B O   
4777 C CB  . LYS B 82  ? 0.9995 0.9229 0.8757 0.0992  0.0474  0.0741  109 LYS B CB  
4778 C CG  . LYS B 82  ? 1.0495 0.9571 0.8933 0.1001  0.0481  0.0814  109 LYS B CG  
4779 C CD  . LYS B 82  ? 1.3839 1.2912 1.2135 0.1156  0.0403  0.0954  109 LYS B CD  
4780 C CE  . LYS B 82  ? 1.3906 1.2801 1.1867 0.1170  0.0450  0.1044  109 LYS B CE  
4781 N NZ  . LYS B 82  ? 1.3582 1.2546 1.1336 0.1098  0.0390  0.0942  109 LYS B NZ  
4782 N N   . SER B 83  ? 1.0992 1.0543 0.9918 0.0690  0.0412  0.0430  110 SER B N   
4783 C CA  . SER B 83  ? 1.0738 1.0357 0.9572 0.0566  0.0347  0.0323  110 SER B CA  
4784 C C   . SER B 83  ? 1.1842 1.1359 1.0703 0.0407  0.0443  0.0237  110 SER B C   
4785 O O   . SER B 83  ? 1.3335 1.2812 1.2073 0.0299  0.0411  0.0161  110 SER B O   
4786 C CB  . SER B 83  ? 1.2037 1.1976 1.1053 0.0565  0.0214  0.0254  110 SER B CB  
4787 O OG  . SER B 83  ? 1.4302 1.4408 1.3623 0.0503  0.0265  0.0188  110 SER B OG  
4788 N N   . LEU B 84  ? 1.1679 1.1136 1.0679 0.0392  0.0554  0.0247  111 LEU B N   
4789 C CA  . LEU B 84  ? 1.1289 1.0643 1.0289 0.0249  0.0638  0.0178  111 LEU B CA  
4790 C C   . LEU B 84  ? 1.2008 1.1081 1.0785 0.0231  0.0700  0.0209  111 LEU B C   
4791 O O   . LEU B 84  ? 1.2581 1.1540 1.1306 0.0121  0.0748  0.0158  111 LEU B O   
4792 C CB  . LEU B 84  ? 1.1470 1.0886 1.0687 0.0240  0.0730  0.0163  111 LEU B CB  
4793 C CG  . LEU B 84  ? 1.2526 1.2238 1.2015 0.0287  0.0692  0.0133  111 LEU B CG  
4794 C CD1 . LEU B 84  ? 1.1836 1.1579 1.1504 0.0273  0.0807  0.0101  111 LEU B CD1 
4795 C CD2 . LEU B 84  ? 1.3486 1.3418 1.3050 0.0181  0.0610  0.0046  111 LEU B CD2 
4796 N N   . TYR B 85  ? 1.1169 1.0132 0.9817 0.0338  0.0704  0.0296  112 TYR B N   
4797 C CA  . TYR B 85  ? 1.0460 0.9196 0.8960 0.0335  0.0779  0.0328  112 TYR B CA  
4798 C C   . TYR B 85  ? 1.0502 0.9161 0.8765 0.0357  0.0739  0.0335  112 TYR B C   
4799 O O   . TYR B 85  ? 1.2486 1.1249 1.0673 0.0404  0.0654  0.0341  112 TYR B O   
4800 C CB  . TYR B 85  ? 1.0358 0.9016 0.8928 0.0424  0.0851  0.0420  112 TYR B CB  
4801 C CG  . TYR B 85  ? 1.0038 0.8705 0.8796 0.0390  0.0913  0.0389  112 TYR B CG  
4802 C CD1 . TYR B 85  ? 0.9925 0.8763 0.8873 0.0415  0.0893  0.0367  112 TYR B CD1 
4803 C CD2 . TYR B 85  ? 1.0644 0.9161 0.9384 0.0338  0.0987  0.0372  112 TYR B CD2 
4804 C CE1 . TYR B 85  ? 1.0708 0.9556 0.9807 0.0388  0.0961  0.0325  112 TYR B CE1 
4805 C CE2 . TYR B 85  ? 1.0241 0.8760 0.9114 0.0307  0.1039  0.0333  112 TYR B CE2 
4806 C CZ  . TYR B 85  ? 1.1091 0.9771 1.0136 0.0331  0.1034  0.0308  112 TYR B CZ  
4807 O OH  . TYR B 85  ? 0.9506 0.8189 0.8665 0.0305  0.1098  0.0258  112 TYR B OH  
4808 N N   . HIS B 86  ? 1.0240 0.8721 0.8384 0.0329  0.0799  0.0326  113 HIS B N   
4809 C CA  . HIS B 86  ? 0.9914 0.8310 0.7830 0.0353  0.0782  0.0314  113 HIS B CA  
4810 C C   . HIS B 86  ? 1.0788 0.9210 0.8603 0.0470  0.0786  0.0413  113 HIS B C   
4811 O O   . HIS B 86  ? 1.0341 0.8782 0.7964 0.0504  0.0732  0.0399  113 HIS B O   
4812 C CB  . HIS B 86  ? 0.9900 0.8118 0.7755 0.0325  0.0855  0.0292  113 HIS B CB  
4813 C CG  . HIS B 86  ? 1.0054 0.8185 0.7699 0.0375  0.0868  0.0285  113 HIS B CG  
4814 N ND1 . HIS B 86  ? 1.1263 0.9323 0.8752 0.0337  0.0819  0.0188  113 HIS B ND1 
4815 C CD2 . HIS B 86  ? 1.0435 0.8535 0.8003 0.0459  0.0937  0.0357  113 HIS B CD2 
4816 C CE1 . HIS B 86  ? 1.1395 0.9391 0.8714 0.0407  0.0856  0.0192  113 HIS B CE1 
4817 N NE2 . HIS B 86  ? 1.0680 0.8711 0.8046 0.0479  0.0933  0.0299  113 HIS B NE2 
4818 N N   . SER B 87  ? 1.0674 0.9082 0.8599 0.0528  0.0851  0.0512  114 SER B N   
4819 C CA  . SER B 87  ? 1.0681 0.9090 0.8515 0.0633  0.0865  0.0630  114 SER B CA  
4820 C C   . SER B 87  ? 1.1698 1.0082 0.9725 0.0670  0.0923  0.0717  114 SER B C   
4821 O O   . SER B 87  ? 1.0495 0.8848 0.8694 0.0614  0.0966  0.0676  114 SER B O   
4822 C CB  . SER B 87  ? 1.0355 0.8656 0.7990 0.0661  0.0939  0.0664  114 SER B CB  
4823 O OG  . SER B 87  ? 1.1019 0.9219 0.8759 0.0628  0.1045  0.0672  114 SER B OG  
4824 N N   . VAL B 88  ? 1.2093 1.0473 1.0071 0.0766  0.0921  0.0838  115 VAL B N   
4825 C CA  . VAL B 88  ? 1.0349 0.8667 0.8490 0.0814  0.0973  0.0931  115 VAL B CA  
4826 C C   . VAL B 88  ? 0.9403 0.7610 0.7393 0.0887  0.1034  0.1081  115 VAL B C   
4827 O O   . VAL B 88  ? 1.1669 0.9914 0.9457 0.0958  0.0977  0.1143  115 VAL B O   
4828 C CB  . VAL B 88  ? 1.0174 0.8618 0.8469 0.0871  0.0884  0.0928  115 VAL B CB  
4829 C CG1 . VAL B 88  ? 1.0825 0.9164 0.9237 0.0953  0.0930  0.1043  115 VAL B CG1 
4830 C CG2 . VAL B 88  ? 0.8794 0.7341 0.7274 0.0784  0.0864  0.0790  115 VAL B CG2 
4831 N N   . GLU B 89  ? 1.0359 0.8430 0.8438 0.0864  0.1149  0.1138  116 GLU B N   
4832 C CA  . GLU B 89  ? 1.1093 0.9040 0.9073 0.0916  0.1231  0.1296  116 GLU B CA  
4833 C C   . GLU B 89  ? 1.1434 0.9276 0.9594 0.0958  0.1249  0.1380  116 GLU B C   
4834 O O   . GLU B 89  ? 1.0994 0.8820 0.9380 0.0913  0.1260  0.1302  116 GLU B O   
4835 C CB  . GLU B 89  ? 0.9645 0.7521 0.7603 0.0847  0.1360  0.1300  116 GLU B CB  
4836 C CG  . GLU B 89  ? 1.2453 1.0215 1.0289 0.0883  0.1465  0.1468  116 GLU B CG  
4837 C CD  . GLU B 89  ? 1.4426 1.2196 1.2170 0.0834  0.1581  0.1461  116 GLU B CD  
4838 O OE1 . GLU B 89  ? 1.3653 1.1510 1.1389 0.0795  0.1558  0.1325  116 GLU B OE1 
4839 O OE2 . GLU B 89  ? 1.3944 1.1630 1.1630 0.0836  0.1700  0.1594  116 GLU B OE2 
4840 N N   . TRP B 90  ? 1.0974 0.8726 0.9015 0.1049  0.1252  0.1539  117 TRP B N   
4841 C CA  . TRP B 90  ? 1.0917 0.8556 0.9100 0.1122  0.1240  0.1626  117 TRP B CA  
4842 C C   . TRP B 90  ? 1.1521 0.8950 0.9587 0.1149  0.1342  0.1817  117 TRP B C   
4843 O O   . TRP B 90  ? 1.1787 0.9203 0.9589 0.1216  0.1329  0.1939  117 TRP B O   
4844 C CB  . TRP B 90  ? 1.1489 0.9259 0.9651 0.1239  0.1089  0.1626  117 TRP B CB  
4845 C CG  . TRP B 90  ? 1.2196 0.9852 1.0461 0.1357  0.1057  0.1734  117 TRP B CG  
4846 C CD1 . TRP B 90  ? 1.2888 1.0526 1.1005 0.1498  0.0970  0.1872  117 TRP B CD1 
4847 C CD2 . TRP B 90  ? 1.2194 0.9730 1.0726 0.1357  0.1102  0.1706  117 TRP B CD2 
4848 N NE1 . TRP B 90  ? 1.4170 1.1675 1.2457 0.1594  0.0960  0.1939  117 TRP B NE1 
4849 C CE2 . TRP B 90  ? 1.1706 0.9141 1.0249 0.1507  0.1044  0.1833  117 TRP B CE2 
4850 C CE3 . TRP B 90  ? 1.1634 0.9128 1.0380 0.1251  0.1180  0.1584  117 TRP B CE3 
4851 C CZ2 . TRP B 90  ? 1.2101 0.9385 1.0874 0.1555  0.1070  0.1831  117 TRP B CZ2 
4852 C CZ3 . TRP B 90  ? 1.2017 0.9372 1.0975 0.1291  0.1203  0.1577  117 TRP B CZ3 
4853 C CH2 . TRP B 90  ? 1.1770 0.9015 1.0745 0.1442  0.1153  0.1696  117 TRP B CH2 
4854 N N   . ARG B 91  ? 1.1550 0.8809 0.9802 0.1090  0.1446  0.1843  118 ARG B N   
4855 C CA  . ARG B 91  ? 1.2945 0.9987 1.1126 0.1078  0.1569  0.2019  118 ARG B CA  
4856 C C   . ARG B 91  ? 1.2012 0.8834 1.0374 0.1119  0.1579  0.2089  118 ARG B C   
4857 O O   . ARG B 91  ? 1.2613 0.9322 1.1195 0.1027  0.1657  0.2037  118 ARG B O   
4858 C CB  . ARG B 91  ? 1.2684 0.9726 1.0927 0.0937  0.1707  0.1978  118 ARG B CB  
4859 C CG  . ARG B 91  ? 1.4395 1.1621 1.2446 0.0912  0.1714  0.1918  118 ARG B CG  
4860 C CD  . ARG B 91  ? 1.4011 1.1252 1.2157 0.0792  0.1852  0.1881  118 ARG B CD  
4861 N NE  . ARG B 91  ? 1.5782 1.2842 1.3989 0.0746  0.1990  0.2032  118 ARG B NE  
4862 C CZ  . ARG B 91  ? 1.5297 1.2370 1.3577 0.0646  0.2134  0.2047  118 ARG B CZ  
4863 N NH1 . ARG B 91  ? 1.2938 1.0197 1.1232 0.0601  0.2156  0.1923  118 ARG B NH1 
4864 N NH2 . ARG B 91  ? 1.1729 0.8625 1.0083 0.0590  0.2260  0.2190  118 ARG B NH2 
4865 N N   . PRO B 92  ? 1.2330 0.9082 1.0605 0.1263  0.1492  0.2200  119 PRO B N   
4866 C CA  . PRO B 92  ? 1.2901 0.9404 1.1330 0.1324  0.1501  0.2279  119 PRO B CA  
4867 C C   . PRO B 92  ? 1.1909 0.8121 1.0188 0.1329  0.1608  0.2512  119 PRO B C   
4868 O O   . PRO B 92  ? 1.2372 0.8594 1.0378 0.1327  0.1653  0.2640  119 PRO B O   
4869 C CB  . PRO B 92  ? 1.2243 0.8854 1.0662 0.1496  0.1338  0.2274  119 PRO B CB  
4870 C CG  . PRO B 92  ? 1.2276 0.9074 1.0402 0.1539  0.1267  0.2322  119 PRO B CG  
4871 C CD  . PRO B 92  ? 1.2576 0.9497 1.0642 0.1385  0.1354  0.2225  119 PRO B CD  
4872 N N   . ALA B 93  ? 1.2127 0.8064 1.0581 0.1333  0.1655  0.2565  120 ALA B N   
4873 C CA  . ALA B 93  ? 1.2885 0.8490 1.1221 0.1331  0.1761  0.2798  120 ALA B CA  
4874 C C   . ALA B 93  ? 1.3663 0.8983 1.2175 0.1423  0.1727  0.2835  120 ALA B C   
4875 O O   . ALA B 93  ? 1.4381 0.9573 1.3159 0.1329  0.1786  0.2727  120 ALA B O   
4876 C CB  . ALA B 93  ? 1.1987 0.7527 1.0387 0.1132  0.1939  0.2804  120 ALA B CB  
4877 N N   . GLU B 94  ? 1.4017 0.9236 1.2377 0.1614  0.1624  0.2982  121 GLU B N   
4878 C CA  . GLU B 94  ? 1.4410 0.9387 1.2945 0.1743  0.1566  0.2998  121 GLU B CA  
4879 C C   . GLU B 94  ? 1.3961 0.8500 1.2569 0.1659  0.1706  0.3124  121 GLU B C   
4880 O O   . GLU B 94  ? 1.5425 0.9804 1.4308 0.1627  0.1728  0.3003  121 GLU B O   
4881 C CB  . GLU B 94  ? 1.3887 0.8865 1.2232 0.1981  0.1415  0.3144  121 GLU B CB  
4882 C CG  . GLU B 94  ? 1.6636 1.2055 1.4938 0.2057  0.1264  0.3011  121 GLU B CG  
4883 C CD  . GLU B 94  ? 1.6581 1.2237 1.5216 0.2035  0.1215  0.2737  121 GLU B CD  
4884 O OE1 . GLU B 94  ? 1.5672 1.1174 1.4539 0.2118  0.1198  0.2688  121 GLU B OE1 
4885 O OE2 . GLU B 94  ? 1.4434 1.0414 1.3087 0.1936  0.1201  0.2573  121 GLU B OE2 
4886 N N   . GLU B 95  ? 1.4060 0.8394 1.2419 0.1616  0.1808  0.3362  122 GLU B N   
4887 C CA  . GLU B 95  ? 1.4796 0.8695 1.3214 0.1521  0.1950  0.3504  122 GLU B CA  
4888 C C   . GLU B 95  ? 1.4256 0.8200 1.2680 0.1276  0.2132  0.3509  122 GLU B C   
4889 O O   . GLU B 95  ? 1.4518 0.8757 1.2768 0.1228  0.2155  0.3501  122 GLU B O   
4890 C CB  . GLU B 95  ? 1.5112 0.8662 1.3244 0.1670  0.1940  0.3815  122 GLU B CB  
4891 C CG  . GLU B 95  ? 1.6810 1.0236 1.4988 0.1924  0.1769  0.3833  122 GLU B CG  
4892 C CD  . GLU B 95  ? 1.8127 1.1164 1.6591 0.1924  0.1805  0.3790  122 GLU B CD  
4893 O OE1 . GLU B 95  ? 1.8165 1.0882 1.6686 0.1751  0.1965  0.3866  122 GLU B OE1 
4894 O OE2 . GLU B 95  ? 1.8155 1.1209 1.6796 0.2096  0.1675  0.3671  122 GLU B OE2 
4895 N N   . PRO B 96  ? 1.4064 0.7735 1.2708 0.1115  0.2262  0.3504  123 PRO B N   
4896 C CA  . PRO B 96  ? 1.3902 0.7204 1.2780 0.1138  0.2251  0.3474  123 PRO B CA  
4897 C C   . PRO B 96  ? 1.4417 0.7917 1.3598 0.1143  0.2156  0.3162  123 PRO B C   
4898 O O   . PRO B 96  ? 1.5175 0.9050 1.4430 0.1054  0.2142  0.2974  123 PRO B O   
4899 C CB  . PRO B 96  ? 1.2619 0.5642 1.1598 0.0909  0.2445  0.3566  123 PRO B CB  
4900 C CG  . PRO B 96  ? 1.3974 0.7390 1.2980 0.0734  0.2525  0.3459  123 PRO B CG  
4901 C CD  . PRO B 96  ? 1.2330 0.6065 1.1024 0.0877  0.2440  0.3510  123 PRO B CD  
4902 N N   . ARG B 97  ? 1.2949 0.6194 1.2297 0.1248  0.2093  0.3100  124 ARG B N   
4903 C CA  . ARG B 97  ? 1.4932 0.8360 1.4541 0.1262  0.2013  0.2805  124 ARG B CA  
4904 C C   . ARG B 97  ? 1.3741 0.7097 1.3610 0.1036  0.2107  0.2629  124 ARG B C   
4905 O O   . ARG B 97  ? 1.3816 0.7387 1.3862 0.1008  0.2054  0.2372  124 ARG B O   
4906 C CB  . ARG B 97  ? 1.3835 0.7051 1.3517 0.1488  0.1908  0.2791  124 ARG B CB  
4907 C CG  . ARG B 97  ? 1.3477 0.6850 1.2945 0.1725  0.1780  0.2924  124 ARG B CG  
4908 C CD  . ARG B 97  ? 1.3571 0.6810 1.3169 0.1960  0.1669  0.2873  124 ARG B CD  
4909 N NE  . ARG B 97  ? 1.6777 0.9463 1.6376 0.2018  0.1715  0.3045  124 ARG B NE  
4910 C CZ  . ARG B 97  ? 1.7801 1.0240 1.7567 0.2187  0.1659  0.2985  124 ARG B CZ  
4911 N NH1 . ARG B 97  ? 1.7702 1.0417 1.7658 0.2312  0.1564  0.2753  124 ARG B NH1 
4912 N NH2 . ARG B 97  ? 1.7168 0.9087 1.6912 0.2222  0.1698  0.3149  124 ARG B NH2 
4913 N N   . SER B 98  ? 1.4077 0.7151 1.3968 0.0870  0.2243  0.2759  125 SER B N   
4914 C CA  . SER B 98  ? 1.3509 0.6535 1.3662 0.0641  0.2325  0.2596  125 SER B CA  
4915 C C   . SER B 98  ? 1.3104 0.6103 1.3213 0.0439  0.2480  0.2759  125 SER B C   
4916 O O   . SER B 98  ? 1.4151 0.7020 1.4024 0.0481  0.2544  0.3024  125 SER B O   
4917 C CB  . SER B 98  ? 1.3663 0.6250 1.4015 0.0648  0.2324  0.2526  125 SER B CB  
4918 O OG  . SER B 98  ? 1.6484 0.8640 1.6698 0.0764  0.2350  0.2781  125 SER B OG  
4919 N N   . TYR B 99  ? 1.2634 0.5775 1.2973 0.0220  0.2542  0.2596  126 TYR B N   
4920 C CA  . TYR B 99  ? 1.3441 0.6631 1.3795 0.0017  0.2697  0.2719  126 TYR B CA  
4921 C C   . TYR B 99  ? 1.4234 0.6950 1.4662 -0.0098 0.2818  0.2887  126 TYR B C   
4922 O O   . TYR B 99  ? 1.4545 0.6996 1.5149 -0.0114 0.2763  0.2772  126 TYR B O   
4923 C CB  . TYR B 99  ? 1.2240 0.5768 1.2844 -0.0168 0.2706  0.2483  126 TYR B CB  
4924 C CG  . TYR B 99  ? 1.2734 0.6745 1.3234 -0.0092 0.2620  0.2360  126 TYR B CG  
4925 C CD1 . TYR B 99  ? 1.2776 0.6945 1.3301 0.0024  0.2469  0.2148  126 TYR B CD1 
4926 C CD2 . TYR B 99  ? 1.2217 0.6510 1.2590 -0.0140 0.2697  0.2453  126 TYR B CD2 
4927 C CE1 . TYR B 99  ? 1.1512 0.6088 1.1939 0.0080  0.2395  0.2044  126 TYR B CE1 
4928 C CE2 . TYR B 99  ? 1.1704 0.6399 1.1980 -0.0071 0.2616  0.2337  126 TYR B CE2 
4929 C CZ  . TYR B 99  ? 1.1368 0.6191 1.1672 0.0033  0.2463  0.2138  126 TYR B CZ  
4930 O OH  . TYR B 99  ? 1.2003 0.7193 1.2208 0.0088  0.2389  0.2033  126 TYR B OH  
4931 N N   . PRO B 100 ? 1.4105 0.6836 1.4382 -0.0184 0.2927  0.3101  127 PRO B N   
4932 C CA  . PRO B 100 ? 1.4301 0.6716 1.4628 -0.0311 0.2988  0.3216  127 PRO B CA  
4933 C C   . PRO B 100 ? 1.4559 0.6944 1.5262 -0.0567 0.3046  0.3041  127 PRO B C   
4934 O O   . PRO B 100 ? 1.4920 0.6992 1.5707 -0.0670 0.3069  0.3090  127 PRO B O   
4935 C CB  . PRO B 100 ? 1.3327 0.5845 1.3390 -0.0350 0.3108  0.3468  127 PRO B CB  
4936 C CG  . PRO B 100 ? 1.4782 0.7566 1.4570 -0.0153 0.3056  0.3514  127 PRO B CG  
4937 C CD  . PRO B 100 ? 1.4492 0.7493 1.4494 -0.0137 0.2991  0.3261  127 PRO B CD  
4938 N N   . ASP B 101 ? 1.4161 0.6850 1.5092 -0.0675 0.3061  0.2840  128 ASP B N   
4939 C CA  . ASP B 101 ? 1.4605 0.7310 1.5908 -0.0920 0.3099  0.2659  128 ASP B CA  
4940 C C   . ASP B 101 ? 1.5373 0.8056 1.6888 -0.0895 0.2974  0.2368  128 ASP B C   
4941 O O   . ASP B 101 ? 1.5127 0.7917 1.6948 -0.1085 0.2980  0.2174  128 ASP B O   
4942 C CB  . ASP B 101 ? 1.4827 0.7922 1.6265 -0.1100 0.3227  0.2656  128 ASP B CB  
4943 C CG  . ASP B 101 ? 1.5537 0.9010 1.6978 -0.1023 0.3175  0.2510  128 ASP B CG  
4944 O OD1 . ASP B 101 ? 1.3901 0.7424 1.5113 -0.0797 0.3042  0.2478  128 ASP B OD1 
4945 O OD2 . ASP B 101 ? 1.5430 0.9265 1.7087 -0.1172 0.3208  0.2385  128 ASP B OD2 
4946 N N   . GLU B 102 ? 1.5272 0.7836 1.6632 -0.0663 0.2859  0.2328  129 GLU B N   
4947 C CA  . GLU B 102 ? 1.2729 0.5299 1.4240 -0.0612 0.2739  0.2047  129 GLU B CA  
4948 C C   . GLU B 102 ? 1.3485 0.5640 1.5085 -0.0594 0.2678  0.1968  129 GLU B C   
4949 O O   . GLU B 102 ? 1.4908 0.6768 1.6380 -0.0540 0.2689  0.2150  129 GLU B O   
4950 C CB  . GLU B 102 ? 1.3782 0.6626 1.5068 -0.0364 0.2609  0.1993  129 GLU B CB  
4951 C CG  . GLU B 102 ? 1.3039 0.5557 1.4163 -0.0128 0.2549  0.2087  129 GLU B CG  
4952 C CD  . GLU B 102 ? 1.4213 0.7035 1.5193 0.0092  0.2412  0.1976  129 GLU B CD  
4953 O OE1 . GLU B 102 ? 1.3432 0.6691 1.4336 0.0082  0.2386  0.1931  129 GLU B OE1 
4954 O OE2 . GLU B 102 ? 1.3552 0.6176 1.4512 0.0271  0.2335  0.1929  129 GLU B OE2 
4955 N N   . GLU B 103 ? 1.4012 0.6152 1.5814 -0.0637 0.2602  0.1683  130 GLU B N   
4956 C CA  . GLU B 103 ? 1.3303 0.5084 1.5183 -0.0603 0.2526  0.1550  130 GLU B CA  
4957 C C   . GLU B 103 ? 1.4511 0.6240 1.6283 -0.0343 0.2424  0.1433  130 GLU B C   
4958 O O   . GLU B 103 ? 1.4902 0.6325 1.6698 -0.0260 0.2361  0.1343  130 GLU B O   
4959 C CB  . GLU B 103 ? 1.3001 0.4785 1.5175 -0.0836 0.2506  0.1289  130 GLU B CB  
4960 C CG  . GLU B 103 ? 1.3325 0.5156 1.5667 -0.1106 0.2605  0.1382  130 GLU B CG  
4961 C CD  . GLU B 103 ? 1.4337 0.6299 1.6990 -0.1334 0.2571  0.1109  130 GLU B CD  
4962 O OE1 . GLU B 103 ? 1.3334 0.5437 1.6035 -0.1286 0.2480  0.0864  130 GLU B OE1 
4963 O OE2 . GLU B 103 ? 1.4950 0.6881 1.7794 -0.1564 0.2630  0.1137  130 GLU B OE2 
4964 N N   . GLY B 104 ? 1.3371 0.5452 1.5014 -0.0212 0.2388  0.1419  131 GLY B N   
4965 C CA  . GLY B 104 ? 1.3359 0.5522 1.4895 0.0029  0.2279  0.1300  131 GLY B CA  
4966 C C   . GLY B 104 ? 1.2461 0.5158 1.3851 0.0104  0.2222  0.1278  131 GLY B C   
4967 O O   . GLY B 104 ? 1.3229 0.6225 1.4617 -0.0034 0.2256  0.1312  131 GLY B O   
4968 N N   . PRO B 105 ? 1.2318 0.5145 1.3597 0.0324  0.2136  0.1215  132 PRO B N   
4969 C CA  . PRO B 105 ? 1.1348 0.4662 1.2485 0.0393  0.2079  0.1198  132 PRO B CA  
4970 C C   . PRO B 105 ? 1.1895 0.5548 1.3109 0.0245  0.2047  0.0974  132 PRO B C   
4971 O O   . PRO B 105 ? 1.1658 0.5683 1.2769 0.0235  0.2027  0.0997  132 PRO B O   
4972 C CB  . PRO B 105 ? 1.1456 0.4791 1.2524 0.0641  0.1999  0.1143  132 PRO B CB  
4973 C CG  . PRO B 105 ? 1.3600 0.6552 1.4819 0.0667  0.2000  0.1002  132 PRO B CG  
4974 C CD  . PRO B 105 ? 1.2426 0.4976 1.3730 0.0513  0.2088  0.1136  132 PRO B CD  
4975 N N   . LYS B 106 ? 1.1980 0.5506 1.3361 0.0136  0.2032  0.0757  133 LYS B N   
4976 C CA  . LYS B 106 ? 1.2621 0.6447 1.4066 0.0004  0.1984  0.0540  133 LYS B CA  
4977 C C   . LYS B 106 ? 1.2978 0.6795 1.4590 -0.0236 0.2034  0.0546  133 LYS B C   
4978 O O   . LYS B 106 ? 1.2654 0.6677 1.4353 -0.0357 0.1983  0.0356  133 LYS B O   
4979 C CB  . LYS B 106 ? 1.1811 0.5559 1.3306 0.0046  0.1918  0.0266  133 LYS B CB  
4980 C CG  . LYS B 106 ? 1.1874 0.5739 1.3231 0.0271  0.1873  0.0223  133 LYS B CG  
4981 C CD  . LYS B 106 ? 1.0950 0.5263 1.2159 0.0305  0.1837  0.0261  133 LYS B CD  
4982 C CE  . LYS B 106 ? 1.2350 0.6774 1.3444 0.0523  0.1809  0.0297  133 LYS B CE  
4983 N NZ  . LYS B 106 ? 1.0381 0.5217 1.1336 0.0541  0.1774  0.0328  133 LYS B NZ  
4984 N N   . HIS B 107 ? 1.2848 0.6442 1.4506 -0.0308 0.2133  0.0762  134 HIS B N   
4985 C CA  . HIS B 107 ? 1.3235 0.6854 1.5080 -0.0543 0.2202  0.0789  134 HIS B CA  
4986 C C   . HIS B 107 ? 1.3431 0.7436 1.5190 -0.0571 0.2238  0.0920  134 HIS B C   
4987 O O   . HIS B 107 ? 1.2600 0.6633 1.4165 -0.0452 0.2281  0.1130  134 HIS B O   
4988 C CB  . HIS B 107 ? 1.3194 0.6362 1.5135 -0.0625 0.2312  0.0961  134 HIS B CB  
4989 C CG  . HIS B 107 ? 1.3572 0.6780 1.5723 -0.0877 0.2406  0.1015  134 HIS B CG  
4990 N ND1 . HIS B 107 ? 1.3427 0.6355 1.5612 -0.0968 0.2546  0.1258  134 HIS B ND1 
4991 C CD2 . HIS B 107 ? 1.3002 0.6511 1.5352 -0.1059 0.2384  0.0859  134 HIS B CD2 
4992 C CE1 . HIS B 107 ? 1.2850 0.5921 1.5264 -0.1204 0.2618  0.1243  134 HIS B CE1 
4993 N NE2 . HIS B 107 ? 1.2687 0.6120 1.5217 -0.1257 0.2514  0.0999  134 HIS B NE2 
4994 N N   . TRP B 108 ? 1.2626 0.6931 1.4529 -0.0720 0.2215  0.0789  135 TRP B N   
4995 C CA  . TRP B 108 ? 1.1754 0.6426 1.3610 -0.0753 0.2254  0.0889  135 TRP B CA  
4996 C C   . TRP B 108 ? 1.2666 0.7269 1.4707 -0.0940 0.2393  0.1033  135 TRP B C   
4997 O O   . TRP B 108 ? 1.2802 0.7549 1.5097 -0.1122 0.2400  0.0922  135 TRP B O   
4998 C CB  . TRP B 108 ? 1.0861 0.5911 1.2758 -0.0782 0.2146  0.0678  135 TRP B CB  
4999 C CG  . TRP B 108 ? 1.0608 0.5806 1.2269 -0.0598 0.2046  0.0606  135 TRP B CG  
5000 C CD1 . TRP B 108 ? 1.1262 0.6368 1.2872 -0.0517 0.1955  0.0434  135 TRP B CD1 
5001 C CD2 . TRP B 108 ? 1.0864 0.6328 1.2314 -0.0482 0.2037  0.0700  135 TRP B CD2 
5002 N NE1 . TRP B 108 ? 1.2142 0.7452 1.3536 -0.0366 0.1896  0.0423  135 TRP B NE1 
5003 C CE2 . TRP B 108 ? 1.1277 0.6800 1.2572 -0.0345 0.1938  0.0583  135 TRP B CE2 
5004 C CE3 . TRP B 108 ? 1.0858 0.6514 1.2232 -0.0484 0.2107  0.0863  135 TRP B CE3 
5005 C CZ2 . TRP B 108 ? 1.0438 0.6196 1.1523 -0.0225 0.1902  0.0626  135 TRP B CZ2 
5006 C CZ3 . TRP B 108 ? 1.0345 0.6222 1.1493 -0.0352 0.2063  0.0894  135 TRP B CZ3 
5007 C CH2 . TRP B 108 ? 1.0046 0.5967 1.1061 -0.0231 0.1959  0.0778  135 TRP B CH2 
5008 N N   . SER B 109 ? 1.1900 0.6286 1.3809 -0.0894 0.2506  0.1289  136 SER B N   
5009 C CA  . SER B 109 ? 1.2004 0.6328 1.4039 -0.1062 0.2667  0.1466  136 SER B CA  
5010 C C   . SER B 109 ? 1.3268 0.8034 1.5281 -0.1093 0.2719  0.1513  136 SER B C   
5011 O O   . SER B 109 ? 1.2520 0.7599 1.4405 -0.0980 0.2623  0.1420  136 SER B O   
5012 C CB  . SER B 109 ? 1.2699 0.6635 1.4546 -0.0986 0.2770  0.1738  136 SER B CB  
5013 O OG  . SER B 109 ? 1.3503 0.7584 1.5027 -0.0797 0.2763  0.1889  136 SER B OG  
5014 N N   . ASP B 110 ? 1.2269 0.7051 1.4409 -0.1250 0.2881  0.1662  137 ASP B N   
5015 C CA  . ASP B 110 ? 1.2462 0.7662 1.4600 -0.1278 0.2950  0.1703  137 ASP B CA  
5016 C C   . ASP B 110 ? 1.2983 0.8242 1.4734 -0.1085 0.2976  0.1884  137 ASP B C   
5017 O O   . ASP B 110 ? 1.2803 0.8417 1.4455 -0.1009 0.2939  0.1832  137 ASP B O   
5018 C CB  . ASP B 110 ? 1.2035 0.7259 1.4440 -0.1506 0.3133  0.1804  137 ASP B CB  
5019 C CG  . ASP B 110 ? 1.3941 0.9321 1.6771 -0.1703 0.3083  0.1576  137 ASP B CG  
5020 O OD1 . ASP B 110 ? 1.2841 0.8361 1.5717 -0.1647 0.2903  0.1342  137 ASP B OD1 
5021 O OD2 . ASP B 110 ? 1.4771 1.0140 1.7885 -0.1916 0.3222  0.1630  137 ASP B OD2 
5022 N N   . SER B 111 ? 1.2266 0.7173 1.3790 -0.1000 0.3032  0.2093  138 SER B N   
5023 C CA  . SER B 111 ? 1.1848 0.6805 1.2990 -0.0812 0.3035  0.2257  138 SER B CA  
5024 C C   . SER B 111 ? 1.3175 0.8290 1.4160 -0.0623 0.2847  0.2105  138 SER B C   
5025 O O   . SER B 111 ? 1.3662 0.8998 1.4404 -0.0500 0.2823  0.2148  138 SER B O   
5026 C CB  . SER B 111 ? 1.1887 0.6414 1.2823 -0.0753 0.3111  0.2512  138 SER B CB  
5027 O OG  . SER B 111 ? 1.5175 0.9555 1.6232 -0.0940 0.3305  0.2675  138 SER B OG  
5028 N N   . ARG B 112 ? 1.2896 0.7902 1.4013 -0.0604 0.2721  0.1920  139 ARG B N   
5029 C CA  . ARG B 112 ? 1.2037 0.7218 1.3032 -0.0449 0.2559  0.1763  139 ARG B CA  
5030 C C   . ARG B 112 ? 1.1654 0.7237 1.2747 -0.0503 0.2506  0.1584  139 ARG B C   
5031 O O   . ARG B 112 ? 1.0781 0.6590 1.1697 -0.0383 0.2425  0.1535  139 ARG B O   
5032 C CB  . ARG B 112 ? 1.1836 0.6768 1.2927 -0.0409 0.2460  0.1623  139 ARG B CB  
5033 C CG  . ARG B 112 ? 0.9971 0.5057 1.0933 -0.0248 0.2312  0.1476  139 ARG B CG  
5034 C CD  . ARG B 112 ? 1.1673 0.6571 1.2777 -0.0244 0.2232  0.1287  139 ARG B CD  
5035 N NE  . ARG B 112 ? 1.1728 0.6731 1.2696 -0.0077 0.2118  0.1179  139 ARG B NE  
5036 C CZ  . ARG B 112 ? 1.1012 0.5894 1.2050 -0.0032 0.2049  0.1008  139 ARG B CZ  
5037 N NH1 . ARG B 112 ? 1.2402 0.7035 1.3631 -0.0137 0.2065  0.0909  139 ARG B NH1 
5038 N NH2 . ARG B 112 ? 1.1147 0.6164 1.2061 0.0117  0.1966  0.0928  139 ARG B NH2 
5039 N N   . TYR B 113 ? 1.2791 0.8464 1.4174 -0.0682 0.2545  0.1484  140 TYR B N   
5040 C CA  . TYR B 113 ? 1.0805 0.6863 1.2294 -0.0727 0.2498  0.1336  140 TYR B CA  
5041 C C   . TYR B 113 ? 1.0963 0.7260 1.2286 -0.0677 0.2581  0.1465  140 TYR B C   
5042 O O   . TYR B 113 ? 1.0533 0.7085 1.1739 -0.0589 0.2502  0.1382  140 TYR B O   
5043 C CB  . TYR B 113 ? 1.0686 0.6803 1.2543 -0.0932 0.2530  0.1226  140 TYR B CB  
5044 C CG  . TYR B 113 ? 1.1228 0.7290 1.3243 -0.0973 0.2388  0.0992  140 TYR B CG  
5045 C CD1 . TYR B 113 ? 1.0257 0.6488 1.2157 -0.0868 0.2237  0.0827  140 TYR B CD1 
5046 C CD2 . TYR B 113 ? 1.1123 0.6949 1.3387 -0.1123 0.2410  0.0936  140 TYR B CD2 
5047 C CE1 . TYR B 113 ? 1.1126 0.7305 1.3132 -0.0903 0.2114  0.0614  140 TYR B CE1 
5048 C CE2 . TYR B 113 ? 1.1079 0.6850 1.3463 -0.1159 0.2278  0.0707  140 TYR B CE2 
5049 C CZ  . TYR B 113 ? 1.0941 0.6896 1.3184 -0.1045 0.2132  0.0548  140 TYR B CZ  
5050 O OH  . TYR B 113 ? 1.2569 0.8467 1.4894 -0.1079 0.2006  0.0322  140 TYR B OH  
5051 N N   . GLU B 114 ? 1.0687 0.6887 1.1984 -0.0733 0.2745  0.1668  141 GLU B N   
5052 C CA  . GLU B 114 ? 1.0275 0.6694 1.1397 -0.0687 0.2841  0.1787  141 GLU B CA  
5053 C C   . GLU B 114 ? 1.0808 0.7233 1.1556 -0.0486 0.2759  0.1838  141 GLU B C   
5054 O O   . GLU B 114 ? 1.1237 0.7926 1.1857 -0.0416 0.2735  0.1796  141 GLU B O   
5055 C CB  . GLU B 114 ? 1.0828 0.7104 1.1957 -0.0787 0.3046  0.2009  141 GLU B CB  
5056 C CG  . GLU B 114 ? 1.1878 0.8334 1.2756 -0.0720 0.3158  0.2149  141 GLU B CG  
5057 C CD  . GLU B 114 ? 1.2486 0.8752 1.3290 -0.0801 0.3365  0.2397  141 GLU B CD  
5058 O OE1 . GLU B 114 ? 1.2857 0.9137 1.3963 -0.0990 0.3498  0.2413  141 GLU B OE1 
5059 O OE2 . GLU B 114 ? 1.4717 1.0822 1.5159 -0.0680 0.3392  0.2579  141 GLU B OE2 
5060 N N   . HIS B 115 ? 1.0871 0.7012 1.1454 -0.0390 0.2709  0.1922  142 HIS B N   
5061 C CA  . HIS B 115 ? 1.0588 0.6749 1.0839 -0.0205 0.2627  0.1976  142 HIS B CA  
5062 C C   . HIS B 115 ? 1.0146 0.6535 1.0387 -0.0133 0.2471  0.1770  142 HIS B C   
5063 O O   . HIS B 115 ? 1.0262 0.6845 1.0302 -0.0045 0.2435  0.1763  142 HIS B O   
5064 C CB  . HIS B 115 ? 1.1834 0.7656 1.1964 -0.0110 0.2593  0.2096  142 HIS B CB  
5065 C CG  . HIS B 115 ? 1.1904 0.7763 1.1723 0.0078  0.2498  0.2153  142 HIS B CG  
5066 N ND1 . HIS B 115 ? 1.0778 0.6726 1.0315 0.0145  0.2550  0.2301  142 HIS B ND1 
5067 C CD2 . HIS B 115 ? 1.1177 0.7017 1.0934 0.0211  0.2354  0.2072  142 HIS B CD2 
5068 C CE1 . HIS B 115 ? 1.0920 0.6900 1.0241 0.0306  0.2427  0.2306  142 HIS B CE1 
5069 N NE2 . HIS B 115 ? 1.1062 0.6989 1.0527 0.0347  0.2311  0.2170  142 HIS B NE2 
5070 N N   . VAL B 116 ? 1.0804 0.7157 1.1244 -0.0174 0.2381  0.1598  143 VAL B N   
5071 C CA  . VAL B 116 ? 0.9728 0.6269 1.0140 -0.0113 0.2241  0.1414  143 VAL B CA  
5072 C C   . VAL B 116 ? 1.0502 0.7343 1.0957 -0.0160 0.2248  0.1333  143 VAL B C   
5073 O O   . VAL B 116 ? 1.1311 0.8322 1.1617 -0.0078 0.2168  0.1264  143 VAL B O   
5074 C CB  . VAL B 116 ? 1.0827 0.7252 1.1422 -0.0153 0.2158  0.1251  143 VAL B CB  
5075 C CG1 . VAL B 116 ? 0.9033 0.5658 0.9593 -0.0112 0.2032  0.1066  143 VAL B CG1 
5076 C CG2 . VAL B 116 ? 1.0714 0.6847 1.1248 -0.0068 0.2142  0.1319  143 VAL B CG2 
5077 N N   . MET B 117 ? 1.0225 0.7137 1.0897 -0.0290 0.2344  0.1339  144 MET B N   
5078 C CA  . MET B 117 ? 0.9766 0.6974 1.0497 -0.0315 0.2361  0.1274  144 MET B CA  
5079 C C   . MET B 117 ? 0.9649 0.6957 1.0105 -0.0215 0.2417  0.1386  144 MET B C   
5080 O O   . MET B 117 ? 0.9559 0.7049 0.9903 -0.0143 0.2349  0.1303  144 MET B O   
5081 C CB  . MET B 117 ? 1.0340 0.7626 1.1385 -0.0473 0.2471  0.1274  144 MET B CB  
5082 C CG  . MET B 117 ? 0.9768 0.7062 1.1103 -0.0576 0.2381  0.1100  144 MET B CG  
5083 S SD  . MET B 117 ? 1.0965 0.8469 1.2714 -0.0759 0.2475  0.1054  144 MET B SD  
5084 C CE  . MET B 117 ? 1.0931 0.8102 1.2835 -0.0903 0.2593  0.1172  144 MET B CE  
5085 N N   . LYS B 118 ? 0.9763 0.6934 1.0089 -0.0208 0.2539  0.1577  145 LYS B N   
5086 C CA  . LYS B 118 ? 0.9080 0.6327 0.9103 -0.0109 0.2588  0.1685  145 LYS B CA  
5087 C C   . LYS B 118 ? 1.0475 0.7734 1.0250 0.0031  0.2438  0.1626  145 LYS B C   
5088 O O   . LYS B 118 ? 1.1213 0.8638 1.0816 0.0100  0.2416  0.1591  145 LYS B O   
5089 C CB  . LYS B 118 ? 0.8864 0.5910 0.8743 -0.0114 0.2723  0.1912  145 LYS B CB  
5090 C CG  . LYS B 118 ? 0.9135 0.6185 0.9228 -0.0265 0.2909  0.1999  145 LYS B CG  
5091 C CD  . LYS B 118 ? 1.0159 0.7171 0.9985 -0.0238 0.3069  0.2210  145 LYS B CD  
5092 C CE  . LYS B 118 ? 1.0269 0.7242 1.0295 -0.0401 0.3277  0.2331  145 LYS B CE  
5093 N NZ  . LYS B 118 ? 1.2290 0.8893 1.2302 -0.0447 0.3321  0.2497  145 LYS B NZ  
5094 N N   . LEU B 119 ? 0.9359 0.6451 0.9131 0.0072  0.2337  0.1605  146 LEU B N   
5095 C CA  . LEU B 119 ? 1.0581 0.7702 1.0153 0.0193  0.2202  0.1551  146 LEU B CA  
5096 C C   . LEU B 119 ? 1.0529 0.7852 1.0136 0.0192  0.2110  0.1370  146 LEU B C   
5097 O O   . LEU B 119 ? 1.0793 0.8233 1.0203 0.0263  0.2065  0.1347  146 LEU B O   
5098 C CB  . LEU B 119 ? 1.1081 0.8007 1.0696 0.0233  0.2126  0.1547  146 LEU B CB  
5099 C CG  . LEU B 119 ? 1.1699 0.8409 1.1175 0.0302  0.2167  0.1740  146 LEU B CG  
5100 C CD1 . LEU B 119 ? 1.1532 0.8072 1.1074 0.0365  0.2080  0.1708  146 LEU B CD1 
5101 C CD2 . LEU B 119 ? 1.0957 0.7755 1.0122 0.0408  0.2153  0.1839  146 LEU B CD2 
5102 N N   . ARG B 120 ? 1.0177 0.7529 1.0022 0.0111  0.2076  0.1239  147 ARG B N   
5103 C CA  . ARG B 120 ? 1.0078 0.7599 0.9940 0.0113  0.1986  0.1082  147 ARG B CA  
5104 C C   . ARG B 120 ? 0.9507 0.7205 0.9301 0.0128  0.2039  0.1089  147 ARG B C   
5105 O O   . ARG B 120 ? 0.9199 0.6997 0.8863 0.0183  0.1966  0.1012  147 ARG B O   
5106 C CB  . ARG B 120 ? 1.0043 0.7572 1.0163 0.0021  0.1947  0.0955  147 ARG B CB  
5107 C CG  . ARG B 120 ? 0.9893 0.7247 1.0071 0.0014  0.1891  0.0913  147 ARG B CG  
5108 C CD  . ARG B 120 ? 0.9296 0.6699 0.9595 -0.0033 0.1794  0.0738  147 ARG B CD  
5109 N NE  . ARG B 120 ? 1.0205 0.7438 1.0547 -0.0035 0.1754  0.0683  147 ARG B NE  
5110 C CZ  . ARG B 120 ? 1.0096 0.7192 1.0631 -0.0114 0.1784  0.0662  147 ARG B CZ  
5111 N NH1 . ARG B 120 ? 1.2073 0.9198 1.2799 -0.0214 0.1854  0.0691  147 ARG B NH1 
5112 N NH2 . ARG B 120 ? 1.1159 0.8089 1.1708 -0.0094 0.1749  0.0604  147 ARG B NH2 
5113 N N   . GLN B 121 ? 0.9825 0.7556 0.9704 0.0078  0.2174  0.1182  148 GLN B N   
5114 C CA  . GLN B 121 ? 0.9441 0.7343 0.9245 0.0105  0.2248  0.1193  148 GLN B CA  
5115 C C   . GLN B 121 ? 0.9242 0.7127 0.8705 0.0214  0.2234  0.1254  148 GLN B C   
5116 O O   . GLN B 121 ? 0.9749 0.7753 0.9090 0.0271  0.2205  0.1183  148 GLN B O   
5117 C CB  . GLN B 121 ? 0.8831 0.6773 0.8792 0.0023  0.2420  0.1294  148 GLN B CB  
5118 C CG  . GLN B 121 ? 0.7488 0.5623 0.7384 0.0056  0.2522  0.1302  148 GLN B CG  
5119 C CD  . GLN B 121 ? 0.8819 0.7153 0.8874 0.0067  0.2452  0.1137  148 GLN B CD  
5120 O OE1 . GLN B 121 ? 1.0260 0.8626 1.0566 0.0005  0.2375  0.1038  148 GLN B OE1 
5121 N NE2 . GLN B 121 ? 0.8646 0.7105 0.8544 0.0154  0.2470  0.1101  148 GLN B NE2 
5122 N N   . ALA B 122 ? 1.0380 0.8108 0.9684 0.0249  0.2246  0.1381  149 ALA B N   
5123 C CA  . ALA B 122 ? 0.9473 0.7192 0.8451 0.0353  0.2211  0.1436  149 ALA B CA  
5124 C C   . ALA B 122 ? 0.9529 0.7300 0.8422 0.0406  0.2056  0.1300  149 ALA B C   
5125 O O   . ALA B 122 ? 1.0323 0.8174 0.9014 0.0464  0.2026  0.1262  149 ALA B O   
5126 C CB  . ALA B 122 ? 0.8628 0.6167 0.7480 0.0390  0.2224  0.1594  149 ALA B CB  
5127 N N   . ALA B 123 ? 0.9311 0.7029 0.8351 0.0380  0.1963  0.1222  150 ALA B N   
5128 C CA  . ALA B 123 ? 1.0145 0.7912 0.9123 0.0409  0.1833  0.1096  150 ALA B CA  
5129 C C   . ALA B 123 ? 0.9995 0.7881 0.8998 0.0393  0.1821  0.0983  150 ALA B C   
5130 O O   . ALA B 123 ? 0.9322 0.7250 0.8167 0.0435  0.1751  0.0917  150 ALA B O   
5131 C CB  . ALA B 123 ? 0.8604 0.6296 0.7738 0.0379  0.1762  0.1035  150 ALA B CB  
5132 N N   . LEU B 124 ? 1.0135 0.8074 0.9349 0.0334  0.1881  0.0956  151 LEU B N   
5133 C CA  . LEU B 124 ? 0.9075 0.7135 0.8334 0.0338  0.1869  0.0857  151 LEU B CA  
5134 C C   . LEU B 124 ? 1.0420 0.8547 0.9479 0.0405  0.1925  0.0880  151 LEU B C   
5135 O O   . LEU B 124 ? 0.9751 0.7910 0.8696 0.0451  0.1862  0.0792  151 LEU B O   
5136 C CB  . LEU B 124 ? 0.9140 0.7279 0.8692 0.0266  0.1929  0.0835  151 LEU B CB  
5137 C CG  . LEU B 124 ? 0.9022 0.7309 0.8669 0.0284  0.1911  0.0733  151 LEU B CG  
5138 C CD1 . LEU B 124 ? 0.8160 0.6409 0.7743 0.0307  0.1761  0.0621  151 LEU B CD1 
5139 C CD2 . LEU B 124 ? 0.9400 0.7804 0.9370 0.0210  0.1972  0.0717  151 LEU B CD2 
5140 N N   . LYS B 125 ? 0.9531 0.7662 0.8527 0.0412  0.2048  0.0999  152 LYS B N   
5141 C CA  . LYS B 125 ? 0.9461 0.7649 0.8226 0.0481  0.2110  0.1019  152 LYS B CA  
5142 C C   . LYS B 125 ? 0.9721 0.7844 0.8202 0.0546  0.1999  0.0995  152 LYS B C   
5143 O O   . LYS B 125 ? 1.0638 0.8799 0.8958 0.0599  0.1973  0.0916  152 LYS B O   
5144 C CB  . LYS B 125 ? 0.9092 0.7278 0.7807 0.0470  0.2268  0.1170  152 LYS B CB  
5145 C CG  . LYS B 125 ? 0.8647 0.6880 0.7066 0.0547  0.2340  0.1200  152 LYS B CG  
5146 C CD  . LYS B 125 ? 0.9709 0.7925 0.8058 0.0527  0.2509  0.1369  152 LYS B CD  
5147 C CE  . LYS B 125 ? 0.8717 0.6939 0.6684 0.0613  0.2556  0.1415  152 LYS B CE  
5148 N NZ  . LYS B 125 ? 1.3815 1.2180 1.1730 0.0664  0.2600  0.1287  152 LYS B NZ  
5149 N N   . SER B 126 ? 0.9929 0.7956 0.8361 0.0543  0.1932  0.1052  153 SER B N   
5150 C CA  . SER B 126 ? 0.9781 0.7779 0.7983 0.0596  0.1821  0.1027  153 SER B CA  
5151 C C   . SER B 126 ? 0.9956 0.7973 0.8165 0.0588  0.1713  0.0878  153 SER B C   
5152 O O   . SER B 126 ? 1.0178 0.8201 0.8185 0.0627  0.1654  0.0820  153 SER B O   
5153 C CB  . SER B 126 ? 0.9397 0.7315 0.7616 0.0600  0.1764  0.1105  153 SER B CB  
5154 O OG  . SER B 126 ? 1.3344 1.1270 1.1345 0.0658  0.1668  0.1102  153 SER B OG  
5155 N N   . ALA B 127 ? 0.9545 0.7556 0.7970 0.0535  0.1683  0.0814  154 ALA B N   
5156 C CA  . ALA B 127 ? 0.8970 0.6975 0.7386 0.0526  0.1591  0.0689  154 ALA B CA  
5157 C C   . ALA B 127 ? 1.0056 0.8099 0.8391 0.0568  0.1622  0.0627  154 ALA B C   
5158 O O   . ALA B 127 ? 1.0724 0.8728 0.8905 0.0591  0.1552  0.0549  154 ALA B O   
5159 C CB  . ALA B 127 ? 0.9322 0.7313 0.7960 0.0468  0.1558  0.0643  154 ALA B CB  
5160 N N   . ARG B 128 ? 0.9966 0.8086 0.8414 0.0578  0.1732  0.0657  155 ARG B N   
5161 C CA  . ARG B 128 ? 0.8895 0.7070 0.7289 0.0636  0.1775  0.0591  155 ARG B CA  
5162 C C   . ARG B 128 ? 1.0115 0.8266 0.8210 0.0697  0.1788  0.0590  155 ARG B C   
5163 O O   . ARG B 128 ? 1.2107 1.0227 1.0074 0.0745  0.1749  0.0491  155 ARG B O   
5164 C CB  . ARG B 128 ? 0.8502 0.6804 0.7101 0.0631  0.1910  0.0629  155 ARG B CB  
5165 C CG  . ARG B 128 ? 0.8574 0.6927 0.7483 0.0575  0.1886  0.0599  155 ARG B CG  
5166 C CD  . ARG B 128 ? 0.8551 0.7072 0.7673 0.0584  0.2006  0.0595  155 ARG B CD  
5167 N NE  . ARG B 128 ? 1.0521 0.9118 0.9959 0.0526  0.1972  0.0558  155 ARG B NE  
5168 C CZ  . ARG B 128 ? 0.9925 0.8599 0.9602 0.0446  0.2056  0.0618  155 ARG B CZ  
5169 N NH1 . ARG B 128 ? 0.9949 0.8618 0.9581 0.0414  0.2190  0.0734  155 ARG B NH1 
5170 N NH2 . ARG B 128 ? 0.9642 0.8390 0.9600 0.0394  0.2000  0.0560  155 ARG B NH2 
5171 N N   . ASP B 129 ? 0.9991 0.8140 0.7957 0.0701  0.1835  0.0696  156 ASP B N   
5172 C CA  . ASP B 129 ? 1.0581 0.8721 0.8240 0.0763  0.1845  0.0695  156 ASP B CA  
5173 C C   . ASP B 129 ? 1.0224 0.8287 0.7715 0.0766  0.1694  0.0608  156 ASP B C   
5174 O O   . ASP B 129 ? 1.0631 0.8674 0.7896 0.0814  0.1674  0.0534  156 ASP B O   
5175 C CB  . ASP B 129 ? 1.0731 0.8878 0.8279 0.0770  0.1919  0.0846  156 ASP B CB  
5176 C CG  . ASP B 129 ? 1.1419 0.9636 0.9111 0.0753  0.2092  0.0938  156 ASP B CG  
5177 O OD1 . ASP B 129 ? 1.1906 1.0204 0.9781 0.0747  0.2154  0.0869  156 ASP B OD1 
5178 O OD2 . ASP B 129 ? 1.1684 0.9876 0.9316 0.0744  0.2164  0.1083  156 ASP B OD2 
5179 N N   . MET B 130 ? 1.0638 0.8661 0.8238 0.0711  0.1593  0.0608  157 MET B N   
5180 C CA  . MET B 130 ? 0.9711 0.7683 0.7196 0.0692  0.1459  0.0530  157 MET B CA  
5181 C C   . MET B 130 ? 0.9944 0.7846 0.7484 0.0664  0.1400  0.0410  157 MET B C   
5182 O O   . MET B 130 ? 1.0768 0.8614 0.8245 0.0625  0.1297  0.0346  157 MET B O   
5183 C CB  . MET B 130 ? 1.0308 0.8291 0.7888 0.0650  0.1392  0.0589  157 MET B CB  
5184 C CG  . MET B 130 ? 0.9472 0.7436 0.7303 0.0592  0.1384  0.0582  157 MET B CG  
5185 S SD  . MET B 130 ? 1.1651 0.9636 0.9582 0.0561  0.1316  0.0630  157 MET B SD  
5186 C CE  . MET B 130 ? 1.1323 0.9346 0.9043 0.0575  0.1206  0.0580  157 MET B CE  
5187 N N   . TRP B 131 ? 0.9423 0.7328 0.7086 0.0684  0.1462  0.0384  158 TRP B N   
5188 C CA  . TRP B 131 ? 0.9939 0.7757 0.7624 0.0685  0.1408  0.0280  158 TRP B CA  
5189 C C   . TRP B 131 ? 1.0268 0.8021 0.8054 0.0608  0.1316  0.0266  158 TRP B C   
5190 O O   . TRP B 131 ? 1.1112 0.8752 0.8814 0.0583  0.1238  0.0193  158 TRP B O   
5191 C CB  . TRP B 131 ? 0.9598 0.7328 0.7043 0.0724  0.1369  0.0184  158 TRP B CB  
5192 C CG  . TRP B 131 ? 1.0562 0.8312 0.7961 0.0817  0.1456  0.0136  158 TRP B CG  
5193 C CD1 . TRP B 131 ? 0.9477 0.7332 0.7059 0.0859  0.1558  0.0166  158 TRP B CD1 
5194 C CD2 . TRP B 131 ? 1.0693 0.8366 0.7861 0.0880  0.1453  0.0037  158 TRP B CD2 
5195 N NE1 . TRP B 131 ? 1.0412 0.8279 0.7902 0.0952  0.1627  0.0096  158 TRP B NE1 
5196 C CE2 . TRP B 131 ? 1.0147 0.7890 0.7368 0.0971  0.1566  0.0013  158 TRP B CE2 
5197 C CE3 . TRP B 131 ? 1.0386 0.7946 0.7318 0.0865  0.1366  -0.0044 158 TRP B CE3 
5198 C CZ2 . TRP B 131 ? 1.1063 0.8754 0.8093 0.1060  0.1601  -0.0092 158 TRP B CZ2 
5199 C CZ3 . TRP B 131 ? 1.0670 0.8161 0.7402 0.0943  0.1390  -0.0151 158 TRP B CZ3 
5200 C CH2 . TRP B 131 ? 1.1855 0.9405 0.8628 0.1046  0.1510  -0.0176 158 TRP B CH2 
5201 N N   . ALA B 132 ? 1.0259 0.8072 0.8217 0.0567  0.1334  0.0335  159 ALA B N   
5202 C CA  . ALA B 132 ? 0.9878 0.7642 0.7928 0.0499  0.1265  0.0318  159 ALA B CA  
5203 C C   . ALA B 132 ? 1.0399 0.8124 0.8556 0.0504  0.1251  0.0276  159 ALA B C   
5204 O O   . ALA B 132 ? 1.0041 0.7828 0.8299 0.0553  0.1307  0.0279  159 ALA B O   
5205 C CB  . ALA B 132 ? 0.8523 0.6353 0.6708 0.0463  0.1287  0.0391  159 ALA B CB  
5206 N N   . ASP B 133 ? 1.0115 0.7745 0.8247 0.0455  0.1175  0.0238  160 ASP B N   
5207 C CA  . ASP B 133 ? 0.9829 0.7412 0.8040 0.0462  0.1140  0.0208  160 ASP B CA  
5208 C C   . ASP B 133 ? 1.0283 0.7958 0.8694 0.0435  0.1161  0.0240  160 ASP B C   
5209 O O   . ASP B 133 ? 0.9943 0.7670 0.8489 0.0467  0.1165  0.0228  160 ASP B O   
5210 C CB  . ASP B 133 ? 0.9650 0.7080 0.7730 0.0411  0.1058  0.0172  160 ASP B CB  
5211 C CG  . ASP B 133 ? 1.0732 0.8036 0.8625 0.0425  0.1030  0.0128  160 ASP B CG  
5212 O OD1 . ASP B 133 ? 0.9724 0.7014 0.7588 0.0508  0.1050  0.0099  160 ASP B OD1 
5213 O OD2 . ASP B 133 ? 1.1120 0.8343 0.8905 0.0351  0.0992  0.0116  160 ASP B OD2 
5214 N N   . TYR B 134 ? 0.9664 0.7363 0.8108 0.0377  0.1168  0.0271  161 TYR B N   
5215 C CA  . TYR B 134 ? 0.9903 0.7654 0.8518 0.0343  0.1182  0.0286  161 TYR B CA  
5216 C C   . TYR B 134 ? 1.0334 0.8146 0.9019 0.0335  0.1245  0.0348  161 TYR B C   
5217 O O   . TYR B 134 ? 0.9892 0.7706 0.8472 0.0345  0.1252  0.0376  161 TYR B O   
5218 C CB  . TYR B 134 ? 0.9991 0.7671 0.8563 0.0286  0.1120  0.0249  161 TYR B CB  
5219 C CG  . TYR B 134 ? 1.0482 0.8067 0.8955 0.0293  0.1049  0.0206  161 TYR B CG  
5220 C CD1 . TYR B 134 ? 1.0308 0.7910 0.8878 0.0308  0.1010  0.0180  161 TYR B CD1 
5221 C CD2 . TYR B 134 ? 0.8876 0.6347 0.7161 0.0283  0.1013  0.0192  161 TYR B CD2 
5222 C CE1 . TYR B 134 ? 1.1124 0.8627 0.9587 0.0331  0.0931  0.0152  161 TYR B CE1 
5223 C CE2 . TYR B 134 ? 1.0754 0.8098 0.8929 0.0295  0.0946  0.0168  161 TYR B CE2 
5224 C CZ  . TYR B 134 ? 1.0860 0.8219 0.9117 0.0327  0.0903  0.0153  161 TYR B CZ  
5225 O OH  . TYR B 134 ? 1.1847 0.9069 0.9979 0.0355  0.0824  0.0140  161 TYR B OH  
5226 N N   . ILE B 135 ? 1.0291 0.8146 0.9157 0.0318  0.1283  0.0368  162 ILE B N   
5227 C CA  . ILE B 135 ? 0.9083 0.6947 0.8028 0.0305  0.1333  0.0427  162 ILE B CA  
5228 C C   . ILE B 135 ? 0.9557 0.7389 0.8615 0.0256  0.1306  0.0383  162 ILE B C   
5229 O O   . ILE B 135 ? 0.9203 0.7042 0.8356 0.0231  0.1281  0.0333  162 ILE B O   
5230 C CB  . ILE B 135 ? 0.9851 0.7764 0.8901 0.0322  0.1425  0.0501  162 ILE B CB  
5231 C CG1 . ILE B 135 ? 0.8726 0.6601 0.7848 0.0311  0.1470  0.0573  162 ILE B CG1 
5232 C CG2 . ILE B 135 ? 0.7870 0.5840 0.7099 0.0301  0.1442  0.0467  162 ILE B CG2 
5233 C CD1 . ILE B 135 ? 0.8807 0.6699 0.7949 0.0332  0.1568  0.0679  162 ILE B CD1 
5234 N N   . LEU B 136 ? 0.9923 0.7727 0.8966 0.0249  0.1305  0.0393  163 LEU B N   
5235 C CA  . LEU B 136 ? 0.9257 0.7024 0.8379 0.0212  0.1288  0.0338  163 LEU B CA  
5236 C C   . LEU B 136 ? 0.9083 0.6819 0.8335 0.0224  0.1342  0.0388  163 LEU B C   
5237 O O   . LEU B 136 ? 0.8946 0.6686 0.8160 0.0266  0.1358  0.0444  163 LEU B O   
5238 C CB  . LEU B 136 ? 0.8431 0.6193 0.7430 0.0199  0.1247  0.0290  163 LEU B CB  
5239 C CG  . LEU B 136 ? 0.9837 0.7572 0.8896 0.0173  0.1248  0.0228  163 LEU B CG  
5240 C CD1 . LEU B 136 ? 0.8085 0.5782 0.7135 0.0131  0.1208  0.0153  163 LEU B CD1 
5241 C CD2 . LEU B 136 ? 0.9036 0.6808 0.8013 0.0169  0.1244  0.0206  163 LEU B CD2 
5242 N N   . PHE B 137 ? 1.0212 0.7910 0.9620 0.0190  0.1363  0.0369  164 PHE B N   
5243 C CA  . PHE B 137 ? 0.8188 0.5809 0.7725 0.0192  0.1413  0.0408  164 PHE B CA  
5244 C C   . PHE B 137 ? 0.8383 0.5950 0.7941 0.0184  0.1385  0.0319  164 PHE B C   
5245 O O   . PHE B 137 ? 0.9982 0.7552 0.9532 0.0141  0.1341  0.0218  164 PHE B O   
5246 C CB  . PHE B 137 ? 0.8221 0.5818 0.7935 0.0142  0.1457  0.0425  164 PHE B CB  
5247 C CG  . PHE B 137 ? 0.8423 0.6078 0.8135 0.0154  0.1518  0.0524  164 PHE B CG  
5248 C CD1 . PHE B 137 ? 0.6946 0.4543 0.6658 0.0181  0.1594  0.0647  164 PHE B CD1 
5249 C CD2 . PHE B 137 ? 0.9048 0.6811 0.8748 0.0147  0.1502  0.0494  164 PHE B CD2 
5250 C CE1 . PHE B 137 ? 0.9154 0.6807 0.8836 0.0190  0.1664  0.0738  164 PHE B CE1 
5251 C CE2 . PHE B 137 ? 0.9170 0.7001 0.8868 0.0165  0.1573  0.0573  164 PHE B CE2 
5252 C CZ  . PHE B 137 ? 0.9559 0.7338 0.9239 0.0182  0.1660  0.0694  164 PHE B CZ  
5253 N N   . VAL B 138 ? 1.0151 0.7674 0.9722 0.0234  0.1408  0.0353  165 VAL B N   
5254 C CA  . VAL B 138 ? 0.8500 0.5971 0.8114 0.0242  0.1402  0.0266  165 VAL B CA  
5255 C C   . VAL B 138 ? 1.0053 0.7395 0.9802 0.0280  0.1449  0.0319  165 VAL B C   
5256 O O   . VAL B 138 ? 1.0770 0.8103 1.0506 0.0347  0.1469  0.0428  165 VAL B O   
5257 C CB  . VAL B 138 ? 0.8907 0.6472 0.8417 0.0281  0.1382  0.0239  165 VAL B CB  
5258 C CG1 . VAL B 138 ? 0.9028 0.6567 0.8575 0.0282  0.1389  0.0125  165 VAL B CG1 
5259 C CG2 . VAL B 138 ? 0.9905 0.7564 0.9264 0.0243  0.1342  0.0223  165 VAL B CG2 
5260 N N   . ASP B 139 ? 0.9979 0.7205 0.9849 0.0237  0.1460  0.0244  166 ASP B N   
5261 C CA  . ASP B 139 ? 1.0686 0.7742 1.0684 0.0270  0.1504  0.0282  166 ASP B CA  
5262 C C   . ASP B 139 ? 0.9964 0.7018 0.9945 0.0372  0.1503  0.0269  166 ASP B C   
5263 O O   . ASP B 139 ? 1.0678 0.7834 1.0596 0.0383  0.1479  0.0167  166 ASP B O   
5264 C CB  . ASP B 139 ? 1.2095 0.9021 1.2222 0.0195  0.1505  0.0171  166 ASP B CB  
5265 C CG  . ASP B 139 ? 1.3271 1.0173 1.3507 0.0103  0.1524  0.0217  166 ASP B CG  
5266 O OD1 . ASP B 139 ? 1.1968 0.8959 1.2165 0.0103  0.1548  0.0334  166 ASP B OD1 
5267 O OD2 . ASP B 139 ? 1.4703 1.1507 1.5072 0.0027  0.1519  0.0126  166 ASP B OD2 
5268 N N   . ALA B 140 ? 1.0090 0.7029 1.0130 0.0450  0.1533  0.0376  167 ALA B N   
5269 C CA  . ALA B 140 ? 1.0491 0.7465 1.0533 0.0571  0.1522  0.0383  167 ALA B CA  
5270 C C   . ALA B 140 ? 0.9421 0.6366 0.9534 0.0592  0.1527  0.0221  167 ALA B C   
5271 O O   . ALA B 140 ? 1.0640 0.7706 1.0754 0.0672  0.1519  0.0179  167 ALA B O   
5272 C CB  . ALA B 140 ? 1.0341 0.7161 1.0431 0.0661  0.1543  0.0536  167 ALA B CB  
5273 N N   . ASP B 141 ? 0.9617 0.6416 0.9794 0.0520  0.1542  0.0118  168 ASP B N   
5274 C CA  . ASP B 141 ? 1.0370 0.7128 1.0582 0.0537  0.1552  -0.0055 168 ASP B CA  
5275 C C   . ASP B 141 ? 1.1329 0.8220 1.1423 0.0446  0.1527  -0.0187 168 ASP B C   
5276 O O   . ASP B 141 ? 1.1750 0.8585 1.1841 0.0431  0.1535  -0.0343 168 ASP B O   
5277 C CB  . ASP B 141 ? 0.9797 0.6277 1.0142 0.0527  0.1577  -0.0104 168 ASP B CB  
5278 C CG  . ASP B 141 ? 1.0054 0.6445 1.0432 0.0386  0.1566  -0.0110 168 ASP B CG  
5279 O OD1 . ASP B 141 ? 1.4191 1.0734 1.4497 0.0314  0.1542  -0.0059 168 ASP B OD1 
5280 O OD2 . ASP B 141 ? 1.1842 0.8014 1.2335 0.0346  0.1581  -0.0172 168 ASP B OD2 
5281 N N   . ASN B 142 ? 1.1011 0.8063 1.0991 0.0393  0.1496  -0.0130 169 ASN B N   
5282 C CA  . ASN B 142 ? 1.0707 0.7865 1.0549 0.0315  0.1465  -0.0228 169 ASN B CA  
5283 C C   . ASN B 142 ? 1.1166 0.8503 1.0900 0.0349  0.1474  -0.0242 169 ASN B C   
5284 O O   . ASN B 142 ? 1.1195 0.8644 1.0905 0.0376  0.1466  -0.0137 169 ASN B O   
5285 C CB  . ASN B 142 ? 1.0591 0.7788 1.0385 0.0235  0.1423  -0.0163 169 ASN B CB  
5286 C CG  . ASN B 142 ? 1.1038 0.8100 1.0956 0.0171  0.1415  -0.0182 169 ASN B CG  
5287 O OD1 . ASN B 142 ? 1.3263 1.0167 1.3310 0.0189  0.1446  -0.0200 169 ASN B OD1 
5288 N ND2 . ASN B 142 ? 1.0061 0.7184 0.9956 0.0097  0.1372  -0.0180 169 ASN B ND2 
5289 N N   . LEU B 143 ? 1.0630 0.7997 1.0295 0.0338  0.1494  -0.0377 170 LEU B N   
5290 C CA  . LEU B 143 ? 1.0240 0.7779 0.9829 0.0358  0.1526  -0.0406 170 LEU B CA  
5291 C C   . LEU B 143 ? 0.9867 0.7480 0.9253 0.0263  0.1496  -0.0416 170 LEU B C   
5292 O O   . LEU B 143 ? 1.0266 0.7831 0.9528 0.0211  0.1489  -0.0517 170 LEU B O   
5293 C CB  . LEU B 143 ? 0.8594 0.6125 0.8224 0.0410  0.1588  -0.0546 170 LEU B CB  
5294 C CG  . LEU B 143 ? 1.0338 0.8071 0.9919 0.0424  0.1646  -0.0590 170 LEU B CG  
5295 C CD1 . LEU B 143 ? 1.0141 0.8031 0.9839 0.0482  0.1640  -0.0474 170 LEU B CD1 
5296 C CD2 . LEU B 143 ? 1.1307 0.9029 1.0941 0.0487  0.1721  -0.0741 170 LEU B CD2 
5297 N N   . ILE B 144 ? 0.9866 0.7581 0.9200 0.0245  0.1473  -0.0314 171 ILE B N   
5298 C CA  . ILE B 144 ? 0.9907 0.7659 0.9045 0.0163  0.1441  -0.0306 171 ILE B CA  
5299 C C   . ILE B 144 ? 0.9706 0.7581 0.8761 0.0143  0.1498  -0.0359 171 ILE B C   
5300 O O   . ILE B 144 ? 1.0121 0.8123 0.9194 0.0140  0.1512  -0.0306 171 ILE B O   
5301 C CB  . ILE B 144 ? 0.9973 0.7751 0.9090 0.0150  0.1393  -0.0187 171 ILE B CB  
5302 C CG1 . ILE B 144 ? 1.0207 0.7892 0.9442 0.0177  0.1367  -0.0129 171 ILE B CG1 
5303 C CG2 . ILE B 144 ? 0.9955 0.7721 0.8873 0.0077  0.1353  -0.0184 171 ILE B CG2 
5304 C CD1 . ILE B 144 ? 0.8883 0.6458 0.8120 0.0136  0.1338  -0.0198 171 ILE B CD1 
5305 N N   . LEU B 145 ? 1.1494 0.9337 1.0455 0.0122  0.1536  -0.0473 172 LEU B N   
5306 C CA  . LEU B 145 ? 1.1365 0.9335 1.0270 0.0107  0.1621  -0.0535 172 LEU B CA  
5307 C C   . LEU B 145 ? 1.0732 0.8752 0.9440 0.0013  0.1619  -0.0483 172 LEU B C   
5308 O O   . LEU B 145 ? 1.1571 0.9742 1.0312 -0.0010 0.1677  -0.0467 172 LEU B O   
5309 C CB  . LEU B 145 ? 1.1033 0.8939 0.9857 0.0113  0.1669  -0.0677 172 LEU B CB  
5310 C CG  . LEU B 145 ? 1.1707 0.9756 1.0559 0.0139  0.1788  -0.0768 172 LEU B CG  
5311 C CD1 . LEU B 145 ? 1.0775 0.8910 0.9921 0.0252  0.1821  -0.0768 172 LEU B CD1 
5312 C CD2 . LEU B 145 ? 1.1272 0.9237 0.9962 0.0132  0.1831  -0.0915 172 LEU B CD2 
5313 N N   . ASN B 146 ? 1.0216 0.8111 0.8732 -0.0042 0.1550  -0.0458 173 ASN B N   
5314 C CA  . ASN B 146 ? 0.8756 0.6639 0.7062 -0.0126 0.1538  -0.0399 173 ASN B CA  
5315 C C   . ASN B 146 ? 0.9777 0.7708 0.8169 -0.0132 0.1502  -0.0294 173 ASN B C   
5316 O O   . ASN B 146 ? 1.0464 0.8327 0.8907 -0.0099 0.1426  -0.0241 173 ASN B O   
5317 C CB  . ASN B 146 ? 1.1262 0.8985 0.9354 -0.0155 0.1455  -0.0401 173 ASN B CB  
5318 C CG  . ASN B 146 ? 1.1243 0.8904 0.9081 -0.0232 0.1439  -0.0338 173 ASN B CG  
5319 O OD1 . ASN B 146 ? 1.2223 0.9944 1.0068 -0.0275 0.1477  -0.0278 173 ASN B OD1 
5320 N ND2 . ASN B 146 ? 1.1528 0.9060 0.9140 -0.0249 0.1375  -0.0351 173 ASN B ND2 
5321 N N   . PRO B 147 ? 0.9755 0.7810 0.8166 -0.0177 0.1554  -0.0270 174 PRO B N   
5322 C CA  . PRO B 147 ? 0.9644 0.7741 0.8127 -0.0185 0.1508  -0.0188 174 PRO B CA  
5323 C C   . PRO B 147 ? 0.9881 0.7822 0.8177 -0.0229 0.1433  -0.0124 174 PRO B C   
5324 O O   . PRO B 147 ? 1.0742 0.8689 0.9079 -0.0225 0.1386  -0.0067 174 PRO B O   
5325 C CB  . PRO B 147 ? 1.0467 0.8740 0.9007 -0.0246 0.1583  -0.0200 174 PRO B CB  
5326 C CG  . PRO B 147 ? 0.7688 0.6043 0.6246 -0.0241 0.1684  -0.0289 174 PRO B CG  
5327 C CD  . PRO B 147 ? 0.9453 0.7621 0.7817 -0.0234 0.1661  -0.0322 174 PRO B CD  
5328 N N   . ASP B 148 ? 1.0455 0.8256 0.8542 -0.0262 0.1414  -0.0136 175 ASP B N   
5329 C CA  . ASP B 148 ? 1.1715 0.9355 0.9622 -0.0286 0.1336  -0.0077 175 ASP B CA  
5330 C C   . ASP B 148 ? 1.1555 0.9114 0.9497 -0.0214 0.1252  -0.0076 175 ASP B C   
5331 O O   . ASP B 148 ? 1.0253 0.7690 0.8065 -0.0213 0.1179  -0.0038 175 ASP B O   
5332 C CB  . ASP B 148 ? 1.0832 0.8360 0.8465 -0.0365 0.1357  -0.0074 175 ASP B CB  
5333 C CG  . ASP B 148 ? 1.2367 0.9969 0.9966 -0.0462 0.1450  -0.0062 175 ASP B CG  
5334 O OD1 . ASP B 148 ? 1.2598 1.0263 1.0311 -0.0485 0.1446  -0.0029 175 ASP B OD1 
5335 O OD2 . ASP B 148 ? 1.1943 0.9549 0.9400 -0.0520 0.1528  -0.0090 175 ASP B OD2 
5336 N N   . THR B 149 ? 1.1296 0.8919 0.9423 -0.0155 0.1261  -0.0118 176 THR B N   
5337 C CA  . THR B 149 ? 1.0154 0.7718 0.8342 -0.0107 0.1192  -0.0126 176 THR B CA  
5338 C C   . THR B 149 ? 1.0039 0.7578 0.8264 -0.0078 0.1137  -0.0054 176 THR B C   
5339 O O   . THR B 149 ? 1.0074 0.7543 0.8242 -0.0063 0.1066  -0.0046 176 THR B O   
5340 C CB  . THR B 149 ? 1.0543 0.8163 0.8944 -0.0061 0.1225  -0.0172 176 THR B CB  
5341 O OG1 . THR B 149 ? 1.1400 0.9055 0.9777 -0.0075 0.1292  -0.0249 176 THR B OG1 
5342 C CG2 . THR B 149 ? 1.0262 0.7823 0.8726 -0.0041 0.1162  -0.0203 176 THR B CG2 
5343 N N   . LEU B 150 ? 1.0547 0.8155 0.8867 -0.0064 0.1166  -0.0007 177 LEU B N   
5344 C CA  . LEU B 150 ? 0.9546 0.7134 0.7887 -0.0030 0.1126  0.0050  177 LEU B CA  
5345 C C   . LEU B 150 ? 1.0532 0.8008 0.8678 -0.0056 0.1076  0.0070  177 LEU B C   
5346 O O   . LEU B 150 ? 1.1106 0.8527 0.9241 -0.0015 0.1022  0.0087  177 LEU B O   
5347 C CB  . LEU B 150 ? 0.8139 0.5820 0.6574 -0.0011 0.1159  0.0088  177 LEU B CB  
5348 C CG  . LEU B 150 ? 0.9244 0.6913 0.7665 0.0023  0.1131  0.0139  177 LEU B CG  
5349 C CD1 . LEU B 150 ? 1.0097 0.7743 0.8597 0.0075  0.1115  0.0154  177 LEU B CD1 
5350 C CD2 . LEU B 150 ? 0.8967 0.6740 0.7466 0.0046  0.1155  0.0169  177 LEU B CD2 
5351 N N   . SER B 151 ? 1.0852 0.8288 0.8850 -0.0124 0.1096  0.0069  178 SER B N   
5352 C CA  . SER B 151 ? 0.9543 0.6824 0.7334 -0.0154 0.1050  0.0097  178 SER B CA  
5353 C C   . SER B 151 ? 1.0422 0.7604 0.8105 -0.0127 0.0987  0.0087  178 SER B C   
5354 O O   . SER B 151 ? 1.0983 0.8054 0.8582 -0.0088 0.0916  0.0113  178 SER B O   
5355 C CB  . SER B 151 ? 0.8492 0.5745 0.6151 -0.0252 0.1101  0.0103  178 SER B CB  
5356 O OG  . SER B 151 ? 1.0809 0.8159 0.8570 -0.0278 0.1134  0.0109  178 SER B OG  
5357 N N   . LEU B 152 ? 1.1314 0.8537 0.9000 -0.0138 0.1003  0.0039  179 LEU B N   
5358 C CA  . LEU B 152 ? 1.0363 0.7508 0.7934 -0.0115 0.0926  0.0017  179 LEU B CA  
5359 C C   . LEU B 152 ? 1.0832 0.8019 0.8572 -0.0038 0.0854  0.0008  179 LEU B C   
5360 O O   . LEU B 152 ? 1.1847 0.8964 0.9504 0.0001  0.0761  0.0013  179 LEU B O   
5361 C CB  . LEU B 152 ? 1.0689 0.7877 0.8224 -0.0146 0.0964  -0.0051 179 LEU B CB  
5362 C CG  . LEU B 152 ? 1.1038 0.8187 0.8368 -0.0225 0.1041  -0.0045 179 LEU B CG  
5363 C CD1 . LEU B 152 ? 1.0154 0.7400 0.7530 -0.0242 0.1118  -0.0129 179 LEU B CD1 
5364 C CD2 . LEU B 152 ? 0.8450 0.5423 0.5469 -0.0247 0.0981  -0.0004 179 LEU B CD2 
5365 N N   . LEU B 153 ? 1.0837 0.8144 0.8820 -0.0013 0.0896  -0.0001 180 LEU B N   
5366 C CA  . LEU B 153 ? 1.0470 0.7837 0.8637 0.0045  0.0851  -0.0005 180 LEU B CA  
5367 C C   . LEU B 153 ? 1.0930 0.8258 0.9071 0.0095  0.0817  0.0045  180 LEU B C   
5368 O O   . LEU B 153 ? 1.0586 0.7930 0.8791 0.0149  0.0750  0.0038  180 LEU B O   
5369 C CB  . LEU B 153 ? 0.9817 0.7295 0.8223 0.0049  0.0921  -0.0011 180 LEU B CB  
5370 C CG  . LEU B 153 ? 1.0526 0.8028 0.8998 0.0018  0.0952  -0.0076 180 LEU B CG  
5371 C CD1 . LEU B 153 ? 0.8769 0.6337 0.7452 0.0031  0.1027  -0.0058 180 LEU B CD1 
5372 C CD2 . LEU B 153 ? 0.9733 0.7229 0.8231 0.0015  0.0874  -0.0144 180 LEU B CD2 
5373 N N   . ILE B 154 ? 1.0779 0.8064 0.8839 0.0080  0.0860  0.0086  181 ILE B N   
5374 C CA  . ILE B 154 ? 1.0057 0.7268 0.8055 0.0127  0.0828  0.0118  181 ILE B CA  
5375 C C   . ILE B 154 ? 1.0220 0.7275 0.8023 0.0144  0.0741  0.0126  181 ILE B C   
5376 O O   . ILE B 154 ? 0.9974 0.6978 0.7774 0.0219  0.0684  0.0135  181 ILE B O   
5377 C CB  . ILE B 154 ? 1.0068 0.7253 0.8003 0.0093  0.0881  0.0143  181 ILE B CB  
5378 C CG1 . ILE B 154 ? 1.0088 0.7424 0.8201 0.0099  0.0950  0.0148  181 ILE B CG1 
5379 C CG2 . ILE B 154 ? 0.9837 0.6911 0.7681 0.0140  0.0845  0.0158  181 ILE B CG2 
5380 C CD1 . ILE B 154 ? 0.9490 0.6829 0.7551 0.0077  0.0980  0.0164  181 ILE B CD1 
5381 N N   . ALA B 155 ? 1.1287 0.8260 0.8915 0.0083  0.0732  0.0124  182 ALA B N   
5382 C CA  . ALA B 155 ? 1.1010 0.7801 0.8402 0.0097  0.0650  0.0152  182 ALA B CA  
5383 C C   . ALA B 155 ? 1.1014 0.7835 0.8462 0.0183  0.0540  0.0130  182 ALA B C   
5384 O O   . ALA B 155 ? 1.2085 0.8758 0.9366 0.0234  0.0449  0.0161  182 ALA B O   
5385 C CB  . ALA B 155 ? 1.0960 0.7672 0.8136 0.0005  0.0682  0.0160  182 ALA B CB  
5386 N N   . GLU B 156 ? 1.0570 0.7577 0.8259 0.0202  0.0541  0.0077  183 GLU B N   
5387 C CA  . GLU B 156 ? 1.0503 0.7577 0.8280 0.0267  0.0431  0.0041  183 GLU B CA  
5388 C C   . GLU B 156 ? 0.9743 0.6881 0.7694 0.0367  0.0390  0.0048  183 GLU B C   
5389 O O   . GLU B 156 ? 1.1325 0.8519 0.9348 0.0437  0.0282  0.0022  183 GLU B O   
5390 C CB  . GLU B 156 ? 1.1160 0.8398 0.9133 0.0227  0.0449  -0.0030 183 GLU B CB  
5391 C CG  . GLU B 156 ? 1.1361 0.8541 0.9151 0.0153  0.0466  -0.0062 183 GLU B CG  
5392 C CD  . GLU B 156 ? 1.2550 0.9615 1.0075 0.0172  0.0347  -0.0064 183 GLU B CD  
5393 O OE1 . GLU B 156 ? 1.2361 0.9450 0.9932 0.0250  0.0225  -0.0068 183 GLU B OE1 
5394 O OE2 . GLU B 156 ? 1.2251 0.9212 0.9520 0.0115  0.0377  -0.0059 183 GLU B OE2 
5395 N N   . ASN B 157 ? 1.1154 0.8297 0.9174 0.0381  0.0472  0.0074  184 ASN B N   
5396 C CA  . ASN B 157 ? 1.1111 0.8321 0.9287 0.0480  0.0460  0.0072  184 ASN B CA  
5397 C C   . ASN B 157 ? 1.1242 0.8683 0.9720 0.0515  0.0434  0.0024  184 ASN B C   
5398 O O   . ASN B 157 ? 1.1469 0.8972 1.0049 0.0609  0.0350  0.0005  184 ASN B O   
5399 C CB  . ASN B 157 ? 1.0573 0.7595 0.8560 0.0565  0.0367  0.0099  184 ASN B CB  
5400 C CG  . ASN B 157 ? 1.0325 0.7378 0.8433 0.0669  0.0385  0.0091  184 ASN B CG  
5401 O OD1 . ASN B 157 ? 1.1774 0.8990 1.0078 0.0668  0.0479  0.0073  184 ASN B OD1 
5402 N ND2 . ASN B 157 ? 1.0828 0.7710 0.8802 0.0766  0.0300  0.0107  184 ASN B ND2 
5403 N N   . LYS B 158 ? 1.0775 0.8343 0.9412 0.0439  0.0504  0.0002  185 LYS B N   
5404 C CA  . LYS B 158 ? 1.0209 0.7993 0.9165 0.0442  0.0509  -0.0040 185 LYS B CA  
5405 C C   . LYS B 158 ? 0.9872 0.7757 0.8998 0.0434  0.0647  -0.0011 185 LYS B C   
5406 O O   . LYS B 158 ? 1.2407 1.0202 1.1399 0.0416  0.0726  0.0033  185 LYS B O   
5407 C CB  . LYS B 158 ? 0.9970 0.7798 0.8984 0.0358  0.0485  -0.0091 185 LYS B CB  
5408 C CG  . LYS B 158 ? 1.0181 0.7904 0.8974 0.0358  0.0356  -0.0122 185 LYS B CG  
5409 C CD  . LYS B 158 ? 1.0706 0.8495 0.9559 0.0451  0.0214  -0.0145 185 LYS B CD  
5410 C CE  . LYS B 158 ? 1.1601 0.9244 1.0157 0.0466  0.0081  -0.0152 185 LYS B CE  
5411 N NZ  . LYS B 158 ? 1.2945 1.0610 1.1508 0.0586  -0.0068 -0.0150 185 LYS B NZ  
5412 N N   . THR B 159 ? 1.0498 0.8580 0.9921 0.0446  0.0673  -0.0033 186 THR B N   
5413 C CA  . THR B 159 ? 0.9463 0.7641 0.9031 0.0439  0.0813  0.0006  186 THR B CA  
5414 C C   . THR B 159 ? 0.9693 0.7881 0.9347 0.0339  0.0896  0.0025  186 THR B C   
5415 O O   . THR B 159 ? 1.0218 0.8372 0.9820 0.0325  0.1001  0.0083  186 THR B O   
5416 C CB  . THR B 159 ? 0.9216 0.7606 0.9066 0.0496  0.0829  -0.0017 186 THR B CB  
5417 O OG1 . THR B 159 ? 1.0758 0.9122 1.0528 0.0610  0.0742  -0.0039 186 THR B OG1 
5418 C CG2 . THR B 159 ? 0.8447 0.6923 0.8395 0.0494  0.0988  0.0033  186 THR B CG2 
5419 N N   . VAL B 160 ? 0.9754 0.7980 0.9531 0.0276  0.0844  -0.0027 187 VAL B N   
5420 C CA  . VAL B 160 ? 0.8839 0.7020 0.8664 0.0188  0.0903  -0.0024 187 VAL B CA  
5421 C C   . VAL B 160 ? 0.9949 0.8034 0.9639 0.0153  0.0801  -0.0092 187 VAL B C   
5422 O O   . VAL B 160 ? 1.0604 0.8757 1.0390 0.0143  0.0701  -0.0165 187 VAL B O   
5423 C CB  . VAL B 160 ? 0.9310 0.7628 0.9460 0.0129  0.0966  -0.0031 187 VAL B CB  
5424 C CG1 . VAL B 160 ? 0.7344 0.5564 0.7526 0.0045  0.1011  -0.0036 187 VAL B CG1 
5425 C CG2 . VAL B 160 ? 0.8097 0.6509 0.8350 0.0159  0.1091  0.0047  187 VAL B CG2 
5426 N N   . VAL B 161 ? 0.9902 0.7847 0.9370 0.0138  0.0826  -0.0074 188 VAL B N   
5427 C CA  . VAL B 161 ? 1.0329 0.8183 0.9639 0.0104  0.0757  -0.0137 188 VAL B CA  
5428 C C   . VAL B 161 ? 0.9374 0.7165 0.8691 0.0053  0.0841  -0.0141 188 VAL B C   
5429 O O   . VAL B 161 ? 1.0213 0.7992 0.9552 0.0061  0.0936  -0.0073 188 VAL B O   
5430 C CB  . VAL B 161 ? 0.8807 0.6551 0.7813 0.0141  0.0701  -0.0117 188 VAL B CB  
5431 C CG1 . VAL B 161 ? 1.0689 0.8354 0.9554 0.0135  0.0792  -0.0055 188 VAL B CG1 
5432 C CG2 . VAL B 161 ? 0.8449 0.6123 0.7285 0.0113  0.0615  -0.0185 188 VAL B CG2 
5433 N N   . ALA B 162 ? 0.9607 0.7356 0.8902 0.0010  0.0800  -0.0227 189 ALA B N   
5434 C CA  . ALA B 162 ? 0.9827 0.7507 0.9143 -0.0025 0.0873  -0.0252 189 ALA B CA  
5435 C C   . ALA B 162 ? 0.9846 0.7448 0.8937 -0.0040 0.0835  -0.0329 189 ALA B C   
5436 O O   . ALA B 162 ? 0.9551 0.7153 0.8553 -0.0050 0.0734  -0.0400 189 ALA B O   
5437 C CB  . ALA B 162 ? 0.9171 0.6874 0.8757 -0.0074 0.0890  -0.0298 189 ALA B CB  
5438 N N   . PRO B 163 ? 0.9822 0.7369 0.8815 -0.0038 0.0913  -0.0319 190 PRO B N   
5439 C CA  . PRO B 163 ? 0.9940 0.7428 0.8724 -0.0055 0.0904  -0.0397 190 PRO B CA  
5440 C C   . PRO B 163 ? 1.1037 0.8485 0.9917 -0.0082 0.0910  -0.0512 190 PRO B C   
5441 O O   . PRO B 163 ? 1.0629 0.8058 0.9693 -0.0078 0.0982  -0.0506 190 PRO B O   
5442 C CB  . PRO B 163 ? 1.0673 0.8159 0.9368 -0.0040 0.0997  -0.0337 190 PRO B CB  
5443 C CG  . PRO B 163 ? 1.0135 0.7656 0.9050 -0.0014 0.1059  -0.0265 190 PRO B CG  
5444 C CD  . PRO B 163 ? 1.0420 0.7976 0.9481 -0.0014 0.1011  -0.0234 190 PRO B CD  
5445 N N   . MET B 164 ? 1.1032 0.7599 1.0146 0.0840  -0.0829 0.0065  191 MET B N   
5446 C CA  . MET B 164 ? 1.0650 0.7197 0.9668 0.0802  -0.0624 -0.0058 191 MET B CA  
5447 C C   . MET B 164 ? 1.2091 0.8626 1.1368 0.0856  -0.0434 -0.0024 191 MET B C   
5448 O O   . MET B 164 ? 1.1563 0.8205 1.0937 0.0829  -0.0352 0.0049  191 MET B O   
5449 C CB  . MET B 164 ? 1.1073 0.7709 0.9768 0.0700  -0.0558 -0.0123 191 MET B CB  
5450 C CG  . MET B 164 ? 1.1188 0.7751 0.9710 0.0604  -0.0338 -0.0314 191 MET B CG  
5451 S SD  . MET B 164 ? 1.2484 0.9226 1.0602 0.0467  -0.0240 -0.0411 191 MET B SD  
5452 C CE  . MET B 164 ? 1.2951 0.9655 1.1228 0.0538  -0.0063 -0.0266 191 MET B CE  
5453 N N   . LEU B 165 ? 1.1565 0.7982 1.0950 0.0954  -0.0339 -0.0054 192 LEU B N   
5454 C CA  . LEU B 165 ? 1.0559 0.6991 1.0191 0.1085  -0.0131 0.0004  192 LEU B CA  
5455 C C   . LEU B 165 ? 1.1814 0.7993 1.1197 0.1056  0.0178  -0.0145 192 LEU B C   
5456 O O   . LEU B 165 ? 1.2991 0.8932 1.2057 0.0938  0.0227  -0.0310 192 LEU B O   
5457 C CB  . LEU B 165 ? 1.0632 0.7051 1.0478 0.1273  -0.0172 0.0095  192 LEU B CB  
5458 C CG  . LEU B 165 ? 1.0697 0.7361 1.0729 0.1286  -0.0482 0.0199  192 LEU B CG  
5459 C CD1 . LEU B 165 ? 0.9850 0.6549 1.0031 0.1495  -0.0513 0.0298  192 LEU B CD1 
5460 C CD2 . LEU B 165 ? 0.9327 0.6325 0.9636 0.1214  -0.0565 0.0287  192 LEU B CD2 
5461 N N   . ASP B 166 ? 1.2511 0.8764 1.2033 0.1143  0.0398  -0.0102 193 ASP B N   
5462 C CA  . ASP B 166 ? 1.1547 0.7521 1.0789 0.1127  0.0728  -0.0263 193 ASP B CA  
5463 C C   . ASP B 166 ? 1.2154 0.7753 1.1418 0.1332  0.0984  -0.0280 193 ASP B C   
5464 O O   . ASP B 166 ? 1.2654 0.8400 1.2281 0.1580  0.0972  -0.0086 193 ASP B O   
5465 C CB  . ASP B 166 ? 1.2104 0.8321 1.1449 0.1155  0.0891  -0.0199 193 ASP B CB  
5466 C CG  . ASP B 166 ? 1.4439 1.0894 1.3638 0.0955  0.0719  -0.0176 193 ASP B CG  
5467 O OD1 . ASP B 166 ? 1.4865 1.1215 1.3667 0.0793  0.0635  -0.0318 193 ASP B OD1 
5468 O OD2 . ASP B 166 ? 1.4356 1.1121 1.3836 0.0962  0.0677  -0.0001 193 ASP B OD2 
5469 N N   . SER B 167 ? 1.1830 0.6941 1.0681 0.1225  0.1224  -0.0511 194 SER B N   
5470 C CA  . SER B 167 ? 1.2979 0.7540 1.1735 0.1411  0.1563  -0.0549 194 SER B CA  
5471 C C   . SER B 167 ? 1.2817 0.7043 1.1267 0.1408  0.1956  -0.0741 194 SER B C   
5472 O O   . SER B 167 ? 1.3272 0.7742 1.1572 0.1245  0.1940  -0.0843 194 SER B O   
5473 C CB  . SER B 167 ? 1.3712 0.7834 1.2194 0.1241  0.1547  -0.0683 194 SER B CB  
5474 O OG  . SER B 167 ? 1.3089 0.7084 1.1144 0.0863  0.1559  -0.0987 194 SER B OG  
5475 N N   . ARG B 168 ? 1.3407 0.7017 1.1713 0.1610  0.2339  -0.0783 195 ARG B N   
5476 C CA  . ARG B 168 ? 1.3955 0.7103 1.1878 0.1611  0.2764  -0.1012 195 ARG B CA  
5477 C C   . ARG B 168 ? 1.4381 0.7185 1.1712 0.1144  0.2793  -0.1411 195 ARG B C   
5478 O O   . ARG B 168 ? 1.6693 0.9265 1.3638 0.1047  0.3062  -0.1653 195 ARG B O   
5479 C CB  . ARG B 168 ? 1.4769 0.7229 1.2640 0.1984  0.3206  -0.0949 195 ARG B CB  
5480 C CG  . ARG B 168 ? 1.4650 0.6347 1.2195 0.1844  0.3317  -0.1075 195 ARG B CG  
5481 C CD  . ARG B 168 ? 1.5385 0.6374 1.2899 0.2293  0.3753  -0.0918 195 ARG B CD  
5482 N NE  . ARG B 168 ? 1.7349 0.7701 1.4643 0.2177  0.3802  -0.0935 195 ARG B NE  
5483 C CZ  . ARG B 168 ? 1.7487 0.6933 1.4212 0.1843  0.4104  -0.1272 195 ARG B CZ  
5484 N NH1 . ARG B 168 ? 1.8116 0.7155 1.4384 0.1596  0.4378  -0.1650 195 ARG B NH1 
5485 N NH2 . ARG B 168 ? 1.7064 0.6004 1.3651 0.1724  0.4141  -0.1240 195 ARG B NH2 
5486 N N   . ALA B 169 ? 1.4280 0.7111 1.1529 0.0852  0.2527  -0.1489 196 ALA B N   
5487 C CA  . ALA B 169 ? 1.4040 0.6696 1.0783 0.0377  0.2521  -0.1865 196 ALA B CA  
5488 C C   . ALA B 169 ? 1.4739 0.8129 1.1587 0.0128  0.2043  -0.1831 196 ALA B C   
5489 O O   . ALA B 169 ? 1.4511 0.8466 1.1746 0.0311  0.1759  -0.1550 196 ALA B O   
5490 C CB  . ALA B 169 ? 1.5197 0.7061 1.1662 0.0220  0.2770  -0.2047 196 ALA B CB  
5491 N N   . ALA B 170 ? 1.4869 0.8274 1.1364 -0.0292 0.1968  -0.2122 197 ALA B N   
5492 C CA  . ALA B 170 ? 1.3915 0.8053 1.0500 -0.0481 0.1538  -0.2074 197 ALA B CA  
5493 C C   . ALA B 170 ? 1.5112 0.9417 1.2107 -0.0333 0.1292  -0.1806 197 ALA B C   
5494 O O   . ALA B 170 ? 1.5529 1.0438 1.2671 -0.0363 0.0942  -0.1689 197 ALA B O   
5495 C CB  . ALA B 170 ? 1.4089 0.8308 1.0235 -0.0969 0.1528  -0.2453 197 ALA B CB  
5496 N N   . TYR B 171 ? 1.5241 0.9016 1.2386 -0.0146 0.1482  -0.1697 198 TYR B N   
5497 C CA  . TYR B 171 ? 1.2984 0.6911 1.0459 0.0000  0.1264  -0.1451 198 TYR B CA  
5498 C C   . TYR B 171 ? 1.4213 0.8696 1.2073 0.0278  0.0959  -0.1155 198 TYR B C   
5499 O O   . TYR B 171 ? 1.4692 0.9243 1.2690 0.0483  0.1027  -0.1046 198 TYR B O   
5500 C CB  . TYR B 171 ? 1.3208 0.6459 1.0727 0.0212  0.1554  -0.1345 198 TYR B CB  
5501 C CG  . TYR B 171 ? 1.3967 0.7397 1.1804 0.0426  0.1340  -0.1056 198 TYR B CG  
5502 C CD1 . TYR B 171 ? 1.2469 0.5839 1.0227 0.0221  0.1282  -0.1097 198 TYR B CD1 
5503 C CD2 . TYR B 171 ? 1.3898 0.7603 1.2103 0.0813  0.1203  -0.0755 198 TYR B CD2 
5504 C CE1 . TYR B 171 ? 1.3509 0.7041 1.1501 0.0429  0.1103  -0.0840 198 TYR B CE1 
5505 C CE2 . TYR B 171 ? 1.3599 0.7488 1.2032 0.0992  0.0998  -0.0522 198 TYR B CE2 
5506 C CZ  . TYR B 171 ? 1.4144 0.7920 1.2447 0.0818  0.0955  -0.0562 198 TYR B CZ  
5507 O OH  . TYR B 171 ? 1.3338 0.7295 1.1815 0.1010  0.0768  -0.0335 198 TYR B OH  
5508 N N   . SER B 172 ? 1.3405 0.8274 1.1425 0.0265  0.0644  -0.1036 199 SER B N   
5509 C CA  . SER B 172 ? 1.1733 0.6995 1.0081 0.0497  0.0370  -0.0778 199 SER B CA  
5510 C C   . SER B 172 ? 1.3388 0.8755 1.1850 0.0533  0.0166  -0.0674 199 SER B C   
5511 O O   . SER B 172 ? 1.3157 0.8334 1.1474 0.0382  0.0251  -0.0778 199 SER B O   
5512 C CB  . SER B 172 ? 1.2227 0.7930 1.0523 0.0422  0.0186  -0.0777 199 SER B CB  
5513 O OG  . SER B 172 ? 1.2239 0.8188 1.0820 0.0609  -0.0021 -0.0547 199 SER B OG  
5514 N N   . ASN B 173 ? 1.2406 0.8061 1.1108 0.0712  -0.0084 -0.0479 200 ASN B N   
5515 C CA  . ASN B 173 ? 1.1578 0.7326 1.0363 0.0791  -0.0270 -0.0375 200 ASN B CA  
5516 C C   . ASN B 173 ? 1.1963 0.8044 1.0627 0.0659  -0.0476 -0.0434 200 ASN B C   
5517 O O   . ASN B 173 ? 1.2002 0.8269 1.0747 0.0779  -0.0694 -0.0322 200 ASN B O   
5518 C CB  . ASN B 173 ? 1.1004 0.6883 1.0060 0.1028  -0.0430 -0.0176 200 ASN B CB  
5519 C CG  . ASN B 173 ? 1.2480 0.8611 1.1634 0.1016  -0.0564 -0.0136 200 ASN B CG  
5520 O OD1 . ASN B 173 ? 1.1554 0.7692 1.0633 0.0924  -0.0443 -0.0204 200 ASN B OD1 
5521 N ND2 . ASN B 173 ? 1.2113 0.8412 1.1397 0.1093  -0.0794 -0.0031 200 ASN B ND2 
5522 N N   . PHE B 174 ? 1.2130 0.8319 1.0585 0.0422  -0.0407 -0.0613 201 PHE B N   
5523 C CA  . PHE B 174 ? 1.1906 0.8539 1.0276 0.0331  -0.0593 -0.0646 201 PHE B CA  
5524 C C   . PHE B 174 ? 1.2890 0.9649 1.1057 0.0007  -0.0467 -0.0880 201 PHE B C   
5525 O O   . PHE B 174 ? 1.2707 0.9226 1.0724 -0.0154 -0.0268 -0.1040 201 PHE B O   
5526 C CB  . PHE B 174 ? 1.1256 0.8186 0.9605 0.0438  -0.0776 -0.0551 201 PHE B CB  
5527 C CG  . PHE B 174 ? 1.1152 0.8171 0.9323 0.0304  -0.0684 -0.0654 201 PHE B CG  
5528 C CD1 . PHE B 174 ? 1.1356 0.8066 0.9555 0.0324  -0.0509 -0.0662 201 PHE B CD1 
5529 C CD2 . PHE B 174 ? 1.1446 0.8922 0.9413 0.0177  -0.0768 -0.0735 201 PHE B CD2 
5530 C CE1 . PHE B 174 ? 1.2278 0.9063 1.0267 0.0210  -0.0402 -0.0763 201 PHE B CE1 
5531 C CE2 . PHE B 174 ? 1.2443 1.0035 1.0187 0.0056  -0.0689 -0.0834 201 PHE B CE2 
5532 C CZ  . PHE B 174 ? 1.2795 1.0004 1.0530 0.0068  -0.0497 -0.0855 201 PHE B CZ  
5533 N N   . TRP B 175 ? 1.2208 0.9371 1.0368 -0.0099 -0.0574 -0.0913 202 TRP B N   
5534 C CA  . TRP B 175 ? 1.2204 0.9720 1.0206 -0.0453 -0.0523 -0.1142 202 TRP B CA  
5535 C C   . TRP B 175 ? 1.3608 1.1860 1.1561 -0.0406 -0.0762 -0.1102 202 TRP B C   
5536 O O   . TRP B 175 ? 1.2950 1.1413 1.1008 -0.0104 -0.0950 -0.0888 202 TRP B O   
5537 C CB  . TRP B 175 ? 1.2685 1.0261 1.0749 -0.0644 -0.0447 -0.1202 202 TRP B CB  
5538 C CG  . TRP B 175 ? 1.3737 1.0573 1.1809 -0.0651 -0.0192 -0.1188 202 TRP B CG  
5539 C CD1 . TRP B 175 ? 1.3723 0.9911 1.1767 -0.0494 -0.0024 -0.1139 202 TRP B CD1 
5540 C CD2 . TRP B 175 ? 1.4042 1.0736 1.2146 -0.0792 -0.0055 -0.1187 202 TRP B CD2 
5541 N NE1 . TRP B 175 ? 1.4845 1.0480 1.2880 -0.0489 0.0204  -0.1090 202 TRP B NE1 
5542 C CE2 . TRP B 175 ? 1.4008 0.9899 1.2061 -0.0685 0.0197  -0.1118 202 TRP B CE2 
5543 C CE3 . TRP B 175 ? 1.3367 1.0573 1.1545 -0.0982 -0.0103 -0.1216 202 TRP B CE3 
5544 C CZ2 . TRP B 175 ? 1.5065 1.0568 1.3088 -0.0761 0.0410  -0.1064 202 TRP B CZ2 
5545 C CZ3 . TRP B 175 ? 1.3805 1.0656 1.1985 -0.1099 0.0111  -0.1182 202 TRP B CZ3 
5546 C CH2 . TRP B 175 ? 1.5459 1.1424 1.3537 -0.0988 0.0369  -0.1100 202 TRP B CH2 
5547 N N   . CYS B 176 ? 1.3508 1.2136 1.1264 -0.0695 -0.0744 -0.1310 203 CYS B N   
5548 C CA  . CYS B 176 ? 1.3495 1.2925 1.1174 -0.0632 -0.0968 -0.1252 203 CYS B CA  
5549 C C   . CYS B 176 ? 1.4456 1.4677 1.2212 -0.0835 -0.1070 -0.1339 203 CYS B C   
5550 O O   . CYS B 176 ? 1.5180 1.6144 1.2959 -0.0646 -0.1280 -0.1195 203 CYS B O   
5551 C CB  . CYS B 176 ? 1.4350 1.3880 1.1733 -0.0779 -0.0929 -0.1395 203 CYS B CB  
5552 S SG  . CYS B 176 ? 1.7846 1.7208 1.5157 -0.0368 -0.1012 -0.1107 203 CYS B SG  
5553 N N   . GLY B 177 ? 1.5294 1.5385 1.3094 -0.1200 -0.0908 -0.1549 204 GLY B N   
5554 C CA  . GLY B 177 ? 1.4542 1.5429 1.2479 -0.1438 -0.0979 -0.1628 204 GLY B CA  
5555 C C   . GLY B 177 ? 1.5201 1.5650 1.3296 -0.1588 -0.0788 -0.1654 204 GLY B C   
5556 O O   . GLY B 177 ? 1.5559 1.5087 1.3574 -0.1655 -0.0554 -0.1710 204 GLY B O   
5557 N N   . MET B 178 ? 1.4656 1.5805 1.2972 -0.1609 -0.0873 -0.1585 205 MET B N   
5558 C CA  . MET B 178 ? 1.3638 1.4523 1.2094 -0.1792 -0.0682 -0.1598 205 MET B CA  
5559 C C   . MET B 178 ? 1.5076 1.6891 1.3656 -0.2278 -0.0677 -0.1796 205 MET B C   
5560 O O   . MET B 178 ? 1.6340 1.9192 1.4972 -0.2322 -0.0892 -0.1837 205 MET B O   
5561 C CB  . MET B 178 ? 1.2518 1.3305 1.1147 -0.1301 -0.0756 -0.1283 205 MET B CB  
5562 C CG  . MET B 178 ? 1.2374 1.2410 1.1022 -0.1342 -0.0516 -0.1230 205 MET B CG  
5563 S SD  . MET B 178 ? 1.3902 1.3850 1.2666 -0.0767 -0.0624 -0.0896 205 MET B SD  
5564 C CE  . MET B 178 ? 1.3140 1.2028 1.1751 -0.0460 -0.0599 -0.0793 205 MET B CE  
5565 N N   . THR B 179 ? 1.5889 1.7361 1.4518 -0.2643 -0.0420 -0.1902 206 THR B N   
5566 C CA  . THR B 179 ? 1.6600 1.8745 1.5310 -0.3283 -0.0329 -0.2173 206 THR B CA  
5567 C C   . THR B 179 ? 1.7031 2.0065 1.6095 -0.3273 -0.0370 -0.2022 206 THR B C   
5568 O O   . THR B 179 ? 1.8303 2.1885 1.7493 -0.3847 -0.0251 -0.2229 206 THR B O   
5569 C CB  . THR B 179 ? 1.7064 1.8151 1.5546 -0.3792 0.0056  -0.2425 206 THR B CB  
5570 O OG1 . THR B 179 ? 1.6741 1.6940 1.5248 -0.3522 0.0265  -0.2183 206 THR B OG1 
5571 C CG2 . THR B 179 ? 1.8768 1.9081 1.6887 -0.3837 0.0129  -0.2618 206 THR B CG2 
5572 N N   . SER B 180 ? 1.5161 1.8343 1.4377 -0.2658 -0.0512 -0.1684 207 SER B N   
5573 C CA  . SER B 180 ? 1.6078 2.0059 1.5607 -0.2554 -0.0523 -0.1513 207 SER B CA  
5574 C C   . SER B 180 ? 1.5789 1.9128 1.5331 -0.2875 -0.0181 -0.1533 207 SER B C   
5575 O O   . SER B 180 ? 1.3552 1.7406 1.3325 -0.2836 -0.0113 -0.1392 207 SER B O   
5576 C CB  . SER B 180 ? 1.6803 2.2344 1.6594 -0.2821 -0.0697 -0.1621 207 SER B CB  
5577 O OG  . SER B 180 ? 1.7461 2.3245 1.7270 -0.3617 -0.0532 -0.1966 207 SER B OG  
5578 N N   . GLN B 181 ? 1.6326 1.8513 1.5593 -0.3164 0.0062  -0.1689 208 GLN B N   
5579 C CA  . GLN B 181 ? 1.5131 1.6369 1.4299 -0.3304 0.0413  -0.1624 208 GLN B CA  
5580 C C   . GLN B 181 ? 1.4903 1.4924 1.3827 -0.2813 0.0472  -0.1425 208 GLN B C   
5581 O O   . GLN B 181 ? 1.4769 1.4053 1.3599 -0.2763 0.0727  -0.1277 208 GLN B O   
5582 C CB  . GLN B 181 ? 1.5371 1.6191 1.4394 -0.4075 0.0732  -0.1957 208 GLN B CB  
5583 C CG  . GLN B 181 ? 1.7284 1.9341 1.6570 -0.4687 0.0707  -0.2187 208 GLN B CG  
5584 C CD  . GLN B 181 ? 1.9947 2.1450 1.9037 -0.5515 0.1057  -0.2553 208 GLN B CD  
5585 O OE1 . GLN B 181 ? 2.0605 2.0706 1.9338 -0.5576 0.1352  -0.2610 208 GLN B OE1 
5586 N NE2 . GLN B 181 ? 2.0085 2.2696 1.9403 -0.6158 0.1039  -0.2808 208 GLN B NE2 
5587 N N   . GLY B 182 ? 1.4649 1.4500 1.3474 -0.2453 0.0250  -0.1402 209 GLY B N   
5588 C CA  . GLY B 182 ? 1.4583 1.3465 1.3236 -0.2003 0.0270  -0.1224 209 GLY B CA  
5589 C C   . GLY B 182 ? 1.5597 1.3642 1.4004 -0.2150 0.0419  -0.1394 209 GLY B C   
5590 O O   . GLY B 182 ? 1.5096 1.2463 1.3405 -0.1765 0.0420  -0.1244 209 GLY B O   
5591 N N   . TYR B 183 ? 1.5743 1.3855 1.4045 -0.2693 0.0548  -0.1712 210 TYR B N   
5592 C CA  . TYR B 183 ? 1.6816 1.4036 1.4826 -0.2855 0.0763  -0.1906 210 TYR B CA  
5593 C C   . TYR B 183 ? 1.6174 1.3683 1.4126 -0.2666 0.0513  -0.1979 210 TYR B C   
5594 O O   . TYR B 183 ? 1.5232 1.3698 1.3334 -0.2560 0.0196  -0.1948 210 TYR B O   
5595 C CB  . TYR B 183 ? 1.7884 1.4916 1.5725 -0.3578 0.1061  -0.2261 210 TYR B CB  
5596 C CG  . TYR B 183 ? 1.7883 1.4604 1.5766 -0.3830 0.1355  -0.2184 210 TYR B CG  
5597 C CD1 . TYR B 183 ? 1.8043 1.3995 1.5892 -0.3415 0.1521  -0.1853 210 TYR B CD1 
5598 C CD2 . TYR B 183 ? 1.8209 1.5468 1.6163 -0.4495 0.1468  -0.2433 210 TYR B CD2 
5599 C CE1 . TYR B 183 ? 1.8510 1.4156 1.6355 -0.3626 0.1815  -0.1748 210 TYR B CE1 
5600 C CE2 . TYR B 183 ? 1.8721 1.5686 1.6713 -0.4754 0.1771  -0.2346 210 TYR B CE2 
5601 C CZ  . TYR B 183 ? 1.9579 1.5700 1.7497 -0.4303 0.1954  -0.1991 210 TYR B CZ  
5602 O OH  . TYR B 183 ? 1.9546 1.5352 1.7459 -0.4545 0.2281  -0.1873 210 TYR B OH  
5603 N N   . TYR B 184 ? 1.6563 1.3216 1.4279 -0.2595 0.0688  -0.2050 211 TYR B N   
5604 C CA  . TYR B 184 ? 1.5736 1.2563 1.3359 -0.2432 0.0513  -0.2113 211 TYR B CA  
5605 C C   . TYR B 184 ? 1.5969 1.3536 1.3471 -0.2902 0.0412  -0.2442 211 TYR B C   
5606 O O   . TYR B 184 ? 1.6980 1.4628 1.4393 -0.3453 0.0575  -0.2714 211 TYR B O   
5607 C CB  . TYR B 184 ? 1.5764 1.1543 1.3160 -0.2292 0.0784  -0.2142 211 TYR B CB  
5608 C CG  . TYR B 184 ? 1.6278 1.2201 1.3570 -0.2131 0.0654  -0.2197 211 TYR B CG  
5609 C CD1 . TYR B 184 ? 1.5438 1.1606 1.2923 -0.1639 0.0405  -0.1913 211 TYR B CD1 
5610 C CD2 . TYR B 184 ? 1.5492 1.1292 1.2461 -0.2498 0.0797  -0.2544 211 TYR B CD2 
5611 C CE1 . TYR B 184 ? 1.5243 1.1532 1.2631 -0.1509 0.0318  -0.1937 211 TYR B CE1 
5612 C CE2 . TYR B 184 ? 1.6309 1.2256 1.3153 -0.2338 0.0699  -0.2575 211 TYR B CE2 
5613 C CZ  . TYR B 184 ? 1.6772 1.2968 1.3841 -0.1840 0.0466  -0.2253 211 TYR B CZ  
5614 O OH  . TYR B 184 ? 1.8419 1.4751 1.5364 -0.1697 0.0399  -0.2257 211 TYR B OH  
5615 N N   . LYS B 185 ? 1.5240 1.3370 1.2724 -0.2699 0.0146  -0.2413 212 LYS B N   
5616 C CA  . LYS B 185 ? 1.5103 1.4125 1.2466 -0.3064 -0.0015 -0.2671 212 LYS B CA  
5617 C C   . LYS B 185 ? 1.5154 1.4256 1.2327 -0.2808 -0.0152 -0.2646 212 LYS B C   
5618 O O   . LYS B 185 ? 1.6476 1.5758 1.3801 -0.2308 -0.0356 -0.2330 212 LYS B O   
5619 C CB  . LYS B 185 ? 1.5559 1.5775 1.3225 -0.3041 -0.0299 -0.2541 212 LYS B CB  
5620 C CG  . LYS B 185 ? 1.6377 1.7748 1.3967 -0.3346 -0.0519 -0.2746 212 LYS B CG  
5621 C CD  . LYS B 185 ? 1.5833 1.8412 1.3779 -0.3232 -0.0770 -0.2560 212 LYS B CD  
5622 C CE  . LYS B 185 ? 1.6054 1.9961 1.3960 -0.3508 -0.1009 -0.2732 212 LYS B CE  
5623 N NZ  . LYS B 185 ? 1.4363 1.9514 1.2657 -0.3346 -0.1226 -0.2522 212 LYS B NZ  
5624 N N   . ARG B 186 ? 1.6089 1.5016 1.2900 -0.3166 -0.0016 -0.2984 213 ARG B N   
5625 C CA  . ARG B 186 ? 1.6467 1.5574 1.3049 -0.2974 -0.0131 -0.2978 213 ARG B CA  
5626 C C   . ARG B 186 ? 1.7243 1.7643 1.3874 -0.2936 -0.0500 -0.2901 213 ARG B C   
5627 O O   . ARG B 186 ? 1.8895 2.0117 1.5579 -0.3309 -0.0610 -0.3073 213 ARG B O   
5628 C CB  . ARG B 186 ? 1.9076 1.7636 1.5192 -0.3377 0.0142  -0.3391 213 ARG B CB  
5629 C CG  . ARG B 186 ? 2.0037 1.7261 1.6042 -0.3345 0.0556  -0.3453 213 ARG B CG  
5630 C CD  . ARG B 186 ? 2.0562 1.7302 1.6680 -0.2751 0.0581  -0.3125 213 ARG B CD  
5631 N NE  . ARG B 186 ? 2.3382 1.9690 1.9127 -0.2751 0.0781  -0.3308 213 ARG B NE  
5632 C CZ  . ARG B 186 ? 2.2249 1.7965 1.8043 -0.2339 0.0937  -0.3114 213 ARG B CZ  
5633 N NH1 . ARG B 186 ? 1.9442 1.4929 1.5632 -0.1918 0.0898  -0.2750 213 ARG B NH1 
5634 N NH2 . ARG B 186 ? 2.1114 1.6516 1.6548 -0.2359 0.1141  -0.3300 213 ARG B NH2 
5635 N N   . THR B 187 ? 1.5704 1.6306 1.2323 -0.2476 -0.0678 -0.2623 214 THR B N   
5636 C CA  . THR B 187 ? 1.4541 1.6250 1.1108 -0.2340 -0.0989 -0.2499 214 THR B CA  
5637 C C   . THR B 187 ? 1.5291 1.6841 1.1495 -0.2193 -0.0973 -0.2489 214 THR B C   
5638 O O   . THR B 187 ? 1.4663 1.5294 1.0804 -0.2033 -0.0765 -0.2447 214 THR B O   
5639 C CB  . THR B 187 ? 1.4669 1.6773 1.1582 -0.1825 -0.1212 -0.2069 214 THR B CB  
5640 O OG1 . THR B 187 ? 1.5533 1.6844 1.2496 -0.1383 -0.1152 -0.1796 214 THR B OG1 
5641 C CG2 . THR B 187 ? 1.5159 1.7370 1.2421 -0.1930 -0.1193 -0.2059 214 THR B CG2 
5642 N N   . PRO B 188 ? 1.5760 1.8254 1.1719 -0.2232 -0.1181 -0.2511 215 PRO B N   
5643 C CA  . PRO B 188 ? 1.5775 1.8139 1.1316 -0.2130 -0.1137 -0.2517 215 PRO B CA  
5644 C C   . PRO B 188 ? 1.5428 1.7179 1.1066 -0.1592 -0.1092 -0.2120 215 PRO B C   
5645 O O   . PRO B 188 ? 1.5279 1.6592 1.0630 -0.1544 -0.0936 -0.2150 215 PRO B O   
5646 C CB  . PRO B 188 ? 1.4646 1.8321 0.9974 -0.2158 -0.1434 -0.2493 215 PRO B CB  
5647 C CG  . PRO B 188 ? 1.4404 1.8835 0.9960 -0.2543 -0.1552 -0.2704 215 PRO B CG  
5648 C CD  . PRO B 188 ? 1.4436 1.8229 1.0465 -0.2401 -0.1449 -0.2551 215 PRO B CD  
5649 N N   . ALA B 189 ? 1.4071 1.5768 1.0087 -0.1213 -0.1205 -0.1771 216 ALA B N   
5650 C CA  . ALA B 189 ? 1.3352 1.4554 0.9450 -0.0752 -0.1187 -0.1405 216 ALA B CA  
5651 C C   . ALA B 189 ? 1.3829 1.3996 1.0126 -0.0717 -0.0949 -0.1418 216 ALA B C   
5652 O O   . ALA B 189 ? 1.3928 1.3687 1.0316 -0.0407 -0.0917 -0.1154 216 ALA B O   
5653 C CB  . ALA B 189 ? 1.2710 1.4289 0.9058 -0.0360 -0.1405 -0.1044 216 ALA B CB  
5654 N N   . TYR B 190 ? 1.3390 1.3138 0.9750 -0.1023 -0.0771 -0.1704 217 TYR B N   
5655 C CA  . TYR B 190 ? 1.3582 1.2432 1.0149 -0.0917 -0.0552 -0.1666 217 TYR B CA  
5656 C C   . TYR B 190 ? 1.4507 1.2908 1.0876 -0.0854 -0.0342 -0.1688 217 TYR B C   
5657 O O   . TYR B 190 ? 1.3270 1.1315 0.9840 -0.0566 -0.0298 -0.1444 217 TYR B O   
5658 C CB  . TYR B 190 ? 1.2444 1.0904 0.9071 -0.1223 -0.0374 -0.1930 217 TYR B CB  
5659 C CG  . TYR B 190 ? 1.3005 1.0607 0.9841 -0.1049 -0.0154 -0.1843 217 TYR B CG  
5660 C CD1 . TYR B 190 ? 1.3691 1.1158 1.0879 -0.0806 -0.0247 -0.1602 217 TYR B CD1 
5661 C CD2 . TYR B 190 ? 1.4427 1.1400 1.1087 -0.1097 0.0150  -0.1994 217 TYR B CD2 
5662 C CE1 . TYR B 190 ? 1.3818 1.0627 1.1191 -0.0625 -0.0074 -0.1502 217 TYR B CE1 
5663 C CE2 . TYR B 190 ? 1.4474 1.0775 1.1347 -0.0880 0.0345  -0.1875 217 TYR B CE2 
5664 C CZ  . TYR B 190 ? 1.4048 1.0310 1.1283 -0.0649 0.0217  -0.1622 217 TYR B CZ  
5665 O OH  . TYR B 190 ? 1.4077 0.9790 1.1519 -0.0415 0.0385  -0.1486 217 TYR B OH  
5666 N N   . ILE B 191 ? 1.4493 1.2924 1.0463 -0.1144 -0.0196 -0.1997 218 ILE B N   
5667 C CA  . ILE B 191 ? 1.4400 1.2414 1.0146 -0.1079 0.0049  -0.2040 218 ILE B CA  
5668 C C   . ILE B 191 ? 1.4073 1.2357 0.9825 -0.0761 -0.0066 -0.1697 218 ILE B C   
5669 O O   . ILE B 191 ? 1.5051 1.2907 1.0922 -0.0568 0.0110  -0.1556 218 ILE B O   
5670 C CB  . ILE B 191 ? 1.5121 1.3142 1.0353 -0.1463 0.0221  -0.2468 218 ILE B CB  
5671 C CG1 . ILE B 191 ? 1.4978 1.2445 1.0201 -0.1780 0.0434  -0.2796 218 ILE B CG1 
5672 C CG2 . ILE B 191 ? 1.6027 1.3688 1.0979 -0.1357 0.0484  -0.2501 218 ILE B CG2 
5673 C CD1 . ILE B 191 ? 1.6133 1.2683 1.1594 -0.1556 0.0734  -0.2708 218 ILE B CD1 
5674 N N   . PRO B 192 ? 1.4529 1.3504 1.0160 -0.0681 -0.0331 -0.1533 219 PRO B N   
5675 C CA  . PRO B 192 ? 1.4747 1.3806 1.0376 -0.0355 -0.0391 -0.1159 219 PRO B CA  
5676 C C   . PRO B 192 ? 1.3777 1.2386 0.9870 -0.0092 -0.0399 -0.0871 219 PRO B C   
5677 O O   . PRO B 192 ? 1.3470 1.1777 0.9632 0.0055  -0.0267 -0.0689 219 PRO B O   
5678 C CB  . PRO B 192 ? 1.4412 1.4275 0.9844 -0.0283 -0.0675 -0.1025 219 PRO B CB  
5679 C CG  . PRO B 192 ? 1.5287 1.5614 1.0454 -0.0658 -0.0711 -0.1413 219 PRO B CG  
5680 C CD  . PRO B 192 ? 1.4491 1.4238 0.9904 -0.0896 -0.0545 -0.1689 219 PRO B CD  
5681 N N   . ILE B 193 ? 1.3497 1.2095 0.9901 -0.0051 -0.0547 -0.0834 220 ILE B N   
5682 C CA  . ILE B 193 ? 1.2587 1.0775 0.9390 0.0162  -0.0568 -0.0609 220 ILE B CA  
5683 C C   . ILE B 193 ? 1.4022 1.1671 1.1030 0.0125  -0.0328 -0.0696 220 ILE B C   
5684 O O   . ILE B 193 ? 1.3444 1.0847 1.0679 0.0275  -0.0272 -0.0504 220 ILE B O   
5685 C CB  . ILE B 193 ? 1.2411 1.0719 0.9441 0.0204  -0.0754 -0.0590 220 ILE B CB  
5686 C CG1 . ILE B 193 ? 1.3387 1.2290 1.0255 0.0328  -0.0977 -0.0449 220 ILE B CG1 
5687 C CG2 . ILE B 193 ? 1.1910 0.9782 0.9298 0.0386  -0.0772 -0.0416 220 ILE B CG2 
5688 C CD1 . ILE B 193 ? 1.4127 1.3275 1.1188 0.0354  -0.1131 -0.0464 220 ILE B CD1 
5689 N N   . ARG B 194 ? 1.4418 1.1887 1.1347 -0.0075 -0.0167 -0.0982 221 ARG B N   
5690 C CA  . ARG B 194 ? 1.2543 0.9489 0.9653 -0.0042 0.0089  -0.1043 221 ARG B CA  
5691 C C   . ARG B 194 ? 1.3220 1.0079 1.0260 0.0045  0.0287  -0.0972 221 ARG B C   
5692 O O   . ARG B 194 ? 1.3758 1.0377 1.1112 0.0202  0.0415  -0.0842 221 ARG B O   
5693 C CB  . ARG B 194 ? 1.3261 0.9930 1.0182 -0.0277 0.0277  -0.1370 221 ARG B CB  
5694 C CG  . ARG B 194 ? 1.3593 0.9662 1.0637 -0.0185 0.0593  -0.1422 221 ARG B CG  
5695 C CD  . ARG B 194 ? 1.2727 0.8634 1.0234 0.0058  0.0521  -0.1179 221 ARG B CD  
5696 N NE  . ARG B 194 ? 1.3129 0.8558 1.0762 0.0214  0.0823  -0.1179 221 ARG B NE  
5697 C CZ  . ARG B 194 ? 1.3370 0.8807 1.1197 0.0424  0.0956  -0.1031 221 ARG B CZ  
5698 N NH1 . ARG B 194 ? 1.3410 0.9234 1.1320 0.0462  0.0828  -0.0877 221 ARG B NH1 
5699 N NH2 . ARG B 194 ? 1.2650 0.7704 1.0592 0.0612  0.1246  -0.1020 221 ARG B NH2 
5700 N N   . LYS B 195 ? 1.3472 1.0599 1.0108 -0.0050 0.0313  -0.1041 222 LYS B N   
5701 C CA  . LYS B 195 ? 1.3065 1.0142 0.9569 0.0017  0.0534  -0.0981 222 LYS B CA  
5702 C C   . LYS B 195 ? 1.3846 1.1138 1.0456 0.0178  0.0417  -0.0631 222 LYS B C   
5703 O O   . LYS B 195 ? 1.5336 1.2657 1.1808 0.0218  0.0596  -0.0543 222 LYS B O   
5704 C CB  . LYS B 195 ? 1.2996 1.0209 0.8922 -0.0182 0.0664  -0.1261 222 LYS B CB  
5705 C CG  . LYS B 195 ? 1.5352 1.2169 1.1102 -0.0381 0.0887  -0.1647 222 LYS B CG  
5706 C CD  . LYS B 195 ? 1.5866 1.2694 1.1017 -0.0569 0.1101  -0.1948 222 LYS B CD  
5707 C CE  . LYS B 195 ? 1.7889 1.4128 1.2833 -0.0768 0.1394  -0.2346 222 LYS B CE  
5708 N NZ  . LYS B 195 ? 2.0753 1.6886 1.5067 -0.0947 0.1656  -0.2680 222 LYS B NZ  
5709 N N   . ARG B 196 ? 1.3984 1.1376 1.0806 0.0269  0.0155  -0.0434 223 ARG B N   
5710 C CA  . ARG B 196 ? 1.3564 1.1014 1.0453 0.0408  0.0063  -0.0106 223 ARG B CA  
5711 C C   . ARG B 196 ? 1.4570 1.2301 1.0979 0.0425  0.0083  -0.0001 223 ARG B C   
5712 O O   . ARG B 196 ? 1.4101 1.1771 1.0488 0.0523  0.0136  0.0275  223 ARG B O   
5713 C CB  . ARG B 196 ? 1.2959 1.0168 1.0245 0.0461  0.0221  0.0047  223 ARG B CB  
5714 C CG  . ARG B 196 ? 1.2277 0.9305 1.0046 0.0500  0.0127  0.0046  223 ARG B CG  
5715 C CD  . ARG B 196 ? 1.1922 0.8889 1.0105 0.0529  0.0238  0.0215  223 ARG B CD  
5716 N NE  . ARG B 196 ? 1.4620 1.1515 1.3237 0.0573  0.0143  0.0198  223 ARG B NE  
5717 C CZ  . ARG B 196 ? 1.3818 1.0685 1.2657 0.0631  0.0284  0.0092  223 ARG B CZ  
5718 N NH1 . ARG B 196 ? 1.2388 0.9218 1.1059 0.0642  0.0552  -0.0036 223 ARG B NH1 
5719 N NH2 . ARG B 196 ? 1.4428 1.1283 1.3624 0.0702  0.0169  0.0120  223 ARG B NH2 
5720 N N   . ASP B 197 ? 1.3854 1.1907 0.9853 0.0316  0.0048  -0.0215 224 ASP B N   
5721 C CA  . ASP B 197 ? 1.3254 1.1705 0.8764 0.0371  -0.0002 -0.0085 224 ASP B CA  
5722 C C   . ASP B 197 ? 1.4292 1.2930 0.9808 0.0579  -0.0253 0.0211  224 ASP B C   
5723 O O   . ASP B 197 ? 1.5891 1.4592 1.1160 0.0751  -0.0241 0.0517  224 ASP B O   
5724 C CB  . ASP B 197 ? 1.4406 1.3255 0.9477 0.0166  -0.0015 -0.0424 224 ASP B CB  
5725 C CG  . ASP B 197 ? 1.6582 1.5157 1.1499 -0.0004 0.0295  -0.0712 224 ASP B CG  
5726 O OD1 . ASP B 197 ? 1.6689 1.4966 1.1722 0.0096  0.0526  -0.0566 224 ASP B OD1 
5727 O OD2 . ASP B 197 ? 1.6456 1.5106 1.1131 -0.0244 0.0328  -0.1091 224 ASP B OD2 
5728 N N   . ARG B 198 ? 1.3525 1.2219 0.9295 0.0588  -0.0451 0.0142  225 ARG B N   
5729 C CA  . ARG B 198 ? 1.3429 1.2170 0.9278 0.0828  -0.0648 0.0415  225 ARG B CA  
5730 C C   . ARG B 198 ? 1.3961 1.2127 1.0263 0.0874  -0.0624 0.0501  225 ARG B C   
5731 O O   . ARG B 198 ? 1.4582 1.2610 1.1199 0.0759  -0.0642 0.0297  225 ARG B O   
5732 C CB  . ARG B 198 ? 1.3948 1.3232 0.9767 0.0821  -0.0876 0.0285  225 ARG B CB  
5733 C CG  . ARG B 198 ? 1.5870 1.5902 1.1237 0.0823  -0.0976 0.0271  225 ARG B CG  
5734 C CD  . ARG B 198 ? 1.7807 1.8482 1.3251 0.0763  -0.1199 0.0119  225 ARG B CD  
5735 N NE  . ARG B 198 ? 1.6555 1.7092 1.2306 0.1015  -0.1319 0.0321  225 ARG B NE  
5736 C CZ  . ARG B 198 ? 1.7047 1.8071 1.2965 0.1016  -0.1487 0.0242  225 ARG B CZ  
5737 N NH1 . ARG B 198 ? 1.8369 2.0088 1.4215 0.0734  -0.1570 -0.0038 225 ARG B NH1 
5738 N NH2 . ARG B 198 ? 1.7011 1.7828 1.3165 0.1282  -0.1557 0.0435  225 ARG B NH2 
5739 N N   . ARG B 199 ? 1.4440 1.2266 1.0747 0.1025  -0.0575 0.0799  226 ARG B N   
5740 C CA  . ARG B 199 ? 1.4161 1.1486 1.0850 0.1033  -0.0574 0.0871  226 ARG B CA  
5741 C C   . ARG B 199 ? 1.3801 1.1023 1.0463 0.1249  -0.0753 0.1016  226 ARG B C   
5742 O O   . ARG B 199 ? 1.2890 1.0397 0.9236 0.1454  -0.0840 0.1159  226 ARG B O   
5743 C CB  . ARG B 199 ? 1.4740 1.1699 1.1470 0.0989  -0.0375 0.1071  226 ARG B CB  
5744 C CG  . ARG B 199 ? 1.4374 1.1424 1.1192 0.0811  -0.0158 0.0945  226 ARG B CG  
5745 C CD  . ARG B 199 ? 1.7103 1.3895 1.3951 0.0764  0.0053  0.1184  226 ARG B CD  
5746 N NE  . ARG B 199 ? 1.9230 1.6186 1.6109 0.0645  0.0294  0.1096  226 ARG B NE  
5747 C CZ  . ARG B 199 ? 1.9837 1.6769 1.7164 0.0529  0.0416  0.0990  226 ARG B CZ  
5748 N NH1 . ARG B 199 ? 1.9106 1.5898 1.6885 0.0488  0.0296  0.0954  226 ARG B NH1 
5749 N NH2 . ARG B 199 ? 1.8704 1.5798 1.6007 0.0477  0.0670  0.0925  226 ARG B NH2 
5750 N N   . GLY B 200 ? 1.3175 1.0020 1.0158 0.1225  -0.0801 0.0980  227 GLY B N   
5751 C CA  . GLY B 200 ? 1.3633 1.0269 1.0584 0.1428  -0.0932 0.1085  227 GLY B CA  
5752 C C   . GLY B 200 ? 1.2346 0.9014 0.9599 0.1373  -0.1059 0.0870  227 GLY B C   
5753 O O   . GLY B 200 ? 1.2995 0.9686 1.0527 0.1178  -0.1024 0.0687  227 GLY B O   
5754 N N   . CYS B 201 ? 1.2697 0.9361 0.9875 0.1581  -0.1183 0.0917  228 CYS B N   
5755 C CA  . CYS B 201 ? 1.2792 0.9547 1.0188 0.1567  -0.1298 0.0741  228 CYS B CA  
5756 C C   . CYS B 201 ? 1.2830 1.0164 1.0102 0.1712  -0.1399 0.0727  228 CYS B C   
5757 O O   . CYS B 201 ? 1.5124 1.2585 1.2153 0.1981  -0.1431 0.0920  228 CYS B O   
5758 C CB  . CYS B 201 ? 1.1418 0.7645 0.8862 0.1663  -0.1340 0.0780  228 CYS B CB  
5759 S SG  . CYS B 201 ? 1.4691 1.0368 1.2331 0.1425  -0.1251 0.0774  228 CYS B SG  
5760 N N   . PHE B 202 ? 1.3037 1.0735 1.0477 0.1538  -0.1432 0.0512  229 PHE B N   
5761 C CA  . PHE B 202 ? 1.2695 1.1078 1.0065 0.1558  -0.1513 0.0453  229 PHE B CA  
5762 C C   . PHE B 202 ? 1.2287 1.0780 0.9853 0.1573  -0.1580 0.0351  229 PHE B C   
5763 O O   . PHE B 202 ? 1.1907 1.0036 0.9666 0.1450  -0.1544 0.0237  229 PHE B O   
5764 C CB  . PHE B 202 ? 1.2394 1.1133 0.9725 0.1261  -0.1451 0.0259  229 PHE B CB  
5765 C CG  . PHE B 202 ? 1.1986 1.0577 0.9120 0.1225  -0.1349 0.0337  229 PHE B CG  
5766 C CD1 . PHE B 202 ? 1.1604 1.0571 0.8428 0.1383  -0.1387 0.0512  229 PHE B CD1 
5767 C CD2 . PHE B 202 ? 1.2346 1.0471 0.9604 0.1064  -0.1204 0.0264  229 PHE B CD2 
5768 C CE1 . PHE B 202 ? 1.2632 1.1458 0.9238 0.1357  -0.1270 0.0605  229 PHE B CE1 
5769 C CE2 . PHE B 202 ? 1.2996 1.1021 1.0084 0.1032  -0.1081 0.0346  229 PHE B CE2 
5770 C CZ  . PHE B 202 ? 1.3745 1.2092 1.0488 0.1167  -0.1108 0.0514  229 PHE B CZ  
5771 N N   . ALA B 203 ? 1.2038 1.1086 0.9549 0.1749  -0.1669 0.0415  230 ALA B N   
5772 C CA  . ALA B 203 ? 1.2904 1.2185 1.0594 0.1752  -0.1709 0.0325  230 ALA B CA  
5773 C C   . ALA B 203 ? 1.2609 1.2225 1.0441 0.1365  -0.1665 0.0077  230 ALA B C   
5774 O O   . ALA B 203 ? 1.1550 1.1721 0.9302 0.1190  -0.1680 -0.0008 230 ALA B O   
5775 C CB  . ALA B 203 ? 1.0275 1.0149 0.7895 0.2079  -0.1794 0.0488  230 ALA B CB  
5776 N N   . VAL B 204 ? 1.1157 1.0405 0.9158 0.1224  -0.1599 -0.0042 231 VAL B N   
5777 C CA  . VAL B 204 ? 1.1378 1.0744 0.9474 0.0860  -0.1499 -0.0266 231 VAL B CA  
5778 C C   . VAL B 204 ? 1.2414 1.1798 1.0667 0.0858  -0.1476 -0.0292 231 VAL B C   
5779 O O   . VAL B 204 ? 1.2556 1.1670 1.0837 0.1120  -0.1522 -0.0168 231 VAL B O   
5780 C CB  . VAL B 204 ? 1.0993 0.9758 0.9090 0.0681  -0.1361 -0.0366 231 VAL B CB  
5781 C CG1 . VAL B 204 ? 1.0362 0.9178 0.8282 0.0653  -0.1350 -0.0354 231 VAL B CG1 
5782 C CG2 . VAL B 204 ? 1.1055 0.9219 0.9264 0.0859  -0.1357 -0.0261 231 VAL B CG2 
5783 N N   . PRO B 205 ? 1.1605 1.1286 0.9930 0.0544  -0.1388 -0.0461 232 PRO B N   
5784 C CA  . PRO B 205 ? 1.1472 1.1171 0.9931 0.0516  -0.1327 -0.0466 232 PRO B CA  
5785 C C   . PRO B 205 ? 1.1314 1.0260 0.9800 0.0476  -0.1190 -0.0481 232 PRO B C   
5786 O O   . PRO B 205 ? 1.3221 1.2119 1.1772 0.0488  -0.1127 -0.0451 232 PRO B O   
5787 C CB  . PRO B 205 ? 1.2491 1.2821 1.1003 0.0128  -0.1262 -0.0648 232 PRO B CB  
5788 C CG  . PRO B 205 ? 1.2864 1.3098 1.1229 -0.0138 -0.1215 -0.0816 232 PRO B CG  
5789 C CD  . PRO B 205 ? 1.2354 1.2449 1.0604 0.0183  -0.1341 -0.0659 232 PRO B CD  
5790 N N   . MET B 206 ? 1.2021 1.0431 1.0458 0.0455  -0.1131 -0.0503 233 MET B N   
5791 C CA  . MET B 206 ? 1.2582 1.0377 1.1059 0.0455  -0.0994 -0.0490 233 MET B CA  
5792 C C   . MET B 206 ? 1.1503 0.8887 0.9989 0.0592  -0.1011 -0.0429 233 MET B C   
5793 O O   . MET B 206 ? 1.1402 0.8797 0.9828 0.0495  -0.0978 -0.0497 233 MET B O   
5794 C CB  . MET B 206 ? 1.1679 0.9289 1.0118 0.0116  -0.0755 -0.0655 233 MET B CB  
5795 C CG  . MET B 206 ? 1.1460 0.8382 0.9901 0.0175  -0.0572 -0.0606 233 MET B CG  
5796 S SD  . MET B 206 ? 1.2608 0.9368 1.1106 0.0416  -0.0587 -0.0411 233 MET B SD  
5797 C CE  . MET B 206 ? 1.3296 1.0237 1.1753 0.0088  -0.0397 -0.0510 233 MET B CE  
5798 N N   . VAL B 207 ? 1.1509 0.8595 1.0067 0.0805  -0.1061 -0.0305 234 VAL B N   
5799 C CA  . VAL B 207 ? 1.1546 0.8301 1.0186 0.0896  -0.1048 -0.0246 234 VAL B CA  
5800 C C   . VAL B 207 ? 1.0849 0.7329 0.9559 0.1007  -0.0987 -0.0165 234 VAL B C   
5801 O O   . VAL B 207 ? 1.2418 0.8947 1.1084 0.1078  -0.1023 -0.0120 234 VAL B O   
5802 C CB  . VAL B 207 ? 1.0400 0.7191 0.9057 0.1052  -0.1232 -0.0157 234 VAL B CB  
5803 C CG1 . VAL B 207 ? 1.0983 0.8027 0.9523 0.1006  -0.1277 -0.0178 234 VAL B CG1 
5804 C CG2 . VAL B 207 ? 1.0421 0.7206 0.9047 0.1231  -0.1380 -0.0085 234 VAL B CG2 
5805 N N   . HIS B 208 ? 1.1415 0.7649 1.0226 0.1053  -0.0883 -0.0126 235 HIS B N   
5806 C CA  . HIS B 208 ? 1.0486 0.6512 0.9357 0.1211  -0.0817 -0.0007 235 HIS B CA  
5807 C C   . HIS B 208 ? 1.0857 0.6845 0.9918 0.1339  -0.0812 0.0076  235 HIS B C   
5808 O O   . HIS B 208 ? 1.1791 0.7887 1.0932 0.1279  -0.0853 0.0036  235 HIS B O   
5809 C CB  . HIS B 208 ? 1.1960 0.7688 1.0717 0.1113  -0.0545 -0.0038 235 HIS B CB  
5810 C CG  . HIS B 208 ? 1.1290 0.6815 0.9979 0.0907  -0.0321 -0.0191 235 HIS B CG  
5811 N ND1 . HIS B 208 ? 1.0829 0.6017 0.9553 0.0995  -0.0109 -0.0164 235 HIS B ND1 
5812 C CD2 . HIS B 208 ? 1.1366 0.7010 0.9928 0.0624  -0.0271 -0.0384 235 HIS B CD2 
5813 C CE1 . HIS B 208 ? 1.1795 0.6817 1.0377 0.0764  0.0077  -0.0357 235 HIS B CE1 
5814 N NE2 . HIS B 208 ? 1.1166 0.6488 0.9645 0.0516  -0.0033 -0.0500 235 HIS B NE2 
5815 N N   . SER B 209 ? 1.1350 0.7240 1.0486 0.1534  -0.0756 0.0218  236 SER B N   
5816 C CA  . SER B 209 ? 1.1130 0.7078 1.0490 0.1702  -0.0710 0.0332  236 SER B CA  
5817 C C   . SER B 209 ? 1.1738 0.8077 1.1294 0.1744  -0.0991 0.0378  236 SER B C   
5818 O O   . SER B 209 ? 1.0759 0.7307 1.0429 0.1919  -0.1103 0.0507  236 SER B O   
5819 C CB  . SER B 209 ? 1.0870 0.6649 1.0260 0.1613  -0.0474 0.0247  236 SER B CB  
5820 O OG  . SER B 209 ? 1.3019 0.8371 1.2184 0.1522  -0.0198 0.0162  236 SER B OG  
5821 N N   . THR B 210 ? 1.1652 0.8920 0.9706 -0.0764 0.1921  -0.0562 237 THR B N   
5822 C CA  . THR B 210 ? 1.0829 0.8119 0.8788 -0.0765 0.1992  -0.0459 237 THR B CA  
5823 C C   . THR B 210 ? 1.1192 0.8399 0.8977 -0.0770 0.1837  -0.0352 237 THR B C   
5824 O O   . THR B 210 ? 1.2563 0.9643 1.0056 -0.0811 0.1730  -0.0372 237 THR B O   
5825 C CB  . THR B 210 ? 0.9647 0.6878 0.7339 -0.0819 0.2162  -0.0510 237 THR B CB  
5826 O OG1 . THR B 210 ? 1.5451 1.2522 1.2756 -0.0871 0.2132  -0.0594 237 THR B OG1 
5827 C CG2 . THR B 210 ? 0.9784 0.7135 0.7737 -0.0794 0.2331  -0.0587 237 THR B CG2 
5828 N N   . PHE B 211 ? 1.1347 0.8615 0.9300 -0.0723 0.1819  -0.0244 238 PHE B N   
5829 C CA  . PHE B 211 ? 1.1340 0.8520 0.9169 -0.0707 0.1691  -0.0135 238 PHE B CA  
5830 C C   . PHE B 211 ? 1.1086 0.8284 0.9027 -0.0668 0.1754  -0.0055 238 PHE B C   
5831 O O   . PHE B 211 ? 1.0860 0.8168 0.8998 -0.0650 0.1860  -0.0080 238 PHE B O   
5832 C CB  . PHE B 211 ? 0.9980 0.7210 0.7993 -0.0664 0.1510  -0.0108 238 PHE B CB  
5833 C CG  . PHE B 211 ? 1.1459 0.8867 0.9890 -0.0607 0.1535  -0.0116 238 PHE B CG  
5834 C CD1 . PHE B 211 ? 1.0746 0.8244 0.9410 -0.0529 0.1556  -0.0032 238 PHE B CD1 
5835 C CD2 . PHE B 211 ? 1.0402 0.7869 0.8980 -0.0631 0.1545  -0.0207 238 PHE B CD2 
5836 C CE1 . PHE B 211 ? 1.0846 0.8508 0.9853 -0.0481 0.1595  -0.0023 238 PHE B CE1 
5837 C CE2 . PHE B 211 ? 0.8885 0.6504 0.7842 -0.0587 0.1570  -0.0186 238 PHE B CE2 
5838 C CZ  . PHE B 211 ? 1.0225 0.7951 0.9383 -0.0515 0.1600  -0.0086 238 PHE B CZ  
5839 N N   . LEU B 212 ? 1.0921 0.7993 0.8723 -0.0654 0.1673  0.0041  239 LEU B N   
5840 C CA  . LEU B 212 ? 0.9247 0.6267 0.7104 -0.0620 0.1715  0.0105  239 LEU B CA  
5841 C C   . LEU B 212 ? 1.0812 0.7842 0.8860 -0.0515 0.1600  0.0173  239 LEU B C   
5842 O O   . LEU B 212 ? 1.1465 0.8443 0.9460 -0.0497 0.1455  0.0231  239 LEU B O   
5843 C CB  . LEU B 212 ? 0.9571 0.6396 0.7114 -0.0695 0.1742  0.0167  239 LEU B CB  
5844 C CG  . LEU B 212 ? 1.0987 0.7717 0.8559 -0.0698 0.1805  0.0209  239 LEU B CG  
5845 C CD1 . LEU B 212 ? 0.9924 0.6793 0.7651 -0.0733 0.1940  0.0129  239 LEU B CD1 
5846 C CD2 . LEU B 212 ? 1.0851 0.7362 0.8118 -0.0782 0.1807  0.0301  239 LEU B CD2 
5847 N N   . ILE B 213 ? 0.9459 0.6561 0.7728 -0.0444 0.1663  0.0166  240 ILE B N   
5848 C CA  . ILE B 213 ? 0.8271 0.5391 0.6747 -0.0328 0.1604  0.0220  240 ILE B CA  
5849 C C   . ILE B 213 ? 1.0927 0.7861 0.9309 -0.0296 0.1640  0.0249  240 ILE B C   
5850 O O   . ILE B 213 ? 1.0701 0.7596 0.9012 -0.0339 0.1743  0.0198  240 ILE B O   
5851 C CB  . ILE B 213 ? 0.9737 0.7072 0.8520 -0.0262 0.1667  0.0187  240 ILE B CB  
5852 C CG1 . ILE B 213 ? 0.9008 0.6493 0.7891 -0.0314 0.1643  0.0149  240 ILE B CG1 
5853 C CG2 . ILE B 213 ? 0.9010 0.6395 0.8036 -0.0136 0.1623  0.0247  240 ILE B CG2 
5854 C CD1 . ILE B 213 ? 0.9803 0.7492 0.9001 -0.0260 0.1702  0.0147  240 ILE B CD1 
5855 N N   . ASP B 214 ? 1.1779 0.8590 1.0180 -0.0222 0.1542  0.0332  241 ASP B N   
5856 C CA  . ASP B 214 ? 0.9971 0.6551 0.8298 -0.0181 0.1561  0.0362  241 ASP B CA  
5857 C C   . ASP B 214 ? 1.1062 0.7707 0.9641 -0.0044 0.1632  0.0318  241 ASP B C   
5858 O O   . ASP B 214 ? 1.0892 0.7595 0.9701 0.0078  0.1576  0.0368  241 ASP B O   
5859 C CB  . ASP B 214 ? 0.9647 0.6039 0.7871 -0.0161 0.1415  0.0488  241 ASP B CB  
5860 C CG  . ASP B 214 ? 1.1191 0.7280 0.9273 -0.0163 0.1434  0.0530  241 ASP B CG  
5861 O OD1 . ASP B 214 ? 1.0382 0.6409 0.8544 -0.0118 0.1535  0.0452  241 ASP B OD1 
5862 O OD2 . ASP B 214 ? 1.1788 0.7683 0.9658 -0.0217 0.1342  0.0644  241 ASP B OD2 
5863 N N   . LEU B 215 ? 1.1080 0.7723 0.9615 -0.0065 0.1756  0.0224  242 LEU B N   
5864 C CA  . LEU B 215 ? 0.9924 0.6605 0.8611 0.0057  0.1848  0.0164  242 LEU B CA  
5865 C C   . LEU B 215 ? 1.0445 0.6847 0.9093 0.0143  0.1851  0.0158  242 LEU B C   
5866 O O   . LEU B 215 ? 1.0120 0.6512 0.8861 0.0260  0.1944  0.0091  242 LEU B O   
5867 C CB  . LEU B 215 ? 0.9610 0.6384 0.8219 -0.0002 0.1955  0.0067  242 LEU B CB  
5868 C CG  . LEU B 215 ? 1.0434 0.7468 0.9120 -0.0071 0.1964  0.0073  242 LEU B CG  
5869 C CD1 . LEU B 215 ? 1.0204 0.7326 0.8836 -0.0109 0.2052  0.0002  242 LEU B CD1 
5870 C CD2 . LEU B 215 ? 0.9908 0.7147 0.8866 0.0014  0.1943  0.0127  242 LEU B CD2 
5871 N N   . ARG B 216 ? 1.0868 0.7025 0.9366 0.0091  0.1763  0.0227  243 ARG B N   
5872 C CA  . ARG B 216 ? 1.0197 0.6072 0.8723 0.0196  0.1741  0.0249  243 ARG B CA  
5873 C C   . ARG B 216 ? 1.0862 0.6826 0.9674 0.0358  0.1668  0.0341  243 ARG B C   
5874 O O   . ARG B 216 ? 1.0132 0.5983 0.9110 0.0515  0.1710  0.0320  243 ARG B O   
5875 C CB  . ARG B 216 ? 1.0654 0.6231 0.8947 0.0082  0.1663  0.0327  243 ARG B CB  
5876 C CG  . ARG B 216 ? 1.0713 0.6257 0.8779 -0.0104 0.1718  0.0268  243 ARG B CG  
5877 C CD  . ARG B 216 ? 1.1244 0.6552 0.9112 -0.0226 0.1649  0.0387  243 ARG B CD  
5878 N NE  . ARG B 216 ? 1.1575 0.6943 0.9423 -0.0208 0.1538  0.0529  243 ARG B NE  
5879 C CZ  . ARG B 216 ? 1.1916 0.7051 0.9604 -0.0252 0.1446  0.0679  243 ARG B CZ  
5880 N NH1 . ARG B 216 ? 1.3255 0.8074 1.0824 -0.0319 0.1461  0.0717  243 ARG B NH1 
5881 N NH2 . ARG B 216 ? 1.0869 0.6080 0.8507 -0.0237 0.1324  0.0799  243 ARG B NH2 
5882 N N   . LYS B 217 ? 1.1121 0.7288 1.0012 0.0324  0.1558  0.0436  244 LYS B N   
5883 C CA  . LYS B 217 ? 1.0178 0.6469 0.9382 0.0458  0.1452  0.0537  244 LYS B CA  
5884 C C   . LYS B 217 ? 1.0143 0.6670 0.9692 0.0602  0.1580  0.0471  244 LYS B C   
5885 O O   . LYS B 217 ? 1.0521 0.7255 1.0078 0.0555  0.1691  0.0390  244 LYS B O   
5886 C CB  . LYS B 217 ? 1.0153 0.6621 0.9332 0.0360  0.1298  0.0622  244 LYS B CB  
5887 C CG  . LYS B 217 ? 0.9795 0.6042 0.8607 0.0227  0.1182  0.0703  244 LYS B CG  
5888 C CD  . LYS B 217 ? 0.9679 0.5626 0.8463 0.0304  0.1089  0.0821  244 LYS B CD  
5889 C CE  . LYS B 217 ? 1.2057 0.7824 1.0488 0.0175  0.0944  0.0952  244 LYS B CE  
5890 N NZ  . LYS B 217 ? 1.1111 0.6831 0.9184 -0.0010 0.1053  0.0882  244 LYS B NZ  
5891 N N   . ALA B 218 ? 1.0049 0.6546 0.9896 0.0782  0.1572  0.0519  245 ALA B N   
5892 C CA  . ALA B 218 ? 0.8963 0.5689 0.9157 0.0933  0.1728  0.0463  245 ALA B CA  
5893 C C   . ALA B 218 ? 1.0176 0.7299 1.0659 0.0904  0.1688  0.0521  245 ALA B C   
5894 O O   . ALA B 218 ? 0.9814 0.7169 1.0492 0.0956  0.1852  0.0468  245 ALA B O   
5895 C CB  . ALA B 218 ? 0.9168 0.5783 0.9671 0.1147  0.1733  0.0507  245 ALA B CB  
5896 N N   . ALA B 219 ? 0.9754 0.6944 1.0254 0.0815  0.1472  0.0630  246 ALA B N   
5897 C CA  . ALA B 219 ? 0.8800 0.6337 0.9588 0.0773  0.1407  0.0676  246 ALA B CA  
5898 C C   . ALA B 219 ? 0.9344 0.6994 0.9943 0.0633  0.1517  0.0582  246 ALA B C   
5899 O O   . ALA B 219 ? 1.0422 0.8357 1.1300 0.0620  0.1552  0.0593  246 ALA B O   
5900 C CB  . ALA B 219 ? 1.0844 0.8382 1.1631 0.0701  0.1125  0.0796  246 ALA B CB  
5901 N N   . SER B 220 ? 0.9939 0.7376 1.0105 0.0527  0.1567  0.0503  247 SER B N   
5902 C CA  . SER B 220 ? 1.1024 0.8563 1.1035 0.0405  0.1657  0.0426  247 SER B CA  
5903 C C   . SER B 220 ? 1.1079 0.8786 1.1251 0.0475  0.1859  0.0372  247 SER B C   
5904 O O   . SER B 220 ? 0.9827 0.7697 1.0013 0.0398  0.1915  0.0352  247 SER B O   
5905 C CB  . SER B 220 ? 1.0517 0.7811 1.0090 0.0290  0.1674  0.0362  247 SER B CB  
5906 O OG  . SER B 220 ? 1.0171 0.7280 0.9619 0.0352  0.1793  0.0297  247 SER B OG  
5907 N N   . ARG B 221 ? 1.0075 0.7734 1.0360 0.0625  0.1977  0.0352  248 ARG B N   
5908 C CA  . ARG B 221 ? 1.0338 0.8146 1.0718 0.0697  0.2191  0.0301  248 ARG B CA  
5909 C C   . ARG B 221 ? 1.0456 0.8616 1.1238 0.0706  0.2219  0.0383  248 ARG B C   
5910 O O   . ARG B 221 ? 0.9808 0.8117 1.0612 0.0709  0.2386  0.0366  248 ARG B O   
5911 C CB  . ARG B 221 ? 0.8525 0.6199 0.8957 0.0873  0.2320  0.0251  248 ARG B CB  
5912 C CG  . ARG B 221 ? 0.9900 0.7197 0.9934 0.0855  0.2315  0.0152  248 ARG B CG  
5913 C CD  . ARG B 221 ? 1.0571 0.7702 1.0647 0.1035  0.2459  0.0073  248 ARG B CD  
5914 N NE  . ARG B 221 ? 1.4069 1.1353 1.4153 0.1109  0.2690  -0.0004 248 ARG B NE  
5915 C CZ  . ARG B 221 ? 1.4894 1.2072 1.4597 0.1047  0.2794  -0.0123 248 ARG B CZ  
5916 N NH1 . ARG B 221 ? 1.4457 1.1403 1.3795 0.0905  0.2690  -0.0183 248 ARG B NH1 
5917 N NH2 . ARG B 221 ? 1.4465 1.1785 1.4155 0.1123  0.3006  -0.0175 248 ARG B NH2 
5918 N N   . ASN B 222 ? 1.0622 0.8912 1.1713 0.0699  0.2049  0.0481  249 ASN B N   
5919 C CA  . ASN B 222 ? 0.8536 0.7158 1.0063 0.0686  0.2044  0.0565  249 ASN B CA  
5920 C C   . ASN B 222 ? 0.9490 0.8173 1.0938 0.0509  0.1927  0.0571  249 ASN B C   
5921 O O   . ASN B 222 ? 0.8929 0.7861 1.0726 0.0470  0.1917  0.0635  249 ASN B O   
5922 C CB  . ASN B 222 ? 0.8456 0.7208 1.0428 0.0778  0.1902  0.0668  249 ASN B CB  
5923 C CG  . ASN B 222 ? 0.9979 0.8708 1.2141 0.0982  0.2044  0.0667  249 ASN B CG  
5924 O OD1 . ASN B 222 ? 1.0308 0.9106 1.2500 0.1067  0.2297  0.0619  249 ASN B OD1 
5925 N ND2 . ASN B 222 ? 1.1216 0.9831 1.3492 0.1066  0.1884  0.0722  249 ASN B ND2 
5926 N N   . LEU B 223 ? 0.9963 0.8422 1.0989 0.0401  0.1846  0.0505  250 LEU B N   
5927 C CA  . LEU B 223 ? 0.9370 0.7863 1.0312 0.0249  0.1761  0.0487  250 LEU B CA  
5928 C C   . LEU B 223 ? 0.9241 0.7839 1.0178 0.0216  0.1933  0.0468  250 LEU B C   
5929 O O   . LEU B 223 ? 0.9979 0.8533 1.0759 0.0274  0.2098  0.0435  250 LEU B O   
5930 C CB  . LEU B 223 ? 0.9319 0.7556 0.9826 0.0157  0.1659  0.0424  250 LEU B CB  
5931 C CG  . LEU B 223 ? 0.9458 0.7559 0.9890 0.0166  0.1470  0.0465  250 LEU B CG  
5932 C CD1 . LEU B 223 ? 0.8363 0.6204 0.8329 0.0078  0.1433  0.0413  250 LEU B CD1 
5933 C CD2 . LEU B 223 ? 0.9114 0.7360 0.9795 0.0114  0.1277  0.0518  250 LEU B CD2 
5934 N N   . ALA B 224 ? 0.9207 0.7928 1.0305 0.0119  0.1881  0.0490  251 ALA B N   
5935 C CA  . ALA B 224 ? 0.8720 0.7549 0.9869 0.0086  0.2024  0.0508  251 ALA B CA  
5936 C C   . ALA B 224 ? 0.9462 0.8298 1.0669 -0.0043 0.1919  0.0497  251 ALA B C   
5937 O O   . ALA B 224 ? 0.9619 0.8523 1.1072 -0.0092 0.1774  0.0519  251 ALA B O   
5938 C CB  . ALA B 224 ? 0.7777 0.6849 0.9305 0.0166  0.2164  0.0607  251 ALA B CB  
5939 N N   . PHE B 225 ? 0.9924 0.8684 1.0918 -0.0096 0.1982  0.0457  252 PHE B N   
5940 C CA  . PHE B 225 ? 0.8986 0.7733 1.0057 -0.0201 0.1911  0.0438  252 PHE B CA  
5941 C C   . PHE B 225 ? 0.8913 0.7839 1.0349 -0.0220 0.1978  0.0543  252 PHE B C   
5942 O O   . PHE B 225 ? 0.9544 0.8483 1.1199 -0.0304 0.1882  0.0544  252 PHE B O   
5943 C CB  . PHE B 225 ? 0.8266 0.6870 0.9022 -0.0238 0.1949  0.0363  252 PHE B CB  
5944 C CG  . PHE B 225 ? 0.8398 0.6825 0.8826 -0.0254 0.1881  0.0267  252 PHE B CG  
5945 C CD1 . PHE B 225 ? 0.7636 0.5960 0.7984 -0.0327 0.1761  0.0193  252 PHE B CD1 
5946 C CD2 . PHE B 225 ? 0.8805 0.7153 0.8986 -0.0205 0.1942  0.0249  252 PHE B CD2 
5947 C CE1 . PHE B 225 ? 0.8071 0.6235 0.8094 -0.0349 0.1720  0.0123  252 PHE B CE1 
5948 C CE2 . PHE B 225 ? 0.9192 0.7373 0.9091 -0.0234 0.1888  0.0183  252 PHE B CE2 
5949 C CZ  . PHE B 225 ? 0.9258 0.7357 0.9076 -0.0305 0.1785  0.0130  252 PHE B CZ  
5950 N N   . TYR B 226 ? 0.8216 0.7264 0.9706 -0.0151 0.2146  0.0630  253 TYR B N   
5951 C CA  . TYR B 226 ? 0.8925 0.8150 1.0735 -0.0168 0.2246  0.0761  253 TYR B CA  
5952 C C   . TYR B 226 ? 0.9905 0.9278 1.1762 -0.0061 0.2428  0.0839  253 TYR B C   
5953 O O   . TYR B 226 ? 1.0628 0.9909 1.2153 0.0016  0.2500  0.0776  253 TYR B O   
5954 C CB  . TYR B 226 ? 0.9287 0.8450 1.0983 -0.0219 0.2294  0.0790  253 TYR B CB  
5955 C CG  . TYR B 226 ? 0.9425 0.8730 1.1466 -0.0265 0.2366  0.0943  253 TYR B CG  
5956 C CD1 . TYR B 226 ? 0.9268 0.8567 1.1637 -0.0363 0.2250  0.0957  253 TYR B CD1 
5957 C CD2 . TYR B 226 ? 0.8691 0.8117 1.0711 -0.0218 0.2551  0.1074  253 TYR B CD2 
5958 C CE1 . TYR B 226 ? 1.0016 0.9424 1.2728 -0.0419 0.2314  0.1112  253 TYR B CE1 
5959 C CE2 . TYR B 226 ? 1.0400 0.9952 1.2732 -0.0269 0.2629  0.1242  253 TYR B CE2 
5960 C CZ  . TYR B 226 ? 1.0584 1.0126 1.3285 -0.0373 0.2509  0.1267  253 TYR B CZ  
5961 O OH  . TYR B 226 ? 1.0880 1.0528 1.3918 -0.0438 0.2585  0.1448  253 TYR B OH  
5962 N N   . PRO B 227 ? 0.9246 0.8842 1.1513 -0.0056 0.2513  0.0966  254 PRO B N   
5963 C CA  . PRO B 227 ? 0.9223 0.8942 1.1952 -0.0157 0.2420  0.1047  254 PRO B CA  
5964 C C   . PRO B 227 ? 0.8996 0.8739 1.1953 -0.0172 0.2223  0.0991  254 PRO B C   
5965 O O   . PRO B 227 ? 0.9376 0.9052 1.2149 -0.0091 0.2181  0.0915  254 PRO B O   
5966 C CB  . PRO B 227 ? 0.6514 0.6483 0.9557 -0.0126 0.2634  0.1217  254 PRO B CB  
5967 C CG  . PRO B 227 ? 0.6598 0.6612 0.9459 0.0022  0.2790  0.1187  254 PRO B CG  
5968 C CD  . PRO B 227 ? 0.8801 0.8548 1.1097 0.0052  0.2739  0.1041  254 PRO B CD  
5969 N N   . PRO B 228 ? 0.9288 0.9106 1.2631 -0.0280 0.2081  0.1028  255 PRO B N   
5970 C CA  . PRO B 228 ? 1.0359 1.0225 1.3930 -0.0299 0.1869  0.0990  255 PRO B CA  
5971 C C   . PRO B 228 ? 0.9104 0.9201 1.2958 -0.0175 0.1957  0.1072  255 PRO B C   
5972 O O   . PRO B 228 ? 1.0112 1.0396 1.4151 -0.0107 0.2192  0.1179  255 PRO B O   
5973 C CB  . PRO B 228 ? 0.9308 0.9250 1.3309 -0.0449 0.1737  0.1039  255 PRO B CB  
5974 C CG  . PRO B 228 ? 0.9186 0.8970 1.2998 -0.0515 0.1816  0.1030  255 PRO B CG  
5975 C CD  . PRO B 228 ? 0.8651 0.8461 1.2197 -0.0403 0.2071  0.1089  255 PRO B CD  
5976 N N   . HIS B 229 ? 0.9251 0.9324 1.3123 -0.0139 0.1773  0.1022  256 HIS B N   
5977 C CA  . HIS B 229 ? 0.8960 0.9241 1.3158 -0.0008 0.1817  0.1094  256 HIS B CA  
5978 C C   . HIS B 229 ? 0.8835 0.9470 1.3714 -0.0035 0.1891  0.1247  256 HIS B C   
5979 O O   . HIS B 229 ? 0.9402 1.0091 1.4545 -0.0188 0.1768  0.1282  256 HIS B O   
5980 C CB  . HIS B 229 ? 0.8344 0.8534 1.2499 0.0003  0.1537  0.1042  256 HIS B CB  
5981 C CG  . HIS B 229 ? 0.9915 1.0239 1.4303 0.0172  0.1577  0.1099  256 HIS B CG  
5982 N ND1 . HIS B 229 ? 0.9445 1.0098 1.4499 0.0211  0.1534  0.1222  256 HIS B ND1 
5983 C CD2 . HIS B 229 ? 0.9618 0.9784 1.3696 0.0317  0.1656  0.1051  256 HIS B CD2 
5984 C CE1 . HIS B 229 ? 0.9980 1.0675 1.5130 0.0388  0.1592  0.1246  256 HIS B CE1 
5985 N NE2 . HIS B 229 ? 1.0286 1.0668 1.4835 0.0454  0.1666  0.1139  256 HIS B NE2 
5986 N N   . PRO B 230 ? 0.8341 0.9217 1.3532 0.0105  0.2101  0.1338  257 PRO B N   
5987 C CA  . PRO B 230 ? 0.8363 0.9614 1.4252 0.0075  0.2205  0.1501  257 PRO B CA  
5988 C C   . PRO B 230 ? 0.8380 0.9796 1.4812 -0.0045 0.1898  0.1550  257 PRO B C   
5989 O O   . PRO B 230 ? 0.8747 1.0415 1.5725 -0.0151 0.1923  0.1674  257 PRO B O   
5990 C CB  . PRO B 230 ? 0.8786 1.0233 1.4864 0.0284  0.2459  0.1549  257 PRO B CB  
5991 C CG  . PRO B 230 ? 0.7412 0.8545 1.2777 0.0389  0.2589  0.1418  257 PRO B CG  
5992 C CD  . PRO B 230 ? 0.7753 0.8555 1.2652 0.0294  0.2301  0.1290  257 PRO B CD  
5993 N N   . ASP B 231 ? 0.8905 1.0180 1.5196 -0.0044 0.1598  0.1465  258 ASP B N   
5994 C CA  . ASP B 231 ? 0.8590 0.9990 1.5317 -0.0168 0.1257  0.1496  258 ASP B CA  
5995 C C   . ASP B 231 ? 0.9397 1.0530 1.5811 -0.0370 0.1019  0.1385  258 ASP B C   
5996 O O   . ASP B 231 ? 0.9902 1.1093 1.6610 -0.0501 0.0713  0.1384  258 ASP B O   
5997 C CB  . ASP B 231 ? 0.7293 0.8686 1.4032 -0.0055 0.1040  0.1482  258 ASP B CB  
5998 C CG  . ASP B 231 ? 0.9553 1.1213 1.6691 0.0160  0.1261  0.1584  258 ASP B CG  
5999 O OD1 . ASP B 231 ? 0.8603 1.0604 1.6312 0.0178  0.1478  0.1707  258 ASP B OD1 
6000 O OD2 . ASP B 231 ? 1.0322 1.1842 1.7209 0.0312  0.1231  0.1544  258 ASP B OD2 
6001 N N   . TYR B 232 ? 0.9664 1.0508 1.5507 -0.0396 0.1147  0.1286  259 TYR B N   
6002 C CA  . TYR B 232 ? 0.9666 1.0225 1.5177 -0.0559 0.0953  0.1158  259 TYR B CA  
6003 C C   . TYR B 232 ? 0.9347 1.0029 1.5351 -0.0731 0.0900  0.1223  259 TYR B C   
6004 O O   . TYR B 232 ? 0.9667 1.0502 1.5944 -0.0735 0.1145  0.1343  259 TYR B O   
6005 C CB  . TYR B 232 ? 0.8845 0.9112 1.3714 -0.0523 0.1134  0.1057  259 TYR B CB  
6006 C CG  . TYR B 232 ? 0.9547 0.9506 1.4043 -0.0657 0.0976  0.0907  259 TYR B CG  
6007 C CD1 . TYR B 232 ? 1.0038 0.9755 1.4072 -0.0670 0.0776  0.0764  259 TYR B CD1 
6008 C CD2 . TYR B 232 ? 0.9042 0.8939 1.3639 -0.0765 0.1043  0.0912  259 TYR B CD2 
6009 C CE1 . TYR B 232 ? 1.0705 1.0141 1.4385 -0.0780 0.0667  0.0611  259 TYR B CE1 
6010 C CE2 . TYR B 232 ? 0.9336 0.8937 1.3614 -0.0868 0.0919  0.0760  259 TYR B CE2 
6011 C CZ  . TYR B 232 ? 1.0424 0.9802 1.4241 -0.0872 0.0742  0.0600  259 TYR B CZ  
6012 O OH  . TYR B 232 ? 1.1816 1.0902 1.5305 -0.0963 0.0650  0.0434  259 TYR B OH  
6013 N N   . THR B 233 ? 0.8731 0.9326 1.4825 -0.0883 0.0574  0.1144  260 THR B N   
6014 C CA  . THR B 233 ? 0.9488 1.0166 1.6080 -0.1070 0.0469  0.1188  260 THR B CA  
6015 C C   . THR B 233 ? 1.0352 1.0663 1.6568 -0.1224 0.0223  0.0991  260 THR B C   
6016 O O   . THR B 233 ? 1.1854 1.2172 1.8401 -0.1393 -0.0031 0.0961  260 THR B O   
6017 C CB  . THR B 233 ? 0.8973 1.0021 1.6304 -0.1116 0.0291  0.1317  260 THR B CB  
6018 O OG1 . THR B 233 ? 0.9502 1.0498 1.6652 -0.1092 -0.0017 0.1235  260 THR B OG1 
6019 C CG2 . THR B 233 ? 0.8844 1.0278 1.6635 -0.0966 0.0595  0.1516  260 THR B CG2 
6020 N N   . TRP B 234 ? 1.1504 1.1491 1.7034 -0.1168 0.0301  0.0846  261 TRP B N   
6021 C CA  . TRP B 234 ? 1.1081 1.0701 1.6174 -0.1281 0.0115  0.0635  261 TRP B CA  
6022 C C   . TRP B 234 ? 1.1673 1.1088 1.6618 -0.1307 0.0318  0.0596  261 TRP B C   
6023 O O   . TRP B 234 ? 1.1450 1.1016 1.6657 -0.1263 0.0566  0.0751  261 TRP B O   
6024 C CB  . TRP B 234 ? 1.0394 0.9812 1.4832 -0.1198 0.0024  0.0501  261 TRP B CB  
6025 C CG  . TRP B 234 ? 1.1581 1.1134 1.6127 -0.1196 -0.0246 0.0531  261 TRP B CG  
6026 C CD1 . TRP B 234 ? 1.2578 1.2392 1.7736 -0.1280 -0.0459 0.0630  261 TRP B CD1 
6027 C CD2 . TRP B 234 ? 1.1694 1.1134 1.5752 -0.1107 -0.0346 0.0482  261 TRP B CD2 
6028 N NE1 . TRP B 234 ? 1.2859 1.2735 1.7939 -0.1239 -0.0700 0.0646  261 TRP B NE1 
6029 C CE2 . TRP B 234 ? 1.2330 1.1964 1.6720 -0.1133 -0.0632 0.0561  261 TRP B CE2 
6030 C CE3 . TRP B 234 ? 1.1852 1.1051 1.5249 -0.1015 -0.0225 0.0395  261 TRP B CE3 
6031 C CZ2 . TRP B 234 ? 1.2849 1.2420 1.6902 -0.1062 -0.0804 0.0564  261 TRP B CZ2 
6032 C CZ3 . TRP B 234 ? 1.1480 1.0613 1.4545 -0.0957 -0.0380 0.0395  261 TRP B CZ3 
6033 C CH2 . TRP B 234 ? 1.2338 1.1646 1.5716 -0.0976 -0.0668 0.0484  261 TRP B CH2 
6034 N N   . SER B 235 ? 1.1405 1.0471 1.5921 -0.1373 0.0214  0.0391  262 SER B N   
6035 C CA  . SER B 235 ? 1.1249 1.0096 1.5652 -0.1391 0.0376  0.0341  262 SER B CA  
6036 C C   . SER B 235 ? 1.0651 0.9516 1.4747 -0.1230 0.0667  0.0407  262 SER B C   
6037 O O   . SER B 235 ? 1.1005 0.9921 1.4779 -0.1116 0.0714  0.0401  262 SER B O   
6038 C CB  . SER B 235 ? 1.2229 1.0694 1.6214 -0.1472 0.0218  0.0082  262 SER B CB  
6039 O OG  . SER B 235 ? 1.6025 1.4430 2.0274 -0.1640 -0.0065 0.0001  262 SER B OG  
6040 N N   . PHE B 236 ? 1.0294 0.9104 1.4496 -0.1228 0.0847  0.0477  263 PHE B N   
6041 C CA  . PHE B 236 ? 1.0219 0.9038 1.4141 -0.1093 0.1097  0.0542  263 PHE B CA  
6042 C C   . PHE B 236 ? 1.0834 0.9368 1.4208 -0.1052 0.1090  0.0341  263 PHE B C   
6043 O O   . PHE B 236 ? 1.1447 0.9801 1.4735 -0.1051 0.1169  0.0295  263 PHE B O   
6044 C CB  . PHE B 236 ? 1.0766 0.9634 1.5001 -0.1111 0.1266  0.0714  263 PHE B CB  
6045 C CG  . PHE B 236 ? 0.9281 0.8246 1.3303 -0.0980 0.1509  0.0836  263 PHE B CG  
6046 C CD1 . PHE B 236 ? 0.9410 0.8640 1.3481 -0.0895 0.1633  0.0966  263 PHE B CD1 
6047 C CD2 . PHE B 236 ? 0.9936 0.8724 1.3719 -0.0940 0.1606  0.0817  263 PHE B CD2 
6048 C CE1 . PHE B 236 ? 0.9618 0.8909 1.3443 -0.0784 0.1842  0.1057  263 PHE B CE1 
6049 C CE2 . PHE B 236 ? 1.1149 1.0026 1.4721 -0.0833 0.1794  0.0929  263 PHE B CE2 
6050 C CZ  . PHE B 236 ? 0.9519 0.8635 1.3084 -0.0761 0.1909  0.1041  263 PHE B CZ  
6051 N N   . ASP B 237 ? 1.0381 0.8883 1.3404 -0.1016 0.0996  0.0232  264 ASP B N   
6052 C CA  . ASP B 237 ? 0.9339 0.7601 1.1832 -0.0984 0.0996  0.0048  264 ASP B CA  
6053 C C   . ASP B 237 ? 1.0117 0.8470 1.2297 -0.0862 0.1115  0.0095  264 ASP B C   
6054 O O   . ASP B 237 ? 1.0242 0.8761 1.2492 -0.0825 0.1073  0.0179  264 ASP B O   
6055 C CB  . ASP B 237 ? 1.0877 0.8965 1.3171 -0.1077 0.0758  -0.0134 264 ASP B CB  
6056 C CG  . ASP B 237 ? 1.2769 1.0576 1.4560 -0.1068 0.0787  -0.0341 264 ASP B CG  
6057 O OD1 . ASP B 237 ? 1.3077 1.0881 1.4552 -0.0974 0.0936  -0.0339 264 ASP B OD1 
6058 O OD2 . ASP B 237 ? 1.3255 1.0840 1.4976 -0.1160 0.0667  -0.0512 264 ASP B OD2 
6059 N N   . ASP B 238 ? 1.0679 0.8920 1.2548 -0.0801 0.1257  0.0041  265 ASP B N   
6060 C CA  . ASP B 238 ? 0.9292 0.7607 1.0899 -0.0700 0.1378  0.0092  265 ASP B CA  
6061 C C   . ASP B 238 ? 1.0361 0.8622 1.1658 -0.0692 0.1265  0.0022  265 ASP B C   
6062 O O   . ASP B 238 ? 1.0357 0.8734 1.1634 -0.0624 0.1289  0.0109  265 ASP B O   
6063 C CB  . ASP B 238 ? 0.9521 0.7737 1.0906 -0.0656 0.1525  0.0047  265 ASP B CB  
6064 C CG  . ASP B 238 ? 0.9757 0.7749 1.0886 -0.0698 0.1484  -0.0141 265 ASP B CG  
6065 O OD1 . ASP B 238 ? 1.0476 0.8356 1.1584 -0.0773 0.1337  -0.0247 265 ASP B OD1 
6066 O OD2 . ASP B 238 ? 1.0734 0.8667 1.1682 -0.0656 0.1600  -0.0186 265 ASP B OD2 
6067 N N   . ILE B 239 ? 1.0221 0.8289 1.1258 -0.0759 0.1146  -0.0133 266 ILE B N   
6068 C CA  . ILE B 239 ? 0.9713 0.7708 1.0401 -0.0759 0.1035  -0.0179 266 ILE B CA  
6069 C C   . ILE B 239 ? 1.0482 0.8609 1.1415 -0.0779 0.0844  -0.0094 266 ILE B C   
6070 O O   . ILE B 239 ? 1.2506 1.0657 1.3288 -0.0734 0.0777  -0.0043 266 ILE B O   
6071 C CB  . ILE B 239 ? 1.1534 0.9282 1.1821 -0.0827 0.0976  -0.0367 266 ILE B CB  
6072 C CG1 . ILE B 239 ? 1.0158 0.7816 1.0598 -0.0933 0.0801  -0.0468 266 ILE B CG1 
6073 C CG2 . ILE B 239 ? 0.8569 0.6227 0.8703 -0.0793 0.1180  -0.0440 266 ILE B CG2 
6074 C CD1 . ILE B 239 ? 0.9888 0.7285 0.9863 -0.1001 0.0722  -0.0671 266 ILE B CD1 
6075 N N   . ILE B 240 ? 1.0606 0.8823 1.1957 -0.0846 0.0749  -0.0067 267 ILE B N   
6076 C CA  . ILE B 240 ? 0.9328 0.7717 1.1004 -0.0869 0.0560  0.0026  267 ILE B CA  
6077 C C   . ILE B 240 ? 0.9906 0.8550 1.1887 -0.0755 0.0695  0.0207  267 ILE B C   
6078 O O   . ILE B 240 ? 0.9624 0.8385 1.1699 -0.0705 0.0596  0.0285  267 ILE B O   
6079 C CB  . ILE B 240 ? 1.0763 0.9174 1.2831 -0.0995 0.0417  -0.0001 267 ILE B CB  
6080 C CG1 . ILE B 240 ? 1.1672 0.9785 1.3382 -0.1101 0.0286  -0.0215 267 ILE B CG1 
6081 C CG2 . ILE B 240 ? 1.0895 0.9520 1.3365 -0.1029 0.0206  0.0104  267 ILE B CG2 
6082 C CD1 . ILE B 240 ? 1.2692 1.0774 1.4756 -0.1241 0.0107  -0.0269 267 ILE B CD1 
6083 N N   . VAL B 241 ? 1.0486 0.9212 1.2612 -0.0705 0.0924  0.0274  268 VAL B N   
6084 C CA  . VAL B 241 ? 0.9581 0.8528 1.1935 -0.0593 0.1084  0.0423  268 VAL B CA  
6085 C C   . VAL B 241 ? 0.9367 0.8250 1.1369 -0.0488 0.1118  0.0413  268 VAL B C   
6086 O O   . VAL B 241 ? 1.0149 0.9179 1.2336 -0.0400 0.1127  0.0506  268 VAL B O   
6087 C CB  . VAL B 241 ? 0.9709 0.8707 1.2155 -0.0569 0.1315  0.0487  268 VAL B CB  
6088 C CG1 . VAL B 241 ? 0.8056 0.7199 1.0505 -0.0440 0.1510  0.0591  268 VAL B CG1 
6089 C CG2 . VAL B 241 ? 0.9991 0.9111 1.2923 -0.0660 0.1295  0.0567  268 VAL B CG2 
6090 N N   . PHE B 242 ? 1.0556 0.9215 1.2077 -0.0495 0.1142  0.0303  269 PHE B N   
6091 C CA  . PHE B 242 ? 1.0054 0.8624 1.1243 -0.0414 0.1177  0.0300  269 PHE B CA  
6092 C C   . PHE B 242 ? 1.0012 0.8536 1.1129 -0.0421 0.0958  0.0308  269 PHE B C   
6093 O O   . PHE B 242 ? 1.0387 0.8952 1.1536 -0.0326 0.0954  0.0384  269 PHE B O   
6094 C CB  . PHE B 242 ? 0.8906 0.7275 0.9652 -0.0434 0.1273  0.0198  269 PHE B CB  
6095 C CG  . PHE B 242 ? 0.9429 0.7695 0.9858 -0.0368 0.1325  0.0203  269 PHE B CG  
6096 C CD1 . PHE B 242 ? 1.0599 0.8948 1.1120 -0.0266 0.1452  0.0276  269 PHE B CD1 
6097 C CD2 . PHE B 242 ? 1.1094 0.9165 1.1124 -0.0413 0.1254  0.0134  269 PHE B CD2 
6098 C CE1 . PHE B 242 ? 1.1368 0.9586 1.1613 -0.0214 0.1490  0.0272  269 PHE B CE1 
6099 C CE2 . PHE B 242 ? 1.0775 0.8735 1.0541 -0.0366 0.1301  0.0155  269 PHE B CE2 
6100 C CZ  . PHE B 242 ? 1.0373 0.8397 1.0259 -0.0269 0.1409  0.0220  269 PHE B CZ  
6101 N N   . ALA B 243 ? 1.0072 0.8495 1.1080 -0.0530 0.0766  0.0228  270 ALA B N   
6102 C CA  . ALA B 243 ? 1.0457 0.8831 1.1356 -0.0550 0.0522  0.0246  270 ALA B CA  
6103 C C   . ALA B 243 ? 1.0069 0.8692 1.1483 -0.0487 0.0421  0.0388  270 ALA B C   
6104 O O   . ALA B 243 ? 1.0818 0.9442 1.2202 -0.0423 0.0301  0.0464  270 ALA B O   
6105 C CB  . ALA B 243 ? 1.0165 0.8396 1.0870 -0.0689 0.0328  0.0122  270 ALA B CB  
6106 N N   . PHE B 244 ? 0.8816 0.7658 1.0733 -0.0502 0.0476  0.0437  271 PHE B N   
6107 C CA  . PHE B 244 ? 0.9567 0.8695 1.2048 -0.0433 0.0434  0.0581  271 PHE B CA  
6108 C C   . PHE B 244 ? 0.9960 0.9159 1.2478 -0.0263 0.0647  0.0662  271 PHE B C   
6109 O O   . PHE B 244 ? 1.0308 0.9672 1.3158 -0.0166 0.0593  0.0768  271 PHE B O   
6110 C CB  . PHE B 244 ? 0.8845 0.8189 1.1851 -0.0503 0.0482  0.0625  271 PHE B CB  
6111 C CG  . PHE B 244 ? 0.9466 0.9141 1.3123 -0.0457 0.0428  0.0774  271 PHE B CG  
6112 C CD1 . PHE B 244 ? 0.9941 0.9718 1.3893 -0.0543 0.0118  0.0801  271 PHE B CD1 
6113 C CD2 . PHE B 244 ? 0.9807 0.9702 1.3786 -0.0328 0.0686  0.0885  271 PHE B CD2 
6114 C CE1 . PHE B 244 ? 0.8611 0.8733 1.3238 -0.0500 0.0064  0.0949  271 PHE B CE1 
6115 C CE2 . PHE B 244 ? 0.9503 0.9730 1.4126 -0.0275 0.0667  0.1024  271 PHE B CE2 
6116 C CZ  . PHE B 244 ? 0.9002 0.9359 1.3985 -0.0360 0.0355  0.1063  271 PHE B CZ  
6117 N N   . SER B 245 ? 0.9668 0.8740 1.1864 -0.0223 0.0881  0.0609  272 SER B N   
6118 C CA  . SER B 245 ? 0.8802 0.7889 1.0963 -0.0073 0.1076  0.0653  272 SER B CA  
6119 C C   . SER B 245 ? 1.0322 0.9230 1.2199 -0.0007 0.0963  0.0656  272 SER B C   
6120 O O   . SER B 245 ? 1.1338 1.0289 1.3352 0.0132  0.1039  0.0717  272 SER B O   
6121 C CB  . SER B 245 ? 0.8053 0.7037 0.9916 -0.0070 0.1312  0.0590  272 SER B CB  
6122 O OG  . SER B 245 ? 0.8905 0.7896 1.0729 0.0065  0.1498  0.0615  272 SER B OG  
6123 N N   . CYS B 246 ? 1.1041 0.9733 1.2513 -0.0102 0.0793  0.0592  273 CYS B N   
6124 C CA  . CYS B 246 ? 0.9082 0.7590 1.0268 -0.0056 0.0670  0.0623  273 CYS B CA  
6125 C C   . CYS B 246 ? 1.0977 0.9626 1.2526 -0.0010 0.0434  0.0739  273 CYS B C   
6126 O O   . CYS B 246 ? 1.1986 1.0572 1.3541 0.0101  0.0386  0.0821  273 CYS B O   
6127 C CB  . CYS B 246 ? 0.9933 0.8181 1.0558 -0.0179 0.0580  0.0533  273 CYS B CB  
6128 S SG  . CYS B 246 ? 1.0143 0.8251 1.0397 -0.0235 0.0836  0.0404  273 CYS B SG  
6129 N N   . LYS B 247 ? 0.9851 0.8687 1.1734 -0.0095 0.0271  0.0754  274 LYS B N   
6130 C CA  . LYS B 247 ? 1.0772 0.9789 1.3077 -0.0059 0.0022  0.0874  274 LYS B CA  
6131 C C   . LYS B 247 ? 1.0573 0.9831 1.3426 0.0119  0.0172  0.0986  274 LYS B C   
6132 O O   . LYS B 247 ? 1.0135 0.9435 1.3191 0.0230  0.0041  0.1095  274 LYS B O   
6133 C CB  . LYS B 247 ? 1.0430 0.9608 1.3024 -0.0206 -0.0178 0.0855  274 LYS B CB  
6134 C CG  . LYS B 247 ? 1.3605 1.2553 1.5711 -0.0362 -0.0444 0.0764  274 LYS B CG  
6135 C CD  . LYS B 247 ? 1.5329 1.4434 1.7785 -0.0505 -0.0674 0.0741  274 LYS B CD  
6136 C CE  . LYS B 247 ? 1.5665 1.4527 1.7606 -0.0655 -0.0968 0.0639  274 LYS B CE  
6137 N NZ  . LYS B 247 ? 1.3089 1.2089 1.5387 -0.0801 -0.1242 0.0612  274 LYS B NZ  
6138 N N   . GLN B 248 ? 0.9802 0.9214 1.2892 0.0154  0.0453  0.0965  275 GLN B N   
6139 C CA  . GLN B 248 ? 0.9201 0.8845 1.2782 0.0326  0.0643  0.1054  275 GLN B CA  
6140 C C   . GLN B 248 ? 1.0045 0.9475 1.3344 0.0484  0.0772  0.1043  275 GLN B C   
6141 O O   . GLN B 248 ? 1.3477 1.3005 1.7125 0.0644  0.0769  0.1130  275 GLN B O   
6142 C CB  . GLN B 248 ? 1.0364 1.0193 1.4165 0.0311  0.0924  0.1037  275 GLN B CB  
6143 C CG  . GLN B 248 ? 1.0593 1.0614 1.4721 0.0149  0.0809  0.1057  275 GLN B CG  
6144 C CD  . GLN B 248 ? 1.0706 1.1013 1.5462 0.0146  0.0574  0.1176  275 GLN B CD  
6145 O OE1 . GLN B 248 ? 1.0771 1.1044 1.5516 0.0012  0.0264  0.1163  275 GLN B OE1 
6146 N NE2 . GLN B 248 ? 1.0670 1.1265 1.5981 0.0296  0.0720  0.1287  275 GLN B NE2 
6147 N N   . ALA B 249 ? 1.0463 0.9599 1.3169 0.0444  0.0885  0.0937  276 ALA B N   
6148 C CA  . ALA B 249 ? 1.0479 0.9360 1.2878 0.0560  0.0971  0.0918  276 ALA B CA  
6149 C C   . ALA B 249 ? 1.0987 0.9674 1.3203 0.0562  0.0700  0.0985  276 ALA B C   
6150 O O   . ALA B 249 ? 1.0614 0.9058 1.2594 0.0651  0.0742  0.0989  276 ALA B O   
6151 C CB  . ALA B 249 ? 0.8995 0.7643 1.0856 0.0492  0.1151  0.0793  276 ALA B CB  
6152 N N   . GLU B 250 ? 1.0929 0.9702 1.3236 0.0461  0.0417  0.1041  277 GLU B N   
6153 C CA  . GLU B 250 ? 1.1174 0.9764 1.3248 0.0441  0.0128  0.1123  277 GLU B CA  
6154 C C   . GLU B 250 ? 1.0736 0.8950 1.2109 0.0371  0.0171  0.1057  277 GLU B C   
6155 O O   . GLU B 250 ? 1.2885 1.0873 1.4039 0.0425  0.0075  0.1136  277 GLU B O   
6156 C CB  . GLU B 250 ? 1.1321 0.9987 1.3826 0.0629  0.0041  0.1267  277 GLU B CB  
6157 C CG  . GLU B 250 ? 1.1783 1.0826 1.4964 0.0651  -0.0146 0.1372  277 GLU B CG  
6158 C CD  . GLU B 250 ? 1.4851 1.4062 1.8630 0.0878  -0.0113 0.1495  277 GLU B CD  
6159 O OE1 . GLU B 250 ? 1.5819 1.4783 1.9423 0.1013  -0.0042 0.1518  277 GLU B OE1 
6160 O OE2 . GLU B 250 ? 1.6896 1.6486 2.1350 0.0921  -0.0151 0.1568  277 GLU B OE2 
6161 N N   . VAL B 251 ? 1.0996 0.9148 1.2046 0.0249  0.0317  0.0925  278 VAL B N   
6162 C CA  . VAL B 251 ? 1.1273 0.9121 1.1703 0.0156  0.0371  0.0856  278 VAL B CA  
6163 C C   . VAL B 251 ? 1.0892 0.8676 1.0998 -0.0006 0.0165  0.0827  278 VAL B C   
6164 O O   . VAL B 251 ? 1.1848 0.9767 1.2043 -0.0099 0.0157  0.0743  278 VAL B O   
6165 C CB  . VAL B 251 ? 1.0380 0.8211 1.0678 0.0133  0.0659  0.0730  278 VAL B CB  
6166 C CG1 . VAL B 251 ? 1.0506 0.8076 1.0234 0.0018  0.0703  0.0662  278 VAL B CG1 
6167 C CG2 . VAL B 251 ? 1.1231 0.9072 1.1740 0.0287  0.0858  0.0738  278 VAL B CG2 
6168 N N   . GLN B 252 ? 1.1309 0.8864 1.1019 -0.0041 0.0001  0.0897  279 GLN B N   
6169 C CA  . GLN B 252 ? 1.1125 0.8577 1.0420 -0.0195 -0.0183 0.0859  279 GLN B CA  
6170 C C   . GLN B 252 ? 1.1907 0.9199 1.0734 -0.0303 0.0023  0.0718  279 GLN B C   
6171 O O   . GLN B 252 ? 1.3057 1.0164 1.1602 -0.0291 0.0173  0.0731  279 GLN B O   
6172 C CB  . GLN B 252 ? 1.2521 0.9788 1.1532 -0.0192 -0.0434 0.1009  279 GLN B CB  
6173 C CG  . GLN B 252 ? 1.2692 0.9842 1.1215 -0.0350 -0.0644 0.0973  279 GLN B CG  
6174 C CD  . GLN B 252 ? 1.4254 1.1626 1.3069 -0.0418 -0.0824 0.0899  279 GLN B CD  
6175 O OE1 . GLN B 252 ? 1.4455 1.2010 1.3704 -0.0365 -0.1057 0.1007  279 GLN B OE1 
6176 N NE2 . GLN B 252 ? 1.2911 1.0267 1.1527 -0.0536 -0.0720 0.0716  279 GLN B NE2 
6177 N N   . MET B 253 ? 1.2089 0.9455 1.0875 -0.0407 0.0032  0.0584  280 MET B N   
6178 C CA  . MET B 253 ? 1.1003 0.8228 0.9366 -0.0507 0.0205  0.0447  280 MET B CA  
6179 C C   . MET B 253 ? 1.1023 0.8014 0.8789 -0.0606 0.0079  0.0454  280 MET B C   
6180 O O   . MET B 253 ? 1.1541 0.8513 0.9205 -0.0651 -0.0186 0.0492  280 MET B O   
6181 C CB  . MET B 253 ? 1.0614 0.7972 0.9162 -0.0571 0.0255  0.0301  280 MET B CB  
6182 C CG  . MET B 253 ? 1.2388 0.9936 1.1388 -0.0498 0.0455  0.0284  280 MET B CG  
6183 S SD  . MET B 253 ? 1.5341 1.3074 1.4726 -0.0561 0.0410  0.0192  280 MET B SD  
6184 C CE  . MET B 253 ? 1.4607 1.2495 1.4360 -0.0542 0.0101  0.0314  280 MET B CE  
6185 N N   . TYR B 254 ? 1.0071 0.6889 0.7436 -0.0648 0.0269  0.0424  281 TYR B N   
6186 C CA  . TYR B 254 ? 1.3061 0.9654 0.9811 -0.0748 0.0214  0.0433  281 TYR B CA  
6187 C C   . TYR B 254 ? 1.3131 0.9670 0.9587 -0.0838 0.0435  0.0258  281 TYR B C   
6188 O O   . TYR B 254 ? 1.3018 0.9648 0.9698 -0.0812 0.0665  0.0183  281 TYR B O   
6189 C CB  . TYR B 254 ? 1.1172 0.7582 0.7694 -0.0719 0.0241  0.0602  281 TYR B CB  
6190 C CG  . TYR B 254 ? 1.3138 0.9547 0.9884 -0.0623 0.0005  0.0791  281 TYR B CG  
6191 C CD1 . TYR B 254 ? 1.2694 0.9239 0.9985 -0.0486 0.0047  0.0841  281 TYR B CD1 
6192 C CD2 . TYR B 254 ? 1.3767 1.0032 1.0169 -0.0661 -0.0255 0.0922  281 TYR B CD2 
6193 C CE1 . TYR B 254 ? 1.2355 0.8904 0.9900 -0.0377 -0.0149 0.1009  281 TYR B CE1 
6194 C CE2 . TYR B 254 ? 1.2955 0.9228 0.9613 -0.0559 -0.0483 0.1110  281 TYR B CE2 
6195 C CZ  . TYR B 254 ? 1.4191 1.0610 1.1448 -0.0411 -0.0421 0.1149  281 TYR B CZ  
6196 O OH  . TYR B 254 ? 1.5876 1.2309 1.3437 -0.0289 -0.0629 0.1331  281 TYR B OH  
6197 N N   . VAL B 255 ? 1.1906 0.8297 0.7855 -0.0940 0.0361  0.0193  282 VAL B N   
6198 C CA  . VAL B 255 ? 1.2200 0.8499 0.7779 -0.1020 0.0589  0.0042  282 VAL B CA  
6199 C C   . VAL B 255 ? 1.3175 0.9253 0.8140 -0.1089 0.0612  0.0140  282 VAL B C   
6200 O O   . VAL B 255 ? 1.2987 0.8945 0.7643 -0.1119 0.0369  0.0249  282 VAL B O   
6201 C CB  . VAL B 255 ? 1.3643 0.9943 0.9139 -0.1081 0.0528  -0.0165 282 VAL B CB  
6202 C CG1 . VAL B 255 ? 1.3736 0.9940 0.8953 -0.1137 0.0194  -0.0139 282 VAL B CG1 
6203 C CG2 . VAL B 255 ? 1.1309 0.7500 0.6413 -0.1145 0.0787  -0.0330 282 VAL B CG2 
6204 N N   . CYS B 256 ? 1.2865 0.8900 0.7671 -0.1119 0.0897  0.0122  283 CYS B N   
6205 C CA  . CYS B 256 ? 1.2813 0.8650 0.7051 -0.1200 0.0977  0.0224  283 CYS B CA  
6206 C C   . CYS B 256 ? 1.3642 0.9429 0.7488 -0.1281 0.1203  0.0044  283 CYS B C   
6207 O O   . CYS B 256 ? 1.3863 0.9783 0.7993 -0.1259 0.1411  -0.0115 283 CYS B O   
6208 C CB  . CYS B 256 ? 1.1748 0.7569 0.6142 -0.1181 0.1136  0.0378  283 CYS B CB  
6209 S SG  . CYS B 256 ? 1.6200 1.2055 1.1081 -0.1061 0.0935  0.0558  283 CYS B SG  
6210 N N   . ASN B 257 ? 1.1979 0.8109 0.7092 0.0428  0.1555  -0.0044 284 ASN B N   
6211 C CA  . ASN B 257 ? 1.2768 0.8781 0.7986 0.0402  0.1760  -0.0050 284 ASN B CA  
6212 C C   . ASN B 257 ? 1.4099 0.9745 0.9062 0.0519  0.2070  0.0088  284 ASN B C   
6213 O O   . ASN B 257 ? 1.3878 0.9415 0.8673 0.0609  0.2257  0.0094  284 ASN B O   
6214 C CB  . ASN B 257 ? 1.3018 0.9196 0.8014 0.0485  0.1675  -0.0190 284 ASN B CB  
6215 C CG  . ASN B 257 ? 1.4543 1.0661 0.8895 0.0747  0.1697  -0.0203 284 ASN B CG  
6216 O OD1 . ASN B 257 ? 1.3580 0.9595 0.7631 0.0868  0.1697  -0.0117 284 ASN B OD1 
6217 N ND2 . ASN B 257 ? 1.5584 1.1769 0.9710 0.0857  0.1711  -0.0321 284 ASN B ND2 
6218 N N   . LYS B 258 ? 1.2467 0.7907 0.7400 0.0523  0.2137  0.0202  285 LYS B N   
6219 C CA  . LYS B 258 ? 1.3059 0.8103 0.7726 0.0634  0.2452  0.0357  285 LYS B CA  
6220 C C   . LYS B 258 ? 1.4934 0.9869 0.9965 0.0510  0.2717  0.0405  285 LYS B C   
6221 O O   . LYS B 258 ? 1.5347 1.0014 1.0113 0.0631  0.3008  0.0522  285 LYS B O   
6222 C CB  . LYS B 258 ? 1.2592 0.7413 0.7244 0.0623  0.2465  0.0453  285 LYS B CB  
6223 C CG  . LYS B 258 ? 1.3572 0.8470 0.7779 0.0797  0.2238  0.0426  285 LYS B CG  
6224 C CD  . LYS B 258 ? 1.2276 0.6891 0.6429 0.0812  0.2273  0.0523  285 LYS B CD  
6225 C CE  . LYS B 258 ? 1.2859 0.7593 0.6576 0.1002  0.2030  0.0489  285 LYS B CE  
6226 N NZ  . LYS B 258 ? 1.4459 0.8884 0.8094 0.1038  0.2060  0.0575  285 LYS B NZ  
6227 N N   . GLU B 259 ? 1.3049 0.8206 0.8671 0.0289  0.2630  0.0324  286 GLU B N   
6228 C CA  . GLU B 259 ? 1.4287 0.9428 1.0265 0.0186  0.2849  0.0339  286 GLU B CA  
6229 C C   . GLU B 259 ? 1.3153 0.8633 0.9614 0.0029  0.2648  0.0201  286 GLU B C   
6230 O O   . GLU B 259 ? 1.3030 0.8728 0.9565 -0.0012 0.2365  0.0117  286 GLU B O   
6231 C CB  . GLU B 259 ? 1.4276 0.9181 1.0550 0.0067  0.3104  0.0456  286 GLU B CB  
6232 C CG  . GLU B 259 ? 1.3624 0.8605 1.0301 -0.0100 0.2942  0.0417  286 GLU B CG  
6233 C CD  . GLU B 259 ? 1.6344 1.1071 1.3316 -0.0224 0.3203  0.0508  286 GLU B CD  
6234 O OE1 . GLU B 259 ? 1.7143 1.1838 1.4373 -0.0301 0.3459  0.0546  286 GLU B OE1 
6235 O OE2 . GLU B 259 ? 1.7632 1.2189 1.4581 -0.0245 0.3159  0.0535  286 GLU B OE2 
6236 N N   . GLU B 260 ? 1.2947 0.8470 0.9723 -0.0044 0.2809  0.0190  287 GLU B N   
6237 C CA  . GLU B 260 ? 1.1917 0.7725 0.9125 -0.0161 0.2652  0.0073  287 GLU B CA  
6238 C C   . GLU B 260 ? 1.2490 0.8460 1.0200 -0.0330 0.2520  0.0050  287 GLU B C   
6239 O O   . GLU B 260 ? 1.3448 0.9320 1.1389 -0.0412 0.2662  0.0107  287 GLU B O   
6240 C CB  . GLU B 260 ? 1.0650 0.6460 0.8046 -0.0167 0.2873  0.0069  287 GLU B CB  
6241 C CG  . GLU B 260 ? 1.3700 0.9743 1.1359 -0.0210 0.2723  -0.0055 287 GLU B CG  
6242 C CD  . GLU B 260 ? 1.5417 1.1436 1.3106 -0.0149 0.2934  -0.0068 287 GLU B CD  
6243 O OE1 . GLU B 260 ? 1.5581 1.1560 1.3497 -0.0194 0.3181  0.0007  287 GLU B OE1 
6244 O OE2 . GLU B 260 ? 1.5173 1.1218 1.2663 -0.0057 0.2857  -0.0160 287 GLU B OE2 
6245 N N   . TYR B 261 ? 1.2792 0.9016 1.0674 -0.0375 0.2252  -0.0038 288 TYR B N   
6246 C CA  . TYR B 261 ? 1.1898 0.8325 1.0224 -0.0494 0.2098  -0.0070 288 TYR B CA  
6247 C C   . TYR B 261 ? 1.0896 0.7576 0.9674 -0.0565 0.2039  -0.0144 288 TYR B C   
6248 O O   . TYR B 261 ? 1.1454 0.8271 1.0687 -0.0654 0.2073  -0.0168 288 TYR B O   
6249 C CB  . TYR B 261 ? 1.0984 0.7515 0.9116 -0.0458 0.1828  -0.0084 288 TYR B CB  
6250 C CG  . TYR B 261 ? 1.0834 0.7134 0.8489 -0.0355 0.1862  -0.0018 288 TYR B CG  
6251 C CD1 . TYR B 261 ? 1.0720 0.6804 0.8403 -0.0375 0.2010  0.0049  288 TYR B CD1 
6252 C CD2 . TYR B 261 ? 1.1517 0.7818 0.8700 -0.0231 0.1747  -0.0030 288 TYR B CD2 
6253 C CE1 . TYR B 261 ? 1.2261 0.8096 0.9474 -0.0254 0.2050  0.0123  288 TYR B CE1 
6254 C CE2 . TYR B 261 ? 1.1420 0.7531 0.8137 -0.0101 0.1772  0.0029  288 TYR B CE2 
6255 C CZ  . TYR B 261 ? 1.3024 0.8882 0.9737 -0.0102 0.1929  0.0116  288 TYR B CZ  
6256 O OH  . TYR B 261 ? 1.4519 1.0148 1.0733 0.0053  0.1966  0.0188  288 TYR B OH  
6257 N N   . GLY B 262 ? 1.1308 0.8051 0.9971 -0.0520 0.1953  -0.0190 289 GLY B N   
6258 C CA  . GLY B 262 ? 1.0523 0.7463 0.9567 -0.0560 0.1902  -0.0246 289 GLY B CA  
6259 C C   . GLY B 262 ? 1.1452 0.8365 1.0286 -0.0506 0.1828  -0.0296 289 GLY B C   
6260 O O   . GLY B 262 ? 1.2585 0.9355 1.1001 -0.0439 0.1829  -0.0307 289 GLY B O   
6261 N N   . PHE B 263 ? 1.1711 0.8766 1.0846 -0.0526 0.1763  -0.0336 290 PHE B N   
6262 C CA  . PHE B 263 ? 1.1101 0.8100 1.0118 -0.0490 0.1710  -0.0394 290 PHE B CA  
6263 C C   . PHE B 263 ? 1.0700 0.7869 0.9946 -0.0526 0.1513  -0.0393 290 PHE B C   
6264 O O   . PHE B 263 ? 1.0209 0.7574 0.9749 -0.0551 0.1441  -0.0354 290 PHE B O   
6265 C CB  . PHE B 263 ? 1.1398 0.8320 1.0512 -0.0442 0.1894  -0.0434 290 PHE B CB  
6266 C CG  . PHE B 263 ? 1.2376 0.9152 1.1288 -0.0392 0.2121  -0.0413 290 PHE B CG  
6267 C CD1 . PHE B 263 ? 1.2521 0.9346 1.1651 -0.0434 0.2274  -0.0353 290 PHE B CD1 
6268 C CD2 . PHE B 263 ? 1.2970 0.9564 1.1482 -0.0298 0.2190  -0.0458 290 PHE B CD2 
6269 C CE1 . PHE B 263 ? 1.2755 0.9426 1.1702 -0.0390 0.2514  -0.0306 290 PHE B CE1 
6270 C CE2 . PHE B 263 ? 1.4120 1.0584 1.2416 -0.0222 0.2417  -0.0416 290 PHE B CE2 
6271 C CZ  . PHE B 263 ? 1.4146 1.0636 1.2658 -0.0272 0.2591  -0.0325 290 PHE B CZ  
6272 N N   . LEU B 264 ? 1.0802 0.7893 0.9915 -0.0522 0.1433  -0.0439 291 LEU B N   
6273 C CA  . LEU B 264 ? 1.1210 0.8416 1.0508 -0.0554 0.1275  -0.0416 291 LEU B CA  
6274 C C   . LEU B 264 ? 1.1613 0.8643 1.0835 -0.0549 0.1282  -0.0487 291 LEU B C   
6275 O O   . LEU B 264 ? 1.1972 0.8835 1.0911 -0.0532 0.1333  -0.0575 291 LEU B O   
6276 C CB  . LEU B 264 ? 1.0751 0.8088 0.9930 -0.0599 0.1098  -0.0374 291 LEU B CB  
6277 C CG  . LEU B 264 ? 1.0733 0.8000 0.9568 -0.0625 0.1013  -0.0430 291 LEU B CG  
6278 C CD1 . LEU B 264 ? 0.9592 0.7064 0.8377 -0.0650 0.0848  -0.0371 291 LEU B CD1 
6279 C CD2 . LEU B 264 ? 1.1386 0.8484 0.9878 -0.0570 0.1129  -0.0500 291 LEU B CD2 
6280 N N   . PRO B 265 ? 1.1688 0.8739 1.1146 -0.0548 0.1237  -0.0459 292 PRO B N   
6281 C CA  . PRO B 265 ? 1.0359 0.7193 0.9757 -0.0553 0.1244  -0.0531 292 PRO B CA  
6282 C C   . PRO B 265 ? 1.0012 0.6817 0.9259 -0.0649 0.1107  -0.0560 292 PRO B C   
6283 O O   . PRO B 265 ? 1.2062 0.9057 1.1334 -0.0700 0.0989  -0.0485 292 PRO B O   
6284 C CB  . PRO B 265 ? 1.0623 0.7488 1.0331 -0.0500 0.1256  -0.0460 292 PRO B CB  
6285 C CG  . PRO B 265 ? 1.1219 0.8374 1.1116 -0.0498 0.1168  -0.0347 292 PRO B CG  
6286 C CD  . PRO B 265 ? 1.1216 0.8478 1.1006 -0.0518 0.1192  -0.0365 292 PRO B CD  
6287 N N   . VAL B 266 ? 1.1501 0.8088 1.0603 -0.0670 0.1122  -0.0687 293 VAL B N   
6288 C CA  . VAL B 266 ? 1.2095 0.8668 1.1109 -0.0782 0.0997  -0.0748 293 VAL B CA  
6289 C C   . VAL B 266 ? 1.1397 0.7951 1.0680 -0.0846 0.0949  -0.0648 293 VAL B C   
6290 O O   . VAL B 266 ? 1.1957 0.8331 1.1393 -0.0794 0.1029  -0.0626 293 VAL B O   
6291 C CB  . VAL B 266 ? 1.1755 0.8112 1.0553 -0.0782 0.1023  -0.0950 293 VAL B CB  
6292 C CG1 . VAL B 266 ? 1.0376 0.6770 0.9116 -0.0913 0.0888  -0.1048 293 VAL B CG1 
6293 C CG2 . VAL B 266 ? 1.1152 0.7525 0.9659 -0.0674 0.1101  -0.1020 293 VAL B CG2 
6294 N N   . PRO B 267 ? 1.2173 0.8913 1.1510 -0.0937 0.0831  -0.0571 294 PRO B N   
6295 C CA  . PRO B 267 ? 1.1751 0.8476 1.1333 -0.0983 0.0808  -0.0442 294 PRO B CA  
6296 C C   . PRO B 267 ? 1.2755 0.9143 1.2394 -0.1050 0.0860  -0.0529 294 PRO B C   
6297 O O   . PRO B 267 ? 1.2665 0.8904 1.2156 -0.1116 0.0852  -0.0719 294 PRO B O   
6298 C CB  . PRO B 267 ? 1.1070 0.8068 1.0635 -0.1081 0.0677  -0.0383 294 PRO B CB  
6299 C CG  . PRO B 267 ? 1.0647 0.7855 1.0017 -0.1020 0.0634  -0.0409 294 PRO B CG  
6300 C CD  . PRO B 267 ? 1.1868 0.8870 1.1045 -0.0966 0.0727  -0.0564 294 PRO B CD  
6301 N N   . LEU B 268 ? 1.1870 0.8136 1.1720 -0.1017 0.0913  -0.0392 295 LEU B N   
6302 C CA  . LEU B 268 ? 1.2172 0.8062 1.2102 -0.1064 0.0982  -0.0440 295 LEU B CA  
6303 C C   . LEU B 268 ? 1.2969 0.8845 1.3021 -0.1241 0.0933  -0.0384 295 LEU B C   
6304 O O   . LEU B 268 ? 1.2277 0.8471 1.2353 -0.1306 0.0844  -0.0295 295 LEU B O   
6305 C CB  . LEU B 268 ? 1.1696 0.7433 1.1761 -0.0897 0.1088  -0.0312 295 LEU B CB  
6306 C CG  . LEU B 268 ? 1.1001 0.6801 1.1006 -0.0727 0.1151  -0.0359 295 LEU B CG  
6307 C CD1 . LEU B 268 ? 1.0900 0.6692 1.1075 -0.0548 0.1226  -0.0210 295 LEU B CD1 
6308 C CD2 . LEU B 268 ? 1.0076 0.5600 0.9915 -0.0723 0.1209  -0.0575 295 LEU B CD2 
6309 N N   . ARG B 269 ? 1.2398 0.7895 1.2540 -0.1318 0.1000  -0.0436 296 ARG B N   
6310 C CA  . ARG B 269 ? 1.2035 0.7468 1.2340 -0.1509 0.0987  -0.0384 296 ARG B CA  
6311 C C   . ARG B 269 ? 1.2469 0.7930 1.2953 -0.1435 0.1051  -0.0079 296 ARG B C   
6312 O O   . ARG B 269 ? 1.4410 0.9886 1.4897 -0.1225 0.1104  0.0057  296 ARG B O   
6313 C CB  . ARG B 269 ? 1.5864 1.0842 1.6211 -0.1632 0.1043  -0.0576 296 ARG B CB  
6314 C CG  . ARG B 269 ? 1.5792 1.0741 1.5938 -0.1654 0.0981  -0.0892 296 ARG B CG  
6315 C CD  . ARG B 269 ? 1.7386 1.1875 1.7583 -0.1753 0.1026  -0.1107 296 ARG B CD  
6316 N NE  . ARG B 269 ? 1.9444 1.3916 1.9416 -0.1708 0.0972  -0.1410 296 ARG B NE  
6317 C CZ  . ARG B 269 ? 2.1336 1.5475 2.1300 -0.1772 0.0974  -0.1674 296 ARG B CZ  
6318 N NH1 . ARG B 269 ? 2.2299 1.6048 2.2483 -0.1910 0.1034  -0.1683 296 ARG B NH1 
6319 N NH2 . ARG B 269 ? 2.0636 1.4823 2.0358 -0.1686 0.0921  -0.1937 296 ARG B NH2 
6320 N N   . ALA B 270 ? 1.0706 0.6205 1.1345 -0.1602 0.1049  0.0025  297 ALA B N   
6321 C CA  . ALA B 270 ? 1.2301 0.7868 1.3086 -0.1519 0.1114  0.0335  297 ALA B CA  
6322 C C   . ALA B 270 ? 1.4463 0.9593 1.5300 -0.1367 0.1267  0.0451  297 ALA B C   
6323 O O   . ALA B 270 ? 1.4257 0.9496 1.5105 -0.1140 0.1307  0.0661  297 ALA B O   
6324 C CB  . ALA B 270 ? 1.0498 0.6151 1.1451 -0.1746 0.1114  0.0418  297 ALA B CB  
6325 N N   . HIS B 271 ? 1.4896 0.9538 1.5758 -0.1471 0.1346  0.0303  298 HIS B N   
6326 C CA  . HIS B 271 ? 1.4017 0.8184 1.4901 -0.1320 0.1496  0.0399  298 HIS B CA  
6327 C C   . HIS B 271 ? 1.4633 0.8701 1.5357 -0.1111 0.1501  0.0255  298 HIS B C   
6328 O O   . HIS B 271 ? 1.5245 0.8843 1.5941 -0.1051 0.1597  0.0180  298 HIS B O   
6329 C CB  . HIS B 271 ? 1.5741 0.9388 1.6749 -0.1537 0.1590  0.0320  298 HIS B CB  
6330 C CG  . HIS B 271 ? 1.7676 1.1362 1.8889 -0.1721 0.1644  0.0521  298 HIS B CG  
6331 N ND1 . HIS B 271 ? 2.0550 1.3969 2.1937 -0.2025 0.1681  0.0399  298 HIS B ND1 
6332 C CD2 . HIS B 271 ? 1.5088 0.9070 1.6369 -0.1639 0.1673  0.0833  298 HIS B CD2 
6333 C CE1 . HIS B 271 ? 2.0876 1.4424 2.2444 -0.2137 0.1745  0.0643  298 HIS B CE1 
6334 N NE2 . HIS B 271 ? 1.7955 1.1844 1.9445 -0.1893 0.1742  0.0916  298 HIS B NE2 
6335 N N   . SER B 272 ? 1.3138 0.7634 1.3762 -0.0997 0.1408  0.0217  299 SER B N   
6336 C CA  . SER B 272 ? 1.4049 0.8540 1.4560 -0.0789 0.1429  0.0120  299 SER B CA  
6337 C C   . SER B 272 ? 1.5030 0.9650 1.5599 -0.0519 0.1487  0.0347  299 SER B C   
6338 O O   . SER B 272 ? 1.6250 1.0965 1.6918 -0.0476 0.1506  0.0580  299 SER B O   
6339 C CB  . SER B 272 ? 1.3506 0.8370 1.3896 -0.0819 0.1320  -0.0041 299 SER B CB  
6340 O OG  . SER B 272 ? 1.4342 0.9108 1.4645 -0.1023 0.1263  -0.0266 299 SER B OG  
6341 N N   . THR B 273 ? 1.2170 0.6832 1.2681 -0.0319 0.1516  0.0273  300 THR B N   
6342 C CA  . THR B 273 ? 1.3252 0.8051 1.3824 -0.0037 0.1568  0.0439  300 THR B CA  
6343 C C   . THR B 273 ? 1.2762 0.8059 1.3356 0.0069  0.1497  0.0382  300 THR B C   
6344 O O   . THR B 273 ? 1.3204 0.8648 1.3732 -0.0057 0.1438  0.0219  300 THR B O   
6345 C CB  . THR B 273 ? 1.5216 0.9582 1.5738 0.0140  0.1694  0.0408  300 THR B CB  
6346 O OG1 . THR B 273 ? 1.7325 1.1851 1.7906 0.0436  0.1742  0.0586  300 THR B OG1 
6347 C CG2 . THR B 273 ? 1.2765 0.7101 1.3187 0.0160  0.1698  0.0161  300 THR B CG2 
6348 N N   . LEU B 274 ? 1.2735 0.8292 1.3425 0.0313  0.1508  0.0516  301 LEU B N   
6349 C CA  . LEU B 274 ? 1.1283 0.7319 1.2050 0.0410  0.1448  0.0449  301 LEU B CA  
6350 C C   . LEU B 274 ? 1.1625 0.7585 1.2347 0.0448  0.1510  0.0253  301 LEU B C   
6351 O O   . LEU B 274 ? 1.1497 0.7754 1.2248 0.0400  0.1473  0.0143  301 LEU B O   
6352 C CB  . LEU B 274 ? 0.9915 0.6269 1.0814 0.0682  0.1439  0.0602  301 LEU B CB  
6353 C CG  . LEU B 274 ? 1.0253 0.6818 1.1200 0.0696  0.1368  0.0805  301 LEU B CG  
6354 C CD1 . LEU B 274 ? 1.0060 0.7025 1.1129 0.1006  0.1342  0.0904  301 LEU B CD1 
6355 C CD2 . LEU B 274 ? 1.1176 0.8004 1.2119 0.0471  0.1245  0.0753  301 LEU B CD2 
6356 N N   . GLN B 275 ? 1.3271 0.8830 1.3918 0.0542  0.1615  0.0212  302 GLN B N   
6357 C CA  . GLN B 275 ? 1.1702 0.7195 1.2290 0.0595  0.1682  0.0028  302 GLN B CA  
6358 C C   . GLN B 275 ? 1.3007 0.8424 1.3462 0.0364  0.1651  -0.0139 302 GLN B C   
6359 O O   . GLN B 275 ? 1.2963 0.8574 1.3401 0.0370  0.1674  -0.0259 302 GLN B O   
6360 C CB  . GLN B 275 ? 1.3583 0.8623 1.4086 0.0751  0.1791  0.0013  302 GLN B CB  
6361 C CG  . GLN B 275 ? 1.3127 0.8135 1.3565 0.0850  0.1866  -0.0169 302 GLN B CG  
6362 C CD  . GLN B 275 ? 1.4743 0.9216 1.5042 0.0959  0.1957  -0.0224 302 GLN B CD  
6363 O OE1 . GLN B 275 ? 1.5070 0.9147 1.5328 0.0937  0.1973  -0.0128 302 GLN B OE1 
6364 N NE2 . GLN B 275 ? 1.4570 0.9016 1.4798 0.1080  0.2027  -0.0378 302 GLN B NE2 
6365 N N   . ASP B 276 ? 1.2179 0.7330 1.2542 0.0167  0.1608  -0.0148 303 ASP B N   
6366 C CA  . ASP B 276 ? 1.2470 0.7626 1.2698 -0.0035 0.1554  -0.0303 303 ASP B CA  
6367 C C   . ASP B 276 ? 1.1811 0.7430 1.2074 -0.0075 0.1489  -0.0289 303 ASP B C   
6368 O O   . ASP B 276 ? 1.2142 0.7840 1.2296 -0.0110 0.1505  -0.0419 303 ASP B O   
6369 C CB  . ASP B 276 ? 1.2819 0.7746 1.3007 -0.0244 0.1494  -0.0300 303 ASP B CB  
6370 C CG  . ASP B 276 ? 1.2961 0.7368 1.3115 -0.0246 0.1564  -0.0354 303 ASP B CG  
6371 O OD1 . ASP B 276 ? 1.5362 0.9554 1.5436 -0.0115 0.1641  -0.0472 303 ASP B OD1 
6372 O OD2 . ASP B 276 ? 1.4773 0.8984 1.4991 -0.0380 0.1550  -0.0279 303 ASP B OD2 
6373 N N   . GLU B 277 ? 1.2033 0.7949 1.2439 -0.0056 0.1421  -0.0130 304 GLU B N   
6374 C CA  . GLU B 277 ? 1.1415 0.7738 1.1861 -0.0100 0.1349  -0.0124 304 GLU B CA  
6375 C C   . GLU B 277 ? 1.1197 0.7747 1.1742 0.0031  0.1418  -0.0183 304 GLU B C   
6376 O O   . GLU B 277 ? 1.1646 0.8351 1.2144 -0.0036 0.1422  -0.0262 304 GLU B O   
6377 C CB  . GLU B 277 ? 1.1328 0.7919 1.1902 -0.0088 0.1252  0.0046  304 GLU B CB  
6378 C CG  . GLU B 277 ? 1.1641 0.8615 1.2242 -0.0139 0.1161  0.0040  304 GLU B CG  
6379 C CD  . GLU B 277 ? 1.1742 0.8671 1.2154 -0.0334 0.1093  -0.0021 304 GLU B CD  
6380 O OE1 . GLU B 277 ? 1.0287 0.7078 1.0643 -0.0437 0.1049  0.0023  304 GLU B OE1 
6381 O OE2 . GLU B 277 ? 1.3039 1.0075 1.3362 -0.0378 0.1090  -0.0113 304 GLU B OE2 
6382 N N   . ALA B 278 ? 1.1501 0.8084 1.2188 0.0224  0.1481  -0.0144 305 ALA B N   
6383 C CA  . ALA B 278 ? 1.1492 0.8339 1.2320 0.0342  0.1552  -0.0216 305 ALA B CA  
6384 C C   . ALA B 278 ? 1.1563 0.8225 1.2242 0.0302  0.1659  -0.0363 305 ALA B C   
6385 O O   . ALA B 278 ? 1.2368 0.9250 1.3102 0.0281  0.1712  -0.0428 305 ALA B O   
6386 C CB  . ALA B 278 ? 0.9276 0.6212 1.0268 0.0583  0.1594  -0.0160 305 ALA B CB  
6387 N N   . GLU B 279 ? 1.1368 0.7620 1.1858 0.0296  0.1699  -0.0419 306 GLU B N   
6388 C CA  . GLU B 279 ? 1.2608 0.8692 1.2920 0.0284  0.1791  -0.0568 306 GLU B CA  
6389 C C   . GLU B 279 ? 1.1738 0.7835 1.1869 0.0105  0.1747  -0.0625 306 GLU B C   
6390 O O   . GLU B 279 ? 1.2845 0.8977 1.2866 0.0111  0.1832  -0.0713 306 GLU B O   
6391 C CB  . GLU B 279 ? 1.1212 0.6854 1.1377 0.0348  0.1832  -0.0638 306 GLU B CB  
6392 C CG  . GLU B 279 ? 1.2306 0.7906 1.2600 0.0570  0.1898  -0.0588 306 GLU B CG  
6393 C CD  . GLU B 279 ? 1.3101 0.8218 1.3234 0.0650  0.1950  -0.0670 306 GLU B CD  
6394 O OE1 . GLU B 279 ? 1.3025 0.7855 1.2965 0.0525  0.1930  -0.0791 306 GLU B OE1 
6395 O OE2 . GLU B 279 ? 1.2926 0.7952 1.3121 0.0852  0.2006  -0.0624 306 GLU B OE2 
6396 N N   . SER B 280 ? 1.1485 0.7569 1.1574 -0.0035 0.1624  -0.0568 307 SER B N   
6397 C CA  . SER B 280 ? 1.0853 0.6984 1.0755 -0.0177 0.1571  -0.0620 307 SER B CA  
6398 C C   . SER B 280 ? 1.2355 0.8808 1.2327 -0.0179 0.1599  -0.0584 307 SER B C   
6399 O O   . SER B 280 ? 1.2232 0.8681 1.2021 -0.0211 0.1651  -0.0651 307 SER B O   
6400 C CB  . SER B 280 ? 1.1218 0.7326 1.1096 -0.0315 0.1432  -0.0561 307 SER B CB  
6401 O OG  . SER B 280 ? 1.1880 0.8030 1.1547 -0.0430 0.1373  -0.0632 307 SER B OG  
6402 N N   . PHE B 281 ? 1.1066 0.7795 1.1300 -0.0134 0.1571  -0.0484 308 PHE B N   
6403 C CA  . PHE B 281 ? 1.0723 0.7742 1.1072 -0.0148 0.1604  -0.0472 308 PHE B CA  
6404 C C   . PHE B 281 ? 1.1762 0.8814 1.2176 -0.0066 0.1776  -0.0542 308 PHE B C   
6405 O O   . PHE B 281 ? 1.1681 0.8856 1.2102 -0.0109 0.1855  -0.0557 308 PHE B O   
6406 C CB  . PHE B 281 ? 1.0225 0.7560 1.0859 -0.0111 0.1511  -0.0381 308 PHE B CB  
6407 C CG  . PHE B 281 ? 0.9717 0.7339 1.0507 -0.0145 0.1529  -0.0392 308 PHE B CG  
6408 C CD1 . PHE B 281 ? 0.9589 0.7253 1.0255 -0.0257 0.1453  -0.0371 308 PHE B CD1 
6409 C CD2 . PHE B 281 ? 1.0411 0.8263 1.1483 -0.0066 0.1625  -0.0434 308 PHE B CD2 
6410 C CE1 . PHE B 281 ? 0.8161 0.6032 0.8972 -0.0294 0.1479  -0.0386 308 PHE B CE1 
6411 C CE2 . PHE B 281 ? 0.9918 0.8015 1.1175 -0.0124 0.1650  -0.0461 308 PHE B CE2 
6412 C CZ  . PHE B 281 ? 0.9053 0.7131 1.0174 -0.0241 0.1580  -0.0434 308 PHE B CZ  
6413 N N   . MET B 282 ? 1.1635 0.8576 1.2096 0.0058  0.1847  -0.0579 309 MET B N   
6414 C CA  . MET B 282 ? 1.0400 0.7391 1.0910 0.0149  0.2018  -0.0648 309 MET B CA  
6415 C C   . MET B 282 ? 1.1010 0.7793 1.1205 0.0110  0.2109  -0.0721 309 MET B C   
6416 O O   . MET B 282 ? 1.1496 0.8387 1.1710 0.0132  0.2261  -0.0743 309 MET B O   
6417 C CB  . MET B 282 ? 1.0677 0.7580 1.1265 0.0318  0.2061  -0.0675 309 MET B CB  
6418 C CG  . MET B 282 ? 1.2292 0.9286 1.2942 0.0438  0.2238  -0.0749 309 MET B CG  
6419 S SD  . MET B 282 ? 1.3947 1.0554 1.4211 0.0488  0.2337  -0.0862 309 MET B SD  
6420 C CE  . MET B 282 ? 1.2056 0.8265 1.2187 0.0536  0.2212  -0.0878 309 MET B CE  
6421 N N   . HIS B 283 ? 1.1550 0.8052 1.1459 0.0058  0.2026  -0.0762 310 HIS B N   
6422 C CA  . HIS B 283 ? 1.2101 0.8450 1.1685 0.0047  0.2093  -0.0843 310 HIS B CA  
6423 C C   . HIS B 283 ? 1.2745 0.9247 1.2263 -0.0043 0.2111  -0.0785 310 HIS B C   
6424 O O   . HIS B 283 ? 1.2328 0.8800 1.1655 -0.0006 0.2246  -0.0810 310 HIS B O   
6425 C CB  . HIS B 283 ? 1.0893 0.6954 1.0221 0.0008  0.1978  -0.0933 310 HIS B CB  
6426 C CG  . HIS B 283 ? 1.2138 0.8048 1.1119 0.0055  0.2040  -0.1057 310 HIS B CG  
6427 N ND1 . HIS B 283 ? 1.2198 0.8096 1.0918 -0.0016 0.1969  -0.1092 310 HIS B ND1 
6428 C CD2 . HIS B 283 ? 1.2489 0.8280 1.1323 0.0195  0.2165  -0.1159 310 HIS B CD2 
6429 C CE1 . HIS B 283 ? 1.4916 1.0697 1.3337 0.0086  0.2046  -0.1212 310 HIS B CE1 
6430 N NE2 . HIS B 283 ? 1.2976 0.8688 1.1460 0.0213  0.2166  -0.1254 310 HIS B NE2 
6431 N N   . VAL B 284 ? 1.2191 0.8845 1.1846 -0.0142 0.1987  -0.0702 311 VAL B N   
6432 C CA  . VAL B 284 ? 1.1267 0.8054 1.0886 -0.0216 0.2005  -0.0644 311 VAL B CA  
6433 C C   . VAL B 284 ? 1.1428 0.8369 1.1247 -0.0185 0.2195  -0.0621 311 VAL B C   
6434 O O   . VAL B 284 ? 1.1952 0.8855 1.1611 -0.0196 0.2323  -0.0603 311 VAL B O   
6435 C CB  . VAL B 284 ? 1.0812 0.7763 1.0585 -0.0303 0.1830  -0.0568 311 VAL B CB  
6436 C CG1 . VAL B 284 ? 0.9651 0.6729 0.9427 -0.0364 0.1856  -0.0516 311 VAL B CG1 
6437 C CG2 . VAL B 284 ? 1.2144 0.8964 1.1706 -0.0355 0.1667  -0.0583 311 VAL B CG2 
6438 N N   . GLN B 285 ? 1.0988 0.8116 1.1163 -0.0138 0.2225  -0.0621 312 GLN B N   
6439 C CA  . GLN B 285 ? 1.1055 0.8372 1.1474 -0.0116 0.2416  -0.0622 312 GLN B CA  
6440 C C   . GLN B 285 ? 1.1899 0.9056 1.2079 -0.0035 0.2613  -0.0659 312 GLN B C   
6441 O O   . GLN B 285 ? 1.0838 0.8061 1.1051 -0.0056 0.2799  -0.0628 312 GLN B O   
6442 C CB  . GLN B 285 ? 0.9337 0.6911 1.0156 -0.0043 0.2398  -0.0645 312 GLN B CB  
6443 C CG  . GLN B 285 ? 1.0572 0.8428 1.1710 -0.0104 0.2264  -0.0615 312 GLN B CG  
6444 C CD  . GLN B 285 ? 1.1324 0.9358 1.2707 0.0014  0.2160  -0.0627 312 GLN B CD  
6445 O OE1 . GLN B 285 ? 1.2581 1.0414 1.3793 0.0085  0.2078  -0.0610 312 GLN B OE1 
6446 N NE2 . GLN B 285 ? 0.8379 0.6792 1.0167 0.0041  0.2169  -0.0662 312 GLN B NE2 
6447 N N   . LEU B 286 ? 1.1724 0.8663 1.1661 0.0062  0.2581  -0.0726 313 LEU B N   
6448 C CA  . LEU B 286 ? 1.0931 0.7721 1.0595 0.0170  0.2746  -0.0778 313 LEU B CA  
6449 C C   . LEU B 286 ? 1.1728 0.8390 1.1038 0.0137  0.2801  -0.0747 313 LEU B C   
6450 O O   . LEU B 286 ? 1.2157 0.8833 1.1370 0.0191  0.3011  -0.0714 313 LEU B O   
6451 C CB  . LEU B 286 ? 1.1594 0.8151 1.1063 0.0276  0.2664  -0.0884 313 LEU B CB  
6452 C CG  . LEU B 286 ? 1.1144 0.7752 1.0867 0.0375  0.2654  -0.0918 313 LEU B CG  
6453 C CD1 . LEU B 286 ? 1.1690 0.7978 1.1172 0.0462  0.2570  -0.1026 313 LEU B CD1 
6454 C CD2 . LEU B 286 ? 1.1086 0.7908 1.0992 0.0481  0.2865  -0.0918 313 LEU B CD2 
6455 N N   . GLU B 287 ? 1.2059 0.8607 1.1164 0.0065  0.2622  -0.0750 314 GLU B N   
6456 C CA  . GLU B 287 ? 1.2283 0.8721 1.1015 0.0065  0.2655  -0.0727 314 GLU B CA  
6457 C C   . GLU B 287 ? 1.3685 1.0230 1.2529 0.0007  0.2814  -0.0604 314 GLU B C   
6458 O O   . GLU B 287 ? 1.4248 1.0697 1.2807 0.0071  0.2976  -0.0560 314 GLU B O   
6459 C CB  . GLU B 287 ? 1.0994 0.7364 0.9557 -0.0012 0.2420  -0.0755 314 GLU B CB  
6460 C CG  . GLU B 287 ? 1.0965 0.7186 0.9386 0.0024  0.2283  -0.0890 314 GLU B CG  
6461 C CD  . GLU B 287 ? 1.4612 1.0679 1.2653 0.0170  0.2373  -0.1004 314 GLU B CD  
6462 O OE1 . GLU B 287 ? 1.4733 1.0758 1.2426 0.0202  0.2347  -0.1031 314 GLU B OE1 
6463 O OE2 . GLU B 287 ? 1.5242 1.1244 1.3315 0.0276  0.2465  -0.1073 314 GLU B OE2 
6464 N N   . VAL B 288 ? 1.2077 0.8817 1.1335 -0.0105 0.2778  -0.0552 315 VAL B N   
6465 C CA  . VAL B 288 ? 1.1517 0.8351 1.0952 -0.0183 0.2932  -0.0460 315 VAL B CA  
6466 C C   . VAL B 288 ? 1.2407 0.9281 1.1925 -0.0119 0.3219  -0.0438 315 VAL B C   
6467 O O   . VAL B 288 ? 1.2985 0.9788 1.2398 -0.0130 0.3422  -0.0350 315 VAL B O   
6468 C CB  . VAL B 288 ? 1.1411 0.8487 1.1311 -0.0302 0.2811  -0.0452 315 VAL B CB  
6469 C CG1 . VAL B 288 ? 1.1615 0.8782 1.1756 -0.0401 0.2978  -0.0389 315 VAL B CG1 
6470 C CG2 . VAL B 288 ? 1.0976 0.8026 1.0766 -0.0352 0.2548  -0.0452 315 VAL B CG2 
6471 N N   . MET B 289 ? 1.0909 0.7891 1.0603 -0.0039 0.3252  -0.0508 316 MET B N   
6472 C CA  . MET B 289 ? 1.2234 0.9321 1.2060 0.0028  0.3523  -0.0491 316 MET B CA  
6473 C C   . MET B 289 ? 1.2825 0.9703 1.2178 0.0179  0.3687  -0.0475 316 MET B C   
6474 O O   . MET B 289 ? 1.1972 0.8933 1.1384 0.0250  0.3940  -0.0440 316 MET B O   
6475 C CB  . MET B 289 ? 1.1088 0.8380 1.1235 0.0096  0.3493  -0.0578 316 MET B CB  
6476 C CG  . MET B 289 ? 1.1114 0.8716 1.1796 -0.0015 0.3416  -0.0590 316 MET B CG  
6477 S SD  . MET B 289 ? 1.3685 1.1539 1.4693 0.0118  0.3381  -0.0689 316 MET B SD  
6478 C CE  . MET B 289 ? 1.0074 0.7630 1.0742 0.0202  0.3116  -0.0735 316 MET B CE  
6479 N N   . VAL B 290 ? 1.2319 0.8964 1.1214 0.0241  0.3552  -0.0508 317 VAL B N   
6480 C CA  . VAL B 290 ? 1.3767 1.0240 1.2177 0.0413  0.3693  -0.0506 317 VAL B CA  
6481 C C   . VAL B 290 ? 1.3766 1.0197 1.2069 0.0400  0.3946  -0.0346 317 VAL B C   
6482 O O   . VAL B 290 ? 1.4155 1.0578 1.2321 0.0526  0.4208  -0.0287 317 VAL B O   
6483 C CB  . VAL B 290 ? 1.3455 0.9739 1.1437 0.0475  0.3465  -0.0608 317 VAL B CB  
6484 C CG1 . VAL B 290 ? 1.3929 1.0071 1.1383 0.0674  0.3599  -0.0613 317 VAL B CG1 
6485 C CG2 . VAL B 290 ? 1.4504 1.0774 1.2581 0.0497  0.3269  -0.0762 317 VAL B CG2 
6486 N N   . LYS B 291 ? 1.4179 1.0569 1.2539 0.0257  0.3881  -0.0267 318 LYS B N   
6487 C CA  . LYS B 291 ? 1.3631 0.9905 1.1851 0.0243  0.4111  -0.0108 318 LYS B CA  
6488 C C   . LYS B 291 ? 1.3605 0.9993 1.2327 0.0028  0.4182  -0.0030 318 LYS B C   
6489 O O   . LYS B 291 ? 1.5120 1.1370 1.3768 -0.0013 0.4375  0.0106  318 LYS B O   
6490 C CB  . LYS B 291 ? 1.6544 1.2598 1.4242 0.0316  0.3991  -0.0085 318 LYS B CB  
6491 C CG  . LYS B 291 ? 1.7554 1.3480 1.4678 0.0566  0.4036  -0.0128 318 LYS B CG  
6492 C CD  . LYS B 291 ? 2.0712 1.6475 1.7347 0.0644  0.3919  -0.0110 318 LYS B CD  
6493 C CE  . LYS B 291 ? 2.1098 1.6730 1.7147 0.0920  0.4094  -0.0076 318 LYS B CE  
6494 N NZ  . LYS B 291 ? 1.9650 1.5137 1.5231 0.1014  0.4031  -0.0023 318 LYS B NZ  
6495 N N   . HIS B 292 ? 1.4668 0.9010 1.3355 0.1403  0.1167  0.0722  319 HIS B N   
6496 C CA  . HIS B 292 ? 1.3296 0.7528 1.1995 0.1303  0.1263  0.0748  319 HIS B CA  
6497 C C   . HIS B 292 ? 1.2719 0.7209 1.1497 0.1162  0.1412  0.0714  319 HIS B C   
6498 O O   . HIS B 292 ? 1.3728 0.8461 1.2592 0.1184  0.1433  0.0667  319 HIS B O   
6499 C CB  . HIS B 292 ? 1.2447 0.6718 1.1438 0.1386  0.1222  0.0683  319 HIS B CB  
6500 C CG  . HIS B 292 ? 1.3400 0.7556 1.2391 0.1568  0.1061  0.0667  319 HIS B CG  
6501 N ND1 . HIS B 292 ? 1.4704 0.9071 1.3808 0.1676  0.0959  0.0588  319 HIS B ND1 
6502 C CD2 . HIS B 292 ? 1.2620 0.6502 1.1507 0.1674  0.0986  0.0700  319 HIS B CD2 
6503 C CE1 . HIS B 292 ? 1.5025 0.9324 1.4119 0.1848  0.0816  0.0562  319 HIS B CE1 
6504 N NE2 . HIS B 292 ? 1.4027 0.8012 1.2980 0.1871  0.0824  0.0637  319 HIS B NE2 
6505 N N   . PRO B 293 ? 1.2984 0.7441 1.1716 0.1023  0.1523  0.0722  320 PRO B N   
6506 C CA  . PRO B 293 ? 1.1866 0.6684 1.0760 0.0940  0.1646  0.0651  320 PRO B CA  
6507 C C   . PRO B 293 ? 1.2389 0.7406 1.1610 0.1061  0.1623  0.0584  320 PRO B C   
6508 O O   . PRO B 293 ? 1.2369 0.7248 1.1719 0.1149  0.1539  0.0578  320 PRO B O   
6509 C CB  . PRO B 293 ? 1.2043 0.6771 1.0829 0.0757  0.1757  0.0649  320 PRO B CB  
6510 C CG  . PRO B 293 ? 1.2527 0.6772 1.0958 0.0710  0.1727  0.0744  320 PRO B CG  
6511 C CD  . PRO B 293 ? 1.2546 0.6619 1.1013 0.0931  0.1554  0.0788  320 PRO B CD  
6512 N N   . PRO B 294 ? 1.2701 0.8035 1.2035 0.1080  0.1700  0.0525  321 PRO B N   
6513 C CA  . PRO B 294 ? 1.1592 0.7037 1.1158 0.1192  0.1699  0.0471  321 PRO B CA  
6514 C C   . PRO B 294 ? 1.0974 0.6386 1.0696 0.1153  0.1711  0.0453  321 PRO B C   
6515 O O   . PRO B 294 ? 1.3158 0.8621 1.2841 0.1032  0.1776  0.0451  321 PRO B O   
6516 C CB  . PRO B 294 ? 1.1246 0.6999 1.0799 0.1240  0.1790  0.0426  321 PRO B CB  
6517 C CG  . PRO B 294 ? 1.3186 0.9101 1.2597 0.1104  0.1853  0.0424  321 PRO B CG  
6518 C CD  . PRO B 294 ? 1.2501 0.8110 1.1728 0.1014  0.1795  0.0495  321 PRO B CD  
6519 N N   . ALA B 295 ? 1.2912 0.8245 1.2805 0.1236  0.1659  0.0423  322 ALA B N   
6520 C CA  . ALA B 295 ? 1.0770 0.6083 1.0832 0.1211  0.1667  0.0393  322 ALA B CA  
6521 C C   . ALA B 295 ? 1.0972 0.6558 1.1114 0.1193  0.1771  0.0352  322 ALA B C   
6522 O O   . ALA B 295 ? 1.1993 0.7704 1.2163 0.1290  0.1806  0.0324  322 ALA B O   
6523 C CB  . ALA B 295 ? 1.0656 0.5885 1.0889 0.1294  0.1597  0.0342  322 ALA B CB  
6524 N N   . GLU B 296 ? 1.1490 0.7153 1.1630 0.1073  0.1828  0.0341  323 GLU B N   
6525 C CA  . GLU B 296 ? 1.1239 0.7252 1.1446 0.1051  0.1923  0.0281  323 GLU B CA  
6526 C C   . GLU B 296 ? 1.2463 0.8524 1.2864 0.1120  0.1927  0.0240  323 GLU B C   
6527 O O   . GLU B 296 ? 1.1659 0.7495 1.2169 0.1115  0.1875  0.0240  323 GLU B O   
6528 C CB  . GLU B 296 ? 1.2768 0.8870 1.2906 0.0854  0.2002  0.0249  323 GLU B CB  
6529 C CG  . GLU B 296 ? 1.5648 1.1664 1.5547 0.0741  0.2024  0.0283  323 GLU B CG  
6530 C CD  . GLU B 296 ? 1.5649 1.2001 1.5486 0.0813  0.2050  0.0257  323 GLU B CD  
6531 O OE1 . GLU B 296 ? 1.3433 1.0159 1.3377 0.0920  0.2083  0.0191  323 GLU B OE1 
6532 O OE2 . GLU B 296 ? 1.5778 1.2012 1.5434 0.0783  0.2034  0.0300  323 GLU B OE2 
6533 N N   . PRO B 297 ? 1.1461 0.7821 1.1887 0.1201  0.1986  0.0197  324 PRO B N   
6534 C CA  . PRO B 297 ? 1.1469 0.7871 1.2032 0.1258  0.2005  0.0160  324 PRO B CA  
6535 C C   . PRO B 297 ? 1.1527 0.8097 1.2214 0.1117  0.2050  0.0102  324 PRO B C   
6536 O O   . PRO B 297 ? 1.2946 0.9558 1.3590 0.0962  0.2081  0.0085  324 PRO B O   
6537 C CB  . PRO B 297 ? 1.1592 0.8220 1.2043 0.1436  0.2050  0.0149  324 PRO B CB  
6538 C CG  . PRO B 297 ? 1.0080 0.6998 1.0422 0.1421  0.2074  0.0132  324 PRO B CG  
6539 C CD  . PRO B 297 ? 1.0924 0.7593 1.1221 0.1285  0.2031  0.0179  324 PRO B CD  
6540 N N   . SER B 298 ? 1.1285 0.7923 1.2098 0.1156  0.2070  0.0062  325 SER B N   
6541 C CA  . SER B 298 ? 1.2047 0.8886 1.2983 0.1027  0.2124  -0.0012 325 SER B CA  
6542 C C   . SER B 298 ? 1.2951 1.0285 1.3833 0.1013  0.2196  -0.0082 325 SER B C   
6543 O O   . SER B 298 ? 1.3483 1.1043 1.4260 0.1185  0.2197  -0.0078 325 SER B O   
6544 C CB  . SER B 298 ? 1.1219 0.8033 1.2294 0.1080  0.2127  -0.0043 325 SER B CB  
6545 O OG  . SER B 298 ? 1.2289 0.9423 1.3459 0.0996  0.2193  -0.0128 325 SER B OG  
6546 N N   . ARG B 299 ? 1.2661 1.0176 1.3598 0.0807  0.2264  -0.0166 326 ARG B N   
6547 C CA  . ARG B 299 ? 1.2294 1.0396 1.3222 0.0765  0.2342  -0.0284 326 ARG B CA  
6548 C C   . ARG B 299 ? 1.2434 1.0901 1.3459 0.0901  0.2353  -0.0349 326 ARG B C   
6549 O O   . ARG B 299 ? 1.3628 1.2670 1.4668 0.0890  0.2409  -0.0473 326 ARG B O   
6550 C CB  . ARG B 299 ? 1.2898 1.1071 1.3819 0.0452  0.2443  -0.0383 326 ARG B CB  
6551 C CG  . ARG B 299 ? 1.5340 1.3183 1.6357 0.0298  0.2470  -0.0396 326 ARG B CG  
6552 C CD  . ARG B 299 ? 1.7585 1.5276 1.8477 -0.0016 0.2586  -0.0463 326 ARG B CD  
6553 N NE  . ARG B 299 ? 1.9593 1.6824 2.0512 -0.0126 0.2605  -0.0454 326 ARG B NE  
6554 C CZ  . ARG B 299 ? 1.8990 1.5605 1.9826 -0.0065 0.2528  -0.0333 326 ARG B CZ  
6555 N NH1 . ARG B 299 ? 1.7342 1.3729 1.8077 0.0085  0.2426  -0.0210 326 ARG B NH1 
6556 N NH2 . ARG B 299 ? 1.5474 1.1720 1.6325 -0.0140 0.2551  -0.0349 326 ARG B NH2 
6557 N N   . PHE B 300 ? 1.1225 0.9397 1.2301 0.1026  0.2306  -0.0281 327 PHE B N   
6558 C CA  . PHE B 300 ? 1.1570 0.9995 1.2670 0.1179  0.2317  -0.0318 327 PHE B CA  
6559 C C   . PHE B 300 ? 1.2392 1.0580 1.3324 0.1453  0.2276  -0.0218 327 PHE B C   
6560 O O   . PHE B 300 ? 1.2448 1.0832 1.3290 0.1634  0.2291  -0.0234 327 PHE B O   
6561 C CB  . PHE B 300 ? 1.1260 0.9554 1.2543 0.1038  0.2339  -0.0359 327 PHE B CB  
6562 C CG  . PHE B 300 ? 1.1655 1.0002 1.3052 0.0752  0.2398  -0.0449 327 PHE B CG  
6563 C CD1 . PHE B 300 ? 1.2403 1.1289 1.3817 0.0624  0.2480  -0.0588 327 PHE B CD1 
6564 C CD2 . PHE B 300 ? 1.2559 1.0413 1.4015 0.0615  0.2382  -0.0409 327 PHE B CD2 
6565 C CE1 . PHE B 300 ? 1.1150 1.0012 1.2610 0.0322  0.2569  -0.0683 327 PHE B CE1 
6566 C CE2 . PHE B 300 ? 1.2055 0.9843 1.3530 0.0364  0.2456  -0.0483 327 PHE B CE2 
6567 C CZ  . PHE B 300 ? 1.2245 1.0502 1.3709 0.0196  0.2562  -0.0619 327 PHE B CZ  
6568 N N   . ILE B 301 ? 1.2270 1.0021 1.3119 0.1484  0.2235  -0.0124 328 ILE B N   
6569 C CA  . ILE B 301 ? 1.1910 0.9379 1.2545 0.1706  0.2225  -0.0044 328 ILE B CA  
6570 C C   . ILE B 301 ? 1.2873 1.0419 1.3330 0.1824  0.2210  -0.0012 328 ILE B C   
6571 O O   . ILE B 301 ? 1.1878 0.9438 1.2396 0.1684  0.2188  -0.0014 328 ILE B O   
6572 C CB  . ILE B 301 ? 1.2115 0.9059 1.2798 0.1632  0.2204  0.0004  328 ILE B CB  
6573 C CG1 . ILE B 301 ? 1.1784 0.8688 1.2680 0.1496  0.2215  -0.0048 328 ILE B CG1 
6574 C CG2 . ILE B 301 ? 1.3239 0.9862 1.3659 0.1814  0.2236  0.0060  328 ILE B CG2 
6575 C CD1 . ILE B 301 ? 1.2594 0.9091 1.3569 0.1424  0.2191  -0.0042 328 ILE B CD1 
6576 N N   . SER B 302 ? 1.5071 1.2634 1.5272 0.2093  0.2227  0.0017  329 SER B N   
6577 C CA  . SER B 302 ? 1.5096 1.2710 1.5098 0.2250  0.2217  0.0040  329 SER B CA  
6578 C C   . SER B 302 ? 1.5548 1.2591 1.5294 0.2389  0.2236  0.0129  329 SER B C   
6579 O O   . SER B 302 ? 1.6669 1.3470 1.6211 0.2544  0.2283  0.0159  329 SER B O   
6580 C CB  . SER B 302 ? 1.6863 1.5038 1.6740 0.2485  0.2226  -0.0029 329 SER B CB  
6581 O OG  . SER B 302 ? 1.5980 1.4731 1.6098 0.2308  0.2231  -0.0149 329 SER B OG  
6582 N N   . ALA B 303 ? 1.5095 1.1901 1.4820 0.2317  0.2215  0.0163  330 ALA B N   
6583 C CA  . ALA B 303 ? 1.6942 1.3231 1.6412 0.2416  0.2251  0.0220  330 ALA B CA  
6584 C C   . ALA B 303 ? 1.6333 1.2629 1.5433 0.2743  0.2294  0.0241  330 ALA B C   
6585 O O   . ALA B 303 ? 1.5494 1.2263 1.4587 0.2872  0.2265  0.0202  330 ALA B O   
6586 C CB  . ALA B 303 ? 1.7040 1.3149 1.6591 0.2258  0.2211  0.0234  330 ALA B CB  
6587 N N   . PRO B 304 ? 1.7629 1.3398 1.6387 0.2885  0.2372  0.0287  331 PRO B N   
6588 C CA  . PRO B 304 ? 1.9558 1.5235 1.7880 0.3247  0.2420  0.0317  331 PRO B CA  
6589 C C   . PRO B 304 ? 1.9043 1.4842 1.7290 0.3340  0.2393  0.0307  331 PRO B C   
6590 O O   . PRO B 304 ? 1.8457 1.4118 1.6841 0.3132  0.2375  0.0306  331 PRO B O   
6591 C CB  . PRO B 304 ? 1.8105 1.3029 1.6046 0.3289  0.2540  0.0368  331 PRO B CB  
6592 C CG  . PRO B 304 ? 1.8513 1.3204 1.6733 0.2926  0.2543  0.0340  331 PRO B CG  
6593 C CD  . PRO B 304 ? 1.7494 1.2719 1.6215 0.2720  0.2435  0.0299  331 PRO B CD  
6594 N N   . THR B 305 ? 1.8815 1.4911 1.6832 0.3674  0.2385  0.0290  332 THR B N   
6595 C CA  . THR B 305 ? 1.9569 1.5858 1.7509 0.3794  0.2362  0.0261  332 THR B CA  
6596 C C   . THR B 305 ? 2.0053 1.5626 1.7605 0.3887  0.2446  0.0319  332 THR B C   
6597 O O   . THR B 305 ? 2.1005 1.6042 1.8126 0.4102  0.2537  0.0372  332 THR B O   
6598 C CB  . THR B 305 ? 2.0309 1.7178 1.8109 0.4160  0.2328  0.0197  332 THR B CB  
6599 O OG1 . THR B 305 ? 2.0007 1.7626 1.8204 0.4004  0.2263  0.0102  332 THR B OG1 
6600 C CG2 . THR B 305 ? 1.8858 1.5872 1.6513 0.4334  0.2318  0.0156  332 THR B CG2 
6601 N N   . LYS B 306 ? 1.8130 1.3666 1.5799 0.3715  0.2429  0.0303  333 LYS B N   
6602 C CA  . LYS B 306 ? 1.8048 1.2959 1.5378 0.3761  0.2516  0.0331  333 LYS B CA  
6603 C C   . LYS B 306 ? 1.8310 1.3335 1.5338 0.4102  0.2525  0.0308  333 LYS B C   
6604 O O   . LYS B 306 ? 1.7964 1.3664 1.5174 0.4196  0.2444  0.0247  333 LYS B O   
6605 C CB  . LYS B 306 ? 1.7189 1.1991 1.4796 0.3393  0.2491  0.0315  333 LYS B CB  
6606 C CG  . LYS B 306 ? 1.4370 0.9786 1.2425 0.3180  0.2372  0.0282  333 LYS B CG  
6607 C CD  . LYS B 306 ? 1.4628 0.9860 1.2921 0.2843  0.2339  0.0284  333 LYS B CD  
6608 C CE  . LYS B 306 ? 1.5479 1.0338 1.3816 0.2704  0.2379  0.0292  333 LYS B CE  
6609 N NZ  . LYS B 306 ? 1.5551 1.0320 1.4137 0.2413  0.2329  0.0269  333 LYS B NZ  
6610 N N   . THR B 307 ? 1.8369 1.2721 1.4914 0.4279  0.2639  0.0340  334 THR B N   
6611 C CA  . THR B 307 ? 1.8971 1.3294 1.5157 0.4632  0.2666  0.0319  334 THR B CA  
6612 C C   . THR B 307 ? 1.7887 1.1710 1.3939 0.4464  0.2743  0.0308  334 THR B C   
6613 O O   . THR B 307 ? 1.8737 1.1813 1.4501 0.4359  0.2873  0.0337  334 THR B O   
6614 C CB  . THR B 307 ? 1.9233 1.3135 1.4826 0.5090  0.2749  0.0368  334 THR B CB  
6615 O OG1 . THR B 307 ? 1.9752 1.2791 1.5018 0.4970  0.2892  0.0435  334 THR B OG1 
6616 C CG2 . THR B 307 ? 1.7434 1.1981 1.3164 0.5304  0.2652  0.0353  334 THR B CG2 
6617 N N   . PRO B 308 ? 1.7310 1.1520 1.3550 0.4410  0.2682  0.0252  335 PRO B N   
6618 C CA  . PRO B 308 ? 1.7612 1.1412 1.3765 0.4221  0.2747  0.0230  335 PRO B CA  
6619 C C   . PRO B 308 ? 1.8594 1.1930 1.4192 0.4562  0.2859  0.0215  335 PRO B C   
6620 O O   . PRO B 308 ? 1.9709 1.3066 1.4976 0.4989  0.2872  0.0225  335 PRO B O   
6621 C CB  . PRO B 308 ? 1.6834 1.1317 1.3453 0.3998  0.2620  0.0180  335 PRO B CB  
6622 C CG  . PRO B 308 ? 1.5656 1.0836 1.2371 0.4252  0.2540  0.0142  335 PRO B CG  
6623 C CD  . PRO B 308 ? 1.6907 1.2007 1.3504 0.4438  0.2554  0.0188  335 PRO B CD  
6624 N N   . ASP B 309 ? 1.8784 1.1705 1.4270 0.4377  0.2939  0.0182  336 ASP B N   
6625 C CA  . ASP B 309 ? 2.0204 1.2642 1.5174 0.4642  0.3059  0.0153  336 ASP B CA  
6626 C C   . ASP B 309 ? 1.9621 1.2136 1.4774 0.4366  0.3053  0.0082  336 ASP B C   
6627 O O   . ASP B 309 ? 1.7975 1.0901 1.3615 0.4008  0.2950  0.0068  336 ASP B O   
6628 C CB  . ASP B 309 ? 1.9921 1.1355 1.4279 0.4737  0.3263  0.0190  336 ASP B CB  
6629 C CG  . ASP B 309 ? 1.8702 0.9756 1.3204 0.4272  0.3340  0.0176  336 ASP B CG  
6630 O OD1 . ASP B 309 ? 1.9390 1.0550 1.4171 0.3929  0.3325  0.0107  336 ASP B OD1 
6631 O OD2 . ASP B 309 ? 1.9657 1.0332 1.3984 0.4256  0.3417  0.0222  336 ASP B OD2 
6632 N N   . LYS B 310 ? 2.0596 1.2688 1.5321 0.4551  0.3167  0.0038  337 LYS B N   
6633 C CA  . LYS B 310 ? 2.0245 1.2308 1.5058 0.4299  0.3190  -0.0039 337 LYS B CA  
6634 C C   . LYS B 310 ? 2.0112 1.1430 1.4712 0.3993  0.3354  -0.0076 337 LYS B C   
6635 O O   . LYS B 310 ? 2.0043 1.1172 1.4559 0.3838  0.3423  -0.0159 337 LYS B O   
6636 C CB  . LYS B 310 ? 2.0819 1.2877 1.5310 0.4638  0.3230  -0.0095 337 LYS B CB  
6637 C CG  . LYS B 310 ? 1.9711 1.2628 1.4443 0.4909  0.3075  -0.0112 337 LYS B CG  
6638 C CD  . LYS B 310 ? 1.8572 1.2279 1.3931 0.4549  0.2917  -0.0134 337 LYS B CD  
6639 C CE  . LYS B 310 ? 1.8532 1.3098 1.4098 0.4765  0.2802  -0.0192 337 LYS B CE  
6640 N NZ  . LYS B 310 ? 1.8303 1.2916 1.3594 0.5049  0.2848  -0.0287 337 LYS B NZ  
6641 N N   . MET B 311 ? 1.9426 1.0356 1.3940 0.3886  0.3425  -0.0037 338 MET B N   
6642 C CA  . MET B 311 ? 1.9359 0.9619 1.3666 0.3565  0.3603  -0.0105 338 MET B CA  
6643 C C   . MET B 311 ? 2.0075 0.9513 1.3715 0.3690  0.3837  -0.0167 338 MET B C   
6644 O O   . MET B 311 ? 2.0731 0.9771 1.4256 0.3369  0.3981  -0.0280 338 MET B O   
6645 C CB  . MET B 311 ? 1.9502 1.0181 1.4335 0.3113  0.3509  -0.0187 338 MET B CB  
6646 C CG  . MET B 311 ? 1.8335 0.9656 1.3752 0.2954  0.3314  -0.0133 338 MET B CG  
6647 S SD  . MET B 311 ? 1.8788 1.0459 1.4694 0.2479  0.3222  -0.0236 338 MET B SD  
6648 C CE  . MET B 311 ? 1.8514 1.0425 1.4407 0.2512  0.3178  -0.0283 338 MET B CE  
6649 N N   . GLY B 312 ? 1.9378 0.8562 1.2555 0.4164  0.3881  -0.0109 339 GLY B N   
6650 C CA  . GLY B 312 ? 1.9002 0.7352 1.1487 0.4335  0.4106  -0.0161 339 GLY B CA  
6651 C C   . GLY B 312 ? 1.8928 0.7516 1.1506 0.4295  0.4085  -0.0258 339 GLY B C   
6652 O O   . GLY B 312 ? 2.2516 1.0433 1.4553 0.4361  0.4275  -0.0319 339 GLY B O   
6653 N N   . PHE B 313 ? 1.9785 0.9311 1.3014 0.4159  0.3861  -0.0272 340 PHE B N   
6654 C CA  . PHE B 313 ? 2.0766 1.0588 1.4096 0.4131  0.3827  -0.0359 340 PHE B CA  
6655 C C   . PHE B 313 ? 2.0177 1.0271 1.3327 0.4638  0.3764  -0.0336 340 PHE B C   
6656 O O   . PHE B 313 ? 2.0570 1.0882 1.3685 0.4980  0.3685  -0.0255 340 PHE B O   
6657 C CB  . PHE B 313 ? 1.9344 1.0004 1.3384 0.3760  0.3626  -0.0382 340 PHE B CB  
6658 C CG  . PHE B 313 ? 1.9259 0.9742 1.3476 0.3280  0.3679  -0.0455 340 PHE B CG  
6659 C CD1 . PHE B 313 ? 1.9172 0.9376 1.3241 0.3048  0.3800  -0.0589 340 PHE B CD1 
6660 C CD2 . PHE B 313 ? 1.9066 0.9715 1.3607 0.3065  0.3606  -0.0410 340 PHE B CD2 
6661 C CE1 . PHE B 313 ? 1.8175 0.8319 1.2423 0.2613  0.3844  -0.0691 340 PHE B CE1 
6662 C CE2 . PHE B 313 ? 1.8358 0.8931 1.3078 0.2648  0.3645  -0.0506 340 PHE B CE2 
6663 C CZ  . PHE B 313 ? 1.8702 0.9048 1.3280 0.2424  0.3762  -0.0654 340 PHE B CZ  
6664 N N   . ASP B 314 ? 1.8470 0.8597 1.1511 0.4689  0.3799  -0.0429 341 ASP B N   
6665 C CA  . ASP B 314 ? 2.0363 1.0922 1.3328 0.5141  0.3718  -0.0445 341 ASP B CA  
6666 C C   . ASP B 314 ? 2.0004 1.1695 1.3647 0.5046  0.3474  -0.0439 341 ASP B C   
6667 O O   . ASP B 314 ? 1.8769 1.1000 1.2456 0.5409  0.3375  -0.0444 341 ASP B O   
6668 C CB  . ASP B 314 ? 2.0646 1.0866 1.3263 0.5221  0.3846  -0.0559 341 ASP B CB  
6669 C CG  . ASP B 314 ? 2.2312 1.1344 1.4116 0.5430  0.4114  -0.0570 341 ASP B CG  
6670 O OD1 . ASP B 314 ? 2.1693 1.0095 1.3322 0.5145  0.4244  -0.0539 341 ASP B OD1 
6671 O OD2 . ASP B 314 ? 2.4388 1.3277 1.5805 0.5777  0.4139  -0.0585 341 ASP B OD2 
6672 N N   . GLU B 315 ? 2.0920 1.2975 1.5060 0.4568  0.3383  -0.0439 342 GLU B N   
6673 C CA  . GLU B 315 ? 1.9778 1.2772 1.4504 0.4415  0.3179  -0.0421 342 GLU B CA  
6674 C C   . GLU B 315 ? 1.8194 1.1262 1.3308 0.3918  0.3117  -0.0392 342 GLU B C   
6675 O O   . GLU B 315 ? 1.7824 1.0450 1.2828 0.3671  0.3210  -0.0440 342 GLU B O   
6676 C CB  . GLU B 315 ? 1.8054 1.1626 1.2888 0.4495  0.3120  -0.0516 342 GLU B CB  
6677 C CG  . GLU B 315 ? 1.7571 1.2082 1.2925 0.4343  0.2943  -0.0513 342 GLU B CG  
6678 C CD  . GLU B 315 ? 1.8866 1.3818 1.4308 0.4625  0.2870  -0.0487 342 GLU B CD  
6679 O OE1 . GLU B 315 ? 1.9066 1.3878 1.4603 0.4557  0.2845  -0.0395 342 GLU B OE1 
6680 O OE2 . GLU B 315 ? 1.8873 1.4359 1.4295 0.4913  0.2839  -0.0579 342 GLU B OE2 
6681 N N   . VAL B 316 ? 1.7009 1.0644 1.2555 0.3784  0.2965  -0.0328 343 VAL B N   
6682 C CA  . VAL B 316 ? 1.6600 1.0400 1.2529 0.3368  0.2874  -0.0296 343 VAL B CA  
6683 C C   . VAL B 316 ? 1.7245 1.1787 1.3528 0.3246  0.2729  -0.0297 343 VAL B C   
6684 O O   . VAL B 316 ? 1.7260 1.2280 1.3721 0.3347  0.2651  -0.0268 343 VAL B O   
6685 C CB  . VAL B 316 ? 1.6774 1.0451 1.2842 0.3296  0.2847  -0.0214 343 VAL B CB  
6686 C CG1 . VAL B 316 ? 1.6957 1.0841 1.3414 0.2910  0.2739  -0.0192 343 VAL B CG1 
6687 C CG2 . VAL B 316 ? 1.5051 0.7947 1.0704 0.3396  0.3020  -0.0221 343 VAL B CG2 
6688 N N   . PHE B 317 ? 1.6195 1.0827 1.2549 0.3017  0.2705  -0.0341 344 PHE B N   
6689 C CA  . PHE B 317 ? 1.5538 1.0777 1.2145 0.2869  0.2593  -0.0342 344 PHE B CA  
6690 C C   . PHE B 317 ? 1.6092 1.1465 1.3003 0.2556  0.2476  -0.0262 344 PHE B C   
6691 O O   . PHE B 317 ? 1.5669 1.0704 1.2616 0.2416  0.2474  -0.0238 344 PHE B O   
6692 C CB  . PHE B 317 ? 1.6249 1.1518 1.2725 0.2811  0.2629  -0.0430 344 PHE B CB  
6693 C CG  . PHE B 317 ? 1.7080 1.2233 1.3242 0.3137  0.2742  -0.0521 344 PHE B CG  
6694 C CD1 . PHE B 317 ? 1.7078 1.2761 1.3263 0.3346  0.2719  -0.0575 344 PHE B CD1 
6695 C CD2 . PHE B 317 ? 1.7618 1.2133 1.3438 0.3232  0.2881  -0.0572 344 PHE B CD2 
6696 C CE1 . PHE B 317 ? 1.7038 1.2639 1.2921 0.3695  0.2811  -0.0671 344 PHE B CE1 
6697 C CE2 . PHE B 317 ? 1.7445 1.1779 1.2916 0.3565  0.2991  -0.0652 344 PHE B CE2 
6698 C CZ  . PHE B 317 ? 1.7778 1.2668 1.3287 0.3821  0.2945  -0.0698 344 PHE B CZ  
6699 N N   . MET B 318 ? 1.6096 1.1964 1.3201 0.2446  0.2387  -0.0235 345 MET B N   
6700 C CA  . MET B 318 ? 1.4787 1.0755 1.2108 0.2170  0.2278  -0.0155 345 MET B CA  
6701 C C   . MET B 318 ? 1.5480 1.1839 1.2820 0.2021  0.2236  -0.0166 345 MET B C   
6702 O O   . MET B 318 ? 1.5554 1.2315 1.2942 0.2057  0.2248  -0.0193 345 MET B O   
6703 C CB  . MET B 318 ? 1.4909 1.0956 1.2414 0.2173  0.2234  -0.0082 345 MET B CB  
6704 C CG  . MET B 318 ? 1.3461 0.9579 1.1141 0.1919  0.2129  0.0000  345 MET B CG  
6705 S SD  . MET B 318 ? 1.6976 1.3292 1.4858 0.1904  0.2096  0.0060  345 MET B SD  
6706 C CE  . MET B 318 ? 1.3990 1.0526 1.1899 0.1629  0.2033  0.0110  345 MET B CE  
6707 N N   . ILE B 319 ? 1.5099 1.1361 1.2387 0.1843  0.2196  -0.0161 346 ILE B N   
6708 C CA  . ILE B 319 ? 1.5915 1.2469 1.3158 0.1678  0.2165  -0.0162 346 ILE B CA  
6709 C C   . ILE B 319 ? 1.4998 1.1630 1.2344 0.1492  0.2086  -0.0057 346 ILE B C   
6710 O O   . ILE B 319 ? 1.4773 1.1161 1.2207 0.1441  0.2013  0.0022  346 ILE B O   
6711 C CB  . ILE B 319 ? 1.5544 1.1948 1.2654 0.1574  0.2148  -0.0192 346 ILE B CB  
6712 C CG1 . ILE B 319 ? 1.5284 1.1434 1.2280 0.1733  0.2239  -0.0291 346 ILE B CG1 
6713 C CG2 . ILE B 319 ? 1.4538 1.1248 1.1532 0.1458  0.2158  -0.0224 346 ILE B CG2 
6714 C CD1 . ILE B 319 ? 1.4414 1.0445 1.1288 0.1615  0.2236  -0.0350 346 ILE B CD1 
6715 N N   . ASN B 320 ? 1.4467 1.1431 1.1780 0.1383  0.2112  -0.0071 347 ASN B N   
6716 C CA  . ASN B 320 ? 1.4656 1.1625 1.1991 0.1185  0.2070  0.0020  347 ASN B CA  
6717 C C   . ASN B 320 ? 1.4058 1.1306 1.1237 0.0990  0.2127  -0.0018 347 ASN B C   
6718 O O   . ASN B 320 ? 1.4323 1.1968 1.1505 0.1041  0.2213  -0.0146 347 ASN B O   
6719 C CB  . ASN B 320 ? 1.4756 1.1824 1.2272 0.1253  0.2088  0.0028  347 ASN B CB  
6720 C CG  . ASN B 320 ? 1.4737 1.1802 1.2242 0.1031  0.2078  0.0099  347 ASN B CG  
6721 O OD1 . ASN B 320 ? 1.5360 1.2767 1.2868 0.0930  0.2158  0.0031  347 ASN B OD1 
6722 N ND2 . ASN B 320 ? 1.4582 1.1264 1.2052 0.0954  0.1987  0.0221  347 ASN B ND2 
6723 N N   . LEU B 321 ? 1.5304 1.2340 1.2318 0.0777  0.2084  0.0082  348 LEU B N   
6724 C CA  . LEU B 321 ? 1.4864 1.2076 1.1669 0.0538  0.2162  0.0057  348 LEU B CA  
6725 C C   . LEU B 321 ? 1.5971 1.3333 1.2836 0.0406  0.2235  0.0043  348 LEU B C   
6726 O O   . LEU B 321 ? 1.5847 1.2935 1.2778 0.0405  0.2183  0.0142  348 LEU B O   
6727 C CB  . LEU B 321 ? 1.5103 1.1940 1.1615 0.0382  0.2097  0.0181  348 LEU B CB  
6728 C CG  . LEU B 321 ? 1.5626 1.2602 1.1875 0.0230  0.2160  0.0127  348 LEU B CG  
6729 C CD1 . LEU B 321 ? 1.5117 1.1679 1.1066 0.0158  0.2062  0.0263  348 LEU B CD1 
6730 C CD2 . LEU B 321 ? 1.6923 1.4178 1.3048 -0.0016 0.2309  0.0047  348 LEU B CD2 
6731 N N   . ARG B 322 ? 1.6079 1.3915 1.2928 0.0288  0.2361  -0.0104 349 ARG B N   
6732 C CA  . ARG B 322 ? 1.6562 1.4674 1.3514 0.0169  0.2450  -0.0176 349 ARG B CA  
6733 C C   . ARG B 322 ? 1.7211 1.4893 1.3953 -0.0099 0.2468  -0.0050 349 ARG B C   
6734 O O   . ARG B 322 ? 1.7789 1.5467 1.4650 -0.0138 0.2491  -0.0046 349 ARG B O   
6735 C CB  . ARG B 322 ? 1.7344 1.6117 1.4296 0.0056  0.2590  -0.0395 349 ARG B CB  
6736 C CG  . ARG B 322 ? 1.8403 1.7614 1.5505 -0.0055 0.2690  -0.0527 349 ARG B CG  
6737 C CD  . ARG B 322 ? 1.9121 1.9135 1.6283 -0.0115 0.2818  -0.0795 349 ARG B CD  
6738 N NE  . ARG B 322 ? 2.1459 2.1513 1.8331 -0.0460 0.2934  -0.0856 349 ARG B NE  
6739 C CZ  . ARG B 322 ? 2.0931 2.1214 1.7723 -0.0419 0.2951  -0.0943 349 ARG B CZ  
6740 N NH1 . ARG B 322 ? 2.0608 2.1083 1.7572 -0.0041 0.2865  -0.0985 349 ARG B NH1 
6741 N NH2 . ARG B 322 ? 1.9257 1.9541 1.5753 -0.0772 0.3070  -0.0993 349 ARG B NH2 
6742 N N   . ARG B 323 ? 1.7667 1.4951 1.4063 -0.0269 0.2460  0.0055  350 ARG B N   
6743 C CA  . ARG B 323 ? 1.7880 1.4656 1.3978 -0.0494 0.2487  0.0186  350 ARG B CA  
6744 C C   . ARG B 323 ? 1.7674 1.3984 1.3869 -0.0307 0.2338  0.0350  350 ARG B C   
6745 O O   . ARG B 323 ? 1.8111 1.4026 1.4124 -0.0436 0.2361  0.0442  350 ARG B O   
6746 C CB  . ARG B 323 ? 1.7402 1.3830 1.3030 -0.0687 0.2515  0.0266  350 ARG B CB  
6747 C CG  . ARG B 323 ? 1.7362 1.3423 1.2901 -0.0477 0.2338  0.0411  350 ARG B CG  
6748 C CD  . ARG B 323 ? 1.7916 1.3506 1.2908 -0.0661 0.2356  0.0531  350 ARG B CD  
6749 N NE  . ARG B 323 ? 1.7911 1.3159 1.2804 -0.0445 0.2167  0.0669  350 ARG B NE  
6750 C CZ  . ARG B 323 ? 1.7092 1.2509 1.1990 -0.0351 0.2103  0.0635  350 ARG B CZ  
6751 N NH1 . ARG B 323 ? 1.8122 1.4005 1.3110 -0.0433 0.2207  0.0479  350 ARG B NH1 
6752 N NH2 . ARG B 323 ? 1.6386 1.1533 1.1199 -0.0167 0.1932  0.0741  350 ARG B NH2 
6753 N N   . ARG B 324 ? 1.6792 1.3129 1.3248 -0.0018 0.2201  0.0372  351 ARG B N   
6754 C CA  . ARG B 324 ? 1.6578 1.2580 1.3181 0.0158  0.2068  0.0484  351 ARG B CA  
6755 C C   . ARG B 324 ? 1.6174 1.2442 1.3128 0.0250  0.2099  0.0410  351 ARG B C   
6756 O O   . ARG B 324 ? 1.5209 1.1607 1.2436 0.0475  0.2040  0.0376  351 ARG B O   
6757 C CB  . ARG B 324 ? 1.5842 1.1749 1.2522 0.0373  0.1930  0.0516  351 ARG B CB  
6758 C CG  . ARG B 324 ? 1.5115 1.0777 1.1449 0.0309  0.1877  0.0590  351 ARG B CG  
6759 C CD  . ARG B 324 ? 1.6646 1.2207 1.3080 0.0511  0.1728  0.0611  351 ARG B CD  
6760 N NE  . ARG B 324 ? 1.7879 1.3216 1.3974 0.0478  0.1652  0.0686  351 ARG B NE  
6761 C CZ  . ARG B 324 ? 1.7452 1.2947 1.3464 0.0478  0.1650  0.0627  351 ARG B CZ  
6762 N NH1 . ARG B 324 ? 1.8926 1.4766 1.5155 0.0520  0.1724  0.0492  351 ARG B NH1 
6763 N NH2 . ARG B 324 ? 1.6610 1.1894 1.2285 0.0455  0.1572  0.0704  351 ARG B NH2 
6764 N N   . GLN B 325 ? 1.6278 1.2601 1.3182 0.0054  0.2209  0.0379  352 GLN B N   
6765 C CA  . GLN B 325 ? 1.5606 1.2262 1.2818 0.0113  0.2254  0.0287  352 GLN B CA  
6766 C C   . GLN B 325 ? 1.5771 1.2138 1.3182 0.0292  0.2139  0.0382  352 GLN B C   
6767 O O   . GLN B 325 ? 1.6821 1.3442 1.4520 0.0460  0.2127  0.0321  352 GLN B O   
6768 C CB  . GLN B 325 ? 1.7474 1.4274 1.4565 -0.0186 0.2414  0.0206  352 GLN B CB  
6769 C CG  . GLN B 325 ? 1.8436 1.5626 1.5830 -0.0147 0.2463  0.0096  352 GLN B CG  
6770 C CD  . GLN B 325 ? 1.9642 1.7053 1.6914 -0.0486 0.2645  -0.0030 352 GLN B CD  
6771 O OE1 . GLN B 325 ? 2.0178 1.7352 1.7095 -0.0771 0.2748  -0.0020 352 GLN B OE1 
6772 N NE2 . GLN B 325 ? 2.0588 1.8449 1.8125 -0.0470 0.2698  -0.0161 352 GLN B NE2 
6773 N N   . ASP B 326 ? 1.5133 1.0979 1.2374 0.0273  0.2054  0.0522  353 ASP B N   
6774 C CA  . ASP B 326 ? 1.4877 1.0494 1.2316 0.0431  0.1949  0.0588  353 ASP B CA  
6775 C C   . ASP B 326 ? 1.3904 0.9562 1.1548 0.0673  0.1836  0.0582  353 ASP B C   
6776 O O   . ASP B 326 ? 1.4015 0.9685 1.1912 0.0807  0.1794  0.0569  353 ASP B O   
6777 C CB  . ASP B 326 ? 1.3449 0.8522 1.0620 0.0367  0.1891  0.0722  353 ASP B CB  
6778 C CG  . ASP B 326 ? 1.7890 1.2815 1.4841 0.0113  0.2033  0.0721  353 ASP B CG  
6779 O OD1 . ASP B 326 ? 1.7967 1.3262 1.5115 0.0019  0.2145  0.0607  353 ASP B OD1 
6780 O OD2 . ASP B 326 ? 1.8137 1.2568 1.4690 0.0009  0.2040  0.0826  353 ASP B OD2 
6781 N N   . ARG B 327 ? 1.4708 1.0377 1.2228 0.0709  0.1802  0.0578  354 ARG B N   
6782 C CA  . ARG B 327 ? 1.3474 0.9214 1.1163 0.0896  0.1742  0.0532  354 ARG B CA  
6783 C C   . ARG B 327 ? 1.4916 1.0984 1.2802 0.1003  0.1828  0.0427  354 ARG B C   
6784 O O   . ARG B 327 ? 1.4495 1.0525 1.2536 0.1160  0.1806  0.0396  354 ARG B O   
6785 C CB  . ARG B 327 ? 1.3891 0.9607 1.1386 0.0888  0.1708  0.0529  354 ARG B CB  
6786 C CG  . ARG B 327 ? 1.4101 0.9504 1.1421 0.0888  0.1582  0.0620  354 ARG B CG  
6787 C CD  . ARG B 327 ? 1.3090 0.8546 1.0271 0.0905  0.1549  0.0587  354 ARG B CD  
6788 N NE  . ARG B 327 ? 1.6885 1.2091 1.3826 0.0908  0.1427  0.0674  354 ARG B NE  
6789 C CZ  . ARG B 327 ? 1.7265 1.2495 1.4033 0.0914  0.1377  0.0660  354 ARG B CZ  
6790 N NH1 . ARG B 327 ? 1.5809 1.1274 1.2621 0.0899  0.1447  0.0559  354 ARG B NH1 
6791 N NH2 . ARG B 327 ? 1.9247 1.4258 1.5770 0.0954  0.1251  0.0744  354 ARG B NH2 
6792 N N   . ARG B 328 ? 1.3841 1.0232 1.1690 0.0924  0.1933  0.0359  355 ARG B N   
6793 C CA  . ARG B 328 ? 1.3703 1.0450 1.1696 0.1077  0.2003  0.0251  355 ARG B CA  
6794 C C   . ARG B 328 ? 1.3845 1.0615 1.2044 0.1162  0.2004  0.0252  355 ARG B C   
6795 O O   . ARG B 328 ? 1.2510 0.9279 1.0811 0.1368  0.2003  0.0223  355 ARG B O   
6796 C CB  . ARG B 328 ? 1.2684 0.9871 1.0595 0.0972  0.2107  0.0145  355 ARG B CB  
6797 C CG  . ARG B 328 ? 1.2608 1.0225 1.0629 0.1188  0.2165  0.0015  355 ARG B CG  
6798 C CD  . ARG B 328 ? 1.2323 1.0449 1.0266 0.1092  0.2259  -0.0124 355 ARG B CD  
6799 N NE  . ARG B 328 ? 1.4466 1.2792 1.2393 0.0809  0.2332  -0.0163 355 ARG B NE  
6800 C CZ  . ARG B 328 ? 1.5244 1.3448 1.2962 0.0514  0.2380  -0.0140 355 ARG B CZ  
6801 N NH1 . ARG B 328 ? 1.4062 1.1988 1.1585 0.0475  0.2343  -0.0071 355 ARG B NH1 
6802 N NH2 . ARG B 328 ? 1.5924 1.4268 1.3591 0.0240  0.2479  -0.0194 355 ARG B NH2 
6803 N N   . GLU B 329 ? 1.3219 0.9970 1.1444 0.1000  0.2018  0.0282  356 GLU B N   
6804 C CA  . GLU B 329 ? 1.4126 1.0927 1.2549 0.1064  0.2023  0.0274  356 GLU B CA  
6805 C C   . GLU B 329 ? 1.4111 1.0546 1.2642 0.1188  0.1932  0.0347  356 GLU B C   
6806 O O   . GLU B 329 ? 1.4329 1.0806 1.3009 0.1328  0.1940  0.0323  356 GLU B O   
6807 C CB  . GLU B 329 ? 1.5175 1.1988 1.3574 0.0832  0.2073  0.0280  356 GLU B CB  
6808 C CG  . GLU B 329 ? 1.5895 1.3109 1.4185 0.0648  0.2193  0.0171  356 GLU B CG  
6809 C CD  . GLU B 329 ? 1.8100 1.5255 1.6317 0.0375  0.2275  0.0161  356 GLU B CD  
6810 O OE1 . GLU B 329 ? 1.6417 1.3265 1.4707 0.0377  0.2232  0.0236  356 GLU B OE1 
6811 O OE2 . GLU B 329 ? 1.7285 1.4693 1.5358 0.0145  0.2396  0.0064  356 GLU B OE2 
6812 N N   . ARG B 330 ? 1.3928 1.0029 1.2370 0.1141  0.1849  0.0422  357 ARG B N   
6813 C CA  . ARG B 330 ? 1.2944 0.8780 1.1502 0.1238  0.1766  0.0452  357 ARG B CA  
6814 C C   . ARG B 330 ? 1.3940 0.9793 1.2538 0.1400  0.1794  0.0389  357 ARG B C   
6815 O O   . ARG B 330 ? 1.3780 0.9537 1.2504 0.1489  0.1799  0.0369  357 ARG B O   
6816 C CB  . ARG B 330 ? 1.2528 0.8097 1.0966 0.1181  0.1662  0.0517  357 ARG B CB  
6817 C CG  . ARG B 330 ? 1.3767 0.9140 1.2353 0.1251  0.1568  0.0524  357 ARG B CG  
6818 C CD  . ARG B 330 ? 1.2985 0.8203 1.1457 0.1263  0.1453  0.0547  357 ARG B CD  
6819 N NE  . ARG B 330 ? 1.6321 1.1610 1.4797 0.1316  0.1458  0.0467  357 ARG B NE  
6820 C CZ  . ARG B 330 ? 1.6185 1.1461 1.4815 0.1373  0.1443  0.0381  357 ARG B CZ  
6821 N NH1 . ARG B 330 ? 1.5645 1.0874 1.4459 0.1399  0.1409  0.0363  357 ARG B NH1 
6822 N NH2 . ARG B 330 ? 1.3953 0.9258 1.2534 0.1385  0.1479  0.0296  357 ARG B NH2 
6823 N N   . MET B 331 ? 1.3937 0.9871 1.2393 0.1432  0.1826  0.0351  358 MET B N   
6824 C CA  . MET B 331 ? 1.3548 0.9412 1.1967 0.1585  0.1876  0.0288  358 MET B CA  
6825 C C   . MET B 331 ? 1.4207 1.0213 1.2652 0.1748  0.1960  0.0248  358 MET B C   
6826 O O   . MET B 331 ? 1.3532 0.9336 1.1950 0.1880  0.2004  0.0223  358 MET B O   
6827 C CB  . MET B 331 ? 1.4130 1.0047 1.2372 0.1583  0.1897  0.0250  358 MET B CB  
6828 C CG  . MET B 331 ? 1.4336 1.0096 1.2515 0.1468  0.1812  0.0274  358 MET B CG  
6829 S SD  . MET B 331 ? 1.4943 1.0430 1.3191 0.1501  0.1787  0.0218  358 MET B SD  
6830 C CE  . MET B 331 ? 1.3858 0.9256 1.1958 0.1644  0.1932  0.0123  358 MET B CE  
6831 N N   . LEU B 332 ? 1.4724 1.1080 1.3192 0.1739  0.1992  0.0230  359 LEU B N   
6832 C CA  . LEU B 332 ? 1.3815 1.0387 1.2304 0.1928  0.2054  0.0180  359 LEU B CA  
6833 C C   . LEU B 332 ? 1.4134 1.0564 1.2764 0.1949  0.2040  0.0216  359 LEU B C   
6834 O O   . LEU B 332 ? 1.3516 0.9885 1.2099 0.2147  0.2086  0.0197  359 LEU B O   
6835 C CB  . LEU B 332 ? 1.3400 1.0487 1.1908 0.1887  0.2090  0.0112  359 LEU B CB  
6836 C CG  . LEU B 332 ? 1.2579 0.9890 1.0945 0.1888  0.2122  0.0046  359 LEU B CG  
6837 C CD1 . LEU B 332 ? 1.4127 1.2007 1.2536 0.1789  0.2173  -0.0054 359 LEU B CD1 
6838 C CD2 . LEU B 332 ? 1.6938 1.4172 1.5156 0.2175  0.2161  -0.0001 359 LEU B CD2 
6839 N N   . ARG B 333 ? 1.2448 0.8793 1.1215 0.1761  0.1983  0.0268  360 ARG B N   
6840 C CA  . ARG B 333 ? 1.3660 0.9862 1.2573 0.1770  0.1968  0.0293  360 ARG B CA  
6841 C C   . ARG B 333 ? 1.4744 1.0565 1.3633 0.1832  0.1962  0.0297  360 ARG B C   
6842 O O   . ARG B 333 ? 1.3798 0.9500 1.2725 0.1914  0.1997  0.0288  360 ARG B O   
6843 C CB  . ARG B 333 ? 1.2027 0.8202 1.1063 0.1570  0.1911  0.0338  360 ARG B CB  
6844 C CG  . ARG B 333 ? 1.3033 0.9541 1.2077 0.1451  0.1954  0.0312  360 ARG B CG  
6845 C CD  . ARG B 333 ? 1.4548 1.0913 1.3675 0.1278  0.1925  0.0355  360 ARG B CD  
6846 N NE  . ARG B 333 ? 1.5943 1.2476 1.4978 0.1079  0.1982  0.0334  360 ARG B NE  
6847 C CZ  . ARG B 333 ? 1.7516 1.3829 1.6371 0.0927  0.1965  0.0388  360 ARG B CZ  
6848 N NH1 . ARG B 333 ? 1.5345 1.1322 1.4120 0.0976  0.1872  0.0464  360 ARG B NH1 
6849 N NH2 . ARG B 333 ? 1.8630 1.5064 1.7354 0.0715  0.2053  0.0354  360 ARG B NH2 
6850 N N   . ALA B 334 ? 1.4300 0.9944 1.3111 0.1776  0.1932  0.0293  361 ALA B N   
6851 C CA  . ALA B 334 ? 1.3338 0.8669 1.2124 0.1787  0.1947  0.0256  361 ALA B CA  
6852 C C   . ALA B 334 ? 1.4318 0.9481 1.2893 0.1954  0.2065  0.0212  361 ALA B C   
6853 O O   . ALA B 334 ? 1.4069 0.8968 1.2598 0.1993  0.2130  0.0185  361 ALA B O   
6854 C CB  . ALA B 334 ? 1.3674 0.8930 1.2438 0.1674  0.1878  0.0241  361 ALA B CB  
6855 N N   . LEU B 335 ? 1.5060 1.0341 1.3466 0.2059  0.2103  0.0199  362 LEU B N   
6856 C CA  . LEU B 335 ? 1.5219 1.0293 1.3359 0.2268  0.2218  0.0162  362 LEU B CA  
6857 C C   . LEU B 335 ? 1.5525 1.0637 1.3628 0.2454  0.2263  0.0183  362 LEU B C   
6858 O O   . LEU B 335 ? 1.5696 1.0442 1.3572 0.2595  0.2360  0.0173  362 LEU B O   
6859 C CB  . LEU B 335 ? 1.4546 0.9802 1.2531 0.2365  0.2237  0.0133  362 LEU B CB  
6860 C CG  . LEU B 335 ? 1.4738 0.9903 1.2685 0.2213  0.2214  0.0103  362 LEU B CG  
6861 C CD1 . LEU B 335 ? 1.5384 1.0802 1.3207 0.2292  0.2228  0.0070  362 LEU B CD1 
6862 C CD2 . LEU B 335 ? 1.5076 0.9769 1.2852 0.2199  0.2302  0.0047  362 LEU B CD2 
6863 N N   . GLN B 336 ? 1.4943 1.0477 1.3233 0.2446  0.2204  0.0203  363 GLN B N   
6864 C CA  . GLN B 336 ? 1.4013 0.9665 1.2299 0.2612  0.2231  0.0210  363 GLN B CA  
6865 C C   . GLN B 336 ? 1.4184 0.9487 1.2517 0.2547  0.2252  0.0237  363 GLN B C   
6866 O O   . GLN B 336 ? 1.4715 0.9788 1.2850 0.2728  0.2328  0.0243  363 GLN B O   
6867 C CB  . GLN B 336 ? 1.4314 1.0519 1.2825 0.2538  0.2173  0.0198  363 GLN B CB  
6868 C CG  . GLN B 336 ? 1.5939 1.2314 1.4542 0.2618  0.2179  0.0198  363 GLN B CG  
6869 C CD  . GLN B 336 ? 1.6285 1.3166 1.5127 0.2455  0.2139  0.0164  363 GLN B CD  
6870 O OE1 . GLN B 336 ? 1.5245 1.2098 1.4239 0.2196  0.2097  0.0188  363 GLN B OE1 
6871 N NE2 . GLN B 336 ? 1.6192 1.3534 1.5036 0.2611  0.2159  0.0095  363 GLN B NE2 
6872 N N   . ALA B 337 ? 1.4108 0.9362 1.2675 0.2302  0.2187  0.0248  364 ALA B N   
6873 C CA  . ALA B 337 ? 1.3489 0.8490 1.2145 0.2219  0.2203  0.0246  364 ALA B CA  
6874 C C   . ALA B 337 ? 1.4451 0.8962 1.2849 0.2254  0.2315  0.0206  364 ALA B C   
6875 O O   . ALA B 337 ? 1.4137 0.8398 1.2467 0.2267  0.2386  0.0197  364 ALA B O   
6876 C CB  . ALA B 337 ? 1.1665 0.6742 1.0604 0.1987  0.2100  0.0247  364 ALA B CB  
6877 N N   . GLN B 338 ? 1.4905 0.9253 1.3133 0.2246  0.2349  0.0172  365 GLN B N   
6878 C CA  . GLN B 338 ? 1.2777 0.6622 1.0706 0.2248  0.2488  0.0113  365 GLN B CA  
6879 C C   . GLN B 338 ? 1.4699 0.8268 1.2209 0.2531  0.2610  0.0136  365 GLN B C   
6880 O O   . GLN B 338 ? 1.6411 0.9468 1.3573 0.2551  0.2755  0.0090  365 GLN B O   
6881 C CB  . GLN B 338 ? 1.4296 0.8094 1.2227 0.2093  0.2476  0.0044  365 GLN B CB  
6882 C CG  . GLN B 338 ? 1.4113 0.8117 1.2385 0.1854  0.2360  0.0004  365 GLN B CG  
6883 C CD  . GLN B 338 ? 1.4527 0.8570 1.2795 0.1733  0.2326  -0.0064 365 GLN B CD  
6884 O OE1 . GLN B 338 ? 1.5333 0.9234 1.3604 0.1575  0.2370  -0.0181 365 GLN B OE1 
6885 N NE2 . GLN B 338 ? 1.2775 0.7048 1.1033 0.1793  0.2255  -0.0011 365 GLN B NE2 
6886 N N   . GLU B 339 ? 1.5491 0.9388 1.3004 0.2755  0.2562  0.0192  366 GLU B N   
6887 C CA  . GLU B 339 ? 1.5380 0.9109 1.2491 0.3098  0.2648  0.0210  366 GLU B CA  
6888 C C   . GLU B 339 ? 1.4888 0.8386 1.1718 0.3178  0.2716  0.0169  366 GLU B C   
6889 O O   . GLU B 339 ? 1.5978 0.8895 1.2363 0.3314  0.2863  0.0155  366 GLU B O   
6890 C CB  . GLU B 339 ? 1.5560 0.8767 1.2344 0.3216  0.2775  0.0234  366 GLU B CB  
6891 C CG  . GLU B 339 ? 1.5903 0.9374 1.2930 0.3190  0.2713  0.0272  366 GLU B CG  
6892 C CD  . GLU B 339 ? 1.8447 1.1400 1.5083 0.3344  0.2844  0.0304  366 GLU B CD  
6893 O OE1 . GLU B 339 ? 2.0436 1.2804 1.6855 0.3184  0.2977  0.0272  366 GLU B OE1 
6894 O OE2 . GLU B 339 ? 1.9401 1.2536 1.5918 0.3621  0.2822  0.0349  366 GLU B OE2 
6895 N N   . ILE B 340 ? 1.5786 0.9712 1.2852 0.3080  0.2618  0.0146  367 ILE B N   
6896 C CA  . ILE B 340 ? 1.6676 1.0496 1.3542 0.3128  0.2661  0.0098  367 ILE B CA  
6897 C C   . ILE B 340 ? 1.6312 1.0744 1.3304 0.3261  0.2570  0.0089  367 ILE B C   
6898 O O   . ILE B 340 ? 1.5220 1.0152 1.2566 0.3102  0.2457  0.0103  367 ILE B O   
6899 C CB  . ILE B 340 ? 1.5499 0.9207 1.2514 0.2801  0.2646  0.0050  367 ILE B CB  
6900 C CG1 . ILE B 340 ? 1.5250 0.8459 1.2182 0.2630  0.2744  0.0015  367 ILE B CG1 
6901 C CG2 . ILE B 340 ? 1.5024 0.8624 1.1818 0.2847  0.2700  -0.0009 367 ILE B CG2 
6902 C CD1 . ILE B 340 ? 1.5310 0.8517 1.2424 0.2316  0.2716  -0.0065 367 ILE B CD1 
6903 N N   . GLU B 341 ? 1.6231 1.0611 1.2911 0.3548  0.2632  0.0052  368 GLU B N   
6904 C CA  . GLU B 341 ? 1.7058 1.2056 1.3824 0.3699  0.2566  0.0005  368 GLU B CA  
6905 C C   . GLU B 341 ? 1.7863 1.2875 1.4588 0.3598  0.2577  -0.0052 368 GLU B C   
6906 O O   . GLU B 341 ? 1.7504 1.1972 1.3964 0.3588  0.2672  -0.0070 368 GLU B O   
6907 C CB  . GLU B 341 ? 1.7413 1.2451 1.3861 0.4157  0.2611  -0.0016 368 GLU B CB  
6908 C CG  . GLU B 341 ? 1.8861 1.4733 1.5490 0.4311  0.2527  -0.0095 368 GLU B CG  
6909 C CD  . GLU B 341 ? 2.0288 1.6253 1.6597 0.4816  0.2552  -0.0130 368 GLU B CD  
6910 O OE1 . GLU B 341 ? 1.9211 1.4501 1.5114 0.5045  0.2640  -0.0066 368 GLU B OE1 
6911 O OE2 . GLU B 341 ? 2.1009 1.7722 1.7443 0.4986  0.2491  -0.0232 368 GLU B OE2 
6912 N N   . CYS B 342 ? 1.8436 1.4067 1.5405 0.3499  0.2493  -0.0093 369 CYS B N   
6913 C CA  . CYS B 342 ? 1.8577 1.4277 1.5541 0.3358  0.2492  -0.0143 369 CYS B CA  
6914 C C   . CYS B 342 ? 1.8134 1.4449 1.5113 0.3512  0.2473  -0.0236 369 CYS B C   
6915 O O   . CYS B 342 ? 2.0189 1.7021 1.7301 0.3618  0.2435  -0.0269 369 CYS B O   
6916 C CB  . CYS B 342 ? 1.8505 1.4280 1.5755 0.2957  0.2409  -0.0099 369 CYS B CB  
6917 S SG  . CYS B 342 ? 1.5182 1.1657 1.2764 0.2759  0.2308  -0.0093 369 CYS B SG  
6918 N N   . ARG B 343 ? 1.6510 1.2805 1.3356 0.3512  0.2508  -0.0301 370 ARG B N   
6919 C CA  . ARG B 343 ? 1.5992 1.2916 1.2901 0.3551  0.2489  -0.0408 370 ARG B CA  
6920 C C   . ARG B 343 ? 1.6562 1.3681 1.3687 0.3139  0.2434  -0.0391 370 ARG B C   
6921 O O   . ARG B 343 ? 1.5932 1.2669 1.2994 0.2966  0.2440  -0.0356 370 ARG B O   
6922 C CB  . ARG B 343 ? 1.5999 1.2780 1.2590 0.3842  0.2569  -0.0501 370 ARG B CB  
6923 C CG  . ARG B 343 ? 1.4459 1.1953 1.1119 0.3902  0.2556  -0.0643 370 ARG B CG  
6924 C CD  . ARG B 343 ? 1.7115 1.4436 1.3449 0.4208  0.2635  -0.0741 370 ARG B CD  
6925 N NE  . ARG B 343 ? 1.8532 1.6624 1.4941 0.4325  0.2623  -0.0906 370 ARG B NE  
6926 C CZ  . ARG B 343 ? 1.8910 1.7310 1.5409 0.4083  0.2626  -0.0984 370 ARG B CZ  
6927 N NH1 . ARG B 343 ? 1.8927 1.6935 1.5441 0.3740  0.2629  -0.0904 370 ARG B NH1 
6928 N NH2 . ARG B 343 ? 1.9100 1.8254 1.5669 0.4192  0.2627  -0.1159 370 ARG B NH2 
6929 N N   . LEU B 344 ? 1.4756 1.2451 1.2102 0.2980  0.2389  -0.0421 371 LEU B N   
6930 C CA  . LEU B 344 ? 1.4575 1.2391 1.2047 0.2599  0.2349  -0.0391 371 LEU B CA  
6931 C C   . LEU B 344 ? 1.4965 1.3008 1.2320 0.2572  0.2385  -0.0492 371 LEU B C   
6932 O O   . LEU B 344 ? 1.5574 1.4124 1.2909 0.2734  0.2425  -0.0630 371 LEU B O   
6933 C CB  . LEU B 344 ? 1.5156 1.3429 1.2834 0.2413  0.2325  -0.0401 371 LEU B CB  
6934 C CG  . LEU B 344 ? 1.5475 1.3652 1.3221 0.2021  0.2287  -0.0317 371 LEU B CG  
6935 C CD1 . LEU B 344 ? 1.6228 1.3823 1.4006 0.1949  0.2222  -0.0170 371 LEU B CD1 
6936 C CD2 . LEU B 344 ? 1.5701 1.4337 1.3580 0.1832  0.2308  -0.0366 371 LEU B CD2 
6937 N N   . VAL B 345 ? 1.4763 1.2475 1.2044 0.2378  0.2370  -0.0440 372 VAL B N   
6938 C CA  . VAL B 345 ? 1.5875 1.3760 1.3037 0.2312  0.2402  -0.0527 372 VAL B CA  
6939 C C   . VAL B 345 ? 1.6368 1.4428 1.3589 0.1943  0.2364  -0.0484 372 VAL B C   
6940 O O   . VAL B 345 ? 1.5887 1.3603 1.3131 0.1749  0.2299  -0.0357 372 VAL B O   
6941 C CB  . VAL B 345 ? 1.4874 1.2254 1.1856 0.2374  0.2427  -0.0520 372 VAL B CB  
6942 C CG1 . VAL B 345 ? 1.3550 1.1129 1.0416 0.2285  0.2458  -0.0612 372 VAL B CG1 
6943 C CG2 . VAL B 345 ? 1.4739 1.1831 1.1565 0.2734  0.2497  -0.0559 372 VAL B CG2 
6944 N N   . GLU B 346 ? 1.6071 1.4657 1.3283 0.1854  0.2412  -0.0598 373 GLU B N   
6945 C CA  . GLU B 346 ? 1.4572 1.3271 1.1748 0.1489  0.2410  -0.0566 373 GLU B CA  
6946 C C   . GLU B 346 ? 1.4366 1.2733 1.1372 0.1357  0.2380  -0.0509 373 GLU B C   
6947 O O   . GLU B 346 ? 1.6176 1.4617 1.3085 0.1467  0.2419  -0.0604 373 GLU B O   
6948 C CB  . GLU B 346 ? 1.5814 1.5190 1.3004 0.1404  0.2497  -0.0741 373 GLU B CB  
6949 C CG  . GLU B 346 ? 1.7528 1.7329 1.4895 0.1455  0.2525  -0.0816 373 GLU B CG  
6950 C CD  . GLU B 346 ? 1.9020 1.9095 1.6381 0.1066  0.2588  -0.0850 373 GLU B CD  
6951 O OE1 . GLU B 346 ? 1.9855 1.9923 1.7044 0.0796  0.2634  -0.0861 373 GLU B OE1 
6952 O OE2 . GLU B 346 ? 1.8929 1.9193 1.6425 0.1017  0.2604  -0.0869 373 GLU B OE2 
6953 N N   . ALA B 347 ? 1.5124 1.3137 1.2080 0.1141  0.2310  -0.0361 374 ALA B N   
6954 C CA  . ALA B 347 ? 1.5399 1.3121 1.2189 0.1034  0.2261  -0.0306 374 ALA B CA  
6955 C C   . ALA B 347 ? 1.5130 1.3117 1.1731 0.0829  0.2319  -0.0369 374 ALA B C   
6956 O O   . ALA B 347 ? 1.5773 1.4027 1.2336 0.0646  0.2380  -0.0398 374 ALA B O   
6957 C CB  . ALA B 347 ? 1.4651 1.1958 1.1422 0.0913  0.2154  -0.0139 374 ALA B CB  
6958 N N   . VAL B 348 ? 1.5278 1.3192 1.1747 0.0836  0.2314  -0.0407 375 VAL B N   
6959 C CA  . VAL B 348 ? 1.6413 1.4547 1.2676 0.0636  0.2369  -0.0467 375 VAL B CA  
6960 C C   . VAL B 348 ? 1.6980 1.4819 1.3027 0.0374  0.2311  -0.0310 375 VAL B C   
6961 O O   . VAL B 348 ? 1.6650 1.4120 1.2619 0.0387  0.2203  -0.0198 375 VAL B O   
6962 C CB  . VAL B 348 ? 1.5857 1.3988 1.2036 0.0733  0.2383  -0.0560 375 VAL B CB  
6963 C CG1 . VAL B 348 ? 1.5742 1.4042 1.1681 0.0496  0.2425  -0.0598 375 VAL B CG1 
6964 C CG2 . VAL B 348 ? 1.5752 1.4144 1.2057 0.1012  0.2462  -0.0723 375 VAL B CG2 
6965 N N   . ASP B 349 ? 1.6674 1.4670 1.2591 0.0141  0.2388  -0.0312 376 ASP B N   
6966 C CA  . ASP B 349 ? 1.8086 1.5719 1.3690 -0.0105 0.2361  -0.0159 376 ASP B CA  
6967 C C   . ASP B 349 ? 1.9652 1.7223 1.4962 -0.0212 0.2355  -0.0159 376 ASP B C   
6968 O O   . ASP B 349 ? 1.8481 1.6356 1.3646 -0.0381 0.2473  -0.0274 376 ASP B O   
6969 C CB  . ASP B 349 ? 1.8545 1.6325 1.4043 -0.0359 0.2489  -0.0189 376 ASP B CB  
6970 C CG  . ASP B 349 ? 1.9736 1.6970 1.4917 -0.0545 0.2458  0.0004  376 ASP B CG  
6971 O OD1 . ASP B 349 ? 1.9971 1.6806 1.4875 -0.0549 0.2365  0.0139  376 ASP B OD1 
6972 O OD2 . ASP B 349 ? 2.0055 1.7255 1.5243 -0.0671 0.2529  0.0015  376 ASP B OD2 
6973 N N   . GLY B 350 ? 2.0679 1.7898 1.5904 -0.0119 0.2218  -0.0046 377 GLY B N   
6974 C CA  . GLY B 350 ? 2.1640 1.8834 1.6609 -0.0186 0.2197  -0.0057 377 GLY B CA  
6975 C C   . GLY B 350 ? 2.3007 2.0026 1.7516 -0.0460 0.2248  0.0028  377 GLY B C   
6976 O O   . GLY B 350 ? 2.3020 2.0166 1.7305 -0.0578 0.2298  -0.0033 377 GLY B O   
6977 N N   . LYS B 351 ? 2.1892 1.8579 1.6216 -0.0572 0.2251  0.0167  378 LYS B N   
6978 C CA  . LYS B 351 ? 2.2389 1.8775 1.6178 -0.0843 0.2324  0.0263  378 LYS B CA  
6979 C C   . LYS B 351 ? 2.1447 1.8186 1.5147 -0.1131 0.2544  0.0108  378 LYS B C   
6980 O O   . LYS B 351 ? 2.1025 1.7616 1.4264 -0.1388 0.2642  0.0128  378 LYS B O   
6981 C CB  . LYS B 351 ? 2.2487 1.8310 1.6044 -0.0857 0.2268  0.0463  378 LYS B CB  
6982 C CG  . LYS B 351 ? 2.1621 1.7029 1.5036 -0.0633 0.2054  0.0633  378 LYS B CG  
6983 C CD  . LYS B 351 ? 2.1232 1.6839 1.5177 -0.0341 0.1913  0.0585  378 LYS B CD  
6984 C CE  . LYS B 351 ? 2.0623 1.5907 1.4451 -0.0134 0.1704  0.0717  378 LYS B CE  
6985 N NZ  . LYS B 351 ? 1.8839 1.3608 1.2371 -0.0127 0.1660  0.0898  378 LYS B NZ  
6986 N N   . ALA B 352 ? 2.1829 1.9054 1.5939 -0.1092 0.2628  -0.0060 379 ALA B N   
6987 C CA  . ALA B 352 ? 2.2082 1.9777 1.6165 -0.1353 0.2836  -0.0256 379 ALA B CA  
6988 C C   . ALA B 352 ? 2.2224 2.0426 1.6363 -0.1354 0.2897  -0.0449 379 ALA B C   
6989 O O   . ALA B 352 ? 2.2036 2.0758 1.6210 -0.1539 0.3064  -0.0658 379 ALA B O   
6990 C CB  . ALA B 352 ? 2.1304 1.9388 1.5802 -0.1276 0.2888  -0.0377 379 ALA B CB  
6991 N N   . MET B 353 ? 2.2246 2.0346 1.6395 -0.1162 0.2774  -0.0407 380 MET B N   
6992 C CA  . MET B 353 ? 2.1458 1.9994 1.5654 -0.1140 0.2827  -0.0589 380 MET B CA  
6993 C C   . MET B 353 ? 2.2780 2.1074 1.6477 -0.1388 0.2858  -0.0523 380 MET B C   
6994 O O   . MET B 353 ? 2.2804 2.0617 1.6270 -0.1324 0.2722  -0.0338 380 MET B O   
6995 C CB  . MET B 353 ? 2.0450 1.9029 1.4964 -0.0784 0.2699  -0.0617 380 MET B CB  
6996 C CG  . MET B 353 ? 2.0295 1.9061 1.5243 -0.0510 0.2676  -0.0680 380 MET B CG  
6997 S SD  . MET B 353 ? 2.0737 1.9339 1.5926 -0.0144 0.2552  -0.0684 380 MET B SD  
6998 C CE  . MET B 353 ? 1.9908 1.8873 1.5004 -0.0149 0.2639  -0.0887 380 MET B CE  
6999 N N   . ASN B 354 ? 2.4077 2.2733 1.7596 -0.1663 0.3036  -0.0687 381 ASN B N   
7000 C CA  . ASN B 354 ? 2.5416 2.3884 1.8448 -0.1897 0.3082  -0.0649 381 ASN B CA  
7001 C C   . ASN B 354 ? 2.5500 2.4158 1.8658 -0.1693 0.2992  -0.0722 381 ASN B C   
7002 O O   . ASN B 354 ? 2.4042 2.2949 1.7633 -0.1390 0.2920  -0.0812 381 ASN B O   
7003 C CB  . ASN B 354 ? 2.4884 2.3709 1.7687 -0.2289 0.3324  -0.0831 381 ASN B CB  
7004 C CG  . ASN B 354 ? 2.4435 2.4097 1.7716 -0.2219 0.3428  -0.1138 381 ASN B CG  
7005 O OD1 . ASN B 354 ? 2.4819 2.4903 1.8348 -0.2017 0.3401  -0.1293 381 ASN B OD1 
7006 N ND2 . ASN B 354 ? 2.4373 2.4285 1.7763 -0.2373 0.3551  -0.1238 381 ASN B ND2 
7007 N N   . THR B 355 ? 2.5980 2.4481 1.8709 -0.1871 0.3011  -0.0683 382 THR B N   
7008 C CA  . THR B 355 ? 2.5253 2.3886 1.8047 -0.1710 0.2928  -0.0746 382 THR B CA  
7009 C C   . THR B 355 ? 2.4695 2.4006 1.7832 -0.1641 0.3037  -0.1039 382 THR B C   
7010 O O   . THR B 355 ? 2.4045 2.3484 1.7391 -0.1413 0.2970  -0.1121 382 THR B O   
7011 C CB  . THR B 355 ? 2.4867 2.3206 1.7089 -0.1927 0.2929  -0.0645 382 THR B CB  
7012 O OG1 . THR B 355 ? 2.5600 2.4177 1.7539 -0.2283 0.3144  -0.0772 382 THR B OG1 
7013 C CG2 . THR B 355 ? 2.5347 2.2983 1.7172 -0.1929 0.2806  -0.0351 382 THR B CG2 
7014 N N   . SER B 356 ? 2.4787 2.4546 1.7970 -0.1832 0.3214  -0.1216 383 SER B N   
7015 C CA  . SER B 356 ? 2.4081 2.4541 1.7584 -0.1724 0.3312  -0.1515 383 SER B CA  
7016 C C   . SER B 356 ? 2.4474 2.5081 1.8469 -0.1311 0.3227  -0.1571 383 SER B C   
7017 O O   . SER B 356 ? 2.3978 2.4804 1.8171 -0.1058 0.3210  -0.1709 383 SER B O   
7018 C CB  . SER B 356 ? 2.2999 2.3979 1.6440 -0.2033 0.3521  -0.1718 383 SER B CB  
7019 O OG  . SER B 356 ? 2.2654 2.3657 1.6260 -0.2048 0.3545  -0.1692 383 SER B OG  
7020 N N   . GLN B 357 ? 2.4396 2.4845 1.8554 -0.1239 0.3185  -0.1465 384 GLN B N   
7021 C CA  . GLN B 357 ? 2.3057 2.3611 1.7633 -0.0853 0.3115  -0.1510 384 GLN B CA  
7022 C C   . GLN B 357 ? 2.2491 2.2576 1.7121 -0.0598 0.2965  -0.1378 384 GLN B C   
7023 O O   . GLN B 357 ? 2.1996 2.2143 1.6891 -0.0274 0.2938  -0.1458 384 GLN B O   
7024 C CB  . GLN B 357 ? 2.3428 2.3920 1.8140 -0.0869 0.3109  -0.1426 384 GLN B CB  
7025 C CG  . GLN B 357 ? 2.3210 2.4201 1.7874 -0.1161 0.3279  -0.1590 384 GLN B CG  
7026 C CD  . GLN B 357 ? 2.3911 2.4622 1.8516 -0.1337 0.3288  -0.1446 384 GLN B CD  
7027 O OE1 . GLN B 357 ? 2.3294 2.3413 1.7873 -0.1237 0.3156  -0.1206 384 GLN B OE1 
7028 N NE2 . GLN B 357 ? 2.4005 2.5164 1.8588 -0.1610 0.3453  -0.1614 384 GLN B NE2 
7029 N N   . VAL B 358 ? 2.1375 2.0989 1.5726 -0.0737 0.2876  -0.1190 385 VAL B N   
7030 C CA  . VAL B 358 ? 2.0777 2.0042 1.5172 -0.0541 0.2747  -0.1112 385 VAL B CA  
7031 C C   . VAL B 358 ? 2.1628 2.1143 1.6042 -0.0451 0.2802  -0.1306 385 VAL B C   
7032 O O   . VAL B 358 ? 2.1288 2.0711 1.5888 -0.0198 0.2774  -0.1369 385 VAL B O   
7033 C CB  . VAL B 358 ? 1.9498 1.8292 1.3571 -0.0695 0.2628  -0.0887 385 VAL B CB  
7034 C CG1 . VAL B 358 ? 1.9012 1.7571 1.3138 -0.0524 0.2502  -0.0858 385 VAL B CG1 
7035 C CG2 . VAL B 358 ? 1.7825 1.6312 1.1879 -0.0736 0.2574  -0.0700 385 VAL B CG2 
7036 N N   . GLU B 359 ? 2.2632 2.2437 1.6825 -0.0668 0.2898  -0.1414 386 GLU B N   
7037 C CA  . GLU B 359 ? 2.2398 2.2461 1.6600 -0.0590 0.2961  -0.1614 386 GLU B CA  
7038 C C   . GLU B 359 ? 2.2715 2.3180 1.7211 -0.0324 0.3054  -0.1835 386 GLU B C   
7039 O O   . GLU B 359 ? 2.2993 2.3503 1.7550 -0.0126 0.3085  -0.1979 386 GLU B O   
7040 C CB  . GLU B 359 ? 2.3093 2.3387 1.6973 -0.0903 0.3047  -0.1679 386 GLU B CB  
7041 C CG  . GLU B 359 ? 2.3569 2.3442 1.7062 -0.1138 0.2958  -0.1458 386 GLU B CG  
7042 C CD  . GLU B 359 ? 2.4448 2.4512 1.7567 -0.1450 0.3061  -0.1526 386 GLU B CD  
7043 O OE1 . GLU B 359 ? 2.3210 2.3762 1.6417 -0.1470 0.3190  -0.1767 386 GLU B OE1 
7044 O OE2 . GLU B 359 ? 2.5880 2.5594 1.8590 -0.1662 0.3017  -0.1340 386 GLU B OE2 
7045 N N   . ALA B 360 ? 2.3346 2.4097 1.7999 -0.0302 0.3103  -0.1873 387 ALA B N   
7046 C CA  . ALA B 360 ? 2.2693 2.3906 1.7595 -0.0018 0.3182  -0.2096 387 ALA B CA  
7047 C C   . ALA B 360 ? 2.2669 2.3560 1.7747 0.0385  0.3125  -0.2078 387 ALA B C   
7048 O O   . ALA B 360 ? 2.2193 2.3373 1.7407 0.0692  0.3185  -0.2258 387 ALA B O   
7049 C CB  . ALA B 360 ? 2.2051 2.3675 1.7080 -0.0102 0.3236  -0.2142 387 ALA B CB  
7050 N N   . LEU B 361 ? 2.2367 2.2668 1.7419 0.0398  0.3019  -0.1879 388 LEU B N   
7051 C CA  . LEU B 361 ? 2.2205 2.2125 1.7368 0.0721  0.2990  -0.1866 388 LEU B CA  
7052 C C   . LEU B 361 ? 2.2119 2.1641 1.7143 0.0689  0.2967  -0.1854 388 LEU B C   
7053 O O   . LEU B 361 ? 2.1705 2.0800 1.6772 0.0857  0.2944  -0.1815 388 LEU B O   
7054 C CB  . LEU B 361 ? 2.1338 2.0964 1.6643 0.0778  0.2902  -0.1680 388 LEU B CB  
7055 C CG  . LEU B 361 ? 2.0077 2.0100 1.5534 0.0801  0.2927  -0.1700 388 LEU B CG  
7056 C CD1 . LEU B 361 ? 1.8353 1.8040 1.3939 0.0849  0.2839  -0.1513 388 LEU B CD1 
7057 C CD2 . LEU B 361 ? 2.0019 2.0461 1.5579 0.1124  0.3017  -0.1923 388 LEU B CD2 
7058 N N   . GLY B 362 ? 2.0216 1.9883 1.5060 0.0459  0.2984  -0.1902 389 GLY B N   
7059 C CA  . GLY B 362 ? 1.9747 1.9120 1.4458 0.0405  0.2964  -0.1919 389 GLY B CA  
7060 C C   . GLY B 362 ? 2.0936 1.9896 1.5640 0.0311  0.2831  -0.1727 389 GLY B C   
7061 O O   . GLY B 362 ? 2.1444 2.0105 1.6140 0.0371  0.2822  -0.1764 389 GLY B O   
7062 N N   . ILE B 363 ? 2.1882 2.0825 1.6570 0.0163  0.2736  -0.1542 390 ILE B N   
7063 C CA  . ILE B 363 ? 2.2759 2.1347 1.7452 0.0118  0.2596  -0.1360 390 ILE B CA  
7064 C C   . ILE B 363 ? 2.2028 2.0587 1.6470 -0.0088 0.2515  -0.1312 390 ILE B C   
7065 O O   . ILE B 363 ? 2.1214 1.9932 1.5432 -0.0279 0.2520  -0.1266 390 ILE B O   
7066 C CB  . ILE B 363 ? 2.1968 2.0500 1.6731 0.0089  0.2535  -0.1184 390 ILE B CB  
7067 C CG1 . ILE B 363 ? 2.0449 1.9020 1.5469 0.0321  0.2598  -0.1235 390 ILE B CG1 
7068 C CG2 . ILE B 363 ? 2.1330 1.9525 1.6058 0.0045  0.2380  -0.1000 390 ILE B CG2 
7069 C CD1 . ILE B 363 ? 2.0009 1.8559 1.5119 0.0287  0.2553  -0.1088 390 ILE B CD1 
7070 N N   . GLN B 364 ? 2.1262 1.9628 1.5717 -0.0055 0.2450  -0.1336 391 GLN B N   
7071 C CA  . GLN B 364 ? 2.0612 1.8985 1.4845 -0.0205 0.2350  -0.1306 391 GLN B CA  
7072 C C   . GLN B 364 ? 2.0936 1.9093 1.5274 -0.0142 0.2223  -0.1256 391 GLN B C   
7073 O O   . GLN B 364 ? 2.2016 2.0051 1.6551 -0.0034 0.2280  -0.1373 391 GLN B O   
7074 C CB  . GLN B 364 ? 2.1296 1.9857 1.5423 -0.0265 0.2447  -0.1513 391 GLN B CB  
7075 C CG  . GLN B 364 ? 2.1070 1.9918 1.5087 -0.0338 0.2573  -0.1598 391 GLN B CG  
7076 C CD  . GLN B 364 ? 2.1533 2.0521 1.5546 -0.0303 0.2705  -0.1843 391 GLN B CD  
7077 O OE1 . GLN B 364 ? 2.1738 2.0542 1.5853 -0.0195 0.2741  -0.1956 391 GLN B OE1 
7078 N NE2 . GLN B 364 ? 2.0545 1.9841 1.4416 -0.0408 0.2794  -0.1939 391 GLN B NE2 
7079 N N   . MET B 365 ? 2.0131 1.8232 1.4308 -0.0205 0.2061  -0.1095 392 MET B N   
7080 C CA  . MET B 365 ? 2.1073 1.9062 1.5355 -0.0135 0.1924  -0.1068 392 MET B CA  
7081 C C   . MET B 365 ? 2.2311 2.0437 1.6621 -0.0172 0.1946  -0.1286 392 MET B C   
7082 O O   . MET B 365 ? 2.1967 2.0268 1.6117 -0.0269 0.2012  -0.1403 392 MET B O   
7083 C CB  . MET B 365 ? 1.9989 1.7911 1.4026 -0.0155 0.1737  -0.0862 392 MET B CB  
7084 C CG  . MET B 365 ? 2.0694 1.8547 1.4867 -0.0041 0.1577  -0.0827 392 MET B CG  
7085 S SD  . MET B 365 ? 2.0806 1.8633 1.4597 -0.0004 0.1339  -0.0643 392 MET B SD  
7086 C CE  . MET B 365 ? 2.1608 1.9749 1.5151 -0.0117 0.1339  -0.0803 392 MET B CE  
7087 N N   . LEU B 366 ? 2.3971 2.2029 1.8484 -0.0113 0.1906  -0.1359 393 LEU B N   
7088 C CA  . LEU B 366 ? 2.5047 2.3247 1.9585 -0.0186 0.1937  -0.1592 393 LEU B CA  
7089 C C   . LEU B 366 ? 2.6684 2.5166 2.0982 -0.0264 0.1781  -0.1581 393 LEU B C   
7090 O O   . LEU B 366 ? 2.6606 2.5111 2.0813 -0.0200 0.1591  -0.1415 393 LEU B O   
7091 C CB  . LEU B 366 ? 2.4978 2.3077 1.9764 -0.0143 0.1925  -0.1678 393 LEU B CB  
7092 C CG  . LEU B 366 ? 2.5982 2.4211 2.0816 -0.0259 0.2000  -0.1964 393 LEU B CG  
7093 C CD1 . LEU B 366 ? 2.4956 2.2890 1.9991 -0.0243 0.2155  -0.2086 393 LEU B CD1 
7094 C CD2 . LEU B 366 ? 2.7069 2.5651 2.1881 -0.0295 0.1796  -0.2000 393 LEU B CD2 
7095 N N   . PRO B 367 ? 2.7196 2.5879 2.1353 -0.0381 0.1855  -0.1753 394 PRO B N   
7096 C CA  . PRO B 367 ? 2.6703 2.5671 2.0593 -0.0442 0.1704  -0.1742 394 PRO B CA  
7097 C C   . PRO B 367 ? 2.7269 2.6443 2.1229 -0.0392 0.1523  -0.1797 394 PRO B C   
7098 O O   . PRO B 367 ? 2.7057 2.6390 2.1204 -0.0459 0.1583  -0.2047 394 PRO B O   
7099 C CB  . PRO B 367 ? 2.6878 2.6023 2.0686 -0.0584 0.1858  -0.1978 394 PRO B CB  
7100 C CG  . PRO B 367 ? 2.5316 2.4222 1.9246 -0.0565 0.2074  -0.2019 394 PRO B CG  
7101 C CD  . PRO B 367 ? 2.6537 2.5173 2.0731 -0.0441 0.2082  -0.1953 394 PRO B CD  
7102 N N   . GLY B 368 ? 2.8042 2.7214 2.1828 -0.0275 0.1312  -0.1579 395 GLY B N   
7103 C CA  . GLY B 368 ? 2.9007 2.8436 2.2828 -0.0174 0.1109  -0.1623 395 GLY B CA  
7104 C C   . GLY B 368 ? 2.8833 2.8118 2.2925 -0.0043 0.1040  -0.1555 395 GLY B C   
7105 O O   . GLY B 368 ? 2.9002 2.8580 2.3261 0.0002  0.0937  -0.1709 395 GLY B O   
7106 N N   . TYR B 369 ? 2.7916 2.6809 2.2064 0.0012  0.1098  -0.1351 396 TYR B N   
7107 C CA  . TYR B 369 ? 2.7728 2.6471 2.2127 0.0134  0.1038  -0.1280 396 TYR B CA  
7108 C C   . TYR B 369 ? 2.8271 2.6970 2.2445 0.0319  0.0798  -0.1055 396 TYR B C   
7109 O O   . TYR B 369 ? 2.7765 2.6259 2.1567 0.0346  0.0749  -0.0837 396 TYR B O   
7110 C CB  . TYR B 369 ? 2.6875 2.5242 2.1434 0.0123  0.1205  -0.1175 396 TYR B CB  
7111 C CG  . TYR B 369 ? 2.6602 2.4788 2.1370 0.0251  0.1131  -0.1060 396 TYR B CG  
7112 C CD1 . TYR B 369 ? 2.6646 2.4976 2.1703 0.0274  0.1107  -0.1229 396 TYR B CD1 
7113 C CD2 . TYR B 369 ? 2.5576 2.3461 2.0243 0.0327  0.1100  -0.0802 396 TYR B CD2 
7114 C CE1 . TYR B 369 ? 2.5479 2.3666 2.0732 0.0386  0.1043  -0.1136 396 TYR B CE1 
7115 C CE2 . TYR B 369 ? 2.6052 2.3775 2.0910 0.0441  0.1036  -0.0706 396 TYR B CE2 
7116 C CZ  . TYR B 369 ? 2.5614 2.3493 2.0770 0.0480  0.1002  -0.0869 396 TYR B CZ  
7117 O OH  . TYR B 369 ? 2.4823 2.2561 2.0174 0.0589  0.0942  -0.0785 396 TYR B OH  
7118 N N   . ARG B 370 ? 2.8084 2.6955 2.2455 0.0445  0.0659  -0.1119 397 ARG B N   
7119 C CA  . ARG B 370 ? 2.8427 2.7243 2.2593 0.0674  0.0424  -0.0924 397 ARG B CA  
7120 C C   . ARG B 370 ? 2.8121 2.6878 2.2636 0.0778  0.0388  -0.0931 397 ARG B C   
7121 O O   . ARG B 370 ? 2.7410 2.6409 2.2300 0.0696  0.0463  -0.1175 397 ARG B O   
7122 C CB  . ARG B 370 ? 2.8183 2.7451 2.2136 0.0789  0.0216  -0.1030 397 ARG B CB  
7123 C CG  . ARG B 370 ? 2.6927 2.6201 2.0435 0.0725  0.0214  -0.0966 397 ARG B CG  
7124 C CD  . ARG B 370 ? 2.5980 2.5703 1.9234 0.0886  -0.0017 -0.1050 397 ARG B CD  
7125 N NE  . ARG B 370 ? 2.6049 2.5704 1.8805 0.0842  -0.0025 -0.0946 397 ARG B NE  
7126 C CZ  . ARG B 370 ? 2.6338 2.6315 1.8746 0.0987  -0.0218 -0.0975 397 ARG B CZ  
7127 N NH1 . ARG B 370 ? 2.5896 2.6352 1.8412 0.1204  -0.0431 -0.1121 397 ARG B NH1 
7128 N NH2 . ARG B 370 ? 2.6722 2.6571 1.8654 0.0920  -0.0197 -0.0866 397 ARG B NH2 
7129 N N   . ASP B 371 ? 3.0074 2.8478 2.4433 0.0939  0.0291  -0.0669 398 ASP B N   
7130 C CA  . ASP B 371 ? 2.9884 2.8194 2.4543 0.1048  0.0252  -0.0646 398 ASP B CA  
7131 C C   . ASP B 371 ? 2.9932 2.8757 2.4822 0.1159  0.0099  -0.0882 398 ASP B C   
7132 O O   . ASP B 371 ? 3.0528 2.9659 2.5179 0.1309  -0.0095 -0.0912 398 ASP B O   
7133 C CB  . ASP B 371 ? 3.0503 2.8360 2.4850 0.1221  0.0147  -0.0331 398 ASP B CB  
7134 C CG  . ASP B 371 ? 3.0456 2.8087 2.5106 0.1271  0.0180  -0.0268 398 ASP B CG  
7135 O OD1 . ASP B 371 ? 3.0515 2.8433 2.5555 0.1302  0.0155  -0.0456 398 ASP B OD1 
7136 O OD2 . ASP B 371 ? 3.0095 2.7271 2.4583 0.1263  0.0241  -0.0043 398 ASP B OD2 
7137 N N   . PRO B 372 ? 2.7458 2.6421 2.2792 0.1086  0.0185  -0.1068 399 PRO B N   
7138 C CA  . PRO B 372 ? 2.6615 2.6139 2.2190 0.1156  0.0057  -0.1336 399 PRO B CA  
7139 C C   . PRO B 372 ? 2.7134 2.6776 2.2568 0.1482  -0.0221 -0.1220 399 PRO B C   
7140 O O   . PRO B 372 ? 2.5473 2.5701 2.1016 0.1591  -0.0377 -0.1447 399 PRO B O   
7141 C CB  . PRO B 372 ? 2.5547 2.5015 2.1560 0.0995  0.0242  -0.1497 399 PRO B CB  
7142 C CG  . PRO B 372 ? 2.5115 2.4139 2.1099 0.0806  0.0487  -0.1412 399 PRO B CG  
7143 C CD  . PRO B 372 ? 2.6331 2.4997 2.1942 0.0906  0.0428  -0.1094 399 PRO B CD  
7144 N N   . TYR B 373 ? 2.9752 2.8869 2.4935 0.1647  -0.0283 -0.0894 400 TYR B N   
7145 C CA  . TYR B 373 ? 2.9794 2.8915 2.4799 0.1986  -0.0533 -0.0772 400 TYR B CA  
7146 C C   . TYR B 373 ? 3.0365 2.9038 2.4740 0.2175  -0.0649 -0.0454 400 TYR B C   
7147 O O   . TYR B 373 ? 3.0256 2.8828 2.4369 0.2496  -0.0856 -0.0325 400 TYR B O   
7148 C CB  . TYR B 373 ? 2.9269 2.8132 2.4564 0.2037  -0.0500 -0.0702 400 TYR B CB  
7149 C CG  . TYR B 373 ? 2.8845 2.8056 2.4702 0.1836  -0.0361 -0.0999 400 TYR B CG  
7150 C CD1 . TYR B 373 ? 2.8043 2.7884 2.4182 0.1920  -0.0483 -0.1288 400 TYR B CD1 
7151 C CD2 . TYR B 373 ? 2.8234 2.7145 2.4305 0.1565  -0.0100 -0.1003 400 TYR B CD2 
7152 C CE1 . TYR B 373 ? 2.7346 2.7457 2.3946 0.1693  -0.0324 -0.1573 400 TYR B CE1 
7153 C CE2 . TYR B 373 ? 2.7882 2.7007 2.4375 0.1382  0.0047  -0.1261 400 TYR B CE2 
7154 C CZ  . TYR B 373 ? 2.7512 2.7212 2.4259 0.1423  -0.0053 -0.1545 400 TYR B CZ  
7155 O OH  . TYR B 373 ? 2.7107 2.6972 2.4224 0.1199  0.0124  -0.1813 400 TYR B OH  
7156 N N   . HIS B 374 ? 3.0982 2.9359 2.5072 0.1987  -0.0512 -0.0333 401 HIS B N   
7157 C CA  . HIS B 374 ? 3.1222 2.9175 2.4649 0.2116  -0.0595 -0.0059 401 HIS B CA  
7158 C C   . HIS B 374 ? 3.1382 2.9433 2.4551 0.1931  -0.0513 -0.0094 401 HIS B C   
7159 O O   . HIS B 374 ? 3.1915 2.9668 2.4487 0.2034  -0.0589 0.0105  401 HIS B O   
7160 C CB  . HIS B 374 ? 3.0583 2.7788 2.3791 0.2073  -0.0479 0.0239  401 HIS B CB  
7161 C CG  . HIS B 374 ? 2.9529 2.6511 2.2781 0.2320  -0.0598 0.0342  401 HIS B CG  
7162 N ND1 . HIS B 374 ? 2.8373 2.5283 2.1228 0.2691  -0.0842 0.0442  401 HIS B ND1 
7163 C CD2 . HIS B 374 ? 2.8885 2.5696 2.2509 0.2268  -0.0508 0.0357  401 HIS B CD2 
7164 C CE1 . HIS B 374 ? 2.7904 2.4604 2.0899 0.2851  -0.0892 0.0509  401 HIS B CE1 
7165 N NE2 . HIS B 374 ? 2.7811 2.4456 2.1281 0.2585  -0.0690 0.0458  401 HIS B NE2 
7166 N N   . GLY B 375 ? 3.1893 3.0305 2.5444 0.1665  -0.0352 -0.0336 402 GLY B N   
7167 C CA  . GLY B 375 ? 3.1878 3.0453 2.5215 0.1499  -0.0282 -0.0408 402 GLY B CA  
7168 C C   . GLY B 375 ? 3.1926 2.9996 2.4951 0.1310  -0.0103 -0.0201 402 GLY B C   
7169 O O   . GLY B 375 ? 3.1934 3.0044 2.4606 0.1232  -0.0090 -0.0188 402 GLY B O   
7170 N N   . ARG B 376 ? 3.0869 2.8511 2.4020 0.1221  0.0040  -0.0063 403 ARG B N   
7171 C CA  . ARG B 376 ? 2.9444 2.6648 2.2316 0.1040  0.0214  0.0116  403 ARG B CA  
7172 C C   . ARG B 376 ? 2.8457 2.5815 2.1705 0.0782  0.0451  -0.0052 403 ARG B C   
7173 O O   . ARG B 376 ? 2.8497 2.6093 2.2231 0.0756  0.0507  -0.0241 403 ARG B O   
7174 C CB  . ARG B 376 ? 2.9211 2.5882 2.1966 0.1104  0.0231  0.0354  403 ARG B CB  
7175 C CG  . ARG B 376 ? 2.9630 2.6051 2.1986 0.1400  0.0007  0.0529  403 ARG B CG  
7176 C CD  . ARG B 376 ? 2.8572 2.4573 2.1003 0.1479  0.0020  0.0683  403 ARG B CD  
7177 N NE  . ARG B 376 ? 2.8068 2.3598 2.0303 0.1253  0.0229  0.0840  403 ARG B NE  
7178 C CZ  . ARG B 376 ? 2.8597 2.4186 2.1259 0.1051  0.0419  0.0765  403 ARG B CZ  
7179 N NH1 . ARG B 376 ? 2.8068 2.4063 2.1332 0.1044  0.0441  0.0562  403 ARG B NH1 
7180 N NH2 . ARG B 376 ? 2.9210 2.4442 2.1658 0.0850  0.0598  0.0886  403 ARG B NH2 
7181 N N   . PRO B 377 ? 2.7691 2.4903 2.0691 0.0597  0.0600  0.0006  404 PRO B N   
7182 C CA  . PRO B 377 ? 2.6364 2.3706 1.9689 0.0400  0.0823  -0.0148 404 PRO B CA  
7183 C C   . PRO B 377 ? 2.5969 2.3108 1.9622 0.0389  0.0937  -0.0104 404 PRO B C   
7184 O O   . PRO B 377 ? 2.6422 2.3330 2.0086 0.0510  0.0850  0.0036  404 PRO B O   
7185 C CB  . PRO B 377 ? 2.5952 2.3196 1.8867 0.0230  0.0930  -0.0078 404 PRO B CB  
7186 C CG  . PRO B 377 ? 2.6513 2.3677 1.8905 0.0327  0.0753  0.0048  404 PRO B CG  
7187 C CD  . PRO B 377 ? 2.7711 2.4679 2.0087 0.0565  0.0572  0.0181  404 PRO B CD  
7188 N N   . LEU B 378 ? 2.3973 2.1202 1.7876 0.0264  0.1130  -0.0229 405 LEU B N   
7189 C CA  . LEU B 378 ? 2.2441 1.9529 1.6648 0.0274  0.1240  -0.0206 405 LEU B CA  
7190 C C   . LEU B 378 ? 2.2261 1.9063 1.6217 0.0213  0.1281  -0.0001 405 LEU B C   
7191 O O   . LEU B 378 ? 2.0864 1.7623 1.4469 0.0079  0.1342  0.0055  405 LEU B O   
7192 C CB  . LEU B 378 ? 2.0223 1.7475 1.4686 0.0201  0.1430  -0.0396 405 LEU B CB  
7193 C CG  . LEU B 378 ? 1.9642 1.6794 1.4421 0.0252  0.1545  -0.0405 405 LEU B CG  
7194 C CD1 . LEU B 378 ? 1.9843 1.7078 1.4904 0.0293  0.1642  -0.0614 405 LEU B CD1 
7195 C CD2 . LEU B 378 ? 1.8907 1.6068 1.3593 0.0164  0.1685  -0.0364 405 LEU B CD2 
7196 N N   . THR B 379 ? 2.2763 1.9369 1.6887 0.0288  0.1265  0.0096  406 THR B N   
7197 C CA  . THR B 379 ? 2.2226 1.8529 1.6113 0.0220  0.1307  0.0279  406 THR B CA  
7198 C C   . THR B 379 ? 2.1515 1.7921 1.5614 0.0106  0.1502  0.0213  406 THR B C   
7199 O O   . THR B 379 ? 2.1400 1.8036 1.5863 0.0153  0.1578  0.0058  406 THR B O   
7200 C CB  . THR B 379 ? 2.2542 1.8579 1.6471 0.0372  0.1177  0.0414  406 THR B CB  
7201 O OG1 . THR B 379 ? 2.1092 1.7225 1.5502 0.0434  0.1226  0.0332  406 THR B OG1 
7202 C CG2 . THR B 379 ? 2.3356 1.9430 1.7186 0.0548  0.0967  0.0418  406 THR B CG2 
7203 N N   . LYS B 380 ? 2.2478 1.8704 1.6307 -0.0042 0.1591  0.0323  407 LYS B N   
7204 C CA  . LYS B 380 ? 2.1431 1.7828 1.5463 -0.0146 0.1766  0.0245  407 LYS B CA  
7205 C C   . LYS B 380 ? 2.0106 1.6498 1.4552 -0.0003 0.1752  0.0236  407 LYS B C   
7206 O O   . LYS B 380 ? 2.0207 1.6852 1.4946 0.0014  0.1865  0.0115  407 LYS B O   
7207 C CB  . LYS B 380 ? 2.1390 1.7597 1.5024 -0.0376 0.1876  0.0343  407 LYS B CB  
7208 C CG  . LYS B 380 ? 2.1088 1.7341 1.4306 -0.0563 0.1945  0.0321  407 LYS B CG  
7209 C CD  . LYS B 380 ? 2.1943 1.8700 1.5419 -0.0597 0.2058  0.0098  407 LYS B CD  
7210 C CE  . LYS B 380 ? 2.2994 1.9829 1.6068 -0.0800 0.2135  0.0060  407 LYS B CE  
7211 N NZ  . LYS B 380 ? 2.1751 1.9083 1.5076 -0.0806 0.2240  -0.0171 407 LYS B NZ  
7212 N N   . GLY B 381 ? 1.8811 1.4932 1.3273 0.0119  0.1612  0.0357  408 GLY B N   
7213 C CA  . GLY B 381 ? 1.8873 1.4995 1.3731 0.0253  0.1595  0.0340  408 GLY B CA  
7214 C C   . GLY B 381 ? 1.8164 1.4516 1.3376 0.0382  0.1596  0.0177  408 GLY B C   
7215 O O   . GLY B 381 ? 1.7975 1.4446 1.3473 0.0438  0.1688  0.0093  408 GLY B O   
7216 N N   . GLU B 382 ? 1.8797 1.5196 1.3956 0.0429  0.1502  0.0123  409 GLU B N   
7217 C CA  . GLU B 382 ? 1.7900 1.4467 1.3326 0.0503  0.1537  -0.0055 409 GLU B CA  
7218 C C   . GLU B 382 ? 1.8726 1.5482 1.4178 0.0456  0.1703  -0.0187 409 GLU B C   
7219 O O   . GLU B 382 ? 1.7978 1.4776 1.3643 0.0540  0.1787  -0.0319 409 GLU B O   
7220 C CB  . GLU B 382 ? 1.8365 1.5004 1.3700 0.0522  0.1416  -0.0116 409 GLU B CB  
7221 C CG  . GLU B 382 ? 1.8701 1.5236 1.4049 0.0626  0.1238  -0.0031 409 GLU B CG  
7222 C CD  . GLU B 382 ? 2.0214 1.6921 1.5442 0.0656  0.1105  -0.0111 409 GLU B CD  
7223 O OE1 . GLU B 382 ? 2.0523 1.7357 1.5541 0.0572  0.1133  -0.0163 409 GLU B OE1 
7224 O OE2 . GLU B 382 ? 1.9231 1.5992 1.4583 0.0765  0.0972  -0.0138 409 GLU B OE2 
7225 N N   . LEU B 383 ? 2.0049 1.6900 1.5254 0.0327  0.1761  -0.0162 410 LEU B N   
7226 C CA  . LEU B 383 ? 1.9988 1.7079 1.5222 0.0298  0.1917  -0.0301 410 LEU B CA  
7227 C C   . LEU B 383 ? 1.9228 1.6394 1.4697 0.0386  0.2015  -0.0331 410 LEU B C   
7228 O O   . LEU B 383 ? 1.9451 1.6716 1.5080 0.0516  0.2105  -0.0466 410 LEU B O   
7229 C CB  . LEU B 383 ? 2.0468 1.7674 1.5378 0.0112  0.1961  -0.0277 410 LEU B CB  
7230 C CG  . LEU B 383 ? 2.0368 1.7900 1.5298 0.0066  0.2124  -0.0431 410 LEU B CG  
7231 C CD1 . LEU B 383 ? 2.1227 1.8877 1.6278 0.0184  0.2174  -0.0610 410 LEU B CD1 
7232 C CD2 . LEU B 383 ? 1.9962 1.7590 1.4542 -0.0164 0.2174  -0.0406 410 LEU B CD2 
7233 N N   . GLY B 384 ? 1.8652 1.5756 1.4107 0.0327  0.2005  -0.0211 411 GLY B N   
7234 C CA  . GLY B 384 ? 1.7658 1.4888 1.3340 0.0411  0.2086  -0.0247 411 GLY B CA  
7235 C C   . GLY B 384 ? 1.7202 1.4274 1.3150 0.0610  0.2051  -0.0256 411 GLY B C   
7236 O O   . GLY B 384 ? 1.6665 1.3853 1.2787 0.0749  0.2130  -0.0330 411 GLY B O   
7237 N N   . CYS B 385 ? 1.7710 1.4534 1.3673 0.0632  0.1935  -0.0192 412 CYS B N   
7238 C CA  . CYS B 385 ? 1.8113 1.4781 1.4306 0.0781  0.1920  -0.0223 412 CYS B CA  
7239 C C   . CYS B 385 ? 1.8183 1.4859 1.4405 0.0878  0.2017  -0.0388 412 CYS B C   
7240 O O   . CYS B 385 ? 1.8067 1.4638 1.4419 0.1022  0.2090  -0.0441 412 CYS B O   
7241 C CB  . CYS B 385 ? 1.7014 1.3493 1.3217 0.0763  0.1772  -0.0145 412 CYS B CB  
7242 S SG  . CYS B 385 ? 1.8531 1.4830 1.5023 0.0893  0.1756  -0.0171 412 CYS B SG  
7243 N N   . PHE B 386 ? 1.8448 1.5207 1.4511 0.0803  0.2031  -0.0469 413 PHE B N   
7244 C CA  . PHE B 386 ? 1.7752 1.4476 1.3794 0.0881  0.2146  -0.0638 413 PHE B CA  
7245 C C   . PHE B 386 ? 1.8076 1.4926 1.4121 0.1022  0.2278  -0.0707 413 PHE B C   
7246 O O   . PHE B 386 ? 1.7977 1.4658 1.4036 0.1189  0.2380  -0.0802 413 PHE B O   
7247 C CB  . PHE B 386 ? 1.8076 1.4905 1.3940 0.0756  0.2133  -0.0718 413 PHE B CB  
7248 C CG  . PHE B 386 ? 1.7975 1.4709 1.3789 0.0807  0.2260  -0.0904 413 PHE B CG  
7249 C CD1 . PHE B 386 ? 1.8355 1.5182 1.4078 0.0894  0.2392  -0.1009 413 PHE B CD1 
7250 C CD2 . PHE B 386 ? 1.8306 1.4861 1.4146 0.0765  0.2258  -0.0995 413 PHE B CD2 
7251 C CE1 . PHE B 386 ? 1.9546 1.6205 1.5171 0.0954  0.2523  -0.1179 413 PHE B CE1 
7252 C CE2 . PHE B 386 ? 1.8497 1.4896 1.4242 0.0780  0.2404  -0.1179 413 PHE B CE2 
7253 C CZ  . PHE B 386 ? 1.9329 1.5738 1.4948 0.0883  0.2538  -0.1261 413 PHE B CZ  
7254 N N   . LEU B 387 ? 1.7496 1.4641 1.3497 0.0962  0.2285  -0.0675 414 LEU B N   
7255 C CA  . LEU B 387 ? 1.7612 1.5006 1.3636 0.1107  0.2397  -0.0773 414 LEU B CA  
7256 C C   . LEU B 387 ? 1.7691 1.5031 1.3880 0.1295  0.2413  -0.0738 414 LEU B C   
7257 O O   . LEU B 387 ? 1.7709 1.5168 1.3905 0.1514  0.2503  -0.0840 414 LEU B O   
7258 C CB  . LEU B 387 ? 1.7247 1.5030 1.3188 0.0942  0.2412  -0.0777 414 LEU B CB  
7259 C CG  . LEU B 387 ? 1.7877 1.5761 1.3614 0.0777  0.2422  -0.0834 414 LEU B CG  
7260 C CD1 . LEU B 387 ? 1.8984 1.7171 1.4596 0.0557  0.2441  -0.0811 414 LEU B CD1 
7261 C CD2 . LEU B 387 ? 1.6956 1.4927 1.2651 0.0935  0.2529  -0.1020 414 LEU B CD2 
7262 N N   . SER B 388 ? 1.8772 1.5942 1.5077 0.1235  0.2325  -0.0602 415 SER B N   
7263 C CA  . SER B 388 ? 1.8077 1.5177 1.4534 0.1407  0.2339  -0.0569 415 SER B CA  
7264 C C   . SER B 388 ? 1.7374 1.4121 1.3804 0.1610  0.2404  -0.0634 415 SER B C   
7265 O O   . SER B 388 ? 1.7409 1.4157 1.3824 0.1851  0.2484  -0.0691 415 SER B O   
7266 C CB  . SER B 388 ? 1.7479 1.4458 1.4054 0.1282  0.2232  -0.0417 415 SER B CB  
7267 O OG  . SER B 388 ? 1.7379 1.4593 1.3907 0.1094  0.2205  -0.0357 415 SER B OG  
7268 N N   . HIS B 389 ? 1.6876 1.3311 1.3267 0.1516  0.2380  -0.0636 416 HIS B N   
7269 C CA  . HIS B 389 ? 1.6256 1.2305 1.2551 0.1647  0.2483  -0.0726 416 HIS B CA  
7270 C C   . HIS B 389 ? 1.7938 1.3989 1.4030 0.1789  0.2611  -0.0866 416 HIS B C   
7271 O O   . HIS B 389 ? 1.8153 1.3882 1.4101 0.2001  0.2731  -0.0933 416 HIS B O   
7272 C CB  . HIS B 389 ? 1.6739 1.2558 1.3040 0.1465  0.2443  -0.0747 416 HIS B CB  
7273 C CG  . HIS B 389 ? 1.6148 1.1914 1.2636 0.1382  0.2329  -0.0638 416 HIS B CG  
7274 N ND1 . HIS B 389 ? 1.6393 1.1869 1.2945 0.1460  0.2374  -0.0633 416 HIS B ND1 
7275 C CD2 . HIS B 389 ? 1.6533 1.2475 1.3128 0.1241  0.2178  -0.0533 416 HIS B CD2 
7276 C CE1 . HIS B 389 ? 1.6453 1.1981 1.3186 0.1366  0.2250  -0.0542 416 HIS B CE1 
7277 N NE2 . HIS B 389 ? 1.6249 1.2042 1.3001 0.1248  0.2127  -0.0477 416 HIS B NE2 
7278 N N   . TYR B 390 ? 1.7818 1.4193 1.3859 0.1685  0.2596  -0.0913 417 TYR B N   
7279 C CA  . TYR B 390 ? 1.7636 1.4065 1.3493 0.1826  0.2714  -0.1060 417 TYR B CA  
7280 C C   . TYR B 390 ? 1.7140 1.3742 1.2987 0.2128  0.2773  -0.1095 417 TYR B C   
7281 O O   . TYR B 390 ? 1.7233 1.3645 1.2886 0.2381  0.2890  -0.1205 417 TYR B O   
7282 C CB  . TYR B 390 ? 1.8442 1.5239 1.4263 0.1627  0.2677  -0.1099 417 TYR B CB  
7283 C CG  . TYR B 390 ? 1.8537 1.5487 1.4195 0.1756  0.2791  -0.1263 417 TYR B CG  
7284 C CD1 . TYR B 390 ? 1.8097 1.4708 1.3562 0.1806  0.2898  -0.1388 417 TYR B CD1 
7285 C CD2 . TYR B 390 ? 1.8350 1.5804 1.4041 0.1812  0.2801  -0.1313 417 TYR B CD2 
7286 C CE1 . TYR B 390 ? 1.8822 1.5552 1.4123 0.1940  0.3004  -0.1543 417 TYR B CE1 
7287 C CE2 . TYR B 390 ? 1.8967 1.6611 1.4522 0.1946  0.2899  -0.1481 417 TYR B CE2 
7288 C CZ  . TYR B 390 ? 1.9729 1.6992 1.5085 0.2025  0.2996  -0.1588 417 TYR B CZ  
7289 O OH  . TYR B 390 ? 1.9323 1.6754 1.4529 0.2177  0.3098  -0.1761 417 TYR B OH  
7290 N N   . ASN B 391 ? 1.6605 1.3564 1.2635 0.2119  0.2698  -0.1014 418 ASN B N   
7291 C CA  . ASN B 391 ? 1.7093 1.4317 1.3141 0.2413  0.2739  -0.1067 418 ASN B CA  
7292 C C   . ASN B 391 ? 1.7016 1.3771 1.2973 0.2690  0.2790  -0.1038 418 ASN B C   
7293 O O   . ASN B 391 ? 1.6669 1.3407 1.2468 0.3036  0.2868  -0.1123 418 ASN B O   
7294 C CB  . ASN B 391 ? 1.6690 1.4413 1.2956 0.2282  0.2660  -0.1008 418 ASN B CB  
7295 C CG  . ASN B 391 ? 1.7372 1.5560 1.3647 0.2035  0.2652  -0.1063 418 ASN B CG  
7296 O OD1 . ASN B 391 ? 1.6923 1.5081 1.3063 0.1962  0.2686  -0.1135 418 ASN B OD1 
7297 N ND2 . ASN B 391 ? 1.8756 1.7358 1.5164 0.1884  0.2621  -0.1040 418 ASN B ND2 
7298 N N   . ILE B 392 ? 1.6307 1.2674 1.2332 0.2557  0.2750  -0.0923 419 ILE B N   
7299 C CA  . ILE B 392 ? 1.6222 1.2097 1.2128 0.2777  0.2814  -0.0892 419 ILE B CA  
7300 C C   . ILE B 392 ? 1.6809 1.2151 1.2370 0.2931  0.2964  -0.0996 419 ILE B C   
7301 O O   . ILE B 392 ? 1.8103 1.3116 1.3419 0.3259  0.3061  -0.1022 419 ILE B O   
7302 C CB  . ILE B 392 ? 1.6537 1.2161 1.2607 0.2559  0.2744  -0.0771 419 ILE B CB  
7303 C CG1 . ILE B 392 ? 1.4057 1.0142 1.0417 0.2424  0.2612  -0.0668 419 ILE B CG1 
7304 C CG2 . ILE B 392 ? 1.5667 1.0760 1.1585 0.2753  0.2829  -0.0746 419 ILE B CG2 
7305 C CD1 . ILE B 392 ? 1.3864 0.9722 1.0383 0.2287  0.2543  -0.0555 419 ILE B CD1 
7306 N N   . TRP B 393 ? 1.7177 1.2398 1.2674 0.2704  0.2994  -0.1063 420 TRP B N   
7307 C CA  . TRP B 393 ? 1.7368 1.2099 1.2514 0.2818  0.3159  -0.1190 420 TRP B CA  
7308 C C   . TRP B 393 ? 1.8632 1.3519 1.3581 0.3182  0.3227  -0.1283 420 TRP B C   
7309 O O   . TRP B 393 ? 1.8890 1.3257 1.3477 0.3470  0.3372  -0.1344 420 TRP B O   
7310 C CB  . TRP B 393 ? 1.8233 1.2977 1.3384 0.2498  0.3164  -0.1269 420 TRP B CB  
7311 C CG  . TRP B 393 ? 1.8450 1.3159 1.3804 0.2166  0.3074  -0.1205 420 TRP B CG  
7312 C CD1 . TRP B 393 ? 1.7478 1.1955 1.2935 0.2124  0.3046  -0.1119 420 TRP B CD1 
7313 C CD2 . TRP B 393 ? 1.8424 1.3377 1.3895 0.1856  0.2992  -0.1234 420 TRP B CD2 
7314 N NE1 . TRP B 393 ? 1.7676 1.2263 1.3321 0.1819  0.2949  -0.1104 420 TRP B NE1 
7315 C CE2 . TRP B 393 ? 1.8393 1.3268 1.4037 0.1664  0.2909  -0.1170 420 TRP B CE2 
7316 C CE3 . TRP B 393 ? 1.7155 1.2398 1.2585 0.1737  0.2978  -0.1314 420 TRP B CE3 
7317 C CZ2 . TRP B 393 ? 1.8068 1.3163 1.3836 0.1392  0.2801  -0.1185 420 TRP B CZ2 
7318 C CZ3 . TRP B 393 ? 1.7752 1.3180 1.3288 0.1449  0.2876  -0.1316 420 TRP B CZ3 
7319 C CH2 . TRP B 393 ? 1.8414 1.3773 1.4112 0.1296  0.2783  -0.1252 420 TRP B CH2 
7320 N N   . LYS B 394 ? 1.9362 1.4955 1.4515 0.3179  0.3134  -0.1306 421 LYS B N   
7321 C CA  . LYS B 394 ? 1.8922 1.4816 1.3940 0.3537  0.3181  -0.1423 421 LYS B CA  
7322 C C   . LYS B 394 ? 1.9148 1.4978 1.4082 0.3935  0.3187  -0.1385 421 LYS B C   
7323 O O   . LYS B 394 ? 1.9423 1.5076 1.4052 0.4349  0.3277  -0.1474 421 LYS B O   
7324 C CB  . LYS B 394 ? 1.9078 1.5806 1.4358 0.3384  0.3089  -0.1476 421 LYS B CB  
7325 C CG  . LYS B 394 ? 1.8101 1.4937 1.3335 0.3144  0.3118  -0.1570 421 LYS B CG  
7326 C CD  . LYS B 394 ? 1.9241 1.6887 1.4667 0.3030  0.3059  -0.1643 421 LYS B CD  
7327 C CE  . LYS B 394 ? 2.0486 1.8265 1.5792 0.2916  0.3118  -0.1780 421 LYS B CE  
7328 N NZ  . LYS B 394 ? 2.0334 1.8903 1.5783 0.2814  0.3090  -0.1881 421 LYS B NZ  
7329 N N   . GLU B 395 ? 1.9126 1.5092 1.4302 0.3839  0.3090  -0.1255 422 GLU B N   
7330 C CA  . GLU B 395 ? 1.7692 1.3606 1.2786 0.4208  0.3089  -0.1215 422 GLU B CA  
7331 C C   . GLU B 395 ? 1.8245 1.3239 1.2915 0.4433  0.3224  -0.1182 422 GLU B C   
7332 O O   . GLU B 395 ? 1.8749 1.3564 1.3136 0.4882  0.3275  -0.1199 422 GLU B O   
7333 C CB  . GLU B 395 ? 1.6542 1.2779 1.1989 0.4011  0.2965  -0.1090 422 GLU B CB  
7334 C CG  . GLU B 395 ? 1.6949 1.3096 1.2314 0.4356  0.2961  -0.1037 422 GLU B CG  
7335 C CD  . GLU B 395 ? 1.7545 1.4479 1.3260 0.4326  0.2845  -0.1034 422 GLU B CD  
7336 O OE1 . GLU B 395 ? 1.9014 1.6480 1.5011 0.4000  0.2781  -0.1059 422 GLU B OE1 
7337 O OE2 . GLU B 395 ? 1.6490 1.3493 1.2165 0.4621  0.2828  -0.1014 422 GLU B OE2 
7338 N N   . VAL B 396 ? 1.8166 1.2570 1.2752 0.4132  0.3292  -0.1147 423 VAL B N   
7339 C CA  . VAL B 396 ? 1.9512 1.2988 1.3657 0.4271  0.3457  -0.1135 423 VAL B CA  
7340 C C   . VAL B 396 ? 1.9523 1.2595 1.3183 0.4612  0.3614  -0.1260 423 VAL B C   
7341 O O   . VAL B 396 ? 1.9992 1.2473 1.3200 0.4997  0.3730  -0.1249 423 VAL B O   
7342 C CB  . VAL B 396 ? 1.8630 1.1685 1.2834 0.3819  0.3502  -0.1116 423 VAL B CB  
7343 C CG1 . VAL B 396 ? 2.0518 1.2584 1.4203 0.3903  0.3723  -0.1152 423 VAL B CG1 
7344 C CG2 . VAL B 396 ? 1.6505 0.9850 1.1117 0.3569  0.3357  -0.0988 423 VAL B CG2 
7345 N N   . VAL B 397 ? 1.9506 1.2857 1.3214 0.4490  0.3624  -0.1379 424 VAL B N   
7346 C CA  . VAL B 397 ? 1.9781 1.2737 1.3027 0.4799  0.3779  -0.1513 424 VAL B CA  
7347 C C   . VAL B 397 ? 2.0704 1.4034 1.3829 0.5354  0.3737  -0.1554 424 VAL B C   
7348 O O   . VAL B 397 ? 2.1345 1.4079 1.3945 0.5800  0.3869  -0.1592 424 VAL B O   
7349 C CB  . VAL B 397 ? 1.8338 1.1560 1.1700 0.4501  0.3793  -0.1638 424 VAL B CB  
7350 C CG1 . VAL B 397 ? 1.9037 1.2070 1.1996 0.4868  0.3922  -0.1793 424 VAL B CG1 
7351 C CG2 . VAL B 397 ? 1.8399 1.1105 1.1729 0.4047  0.3879  -0.1642 424 VAL B CG2 
7352 N N   . ASP B 398 ? 2.2668 1.6986 1.6246 0.5343  0.3562  -0.1561 425 ASP B N   
7353 C CA  . ASP B 398 ? 2.2648 1.7503 1.6173 0.5851  0.3510  -0.1645 425 ASP B CA  
7354 C C   . ASP B 398 ? 2.3181 1.7581 1.6387 0.6289  0.3534  -0.1553 425 ASP B C   
7355 O O   . ASP B 398 ? 2.5853 1.9951 1.8600 0.6832  0.3610  -0.1618 425 ASP B O   
7356 C CB  . ASP B 398 ? 2.1633 1.7630 1.5720 0.5661  0.3338  -0.1679 425 ASP B CB  
7357 C CG  . ASP B 398 ? 2.4183 2.0647 1.8510 0.5284  0.3322  -0.1779 425 ASP B CG  
7358 O OD1 . ASP B 398 ? 2.4615 2.0627 1.8683 0.5249  0.3433  -0.1849 425 ASP B OD1 
7359 O OD2 . ASP B 398 ? 2.4173 2.1427 1.8916 0.5008  0.3209  -0.1789 425 ASP B OD2 
7360 N N   . ARG B 399 ? 2.2458 1.6788 1.5872 0.6079  0.3469  -0.1400 426 ARG B N   
7361 C CA  . ARG B 399 ? 2.2413 1.6358 1.5547 0.6461  0.3482  -0.1303 426 ARG B CA  
7362 C C   . ARG B 399 ? 2.2330 1.5007 1.4852 0.6551  0.3680  -0.1232 426 ARG B C   
7363 O O   . ARG B 399 ? 2.1764 1.3965 1.3917 0.6913  0.3722  -0.1150 426 ARG B O   
7364 C CB  . ARG B 399 ? 1.9823 1.4215 1.3425 0.6186  0.3342  -0.1181 426 ARG B CB  
7365 C CG  . ARG B 399 ? 1.9201 1.4794 1.3312 0.6152  0.3175  -0.1262 426 ARG B CG  
7366 C CD  . ARG B 399 ? 1.8126 1.4073 1.2706 0.5751  0.3061  -0.1147 426 ARG B CD  
7367 N NE  . ARG B 399 ? 1.8700 1.4093 1.3108 0.5876  0.3080  -0.1007 426 ARG B NE  
7368 C CZ  . ARG B 399 ? 1.9685 1.5218 1.4421 0.5586  0.3000  -0.0895 426 ARG B CZ  
7369 N NH1 . ARG B 399 ? 1.9552 1.5709 1.4773 0.5168  0.2898  -0.0896 426 ARG B NH1 
7370 N NH2 . ARG B 399 ? 1.9494 1.4489 1.4028 0.5721  0.3034  -0.0781 426 ARG B NH2 
7371 N N   . GLY B 400 ? 1.9476 1.4244 1.5077 0.6348  0.4997  0.1180  427 GLY B N   
7372 C CA  . GLY B 400 ? 1.9660 1.3319 1.5089 0.6343  0.5156  0.0929  427 GLY B CA  
7373 C C   . GLY B 400 ? 2.0881 1.4209 1.6430 0.5913  0.4960  0.0937  427 GLY B C   
7374 O O   . GLY B 400 ? 2.1216 1.3790 1.6732 0.5965  0.5100  0.0943  427 GLY B O   
7375 N N   . LEU B 401 ? 2.1660 1.5516 1.7337 0.5495  0.4654  0.0943  428 LEU B N   
7376 C CA  . LEU B 401 ? 2.1155 1.4749 1.6955 0.5091  0.4483  0.0940  428 LEU B CA  
7377 C C   . LEU B 401 ? 2.1234 1.3947 1.6851 0.4852  0.4535  0.0482  428 LEU B C   
7378 O O   . LEU B 401 ? 2.2620 1.5291 1.8071 0.4714  0.4479  0.0126  428 LEU B O   
7379 C CB  . LEU B 401 ? 2.0526 1.4882 1.6491 0.4738  0.4163  0.1037  428 LEU B CB  
7380 C CG  . LEU B 401 ? 1.9841 1.5125 1.5970 0.4902  0.4079  0.1466  428 LEU B CG  
7381 C CD1 . LEU B 401 ? 1.9650 1.5587 1.5862 0.4546  0.3779  0.1484  428 LEU B CD1 
7382 C CD2 . LEU B 401 ? 2.0553 1.5871 1.6840 0.5013  0.4113  0.1869  428 LEU B CD2 
7383 N N   . GLN B 402 ? 2.1150 1.3180 1.6791 0.4781  0.4635  0.0501  429 GLN B N   
7384 C CA  . GLN B 402 ? 2.1202 1.2361 1.6679 0.4552  0.4711  0.0086  429 GLN B CA  
7385 C C   . GLN B 402 ? 2.0376 1.1704 1.5979 0.4038  0.4446  -0.0138 429 GLN B C   
7386 O O   . GLN B 402 ? 1.9124 1.0104 1.4589 0.3824  0.4415  -0.0543 429 GLN B O   
7387 C CB  . GLN B 402 ? 2.0063 1.0425 1.5522 0.4639  0.4922  0.0206  429 GLN B CB  
7388 C CG  . GLN B 402 ? 2.1271 1.1491 1.6659 0.5184  0.5177  0.0504  429 GLN B CG  
7389 C CD  . GLN B 402 ? 2.3201 1.3058 1.8302 0.5518  0.5397  0.0235  429 GLN B CD  
7390 O OE1 . GLN B 402 ? 2.4647 1.4101 1.9528 0.5309  0.5394  -0.0218 429 GLN B OE1 
7391 N NE2 . GLN B 402 ? 2.2936 1.2953 1.8031 0.6043  0.5593  0.0513  429 GLN B NE2 
7392 N N   . LYS B 403 ? 1.9925 1.1783 1.5783 0.3839  0.4254  0.0116  430 LYS B N   
7393 C CA  . LYS B 403 ? 2.0808 1.2879 1.6825 0.3398  0.4012  -0.0057 430 LYS B CA  
7394 C C   . LYS B 403 ? 1.9572 1.2489 1.5771 0.3329  0.3790  0.0229  430 LYS B C   
7395 O O   . LYS B 403 ? 1.8926 1.2077 1.5206 0.3449  0.3813  0.0593  430 LYS B O   
7396 C CB  . LYS B 403 ? 2.0491 1.1997 1.6625 0.3120  0.4063  -0.0123 430 LYS B CB  
7397 C CG  . LYS B 403 ? 2.1175 1.2517 1.7361 0.3258  0.4198  0.0250  430 LYS B CG  
7398 C CD  . LYS B 403 ? 2.1289 1.2438 1.7651 0.2899  0.4159  0.0251  430 LYS B CD  
7399 C CE  . LYS B 403 ? 2.2073 1.2977 1.8420 0.3024  0.4310  0.0611  430 LYS B CE  
7400 N NZ  . LYS B 403 ? 2.0655 1.1519 1.7161 0.2674  0.4266  0.0651  430 LYS B NZ  
7401 N N   . SER B 404 ? 1.8058 1.1409 1.4299 0.3122  0.3569  0.0070  431 SER B N   
7402 C CA  . SER B 404 ? 1.7195 1.1296 1.3566 0.3040  0.3353  0.0309  431 SER B CA  
7403 C C   . SER B 404 ? 1.6632 1.0870 1.3147 0.2672  0.3123  0.0111  431 SER B C   
7404 O O   . SER B 404 ? 1.6424 1.0405 1.2905 0.2530  0.3089  -0.0225 431 SER B O   
7405 C CB  . SER B 404 ? 1.7416 1.2063 1.3658 0.3279  0.3328  0.0407  431 SER B CB  
7406 O OG  . SER B 404 ? 1.9613 1.4127 1.5742 0.3664  0.3566  0.0555  431 SER B OG  
7407 N N   . LEU B 405 ? 1.6013 1.0658 1.2684 0.2519  0.2965  0.0324  432 LEU B N   
7408 C CA  . LEU B 405 ? 1.5431 1.0280 1.2262 0.2220  0.2744  0.0194  432 LEU B CA  
7409 C C   . LEU B 405 ? 1.5309 1.0790 1.2094 0.2231  0.2547  0.0331  432 LEU B C   
7410 O O   . LEU B 405 ? 1.4937 1.0775 1.1672 0.2354  0.2546  0.0633  432 LEU B O   
7411 C CB  . LEU B 405 ? 1.5492 1.0237 1.2509 0.2024  0.2735  0.0305  432 LEU B CB  
7412 C CG  . LEU B 405 ? 1.5191 1.0103 1.2413 0.1745  0.2541  0.0177  432 LEU B CG  
7413 C CD1 . LEU B 405 ? 1.4010 0.8708 1.1321 0.1620  0.2503  -0.0177 432 LEU B CD1 
7414 C CD2 . LEU B 405 ? 1.4180 0.8945 1.1547 0.1591  0.2594  0.0281  432 LEU B CD2 
7415 N N   . VAL B 406 ? 1.5888 1.1521 1.2689 0.2088  0.2373  0.0126  433 VAL B N   
7416 C CA  . VAL B 406 ? 1.6232 1.2415 1.2957 0.2083  0.2185  0.0238  433 VAL B CA  
7417 C C   . VAL B 406 ? 1.6189 1.2528 1.3101 0.1823  0.1961  0.0226  433 VAL B C   
7418 O O   . VAL B 406 ? 1.5456 1.1568 1.2522 0.1666  0.1906  -0.0011 433 VAL B O   
7419 C CB  . VAL B 406 ? 1.6332 1.2579 1.2843 0.2181  0.2177  0.0031  433 VAL B CB  
7420 C CG1 . VAL B 406 ? 1.5136 1.1966 1.1550 0.2164  0.1991  0.0180  433 VAL B CG1 
7421 C CG2 . VAL B 406 ? 1.6464 1.2481 1.2783 0.2471  0.2437  0.0017  433 VAL B CG2 
7422 N N   . PHE B 407 ? 1.5583 1.2309 1.2491 0.1778  0.1834  0.0487  434 PHE B N   
7423 C CA  . PHE B 407 ? 1.4212 1.1058 1.1266 0.1566  0.1634  0.0511  434 PHE B CA  
7424 C C   . PHE B 407 ? 1.4828 1.2108 1.1759 0.1542  0.1437  0.0614  434 PHE B C   
7425 O O   . PHE B 407 ? 1.4317 1.1895 1.1059 0.1672  0.1466  0.0761  434 PHE B O   
7426 C CB  . PHE B 407 ? 1.3656 1.0473 1.0771 0.1483  0.1658  0.0730  434 PHE B CB  
7427 C CG  . PHE B 407 ? 1.4859 1.1249 1.2128 0.1423  0.1806  0.0623  434 PHE B CG  
7428 C CD1 . PHE B 407 ? 1.6548 1.2664 1.4001 0.1347  0.1828  0.0340  434 PHE B CD1 
7429 C CD2 . PHE B 407 ? 1.4453 1.0746 1.1678 0.1423  0.1919  0.0817  434 PHE B CD2 
7430 C CE1 . PHE B 407 ? 1.6227 1.1978 1.3833 0.1272  0.1980  0.0256  434 PHE B CE1 
7431 C CE2 . PHE B 407 ? 1.5201 1.1106 1.2539 0.1359  0.2069  0.0734  434 PHE B CE2 
7432 C CZ  . PHE B 407 ? 1.5549 1.1182 1.3086 0.1283  0.2109  0.0455  434 PHE B CZ  
7433 N N   . GLU B 408 ? 1.5364 1.2689 1.2414 0.1384  0.1243  0.0551  435 GLU B N   
7434 C CA  . GLU B 408 ? 1.4812 1.2496 1.1753 0.1324  0.1039  0.0702  435 GLU B CA  
7435 C C   . GLU B 408 ? 1.4715 1.2413 1.1712 0.1190  0.0960  0.0918  435 GLU B C   
7436 O O   . GLU B 408 ? 1.6060 1.3568 1.3112 0.1172  0.1083  0.0979  435 GLU B O   
7437 C CB  . GLU B 408 ? 1.5863 1.3580 1.2860 0.1262  0.0865  0.0502  435 GLU B CB  
7438 C CG  . GLU B 408 ? 1.5258 1.3011 1.2075 0.1370  0.0919  0.0307  435 GLU B CG  
7439 C CD  . GLU B 408 ? 1.7028 1.4906 1.3831 0.1287  0.0705  0.0151  435 GLU B CD  
7440 O OE1 . GLU B 408 ? 1.9648 1.7463 1.6708 0.1165  0.0560  0.0093  435 GLU B OE1 
7441 O OE2 . GLU B 408 ? 1.7460 1.5520 1.3989 0.1351  0.0684  0.0093  435 GLU B OE2 
7442 N N   . ASP B 409 ? 1.4844 1.2731 1.1792 0.1089  0.0759  0.1036  436 ASP B N   
7443 C CA  . ASP B 409 ? 1.3762 1.1639 1.0677 0.0953  0.0687  0.1251  436 ASP B CA  
7444 C C   . ASP B 409 ? 1.4572 1.2196 1.1670 0.0842  0.0572  0.1172  436 ASP B C   
7445 O O   . ASP B 409 ? 1.5692 1.3196 1.2742 0.0726  0.0536  0.1309  436 ASP B O   
7446 C CB  . ASP B 409 ? 1.3312 1.1571 0.9994 0.0906  0.0566  0.1510  436 ASP B CB  
7447 C CG  . ASP B 409 ? 1.4291 1.2749 1.0905 0.0921  0.0408  0.1469  436 ASP B CG  
7448 O OD1 . ASP B 409 ? 1.5292 1.3621 1.2034 0.0972  0.0381  0.1232  436 ASP B OD1 
7449 O OD2 . ASP B 409 ? 1.5461 1.4225 1.1881 0.0863  0.0307  0.1684  436 ASP B OD2 
7450 N N   . ASP B 410 ? 1.4964 1.2508 1.2269 0.0874  0.0518  0.0954  437 ASP B N   
7451 C CA  . ASP B 410 ? 1.4699 1.2058 1.2241 0.0810  0.0418  0.0887  437 ASP B CA  
7452 C C   . ASP B 410 ? 1.4261 1.1458 1.2118 0.0844  0.0518  0.0618  437 ASP B C   
7453 O O   . ASP B 410 ? 1.6503 1.3820 1.4494 0.0869  0.0421  0.0465  437 ASP B O   
7454 C CB  . ASP B 410 ? 1.7244 1.4789 1.4751 0.0793  0.0173  0.0965  437 ASP B CB  
7455 C CG  . ASP B 410 ? 2.0966 1.8797 1.8371 0.0859  0.0095  0.0885  437 ASP B CG  
7456 O OD1 . ASP B 410 ? 2.0604 1.8458 1.7954 0.0926  0.0243  0.0757  437 ASP B OD1 
7457 O OD2 . ASP B 410 ? 2.1371 1.9378 1.8722 0.0845  -0.0112 0.0952  437 ASP B OD2 
7458 N N   . LEU B 411 ? 1.4784 1.1721 1.2743 0.0821  0.0708  0.0570  438 LEU B N   
7459 C CA  . LEU B 411 ? 1.5684 1.2463 1.3944 0.0823  0.0832  0.0336  438 LEU B CA  
7460 C C   . LEU B 411 ? 1.3836 1.0333 1.2201 0.0769  0.1003  0.0342  438 LEU B C   
7461 O O   . LEU B 411 ? 1.5277 1.1676 1.3398 0.0741  0.1081  0.0502  438 LEU B O   
7462 C CB  . LEU B 411 ? 1.5134 1.1896 1.3300 0.0880  0.0961  0.0225  438 LEU B CB  
7463 C CG  . LEU B 411 ? 1.5184 1.1910 1.3052 0.0941  0.1105  0.0387  438 LEU B CG  
7464 C CD1 . LEU B 411 ? 1.5588 1.2007 1.3529 0.0924  0.1336  0.0354  438 LEU B CD1 
7465 C CD2 . LEU B 411 ? 1.5776 1.2649 1.3449 0.1053  0.1117  0.0351  438 LEU B CD2 
7466 N N   . ARG B 412 ? 1.3894 1.0297 1.2618 0.0744  0.1059  0.0172  439 ARG B N   
7467 C CA  . ARG B 412 ? 1.4252 1.0398 1.3094 0.0695  0.1251  0.0146  439 ARG B CA  
7468 C C   . ARG B 412 ? 1.3950 0.9956 1.2931 0.0668  0.1464  -0.0002 439 ARG B C   
7469 O O   . ARG B 412 ? 1.5131 1.1229 1.4266 0.0670  0.1438  -0.0150 439 ARG B O   
7470 C CB  . ARG B 412 ? 1.4752 1.0903 1.3927 0.0698  0.1193  0.0083  439 ARG B CB  
7471 C CG  . ARG B 412 ? 1.5089 1.1476 1.4683 0.0719  0.1091  -0.0087 439 ARG B CG  
7472 C CD  . ARG B 412 ? 1.4618 1.1001 1.4633 0.0739  0.1138  -0.0161 439 ARG B CD  
7473 N NE  . ARG B 412 ? 1.4155 1.0366 1.4021 0.0783  0.1112  -0.0021 439 ARG B NE  
7474 C CZ  . ARG B 412 ? 1.6591 1.2724 1.6741 0.0840  0.1176  -0.0057 439 ARG B CZ  
7475 N NH1 . ARG B 412 ? 1.5761 1.2051 1.6411 0.0859  0.1269  -0.0210 439 ARG B NH1 
7476 N NH2 . ARG B 412 ? 1.7998 1.3887 1.7927 0.0874  0.1156  0.0063  439 ARG B NH2 
7477 N N   . PHE B 413 ? 1.4277 1.0035 1.3174 0.0623  0.1674  0.0039  440 PHE B N   
7478 C CA  . PHE B 413 ? 1.3356 0.8923 1.2297 0.0589  0.1897  -0.0043 440 PHE B CA  
7479 C C   . PHE B 413 ? 1.2891 0.8369 1.2212 0.0513  0.2049  -0.0197 440 PHE B C   
7480 O O   . PHE B 413 ? 1.3281 0.8749 1.2720 0.0501  0.2067  -0.0191 440 PHE B O   
7481 C CB  . PHE B 413 ? 1.2699 0.8079 1.1264 0.0589  0.2035  0.0139  440 PHE B CB  
7482 C CG  . PHE B 413 ? 1.3367 0.8890 1.1612 0.0674  0.1926  0.0302  440 PHE B CG  
7483 C CD1 . PHE B 413 ? 1.2761 0.8471 1.0812 0.0678  0.1748  0.0456  440 PHE B CD1 
7484 C CD2 . PHE B 413 ? 1.3601 0.9065 1.1746 0.0753  0.2017  0.0305  440 PHE B CD2 
7485 C CE1 . PHE B 413 ? 1.3933 0.9843 1.1726 0.0750  0.1662  0.0618  440 PHE B CE1 
7486 C CE2 . PHE B 413 ? 1.4784 1.0424 1.2668 0.0862  0.1943  0.0460  440 PHE B CE2 
7487 C CZ  . PHE B 413 ? 1.6039 1.1941 1.3763 0.0856  0.1766  0.0620  440 PHE B CZ  
7488 N N   . GLU B 414 ? 1.3371 0.8775 1.2881 0.0459  0.2172  -0.0336 441 GLU B N   
7489 C CA  . GLU B 414 ? 1.3121 0.8470 1.3003 0.0361  0.2351  -0.0468 441 GLU B CA  
7490 C C   . GLU B 414 ? 1.3362 0.8405 1.3034 0.0311  0.2618  -0.0375 441 GLU B C   
7491 O O   . GLU B 414 ? 1.3244 0.8111 1.2511 0.0345  0.2664  -0.0222 441 GLU B O   
7492 C CB  . GLU B 414 ? 1.2728 0.8113 1.2888 0.0275  0.2367  -0.0654 441 GLU B CB  
7493 C CG  . GLU B 414 ? 1.4058 0.9809 1.4606 0.0261  0.2142  -0.0794 441 GLU B CG  
7494 C CD  . GLU B 414 ? 1.5153 1.1100 1.6209 0.0207  0.2210  -0.0872 441 GLU B CD  
7495 O OE1 . GLU B 414 ? 1.4960 1.0735 1.6108 0.0133  0.2472  -0.0881 441 GLU B OE1 
7496 O OE2 . GLU B 414 ? 1.4122 1.0413 1.5488 0.0251  0.2008  -0.0912 441 GLU B OE2 
7497 N N   . ILE B 415 ? 1.2922 0.7942 1.2883 0.0234  0.2796  -0.0458 442 ILE B N   
7498 C CA  . ILE B 415 ? 1.3546 0.8285 1.3300 0.0168  0.3065  -0.0381 442 ILE B CA  
7499 C C   . ILE B 415 ? 1.4545 0.9045 1.4159 0.0108  0.3208  -0.0354 442 ILE B C   
7500 O O   . ILE B 415 ? 1.4227 0.8754 1.4086 0.0059  0.3192  -0.0482 442 ILE B O   
7501 C CB  . ILE B 415 ? 1.4091 0.8894 1.4222 0.0104  0.3249  -0.0496 442 ILE B CB  
7502 C CG1 . ILE B 415 ? 1.3361 0.7873 1.3202 0.0033  0.3533  -0.0412 442 ILE B CG1 
7503 C CG2 . ILE B 415 ? 1.2904 0.7891 1.3568 0.0010  0.3296  -0.0669 442 ILE B CG2 
7504 C CD1 . ILE B 415 ? 1.3603 0.8179 1.3741 0.0004  0.3733  -0.0516 442 ILE B CD1 
7505 N N   . PHE B 416 ? 1.3541 0.7784 1.2733 0.0110  0.3341  -0.0179 443 PHE B N   
7506 C CA  . PHE B 416 ? 1.4053 0.8015 1.3046 0.0092  0.3479  -0.0096 443 PHE B CA  
7507 C C   . PHE B 416 ? 1.4704 0.8691 1.3633 0.0199  0.3313  -0.0105 443 PHE B C   
7508 O O   . PHE B 416 ? 1.5094 0.8871 1.4077 0.0171  0.3403  -0.0169 443 PHE B O   
7509 C CB  . PHE B 416 ? 1.3438 0.7238 1.2719 -0.0062 0.3722  -0.0212 443 PHE B CB  
7510 C CG  . PHE B 416 ? 1.3259 0.7109 1.2700 -0.0162 0.3903  -0.0253 443 PHE B CG  
7511 C CD1 . PHE B 416 ? 1.4171 0.7870 1.3229 -0.0166 0.4029  -0.0099 443 PHE B CD1 
7512 C CD2 . PHE B 416 ? 1.3192 0.7262 1.3165 -0.0253 0.3954  -0.0447 443 PHE B CD2 
7513 C CE1 . PHE B 416 ? 1.3684 0.7400 1.2847 -0.0248 0.4224  -0.0158 443 PHE B CE1 
7514 C CE2 . PHE B 416 ? 1.3255 0.7393 1.3397 -0.0316 0.4154  -0.0487 443 PHE B CE2 
7515 C CZ  . PHE B 416 ? 1.3421 0.7357 1.3138 -0.0308 0.4301  -0.0352 443 PHE B CZ  
7516 N N   . PHE B 417 ? 1.4673 0.8893 1.3464 0.0316  0.3082  -0.0045 444 PHE B N   
7517 C CA  . PHE B 417 ? 1.3483 0.7765 1.2202 0.0427  0.2937  -0.0068 444 PHE B CA  
7518 C C   . PHE B 417 ? 1.4173 0.8167 1.2596 0.0516  0.3070  0.0071  444 PHE B C   
7519 O O   . PHE B 417 ? 1.5536 0.9370 1.3984 0.0556  0.3096  -0.0031 444 PHE B O   
7520 C CB  . PHE B 417 ? 1.3943 0.8539 1.2521 0.0529  0.2692  0.0019  444 PHE B CB  
7521 C CG  . PHE B 417 ? 1.4126 0.8808 1.2559 0.0661  0.2573  0.0027  444 PHE B CG  
7522 C CD1 . PHE B 417 ? 1.4854 0.9640 1.3486 0.0653  0.2457  -0.0181 444 PHE B CD1 
7523 C CD2 . PHE B 417 ? 1.2892 0.7574 1.0986 0.0795  0.2582  0.0243  444 PHE B CD2 
7524 C CE1 . PHE B 417 ? 1.3350 0.8192 1.1800 0.0776  0.2372  -0.0195 444 PHE B CE1 
7525 C CE2 . PHE B 417 ? 1.3815 0.8592 1.1784 0.0941  0.2508  0.0244  444 PHE B CE2 
7526 C CZ  . PHE B 417 ? 1.4056 0.8888 1.2180 0.0932  0.2413  0.0015  444 PHE B CZ  
7527 N N   . LYS B 418 ? 1.4192 0.8102 1.2319 0.0549  0.3155  0.0307  445 LYS B N   
7528 C CA  . LYS B 418 ? 1.3419 0.7114 1.1267 0.0678  0.3256  0.0493  445 LYS B CA  
7529 C C   . LYS B 418 ? 1.4913 0.8174 1.2838 0.0612  0.3489  0.0423  445 LYS B C   
7530 O O   . LYS B 418 ? 1.5315 0.8337 1.3174 0.0722  0.3544  0.0410  445 LYS B O   
7531 C CB  . LYS B 418 ? 1.4555 0.8326 1.2078 0.0704  0.3261  0.0780  445 LYS B CB  
7532 C CG  . LYS B 418 ? 1.5279 0.8931 1.2533 0.0876  0.3328  0.1028  445 LYS B CG  
7533 C CD  . LYS B 418 ? 1.5257 0.9071 1.2201 0.0868  0.3291  0.1318  445 LYS B CD  
7534 C CE  . LYS B 418 ? 1.5013 0.8763 1.1734 0.1062  0.3353  0.1600  445 LYS B CE  
7535 N NZ  . LYS B 418 ? 1.6344 1.0308 1.2763 0.1027  0.3290  0.1899  445 LYS B NZ  
7536 N N   . ARG B 419 ? 1.5393 0.8523 1.3446 0.0431  0.3644  0.0378  446 ARG B N   
7537 C CA  . ARG B 419 ? 1.4779 0.7494 1.2908 0.0328  0.3876  0.0328  446 ARG B CA  
7538 C C   . ARG B 419 ? 1.5161 0.7798 1.3596 0.0256  0.3847  0.0048  446 ARG B C   
7539 O O   . ARG B 419 ? 1.6656 0.8888 1.5048 0.0243  0.3979  0.0013  446 ARG B O   
7540 C CB  . ARG B 419 ? 1.4747 0.7405 1.2961 0.0133  0.4059  0.0336  446 ARG B CB  
7541 C CG  . ARG B 419 ? 1.4536 0.6998 1.2361 0.0150  0.4206  0.0622  446 ARG B CG  
7542 C CD  . ARG B 419 ? 1.4732 0.7058 1.2635 -0.0062 0.4445  0.0597  446 ARG B CD  
7543 N NE  . ARG B 419 ? 1.4887 0.7534 1.2969 -0.0149 0.4402  0.0463  446 ARG B NE  
7544 C CZ  . ARG B 419 ? 1.5389 0.8024 1.3619 -0.0316 0.4605  0.0386  446 ARG B CZ  
7545 N NH1 . ARG B 419 ? 1.6267 0.8608 1.4496 -0.0451 0.4863  0.0431  446 ARG B NH1 
7546 N NH2 . ARG B 419 ? 1.4776 0.7687 1.3155 -0.0343 0.4563  0.0266  446 ARG B NH2 
7547 N N   . ARG B 420 ? 1.4522 0.7523 1.3245 0.0201  0.3667  -0.0149 447 ARG B N   
7548 C CA  . ARG B 420 ? 1.5323 0.8309 1.4355 0.0082  0.3620  -0.0423 447 ARG B CA  
7549 C C   . ARG B 420 ? 1.5997 0.8813 1.4826 0.0222  0.3535  -0.0483 447 ARG B C   
7550 O O   . ARG B 420 ? 1.6161 0.8644 1.5039 0.0127  0.3617  -0.0645 447 ARG B O   
7551 C CB  . ARG B 420 ? 1.4840 0.8305 1.4237 0.0006  0.3433  -0.0582 447 ARG B CB  
7552 C CG  . ARG B 420 ? 1.3886 0.7467 1.3609 -0.0165 0.3572  -0.0617 447 ARG B CG  
7553 C CD  . ARG B 420 ? 1.3397 0.7456 1.3428 -0.0155 0.3390  -0.0700 447 ARG B CD  
7554 N NE  . ARG B 420 ? 1.4844 0.9152 1.5255 -0.0243 0.3227  -0.0923 447 ARG B NE  
7555 C CZ  . ARG B 420 ? 1.5399 1.0141 1.6167 -0.0244 0.3060  -0.1009 447 ARG B CZ  
7556 N NH1 . ARG B 420 ? 1.3523 0.8445 1.4314 -0.0152 0.3049  -0.0908 447 ARG B NH1 
7557 N NH2 . ARG B 420 ? 1.6538 1.1523 1.7633 -0.0341 0.2897  -0.1196 447 ARG B NH2 
7558 N N   . LEU B 421 ? 1.5891 0.8919 1.4477 0.0437  0.3384  -0.0361 448 LEU B N   
7559 C CA  . LEU B 421 ? 1.6267 0.9153 1.4639 0.0600  0.3333  -0.0417 448 LEU B CA  
7560 C C   . LEU B 421 ? 1.6547 0.8922 1.4643 0.0728  0.3554  -0.0270 448 LEU B C   
7561 O O   . LEU B 421 ? 1.6241 0.8248 1.4235 0.0774  0.3622  -0.0407 448 LEU B O   
7562 C CB  . LEU B 421 ? 1.5442 0.8752 1.3654 0.0790  0.3127  -0.0308 448 LEU B CB  
7563 C CG  . LEU B 421 ? 1.5640 0.8891 1.3638 0.0970  0.3076  -0.0387 448 LEU B CG  
7564 C CD1 . LEU B 421 ? 1.4658 0.7808 1.2806 0.0820  0.3010  -0.0725 448 LEU B CD1 
7565 C CD2 . LEU B 421 ? 1.4199 0.7924 1.2052 0.1136  0.2889  -0.0245 448 LEU B CD2 
7566 N N   . MET B 422 ? 1.6456 0.8776 1.4406 0.0786  0.3668  0.0009  449 MET B N   
7567 C CA  . MET B 422 ? 1.7008 0.8863 1.4699 0.0933  0.3867  0.0200  449 MET B CA  
7568 C C   . MET B 422 ? 1.8133 0.9418 1.5910 0.0754  0.4072  0.0057  449 MET B C   
7569 O O   . MET B 422 ? 1.8985 0.9765 1.6568 0.0880  0.4215  0.0089  449 MET B O   
7570 C CB  . MET B 422 ? 1.5861 0.7830 1.3374 0.0994  0.3919  0.0540  449 MET B CB  
7571 C CG  . MET B 422 ? 1.5886 0.8280 1.3209 0.1225  0.3760  0.0758  449 MET B CG  
7572 S SD  . MET B 422 ? 1.8623 1.1117 1.5683 0.1277  0.3811  0.1172  449 MET B SD  
7573 C CE  . MET B 422 ? 2.0137 1.1956 1.7050 0.1363  0.4088  0.1312  449 MET B CE  
7574 N N   . ASN B 423 ? 1.8385 0.9734 1.6457 0.0464  0.4099  -0.0096 450 ASN B N   
7575 C CA  . ASN B 423 ? 1.9126 0.9993 1.7326 0.0238  0.4283  -0.0244 450 ASN B CA  
7576 C C   . ASN B 423 ? 1.9555 1.0267 1.7854 0.0154  0.4203  -0.0570 450 ASN B C   
7577 O O   . ASN B 423 ? 2.0551 1.0729 1.8846 0.0003  0.4357  -0.0689 450 ASN B O   
7578 C CB  . ASN B 423 ? 1.7908 0.8976 1.6425 -0.0046 0.4354  -0.0284 450 ASN B CB  
7579 C CG  . ASN B 423 ? 1.7130 0.8251 1.5474 -0.0001 0.4470  0.0016  450 ASN B CG  
7580 O OD1 . ASN B 423 ? 1.7945 0.8860 1.5938 0.0204  0.4526  0.0275  450 ASN B OD1 
7581 N ND2 . ASN B 423 ? 1.6684 0.8099 1.5266 -0.0185 0.4508  -0.0017 450 ASN B ND2 
7582 N N   . LEU B 424 ? 1.8026 0.9170 1.6384 0.0229  0.3964  -0.0716 451 LEU B N   
7583 C CA  . LEU B 424 ? 1.8191 0.9161 1.6523 0.0187  0.3881  -0.1010 451 LEU B CA  
7584 C C   . LEU B 424 ? 1.8660 0.9171 1.6577 0.0473  0.3977  -0.0948 451 LEU B C   
7585 O O   . LEU B 424 ? 1.8769 0.8741 1.6558 0.0415  0.4070  -0.1149 451 LEU B O   
7586 C CB  . LEU B 424 ? 1.5806 0.7397 1.4304 0.0175  0.3593  -0.1166 451 LEU B CB  
7587 C CG  . LEU B 424 ? 1.6092 0.7564 1.4538 0.0092  0.3478  -0.1489 451 LEU B CG  
7588 C CD1 . LEU B 424 ? 1.6382 0.7683 1.5129 -0.0283 0.3510  -0.1734 451 LEU B CD1 
7589 C CD2 . LEU B 424 ? 1.6888 0.8963 1.5371 0.0169  0.3193  -0.1560 451 LEU B CD2 
7590 N N   . MET B 425 ? 1.7885 0.8598 1.5592 0.0782  0.3965  -0.0671 452 MET B N   
7591 C CA  . MET B 425 ? 1.8489 0.8850 1.5846 0.1106  0.4069  -0.0578 452 MET B CA  
7592 C C   . MET B 425 ? 2.0295 0.9918 1.7494 0.1141  0.4344  -0.0451 452 MET B C   
7593 O O   . MET B 425 ? 1.8192 0.7290 1.5136 0.1336  0.4473  -0.0499 452 MET B O   
7594 C CB  . MET B 425 ? 1.6497 0.7364 1.3732 0.1403  0.3975  -0.0282 452 MET B CB  
7595 C CG  . MET B 425 ? 1.8038 0.9579 1.5382 0.1382  0.3711  -0.0380 452 MET B CG  
7596 S SD  . MET B 425 ? 1.9190 1.0666 1.6439 0.1383  0.3608  -0.0762 452 MET B SD  
7597 C CE  . MET B 425 ? 1.6588 0.7866 1.3456 0.1829  0.3750  -0.0607 452 MET B CE  
7598 N N   . ARG B 426 ? 2.0150 0.9692 1.7472 0.0965  0.4450  -0.0287 453 ARG B N   
7599 C CA  . ARG B 426 ? 2.1043 0.9846 1.8222 0.0942  0.4710  -0.0176 453 ARG B CA  
7600 C C   . ARG B 426 ? 2.1336 0.9629 1.8626 0.0614  0.4793  -0.0505 453 ARG B C   
7601 O O   . ARG B 426 ? 2.1595 0.9133 1.8706 0.0603  0.5009  -0.0479 453 ARG B O   
7602 C CB  . ARG B 426 ? 2.0720 0.9624 1.7939 0.0862  0.4805  0.0137  453 ARG B CB  
7603 C CG  . ARG B 426 ? 2.1864 1.0225 1.8785 0.1084  0.5017  0.0471  453 ARG B CG  
7604 C CD  . ARG B 426 ? 2.2444 1.1059 1.9326 0.1057  0.5057  0.0820  453 ARG B CD  
7605 N NE  . ARG B 426 ? 2.3450 1.2846 2.0388 0.1136  0.4840  0.0911  453 ARG B NE  
7606 C CZ  . ARG B 426 ? 2.3125 1.2959 2.0229 0.0907  0.4768  0.0893  453 ARG B CZ  
7607 N NH1 . ARG B 426 ? 2.1011 1.0660 1.8270 0.0596  0.4904  0.0805  453 ARG B NH1 
7608 N NH2 . ARG B 426 ? 2.0419 1.0880 1.7529 0.0990  0.4569  0.0967  453 ARG B NH2 
7609 N N   . ASP B 427 ? 2.0385 0.9071 1.7964 0.0338  0.4619  -0.0804 454 ASP B N   
7610 C CA  . ASP B 427 ? 2.0043 0.8327 1.7736 0.0002  0.4655  -0.1139 454 ASP B CA  
7611 C C   . ASP B 427 ? 2.0291 0.8262 1.7727 0.0114  0.4595  -0.1414 454 ASP B C   
7612 O O   . ASP B 427 ? 2.1808 0.9050 1.9082 -0.0018 0.4734  -0.1598 454 ASP B O   
7613 C CB  . ASP B 427 ? 1.9627 0.8522 1.7781 -0.0348 0.4490  -0.1319 454 ASP B CB  
7614 C CG  . ASP B 427 ? 2.1269 1.0220 1.9679 -0.0576 0.4641  -0.1154 454 ASP B CG  
7615 O OD1 . ASP B 427 ? 2.1847 1.0410 2.0042 -0.0460 0.4849  -0.0874 454 ASP B OD1 
7616 O OD2 . ASP B 427 ? 1.9992 0.9391 1.8817 -0.0865 0.4557  -0.1297 454 ASP B OD2 
7617 N N   . VAL B 428 ? 2.0534 0.9019 1.7899 0.0343  0.4399  -0.1449 455 VAL B N   
7618 C CA  . VAL B 428 ? 1.9801 0.8021 1.6867 0.0482  0.4360  -0.1703 455 VAL B CA  
7619 C C   . VAL B 428 ? 2.2263 0.9714 1.8930 0.0804  0.4617  -0.1576 455 VAL B C   
7620 O O   . VAL B 428 ? 2.3303 1.0097 1.9698 0.0799  0.4717  -0.1832 455 VAL B O   
7621 C CB  . VAL B 428 ? 1.8688 0.7666 1.5750 0.0680  0.4117  -0.1704 455 VAL B CB  
7622 C CG1 . VAL B 428 ? 1.9517 0.8217 1.6205 0.0874  0.4118  -0.1931 455 VAL B CG1 
7623 C CG2 . VAL B 428 ? 1.8097 0.7743 1.5538 0.0369  0.3859  -0.1859 455 VAL B CG2 
7624 N N   . GLU B 429 ? 2.2684 1.0193 1.9301 0.1091  0.4729  -0.1177 456 GLU B N   
7625 C CA  . GLU B 429 ? 2.3105 0.9949 1.9384 0.1450  0.4969  -0.0998 456 GLU B CA  
7626 C C   . GLU B 429 ? 2.4420 1.0312 2.0601 0.1251  0.5207  -0.1053 456 GLU B C   
7627 O O   . GLU B 429 ? 2.5059 1.0165 2.0922 0.1415  0.5386  -0.1160 456 GLU B O   
7628 C CB  . GLU B 429 ? 2.2751 0.9989 1.9036 0.1771  0.4993  -0.0528 456 GLU B CB  
7629 C CG  . GLU B 429 ? 2.5032 1.1664 2.1025 0.2175  0.5233  -0.0272 456 GLU B CG  
7630 C CD  . GLU B 429 ? 2.6528 1.3511 2.2559 0.2385  0.5253  0.0219  456 GLU B CD  
7631 O OE1 . GLU B 429 ? 2.7979 1.5140 2.4180 0.2113  0.5225  0.0353  456 GLU B OE1 
7632 O OE2 . GLU B 429 ? 2.7146 1.4256 2.3036 0.2818  0.5296  0.0471  456 GLU B OE2 
7633 N N   . ARG B 430 ? 2.4195 1.0121 2.0633 0.0898  0.5229  -0.0979 457 ARG B N   
7634 C CA  . ARG B 430 ? 2.4329 0.9373 2.0681 0.0684  0.5466  -0.0979 457 ARG B CA  
7635 C C   . ARG B 430 ? 2.5560 1.0021 2.1829 0.0374  0.5481  -0.1431 457 ARG B C   
7636 O O   . ARG B 430 ? 2.7761 1.1331 2.3871 0.0221  0.5694  -0.1466 457 ARG B O   
7637 C CB  . ARG B 430 ? 2.4717 1.0040 2.1379 0.0360  0.5490  -0.0795 457 ARG B CB  
7638 C CG  . ARG B 430 ? 2.4375 0.8857 2.0908 0.0229  0.5770  -0.0618 457 ARG B CG  
7639 C CD  . ARG B 430 ? 2.2269 0.7112 1.9082 -0.0061 0.5810  -0.0413 457 ARG B CD  
7640 N NE  . ARG B 430 ? 2.3271 0.8695 2.0068 0.0219  0.5760  -0.0039 457 ARG B NE  
7641 C CZ  . ARG B 430 ? 2.4359 1.0676 2.1414 0.0169  0.5569  -0.0034 457 ARG B CZ  
7642 N NH1 . ARG B 430 ? 2.3994 1.0779 2.1380 -0.0113 0.5405  -0.0357 457 ARG B NH1 
7643 N NH2 . ARG B 430 ? 2.0965 0.7703 1.7935 0.0405  0.5536  0.0308  457 ARG B NH2 
7644 N N   . GLU B 431 ? 2.5722 1.0635 2.2064 0.0266  0.5255  -0.1768 458 GLU B N   
7645 C CA  . GLU B 431 ? 2.6111 1.0546 2.2347 -0.0058 0.5227  -0.2218 458 GLU B CA  
7646 C C   . GLU B 431 ? 2.5418 0.9453 2.1207 0.0247  0.5249  -0.2443 458 GLU B C   
7647 O O   . GLU B 431 ? 2.7172 1.0738 2.2777 -0.0008 0.5229  -0.2843 458 GLU B O   
7648 C CB  . GLU B 431 ? 2.5725 1.0952 2.2368 -0.0469 0.4944  -0.2462 458 GLU B CB  
7649 C CG  . GLU B 431 ? 2.6463 1.2130 2.3575 -0.0767 0.4940  -0.2274 458 GLU B CG  
7650 C CD  . GLU B 431 ? 2.7505 1.2366 2.4582 -0.1007 0.5210  -0.2189 458 GLU B CD  
7651 O OE1 . GLU B 431 ? 2.6989 1.1170 2.3924 -0.1299 0.5275  -0.2478 458 GLU B OE1 
7652 O OE2 . GLU B 431 ? 2.8244 1.3130 2.5401 -0.0920 0.5357  -0.1830 458 GLU B OE2 
7653 N N   . GLY B 432 ? 2.4350 0.8575 1.9956 0.0770  0.5293  -0.2204 459 GLY B N   
7654 C CA  . GLY B 432 ? 2.5905 0.9770 2.1086 0.1105  0.5358  -0.2399 459 GLY B CA  
7655 C C   . GLY B 432 ? 2.6317 1.0626 2.1455 0.0926  0.5113  -0.2801 459 GLY B C   
7656 O O   . GLY B 432 ? 2.5749 0.9468 2.0495 0.0935  0.5179  -0.3147 459 GLY B O   
7657 N N   . LEU B 433 ? 2.4432 0.9747 1.9937 0.0764  0.4834  -0.2760 460 LEU B N   
7658 C CA  . LEU B 433 ? 2.3560 0.9357 1.9057 0.0561  0.4569  -0.3106 460 LEU B CA  
7659 C C   . LEU B 433 ? 2.4437 1.0439 1.9587 0.0990  0.4559  -0.3136 460 LEU B C   
7660 O O   . LEU B 433 ? 2.4182 1.0675 1.9393 0.1368  0.4572  -0.2799 460 LEU B O   
7661 C CB  . LEU B 433 ? 2.3196 0.9985 1.9205 0.0305  0.4289  -0.3008 460 LEU B CB  
7662 C CG  . LEU B 433 ? 2.3568 1.0896 1.9675 -0.0001 0.3980  -0.3337 460 LEU B CG  
7663 C CD1 . LEU B 433 ? 2.3241 0.9961 1.9256 -0.0448 0.3984  -0.3734 460 LEU B CD1 
7664 C CD2 . LEU B 433 ? 2.2107 1.0389 1.8750 -0.0163 0.3740  -0.3164 460 LEU B CD2 
7665 N N   . ASP B 434 ? 2.5119 1.0752 1.9888 0.0914  0.4542  -0.3542 461 ASP B N   
7666 C CA  . ASP B 434 ? 2.5827 1.1674 2.0234 0.1273  0.4535  -0.3631 461 ASP B CA  
7667 C C   . ASP B 434 ? 2.5963 1.2898 2.0611 0.1149  0.4188  -0.3623 461 ASP B C   
7668 O O   . ASP B 434 ? 2.7190 1.4296 2.1775 0.0821  0.3972  -0.3955 461 ASP B O   
7669 C CB  . ASP B 434 ? 2.6476 1.1470 2.0333 0.1208  0.4657  -0.4093 461 ASP B CB  
7670 C CG  . ASP B 434 ? 2.7247 1.2401 2.0678 0.1605  0.4705  -0.4196 461 ASP B CG  
7671 O OD1 . ASP B 434 ? 2.7179 1.3004 2.0743 0.1988  0.4701  -0.3859 461 ASP B OD1 
7672 O OD2 . ASP B 434 ? 2.7633 1.2245 2.0580 0.1517  0.4752  -0.4621 461 ASP B OD2 
7673 N N   . TRP B 435 ? 2.4242 1.1914 1.9157 0.1403  0.4125  -0.3230 462 TRP B N   
7674 C CA  . TRP B 435 ? 2.3533 1.2203 1.8711 0.1297  0.3808  -0.3157 462 TRP B CA  
7675 C C   . TRP B 435 ? 2.2411 1.1598 1.7414 0.1719  0.3809  -0.2959 462 TRP B C   
7676 O O   . TRP B 435 ? 2.1401 1.0377 1.6267 0.2115  0.4045  -0.2734 462 TRP B O   
7677 C CB  . TRP B 435 ? 2.2493 1.1637 1.8210 0.1116  0.3694  -0.2870 462 TRP B CB  
7678 C CG  . TRP B 435 ? 2.1759 1.0966 1.7576 0.1443  0.3861  -0.2439 462 TRP B CG  
7679 C CD1 . TRP B 435 ? 2.0879 0.9484 1.6706 0.1516  0.4109  -0.2272 462 TRP B CD1 
7680 C CD2 . TRP B 435 ? 2.0829 1.0752 1.6735 0.1719  0.3777  -0.2108 462 TRP B CD2 
7681 N NE1 . TRP B 435 ? 1.9526 0.8460 1.5438 0.1827  0.4172  -0.1856 462 TRP B NE1 
7682 C CE2 . TRP B 435 ? 1.8986 0.8730 1.4953 0.1944  0.3971  -0.1757 462 TRP B CE2 
7683 C CE3 . TRP B 435 ? 2.0456 1.1147 1.6382 0.1779  0.3552  -0.2064 462 TRP B CE3 
7684 C CZ2 . TRP B 435 ? 1.8752 0.9083 1.4805 0.2205  0.3934  -0.1381 462 TRP B CZ2 
7685 C CZ3 . TRP B 435 ? 1.9200 1.0434 1.5213 0.2034  0.3532  -0.1690 462 TRP B CZ3 
7686 C CH2 . TRP B 435 ? 2.0404 1.1469 1.6483 0.2235  0.3716  -0.1361 462 TRP B CH2 
7687 N N   . ASP B 436 ? 2.1984 1.1884 1.7013 0.1626  0.3540  -0.3023 463 ASP B N   
7688 C CA  . ASP B 436 ? 2.0301 1.0801 1.5190 0.1953  0.3503  -0.2838 463 ASP B CA  
7689 C C   . ASP B 436 ? 1.9608 1.0998 1.4878 0.1881  0.3244  -0.2545 463 ASP B C   
7690 O O   . ASP B 436 ? 1.8816 1.0643 1.4122 0.2163  0.3276  -0.2223 463 ASP B O   
7691 C CB  . ASP B 436 ? 2.0962 1.1459 1.5403 0.1943  0.3439  -0.3184 463 ASP B CB  
7692 C CG  . ASP B 436 ? 2.3009 1.2573 1.6984 0.2044  0.3716  -0.3504 463 ASP B CG  
7693 O OD1 . ASP B 436 ? 2.3650 1.2711 1.7570 0.2347  0.4012  -0.3352 463 ASP B OD1 
7694 O OD2 . ASP B 436 ? 2.4506 1.3821 1.8151 0.1819  0.3634  -0.3906 463 ASP B OD2 
7695 N N   . LEU B 437 ? 1.9411 1.1079 1.4973 0.1509  0.2990  -0.2646 464 LEU B N   
7696 C CA  . LEU B 437 ? 1.8365 1.0827 1.4245 0.1434  0.2731  -0.2418 464 LEU B CA  
7697 C C   . LEU B 437 ? 1.9280 1.1787 1.5618 0.1107  0.2617  -0.2418 464 LEU B C   
7698 O O   . LEU B 437 ? 2.0143 1.2525 1.6559 0.0801  0.2501  -0.2703 464 LEU B O   
7699 C CB  . LEU B 437 ? 1.7728 1.0665 1.3416 0.1368  0.2486  -0.2569 464 LEU B CB  
7700 C CG  . LEU B 437 ? 1.9454 1.3186 1.5368 0.1349  0.2225  -0.2318 464 LEU B CG  
7701 C CD1 . LEU B 437 ? 1.8097 1.2125 1.3924 0.1680  0.2334  -0.1974 464 LEU B CD1 
7702 C CD2 . LEU B 437 ? 2.0080 1.4169 1.5813 0.1201  0.1962  -0.2518 464 LEU B CD2 
7703 N N   . ILE B 438 ? 1.8555 1.1266 1.5192 0.1162  0.2651  -0.2102 465 ILE B N   
7704 C CA  . ILE B 438 ? 1.8020 1.0824 1.5100 0.0889  0.2576  -0.2072 465 ILE B CA  
7705 C C   . ILE B 438 ? 1.7729 1.1249 1.5056 0.0872  0.2337  -0.1875 465 ILE B C   
7706 O O   . ILE B 438 ? 1.6911 1.0681 1.4214 0.1071  0.2362  -0.1579 465 ILE B O   
7707 C CB  . ILE B 438 ? 1.8393 1.0775 1.5581 0.0935  0.2829  -0.1888 465 ILE B CB  
7708 C CG1 . ILE B 438 ? 1.9055 1.0647 1.6014 0.0911  0.3058  -0.2098 465 ILE B CG1 
7709 C CG2 . ILE B 438 ? 1.7394 0.9983 1.5035 0.0680  0.2764  -0.1822 465 ILE B CG2 
7710 C CD1 . ILE B 438 ? 1.8796 0.9921 1.5873 0.0890  0.3295  -0.1938 465 ILE B CD1 
7711 N N   . TYR B 439 ? 1.8565 1.2407 1.6129 0.0629  0.2099  -0.2033 466 TYR B N   
7712 C CA  . TYR B 439 ? 1.6578 1.1042 1.4376 0.0614  0.1864  -0.1864 466 TYR B CA  
7713 C C   . TYR B 439 ? 1.6955 1.1483 1.5123 0.0563  0.1932  -0.1662 466 TYR B C   
7714 O O   . TYR B 439 ? 1.7065 1.1423 1.5532 0.0363  0.1997  -0.1770 466 TYR B O   
7715 C CB  . TYR B 439 ? 1.7236 1.2023 1.5192 0.0390  0.1588  -0.2082 466 TYR B CB  
7716 C CG  . TYR B 439 ? 1.8165 1.3130 1.5735 0.0456  0.1433  -0.2197 466 TYR B CG  
7717 C CD1 . TYR B 439 ? 1.7611 1.3070 1.5097 0.0582  0.1251  -0.2001 466 TYR B CD1 
7718 C CD2 . TYR B 439 ? 1.8424 1.3038 1.5680 0.0375  0.1472  -0.2506 466 TYR B CD2 
7719 C CE1 . TYR B 439 ? 1.8002 1.3642 1.5110 0.0632  0.1120  -0.2093 466 TYR B CE1 
7720 C CE2 . TYR B 439 ? 1.9202 1.3977 1.6055 0.0429  0.1343  -0.2625 466 TYR B CE2 
7721 C CZ  . TYR B 439 ? 1.7946 1.3257 1.4732 0.0561  0.1170  -0.2410 466 TYR B CZ  
7722 O OH  . TYR B 439 ? 1.9184 1.4670 1.5544 0.0607  0.1054  -0.2514 466 TYR B OH  
7723 N N   . VAL B 440 ? 1.6779 1.1558 1.4912 0.0728  0.1921  -0.1374 467 VAL B N   
7724 C CA  . VAL B 440 ? 1.5633 1.0522 1.4067 0.0671  0.1951  -0.1196 467 VAL B CA  
7725 C C   . VAL B 440 ? 1.5561 1.0928 1.4272 0.0584  0.1700  -0.1176 467 VAL B C   
7726 O O   . VAL B 440 ? 1.4760 1.0199 1.3805 0.0488  0.1718  -0.1132 467 VAL B O   
7727 C CB  . VAL B 440 ? 1.4146 0.9001 1.2371 0.0864  0.2080  -0.0897 467 VAL B CB  
7728 C CG1 . VAL B 440 ? 1.5740 1.0572 1.4196 0.0783  0.2166  -0.0753 467 VAL B CG1 
7729 C CG2 . VAL B 440 ? 1.4486 0.8925 1.2419 0.1016  0.2303  -0.0886 467 VAL B CG2 
7730 N N   . GLY B 441 ? 1.5438 1.1119 1.4012 0.0625  0.1478  -0.1203 468 GLY B N   
7731 C CA  . GLY B 441 ? 1.5105 1.1214 1.3920 0.0563  0.1223  -0.1169 468 GLY B CA  
7732 C C   . GLY B 441 ? 1.6761 1.3135 1.5396 0.0556  0.0988  -0.1277 468 GLY B C   
7733 O O   . GLY B 441 ? 1.8350 1.4773 1.6599 0.0692  0.0974  -0.1199 468 GLY B O   
7734 N N   . ARG B 442 ? 1.6720 1.3304 1.5631 0.0396  0.0802  -0.1447 469 ARG B N   
7735 C CA  . ARG B 442 ? 1.7272 1.4104 1.5993 0.0351  0.0563  -0.1575 469 ARG B CA  
7736 C C   . ARG B 442 ? 1.8112 1.5367 1.7259 0.0229  0.0294  -0.1589 469 ARG B C   
7737 O O   . ARG B 442 ? 1.8264 1.5616 1.7836 0.0218  0.0314  -0.1486 469 ARG B O   
7738 C CB  . ARG B 442 ? 1.7591 1.4098 1.6072 0.0251  0.0656  -0.1871 469 ARG B CB  
7739 C CG  . ARG B 442 ? 1.6897 1.3109 1.5708 0.0070  0.0812  -0.2039 469 ARG B CG  
7740 C CD  . ARG B 442 ? 1.6744 1.2868 1.5514 -0.0161 0.0719  -0.2368 469 ARG B CD  
7741 N NE  . ARG B 442 ? 1.8059 1.3995 1.7229 -0.0382 0.0835  -0.2500 469 ARG B NE  
7742 C CZ  . ARG B 442 ? 1.8980 1.4870 1.8250 -0.0658 0.0751  -0.2778 469 ARG B CZ  
7743 N NH1 . ARG B 442 ? 1.9989 1.5985 1.8957 -0.0752 0.0543  -0.2975 469 ARG B NH1 
7744 N NH2 . ARG B 442 ? 1.9319 1.5064 1.8985 -0.0866 0.0880  -0.2859 469 ARG B NH2 
7745 N N   . LYS B 443 ? 1.8845 1.6364 1.7868 0.0146  0.0045  -0.1713 470 LYS B N   
7746 C CA  . LYS B 443 ? 1.8992 1.6957 1.8421 0.0022  -0.0240 -0.1741 470 LYS B CA  
7747 C C   . LYS B 443 ? 1.9678 1.7627 1.9121 -0.0219 -0.0316 -0.2062 470 LYS B C   
7748 O O   . LYS B 443 ? 2.0373 1.8371 1.9406 -0.0271 -0.0460 -0.2196 470 LYS B O   
7749 C CB  . LYS B 443 ? 1.8947 1.7303 1.8205 0.0122  -0.0523 -0.1553 470 LYS B CB  
7750 C CG  . LYS B 443 ? 1.8572 1.7418 1.8299 0.0049  -0.0825 -0.1509 470 LYS B CG  
7751 C CD  . LYS B 443 ? 1.8613 1.7787 1.8128 0.0162  -0.1098 -0.1283 470 LYS B CD  
7752 C CE  . LYS B 443 ? 1.6750 1.6393 1.6787 0.0149  -0.1380 -0.1176 470 LYS B CE  
7753 N NZ  . LYS B 443 ? 1.6677 1.6588 1.6493 0.0268  -0.1643 -0.0920 470 LYS B NZ  
7754 N N   . ARG B 444 ? 1.9741 1.7613 1.9630 -0.0385 -0.0213 -0.2190 471 ARG B N   
7755 C CA  . ARG B 444 ? 1.9997 1.7828 1.9936 -0.0667 -0.0277 -0.2499 471 ARG B CA  
7756 C C   . ARG B 444 ? 1.9948 1.8364 2.0032 -0.0798 -0.0672 -0.2546 471 ARG B C   
7757 O O   . ARG B 444 ? 2.0129 1.9032 2.0743 -0.0783 -0.0845 -0.2394 471 ARG B O   
7758 C CB  . ARG B 444 ? 1.9762 1.7465 2.0220 -0.0828 -0.0084 -0.2573 471 ARG B CB  
7759 C CG  . ARG B 444 ? 2.0140 1.7838 2.0745 -0.1175 -0.0157 -0.2878 471 ARG B CG  
7760 C CD  . ARG B 444 ? 1.9525 1.7128 2.0669 -0.1331 0.0060  -0.2902 471 ARG B CD  
7761 N NE  . ARG B 444 ? 2.0073 1.7785 2.1467 -0.1708 -0.0044 -0.3166 471 ARG B NE  
7762 C CZ  . ARG B 444 ? 1.9990 1.7704 2.1886 -0.1923 0.0108  -0.3220 471 ARG B CZ  
7763 N NH1 . ARG B 444 ? 2.0135 1.7731 2.2315 -0.1789 0.0383  -0.3038 471 ARG B NH1 
7764 N NH2 . ARG B 444 ? 2.1006 1.8854 2.3107 -0.2302 -0.0018 -0.3462 471 ARG B NH2 
7765 N N   . MET B 445 ? 2.0333 1.8697 1.9929 -0.0915 -0.0813 -0.2753 472 MET B N   
7766 C CA  . MET B 445 ? 1.9607 1.8520 1.9220 -0.1048 -0.1211 -0.2794 472 MET B CA  
7767 C C   . MET B 445 ? 1.9615 1.8664 1.9472 -0.1419 -0.1353 -0.3088 472 MET B C   
7768 O O   . MET B 445 ? 1.9719 1.9307 1.9686 -0.1564 -0.1713 -0.3114 472 MET B O   
7769 C CB  . MET B 445 ? 1.9624 1.8463 1.8485 -0.0961 -0.1309 -0.2828 472 MET B CB  
7770 C CG  . MET B 445 ? 2.1309 2.0036 1.9882 -0.0631 -0.1170 -0.2542 472 MET B CG  
7771 S SD  . MET B 445 ? 1.9973 1.9306 1.8853 -0.0454 -0.1459 -0.2144 472 MET B SD  
7772 C CE  . MET B 445 ? 1.9709 1.9434 1.8096 -0.0560 -0.1840 -0.2211 472 MET B CE  
7773 N N   . GLN B 446 ? 2.1236 1.9822 2.1175 -0.1590 -0.1093 -0.3294 473 GLN B N   
7774 C CA  . GLN B 446 ? 2.2200 2.0847 2.2352 -0.1991 -0.1199 -0.3587 473 GLN B CA  
7775 C C   . GLN B 446 ? 2.2333 2.1123 2.3264 -0.2083 -0.1054 -0.3508 473 GLN B C   
7776 O O   . GLN B 446 ? 2.2787 2.1029 2.3722 -0.2129 -0.0720 -0.3585 473 GLN B O   
7777 C CB  . GLN B 446 ? 2.2502 2.0402 2.2006 -0.2149 -0.1006 -0.3923 473 GLN B CB  
7778 C CG  . GLN B 446 ? 2.2592 2.0527 2.2105 -0.2608 -0.1190 -0.4269 473 GLN B CG  
7779 C CD  . GLN B 446 ? 2.3228 2.1076 2.3341 -0.2876 -0.1035 -0.4344 473 GLN B CD  
7780 O OE1 . GLN B 446 ? 2.4010 2.2347 2.4581 -0.3217 -0.1275 -0.4445 473 GLN B OE1 
7781 N NE2 . GLN B 446 ? 2.2978 2.0233 2.3095 -0.2733 -0.0637 -0.4279 473 GLN B NE2 
7782 N N   . VAL B 447 ? 2.2234 2.1770 2.3822 -0.2096 -0.1297 -0.3342 474 VAL B N   
7783 C CA  . VAL B 447 ? 2.2149 2.1935 2.4525 -0.2138 -0.1158 -0.3236 474 VAL B CA  
7784 C C   . VAL B 447 ? 2.3006 2.3352 2.5955 -0.2521 -0.1385 -0.3388 474 VAL B C   
7785 O O   . VAL B 447 ? 2.1771 2.2430 2.5438 -0.2581 -0.1279 -0.3306 474 VAL B O   
7786 C CB  . VAL B 447 ? 1.9869 2.0041 2.2633 -0.1780 -0.1174 -0.2884 474 VAL B CB  
7787 C CG1 . VAL B 447 ? 1.9782 1.9427 2.1992 -0.1446 -0.0958 -0.2728 474 VAL B CG1 
7788 C CG2 . VAL B 447 ? 1.9928 2.0857 2.2919 -0.1739 -0.1609 -0.2757 474 VAL B CG2 
7789 N N   . GLU B 448 ? 2.4514 2.5027 2.7169 -0.2792 -0.1691 -0.3605 475 GLU B N   
7790 C CA  . GLU B 448 ? 2.4080 2.5156 2.7258 -0.3208 -0.1936 -0.3760 475 GLU B CA  
7791 C C   . GLU B 448 ? 2.3928 2.4527 2.7245 -0.3539 -0.1637 -0.3985 475 GLU B C   
7792 O O   . GLU B 448 ? 2.3503 2.4427 2.7562 -0.3625 -0.1514 -0.3895 475 GLU B O   
7793 C CB  . GLU B 448 ? 2.4113 2.5410 2.6822 -0.3447 -0.2337 -0.3959 475 GLU B CB  
7794 C CG  . GLU B 448 ? 2.4157 2.6249 2.7025 -0.3247 -0.2744 -0.3709 475 GLU B CG  
7795 C CD  . GLU B 448 ? 2.5239 2.7080 2.7695 -0.2767 -0.2645 -0.3452 475 GLU B CD  
7796 O OE1 . GLU B 448 ? 2.5953 2.7064 2.7660 -0.2670 -0.2424 -0.3565 475 GLU B OE1 
7797 O OE2 . GLU B 448 ? 2.5097 2.7468 2.7988 -0.2488 -0.2780 -0.3130 475 GLU B OE2 
7798 N N   . HIS B 449 ? 2.4093 2.3906 2.6692 -0.3721 -0.1507 -0.4274 476 HIS B N   
7799 C CA  . HIS B 449 ? 2.4060 2.3290 2.6750 -0.3978 -0.1169 -0.4436 476 HIS B CA  
7800 C C   . HIS B 449 ? 2.3940 2.2363 2.6251 -0.3631 -0.0733 -0.4322 476 HIS B C   
7801 O O   . HIS B 449 ? 2.3835 2.1894 2.5511 -0.3327 -0.0698 -0.4283 476 HIS B O   
7802 C CB  . HIS B 449 ? 2.3930 2.2703 2.6126 -0.4438 -0.1252 -0.4838 476 HIS B CB  
7803 C CG  . HIS B 449 ? 2.3927 2.2162 2.5159 -0.4312 -0.1310 -0.5008 476 HIS B CG  
7804 N ND1 . HIS B 449 ? 2.4179 2.1437 2.4741 -0.4112 -0.0952 -0.5090 476 HIS B ND1 
7805 C CD2 . HIS B 449 ? 2.3715 2.2276 2.4541 -0.4351 -0.1672 -0.5107 476 HIS B CD2 
7806 C CE1 . HIS B 449 ? 2.3863 2.0877 2.3666 -0.4023 -0.1073 -0.5241 476 HIS B CE1 
7807 N NE2 . HIS B 449 ? 2.3697 2.1476 2.3617 -0.4176 -0.1507 -0.5259 476 HIS B NE2 
7808 N N   . PRO B 450 ? 2.3233 2.1411 2.5927 -0.3673 -0.0401 -0.4249 477 PRO B N   
7809 C CA  . PRO B 450 ? 2.2770 2.0286 2.5161 -0.3328 -0.0012 -0.4088 477 PRO B CA  
7810 C C   . PRO B 450 ? 2.3883 2.0462 2.5409 -0.3296 0.0157  -0.4284 477 PRO B C   
7811 O O   . PRO B 450 ? 2.4752 2.0947 2.5990 -0.3640 0.0125  -0.4588 477 PRO B O   
7812 C CB  . PRO B 450 ? 2.2888 2.0353 2.5853 -0.3497 0.0277  -0.4023 477 PRO B CB  
7813 C CG  . PRO B 450 ? 2.1785 1.9571 2.5129 -0.4017 0.0098  -0.4255 477 PRO B CG  
7814 C CD  . PRO B 450 ? 2.1794 2.0323 2.5214 -0.4053 -0.0367 -0.4298 477 PRO B CD  
7815 N N   . GLU B 451 ? 2.3406 1.9624 2.4519 -0.2878 0.0340  -0.4107 478 GLU B N   
7816 C CA  . GLU B 451 ? 2.3154 1.8533 2.3479 -0.2761 0.0527  -0.4248 478 GLU B CA  
7817 C C   . GLU B 451 ? 2.3008 1.7602 2.3259 -0.2943 0.0874  -0.4360 478 GLU B C   
7818 O O   . GLU B 451 ? 2.3716 1.8335 2.4434 -0.2986 0.1071  -0.4204 478 GLU B O   
7819 C CB  . GLU B 451 ? 2.2932 1.8225 2.2935 -0.2272 0.0641  -0.3985 478 GLU B CB  
7820 C CG  . GLU B 451 ? 2.2995 1.8947 2.2950 -0.2090 0.0314  -0.3870 478 GLU B CG  
7821 C CD  . GLU B 451 ? 2.2509 1.8419 2.2211 -0.1650 0.0429  -0.3585 478 GLU B CD  
7822 O OE1 . GLU B 451 ? 2.1847 1.7375 2.1562 -0.1483 0.0734  -0.3431 478 GLU B OE1 
7823 O OE2 . GLU B 451 ? 2.2039 1.8313 2.1522 -0.1489 0.0206  -0.3505 478 GLU B OE2 
7824 N N   . LYS B 452 ? 2.3323 1.7184 2.2950 -0.3047 0.0958  -0.4633 479 LYS B N   
7825 C CA  . LYS B 452 ? 2.2632 1.5672 2.2136 -0.3281 0.1252  -0.4782 479 LYS B CA  
7826 C C   . LYS B 452 ? 2.1780 1.4362 2.1266 -0.2963 0.1628  -0.4504 479 LYS B C   
7827 O O   . LYS B 452 ? 2.1902 1.4182 2.0941 -0.2560 0.1757  -0.4380 479 LYS B O   
7828 C CB  . LYS B 452 ? 2.2912 1.5198 2.1665 -0.3390 0.1271  -0.5133 479 LYS B CB  
7829 C CG  . LYS B 452 ? 2.3231 1.4693 2.1868 -0.3770 0.1483  -0.5370 479 LYS B CG  
7830 C CD  . LYS B 452 ? 2.2793 1.3572 2.0684 -0.3926 0.1444  -0.5771 479 LYS B CD  
7831 C CE  . LYS B 452 ? 2.3473 1.3360 2.1221 -0.4338 0.1647  -0.6021 479 LYS B CE  
7832 N NZ  . LYS B 452 ? 2.4876 1.4062 2.1869 -0.4529 0.1601  -0.6454 479 LYS B NZ  
7833 N N   . ALA B 453 ? 2.1572 1.4138 2.1546 -0.3156 0.1803  -0.4397 480 ALA B N   
7834 C CA  . ALA B 453 ? 2.1115 1.3300 2.1093 -0.2894 0.2145  -0.4116 480 ALA B CA  
7835 C C   . ALA B 453 ? 2.2102 1.3216 2.1450 -0.2806 0.2434  -0.4202 480 ALA B C   
7836 O O   . ALA B 453 ? 2.3835 1.4388 2.2925 -0.3108 0.2454  -0.4496 480 ALA B O   
7837 C CB  . ALA B 453 ? 2.0610 1.3048 2.1240 -0.3158 0.2270  -0.3998 480 ALA B CB  
7838 N N   . VAL B 454 ? 2.1855 1.2681 2.0956 -0.2389 0.2654  -0.3939 481 VAL B N   
7839 C CA  . VAL B 454 ? 2.2046 1.1892 2.0583 -0.2213 0.2946  -0.3952 481 VAL B CA  
7840 C C   . VAL B 454 ? 2.2786 1.2100 2.1504 -0.2426 0.3232  -0.3860 481 VAL B C   
7841 O O   . VAL B 454 ? 2.3021 1.2626 2.2091 -0.2351 0.3344  -0.3569 481 VAL B O   
7842 C CB  . VAL B 454 ? 2.2064 1.1913 2.0290 -0.1674 0.3041  -0.3680 481 VAL B CB  
7843 C CG1 . VAL B 454 ? 2.0215 0.9095 1.7952 -0.1461 0.3367  -0.3635 481 VAL B CG1 
7844 C CG2 . VAL B 454 ? 2.1129 1.1431 1.9113 -0.1487 0.2783  -0.3780 481 VAL B CG2 
7845 N N   . PRO B 455 ? 2.3475 1.1982 2.1934 -0.2705 0.3364  -0.4098 482 PRO B N   
7846 C CA  . PRO B 455 ? 2.3782 1.1757 2.2404 -0.2945 0.3639  -0.3998 482 PRO B CA  
7847 C C   . PRO B 455 ? 2.4095 1.1554 2.2457 -0.2542 0.3948  -0.3661 482 PRO B C   
7848 O O   . PRO B 455 ? 2.4330 1.1471 2.2229 -0.2123 0.4009  -0.3600 482 PRO B O   
7849 C CB  . PRO B 455 ? 2.2689 0.9833 2.0971 -0.3315 0.3682  -0.4364 482 PRO B CB  
7850 C CG  . PRO B 455 ? 2.2722 1.0258 2.0859 -0.3399 0.3354  -0.4683 482 PRO B CG  
7851 C CD  . PRO B 455 ? 2.3220 1.1295 2.1240 -0.2879 0.3249  -0.4493 482 PRO B CD  
7852 N N   . ARG B 456 ? 2.4123 1.1548 2.2801 -0.2677 0.4142  -0.3429 483 ARG B N   
7853 C CA  . ARG B 456 ? 2.4386 1.1332 2.2873 -0.2392 0.4440  -0.3081 483 ARG B CA  
7854 C C   . ARG B 456 ? 2.3932 1.1436 2.2406 -0.1916 0.4393  -0.2775 483 ARG B C   
7855 O O   . ARG B 456 ? 2.4029 1.1233 2.2339 -0.1663 0.4607  -0.2462 483 ARG B O   
7856 C CB  . ARG B 456 ? 2.4711 1.0505 2.2601 -0.2254 0.4671  -0.3133 483 ARG B CB  
7857 C CG  . ARG B 456 ? 2.4370 0.9394 2.2230 -0.2737 0.4816  -0.3336 483 ARG B CG  
7858 C CD  . ARG B 456 ? 2.5485 0.9300 2.2710 -0.2569 0.5037  -0.3418 483 ARG B CD  
7859 N NE  . ARG B 456 ? 2.6663 1.0145 2.3585 -0.2741 0.4897  -0.3864 483 ARG B NE  
7860 C CZ  . ARG B 456 ? 2.8146 1.1826 2.4770 -0.2426 0.4744  -0.4017 483 ARG B CZ  
7861 N NH1 . ARG B 456 ? 2.6540 1.0781 2.3163 -0.1931 0.4698  -0.3757 483 ARG B NH1 
7862 N NH2 . ARG B 456 ? 2.8120 1.1429 2.4420 -0.2635 0.4635  -0.4443 483 ARG B NH2 
7863 N N   . VAL B 457 ? 2.2825 1.1122 2.1454 -0.1803 0.4114  -0.2841 484 VAL B N   
7864 C CA  . VAL B 457 ? 2.0834 0.9713 1.9492 -0.1420 0.4045  -0.2561 484 VAL B CA  
7865 C C   . VAL B 457 ? 2.0730 1.0536 1.9940 -0.1594 0.3833  -0.2567 484 VAL B C   
7866 O O   . VAL B 457 ? 1.9681 0.9957 1.9030 -0.1692 0.3566  -0.2782 484 VAL B O   
7867 C CB  . VAL B 457 ? 2.1298 1.0200 1.9545 -0.1044 0.3926  -0.2596 484 VAL B CB  
7868 C CG1 . VAL B 457 ? 1.9534 0.9000 1.7813 -0.0690 0.3873  -0.2275 484 VAL B CG1 
7869 C CG2 . VAL B 457 ? 2.1019 0.8985 1.8740 -0.0861 0.4147  -0.2634 484 VAL B CG2 
7870 N N   . ARG B 458 ? 2.0393 1.0457 1.9900 -0.1617 0.3956  -0.2326 485 ARG B N   
7871 C CA  . ARG B 458 ? 1.8453 0.9340 1.8508 -0.1764 0.3807  -0.2325 485 ARG B CA  
7872 C C   . ARG B 458 ? 1.7494 0.8995 1.7530 -0.1457 0.3573  -0.2240 485 ARG B C   
7873 O O   . ARG B 458 ? 1.7194 0.8554 1.6849 -0.1119 0.3599  -0.2066 485 ARG B O   
7874 C CB  . ARG B 458 ? 1.8015 0.8943 1.8323 -0.1852 0.4047  -0.2097 485 ARG B CB  
7875 C CG  . ARG B 458 ? 1.9541 1.1195 2.0482 -0.2087 0.3973  -0.2145 485 ARG B CG  
7876 C CD  . ARG B 458 ? 2.1112 1.2741 2.2209 -0.2142 0.4256  -0.1917 485 ARG B CD  
7877 N NE  . ARG B 458 ? 2.2697 1.3512 2.3451 -0.2222 0.4532  -0.1825 485 ARG B NE  
7878 C CZ  . ARG B 458 ? 2.3752 1.4355 2.4476 -0.2260 0.4811  -0.1597 485 ARG B CZ  
7879 N NH1 . ARG B 458 ? 2.4670 1.5799 2.5669 -0.2233 0.4874  -0.1461 485 ARG B NH1 
7880 N NH2 . ARG B 458 ? 2.1922 1.1738 2.2302 -0.2321 0.5040  -0.1501 485 ARG B NH2 
7881 N N   . ASN B 459 ? 1.6348 0.8550 1.6817 -0.1586 0.3339  -0.2352 486 ASN B N   
7882 C CA  . ASN B 459 ? 1.7526 1.0332 1.8032 -0.1338 0.3103  -0.2270 486 ASN B CA  
7883 C C   . ASN B 459 ? 1.7718 1.0378 1.7746 -0.1115 0.2951  -0.2340 486 ASN B C   
7884 O O   . ASN B 459 ? 1.7807 1.0640 1.7613 -0.0814 0.2891  -0.2163 486 ASN B O   
7885 C CB  . ASN B 459 ? 1.6588 0.9549 1.7100 -0.1114 0.3227  -0.1969 486 ASN B CB  
7886 C CG  . ASN B 459 ? 1.6038 0.9270 1.7041 -0.1308 0.3361  -0.1916 486 ASN B CG  
7887 O OD1 . ASN B 459 ? 1.7698 1.0553 1.8675 -0.1412 0.3633  -0.1824 486 ASN B OD1 
7888 N ND2 . ASN B 459 ? 1.4714 0.8607 1.6167 -0.1347 0.3181  -0.1962 486 ASN B ND2 
7889 N N   . LEU B 460 ? 1.8232 1.0573 1.8086 -0.1281 0.2896  -0.2606 487 LEU B N   
7890 C CA  . LEU B 460 ? 1.8413 1.0605 1.7795 -0.1092 0.2773  -0.2717 487 LEU B CA  
7891 C C   . LEU B 460 ? 1.8748 1.0972 1.8157 -0.1391 0.2579  -0.3064 487 LEU B C   
7892 O O   . LEU B 460 ? 1.8602 1.0474 1.8123 -0.1714 0.2671  -0.3240 487 LEU B O   
7893 C CB  . LEU B 460 ? 1.8826 1.0256 1.7695 -0.0870 0.3033  -0.2642 487 LEU B CB  
7894 C CG  . LEU B 460 ? 1.7469 0.8733 1.5829 -0.0607 0.2970  -0.2726 487 LEU B CG  
7895 C CD1 . LEU B 460 ? 1.7887 0.9755 1.6218 -0.0311 0.2817  -0.2505 487 LEU B CD1 
7896 C CD2 . LEU B 460 ? 1.8477 0.8926 1.6401 -0.0413 0.3260  -0.2679 487 LEU B CD2 
7897 N N   . VAL B 461 ? 1.8586 1.1234 1.7874 -0.1308 0.2305  -0.3155 488 VAL B N   
7898 C CA  . VAL B 461 ? 1.9056 1.1804 1.8308 -0.1586 0.2076  -0.3480 488 VAL B CA  
7899 C C   . VAL B 461 ? 1.9602 1.2129 1.8235 -0.1374 0.2010  -0.3599 488 VAL B C   
7900 O O   . VAL B 461 ? 2.0299 1.2834 1.8661 -0.1008 0.2077  -0.3398 488 VAL B O   
7901 C CB  . VAL B 461 ? 1.7696 1.1323 1.7480 -0.1750 0.1757  -0.3483 488 VAL B CB  
7902 C CG1 . VAL B 461 ? 1.7839 1.1714 1.8262 -0.1959 0.1850  -0.3387 488 VAL B CG1 
7903 C CG2 . VAL B 461 ? 1.8126 1.2285 1.7869 -0.1417 0.1592  -0.3260 488 VAL B CG2 
7904 N N   . GLU B 462 ? 1.9571 1.1919 1.7978 -0.1625 0.1880  -0.3936 489 GLU B N   
7905 C CA  . GLU B 462 ? 1.9554 1.1737 1.7357 -0.1463 0.1804  -0.4098 489 GLU B CA  
7906 C C   . GLU B 462 ? 1.9768 1.2786 1.7665 -0.1360 0.1479  -0.4000 489 GLU B C   
7907 O O   . GLU B 462 ? 2.0201 1.3793 1.8482 -0.1618 0.1199  -0.4065 489 GLU B O   
7908 C CB  . GLU B 462 ? 2.0378 1.2063 1.7862 -0.1803 0.1768  -0.4514 489 GLU B CB  
7909 C CG  . GLU B 462 ? 2.1848 1.2646 1.9243 -0.1952 0.2082  -0.4617 489 GLU B CG  
7910 C CD  . GLU B 462 ? 2.2088 1.2329 1.9122 -0.2320 0.2042  -0.5050 489 GLU B CD  
7911 O OE1 . GLU B 462 ? 2.1581 1.1760 1.8104 -0.2264 0.1922  -0.5274 489 GLU B OE1 
7912 O OE2 . GLU B 462 ? 2.3446 1.3308 2.0687 -0.2685 0.2133  -0.5171 489 GLU B OE2 
7913 N N   . ALA B 463 ? 2.0633 1.3736 1.8199 -0.0984 0.1516  -0.3823 490 ALA B N   
7914 C CA  . ALA B 463 ? 2.1372 1.5223 1.9009 -0.0861 0.1235  -0.3671 490 ALA B CA  
7915 C C   . ALA B 463 ? 2.2307 1.6371 1.9672 -0.1061 0.0952  -0.3953 490 ALA B C   
7916 O O   . ALA B 463 ? 2.2184 1.5834 1.8958 -0.1010 0.1026  -0.4169 490 ALA B O   
7917 C CB  . ALA B 463 ? 2.0319 1.4178 1.7638 -0.0444 0.1364  -0.3415 490 ALA B CB  
7918 N N   . ASP B 464 ? 2.4008 1.8722 2.1793 -0.1281 0.0633  -0.3949 491 ASP B N   
7919 C CA  . ASP B 464 ? 2.4191 1.9263 2.1734 -0.1447 0.0306  -0.4144 491 ASP B CA  
7920 C C   . ASP B 464 ? 2.3843 1.9407 2.1203 -0.1153 0.0153  -0.3899 491 ASP B C   
7921 O O   . ASP B 464 ? 2.3621 1.9058 2.0845 -0.0827 0.0355  -0.3667 491 ASP B O   
7922 C CB  . ASP B 464 ? 2.4604 2.0189 2.2704 -0.1821 0.0015  -0.4234 491 ASP B CB  
7923 C CG  . ASP B 464 ? 2.5483 2.0590 2.3686 -0.2188 0.0134  -0.4521 491 ASP B CG  
7924 O OD1 . ASP B 464 ? 2.5491 1.9803 2.3318 -0.2136 0.0451  -0.4645 491 ASP B OD1 
7925 O OD2 . ASP B 464 ? 2.5694 2.1225 2.4367 -0.2530 -0.0088 -0.4612 491 ASP B OD2 
7926 N N   . TYR B 465 ? 2.0442 1.6581 1.7797 -0.1277 -0.0207 -0.3930 492 TYR B N   
7927 C CA  . TYR B 465 ? 2.0504 1.7069 1.7622 -0.1026 -0.0356 -0.3699 492 TYR B CA  
7928 C C   . TYR B 465 ? 2.0694 1.7577 1.8286 -0.0795 -0.0322 -0.3302 492 TYR B C   
7929 O O   . TYR B 465 ? 2.0311 1.7596 1.8505 -0.0896 -0.0476 -0.3184 492 TYR B O   
7930 C CB  . TYR B 465 ? 2.0565 1.7696 1.7615 -0.1225 -0.0771 -0.3783 492 TYR B CB  
7931 C CG  . TYR B 465 ? 2.1543 1.9067 1.8263 -0.0993 -0.0924 -0.3552 492 TYR B CG  
7932 C CD1 . TYR B 465 ? 2.0487 1.7699 1.6612 -0.0740 -0.0699 -0.3526 492 TYR B CD1 
7933 C CD2 . TYR B 465 ? 2.1522 1.9736 1.8533 -0.1023 -0.1285 -0.3345 492 TYR B CD2 
7934 C CE1 . TYR B 465 ? 2.0423 1.8014 1.6251 -0.0554 -0.0825 -0.3302 492 TYR B CE1 
7935 C CE2 . TYR B 465 ? 2.1098 1.9634 1.7786 -0.0830 -0.1420 -0.3114 492 TYR B CE2 
7936 C CZ  . TYR B 465 ? 2.0805 1.9033 1.6897 -0.0613 -0.1187 -0.3096 492 TYR B CZ  
7937 O OH  . TYR B 465 ? 2.0602 1.9173 1.6377 -0.0448 -0.1311 -0.2854 492 TYR B OH  
7938 N N   . SER B 466 ? 2.0301 1.7000 1.7617 -0.0488 -0.0110 -0.3102 493 SER B N   
7939 C CA  . SER B 466 ? 2.0267 1.7203 1.7894 -0.0270 -0.0068 -0.2734 493 SER B CA  
7940 C C   . SER B 466 ? 2.0853 1.8219 1.8211 -0.0115 -0.0268 -0.2524 493 SER B C   
7941 O O   . SER B 466 ? 2.1035 1.8546 1.7990 -0.0177 -0.0439 -0.2658 493 SER B O   
7942 C CB  . SER B 466 ? 2.0447 1.6894 1.7982 -0.0073 0.0304  -0.2635 493 SER B CB  
7943 O OG  . SER B 466 ? 1.9231 1.5213 1.6921 -0.0227 0.0498  -0.2838 493 SER B OG  
7944 N N   . TYR B 467 ? 2.1576 1.9126 1.9122 0.0072  -0.0244 -0.2192 494 TYR B N   
7945 C CA  . TYR B 467 ? 2.2198 2.0158 1.9537 0.0184  -0.0450 -0.1962 494 TYR B CA  
7946 C C   . TYR B 467 ? 2.1706 1.9649 1.8985 0.0412  -0.0298 -0.1640 494 TYR B C   
7947 O O   . TYR B 467 ? 2.2548 2.0785 1.9614 0.0501  -0.0434 -0.1428 494 TYR B O   
7948 C CB  . TYR B 467 ? 2.2774 2.1216 2.0526 0.0070  -0.0792 -0.1870 494 TYR B CB  
7949 C CG  . TYR B 467 ? 2.3517 2.2365 2.0957 0.0105  -0.1072 -0.1726 494 TYR B CG  
7950 C CD1 . TYR B 467 ? 2.3464 2.2412 2.0466 -0.0015 -0.1224 -0.1939 494 TYR B CD1 
7951 C CD2 . TYR B 467 ? 2.3283 2.2381 2.0828 0.0244  -0.1181 -0.1377 494 TYR B CD2 
7952 C CE1 . TYR B 467 ? 2.4558 2.3883 2.1238 0.0009  -0.1477 -0.1791 494 TYR B CE1 
7953 C CE2 . TYR B 467 ? 2.4451 2.3895 2.1693 0.0266  -0.1433 -0.1220 494 TYR B CE2 
7954 C CZ  . TYR B 467 ? 2.5391 2.4967 2.2203 0.0152  -0.1581 -0.1419 494 TYR B CZ  
7955 O OH  . TYR B 467 ? 2.6059 2.5987 2.2534 0.0166  -0.1830 -0.1247 494 TYR B OH  
7956 N N   . TRP B 468 ? 2.0409 1.8022 1.7855 0.0488  -0.0026 -0.1590 495 TRP B N   
7957 C CA  . TRP B 468 ? 1.9784 1.7394 1.7181 0.0669  0.0107  -0.1289 495 TRP B CA  
7958 C C   . TRP B 468 ? 1.9414 1.6630 1.6586 0.0796  0.0434  -0.1326 495 TRP B C   
7959 O O   . TRP B 468 ? 2.1475 1.8337 1.8600 0.0744  0.0582  -0.1577 495 TRP B O   
7960 C CB  . TRP B 468 ? 2.0140 1.7807 1.8019 0.0650  0.0081  -0.1106 495 TRP B CB  
7961 C CG  . TRP B 468 ? 2.0484 1.8537 1.8583 0.0604  -0.0220 -0.0978 495 TRP B CG  
7962 C CD1 . TRP B 468 ? 2.0586 1.8958 1.8430 0.0616  -0.0458 -0.0889 495 TRP B CD1 
7963 C CD2 . TRP B 468 ? 1.9960 1.8110 1.8575 0.0558  -0.0303 -0.0912 495 TRP B CD2 
7964 N NE1 . TRP B 468 ? 2.0057 1.8700 1.8233 0.0587  -0.0699 -0.0755 495 TRP B NE1 
7965 C CE2 . TRP B 468 ? 1.9990 1.8507 1.8655 0.0564  -0.0602 -0.0774 495 TRP B CE2 
7966 C CE3 . TRP B 468 ? 1.8896 1.6861 1.7929 0.0523  -0.0141 -0.0950 495 TRP B CE3 
7967 C CZ2 . TRP B 468 ? 1.9928 1.8619 1.9070 0.0564  -0.0738 -0.0674 495 TRP B CZ2 
7968 C CZ3 . TRP B 468 ? 1.8240 1.6402 1.7737 0.0511  -0.0262 -0.0867 495 TRP B CZ3 
7969 C CH2 . TRP B 468 ? 1.9400 1.7916 1.8961 0.0545  -0.0556 -0.0731 495 TRP B CH2 
7970 N N   . THR B 469 ? 1.7303 1.4584 1.4338 0.0959  0.0541  -0.1059 496 THR B N   
7971 C CA  . THR B 469 ? 1.8341 1.5330 1.5232 0.1114  0.0839  -0.1005 496 THR B CA  
7972 C C   . THR B 469 ? 1.7168 1.4212 1.4253 0.1166  0.0898  -0.0704 496 THR B C   
7973 O O   . THR B 469 ? 1.4847 1.2003 1.1744 0.1305  0.0993  -0.0485 496 THR B O   
7974 C CB  . THR B 469 ? 1.7432 1.4502 1.3859 0.1284  0.0933  -0.0997 496 THR B CB  
7975 O OG1 . THR B 469 ? 1.7823 1.5343 1.4125 0.1322  0.0780  -0.0739 496 THR B OG1 
7976 C CG2 . THR B 469 ? 1.7642 1.4584 1.3799 0.1222  0.0896  -0.1332 496 THR B CG2 
7977 N N   . LEU B 470 ? 1.7145 1.4129 1.4611 0.1043  0.0845  -0.0695 497 LEU B N   
7978 C CA  . LEU B 470 ? 1.6018 1.3014 1.3632 0.1061  0.0891  -0.0441 497 LEU B CA  
7979 C C   . LEU B 470 ? 1.6032 1.2738 1.3575 0.1157  0.1164  -0.0374 497 LEU B C   
7980 O O   . LEU B 470 ? 1.4163 1.0975 1.1564 0.1248  0.1221  -0.0128 497 LEU B O   
7981 C CB  . LEU B 470 ? 1.5111 1.2091 1.3138 0.0926  0.0800  -0.0481 497 LEU B CB  
7982 C CG  . LEU B 470 ? 1.7654 1.4950 1.5819 0.0861  0.0515  -0.0464 497 LEU B CG  
7983 C CD1 . LEU B 470 ? 1.7309 1.4575 1.5945 0.0758  0.0479  -0.0555 497 LEU B CD1 
7984 C CD2 . LEU B 470 ? 1.6859 1.4356 1.4858 0.0914  0.0403  -0.0176 497 LEU B CD2 
7985 N N   . ALA B 471 ? 1.5010 1.2101 1.3315 0.1260  0.1749  -0.0240 498 ALA B N   
7986 C CA  . ALA B 471 ? 1.3540 1.0404 1.1836 0.1281  0.2014  -0.0219 498 ALA B CA  
7987 C C   . ALA B 471 ? 1.4489 1.1002 1.2720 0.1167  0.2001  -0.0420 498 ALA B C   
7988 O O   . ALA B 471 ? 1.5098 1.1662 1.3604 0.0986  0.1832  -0.0556 498 ALA B O   
7989 C CB  . ALA B 471 ? 1.3861 1.0877 1.2606 0.1231  0.2161  -0.0094 498 ALA B CB  
7990 N N   . TYR B 472 ? 1.5473 1.1632 1.3344 0.1275  0.2176  -0.0446 499 TYR B N   
7991 C CA  . TYR B 472 ? 1.4586 1.0286 1.2310 0.1177  0.2195  -0.0640 499 TYR B CA  
7992 C C   . TYR B 472 ? 1.5165 1.0488 1.2627 0.1344  0.2461  -0.0578 499 TYR B C   
7993 O O   . TYR B 472 ? 1.4685 1.0153 1.1985 0.1565  0.2582  -0.0428 499 TYR B O   
7994 C CB  . TYR B 472 ? 1.4253 0.9815 1.1584 0.1163  0.1996  -0.0844 499 TYR B CB  
7995 C CG  . TYR B 472 ? 1.4335 0.9916 1.1164 0.1407  0.2048  -0.0797 499 TYR B CG  
7996 C CD1 . TYR B 472 ? 1.5646 1.0857 1.2074 0.1588  0.2246  -0.0846 499 TYR B CD1 
7997 C CD2 . TYR B 472 ? 1.5629 1.1591 1.2383 0.1461  0.1914  -0.0702 499 TYR B CD2 
7998 C CE1 . TYR B 472 ? 1.5346 1.0648 1.1366 0.1808  0.2320  -0.0815 499 TYR B CE1 
7999 C CE2 . TYR B 472 ? 1.6454 1.2454 1.2755 0.1648  0.1994  -0.0658 499 TYR B CE2 
8000 C CZ  . TYR B 472 ? 1.6680 1.2391 1.2642 0.1817  0.2202  -0.0722 499 TYR B CZ  
8001 O OH  . TYR B 472 ? 1.6206 1.2027 1.1770 0.2002  0.2307  -0.0688 499 TYR B OH  
8002 N N   . VAL B 473 ? 1.5757 1.0592 1.3179 0.1234  0.2544  -0.0695 500 VAL B N   
8003 C CA  . VAL B 473 ? 1.4810 0.9143 1.1889 0.1417  0.2768  -0.0668 500 VAL B CA  
8004 C C   . VAL B 473 ? 1.6014 0.9933 1.2598 0.1495  0.2723  -0.0889 500 VAL B C   
8005 O O   . VAL B 473 ? 1.6693 1.0488 1.3246 0.1279  0.2546  -0.1105 500 VAL B O   
8006 C CB  . VAL B 473 ? 1.5036 0.8970 1.2298 0.1251  0.2921  -0.0641 500 VAL B CB  
8007 C CG1 . VAL B 473 ? 1.6164 0.9589 1.3053 0.1505  0.3152  -0.0548 500 VAL B CG1 
8008 C CG2 . VAL B 473 ? 1.4454 0.8827 1.2224 0.1118  0.2948  -0.0474 500 VAL B CG2 
8009 N N   . ILE B 474 ? 1.5851 0.9584 1.2049 0.1808  0.2878  -0.0847 501 ILE B N   
8010 C CA  . ILE B 474 ? 1.6894 1.0190 1.2576 0.1935  0.2888  -0.1061 501 ILE B CA  
8011 C C   . ILE B 474 ? 1.8075 1.0805 1.3479 0.2190  0.3132  -0.1025 501 ILE B C   
8012 O O   . ILE B 474 ? 1.8475 1.1388 1.3985 0.2409  0.3275  -0.0799 501 ILE B O   
8013 C CB  . ILE B 474 ? 1.6687 1.0404 1.2124 0.2117  0.2828  -0.1070 501 ILE B CB  
8014 C CG1 . ILE B 474 ? 1.8197 1.1451 1.3068 0.2222  0.2840  -0.1329 501 ILE B CG1 
8015 C CG2 . ILE B 474 ? 1.6611 1.0736 1.2112 0.2406  0.2994  -0.0832 501 ILE B CG2 
8016 C CD1 . ILE B 474 ? 1.8238 1.1875 1.2812 0.2364  0.2799  -0.1355 501 ILE B CD1 
8017 N N   . SER B 475 ? 1.8332 1.0349 1.3365 0.2164  0.3167  -0.1250 502 SER B N   
8018 C CA  . SER B 475 ? 1.8918 1.0278 1.3608 0.2444  0.3394  -0.1235 502 SER B CA  
8019 C C   . SER B 475 ? 2.0687 1.1987 1.4920 0.2809  0.3472  -0.1349 502 SER B C   
8020 O O   . SER B 475 ? 2.0788 1.2389 1.4878 0.2771  0.3352  -0.1493 502 SER B O   
8021 C CB  . SER B 475 ? 1.9324 0.9814 1.3846 0.2196  0.3428  -0.1412 502 SER B CB  
8022 O OG  . SER B 475 ? 1.9741 0.9919 1.3947 0.2033  0.3300  -0.1738 502 SER B OG  
8023 N N   . LEU B 476 ? 2.1822 1.2735 1.5815 0.3184  0.3685  -0.1273 503 LEU B N   
8024 C CA  . LEU B 476 ? 2.0769 1.1606 1.4349 0.3574  0.3803  -0.1392 503 LEU B CA  
8025 C C   . LEU B 476 ? 2.1854 1.2090 1.4958 0.3448  0.3755  -0.1749 503 LEU B C   
8026 O O   . LEU B 476 ? 2.2440 1.2844 1.5239 0.3624  0.3777  -0.1898 503 LEU B O   
8027 C CB  . LEU B 476 ? 2.1210 1.1654 1.4631 0.4016  0.4027  -0.1257 503 LEU B CB  
8028 C CG  . LEU B 476 ? 2.2510 1.2888 1.5559 0.4500  0.4193  -0.1364 503 LEU B CG  
8029 C CD1 . LEU B 476 ? 2.1668 1.3082 1.4942 0.4640  0.4180  -0.1273 503 LEU B CD1 
8030 C CD2 . LEU B 476 ? 2.1871 1.1763 1.4784 0.4935  0.4384  -0.1220 503 LEU B CD2 
8031 N N   . GLN B 477 ? 2.3574 1.3117 1.6597 0.3121  0.3695  -0.1899 504 GLN B N   
8032 C CA  . GLN B 477 ? 2.4658 1.3644 1.7238 0.2926  0.3607  -0.2264 504 GLN B CA  
8033 C C   . GLN B 477 ? 2.4183 1.3832 1.6844 0.2683  0.3358  -0.2372 504 GLN B C   
8034 O O   . GLN B 477 ? 2.4714 1.4253 1.6913 0.2754  0.3328  -0.2610 504 GLN B O   
8035 C CB  . GLN B 477 ? 2.4373 1.2576 1.6942 0.2547  0.3577  -0.2389 504 GLN B CB  
8036 C CG  . GLN B 477 ? 2.5646 1.3326 1.7819 0.2240  0.3434  -0.2787 504 GLN B CG  
8037 C CD  . GLN B 477 ? 2.6213 1.3206 1.8457 0.1795  0.3401  -0.2907 504 GLN B CD  
8038 O OE1 . GLN B 477 ? 2.6879 1.3239 1.9081 0.1864  0.3605  -0.2785 504 GLN B OE1 
8039 N NE2 . GLN B 477 ? 2.6350 1.3477 1.8700 0.1327  0.3141  -0.3143 504 GLN B NE2 
8040 N N   . GLY B 478 ? 2.1844 1.2163 1.5055 0.2416  0.3183  -0.2194 505 GLY B N   
8041 C CA  . GLY B 478 ? 2.0556 1.1469 1.3844 0.2203  0.2927  -0.2265 505 GLY B CA  
8042 C C   . GLY B 478 ? 2.1569 1.3079 1.4715 0.2497  0.2976  -0.2162 505 GLY B C   
8043 O O   . GLY B 478 ? 2.2224 1.3965 1.5122 0.2412  0.2818  -0.2291 505 GLY B O   
8044 N N   . ALA B 479 ? 2.1233 1.3010 1.4522 0.2830  0.3191  -0.1926 506 ALA B N   
8045 C CA  . ALA B 479 ? 2.0421 1.2806 1.3618 0.3081  0.3268  -0.1828 506 ALA B CA  
8046 C C   . ALA B 479 ? 2.2459 1.4502 1.5022 0.3304  0.3386  -0.2083 506 ALA B C   
8047 O O   . ALA B 479 ? 2.2058 1.4497 1.4393 0.3332  0.3359  -0.2121 506 ALA B O   
8048 C CB  . ALA B 479 ? 1.8323 1.1099 1.1850 0.3370  0.3460  -0.1541 506 ALA B CB  
8049 N N   . ARG B 480 ? 2.3324 1.4588 1.5554 0.3465  0.3534  -0.2262 507 ARG B N   
8050 C CA  . ARG B 480 ? 2.3521 1.4372 1.5107 0.3684  0.3664  -0.2542 507 ARG B CA  
8051 C C   . ARG B 480 ? 2.4114 1.4738 1.5305 0.3347  0.3430  -0.2828 507 ARG B C   
8052 O O   . ARG B 480 ? 2.4495 1.5207 1.5212 0.3447  0.3464  -0.2985 507 ARG B O   
8053 C CB  . ARG B 480 ? 2.4690 1.4662 1.5994 0.3947  0.3877  -0.2668 507 ARG B CB  
8054 C CG  . ARG B 480 ? 2.4506 1.4649 1.6119 0.4345  0.4097  -0.2395 507 ARG B CG  
8055 C CD  . ARG B 480 ? 2.6372 1.5659 1.7533 0.4738  0.4340  -0.2557 507 ARG B CD  
8056 N NE  . ARG B 480 ? 2.6795 1.6091 1.8234 0.5098  0.4500  -0.2291 507 ARG B NE  
8057 C CZ  . ARG B 480 ? 2.6757 1.5393 1.8252 0.5046  0.4510  -0.2197 507 ARG B CZ  
8058 N NH1 . ARG B 480 ? 2.6466 1.4399 1.7813 0.4621  0.4388  -0.2354 507 ARG B NH1 
8059 N NH2 . ARG B 480 ? 2.6104 1.4794 1.7796 0.5419  0.4644  -0.1936 507 ARG B NH2 
8060 N N   . LYS B 481 ? 2.3622 1.3978 1.4997 0.2942  0.3192  -0.2900 508 LYS B N   
8061 C CA  . LYS B 481 ? 2.4248 1.4427 1.5284 0.2604  0.2922  -0.3180 508 LYS B CA  
8062 C C   . LYS B 481 ? 2.3315 1.4264 1.4353 0.2536  0.2744  -0.3081 508 LYS B C   
8063 O O   . LYS B 481 ? 2.3005 1.3855 1.3491 0.2477  0.2634  -0.3305 508 LYS B O   
8064 C CB  . LYS B 481 ? 2.2986 1.2916 1.4377 0.2168  0.2694  -0.3241 508 LYS B CB  
8065 C CG  . LYS B 481 ? 2.3054 1.2012 1.4237 0.2117  0.2827  -0.3439 508 LYS B CG  
8066 C CD  . LYS B 481 ? 2.3070 1.1880 1.4614 0.1609  0.2589  -0.3525 508 LYS B CD  
8067 C CE  . LYS B 481 ? 2.3982 1.1792 1.5355 0.1516  0.2753  -0.3677 508 LYS B CE  
8068 N NZ  . LYS B 481 ? 2.4009 1.1754 1.5816 0.0986  0.2557  -0.3741 508 LYS B NZ  
8069 N N   . LEU B 482 ? 2.2344 1.4015 1.3949 0.2538  0.2716  -0.2746 509 LEU B N   
8070 C CA  . LEU B 482 ? 2.2237 1.4570 1.3826 0.2477  0.2562  -0.2620 509 LEU B CA  
8071 C C   . LEU B 482 ? 2.2927 1.5425 1.4037 0.2790  0.2798  -0.2628 509 LEU B C   
8072 O O   . LEU B 482 ? 2.3284 1.5921 1.3947 0.2729  0.2690  -0.2711 509 LEU B O   
8073 C CB  . LEU B 482 ? 2.0630 1.3607 1.2924 0.2403  0.2501  -0.2273 509 LEU B CB  
8074 C CG  . LEU B 482 ? 1.9084 1.2043 1.1909 0.2082  0.2274  -0.2245 509 LEU B CG  
8075 C CD1 . LEU B 482 ? 1.8025 1.1614 1.1478 0.2056  0.2253  -0.1913 509 LEU B CD1 
8076 C CD2 . LEU B 482 ? 1.9990 1.2876 1.2622 0.1780  0.1928  -0.2463 509 LEU B CD2 
8077 N N   . LEU B 483 ? 2.2885 1.5389 1.4075 0.3130  0.3123  -0.2540 510 LEU B N   
8078 C CA  . LEU B 483 ? 2.2777 1.5523 1.3593 0.3437  0.3384  -0.2552 510 LEU B CA  
8079 C C   . LEU B 483 ? 2.3812 1.5941 1.3851 0.3531  0.3462  -0.2919 510 LEU B C   
8080 O O   . LEU B 483 ? 2.3859 1.6190 1.3434 0.3637  0.3571  -0.2987 510 LEU B O   
8081 C CB  . LEU B 483 ? 2.1391 1.4377 1.2569 0.3794  0.3688  -0.2369 510 LEU B CB  
8082 C CG  . LEU B 483 ? 2.0247 1.3893 1.2130 0.3735  0.3650  -0.2012 510 LEU B CG  
8083 C CD1 . LEU B 483 ? 1.9493 1.3282 1.1680 0.4095  0.3911  -0.1873 510 LEU B CD1 
8084 C CD2 . LEU B 483 ? 1.9185 1.3535 1.1099 0.3622  0.3605  -0.1845 510 LEU B CD2 
8085 N N   . ALA B 484 ? 2.4566 1.5912 1.4419 0.3476  0.3422  -0.3165 511 ALA B N   
8086 C CA  . ALA B 484 ? 2.5600 1.6258 1.4675 0.3564  0.3508  -0.3546 511 ALA B CA  
8087 C C   . ALA B 484 ? 2.6088 1.6712 1.4655 0.3251  0.3219  -0.3743 511 ALA B C   
8088 O O   . ALA B 484 ? 2.6689 1.6883 1.4511 0.3333  0.3300  -0.4046 511 ALA B O   
8089 C CB  . ALA B 484 ? 2.5030 1.4784 1.4035 0.3553  0.3540  -0.3752 511 ALA B CB  
8090 N N   . ALA B 485 ? 2.5030 1.6087 1.3956 0.2916  0.2883  -0.3582 512 ALA B N   
8091 C CA  . ALA B 485 ? 2.5447 1.6532 1.3918 0.2638  0.2561  -0.3733 512 ALA B CA  
8092 C C   . ALA B 485 ? 2.6628 1.8225 1.4721 0.2759  0.2637  -0.3605 512 ALA B C   
8093 O O   . ALA B 485 ? 2.7434 1.9087 1.5097 0.2557  0.2363  -0.3682 512 ALA B O   
8094 C CB  . ALA B 485 ? 2.5375 1.6743 1.4413 0.2266  0.2162  -0.3606 512 ALA B CB  
8095 N N   . GLU B 486 ? 2.6605 1.8567 1.4827 0.3078  0.3001  -0.3416 513 GLU B N   
8096 C CA  . GLU B 486 ? 2.6991 1.9512 1.4975 0.3185  0.3149  -0.3241 513 GLU B CA  
8097 C C   . GLU B 486 ? 2.6425 1.9301 1.4381 0.2886  0.2793  -0.3072 513 GLU B C   
8098 O O   . GLU B 486 ? 2.6228 1.9003 1.3471 0.2807  0.2686  -0.3193 513 GLU B O   
8099 C CB  . GLU B 486 ? 2.6348 1.8557 1.3474 0.3397  0.3414  -0.3519 513 GLU B CB  
8100 C CG  . GLU B 486 ? 2.8475 1.9952 1.4853 0.3245  0.3212  -0.3921 513 GLU B CG  
8101 C CD  . GLU B 486 ? 2.9586 2.0781 1.5075 0.3469  0.3507  -0.4188 513 GLU B CD  
8102 O OE1 . GLU B 486 ? 2.9591 2.1202 1.5105 0.3753  0.3888  -0.4055 513 GLU B OE1 
8103 O OE2 . GLU B 486 ? 3.1638 2.2216 1.6405 0.3353  0.3364  -0.4543 513 GLU B OE2 
8104 N N   . PRO B 487 ? 2.4550 1.7824 1.3233 0.2736  0.2606  -0.2789 514 PRO B N   
8105 C CA  . PRO B 487 ? 2.5279 1.8849 1.3963 0.2488  0.2251  -0.2625 514 PRO B CA  
8106 C C   . PRO B 487 ? 2.4929 1.8970 1.3400 0.2547  0.2385  -0.2362 514 PRO B C   
8107 O O   . PRO B 487 ? 2.5124 1.9327 1.3451 0.2377  0.2104  -0.2221 514 PRO B O   
8108 C CB  . PRO B 487 ? 2.3646 1.7438 1.3222 0.2350  0.2071  -0.2435 514 PRO B CB  
8109 C CG  . PRO B 487 ? 2.3676 1.7565 1.3711 0.2573  0.2429  -0.2331 514 PRO B CG  
8110 C CD  . PRO B 487 ? 2.4302 1.7739 1.3807 0.2801  0.2708  -0.2612 514 PRO B CD  
8111 N N   . LEU B 488 ? 2.4150 1.8418 1.2605 0.2778  0.2803  -0.2287 515 LEU B N   
8112 C CA  . LEU B 488 ? 2.4103 1.8821 1.2361 0.2788  0.2964  -0.2040 515 LEU B CA  
8113 C C   . LEU B 488 ? 2.5193 1.9686 1.2496 0.2719  0.2882  -0.2161 515 LEU B C   
8114 O O   . LEU B 488 ? 2.5750 2.0448 1.2821 0.2587  0.2765  -0.1937 515 LEU B O   
8115 C CB  . LEU B 488 ? 2.3660 1.8726 1.2131 0.3040  0.3437  -0.1976 515 LEU B CB  
8116 C CG  . LEU B 488 ? 2.1179 1.6573 1.0558 0.3121  0.3529  -0.1797 515 LEU B CG  
8117 C CD1 . LEU B 488 ? 2.1284 1.7157 1.0839 0.3358  0.3964  -0.1711 515 LEU B CD1 
8118 C CD2 . LEU B 488 ? 1.9611 1.5293 0.9501 0.2887  0.3265  -0.1504 515 LEU B CD2 
8119 N N   . SER B 489 ? 2.5693 1.9709 1.2378 0.2807  0.2941  -0.2513 516 SER B N   
8120 C CA  . SER B 489 ? 2.6837 2.0577 1.2531 0.2734  0.2839  -0.2664 516 SER B CA  
8121 C C   . SER B 489 ? 2.7086 2.0593 1.2602 0.2478  0.2288  -0.2713 516 SER B C   
8122 O O   . SER B 489 ? 2.7086 2.0436 1.1795 0.2392  0.2121  -0.2763 516 SER B O   
8123 C CB  . SER B 489 ? 2.6815 2.0094 1.1870 0.2923  0.3103  -0.3055 516 SER B CB  
8124 O OG  . SER B 489 ? 2.7039 1.9860 1.2341 0.2926  0.2971  -0.3324 516 SER B OG  
8125 N N   . LYS B 490 ? 2.6965 2.0475 1.3208 0.2359  0.2005  -0.2699 517 LYS B N   
8126 C CA  . LYS B 490 ? 2.6572 1.9990 1.2807 0.2121  0.1473  -0.2736 517 LYS B CA  
8127 C C   . LYS B 490 ? 2.6189 2.0065 1.3265 0.2029  0.1284  -0.2384 517 LYS B C   
8128 O O   . LYS B 490 ? 2.6217 2.0109 1.3909 0.1901  0.1019  -0.2423 517 LYS B O   
8129 C CB  . LYS B 490 ? 2.6566 1.9533 1.2873 0.2021  0.1292  -0.3108 517 LYS B CB  
8130 C CG  . LYS B 490 ? 2.6311 1.8775 1.2047 0.2182  0.1624  -0.3453 517 LYS B CG  
8131 C CD  . LYS B 490 ? 2.6131 1.8166 1.2241 0.2119  0.1582  -0.3723 517 LYS B CD  
8132 C CE  . LYS B 490 ? 2.7480 1.9018 1.3165 0.2363  0.2000  -0.4000 517 LYS B CE  
8133 N NZ  . LYS B 490 ? 2.7839 1.8901 1.3918 0.2323  0.2010  -0.4208 517 LYS B NZ  
8134 N N   . MET B 491 ? 2.7182 2.1411 1.4272 0.2083  0.1437  -0.2050 518 MET B N   
8135 C CA  . MET B 491 ? 2.6265 2.0896 1.4162 0.2036  0.1369  -0.1718 518 MET B CA  
8136 C C   . MET B 491 ? 2.5302 1.9976 1.3428 0.1872  0.0853  -0.1666 518 MET B C   
8137 O O   . MET B 491 ? 2.5531 2.0129 1.3068 0.1816  0.0569  -0.1635 518 MET B O   
8138 C CB  . MET B 491 ? 2.6866 2.1788 1.4594 0.2089  0.1627  -0.1397 518 MET B CB  
8139 C CG  . MET B 491 ? 2.6116 2.1419 1.4659 0.2057  0.1655  -0.1075 518 MET B CG  
8140 S SD  . MET B 491 ? 2.4527 2.0019 1.4001 0.2151  0.1927  -0.1115 518 MET B SD  
8141 C CE  . MET B 491 ? 2.4321 1.9909 1.3434 0.2344  0.2462  -0.1182 518 MET B CE  
8142 N N   . LEU B 492 ? 2.3844 1.8659 1.2830 0.1809  0.0738  -0.1653 519 LEU B N   
8143 C CA  . LEU B 492 ? 2.2643 1.7606 1.2087 0.1670  0.0296  -0.1612 519 LEU B CA  
8144 C C   . LEU B 492 ? 2.1905 1.7192 1.2270 0.1684  0.0421  -0.1371 519 LEU B C   
8145 O O   . LEU B 492 ? 2.1355 1.6642 1.2049 0.1756  0.0766  -0.1382 519 LEU B O   
8146 C CB  . LEU B 492 ? 2.2769 1.7493 1.2277 0.1529  0.0049  -0.1973 519 LEU B CB  
8147 C CG  . LEU B 492 ? 2.2525 1.7450 1.2558 0.1354  -0.0419 -0.2017 519 LEU B CG  
8148 C CD1 . LEU B 492 ? 2.4477 1.9469 1.3958 0.1325  -0.0842 -0.1983 519 LEU B CD1 
8149 C CD2 . LEU B 492 ? 2.2775 1.7445 1.3010 0.1188  -0.0492 -0.2379 519 LEU B CD2 
8150 N N   . PRO B 493 ? 2.1181 1.6735 1.1943 0.1640  0.0158  -0.1152 520 PRO B N   
8151 C CA  . PRO B 493 ? 2.0012 1.5846 1.1592 0.1655  0.0295  -0.0933 520 PRO B CA  
8152 C C   . PRO B 493 ? 1.9924 1.5734 1.2132 0.1600  0.0404  -0.1107 520 PRO B C   
8153 O O   . PRO B 493 ? 2.1033 1.6688 1.3279 0.1488  0.0211  -0.1368 520 PRO B O   
8154 C CB  . PRO B 493 ? 1.9556 1.5606 1.1407 0.1620  -0.0088 -0.0764 520 PRO B CB  
8155 C CG  . PRO B 493 ? 2.0215 1.6109 1.1218 0.1645  -0.0313 -0.0751 520 PRO B CG  
8156 C CD  . PRO B 493 ? 2.1927 1.7528 1.2366 0.1605  -0.0270 -0.1080 520 PRO B CD  
8157 N N   . VAL B 494 ? 1.9531 1.5474 1.2199 0.1664  0.0719  -0.0960 521 VAL B N   
8158 C CA  . VAL B 494 ? 2.0336 1.6173 1.3445 0.1650  0.0902  -0.1097 521 VAL B CA  
8159 C C   . VAL B 494 ? 2.1349 1.7245 1.5052 0.1485  0.0644  -0.1193 521 VAL B C   
8160 O O   . VAL B 494 ? 2.1386 1.7046 1.5236 0.1402  0.0682  -0.1406 521 VAL B O   
8161 C CB  . VAL B 494 ? 1.9307 1.5330 1.2770 0.1761  0.1253  -0.0888 521 VAL B CB  
8162 C CG1 . VAL B 494 ? 1.8939 1.5290 1.2918 0.1718  0.1169  -0.0629 521 VAL B CG1 
8163 C CG2 . VAL B 494 ? 1.8955 1.4800 1.2738 0.1789  0.1456  -0.1014 521 VAL B CG2 
8164 N N   . ASP B 495 ? 2.1115 1.7315 1.5165 0.1433  0.0388  -0.1043 522 ASP B N   
8165 C CA  . ASP B 495 ? 2.0732 1.7092 1.5404 0.1278  0.0144  -0.1135 522 ASP B CA  
8166 C C   . ASP B 495 ? 2.1145 1.7401 1.5557 0.1136  -0.0204 -0.1408 522 ASP B C   
8167 O O   . ASP B 495 ? 2.1831 1.8245 1.6773 0.0968  -0.0407 -0.1534 522 ASP B O   
8168 C CB  . ASP B 495 ? 2.0746 1.7492 1.5898 0.1312  -0.0003 -0.0891 522 ASP B CB  
8169 C CG  . ASP B 495 ? 2.1429 1.8216 1.6062 0.1426  -0.0169 -0.0720 522 ASP B CG  
8170 O OD1 . ASP B 495 ? 2.1846 1.8423 1.5828 0.1506  0.0003  -0.0684 522 ASP B OD1 
8171 O OD2 . ASP B 495 ? 2.3156 2.0180 1.8027 0.1445  -0.0461 -0.0616 522 ASP B OD2 
8172 N N   . GLU B 496 ? 2.2557 1.8574 1.6168 0.1184  -0.0274 -0.1510 523 GLU B N   
8173 C CA  . GLU B 496 ? 2.2853 1.8688 1.6087 0.1039  -0.0572 -0.1817 523 GLU B CA  
8174 C C   . GLU B 496 ? 2.3024 1.8350 1.5743 0.1023  -0.0339 -0.2084 523 GLU B C   
8175 O O   . GLU B 496 ? 2.2866 1.7968 1.5470 0.0841  -0.0519 -0.2390 523 GLU B O   
8176 C CB  . GLU B 496 ? 2.1731 1.7639 1.4339 0.1100  -0.0891 -0.1759 523 GLU B CB  
8177 C CG  . GLU B 496 ? 2.2494 1.8852 1.5568 0.1094  -0.1272 -0.1596 523 GLU B CG  
8178 C CD  . GLU B 496 ? 2.3968 2.0333 1.6361 0.1140  -0.1659 -0.1588 523 GLU B CD  
8179 O OE1 . GLU B 496 ? 2.5434 2.1450 1.6988 0.1133  -0.1640 -0.1751 523 GLU B OE1 
8180 O OE2 . GLU B 496 ? 2.4481 2.1188 1.7153 0.1200  -0.1980 -0.1417 523 GLU B OE2 
8181 N N   . PHE B 497 ? 2.2514 1.7658 1.4929 0.1211  0.0057  -0.1985 524 PHE B N   
8182 C CA  . PHE B 497 ? 2.1995 1.6650 1.3976 0.1254  0.0318  -0.2229 524 PHE B CA  
8183 C C   . PHE B 497 ? 2.3486 1.7927 1.6004 0.1138  0.0434  -0.2362 524 PHE B C   
8184 O O   . PHE B 497 ? 2.4356 1.8306 1.6549 0.1075  0.0491  -0.2652 524 PHE B O   
8185 C CB  . PHE B 497 ? 2.1259 1.5893 1.2910 0.1509  0.0718  -0.2067 524 PHE B CB  
8186 C CG  . PHE B 497 ? 2.1824 1.6033 1.3270 0.1628  0.1057  -0.2252 524 PHE B CG  
8187 C CD1 . PHE B 497 ? 2.2436 1.6170 1.3181 0.1631  0.1060  -0.2570 524 PHE B CD1 
8188 C CD2 . PHE B 497 ? 2.0306 1.4569 1.2227 0.1757  0.1370  -0.2108 524 PHE B CD2 
8189 C CE1 . PHE B 497 ? 2.1786 1.5079 1.2329 0.1781  0.1382  -0.2741 524 PHE B CE1 
8190 C CE2 . PHE B 497 ? 2.0533 1.4390 1.2258 0.1914  0.1669  -0.2259 524 PHE B CE2 
8191 C CZ  . PHE B 497 ? 2.1469 1.4828 1.2514 0.1937  0.1683  -0.2575 524 PHE B CZ  
8192 N N   . LEU B 498 ? 2.2721 1.7473 1.6016 0.1103  0.0483  -0.2157 525 LEU B N   
8193 C CA  . LEU B 498 ? 2.2202 1.6735 1.5984 0.0965  0.0595  -0.2263 525 LEU B CA  
8194 C C   . LEU B 498 ? 2.3181 1.7653 1.7139 0.0651  0.0265  -0.2528 525 LEU B C   
8195 O O   . LEU B 498 ? 2.3225 1.7206 1.7074 0.0514  0.0347  -0.2776 525 LEU B O   
8196 C CB  . LEU B 498 ? 1.9573 1.4452 1.4073 0.1012  0.0758  -0.1973 525 LEU B CB  
8197 C CG  . LEU B 498 ? 1.9482 1.4401 1.3889 0.1284  0.1111  -0.1744 525 LEU B CG  
8198 C CD1 . LEU B 498 ? 1.7464 1.2683 1.2562 0.1283  0.1237  -0.1501 525 LEU B CD1 
8199 C CD2 . LEU B 498 ? 1.9518 1.3918 1.3501 0.1423  0.1394  -0.1896 525 LEU B CD2 
8200 N N   . PRO B 499 ? 2.3646 1.8583 1.7879 0.0523  -0.0111 -0.2499 526 PRO B N   
8201 C CA  . PRO B 499 ? 2.4357 1.9290 1.8713 0.0213  -0.0457 -0.2792 526 PRO B CA  
8202 C C   . PRO B 499 ? 2.4942 1.9382 1.8466 0.0147  -0.0566 -0.3120 526 PRO B C   
8203 O O   . PRO B 499 ? 2.4572 1.8810 1.8136 -0.0145 -0.0746 -0.3425 526 PRO B O   
8204 C CB  . PRO B 499 ? 2.3722 1.9320 1.8450 0.0197  -0.0842 -0.2647 526 PRO B CB  
8205 C CG  . PRO B 499 ? 2.2585 1.8489 1.7709 0.0414  -0.0622 -0.2282 526 PRO B CG  
8206 C CD  . PRO B 499 ? 2.2531 1.8037 1.7105 0.0640  -0.0233 -0.2193 526 PRO B CD  
8207 N N   . VAL B 500 ? 2.6467 2.0705 1.9225 0.0388  -0.0454 -0.3082 527 VAL B N   
8208 C CA  . VAL B 500 ? 2.6729 2.0418 1.8632 0.0353  -0.0481 -0.3411 527 VAL B CA  
8209 C C   . VAL B 500 ? 2.7193 2.0224 1.8995 0.0343  -0.0126 -0.3600 527 VAL B C   
8210 O O   . VAL B 500 ? 2.7600 2.0107 1.8959 0.0173  -0.0195 -0.3956 527 VAL B O   
8211 C CB  . VAL B 500 ? 2.6832 2.0510 1.7947 0.0622  -0.0408 -0.3302 527 VAL B CB  
8212 C CG1 . VAL B 500 ? 2.7730 2.0770 1.7927 0.0649  -0.0300 -0.3636 527 VAL B CG1 
8213 C CG2 . VAL B 500 ? 2.6358 2.0521 1.7390 0.0593  -0.0830 -0.3177 527 VAL B CG2 
8214 N N   . MET B 501 ? 2.6743 1.9762 1.8940 0.0519  0.0242  -0.3370 528 MET B N   
8215 C CA  . MET B 501 ? 2.6793 1.9149 1.8813 0.0590  0.0597  -0.3505 528 MET B CA  
8216 C C   . MET B 501 ? 2.6427 1.8491 1.8916 0.0269  0.0559  -0.3666 528 MET B C   
8217 O O   . MET B 501 ? 2.6359 1.7696 1.8492 0.0221  0.0723  -0.3911 528 MET B O   
8218 C CB  . MET B 501 ? 2.6822 1.9286 1.9021 0.0928  0.0989  -0.3195 528 MET B CB  
8219 C CG  . MET B 501 ? 2.6861 1.9394 1.8449 0.1244  0.1150  -0.3123 528 MET B CG  
8220 S SD  . MET B 501 ? 2.6251 1.8047 1.6815 0.1310  0.1222  -0.3536 528 MET B SD  
8221 C CE  . MET B 501 ? 2.6756 1.7815 1.7409 0.1402  0.1575  -0.3661 528 MET B CE  
8222 N N   . PHE B 502 ? 2.3873 1.9313 1.9274 0.1063  0.0634  -0.4737 529 PHE B N   
8223 C CA  . PHE B 502 ? 2.3566 1.8216 1.9203 0.0856  0.0800  -0.5018 529 PHE B CA  
8224 C C   . PHE B 502 ? 2.3165 1.7963 1.9173 0.0558  0.0565  -0.5416 529 PHE B C   
8225 O O   . PHE B 502 ? 2.2780 1.7141 1.9209 0.0260  0.0683  -0.5695 529 PHE B O   
8226 C CB  . PHE B 502 ? 2.2027 1.6329 1.8009 0.0705  0.0990  -0.4781 529 PHE B CB  
8227 C CG  . PHE B 502 ? 2.2243 1.7166 1.8789 0.0466  0.0758  -0.4575 529 PHE B CG  
8228 C CD1 . PHE B 502 ? 2.2008 1.7015 1.9143 0.0125  0.0617  -0.4854 529 PHE B CD1 
8229 C CD2 . PHE B 502 ? 2.1551 1.6953 1.8051 0.0590  0.0690  -0.4142 529 PHE B CD2 
8230 C CE1 . PHE B 502 ? 2.0598 1.6125 1.8195 -0.0023 0.0375  -0.4687 529 PHE B CE1 
8231 C CE2 . PHE B 502 ? 2.0028 1.5866 1.6945 0.0390  0.0482  -0.3947 529 PHE B CE2 
8232 C CZ  . PHE B 502 ? 1.9776 1.5653 1.7210 0.0113  0.0310  -0.4210 529 PHE B CZ  
8233 N N   . ASP B 503 ? 2.3389 1.8794 1.9224 0.0635  0.0243  -0.5481 530 ASP B N   
8234 C CA  . ASP B 503 ? 2.3921 1.9414 1.9880 0.0503  -0.0017 -0.5948 530 ASP B CA  
8235 C C   . ASP B 503 ? 2.3361 1.9064 2.0078 0.0182  -0.0233 -0.6156 530 ASP B C   
8236 O O   . ASP B 503 ? 2.3201 1.8719 2.0312 -0.0039 -0.0253 -0.6659 530 ASP B O   
8237 C CB  . ASP B 503 ? 2.3621 1.8432 1.9341 0.0522  0.0211  -0.6352 530 ASP B CB  
8238 C CG  . ASP B 503 ? 2.3147 1.8158 1.8700 0.0544  -0.0077 -0.6781 530 ASP B CG  
8239 O OD1 . ASP B 503 ? 2.3270 1.8900 1.8863 0.0561  -0.0470 -0.6776 530 ASP B OD1 
8240 O OD2 . ASP B 503 ? 2.4449 1.8914 1.9740 0.0569  0.0082  -0.7127 530 ASP B OD2 
8241 N N   . LYS B 504 ? 2.3564 1.9689 2.0502 0.0155  -0.0398 -0.5811 531 LYS B N   
8242 C CA  . LYS B 504 ? 2.2698 1.9136 2.0329 -0.0064 -0.0672 -0.6014 531 LYS B CA  
8243 C C   . LYS B 504 ? 2.2330 1.9311 1.9719 0.0087  -0.1130 -0.5794 531 LYS B C   
8244 O O   . LYS B 504 ? 2.2611 1.9856 2.0467 -0.0002 -0.1367 -0.5807 531 LYS B O   
8245 C CB  . LYS B 504 ? 2.2309 1.8509 2.0500 -0.0285 -0.0372 -0.5860 531 LYS B CB  
8246 C CG  . LYS B 504 ? 2.1281 1.6771 1.9684 -0.0512 0.0089  -0.6159 531 LYS B CG  
8247 C CD  . LYS B 504 ? 2.1269 1.6859 2.0321 -0.0820 -0.0009 -0.6847 531 LYS B CD  
8248 C CE  . LYS B 504 ? 2.0975 1.5728 2.0184 -0.1145 0.0541  -0.7141 531 LYS B CE  
8249 N NZ  . LYS B 504 ? 2.2290 1.6668 2.1704 -0.1302 0.0907  -0.6829 531 LYS B NZ  
8250 N N   . HIS B 505 ? 2.2136 1.9222 1.8731 0.0317  -0.1240 -0.5607 532 HIS B N   
8251 C CA  . HIS B 505 ? 2.1559 1.8942 1.7683 0.0445  -0.1625 -0.5393 532 HIS B CA  
8252 C C   . HIS B 505 ? 2.1985 1.9518 1.8157 0.0516  -0.2134 -0.5887 532 HIS B C   
8253 O O   . HIS B 505 ? 2.1575 1.9038 1.7744 0.0540  -0.2173 -0.6329 532 HIS B O   
8254 C CB  . HIS B 505 ? 2.1645 1.9045 1.6856 0.0612  -0.1494 -0.5071 532 HIS B CB  
8255 C CG  . HIS B 505 ? 2.2027 1.9545 1.6631 0.0661  -0.1714 -0.4711 532 HIS B CG  
8256 N ND1 . HIS B 505 ? 2.1725 1.9309 1.6347 0.0568  -0.1550 -0.4242 532 HIS B ND1 
8257 C CD2 . HIS B 505 ? 2.2431 1.9894 1.6285 0.0791  -0.2075 -0.4758 532 HIS B CD2 
8258 C CE1 . HIS B 505 ? 2.1626 1.9166 1.5534 0.0601  -0.1770 -0.4014 532 HIS B CE1 
8259 N NE2 . HIS B 505 ? 2.2162 1.9579 1.5539 0.0751  -0.2089 -0.4308 532 HIS B NE2 
8260 N N   . PRO B 506 ? 2.2997 2.0713 1.9175 0.0586  -0.2557 -0.5853 533 PRO B N   
8261 C CA  . PRO B 506 ? 2.2860 2.0759 1.9125 0.0731  -0.3114 -0.6401 533 PRO B CA  
8262 C C   . PRO B 506 ? 2.2222 1.9970 1.7467 0.0987  -0.3364 -0.6490 533 PRO B C   
8263 O O   . PRO B 506 ? 2.2042 1.9872 1.7419 0.1062  -0.3611 -0.7052 533 PRO B O   
8264 C CB  . PRO B 506 ? 2.2298 2.0342 1.8662 0.0824  -0.3495 -0.6261 533 PRO B CB  
8265 C CG  . PRO B 506 ? 2.1003 1.8820 1.6806 0.0781  -0.3191 -0.5538 533 PRO B CG  
8266 C CD  . PRO B 506 ? 2.1412 1.9151 1.7506 0.0571  -0.2576 -0.5360 533 PRO B CD  
8267 N N   . VAL B 507 ? 2.3136 2.0654 1.7352 0.1099  -0.3282 -0.5982 534 VAL B N   
8268 C CA  . VAL B 507 ? 2.3850 2.1141 1.6955 0.1324  -0.3463 -0.6033 534 VAL B CA  
8269 C C   . VAL B 507 ? 2.4764 2.2036 1.7821 0.1270  -0.3059 -0.6152 534 VAL B C   
8270 O O   . VAL B 507 ? 2.4962 2.2264 1.8221 0.1125  -0.2552 -0.5856 534 VAL B O   
8271 C CB  . VAL B 507 ? 2.4460 2.1449 1.6437 0.1385  -0.3423 -0.5467 534 VAL B CB  
8272 C CG1 . VAL B 507 ? 2.6007 2.2641 1.6704 0.1619  -0.3635 -0.5555 534 VAL B CG1 
8273 C CG2 . VAL B 507 ? 2.3930 2.0839 1.5967 0.1432  -0.3762 -0.5293 534 VAL B CG2 
8274 N N   . SER B 508 ? 2.5806 2.3015 1.8563 0.1431  -0.3312 -0.6614 535 SER B N   
8275 C CA  . SER B 508 ? 2.6318 2.3448 1.8921 0.1430  -0.2981 -0.6774 535 SER B CA  
8276 C C   . SER B 508 ? 2.7351 2.4312 1.8753 0.1579  -0.2821 -0.6485 535 SER B C   
8277 O O   . SER B 508 ? 2.6438 2.3387 1.7682 0.1597  -0.2470 -0.6531 535 SER B O   
8278 C CB  . SER B 508 ? 2.5368 2.2516 1.8314 0.1491  -0.3296 -0.7474 535 SER B CB  
8279 O OG  . SER B 508 ? 2.4923 2.2233 1.9067 0.1247  -0.3237 -0.7799 535 SER B OG  
8280 N N   . GLU B 509 ? 2.8529 2.5309 1.9027 0.1684  -0.3046 -0.6211 536 GLU B N   
8281 C CA  . GLU B 509 ? 2.9213 2.5810 1.8556 0.1729  -0.2771 -0.5908 536 GLU B CA  
8282 C C   . GLU B 509 ? 2.9268 2.6122 1.8827 0.1515  -0.2171 -0.5464 536 GLU B C   
8283 O O   . GLU B 509 ? 3.0206 2.7113 1.9120 0.1510  -0.1809 -0.5335 536 GLU B O   
8284 C CB  . GLU B 509 ? 2.9771 2.5917 1.7942 0.1860  -0.3120 -0.5720 536 GLU B CB  
8285 C CG  . GLU B 509 ? 3.1587 2.7406 1.8374 0.1896  -0.2858 -0.5535 536 GLU B CG  
8286 C CD  . GLU B 509 ? 3.3852 2.9028 1.9328 0.1950  -0.3062 -0.5229 536 GLU B CD  
8287 O OE1 . GLU B 509 ? 3.3259 2.8270 1.8923 0.2006  -0.3444 -0.5149 536 GLU B OE1 
8288 O OE2 . GLU B 509 ? 3.4523 2.9299 1.8716 0.1938  -0.2820 -0.5080 536 GLU B OE2 
8289 N N   . TYR B 510 ? 2.8117 2.5171 1.8582 0.1351  -0.2063 -0.5272 537 TYR B N   
8290 C CA  . TYR B 510 ? 2.7407 2.4745 1.8178 0.1194  -0.1550 -0.4913 537 TYR B CA  
8291 C C   . TYR B 510 ? 2.6901 2.4407 1.8352 0.1239  -0.1252 -0.5128 537 TYR B C   
8292 O O   . TYR B 510 ? 2.6349 2.4087 1.7652 0.1276  -0.0855 -0.5024 537 TYR B O   
8293 C CB  . TYR B 510 ? 2.6005 2.3391 1.7299 0.1027  -0.1582 -0.4582 537 TYR B CB  
8294 C CG  . TYR B 510 ? 2.6432 2.3532 1.6966 0.0994  -0.1844 -0.4315 537 TYR B CG  
8295 C CD1 . TYR B 510 ? 2.8570 2.5327 1.7880 0.1083  -0.1952 -0.4309 537 TYR B CD1 
8296 C CD2 . TYR B 510 ? 2.5579 2.2645 1.6511 0.0887  -0.1970 -0.4063 537 TYR B CD2 
8297 C CE1 . TYR B 510 ? 2.9549 2.5831 1.7965 0.1076  -0.2180 -0.4053 537 TYR B CE1 
8298 C CE2 . TYR B 510 ? 2.6870 2.3541 1.6992 0.0891  -0.2219 -0.3818 537 TYR B CE2 
8299 C CZ  . TYR B 510 ? 2.8567 2.4796 1.7389 0.0989  -0.2323 -0.3809 537 TYR B CZ  
8300 O OH  . TYR B 510 ? 2.9541 2.5173 1.7359 0.1015  -0.2562 -0.3556 537 TYR B OH  
8301 N N   . LYS B 511 ? 2.6663 2.4029 1.8826 0.1242  -0.1426 -0.5464 538 LYS B N   
8302 C CA  . LYS B 511 ? 2.5928 2.3208 1.8551 0.1286  -0.1143 -0.5688 538 LYS B CA  
8303 C C   . LYS B 511 ? 2.5667 2.2877 1.7707 0.1485  -0.1068 -0.5975 538 LYS B C   
8304 O O   . LYS B 511 ? 2.4375 2.1446 1.6584 0.1583  -0.0801 -0.6130 538 LYS B O   
8305 C CB  . LYS B 511 ? 2.4944 2.1998 1.8383 0.1158  -0.1299 -0.6025 538 LYS B CB  
8306 C CG  . LYS B 511 ? 2.4350 2.1443 1.8495 0.0965  -0.1242 -0.5776 538 LYS B CG  
8307 C CD  . LYS B 511 ? 2.3287 2.0152 1.8249 0.0783  -0.1271 -0.6174 538 LYS B CD  
8308 C CE  . LYS B 511 ? 2.2772 1.9751 1.7867 0.0769  -0.1743 -0.6667 538 LYS B CE  
8309 N NZ  . LYS B 511 ? 2.2006 1.8915 1.8046 0.0511  -0.1745 -0.7103 538 LYS B NZ  
8310 N N   . ALA B 512 ? 2.7010 2.4225 1.8278 0.1574  -0.1298 -0.6052 539 ALA B N   
8311 C CA  . ALA B 512 ? 2.7735 2.4888 1.8380 0.1770  -0.1217 -0.6321 539 ALA B CA  
8312 C C   . ALA B 512 ? 2.7673 2.5146 1.7887 0.1846  -0.0773 -0.6078 539 ALA B C   
8313 O O   . ALA B 512 ? 2.7160 2.4655 1.7202 0.2036  -0.0564 -0.6302 539 ALA B O   
8314 C CB  . ALA B 512 ? 2.8082 2.5055 1.7965 0.1861  -0.1631 -0.6514 539 ALA B CB  
8315 N N   . HIS B 513 ? 2.8094 2.5839 1.8152 0.1699  -0.0618 -0.5666 540 HIS B N   
8316 C CA  . HIS B 513 ? 2.7777 2.5970 1.7512 0.1723  -0.0177 -0.5513 540 HIS B CA  
8317 C C   . HIS B 513 ? 2.6710 2.5165 1.7131 0.1858  0.0121  -0.5541 540 HIS B C   
8318 O O   . HIS B 513 ? 2.6188 2.4998 1.6430 0.2044  0.0419  -0.5669 540 HIS B O   
8319 C CB  . HIS B 513 ? 2.8934 2.7304 1.8324 0.1466  -0.0067 -0.5106 540 HIS B CB  
8320 C CG  . HIS B 513 ? 2.9961 2.7937 1.8327 0.1396  -0.0287 -0.5067 540 HIS B CG  
8321 N ND1 . HIS B 513 ? 3.0976 2.8476 1.9215 0.1375  -0.0762 -0.5024 540 HIS B ND1 
8322 C CD2 . HIS B 513 ? 2.8522 2.6450 1.5859 0.1374  -0.0097 -0.5087 540 HIS B CD2 
8323 C CE1 . HIS B 513 ? 2.9741 2.6837 1.6833 0.1389  -0.0894 -0.5002 540 HIS B CE1 
8324 N NE2 . HIS B 513 ? 2.8024 2.5325 1.4517 0.1360  -0.0468 -0.5024 540 HIS B NE2 
8325 N N   . PHE B 514 ? 2.5906 2.4162 1.7058 0.1802  0.0041  -0.5450 541 PHE B N   
8326 C CA  . PHE B 514 ? 2.4491 2.2764 1.6144 0.1982  0.0279  -0.5483 541 PHE B CA  
8327 C C   . PHE B 514 ? 2.5301 2.2996 1.7012 0.2161  0.0204  -0.5866 541 PHE B C   
8328 O O   . PHE B 514 ? 2.6089 2.3353 1.8010 0.2009  -0.0048 -0.6017 541 PHE B O   
8329 C CB  . PHE B 514 ? 2.2463 2.0696 1.4745 0.1818  0.0282  -0.5176 541 PHE B CB  
8330 C CG  . PHE B 514 ? 2.1576 2.0347 1.3828 0.1644  0.0406  -0.4813 541 PHE B CG  
8331 C CD1 . PHE B 514 ? 2.2482 2.1215 1.4525 0.1368  0.0208  -0.4591 541 PHE B CD1 
8332 C CD2 . PHE B 514 ? 2.1856 2.1145 1.4256 0.1772  0.0709  -0.4733 541 PHE B CD2 
8333 C CE1 . PHE B 514 ? 2.2697 2.1801 1.4624 0.1166  0.0357  -0.4264 541 PHE B CE1 
8334 C CE2 . PHE B 514 ? 2.1863 2.1672 1.4276 0.1554  0.0852  -0.4450 541 PHE B CE2 
8335 C CZ  . PHE B 514 ? 2.2116 2.1784 1.4266 0.1222  0.0699  -0.4200 541 PHE B CZ  
8336 N N   . SER B 515 ? 2.5331 2.3023 1.6856 0.2487  0.0427  -0.6062 542 SER B N   
8337 C CA  . SER B 515 ? 2.5106 2.2136 1.6506 0.2666  0.0393  -0.6444 542 SER B CA  
8338 C C   . SER B 515 ? 2.5796 2.2153 1.7626 0.2654  0.0474  -0.6437 542 SER B C   
8339 O O   . SER B 515 ? 2.6795 2.2654 1.8927 0.2390  0.0336  -0.6556 542 SER B O   
8340 C CB  . SER B 515 ? 2.4274 2.1482 1.5166 0.3069  0.0579  -0.6684 542 SER B CB  
8341 O OG  . SER B 515 ? 2.4590 2.2132 1.5615 0.3344  0.0821  -0.6566 542 SER B OG  
8342 N N   . LEU B 516 ? 2.4599 2.0918 1.6430 0.2944  0.0705  -0.6335 543 LEU B N   
8343 C CA  . LEU B 516 ? 2.3685 1.9172 1.5689 0.2987  0.0827  -0.6323 543 LEU B CA  
8344 C C   . LEU B 516 ? 2.4159 1.9774 1.6731 0.2678  0.0808  -0.5964 543 LEU B C   
8345 O O   . LEU B 516 ? 2.3163 1.9440 1.5891 0.2725  0.0847  -0.5672 543 LEU B O   
8346 C CB  . LEU B 516 ? 2.2197 1.7488 1.3823 0.3524  0.1027  -0.6385 543 LEU B CB  
8347 C CG  . LEU B 516 ? 2.3474 1.7679 1.5005 0.3650  0.1179  -0.6363 543 LEU B CG  
8348 C CD1 . LEU B 516 ? 2.3265 1.6386 1.4638 0.3402  0.1208  -0.6645 543 LEU B CD1 
8349 C CD2 . LEU B 516 ? 2.3322 1.7331 1.4341 0.4304  0.1300  -0.6454 543 LEU B CD2 
8350 N N   . ARG B 517 ? 2.4310 1.9317 1.7218 0.2345  0.0764  -0.6025 544 ARG B N   
8351 C CA  . ARG B 517 ? 2.4917 1.9991 1.8390 0.2034  0.0739  -0.5737 544 ARG B CA  
8352 C C   . ARG B 517 ? 2.4966 1.9011 1.8543 0.1934  0.0955  -0.5831 544 ARG B C   
8353 O O   . ARG B 517 ? 2.4403 1.8143 1.8390 0.1547  0.0920  -0.5994 544 ARG B O   
8354 C CB  . ARG B 517 ? 2.4959 2.0481 1.8795 0.1665  0.0440  -0.5757 544 ARG B CB  
8355 C CG  . ARG B 517 ? 2.5269 2.1464 1.8729 0.1745  0.0243  -0.5769 544 ARG B CG  
8356 C CD  . ARG B 517 ? 2.5128 2.1537 1.8778 0.1468  -0.0110 -0.5848 544 ARG B CD  
8357 N NE  . ARG B 517 ? 2.5223 2.1159 1.9176 0.1301  -0.0226 -0.6276 544 ARG B NE  
8358 C CZ  . ARG B 517 ? 2.3990 1.9783 1.7658 0.1359  -0.0365 -0.6684 544 ARG B CZ  
8359 N NH1 . ARG B 517 ? 2.4243 2.0280 1.7260 0.1601  -0.0405 -0.6703 544 ARG B NH1 
8360 N NH2 . ARG B 517 ? 2.3341 1.8753 1.7398 0.1148  -0.0445 -0.7116 544 ARG B NH2 
8361 N N   . ASN B 518 ? 2.5374 1.8866 1.8540 0.2293  0.1189  -0.5759 545 ASN B N   
8362 C CA  . ASN B 518 ? 2.5336 1.7600 1.8307 0.2252  0.1460  -0.5840 545 ASN B CA  
8363 C C   . ASN B 518 ? 2.4474 1.6585 1.7567 0.2315  0.1588  -0.5470 545 ASN B C   
8364 O O   . ASN B 518 ? 2.5274 1.6445 1.7827 0.2613  0.1810  -0.5440 545 ASN B O   
8365 C CB  . ASN B 518 ? 2.5849 1.7232 1.7987 0.2681  0.1619  -0.6098 545 ASN B CB  
8366 C CG  . ASN B 518 ? 2.5130 1.6905 1.6838 0.3312  0.1595  -0.5958 545 ASN B CG  
8367 O OD1 . ASN B 518 ? 2.4807 1.7740 1.6870 0.3374  0.1448  -0.5745 545 ASN B OD1 
8368 N ND2 . ASN B 518 ? 2.5172 1.5963 1.6086 0.3787  0.1745  -0.6117 545 ASN B ND2 
8369 N N   . LEU B 519 ? 2.3980 1.6926 1.7695 0.2061  0.1438  -0.5191 546 LEU B N   
8370 C CA  . LEU B 519 ? 2.2923 1.5814 1.6791 0.2107  0.1530  -0.4839 546 LEU B CA  
8371 C C   . LEU B 519 ? 2.3483 1.5498 1.7586 0.1717  0.1737  -0.4863 546 LEU B C   
8372 O O   . LEU B 519 ? 2.3071 1.5229 1.7697 0.1259  0.1671  -0.5042 546 LEU B O   
8373 C CB  . LEU B 519 ? 2.1069 1.5155 1.5438 0.1984  0.1304  -0.4538 546 LEU B CB  
8374 C CG  . LEU B 519 ? 2.0163 1.4497 1.4552 0.2218  0.1351  -0.4200 546 LEU B CG  
8375 C CD1 . LEU B 519 ? 1.8923 1.3406 1.2801 0.2791  0.1389  -0.4283 546 LEU B CD1 
8376 C CD2 . LEU B 519 ? 1.9908 1.5248 1.4800 0.1955  0.1162  -0.3920 546 LEU B CD2 
8377 N N   . HIS B 520 ? 2.6941 1.8049 2.0633 0.1914  0.1989  -0.4720 547 HIS B N   
8378 C CA  . HIS B 520 ? 2.6962 1.7123 2.0764 0.1538  0.2278  -0.4732 547 HIS B CA  
8379 C C   . HIS B 520 ? 2.6222 1.6978 2.0590 0.1391  0.2196  -0.4368 547 HIS B C   
8380 O O   . HIS B 520 ? 2.6030 1.6544 2.0082 0.1709  0.2260  -0.4086 547 HIS B O   
8381 C CB  . HIS B 520 ? 2.8926 1.7529 2.1750 0.1839  0.2629  -0.4781 547 HIS B CB  
8382 C CG  . HIS B 520 ? 2.9719 1.7562 2.1883 0.1985  0.2730  -0.5146 547 HIS B CG  
8383 N ND1 . HIS B 520 ? 3.1947 1.8134 2.3355 0.1896  0.3131  -0.5351 547 HIS B ND1 
8384 C CD2 . HIS B 520 ? 2.8669 1.7101 2.0741 0.2208  0.2505  -0.5348 547 HIS B CD2 
8385 C CE1 . HIS B 520 ? 3.2572 1.8363 2.3468 0.2065  0.3126  -0.5665 547 HIS B CE1 
8386 N NE2 . HIS B 520 ? 3.1382 1.8553 2.2693 0.2270  0.2739  -0.5671 547 HIS B NE2 
8387 N N   . ALA B 521 ? 2.2819 1.4346 1.8001 0.0943  0.2022  -0.4399 548 ALA B N   
8388 C CA  . ALA B 521 ? 2.2264 1.4412 1.7996 0.0794  0.1899  -0.4074 548 ALA B CA  
8389 C C   . ALA B 521 ? 2.2089 1.3666 1.8232 0.0351  0.2146  -0.4163 548 ALA B C   
8390 O O   . ALA B 521 ? 2.2261 1.3634 1.8728 -0.0026 0.2238  -0.4552 548 ALA B O   
8391 C CB  . ALA B 521 ? 2.0766 1.4156 1.7015 0.0670  0.1498  -0.4027 548 ALA B CB  
8392 N N   . PHE B 522 ? 2.1969 1.3338 1.8126 0.0389  0.2261  -0.3841 549 PHE B N   
8393 C CA  . PHE B 522 ? 2.1140 1.2061 1.7708 -0.0024 0.2517  -0.3889 549 PHE B CA  
8394 C C   . PHE B 522 ? 2.0631 1.2309 1.7691 -0.0043 0.2301  -0.3530 549 PHE B C   
8395 O O   . PHE B 522 ? 2.0297 1.2673 1.7273 0.0253  0.2016  -0.3233 549 PHE B O   
8396 C CB  . PHE B 522 ? 2.0387 0.9792 1.6192 0.0037  0.3017  -0.3888 549 PHE B CB  
8397 C CG  . PHE B 522 ? 2.2734 1.1188 1.7906 0.0054  0.3263  -0.4236 549 PHE B CG  
8398 C CD1 . PHE B 522 ? 2.2394 1.0767 1.8011 -0.0453 0.3406  -0.4707 549 PHE B CD1 
8399 C CD2 . PHE B 522 ? 2.3905 1.1561 1.8037 0.0598  0.3331  -0.4136 549 PHE B CD2 
8400 C CE1 . PHE B 522 ? 2.2979 1.0419 1.7981 -0.0470 0.3646  -0.5044 549 PHE B CE1 
8401 C CE2 . PHE B 522 ? 2.4413 1.1088 1.7868 0.0638  0.3551  -0.4457 549 PHE B CE2 
8402 C CZ  . PHE B 522 ? 2.3644 1.0174 1.7517 0.0078  0.3726  -0.4897 549 PHE B CZ  
8403 N N   . SER B 523 ? 2.0490 1.2030 1.8074 -0.0422 0.2463  -0.3592 550 SER B N   
8404 C CA  . SER B 523 ? 1.9570 1.1756 1.7633 -0.0465 0.2263  -0.3288 550 SER B CA  
8405 C C   . SER B 523 ? 2.0521 1.1922 1.8626 -0.0677 0.2664  -0.3240 550 SER B C   
8406 O O   . SER B 523 ? 2.0322 1.1096 1.8569 -0.1041 0.3032  -0.3597 550 SER B O   
8407 C CB  . SER B 523 ? 1.8917 1.2160 1.7788 -0.0709 0.1874  -0.3472 550 SER B CB  
8408 O OG  . SER B 523 ? 1.8716 1.2395 1.8009 -0.0775 0.1725  -0.3221 550 SER B OG  
8409 N N   . VAL B 524 ? 1.9996 1.1419 1.7956 -0.0474 0.2618  -0.2824 551 VAL B N   
8410 C CA  . VAL B 524 ? 1.9364 1.0128 1.7374 -0.0667 0.2964  -0.2746 551 VAL B CA  
8411 C C   . VAL B 524 ? 1.9256 1.0691 1.8273 -0.1121 0.2896  -0.3003 551 VAL B C   
8412 O O   . VAL B 524 ? 1.7617 1.0128 1.7191 -0.1114 0.2437  -0.2977 551 VAL B O   
8413 C CB  . VAL B 524 ? 2.0119 1.0862 1.7770 -0.0311 0.2858  -0.2259 551 VAL B CB  
8414 C CG1 . VAL B 524 ? 2.0819 1.0679 1.8335 -0.0468 0.3263  -0.2178 551 VAL B CG1 
8415 C CG2 . VAL B 524 ? 1.9180 0.9566 1.5969 0.0215  0.2806  -0.2090 551 VAL B CG2 
8416 N N   . GLU B 525 ? 2.0136 1.0904 1.9343 -0.1509 0.3363  -0.3287 552 GLU B N   
8417 C CA  . GLU B 525 ? 1.9778 1.1229 2.0027 -0.1936 0.3337  -0.3637 552 GLU B CA  
8418 C C   . GLU B 525 ? 1.9906 1.0664 2.0181 -0.2180 0.3822  -0.3599 552 GLU B C   
8419 O O   . GLU B 525 ? 2.1321 1.1100 2.1149 -0.2390 0.4362  -0.3725 552 GLU B O   
8420 C CB  . GLU B 525 ? 1.9989 1.1609 2.0729 -0.2305 0.3435  -0.4271 552 GLU B CB  
8421 C CG  . GLU B 525 ? 1.8747 1.1328 2.0690 -0.2679 0.3298  -0.4749 552 GLU B CG  
8422 C CD  . GLU B 525 ? 2.0362 1.4195 2.2772 -0.2397 0.2568  -0.4612 552 GLU B CD  
8423 O OE1 . GLU B 525 ? 2.0560 1.4595 2.2442 -0.2026 0.2196  -0.4282 552 GLU B OE1 
8424 O OE2 . GLU B 525 ? 2.0169 1.4737 2.3420 -0.2542 0.2382  -0.4855 552 GLU B OE2 
8425 N N   . PRO B 526 ? 1.8942 1.0275 1.9666 -0.2139 0.3613  -0.3376 553 PRO B N   
8426 C CA  . PRO B 526 ? 1.7854 1.0381 1.9042 -0.1907 0.2959  -0.3170 553 PRO B CA  
8427 C C   . PRO B 526 ? 1.7837 1.0415 1.8306 -0.1429 0.2633  -0.2635 553 PRO B C   
8428 O O   . PRO B 526 ? 1.8216 0.9965 1.7882 -0.1200 0.2876  -0.2369 553 PRO B O   
8429 C CB  . PRO B 526 ? 1.7387 1.0087 1.9076 -0.2048 0.3032  -0.3111 553 PRO B CB  
8430 C CG  . PRO B 526 ? 1.7504 0.8932 1.8532 -0.2120 0.3656  -0.2957 553 PRO B CG  
8431 C CD  . PRO B 526 ? 1.7278 0.7910 1.7943 -0.2337 0.4089  -0.3309 553 PRO B CD  
8432 N N   . LEU B 527 ? 1.5995 0.9531 1.6708 -0.1268 0.2084  -0.2513 554 LEU B N   
8433 C CA  . LEU B 527 ? 1.5640 0.9361 1.5770 -0.0898 0.1811  -0.2074 554 LEU B CA  
8434 C C   . LEU B 527 ? 1.5419 0.8853 1.5273 -0.0737 0.1881  -0.1644 554 LEU B C   
8435 O O   . LEU B 527 ? 1.6076 0.9593 1.6334 -0.0880 0.1893  -0.1607 554 LEU B O   
8436 C CB  . LEU B 527 ? 1.4749 0.9431 1.5122 -0.0839 0.1271  -0.2057 554 LEU B CB  
8437 C CG  . LEU B 527 ? 1.6800 1.1805 1.7325 -0.0914 0.1117  -0.2460 554 LEU B CG  
8438 C CD1 . LEU B 527 ? 1.6960 1.2765 1.7636 -0.0848 0.0577  -0.2448 554 LEU B CD1 
8439 C CD2 . LEU B 527 ? 1.6803 1.1451 1.6692 -0.0728 0.1266  -0.2429 554 LEU B CD2 
8440 N N   . LEU B 528 ? 1.5649 0.8782 1.4827 -0.0412 0.1911  -0.1360 555 LEU B N   
8441 C CA  . LEU B 528 ? 1.5615 0.8440 1.4465 -0.0208 0.1966  -0.0995 555 LEU B CA  
8442 C C   . LEU B 528 ? 1.5126 0.8765 1.4063 -0.0088 0.1556  -0.0687 555 LEU B C   
8443 O O   . LEU B 528 ? 1.4270 0.7792 1.3087 0.0020  0.1548  -0.0413 555 LEU B O   
8444 C CB  . LEU B 528 ? 1.5546 0.7546 1.3578 0.0139  0.2210  -0.0918 555 LEU B CB  
8445 C CG  . LEU B 528 ? 1.7316 0.8147 1.4972 0.0034  0.2703  -0.1162 555 LEU B CG  
8446 C CD1 . LEU B 528 ? 1.6996 0.6974 1.3672 0.0488  0.2846  -0.1094 555 LEU B CD1 
8447 C CD2 . LEU B 528 ? 1.6288 0.6528 1.4087 -0.0215 0.3026  -0.1138 555 LEU B CD2 
8448 N N   . ILE B 529 ? 1.4452 0.8833 1.3524 -0.0121 0.1241  -0.0735 556 ILE B N   
8449 C CA  . ILE B 529 ? 1.3752 0.8789 1.2771 -0.0068 0.0918  -0.0462 556 ILE B CA  
8450 C C   . ILE B 529 ? 1.2829 0.8422 1.2133 -0.0261 0.0599  -0.0570 556 ILE B C   
8451 O O   . ILE B 529 ? 1.3586 0.9294 1.2959 -0.0315 0.0558  -0.0852 556 ILE B O   
8452 C CB  . ILE B 529 ? 1.4203 0.9480 1.2771 0.0186  0.0898  -0.0379 556 ILE B CB  
8453 C CG1 . ILE B 529 ? 1.4946 0.9735 1.3179 0.0474  0.1092  -0.0245 556 ILE B CG1 
8454 C CG2 . ILE B 529 ? 1.3009 0.9017 1.1542 0.0111  0.0620  -0.0199 556 ILE B CG2 
8455 C CD1 . ILE B 529 ? 1.5228 1.0404 1.3124 0.0774  0.1029  -0.0228 556 ILE B CD1 
8456 N N   . TYR B 530 ? 1.3433 0.9295 1.2822 -0.0334 0.0356  -0.0359 557 TYR B N   
8457 C CA  . TYR B 530 ? 1.3965 1.0210 1.3429 -0.0437 -0.0001 -0.0424 557 TYR B CA  
8458 C C   . TYR B 530 ? 1.4725 1.1242 1.3717 -0.0434 -0.0195 -0.0110 557 TYR B C   
8459 O O   . TYR B 530 ? 1.4963 1.1479 1.3762 -0.0383 -0.0057 0.0122  557 TYR B O   
8460 C CB  . TYR B 530 ? 1.4580 1.0764 1.4524 -0.0525 -0.0118 -0.0527 557 TYR B CB  
8461 C CG  . TYR B 530 ? 1.4308 1.0292 1.4792 -0.0625 0.0124  -0.0919 557 TYR B CG  
8462 C CD1 . TYR B 530 ? 1.4530 1.0758 1.5314 -0.0694 0.0001  -0.1340 557 TYR B CD1 
8463 C CD2 . TYR B 530 ? 1.4075 0.9588 1.4731 -0.0673 0.0496  -0.0895 557 TYR B CD2 
8464 C CE1 . TYR B 530 ? 1.4556 1.0635 1.5882 -0.0861 0.0268  -0.1759 557 TYR B CE1 
8465 C CE2 . TYR B 530 ? 1.5074 1.0327 1.6166 -0.0845 0.0801  -0.1279 557 TYR B CE2 
8466 C CZ  . TYR B 530 ? 1.5264 1.0837 1.6735 -0.0965 0.0698  -0.1726 557 TYR B CZ  
8467 O OH  . TYR B 530 ? 1.5346 1.0694 1.7299 -0.1207 0.1046  -0.2168 557 TYR B OH  
8468 N N   . PRO B 531 ? 1.5984 1.2697 1.4722 -0.0491 -0.0498 -0.0123 558 PRO B N   
8469 C CA  . PRO B 531 ? 1.5264 1.2079 1.3449 -0.0566 -0.0619 0.0177  558 PRO B CA  
8470 C C   . PRO B 531 ? 1.5555 1.2172 1.3758 -0.0609 -0.0716 0.0435  558 PRO B C   
8471 O O   . PRO B 531 ? 1.5939 1.2388 1.4564 -0.0563 -0.0781 0.0361  558 PRO B O   
8472 C CB  . PRO B 531 ? 1.6233 1.3081 1.4003 -0.0585 -0.0914 0.0060  558 PRO B CB  
8473 C CG  . PRO B 531 ? 1.6390 1.3328 1.4520 -0.0501 -0.0902 -0.0322 558 PRO B CG  
8474 C CD  . PRO B 531 ? 1.6241 1.3053 1.5059 -0.0481 -0.0712 -0.0449 558 PRO B CD  
8475 N N   . THR B 532 ? 1.5855 1.2512 1.3600 -0.0723 -0.0702 0.0710  559 THR B N   
8476 C CA  . THR B 532 ? 1.6346 1.2765 1.3991 -0.0784 -0.0804 0.0969  559 THR B CA  
8477 C C   . THR B 532 ? 1.7799 1.3914 1.5092 -0.0778 -0.1170 0.0988  559 THR B C   
8478 O O   . THR B 532 ? 1.6854 1.2800 1.4480 -0.0664 -0.1340 0.0927  559 THR B O   
8479 C CB  . THR B 532 ? 1.5853 1.2418 1.3123 -0.0954 -0.0653 0.1200  559 THR B CB  
8480 O OG1 . THR B 532 ? 1.8477 1.5157 1.5159 -0.1119 -0.0657 0.1190  559 THR B OG1 
8481 C CG2 . THR B 532 ? 1.2934 0.9804 1.0574 -0.0849 -0.0370 0.1143  559 THR B CG2 
8482 N N   . HIS B 533 ? 1.9175 1.5177 1.5728 -0.0878 -0.1292 0.1048  560 HIS B N   
8483 C CA  . HIS B 533 ? 2.0839 1.6392 1.6805 -0.0804 -0.1678 0.1070  560 HIS B CA  
8484 C C   . HIS B 533 ? 2.0702 1.6328 1.6749 -0.0600 -0.1935 0.0727  560 HIS B C   
8485 O O   . HIS B 533 ? 2.2612 1.7851 1.7941 -0.0494 -0.2274 0.0707  560 HIS B O   
8486 C CB  . HIS B 533 ? 1.9755 1.4926 1.4659 -0.1033 -0.1654 0.1333  560 HIS B CB  
8487 C CG  . HIS B 533 ? 1.9561 1.4523 1.4298 -0.1225 -0.1531 0.1633  560 HIS B CG  
8488 N ND1 . HIS B 533 ? 1.7170 1.2572 1.2449 -0.1355 -0.1204 0.1696  560 HIS B ND1 
8489 C CD2 . HIS B 533 ? 2.0754 1.5074 1.4810 -0.1280 -0.1716 0.1861  560 HIS B CD2 
8490 C CE1 . HIS B 533 ? 2.0566 1.5676 1.5572 -0.1511 -0.1187 0.1937  560 HIS B CE1 
8491 N NE2 . HIS B 533 ? 2.1760 1.6184 1.6011 -0.1489 -0.1477 0.2053  560 HIS B NE2 
8492 N N   . TYR B 534 ? 1.9775 1.5814 1.6612 -0.0532 -0.1788 0.0439  561 TYR B N   
8493 C CA  . TYR B 534 ? 2.1430 1.7633 1.8509 -0.0370 -0.2002 0.0037  561 TYR B CA  
8494 C C   . TYR B 534 ? 2.1555 1.7536 1.7720 -0.0314 -0.2258 0.0007  561 TYR B C   
8495 O O   . TYR B 534 ? 2.0784 1.6590 1.6721 -0.0090 -0.2688 -0.0198 561 TYR B O   
8496 C CB  . TYR B 534 ? 2.2604 1.8842 2.0281 -0.0185 -0.2293 -0.0228 561 TYR B CB  
8497 C CG  . TYR B 534 ? 2.2310 1.8868 2.1038 -0.0235 -0.2005 -0.0489 561 TYR B CG  
8498 C CD1 . TYR B 534 ? 2.1858 1.8421 2.0806 -0.0385 -0.1546 -0.0309 561 TYR B CD1 
8499 C CD2 . TYR B 534 ? 2.1760 1.8579 2.1207 -0.0130 -0.2182 -0.0956 561 TYR B CD2 
8500 C CE1 . TYR B 534 ? 2.1473 1.8106 2.1165 -0.0434 -0.1244 -0.0530 561 TYR B CE1 
8501 C CE2 . TYR B 534 ? 2.1079 1.8085 2.1403 -0.0254 -0.1833 -0.1214 561 TYR B CE2 
8502 C CZ  . TYR B 534 ? 2.1700 1.8520 2.2060 -0.0409 -0.1351 -0.0971 561 TYR B CZ  
8503 O OH  . TYR B 534 ? 2.1248 1.8038 2.2268 -0.0535 -0.0967 -0.1207 561 TYR B OH  
# 
